# Patent

## Title
Ribosomal targets for antibiotic drug discovery

## Abstract

The present invention relates to methods to identify molecules that binds in the neomycin binding pocket of a bacterial ribosome using structures of an intact bacterial ribosome that reveal how the ribosome binds tRNA in two functionally distinct states, determined by x-ray crystallography. One state positions tRNA in the peptidyl-tRNA binding site. The second, a fully rotated state, is stabilized by ribosome recycling factor (RRF) and binds tRNA in a highly bent conformation in a hybrid peptidyl/exit (P/E) site. Additionally, the invention relates to various assays, including single-molecule assay for ribosome recycling, and methods to identify compounds that interfere with ribosomal function by detecting newly identified intermediate FRET states using known and novel FRET pairs on the ribosome. The invention also provides vectors and compositions with an N-terminally tagged S13 protein.

## Background
CROSS-REFERENCE TO RELATED APPLICATIONS
This application claims priority from U.S. Provisional Application No. 61/476,102, filed Apr. 15, 2011, and U.S. Provisional Application No. 61/603,023, filed Feb. 24, 2012 which are herein incorporated by reference in their entirety.


GOVERNMENT FUNDING
This invention was made with Government support under Grant Number 2R01GM079238, 1R01GM65050 awarded by National Institute of Health; National Cancer Institute grant CA92584; U.S. Department of Energy DE-AC0376SF00098; National Institutes of Health Medical Scientist Training Program grant GM07739; National Institute of Health NRSA fellowship 1F31DC012026-01. The United States Government has certain rights in the invention.


FIELD OF THE INVENTION
During protein synthesis, the ribosome controls the movement of transfer RNA (tRNA) and messenger RNA (mRNA) by means of large-scale structural rearrangements. The present invention describes structures of the intact bacterial ribosome from Escherichia coli that reveal how the ribosome binds tRNA in two functionally distinct states, determined by x-ray crystallography. One state positions tRNA in the peptidyl-tRNA binding site. The second, a fully rotated state, is stabilized by ribosome recycling factor (RRF) and binds tRNA in a highly bent conformation in a hybrid peptidyl/exit (P/E) site. The structures help to explain how the ratchet-like motion of the two ribosomal subunits contributes to the mechanisms of translocation, termination, and ribosome recycling
INCORPORATION BY REFERENCE OF SEQUENCE LISTING
The Sequence Listing in an ASCII text file, named 28553_5468_02_SequenceListing.txt of 1 KB, created on Dec. 18, 2013, and submitted to the United States Patent and Trademark Office via EFS-Web, is incorporated herein by reference.
BACKGROUND OF THE INVENTION
Protein biosynthesis by the ribosome proceeds in defined phases of initiation, protein elongation, termination, and ribosome recycling (Schmeing 2009a). Understanding the molecular mechanism of translation requires high-resolution descriptions of the motions in the ribosome that enable key translational events (Munro 2009; Schmeing 2009a; Dunkle 2010). A ratchet-like rotation of the small ribosomal subunit relative to the large ribosomal subunit (Frank 2000) is crucial to the positioning of tRNAs in intermediate—or hybrid—binding sites, in which the 3′-CCA termini and acceptor stems of tRNA advance by one site on the large subunit while the anticodon elements of tRNA remain fixed on the small subunit (Moazed 1989). Binding of tRNAs in hybrid sites is central to mRNA and tRNA movements on the ribosome when they are translocated after each peptide bond is formed, during termination, and during ribosome recycling (Semenkov 2000; Zavialov 2003). However, the molecular basis for ribosome positioning of tRNAs in hybrid sites has been unclear.
Atomic resolution x-ray crystal structures of the bacterial ribosome with ligands bound have revealed molecular details of conformational rearrangements taking place in the unratcheted ribosome (Schmeing 2009a). The first molecular descriptions of intermediate states of ribosome ratchet-like rotation at atomic resolution were provided by x-ray crystal structures of the Escherichia coli 70S ribosome (Zhang 2009), with additional sub-steps proposed based on cryo-EM reconstructions (Fischer 2010). A post-translocation rotated state of the ribosome was recently identified by cryo-EM (Ratje 2010), in a conformation similar to that of the Saccharomyces cerevisiae 80S ribosome in the absence of bound substrates (Ben-Shem 2010).
After the termination of protein synthesis, ribosome recycling is required to free ribosomes from the mRNA transcript to enable further rounds of translation. In bacteria and organelles, ribosome recycling factor (RRF) binds in the tRNA binding cleft of the 70S ribosome at the interface of the large (50S) and small (30S) subunits and interacts with the 50S subunit peptidyl transferase center (PTC) (Lancaster 2002; Agrawal. 2004). In so doing, RRF sterically occludes deacylated tRNA binding in the peptidyl-tRNA site (P site, P/P configuration) to favor tRNA positioning in the hybrid peptidyl/exit tRNA binding site (P/E configuration) (FIG. 1A) (Gao 2005; Sternberg 2009). In the P/E configuration, tRNA is bound simultaneously to the P site of the small (30S) subunit and to the E site of the large (50S) subunit (Moazed 1989). Binding of the GTPase elongation factor-G (EF-G) to the RRF-ribosome complex and subsequent GTP hydrolysis lead to the dissociation of ribosomal subunits (Savelsbergh 2009).
Using single-molecule fluorescence resonance energy transfer (smFRET) techniques to interrogate the conformational states of the ribosome, conditions were found that favored positioning the tRNA in the hybrid P/E configuration for longer periods and allowed crystallization of the ribosome with tRNA bound in the P/E hybrid site. From these crystals, the structure of the intact E. coli 70S ribosome at a resolution of  ̃3.2 Å was determined and showed that the crystals contain two independent copies of the ribosome per asymmetric unit in a “top-top” polysome configuration (Brandt 2009), with one ribosome in an unrotated state with the classic positioning of the tRNA at the P/P site and, as heretofore never crytallographically observed at this resolution, with the second ribosome in a fully-rotated state and having the tRNA bound in the hybrid P/E configuration, revealing new targets on the ribosome for drug discovery.
Many antibiotic agents in clinical use target bacterial protein synthesis. The majority of these chemically diverse compounds inhibit translation by targeting functional centers in the ribosome (Blanchard 2010). Despite the enormous size and complexity of the 2.5 Megadalton ribosome particle, only a few target sites have been identified: near the Peptidyl- (P) tRNA binding and messenger RNA (mRNA) decoding sites of the small ribosomal subunit, and near the peptidyl transferase and GTPase centers of the large ribosomal subunit (Poehlsgaard 2005; Tenson 2006). The ability to identify new target sites within this dynamic macromolecular machine depends on sensitive methods for their identification and validation (Llano-Sotelo 2009; David-Eden, 2010).
Aminoglycoside antibiotics in the 2-deoxystreptamine family are broad spectrum bacteriocidal agents used to treat gram-negative bacterial infections. In vivo, these compounds are thought to act by altering the mechanism of aminoacyl-tRNA (aa-tRNA) selection during mRNA decoding on the ribosome (Fourmy 1996; Rodnina 2000; Schmeing 2009a). Aminoglycosides do so by inducing local rearrangements in ribosomal RNA (rRNA) within the highly conserved helix 44 (h44) decoding site of the small (30S) subunit that allow near- and non-cognate tRNAs to be inappropriately recognized and incorporated into the Aminoacyl- (A) tRNA binding site. Increased levels of aa-tRNA mis-incorporation eventually exceed the cell's capacity to cope with the reductions in translational fidelity, ultimately leading to cell death (Zaher 2009). However, in vitro, these aminoglycosides inhibit a range of steps in the translation mechanism. This includes mRNA and tRNA translocation, the directional movement of substrates with respect to both subunits of the intact (70S) ribosome (Gale 1981; Feldman 2010), and ribosome recycling, the process of subunit separation following the termination phase of protein synthesis (Hirokawa 2002). The physical origins of these aminoglycoside-induced effects are not known.
Early biochemical studies demonstrated that aminoglycosides can bind to regions of the ribosome outside the canonical decoding region (Davies 1968; Dahlberg 1978). Recently, the aminoglycoside neomycin was shown crystallographically, on classic ribosomal structures, to bind to the bacterial ribosome within Helix 69 (H69) of 23S ribosomal RNA (rRNA) in the large (50S) subunit (Borovinskaya 2007). While binding at this site was proposed to be responsible for inhibition of ribosome recycling and possibly translocation, the structural refinement at the time was insufficient to identify the points of contact and interaction (Feldman 2010; Borovinskaya 2007). Notably, neomycin concentrations higher than 100 nM inhibit translocation as potently as the most effective translocation inhibitor known, viomycin (Feldman 2010). Ribosome complexes bearing the well-established A1408G neomycin-resistance mutation in the small subunit ribosomal RNA (rRNA) which disrupts neomycin binding to the h44 decoding site (Recht 1999) exhibit a similar translocation inhibition profile at the higher (micromolar) neomycin concentrations, suggesting that strong inhibitory effects arise from the binding of neomycin outside of the canonical h44 decoding region (Feldman 2010).
Using the crystals reported herein with a combination of smFRET and further detailed x-ray crystallographic methods, the molecular basis of neomycin-induced inhibition of translation processes specific to its interactions with H69 of the large subunit have been determined and reveal the complete structural extent of a neomycin-binding pocket on the ribosome when neomycin stabilizes an inactive configuration of the ribosome. This site is termed the H69 neomycin-binding site or pocket and provides a powerful starting point for rational drug design.
SUMMARY OF THE INVENTION
The present invention is directed to methods of identifying candidate molecules, and in some embodiments candidate antibiotics, that bind in the H69 neomycin-binding pocket of a bacterial ribosome. These methods can be accomplished by providing a molecular model comprising the neomycin-binding pocket prepared from the atomic coordinates for an E. coli ribosome and from the neomycin binding pocket having the atomic coordinates in any one of Tables 6 to 9, or from atomic coordinates that may be derived from those of the ribosome or the tables using molecular modeling. Chemical structures are then docked to or fit to the molecular model to identify a candidate molecule that can bind to the neomycin binding pocket.
In one embodiment, the method comprises (a) providing a molecular model comprising of the neomycin binding pocket prepared from the atomic coordinates for an E. coli ribosome in a fully-rotated or intermediately-rotated state along with the neomycin binding pocket atomic coordinates in Table 6 or 8, respectively, (or atomic coordinates derived by molecular modeling any of those coordinates) and (b) docking or fitting chemical structures to the molecular model to identify a candidate molecule that can bind to the neomycin binding pocket.
In further embodiments, once a candidate molecule is identified, it can be produced for testing identified and determining whether it is capable of modulating ribosomal activity. All of the foregoing can be iteratively repeated to identify and produce a modified candidate molecule having higher binding specificity, higher binding affinity or higher potency relative to the candidate molecule.
In the above modeling candidate molecule can have a chemical structure suitable for binding/docking to the region defined by the residues from about 1905 to about 1931 in helix 69 (H69) in 23S ribosomal RNA, and in addition or in alternative to, can have a chemical structure suitable for binding/docking to a region defined by residues from about 1402 to about 1412 and residues from about 1488 to about 1500 in helix 44 (h44) in 16S ribosomal RNA.
Another aspect of the invention provides a crystal of a fully rotated or an intermediately-rotated ribosome having the three-dimensional structures (atomic coordinates) of the ribosomal crystals described in Examples 3 and 4.
Still another aspect of the invention relates to a single-molecule assay for ribosome recycling which comprises surface-immobilizing a ribosome labeled on the 50S subunit in the presence of tRNA, RRF and EF-G under translation conditions; and monitoring changes in the signal from the label, wherein a change in the signal indicates recycling or lack thereof. For example, this assay can be conducted in solution or using smFRET like imaging techniques (following fluorescence decay), with the label on the ribosome being a fluorophore. Further, if a test compound is added, then the presence of a signal indicates that recycling has been altered.
Further still, the invention is directed to an expression vector comprising a nucleic acid encoding ribosomal protein S13 having an N-terminal tag for attachment of a fluorophore. In some embodiments, the N-terminal tag is an SFP tag or an AcpS tag.
The invention also provides compositions comprising isolated N-terminal tagged S13. In some embodiments, the tagged S13 has a fluorophore linked via the tag to produce labeled S13 which in certain embodiments, is useful to assess ribosome structural states, for example, when incorporated into translationally competent ribosomes, especially when used as a FRET pair in conjunction with fluorophore-labeled L1. Any of these compositions can additionally include the components for in vitro translation.
Yet another aspect of the instant invention relates to methods to identify a compound that interferes with ribosomal function by assessing test compounds which cause the ribosome to alter, form adopt, change rate of formation into or out of, or otherwise be in, an intermediate FRET state. This method comprises (a) surface-immobilizing a ribosome having a FRET pair sensitive to transitioning between low FRET and high FRET states under translation competent conditions; (b) adding a test compound to the immobilized ribosome; and (c) monitoring or detecting changes in FRET states using smFRET imaging techniques to identify a test compound capable of (i) stabilizing the ribosome in an intermediate FRET state, (ii) changing the ribosome's distribution into or out of an intermediate FRET state, or (iii) changing the ribosome's rate of transition into or out of an intermediate FRET state. This method can be conducted with a FRET pair formed by a fluorophore on ribosomal protein L1 and a fluorophore on ribosomal protein S13.
Yet still a further method of the invention provides methods to identify a compound that interferes with ribosomal function using a FRET pair which has a fluorophore on ribosomal protein L1 and a fluorophore on ribosomal protein S13. This method comprises (a) surface-immobilizing a ribosome having a FRET pair sensitive to transitioning between a low FRET state and a high FRET state under translation competent conditions, wherein the FRET pair is formed with a fluorophore on ribosomal protein L1 and a fluorophore on ribosomal protein S13; (b) adding a test compound to the immobilized ribosome; and (c) monitoring or detecting changes in FRET states using smFRET imaging techniques to identify a test compound capable of (i) stabilizing the ribosome in a low FRET state, an intermediate FRET state or in a high FRET state, (ii) changing the ribosome's distribution among low, intermediate and high FRET states, (iii) changing the ribosome's rate of transition among low, intermediate and high FRET states, or (iv) abolishing FRET signals.
For either of the two foregoing methods, in certain embodiments, the L1 fluorophore is at (T202C) L1 and the fluorophore on S13 is at or near the amino terminus of S13. FRET pairs that are a donor-acceptor fluorophore pair or a donor-quencher fluorophore pair are useful.
Similarly, the two foregoing methods can be used in certain embodiments to identify candidate antibiotics. For example, a test compound is considered a candidate antibiotic when the test compound (i) stabilizes the ribosome in an intermediate FRET state or in a high FRET state, (ii) increases the ribosome's distribution in intermediate or high FRET states, (iii) increases the ribosome's rate of transition into intermediate or high FRET states, or abolishes FRET. Such candidate antibiotics can be tested to establish whether they inhibit function of a bacterial ribosome of pathological interest. The intermediate FRET state includes ribosomes having a structure assumed when the tRNA is present at the P/pe tRNA binding state (see Example 4).



BRIEF DESCRIPTION OF THE DRAWINGS
The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Patent and Trademark Office upon request and payment of the necessary fee.
FIG. 1A and FIG. 1B illustrate ribosome recycling in bacteria and organelles. Panel A is a schematic drawing showing the steps of ribosome recycling. After termination, ribosomes with deacylated tRNA in the P site undergo a structural rearrangement to a fully rotated state in which tRNA adopts a P/E hybrid state of binding and RRF is bound in the 50S P site. EF-G then catalyzes subunit dissociation (not shown). Panel B shows a global view of the ribosome in an unrotated, post-termination state (left) and in a fully rotated, intermediate state of recycling (right). The small subunit rRNA and proteins at the bottom of the complex are colored lighter and darker, respectively, with the large subunit rRNA and proteins at the top of the complex colored lighter and darker, respectively. Bound tRNA (dark form in center of image A), mRNA (dark grey at top of complexes shown in D), and RRF are also shown.
FIG. 1C illustrates the dependence of subunit release on RRF, EF-G and GTP under crystallographic buffer conditions. Release was monitored by the loss of Cy5-labeled L1 fluorescence in 50S subunits from surface-immobilized ribosome complexes carrying Cy3-labeled tRNAPhe in the P site. Complexes imaged in the absence of factors (diamonds) or in the presence of 10 μM RRF (circles); 20 μM EF-G and 2 mM GTP (inverted triangles); 10 μM RRF, 20 μM EF-G and 2 mM GDPNP (triangles); or 10 μM RRF, 20 μM EF-G and 2 mM GTP (squares). Data reflect the mean±SD of normalized Cy5 fluorescence intensity as a function of time from three experimental replicates.
FIG. 1D shows the conformational changes in the 70S ribosome during ratcheting with a view of the 30S subunit from the perspective of the 50S subunit (inset). Shifts between equivalent RNA phosphorus atoms and protein Cα atoms in the unrotated (R0) and fully rotated (RF) states are color coded as indicated by the scale. Ribosomes were superimposed using the 50S subunit as the frame of reference (Frank, Gao et al. 2007). Difference vectors between equivalent phosphorus or Cα atoms of the 30S subunits in the unrotated and fully rotated ribosome structures are shown on the right.
FIG. 2 depicts models of the conformation of tRNA in the P/E hybrid state. (A) Movement of P/E tRNA and mRNA towards the E site when compared to P/P tRNA and mRNA. The direction of view is shown to the right. (B) View of mRNA and P/E tRNA interactions with the 30S subunit P site and 50S subunit E site. Residues that contact mRNA (darker) and P/E tRNA (darkest) are shown. Colors for the ribosome, mRNA and tRNA as in FIG. 1. (C) View of the P/E tRNA ASL/D stem junction (darkest grey). P/P tRNA (lighter grey) is shown for comparison, with an arrow indicating the widening of the helix major groove. (D) Comparison of ASL/D stem junctions between P/E tRNA (darkest grey at bottom left), P/P tRNA (light grey in center), and A/T tRNA (darker grey toward upper right part of complex). A/T tRNA structure is a homology model adapted from Voorhees 2010. The bending angle for the A/T to P/E conformational change (70°) is shown.
FIG. 3 shows stereo views of electron density maps for P/P tRNA and P/E tRNA. (A) Electron density map for the anticodon stem-loop region of P/E tRNA. Shown is a (2Fobs−Fcalc) electron density map, calculated using sharpened amplitudes and Pirate density-modified structure factor phases and contoured at 0.7 standard deviations from the mean. (B) Electron density map for P/P tRNA. Shown is a (2Fobs−Fcalc) electron density map, calculated in Phenix and contoured at 1.1 standard deviations from the mean. The region shown is the junction between the anticodon stem, variable loop, and D stem. (C) Electron density map for P/E tRNA, as in B. In B and C, the base triple between G10, C25, and G44 in tRNAPhe in these structures is marked.
FIG. 4 illustrates the interactions of the 3′-CCA end of P/E tRNA with the 50S subunit E site. Elements of 23S rRNA (lighter grey), tRNA (darkest grey) and ribosomal proteins (medium grey) are shown. E. coli numbering is used for nucleotides and amino acids for the left and middle panels. Numbering for H. marismortui is used in the right panel. The positions of proteins L35, L28, and L44e are marked.
FIG. 5 is an expanded view of FIG. 4 showing the interactions of the 3′-CCA end of P/E tRNA with the 50S subunit E site in E. coli. 
FIG. 6 depicts the inter-subunit contacts in the fully rotated state. (A) Global view of inter-subunit contacts of the fully rotated state. Ribosomal RNAs and proteins are colored as in FIG. 1. Bridge numbering is adapted from (Schuwirth 2005; Ben-Shem 2010). The tip of helix H38 in bridge B1a is disordered in the present structures. (B) Bridge B3 serves as the pivot of inter-subunit rotation. The Mg2+ ion involved in inner-sphere coordination to the tandem sheared GA pairs in 16S rRNA and a fully hydrated Mg2+ ion in 23S rRNA are also shown. Ribosomal RNA colored as in FIG. 1. (C) Compression of helix H69 in 23S rRNA due to inter-subunit rotation. The direction of view is similar to FIG. 1. Color coding of the fully rotated ribosome (R) as in FIG. 1, with unrotated ribosome (U) in darkest grey. Nucleotide A1928 in 23S rRNA, nearly invariant in position, is shown for reference. Dashed circle shows the novel neomycin binding pocket. (D) Movement of H68 due to disruption of A702 interactions and packing with P/E tRNA. Nucleotides involved in H68 packing with P/E tRNA are indicated. Elements of the fully rotated ribosome are colored as in FIG. 1. Elements of the unrotated ribosome are shown in darkest grey. Arrows indicate movement from the unrotated to fully rotated state. (E) Bridge B4 in the fully rotated state compared to that in state R0 (darkest grey). Residues involved in direct contact in the fully rotated state are shown. Coloring for the fully rotated state as in FIG. 1.
FIG. 7 identifies the bridges between the two ribosomal subunits in the unrotated state. The small subunit rRNA and proteins are colored lighter and darker, respectively, with the large subunit rRNA and proteins colored lighter and darker, respectively. The tip of helix H38 in bridge B1a is disordered in the present structures.
FIG. 8 illustrates the extrusion of C1925 and U1926 due to helix H69 compression. The (2FObs−FCalc) electron density map contoured at 1.3 standard deviations from the mean is also shown.
FIG. 9 shows the RRF interactions with the ribosome in the fully rotated state. (A) Contacts between RRF domain I and the P and A sites of the 50S subunit. Amino acids in RRF (grey helix across top of figure) and nucleotides in 23S rRNA (grey) in direct contact are shown. Helix H69 and the 30S subunit are behind the view shown. (B) Contacts between RRF and protein S12 in the 30S subunit. Amino acids at the junction of RRF domains I and II that interact closely with S12 are indicated. RRF, S12 and rRNAs colored as in FIG. 1.
FIG. 10 depicts the superposition of a fully rotated ribosome in a pre-translocation complex mimic (Ratje 2010) with the recycling intermediate structure. Domains IV and V of EF-G (darkest grey) and domain II of RRF (lightest grey) significantly overlap, with some overlap of domain III in EF-G and hinge region of RRF. H69 in the recycling complex is also shown for reference. Superposition used the 50S subunit as a frame of reference (Frank 2007).
FIG. 11 illustrates that neomycin inhibits ribosome functions in vitro. (A) EF-Tu(GTP)-catalyzed accommodation of Phe-tRNAPhe at the A site of wild-type ribosomes programmed with cognate (UUC) and near-cognate (UCU) codons was monitored via FRET. The incorporation of cognate (Cog) tRNA (closed circles) and near-cognate (NC) tRNA (open circles) in the absence of antibiotics is shown. The incorporation of cognate tRNA (grey triangles) and of near-cognate tRNA (open triangles) in the presence of 100 nM neomycin, and the incorporation of cognate and near cognate tRNAs (grey closed diamond and open diamond, respectively) in the presence of 20 μM neomycin are also shown. (B) EF-G catalyzed translocation, monitored by smFRET, was normalized to the no drug case. The fractions of translocated molecules observed at neomycin concentrations of 0 μM (red squares), 0.01 μM (open triangles), 0.1 μM (inverted grey triangles), 1 μM (dark grey squares), 10 μM (diamonds) and 100 μM (open squares) are shown. (C) Recycling of wild-type 70S ribosome complexes was monitored by the disappearance of Cy5-labeled L1 fluorescence in 50S subunits from surface-immobilized wild-type ribosome complexes. Ribosome recycling at neomycin concentrations of 0 μM (squares), 0.1 μM (inverted grey triangles), 1 μM (dark grey squares), 10 μM (blue diamonds) and 100 μM (open squares) are shown. Under identical conditions, photobleaching was negligible (black circles).
FIG. 12 illustrates that neomycin inhibits ribosomal functions in A1408G mutant ribosomes. (A) The process of EF-Tu(GTP)-catalyzed accommodation of Phe-tRNAPhe aa-tRNA at the A site of A1408G mutant ribosomes programmed with cognate (UUC) and near-cognate (UCU) codons were monitored via smFRET. In the absence of antibiotic, the incorporation of cognate (Cog) tRNA into A1408G ribosomes (closed circles) was similar to that of the wild-type system (FIG. 11). The incorporation of near-cognate (NC) tRNA (open circles) was minimal, similar to the wild-type system (FIG. 11). In the presence of 100 nM neomycin, the incorporation of cognate (dark grey triangles) was similar to that of the wild-type system while the incorporation of near-cognate (grey open triangles) tRNAs was reduced. At a neomycin concentration of 20 μM, the incorporation of cognate (grey closed diamond) and near-cognate (open black diamond) tRNAs were both reduced. (B) Neomycin inhibits EF-G catalyzed translocation in a concentration dependent manner in the A1408G mutant background. The fraction of molecules that translocated under each neomycin concentration was normalized to the no drug case. Neomycin concentrations of 0 μM (red squares, at top), 0.01 μM (open black triangles), 0.1 μM (inverted grey triangles), 1 μM (dark grey squares), 10 μM (blue squares, in middle) and 100 μM (black open squares) were tested. (C) Neomycin inhibits the process of ribosome recycling catalyzed by RRF, EF-G and GTP in a concentration-dependent manner in the A1408G mutant background. Neomycin concentrations of 0 μM (red squares, at bottom), 0.1 μM (inverted grey triangles), 1 μM (dark grey squares), 10 μM (blue squares, in lower middle) and 100 μM (black open squares) were tested. Under identical conditions, photobleaching was minimal (black circles).
FIG. 13 illustrates that neomycin stabilizes an intermediate conformation of the ribosome. (A) Cartoon depicting the low FRET and High FRET states of the ribosome. (B, C) Single-molecule FRET trajectories, as shown in FIG. 14, were summed into population FRET histograms to reveal the population behaviors of Cy3-labeled S13 (N-terminus) and Cy5-labeled L1 (T202C) ribosome complexes bearing (B) deacylated tRNAfMet or (C) deacylated tRNAPhe in the P site.
FIG. 14 illustrates the dynamics between S13 and L1 in the absence of neomycin. (A) A representative smFRET trajectory from a ribosome complex labeled with Cy3-S13 and Cy5-L1 imaged at 40 ms time resolution in the absence of drug. FRET efficiency (FRET=ICy5/[ICy3+ICy5]) is shown in blue. The inset reveals short-lived dwells in multiple FRET states. (B) A population FRET histogram, composed of >1500 smFRET trajectories, reveals the existence of multiple, FRET states. The representative smFRET trajectory shown in the inset of FIG. 14A is idealized using the segmental k-means algorithm in QuB (Qin 1996) to (C) 2- and (E) 3-state models. Transition density plots (Munro 2007), obtained by the idealization of individual smFRET trajectories to the (D) 2- and (F) 3-state model, suggest the existence of at least one short-lived intermediate-FRET state. Population FRET histograms fit using Gaussian distributions to the sum (black) of (D) two or (F) three non-zero FRET states (red).
FIG. 15 shows that ribosome release factor (RF)-1 stabilizes the post-termination ribosome complex bearing deacylated tRNAPhe in the P site in a high-FRET, unrotated state. Top panel, cartoon depicting binding sites. Bottom panel, population FRET histograms, generated as described in FIG. 14, reveal the population behavior in the absence (left) and presence (right) of 10 μM RF-1.
FIG. 16 shows that kanamycin stabilizes ribosome complexes bearing deacylated tRNAfMet in the P site in a low-FRET, unrotated state. Top panel, cartoon depicting binding sites and kanamycin structure. Bottom panel, population FRET histograms, generated as described in FIG. 14, reveal the kanamycin concentration dependence of low-FRET, unrotated, state stabilization.
FIG. 17 shows that ribosome recycling factor (RRF) stabilizes ribosome complexes bearing deacylated tRNAfMet in the P site in a high-FRET rotated state. Top panel, cartoon depicting binding sites. Bottom panel, population FRET histograms, generated as described in FIG. 14, reveal the RRF concentration dependence of high-FRET, rotated, state stabilization.
FIG. 18 shows that elongation factor (EF)-G stabilizes ribosome complexes bearing deacylated tRNAfMet in the P site in a high-FRET, rotated state. Top panel, cartoon depicting binding sites. Bottom panel, population FRET histograms, generated as described in FIG. 14, reveal the EF-G concentration dependence of high-FRET, rotated, state stabilization.
FIG. 19 shows that viomycin stabilizes ribosome complexes bearing deacylated tRNAfMet in the P site in a rotated state. Top panel, cartoon depicting binding sites and viomycin structure. Bottom panel, population FRET histograms, generated as described in FIG. 14, reveal the viomycin concentration dependence of high-FRET, rotated, state stabilization.
FIG. 20 provides a 2Fobs−Fcalc electron density difference map of neomycin bound in the h44 decoding site of the intermediate-rotated ribosome, contoured at 1.7 standard deviations from the mean. Colors for 16S rRNA and neomycin are as in FIG. 23A. The 16S rRNA residues A1492 and A1493 are extruded from h44 as previously reported Borovinskaya 2007).
FIG. 21 shows that the neomycin contacts within H69 of 23S rRNA and its bridging interactions with h45 of 16S rRNA induce global rearrangements in the 70S ribosome. (A) Electron density map for neomycin within the H69 binding site. The 23S rRNA helix H69 (grey), 16S rRNA helix h45 (blue) and neomycin (light blue) are shown, along with a (2Fobs−Fcalc) electron density map, calculated in Phenix and contoured at 1.4 standard deviations from the mean. (B) Neomycin interactions with the H69 binding site showing points of contacts with the major groove and bridging interactions with the backbone of rRNA helix h45 of the small subunit. Neomycin and rRNA contacts <3.5 Å are shown as dashed lines. Ring II of neomycin packs against the major groove face of residues G1921, G1922 and U1923, while rings I, III and IV largely participate in backbone contacts. (C) Effects of neomycin binding to H69 on inter-subunit rotation in the ribosome. (Inset) View of the 30S subunit from the perspective of the 50S subunit. Difference vector shifts between equivalent RNA phosphorus atoms and protein Ca atoms in the unrotated (R0) vs. fully rotated (RF) states on the left; unrotated (R0) vs. intermediate-rotated (RI) state with neomycin bound to H69 in the middle; fully rotated (RF) state vs. intermediate-rotated (RI) state with neomycin bound to H69 on the right. Vectors are color coded as indicated by the scale. Ribosomes were superimposed using the 50S subunit as the frame of reference as described in the Example 4.
FIG. 22 depicts structural models of ribosome complexes with fluorescence components in (A) the unrotated, (B) partially rotated and (C) fully rotated configurations. The unrotated and fully rotated models were constructed using coordinates from Example 3. The partially rotated model was obtained by superimposing the neomycin-bound, partially rotated structure reported here onto the fully rotated structure (Example 3) using PyMOL (see Examples). The various components are marked and in a color version of this figure, the L1 stalk (L1 protein and 23S rRNA helices 76-78) is shown in pink. Ribosomal protein S13 of the small subunit is shown in cyan. Classically configured (P/P) P-site tRNA is shown in red; P/pe tRNA in green and P/E tRNA in blue. RRF is shown in orange. Approximate positions of Cy3 and Cy5 are shown as green and red circles, respectively; and distances between them in each model were estimated using PyMOL.
FIG. 23 shows the position of tRNAPhe in the intermediate-rotated and neomycin-bound ribosome. (A) Fobs−Fcalc difference electron density map for P/pe tRNA in the neomycin-bound, intermediate-rotated ribosome configuration with its position relative to rRNA elements h24, h29, h30, h31 and h44 of the small subunit and rRNA elements H69 and H88 (grey) of the large subunit and neomycin bound to H69. Shown is a (Fobs−Fcalc) electron density map, calculated in Phenix and contoured at 2.5 standard deviations from the mean. (B) The position of P-site tRNA observed (P/pe in pale grey) is intermediate between classical (P/P, right) and hybrid (P/E, left) configurations showing the relative angle of T stem displacement towards the large subunit E site and the extent of anticodon movement towards the small subunit E site. The D stem corresponds to the dihydrouridine loop (residues 14-21) of P-site tRNA; ASL refers to its anticodon stem loop; the 3′ CCA end is denoted with an asterisk. The tRNA anticodon stem loops move 2 and 4 Ångstroms from P/P to P/pe, and P/pe to P/E, respectively. (C) Superposition of unrotated R0 (classical, P/P tRNA), fully rotated RF (P/E tRNA) and intermediate RI (P/pe tRNA) ribosome configurations showing the change in major groove width of H69 of the large subunit rRNA, the relative positions of H69 and h45 of the small subunit rRNA, as well as the observed position of neomycin (Neo) in the RI structure. The helix conformation of H69 in the unrotated state is essentially unchanged by neomycin binding. (D) In the intermediate-rotated configuration, helix h24 near position A790 in the small ribosomal subunit sterically blocks the transition of P-site tRNA (near position U39) into the P/E hybrid configuration. The P/E tRNA (dark grey), and P/pe tRNA (light grey) anticodon stem loop region, and 16S rRNA helix 24 of fully rotated (RF, dark) or intermediate-rotated (RI, light) conformations are shown. Directional arrows indicate movements of tRNA or h24, and the extent of the movement is shown in Ångstroms.
FIG. 24 shows a view of mRNA and Pipe tRNA interactions with the 30S subunit P site. Residues that contact P/pe tRNA (spheres) are shown. Colors for the ribosome and tRNA are as in FIG. 23A. Additionally, mRNA and small subunit protein S9 are shown. The key contacts between P-site tRNA and the small subunit are maintained in the neomycin-bound, intermediate-rotated ribosome configuration, as are the contacts between the tRNA ASL-D-stem junction and the minor groove of H69.
FIG. 25 illustrates that the CCA-end of P/pe tRNA occupies the large subunit E site. Shown is a (Fobs−Fcalc) difference electron density map, calculated in Phenix and contoured at 2.5 standard deviations from the mean. P/pe tRNA CCA-end contacts are similar to the P/E tRNA CCA-end in Example 3. P/pe tRNA position A76 interacts with H88 near positions G2421 and C2395, and to ribosomal protein L35 H is 30. C75 of P/pe tRNA is close to 23S rRNA position A2432, and to L28 H is 20.
FIG. 26 shows that neomycin binding to H69 stabilizes the small subunit platform conformation through interactions with neomycin ring IV, h45 position G1517 backbone, and h24 position U793 N3 or O4 group. Shown is neomycin ring IV, 16S RNA helix h45 and h24 and 23S rRNA H69. Dashed lines indicate possible hydrogen-bond contacts between neomycin ring IV, G1517 backbone phosphate oxygen, and U793 N3 or O4 position.
FIG. 27 shows that EF-G and EF-Tu clash with the neomycin stabilized intermediate ribosome conformation. (A) Intermediate (RI) ribosome structure was superimposed to the T. thermophilus ribosome structure containing EF-G (dark; Ratje 2010). EF-G domain II clashes with the 30S body near helix h15 (spheres), and EF-G domain V clashes with L7/L12 stalk protein L11 (spheres) and 23S rRNA H43 (grey). (B) Superposition of the intermediate structure with the EF-Tu (darkd) bound T. thermophilus ribosome structure (Schmeing 2009b). Domain II of EF-Tu sterically clashes with 30S body of the intermediate conformation. Superpositions were carried out by using the Pymol pairfit function.
FIG. 28 shows the results from an smFRET tRNA incorporation assay. (A, B) Repeat of the structures depicted in FIG. 27. (C, D) In these bar graphs, all selected traces were manually inspected for the appearance of stable 0.15-0.2 FRET state, which indicated Cy5-tRNAPhe incorporation into the A site. The ratio of the number of molecules showing A-site tRNA incorporation to the total number of molecules inspected for all experiments (no drug, 100 μM neomycin, 100 μM viomycin and 100 μM kanamycin) were normalized to that of the no drug case and are shown.



DETAILED DESCRIPTION OF THE INVENTION
In the following description, reference is made to the accompanying drawings that form a part hereof, and in which is shown by way of illustration specific embodiments which may be practiced. These embodiments are described in detail to enable those skilled in the art to practice the invention, and it is to be understood that other embodiments may be utilized and that logical changes may be made without departing from the scope of the present invention. The following description of example embodiments is, therefore, not to be taken in a limited sense, and the scope of the present invention is defined by the appended claims.
1. Definitions
“Single-molecule fluorescence resonance energy transfer” (or “smFRET”) is the application of FRET techniques to study a single molecule with at least two fluorescent labels, or the interaction of at least two molecules, each with a label. Fluorescence Resonance Energy Transfer (FRET) is a non-radiative pathway by which a molecule in an electronic excited state may relax back to the more stable ground state. The transfer of energy occurs through space via dipole-dipole interaction: energy from the excited state molecule (the donor fluorophore) may transfer to a neighboring molecule (the acceptor fluorophore) given significant degree of spectral overlap between donor emission and acceptor absorption, properly oriented dipole moments of the interacting dye molecules, and the appropriate distance between the two fluorophores. The Förster relationship defining the efficiency of FRET as a function of distance is unique for each dye pair. In smFRET the donor and receptor fluorophores are on the same molecule, or are on different molecules that interact, bringing the two fluorophores into proximity. The detection of FRET at the single-molecule scale enables the direct measurement of conformational events and/or binding processes on biologically-relevant time scales. Methods to perform smFRET imaging are known in the art, and are described, for example, in Blanchard 2004. Methods to attach translationally competent ribosomes to a surface are described, for example, in U.S. Pat. No. 7,297,532.
Dynamic smFRET refers to the use of smFRET techniques to interrogate biological samples of interest over extended periods of time in order to quantify changes in the amount of time that the sample spends in its various conformational states. By measuring time-dependent conformational dynamics in a biomolecule, insights into the physical parameters of motion are obtained that relate to regulation and function.
The labels used herein will generally comprise fluorophores. A “fluorophore” is a component of a molecule which causes a molecule to be fluorescent. It is a functional group in a molecule which will absorb energy of a specific wavelength and re-emit energy at a specific wavelength. The amount and wavelength of the emitted energy depend on both the fluorophore and the chemical environment of the fluorophore. Fluorescein isothiocyanate (FITC), a reactive derivative of fluorescein, has been one of the most common fluorophores chemically attached to other, non-fluorescent molecules to create new fluorescent molecules for a variety of applications. Other common fluorophores are derivatives of rhodamine (TRITC), coumarin, and cyanine Newer generations of fluorophores such as the CF dyes, Cyanin (Cy) dyes, the FluoProbes dyes, the DyLight Fluors, the Oyester dyes, the Atto dyes, the HiLyte Fluors, and the Alexa Fluors are claimed to be perform better (more photostable, brighter, and/or less pH-sensitive) than other standard dyes of comparable excitation and emission. Fluorophores especially useful for practicing the instant invention are described in PCT application PCT/US10/24824 which is incorporated herein in its entirety by reference.
The fluorophore may incorporate or be located proximally to a “protective agent” (or “quencher” or “triplet state quencher” or “fluorescence modifier”, in particular embodiments), which is a molecule or a moiety (i.e., chemical group) that has the ability to alter the photophysical properties of a fluorophore, particularly by altering the light state-dark state (i.e., singlet-triplet) occupancy distribution or relaxation pathway of excited and relaxing electrons. The ability of a molecule to function as a protective agent is often evidenced by its ability to alter the blinking and/or photobleaching characteristics of a fluorophore.
Those of skill in the art can readily select appropriate donor-acceptor pairs for FRET in accordance with the invention as well as modify the biomolecules of the invention to attach the donor and acceptor fluorophores in site-specific manner without substantially altering functionality of the biomolecule.
As used herein, “h44” is helix 44 (h44) decoding site of the small (30S) subunit.
As used herein, H69 is Helix 69 (H69) of 23S ribosomal RNA (rRNA) in the large (50S) subunit.
As used herein, “H69 neomycin-binding site” or “H69 neomycin-binding pocket” and neomycin-binding site refers to the location of neomycin binding or interaction at H69 on any one of the crystal structures described in Examples 3 and 4 herein. This term is used as a general shorthand to refer and to identify the contact points between neomycin and the ribosome at this site and embraces points of contact at this site or pocket to other parts of the ribosome in addition to those found on H69. These terms are also used to refer to the equivalent sites as found in the structures known in the art for other bacterial ribosomes.
The FRET states described herein depend upon the selected FRET pair used to interrogate structural transitions. The top panel of FIG. 13 shows a particularly useful example with its schematic diagram of the low FRET and High FRET states using an L1 with S13 pair. The general locations of L1, S13, their respective fluorophores and tRNA relative to the E, P and A sites on the ribosome are indicated. The intermediate FRET state of the present invention is one in which the ribosome has the structure assumed when the tRNA is present at the P/pe tRNA binding state (see Example 4). This intermediate state is stabilized by at least neomycin.
2. Overview
A combination of smFRET techniques and x-ray crystallographic methods were used to probe the molecular basis of neomycin-induced inhibition of translation processes specific to its interactions with H69 of the large subunit.
3. Ribosome Structure in Unrotated (classic P/P tRNA Bound) and Rotated (hybrid P/E tRNA Bound) States without Neomycin
The structures were determined for the intact E. coli 70S ribosomes at a resolution of  ̃3.2 Å (Table 1, 2), based on crystals that contain two independent copies of the ribosome per asymmetric unit in a “top-top” polysome configuration (Brand 2009). Prior to this work, a rotated x-ray crystal structure had never before been obtained for any ribosome.
One ribosome adopts an unrotated state, with tRNAPhe bound in the “classical” peptidyl-tRNA (P/P) binding site (FIG. 1B) (Selmer 2006) that mimics a post-termination state of the translation cycle. The second ribosome adopts a fully rotated conformation that contains tRNAPhe bound in the hybrid P/E binding site and RRF bound at the ribosomal subunit interface (FIG. 1B). This structure is thought to represent an early intermediate in bacterial ribosome recycling (FIG. 1A; Gao 2005). A similar hybrid P-site tRNA configuration may also be found in other functionally relevant configurations of the ribosome (e.g., the intermediate, “unlocked state” prior to translocation; Munro 2010a, b, c; Munro 2010).
When compared to the post-termination ribosome complex, the 30S subunit of the RRF-bound ribosome is rotated  ̃9° relative to the 50S subunit. An approximately orthogonal rotation of the head domain of the 30S subunit of  ̃4° swivels the head domain in the direction of the ribosomal E site on the 50S subunit. These motions of the 30S subunit into the rotated state result in shifts at the periphery of the ribosome of more than 20 Å (FIG. 1D) that direct deacylated P-site tRNA into the P/E hybrid site. The tRNA anticodon stem-loop (ASL) and mRNA move laterally by  ̃6 Å relative to the 50S subunit, coupled to the motion of the 30S subunit platform domain (FIG. 1D, FIG. 2A). When tRNA moves into the P/E site from the P/P site, ASL of the tRNA remains in contact with the 30S subunit head and platform domains (FIG. 2B, FIG. 3A), but breaks its interactions with 23S ribosomal RNA (rRNA) helix H69 in the large subunit (Selmer 2006) (FIG. 2B).
Bound in the hybrid P/E site, tRNAPhe is severely kinked at the junction between the ASL and D stem when compared to tRNAPhe bound in the P/P site. Although the conformation of the anticodon and two closing base pairs of the ASL region remain essentially unchanged, the major groove widens by  ̃4 Å at the junction of the ASL and D stem (FIG. 2C, FIG. 3). The kink between the ASL and D stems allows the acceptor stem of P/E tRNA to swing by  ̃37° into the 50S E site (FIG. 2D). This abrupt kink contrasts with the more distributed bend that occurs in mRNA decoding complexes bound to elongation factor EF-Tu (A/T state, (Schmeing 2009b; Voorhees 2010), in which tRNA bends in the opposite direction. Comparing P/E tRNA to A/T tRNA, the total extent of tRNA bending at the ASL/D-stem junction amounts to  ̃70° (FIG. 2D).
In the large subunit E site, P/E tRNA contacts the ribosome in a similar manner to tRNA bound in the E/E site (FIG. 2B; Selmer 2006). Nucleotides G2112 and G2168 in 23S rRNA, part of the protein L1-containing arm of the 50S subunit, stack on the D-loop and T-loop of P/E tRNA (FIG. 1C, FIG. 2B). Consistent with biochemical studies of the mechanism of translocation (Lill 1989), nucleotide A76 at the acceptor end of P/E tRNA stacks between nucleotides in helix H88 of 23S rRNA (FIG. 2B, FIG. 4, FIG. 5), where the terminal ribose engages the Watson-Crick face of nucleotide C2394 (Schmeing 2003; Selmer 2006). In contrast to the positioning of C75 in E-site tRNA in the bacterium T. thermophilus (Selmer 2006) and in the archaeal large subunit (Schmeing 2003), in E. coli, nucleotide C75 in P/E tRNA stacks on nucleotide A2432 in 23S rRNA, away from the tRNA acceptor stem (FIG. 4, FIG. 5). The striking divergence of the 50S E site contacts contrasts with the high level of conservation in the peptidyl transferase center, supporting the notion that the ribosomal E site evolved relatively late, and has continued to diverge (Selmer 2006; Bokov 2009).
The divergence among species shown in FIG. 4 (see also, FIG. 5) indicates that this is a site that may be targeted for drug discovery efforts in order to generate compounds that will bind this region to preferentially stabilize or inhibit formation of the P/E hybrid configuration in a target cell (e.g. pathogenic organism or cancerous cell) while not negatively affecting the performance of normal mammalian ribosome functions in an unwanted manner.
The molecular contacts between the two ribosomal subunits are composed of both rRNA and ribosomal proteins, with the central contacts, or bridges, conserved across kingdoms (Schuwirth 2005; Ben-Shem 2010). In the fully-rotated state, the pivot point for inter-subunit ratcheting occurs at bridge B3 (FIG. 6A, FIG. 7), which maintains the same conformation and contacts when compared to the unrotated ribosome (Schuwirth 2005). Bridge B3 is composed of a cross-strand adenosine stacking motif (Cate 1996a,b) in which residues A1418 and A1483 within helix 44 (h44) of 16S rRNA in the 30S subunit dock into the minor groove of helix 71 (H71) in 23S rRNA of the 50S subunit. Residues A1418 and A1483 lie within adjacent sheared G-A base pairs that coordinate an inner-sphere magnesium ion that possibly contributes to subunit association in all organisms (Schuwirth 2005; Shenvi 2005) (FIG. 6B).
In the aminoacyl-tRNA (A) and P sites, bridge B2a involves contacts between 23S rRNA helix H69 in the 50S subunit and 16S rRNA residues at the end of helix h44 in the 30S subunit, and is preserved in both the unrotated and fully-rotated states of the ribosome (FIG. 6A). In both states, residue A1913 of H69 penetrates the minor groove of the h44 mRNA decoding site. However, in going from the unrotated to fully-rotated state, the P-site tRNA anticodon and mRNA (FIG. 2A) and the end of helix h44 move laterally by  ̃6 Å towards the E site (FIG. 6C). Remarkably, the interactions between H69 and h44 are maintained during this movement due to a  ̃5 Å compression of H69 (FIG. 6C). In part, this compression is enabled by disruption of the terminal base pair (C1925-G1929) of H69 and extrusion of the nearly universally conserved uridine U1926 (Cannone 2002) from the tight U-turn motif at the base of H69 (Schuwirth 2005) (FIG. 8).
The observed conformational rearrangements in bridge B2a may help explain how antibiotics such as viomycin that target translocation stabilize the fully rotated state of the ribosome (Ermolenko 2007; Cornish 2008). Viomycin and the related antibiotic capreomycin bind to the unrotated state of the ribosome in the vicinity of nt A1913 in 23S rRNA (Stanley 2010), the only nucleotide whose contacts with h44 change appreciably during inter-subunit rotation. Aminoglycosides such as neomycin, which bind to two sites in bridge B2a (Borovinskaya 2007; Feldman 2010), may favor the fully rotated state of the ribosome by stabilizing the compressed conformation of helix H69.
On the opposite end of the tRNA binding cleft, bridge B7a is disrupted due to the rotation of the 30S platform domain (FIG. 1D). In the unrotated state, nucleotide A702 in 16S rRNA stacks on an A-A dinucleotide platform near the end of helix H68 of 23S rRNA (Cate 1996a,b). This interaction involves a hydrogen bond between N1 of A702 and G1846 in 23S rRNA (Schuwirth 2005). Consistent with chemical probing data used to identify hybrid tRNA binding sites (Moazed 1989), rotation of the 30S platform domain into the fully rotated position results in a  ̃13 Å displacement of A702 away from H68 that exposes the base pairing face of A702 to solvent (FIG. 6D). Consistent with biochemical observations (Feinberg 2001), H68 moves in the opposite direction by 2-3 Å to pack in the minor groove of the acceptor stem of P/E tRNA (FIG. 6D) likely helping to stabilize tRNA in the P/E hybrid site.
The absence of bridge B7a in the fully rotated state appears to be partially compensated for by new contacts between protein L2 in the large subunit and helices h23 and h24 in 16S rRNA (Bridges B7b, B7c; FIG. 6A). However, the most significant stabilizing contact to the 30S platform region in both the unrotated and fully rotated ribosome configurations remains bridge B4, which in bacteria involves intimate contacts between the hairpin loop at the end of helix H34 in 23S rRNA of the large subunit and protein S15 in the small subunit. Helix H34 bends by  ̃7 Å, or 12°, due to inter-subunit rotation and slightly adjusts how nucleotide A715 packs on the hydrophobic surface of protein S15 (Schuwirth 2005; FIG. 6E). Compensation for the loss of bridge B7a in the fully rotated state may also result from the formation of more extensive interactions between the 30S subunit body domain and the 50S subunit near bridge B8. In bridge B8, large subunit proteins L14 and L19 interact more strongly with helices h8 and h14 in the 30S subunit (FIG. 6A).
As the mechanism of translation hinges on bridge B7a remodeling during the normal process of translation, this site, encompassing the AA platform at the base of helix 68 in the 23S rRNA and residues from about A650—to about A750 of 16s rRNA (in E. coli numbering) may also be considered a key target for drug discovery as small molecules affecting the stability of this bridge interaction are expected to strongly inhibit translation performance.
In the fully rotated state, the head domain of the 30S subunit swivels as a rigid body in the direction of tRNA movement, rearranging bridge B1b to place the central alpha helix of protein S13 directly across from protein L5 in the 50S subunit (FIG. 1C) (Valle 2003a,b). This lateral change in protein S13 position correlates with tRNA binding in the hybrid P/E site and may help control the position of tRNAs on the ribosome (Frank 2007). Thus, the contacts between protein S13 and protein L5 probably play an important role in the ribosome ratcheting mechanism. Consistent with this view, deletions in protein S13 result in more rapid and lower fidelity translocation of mRNA and tRNA (Cukras 2005). Mutations in the other major contact between the 30S subunit head domain and helix H38 in the 50S subunit, bridge B1a, have a similar effect (Komoda 2006).
As head swivel is understood to play a key role in the translation mechanism (e.g. translocation), the two structures reported here also provide insights into means to regulate the observed motions of the head domain using small molecule compounds to either stabilize or disrupt the key points of contact between the small subunit head domain via small subunit ribosomal proteins S13, and the central protuberance (via large subunit ribosomal protein L5) and/or H38 (the so-called A-site finger helix) of the large subunit as well as points of contact between the small subunit head domain and tRNA substrates.
In the fully rotated ribosome, RRF binds in the P-site and A-site cleft of the 50S subunit, precluding tRNA binding in either site. Its 3-helix bundle domain (domain I) runs nearly parallel to the subunit interface, with alpha helix 3 packed tightly against helix H71 in 23S rRNA (FIG. 9A). Mutations in this region result in lethal or temperature-sensitive phenotypes (Janosi 2000). In addition, conserved amino acids within the tip of RRF domain I (Ashkenazy 2010) interact with rRNA nucleotides of the universally conserved P loop element of the peptidyl transferase center (FIG. 9A). These sets of interactions appear to be the same in both the unrotated and fully rotated states of the ribosome (Borovinskaya 2007; Weixlbaumer 2007), suggesting that they are necessary but not sufficient for the recycling mechanism.
Additional points of contact between RRF and the fully rotated ribosome occur between conserved amino acids near the junction of domains I and II in RRF and ribosomal protein S12 of the small subunit (FIG. 9B) (Ashkenazy 2010). Domain II of RRF is more constrained in its position in the ratcheted state compared to its location in the unratcheted ribosome (Borovinskaya 2007; Weixlbaumer 2007). As suggested by cryo-EM reconstructions of the ribosome in complexes with RRF (Agrawal 2004; Gao, 2005), RRF domain II likely serves a steric function in ribosome recycling. Docking of EF-G from a cryo-EM reconstruction of the ribosome in a rotated conformation related to translocation (Ratje 2010) onto the ratcheted 70S ribosome structure determined here shows significant overlap between domain II of RRF and domains IV and V of EF-G (FIG. 10). Thus, EF-G binding to the RRF-bound ribosome likely entails large-scale rearrangements in RRF, EF-G, and the ribosome (Gao 2005), the precise energetics of which may be altered by small-molecule compounds to alter or inhibit the mechanism of recycling.
When compared to other structures of the ribosome, the structure of the fully rotated state of the ribosome provides critical insights into the molecular description of the ratcheting mechanism in translation. As simple mRNAs can be translated in the absence of exogenous factors like EF-G (Gavrilova 1976), the ribosome itself serves as a Brownian ratchet (Munro 2009a; Spirin 2009a,b), with tRNA substrates likely serving as the “teeth”. A notable feature of the ratcheting mechanism is the use of RNA secondary structural elements to control large-scale conformational rearrangements in the ribosome. These include RNA stem-loops in bridges B2a and B4 that adjust as the 30S subunit rotates relative to the 50S subunit (Spahn 2004; Gao, 2005; Connell 2007; Zhang 2009; Ben-Shem 2010), helix H68 in 23S rRNA adjacent to bridge B7a and P/E tRNA, RNA helices H76 and H42 in the L1 and L11 arms of the large subunit, respectively (Valle 2003a,b; Munro 2009a; Schmeing 2009a; Ben-Shem 2010), and helix h28 in 16S rRNA which directs swiveling of the 30S subunit head domain (Schuwirth 2005). Helix h28 likely serves as the “spring” in the ratcheting process, helping to position the “pawl” between the small subunit P and E sites (Schuwirth 2005; Spirin 2009a,b; Dunkle 2010; Ratje 2010). The hinge-like motion in P/E tRNA observed here, when compared to P/P tRNA, suggests that the conserved tertiary structure of tRNA is required not only for mRNA decoding (Valle 2002; Schmeing 2009b; Voorhees 2010), but also for translocation, termination, and ribosome recycling (Li 2007; Ratje 2010). Intact P-site tRNA is required for translocation (Joseph 1998), a requirement that may in part be due to need for a large distortion of tRNA in the P/E binding site. This distortion may be used to tune the energetics of the transition between the pre-translocation state and post-translocation state of the ribosome. Future structural studies of ribosome complexes with EF-G will be required to explain how this factor controls the conformational events described here to accelerate translocation and ribosome recycling.
As mentioned above, aminoglycosides such as neomycin, which binds to two sites in bridge B2a (Borovinskaya 2007; Feldman 2010), likely favor the fully rotated state of the ribosome by stabilizing the compressed conformation of helix H69. In the aminoglycoside-stabilized rotated state, the normal mechanism of EF-G binding and translocation (Munro 2010c) is markedly more inhibited than observed for aminoglycoside binding to the h44 decoding site of the small subunit and the ribosome, by virtue of being unable to return to the classical unrotated state, is also no longer competent for the process of aminoacyl-tRNA selection mediated by Elongation Factor-Tu. Further, the ribosome is prevented from recycling. These are previously unknown mechanisms of action for antibiotics.
The nature of the secondary aminoglycoside binding site on the ribosome and its central importance to the translation mechanism was not clear until before this structure. It was previously known that loss of the tlyA gene, which encodes a 2′-O-methyltransferase that is specific for ribose methylation at C1409 (helix 44) of 16S rRNA and C1920 (H69) of 23S rRNA, confers ribosome resistance to the viomycin class of antibiotics (Johansen 2006), and it has been reported that viomycin binds the ribosome near the intersubunit bridge B2a (formed between 16S rRNA helix 44 and 23S rRNA H69), stabilizing the translocational intermediate conformation of the ribosome, in which the 30S subunit is rotated counter-clockwise relative to the 50S subunit and the tRNAs are bound in hybrid states (Ermolenko 2007)—this provides evidence that H69 is an antibiotic target and identifies a key residue on H69, but does not identify the boundaries of the location on H69. We previously defined residues C1920-C1925 and G1906 in H69 as well as G1929 in H69 as a neomycin and gentamicin binding site (Borovinskaya 2007) and determined the crystal structure, albeit in the ribosome's classic state. Our work makes it clear that the pocket is the circled region in FIG. 6C, which resides from about residue 1905 to about 1931 of H69 while the ribosome is in the rotated state; in the rotated state this new site is proximal to the canonical binding site for neomycin and other aminoglycosides, namely the residues from about 1402 to about 1412 and the residues from about 1488 to about 1500 in helix 44, in E. coli numbering. The identification of these sites provides rationale for applying in silico and in vitro drug discovery methods (both traditional and/or new (e.g. the proposed use a single-molecule methods described herein or in our previous work)) to identify compounds that bind to one or both sites to inhibit a specified translation activity and/or alter the conformation and/or energetics of the ribosome.
4. smFRET Studies
Consistent with earlier findings (David-Eden 2010); Ogle 2005), pre-steady state smFRET measurements of aa-tRNA selection showed that low concentrations of neomycin (100 nM) substantially increased the rates of near-cognate aa-tRNA accommodation, while having negligible effects on the selection of cognate tRNA (FIG. 11B). These miscoding effects were almost entirely suppressed by the A1408G resistance mutation in the h44 decoding site (FIG. 12A). However, when identical experiments were performed at a higher neomycin concentration (20 μM), the selection of both cognate and near-cognate tRNA was significantly attenuated (FIG. 11B) Inhibition persisted in the A1408G context, suggesting that neomycin binding outside of the h44 decoding region alters the selection mechanism (FIG. 12A). In line with previous investigations (Feldman 2010), neomycin blocked substrate translocation on both wild-type and A1408G ribosomes at concentrations above 1 μM (FIG. 11C and FIG. 12B). Neomycin also inhibited ribosome recycling—mediated by ribosome recycling factor (RRF) and EF-G—on both wild-type and A1408G ribosomes, with similar concentration dependence (FIG. 11D and FIG. 12C). Together, these findings argue that neomycin binding outside the canonical h44 decoding site prevents one or more central aspects of the translation mechanism.
In order to probe neomycin-induced inhibition of these three key translation steps, a new smFRET approach was developed to examine global conformational changes in the ribosome related to subunit rotation and distinct from tRNA motions. A FRET pair with acceptor fluorophore attached to protein L1 in the large subunit (Munro 2010b) and donor fluorophore conjugated to the N-terminus of protein S13, located within the small subunit head domain (FIG. 13A) was designed to report on formation of “unlocked state” configurations achieved prior to translocation and ribosome recycling (Valle 2003b); Munro 2010c); Munro 2010a).
Unlocked state formation entails the repositioning of deacylated tRNA bound in the Peptidyl-tRNA (P) site into the Exit (E) site on the large ribosomal subunit, termed the P/E hybrid state. Formation of the unlocked state also involves closure of the L1 stalk towards the subunit interface and an approximately 9° rotation of the small subunit with respect to the large (Example 3); Valle 2003b). Here, we probed ribosomes lacking A-site tRNA and bearing either deacylated P-site tRNAfMet (FIG. 13B) or tRNAPhe (FIG. 13C), similar to the substrates in the above tRNA selection and recycling studies, respectively.
In the absence of antibiotic, both complexes populated two, dominant FRET states that dynamically exchanged on a sub-second time scale (FIG. 14A-B), as well as one or more short-lived intermediate configurations (FIG. 14C-F) (Munro 2010b; Zhang 2009). The structural origins of these FRET states were probed using translation factors and antibiotics known to stabilize distinct ribosome conformations. In saturating concentration of release factor 1 (RF-1), known to stabilize a “locked” ribosome configuration with P-site tRNA bound in the P site of both ribosomal subunits (P/P site) and the L1 stalk in an “open” state (Sternberg 2009); Laurberg 2008; Petry 2008), the ribosome adopts the low-FRET state (FIG. 15). The addition of the 4,5-linked deoxystreptamine antibiotic kanamycin also stabilized the low-FRET state (FIG. 16). This observation is consistent with kanamycin's ability to stabilize peptidyl-tRNA in the A site of both ribosomal subunits (A/A site) within pre-translocation ribosome complexes by binding to helix h44 in the mRNA decoding site (Feldman 2010). Notably, the present complexes lack peptidyl-tRNA in the A site, indicating that kanamycin stabilizes the unrotated configuration of the ribosome directly—a finding consistent with the notion that the helix h44 decoding site changes conformation in its transition to the rotated ribosome configuration (Feldman 2010; Example 3). The high-FRET state was stabilized by binding of either RRF or EF-G (in the presence of the nonhydrolyzable GTP analog, GDPNP), factors that stabilize the ribosome in a rotated and unlocked state (FIGS. 17 and 18) (Valle 2003b). The high-FRET state was also favored in the presence of viomycin (FIG. 19), an antibiotic previously shown to stabilize a hybrid P/E tRNA position and a rotated state of the ribosome (Cornish 2008; Ermolenko 2007).
By contrast, neomycin exerted a bimodal effect on the dynamics and FRET distributions of ribosomes containing tRNAfMet in the P site (FIG. 13B). At low concentrations of neomycin (<100 nM), the low-FRET state was favored, as expected for ground state stabilization of classical tRNA positions by binding to h44 in the decoding site (Feldman 2010; Peske 2005). At higher concentrations (>1 μM), neomycin surprisingly stabilized a ribosome configuration exhibiting an intermediate FRET value, falling between those assigned above to unrotated (locked) and rotated (unlocked) states. At high neomycin concentrations, a similar intermediate-FRET configuration was also observed for complexes containing tRNAPhe in the P site (FIG. 13C). Taken together, these data suggest that neomycin may stabilize an otherwise transient intermediate in the transition of the ribosome that exists between locked and unlocked states (Munro 2010b) and that this configuration is incompatible with tRNA selection, translocation and ribosome recycling (FIG. 11).
5. Ribosome Structures for Unrotated and Rotated States with Bound Neomycin
Crystals containing 70S ribosomes in both the unrotated and fully rotated states, with bound P/P or P/E deacylated tRNAPhe, respectively, as described in Section 2 above, were soaked with neomycin. These crystals were used to measure diffraction data to a resolution of 3.5 Å (Tables 4 and 5).
After refinement of the 70S ribosome structures with tRNA removed from the models, FObs−FCalc difference electron density maps contained clear, positive electron density for neomycin. In the unrotated ribosome, neomycin was bound in its canonical h44 decoding site (FIG. 20). In the rotated ribosome, neomycin was present in the h44 site as well as a site at the base of helix H69 in the large subunit, near its site of interaction with elements h24 and h45 of the small subunit rRNA in intersubunit bridge B2b (FIG. 21A). In this site, rings I-III of neomycin make specific contacts with residues within the H69 major groove, while ring IV contacts h45 of the small subunit (FIG. 21B).
Notably, neomycin binding within helix H69 was accompanied by a large rearrangement of the rotated configuration of the ribosome. In contrast to the fully rotated state, the overall extent of small subunit rotation was markedly attenuated (FIG. 21C). In addition, motions of the small subunit body along the subunit rotation trajectory were partially uncoupled from those of the platform and head domains. Correspondingly, while the small subunit spur region moved to the same extent as in the fully rotated structure (approximately 20 Å), the small subunit platform domain rotated to a lesser extent (approximately 60 vs. 90). Lateral motions of the small subunit head domain were also less than observed in the fully rotated state (approximately 15 Å vs. 20 Å). The swivel-like rotation of the small subunit head domain in the direction of translocation was likewise reduced (approximately 20 vs. 40). These structural rearrangements agree well with the apparent distance between L1 and S13 observed by smFRET in the neomycin-stabilized intermediate (FIG. 13 and FIG. 22).
Strikingly, FObs−FCalc difference electron density maps also placed P-site tRNA in a position intermediate between classical (P/P) and hybrid (P/E) configurations (Example 3; Jin 2011) (FIG. 23A-B). In this new configuration, the tRNA anticodon stem-loop maintains its key interactions within the small subunit P site that are observed in both unrotated and fully rotated ribosome structures (FIG. 24). The 3′-CCA terminus of the tRNA also occupies the large subunit E site, as previously observed for tRNA in its P/E hybrid position (above); Jin, 2011) (FIG. 25). However, correlating with the intermediate rotation of the small subunit (FIG. 21C), the tRNA anticodon is only partially displaced in the direction of translocation (approximately 2 Å vs. 6 Å observed in the fully rotated state) (FIG. 23B). Furthermore, the P-site tRNA elbow domain is clearly located in a position that is intermediate between classical (P/P) and hybrid (P/E) configurations (above). In this position, the elbow domain of the tRNA does not physically interact with the L1 stalk (FIG. 22B). In keeping with nomenclature previously established for other intersubunit hybrid tRNA positions (Ratje 2010), we define this state as a P/pe hybrid configuration.
The attenuated degree of small subunit rotation and the corresponding positioning of P/E tRNA into the intermediate P/pe site seen in neomycin-soaked crystals can be explained by neomycin's position within H69. In the fully rotated state, compression of the major groove of H69 is required for intersubunit rotation (above). However, neomycin's specific interactions in the major groove of H69 prevent helix compression and enable bridging interactions between ring IV of neomycin and the phosphate of G1517 within h45 and the Watson-Crick face of U793 of h24 (FIG. 26), a residue previously shown to be important for subunit association (Pulk 2006). By altering bridge B2b rearrangements and sterically preventing H69 compression (FIG. 23C) accompanying the unrotated-to-rotated transition, neomycin alters the normal mechanism of 30S subunit rotation such that helix h24 of 16S rRNA sterically blocks P-site tRNA movement into its P/E hybrid position (FIG. 23D).
6. Structural Summary
Taken together, the smFRET and crystallographic data reveal that neomycin binding to the base of H69 can globally inhibit the mechanism of translation by preventing the full extent of H69 compression, thereby interrupting complete subunit rotation and P/E hybrid state formation. Correspondingly, the ribosome is unable to adopt the fully unlocked configuration that precedes both translocation and ribosome recycling (above; Munro 2010b). Neomycin-induced stabilization of this intermediate configuration also inhibits the process of tRNA selection, which occurs on the unrotated state. These inhibitory effects can be rationalized by the partially overlapping EF-G and EF-Tu binding sites. (Ratje 2010; Gao 2009; Schmeing 2009b).
When docked in the intermediate ribosome configuration, both EF-G and EF-Tu would clash sterically with the small subunit (FIG. 27). Furthermore, these results provide structural evidence that translation proceeds through cycles of conformational selection to allow both translation factors to bind overlapping regions of the ribosome without inhibiting translation (Feldman 2010); Munro 2010c; Chan, 2008; Whitford 2011; Wang 2011).
The unrotated ribosome configuration is competent to productively engage EF-Tu in ternary complex with tRNA and GTP; the fully rotated, P/E hybrid ribosome configuration is competent to productively engage EF-G; intermediate configurations of subunit rotation fail to productively bind either factor. This model is supported by direct measurements of elongation factor binding to the A site (FIG. 28).
The present findings further argue that the intrinsically dynamic nature of the ribosome and tRNA motions within the translating particle contribute to each step in the translation process. The capacity of aminoglycosides to alter the global conformation of the ribosome through two distinct sites (small subunit helix h44 and large subunit helix H69) sheds new light on the observed pleiotropic activities of aminoglycosides in translation. Neomycin-induced stabilization of the intermediate state observed here further supports a central role for H69 in the translation mechanism. Future efforts exploring whether ribosome dynamics and conformation can be manipulated through this site in a species-specific manner may offer important new means for therapeutic control of translation.
7. Rational Drug Design
The atomic coordinates for the ribosomal structures described herein and in particular, the coordinates defining the H69 neomycin-binding pocket, whether derived from one or more of X-ray crystallography structures herein, or from molecular modeling, homology modeling or molecular replacement, are used in rational drug design (RDD) to design a novel molecules of interest, and preferably novel antibiotics. The atomic coordinates for the H69 neomycin-binding pocket are provided, with and without bound neomycin as set forth in Tables 6-9.
It is contemplated that, by using the principles disclosed herein, the skilled artisan can design, make, test, refine and use novel protein synthesis inhibitors specifically engineered to reduce, disrupt, or otherwise or inhibit ribosomal function in an organism or species of interest. For example, by using the principles discussed herein, the skilled artisan can engineer new molecules that specifically target and inhibit ribosomal function in a pathogen, for example, a particular prokaryotic, organism, while preserving ribosomal function in a host, for example, a eukaryotic organism, specifically a mammal, and more specifically, a human. As a result, the atomic coordinates provided and discussed herein permit the skilled artisan to design new antibiotics that can kill certain pathogenic organisms while having little or no toxicity in the intended recipient, for example, a human.
It is contemplated that RDD using atomic co-ordinates of the large ribosomal subunit can be facilitated most readily via computer-assisted drug design (CADD) using conventional computer hardware and software known and used in the art. The candidate molecules may be designed de novo or may be designed as a modified version of an already existing molecule, for example, a pre-existing antibiotic, using conventional methodologies. Once designed, candidate molecules can be synthesized using standard methodologies known and used in the art. Following synthesis, the candidate molecules can be screened for bioactivity, for example, by their ability to reduce or inhibit ribosome function, their ability to interact with or bind a ribosome or a ribosomal subunit. Based in part upon these results, the candidate molecules may be refined iteratively using one or more of the foregoing steps to produce a more desirable molecule with a desired biological activity. The resulting molecules can be useful in treating, inhibiting or preventing the biological activities of target organisms, thereby killing the organism or impeding its growth. Alternatively, the resulting molecules can be useful for treating, inhibiting or preventing microbial infections in any organism, particularly animals, more particularly humans.
The tools and methodologies provided by the present invention may be used to identify and/or design molecules which bind and/or interact in desirable ways in with ribosomes and ribosomal subunits, and in particular with the neomucin-binding pocket.
Molecular modeling can be most readily facilitated by using computers to build realistic models of a ribosome, ribosomal subunit, or a portion thereof. Molecular modeling also permits the modeling of new smaller molecules, for example ligands, agents and other molecules, that can bind to a ribosome, ribosomal subunit, or a portion therein. The methods utilized in molecular modeling range from molecular graphics i.e., three-dimensional representations) to computational chemistry (i.e., calculations of the physical and chemical properties) to make predictions about the binding of the smaller molecules or their activities; to design new molecules; and to predict novel molecules, including ligands such as drugs, for chemical synthesis.
For basic information on molecular modeling, see, for example, Schlecht, 1998; Gans 1996; Cohen 1996; and Smith 1996. U.S. patents which provide detailed information on molecular modeling include, for example: U.S. Pat. Nos. 6,093,573; 6,080,576; 6,075,014; 6,075,123; 6,071,700; 5,994,503; 5,884,230; 5,612,894; 5,583,973; 5,030,103; 4,906,122; and 4,812,12.
Three-dimensional modeling can include, but is not limited to, making three-dimensional representations of structures, drawing pictures of structures, building physical models of structures, and determining the structures of related ribosomes, ribosomal subunits and ribosome/ligand and ribosomal subunit/ligand complexes using the known coordinates. The appropriate co-ordinates are entered into one or more computer programs for molecular modeling, as known in the art.
One approach to RDD is to search for known molecular structures that bind to the H69 neomycin-binding pocket. Using molecular modeling, RDD programs can look at a range of different molecular structures of molecules that may fit into this site, and by moving them on the computer screen or via computation it can be decided which structures actually fit the site well (Bains 1998). Examples of modeling software include, but are not limited to, InsightII, Discovery studio and Cerius by Accelrys; Sybyl by Tripos; Molecular Operating Environment (MOE) by Chemical Computing Group; Glide, Prime, and Maestro by Schrödinger Inc.; Bio-Suite by Tata Consultancy Services Ltd; Sanjeevini by Indian Institute of Technology, New Delhi; MoDeST (Molecular Design Software Toolkit) by SimBioSys; ICM-Pro and ICM-VLS by molsoft; VLifeMDS by Vlife Sciences Technologies
To facilitate molecular modeling and/or RDD the skilled artisan may use some or all of the atomic co-ordinates deposited at the RCSB Protein Data Bank under the numbers PDB ID: 3R8N, 3R8O, 3R8S, 3R8T (for structures without neomycin; and incorporated herein by reference), and/or those atomic co-ordinates for the H69 neomycin-binding pocket provided in Tables 6-9.
8. S13 Constructs and Assays
The present invention also provides a tagged S13 protein labeled with a fluorophore. While a tag can be introduced in any number of solvent accessible regions of the protein that do not disrupt its function or binding to the ribosome, a preferred site for introducing a tag is at the N terminus. It has been found that positioning an N-terminal fluorophore provides a FRET pair with labeled L1 (as described herein) that is a sensitive reporter of the transition of the ribosome from an unrotated to fully rotated stated as described herein.
The tag can be an SFP tag as generally described by Yin 2006. Other tags can be used as well including the 12 amino acid acyl carrier protein tag (AcpS) and a shorter, 8 amino acid tag derived therefrom, both of which are described in Zhou 2008.
Further tags for enzymatic labeling include ACP, Q-tag (for example Q3: NH2-GQQQLG-COOH) transglutaminase-catalyzed site-specific conjugation of small-molecule probes to proteins in vitro and on the surface of living cells and FGE-tag (for example: LCTPSR (wild-type), LCTASR, and LCTASA) (Rush 2008). Peptidyl affinity tags can also be present for purification, and include, but are not limited to, Sumo, Glutathione S-transferase (GST), His6, His10 and Flag. These purification tags can be used with a protease cleavage site and when located upstream from the labeling tag obtain the tagged protein. provide a way to fish
They also can also serve as purification tag for pulling out tagged ribosomes from mixed populations of ribosomes. Hence, if both wild-type S13 protein and tagged S13 are incorporated into the ribosome and affinity purification can be used to isolate the “tagged” subpopulation. This is achieved by placing, for example, a His6-10 tag upstream of the SFP tag and using a NTA or cobalt resin to “fish out” the tagged subpopulation.
Further still, the invention is directed to an expression vector comprising a nucleic acid encoding ribosomal protein S13 having an N-terminal tag for attachment of a fluorophore. In some embodiments, the N-terminal tag is an SFP tag or an AcpS tag.
Hence the instant invention relates to a variety of compositions, including compositions comprising isolated N-terminal tagged S13 with or without a label. Fluorophore labeled S13 is particularly useful when incorporated into translationally competent ribosomes and used as part of a FRET pair. When the FRET partner is a fluorophore-labeled L1 as described herein, this composition is useful for interrogating ribosome conformations and dynamics via changes in FRET states in accordance with this invention. Any of these compositions can additionally include the components for in vitro translation.
9. Other Aspects of the Invention
As described in the examples, this invention provides single-molecule assays for ribosome recycling which comprises surface-immobilizing a ribosome labeled on the 50S subunit in the presence of tRNA, RRF and EF-G under translation conditions; and monitoring changes in the signal from the label, wherein a change in the signal indicates recycling or lack thereof. For example, this assay can be conducted in solution or using smFRET like imaging techniques (following fluorescence decay), with the label on the ribosome being a fluorophore. Further, if a test compound is added, then the presence of a signal indicates that recycling has been altered.
Yet another aspect of the instant invention relates to methods to identify a compound that interferes with ribosomal function by assessing test compounds which cause the ribosome to alter, form adopt, change rate of formation into or out of, or otherwise be in, an intermediate FRET state. This method comprises (a) surface-immobilizing a ribosome having a FRET pair sensitive to transitioning between low FRET and high FRET states under translation competent conditions; (b) adding a test compound to the immobilized ribosome; and (c) monitoring or detecting changes in FRET states using smFRET imaging techniques to identify a test compound capable of (i) stabilizing the ribosome in an intermediate FRET state, (ii) changing the ribosome's distribution into or out of an intermediate FRET state, or (iii) changing the ribosome's rate of transition into or out of an intermediate FRET state. This method can be conducted with a FRET pair formed by a fluorophore on ribosomal protein L1 and a fluorophore on ribosomal protein S13.
Yet still a further method of the invention provides methods to identify a compound that interferes with ribosomal function using a FRET pair which has a fluorophore on ribosomal protein L1 and a fluorophore on ribosomal protein S13. This method comprises (a) surface-immobilizing a ribosome having a FRET pair sensitive to transitioning between a low FRET state and a high FRET state under translation competent conditions, wherein the FRET pair is formed with a fluorophore on ribosomal protein L1 and a fluorophore on ribosomal protein S13; (b) adding a test compound to the immobilized ribosome; and (c) monitoring or detecting changes in FRET states using smFRET imaging techniques to identify a test compound capable of (i) stabilizing the ribosome in a low FRET state, an intermediate FRET state or in a high FRET state, (ii) changing the ribosome's distribution among low, intermediate and high FRET states, (iii) changing the ribosome's rate of transition among low, intermediate and high FRET states, or (iv) abolishing FRET signals.
The conditions and smFRET techniques for conducting the foregoing methods can be readily determined by those of skill in the art, are known in the art or are described in the Examples hereof. The methods can be used with any source of bacterial ribosomes as well as with any mutant forms thereof. When testing for antibiotic candidates, one preferably uses ribosomes from a bacterial pathogen.
For either of the two foregoing methods, in certain embodiments, the L1 fluorophore is at (T202C) L1 and the fluorophore on S13 is at or near the amino terminus of S13. FRET pairs that are a donor-acceptor fluorophore pair or a donor-quencher fluorophore pair are useful.
Similarly, the two foregoing methods can be used in certain embodiments to identify candidate antibiotics. For example, a test compound is considered a candidate antibiotic when the test compound (I) stabilizes the ribosome in an intermediate FRET state or in a high FRET state, (ii) increases the ribosome's distribution in intermediate or high FRET states, (iii) increases the ribosome's rate of transition into intermediate or high FRET states, or abolishes FRET. Such candidate antibiotics can be tested to establish whether they inhibit function of a bacterial ribosome of pathological interest. The intermediate FRET state includes ribosomes having a structure assumed when the tRNA is present at the P/pe tRNA binding state (see Example 4).
The foregoing is considered as illustrative only of the principles of the invention. Further, since numerous modifications and changes will readily occur to those skilled in the art, it is not desired to limit the invention to the exact construction and operation shown and described, and accordingly, all suitable modifications and equivalents may be resorted to, falling within the scope of the invention. All references patents, patent applications, PDB data or other documents cited are herein incorporated by reference in their entirety.
EXAMPLE 1
General Methods and Materials
Purification of Native E. coli tRNAPhe.
The purification protocol for tRNAPhe was adapted from a published protocol (Cayama 2000). Briefly, E. coli cells (strain MRE600) harboring plasmid pBS-tRNAPhe, which overexpresses E. coli tRNAPhe, were cultured and harvested as previously described (Junemann 1996). The cell pellets were lysed by sonication in 20 mM Tris HCl, pH 7.5, 50 mM MgCl2 and 20 mM β-mercaptoethanol. The cell lysate was clarified by centrifugation at 35000 rpm in a Beckman Ti-70 rotor at 4° C. for 2 hours. Total cellular RNA was extracted from the supernatant by phenol extraction and ethanol precipitation. High molecular weight RNAs were removed by isopropanol precipitation (von Ehrenstein 1967). The soluble RNA fraction was then incubated for 15 min at 37° C. after adjusting the pH to 8 by addition of 0.5 M Tris HCl, pH 8.8 to deacylate tRNAs. As previously described (Blanchard 2004), tRNAPhe was specifically aminoacylated following brief incubation with phenylalanine, ATP and phenylalanyl-tRNA synthase. The reaction mixture was phenol extracted and the nucleic acid fraction was obtained by ethanol precipitation. After resuspending the pellet in 10 mM ammonium acetate pH 6.3, the sample was applied to a TSK Phenyl 5PW hydrophobic interaction column (Tosoh Bioscience) and Phe-tRNAPhe was purified by fractionation as previously described (Blanchard 2004). The isolated peak was desalted, deacylated by brief incubation at elevated pH and repurified using analogous methods.
Preparation of Dye-Labeled Ribosome Complexes.
The labeling of L1 protein (Cy5-S55C) and tRNAPhe (Cy3-s4U8) for smFRET experiment were performed as previously described (Munro 2010a,b). 70S ribosomes were reconstituted with dye-labeled L1 and non-enzymatically initiated with mRNA and (Cy3-s4U8) tRNAPhe by incubating with 1.5 molar excess of each over ribosomes at 37° C. for 10 minutes. The mRNA used has the same sequence as the one used in crystallization except for biotin modification at 5′ end to enable surface immobilization.
Purification of A1408G Ribosomes.
Wild-type ribosomes and ribosomes bearing A1408G mutation were purified from a Δ7prrn E. coli MG1655 strain (RecA-) for single-molecule translocation and recycling experiments. The A1408G neomycin resistance mutation was introduced into a NT102 (KanR, SpecR) plasmid containing an rrnB operon (Komoda 2006) using Quickchange II site-directed mutagenesis (Stratagene). Wild-type and A1408G containing pRB102 plasmids (Komoda 2006) were then swapped into a Δ7prrn E. coli MG1655 (pKK3535, AmpR; ptRNA67, SpecR) strain. Tightly-coupled 70S ribosomes were purified from these strains in Tris-polymix buffer as previously described (Munro 2007).
Single-Molecule FRET tRNA Incorporation Assay.
The process of tRNA selection on the ribosome was monitored using single-molecule FRET by stropped-flow injection of a 10 nM solution of ternary complex (EF-Tu(GTP)·aa-tRNA) containing Phe-tRNAPhe (Cy5-acp3U47) to surface-immobilized ribosome complexes containing deacylated tRNAfMet (Cy3-s4U8) in the P site as previously described (Geggier 2010). Fluorescence and FRET traces were extracted from video and selected for analysis using automated analysis software implemented in MATLAB (MathWorks) using the segmental k-means algorithm (Qin, 1996). Complete accommodation of Phe-tRNAPhe into the A site was marked by the first observation of a 400 ms dwell in a high (0.55±0.61) FRET state, structurally assigned to the “classical” pre-translocation complex configuration through previous investigations (Geggier 2010). Individual experiments, in which approximately 100 accommodation events were obtained, were performed in triplicate. The mean extent of accommodation and standard deviations are plotted as a function of time. Wild type and mutant ribosomes for these experiments were purified as previously described (Feldman 2010).
Single-Molecule Translocation Assay.
Fluorescence-based, single-molecule translocation assays were carried out as previously described (Munro 2010c) on either wild-type or A1408G mutant pre-translocation ribosome complexes. Experiments were performed in Tris-polymix buffer (pH 7.5, 5 mM Mg(OAc)2) and analyzed as previously described (Munro 2010c; Wang 2011), plotting the fraction of translocating molecules as a function of time.
EXAMPLE 1A
Ribosome Recycling Assays
Ribosome Recycling Factor Purification.
RRF was purified from E. coli strain BL21 Star cells (Invitrogen) expressing a C-terminal hexa-histidine tagged version of the protein. Cells were lysed by sonication in lysis buffer (50 mM HEPES, pH 7.6, 1 M NH4Cl, 10 mM MgCl2, 200 μM PMSF, 7 mM β-mercaptoethanol, 0.1% Triton-X11, and Roche EDTA-free protease inhibitor cocktail). After the lysate was clarified by centrifugation, it was applied to a HisTrap column (GE Healthcare). The column was washed with buffer containing 50 mM HEPES, 1 M NH4Cl, 10 mM MgCl2, 7 mM β-mercaptoethanol, and 20 mM imidizole; RRF was eluted in the same buffer containing 400 mM imidazole. The protein was concentrated by ultrafiltration and applied to Sephacryl 16/60 size exclusion column (GE Healthcare). The RRF containing fractions were concentrated to 550 μM and stored at −80° C.
Single-Molecule Fluorescence Experiments.
All single-molecule fluorescence experiments were performed at room temperature in an MES-Polymix buffer that resembled the crystallization condition (50 mM MES, pH 6.5, 5.0 mM MgCl2, 350 mM NH4Cl, 5.0 mM putrescine, 5.0 mM spermidine, 5 mM (3-mercaptoethanol and 0.5 mM EDTA). Oxygen scavenging and triplet-state quenching systems used were as previously described (Dave 2009). The smFRET data were acquired with Metamorph (Molecular Device), and analyzed in MATLAB (Mathwork) and QuB (www.qub.buffalo.edu) as previously described (Munro 2010a,b). Subunit release was monitored by directly exciting the Cy5 fluorophore within surface-immobilized ribosome complexes (Coherent) at 10 mW laser power. Time lapse imaging of the recycling reaction was performed by acquiring snapshot images (40 millisecond integration time) every 20 seconds over the course of 20 minutes. Changes in fluorescence intensity were analyzed and plotted in Origin (OriginLab).
Single-Molecule FRET tRNA Incorporation Assay.
The process of tRNA selection on the ribosome was monitored using single-molecule FRET by stopped-flow injection of a 10 nM solution of ternary complex (EF-Tu(GTP)·aa-tRNA) containing Phe-tRNAPhe (Cy5-acp3U47) to surface-immobilized ribosome complexes containing Cy3-labeled S13 and deacylated tRNAfMet in the P site as generally described in PCT/US12/32602, filed Apr. 6, 2012. After 30 seconds incubation, ternary complex was washed out with Tris-polymix Mg2+ buffer. The smFRET data were acquired by directly exciting the Cy3 fluorophore at 532 nm (LaserQuantum) while simultaneously recording Cy3 and Cy5 intensities in Metamorph (Molecular Devices) with 100 ms integration time. Fluorescence and FRET traces were extracted from video and traces from each movie were selected according to the criteria: signal-to-noise>5, background intensity<1500 and Cy3 blinking<1. All selected traces were then manually inspected for the appearance of stable 0.15-0.2 FRET state, which indicated Cy5-tRNAPhe incorporation into the A site. The ratio of the number of molecules showing A-site tRNA incorporation to the total number of molecules inspected for all experiments (no drug, 100 μM neomycin, 100 μM viomycin and 100 μM kanamycin) were normalized to that of the no drug case. Three independent experiments were performed under each condition and the mean with standard deviation were plotted using Origin (OriginLab). The results are shown in FIG. 28.
EXAMPLE 2
Tagged S13 and Its Uses
Generation of Site-Specifically Labeled 30S Subunits and 50S Subunits.
Ribosomal protein S13 was PCR-cloned from E. coli strain K12 genomic DNA into the pPROEX HTb vector with a TEV-cleavable His6-tag and a 12-residue peptide encoding the S6 epitope for the Sfp phosphopantetheinyl transferase reaction (Yin 2006), fused at the N terminus. Following transformation of this plasmid into an E. coli ΔS13 knockout strain (Cukras 2005), cells were cultured and ribosomes were harvested as previously described (Wang 2011). Pure 30S subunits were isolated via sucrose gradient centrifugation in a low magnesium buffer (20 mM HEPES pH 7.5, 50 mM KCl, 10 mM NH4Cl, 0.5 mM EDTA, 6 mM BME, 1 mM MgCl2). 30S subunits containing Sfp-tagged S13 were isolated from this population by cobalt affinity chromatography (Clontech). Subsequently, the Sfp tag was enzymatically labeled and the His6-tag was enzymatically removed in a buffer containing 20 mM HEPES, pH 7.5, 100 mM KCl, 10 mM MgCl, and 6 mM BME. 20 μM N-Sfp-S13 30S subunits, 5 μM TEV protease, 250 μM Cy3-CoA and 25 μM Sfp were incubated for 24 h at 18° C. Sfp enzyme, TEV protease and unbound Cy3-CoA were then removed by filtration over a 100K membrane (Millipore). Prior to 70S complex formation, ribosomes were buffer exchanged into Tris-polymix buffer (Munro 2010c). 50S subunits labeled with Cy5-L1 (T202C) were prepared and purified as previously described (Munro 2010b).
Preparation of L1-S13 FRET Ribosome Complexes with tRNAfMet or tRNAPhe in the P Site.
Cy3-S13 30S and Cy5-L1 50S subunits were heat activated at 42° C. for 10 min in Tris-polymix Mg2+ buffer and ribosomes were then initiated with fMet-tRNAfMet or NAc-Phe-tRNAPhe as previously described (Munro 2010c).
Single-Molecule L1-S13 FRET Assay.
All single-molecule FRET experiments were performed at room temperature in Tris-Polymix with 5 mM Mg2+ buffer as previously described (Wang 2011), where oxygen scavenging and triplet-state quenching systems were employed (Dave 2009). Following surface immobilization (Munro 2007), the ribosome-bound, P-site tRNA was deacylated by incubation with 2 mM puromycin for 10 min at room temperature. The smFRET data were acquired by directly exciting the Cy3 fluorophore at 532 nm (LaserQuantum) while Cy3 and Cy5 intensities were simultaneously recorded in Metamorph (Molecular Devices) with 40 ms integration time. The data were analyzed in MATLAB (MathWorks) and plotted in Origin (OriginLab) as previously described (Munro 2007).
Monitoring FRET Between Elongation Factors and the Ribosome During Translocation and tRNA Selection.
To monitor EF-G productively engaging the pre-translocation complex, EF-G was labeled with Cy5 fluorophore and stop-flow delivered to surface-immobilized ribosome complexes bearing deacylated tRNAfMet in the P site and Cy3-labeled dipeptidyl fMet-Phe-tRNAPhe (Cy3-acp3U47) in the A site, as previously described (Munro 2010c; Wang 2011). Pre-steady state smFRET measurements of this kind were taken in the absence and presence of 20 μM neomycin at 100 ms time resolution. Fluorescent traces were analyzed with MATLAB (MathWorks). All molecules with signal/noise>3 were inspected individually. Productive EF-G binding events were marked by the appearance of FRET (≧0.2), indicative of EF-G's domain IV entering the A site (Munro 2010c). The interaction of ternary complex (EF-Tu(GTP)·aa-tRNA) with the ribosome was similarly monitored in pre-steady state experiments collected at 15 ms time resolution in the absence and presence of 20 μM neomycin. Here, productive binding was marked by the appearance of FRET (>0.15) between the ternary complex containing Phe-tRNAPhe (Cy5-acp3U47) and deacylated tRNAfMet (Cy3-S4U8) within the P site of surface-immobilized 70S ribosome complexes (Geggier 2010). Complete accommodation was marked by the appearance of a relatively stable (>200 ms) high-FRET state (0.55±0.61). Fluorescent traces were analyzed with MATLAB (MathWorks). All molecules with signal/noise>3 were inspected individually. Each tRNA selection and translocation experiment were performed in triplicate and the average number and standard deviation of each event type were calculated and plotted in Origin (OriginLab).
EXAMPLE 3
Structural Analysis of Unrotated and Rotated Ribosome without Neomycin
Ribosome Purification and Crystallization.
Ribosomes lacking protein S1 were purified from E. coli strain MRE600 using sucrose gradient centrifugation, as described (Blaha 2000). Ribosomes were crystallized at 18° C. using microbatch 96-well plates and buffers containing 4.0-6.0% 2-methyl-2,4-pentanediol (MPD), 4.1-4.5% PEG 8000, 4.0 mM MgCl2, 380 mM NH4Cl, 5.7 mM putrescine, 5.0 mM spermidine, 10 mM Tris plus 40 mM MES, pH 6.5-7.0, and 0.25 mM EDTA. Ribosome complexes were formed by incubating 4 μM deacylated tRNAPhe and 8 μM mRNA of sequence 5′-GGCAAG GAGGUAAAAUUCUACAAA-3′ (SEQ ID NO: 1; Dharmacon) with 2 μM ribosomes at 37° C. for 15 minutes. 8 μM RRF was then added and the samples were incubated for an additional 15 minutes at 37° C. Prior to crystallization, samples were subjected to ultrafiltration to remove excess ligands.
Data Collection and Processing.
Ribosome crystals were stabilized with crystallization buffer containing 7.0% MPD, 7.0% PEG 8000 and 24% PEG 400, pH 4.8, to allow cryocooling of the crystals to liquid nitrogen temperatures. Diffraction data were measured from crystals cooled to 100° K using 0.1-0.3° oscillations at beamlines 241D-C at the Advanced Photon Source or at the Advanced Light Source (SIBYLS and 8.3.1 beamlines), each of which is equipped with an ADSC Q315 area detector. Data were reduced using XDS (Kabsch 1993), yielding the statistics shown in Table 1.







TABLE 1





X-ray crystallographic statistics


















Space group
P212121



unit cell (a, b, c in Å)
211.67, 438.07, 613.42



Resolution (Å)
 70-3.0



(high-resolution shell)*
(3.35-3.16)



Rmerge†
19.4 (57.7)



I/σ (I)
7.4 (1.8)



Completeness (%)
83.5 (66.1)



Measurement redundancy
5.3 (3.3)



Unique reflections
938,380 (101,586)



No. crystals used
10







*Data beyond the high-resolution shell in parenthesis was used for refinement and map calculation, and extend to an I/σ (I) of about 1. Data are 92.5% complete in the 3.9 Å-3.6 Å resolution shell, and 99% complete in lower-resolution shells.



†All statistics not in parentheses include data over the whole reported resolution range.






Molecular Replacement and Structure Refinement.

The two copies of the 70S ribosome in the crystallographic asymmetric unit were located using rigid-body refinement in Phenix (Adams 2010) of the well-ordered E. coli ribosome from a recent atomic-resolution structure determination (Zhang 2009). That starting model had previously been improved by diagnosing problems with stereochemistry, all-atom sterics, and conformations using MolProbity (Chen 2010) and correcting them using a variety of protein and RNA remodeling tools. RNA corrections were carried out with the automated RNABC software (Wang 2008), and were accepted if the fixes of all-atom clashes (Word 1999a,b), ribose pucker outliers or backbone conformer outliers (Richardson 2008) survived in refinement without compromising model geometry or R-factors. Protein corrections first included automated correction of Asn/Gln/His 180° “flips” (Word 1999a,b) in MolProbity or Phenix. More extensive corrections were carried out in Coot (Emsley 2010) or with the backrub (Davis 2006) and sidechain-rotator tools in KiNG (Chen 2009). Refinement was carried out in Phenix, including the use of pucker-specific target parameters. Corrections made prior to this new structure included rebuilds of 20 RNA suites with RNABC, plus pucker corrections in refinement, and numerous improvements to 50S proteins (Chen 2010), including sequence register-shifts, peptide flips in β-strands, and rotamer repairs of H-bonding at protein/RNA interfaces, to produce the model used in molecular replacement.
The resulting structural models were then refined using rounds of manual rebuilding in O (Jones 1991), Coot, or KiNG as well as positional refinement in Phenix, including use of a new functionality for automatic assignment of H-bond restraints using the Saenger base-pair types (Saenger 1984). Electron density maps were generated from the Phenix output directly, or using the program Pirate (Cowtan 2000). RNA rebuilding concentrated on the tRNAs and mRNAs, using the RNArotator tool in KiNG to make changes that improved both steric clashes and ribose pucker outliers in those regions to 80-90th percentile levels for this resolution. Protein corrections concentrated on RRF, L5, L27, and S12, in some cases making dramatic improvements such as taking L27 from a 0th percentile MolProbity score (combined clash, Ramachandran, and rotamer criteria) to 53rd percentile for the R0 molecule and 88th percentile for the RF molecule. While the overall sterics, geometry, and RNA conformations are all well above median quality (high percentile scores in Tables 2, 3), future rebuilding and refinements will be used to further improve protein and RNA sterics and geometry. In contrast to the earlier E. coli 70S structure determination (Zhang 2009), in which one of the two molecules was partially disordered, both ribosomes in the present structure are well ordered, with similar B-factors, validation statistics, and electron density quality.
The structures are deposited under PDB ID codes (searchable, e.g., at www.rcsb.org/pdb and www.wwpdb.org) as follows:

    
    
        Fully rotated state: 3R8N, 3R8S
        Unrotated state: 3R8O, 3R8T (the letter O, not zero)
    
    









TABLE 2





X-ray structure refinement



















Resolution (Å)
40-3.0




No. Reflections
938,304



Rfree Set
 19,021



R/Rfree (%)*
20.2/26.1



No. non-H Atoms
293,365



R.m.s. deviations
Bond lengths (Å)
0.013




Bond angles (°)
1.39



Mean ADP values (Å2)†
State R0 70S
29.0




State RF 70S
24.6







*Refinement in Phenix (Adams 2010) with riding H atoms.



†Atomic displacement parameter values are reported as isotropic B-factors. B-factor model is 2 per residue, wxu weight set to 1.66.













TABLE 3







Validation statistics**










State R0 70S
State RF 70S













All-atom clashscore
44.1 56th percentile
38.5 68th percentile


Ramachandran outliers
 9.2% 10th percentile
 8.4% 12th percentile


Ribose pucker outliers
 1.6% 73rd percentile
 1.9% 70th percentile


Bond + angle outliers
0.63%
1.77%





**From MolProbity (Chen 2010).


**From MolProbity (Chen 2010).






Comparisons to atomic-resolution structures of the ribosome, and to structural models of the intact ribosome refined against cryo-EM density maps, were carried out by least-squares superposition in the program O (Jones 1991), using ribose C1′ positions or phosphorous atoms in nucleotides. Superpositions to identify the relative position of the small and large subunits in the ribosome used the large subunit as the frame of reference (Frank 2007). The angles of rotation of the 30S subunit domains were calculated essentially as described in (Zhang 2009). Angles given for the rotation of the head domain were calculated from 30S subunit structures superimposed by means of their platform domains. A rotation of 0° is defined as centering the head domain over the 30S P site, as seen in the structure of the unratcheted ribosome presented here. The bending angle of helix H34 in 23S rRNA, part of bridge B4, was determined from the shift in position of A715 relative to G725 at the based of the helix. Superpositions of P/E, P/P and A/T tRNAs utilized the C1′ atoms of nucleotides 31-39 in the anticodon stem-loop. Comparisons of tRNA bending angles used the glycosidic bond of position 31 near the end of the anticodon stem-loop and the glycosidic bond of nucleotide 63 in the superimposed tRNAs. The bending angles calculated in this way are 37° for A/T tRNA compared to P/P tRNA, 37° for P/P tRNA compared to P/E tRNA, and 70° for A/T tRNA compared to P/E tRNA.
Structurally conserved nucleotides in the yeast 80S ribosome were used for superpositions of the two yeast 80S ribosome structures (Ben-Shem 2010) with the bacterial 30S and 50S subunits (Dunkle 2011, Table S3). One of the yeast 80S ribosomes most closely aligns with the post-translocation state recently identified (Ratje 2010). The body and platform domains are not fully rotated, and the small subunit head domain is rotated towards the E site by  ̃16°. In the yeast 80S ribosome, H69 is extended, as seen in the unrotated state R0 and the ratcheting intermediate R2 (Zhang 2009), and is not compressed, as seen in the present structure of the fully rotated state RF.
Intersubunit Contacts.
Contacts, or bridges, between the ribosomal subunits were determined using the program Probe (Word 1999a,b). Identified contacts were manually examined by comparison to difference electron density maps, calculated either in Phenix or using Pirate density modified phases, to discount disordered side chains. Only direct contacts are shown in FIGS. 6 and 7. Nomenclature for bridges adapted from (Yusupov 2001; Schuwirth 2005; Ben-Shem 2010). The dinucleotide platform formed by nucleotides A1847-A1848 in 23S rRNA differs from prior structural models of the 70S ribosome 2006; Laurberg 2008; Jenner 2010a,b), although in Haloarcula marismortui the motif is conserved as a U-A dinucleotide platform (nts U1888-A1889)(Klein 2004).
Figure Preparation.
Figures for Examples 3 and 4 were made using the program Pymol (Delano 2002). Numbering for ribosomal proteins follows that in the UniProt database (http://www.uniprot.org) (Uniprot 2010). Morphing movies were made using interpolation scripts written for CNS (Brünger 1998; Echols 2003) and were rendered in Pymol (Delano 2002).
EXAMPLE 4
Structural Analysis of Unrotated and Rotated Ribosome with Neomycin
Ribosome Purification and Crystallization.
Ribosomes were purified and crystallized as described in Example 3. Ribosome crystals were stabilized with crystallization buffer containing 7.0% MPD, 7.0% PEG 8000, 24% PEG 400, pH 4.8, to allow cryo-cooling of the crystals to liquid nitrogen temperatures. During the last cryo-cooling step (PEG 400 24%), neomycin (Sigma-Aldrich) was added at 100 μM concentration to the cryo-protection buffer, and crystals were incubated at 4° C. with neomycin containing cryo-protection buffer. After two hours of incubation, the concentration of neomycin was reduced to 2 μM by cryo-protection buffer exchange, and crystals were frozen with liquid nitrogen after 1-4 days of incubation at 4° C.
Data Collection and Processing.
Diffraction data were measured from crystals cooled to 100° K using 0.1-0.3° oscillations at the Advanced Light Source (beamlines 8.3.1 and 12.3.1), each of which is equipped with an ADSC Q315 area detector. Data were reduced using XDS (Kabsch 1993), yielding the statistics shown in Tables 4 and 5.







TABLE 4





X-ray crystallographic statistics


















Space group
P 212121



Unit cell (a, b, c in Å)
212.18 433.90 608.83



Resolution (Å)
70-3.3



(high-resolution shell)*
(3.58-3.48)



Rmerge†
23.1 (77.8)



I/σ (I)
5.76 (1.64)



Completeness (%)
95.2 (89.2)



Measurement redundancy
5.6 (3.4)



Unique reflections
793808 (51869) 



No. crystals used
1







*Data beyond the high-resolution shell in parentheses were used for refinement and map calculation, and extend to an I/σ (I) of about 1.12. Data are 96% complete in the 4.09-3.94 Å resolution shell, and 99% complete in lower-resolution shells.



†All statistics not in parentheses include data over the whole reported resolution range.













TABLE 5





X-ray structure refinement


















Resolution (Å)
70-3.3



No. reflections
792715



Rfree set
1997



R/Rfree (%)*
0.22/0.27



No. non-H atoms
293687



R.m.s. deviations



Bond lengths (Å)
0.006



Bond angles (°)
0.98



Molprobity statistics



All-atom clashscore
24.53



Ramachandran plot



Outliers
12.25%



Allowed
 19.1%



Favored
68.65%



Rotamer outliers
 22.1%







*Refinement in Phenix (Adams 2010) with riding H atoms.






Molecular Replacement and Structure Refinement.

The two copies of the 70S ribosome in the crystallographic asymmetric unit were located using rigid-body refinement in Phenix (Adams et al. 2010) of the well-ordered E. coli ribosome from a the atomic-resolution structure determination in Example 3. More extensive corrections were carried out in Coot (Emsley 2010) and sidechain-rotator tools in KiNG (Chen 2009a,b). Refinement was carried out in Phenix, including the use of pucker-specific target parameters. The resulting structural models were then refined using rounds of manual rebuilding in Coot, or KiNG as well as positional refinement in Phenix, including the use of a new functionality for automatic assignment of H-bond restraints using the Saenger base-pair types (Saenger 1984). Electron density maps were generated from the Phenix output directly. RNA rebuilding concentrated on the tRNAs, H69 and h44 (neomycin binding sites) and neomycin structure was inserted and fitted by using the Coot and Phenix.
Superpositions.
Comparisons to atomic-resolution structures of the ribosome were carried out by the “pair_fit” command in PyMOL that fits a set of atom pairs between two models. From the chosen atom pairs, disordered or moving regions of 23S rRNA were not used (e.g. L1 stalk, L7/L12 stalk, H38, H69) in the superpositions. Superpositions were performed using ribose C1′ positions or phosphorus atoms in nucleotides. The angles of rotation of the 30S subunit domains were calculated essentially as described in (Zhang 2009). Angles given for the rotation of the head domain were calculated from 30S subunit structures superimposed by means of their platform domains. A rotation of 0° is defined as centering the head domain over the 30S P site, as seen in the structure of the unratcheted ribosome (Example 3). Superpositions of P/P, P/pe and P/E tRNAs utilized the C1′ atoms of nucleotides 31-39 in the anticodon stem-loop (Example 3). Comparisons of tRNA bending angles used the glycosidic bond of position 31 near the end of the anticodon stem-loop and the glycosidic bond of nucleotide 63 in the superimposed tRNAs (Example 3). The bending angles calculated in this way are 24° for P/P tRNA compared to P/pe tRNA, 14° for P/pe tRNA compared to P/E tRNA.
EXAMPLE 5
Atomic Coordinates of H69Neomycin-Binding Pocket
The atomic coordinates for the H69 neomycin-binding pocket are provided in Tables 6-9. These tables contain the data from PDB files for the crystals described in Example 3 (Tables 6 and 7) and for the crystals described in Example 4 (Tables 8 and 9).
Table 6 provides the ribosomal coordinates for the residues involved in neormycin binding at the H69 site for the fully-rotated ribosome with the compressed H69 neomycin-binding site. Table 7 provides the same coordinates for the unrotated ribosome but the binding site is open (uncompressed).
Since the crystals from Example 4 were solved with neomycin bound, Table 8 provides the H69 neomycin-binding pocket coordinates for both neomycin and the ribosome in an intermediate-rotated state. Table 9 provides the same information as in Table 8 but for the ribosome in an unrotated state. These two latter sets of coordinates can be used for molecular modeling with or without the neomycin coordinates.
The tables are set forth after the References section.
REFERENCES


    Adams et al. (2010) Acta Crystallogr D Biol Crystallogr 66(Pt 2): 213-21.
    Agrawal et al. (2004. Proc Natl Acad Sci USA 101(24): 8900-5.
    Ashkenazy et al. (2010) Nucleic Acids Res 38(Web Server issue): W529-33.
    Bains (1998) Biotechnology from A to Z, 2nd ed., Oxford University Press, p. 259.
    Ben-Shem, et al. (2010) Science 330(6008): 1203-9.
    Blaha et al. (2000). Methods Enzymol 317: 292-309.
    Blanchard et al. (2010) Chem Biol 17, 633.
    Blanchard et al. (2004 Proc Natl Acad Sci USA 101(35): 12893-8.
    Bokov et al. 2009). Nature 457(7232): 977-80.
    Borovinskaya et al. (2007) Nat Struct Mol Biol 14(8): 727-32.
    Brandt et al. (2009) Cell 136(2): 261-71.
    Brünger et al. (1998) Acta Crystallogr. D Biol. Crystallogr. 54(Pt 5): 905-21.
    Cannone et al. (2002) BMC Bioinformatics 3: 2.
    Cate et al. (1996) Science 273(5282): 1678-85.
    Cate et al. (1996) Science 273(5282): 1696-9.
    Cayama et al. (2000) Nucleic Acids Res 28(12): E64.
    Chan et al. (2008) J Mol Biol 378, 12.
    Chen, V. B. (2010). Building Better Backbones: Visualizations, Analyses, and Tools for Higher Quality Macromolecular Structure Models. Biochemistry. Durham, N.C., Duke University. Ph.D.: 272.
    Chen et al. (2009) Protein Sci 18(11): 2403-9.
    Chen et al. (2010) Acta Crystallogr D Biol Crystallogr 66(Pt 1): 12-21.
    Cohen, ed. (1996) Guidebook on Molecular Modeling in Drug Design, Academic Press.
    Connell et al. (2007) Mol Cell 25(5): 751-64.
    Cornish et al. (2008). Mol Cell 30(5): 578-88.
    Cowtan (2000) Acta Crystallogr D Biol Crystallogr 56 Pt 12: 1612-21.
    Cukras et al. (2005) J Mol Biol 349(1): 47-59.
    Dahlberg et al. (1978) Antimicrob Agents Chemother 13, 331.
    Dave, et al. (2009) Biophys J 96(6): 2371-81.
    David-Eden et al. (2010) Nucleic Acids Res 38, 5982.
    Davies et al. (1968) J Biol Chem 243, 3312.
    Davis et al. (2006). Structure 14(2): 265-74.
    Delano, W. L. (2002) The PyMOL User's Manual. San Carlos, Calif., USA., Delano Scientific.
    Dunkle et al. (2011) Science 332, 981.
    Dunkle et al. (2010) Annu Rev Biophys 39: 227-44.
    Echols et al. (2003) Nucleic Acids Res 31(1): 478-82.
    Emsley et al. (2010) Acta Crystallogr D Biol Crystallogr 66(Pt 4): 486-501.
    Ermolenko et al. (2007) Nat Struct Mol Biol 14(6): 493-7.
    Feinberg and Joseph (2001) Proc Natl Acad Sci USA 98(20): 11120-5.
    Feldman et al. (2010) Nat Chem Biol 6(1): 54-62.
    Fischer et al. (2010) Nature 466(7304): 329-33.
    Fourmy et al. (1996) Science 274, 1367.
    Frank, J. et al. (2000) Nature 406(6793): 318-22.
    Frank et al. (2007) Proc Natl Acad Sci USA 104(50): 19671-8.
    Gale et al. (1981) The Molecular Basis of Antibiotic Action. (John Wiley & Sons Ltd, ed. 2nd.
    Gans et al. (1996) Fundamental Principals of Molecular Modeling, Plenum Pub. Corp. Gao et al. (2009) Science 326, 694.
    Gao (2005) Mol Cell 18(6): 663-74.
    Gavrilova et al. (1976) J Mol Biol 101(4): 537-52.
    Geggier et al. (2010) J Mol Biol 399, 576.
    Hirokawa et al. (2002) EMBO J 21, 2272.
    Janosi, L et al. (2000) J Mol Biol 295(4): 815-29.
    Jenner et al. (2010) Nat Struct Mol Biol 17(5): 555-60.
    Jenner et al. (2010) Nat Struct Mol Biol 17(9): 1072-8.
    Jin et al (2011) Proc Natl Acad Sci USA 108, 15798.
    Johansen et al. (2006) Mol. Cell 23, 173-182
    Joseph et al. (1998) EMBO J 17(12): 3478-83.
    Jones et al. (1991) Acta Crystallogr. A 47: 110-9.
    Junemann et al. (1996) Nucleic Acids Res 24(5): 907-13.
    Kabsch, (1993) J. Appl. Cryst. 26: 795-800.
    Klein et al. (2004) J Mol Biol 340(1): 141-77.
    Komoda et al. (2006) J Biol Chem 281(43): 32303-9.
    Lancaster et al. (2002) Cell 111(1): 129-40.
    Laurberg et al. (2008) Nature 454, 852.
    Laurberg et al. (2008) Nature 454(7206): 852-7.
    Li, W. et al. (2007) Proc Natl Acad Sci USA 104(42): 16540-5.
    Lill et al. (1989) EMBO J 8(12): 3933-8.
    Llano-Sotelo et al. (2009) RNA 15, 1597.
    Moazed et al. (1989). Nature 342(6246): 142-8.
    Munro et al. (2007) Mol Cell 25, 505.
    Munro (2009) Trends Biochem Sci 34(8): 390-400.
    Munro (2010a) EMBO J 29(4): 770-81.
    Munro et al. (2010b) Proc Natl Acad Sci USA 107(2): 709-14.
    Munro et al. (2010c) Nat Struct Mol Biol. 2010 December; 17(12):1470-7.
    Ogle et al. (2005) Annu Rev Biochem 74, 129.
    Peske et al. (2005) Mol Cell 18, 403.
    Petry et al. (2008) Curr Opin Struct Biol 18, 70.
    Poehlsgaard et al. (2005) Nat Rev Microbiol 3, 870.
    Pulk et al. (2006) RNA 12, 790.
    Qin et al. (1996) Biophys J 70, 264.
    Ratje et al. (2010) Nature 468(7324): 713-6.
    Recht et al. (1999) EMBO J 18, 3133.
    Richardson et al. (2008) RNA 14(3): 465-81.
    Rodnina et al. (2000) Biol Chem 381, 377.
    Rush et al. (2008) J. Am. Chem. Soc. 2008, 130, 12240-12241.
    Saenger, W. (1984). Principles of Nucleic Acid Structure. New York, Springer-Verlag.
    Savelsbergh et al. (2009) RNA 15(5): 772-80.
    Schlecht (1998) Molecular Modeling on the PC, John Wiley & Sons.
    Schmeing et al. (2009) Nature 461(7268): 1234-42.
    Schmeing et al. (2003) RNA 9(11): 1345-52.
    Schmeing et al. (2009) Science 326(5953): 688-94.
    Schuwirth et al. (2005) Science 310(5749): 827-34.
    Selmer et al. (2006) Science 313(5795): 1935-42.
    Semenkov et al. (2000). Nat Struct Biol 7(11): 1027-31.
    Shenvi et al. (2005) RNA 11(12): 1898-908.
    Smith (1996) Introduction to Theoretical Organic Chemistry and Molecular Modeling.
    Spahn et al. (2004) EMBO J 23(5): 1008-19.
    Spirin (2009a) Biochemistry 48(45): 10688-92.
    Spirin. (2009b) J Biol Chem 284(32): 21103-19.
    Stanley et al. (2010) Nat Struct Mol Biol 17(3): 289-93.
    Sternberg et al. (2009) Nat Struct Mol Biol 16(8): 861-8.
    Tenson et al. (2006) Mol Microbiol 59, 1664.
    Uniprot (2010). “The Universal Protein Resource (UniProt) in 2010.” Nucleic Acids Res 38(Database issue): D142-8.
    Valle et al. (2003a) Nat Struct Biol 10(11): 899-906.
    Valle et al. (2003b) Cell 114(1): 123-34.
    Valle et al. (2002) EMBO J 21(13): 3557-67.
    von Ehrenstein et al. (1967). Isolation of sRNA from intact Escherichia coli cells. Methods in Enzymology, Academic Press. Volume 12, Part 1: 588-596.
    Voorhees et al. (2010) Science 330(6005): 835-8.
    Wang et al. (2011) RNA 17, 2189.
    Wan et al. (2008). J Math Biol 56(1-2): 253-78.
    Weixlbaumer et al. (2007) Nat Struct Mol Biol 14(8): 733-7.
    Whitford et al. (2011) Proc Natl Acad Sci USA 108, 18943.
    Word et al. (1999a) J Mol Biol 285(4): 1735-47.
    Word et al. (1999b) J Mol Biol 285(4): 1711-33.
    Yin et al. (2006) Nat Protoc 1, 280-5.
    Yusupov et al. (2001) Science 292(5518): 883-96.
    Zaher et al. (2009) Cell 136, 746.
    Zavialov et al. (2003) Cell 114(1): 113-22.
    Zhang et al. (2009) Science 325(5943): 1014-7.
    Zhou et al. (2008) J. Am. Chem. Soc. 130, 9925-9930.









TABLE 6





H69 Neomycin Binding Site for Fully-Rotated Ribosome
























ATOM
32464
P
G A1515
−73.805
5.885
3.472
1.00
0.65
P


ATOM
32465
OP1
G A1515
−73.359
4.506
3.851
1.00
0.65
O


ATOM
32466
OP2
G A1515
−73.520
6.372
2.097
1.00
0.65
O


ATOM
32467
O5′
G A1515
−75.359
6.088
3.818
1.00
0.65
O


ATOM
32468
C5′
G A1515
−75.847
5.853
5.130
1.00
0.65
C


ATOM
32469
C4′
G A1515
−77.109
6.620
5.398
1.00
0.65
C


ATOM
32470
O4′
G A1515
−76.909
8.001
5.036
1.00
0.65
O


ATOM
32471
C3′
G A1515
−78.307
6.235
4.567
1.00
0.65
C


ATOM
32472
O3′
G A1515
−78.923
5.028
4.972
1.00
0.65
O


ATOM
32473
C2′
G A1515
−79.186
7.468
4.687
1.00
0.65
C


ATOM
32474
O2′
G A1515
−79.792
7.536
5.965
1.00
0.65
O


ATOM
32475
C1′
G A1515
−78.129
8.565
4.592
1.00
0.65
C


ATOM
32476
N9
G A1515
−77.952
9.050
3.209
1.00
0.68
N


ATOM
32477
C8
G A1515
−76.918
8.758
2.353
1.00
0.68
C


ATOM
32478
N7
G A1515
−77.047
9.322
1.175
1.00
0.68
N


ATOM
32479
C5
G A1515
−78.234
10.039
1.274
1.00
0.68
C


ATOM
32480
C6
G A1515
−78.906
10.852
0.326
1.00
0.68
C


ATOM
32481
O6
G A1515
−78.520
11.071
−0.819
1.00
0.68
O


ATOM
32482
N1
G A1515
−80.087
11.410
0.799
1.00
0.68
N


ATOM
32483
C2
G A1515
−80.547
11.190
2.054
1.00
0.68
C


ATOM
32484
N2
G A1515
−81.693
11.769
2.400
1.00
0.68
N


ATOM
32485
N3
G A1515
−79.937
10.441
2.950
1.00
0.68
N


ATOM
32486
C4
G A1515
−78.793
9.889
2.514
1.00
0.68
C


ATOM
32487
P
G A1516
−79.407
3.970
3.847
1.00
5.61
P


ATOM
32488
OP1
G A1516
−79.551
2.635
4.515
1.00
5.61
O


ATOM
32489
OP2
G A1516
−78.484
4.104
2.693
1.00
5.61
O


ATOM
32490
O5′
G A1516
−80.827
4.536
3.464
1.00
5.61
O


ATOM
32491
C5′
G A1516
−81.759
4.843
4.477
1.00
5.61
C


ATOM
32492
C4′
G A1516
−82.904
5.610
3.921
1.00
5.61
C


ATOM
32493
O4′
G A1516
−82.485
6.974
3.662
1.00
5.61
O


ATOM
32494
C3′
G A1516
−83.414
5.136
2.573
1.00
5.61
C


ATOM
32495
O3′
G A1516
−84.238
3.987
2.648
1.00
5.61
O


ATOM
32496
C2′
G A1516
−84.124
6.371
2.060
1.00
5.61
C


ATOM
32497
O2′
G A1516
−85.380
6.519
2.693
1.00
5.61
O


ATOM
32498
C1′
G A1516
−83.185
7.482
2.550
1.00
5.61
C


ATOM
32499
N9
G A1516
−82.218
7.834
1.516
1.00
5.64
N


ATOM
32500
C8
G A1516
−80.895
7.517
1.408
1.00
5.64
C


ATOM
32501
N7
G A1516
−80.369
7.946
0.287
1.00
5.64
N


ATOM
32502
C5
G A1516
−81.436
8.535
−0.366
1.00
5.64
C


ATOM
32503
C6
G A1516
−81.514
9.151
−1.614
1.00
5.64
C


ATOM
32504
O6
G A1516
−80.569
9.310
−2.403
1.00
5.64
O


ATOM
32505
N1
G A1516
−82.796
9.606
−1.902
1.00
5.64
N


ATOM
32506
C2
G A1516
−83.868
9.479
−1.090
1.00
5.64
C


ATOM
32507
N2
G A1516
−85.040
9.958
−1.478
1.00
5.64
N


ATOM
32508
N3
G A1516
−83.804
8.910
0.074
1.00
5.64
N


ATOM
32509
C4
G A1516
−82.571
8.467
0.369
1.00
5.64
C


ATOM
32510
P
G A1517
−84.128
2.853
1.506
1.00
8.95
P


ATOM
32511
OP1
G A1517
−84.956
1.700
1.947
1.00
8.95
O


ATOM
32512
OP2
G A1517
−82.680
2.627
1.226
1.00
8.95
O


ATOM
32513
O5′
G A1517
−84.820
3.557
0.270
1.00
8.95
O


ATOM
32514
C5′
G A1517
−86.228
3.744
0.253
1.00
8.95
C


ATOM
32515
C4′
G A1517
−86.790
3.530
−1.123
1.00
8.95
C


ATOM
32516
O4′
G A1517
−88.194
3.199
−1.023
1.00
8.95
O


ATOM
32517
C3′
G A1517
−86.761
4.739
−2.032
1.00
8.95
C


ATOM
32518
O3′
G A1517
−85.521
4.917
−2.667
1.00
8.95
O


ATOM
32519
C2′
G A1517
−87.896
4.462
−2.985
1.00
8.95
C


ATOM
32520
O2′
G A1517
−87.522
3.473
−3.933
1.00
8.95
O


ATOM
32521
C1′
G A1517
−88.913
3.857
−2.037
1.00
8.95
C


ATOM
32522
N9
G A1517
−89.758
4.879
−1.401
1.00
8.51
N


ATOM
32523
C8
G A1517
−89.727
5.231
−0.072
1.00
8.51
C


ATOM
32524
N7
G A1517
−90.600
6.159
0.250
1.00
8.51
N


ATOM
32525
C5
G A1517
−91.241
6.408
−0.944
1.00
8.51
C


ATOM
32526
C6
G A1517
−92.272
7.302
−1.224
1.00
8.51
C


ATOM
32527
O6
G A1517
−92.831
8.057
−0.466
1.00
8.51
O


ATOM
32528
N1
G A1517
−92.656
7.272
−2.528
1.00
8.51
N


ATOM
32529
C2
G A1517
−92.085
6.475
−3.457
1.00
8.51
C


ATOM
32530
N2
G A1517
−92.588
6.601
−4.681
1.00
8.51
N


ATOM
32531
N3
G A1517
−91.109
5.626
−3.234
1.00
8.51
N


ATOM
32532
C4
G A1517
−90.741
5.638
−1.962
1.00
8.51
C


ATOM
32533
P
A A1518
−84.783
6.329
−2.553
1.00
8.03
P


ATOM
32534
OP1
A A1518
−83.411
6.148
−3.107
1.00
8.03
O


ATOM
32535
OP2
A A1518
−84.952
6.797
−1.157
1.00
8.03
O


ATOM
32536
O5′
A A1518
−85.626
7.247
−3.506
1.00
8.03
O


ATOM
32537
C5′
A A1518
−85.517
7.125
−4.890
1.00
8.03
C


ATOM
32538
C4′
A A1518
−86.576
7.930
−5.535
1.00
8.03
C


ATOM
32539
O4′
A A1518
−87.850
7.546
−4.975
1.00
8.03
O


ATOM
32540
C3′
A A1518
−86.488
9.412
−5.267
1.00
8.03
C


ATOM
32541
O3′
A A1518
−85.581
10.062
−6.140
1.00
8.03
O


ATOM
32542
C2′
A A1518
−87.930
9.857
−5.421
1.00
8.03
C


ATOM
32543
O2′
A A1518
−88.283
9.923
−6.795
1.00
8.03
O


ATOM
32544
C1′
A A1518
−88.662
8.676
−4.798
1.00
8.03
C


ATOM
32545
N9
A A1518
−88.891
8.837
−3.354
1.00
8.10
N


ATOM
32546
C8
A A1518
−88.133
8.263
−2.353
1.00
8.10
C


ATOM
32547
N7
A A1518
−88.576
8.547
−1.141
1.00
8.10
N


ATOM
32548
C5
A A1518
−89.722
9.325
−1.361
1.00
8.10
C


ATOM
32549
C6
A A1518
−90.650
9.937
−0.485
1.00
8.10
C


ATOM
32550
N6
A A1518
−90.594
9.867
0.847
1.00
8.10
N


ATOM
32551
N1
A A1518
−91.657
10.642
−1.054
1.00
8.10
N


ATOM
32552
C2
A A1518
−91.731
10.715
−2.390
1.00
8.10
C


ATOM
32553
N3
A A1518
−90.925
10.189
−3.310
1.00
8.10
N


ATOM
32554
C4
A A1518
−89.930
9.500
−2.730
1.00
8.10
C


TER


ATOM
40759
P
G A1903
−77.149
−18.965
16.920
1.00
1.59
P


ATOM
40760
OP1
G A1903
−77.353
−20.402
16.624
1.00
1.59
O


ATOM
40761
OP2
G A1903
−76.245
−18.169
16.052
1.00
1.59
O


ATOM
40762
O5′
G A1903
−78.554
−18.232
17.082
1.00
1.59
O


ATOM
40763
C5′
G A1903
−79.415
−17.998
15.987
1.00
1.59
C


ATOM
40764
C4′
G A1903
−80.810
−17.639
16.459
1.00
1.59
C


ATOM
40765
O4′
G A1903
−80.749
−16.623
17.512
1.00
1.59
O


ATOM
40766
C3′
G A1903
−81.733
−17.049
15.404
1.00
1.59
C


ATOM
40767
O3′
G A1903
−82.405
−18.042
14.682
1.00
1.59
O


ATOM
40768
C2′
G A1903
−82.668
−16.173
16.217
1.00
1.59
C


ATOM
40769
O2′
G A1903
−83.662
−16.958
16.836
1.00
1.59
O


ATOM
40770
C1′
G A1903
−81.730
−15.634
17.291
1.00
1.59
C


ATOM
40771
N9
G A1903
−81.042
−14.423
16.829
1.00
1.70
N


ATOM
40772
C8
G A1903
−79.720
−14.396
16.503
1.00
1.70
C


ATOM
40773
N7
G A1903
−79.323
−13.244
16.069
1.00
1.70
N


ATOM
40774
C5
G A1903
−80.457
−12.458
16.092
1.00
1.70
C


ATOM
40775
C6
G A1903
−80.617
−11.092
15.729
1.00
1.70
C


ATOM
40776
O6
G A1903
−79.777
−10.285
15.301
1.00
1.70
O


ATOM
40777
N1
G A1903
−81.917
−10.686
15.887
1.00
1.70
N


ATOM
40778
C2
G A1903
−82.903
−11.490
16.333
1.00
1.70
C


ATOM
40779
N2
G A1903
−84.074
−10.873
16.392
1.00
1.70
N


ATOM
40780
N3
G A1903
−82.785
−12.761
16.696
1.00
1.70
N


ATOM
40781
C4
G A1903
−81.530
−13.184
16.545
1.00
1.70
C


ATOM
40782
P
G A1904
−82.389
−18.034
13.095
1.00
15.24
P


ATOM
40783
OP1
G A1904
−82.621
−19.429
12.662
1.00
15.24
O


ATOM
40784
OP2
G A1904
−81.167
−17.351
12.660
1.00
15.24
O


ATOM
40785
O5′
G A1904
−83.649
−17.153
12.758
1.00
15.24
O


ATOM
40786
C5′
G A1904
−84.894
−17.439
13.376
1.00
15.24
C


ATOM
40787
C4′
G A1904
−85.865
−16.304
13.217
1.00
15.24
C


ATOM
40788
O4′
G A1904
−85.530
−15.238
14.129
1.00
15.24
O


ATOM
40789
C3′
G A1904
−85.875
−15.627
11.865
1.00
15.24
C


ATOM
40790
O3′
G A1904
−86.607
−16.337
10.904
1.00
15.24
O


ATOM
40791
C2′
G A1904
−86.494
−14.317
12.206
1.00
15.24
C


ATOM
40792
O2′
G A1904
−87.866
−14.517
12.497
1.00
15.24
O


ATOM
40793
C1′
G A1904
−85.780
−14.009
13.510
1.00
15.24
C


ATOM
40794
N9
G A1904
−84.486
−13.322
13.298
1.00
15.28
N


ATOM
40795
C8
G A1904
−83.250
−13.814
13.634
1.00
15.28
C


ATOM
40796
N7
G A1904
−82.284
−12.988
13.375
1.00
15.28
N


ATOM
40797
C5
G A1904
−82.914
−11.868
12.848
1.00
15.28
C


ATOM
40798
C6
G A1904
−82.387
−10.645
12.367
1.00
15.28
C


ATOM
40799
O6
G A1904
−81.236
−10.247
12.291
1.00
15.28
O


ATOM
40800
N1
G A1904
−83.336
−9.785
11.915
1.00
15.28
N


ATOM
40801
C2
G A1904
−84.656
−10.056
11.921
1.00
15.28
C


ATOM
40802
N2
G A1904
−85.404
−9.057
11.424
1.00
15.28
N


ATOM
40803
N3
G A1904
−85.190
−11.187
12.357
1.00
15.28
N


ATOM
40804
C4
G A1904
−84.264
−12.051
12.805
1.00
15.28
C


ATOM
40805
P
C A1905
−86.064
−16.416
9.417
1.00
12.32
P


ATOM
40806
OP1
C A1905
−86.932
−17.354
8.669
1.00
12.32
O


ATOM
40807
OP2
C A1905
−84.602
−16.700
9.498
1.00
12.32
O


ATOM
40808
O5′
C A1905
−86.301
−14.940
8.906
1.00
12.32
O


ATOM
40809
C5′
C A1905
−87.558
−14.325
9.064
1.00
12.32
C


ATOM
40810
C4′
C A1905
−87.505
−12.908
8.616
1.00
12.32
C


ATOM
40811
O4′
C A1905
−86.525
−12.205
9.397
1.00
12.32
O


ATOM
40812
C3′
C A1905
−87.066
−12.702
7.190
1.00
12.32
C


ATOM
40813
O3′
C A1905
−88.132
−12.865
6.287
1.00
12.32
O


ATOM
40814
C2′
C A1905
−86.505
−11.297
7.208
1.00
12.32
C


ATOM
40815
O2′
C A1905
−87.548
−10.354
7.078
1.00
12.32
O


ATOM
40816
C1′
C A1905
−85.942
−11.194
8.627
1.00
12.32
C


ATOM
40817
N1
C A1905
−84.468
−11.341
8.696
1.00
13.11
N


ATOM
40818
C2
C A1905
−83.623
−10.390
8.109
1.00
13.11
C


ATOM
40819
O2
C A1905
−84.161
−9.480
7.460
1.00
13.11
O


ATOM
40820
N3
C A1905
−82.272
−10.491
8.213
1.00
13.11
N


ATOM
40821
C4
C A1905
−81.760
−11.491
8.909
1.00
13.11
C


ATOM
40822
N4
C A1905
−80.430
−11.593
9.012
1.00
13.11
N


ATOM
40823
C5
C A1905
−82.600
−12.449
9.549
1.00
13.11
C


ATOM
40824
C6
C A1905
−83.927
−12.341
9.429
1.00
13.11
C


ATOM
40825
P
G A1906
−87.983
−13.826
5.008
1.00
33.88
P


ATOM
40826
OP1
G A1906
−86.784
−14.680
5.212
1.00
33.88
O


ATOM
40827
OP2
G A1906
−88.039
−12.965
3.818
1.00
33.88
O


ATOM
40828
O5′
G A1906
−89.283
−14.724
5.089
1.00
33.88
O


ATOM
40829
C5′
G A1906
−90.556
−14.187
4.805
1.00
33.88
C


ATOM
40830
C4′
G A1906
−91.611
−14.868
5.623
1.00
33.88
C


ATOM
40831
O4′
G A1906
−91.809
−14.152
6.869
1.00
33.88
O


ATOM
40832
C3′
G A1906
−92.988
−14.927
5.006
1.00
33.88
C


ATOM
40833
O3′
G A1906
−93.118
−15.984
4.081
1.00
33.88
O


ATOM
40834
C2′
G A1906
−93.889
−15.059
6.229
1.00
33.88
C


ATOM
40835
O2′
G A1906
−93.874
−16.386
6.741
1.00
33.88
O


ATOM
40836
C1′
G A1906
−93.171
−14.161
7.220
1.00
33.88
C


ATOM
40837
N9
G A1906
−93.666
−12.780
7.175
1.00
33.83
N


ATOM
40838
C8
G A1906
−93.015
−11.685
6.689
1.00
33.83
C


ATOM
40839
N7
G A1906
−93.699
−10.589
6.816
1.00
33.83
N


ATOM
40840
C5
G A1906
−94.870
−10.989
7.432
1.00
33.83
C


ATOM
40841
C6
G A1906
−96.016
−10.252
7.833
1.00
33.83
C


ATOM
40842
O6
G A1906
−96.273
−9.037
7.734
1.00
33.83
O


ATOM
40843
N1
G A1906
−96.956
−11.082
8.416
1.00
33.83
N


ATOM
40844
C2
G A1906
−96.818
−12.423
8.586
1.00
33.83
C


ATOM
40845
N2
G A1906
−97.845
−13.047
9.172
1.00
33.83
N


ATOM
40846
N3
G A1906
−95.765
−13.109
8.212
1.00
33.83
N


ATOM
40847
C4
G A1906
−94.846
−12.334
7.655
1.00
33.83
C


ATOM
40848
P
G A1907
−93.834
−15.733
2.668
1.00
44.42
P


ATOM
40849
OP1
G A1907
−94.331
−17.051
2.204
1.00
44.42
O


ATOM
40850
OP2
G A1907
−92.878
−14.979
1.809
1.00
44.42
O


ATOM
40851
O5′
G A1907
−95.058
−14.809
3.051
1.00
44.42
O


ATOM
40852
C5′
G A1907
−96.350
−15.115
2.581
1.00
44.42
C


ATOM
40853
C4′
G A1907
−97.194
−15.712
3.665
1.00
44.42
C


ATOM
40854
O4′
G A1907
−96.841
−15.100
4.932
1.00
44.42
O


ATOM
40855
C3′
G A1907
−98.690
−15.469
3.526
1.00
44.42
C


ATOM
40856
O3′
G A1907
−99.331
−16.425
2.708
1.00
44.42
O


ATOM
40857
C2′
G A1907
−99.167
−15.451
4.965
1.00
44.42
C


ATOM
40858
O2′
G A1907
−99.225
−16.764
5.493
1.00
44.42
O


ATOM
40859
C1′
G A1907
−98.008
−14.716
5.626
1.00
44.42
C


ATOM
40860
N9
G A1907
−98.152
−13.240
5.510
1.00
43.98
N


ATOM
40861
C8
G A1907
−97.273
−12.318
4.956
1.00
43.98
C


ATOM
40862
N7
G A1907
−97.701
−11.084
4.995
1.00
43.98
N


ATOM
40863
C5
G A1907
−98.942
−11.193
5.609
1.00
43.98
C


ATOM
40864
C6
G A1907
−99.899
−10.202
5.933
1.00
43.98
C


ATOM
40865
O6
G A1907
−99.820
−8.993
5.718
1.00
43.98
O


ATOM
40866
N1
G A1907
−101.028
−10.751
6.550
1.00
43.98
N


ATOM
40867
C2
G A1907
−101.216
−12.090
6.825
1.00
43.98
C


ATOM
40868
N2
G A1907
−102.362
−12.444
7.428
1.00
43.98
N


ATOM
40869
N3
G A1907
−100.334
−13.023
6.528
1.00
43.98
N


ATOM
40870
C4
G A1907
−99.234
−12.507
5.931
1.00
43.98
C


ATOM
40871
P
C A1908
−99.500
−16.147
1.131
1.00
35.91
P


ATOM
40872
OP1
C A1908
−100.406
−17.193
0.602
1.00
35.91
O


ATOM
40873
OP2
C A1908
−98.150
−16.020
0.549
1.00
35.91
O


ATOM
40874
O5′
C A1908
−100.215
−14.738
1.099
1.00
35.91
O


ATOM
40875
C5′
C A1908
−101.468
−14.582
0.480
1.00
35.91
C


ATOM
40876
C4′
C A1908
−102.581
−14.537
1.491
1.00
35.91
C


ATOM
40877
O4′
C A1908
−102.037
−14.307
2.825
1.00
35.91
O


ATOM
40878
C3′
C A1908
−103.580
−13.407
1.289
1.00
35.91
C


ATOM
40879
O3′
C A1908
−104.591
−13.730
0.363
1.00
35.91
O


ATOM
40880
C2′
C A1908
−104.070
−13.135
2.694
1.00
35.91
C


ATOM
40881
O2′
C A1908
−104.961
−14.154
3.125
1.00
35.91
O


ATOM
40882
C1′
C A1908
−102.758
−13.274
3.454
1.00
35.91
C


ATOM
40883
N1
C A1908
−101.945
−12.053
3.343
1.00
35.20
N


ATOM
40884
C2
C A1908
−102.453
−10.796
3.662
1.00
35.20
C


ATOM
40885
O2
C A1908
−103.619
−10.707
4.069
1.00
35.20
O


ATOM
40886
N3
C A1908
−101.638
−9.723
3.517
1.00
35.20
N


ATOM
40887
C4
C A1908
−100.389
−9.890
3.065
1.00
35.20
C


ATOM
40888
N4
C A1908
−99.588
−8.845
2.932
1.00
35.20
N


ATOM
40889
C5
C A1908
−99.860
−11.147
2.719
1.00
35.20
C


ATOM
40890
C6
C A1908
−100.672
−12.188
2.866
1.00
35.20
C


ATOM
40891
P
C A1909
−104.213
−13.874
−1.194
1.00
33.41
P


ATOM
40892
OP1
C A1909
−104.593
−15.249
−1.604
1.00
33.41
O


ATOM
40893
OP2
C A1909
−102.794
−13.433
−1.368
1.00
33.41
O


ATOM
40894
O5′
C A1909
−105.166
−12.812
−1.874
1.00
33.41
O


ATOM
40895
C5′
C A1909
−104.851
−11.438
−1.817
1.00
33.41
C


ATOM
40896
C4′
C A1909
−105.818
−10.683
−0.951
1.00
33.41
C


ATOM
40897
O4′
C A1909
−105.330
−10.657
0.420
1.00
33.41
O


ATOM
40898
C3′
C A1909
−105.994
−9.219
−1.330
1.00
33.41
C


ATOM
40899
O3′
C A1909
−106.998
−9.029
−2.288
1.00
33.41
O


ATOM
40900
C2′
C A1909
−106.274
−8.549
−0.011
1.00
33.41
C


ATOM
40901
O2′
C A1909
−107.611
−8.791
0.396
1.00
33.41
O


ATOM
40902
C1′
C A1909
−105.321
−9.328
0.890
1.00
33.41
C


ATOM
40903
N1
C A1909
−103.922
−8.821
0.760
1.00
33.15
N


ATOM
40904
C2
C A1909
−103.596
−7.454
0.808
1.00
33.15
C


ATOM
40905
O2
C A1909
−104.469
−6.613
1.014
1.00
33.15
O


ATOM
40906
N3
C A1909
−102.318
−7.075
0.644
1.00
33.15
N


ATOM
40907
C4
C A1909
−101.377
−7.995
0.423
1.00
33.15
C


ATOM
40908
N4
C A1909
−100.110
−7.609
0.256
1.00
33.15
N


ATOM
40909
C5
C A1909
−101.664
−9.383
0.352
1.00
33.15
C


ATOM
40910
C6
C A1909
−102.937
−9.745
0.512
1.00
33.15
C


ATOM
40911
P
G A1910
−106.609
−8.971
−3.844
1.00
37.29
P


ATOM
40912
OP1
G A1910
−107.608
−9.802
−4.576
1.00
37.29
O


ATOM
40913
OP2
G A1910
−105.174
−9.324
−3.952
1.00
37.29
O


ATOM
40914
O5′
G A1910
−106.819
−7.431
−4.181
1.00
37.29
O


ATOM
40915
C5′
G A1910
−107.827
−6.699
−3.510
1.00
37.29
C


ATOM
40916
C4′
G A1910
−107.428
−5.269
−3.273
1.00
37.29
C


ATOM
40917
O4′
G A1910
−106.515
−5.162
−2.146
1.00
37.28
O


ATOM
40918
C3′
G A1910
−106.674
−4.597
−4.383
1.00
37.28
C


ATOM
40919
O3′
G A1910
−107.485
−4.285
−5.485
1.00
37.28
O


ATOM
40920
C2′
G A1910
−106.096
−3.392
−3.662
1.00
37.28
C


ATOM
40921
O2′
G A1910
−107.100
−2.432
−3.389
1.00
37.28
O


ATOM
40922
C1′
G A1910
−105.674
−4.038
−2.342
1.00
37.29
C


ATOM
40923
N9
G A1910
−104.280
−4.492
−2.406
1.00
36.74
N


ATOM
40924
C8
G A1910
−103.758
−5.740
−2.573
1.00
36.74
C


ATOM
40925
N7
G A1910
−102.460
−5.721
−2.627
1.00
36.74
N


ATOM
40926
C5
G A1910
−102.111
−4.387
−2.513
1.00
36.74
C


ATOM
40927
C6
G A1910
−100.846
−3.733
−2.501
1.00
36.74
C


ATOM
40928
O6
G A1910
−99.706
−4.210
−2.601
1.00
36.74
O


ATOM
40929
N1
G A1910
−101.000
−2.353
−2.347
1.00
36.74
N


ATOM
40930
C2
G A1910
−102.207
−1.685
−2.223
1.00
36.74
C


ATOM
40931
N2
G A1910
−102.170
−0.349
−2.085
1.00
36.74
N


ATOM
40932
N3
G A1910
−103.381
−2.290
−2.232
1.00
36.74
N


ATOM
40933
C4
G A1910
−103.242
−3.624
−2.380
1.00
36.74
C


ATOM
40934
P
U A1911
−106.908
−4.492
−6.962
1.00
41.32
P


ATOM
40935
OP1
U A1911
−108.063
−4.501
−7.885
1.00
41.32
O


ATOM
40936
OP2
U A1911
−106.012
−5.673
−6.925
1.00
41.32
O


ATOM
40937
O5′
U A1911
−106.063
−3.167
−7.165
1.00
41.32
O


ATOM
40938
C5′
U A1911
−106.529
−1.944
−6.624
1.00
41.32
C


ATOM
40939
C4′
U A1911
−105.443
−0.914
−6.584
1.00
41.32
C


ATOM
40940
O4′
U A1911
−104.510
−1.221
−5.528
1.00
41.32
O


ATOM
40941
C3′
U A1911
−104.583
−0.831
−7.818
1.00
41.32
C


ATOM
40942
O3′
U A1911
−105.202
−0.108
−8.848
1.00
41.32
O


ATOM
40943
C2′
U A1911
−103.318
−0.180
−7.298
1.00
41.32
C


ATOM
40944
O2′
U A1911
−103.486
1.227
−7.187
1.00
41.32
O


ATOM
40945
C1′
U A1911
−103.224
−0.772
−5.890
1.00
41.32
C


ATOM
40946
N1
U A1911
−102.268
−1.909
−5.807
1.00
41.23
N


ATOM
40947
C2
U A1911
−100.939
−1.553
−5.624
1.00
41.23
C


ATOM
40948
O2
U A1911
−100.552
−0.397
−5.566
1.00
41.23
O


ATOM
40949
N3
U A1911
−100.067
−2.604
−5.536
1.00
41.23
N


ATOM
40950
C4
U A1911
−100.378
−3.941
−5.600
1.00
41.23
C


ATOM
40951
O4
U A1911
−99.450
−4.734
−5.501
1.00
41.23
O


ATOM
40952
C5
U A1911
−101.768
−4.251
−5.775
1.00
41.23
C


ATOM
40953
C6
U A1911
−102.648
−3.242
−5.867
1.00
41.23
C


ATOM
40954
P
A A1912
−104.946
−0.526
−10.364
1.00
28.49
P


ATOM
40955
OP1
A A1912
−105.973
0.165
−11.203
1.00
28.49
O


ATOM
40956
OP2
A A1912
−104.874
−2.011
−10.392
1.00
28.49
O


ATOM
40957
O5′
A A1912
−103.508
0.089
−10.651
1.00
28.49
O


ATOM
40958
C5′
A A1912
−103.253
1.459
−10.428
1.00
28.49
C


ATOM
40959
C4′
A A1912
−102.201
1.975
−11.359
1.00
28.49
C


ATOM
40960
O4′
A A1912
−100.904
1.750
−10.791
1.00
28.49
O


ATOM
40961
C3′
A A1912
−102.121
1.313
−12.720
1.00
28.49
C


ATOM
40962
O3′
A A1912
−103.097
1.813
−13.629
1.00
28.49
O


ATOM
40963
C2′
A A1912
−100.675
1.588
−13.151
1.00
28.49
C


ATOM
40964
O2′
A A1912
−100.578
2.803
−13.874
1.00
28.49
O


ATOM
40965
C1′
A A1912
−99.950
1.760
−11.812
1.00
28.49
C


ATOM
40966
N9
A A1912
−98.962
0.708
−11.550
1.00
27.91
N


ATOM
40967
C8
A A1912
−98.969
−0.642
−11.765
1.00
27.91
C


ATOM
40968
N7
A A1912
−97.855
−1.213
−11.374
1.00
27.91
N


ATOM
40969
C5
A A1912
−97.081
−0.176
−10.869
1.00
27.91
C


ATOM
40970
C6
A A1912
−95.802
−0.104
−10.297
1.00
27.91
C


ATOM
40971
N6
A A1912
−94.984
−1.143
−10.104
1.00
27.91
N


ATOM
40972
N1
A A1912
−95.362
1.109
−9.925
1.00
27.91
N


ATOM
40973
C2
A A1912
−96.144
2.168
−10.106
1.00
27.91
C


ATOM
40974
N3
A A1912
−97.354
2.223
−10.628
1.00
27.91
N


ATOM
40975
C4
A A1912
−97.760
1.006
−10.986
1.00
27.91
C


ATOM
40976
P
A A1913
−103.317
1.105
−15.057
1.00
66.34
P


ATOM
40977
OP1
A A1913
−104.778
0.948
−15.242
1.00
66.34
O


ATOM
40978
OP2
A A1913
−102.463
−0.102
−15.082
1.00
66.34
O


ATOM
40979
O5′
A A1913
−102.752
2.179
−16.079
1.00
66.34
O


ATOM
40980
C5′
A A1913
−103.582
3.221
−16.571
1.00
66.34
C


ATOM
40981
C4′
A A1913
−103.815
3.087
−18.053
1.00
66.34
C


ATOM
40982
O4′
A A1913
−102.818
3.865
−18.761
1.00
66.34
O


ATOM
40983
C3′
A A1913
−103.711
1.660
−18.599
1.00
66.34
C


ATOM
40984
O3′
A A1913
−104.674
1.466
−19.643
1.00
66.34
O


ATOM
40985
C2′
A A1913
−102.293
1.611
−19.167
1.00
66.34
C


ATOM
40986
O2′
A A1913
−102.082
0.659
−20.196
1.00
66.34
O


ATOM
40987
C1′
A A1913
−102.122
3.033
−19.670
1.00
66.34
C


ATOM
40988
N9
A A1913
−100.735
3.471
−19.715
1.00
67.09
N


ATOM
40989
C8
A A1913
−99.646
2.711
−20.091
1.00
67.09
C


ATOM
40990
N7
A A1913
−98.520
3.373
−20.051
1.00
67.09
N


ATOM
40991
C5
A A1913
−98.915
4.639
−19.613
1.00
67.09
C


ATOM
40992
C6
A A1913
−98.165
5.788
−19.369
1.00
67.09
C


ATOM
40993
N6
A A1913
−96.834
5.774
−19.554
1.00
67.09
N


ATOM
40994
N1
A A1913
−98.847
6.886
−18.939
1.00
67.08
N


ATOM
40995
C2
A A1913
−100.181
6.816
−18.779
1.00
67.09
C


ATOM
40996
N3
A A1913
−100.997
5.790
−18.980
1.00
67.09
N


ATOM
40997
C4
A A1913
−100.281
4.725
−19.396
1.00
67.09
C


ATOM
40998
P
C A1914
−105.960
0.510
−19.393
1.00
64.06
P


ATOM
40999
OP1
C A1914
−107.182
1.338
−19.641
1.00
64.06
O


ATOM
41000
OP2
C A1914
−105.784
−0.128
−18.050
1.00
64.06
O


ATOM
41001
O5′
C A1914
−105.798
−0.595
−20.531
1.00
64.06
O


ATOM
41002
C5′
C A1914
−104.513
−1.078
−20.891
1.00
64.06
C


ATOM
41003
C4′
C A1914
−104.521
−2.567
−21.101
1.00
64.06
C


ATOM
41004
O4′
C A1914
−103.630
−2.911
−22.195
1.00
64.06
O


ATOM
41005
C3′
C A1914
−104.012
−3.413
−19.946
1.00
64.06
C


ATOM
41006
O3′
C A1914
−104.963
−3.584
−18.905
1.00
64.06
O


ATOM
41007
C2′
C A1914
−103.640
−4.707
−20.652
1.00
64.06
C


ATOM
41008
O2′
C A1914
−104.803
−5.458
−20.967
1.00
64.06
O


ATOM
41009
C1′
C A1914
−103.051
−4.176
−21.957
1.00
64.06
C


ATOM
41010
N1
C A1914
−101.568
−4.028
−21.902
1.00
63.15
N


ATOM
41011
C2
C A1914
−100.778
−4.976
−22.588
1.00
63.15
C


ATOM
41012
O2
C A1914
−101.322
−5.911
−23.202
1.00
63.15
O


ATOM
41013
N3
C A1914
−99.427
−4.874
−22.570
1.00
63.15
N


ATOM
41014
C4
C A1914
−98.845
−3.874
−21.911
1.00
63.15
C


ATOM
41015
N4
C A1914
−97.503
−3.826
−21.940
1.00
63.15
N


ATOM
41016
C5
C A1914
−99.622
−2.890
−21.209
1.00
63.15
C


ATOM
41017
C6
C A1914
−100.962
−2.998
−21.228
1.00
63.15
C


ATOM
41018
P
U A1915
−104.618
−4.540
−17.652
1.00
50.19
P


ATOM
41019
OP1
U A1915
−105.832
−4.587
−16.774
1.00
50.19
O


ATOM
41020
OP2
U A1915
−103.337
−4.051
−17.075
1.00
50.19
O


ATOM
41021
O5′
U A1915
−104.388
−5.960
−18.348
1.00
50.19
O


ATOM
41022
C5′
U A1915
−104.003
−7.098
−17.588
1.00
50.19
C


ATOM
41023
C4′
U A1915
−103.236
−8.090
−18.426
1.00
50.19
C


ATOM
41024
O4′
U A1915
−102.549
−7.397
−19.499
1.00
50.19
O


ATOM
41025
C3′
U A1915
−102.133
−8.844
−17.704
1.00
50.19
C


ATOM
41026
O3′
U A1915
−102.606
−9.956
−16.990
1.00
50.19
O


ATOM
41027
C2′
U A1915
−101.181
−9.208
−18.827
1.00
50.19
C


ATOM
41028
O2′
U A1915
−101.676
−10.310
−19.563
1.00
50.19
O


ATOM
41029
C1′
U A1915
−101.268
−7.963
−19.701
1.00
50.19
C


ATOM
41030
N1
U A1915
−100.226
−6.943
−19.339
1.00
50.55
N


ATOM
41031
C2
U A1915
−98.869
−7.294
−19.304
1.00
50.55
C


ATOM
41032
O2
U A1915
−98.424
−8.407
−19.545
1.00
50.55
O


ATOM
41033
N3
U A1915
−98.014
−6.275
−18.956
1.00
50.55
N


ATOM
41034
C4
U A1915
−98.338
−4.969
−18.647
1.00
50.55
C


ATOM
41035
O4
U A1915
−97.440
−4.178
−18.354
1.00
50.55
O


ATOM
41036
C5
U A1915
−99.737
−4.670
−18.700
1.00
50.55
C


ATOM
41037
C6
U A1915
−100.601
−5.640
−19.034
1.00
50.55
C


ATOM
41038
P
A A1916
−102.792
−9.865
−15.403
1.00
36.99
P


ATOM
41039
OP1
A A1916
−103.479
−11.101
−14.985
1.00
36.99
O


ATOM
41040
OP2
A A1916
−103.425
−8.556
−15.107
1.00
36.99
O


ATOM
41041
O5′
A A1916
−101.303
−9.883
−14.867
1.00
36.99
O


ATOM
41042
C5′
A A1916
−100.559
−11.079
−14.906
1.00
36.99
C


ATOM
41043
C4′
A A1916
−99.103
−10.807
−15.088
1.00
36.99
C


ATOM
41044
O4′
A A1916
−98.901
−9.886
−16.192
1.00
36.99
O


ATOM
41045
C3′
A A1916
−98.419
−10.135
−13.926
1.00
36.99
C


ATOM
41046
O3′
A A1916
−98.121
−11.031
−12.884
1.00
36.99
O


ATOM
41047
C2′
A A1916
−97.196
−9.536
−14.586
1.00
36.99
C


ATOM
41048
O2′
A A1916
−96.226
−10.531
−14.846
1.00
36.99
O


ATOM
41049
C1′
A A1916
−97.791
−9.060
−15.911
1.00
36.99
C


ATOM
41050
N9
A A1916
−98.264
−7.682
−15.790
1.00
37.66
N


ATOM
41051
C8
A A1916
−99.537
−7.185
−15.847
1.00
37.66
C


ATOM
41052
N7
A A1916
−99.593
−5.893
−15.623
1.00
37.66
N


ATOM
41053
C5
A A1916
−98.273
−5.534
−15.375
1.00
37.66
C


ATOM
41054
C6
A A1916
−97.663
−4.307
−15.072
1.00
37.66
C


ATOM
41055
N6
A A1916
−98.330
−3.155
−14.956
1.00
37.66
N


ATOM
41056
N1
A A1916
−96.323
−4.318
−14.887
1.00
37.66
N


ATOM
41057
C2
A A1916
−95.652
−5.480
−14.999
1.00
37.66
C


ATOM
41058
N3
A A1916
−96.117
−6.696
−15.285
1.00
37.66
N


ATOM
41059
C4
A A1916
−97.447
−6.640
−15.463
1.00
37.66
C


ATOM
41060
P
U A1917
−98.719
−10.782
−11.417
1.00
30.02
P


ATOM
41061
OP1
U A1917
−98.859
−12.125
−10.763
1.00
30.02
O


ATOM
41062
OP2
U A1917
−99.937
−9.918
−11.580
1.00
30.02
O


ATOM
41063
O5′
U A1917
−97.558
−9.957
−10.706
1.00
30.02
O


ATOM
41064
C5′
U A1917
−96.215
−10.394
−10.778
1.00
30.02
C


ATOM
41065
C4′
U A1917
−95.278
−9.239
−10.936
1.00
30.02
C


ATOM
41066
O4′
U A1917
−95.691
−8.425
−12.060
1.00
30.02
O


ATOM
41067
C3′
U A1917
−95.233
−8.266
−9.783
1.00
30.02
C


ATOM
41068
O3′
U A1917
−94.438
−8.723
−8.718
1.00
30.02
O


ATOM
41069
C2′
U A1917
−94.687
−7.026
−10.442
1.00
30.02
C


ATOM
41070
O2′
U A1917
−93.298
−7.156
−10.649
1.00
30.02
O


ATOM
41071
C1′
U A1917
−95.382
−7.076
−11.800
1.00
30.02
C


ATOM
41072
N1
U A1917
−96.642
−6.277
−11.816
1.00
30.05
N


ATOM
41073
C2
U A1917
−96.542
−4.920
−11.520
1.00
30.05
C


ATOM
41074
O2
U A1917
−95.484
−4.363
−11.260
1.00
30.05
O


ATOM
41075
N3
U A1917
−97.723
−4.228
−11.530
1.00
30.05
N


ATOM
41076
C4
U A1917
−98.963
−4.721
−11.815
1.00
30.05
C


ATOM
41077
O4
U A1917
−99.905
−3.945
−11.790
1.00
30.05
O


ATOM
41078
C5
U A1917
−99.017
−6.114
−12.114
1.00
30.05
C


ATOM
41079
C6
U A1917
−97.881
−6.825
−12.105
1.00
30.05
C


ATOM
41080
P
A A1918
−94.870
−8.410
−7.211
1.00
31.13
P


ATOM
41081
OP1
A A1918
−93.796
−8.908
−6.325
1.00
31.14
O


ATOM
41082
OP2
A A1918
−96.242
−8.926
−7.041
1.00
31.14
O


ATOM
41083
O5′
A A1918
−94.897
−6.831
−7.176
1.00
31.13
O


ATOM
41084
C5′
A A1918
−93.714
−6.074
−7.385
1.00
31.13
C


ATOM
41085
C4′
A A1918
−93.982
−4.607
−7.217
1.00
31.13
C


ATOM
41086
O4′
A A1918
−95.048
−4.223
−8.124
1.00
31.13
O


ATOM
41087
C3′
A A1918
−94.443
−4.204
−5.830
1.00
31.14
C


ATOM
41088
O3′
A A1918
−93.916
−2.927
−5.511
1.00
31.14
O


ATOM
41089
C2′
A A1918
−95.959
−4.124
−5.973
1.00
31.14
C


ATOM
41090
O2′
A A1918
−96.579
−3.244
−5.073
1.00
31.13
O


ATOM
41091
C1′
A A1918
−96.115
−3.650
−7.403
1.00
31.14
C


ATOM
41092
N9
A A1918
−97.369
−4.056
−8.037
1.00
31.95
N


ATOM
41093
C8
A A1918
−97.713
−5.286
−8.508
1.00
31.95
C


ATOM
41094
N7
A A1918
−98.908
−5.329
−9.053
1.00
31.95
N


ATOM
41095
C5
A A1918
−99.393
−4.041
−8.939
1.00
31.95
C


ATOM
41096
C6
A A1918
−100.611
−3.431
−9.321
1.00
31.95
C


ATOM
41097
N6
A A1918
−101.636
−4.038
−9.923
1.00
31.95
N


ATOM
41098
N1
A A1918
−100.761
−2.120
−9.070
1.00
31.95
N


ATOM
41099
C2
A A1918
−99.753
−1.479
−8.463
1.00
31.95
C


ATOM
41100
N3
A A1918
−98.572
−1.949
−8.055
1.00
31.95
N


ATOM
41101
C4
A A1918
−98.445
−3.254
−8.323
1.00
31.95
C


ATOM
41102
P
A A1919
−92.596
−2.812
−4.603
1.00
23.80
P


ATOM
41103
OP1
A A1919
−91.434
−3.220
−5.448
1.00
23.80
O


ATOM
41104
OP2
A A1919
−92.872
−3.558
−3.348
1.00
23.80
O


ATOM
41105
O5′
A A1919
−92.522
−1.247
−4.291
1.00
23.80
O


ATOM
41106
C5′
A A1919
−91.306
−0.622
−3.878
1.00
23.80
C


ATOM
41107
C4′
A A1919
−91.191
0.775
−4.441
1.00
23.80
C


ATOM
41108
O4′
A A1919
−91.456
0.723
−5.869
1.00
23.80
O


ATOM
41109
C3′
A A1919
−92.191
1.809
−3.915
1.00
23.80
C


ATOM
41110
O3′
A A1919
−91.774
2.445
−2.721
1.00
23.80
O


ATOM
41111
C2′
A A1919
−92.298
2.763
−5.091
1.00
23.80
C


ATOM
41112
O2′
A A1919
−91.130
3.567
−5.199
1.00
23.80
O


ATOM
41113
C1′
A A1919
−92.297
1.787
−6.248
1.00
23.80
C


ATOM
41114
N9
A A1919
−93.641
1.250
−6.494
1.00
23.52
N


ATOM
41115
C8
A A1919
−94.017
−0.045
−6.750
1.00
23.52
C


ATOM
41116
N7
A A1919
−95.311
−0.190
−6.886
1.00
23.52
N


ATOM
41117
C5
A A1919
−95.807
1.094
−6.697
1.00
23.52
C


ATOM
41118
C6
A A1919
−97.106
1.616
−6.712
1.00
23.52
C


ATOM
41119
N6
A A1919
−98.209
0.886
−6.937
1.00
23.52
N


ATOM
41120
N1
A A1919
−97.222
2.941
−6.486
1.00
23.52
N


ATOM
41121
C2
A A1919
−96.132
3.675
−6.273
1.00
23.52
C


ATOM
41122
N3
A A1919
−94.870
3.294
−6.244
1.00
23.52
N


ATOM
41123
C4
A A1919
−94.782
1.986
−6.457
1.00
23.52
C


ATOM
41124
P
C A1920
−92.289
1.931
−1.293
1.00
19.37
P


ATOM
41125
OP1
C A1920
−91.485
2.625
−0.268
1.00
19.37
O


ATOM
41126
OP2
C A1920
−92.276
0.452
−1.315
1.00
19.37
O


ATOM
41127
O5′
C A1920
−93.782
2.437
−1.245
1.00
19.37
O


ATOM
41128
C5′
C A1920
−94.190
3.559
−1.982
1.00
19.37
C


ATOM
41129
C4′
C A1920
−95.678
3.619
−2.048
1.00
19.37
C


ATOM
41130
O4′
C A1920
−96.144
2.780
−3.145
1.00
19.37
O


ATOM
41131
C3′
C A1920
−96.401
3.063
−0.839
1.00
19.37
C


ATOM
41132
O3′
C A1920
−96.446
3.959
0.266
1.00
19.37
O


ATOM
41133
C2′
C A1920
−97.760
2.703
−1.428
1.00
19.37
C


ATOM
41134
O2′
C A1920
−98.520
3.870
−1.707
1.00
19.37
O


ATOM
41135
C1′
C A1920
−97.325
2.093
−2.761
1.00
19.37
C


ATOM
41136
N1
C A1920
−97.021
0.609
−2.637
1.00
19.84
N


ATOM
41137
C2
C A1920
−98.087
−0.310
−2.527
1.00
19.84
C


ATOM
41138
O2
C A1920
−99.239
0.148
−2.565
1.00
19.84
O


ATOM
41139
N3
C A1920
−97.837
−1.652
−2.383
1.00
19.84
N


ATOM
41140
C4
C A1920
−96.566
−2.111
−2.347
1.00
19.84
C


ATOM
41141
N4
C A1920
−96.329
−3.423
−2.194
1.00
19.84
N


ATOM
41142
C5
C A1920
−95.459
−1.211
−2.466
1.00
19.84
C


ATOM
41143
C6
C A1920
−95.726
0.108
−2.596
1.00
19.84
C


ATOM
41144
P
G A1921
−96.436
3.384
1.780
1.00
18.78
P


ATOM
41145
OP1
G A1921
−96.230
4.534
2.694
1.00
18.78
O


ATOM
41146
OP2
G A1921
−95.478
2.269
1.817
1.00
18.78
O


ATOM
41147
O5′
G A1921
−97.911
2.840
1.940
1.00
18.78
O


ATOM
41148
C5′
G A1921
−99.002
3.681
1.620
1.00
18.78
C


ATOM
41149
C4′
G A1921
−100.311
2.969
1.752
1.00
18.78
C


ATOM
41150
O4′
G A1921
−100.514
2.107
0.610
1.00
18.78
O


ATOM
41151
C3′
G A1921
−100.440
2.031
2.933
1.00
18.78
C


ATOM
41152
O3′
G A1921
−100.716
2.694
4.146
1.00
18.78
O


ATOM
41153
C2′
G A1921
−101.552
1.112
2.475
1.00
18.78
C


ATOM
41154
O2′
G A1921
−102.806
1.771
2.517
1.00
18.78
O


ATOM
41155
C1′
G A1921
−101.170
0.926
1.022
1.00
18.78
C


ATOM
41156
N9
G A1921
−100.251
−0.200
0.862
1.00
19.32
N


ATOM
41157
C8
G A1921
−98.887
−0.187
0.823
1.00
19.32
C


ATOM
41158
N7
G A1921
−98.383
−1.377
0.681
1.00
19.32
N


ATOM
41159
C5
G A1921
−99.489
−2.193
0.645
1.00
19.32
C


ATOM
41160
C6
G A1921
−99.580
−3.581
0.507
1.00
19.32
C


ATOM
41161
O6
G A1921
−98.652
−4.381
0.389
1.00
19.32
O


ATOM
41162
N1
G A1921
−100.900
−4.024
0.514
1.00
19.32
N


ATOM
41163
C2
G A1921
−102.002
−3.225
0.644
1.00
19.32
C


ATOM
41164
N2
G A1921
−103.189
−3.849
0.632
1.00
19.32
N


ATOM
41165
N3
G A1921
−101.925
−1.914
0.765
1.00
19.32
N


ATOM
41166
C4
G A1921
−100.648
−1.488
0.758
1.00
19.32
C


ATOM
41167
P
G A1922
−100.684
1.881
5.528
1.00
37.73
P


ATOM
41168
OP1
G A1922
−100.369
2.855
6.593
1.00
37.73
O


ATOM
41169
OP2
G A1922
−99.793
0.711
5.340
1.00
37.73
O


ATOM
41170
O5′
G A1922
−102.177
1.394
5.675
1.00
37.73
O


ATOM
41171
C5′
G A1922
−102.487
0.279
6.468
1.00
37.73
C


ATOM
41172
C4′
G A1922
−103.640
−0.478
5.895
1.00
37.73
C


ATOM
41173
O4′
G A1922
−103.377
−0.801
4.509
1.00
37.73
O


ATOM
41174
C3′
G A1922
−103.912
−1.812
6.542
1.00
37.73
C


ATOM
41175
O3′
G A1922
−104.661
−1.685
7.713
1.00
37.73
O


ATOM
41176
C2′
G A1922
−104.606
−2.584
5.442
1.00
37.73
C


ATOM
41177
O2′
G A1922
−105.954
−2.157
5.291
1.00
37.73
O


ATOM
41178
C1′
G A1922
−103.808
−2.118
4.236
1.00
37.73
C


ATOM
41179
N9
G A1922
−102.614
−2.945
4.037
1.00
38.39
N


ATOM
41180
C8
G A1922
−101.348
−2.433
3.988
1.00
38.39
C


ATOM
41181
N7
G A1922
−100.440
−3.342
3.811
1.00
38.39
N


ATOM
41182
C5
G A1922
−101.153
−4.531
3.753
1.00
38.39
C


ATOM
41183
C6
G A1922
−100.665
−5.854
3.581
1.00
38.39
C


ATOM
41184
O6
G A1922
−99.480
−6.206
3.445
1.00
38.39
O


ATOM
41185
N1
G A1922
−101.721
−6.768
3.572
1.00
38.39
N


ATOM
41186
C2
G A1922
−103.050
−6.446
3.719
1.00
38.39
C


ATOM
41187
N2
G A1922
−103.899
−7.485
3.686
1.00
38.39
N


ATOM
41188
N3
G A1922
−103.507
−5.210
3.887
1.00
38.39
N


ATOM
41189
C4
G A1922
−102.509
−4.305
3.894
1.00
38.39
C


ATOM
41190
P
U A1923
−103.917
−1.629
9.118
1.00
33.93
P


ATOM
41191
OP1
U A1923
−104.740
−0.762
10.004
1.00
33.93
O


ATOM
41192
OP2
U A1923
−102.500
−1.249
8.862
1.00
33.93
O


ATOM
41193
O5′
U A1923
−104.007
−3.144
9.583
1.00
33.93
O


ATOM
41194
C5′
U A1923
−105.225
−3.855
9.443
1.00
33.93
C


ATOM
41195
C4′
U A1923
−105.005
−5.239
8.908
1.00
33.93
C


ATOM
41196
O4′
U A1923
−104.275
−5.176
7.672
1.00
33.93
O


ATOM
41197
C3′
U A1923
−104.183
−6.163
9.786
1.00
33.93
C


ATOM
41198
O3′
U A1923
−104.964
−6.765
10.798
1.00
33.93
O


ATOM
41199
C2′
U A1923
−103.602
−7.170
8.798
1.00
33.93
C


ATOM
41200
O2′
U A1923
−104.463
−8.288
8.634
1.00
33.93
O


ATOM
41201
C1′
U A1923
−103.554
−6.369
7.487
1.00
33.93
C


ATOM
41202
N1
U A1923
−102.187
−6.033
7.091
1.00
34.23
N


ATOM
41203
C2
U A1923
−101.272
−7.060
7.048
1.00
34.23
C


ATOM
41204
O2
U A1923
−101.560
−8.213
7.328
1.00
34.23
O


ATOM
41205
N3
U A1923
−100.010
−6.678
6.675
1.00
34.23
N


ATOM
41206
C4
U A1923
−99.593
−5.407
6.343
1.00
34.23
C


ATOM
41207
O4
U A1923
−98.413
−5.218
6.012
1.00
34.23
O


ATOM
41208
C5
U A1923
−100.615
−4.409
6.414
1.00
34.23
C


ATOM
41209
C6
U A1923
−101.851
−4.752
6.770
1.00
34.23
C


ATOM
41210
P
C A1924
−104.585
−6.596
12.348
1.00
47.21
P


ATOM
41211
OP1
C A1924
−105.750
−5.976
13.016
1.00
47.21
O


ATOM
41212
OP2
C A1924
−103.273
−5.913
12.422
1.00
47.21
O


ATOM
41213
O5′
C A1924
−104.442
−8.100
12.809
1.00
47.21
O


ATOM
41214
C5′
C A1924
−105.225
−9.105
12.190
1.00
47.21
C


ATOM
41215
C4′
C A1924
−104.384
−10.274
11.770
1.00
47.21
C


ATOM
41216
O4′
C A1924
−103.573
−9.914
10.634
1.00
47.21
O


ATOM
41217
C3′
C A1924
−103.391
−10.768
12.804
1.00
47.21
C


ATOM
41218
O3′
C A1924
−103.990
−11.634
13.747
1.00
47.21
O


ATOM
41219
C2′
C A1924
−102.312
−11.438
11.962
1.00
47.21
C


ATOM
41220
O2′
C A1924
−102.660
−12.784
11.662
1.00
47.21
O


ATOM
41221
C1′
C A1924
−102.356
−10.621
10.671
1.00
47.21
C


ATOM
41222
N1
C A1924
−101.251
−9.658
10.567
1.00
47.75
N


ATOM
41223
C2
C A1924
−100.201
−10.063
9.758
1.00
47.75
C


ATOM
41224
O2
C A1924
−100.272
−11.190
9.251
1.00
47.75
O


ATOM
41225
N3
C A1924
−99.154
−9.224
9.573
1.00
47.75
N


ATOM
41226
C4
C A1924
−99.137
−8.017
10.155
1.00
47.75
C


ATOM
41227
N4
C A1924
−98.064
−7.246
9.928
1.00
47.75
N


ATOM
41228
C5
C A1924
−100.219
−7.575
10.990
1.00
47.75
C


ATOM
41229
C6
C A1924
−101.254
−8.420
11.162
1.00
47.75
C


ATOM
41230
P
C A1925
−103.283
−11.894
15.149
1.00
99.05
P


ATOM
41231
OP1
C A1925
−103.645
−13.272
15.570
1.00
99.05
O


ATOM
41232
OP2
C A1925
−103.631
−10.753
16.037
1.00
99.05
O


ATOM
41233
O5′
C A1925
−101.747
−11.823
14.763
1.00
99.05
O


ATOM
41234
C5′
C A1925
−101.073
−10.573
14.720
1.00
99.05
C


ATOM
41235
C4′
C A1925
−100.095
−10.445
15.857
1.00
99.05
C


ATOM
41236
O4′
C A1925
−99.546
−9.107
15.853
1.00
99.05
O


ATOM
41237
C3′
C A1925
−100.684
−10.686
17.240
1.00
99.05
C


ATOM
41238
O3′
C A1925
−99.769
−11.439
18.043
1.00
99.05
O


ATOM
41239
C2′
C A1925
−100.891
−9.281
17.817
1.00
99.05
C


ATOM
41240
O2′
C A1925
−100.696
−9.192
19.217
1.00
99.05
O


ATOM
41241
C1′
C A1925
−99.880
−8.412
17.041
1.00
99.05
C


ATOM
41242
N1
C A1925
−100.420
−7.078
16.626
1.00
98.62
N


ATOM
41243
C2
C A1925
−99.775
−5.864
16.952
1.00
98.62
C


ATOM
41244
O2
C A1925
−98.736
−5.873
17.642
1.00
98.62
O


ATOM
41245
N3
C A1925
−100.321
−4.694
16.510
1.00
98.62
N


ATOM
41246
C4
C A1925
−101.442
−4.689
15.771
1.00
98.62
C


ATOM
41247
N4
C A1925
−101.940
−3.514
15.364
1.00
98.62
N


ATOM
41248
C5
C A1925
−102.105
−5.902
15.415
1.00
98.62
C


ATOM
41249
C6
C A1925
−101.561
−7.049
15.850
1.00
98.62
C


ATOM
41250
P
U A1926
−100.085
−12.988
18.367
1.00
85.68
P


ATOM
41251
OP1
U A1926
−100.409
−13.654
17.078
1.00
85.68
O


ATOM
41252
OP2
U A1926
−101.090
−13.004
19.453
1.00
85.68
O


ATOM
41253
O5′
U A1926
−98.707
−13.538
18.912
1.00
85.68
O


ATOM
41254
C5′
U A1926
−97.616
−12.674
19.120
1.00
85.68
C


ATOM
41255
C4′
U A1926
−96.429
−13.080
18.294
1.00
85.68
C


ATOM
41256
O4′
U A1926
−96.855
−13.771
17.078
1.00
85.68
O


ATOM
41257
C3′
U A1926
−95.599
−11.945
17.760
1.00
85.68
C


ATOM
41258
O3′
U A1926
−94.819
−11.311
18.740
1.00
85.68
O


ATOM
41259
C2′
U A1926
−94.820
−12.622
16.648
1.00
85.68
C


ATOM
41260
O2′
U A1926
−93.825
−13.495
17.180
1.00
85.68
O


ATOM
41261
C1′
U A1926
−95.942
−13.467
16.023
1.00
85.68
C


ATOM
41262
N1
U A1926
−96.685
−12.719
14.940
1.00
85.26
N


ATOM
41263
C2
U A1926
−96.020
−11.840
14.068
1.00
85.26
C


ATOM
41264
O2
U A1926
−94.820
−11.609
14.087
1.00
85.26
O


ATOM
41265
N3
U A1926
−96.807
−11.210
13.130
1.00
85.26
N


ATOM
41266
C4
U A1926
−98.163
−11.354
12.961
1.00
85.26
C


ATOM
41267
O4
U A1926
−98.726
−10.720
12.073
1.00
85.26
O


ATOM
41268
C5
U A1926
−98.788
−12.265
13.868
1.00
85.26
C


ATOM
41269
C6
U A1926
−98.051
−12.892
14.796
1.00
85.26
C


ATOM
41270
P
A A1927
−95.141
−9.786
19.091
1.00
19.33
P


ATOM
41271
OP1
A A1927
−95.899
−9.774
20.377
1.00
19.33
O


ATOM
41272
OP2
A A1927
−95.773
−9.191
17.876
1.00
19.33
O


ATOM
41273
O5′
A A1927
−93.693
−9.170
19.308
1.00
19.33
O


ATOM
41274
C5′
A A1927
−93.509
−7.767
19.417
1.00
19.33
C


ATOM
41275
C4′
A A1927
−92.318
−7.312
18.620
1.00
19.33
C


ATOM
41276
O4′
A A1927
−91.248
−8.274
18.768
1.00
19.33
O


ATOM
41277
C3′
A A1927
−92.521
−7.196
17.122
1.00
19.33
C


ATOM
41278
O3′
A A1927
−93.137
−5.964
16.763
1.00
19.33
O


ATOM
41279
C2′
A A1927
−91.098
−7.357
16.582
1.00
19.33
C


ATOM
41280
O2′
A A1927
−90.394
−6.117
16.619
1.00
19.33
O


ATOM
41281
C1′
A A1927
−90.463
−8.312
17.610
1.00
19.33
C


ATOM
41282
N9
A A1927
−90.405
−9.708
17.148
1.00
19.12
N


ATOM
41283
C8
A A1927
−91.333
−10.642
17.464
1.00
19.12
C


ATOM
41284
N7
A A1927
−91.085
−11.821
16.962
1.00
19.12
N


ATOM
41285
C5
A A1927
−89.894
−11.662
16.285
1.00
19.12
C


ATOM
41286
C6
A A1927
−89.130
−12.574
15.525
1.00
19.12
C


ATOM
41287
N6
A A1927
−89.457
−13.857
15.347
1.00
19.12
N


ATOM
41288
N1
A A1927
−87.998
−12.114
14.969
1.00
19.12
N


ATOM
41289
C2
A A1927
−87.703
−10.818
15.182
1.00
19.12
C


ATOM
41290
N3
A A1927
−88.356
−9.870
15.872
1.00
19.12
N


ATOM
41291
C4
A A1927
−89.460
−10.362
16.411
1.00
19.12
C


ATOM
41292
P
A A1928
−93.897
−5.791
15.356
1.00
6.80
P


ATOM
41293
OP1
A A1928
−94.452
−4.431
15.324
1.00
6.80
O


ATOM
41294
OP2
A A1928
−94.823
−6.930
15.209
1.00
6.80
O


ATOM
41295
O5′
A A1928
−92.714
−5.913
14.296
1.00
6.80
O


ATOM
41296
C5′
A A1928
−92.119
−4.766
13.719
1.00
6.80
C


ATOM
41297
C4′
A A1928
−90.900
−5.141
12.923
1.00
6.80
C


ATOM
41298
O4′
A A1928
−90.264
−6.274
13.545
1.00
6.80
O


ATOM
41299
C3′
A A1928
−91.145
−5.574
11.476
1.00
6.80
C


ATOM
41300
O3′
A A1928
−91.175
−4.479
10.582
1.00
6.80
O


ATOM
41301
C2′
A A1928
−89.994
−6.535
11.187
1.00
6.80
C


ATOM
41302
O2′
A A1928
−88.836
−5.838
10.729
1.00
6.80
O


ATOM
41303
C1′
A A1928
−89.709
−7.128
12.565
1.00
6.80
C


ATOM
41304
N9
A A1928
−90.292
−8.475
12.728
1.00
6.70
N


ATOM
41305
C8
A A1928
−91.537
−8.774
13.187
1.00
6.70
C


ATOM
41306
N7
A A1928
−91.775
−10.050
13.248
1.00
6.70
N


ATOM
41307
C5
A A1928
−90.609
−10.636
12.794
1.00
6.70
C


ATOM
41308
C6
A A1928
−90.229
−11.971
12.617
1.00
6.70
C


ATOM
41309
N6
A A1928
−91.021
−13.012
12.889
1.00
6.70
N


ATOM
41310
N1
A A1928
−88.995
−12.212
12.161
1.00
6.70
N


ATOM
41311
C2
A A1928
−88.200
−11.193
11.898
1.00
6.70
C


ATOM
41312
N3
A A1928
−88.454
−9.902
12.029
1.00
6.70
N


ATOM
41313
C4
A A1928
−89.687
−9.681
12.484
1.00
6.70
C


ATOM
41314
P
G A1929
−92.480
−4.140
9.728
1.00
9.15
P


ATOM
41315
OP1
G A1929
−92.518
−2.677
9.562
1.00
9.15
O


ATOM
41316
OP2
G A1929
−93.631
−4.834
10.354
1.00
9.15
O


ATOM
41317
O5′
G A1929
−92.155
−4.792
8.374
1.00
9.15
O


ATOM
41318
C5′
G A1929
−91.828
−6.132
8.337
1.00
9.15
C


ATOM
41319
C4′
G A1929
−90.623
−6.350
7.523
1.00
9.15
C


ATOM
41320
O4′
G A1929
−89.989
−7.547
7.982
1.00
9.15
O


ATOM
41321
C3′
G A1929
−90.913
−6.616
6.098
1.00
9.15
C


ATOM
41322
O3′
G A1929
−89.684
−6.581
5.423
1.00
9.15
O


ATOM
41323
C2′
G A1929
−91.407
−8.048
6.176
1.00
9.15
C


ATOM
41324
O2′
G A1929
−91.387
−8.737
4.938
1.00
9.15
O


ATOM
41325
C1′
G A1929
−90.410
−8.635
7.185
1.00
9.15
C


ATOM
41326
N9
G A1929
−90.969
−9.640
8.102
1.00
9.80
N


ATOM
41327
C8
G A1929
−90.493
−10.910
8.340
1.00
9.80
C


ATOM
41328
N7
G A1929
−91.149
−11.543
9.280
1.00
9.80
N


ATOM
41329
C5
G A1929
−92.095
−10.628
9.711
1.00
9.80
C


ATOM
41330
C6
G A1929
−93.108
−10.747
10.692
1.00
9.80
C


ATOM
41331
O6
G A1929
−93.388
−11.717
11.406
1.00
9.80
O


ATOM
41332
N1
G A1929
−93.850
−9.579
10.819
1.00
9.80
N


ATOM
41333
C2
G A1929
−93.660
−8.432
10.080
1.00
9.80
C


ATOM
41334
N2
G A1929
−94.489
−7.387
10.329
1.00
9.80
N


ATOM
41335
N3
G A1929
−92.722
−8.332
9.145
1.00
9.80
N


ATOM
41336
C4
G A1929
−91.982
−9.449
9.014
1.00
9.80
C


ATOM
41337
P
G A1930
−89.610
−6.132
3.910
1.00
14.03
P


ATOM
41338
OP1
G A1930
−89.368
−4.669
3.916
1.00
14.03
O


ATOM
41339
OP2
G A1930
−90.825
−6.674
3.213
1.00
14.03
O


ATOM
41340
O5′
G A1930
−88.320
−6.900
3.408
1.00
14.03
O


ATOM
41341
C5′
G A1930
−87.411
−7.465
4.335
1.00
14.03
C


ATOM
41342
C4′
G A1930
−86.002
−7.175
3.937
1.00
14.03
C


ATOM
41343
O4′
G A1930
−85.134
−8.181
4.497
1.00
14.03
O


ATOM
41344
C3′
G A1930
−85.753
−7.194
2.449
1.00
14.03
C


ATOM
41345
O3′
G A1930
−84.743
−6.247
2.138
1.00
14.03
O


ATOM
41346
C2′
G A1930
−85.244
−8.608
2.206
1.00
14.03
C


ATOM
41347
O2′
G A1930
−84.464
−8.754
1.050
1.00
14.03
O


ATOM
41348
C1′
G A1930
−84.430
−8.837
3.460
1.00
14.03
C


ATOM
41349
N9
G A1930
−84.262
−10.244
3.842
1.00
13.66
N


ATOM
41350
C8
G A1930
−85.162
−11.284
3.826
1.00
13.66
C


ATOM
41351
N7
G A1930
−84.672
−12.400
4.273
1.00
13.66
N


ATOM
41352
C5
G A1930
−83.378
−12.061
4.623
1.00
13.66
C


ATOM
41353
C6
G A1930
−82.342
−12.845
5.168
1.00
13.66
C


ATOM
41354
O6
G A1930
−82.396
−14.041
5.441
1.00
13.66
O


ATOM
41355
N1
G A1930
−81.175
−12.135
5.393
1.00
13.66
N


ATOM
41356
C2
G A1930
−81.019
−10.817
5.104
1.00
13.66
C


ATOM
41357
N2
G A1930
−79.836
−10.285
5.391
1.00
13.66
N


ATOM
41358
N3
G A1930
−81.960
−10.064
4.579
1.00
13.66
N


ATOM
41359
C4
G A1930
−83.109
−10.747
4.374
1.00
13.66
C


ATOM
41360
P
U A1931
−84.547
−5.765
0.622
1.00
13.59
P


ATOM
41361
OP1
U A1931
−85.785
−6.128
−0.112
1.00
13.59
O


ATOM
41362
OP2
U A1931
−83.243
−6.337
0.133
1.00
13.59
O


ATOM
41363
O5′
U A1931
−84.462
−4.168
0.760
1.00
13.59
O


ATOM
41364
C5′
U A1931
−83.944
−3.550
1.913
1.00
13.59
C


ATOM
41365
C4′
U A1931
−82.778
−2.644
1.587
1.00
13.59
C


ATOM
41366
O4′
U A1931
−81.936
−2.542
2.755
1.00
13.59
O


ATOM
41367
C3′
U A1931
−81.848
−3.110
0.465
1.00
13.59
C


ATOM
41368
O3′
U A1931
−82.194
−2.576
−0.801
1.00
13.59
O


ATOM
41369
C2′
U A1931
−80.462
−2.678
0.930
1.00
13.59
C


ATOM
41370
O2′
U A1931
−80.201
−1.326
0.589
1.00
13.59
O


ATOM
41371
C1′
U A1931
−80.594
−2.763
2.427
1.00
13.59
C


ATOM
41372
N1
U A1931
−80.203
−4.071
2.964
1.00
13.70
N


ATOM
41373
C2
U A1931
−78.897
−4.278
3.276
1.00
13.70
C


ATOM
41374
O2
U A1931
−78.072
−3.435
3.038
1.00
13.70
O


ATOM
41375
N3
U A1931
−78.604
−5.487
3.840
1.00
13.70
N


ATOM
41376
C4
U A1931
−79.497
−6.483
4.142
1.00
13.70
C


ATOM
41377
O4
U A1931
−79.130
−7.524
4.669
1.00
13.70
O


ATOM
41378
C5
U A1931
−80.842
−6.193
3.806
1.00
13.70
C


ATOM
41379
C6
U A1931
−81.141
−5.017
3.254
1.00
13.70
C


TER


END
















TABLE 7





H69 Neomycin Binding Site for Unrotated Ribosome
























ATOM
32464
P
G A1515
−31.881
117.606
101.995
1.00
7.98
P


ATOM
32465
OP1
G A1515
−32.095
118.164
103.346
1.00
7.98
O


ATOM
32466
OP2
G A1515
−31.678
116.145
101.830
1.00
7.98
O


ATOM
32467
O5′
G A1515
−33.029
118.085
101.036
1.00
7.98
O


ATOM
32468
C5′
G A1515
−33.496
119.407
101.098
1.00
7.98
C


ATOM
32469
C4′
G A1515
−34.575
119.623
100.099
1.00
7.98
C


ATOM
32470
O4′
G A1515
−34.111
119.230
98.782
1.00
7.98
O


ATOM
32471
C3′
G A1515
−35.806
118.780
100.296
1.00
7.98
C


ATOM
32472
O3′
G A1515
−36.634
119.265
101.315
1.00
7.98
O


ATOM
32473
C2′
G A1515
−36.436
118.834
98.931
1.00
7.98
C


ATOM
32474
O2′
G A1515
−37.017
120.101
98.721
1.00
7.98
O


ATOM
32475
C1′
G A1515
−35.201
118.715
98.039
1.00
7.98
C


ATOM
32476
N9
G A1515
−34.916
117.309
97.694
1.00
8.01
N


ATOM
32477
C8
G A1515
−33.970
116.582
98.350
1.00
8.01
C


ATOM
32478
N7
G A1515
−33.892
115.363
97.913
1.00
8.01
N


ATOM
32479
C5
G A1515
−34.853
115.261
96.929
1.00
8.01
C


ATOM
32480
C6
G A1515
−35.167
114.127
96.160
1.00
8.01
C


ATOM
32481
O6
G A1515
−34.624
112.987
96.223
1.00
8.01
O


ATOM
32482
N1
G A1515
−36.189
114.455
95.277
1.00
8.01
N


ATOM
32483
C2
G A1515
−36.789
115.678
95.166
1.00
8.01
C


ATOM
32484
N2
G A1515
−37.745
115.775
94.249
1.00
8.01
N


ATOM
32485
N3
G A1515
−36.498
116.728
95.892
1.00
8.01
N


ATOM
32486
C4
G A1515
−35.509
116.452
96.764
1.00
8.01
C


ATOM
32487
P
G A1516
−37.407
118.244
102.263
1.00
3.93
P


ATOM
32488
OP1
G A1516
−37.954
119.029
103.387
1.00
3.93
O


ATOM
32489
OP2
G A1516
−36.470
117.138
102.562
1.00
3.93
O


ATOM
32490
O5′
G A1516
−38.596
117.734
101.329
1.00
3.93
O


ATOM
32491
C5′
G A1516
−39.544
118.658
100.841
1.00
3.93
C


ATOM
32492
C4′
G A1516
−40.410
118.079
99.757
1.00
3.93
C


ATOM
32493
O4′
G A1516
−39.618
117.710
98.597
1.00
3.93
O


ATOM
32494
C3′
G A1516
−41.165
116.812
100.097
1.00
3.93
C


ATOM
32495
O3′
G A1516
−42.305
117.060
100.891
1.00
3.93
O


ATOM
32496
C2′
G A1516
−41.516
116.297
98.723
1.00
3.93
C


ATOM
32497
O2′
G A1516
−42.606
117.035
98.192
1.00
3.93
O


ATOM
32498
C1′
G A1516
−40.244
116.637
97.933
1.00
3.93
C


ATOM
32499
N9
G A1516
−39.328
115.498
97.922
1.00
4.29
N


ATOM
32500
C8
G A1516
−38.192
115.311
98.668
1.00
4.29
C


ATOM
32501
N7
G A1516
−37.619
114.144
98.480
1.00
4.29
N


ATOM
32502
C5
G A1516
−38.468
113.523
97.577
1.00
4.29
C


ATOM
32503
C6
G A1516
−38.383
112.245
96.996
1.00
4.29
C


ATOM
32504
O6
G A1516
−37.512
111.412
97.217
1.00
4.29
O


ATOM
32505
N1
G A1516
−39.429
111.994
96.100
1.00
4.29
N


ATOM
32506
C2
G A1516
−40.474
112.861
95.802
1.00
4.29
C


ATOM
32507
N2
G A1516
−41.423
112.444
94.925
1.00
4.29
N


ATOM
32508
N3
G A1516
−40.559
114.069
96.360
1.00
4.29
N


ATOM
32509
C4
G A1516
−39.532
114.334
97.224
1.00
4.29
C


ATOM
32510
P
G A1517
−42.644
116.119
102.144
1.00
20.20
P


ATOM
32511
OP1
G A1517
−43.899
116.654
102.769
1.00
20.20
O


ATOM
32512
OP2
G A1517
−41.402
116.037
102.961
1.00
20.20
O


ATOM
32513
O5′
G A1517
−42.934
114.712
101.467
1.00
20.20
O


ATOM
32514
C5′
G A1517
−44.109
114.507
100.710
1.00
20.20
C


ATOM
32515
C4′
G A1517
−44.675
113.137
100.949
1.00
20.20
C


ATOM
32516
O4′
G A1517
−46.123
113.216
100.986
1.00
20.20
O


ATOM
32517
C3′
G A1517
−44.370
112.106
99.879
1.00
20.20
C


ATOM
32518
O3′
G A1517
−43.127
111.469
100.069
1.00
20.20
O


ATOM
32519
C2′
G A1517
−45.564
111.179
99.945
1.00
20.20
C


ATOM
32520
O2′
G A1517
−45.451
110.289
101.038
1.00
20.20
O


ATOM
32521
C1′
G A1517
−46.684
112.173
100.242
1.00
20.20
C


ATOM
32522
N9
G A1517
−47.240
112.764
99.013
1.00
20.45
N


ATOM
32523
C8
G A1517
−47.033
114.049
98.561
1.00
20.45
C


ATOM
32524
N7
G A1517
−47.658
114.296
97.435
1.00
20.45
N


ATOM
32525
C5
G A1517
−48.317
113.103
97.126
1.00
20.45
C


ATOM
32526
C6
G A1517
−49.151
112.737
96.037
1.00
20.45
C


ATOM
32527
O6
G A1517
−49.521
113.398
95.063
1.00
20.45
O


ATOM
32528
N1
G A1517
−49.583
111.431
96.151
1.00
20.45
N


ATOM
32529
C2
G A1517
−49.268
110.579
97.170
1.00
20.45
C


ATOM
32530
N2
G A1517
−49.779
109.349
97.121
1.00
20.45
N


ATOM
32531
N3
G A1517
−48.511
110.891
98.180
1.00
20.45
N


ATOM
32532
C4
G A1517
−48.072
112.157
98.100
1.00
20.45
C


ATOM
32533
P
A A1518
−41.997
111.615
98.942
1.00
10.21
P


ATOM
32534
OP1
A A1518
−40.725
111.069
99.488
1.00
10.21
O


ATOM
32535
OP2
A A1518
−42.035
113.035
98.468
1.00
10.21
O


ATOM
32536
O5′
A A1518
−42.538
110.652
97.804
1.00
10.21
O


ATOM
32537
C5′
A A1518
−42.626
109.254
98.025
1.00
10.21
C


ATOM
32538
C4′
A A1518
−43.607
108.598
97.084
1.00
10.21
C


ATOM
32539
O4′
A A1518
−44.906
109.243
97.171
1.00
10.21
O


ATOM
32540
C3′
A A1518
−43.273
108.672
95.615
1.00
10.21
C


ATOM
32541
O3′
A A1518
−42.258
107.763
95.236
1.00
10.21
O


ATOM
32542
C2′
A A1518
−44.618
108.394
94.978
1.00
10.21
C


ATOM
32543
O2′
A A1518
−44.920
107.011
95.056
1.00
10.21
O


ATOM
32544
C1′
A A1518
−45.556
109.165
95.921
1.00
10.21
C


ATOM
32545
N9
A A1518
−45.812
110.546
95.454
1.00
10.45
N


ATOM
32546
C8
A A1518
−45.390
111.655
96.119
1.00
10.45
C


ATOM
32547
N7
A A1518
−45.713
112.790
95.547
1.00
10.45
N


ATOM
32548
C5
A A1518
−46.392
112.422
94.411
1.00
10.45
C


ATOM
32549
C6
A A1518
−46.969
113.199
93.389
1.00
10.45
C


ATOM
32550
N6
A A1518
−46.979
114.532
93.329
1.00
10.45
N


ATOM
32551
N1
A A1518
−47.568
112.517
92.397
1.00
10.45
N


ATOM
32552
C2
A A1518
−47.581
111.172
92.460
1.00
10.45
C


ATOM
32553
N3
A A1518
−47.071
110.353
93.379
1.00
10.45
N


ATOM
32554
C4
A A1518
−46.471
111.042
94.346
1.00
10.45
C


TER


ATOM
40737
P
G A1903
−34.819
134.604
124.042
1.00
0.04
P


ATOM
40738
OP1
G A1903
−35.213
134.085
125.364
1.00
0.04
O


ATOM
40739
OP2
G A1903
−33.506
134.200
123.461
1.00
0.04
O


ATOM
40740
O5′
G A1903
−35.985
134.356
122.997
1.00
0.04
O


ATOM
40741
C5′
G A1903
−37.326
134.217
123.430
1.00
0.04
C


ATOM
40742
C4′
G A1903
−38.312
134.513
122.328
1.00
0.04
C


ATOM
40743
O4′
G A1903
−37.689
135.289
121.274
1.00
0.04
O


ATOM
40744
C3′
G A1903
−38.877
133.325
121.590
1.00
0.04
C


ATOM
40745
O3′
G A1903
−39.859
132.644
122.335
1.00
0.04
O


ATOM
40746
C2′
G A1903
−39.425
133.986
120.341
1.00
0.04
C


ATOM
40747
O2′
G A1903
−40.636
134.646
120.626
1.00
0.04
O


ATOM
40748
C1′
G A1903
−38.368
135.045
120.061
1.00
0.04
C


ATOM
40749
N9
G A1903
−37.414
134.592
119.035
1.00
0.01
N


ATOM
40750
C8
G A1903
−36.064
134.282
119.063
1.00
0.01
C


ATOM
40751
N7
G A1903
−35.630
133.881
117.884
1.00
0.01
N


ATOM
40752
C5
G A1903
−36.755
133.917
117.064
1.00
0.01
C


ATOM
40753
C6
G A1903
−36.941
133.614
115.704
1.00
0.01
C


ATOM
40754
O6
G A1903
−36.138
133.228
114.878
1.00
0.01
O


ATOM
40755
N1
G A1903
−38.218
133.802
115.256
1.00
0.01
N


ATOM
40756
C2
G A1903
−39.238
134.231
116.030
1.00
0.01
C


ATOM
40757
N2
G A1903
−40.411
134.335
115.387
1.00
0.01
N


ATOM
40758
N3
G A1903
−39.110
134.530
117.320
1.00
0.01
N


ATOM
40759
C4
G A1903
−37.847
134.351
117.759
1.00
0.01
C


ATOM
40760
P
G A1904
−40.245
131.107
121.998
1.00
0.68
P


ATOM
40761
OP1
G A1904
−41.073
130.609
123.141
1.00
0.68
O


ATOM
40762
OP2
G A1904
−38.979
130.391
121.662
1.00
0.68
O


ATOM
40763
O5′
G A1904
−41.156
131.234
120.695
1.00
0.68
O


ATOM
40764
C5′
G A1904
−42.460
131.780
120.775
1.00
0.68
C


ATOM
40765
C4′
G A1904
−43.131
131.765
119.439
1.00
0.68
C


ATOM
40766
O4′
G A1904
−42.329
132.516
118.487
1.00
0.68
O


ATOM
40767
C3′
G A1904
−43.262
130.399
118.792
1.00
0.68
C


ATOM
40768
O3′
G A1904
−44.334
129.633
119.291
1.00
0.68
O


ATOM
40769
C2′
G A1904
−43.418
130.759
117.340
1.00
0.68
C


ATOM
40770
O2′
G A1904
−44.721
131.292
117.119
1.00
0.68
O


ATOM
40771
C1′
G A1904
−42.379
131.886
117.222
1.00
0.68
C


ATOM
40772
N9
G A1904
−41.017
131.365
116.897
1.00
0.52
N


ATOM
40773
C8
G A1904
−39.972
131.266
117.768
1.00
0.52
C


ATOM
40774
N7
G A1904
−38.878
130.767
117.255
1.00
0.52
N


ATOM
40775
C5
G A1904
−39.191
130.496
115.947
1.00
0.52
C


ATOM
40776
C6
G A1904
−38.394
129.941
114.902
1.00
0.52
C


ATOM
40777
O6
G A1904
−37.219
129.565
114.912
1.00
0.52
O


ATOM
40778
N1
G A1904
−39.078
129.832
113.721
1.00
0.52
N


ATOM
40779
C2
G A1904
−40.368
130.213
113.573
1.00
0.52
C


ATOM
40780
N2
G A1904
−40.864
130.044
112.351
1.00
0.52
N


ATOM
40781
N3
G A1904
−41.130
130.729
114.528
1.00
0.52
N


ATOM
40782
C4
G A1904
−40.493
130.859
115.709
1.00
0.52
C


ATOM
40783
P
C A1905
−44.210
128.036
119.281
1.00
0.21
P


ATOM
40784
OP1
C A1905
−45.534
127.470
119.728
1.00
0.21
O


ATOM
40785
OP2
C A1905
−42.980
127.697
120.055
1.00
0.21
O


ATOM
40786
O5′
C A1905
−43.971
127.728
117.727
1.00
0.21
O


ATOM
40787
C5′
C A1905
−45.066
127.557
116.833
1.00
0.21
C


ATOM
40788
C4′
C A1905
−44.601
127.423
115.398
1.00
0.21
C


ATOM
40789
O4′
C A1905
−43.316
128.060
115.240
1.00
0.21
O


ATOM
40790
C3′
C A1905
−44.408
126.001
114.888
1.00
0.21
C


ATOM
40791
O3′
C A1905
−45.612
125.469
114.350
1.00
0.21
O


ATOM
40792
C2′
C A1905
−43.293
126.130
113.842
1.00
0.21
C


ATOM
40793
O2′
C A1905
−43.822
126.333
112.529
1.00
0.21
O


ATOM
40794
C1′
C A1905
−42.550
127.392
114.273
1.00
0.21
C


ATOM
40795
N1
C A1905
−41.246
127.091
114.842
1.00
0.07
N


ATOM
40796
C2
C A1905
−40.235
126.639
113.998
1.00
0.07
C


ATOM
40797
O2
C A1905
−40.483
126.484
112.792
1.00
0.07
O


ATOM
40798
N3
C A1905
−39.021
126.356
114.496
1.00
0.07
N


ATOM
40799
C4
C A1905
−38.821
126.524
115.783
1.00
0.07
C


ATOM
40800
N4
C A1905
−37.618
126.230
116.293
1.00
0.07
N


ATOM
40801
C5
C A1905
−39.849
127.003
116.645
1.00
0.07
C


ATOM
40802
C6
C A1905
−41.046
127.275
116.150
1.00
0.07
C


ATOM
40803
P
G A1906
−46.331
124.191
115.013
1.00
22.98
P


ATOM
40804
OP1
G A1906
−45.660
123.936
116.329
1.00
22.98
O


ATOM
40805
OP2
G A1906
−46.340
123.108
113.985
1.00
22.98
O


ATOM
40806
O5′
G A1906
−47.808
124.710
115.255
1.00
22.98
O


ATOM
40807
C5′
G A1906
−48.903
124.008
114.730
1.00
22.98
C


ATOM
40808
C4′
G A1906
−50.188
124.644
115.135
1.00
22.98
C


ATOM
40809
O4′
G A1906
−50.464
125.789
114.294
1.00
22.98
O


ATOM
40810
C3′
G A1906
−51.405
123.765
115.007
1.00
22.98
C


ATOM
40811
O3′
G A1906
−51.549
122.919
116.127
1.00
22.98
O


ATOM
40812
C2′
G A1906
−52.534
124.770
114.851
1.00
22.98
C


ATOM
40813
O2′
G A1906
−52.964
125.254
116.120
1.00
22.98
O


ATOM
40814
C1′
G A1906
−51.841
125.898
114.064
1.00
22.98
C


ATOM
40815
N9
G A1906
−52.066
125.751
112.623
1.00
22.86
N


ATOM
40816
C8
G A1906
−51.277
125.085
111.736
1.00
22.86
C


ATOM
40817
N7
G A1906
−51.766
125.078
110.524
1.00
22.86
N


ATOM
40818
C5
G A1906
−52.963
125.766
110.627
1.00
22.86
C


ATOM
40819
C6
G A1906
−53.952
126.088
109.663
1.00
22.86
C


ATOM
40820
O6
G A1906
−53.981
125.834
108.460
1.00
22.86
O


ATOM
40821
N1
G A1906
−55.001
126.803
110.221
1.00
22.86
N


ATOM
40822
C2
G A1906
−55.090
127.165
111.536
1.00
22.86
C


ATOM
40823
N2
G A1906
−56.163
127.854
111.946
1.00
22.86
N


ATOM
40824
N3
G A1906
−54.173
126.866
112.422
1.00
22.86
N


ATOM
40825
C4
G A1906
−53.147
126.176
111.915
1.00
22.86
C


ATOM
40826
P
G A1907
−52.488
121.623
116.062
1.00
13.06
P


ATOM
40827
OP1
G A1907
−52.081
120.742
117.195
1.00
13.06
O


ATOM
40828
OP2
G A1907
−52.434
121.083
114.673
1.00
13.06
O


ATOM
40829
O5′
G A1907
−53.913
122.242
116.328
1.00
13.06
O


ATOM
40830
C5′
G A1907
−54.754
122.498
115.248
1.00
13.06
C


ATOM
40831
C4′
G A1907
−56.004
123.171
115.672
1.00
13.06
C


ATOM
40832
O4′
G A1907
−56.100
124.427
114.959
1.00
13.06
O


ATOM
40833
C3′
G A1907
−57.281
122.398
115.332
1.00
13.06
C


ATOM
40834
O3′
G A1907
−57.750
121.598
116.409
1.00
13.06
O


ATOM
40835
C2′
G A1907
−58.255
123.477
114.882
1.00
13.06
C


ATOM
40836
O2′
G A1907
−58.897
124.074
116.000
1.00
13.06
O


ATOM
40837
C1′
G A1907
−57.305
124.495
114.248
1.00
13.06
C


ATOM
40838
N9
G A1907
−56.998
124.191
112.830
1.00
13.23
N


ATOM
40839
C8
G A1907
−55.754
123.797
112.378
1.00
13.23
C


ATOM
40840
N7
G A1907
−55.692
123.603
111.087
1.00
13.23
N


ATOM
40841
C5
G A1907
−56.972
123.906
110.639
1.00
13.23
C


ATOM
40842
C6
G A1907
−57.513
123.868
109.319
1.00
13.23
C


ATOM
40843
O6
G A1907
−56.971
123.558
108.236
1.00
13.23
O


ATOM
40844
N1
G A1907
−58.848
124.247
109.336
1.00
13.23
N


ATOM
40845
C2
G A1907
−59.569
124.605
110.446
1.00
13.23
C


ATOM
40846
N2
G A1907
−60.847
124.944
110.239
1.00
13.23
N


ATOM
40847
N3
G A1907
−59.085
124.644
111.670
1.00
13.23
N


ATOM
40848
C4
G A1907
−57.785
124.285
111.698
1.00
13.23
C


ATOM
40849
P
C A1908
−58.077
120.042
116.166
1.00
22.31
P


ATOM
40850
OP1
C A1908
−58.340
119.430
117.489
1.00
22.31
O


ATOM
40851
OP2
C A1908
−56.981
119.485
115.328
1.00
22.31
O


ATOM
40852
O5′
C A1908
−59.427
120.100
115.327
1.00
22.31
O


ATOM
40853
C5′
C A1908
−60.560
120.792
115.830
1.00
22.31
C


ATOM
40854
C4′
C A1908
−61.604
121.008
114.764
1.00
22.31
C


ATOM
40855
O4′
C A1908
−61.160
122.035
113.841
1.00
22.31
O


ATOM
40856
C3′
C A1908
−61.897
119.813
113.886
1.00
22.31
C


ATOM
40857
O3′
C A1908
−62.824
118.928
114.465
1.00
22.31
O


ATOM
40858
C2′
C A1908
−62.376
120.449
112.588
1.00
22.31
C


ATOM
40859
O2′
C A1908
−63.716
120.895
112.696
1.00
22.31
O


ATOM
40860
C1′
C A1908
−61.476
121.667
112.516
1.00
22.31
C


ATOM
40861
N1
C A1908
−60.223
121.375
111.800
1.00
22.46
N


ATOM
40862
C2
C A1908
−60.343
121.151
110.452
1.00
22.46
C


ATOM
40863
O2
C A1908
−61.493
121.218
110.015
1.00
22.46
O


ATOM
40864
N3
C A1908
−59.244
120.879
109.708
1.00
22.46
N


ATOM
40865
C4
C A1908
−58.049
120.837
110.296
1.00
22.46
C


ATOM
40866
N4
C A1908
−56.975
120.568
109.562
1.00
22.46
N


ATOM
40867
C5
C A1908
−57.895
121.072
111.687
1.00
22.46
C


ATOM
40868
C6
C A1908
−58.999
121.331
112.399
1.00
22.46
C


ATOM
40869
P
C A1909
−62.666
117.352
114.219
1.00
18.48
P


ATOM
40870
OP1
C A1909
−63.508
116.660
115.233
1.00
18.48
O


ATOM
40871
OP2
C A1909
−61.196
117.064
114.187
1.00
18.48
O


ATOM
40872
O5′
C A1909
−63.298
117.159
112.761
1.00
18.48
O


ATOM
40873
C5′
C A1909
−64.625
117.585
112.492
1.00
18.48
C


ATOM
40874
C4′
C A1909
−64.973
117.446
111.036
1.00
18.48
C


ATOM
40875
O4′
C A1909
−64.289
118.462
110.249
1.00
18.48
O


ATOM
40876
C3′
C A1909
−64.561
116.145
110.374
1.00
18.48
C


ATOM
40877
O3′
C A1909
−65.413
115.062
110.684
1.00
18.48
O


ATOM
40878
C2′
C A1909
−64.564
116.533
108.905
1.00
18.48
C


ATOM
40879
O2′
C A1909
−65.892
116.682
108.420
1.00
18.48
O


ATOM
40880
C1′
C A1909
−63.917
117.910
108.992
1.00
18.48
C


ATOM
40881
N1
C A1909
−62.463
117.797
108.961
1.00
18.22
N


ATOM
40882
C2
C A1909
−61.833
117.441
107.775
1.00
18.22
C


ATOM
40883
O2
C A1909
−62.546
117.266
106.784
1.00
18.22
O


ATOM
40884
N3
C A1909
−60.481
117.310
107.753
1.00
18.22
N


ATOM
40885
C4
C A1909
−59.784
117.517
108.876
1.00
18.22
C


ATOM
40886
N4
C A1909
−58.460
117.390
108.881
1.00
18.22
N


ATOM
40887
C5
C A1909
−60.419
117.878
110.097
1.00
18.22
C


ATOM
40888
C6
C A1909
−61.751
117.991
110.105
1.00
18.22
C


ATOM
40889
P
G A1910
−64.898
113.559
110.468
1.00
17.57
P


ATOM
40890
OP1
G A1910
−65.973
112.660
110.944
1.00
17.57
O


ATOM
40891
OP2
G A1910
−63.549
113.455
111.092
1.00
17.57
O


ATOM
40892
O5′
G A1910
−64.772
113.464
108.885
1.00
17.57
O


ATOM
40893
C5′
G A1910
−65.931
113.377
108.081
1.00
17.57
C


ATOM
40894
C4′
G A1910
−65.592
113.385
106.621
1.00
17.57
C


ATOM
40895
O4′
G A1910
−64.610
114.408
106.359
1.00
17.57
O


ATOM
40896
C3′
G A1910
−64.925
112.141
106.083
1.00
17.57
C


ATOM
40897
O3′
G A1910
−65.806
111.069
105.891
1.00
17.57
O


ATOM
40898
C2′
G A1910
−64.323
112.650
104.805
1.00
17.57
C


ATOM
40899
O2′
G A1910
−65.339
112.857
103.839
1.00
17.57
O


ATOM
40900
C1′
G A1910
−63.804
114.007
105.268
1.00
17.57
C


ATOM
40901
N9
G A1910
−62.390
113.947
105.701
1.00
17.29
N


ATOM
40902
C8
G A1910
−61.836
114.163
106.930
1.00
17.29
C


ATOM
40903
N7
G A1910
−60.534
114.029
106.926
1.00
17.29
N


ATOM
40904
C5
G A1910
−60.192
113.708
105.616
1.00
17.29
C


ATOM
40905
C6
G A1910
−58.933
113.441
104.969
1.00
17.29
C


ATOM
40906
O6
G A1910
−57.780
113.423
105.424
1.00
17.29
O


ATOM
40907
N1
G A1910
−59.102
113.164
103.617
1.00
17.29
N


ATOM
40908
C2
G A1910
−60.316
113.147
102.967
1.00
17.29
C


ATOM
40909
N2
G A1910
−60.336
112.866
101.655
1.00
17.29
N


ATOM
40910
N3
G A1910
−61.471
113.394
103.555
1.00
17.29
N


ATOM
40911
C4
G A1910
−61.343
113.664
104.865
1.00
17.29
C


ATOM
40912
P
U A1911
−65.303
109.592
106.231
1.00
11.08
P


ATOM
40913
OP1
U A1911
−66.489
108.696
106.169
1.00
11.08
O


ATOM
40914
OP2
U A1911
−64.537
109.691
107.503
1.00
11.08
O


ATOM
40915
O5′
U A1911
−64.311
109.265
105.022
1.00
11.08
O


ATOM
40916
C5′
U A1911
−64.701
109.489
103.674
1.00
11.08
C


ATOM
40917
C4′
U A1911
−63.525
109.385
102.734
1.00
11.08
C


ATOM
40918
O4′
U A1911
−62.585
110.457
103.001
1.00
11.08
O


ATOM
40919
C3′
U A1911
−62.692
108.121
102.856
1.00
11.08
C


ATOM
40920
O3′
U A1911
−63.255
107.022
102.172
1.00
11.08
O


ATOM
40921
C2′
U A1911
−61.336
108.553
102.314
1.00
11.08
C


ATOM
40922
O2′
U A1911
−61.308
108.531
100.894
1.00
11.08
O


ATOM
40923
C1′
U A1911
−61.266
110.006
102.789
1.00
11.08
C


ATOM
40924
N1
U A1911
−60.515
110.131
104.053
1.00
11.00
N


ATOM
40925
C2
U A1911
−59.115
110.085
103.953
1.00
11.00
C


ATOM
40926
O2
U A1911
−58.479
109.968
102.911
1.00
11.00
O


ATOM
40927
N3
U A1911
−58.443
110.185
105.133
1.00
11.00
N


ATOM
40928
C4
U A1911
−59.019
110.340
106.367
1.00
11.00
C


ATOM
40929
O4
U A1911
−58.253
110.425
107.322
1.00
11.00
O


ATOM
40930
C5
U A1911
−60.471
110.373
106.394
1.00
11.00
C


ATOM
40931
C6
U A1911
−61.164
110.265
105.256
1.00
11.00
C


ATOM
40932
P
A A1912
−63.221
105.563
102.838
1.00
13.79
P


ATOM
40933
OP1
A A1912
−64.413
104.821
102.339
1.00
13.79
O


ATOM
40934
OP2
A A1912
−63.054
105.748
104.313
1.00
13.79
O


ATOM
40935
O5′
A A1912
−61.907
104.937
102.218
1.00
13.79
O


ATOM
40936
C5′
A A1912
−61.862
104.600
100.850
1.00
13.79
C


ATOM
40937
C4′
A A1912
−60.644
103.778
100.516
1.00
13.79
C


ATOM
40938
O4′
A A1912
−59.450
104.454
100.949
1.00
13.79
O


ATOM
40939
C3′
A A1912
−60.562
102.416
101.169
1.00
13.79
C


ATOM
40940
O3′
A A1912
−61.323
101.452
100.470
1.00
13.79
O


ATOM
40941
C2′
A A1912
−59.055
102.115
101.206
1.00
13.79
C


ATOM
40942
O2′
A A1912
−58.648
101.347
100.080
1.00
13.79
O


ATOM
40943
C1′
A A1912
−58.422
103.513
101.114
1.00
13.79
C


ATOM
40944
N9
A A1912
−57.661
103.864
102.306
1.00
13.81
N


ATOM
40945
C8
A A1912
−58.142
104.009
103.572
1.00
13.81
C


ATOM
40946
N7
A A1912
−57.203
104.340
104.411
1.00
13.81
N


ATOM
40947
C5
A A1912
−56.060
104.415
103.630
1.00
13.81
C


ATOM
40948
C6
A A1912
−54.754
104.712
103.951
1.00
13.81
C


ATOM
40949
N6
A A1912
−54.373
105.006
105.195
1.00
13.81
N


ATOM
40950
N1
A A1912
−53.870
104.697
102.949
1.00
13.81
N


ATOM
40951
C2
A A1912
−54.278
104.407
101.719
1.00
13.81
C


ATOM
40952
N3
A A1912
−55.486
104.108
101.307
1.00
13.81
N


ATOM
40953
C4
A A1912
−56.327
104.131
102.328
1.00
13.81
C


ATOM
40954
P
A A1913
−62.512
100.696
101.214
1.00
52.95
P


ATOM
40955
OP1
A A1913
−63.758
101.046
100.505
1.00
52.95
O


ATOM
40956
OP2
A A1913
−62.403
101.007
102.658
1.00
52.95
O


ATOM
40957
O5′
A A1913
−62.147
99.179
100.967
1.00
52.95
O


ATOM
40958
C5′
A A1913
−61.978
98.678
99.649
1.00
52.95
C


ATOM
40959
C4′
A A1913
−62.318
97.222
99.587
1.00
52.95
C


ATOM
40960
O4′
A A1913
−61.471
96.577
98.608
1.00
52.95
O


ATOM
40961
C3′
A A1913
−62.111
96.478
100.900
1.00
52.95
C


ATOM
40962
O3′
A A1913
−63.152
95.521
101.080
1.00
52.95
O


ATOM
40963
C2′
A A1913
−60.761
95.784
100.717
1.00
52.95
C


ATOM
40964
O2′
A A1913
−60.605
94.585
101.450
1.00
52.95
O


ATOM
40965
C1′
A A1913
−60.724
95.535
99.214
1.00
52.95
C


ATOM
40966
N9
A A1913
−59.381
95.580
98.653
1.00
53.35
N


ATOM
40967
C8
A A1913
−58.254
96.230
99.112
1.00
53.35
C


ATOM
40968
N7
A A1913
−57.209
96.083
98.333
1.00
53.35
N


ATOM
40969
C5
A A1913
−57.704
95.297
97.306
1.00
53.35
C


ATOM
40970
C6
A A1913
−57.112
94.779
96.163
1.00
53.35
C


ATOM
40971
N6
A A1913
−55.844
95.010
95.865
1.00
53.35
N


ATOM
40972
N1
A A1913
−57.886
94.036
95.338
1.00
53.35
N


ATOM
40973
C2
A A1913
−59.173
93.819
95.655
1.00
53.35
C


ATOM
40974
N3
A A1913
−59.846
94.248
96.711
1.00
53.35
N


ATOM
40975
C4
A A1913
−59.036
94.983
97.487
1.00
53.35
C


ATOM
40976
P
C A1914
−64.614
96.012
101.541
1.00
66.92
P


ATOM
40977
OP1
C A1914
−65.572
94.946
101.149
1.00
66.92
O


ATOM
40978
OP2
C A1914
−64.813
97.382
100.992
1.00
66.92
O


ATOM
40979
O5′
C A1914
−64.478
96.073
103.136
1.00
66.92
O


ATOM
40980
C5′
C A1914
−63.481
95.313
103.824
1.00
66.92
C


ATOM
40981
C4′
C A1914
−63.972
94.848
105.176
1.00
66.92
C


ATOM
40982
O4′
C A1914
−63.129
93.786
105.682
1.00
66.92
O


ATOM
40983
C3′
C A1914
−63.954
95.876
106.293
1.00
66.92
C


ATOM
40984
O3′
C A1914
−65.032
96.795
106.213
1.00
66.92
O


ATOM
40985
C2′
C A1914
−63.990
95.003
107.545
1.00
66.92
C


ATOM
40986
O2′
C A1914
−65.323
94.621
107.856
1.00
66.92
O


ATOM
40987
C1′
C A1914
−63.212
93.756
107.092
1.00
66.92
C


ATOM
40988
N1
C A1914
−61.839
93.677
107.676
1.00
65.84
N


ATOM
40989
C2
C A1914
−60.697
93.544
106.863
1.00
65.84
C


ATOM
40990
O2
C A1914
−60.808
93.516
105.625
1.00
65.84
O


ATOM
40991
N3
C A1914
−59.473
93.459
107.451
1.00
65.84
N


ATOM
40992
C4
C A1914
−59.341
93.490
108.781
1.00
65.84
C


ATOM
40993
N4
C A1914
−58.106
93.407
109.294
1.00
65.84
N


ATOM
40994
C5
C A1914
−60.483
93.615
109.630
1.00
65.84
C


ATOM
40995
C6
C A1914
−61.691
93.697
109.044
1.00
65.84
C


ATOM
40996
P
U A1915
−64.847
98.301
106.742
1.00
39.28
P


ATOM
40997
OP1
U A1915
−66.208
98.875
106.923
1.00
39.28
O


ATOM
40998
OP2
U A1915
−63.899
98.978
105.806
1.00
39.28
O


ATOM
40999
O5′
U A1915
−64.150
98.082
108.167
1.00
39.28
O


ATOM
41000
C5′
U A1915
−64.923
97.857
109.342
1.00
39.28
C


ATOM
41001
C4′
U A1915
−64.051
97.713
110.575
1.00
39.28
C


ATOM
41002
O4′
U A1915
−63.158
96.579
110.423
1.00
39.28
O


ATOM
41003
C3′
U A1915
−63.126
98.877
110.888
1.00
39.28
C


ATOM
41004
O3′
U A1915
−63.774
99.931
111.572
1.00
39.28
O


ATOM
41005
C2′
U A1915
−62.013
98.219
111.695
1.00
39.28
C


ATOM
41006
O2′
U A1915
−62.397
98.036
113.042
1.00
39.28
O


ATOM
41007
C1′
U A1915
−61.915
96.854
111.028
1.00
39.28
C


ATOM
41008
N1
U A1915
−60.870
96.837
109.987
1.00
39.93
N


ATOM
41009
C2
U A1915
−59.553
96.781
110.443
1.00
39.93
C


ATOM
41010
O2
U A1915
−59.248
96.718
111.640
1.00
39.93
O


ATOM
41011
N3
U A1915
−58.617
96.798
109.431
1.00
39.93
N


ATOM
41012
C4
U A1915
−58.869
96.866
108.072
1.00
39.93
C


ATOM
41013
O4
U A1915
−57.910
96.863
107.303
1.00
39.93
O


ATOM
41014
C5
U A1915
−60.250
96.933
107.682
1.00
39.93
C


ATOM
41015
C6
U A1915
−61.181
96.921
108.639
1.00
39.93
C


ATOM
41016
P
A A1916
−62.990
101.299
111.861
1.00
40.79
P


ATOM
41017
OP1
A A1916
−63.608
101.913
113.062
1.00
40.79
O


ATOM
41018
OP2
A A1916
−62.979
102.068
110.589
1.00
40.79
O


ATOM
41019
O5′
A A1916
−61.508
100.800
112.206
1.00
40.79
O


ATOM
41020
C5′
A A1916
−60.962
100.968
113.508
1.00
40.79
C


ATOM
41021
C4′
A A1916
−59.454
100.912
113.494
1.00
40.79
C


ATOM
41022
O4′
A A1916
−59.011
99.843
112.627
1.00
40.79
O


ATOM
41023
C3′
A A1916
−58.756
102.135
112.941
1.00
40.79
C


ATOM
41024
O3′
A A1916
−58.643
103.167
113.875
1.00
40.79
O


ATOM
41025
C2′
A A1916
−57.426
101.592
112.472
1.00
40.79
C


ATOM
41026
O2′
A A1916
−56.547
101.396
113.564
1.00
40.79
O


ATOM
41027
C1′
A A1916
−57.849
100.241
111.926
1.00
40.79
C


ATOM
41028
N9
A A1916
−58.191
100.324
110.505
1.00
40.80
N


ATOM
41029
C8
A A1916
−59.444
100.378
109.947
1.00
40.80
C


ATOM
41030
N7
A A1916
−59.451
100.441
108.641
1.00
40.80
N


ATOM
41031
C5
A A1916
−58.104
100.429
108.339
1.00
40.80
C


ATOM
41032
C6
A A1916
−57.446
100.475
107.115
1.00
40.80
C


ATOM
41033
N6
A A1916
−58.091
100.544
105.947
1.00
40.80
N


ATOM
41034
N1
A A1916
−56.095
100.454
107.160
1.00
40.80
N


ATOM
41035
C2
A A1916
−55.474
100.386
108.353
1.00
40.80
C


ATOM
41036
N3
A A1916
−55.994
100.340
109.576
1.00
40.80
N


ATOM
41037
C4
A A1916
−57.321
100.361
109.477
1.00
40.80
C


ATOM
41038
P
U A1917
−59.362
104.553
113.563
1.00
18.47
P


ATOM
41039
OP1
U A1917
−59.681
105.177
114.864
1.00
18.47
O


ATOM
41040
OP2
U A1917
−60.476
104.252
112.608
1.00
18.47
O


ATOM
41041
O5′
U A1917
−58.219
105.381
112.820
1.00
18.47
O


ATOM
41042
C5′
U A1917
−56.958
105.559
113.430
1.00
18.47
C


ATOM
41043
C4′
U A1917
−55.843
105.202
112.504
1.00
18.47
C


ATOM
41044
O4′
U A1917
−56.155
103.974
111.813
1.00
18.47
O


ATOM
41045
C3′
U A1917
−55.570
106.188
111.391
1.00
18.47
C


ATOM
41046
O3′
U A1917
−54.811
107.294
111.827
1.00
18.47
O


ATOM
41047
C2′
U A1917
−54.859
105.328
110.359
1.00
18.47
C


ATOM
41048
O2′
U A1917
−53.498
105.132
110.711
1.00
18.47
O


ATOM
41049
C1′
U A1917
−55.595
104.000
110.517
1.00
18.47
C


ATOM
41050
N1
U A1917
−56.680
103.850
109.529
1.00
18.57
N


ATOM
41051
C2
U A1917
−56.296
103.875
108.216
1.00
18.57
C


ATOM
41052
O2
U A1917
−55.141
104.009
107.861
1.00
18.57
O


ATOM
41053
N3
U A1917
−57.329
103.735
107.336
1.00
18.57
N


ATOM
41054
C4
U A1917
−58.667
103.579
107.612
1.00
18.57
C


ATOM
41055
O4
U A1917
−59.448
103.474
106.668
1.00
18.57
O


ATOM
41056
C5
U A1917
−59.000
103.565
108.999
1.00
18.57
C


ATOM
41057
C6
U A1917
−58.008
103.699
109.888
1.00
18.57
C


ATOM
41058
P
A A1918
−55.215
108.775
111.370
1.00
15.03
P


ATOM
41059
OP1
A A1918
−54.284
109.710
112.047
1.00
15.03
O


ATOM
41060
OP2
A A1918
−56.683
108.926
111.598
1.00
15.03
O


ATOM
41061
O5′
A A1918
−54.889
108.735
109.817
1.00
15.03
O


ATOM
41062
C5′
A A1918
−53.601
108.312
109.379
1.00
15.03
C


ATOM
41063
C4′
A A1918
−53.522
108.199
107.880
1.00
15.03
C


ATOM
41064
O4′
A A1918
−54.519
107.246
107.415
1.00
15.03
O


ATOM
41065
C3′
A A1918
−53.755
109.498
107.128
1.00
15.03
C


ATOM
41066
O3′
A A1918
−52.817
109.622
106.080
1.00
15.03
O


ATOM
41067
C2′
A A1918
−55.151
109.354
106.547
1.00
15.03
C


ATOM
41068
O2′
A A1918
−55.317
109.983
105.290
1.00
15.03
O


ATOM
41069
C1′
A A1918
−55.352
107.834
106.447
1.00
15.03
C


ATOM
41070
N9
A A1918
−56.723
107.435
106.738
1.00
14.94
N


ATOM
41071
C8
A A1918
−57.255
107.364
107.990
1.00
14.94
C


ATOM
41072
N7
A A1918
−58.518
107.046
108.006
1.00
14.94
N


ATOM
41073
C5
A A1918
−58.840
106.921
106.670
1.00
14.94
C


ATOM
41074
C6
A A1918
−60.050
106.598
106.033
1.00
14.94
C


ATOM
41075
N6
A A1918
−61.171
106.337
106.718
1.00
14.94
N


ATOM
41076
N1
A A1918
−60.064
106.555
104.674
1.00
14.94
N


ATOM
41077
C2
A A1918
−58.922
106.828
104.025
1.00
14.94
C


ATOM
41078
N3
A A1918
−57.728
107.151
104.535
1.00
14.94
N


ATOM
41079
C4
A A1918
−57.748
107.179
105.874
1.00
14.94
C


ATOM
41080
P
A A1919
−51.570
110.612
106.246
1.00
18.21
P


ATOM
41081
OP1
A A1919
−50.538
109.875
107.053
1.00
18.21
O


ATOM
41082
OP2
A A1919
−52.104
111.911
106.763
1.00
18.21
O


ATOM
41083
O5′
A A1919
−51.075
110.793
104.733
1.00
18.21
O


ATOM
41084
C5′
A A1919
−49.698
110.910
104.410
1.00
18.21
C


ATOM
41085
C4′
A A1919
−49.386
110.225
103.107
1.00
18.21
C


ATOM
41086
O4′
A A1919
−49.758
108.824
103.200
1.00
18.21
O


ATOM
41087
C3′
A A1919
−50.158
110.720
101.894
1.00
18.21
C


ATOM
41088
O3′
A A1919
−49.597
111.864
101.307
1.00
18.21
O


ATOM
41089
C2′
A A1919
−50.149
109.508
100.991
1.00
18.21
C


ATOM
41090
O2′
A A1919
−48.856
109.307
100.440
1.00
18.21
O


ATOM
41091
C1′
A A1919
−50.415
108.422
102.014
1.00
18.21
C


ATOM
41092
N9
A A1919
−51.847
108.317
102.324
1.00
18.07
N


ATOM
41093
C8
A A1919
−52.370
108.370
103.592
1.00
18.07
C


ATOM
41094
N7
A A1919
−53.670
108.295
103.642
1.00
18.07
N


ATOM
41095
C5
A A1919
−54.022
108.193
102.315
1.00
18.07
C


ATOM
41096
C6
A A1919
−55.269
108.072
101.717
1.00
18.07
C


ATOM
41097
N6
A A1919
−56.395
108.041
102.426
1.00
18.07
N


ATOM
41098
N1
A A1919
−55.311
108.003
100.373
1.00
18.07
N


ATOM
41099
C2
A A1919
−54.162
108.043
99.694
1.00
18.07
C


ATOM
41100
N3
A A1919
−52.918
108.155
100.151
1.00
18.07
N


ATOM
41101
C4
A A1919
−52.919
108.222
101.487
1.00
18.07
C


ATOM
41102
P
C A1920
−50.378
113.246
101.400
1.00
13.85
P


ATOM
41103
OP1
C A1920
−49.583
114.235
100.648
1.00
13.85
O


ATOM
41104
OP2
C A1920
−50.665
113.492
102.828
1.00
13.85
O


ATOM
41105
O5′
C A1920
−51.732
112.941
100.633
1.00
13.85
O


ATOM
41106
C5′
C A1920
−51.751
112.689
99.236
1.00
13.85
C


ATOM
41107
C4′
C A1920
−53.169
112.601
98.738
1.00
13.85
C


ATOM
41108
O4′
C A1920
−53.847
111.497
99.404
1.00
13.85
O


ATOM
41109
C3′
C A1920
−54.028
113.813
99.038
1.00
13.85
C


ATOM
41110
O3′
C A1920
−53.926
114.801
98.047
1.00
13.85
O


ATOM
41111
C2′
C A1920
−55.429
113.231
99.195
1.00
13.85
C


ATOM
41112
O2′
C A1920
−56.029
112.977
97.931
1.00
13.85
O


ATOM
41113
C1′
C A1920
−55.112
111.900
99.871
1.00
13.85
C


ATOM
41114
N1
C A1920
−55.024
112.038
101.349
1.00
14.42
N


ATOM
41115
C2
C A1920
−56.108
112.548
102.080
1.00
14.42
C


ATOM
41116
O2
C A1920
−57.128
112.854
101.452
1.00
14.42
O


ATOM
41117
N3
C A1920
−56.010
112.699
103.438
1.00
14.42
N


ATOM
41118
C4
C A1920
−54.869
112.349
104.069
1.00
14.42
C


ATOM
41119
N4
C A1920
−54.789
112.501
105.400
1.00
14.42
N


ATOM
41120
C5
C A1920
−53.754
111.812
103.334
1.00
14.42
C


ATOM
41121
C6
C A1920
−53.866
111.685
101.997
1.00
14.42
C


ATOM
41122
P
G A1921
−53.726
116.329
98.472
1.00
15.45
P


ATOM
41123
OP1
G A1921
−53.165
117.033
97.283
1.00
15.45
O


ATOM
41124
OP2
G A1921
−52.967
116.347
99.758
1.00
15.45
O


ATOM
41125
O5′
G A1921
−55.210
116.804
98.723
1.00
15.45
O


ATOM
41126
C5′
G A1921
−56.168
116.637
97.714
1.00
15.45
C


ATOM
41127
C4′
G A1921
−57.535
116.564
98.281
1.00
15.45
C


ATOM
41128
O4′
G A1921
−57.567
115.626
99.389
1.00
15.45
O


ATOM
41129
C3′
G A1921
−58.053
117.841
98.886
1.00
15.45
C


ATOM
41130
O3′
G A1921
−58.430
118.798
97.911
1.00
15.45
O


ATOM
41131
C2′
G A1921
−59.195
117.323
99.753
1.00
15.45
C


ATOM
41132
O2′
G A1921
−60.346
117.013
98.981
1.00
15.45
O


ATOM
41133
C1′
G A1921
−58.589
116.015
100.281
1.00
15.45
C


ATOM
41134
N9
G A1921
−58.016
116.201
101.613
1.00
15.48
N


ATOM
41135
C8
G A1921
−56.729
116.255
102.059
1.00
15.48
C


ATOM
41136
N7
G A1921
−56.683
116.492
103.349
1.00
15.48
N


ATOM
41137
C5
G A1921
−58.008
116.601
103.739
1.00
15.48
C


ATOM
41138
C6
G A1921
−58.605
116.844
104.989
1.00
15.48
C


ATOM
41139
O6
G A1921
−58.040
117.014
106.064
1.00
15.48
O


ATOM
41140
N1
G A1921
−59.991
116.876
104.931
1.00
15.48
N


ATOM
41141
C2
G A1921
−60.712
116.691
103.792
1.00
15.48
C


ATOM
41142
N2
G A1921
−62.042
116.748
103.895
1.00
15.48
N


ATOM
41143
N3
G A1921
−60.172
116.464
102.619
1.00
15.48
N


ATOM
41144
C4
G A1921
−58.830
116.432
102.677
1.00
15.48
C


ATOM
41145
P
G A1922
−58.188
120.379
98.166
1.00
22.26
P


ATOM
41146
OP1
G A1922
−58.232
121.061
96.833
1.00
22.26
O


ATOM
41147
OP2
G A1922
−56.962
120.522
99.006
1.00
22.26
O


ATOM
41148
O5′
G A1922
−59.459
120.772
99.011
1.00
22.26
O


ATOM
41149
C5′
G A1922
−60.729
120.253
98.687
1.00
22.26
C


ATOM
41150
C4′
G A1922
−61.662
120.463
99.821
1.00
22.26
C


ATOM
41151
O4′
G A1922
−61.374
119.496
100.862
1.00
22.26
O


ATOM
41152
C3′
G A1922
−61.523
121.799
100.524
1.00
22.26
C


ATOM
41153
O3′
G A1922
−62.172
122.851
99.841
1.00
22.26
O


ATOM
41154
C2′
G A1922
−62.113
121.502
101.888
1.00
22.26
C


ATOM
41155
O2′
G A1922
−63.539
121.492
101.829
1.00
22.26
O


ATOM
41156
C1′
G A1922
−61.614
120.072
102.123
1.00
22.26
C


ATOM
41157
N9
G A1922
−60.368
120.037
102.904
1.00
21.71
N


ATOM
41158
C8
G A1922
−59.077
119.846
102.487
1.00
21.71
C


ATOM
41159
N7
G A1922
−58.214
119.880
103.472
1.00
21.71
N


ATOM
41160
C5
G A1922
−58.999
120.115
104.594
1.00
21.71
C


ATOM
41161
C6
G A1922
−58.660
120.257
105.962
1.00
21.71
C


ATOM
41162
O6
G A1922
−57.541
120.213
106.482
1.00
21.71
O


ATOM
41163
N1
G A1922
−59.777
120.478
106.759
1.00
21.71
N


ATOM
41164
C2
G A1922
−61.064
120.564
106.304
1.00
21.71
C


ATOM
41165
N2
G A1922
−62.033
120.793
107.206
1.00
21.71
N


ATOM
41166
N3
G A1922
−61.381
120.437
105.030
1.00
21.71
N


ATOM
41167
C4
G A1922
−60.317
120.211
104.249
1.00
21.71
C


ATOM
41168
P
U A1923
−61.367
124.177
99.427
1.00
15.44
P


ATOM
41169
OP1
U A1923
−62.103
124.790
98.303
1.00
15.44
O


ATOM
41170
OP2
U A1923
−59.953
123.800
99.217
1.00
15.44
O


ATOM
41171
O5′
U A1923
−61.492
125.085
100.727
1.00
15.44
O


ATOM
41172
C5′
U A1923
−62.764
125.452
101.239
1.00
15.44
C


ATOM
41173
C4′
U A1923
−62.754
125.551
102.748
1.00
15.44
C


ATOM
41174
O4′
U A1923
−62.186
124.344
103.329
1.00
15.44
O


ATOM
41175
C3′
U A1923
−61.913
126.670
103.354
1.00
15.44
C


ATOM
41176
O3′
U A1923
−62.541
127.935
103.282
1.00
15.44
O


ATOM
41177
C2′
U A1923
−61.693
126.178
104.781
1.00
15.44
C


ATOM
41178
O2′
U A1923
−62.806
126.479
105.604
1.00
15.44
O


ATOM
41179
C1′
U A1923
−61.617
124.654
104.585
1.00
15.44
C


ATOM
41180
N1
U A1923
−60.218
124.166
104.638
1.00
16.02
N


ATOM
41181
C2
U A1923
−59.879
123.670
105.878
1.00
16.02
C


ATOM
41182
O2
U A1923
−60.695
123.600
106.798
1.00
16.02
O


ATOM
41183
N3
U A1923
−58.574
123.250
106.008
1.00
16.02
N


ATOM
41184
C4
U A1923
−57.581
123.279
105.056
1.00
16.02
C


ATOM
41185
O4
U A1923
−56.462
122.846
105.370
1.00
16.02
O


ATOM
41186
C5
U A1923
−58.002
123.832
103.796
1.00
16.02
C


ATOM
41187
C6
U A1923
−59.274
124.249
103.635
1.00
16.02
C


ATOM
41188
P
C A1924
−61.704
129.278
103.562
1.00
19.15
P


ATOM
41189
OP1
C A1924
−62.594
130.418
103.220
1.00
19.15
O


ATOM
41190
OP2
C A1924
−60.410
129.152
102.853
1.00
19.15
O


ATOM
41191
O5′
C A1924
−61.462
129.230
105.139
1.00
19.15
O


ATOM
41192
C5′
C A1924
−62.532
129.440
106.040
1.00
19.15
C


ATOM
41193
C4′
C A1924
−62.045
129.566
107.457
1.00
19.15
C


ATOM
41194
O4′
C A1924
−61.628
128.271
107.957
1.00
19.15
O


ATOM
41195
C3′
C A1924
−60.828
130.435
107.673
1.00
19.15
C


ATOM
41196
O3′
C A1924
−61.139
131.799
107.710
1.00
19.15
O


ATOM
41197
C2′
C A1924
−60.301
129.912
108.990
1.00
19.15
C


ATOM
41198
O2′
C A1924
−61.130
130.337
110.057
1.00
19.15
O


ATOM
41199
C1′
C A1924
−60.512
128.424
108.804
1.00
19.15
C


ATOM
41200
N1
C A1924
−59.359
127.778
108.167
1.00
18.80
N


ATOM
41201
C2
C A1924
−58.264
127.499
108.968
1.00
18.80
C


ATOM
41202
O2
C A1924
−58.333
127.843
110.152
1.00
18.80
O


ATOM
41203
N3
C A1924
−57.190
126.882
108.425
1.00
18.80
N


ATOM
41204
C4
C A1924
−57.208
126.546
107.134
1.00
18.80
C


ATOM
41205
N4
C A1924
−56.132
125.939
106.638
1.00
18.80
N


ATOM
41206
C5
C A1924
−58.328
126.817
106.290
1.00
18.80
C


ATOM
41207
C6
C A1924
−59.373
127.435
106.844
1.00
18.80
C


ATOM
41208
P
C A1925
−60.072
132.865
107.204
1.00
14.22
P


ATOM
41209
OP1
C A1925
−60.667
134.209
107.423
1.00
14.22
O


ATOM
41210
OP2
C A1925
−59.687
132.466
105.831
1.00
14.22
O


ATOM
41211
O5′
C A1925
−58.854
132.637
108.204
1.00
14.22
O


ATOM
41212
C5′
C A1925
−59.006
132.921
109.583
1.00
14.22
C


ATOM
41213
C4′
C A1925
−57.781
132.549
110.374
1.00
14.22
C


ATOM
41214
O4′
C A1925
−57.538
131.126
110.283
1.00
14.22
O


ATOM
41215
C3′
C A1925
−56.481
133.171
109.914
1.00
14.22
C


ATOM
41216
O3′
C A1925
−56.332
134.504
110.351
1.00
14.22
O


ATOM
41217
C2′
C A1925
−55.464
132.223
110.499
1.00
14.22
C


ATOM
41218
O2′
C A1925
−55.350
132.411
111.901
1.00
14.22
O


ATOM
41219
C1′
C A1925
−56.155
130.890
110.238
1.00
14.22
C


ATOM
41220
N1
C A1925
−55.833
130.374
108.908
1.00
14.59
N


ATOM
41221
C2
C A1925
−54.641
129.678
108.756
1.00
14.59
C


ATOM
41222
O2
C A1925
−53.954
129.522
109.767
1.00
14.59
O


ATOM
41223
N3
C A1925
−54.275
129.188
107.544
1.00
14.59
N


ATOM
41224
C4
C A1925
−55.084
129.393
106.490
1.00
14.59
C


ATOM
41225
N4
C A1925
−54.695
128.898
105.294
1.00
14.59
N


ATOM
41226
C5
C A1925
−56.324
130.120
106.620
1.00
14.59
C


ATOM
41227
C6
C A1925
−56.653
130.592
107.839
1.00
14.59
C


ATOM
41228
P
U A1926
−55.180
135.426
109.735
1.00
30.05
P


ATOM
41229
OP1
U A1926
−55.658
136.829
109.765
1.00
30.05
O


ATOM
41230
OP2
U A1926
−54.790
134.829
108.425
1.00
30.05
O


ATOM
41231
O5′
U A1926
−54.021
135.238
110.785
1.00
30.05
O


ATOM
41232
C5′
U A1926
−52.703
135.533
110.425
1.00
30.05
C


ATOM
41233
C4′
U A1926
−51.762
134.501
110.947
1.00
30.05
C


ATOM
41234
O4′
U A1926
−52.233
133.171
110.619
1.00
30.05
O


ATOM
41235
C3′
U A1926
−50.377
134.532
110.362
1.00
30.05
C


ATOM
41236
O3′
U A1926
−49.606
135.599
110.865
1.00
30.05
O


ATOM
41237
C2′
U A1926
−49.874
133.154
110.712
1.00
30.05
C


ATOM
41238
O2′
U A1926
−49.625
133.058
112.107
1.00
30.05
O


ATOM
41239
C1′
U A1926
−51.119
132.331
110.387
1.00
30.05
C


ATOM
41240
N1
U A1926
−51.157
131.906
108.976
1.00
30.24
N


ATOM
41241
C2
U A1926
−50.074
131.318
108.350
1.00
30.24
C


ATOM
41242
O2
U A1926
−48.999
131.089
108.848
1.00
30.24
O


ATOM
41243
N3
U A1926
−50.284
130.995
107.051
1.00
30.24
N


ATOM
41244
C4
U A1926
−51.438
131.188
106.331
1.00
30.24
C


ATOM
41245
O4
U A1926
−51.468
130.834
105.152
1.00
30.24
O


ATOM
41246
C5
U A1926
−52.516
131.791
107.033
1.00
30.24
C


ATOM
41247
C6
U A1926
−52.331
132.118
108.303
1.00
30.24
C


ATOM
41248
P
A A1927
−49.933
137.083
110.347
1.00
11.68
P


ATOM
41249
OP1
A A1927
−50.521
137.843
111.490
1.00
11.68
O


ATOM
41250
OP2
A A1927
−50.739
136.918
109.106
1.00
11.68
O


ATOM
41251
O5′
A A1927
−48.485
137.648
109.980
1.00
11.68
O


ATOM
41252
C5′
A A1927
−47.960
137.503
108.665
1.00
11.68
C


ATOM
41253
C4′
A A1927
−46.591
136.860
108.664
1.00
11.68
C


ATOM
41254
O4′
A A1927
−45.944
137.057
109.932
1.00
11.68
O


ATOM
41255
C3′
A A1927
−46.553
135.358
108.469
1.00
11.68
C


ATOM
41256
O3′
A A1927
−46.689
134.991
107.123
1.00
11.68
O


ATOM
41257
C2′
A A1927
−45.207
134.974
109.057
1.00
11.68
C


ATOM
41258
O2′
A A1927
−44.151
135.210
108.120
1.00
11.68
O


ATOM
41259
C1′
A A1927
−45.082
135.971
110.201
1.00
11.68
C


ATOM
41260
N9
A A1927
−45.450
135.413
111.507
1.00
11.46
N


ATOM
41261
C8
A A1927
−46.647
135.641
112.104
1.00
11.46
C


ATOM
41262
N7
A A1927
−46.730
135.142
113.305
1.00
11.46
N


ATOM
41263
C5
A A1927
−45.495
134.561
113.512
1.00
11.46
C


ATOM
41264
C6
A A1927
−44.974
133.860
114.612
1.00
11.46
C


ATOM
41265
N6
A A1927
−45.697
133.645
115.712
1.00
11.46
N


ATOM
41266
N1
A A1927
−43.702
133.391
114.546
1.00
11.46
N


ATOM
41267
C2
A A1927
−43.022
133.651
113.423
1.00
11.46
C


ATOM
41268
N3
A A1927
−43.425
134.300
112.327
1.00
11.46
N


ATOM
41269
C4
A A1927
−44.683
134.738
112.424
1.00
11.46
C


ATOM
41270
P
A A1928
−47.798
133.927
106.706
1.00
9.61
P


ATOM
41271
OP1
A A1928
−48.017
134.087
105.251
1.00
9.61
O


ATOM
41272
OP2
A A1928
−48.955
134.116
107.631
1.00
9.61
O


ATOM
41273
O5′
A A1928
−47.067
132.532
106.996
1.00
9.61
O


ATOM
41274
C5′
A A1928
−45.886
132.178
106.287
1.00
9.61
C


ATOM
41275
C4′
A A1928
−44.957
131.314
107.111
1.00
9.61
C


ATOM
41276
O4′
A A1928
−44.628
131.969
108.360
1.00
9.61
O


ATOM
41277
C3′
A A1928
−45.496
129.958
107.537
1.00
9.61
C


ATOM
41278
O3′
A A1928
−45.400
128.984
106.516
1.00
9.61
O


ATOM
41279
C2′
A A1928
−44.647
129.628
108.753
1.00
9.61
C


ATOM
41280
O2′
A A1928
−43.390
129.099
108.366
1.00
9.61
O


ATOM
41281
C1′
A A1928
−44.432
131.002
109.371
1.00
9.61
C


ATOM
41282
N9
A A1928
−45.385
131.253
110.453
1.00
9.14
N


ATOM
41283
C8
A A1928
−46.650
131.728
110.322
1.00
9.14
C


ATOM
41284
N7
A A1928
−47.268
131.842
111.462
1.00
9.14
N


ATOM
41285
C5
A A1928
−46.352
131.408
112.392
1.00
9.14
C


ATOM
41286
C6
A A1928
−46.429
131.280
113.781
1.00
9.14
C


ATOM
41287
N6
A A1928
−47.561
131.613
114.415
1.00
9.14
N


ATOM
41288
N1
A A1928
−45.326
130.795
114.456
1.00
9.14
N


ATOM
41289
C2
A A1928
−44.229
130.446
113.761
1.00
9.14
C


ATOM
41290
N3
A A1928
−44.055
130.522
112.430
1.00
9.14
N


ATOM
41291
C4
A A1928
−45.167
131.024
111.795
1.00
9.14
C


ATOM
41292
P
G A1929
−46.705
128.158
106.070
1.00
23.81
P


ATOM
41293
OP1
G A1929
−46.216
126.936
105.362
1.00
23.81
O


ATOM
41294
OP2
G A1929
−47.597
129.115
105.346
1.00
23.81
O


ATOM
41295
O5′
G A1929
−47.372
127.754
107.466
1.00
23.81
O


ATOM
41296
C5′
G A1929
−47.526
126.386
107.845
1.00
23.81
C


ATOM
41297
C4′
G A1929
−46.609
126.004
108.989
1.00
23.81
C


ATOM
41298
O4′
G A1929
−46.616
127.053
109.996
1.00
23.81
O


ATOM
41299
C3′
G A1929
−47.002
124.738
109.724
1.00
23.81
C


ATOM
41300
O3′
G A1929
−45.847
124.141
110.261
1.00
23.81
O


ATOM
41301
C2′
G A1929
−47.846
125.261
110.856
1.00
23.81
C


ATOM
41302
O2′
G A1929
−47.945
124.390
111.955
1.00
23.81
O


ATOM
41303
C1′
G A1929
−47.096
126.534
111.217
1.00
23.81
C


ATOM
41304
N9
G A1929
−47.952
127.533
111.841
1.00
23.23
N


ATOM
41305
C8
G A1929
−47.826
128.131
113.061
1.00
23.23
C


ATOM
41306
N7
G A1929
−48.821
128.925
113.318
1.00
23.23
N


ATOM
41307
C5
G A1929
−49.657
128.810
112.216
1.00
23.23
C


ATOM
41308
C6
G A1929
−50.889
129.430
111.904
1.00
23.23
C


ATOM
41309
O6
G A1929
−51.544
130.240
112.567
1.00
23.23
O


ATOM
41310
N1
G A1929
−51.370
129.040
110.669
1.00
23.23
N


ATOM
41311
C2
G A1929
−50.762
128.165
109.833
1.00
23.23
C


ATOM
41312
N2
G A1929
−51.396
127.921
108.687
1.00
23.23
N


ATOM
41313
N3
G A1929
−49.624
127.571
110.102
1.00
23.23
N


ATOM
41314
C4
G A1929
−49.134
127.944
111.302
1.00
23.23
C


ATOM
41315
P
G A1930
−44.794
123.454
109.288
1.00
15.78
P


ATOM
41316
OP1
G A1930
−44.061
124.570
108.592
1.00
15.78
O


ATOM
41317
OP2
G A1930
−45.524
122.430
108.477
1.00
15.78
O


ATOM
41318
O5′
G A1930
−43.842
122.728
110.306
1.00
15.78
O


ATOM
41319
C5′
G A1930
−42.827
123.445
110.976
1.00
15.78
C


ATOM
41320
C4′
G A1930
−41.830
122.506
111.544
1.00
15.78
C


ATOM
41321
O4′
G A1930
−41.384
123.018
112.822
1.00
15.78
O


ATOM
41322
C3′
G A1930
−42.384
121.113
111.827
1.00
15.78
C


ATOM
41323
O3′
G A1930
−41.349
120.148
111.661
1.00
15.78
O


ATOM
41324
C2′
G A1930
−42.753
121.213
113.293
1.00
15.78
C


ATOM
41325
O2′
G A1930
−42.869
119.978
113.951
1.00
15.78
O


ATOM
41326
C1′
G A1930
−41.568
122.018
113.789
1.00
15.78
C


ATOM
41327
N9
G A1930
−41.737
122.649
115.078
1.00
14.92
N


ATOM
41328
C8
G A1930
−42.851
123.023
115.766
1.00
14.92
C


ATOM
41329
N7
G A1930
−42.541
123.553
116.913
1.00
14.92
N


ATOM
41330
C5
G A1930
−41.141
123.501
116.954
1.00
14.92
C


ATOM
41331
C6
G A1930
−40.206
123.927
117.925
1.00
14.92
C


ATOM
41332
O6
G A1930
−40.456
124.460
119.006
1.00
14.92
O


ATOM
41333
N1
G A1930
−38.889
123.703
117.550
1.00
14.92
N


ATOM
41334
C2
G A1930
−38.523
123.142
116.376
1.00
14.92
C


ATOM
41335
N2
G A1930
−37.222
123.010
116.179
1.00
14.92
N


ATOM
41336
N3
G A1930
−39.365
122.743
115.459
1.00
14.92
N


ATOM
41337
C4
G A1930
−40.642
122.948
115.820
1.00
14.92
C


ATOM
41338
P
U A1931
−41.710
118.593
111.605
1.00
20.12
P


ATOM
41339
OP1
U A1931
−42.990
118.465
110.881
1.00
20.12
O


ATOM
41340
OP2
U A1931
−41.632
118.084
112.977
1.00
20.12
O


ATOM
41341
O5′
U A1931
−40.526
117.988
110.724
1.00
20.12
O


ATOM
41342
C5′
U A1931
−40.642
117.903
109.314
1.00
20.12
C


ATOM
41343
C4′
U A1931
−39.405
118.415
108.615
1.00
20.12
C


ATOM
41344
O4′
U A1931
−39.127
119.776
109.011
1.00
20.12
O


ATOM
41345
C3′
U A1931
−38.103
117.689
108.911
1.00
20.12
C


ATOM
41346
O3′
U A1931
−37.987
116.478
108.217
1.00
20.12
O


ATOM
41347
C2′
U A1931
−37.068
118.703
108.485
1.00
20.12
C


ATOM
41348
O2′
U A1931
−36.926
118.705
107.071
1.00
20.12
O


ATOM
41349
C1′
U A1931
−37.734
120.011
108.902
1.00
20.12
C


ATOM
41350
N1
U A1931
−37.208
120.525
110.197
1.00
20.00
N


ATOM
41351
C2
U A1931
−35.807
120.615
110.367
1.00
20.00
C


ATOM
41352
O2
U A1931
−34.940
120.268
109.566
1.00
20.00
O


ATOM
41353
N3
U A1931
−35.429
121.128
111.575
1.00
20.00
N


ATOM
41354
C4
U A1931
−36.252
121.561
112.583
1.00
20.00
C


ATOM
41355
O4
U A1931
−35.739
121.996
113.605
1.00
20.00
O


ATOM
41356
C5
U A1931
−37.654
121.441
112.336
1.00
20.00
C


ATOM
41357
C6
U A1931
−38.081
120.941
111.179
1.00
20.00
C


TER


END
















TABLE 8





H69 Neomycin Binding Site for Intermediate-Rotated Ribosome

























ATOM
48797
P
G
A1515
−75.974
5.456
3.358
1.00
86.56
P


ATOM
48798
OP1
G
A1515
−75.617
4.050
3.662
1.00
86.56
O


ATOM
48799
OP2
G
A1515
−76.170
5.852
1.942
1.00
86.56
O


ATOM
48800
O5′
G
A1515
−77.235
5.896
4.223
1.00
86.56
O


ATOM
48801
C5′
G
A1515
−78.538
5.476
3.865
1.00
86.56
C


ATOM
48802
C4′
G
A1515
−79.598
6.372
4.449
1.00
86.56
C


ATOM
48803
O4′
G
A1515
−79.192
7.763
4.344
1.00
86.56
O


ATOM
48804
C1′
G
A1515
−80.318
8.574
4.069
1.00
86.56
C


ATOM
48805
N9
G
A1515
−80.130
9.194
2.744
1.00
102.19
N


ATOM
48806
C4
G
A1515
−81.026
9.974
2.051
1.00
102.19
C


ATOM
48807
N3
G
A1515
−82.267
10.320
2.452
1.00
102.19
N


ATOM
48808
C2
G
A1515
−82.883
11.075
1.556
1.00
102.19
C


ATOM
48809
N2
G
A1515
−84.132
11.510
1.797
1.00
102.19
N


ATOM
48810
N1
G
A1515
−82.322
11.461
0.362
1.00
102.19
N


ATOM
48811
C6
G
A1515
−81.048
11.115
−0.070
1.00
102.19
C


ATOM
48812
O6
G
A1515
−80.632
11.508
−1.164
1.00
102.19
O


ATOM
48813
C5
G
A1515
−80.383
10.306
0.879
1.00
102.19
C


ATOM
48814
N7
G
A1515
−79.114
9.757
0.830
1.00
102.19
N


ATOM
48815
C8
G
A1515
−79.009
9.108
1.953
1.00
102.19
C


ATOM
48816
C2′
G
A1515
−81.552
7.674
4.109
1.00
86.56
C


ATOM
48817
O2′
G
A1515
−82.068
7.664
5.432
1.00
86.56
O


ATOM
48818
C3′
G
A1515
−80.943
6.329
3.751
1.00
86.56
C


ATOM
48819
O3′
G
A1515
−81.726
5.220
4.140
1.00
86.56
O


ATOM
48831
P
G
A1516
−81.762
3.900
3.228
1.00
74.90
P


ATOM
48832
OP1
G
A1516
−81.772
2.736
4.146
1.00
74.90
O


ATOM
48833
OP2
G
A1516
−80.664
4.014
2.235
1.00
74.90
O


ATOM
48834
O5′
G
A1516
−83.166
4.027
2.501
1.00
74.90
O


ATOM
48835
C5′
G
A1516
−84.358
4.103
3.261
1.00
74.90
C


ATOM
48836
C4′
G
A1516
−85.241
5.234
2.806
1.00
74.90
C


ATOM
48837
O4′
G
A1516
−84.463
6.443
2.620
1.00
74.90
O


ATOM
48838
C1′
G
A1516
−85.101
7.263
1.660
1.00
74.90
C


ATOM
48839
N9
G
A1516
−84.128
7.628
0.609
1.00
126.22
N


ATOM
48840
C4
G
A1516
−84.429
8.309
−0.545
1.00
126.22
C


ATOM
48841
N3
G
A1516
−85.656
8.735
−0.903
1.00
126.22
N


ATOM
48842
C2
G
A1516
−85.647
9.350
−2.071
1.00
126.22
C


ATOM
48843
N2
G
A1516
−86.799
9.831
−2.563
1.00
126.22
N


ATOM
48844
N1
G
A1516
−84.520
9.541
−2.830
1.00
126.22
N


ATOM
48845
C6
G
A1516
−83.242
9.113
−2.480
1.00
126.22
C


ATOM
48846
O6
G
A1516
−82.293
9.339
−3.240
1.00
126.22
O


ATOM
48847
C5
G
A1516
−83.241
8.445
−1.226
1.00
126.22
C


ATOM
48848
N7
G
A1516
−82.204
7.866
−0.508
1.00
126.22
N


ATOM
48849
C8
G
A1516
−82.776
7.399
0.570
1.00
126.22
C


ATOM
48850
C2′
G
A1516
−86.298
6.481
1.100
1.00
74.90
C


ATOM
48851
O2′
G
A1516
−87.473
6.894
1.783
1.00
74.90
O


ATOM
48852
C3′
G
A1516
−85.929
5.050
1.469
1.00
74.90
C


ATOM
48853
O3′
G
A1516
−87.037
4.170
1.536
1.00
74.90
O


ATOM
48865
P
G
A1517
−86.971
2.734
0.819
1.00
77.49
P


ATOM
48866
OP1
G
A1517
−88.091
1.925
1.356
1.00
77.49
O


ATOM
48867
OP2
G
A1517
−85.585
2.228
0.975
1.00
77.49
O


ATOM
48868
O5′
G
A1517
−87.246
3.095
−0.704
1.00
77.49
O


ATOM
48869
C5′
G
A1517
−88.193
4.092
−1.043
1.00
77.49
C


ATOM
48870
C4′
G
A1517
−88.783
3.861
−2.410
1.00
77.49
C


ATOM
48871
O4′
G
A1517
−90.198
3.570
−2.276
1.00
77.49
O


ATOM
48872
C1′
G
A1517
−90.927
4.204
−3.300
1.00
77.49
C


ATOM
48873
N9
G
A1517
−91.823
5.200
−2.680
1.00
92.53
N


ATOM
48874
C4
G
A1517
−92.819
5.937
−3.279
1.00
92.53
C


ATOM
48875
N3
G
A1517
−93.162
5.909
−4.583
1.00
92.53
N


ATOM
48876
C2
G
A1517
−94.155
6.741
−4.853
1.00
92.53
C


ATOM
48877
N2
G
A1517
−94.621
6.835
−6.107
1.00
92.53
N


ATOM
48878
N1
G
A1517
−94.764
7.540
−3.918
1.00
92.53
N


ATOM
48879
C6
G
A1517
−94.428
7.587
−2.571
1.00
92.53
C


ATOM
48880
O6
G
A1517
−95.042
8.342
−1.809
1.00
92.53
O


ATOM
48881
C5
G
A1517
−93.365
6.700
−2.269
1.00
92.53
C


ATOM
48882
N7
G
A1517
−92.738
6.447
−1.059
1.00
92.53
N


ATOM
48883
C8
G
A1517
−91.837
5.551
−1.349
1.00
92.53
C


ATOM
48884
C2′
G
A1517
−89.930
4.833
−4.264
1.00
77.49
C


ATOM
48885
O2′
G
A1517
−89.639
3.896
−5.292
1.00
77.49
O


ATOM
48886
C3′
G
A1517
−88.719
5.046
−3.364
1.00
77.49
C


ATOM
48887
O3′
G
A1517
−87.493
5.113
−4.072
1.00
77.49
O


ATOM
48899
P
A
A1518
−86.457
6.308
−3.792
1.00
74.99
P


ATOM
48900
OP1
A
A1518
−85.146
5.887
−4.341
1.00
74.99
O


ATOM
48901
OP2
A
A1518
−86.552
6.635
−2.356
1.00
74.99
O


ATOM
48902
O5′
A
A1518
−87.050
7.500
−4.661
1.00
74.99
O


ATOM
48903
C5′
A
A1518
−87.174
7.376
−6.068
1.00
74.99
C


ATOM
48904
C4′
A
A1518
−88.306
8.212
−6.603
1.00
74.99
C


ATOM
48905
O4′
A
A1518
−89.564
7.780
−6.023
1.00
74.99
O


ATOM
48906
C1′
A
A1518
−90.431
8.884
−5.879
1.00
74.99
C


ATOM
48907
N9
A
A1518
−90.766
9.036
−4.450
1.00
69.86
N


ATOM
48908
C4
A
A1518
−91.863
9.689
−3.946
1.00
69.86
C


ATOM
48909
N3
A
A1518
−92.834
10.301
−4.642
1.00
69.86
N


ATOM
48910
C2
A
A1518
−93.742
10.828
−3.824
1.00
69.86
C


ATOM
48911
N1
A
A1518
−93.785
10.813
−2.485
1.00
69.86
N


ATOM
48912
C6
A
A1518
−92.791
10.191
−1.814
1.00
69.86
C


ATOM
48913
N6
A
A1518
−92.841
10.173
−0.480
1.00
69.86
N


ATOM
48914
C5
A
A1518
−91.769
9.588
−2.570
1.00
69.86
C


ATOM
48915
N7
A
A1518
−90.629
8.884
−2.207
1.00
69.86
N


ATOM
48916
C8
A
A1518
−90.070
8.581
−3.355
1.00
69.86
C


ATOM
48917
C2′
A
A1518
−89.704
10.115
−6.430
1.00
74.99
C


ATOM
48918
O2′
A
A1518
−90.051
10.288
−7.798
1.00
74.99
O


ATOM
48919
C3′
A
A1518
−88.249
9.695
−6.285
1.00
74.99
C


ATOM
48920
O3′
A
A1518
−87.364
10.402
−7.136
1.00
74.99
O


TER


ATOM
A11M5
P
G
C1903
−76.679
−18.653
17.908
1.00
59.96
P


ATOM
A11M6
OP1
G
C1903
−77.065
−20.028
17.506
1.00
59.96
O


ATOM
A11M7
OP2
G
C1903
−75.411
−18.088
17.385
1.00
59.96
O


ATOM
A11M8
O5′
G
C1903
−77.876
−17.643
17.627
1.00
59.96
O


ATOM
A11M9
C5′
G
C1903
−78.973
−18.009
16.806
1.00
59.96
C


ATOM
A11MA
C4′
G
C1903
−80.265
−17.456
17.344
1.00
59.96
C


ATOM
A11MB
O4′
G
C1903
−79.987
−16.435
18.341
1.00
59.96
O


ATOM
A11MC
C1′
G
C1903
−80.957
−15.413
18.267
1.00
59.96
C


ATOM
A11MD
N9
G
C1903
−80.282
−14.153
17.900
1.00
57.44
N


ATOM
A11ME
C4
G
C1903
−80.886
−12.946
17.653
1.00
57.44
C


ATOM
A11MF
N3
G
C1903
−82.210
−12.703
17.702
1.00
57.44
N


ATOM
A11MG
C2
G
C1903
−82.494
−11.446
17.411
1.00
57.44
C


ATOM
A11MH
N2
G
C1903
−83.775
−11.048
17.418
1.00
57.44
N


ATOM
A11MI
N1
G
C1903
−81.548
−10.498
17.098
1.00
57.44
N


ATOM
A11MJ
C6
G
C1903
−80.177
−10.727
17.042
1.00
57.44
C


ATOM
A11MK
O6
G
C1903
−79.408
−9.804
16.750
1.00
57.44
O


ATOM
A11ML
C5
G
C1903
−79.861
−12.075
17.351
1.00
57.44
C


ATOM
A11MM
N7
G
C1903
−78.634
−12.718
17.409
1.00
57.44
N


ATOM
A11MN
C8
G
C1903
−78.932
−13.945
17.737
1.00
57.44
C


ATOM
A11MO
C2′
G
C1903
−81.990
−15.837
17.222
1.00
59.96
C


ATOM
A11MP
O2′
G
C1903
−83.022
−16.563
17.872
1.00
59.96
O


ATOM
A11MQ
C3′
G
C1903
−81.157
−16.751
16.337
1.00
59.96
C


ATOM
A11MR
O3′
G
C1903
−81.927
−17.652
15.560
1.00
59.96
O


ATOM
A11N3
P
G
C1904
−82.022
−17.478
13.964
1.00
55.65
P


ATOM
A11N4
OP1
G
C1904
−82.374
−18.805
13.402
1.00
55.65
O


ATOM
A11N5
OP2
G
C1904
−80.768
−16.825
13.513
1.00
55.65
O


ATOM
A11N6
O5′
G
C1904
−83.245
−16.477
13.793
1.00
55.65
O


ATOM
A11N7
C5′
G
C1904
−84.532
−16.806
14.292
1.00
55.65
C


ATOM
A11N8
C4′
G
C1904
−85.449
−15.610
14.284
1.00
55.65
C


ATOM
A11N9
O4′
G
C1904
−84.935
−14.594
15.186
1.00
55.65
O


ATOM
A11NA
C1′
G
C1904
−85.187
−13.309
14.657
1.00
55.65
C


ATOM
A11NB
N9
G
C1904
−83.893
−12.657
14.376
1.00
66.38
N


ATOM
A11NC
C4
G
C1904
−83.697
−11.356
13.975
1.00
66.38
C


ATOM
A11ND
N3
G
C1904
−84.654
−10.427
13.770
1.00
66.38
N


ATOM
A11NE
C2
G
C1904
−84.147
−9.265
13.391
1.00
66.38
C


ATOM
A11NF
N2
G
C1904
−84.963
−8.231
13.144
1.00
66.38
N


ATOM
A11NG
N1
G
C1904
−82.806
−9.032
13.225
1.00
66.38
N


ATOM
A11NH
C6
G
C1904
−81.804
−9.973
13.430
1.00
66.38
C


ATOM
A11NI
O6
G
C1904
−80.621
−9.665
13.253
1.00
66.38
O


ATOM
A11NJ
C5
G
C1904
−82.333
−11.223
13.836
1.00
66.38
C


ATOM
A11NK
N7
G
C1904
−81.683
−12.409
14.138
1.00
66.38
N


ATOM
A11NL
C8
G
C1904
−82.646
−13.229
14.449
1.00
66.38
C


ATOM
A11NM
C2′
G
C1904
−86.017
−13.491
13.390
1.00
55.65
C


ATOM
A11NN
O2′
G
C1904
−87.393
−13.472
13.740
1.00
55.65
O


ATOM
A11NO
C3′
G
C1904
−85.585
−14.882
12.954
1.00
55.65
C


ATOM
A11NP
O3′
G
C1904
−86.492
−15.509
12.065
1.00
55.65
O


ATOM
A11O1
P
C
C1905
−86.064
−15.792
10.540
1.00
64.97
P


ATOM
A11O2
OP1
C
C1905
−87.067
−16.724
9.974
1.00
64.97
O


ATOM
A11O3
OP2
C
C1905
−84.638
−16.202
10.552
1.00
64.97
O


ATOM
A11O4
O5′
C
C1905
−86.209
−14.361
9.858
1.00
64.97
O


ATOM
A11O5
C5′
C
C1905
−87.469
−13.713
9.784
1.00
64.97
C


ATOM
A11O6
C4′
C
C1905
−87.320
−12.215
9.707
1.00
64.97
C


ATOM
A11O7
O4′
C
C1905
−86.285
−11.776
10.617
1.00
64.97
O


ATOM
A11O8
C1′
C
C1905
−85.660
−10.616
10.119
1.00
64.97
C


ATOM
A11O9
N1
C
C1905
−84.194
−10.836
10.074
1.00
64.02
N


ATOM
A11OA
C6
C
C1905
−83.631
−12.085
10.082
1.00
64.02
C


ATOM
A11OB
C2
C
C1905
−83.370
−9.709
10.046
1.00
64.02
C


ATOM
A11OC
O2
C
C1905
−83.890
−8.584
10.044
1.00
64.02
O


ATOM
A11OD
N3
C
C1905
−82.026
−9.862
10.014
1.00
64.02
N


ATOM
A11OE
C4
C
C1905
−81.491
−11.080
10.016
1.00
64.02
C


ATOM
A11OF
N4
C
C1905
−80.161
−11.186
9.984
1.00
64.02
N


ATOM
A11OG
C5
C
C1905
−82.302
−12.249
10.052
1.00
64.02
C


ATOM
A11OH
C2′
C
C1905
−86.252
−10.316
8.737
1.00
64.97
C


ATOM
A11OI
O2′
C
C1905
−87.233
−9.298
8.874
1.00
64.97
O


ATOM
A11OJ
C3′
C
C1905
−86.895
−11.648
8.361
1.00
64.97
C


ATOM
A11OK
O3′
C
C1905
−87.985
−11.509
7.463
1.00
64.97
O


ATOM
A11OW
P
G
C1906
−88.145
−12.490
6.200
1.00
96.23
P


ATOM
A11OX
OP1
G
C1906
−87.207
−13.622
6.396
1.00
96.23
O


ATOM
A11OY
OP2
G
C1906
−88.011
−11.656
4.981
1.00
96.23
O


ATOM
A11OZ
O5′
G
C1906
−89.646
−13.005
6.339
1.00
96.23
O


ATOM
A11P0
C5′
G
C1906
−90.638
−12.211
6.977
1.00
96.23
C


ATOM
A11P1
C4′
G
C1906
−91.918
−12.985
7.171
1.00
96.23
C


ATOM
A11P2
O4′
G
C1906
−92.676
−12.415
8.271
1.00
96.23
O


ATOM
A11P3
C1′
G
C1906
−94.060
−12.519
8.009
1.00
96.23
C


ATOM
A11P4
N9
G
C1906
−94.624
−11.158
7.937
1.00
78.74
N


ATOM
A11P5
C4
G
C1906
−95.933
−10.797
8.146
1.00
78.74
C


ATOM
A11P6
N3
G
C1906
−96.945
−11.632
8.464
1.00
78.74
N


ATOM
A11P7
C2
G
C1906
−98.090
−10.987
8.606
1.00
78.74
C


ATOM
A11P8
N2
G
C1906
−99.200
−11.672
8.919
1.00
78.74
N


ATOM
A11P9
N1
G
C1906
−98.229
−9.629
8.447
1.00
78.74
N


ATOM
A11PA
C6
G
C1906
−97.203
−8.751
8.121
1.00
78.74
C


ATOM
A11PB
O6
G
C1906
−97.440
−7.543
8.003
1.00
78.74
O


ATOM
A11PC
C5
G
C1906
−95.967
−9.430
7.966
1.00
78.74
C


ATOM
A11PD
N7
G
C1906
−94.708
−8.942
7.646
1.00
78.74
N


ATOM
A11PE
C8
G
C1906
−93.946
−10.001
7.640
1.00
78.74
C


ATOM
A11PF
C2′
G
C1906
−94.225
−13.276
6.692
1.00
96.23
C


ATOM
A11PG
O2′
G
C1906
−94.360
−14.662
6.982
1.00
96.23
O


ATOM
A11PH
C3′
G
C1906
−92.897
−12.976
6.004
1.00
96.23
C


ATOM
A11PI
O3′
G
C1906
−92.537
−13.892
4.973
1.00
96.23
O


ATOM
A11PU
P
G
C1907
−93.655
−14.707
4.144
1.00
102.68
P


ATOM
A11PV
OP1
G
C1907
−94.126
−15.810
5.017
1.00
102.68
O


ATOM
A11PW
OP2
G
C1907
−93.056
−15.048
2.830
1.00
102.68
O


ATOM
A11PX
O5′
G
C1907
−94.819
−13.642
3.942
1.00
102.68
O


ATOM
A11PY
C5′
G
C1907
−95.987
−13.972
3.204
1.00
102.68
C


ATOM
A11PZ
C4′
G
C1907
−97.106
−14.434
4.106
1.00
102.68
C


ATOM
A11Q0
O4′
G
C1907
−97.072
−13.687
5.351
1.00
102.68
O


ATOM
A11Q1
C1′
G
C1907
−98.378
−13.339
5.749
1.00
102.68
C


ATOM
A11Q2
N9
G
C1907
−98.520
−11.878
5.614
1.00
85.50
N


ATOM
A11Q3
C4
G
C1907
−99.632
−11.104
5.848
1.00
85.50
C


ATOM
A11Q4
N3
G
C1907
−100.845
−11.533
6.253
1.00
85.50
N


ATOM
A11Q5
C2
G
C1907
−101.704
−10.533
6.384
1.00
85.50
C


ATOM
A11Q6
N2
G
C1907
−102.961
−10.779
6.779
1.00
85.50
N


ATOM
A11Q7
N1
G
C1907
−101.397
−9.218
6.138
1.00
85.50
N


ATOM
A11Q8
C6
G
C1907
−100.154
−8.757
5.721
1.00
85.50
C


ATOM
A11Q9
O6
G
C1907
−99.967
−7.552
5.523
1.00
85.50
O


ATOM
A11QA
C5
G
C1907
−99.227
−9.815
5.575
1.00
85.50
C


ATOM
A11QB
N7
G
C1907
−97.899
−9.772
5.183
1.00
85.50
N


ATOM
A11QC
C8
G
C1907
−97.522
−11.016
5.222
1.00
85.50
C


ATOM
A11QD
C2′
G
C1907
−99.344
−14.095
4.843
1.00
102.68
C


ATOM
A11QE
O2′
G
C1907
−99.597
−15.371
5.415
1.00
102.68
O


ATOM
A11QF
C3′
G
C1907
−98.518
−14.223
3.573
1.00
102.68
C


ATOM
A11QG
O3′
G
C1907
−98.946
−15.268
2.716
1.00
102.68
O


ATOM
A11QS
P
C
C1908
−99.370
−14.952
1.199
1.00
90.49
P


ATOM
A11QT
OP1
C
C1908
−99.405
−16.249
0.478
1.00
90.49
O


ATOM
A11QU
OP2
C
C1908
−98.467
−13.885
0.702
1.00
90.49
O


ATOM
A11QV
O5′
C
C1908
−100.847
−14.382
1.357
1.00
90.49
O


ATOM
A11QW
C5′
C
C1908
−101.877
−15.180
1.918
1.00
90.49
C


ATOM
A11QX
C4′
C
C1908
−102.995
−14.335
2.473
1.00
90.49
C


ATOM
A11QY
O4′
C
C1908
−102.482
−13.431
3.489
1.00
90.49
O


ATOM
A11QZ
C1′
C
C1908
−103.218
−12.224
3.469
1.00
90.49
C


ATOM
A11R0
N1
C
C1908
−102.299
−11.102
3.156
1.00
79.94
N


ATOM
A11R1
C6
C
C1908
−101.011
−11.299
2.730
1.00
79.94
C


ATOM
A11R2
C2
C
C1908
−102.787
−9.801
3.311
1.00
79.94
C


ATOM
A11R3
O2
C
C1908
−103.955
−9.638
3.697
1.00
79.94
O


ATOM
A11R4
N3
C
C1908
−101.984
−8.749
3.034
1.00
79.94
N


ATOM
A11R5
C4
C
C1908
−100.734
−8.953
2.619
1.00
79.94
C


ATOM
A11R6
N4
C
C1908
−99.976
−7.886
2.360
1.00
79.94
N


ATOM
A11R7
C5
C
C1908
−100.206
−10.264
2.454
1.00
79.94
C


ATOM
A11R8
C2′
C
C1908
−104.316
−12.377
2.414
1.00
90.49
C


ATOM
A11R9
O2′
C
C1908
−105.476
−12.900
3.047
1.00
90.49
O


ATOM
A11RA
C3′
C
C1908
−103.687
−13.407
1.489
1.00
90.49
C


ATOM
A11RB
O3′
C
C1908
−104.620
−14.077
0.656
1.00
90.49
O


ATOM
A11RN
P
C
C1909
−104.615
−13.829
−0.935
1.00
97.60
P


ATOM
A11RO
OP1
C
C1909
−105.274
−15.002
−1.562
1.00
97.60
O


ATOM
A11RP
OP2
C
C1909
−103.223
−13.501
−1.329
1.00
97.60
O


ATOM
A11RQ
O5′
C
C1909
−105.538
−12.544
−1.093
1.00
97.60
O


ATOM
A11RR
C5′
C
C1909
−106.874
−12.542
−0.614
1.00
97.60
C


ATOM
A11RS
C4′
C
C1909
−107.414
−11.141
−0.490
1.00
97.60
C


ATOM
A11RT
O4′
C
C1909
−106.609
−10.380
0.449
1.00
97.60
O


ATOM
A11RU
C1′
C
C1909
−106.557
−9.026
0.050
1.00
97.60
C


ATOM
A11RV
N1
C
C1909
−105.140
−8.645
−0.176
1.00
95.16
N


ATOM
A11RW
C6
C
C1909
−104.137
−9.574
−0.279
1.00
95.16
C


ATOM
A11RX
C2
C
C1909
−104.836
−7.284
−0.282
1.00
95.16
C


ATOM
A11RY
O2
C
C1909
−105.753
−6.456
−0.186
1.00
95.16
O


ATOM
A11RZ
N3
C
C1909
−103.555
−6.898
−0.486
1.00
95.16
N


ATOM
A11S0
C4
C
C1909
−102.590
−7.811
−0.585
1.00
95.16
C


ATOM
A11S1
N4
C
C1909
−101.340
−7.390
−0.789
1.00
95.16
N


ATOM
A11S2
C5
C
C1909
−102.866
−9.203
−0.481
1.00
95.16
C


ATOM
A11S3
C2′
C
C1909
−107.400
−8.882
−1.218
1.00
97.60
C


ATOM
A11S4
O2′
C
C1909
−108.715
−8.492
−0.850
1.00
97.60
O


ATOM
A11S5
C3′
C
C1909
−107.383
−10.307
−1.757
1.00
97.60
C


ATOM
A11S6
O3′
C
C1909
−108.455
−10.600
−2.636
1.00
97.60
O


ATOM
A11SI
P
G
C1910
−108.248
−10.478
−4.223
1.00
96.71
P


ATOM
A11SJ
OP1
G
C1910
−109.593
−10.316
−4.828
1.00
96.71
O


ATOM
A11SK
OP2
G
C1910
−107.409
−11.627
−4.647
1.00
96.71
O


ATOM
A11SL
O5′
G
C1910
−107.422
−9.126
−4.359
1.00
96.71
O


ATOM
A11SM
C5′
G
C1910
−107.638
−8.237
−5.443
1.00
96.71
C


ATOM
A11SN
C4′
G
C1910
−107.890
−6.834
−4.959
1.00
96.71
C


ATOM
A11SO
O4′
G
C1910
−107.198
−6.620
−3.700
1.00
96.70
O


ATOM
A11SP
C1′
G
C1910
−106.651
−5.325
−3.657
1.00
96.71
C


ATOM
A11SQ
N9
G
C1910
−105.182
−5.448
−3.622
1.00
106.21
N


ATOM
A11SR
C4
G
C1910
−104.255
−4.436
−3.616
1.00
106.21
C


ATOM
A11SS
N3
G
C1910
−104.516
−3.114
−3.657
1.00
106.21
N


ATOM
A11ST
C2
G
C1910
−103.407
−2.394
−3.644
1.00
106.21
C


ATOM
A11SU
N2
G
C1910
−103.488
−1.055
−3.679
1.00
106.21
N


ATOM
A11SV
N1
G
C1910
−102.144
−2.932
−3.600
1.00
106.21
N


ATOM
A11SW
C6
G
C1910
−101.855
−4.291
−3.561
1.00
106.21
C


ATOM
A11SX
O6
G
C1910
−100.682
−4.679
−3.519
1.00
106.21
O


ATOM
A11SY
C5
G
C1910
−103.033
−5.072
−3.571
1.00
106.21
C


ATOM
A11SZ
N7
G
C1910
−103.183
−6.449
−3.543
1.00
106.21
N


ATOM
A11TO
C8
G
C1910
−104.473
−6.625
−3.572
1.00
106.21
C


ATOM
A11T1
C2′
G
C1910
−107.139
−4.576
−4.897
1.00
96.70
C


ATOM
A11T2
O2′
G
C1910
−108.351
−3.911
−4.576
1.00
96.70
O


ATOM
A11T3
C3′
G
C1910
−107.386
−5.723
−5.865
1.00
96.70
C


ATOM
A11T4
O3′
G
C1910
−108.303
−5.410
−6.899
1.00
96.70
O


ATOM
A11TG
P
U
C1911
−107.815
−5.339
−8.427
1.00
111.47
P


ATOM
A11TH
OP1
U
C1911
−109.025
−5.462
−9.276
1.00
111.47
O


ATOM
A11TI
OP2
U
C1911
−106.727
−6.335
−8.590
1.00
111.47
O


ATOM
A11TJ
O5′
U
C1911
−107.224
−3.867
−8.538
1.00
111.47
O


ATOM
A11TK
C5′
U
C1911
−107.947
−2.750
−8.040
1.00
111.47
C


ATOM
A11TL
C4′
U
C1911
−107.068
−1.533
−7.908
1.00
111.47
C


ATOM
A11TM
O4′
U
C1911
−106.198
−1.669
−6.754
1.00
111.47
O


ATOM
A11TN
C1′
U
C1911
−104.959
−1.040
−7.010
1.00
111.47
C


ATOM
A11TO
N1
U
C1911
−103.884
−2.059
−6.934
1.00
107.82
N


ATOM
A11TP
C6
U
C1911
−104.111
−3.380
−7.243
1.00
107.82
C


ATOM
A11TQ
C2
U
C1911
−102.629
−1.635
−6.542
1.00
107.82
C


ATOM
A11TR
O2
U
C1911
−102.375
−0.479
−6.255
1.00
107.82
O


ATOM
A11TS
N3
U
C1911
−101.676
−2.620
−6.486
1.00
107.82
N


ATOM
A11TT
C4
U
C1911
−101.841
−3.955
−6.782
1.00
107.82
C


ATOM
A11TU
O4
U
C1911
−100.882
−4.721
−6.685
1.00
107.82
O


ATOM
A11TV
C5
U
C1911
−103.164
−4.321
−7.183
1.00
107.82
C


ATOM
A11TW
C2′
U
C1911
−105.048
−0.400
−8.398
1.00
111.47
C


ATOM
A11TX
O2′
U
C1911
−105.506
0.938
−8.249
1.00
111.47
O


ATOM
A11TY
C3′
U
C1911
−106.108
−1.271
−9.056
1.00
111.47
C


ATOM
A11TZ
O3′
U
C1911
−106.737
−0.666
−10.173
1.00
111.47
O


ATOM
A11UA
P
A
C1912
−106.485
−1.236
−11.657
1.00
87.86
P


ATOM
A11UB
OP1
A
C1912
−106.258
−2.698
−11.538
1.00
87.86
O


ATOM
A11UC
OP2
A
C1912
−107.606
−0.758
−12.504
1.00
87.86
O


ATOM
A11UD
O5′
A
C1912
−105.135
−0.511
−12.083
1.00
87.86
O


ATOM
A11UE
C5′
A
C1912
−104.994
0.895
−11.953
1.00
87.86
C


ATOM
A11UF
C4′
A
C1912
−104.151
1.477
−13.059
1.00
87.86
C


ATOM
A11UG
O4′
A
C1912
−102.766
1.527
−12.647
1.00
87.86
O


ATOM
A11UH
C1′
A
C1912
−101.924
1.388
−13.766
1.00
87.86
C


ATOM
A11UI
N9
A
C1912
−100.952
0.310
−13.498
1.00
101.33
N


ATOM
A11UJ
C4
A
C1912
−99.807
0.497
−12.762
1.00
101.33
C


ATOM
A11UK
N3
A
C1912
−99.397
1.644
−12.194
1.00
101.33
N


ATOM
A11UL
C2
A
C1912
−98.243
1.471
−11.559
1.00
101.33
C


ATOM
A11UM
N1
A
C1912
−97.507
0.363
−11.435
1.00
101.33
N


ATOM
A11UN
C6
A
C1912
−97.945
−0.774
−12.016
1.00
101.33
C


ATOM
A11UO
N6
A
C1912
−97.199
−1.873
−11.883
1.00
101.33
N


ATOM
A11UP
C5
A
C1912
−99.162
−0.724
−12.724
1.00
101.33
C


ATOM
A11UQ
N7
A
C1912
−99.893
−1.674
−13.426
1.00
101.33
N


ATOM
A11UR
C8
A
C1912
−100.943
−1.016
−13.863
1.00
101.33
C


ATOM
A11US
C2′
A
C1912
−102.800
1.116
−14.997
1.00
87.86
C


ATOM
A11UT
O2′
A
C1912
−102.934
2.322
−15.734
1.00
87.86
O


ATOM
A11UU
C3′
A
C1912
−104.133
0.707
−14.371
1.00
87.86
C


ATOM
A11UV
O3′
A
C1912
−105.255
1.009
−15.185
1.00
87.86
O


ATOM
A11V7
P
A
C1913
−105.782
−0.039
−16.281
1.00
141.29
P


ATOM
A11V8
OP1
A
C1913
−104.715
−1.051
−16.471
1.00
141.29
O


ATOM
A11V9
OP2
A
C1913
−107.125
−0.492
−15.842
1.00
141.29
O


ATOM
A11VA
O5′
A
C1913
−105.915
0.859
−17.590
1.00
141.29
O


ATOM
A11VB
C5′
A
C1913
−106.630
2.087
−17.564
1.00
141.29
C


ATOM
A11VC
C4′
A
C1913
−106.259
2.972
−18.733
1.00
141.29
C


ATOM
A11VD
O4′
A
C1913
−104.878
3.403
−18.608
1.00
141.29
O


ATOM
A11VE
C1′
A
C1913
−104.321
3.587
−19.898
1.00
141.29
C


ATOM
A11VF
N9
A
C1913
−103.114
2.740
−20.030
1.00
263.81
N


ATOM
A11VG
C4
A
C1913
−102.970
1.391
−19.780
1.00
263.81
C


ATOM
A11VH
N3
A
C1913
−103.894
0.529
−19.331
1.00
263.81
N


ATOM
A11VI
C2
A
C1913
−103.406
−0.696
−19.198
1.00
263.81
C


ATOM
A11VJ
N1
A
C1913
−102.172
−1.136
−19.442
1.00
263.80
N


ATOM
A11VK
C6
A
C1913
−101.256
−0.255
−19.889
1.00
263.81
C


ATOM
A11VL
N6
A
C1913
−100.027
−0.709
−20.129
1.00
263.81
N


ATOM
A11VM
C5
A
C1913
−101.654
1.083
−20.074
1.00
263.81
C


ATOM
A11VN
N7
A
C1913
−100.974
2.210
−20.510
1.00
263.81
N


ATOM
A11VO
C8
A
C1913
−101.880
3.156
−20.468
1.00
263.81
C


ATOM
A11VP
C2′
A
C1913
−105.395
3.231
−20.924
1.00
141.29
C


ATOM
A11VQ
O2′
A
C1913
−106.069
4.423
−21.306
1.00
141.29
O


ATOM
A11VR
C3′
A
C1913
−106.309
2.327
−20.105
1.00
141.29
C


ATOM
A11VS
O3′
A
C1913
−107.617
2.205
−20.626
1.00
141.29
O


ATOM
A11W4
P
C
C1914
−108.084
0.831
−21.319
1.00
227.50
P


ATOM
A11W5
OP1
C
C1914
−109.108
1.179
−22.332
1.00
227.50
O


ATOM
A11W6
OP2
C
C1914
−108.452
−0.104
−20.229
1.00
227.50
O


ATOM
A11W7
O5′
C
C1914
−106.753
0.324
−22.045
1.00
227.50
O


ATOM
A11W8
C5′
C
C1914
−105.940
−0.699
−21.475
1.00
227.50
C


ATOM
A11W9
C4′
C
C1914
−106.107
−2.010
−22.202
1.00
227.50
C


ATOM
A11WA
O4′
C
C1914
−105.219
−2.057
−23.351
1.00
227.50
O


ATOM
A11WB
C1′
C
C1914
−104.865
−3.399
−23.620
1.00
227.50
C


ATOM
A11WC
N1
C
C1914
−103.382
−3.522
−23.661
1.00
124.89
N


ATOM
A11WD
C6
C
C1914
−102.509
−2.517
−23.320
1.00
124.89
C


ATOM
A11WE
C2
C
C1914
−102.881
−4.748
−24.109
1.00
124.89
C


ATOM
A11WF
O2
C
C1914
−103.679
−5.645
−24.418
1.00
124.89
O


ATOM
A11WG
N3
C
C1914
−101.547
−4.943
−24.188
1.00
124.89
N


ATOM
A11WH
C4
C
C1914
−100.708
−3.969
−23.849
1.00
124.89
C


ATOM
A11WI
N4
C
C1914
−99.401
−4.220
−23.950
1.00
124.89
N


ATOM
A11WJ
C5
C
C1914
−101.180
−2.702
−23.397
1.00
124.89
C


ATOM
A11WK
C2′
C
C1914
−105.495
−4.278
−22.533
1.00
227.50
C


ATOM
A11WL
O2′
C
C1914
−106.722
−4.802
−23.027
1.00
227.50
O


ATOM
A11WM
C3′
C
C1914
−105.744
−3.264
−21.423
1.00
227.50
C


ATOM
A11WN
O3′
C
C1914
−106.752
−3.661
−20.509
1.00
227.50
O


ATOM
A11WZ
P
U
C1915
−106.355
−4.438
−19.159
1.00
143.42
P


ATOM
A11X0
OP1
U
C1915
−107.601
−5.025
−18.612
1.00
143.42
O


ATOM
A11X1
OP2
U
C1915
−105.584
−3.489
−18.318
1.00
143.42
O


ATOM
A11X2
O5′
U
C1915
−105.398
−5.597
−19.684
1.00
143.42
O


ATOM
A11X3
C5′
U
C1915
−105.924
−6.845
−20.111
1.00
143.42
C


ATOM
A11X4
C4′
U
C1915
−104.832
−7.868
−20.315
1.00
143.42
C


ATOM
A11X5
O4′
U
C1915
−103.846
−7.363
−21.250
1.00
143.42
O


ATOM
A11X6
C1′
U
C1915
−102.572
−7.886
−20.932
1.00
143.42
C


ATOM
A11X7
N1
U
C1915
−101.635
−6.761
−20.696
1.00
169.91
N


ATOM
A11X8
C6
U
C1915
−102.068
−5.509
−20.325
1.00
169.91
C


ATOM
A11X9
C2
U
C1915
−100.286
−7.018
−20.860
1.00
169.91
C


ATOM
A11XA
O2
U
C1915
−99.851
−8.108
−21.186
1.00
169.91
O


ATOM
A11XB
N3
U
C1915
−99.458
−5.950
−20.629
1.00
169.91
N


ATOM
A11XC
C4
U
C1915
−99.833
−4.676
−20.257
1.00
169.91
C


ATOM
A11XD
O4
U
C1915
−98.971
−3.817
−20.084
1.00
169.91
O


ATOM
A11XE
C5
U
C1915
−101.241
−4.484
−20.106
1.00
169.91
C


ATOM
A11XF
C2′
U
C1915
−102.728
−8.775
−19.696
1.00
143.42
C


ATOM
A11XG
O2′
U
C1915
−102.891
−10.121
−20.119
1.00
143.42
O


ATOM
A11XH
C3′
U
C1915
−104.017
−8.233
−19.085
1.00
143.42
C


ATOM
A11XI
O3′
U
C1915
−104.683
−9.158
−18.241
1.00
143.42
O


ATOM
A11XT
P
A
C1916
−104.077
−9.532
−16.800
1.00
104.25
P


ATOM
A11XU
OP1
A
C1916
−104.986
−10.534
−16.192
1.00
104.25
O


ATOM
A11XV
OP2
A
C1916
−103.841
−8.257
−16.078
1.00
104.25
O


ATOM
A11XW
O5′
A
C1916
−102.689
−10.215
−17.172
1.00
104.25
O


ATOM
A11XX
C5′
A
C1916
−101.891
−10.838
−16.180
1.00
104.25
C


ATOM
A11XY
C4′
A
C1916
−100.423
−10.720
−16.499
1.00
104.25
C


ATOM
A11XZ
O4′
A
C1916
−100.238
−9.814
−17.623
1.00
104.25
O


ATOM
A11Y0
C1′
A
C1916
−99.091
−9.016
−17.416
1.00
104.25
C


ATOM
A11Y1
N9
A
C1916
−99.531
−7.620
−17.225
1.00
118.95
N


ATOM
A11Y2
C4
A
C1916
−98.757
−6.485
−17.189
1.00
118.95
C


ATOM
A11Y3
N3
A
C1916
−97.426
−6.385
−17.334
1.00
118.95
N


ATOM
A11Y4
C2
A
C1916
−97.042
−5.114
−17.244
1.00
118.95
C


ATOM
A11Y5
N1
A
C1916
−97.775
−4.010
−17.039
1.00
118.95
N


ATOM
A11Y6
C6
A
C1916
−99.112
−4.147
−16.897
1.00
118.95
C


ATOM
A11Y7
N6
A
C1916
−99.873
−3.068
−16.690
1.00
118.95
N


ATOM
A11Y8
C5
A
C1916
−99.641
−5.443
−16.974
1.00
118.95
C


ATOM
A11Y9
N7
A
C1916
−100.941
−5.906
−16.869
1.00
118.95
N


ATOM
A11YA
C8
A
C1916
−100.818
−7.198
−17.021
1.00
118.95
C


ATOM
A11YB
C2′
A
C1916
−98.381
−9.555
−16.180
1.00
104.25
C


ATOM
A11YC
O2′
A
C1916
−97.482
−10.579
−16.582
1.00
104.25
O


ATOM
A11YD
C3′
A
C1916
−99.551
−10.134
−15.400
1.00
104.25
C


ATOM
A11YE
O3′
A
C1916
−99.173
−11.090
−14.424
1.00
104.25
O


ATOM
A11YQ
P
U
C1917
−99.700
−10.963
−12.909
1.00
94.66
P


ATOM
A11YR
OP1
U
C1917
−99.673
−12.325
−12.323
1.00
94.66
O


ATOM
A11YS
OP2
U
C1917
−100.992
−10.232
−12.951
1.00
94.66
O


ATOM
A11YT
O5′
U
C1917
−98.587
−10.056
−12.221
1.00
94.66
O


ATOM
A11YU
C5′
U
C1917
−97.217
−10.428
−12.258
1.00
94.66
C


ATOM
A11YV
C4′
U
C1917
−96.320
−9.229
−12.435
1.00
94.66
C


ATOM
A11YW
O4′
U
C1917
−96.683
−8.514
−13.646
1.00
94.66
O


ATOM
A11YX
C1′
U
C1917
−96.487
−7.126
−13.463
1.00
94.66
C


ATOM
A11YY
N1
U
C1917
−97.792
−6.430
−13.606
1.00
97.62
N


ATOM
A11YZ
C6
U
C1917
−98.995
−7.095
−13.659
1.00
97.62
C


ATOM
A11Z0
C2
U
C1917
−97.753
−5.052
−13.696
1.00
97.62
C


ATOM
A11Z1
O2
U
C1917
−96.713
−4.418
−13.654
1.00
97.62
O


ATOM
A11Z2
N3
U
C1917
−98.974
−4.440
−13.830
1.00
97.62
N


ATOM
A11Z3
C4
U
C1917
−100.208
−5.050
−13.889
1.00
97.62
C


ATOM
A11Z4
O4
U
C1917
−101.222
−4.362
−14.012
1.00
97.62
O


ATOM
A11Z5
C5
U
C1917
−100.172
−6.476
−13.792
1.00
97.62
C


ATOM
A11Z6
C2′
U
C1917
−95.881
−6.930
−12.076
1.00
94.66
C


ATOM
A11Z7
O2′
U
C1917
−94.464
−6.967
−12.198
1.00
94.66
O


ATOM
A11Z8
C3′
U
C1917
−96.403
−8.165
−11.355
1.00
94.66
C


ATOM
A11Z9
O3′
U
C1917
−95.677
−8.499
−10.186
1.00
94.66
O


ATOM
A11ZK
P
A
C1918
−96.359
−8.323
−8.741
1.00
79.74
P


ATOM
A11ZL
OP1
A
C1918
−95.370
−8.774
−7.732
1.00
79.75
O


ATOM
A11ZM
OP2
A
C1918
−97.683
−8.994
−8.794
1.00
79.75
O


ATOM
A11ZN
O5′
A
C1918
−96.554
−6.751
−8.639
1.00
79.74
O


ATOM
A11ZO
C5′
A
C1918
−95.451
−5.871
−8.810
1.00
79.74
C


ATOM
A11ZP
C4′
A
C1918
−95.851
−4.436
−8.605
1.00
79.74
C


ATOM
A11ZQ
O4′
A
C1918
−96.839
−4.068
−9.607
1.00
79.74
O


ATOM
A11ZR
C1′
A
C1918
−97.972
−3.502
−8.982
1.00
79.75
C


ATOM
A11ZS
N9
A
C1918
−99.163
−3.895
−9.739
1.00
105.75
N


ATOM
A11ZT
C4
A
C1918
−100.289
−3.136
−9.948
1.00
105.75
C


ATOM
A11ZU
N3
A
C1918
−100.529
−1.889
−9.510
1.00
105.75
N


ATOM
A11ZV
C2
A
C1918
−101.731
−1.475
−9.907
1.00
105.75
C


ATOM
A11ZW
N1
A
C1918
−102.654
−2.117
−10.634
1.00
105.75
N


ATOM
A11ZX
C6
A
C1918
−102.385
−3.370
−11.056
1.00
105.75
C


ATOM
A11ZY
N6
A
C1918
−103.304
−4.011
−11.782
1.00
105.75
N


ATOM
A11ZZ
C5
A
C1918
−101.141
−3.923
−10.701
1.00
105.75
C


ATOM
A1200
N7
A
C1918
−100.562
−5.156
−10.963
1.00
105.75
N


ATOM
A1201
C8
A
C1918
−99.394
−5.089
−10.372
1.00
105.75
C


ATOM
A1202
C2′
A
C1918
−97.967
−4.015
−7.547
1.00
79.75
C


ATOM
A1203
O2′
A
C1918
−98.681
−3.155
−6.687
1.00
79.74
O


ATOM
A1204
C3′
A
C1918
−96.473
−4.128
−7.245
1.00
79.75
C


ATOM
A1205
O3′
A
C1918
−95.970
−2.890
−6.753
1.00
79.75
O


ATOM
A120H
P
A
C1919
−94.589
−2.863
−5.928
1.00
82.74
P


ATOM
A120I
OP1
A
C1919
−93.590
−3.619
−6.722
1.00
82.74
O


ATOM
A120J
OP2
A
C1919
−94.894
−3.317
−4.550
1.00
82.74
O


ATOM
A120K
O5′
A
C1919
−94.215
−1.319
−5.917
1.00
82.74
O


ATOM
A120L
C5′
A
C1919
−92.866
−0.889
−5.815
1.00
82.74
C


ATOM
A120M
C4′
A
C1919
−92.746
0.576
−6.134
1.00
82.74
C


ATOM
A120N
O4′
A
C1919
−93.107
0.796
−7.527
1.00
82.74
O


ATOM
A120O
C1′
A
C1919
−93.947
1.920
−7.641
1.00
82.74
C


ATOM
A120P
N9
A
C1919
−95.304
1.440
−7.970
1.00
96.93
N


ATOM
A120Q
C4
A
C1919
−96.499
2.123
−7.937
1.00
96.93
C


ATOM
A120R
N3
A
C1919
−96.718
3.401
−7.587
1.00
96.93
N


ATOM
A120S
C2
A
C1919
−98.012
3.704
−7.675
1.00
96.93
C


ATOM
A120T
N1
A
C1919
−99.042
2.932
−8.046
1.00
96.93
N


ATOM
A120U
C6
A
C1919
−98.790
1.653
−8.391
1.00
96.93
C


ATOM
A120V
N6
A
C1919
−99.806
0.873
−8.763
1.00
96.93
N


ATOM
A120W
C5
A
C1919
−97.460
1.211
−8.338
1.00
96.93
C


ATOM
A120X
N7
A
C1919
−96.892
−0.017
−8.624
1.00
96.93
N


ATOM
A120Y
C8
A
C1919
−95.619
0.170
−8.392
1.00
96.93
C


ATOM
A120Z
C2′
A
C1919
−93.905
2.651
−6.303
1.00
82.74
C


ATOM
A1210
O2′
A
C1919
−92.792
3.534
−6.304
1.00
82.74
O


ATOM
A1211
C3′
A
C1919
−93.677
1.492
−5.347
1.00
82.74
C


ATOM
A1212
O3′
A
C1919
−93.142
1.877
−4.092
1.00
82.74
O


ATOM
A121E
P
C
C1920
−94.102
2.023
−2.812
1.00
71.50
P


ATOM
A121F
OP1
C
C1920
−94.344
0.655
−2.289
1.00
71.50
O


ATOM
A121G
OP2
C
C1920
−93.487
3.030
−1.914
1.00
71.50
O


ATOM
A121H
O5′
C
C1920
−95.440
2.603
−3.443
1.00
71.50
O


ATOM
A121I
C5′
C
C1920
−95.937
3.878
−3.076
1.00
71.50
C


ATOM
A121J
C4′
C
C1920
−97.426
3.964
−3.292
1.00
71.50
C


ATOM
A121K
O4′
C
C1920
−97.800
3.180
−4.458
1.00
71.50
O


ATOM
A121L
C1′
C
C1920
−99.057
2.570
−4.249
1.00
71.50
C


ATOM
A121M
N1
C
C1920
−98.883
1.097
−4.281
1.00
99.59
N


ATOM
A121N
C6
C
C1920
−97.654
0.499
−4.381
1.00
99.59
C


ATOM
A121O
C2
C
C1920
−100.029
0.301
−4.221
1.00
99.59
C


ATOM
A121P
O2
C
C1920
−101.137
0.849
−4.135
1.00
99.59
O


ATOM
A121Q
N3
C
C1920
−99.908
−1.046
−4.247
1.00
99.59
N


ATOM
A121R
C4
C
C1920
−98.702
−1.606
−4.333
1.00
99.59
C


ATOM
A121S
N4
C
C1920
−98.608
−2.935
−4.367
1.00
99.59
N


ATOM
A121T
C5
C
C1920
−97.520
−0.830
−4.409
1.00
99.59
C


ATOM
A121U
C2′
C
C1920
−99.584
3.058
−2.897
1.00
71.50
C


ATOM
A121V
O2′
C
C1920
−100.378
4.218
−3.103
1.00
71.50
O


ATOM
A121W
C3′
C
C1920
−98.290
3.403
−2.175
1.00
71.50
C


ATOM
A121X
O3′
C
C1920
−98.460
4.317
−1.104
1.00
71.50
O


ATOM
A1229
P
G
C1921
−98.648
3.781
0.397
1.00
93.18
P


ATOM
A122A
OP1
G
C1921
−97.734
2.625
0.571
1.00
93.18
O


ATOM
A122B
OP2
G
C1921
−98.500
4.948
1.299
1.00
93.18
O


ATOM
A122C
O5′
G
C1921
−100.157
3.283
0.402
1.00
93.18
O


ATOM
A122D
C5′
G
C1921
−101.216
4.169
0.075
1.00
93.18
C


ATOM
A122E
C4′
G
C1921
−102.526
3.438
−0.056
1.00
93.18
C


ATOM
A122F
O4′
G
C1921
−102.447
2.459
−1.126
1.00
93.18
O


ATOM
A122G
C1′
G
C1921
−103.255
1.342
−0.810
1.00
93.18
C


ATOM
A122H
N9
G
C1921
−102.404
0.139
−0.756
1.00
85.51
N


ATOM
A122I
C4
G
C1921
−102.859
−1.157
−0.708
1.00
85.51
C


ATOM
A122J
N3
G
C1921
−104.152
−1.543
−0.719
1.00
85.51
N


ATOM
A122K
C2
G
C1921
−104.277
−2.859
−0.669
1.00
85.51
C


ATOM
A122L
N2
G
C1921
−105.500
−3.412
−0.674
1.00
85.51
N


ATOM
A122M
N1
G
C1921
−103.215
−3.728
−0.617
1.00
85.51
N


ATOM
A122N
C6
G
C1921
−101.877
−3.351
−0.603
1.00
85.51
C


ATOM
A122O
O6
G
C1921
−100.998
−4.219
−0.558
1.00
85.51
O


ATOM
A122P
C5
G
C1921
−101.727
−1.941
−0.657
1.00
85.51
C


ATOM
A122Q
N7
G
C1921
−100.583
−1.156
−0.664
1.00
85.51
N


ATOM
A122R
C8
G
C1921
−101.032
0.069
−0.720
1.00
85.51
C


ATOM
A122S
C2′
G
C1921
−103.924
1.624
0.533
1.00
93.18
C


ATOM
A122T
O2′
G
C1921
−105.188
2.226
0.294
1.00
93.18
O


ATOM
A122U
C3′
G
C1921
−102.952
2.618
1.147
1.00
93.18
C


ATOM
A122V
O3′
G
C1921
−103.512
3.404
2.183
1.00
93.18
O


ATOM
A1237
P
G
C1922
−103.338
2.961
3.719
1.00
85.73
P


ATOM
A1238
OP1
G
C1922
−103.763
4.109
4.554
1.00
85.73
O


ATOM
A1239
OP2
G
C1922
−101.957
2.440
3.874
1.00
85.73
O


ATOM
A123A
O5′
G
C1922
−104.384
1.772
3.860
1.00
85.73
O


ATOM
A123B
C5′
G
C1922
−105.752
1.964
3.533
1.00
85.73
C


ATOM
A123C
C4′
G
C1922
−106.469
0.650
3.351
1.00
85.73
C


ATOM
A123D
O4′
G
C1922
−105.811
−0.136
2.323
1.00
85.73
O


ATOM
A123E
C1′
G
C1922
−105.905
−1.512
2.638
1.00
85.73
C


ATOM
A123F
N9
G
C1922
−104.542
−2.057
2.796
1.00
120.70
N


ATOM
A123G
C4
G
C1922
−104.196
−3.390
2.823
1.00
120.70
C


ATOM
A123H
N3
G
C1922
−105.038
−4.437
2.694
1.00
120.70
N


ATOM
A123I
C2
G
C1922
−104.404
−5.598
2.754
1.00
120.70
C


ATOM
A123J
N2
G
C1922
−105.096
−6.742
2.644
1.00
120.70
N


ATOM
A123K
N1
G
C1922
−103.048
−5.723
2.928
1.00
120.70
N


ATOM
A123L
C6
G
C1922
−102.163
−4.661
3.063
1.00
120.70
C


ATOM
A123M
O6
G
C1922
−100.957
−4.885
3.217
1.00
120.70
O


ATOM
A123N
C5
G
C1922
−102.829
−3.410
3.000
1.00
120.70
C


ATOM
A123O
N7
G
C1922
−102.324
−2.122
3.090
1.00
120.70
N


ATOM
A123P
C8
G
C1922
−103.372
−1.355
2.968
1.00
120.70
C


ATOM
A123Q
C2′
G
C1922
−106.719
−1.634
3.922
1.00
85.73
C


ATOM
A123R
O2′
G
C1922
−108.086
−1.808
3.582
1.00
85.73
O


ATOM
A123S
C3′
G
C1922
−106.484
−0.270
4.558
1.00
85.73
C


ATOM
A123T
O3′
G
C1922
−107.457
0.093
5.520
1.00
85.73
O


ATOM
A1245
P
U
C1923
−107.087
0.072
7.082
1.00
93.79
P


ATOM
A1246
OP1
U
C1923
−108.367
0.090
7.833
1.00
93.79
O


ATOM
A1247
OP2
U
C1923
−106.108
1.162
7.316
1.00
93.79
O


ATOM
A1248
O5′
U
C1923
−106.373
−1.340
7.249
1.00
93.79
O


ATOM
A1249
C5′
U
C1923
−106.811
−2.281
8.217
1.00
93.79
C


ATOM
A124A
C4′
U
C1923
−106.981
−3.650
7.612
1.00
93.79
C


ATOM
A124B
O4′
U
C1923
−106.258
−3.723
6.357
1.00
93.79
O


ATOM
A124C
C1′
U
C1923
−105.649
−4.985
6.216
1.00
93.79
C


ATOM
A124D
N1
U
C1923
−104.176
−4.797
6.216
1.00
127.15
N


ATOM
A124E
C6
U
C1923
−103.601
−3.559
6.427
1.00
127.15
C


ATOM
A124F
C2
U
C1923
−103.386
−5.901
5.964
1.00
127.15
C


ATOM
A124G
O2
U
C1923
−103.838
−7.016
5.765
1.00
127.15
O


ATOM
A124H
N3
U
C1923
−102.039
−5.654
5.969
1.00
127.15
N


ATOM
A124I
C4
U
C1923
−101.402
−4.450
6.181
1.00
127.15
C


ATOM
A124J
O4
U
C1923
−100.171
−4.397
6.149
1.00
127.15
O


ATOM
A124K
C5
U
C1923
−102.281
−3.351
6.423
1.00
127.15
C


ATOM
A124L
C2′
U
C1923
−106.126
−5.857
7.377
1.00
93.79
C


ATOM
A124M
O2′
U
C1923
−107.307
−6.538
6.976
1.00
93.79
O


ATOM
A124N
C3′
U
C1923
−106.435
−4.806
8.432
1.00
93.79
C


ATOM
A124O
O3′
U
C1923
−107.346
−5.244
9.422
1.00
93.79
O


ATOM
A124Z
P
C
C1924
−107.003
−5.068
10.982
1.00
116.36
P


ATOM
A1250
OP1
C
C1924
−108.293
−4.922
11.699
1.00
116.36
O


ATOM
A1251
OP2
C
C1924
−105.996
−3.984
11.096
1.00
116.36
O


ATOM
A1252
O5′
C
C1924
−106.338
−6.463
11.345
1.00
116.36
O


ATOM
A1253
C5′
C
C1924
−106.956
−7.683
10.967
1.00
116.36
C


ATOM
A1254
C4′
C
C1924
−105.978
−8.826
10.993
1.00
116.36
C


ATOM
A1255
O4′
C
C1924
−105.175
−8.820
9.784
1.00
116.36
O


ATOM
A1256
C1′
C
C1924
−103.877
−9.300
10.067
1.00
116.36
C


ATOM
A1257
N1
C
C1924
−102.887
−8.252
9.709
1.00
91.52
N


ATOM
A1258
C6
C
C1924
−103.230
−6.939
9.506
1.00
91.52
C


ATOM
A1259
C2
C
C1924
−101.552
−8.641
9.577
1.00
91.52
C


ATOM
A125A
O2
C
C1924
−101.255
−9.830
9.763
1.00
91.52
O


ATOM
A125B
N3
C
C1924
−100.611
−7.725
9.251
1.00
91.52
N


ATOM
A125C
C4
C
C1924
−100.952
−6.452
9.055
1.00
91.52
C


ATOM
A125D
N4
C
C1924
−99.981
−5.589
8.738
1.00
91.52
N


ATOM
A125E
C5
C
C1924
−102.305
−6.020
9.182
1.00
91.52
C


ATOM
A125F
C2′
C
C1924
−103.827
−9.656
11.555
1.00
116.36
C


ATOM
A125G
O2′
C
C1924
−104.119
−11.038
11.705
1.00
116.36
O


ATOM
A125H
C3′
C
C1924
−104.952
−8.797
12.114
1.00
116.36
C


ATOM
A125I
O3′
C
C1924
−105.470
−9.262
13.346
1.00
116.36
O


ATOM
A125U
P
C
C1925
−104.585
−9.163
14.682
1.00
90.13
P


ATOM
A125V
OP1
C
C1925
−105.492
−9.418
15.827
1.00
90.13
O


ATOM
A125W
OP2
C
C1925
−103.850
−7.875
14.627
1.00
90.13
O


ATOM
A125X
O5′
C
C1925
−103.569
−10.375
14.516
1.00
90.13
O


ATOM
A125Y
C5′
C
C1925
−102.460
−10.516
15.386
1.00
90.13
C


ATOM
A125Z
C4′
C
C1925
−101.294
−11.168
14.687
1.00
90.13
C


ATOM
A1260
O4′
C
C1925
−101.269
−10.757
13.294
1.00
90.13
O


ATOM
A1261
C1′
C
C1925
−99.938
−10.547
12.877
1.00
90.13
C


ATOM
A1262
N1
C
C1925
−99.757
−9.101
12.611
1.00
79.97
N


ATOM
A1263
C6
C
C1925
−100.626
−8.155
13.093
1.00
79.97
C


ATOM
A1264
C2
C
C1925
−98.653
−8.707
11.859
1.00
79.97
C


ATOM
A1265
O2
C
C1925
−97.874
−9.572
11.435
1.00
79.97
O


ATOM
A1266
N3
C
C1925
−98.452
−7.393
11.604
1.00
79.97
N


ATOM
A1267
C4
C
C1925
−99.302
−6.482
12.072
1.00
79.97
C


ATOM
A1268
N4
C
C1925
−99.067
−5.199
11.794
1.00
79.97
N


ATOM
A1269
C5
C
C1925
−100.438
−6.850
12.846
1.00
79.97
C


ATOM
A126A
C2′
C
C1925
−99.028
−11.034
13.999
1.00
90.13
C


ATOM
A126B
O2′
C
C1925
−98.765
−12.418
13.816
1.00
90.13
O


ATOM
A126C
C3′
C
C1925
−99.915
−10.801
15.216
1.00
90.13
C


ATOM
A126D
O3′
C
C1925
−99.536
−11.558
16.354
1.00
90.13
O


ATOM
A126P
P
U
C1926
−99.850
−11.017
17.838
1.00
110.07
P


ATOM
A126Q
OP1
U
C1926
−100.305
−12.177
18.639
1.00
110.07
O


ATOM
A126R
OP2
U
C1926
−100.751
−9.846
17.702
1.00
110.07
O


ATOM
A126S
O5′
U
C1926
−98.422
−10.538
18.344
1.00
110.07
O


ATOM
A126T
C5′
U
C1926
−97.767
−9.458
17.708
1.00
110.07
C


ATOM
A126U
C4′
U
C1926
−96.544
−9.914
16.952
1.00
110.07
C


ATOM
A126V
O4′
U
C1926
−96.702
−9.557
15.557
1.00
110.07
O


ATOM
A126W
C1′
U
C1926
−95.498
−9.068
15.028
1.00
110.07
C


ATOM
A126X
N1
U
C1926
−95.698
−7.648
14.647
1.00
89.96
N


ATOM
A126Y
C6
U
C1926
−96.778
−6.906
15.078
1.00
89.96
C


ATOM
A126Z
C2
U
C1926
−94.755
−7.100
13.808
1.00
89.96
C


ATOM
A1270
O2
U
C1926
−93.801
−7.742
13.414
1.00
89.96
O


ATOM
A1271
N3
U
C1926
−94.969
−5.789
13.466
1.00
89.96
N


ATOM
A1272
C4
U
C1926
−96.021
−4.990
13.867
1.00
89.96
C


ATOM
A1273
O4
U
C1926
−96.082
−3.823
13.477
1.00
89.96
O


ATOM
A1274
C5
U
C1926
−96.967
−5.629
14.730
1.00
89.96
C


ATOM
A1275
C2′
U
C1926
−94.413
−9.239
16.086
1.00
110.07
C


ATOM
A1276
O2′
U
C1926
−93.734
−10.469
15.864
1.00
110.07
O


ATOM
A1277
C3′
U
C1926
−95.219
−9.288
17.382
1.00
110.07
C


ATOM
A1278
O3′
U
C1926
−94.574
−10.025
18.406
1.00
110.07
O


ATOM
A127J
P
A
C1927
−94.770
−9.646
19.957
1.00
87.96
P


ATOM
A127K
OP1
A
C1927
−94.740
−10.918
20.721
1.00
87.96
O


ATOM
A127L
OP2
A
C1927
−95.971
−8.788
20.057
1.00
87.96
O


ATOM
A127M
O5′
A
C1927
−93.467
−8.788
20.278
1.00
87.96
O


ATOM
A127N
C5′
A
C1927
−93.485
−7.369
20.209
1.00
87.96
C


ATOM
A127O
C4′
A
C1927
−92.143
−6.823
19.788
1.00
87.96
C


ATOM
A127P
O4′
A
C1927
−91.116
−7.797
20.088
1.00
87.96
O


ATOM
A127Q
C1′
A
C1927
−90.116
−7.777
19.098
1.00
87.96
C


ATOM
A127R
N9
A
C1927
−90.000
−9.135
18.523
1.00
70.80
N


ATOM
A127S
C4
A
C1927
−88.972
−9.623
17.750
1.00
70.80
C


ATOM
A127T
N3
A
C1927
−87.885
−8.962
17.330
1.00
70.80
N


ATOM
A127U
C2
A
C1927
−87.109
−9.745
16.587
1.00
70.80
C


ATOM
A127V
N1
A
C1927
−87.282
−11.024
16.241
1.00
70.80
N


ATOM
A127W
C6
A
C1927
−88.380
−11.667
16.682
1.00
70.80
C


ATOM
A127X
N6
A
C1927
−88.548
−12.944
16.333
1.00
70.80
N


ATOM
A127Y
C5
A
C1927
−89.284
−10.941
17.475
1.00
70.80
C


ATOM
A127Z
N7
A
C1927
−90.481
−11.295
18.070
1.00
70.80
N


ATOM
A1280
C8
A
C1927
−90.859
−10.199
18.683
1.00
70.80
C


ATOM
A1281
C2′
A
C1927
−90.489
−6.720
18.059
1.00
87.96
C


ATOM
A1282
O2′
A
C1927
−89.771
−5.523
18.331
1.00
87.96
O


ATOM
A1283
C3′
A
C1927
−91.984
−6.528
18.303
1.00
87.96
C


ATOM
A1284
O3′
A
C1927
−92.444
−5.231
17.958
1.00
87.96
O


ATOM
A128G
P
A
C1928
−93.676
−5.041
16.945
1.00
70.25
P


ATOM
A128H
OP1
A
C1928
−94.137
−3.638
17.078
1.00
70.25
O


ATOM
A128I
OP2
A
C1928
−94.639
−6.130
17.215
1.00
70.25
O


ATOM
A128J
O5′
A
C1928
−92.998
−5.255
15.521
1.00
70.25
O


ATOM
A128K
C5′
A
C1928
−92.479
−4.155
14.796
1.00
70.25
C


ATOM
A128L
C4′
A
C1928
−91.247
−4.528
14.006
1.00
70.25
C


ATOM
A128M
O4′
A
C1928
−90.354
−5.344
14.820
1.00
70.25
O


ATOM
A128N
C1′
A
C1928
−89.670
−6.269
13.979
1.00
70.25
C


ATOM
A128O
N9
A
C1928
−90.117
−7.634
14.311
1.00
59.11
N


ATOM
A128P
C4
A
C1928
−89.505
−8.789
13.892
1.00
59.11
C


ATOM
A128Q
N3
A
C1928
−88.367
−8.892
13.189
1.00
59.11
N


ATOM
A128R
C2
A
C1928
−88.053
−10.169
12.990
1.00
59.11
C


ATOM
A128S
N1
A
C1928
−88.697
−11.273
13.383
1.00
59.11
N


ATOM
A128T
C6
A
C1928
−89.840
−11.135
14.084
1.00
59.11
C


ATOM
A128U
N6
A
C1928
−90.481
−12.238
14.478
1.00
59.11
N


ATOM
A128V
C5
A
C1928
−90.279
−9.830
14.366
1.00
59.11
C


ATOM
A128W
N7
A
C1928
−91.383
−9.345
15.048
1.00
59.11
N


ATOM
A128X
C8
A
C1928
−91.250
−8.044
14.966
1.00
59.11
C


ATOM
A128Y
C2′
A
C1928
−90.052
−5.923
12.548
1.00
70.25
C


ATOM
A128Z
O2′
A
C1928
−89.193
−4.890
12.085
1.00
70.25
O


ATOM
A1290
C3′
A
C1928
−91.461
−5.406
12.787
1.00
70.25
C


ATOM
A1291
O3′
A
C1928
−92.073
−4.765
11.674
1.00
70.25
O


ATOM
A129D
P
G
C1929
−91.583
−3.330
11.139
1.00
85.66
P


ATOM
A129E
OP1
G
C1929
−92.590
−2.334
11.584
1.00
85.66
O


ATOM
A129F
OP2
G
C1929
−90.174
−3.152
11.557
1.00
85.66
O


ATOM
A129G
O5′
G
C1929
−91.657
−3.503
9.554
1.00
85.66
O


ATOM
A129H
C5′
G
C1929
−91.978
−4.760
8.953
1.00
85.66
C


ATOM
A129I
C4′
G
C1929
−90.750
−5.619
8.754
1.00
85.66
C


ATOM
A129J
O4′
G
C1929
−90.704
−6.646
9.784
1.00
85.66
O


ATOM
A129K
C1′
G
C1929
−90.576
−7.916
9.175
1.00
85.66
C


ATOM
A129L
N9
G
C1929
−91.242
−8.914
10.014
1.00
94.85
N


ATOM
A129M
C4
G
C1929
−92.549
−8.923
10.423
1.00
94.85
C


ATOM
A129N
N3
G
C1929
−93.462
−7.980
10.131
1.00
94.85
N


ATOM
A129O
C2
G
C1929
−94.634
−8.258
10.670
1.00
94.85
C


ATOM
A129P
N2
G
C1929
−95.651
−7.411
10.473
1.00
94.85
N


ATOM
A129Q
N1
G
C1929
−94.891
−9.369
11.438
1.00
94.85
N


ATOM
A129R
C6
G
C1929
−93.958
−10.352
11.751
1.00
94.85
C


ATOM
A129S
O6
G
C1929
−94.289
−11.316
12.449
1.00
94.85
O


ATOM
A129T
C5
G
C1929
−92.693
−10.068
11.176
1.00
94.85
C


ATOM
A129U
N7
G
C1929
−91.500
−10.771
11.234
1.00
94.85
N


ATOM
A129V
C8
G
C1929
−90.673
−10.051
10.529
1.00
94.85
C


ATOM
A129W
C2′
G
C1929
−91.179
−7.756
7.788
1.00
85.66
C


ATOM
A129X
O2′
G
C1929
−90.760
−8.781
6.913
1.00
85.66
O


ATOM
A129Y
C3′
G
C1929
−90.682
−6.366
7.419
1.00
85.66
C


ATOM
A129Z
O3′
G
C1929
−89.325
−6.454
6.995
1.00
85.66
O


ATOM
A12AB
P
G
C1930
−88.636
−5.235
6.217
1.00
81.43
P


ATOM
A12AC
OP1
G
C1930
−88.069
−4.326
7.243
1.00
81.43
O


ATOM
A12AD
OP2
G
C1930
−89.640
−4.700
5.267
1.00
81.43
O


ATOM
A12AE
O5′
G
C1930
−87.462
−5.951
5.418
1.00
81.43
O


ATOM
A12AF
C5′
G
C1930
−86.500
−6.755
6.094
1.00
81.43
C


ATOM
A12AG
C4′
G
C1930
−85.165
−6.726
5.394
1.00
81.43
C


ATOM
A12AH
O4′
G
C1930
−84.313
−7.775
5.937
1.00
81.43
O


ATOM
A12AI
C1′
G
C1930
−83.857
−8.599
4.882
1.00
81.43
C


ATOM
A12AJ
N9
G
C1930
−83.693
−9.963
5.387
1.00
75.46
N


ATOM
A12AK
C4
G
C1930
−82.546
−10.427
5.973
1.00
75.46
C


ATOM
A12AL
N3
G
C1930
−81.428
−9.702
6.167
1.00
75.46
N


ATOM
A12AM
C2
G
C1930
−80.483
−10.408
6.755
1.00
75.46
C


ATOM
A12AN
N2
G
C1930
−79.304
−9.829
7.021
1.00
75.46
N


ATOM
A12AO
N1
G
C1930
−80.625
−11.723
7.122
1.00
75.46
N


ATOM
A12AP
C6
G
C1930
−81.771
−12.488
6.928
1.00
75.46
C


ATOM
A12AQ
O6
G
C1930
−81.791
−13.667
7.300
1.00
75.46
O


ATOM
A12AR
C5
G
C1930
−82.797
−11.739
6.296
1.00
75.46
C


ATOM
A12AS
N7
G
C1930
−84.083
−12.097
5.918
1.00
75.46
N


ATOM
A12AT
C8
G
C1930
−84.578
−11.013
5.381
1.00
75.46
C


ATOM
A12AU
C2′
G
C1930
−84.893
−8.452
3.777
1.00
81.43
C


ATOM
A12AV
O2′
G
C1930
−84.389
−8.859
2.524
1.00
81.43
O


ATOM
A12AW
C3′
G
C1930
−85.217
−6.966
3.886
1.00
81.43
C


ATOM
A12AX
O3′
G
C1930
−84.192
−6.201
3.251
1.00
81.43
O


ATOM
A12B9
P
U
C1931
−84.240
−5.933
1.668
1.00
64.85
P


ATOM
A12BA
OP1
U
C1931
−85.571
−6.376
1.192
1.00
64.85
O


ATOM
A12BB
OP2
U
C1931
−83.030
−6.565
1.086
1.00
64.85
O


ATOM
A12BC
O5′
U
C1931
−84.129
−4.343
1.552
1.00
64.85
O


ATOM
A12BD
C5′
U
C1931
−84.175
−3.499
2.697
1.00
64.85
C


ATOM
A12BE
C4′
U
C1931
−82.990
−2.569
2.742
1.00
64.85
C


ATOM
A12BF
O4′
U
C1931
−82.378
−2.614
4.058
1.00
64.85
O


ATOM
A12BG
C1′
U
C1931
−80.974
−2.553
3.947
1.00
64.85
C


ATOM
A12BH
N1
U
C1931
−80.406
−3.830
4.444
1.00
66.05
N


ATOM
A12BI
C6
U
C1931
−81.207
−4.895
4.804
1.00
66.05
C


ATOM
A12BJ
C2
U
C1931
−79.033
−3.910
4.561
1.00
66.05
C


ATOM
A12BK
O2
U
C1931
−78.284
−2.997
4.261
1.00
66.05
O


ATOM
A12BL
N3
U
C1931
−78.562
−5.106
5.031
1.00
66.05
N


ATOM
A12BM
C4
U
C1931
−79.305
−6.207
5.401
1.00
66.05
C


ATOM
A12BN
O4
U
C1931
−78.739
−7.219
5.809
1.00
66.05
O


ATOM
A12BO
C5
U
C1931
−80.718
−6.051
5.262
1.00
66.05
C


ATOM
A12BP
C2′
U
C1931
−80.636
−2.305
2.478
1.00
64.85
C


ATOM
A12BQ
O2′
U
C1931
−80.550
−0.904
2.259
1.00
64.85
O


ATOM
A12BR
C3′
U
C1931
−81.852
−2.893
1.780
1.00
64.85
C


ATOM
A12BS
O3′
U
C1931
−82.070
−2.366
0.481
1.00
64.85
O


TER


ATOM
A84BU
C1
NMY
12905
−95.087
−4.167
4.519
1.00
232.49
C


ATOM
A84BV
O1
NMY
12905
−96.233
−4.750
3.927
1.00
232.49
O


ATOM
A84BW
C2
NMY
12905
−94.531
−5.207
5.500
1.00
232.49
C


ATOM
A84BX
N2
NMY
12905
−94.072
−6.376
4.798
1.00
232.49
N


ATOM
A84BY
C3
NMY
12905
−95.527
−5.611
6.500
1.00
232.49
C


ATOM
A84BZ
O3
NMY
12905
−94.763
−6.232
7.502
1.00
232.49
O


ATOM
A84C0
C4
NMY
12905
−96.233
−4.486
7.052
1.00
232.49
C


ATOM
A84C1
O4
NMY
12905
−97.190
−4.620
8.089
1.00
232.49
O


ATOM
A84C2
C5
NMY
12905
−96.134
−3.119
6.420
1.00
232.49
C


ATOM
A84C3
O5
NMY
12905
−95.336
−2.955
5.148
1.00
232.49
O


ATOM
A84C4
C6
NMY
12905
−96.532
−1.894
7.215
1.00
232.49
C


ATOM
A84C5
N6
NMY
12905
−95.547
−0.814
7.324
1.00
232.49
N


ATOM
A84C6
C7
NMY
12905
−97.960
−3.496
0.219
1.00
232.49
C


ATOM
A84C7
N7
NMY
12905
−98.173
−2.589
−0.916
1.00
232.49
N


ATOM
A84C8
C8
NMY
12905
−98.695
−3.224
1.511
1.00
232.49
C


ATOM
A84C9
C9
NMY
12905
−98.154
−4.055
2.687
1.00
232.49
C


ATOM
A84CA
N9
NMY
12905
−98.692
−3.584
3.931
1.00
232.49
N


ATOM
A84CB
C10
NMY
12905
−96.623
−4.050
2.755
1.00
232.49
C


ATOM
A84CC
C11
NMY
12905
−95.941
−4.603
1.533
1.00
232.49
C


ATOM
A84CD
O11
NMY
12905
−94.705
−3.954
1.346
1.00
232.49
O


ATOM
A84CE
C12
NMY
12905
−96.762
−4.454
0.230
1.00
232.49
C


ATOM
A84CF
O12
NMY
12905
−96.588
−5.326
−0.806
1.00
232.49
O


ATOM
A84CG
C13
NMY
12905
−93.780
−4.747
0.614
1.00
232.49
C


ATOM
A84CH
C14
NMY
12905
−92.906
−3.918
−0.246
1.00
232.49
C


ATOM
A84CI
O14
NMY
12905
−92.743
−4.635
−1.406
1.00
232.49
O


ATOM
A84CJ
C15
NMY
12905
−91.683
−3.790
0.476
1.00
232.49
C


ATOM
A84CK
C16
NMY
12905
−91.692
−4.853
1.517
1.00
232.49
C


ATOM
A84CL
O16
NMY
12905
−92.902
−5.527
1.439
1.00
232.49
O


ATOM
A84CM
C17
NMY
12905
−91.528
−4.318
2.918
1.00
232.49
C


ATOM
A84CN
O17
NMY
12905
−91.733
−5.183
3.946
1.00
232.49
O


ATOM
A84CO
C18
NMY
12905
−89.713
−2.865
−0.463
1.00
232.49
C


ATOM
A84CP
O18
NMY
12905
−90.639
−3.951
−0.471
1.00
232.49
O


ATOM
A84CQ
C19
NMY
12905
−90.162
−1.430
−0.648
1.00
232.49
C


ATOM
A84CR
N19
NMY
12905
−87.542
−4.535
−2.804
1.00
232.49
N


ATOM
A84CS
C20
NMY
12905
−89.341
−0.689
−1.527
1.00
232.49
C


ATOM
A84CT
O20
NMY
12905
−89.536
0.701
−1.232
1.00
232.49
O


ATOM
A84CU
C21
NMY
12905
−87.915
−1.010
−1.322
1.00
232.49
C


ATOM
A84CV
O21
NMY
12905
−86.929
0.006
−1.297
1.00
232.49
O


ATOM
A84CW
C22
NMY
12905
−87.469
−2.463
−1.348
1.00
232.49
C


ATOM
A84CX
O22
NMY
12905
−88.258
−3.238
−0.502
1.00
232.49
O


ATOM
A84CY
C23
NMY
12905
−87.473
−3.094
−2.737
1.00
232.49
C


ATOM
A84CZ
N23
NMY
12905
−91.491
−1.413
−1.254
1.00
232.49
N


END
















TABLE 9





H69 Neomycin Binding Site for Unrotated Ribosome

























ATOM
A420H
P
G
E1515
−32.433
114.986
100.787
1.00
64.61
P


ATOM
A420I
OP1
G
E1515
−32.585
115.515
102.164
1.00
64.61
O


ATOM
A420J
OP2
G
E1515
−32.068
113.560
100.608
1.00
64.61
O


ATOM
A420K
O5′
G
E1515
−33.730
115.326
99.932
1.00
64.61
O


ATOM
A420L
C5′
G
E1515
−34.372
116.582
100.063
1.00
64.61
C


ATOM
A420M
C4′
G
E1515
−35.385
116.813
98.972
1.00
64.61
C


ATOM
A420N
O4′
G
E1515
−34.809
116.509
97.674
1.00
64.61
O


ATOM
A420O
C1′
G
E1515
−35.813
115.999
96.817
1.00
64.61
C


ATOM
A420P
N9
G
E1515
−35.455
114.620
96.439
1.00
93.72
N


ATOM
A420Q
C4
G
E1515
−36.177
113.821
95.588
1.00
93.72
C


ATOM
A420R
N3
G
E1515
−37.315
114.161
94.948
1.00
93.72
N


ATOM
A420S
C2
G
E1515
−37.771
113.177
94.191
1.00
93.72
C


ATOM
A420T
N2
G
E1515
−38.899
113.349
93.483
1.00
93.72
N


ATOM
A420U
N1
G
E1515
−37.158
111.955
94.075
1.00
93.72
N


ATOM
A420V
C6
G
E1515
−35.988
111.587
94.728
1.00
93.72
C


ATOM
A420W
O6
G
E1515
−35.507
110.463
94.563
1.00
93.72
O


ATOM
A420X
C5
G
E1515
−35.490
112.631
95.540
1.00
93.72
C


ATOM
A420Y
N7
G
E1515
−34.363
112.670
96.344
1.00
93.72
N


ATOM
A420Z
C8
G
E1515
−34.385
113.865
96.860
1.00
93.72
C


ATOM
A4210
C2′
G
E1515
−37.133
116.046
97.587
1.00
64.61
C


ATOM
A4211
O2′
G
E1515
−37.758
117.299
97.345
1.00
64.61
O


ATOM
A4212
C3′
G
E1515
−36.632
115.952
99.019
1.00
64.61
C


ATOM
A4213
O3′
G
E1515
−37.566
116.396
99.983
1.00
64.61
O


ATOM
A421F
P
G
E1516
−37.979
115.445
101.210
1.00
83.64
P


ATOM
A421G
OP1
G
E1516
−38.308
116.328
102.354
1.00
83.64
O


ATOM
A421H
OP2
G
E1516
−36.904
114.436
101.375
1.00
83.64
O


ATOM
A421I
O5′
G
E1516
−39.298
114.748
100.672
1.00
83.64
O


ATOM
A421J
C5′
G
E1516
−40.435
115.528
100.360
1.00
83.64
C


ATOM
A421K
C4′
G
E1516
−41.017
115.163
99.023
1.00
83.64
C


ATOM
A421L
O4′
G
E1516
−39.966
114.817
98.086
1.00
83.64
O


ATOM
A421M
C1′
G
E1516
−40.476
113.920
97.117
1.00
83.64
C


ATOM
A421N
N9
G
E1516
−39.614
112.722
97.060
1.00
95.24
N


ATOM
A421O
C4
G
E1516
−39.911
111.570
96.370
1.00
95.24
C


ATOM
A421P
N3
G
E1516
−41.033
111.351
95.655
1.00
95.24
N


ATOM
A421Q
C2
G
E1516
−41.055
110.149
95.110
1.00
95.24
C


ATOM
A421R
N2
G
E1516
−42.110
109.781
94.366
1.00
95.24
N


ATOM
A421S
N1
G
E1516
−40.043
109.231
95.247
1.00
95.24
N


ATOM
A421T
C6
G
E1516
−38.875
109.434
95.977
1.00
95.24
C


ATOM
A421U
O6
G
E1516
−38.029
108.535
96.034
1.00
95.24
O


ATOM
A421V
C5
G
E1516
−38.845
110.723
96.573
1.00
95.24
C


ATOM
A421W
N7
G
E1516
−37.886
111.333
97.371
1.00
95.24
N


ATOM
A421X
C8
G
E1516
−38.381
112.514
97.633
1.00
95.24
C


ATOM
A421Y
C2′
G
E1516
−41.919
113.578
97.517
1.00
83.64
C


ATOM
A421Z
O2′
G
E1516
−42.803
114.408
96.779
1.00
83.64
O


ATOM
A4220
C3′
G
E1516
−41.923
113.948
98.993
1.00
83.64
C


ATOM
A4221
O3′
G
E1516
−43.212
114.204
99.521
1.00
83.64
O


ATOM
A422D
P
G
E1517
−43.683
113.489
100.880
1.00
79.55
P


ATOM
A422E
OP1
G
E1517
−44.894
114.203
101.356
1.00
79.55
O


ATOM
A422F
OP2
G
E1517
−42.501
113.420
101.772
1.00
79.55
O


ATOM
A422G
O5′
G
E1517
−44.074
112.028
100.393
1.00
79.55
O


ATOM
A422H
C5′
G
E1517
−45.072
111.841
99.403
1.00
79.55
C


ATOM
A422I
C4′
G
E1517
−45.759
110.505
99.551
1.00
79.55
C


ATOM
A422J
O4′
G
E1517
−47.191
110.688
99.426
1.00
79.55
O


ATOM
A422K
C1′
G
E1517
−47.756
109.610
98.712
1.00
79.55
C


ATOM
A422L
N9
G
E1517
−48.347
110.140
97.467
1.00
95.87
N


ATOM
A422M
C4
G
E1517
−49.170
109.483
96.581
1.00
95.87
C


ATOM
A422N
N3
G
E1517
−49.595
108.208
96.680
1.00
95.87
N


ATOM
A422O
C2
G
E1517
−50.375
107.866
95.668
1.00
95.87
C


ATOM
A422P
N2
G
E1517
−50.886
106.628
95.613
1.00
95.87
N


ATOM
A422Q
N1
G
E1517
−50.713
108.708
94.637
1.00
95.87
N


ATOM
A422R
C6
G
E1517
−50.287
110.025
94.513
1.00
95.87
C


ATOM
A422S
O6
G
E1517
−50.648
110.704
93.543
1.00
95.87
O


ATOM
A422T
C5
G
E1517
−49.449
110.404
95.593
1.00
95.87
C


ATOM
A422U
N7
G
E1517
−48.820
111.614
95.849
1.00
95.87
N


ATOM
A422V
C8
G
E1517
−48.181
111.411
96.967
1.00
95.87
C


ATOM
A422W
C2′
G
E1517
−46.658
108.593
98.446
1.00
79.55
C


ATOM
A422X
O2′
G
E1517
−46.657
107.636
99.496
1.00
79.55
O


ATOM
A422Y
C3′
G
E1517
−45.406
109.462
98.501
1.00
79.55
C


ATOM
A422Z
O3′
G
E1517
−44.230
108.740
98.814
1.00
79.55
O


ATOM
A423B
P
A
E1518
−42.948
108.828
97.853
1.00
57.08
P


ATOM
A423C
OP1
A
E1518
−41.810
108.216
98.582
1.00
57.08
O


ATOM
A423D
OP2
A
E1518
−42.835
110.234
97.414
1.00
57.08
O


ATOM
A423E
O5′
A
E1518
−43.364
107.907
96.623
1.00
57.08
O


ATOM
A423F
C5′
A
E1518
−43.642
106.529
96.812
1.00
57.08
C


ATOM
A423G
C4′
A
E1518
−44.650
106.021
95.813
1.00
57.08
C


ATOM
A423H
O4′
A
E1518
−45.868
106.803
95.891
1.00
57.08
O


ATOM
A423I
C1′
A
E1518
−46.473
106.877
94.617
1.00
57.08
C


ATOM
A423J
N9
A
E1518
−46.585
108.292
94.221
1.00
81.47
N


ATOM
A423K
C4
A
E1518
−47.383
108.760
93.210
1.00
81.47
C


ATOM
A423L
N3
A
E1518
−48.192
108.035
92.423
1.00
81.47
N


ATOM
A423M
C2
A
E1518
−48.822
108.818
91.552
1.00
81.47
C


ATOM
A423N
N1
A
E1518
−48.740
110.146
91.392
1.00
81.47
N


ATOM
A423O
C6
A
E1518
−47.916
110.847
92.203
1.00
81.47
C


ATOM
A423P
N6
A
E1518
−47.835
112.170
92.041
1.00
81.47
N


ATOM
A423Q
C5
A
E1518
−47.189
110.128
93.171
1.00
81.47
C


ATOM
A423R
N7
A
E1518
−46.277
110.517
94.142
1.00
81.47
N


ATOM
A423S
C8
A
E1518
−45.947
109.394
94.734
1.00
81.47
C


ATOM
A423T
C2′
A
E1518
−45.602
106.080
93.648
1.00
57.08
C


ATOM
A423U
O2′
A
E1518
−46.099
104.755
93.583
1.00
57.08
O


ATOM
A423V
C3′
A
E1518
−44.253
106.120
94.353
1.00
57.08
C


ATOM
A423W
O3′
A
E1518
−43.370
105.089
93.952
1.00
57.08
O


TER


ATOM
A676E
P
G
G1903
−35.400
131.852
122.787
1.00
74.00
P


ATOM
A676F
OP1
G
G1903
−36.024
131.508
124.089
1.00
74.00
O


ATOM
A676G
OP2
G
G1903
−34.071
131.280
122.460
1.00
74.00
O


ATOM
A676H
O5′
G
G1903
−36.420
131.561
121.599
1.00
74.00
O


ATOM
A676I
C5′
G
G1903
−37.693
130.982
121.843
1.00
74.00
C


ATOM
A676J
C4′
G
G1903
−38.746
131.586
120.952
1.00
74.00
C


ATOM
A676K
O4′
G
G1903
−38.117
132.461
119.981
1.00
74.00
O


ATOM
A676L
C1′
G
G1903
−38.817
132.413
118.760
1.00
74.00
C


ATOM
A676M
N9
G
G1903
−37.892
131.949
117.706
1.00
72.55
N


ATOM
A676N
C4
G
G1903
−38.213
131.642
116.407
1.00
72.55
C


ATOM
A676O
N3
G
G1903
−39.445
131.693
115.865
1.00
72.55
N


ATOM
A676P
C2
G
G1903
−39.447
131.332
114.596
1.00
72.55
C


ATOM
A676Q
N2
G
G1903
−40.608
131.333
113.926
1.00
72.55
N


ATOM
A676R
N1
G
G1903
−38.321
130.948
113.906
1.00
72.55
N


ATOM
A676S
C6
G
G1903
−37.038
130.887
114.445
1.00
72.55
C


ATOM
A676T
O6
G
G1903
−36.088
130.529
113.739
1.00
72.55
O


ATOM
A676U
C5
G
G1903
−37.026
131.273
115.810
1.00
72.55
C


ATOM
A676V
N7
G
G1903
−35.975
131.354
116.710
1.00
72.55
N


ATOM
A676W
C8
G
G1903
−36.533
131.761
117.817
1.00
72.55
C


ATOM
A676X
C2′
G
G1903
−40.011
131.475
118.945
1.00
74.00
C


ATOM
A676Y
O2′
G
G1903
−41.144
132.249
119.307
1.00
74.00
O


ATOM
A676Z
C3′
G
G1903
−39.549
130.608
120.108
1.00
74.00
C


ATOM
A6770
O3′
G
G1903
−40.617
130.011
120.831
1.00
74.00
O


ATOM
A677C
P
G
G1904
−40.936
128.438
120.683
1.00
70.78
P


ATOM
A677D
OP1
G
G1904
−41.613
128.013
121.933
1.00
70.78
O


ATOM
A677E
OP2
G
G1904
−39.675
127.763
120.294
1.00
70.78
O


ATOM
A677F
O5′
G
G1904
−41.966
128.397
119.472
1.00
70.78
O


ATOM
A677G
C5′
G
G1904
−43.168
129.152
119.505
1.00
70.78
C


ATOM
A677H
C4′
G
G1904
−43.857
129.147
118.164
1.00
70.78
C


ATOM
A677I
O4′
G
G1904
−43.059
129.891
117.203
1.00
70.78
O


ATOM
A677J
C1′
G
G1904
−43.103
129.257
115.943
1.00
70.78
C


ATOM
A677K
N9
G
G1904
−41.753
128.748
115.635
1.00
49.07
N


ATOM
A677L
C4
G
G1904
−41.288
128.235
114.445
1.00
49.07
C


ATOM
A677M
N3
G
G1904
−41.978
128.099
113.292
1.00
49.07
N


ATOM
A677N
C2
G
G1904
−41.239
127.572
112.326
1.00
49.07
C


ATOM
A677O
N2
G
G1904
−41.766
127.367
111.109
1.00
49.07
N


ATOM
A677P
N1
G
G1904
−39.925
127.209
112.478
1.00
49.07
N


ATOM
A677Q
C6
G
G1904
−39.196
127.341
113.653
1.00
49.07
C


ATOM
A677R
O6
G
G1904
−38.014
126.984
113.696
1.00
49.07
O


ATOM
A677S
C5
G
G1904
−39.974
127.901
114.692
1.00
49.07
C


ATOM
A677T
N7
G
G1904
−39.616
128.188
115.997
1.00
49.07
N


ATOM
A677U
C8
G
G1904
−40.701
128.684
116.515
1.00
49.07
C


ATOM
A677V
C2′
G
G1904
−44.125
128.128
116.037
1.00
70.78
C


ATOM
A677W
O2′
G
G1904
−45.405
128.646
115.707
1.00
70.78
O


ATOM
A677X
C3′
G
G1904
−44.043
127.781
117.515
1.00
70.78
C


ATOM
A677Y
O3′
G
G1904
−45.176
127.082
118.002
1.00
70.78
O


ATOM
A678A
P
C
G1905
−45.138
125.480
118.153
1.00
73.26
P


ATOM
A678B
OP1
C
G1905
−46.412
125.072
118.791
1.00
73.26
O


ATOM
A678C
OP2
C
G1905
−43.861
125.132
118.825
1.00
73.26
O


ATOM
A678D
O5′
C
G1905
−45.107
124.983
116.641
1.00
73.26
O


ATOM
A678E
C5′
C
G1905
−46.168
125.291
115.749
1.00
73.26
C


ATOM
A678F
C4′
C
G1905
−45.816
124.931
114.328
1.00
73.26
C


ATOM
A678G
O4′
C
G1905
−44.543
125.519
113.980
1.00
73.26
O


ATOM
A678H
C1′
C
G1905
−43.846
124.692
113.083
1.00
73.26
C


ATOM
A678I
N1
C
G1905
−42.483
124.446
113.623
1.00
58.02
N


ATOM
A678J
C6
C
G1905
−42.107
124.859
114.877
1.00
58.02
C


ATOM
A678K
C2
C
G1905
−41.542
123.838
112.794
1.00
58.02
C


ATOM
A678L
O2
C
G1905
−41.886
123.486
111.658
1.00
58.02
O


ATOM
A678M
N3
C
G1905
−40.285
123.625
113.247
1.00
58.02
N


ATOM
A678N
C4
C
G1905
−39.938
124.013
114.472
1.00
58.02
C


ATOM
A678O
N4
C
G1905
−38.691
123.793
114.889
1.00
58.02
N


ATOM
A678P
C5
C
G1905
−40.865
124.654
115.336
1.00
58.02
C


ATOM
A678Q
C2′
C
G1905
−44.656
123.404
112.884
1.00
73.26
C


ATOM
A678R
O2′
C
G1905
−45.330
123.464
111.632
1.00
73.26
O


ATOM
A678S
C3′
C
G1905
−45.650
123.444
114.045
1.00
73.26
C


ATOM
A678T
O3′
C
G1905
−46.890
122.816
113.751
1.00
73.26
O


ATOM
A6795
P
G
G1906
−47.085
121.238
113.975
1.00
86.11
P


ATOM
A6796
OP1
G
G1906
−46.313
120.870
115.186
1.00
86.11
O


ATOM
A6797
OP2
G
G1906
−46.757
120.572
112.691
1.00
86.11
O


ATOM
A6798
O5′
G
G1906
−48.648
121.111
114.272
1.00
86.11
O


ATOM
A6799
C5′
G
G1906
−49.611
121.312
113.245
1.00
86.11
C


ATOM
A679A
C4′
G
G1906
−50.768
122.155
113.729
1.00
86.11
C


ATOM
A679B
O4′
G
G1906
−50.940
123.304
112.851
1.00
86.11
O


ATOM
A679C
C1′
G
G1906
−52.320
123.569
112.676
1.00
86.11
C


ATOM
A679D
N9
G
G1906
−52.684
123.232
111.291
1.00
72.55
N


ATOM
A679E
C4
G
G1906
−53.858
123.526
110.643
1.00
72.55
C


ATOM
A679F
N3
G
G1906
−54.895
124.226
111.148
1.00
72.55
N


ATOM
A679G
C2
G
G1906
−55.873
124.356
110.268
1.00
72.55
C


ATOM
A679H
N2
G
G1906
−56.989
125.024
110.599
1.00
72.55
N


ATOM
A679I
N1
G
G1906
−55.830
123.838
108.999
1.00
72.55
N


ATOM
A679J
C6
G
G1906
−54.776
123.115
108.458
1.00
72.55
C


ATOM
A679K
O6
G
G1906
−54.843
122.693
107.299
1.00
72.55
O


ATOM
A679L
C5
G
G1906
−53.721
122.966
109.391
1.00
72.55
C


ATOM
A679M
N7
G
G1906
−52.496
122.325
109.262
1.00
72.55
N


ATOM
A679N
C8
G
G1906
−51.926
122.502
110.420
1.00
72.55
C


ATOM
A679O
C2′
G
G1906
−53.067
122.691
113.665
1.00
86.11
C


ATOM
A679P
O2′
G
G1906
−53.107
123.357
114.919
1.00
86.11
O


ATOM
A679Q
C3′
G
G1906
−52.139
121.491
113.716
1.00
86.11
C


ATOM
A679R
O3′
G
G1906
−52.373
120.635
114.816
1.00
86.11
O


ATOM
A67A3
P
G
G1907
−53.423
119.426
114.673
1.00
88.28
P


ATOM
A67A4
OP1
G
G1907
−53.600
118.840
116.023
1.00
88.28
O


ATOM
A67A5
OP2
G
G1907
−52.937
118.555
113.575
1.00
88.28
O


ATOM
A67A6
O5′
G
G1907
−54.759
120.167
114.225
1.00
88.28
O


ATOM
A67A7
C5′
G
G1907
−55.480
120.981
115.136
1.00
88.28
C


ATOM
A67A8
C4′
G
G1907
−56.890
121.232
114.667
1.00
88.28
C


ATOM
A67A9
O4′
G
G1907
−56.892
122.091
113.497
1.00
88.28
O


ATOM
A67AA
C1′
G
G1907
−58.027
121.799
112.703
1.00
88.28
C


ATOM
A67AB
N9
G
G1907
−57.584
121.439
111.343
1.00
87.88
N


ATOM
A67AC
C4
G
G1907
−58.377
121.474
110.223
1.00
87.88
C


ATOM
A67AD
N3
G
G1907
−59.670
121.857
110.190
1.00
87.88
N


ATOM
A67AE
C2
G
G1907
−60.175
121.792
108.971
1.00
87.88
C


ATOM
A67AF
N2
G
G1907
−61.453
122.142
108.762
1.00
87.88
N


ATOM
A67AG
N1
G
G1907
−59.462
121.387
107.872
1.00
87.88
N


ATOM
A67AH
C6
G
G1907
−58.129
120.988
107.880
1.00
87.88
C


ATOM
A67AI
O6
G
G1907
−57.588
120.640
106.823
1.00
87.88
O


ATOM
A67AJ
C5
G
G1907
−57.576
121.051
109.186
1.00
87.88
C


ATOM
A67AK
N7
G
G1907
−56.301
120.749
109.648
1.00
87.88
N


ATOM
A67AL
C8
G
G1907
−56.353
120.991
110.931
1.00
87.88
C


ATOM
A67AM
C2′
G
G1907
−58.779
120.650
113.378
1.00
88.28
C


ATOM
A67AN
O2′
G
G1907
−59.792
121.197
114.211
1.00
88.28
O


ATOM
A67AO
C3′
G
G1907
−57.670
120.017
114.208
1.00
88.28
C


ATOM
A67AP
O3′
G
G1907
−58.137
119.221
115.280
1.00
88.28
O


ATOM
A67B1
P
C
G1908
−58.845
117.812
114.984
1.00
68.10
P


ATOM
A67B2
OP1
C
G1908
−58.845
117.047
116.255
1.00
68.10
O


ATOM
A67B3
OP2
C
G1908
−58.177
117.224
113.798
1.00
68.10
O


ATOM
A67B4
O5′
C
G1908
−60.328
118.242
114.612
1.00
68.10
O


ATOM
A67B5
C5′
C
G1908
−61.303
117.274
114.276
1.00
68.10
C


ATOM
A67B6
C4′
C
G1908
−62.390
117.863
113.420
1.00
68.10
C


ATOM
A67B7
O4′
C
G1908
−61.859
118.975
112.647
1.00
68.10
O


ATOM
A67B8
C1′
C
G1908
−62.377
118.942
111.337
1.00
68.10
C


ATOM
A67B9
N1
C
G1908
−61.271
118.596
110.409
1.00
64.93
N


ATOM
A67BA
C6
C
G1908
−60.058
118.171
110.888
1.00
64.93
C


ATOM
A67BB
C2
C
G1908
−61.463
118.727
109.032
1.00
64.93
C


ATOM
A67BC
O2
C
G1908
−62.563
119.113
108.616
1.00
64.93
O


ATOM
A67BD
N3
C
G1908
−60.450
118.421
108.186
1.00
64.93
N


ATOM
A67BE
C4
C
G1908
−59.280
118.005
108.672
1.00
64.93
C


ATOM
A67BF
N4
C
G1908
−58.299
117.714
107.821
1.00
64.93
N


ATOM
A67BG
C5
C
G1908
−59.050
117.868
110.064
1.00
64.93
C


ATOM
A67BH
C2′
C
G1908
−63.491
117.901
111.321
1.00
68.10
C


ATOM
A67BI
O2′
C
G1908
−64.696
118.529
111.740
1.00
68.10
O


ATOM
A67BJ
C3′
C
G1908
−62.986
116.933
112.378
1.00
68.10
C


ATOM
A67BK
O3′
C
G1908
−63.989
116.084
112.911
1.00
68.10
O


ATOM
A67BW
P
C
G1909
−63.895
114.492
112.709
1.00
116.78
P


ATOM
A67BX
OP1
C
G1909
−64.729
113.868
113.765
1.00
116.78
O


ATOM
A67BY
OP2
C
G1909
−62.455
114.137
112.635
1.00
116.78
O


ATOM
A67BZ
O5′
C
G1909
−64.578
114.283
111.290
1.00
116.78
O


ATOM
A67C0
C5′
C
G1909
−65.852
114.839
111.009
1.00
116.78
C


ATOM
A67C1
C4′
C
G1909
−66.095
114.946
109.528
1.00
116.78
C


ATOM
A67C2
O4′
C
G1909
−65.228
115.958
108.947
1.00
116.78
O


ATOM
A67C3
C1′
C
G1909
−64.869
115.576
107.633
1.00
116.78
C


ATOM
A67C4
N1
C
G1909
−63.398
115.397
107.572
1.00
73.62
N


ATOM
A67C5
C6
C
G1909
−62.612
115.314
108.693
1.00
73.62
C


ATOM
A67C6
C2
C
G1909
−62.813
115.299
106.309
1.00
73.62
C


ATOM
A67C7
O2
C
G1909
−63.538
115.371
105.308
1.00
73.62
O


ATOM
A67C8
N3
C
G1909
−61.477
115.127
106.200
1.00
73.62
N


ATOM
A67C9
C4
C
G1909
−60.722
115.050
107.294
1.00
73.62
C


ATOM
A67CA
N4
C
G1909
−59.409
114.882
107.139
1.00
73.62
N


ATOM
A67CB
C5
C
G1909
−61.285
115.145
108.598
1.00
73.62
C


ATOM
A67CC
C2′
C
G1909
−65.611
114.276
107.320
1.00
116.78
C


ATOM
A67CD
O2′
C
G1909
−66.870
114.593
106.738
1.00
116.78
O


ATOM
A67CE
C3′
C
G1909
−65.785
113.704
108.716
1.00
116.78
C


ATOM
A67CF
O3′
C
G1909
−66.793
112.716
108.815
1.00
116.78
O


ATOM
A67CR
P
G
G1910
−66.400
111.158
108.868
1.00
107.42
P


ATOM
A67CS
OP1
G
G1910
−67.527
110.446
109.517
1.00
107.42
O


ATOM
A67CT
OP2
G
G1910
−65.050
111.060
109.478
1.00
107.42
O


ATOM
A67CU
O5′
G
G1910
−66.328
110.769
107.331
1.00
107.42
O


ATOM
A67CV
C5′
G
G1910
−67.397
111.084
106.455
1.00
107.42
C


ATOM
A67CW
C4′
G
G1910
−66.975
111.001
105.013
1.00
107.42
C


ATOM
A67CX
O4′
G
G1910
−65.979
112.020
104.727
1.00
107.42
O


ATOM
A67CY
C1′
G
G1910
−65.073
111.536
103.755
1.00
107.42
C


ATOM
A67CZ
N9
G
G1910
−63.727
111.477
104.349
1.00
63.82
N


ATOM
A67D0
C4
G
G1910
−62.576
111.277
103.633
1.00
63.82
C


ATOM
A67D1
N3
G
G1910
−62.501
111.139
102.294
1.00
63.82
N


ATOM
A67D2
C2
G
G1910
−61.258
110.971
101.884
1.00
63.82
C


ATOM
A67D3
N2
G
G1910
−61.012
110.820
100.574
1.00
63.82
N


ATOM
A67D4
N1
G
G1910
−60.175
110.942
102.728
1.00
63.82
N


ATOM
A67D5
C6
G
G1910
−60.233
111.078
104.113
1.00
63.82
C


ATOM
A67D6
O6
G
G1910
−59.195
111.040
104.781
1.00
63.82
O


ATOM
A67D7
C5
G
G1910
−61.564
111.263
104.564
1.00
63.82
C


ATOM
A67D8
N7
G
G1910
−62.070
111.438
105.846
1.00
63.82
N


ATOM
A67D9
C8
G
G1910
−63.359
111.553
105.671
1.00
63.82
C


ATOM
A67DA
C2′
G
G1910
−65.557
110.151
103.335
1.00
107.42
C


ATOM
A67DB
O2′
G
G1910
−66.453
110.295
102.244
1.00
107.42
O


ATOM
A67DC
C3′
G
G1910
−66.292
109.714
104.589
1.00
107.42
C


ATOM
A67DD
O3′
G
G1910
−67.192
108.642
104.384
1.00
107.42
O


ATOM
A67DP
P
U
G1911
−66.743
107.137
104.731
1.00
103.54
P


ATOM
A67DQ
OP1
U
G1911
−67.950
106.284
104.617
1.00
103.54
O


ATOM
A67DR
OP2
U
G1911
−66.022
107.182
106.028
1.00
103.54
O


ATOM
A67DS
O5′
U
G1911
−65.724
106.795
103.557
1.00
103.54
O


ATOM
A67DT
C5′
U
G1911
−66.099
106.945
102.195
1.00
103.54
C


ATOM
A67DU
C4′
U
G1911
−64.907
106.858
101.273
1.00
103.54
C


ATOM
A67DV
O4′
U
G1911
−63.970
107.928
101.564
1.00
103.54
O


ATOM
A67DW
C1′
U
G1911
−62.647
107.485
101.334
1.00
103.54
C


ATOM
A67DX
N1
U
G1911
−61.879
107.593
102.604
1.00
96.63
N


ATOM
A67DY
C6
U
G1911
−62.487
107.646
103.840
1.00
96.63
C


ATOM
A67DZ
C2
U
G1911
−60.501
107.643
102.501
1.00
96.63
C


ATOM
A67E0
O2
U
G1911
−59.914
107.601
101.435
1.00
96.63
O


ATOM
A67E1
N3
U
G1911
−59.826
107.741
103.692
1.00
96.63
N


ATOM
A67E2
C4
U
G1911
−60.375
107.795
104.955
1.00
96.63
C


ATOM
A67E3
O4
U
G1911
−59.638
107.882
105.939
1.00
96.63
O


ATOM
A67E4
C5
U
G1911
−61.805
107.741
104.988
1.00
96.63
C


ATOM
A67E5
C2′
U
G1911
−62.725
106.042
100.827
1.00
103.54
C


ATOM
A67E6
O2′
U
G1911
−62.741
106.050
99.404
1.00
103.54
O


ATOM
A67E7
C3′
U
G1911
−64.069
105.596
101.387
1.00
103.54
C


ATOM
A67E8
O3′
U
G1911
−64.640
104.497
100.697
1.00
103.54
O


ATOM
A67EJ
P
A
G1912
−64.665
103.035
101.365
1.00
71.84
P


ATOM
A67EK
OP1
A
G1912
−64.679
103.219
102.837
1.00
71.84
O


ATOM
A67EL
OP2
A
G1912
−65.779
102.288
100.732
1.00
71.84
O


ATOM
A67EM
O5′
A
G1912
−63.271
102.419
100.905
1.00
71.84
O


ATOM
A67EN
C5′
A
G1912
−62.873
102.467
99.542
1.00
71.84
C


ATOM
A67EO
C4′
A
G1912
−61.864
101.395
99.209
1.00
71.84
C


ATOM
A67EP
O4′
A
G1912
−60.529
101.854
99.516
1.00
71.84
O


ATOM
A67EQ
C1′
A
G1912
−59.698
100.744
99.766
1.00
71.84
C


ATOM
A67ER
N9
A
G1912
−58.922
100.983
101.000
1.00
73.35
N


ATOM
A67ES
C4
A
G1912
−57.646
101.489
101.023
1.00
73.35
C


ATOM
A67ET
N3
A
G1912
−56.907
101.850
99.962
1.00
73.35
N


ATOM
A67EU
C2
A
G1912
−55.717
102.299
100.346
1.00
73.35
C


ATOM
A67EV
N1
A
G1912
−55.215
102.419
101.580
1.00
73.35
N


ATOM
A67EW
C6
A
G1912
−55.981
102.047
102.628
1.00
73.35
C


ATOM
A67EX
N6
A
G1912
−55.470
102.172
103.856
1.00
73.35
N


ATOM
A67EY
C5
A
G1912
−57.271
101.551
102.351
1.00
73.35
C


ATOM
A67EZ
N7
A
G1912
−58.299
101.090
103.161
1.00
73.35
N


ATOM
A67F0
C8
A
G1912
−59.252
100.764
102.316
1.00
73.35
C


ATOM
A67F1
C2′
A
G1912
−60.584
99.492
99.855
1.00
71.84
C


ATOM
A67F2
O2′
A
G1912
−60.451
98.740
98.655
1.00
71.84
O


ATOM
A67F3
C3′
A
G1912
−61.985
100.088
99.977
1.00
71.84
C


ATOM
A67F4
O3′
A
G1912
−63.002
99.245
99.462
1.00
71.84
O


ATOM
A67FG
P
A
G1913
−64.048
98.540
100.455
1.00
137.65
P


ATOM
A67FH
OP1
A
G1913
−63.284
98.088
101.642
1.00
137.65
O


ATOM
A67FI
OP2
A
G1913
−65.169
99.489
100.650
1.00
137.65
O


ATOM
A67FJ
O5′
A
G1913
−64.547
97.280
99.615
1.00
137.65
O


ATOM
A67FK
C5′
A
G1913
−63.651
96.537
98.793
1.00
137.65
C


ATOM
A67FL
C4′
A
G1913
−63.509
95.111
99.266
1.00
137.65
C


ATOM
A67FM
O4′
A
G1913
−62.917
94.310
98.200
1.00
137.65
O


ATOM
A67FN
C1′
A
G1913
−61.714
93.731
98.670
1.00
137.65
C


ATOM
A67FO
N9
A
G1913
−60.764
93.660
97.569
1.00
496.26
N


ATOM
A67FP
C4
A
G1913
−60.992
93.285
96.273
1.00
496.26
C


ATOM
A67FQ
N3
A
G1913
−62.139
92.924
95.678
1.00
496.26
N


ATOM
A67FR
C2
A
G1913
−61.934
92.649
94.392
1.00
496.26
C


ATOM
A67FS
N1
A
G1913
−60.792
92.695
93.688
1.00
496.26
N


ATOM
A67FT
C6
A
G1913
−59.660
93.067
94.336
1.00
496.26
C


ATOM
A67FU
N6
A
G1913
−58.450
93.160
93.776
1.00
496.26
N


ATOM
A67FV
C5
A
G1913
−59.756
93.382
95.681
1.00
496.26
C


ATOM
A67FW
N7
A
G1913
−58.769
93.784
96.556
1.00
496.26
N


ATOM
A67FX
C8
A
G1913
−59.424
93.931
97.668
1.00
496.26
C


ATOM
A67FY
C2′
A
G1913
−61.262
94.628
99.809
1.00
137.65
C


ATOM
A67FZ
O2′
A
G1913
−60.285
94.014
100.623
1.00
137.65
O


ATOM
A67G0
C3′
A
G1913
−62.598
94.918
100.478
1.00
137.65
C


ATOM
A67G1
O3′
A
G1913
−63.036
93.773
101.212
1.00
137.65
O


ATOM
A67GD
P
C
G1914
−62.121
93.141
102.371
1.00
224.95
P


ATOM
A67GE
OP1
C
G1914
−61.510
91.907
101.820
1.00
224.95
O


ATOM
A67GF
OP2
C
G1914
−61.230
94.218
102.863
1.00
224.95
O


ATOM
A67GG
O5′
C
G1914
−63.185
92.765
103.483
1.00
224.95
O


ATOM
A67GH
C5′
C
G1914
−64.438
92.211
103.124
1.00
224.95
C


ATOM
A67GI
C4′
C
G1914
−65.087
91.531
104.295
1.00
224.95
C


ATOM
A67GJ
O4′
C
G1914
−64.335
90.341
104.646
1.00
224.95
O


ATOM
A67GK
C1′
C
G1914
−64.322
90.171
106.046
1.00
224.95
C


ATOM
A67GL
N1
C
G1914
−62.915
90.261
106.538
1.00
81.16
N


ATOM
A67GM
C6
C
G1914
−62.723
90.146
107.891
1.00
81.16
C


ATOM
A67GN
C2
C
G1914
−61.786
90.426
105.703
1.00
81.16
C


ATOM
A67GO
O2
C
G1914
−61.876
90.533
104.472
1.00
81.16
O


ATOM
A67GP
N3
C
G1914
−60.555
90.487
106.261
1.00
81.16
N


ATOM
A67GQ
C4
C
G1914
−60.399
90.380
107.578
1.00
81.16
C


ATOM
A67GR
N4
C
G1914
−59.163
90.442
108.073
1.00
81.16
N


ATOM
A67GS
C5
C
G1914
−61.508
90.203
108.447
1.00
81.16
C


ATOM
A67GT
C2′
C
G1914
−65.216
91.257
106.647
1.00
224.95
C


ATOM
A67GU
O2′
C
G1914
−66.539
90.752
106.750
1.00
224.95
O


ATOM
A67GV
C3′
C
G1914
−65.129
92.338
105.582
1.00
224.95
C


ATOM
A67GW
O3′
C
G1914
−66.202
93.265
105.618
1.00
224.95
O


ATOM
A67H8
P
U
G1915
−65.932
94.835
105.381
1.00
121.80
P


ATOM
A67H9
OP1
U
G1915
−67.215
95.436
104.942
1.00
121.80
O


ATOM
A67HA
OP2
U
G1915
−64.751
94.948
104.489
1.00
121.80
O


ATOM
A67HB
O5′
U
G1915
−65.559
95.359
106.839
1.00
121.80
O


ATOM
A67HC
C5′
U
G1915
−66.250
94.892
107.989
1.00
121.80
C


ATOM
A67HD
C4′
U
G1915
−65.312
94.687
109.155
1.00
121.80
C


ATOM
A67HE
O4′
U
G1915
−64.344
93.652
108.836
1.00
121.80
O


ATOM
A67HF
C1′
U
G1915
−63.104
93.946
109.446
1.00
121.80
C


ATOM
A67HG
N1
U
G1915
−62.076
94.105
108.388
1.00
72.93
N


ATOM
A67HH
C6
U
G1915
−62.401
94.387
107.081
1.00
72.93
C


ATOM
A67HI
C2
U
G1915
−60.752
93.993
108.768
1.00
72.93
C


ATOM
A67HJ
O2
U
G1915
−60.407
93.754
109.911
1.00
72.93
O


ATOM
A67HK
N3
U
G1915
−59.839
94.165
107.757
1.00
72.93
N


ATOM
A67HL
C4
U
G1915
−60.109
94.439
106.432
1.00
72.93
C


ATOM
A67HM
O4
U
G1915
−59.183
94.570
105.633
1.00
72.93
O


ATOM
A67HN
C5
U
G1915
−61.496
94.550
106.114
1.00
72.93
C


ATOM
A67HO
C2′
U
G1915
−63.282
95.230
110.256
1.00
121.80
C


ATOM
A67HP
O2′
U
G1915
−63.618
94.896
111.596
1.00
121.80
O


ATOM
A67HQ
C3′
U
G1915
−64.458
95.883
109.545
1.00
121.80
C


ATOM
A67HR
O3′
U
G1915
−65.153
96.825
110.345
1.00
121.80
O


ATOM
A67I2
P
A
G1916
−64.984
98.402
110.077
1.00
91.53
P


ATOM
A67I3
OP1
A
G1916
−65.945
99.100
110.964
1.00
91.53
O


ATOM
A67I4
OP2
A
G1916
−65.085
98.612
108.612
1.00
91.53
O


ATOM
A67I5
O5′
A
G1916
−63.495
98.690
110.563
1.00
91.53
O


ATOM
A67I6
C5′
A
G1916
−63.113
98.480
111.914
1.00
91.53
C


ATOM
A67I7
C4′
A
G1916
−61.611
98.403
112.060
1.00
91.53
C


ATOM
A67I8
O4′
A
G1916
−61.105
97.271
111.303
1.00
91.53
O


ATOM
A67I9
C1′
A
G1916
−59.860
97.594
110.720
1.00
91.53
C


ATOM
A67IA
N9
A
G1916
−60.011
97.582
109.250
1.00
100.55
N


ATOM
A67IB
C4
A
G1916
−59.002
97.570
108.311
1.00
100.55
C


ATOM
A67IC
N3
A
G1916
−57.674
97.539
108.521
1.00
100.55
N


ATOM
A67ID
C2
A
G1916
−57.013
97.525
107.365
1.00
100.55
C


ATOM
A67IE
N1
A
G1916
−57.491
97.537
106.111
1.00
100.55
N


ATOM
A67IF
C6
A
G1916
−58.831
97.568
105.934
1.00
100.55
C


ATOM
A67IG
N6
A
G1916
−59.343
97.583
104.699
1.00
100.55
N


ATOM
A67IH
C5
A
G1916
−59.636
97.586
107.082
1.00
100.55
C


ATOM
A67II
N7
A
G1916
−61.010
97.618
107.230
1.00
100.55
N


ATOM
A67IJ
C8
A
G1916
−61.179
97.621
108.526
1.00
100.55
C


ATOM
A67IK
C2′
A
G1916
−59.460
98.971
111.233
1.00
91.53
C


ATOM
A67IL
O2′
A
G1916
−58.703
98.814
112.425
1.00
91.53
O


ATOM
A67IM
C3′
A
G1916
−60.821
99.591
111.529
1.00
91.53
C


ATOM
A67IN
O3′
A
G1916
−60.766
100.675
112.444
1.00
91.53
O


ATOM
A67IZ
P
U
G1917
−61.129
102.171
111.970
1.00
86.96
P


ATOM
A67J0
OP1
U
G1917
−61.457
102.946
113.190
1.00
86.96
O


ATOM
A67J1
OP2
U
G1917
−62.154
102.060
110.902
1.00
86.96
O


ATOM
A67J2
O5′
U
G1917
−59.756
102.693
111.351
1.00
86.96
O


ATOM
A67J3
C5′
U
G1917
−58.591
102.816
112.156
1.00
86.96
C


ATOM
A67J4
C4′
U
G1917
−57.340
102.464
111.385
1.00
86.96
C


ATOM
A67J5
O4′
U
G1917
−57.544
101.223
110.662
1.00
86.96
O


ATOM
A67J6
C1′
U
G1917
−56.855
101.262
109.428
1.00
86.96
C


ATOM
A67J7
N1
U
G1917
−57.840
101.145
108.318
1.00
56.93
N


ATOM
A67J8
C6
U
G1917
−59.205
101.188
108.502
1.00
56.93
C


ATOM
A67J9
C2
U
G1917
−57.320
100.967
107.050
1.00
56.93
C


ATOM
A67JA
O2
U
G1917
−56.121
100.919
106.830
1.00
56.93
O


ATOM
A67JB
N3
U
G1917
−58.249
100.855
106.044
1.00
56.93
N


ATOM
A67JC
C4
U
G1917
−59.621
100.892
106.170
1.00
56.93
C


ATOM
A67JD
O4
U
G1917
−60.335
100.775
105.174
1.00
56.93
O


ATOM
A67JE
C5
U
G1917
−60.090
101.072
107.507
1.00
56.93
C


ATOM
A67JF
C2′
U
G1917
−56.080
102.575
109.378
1.00
86.96
C


ATOM
A67JG
O2′
U
G1917
−54.782
102.353
109.920
1.00
86.96
O


ATOM
A67JH
C3′
U
G1917
−56.915
103.448
110.304
1.00
86.96
C


ATOM
A67JI
O3′
U
G1917
−56.216
104.567
110.814
1.00
86.96
O


ATOM
A67JT
P
A
G1918
−56.422
106.014
110.149
1.00
77.15
P


ATOM
A67JU
OP1
A
G1918
−55.338
106.886
110.661
1.00
77.15
O


ATOM
A67JV
OP2
A
G1918
−57.833
106.411
110.390
1.00
77.15
O


ATOM
A67JW
O5′
A
G1918
−56.197
105.726
108.602
1.00
77.15
O


ATOM
A67JX
C5′
A
G1918
−54.895
105.472
108.088
1.00
77.15
C


ATOM
A67JY
C4′
A
G1918
−54.890
105.417
106.582
1.00
77.15
C


ATOM
A67JZ
O4′
A
G1918
−55.918
104.490
106.136
1.00
77.15
O


ATOM
A67K0
C1′
A
G1918
−56.754
105.117
105.184
1.00
77.15
C


ATOM
A67K1
N9
A
G1918
−58.120
104.623
105.368
1.00
70.62
N


ATOM
A67K2
C4
A
G1918
−59.022
104.329
104.375
1.00
70.62
C


ATOM
A67K3
N3
A
G1918
−58.835
104.421
103.049
1.00
70.62
N


ATOM
A67K4
C2
A
G1918
−59.932
104.048
102.393
1.00
70.62
C


ATOM
A67K5
N1
A
G1918
−61.109
103.631
102.877
1.00
70.62
N


ATOM
A67K6
C6
A
G1918
−61.265
103.555
104.215
1.00
70.62
C


ATOM
A67K7
N6
A
G1918
−62.436
103.139
104.702
1.00
70.62
N


ATOM
A67K8
C5
A
G1918
−60.174
103.922
105.021
1.00
70.62
C


ATOM
A67K9
N7
A
G1918
−60.005
103.958
106.397
1.00
70.62
N


ATOM
A67KA
C8
A
G1918
−58.774
104.383
106.550
1.00
70.62
C


ATOM
A67KB
C2′
A
G1918
−56.617
106.617
105.418
1.00
77.15
C


ATOM
A67KC
O2′
A
G1918
−56.933
107.355
104.256
1.00
77.15
O


ATOM
A67KD
C3′
A
G1918
−55.168
106.747
105.882
1.00
77.15
C


ATOM
A67KE
O3′
A
G1918
−54.304
106.899
104.759
1.00
77.15
O


ATOM
A67KQ
P
A
G1919
−52.939
107.735
104.908
1.00
76.58
P


ATOM
A67KR
OP1
A
G1919
−51.997
106.895
105.689
1.00
76.58
O


ATOM
A67KS
OP2
A
G1919
−53.303
109.074
105.434
1.00
76.58
O


ATOM
A67KT
O5′
A
G1919
−52.433
107.867
103.406
1.00
76.58
O


ATOM
A67KU
C5′
A
G1919
−51.059
108.080
103.113
1.00
76.58
C


ATOM
A67KV
C4′
A
G1919
−50.668
107.406
101.826
1.00
76.58
C


ATOM
A67KW
O4′
A
G1919
−51.141
106.029
101.839
1.00
76.58
O


ATOM
A67KX
C1′
A
G1919
−51.695
105.696
100.586
1.00
76.58
C


ATOM
A67KY
N9
A
G1919
−53.159
105.609
100.746
1.00
55.65
N


ATOM
A67KZ
C4
A
G1919
−54.118
105.573
99.762
1.00
55.65
C


ATOM
A67L0
N3
A
G1919
−53.937
105.600
98.433
1.00
55.65
N


ATOM
A67L1
C2
A
G1919
−55.104
105.552
97.797
1.00
55.65
C


ATOM
A67L2
N1
A
G1919
−56.345
105.480
98.296
1.00
55.65
N


ATOM
A67L3
C6
A
G1919
−56.494
105.455
99.638
1.00
55.65
C


ATOM
A67L4
N6
A
G1919
−57.722
105.387
100.159
1.00
55.65
N


ATOM
A67L5
C5
A
G1919
−55.331
105.505
100.423
1.00
55.65
C


ATOM
A67L6
N7
A
G1919
−55.146
105.496
101.795
1.00
55.65
N


ATOM
A67L7
C8
A
G1919
−53.846
105.561
101.932
1.00
55.65
C


ATOM
A67L8
C2′
A
G1919
−51.300
106.805
99.621
1.00
76.58
C


ATOM
A67L9
O2′
A
G1919
−49.999
106.527
99.123
1.00
76.58
O


ATOM
A67LA
C3′
A
G1919
−51.276
107.997
100.560
1.00
76.58
C


ATOM
A67LB
O3′
A
G1919
−50.549
109.103
100.057
1.00
76.58
O


ATOM
A67LN
P
C
G1920
−51.199
110.573
100.040
1.00
62.49
P


ATOM
A67LO
OP1
C
G1920
−50.354
111.412
99.156
1.00
62.49
O


ATOM
A67LP
OP2
C
G1920
−51.382
110.988
101.451
1.00
62.49
O


ATOM
A67LQ
O5′
C
G1920
−52.614
110.330
99.361
1.00
62.49
O


ATOM
A67LR
C5′
C
G1920
−52.720
109.856
98.029
1.00
62.49
C


ATOM
A67LS
C4′
C
G1920
−54.160
109.749
97.602
1.00
62.49
C


ATOM
A67LT
O4′
C
G1920
−54.830
108.717
98.380
1.00
62.49
O


ATOM
A67LU
C1′
C
G1920
−56.146
109.124
98.689
1.00
62.49
C


ATOM
A67LV
N1
C
G1920
−56.240
109.339
100.152
1.00
114.54
N


ATOM
A67LW
C6
C
G1920
−55.136
109.326
100.960
1.00
114.54
C


ATOM
A67LX
C2
C
G1920
−57.498
109.562
100.713
1.00
114.54
C


ATOM
A67LY
O2
C
G1920
−58.490
109.572
99.969
1.00
114.54
O


ATOM
A67LZ
N3
C
G1920
−57.603
109.767
102.048
1.00
114.54
N


ATOM
A67M0
C4
C
G1920
−56.513
109.756
102.817
1.00
114.54
C


ATOM
A67M1
N4
C
G1920
−56.642
109.952
104.130
1.00
114.54
N


ATOM
A67M2
C5
C
G1920
−55.223
109.524
102.277
1.00
114.54
C


ATOM
A67M3
C2′
C
G1920
−56.413
110.409
97.908
1.00
62.49
C


ATOM
A67M4
O2′
C
G1920
−56.890
110.059
96.616
1.00
62.49
O


ATOM
A67M5
C3′
C
G1920
−55.011
110.988
97.833
1.00
62.49
C


ATOM
A67M6
O3′
C
G1920
−54.844
111.972
96.825
1.00
62.49
O


ATOM
A67MI
P
G
G1921
−54.720
113.529
97.220
1.00
67.45
P


ATOM
A67MJ
OP1
G
G1921
−54.045
114.212
96.090
1.00
67.45
O


ATOM
A67MK
OP2
G
G1921
−54.099
113.599
98.566
1.00
67.45
O


ATOM
A67ML
O5′
G
G1921
−56.238
113.990
97.299
1.00
67.45
O


ATOM
A67MM
C5′
G
G1921
−57.083
113.893
96.165
1.00
67.45
C


ATOM
A67MN
C4′
G
G1921
−58.536
113.983
96.549
1.00
67.45
C


ATOM
A67MO
O4′
G
G1921
−58.859
112.968
97.539
1.00
67.45
O


ATOM
A67MP
C1′
G
G1921
−59.853
113.463
98.417
1.00
67.45
C


ATOM
A67MQ
N9
G
G1921
−59.302
113.496
99.784
1.00
72.72
N


ATOM
A67MR
C4
G
G1921
−60.006
113.735
100.942
1.00
72.72
C


ATOM
A67MS
N3
G
G1921
−61.332
113.962
101.036
1.00
72.72
N


ATOM
A67MT
C2
G
G1921
−61.715
114.152
102.289
1.00
72.72
C


ATOM
A67MU
N2
G
G1921
−63.008
114.392
102.560
1.00
72.72
N


ATOM
A67MV
N1
G
G1921
−60.864
114.120
103.366
1.00
72.72
N


ATOM
A67MW
C6
G
G1921
−59.495
113.892
103.293
1.00
72.72
C


ATOM
A67MX
O6
G
G1921
−58.819
113.880
104.330
1.00
72.72
O


ATOM
A67MY
C5
G
G1921
−59.074
113.682
101.954
1.00
72.72
C


ATOM
A67MZ
N7
G
G1921
−57.812
113.421
101.442
1.00
72.72
N


ATOM
A67N0
C8
G
G1921
−57.992
113.324
100.157
1.00
72.72
C


ATOM
A67N1
C2′
G
G1921
−60.238
114.859
97.929
1.00
67.45
C


ATOM
A67N2
O2′
G
G1921
−61.320
114.738
97.017
1.00
67.45
O


ATOM
A67N3
C3′
G
G1921
−58.964
115.276
97.212
1.00
67.45
C


ATOM
A67N4
O3′
G
G1921
−59.137
116.339
96.293
1.00
67.45
O


ATOM
A67NG
P
G
G1922
−58.745
117.841
96.711
1.00
81.77
P


ATOM
A67NH
OP1
G
G1922
−58.661
118.635
95.461
1.00
81.77
O


ATOM
A67NI
OP2
G
G1922
−57.548
117.759
97.585
1.00
81.77
O


ATOM
A67NJ
O5′
G
G1922
−60.005
118.303
97.558
1.00
81.77
O


ATOM
A67NK
C5′
G
G1922
−61.318
118.141
97.049
1.00
81.77
C


ATOM
A67NL
C4′
G
G1922
−62.351
118.301
98.127
1.00
81.77
C


ATOM
A67NM
O4′
G
G1922
−62.198
117.257
99.122
1.00
81.77
O


ATOM
A67NN
C1′
G
G1922
−62.561
117.749
100.394
1.00
81.77
C


ATOM
A67NO
N9
G
G1922
−61.407
117.616
101.302
1.00
90.75
N


ATOM
A67NP
C4
G
G1922
−61.455
117.738
102.667
1.00
90.75
C


ATOM
A67NQ
N3
G
G1922
−62.559
117.992
103.400
1.00
90.75
N


ATOM
A67NR
C2
G
G1922
−62.292
118.051
104.694
1.00
90.75
C


ATOM
A67NS
N2
G
G1922
−63.282
118.295
105.567
1.00
90.75
N


ATOM
A67NT
N1
G
G1922
−61.039
117.874
105.226
1.00
90.75
N


ATOM
A67NU
C6
G
G1922
−59.893
117.612
104.485
1.00
90.75
C


ATOM
A67NV
O6
G
G1922
−58.815
117.470
105.063
1.00
90.75
O


ATOM
A67NW
C5
G
G1922
−60.162
117.547
103.096
1.00
90.75
C


ATOM
A67NX
N7
G
G1922
−59.314
117.311
102.022
1.00
90.75
N


ATOM
A67NY
C8
G
G1922
−60.096
117.363
100.978
1.00
90.75
C


ATOM
A67NZ
C2′
G
G1922
−62.987
119.208
100.224
1.00
81.77
C


ATOM
A67O0
O2′
G
G1922
−64.397
119.255
100.064
1.00
81.77
O


ATOM
A6701
C3′
G
G1922
−62.276
119.585
98.933
1.00
81.77
C


ATOM
A6702
O3′
G
G1922
−62.854
120.689
98.259
1.00
81.77
O


ATOM
A670E
P
U
G1923
−62.010
122.040
98.038
1.00
83.59
P


ATOM
A670F
OP1
U
G1923
−62.627
122.759
96.899
1.00
83.59
O


ATOM
A670G
OP2
U
G1923
−60.578
121.658
97.948
1.00
83.59
O


ATOM
A670H
O5′
U
G1923
−62.271
122.841
99.386
1.00
83.59
O


ATOM
A670I
C5′
U
G1923
−63.587
123.009
99.890
1.00
83.59
C


ATOM
A670J
C4′
U
G1923
−63.583
123.209
101.384
1.00
83.59
C


ATOM
A670K
O4′
U
G1923
−63.167
121.988
102.044
1.00
83.59
O


ATOM
A670L
C1′
U
G1923
−62.484
122.298
103.240
1.00
83.59
C


ATOM
A670M
N1
U
G1923
−61.135
121.681
103.195
1.00
81.85
N


ATOM
A670N
C6
U
G1923
−60.390
121.627
102.037
1.00
81.85
C


ATOM
A670O
C2
U
G1923
−60.622
121.174
104.375
1.00
81.85
C


ATOM
A670P
O2
U
G1923
−61.229
121.195
105.431
1.00
81.85
O


ATOM
A670Q
N3
U
G1923
−59.368
120.626
104.282
1.00
81.85
N


ATOM
A670R
C4
U
G1923
−58.580
120.538
103.155
1.00
81.85
C


ATOM
A670S
O4
U
G1923
−57.468
120.015
103.235
1.00
81.85
O


ATOM
A670T
C5
U
G1923
−59.167
121.088
101.972
1.00
81.85
C


ATOM
A670U
C2′
U
G1923
−62.411
123.823
103.355
1.00
83.59
C


ATOM
A670V
O2′
U
G1923
−63.468
124.282
104.185
1.00
83.59
O


ATOM
A670W
C3′
U
G1923
−62.623
124.260
101.911
1.00
83.59
C


ATOM
A670X
O3′
U
G1923
−63.132
125.575
101.784
1.00
83.59
O


ATOM
A67P8
P
C
G1924
−62.143
126.838
101.845
1.00
78.08
P


ATOM
A67P9
OP1
C
G1924
−62.902
128.009
101.346
1.00
78.08
O


ATOM
A67PA
OP2
C
G1924
−60.889
126.453
101.151
1.00
78.08
O


ATOM
A67PB
O5′
C
G1924
−61.876
126.994
103.401
1.00
78.08
O


ATOM
A67PC
C5′
C
G1924
−62.945
127.225
104.301
1.00
78.08
C


ATOM
A67PD
C4′
C
G1924
−62.520
127.021
105.730
1.00
78.08
C


ATOM
A67PE
O4′
C
G1924
−62.046
125.662
105.934
1.00
78.08
O


ATOM
A67PF
C1′
C
G1924
−61.051
125.658
106.944
1.00
78.08
C


ATOM
A67PG
N1
C
G1924
−59.793
125.128
106.376
1.00
91.84
N


ATOM
A67PH
C6
C
G1924
−59.506
125.229
105.046
1.00
91.84
C


ATOM
A67PI
C2
C
G1924
−58.869
124.540
107.238
1.00
91.84
C


ATOM
A67PJ
O2
C
G1924
−59.125
124.462
108.448
1.00
91.84
O


ATOM
A67PK
N3
C
G1924
−57.707
124.058
106.737
1.00
91.84
N


ATOM
A67PL
C4
C
G1924
−57.448
124.154
105.433
1.00
91.84
C


ATOM
A67PM
N4
C
G1924
−56.296
123.672
104.965
1.00
91.84
N


ATOM
A67PN
C5
C
G1924
−58.367
124.756
104.535
1.00
91.84
C


ATOM
A67PO
C2′
C
G1924
−60.888
127.099
107.427
1.00
78.08
C


ATOM
A67PP
O2′
C
G1924
−61.767
127.311
108.523
1.00
78.08
O


ATOM
A67PQ
C3′
C
G1924
−61.353
127.864
106.199
1.00
78.08
C


ATOM
A67PR
O3′
C
G1924
−61.706
129.211
106.452
1.00
78.08
O


ATOM
A67Q3
P
C
G1925
−60.840
130.402
105.806
1.00
70.20
P


ATOM
A67Q4
OP1
C
G1925
−61.675
131.628
105.858
1.00
70.20
O


ATOM
A67Q5
OP2
C
G1925
−60.350
129.928
104.487
1.00
70.20
O


ATOM
A67Q6
O5′
C
G1925
−59.625
130.532
106.820
1.00
70.20
O


ATOM
A67Q7
C5′
C
G1925
−59.860
130.745
108.201
1.00
70.20
C


ATOM
A67Q8
C4′
C
G1925
−58.697
130.285
109.039
1.00
70.20
C


ATOM
A67Q9
O4′
C
G1925
−58.458
128.869
108.835
1.00
70.20
O


ATOM
A67QA
C1′
C
G1925
−57.083
128.592
109.018
1.00
70.20
C


ATOM
A67QB
N1
C
G1925
−56.551
127.949
107.795
1.00
103.35
N


ATOM
A67QC
C6
C
G1925
−57.215
127.905
106.597
1.00
103.35
C


ATOM
A67QD
C2
C
G1925
−55.287
127.374
107.909
1.00
103.35
C


ATOM
A67QE
O2
C
G1925
−54.710
127.433
109.004
1.00
103.35
O


ATOM
A67QF
N3
C
G1925
−54.722
126.771
106.840
1.00
103.35
N


ATOM
A67QG
C4
C
G1925
−55.370
126.727
105.680
1.00
103.35
C


ATOM
A67QH
N4
C
G1925
−54.762
126.118
104.658
1.00
103.35
N


ATOM
A67QI
C5
C
G1925
−56.664
127.308
105.527
1.00
103.35
C


ATOM
A67QJ
C2′
C
G1925
−56.380
129.919
109.319
1.00
70.20
C


ATOM
A67QK
O2′
C
G1925
−56.285
130.074
110.728
1.00
70.20
O


ATOM
A67QL
C3′
C
G1925
−57.359
130.920
108.724
1.00
70.20
C


ATOM
A67QM
O3′
C
G1925
−57.234
132.227
109.249
1.00
70.20
O


ATOM
A67QY
P
U
G1926
−56.055
133.188
108.741
1.00
84.21
P


ATOM
A67QZ
OP1
U
G1926
−56.371
134.559
109.216
1.00
84.21
O


ATOM
A67R0
OP2
U
G1926
−55.896
132.957
107.284
1.00
84.21
O


ATOM
A67R1
O5′
U
G1926
−54.789
132.625
109.519
1.00
84.21
O


ATOM
A67R2
C5′
U
G1926
−53.486
133.078
109.208
1.00
84.21
C


ATOM
A67R3
C4′
U
G1926
−52.439
132.101
109.668
1.00
84.21
C


ATOM
A67R4
O4′
U
G1926
−52.855
130.747
109.347
1.00
84.21
O


ATOM
A67R5
C1′
U
G1926
−51.727
129.973
108.994
1.00
84.21
C


ATOM
A67R6
N1
U
G1926
−51.867
129.539
107.582
1.00
85.16
N


ATOM
A67R7
C6
U
G1926
−52.811
130.073
106.731
1.00
85.16
C


ATOM
A67R8
C2
U
G1926
−50.998
128.558
107.145
1.00
85.16
C


ATOM
A67R9
O2
U
G1926
−50.148
128.057
107.858
1.00
85.16
O


ATOM
A67RA
N3
U
G1926
−51.155
128.183
105.836
1.00
85.16
N


ATOM
A67RB
C4
U
G1926
−52.075
128.676
104.936
1.00
85.16
C


ATOM
A67RC
O4
U
G1926
−52.095
128.235
103.787
1.00
85.16
O


ATOM
A67RD
C5
U
G1926
−52.942
129.687
105.457
1.00
85.16
C


ATOM
A67RE
C2′
U
G1926
−50.491
130.841
109.208
1.00
84.21
C


ATOM
A67RF
O2′
U
G1926
−50.040
130.665
110.543
1.00
84.21
O


ATOM
A67RG
C3′
U
G1926
−51.075
132.231
109.013
1.00
84.21
C


ATOM
A67RH
O3′
U
G1926
−50.286
133.264
109.572
1.00
84.21
O


ATOM
A67RS
P
A
G1927
−50.481
134.787
109.094
1.00
73.22
P


ATOM
A67RT
OP1
A
G1927
−50.771
135.590
110.307
1.00
73.22
O


ATOM
A67RU
OP2
A
G1927
−51.473
134.782
107.992
1.00
73.22
O


ATOM
A67RV
O5′
A
G1927
−49.042
135.164
108.525
1.00
73.22
O


ATOM
A67RW
C5′
A
G1927
−48.663
134.805
107.204
1.00
73.22
C


ATOM
A67RX
C4′
A
G1927
−47.295
134.169
107.175
1.00
73.22
C


ATOM
A67RY
O4′
A
G1927
−46.596
134.449
108.412
1.00
73.22
O


ATOM
A67RZ
C1′
A
G1927
−45.786
133.354
108.774
1.00
73.22
C


ATOM
A67S0
N9
A
G1927
−46.187
132.903
110.122
1.00
68.40
N


ATOM
A67S1
C4
A
G1927
−45.471
132.108
110.986
1.00
68.40
C


ATOM
A67S2
N3
A
G1927
−44.268
131.549
110.784
1.00
68.40
N


ATOM
A67S3
C2
A
G1927
−43.894
130.831
111.843
1.00
68.40
C


ATOM
A67S4
N1
A
G1927
−44.538
130.624
112.998
1.00
68.40
N


ATOM
A67S5
C6
A
G1927
−45.746
131.198
113.172
1.00
68.40
C


ATOM
A67S6
N6
A
G1927
−46.395
130.997
114.321
1.00
68.40
N


ATOM
A67S7
C5
A
G1927
−46.250
131.982
112.122
1.00
68.40
C


ATOM
A67S8
N7
A
G1927
−47.431
132.691
111.990
1.00
68.40
N


ATOM
A67S9
C8
A
G1927
−47.340
133.222
110.796
1.00
68.40
C


ATOM
A67SA
C2′
A
G1927
−45.956
132.265
107.712
1.00
73.22
C


ATOM
A67SB
O2′
A
G1927
−44.881
132.343
106.783
1.00
73.22
O


ATOM
A67SC
C3′
A
G1927
−47.278
132.653
107.054
1.00
73.22
C


ATOM
A67SD
O3′
A
G1927
−47.383
132.223
105.707
1.00
73.22
O


ATOM
A67SP
P
A
G1928
−48.556
131.225
105.246
1.00
69.37
P


ATOM
A67SQ
OP1
A
G1928
−48.845
131.523
103.823
1.00
69.37
O


ATOM
A67SR
OP2
A
G1928
−49.655
131.341
106.232
1.00
69.37
O


ATOM
A67SS
O5′
A
G1928
−47.861
129.801
105.366
1.00
69.37
O


ATOM
A67ST
C5′
A
G1928
−46.650
129.529
104.680
1.00
69.37
C


ATOM
A67SU
C4′
A
G1928
−45.703
128.714
105.522
1.00
69.37
C


ATOM
A67SV
O4′
A
G1928
−45.408
129.411
106.761
1.00
69.37
O


ATOM
A67SW
C1′
A
G1928
−45.187
128.470
107.794
1.00
69.37
C


ATOM
A67SX
N9
A
G1928
−46.187
128.687
108.856
1.00
68.06
N


ATOM
A67SY
C4
A
G1928
−46.010
128.425
110.191
1.00
68.06
C


ATOM
A67SZ
N3
A
G1928
−44.905
127.947
110.783
1.00
68.06
N


ATOM
A67T0
C2
A
G1928
−45.095
127.824
112.093
1.00
68.06
C


ATOM
A67T1
N1
A
G1928
−46.176
128.106
112.830
1.00
68.06
N


ATOM
A67T2
C6
A
G1928
−47.271
128.586
112.205
1.00
68.06
C


ATOM
A67T3
N6
A
G1928
−48.351
128.868
112.937
1.00
68.06
N


ATOM
A67T4
C5
A
G1928
−47.198
128.760
110.813
1.00
68.06
C


ATOM
A67T5
N7
A
G1928
−48.117
129.220
109.886
1.00
68.06
N


ATOM
A67T6
C8
A
G1928
−47.475
129.154
108.744
1.00
68.06
C


ATOM
A67T7
C2′
A
G1928
−45.311
127.078
107.177
1.00
69.37
C


ATOM
A67T8
O2′
A
G1928
−44.026
126.647
106.746
1.00
69.37
O


ATOM
A67T9
C3′
A
G1928
−46.217
127.367
105.989
1.00
69.37
C


ATOM
A67TA
O3′
A
G1928
−46.179
126.376
104.980
1.00
69.37
O


ATOM
A67TM
P
G
G1929
−47.428
125.385
104.781
1.00
75.01
P


ATOM
A67TN
OP1
G
G1929
−47.145
124.563
103.582
1.00
75.01
O


ATOM
A67TO
OP2
G
G1929
−48.658
126.216
104.803
1.00
75.01
O


ATOM
A67TP
O5′
G
G1929
−47.362
124.480
106.086
1.00
75.01
O


ATOM
A67TQ
C5′
G
G1929
−46.142
123.864
106.476
1.00
75.01
C


ATOM
A67TR
C4′
G
G1929
−46.251
123.191
107.819
1.00
75.01
C


ATOM
A67TS
O4′
G
G1929
−46.728
124.140
108.815
1.00
75.01
O


ATOM
A67TT
C1′
G
G1929
−47.763
123.532
109.554
1.00
75.01
C


ATOM
A67TU
N9
G
G1929
−48.629
124.565
110.132
1.00
75.35
N


ATOM
A67TV
C4
G
G1929
−49.870
125.032
109.755
1.00
75.35
C


ATOM
A67TW
N3
G
G1929
−50.593
124.631
108.694
1.00
75.35
N


ATOM
A67TX
C2
G
G1929
−51.740
125.273
108.602
1.00
75.35
C


ATOM
A67TY
N2
G
G1929
−52.566
124.979
107.589
1.00
75.35
N


ATOM
A67TZ
N1
G
G1929
−52.155
126.236
109.487
1.00
75.35
N


ATOM
A67U0
C6
G
G1929
−51.435
126.668
110.592
1.00
75.35
C


ATOM
A67U1
O6
G
G1929
−51.895
127.543
111.335
1.00
75.35
O


ATOM
A67U2
C5
G
G1929
−50.200
125.986
110.698
1.00
75.35
C


ATOM
A67U3
N7
G
G1929
−49.201
126.120
111.646
1.00
75.35
N


ATOM
A67U4
C8
G
G1929
−48.302
125.260
111.270
1.00
75.35
C


ATOM
A67U5
C2′
G
G1929
−48.435
122.587
108.567
1.00
75.01
C


ATOM
A67U6
O2′
G
G1929
−49.248
121.637
109.222
1.00
75.01
O


ATOM
A67U7
C3′
G
G1929
−47.216
121.999
107.875
1.00
75.01
C


ATOM
A67U8
O3′
G
G1929
−46.659
120.982
108.697
1.00
75.01
O


ATOM
A67UK
P
G
G1930
−45.500
120.025
108.142
1.00
79.14
P


ATOM
A67UL
OP1
G
G1930
−44.708
120.808
107.160
1.00
79.14
O


ATOM
A67UM
OP2
G
G1930
−46.149
118.771
107.692
1.00
79.14
O


ATOM
A67UN
O5′
G
G1930
−44.635
119.749
109.447
1.00
79.14
O


ATOM
A67UO
C5′
G
G1930
−43.395
120.411
109.675
1.00
79.14
C


ATOM
A67UP
C4′
G
G1930
−42.381
119.481
110.290
1.00
79.14
C


ATOM
A67UQ
O4′
G
G1930
−41.837
120.090
111.498
1.00
79.14
O


ATOM
A67UR
C1′
G
G1930
−41.958
119.176
112.567
1.00
79.14
C


ATOM
A67US
N9
G
G1930
−42.096
119.918
113.821
1.00
65.34
N


ATOM
A67UT
C4
G
G1930
−41.031
120.378
114.542
1.00
65.34
C


ATOM
A67UU
N3
G
G1930
−39.747
120.223
114.178
1.00
65.34
N


ATOM
A67UV
C2
G
G1930
−38.929
120.768
115.052
1.00
65.34
C


ATOM
A67UW
N2
G
G1930
−37.614
120.699
114.824
1.00
65.34
N


ATOM
A67UX
N1
G
G1930
−39.340
121.413
116.195
1.00
65.34
N


ATOM
A67UY
C6
G
G1930
−40.667
121.583
116.586
1.00
65.34
C


ATOM
A67UZ
O6
G
G1930
−40.925
122.183
117.636
1.00
65.34
O


ATOM
A67V0
C5
G
G1930
−41.560
120.998
115.650
1.00
65.34
C


ATOM
A67V1
N7
G
G1930
−42.947
120.920
115.627
1.00
65.34
N


ATOM
A67V2
C8
G
G1930
−43.221
120.268
114.526
1.00
65.34
C


ATOM
A67V3
C2′
G
G1930
−43.149
118.299
112.214
1.00
79.14
C


ATOM
A67V4
O2′
G
G1930
−43.164
117.103
112.962
1.00
79.14
O


ATOM
A67V5
C3′
G
G1930
−42.926
118.115
110.720
1.00
79.14
C


ATOM
A67V6
O3′
G
G1930
−41.934
117.114
110.504
1.00
79.14
O


ATOM
A67VI
P
U
G1931
−42.362
115.620
110.091
1.00
95.44
P


ATOM
A67VJ
OP1
U
G1931
−43.842
115.557
110.146
1.00
95.44
O


ATOM
A67VK
OP2
U
G1931
−41.580
114.694
110.945
1.00
95.44
O


ATOM
A67VL
O5′
U
G1931
−41.876
115.499
108.576
1.00
95.44
O


ATOM
A67VM
C5′
U
G1931
−41.531
116.644
107.804
1.00
95.44
C


ATOM
A67VN
C4′
U
G1931
−40.245
116.425
107.054
1.00
95.44
C


ATOM
A67VO
O4′
U
G1931
−39.402
117.603
107.160
1.00
95.44
O


ATOM
A67VP
C1′
U
G1931
−38.047
117.223
107.272
1.00
95.44
C


ATOM
A67VQ
N1
U
G1931
−37.539
117.663
108.595
1.00
85.53
N


ATOM
A67VR
C6
U
G1931
−38.387
118.032
109.619
1.00
85.53
C


ATOM
A67VS
C2
U
G1931
−36.169
117.694
108.770
1.00
85.53
C


ATOM
A67VT
O2
U
G1931
−35.383
117.379
107.894
1.00
85.53
O


ATOM
A67VU
N3
U
G1931
−35.749
118.108
110.008
1.00
85.53
N


ATOM
A67VV
C4
U
G1931
−36.544
118.487
111.069
1.00
85.53
C


ATOM
A67VW
O4
U
G1931
−36.025
118.836
112.128
1.00
85.53
O


ATOM
A67VX
C5
U
G1931
−37.950
118.431
110.818
1.00
85.53
C


ATOM
A67VY
C2′
U
G1931
−37.979
115.705
107.111
1.00
95.44
C


ATOM
A67VZ
O2′
U
G1931
−37.782
115.399
105.738
1.00
95.44
O


ATOM
A67W0
C3′
U
G1931
−39.369
115.291
107.568
1.00
95.44
C


ATOM
A67W1
O3′
U
G1931
−39.777
114.024
107.084
1.00
95.44
O


TER


ATOM
A88BI
C1
NMY
N2905
−52.949
118.562
103.968
0.77
92.97
C


ATOM
A88BJ
O1
NMY
N2905
−54.161
118.135
104.561
0.77
92.97
O


ATOM
A88BK
C2
NMY
N2905
−52.426
119.752
104.791
0.77
92.97
C


ATOM
A88BL
N2
NMY
N2905
−52.473
119.418
106.186
0.77
92.97
N


ATOM
A88BM
C3
NMY
N2905
−53.198
120.986
104.611
0.77
92.97
C


ATOM
A88BN
O3
NMY
N2905
−52.453
121.996
105.253
0.77
92.97
O


ATOM
A88BO
C4
NMY
N2905
−53.381
121.347
103.242
0.77
92.97
C


ATOM
A88BP
O4
NMY
N2905
−54.435
122.280
103.139
0.77
92.97
O


ATOM
A88BQ
C5
NMY
N2905
−53.764
120.175
102.380
0.77
92.97
C


ATOM
A88BR
O5
NMY
N2905
−53.071
118.856
102.616
0.77
92.97
O


ATOM
A88BS
C6
NMY
N2905
−54.564
120.406
101.114
0.77
92.97
C


ATOM
A88BT
N6
NMY
N2905
−55.382
121.622
101.028
0.77
92.97
N


ATOM
A88BU
C7
NMY
N2905
−55.891
114.385
103.460
0.77
92.97
C


ATOM
A88BV
N7
NMY
N2905
−55.877
113.133
102.690
0.77
92.97
N


ATOM
A88BW
C8
NMY
N2905
−56.357
115.659
102.788
0.77
92.97
C


ATOM
A88BX
C9
NMY
N2905
−55.969
116.906
103.599
0.77
92.97
C


ATOM
A88BY
N9
NMY
N2905
−56.182
118.116
102.864
0.77
92.97
N


ATOM
A88BZ
C10
NMY
N2905
−54.516
116.858
104.054
0.77
92.97
C


ATOM
A88C0
C11
NMY
N2905
−54.255
115.752
105.031
0.77
92.97
C


ATOM
A88C1
O11
NMY
N2905
−52.910
115.367
104.953
0.77
92.97
O


ATOM
A88C2
C12
NMY
N2905
−55.097
114.486
104.767
0.77
92.97
C


ATOM
A88C3
O12
NMY
N2905
−55.308
113.574
105.759
0.77
92.97
O


ATOM
A88C4
C13
NMY
N2905
−52.251
115.505
106.199
0.77
92.97
C


ATOM
A88C5
C14
NMY
N2905
−51.065
114.624
106.245
0.77
92.97
C


ATOM
A88C6
O14
NMY
N2905
−50.999
114.167
107.537
0.77
92.97
O


ATOM
A88C7
C15
NMY
N2905
−49.996
115.502
105.921
0.77
92.97
C


ATOM
A88C8
C16
NMY
N2905
−50.398
116.771
106.577
0.77
92.97
C


ATOM
A88C9
O16
NMY
N2905
−51.782
116.839
106.466
0.77
92.97
O


ATOM
A88CA
C17
NMY
N2905
−49.774
118.012
105.983
0.77
92.97
C


ATOM
A88CB
O17
NMY
N2905
−50.028
119.199
106.600
0.77
92.97
O


ATOM
A88CC
C18
NMY
N2905
−48.048
114.253
105.483
0.77
92.97
C


ATOM
A88CD
O18
NMY
N2905
−48.807
114.958
106.462
0.77
92.97
O


ATOM
A88CE
C19
NMY
N2905
−48.682
113.160
104.640
0.77
92.97
C


ATOM
A88CF
N19
NMY
N2905
−45.843
113.148
107.725
0.77
92.97
N


ATOM
A88CG
C20
NMY
N2905
−47.801
112.336
103.890
0.77
92.97
C


ATOM
A88CH
O20
NMY
N2905
−48.193
112.474
102.516
0.77
92.97
O


ATOM
A88CI
C21
NMY
N2905
−46.371
112.703
103.976
0.77
92.97
C


ATOM
A88CJ
O21
NMY
N2905
−45.464
112.248
102.993
0.77
92.97
O


ATOM
A88CK
C22
NMY
N2905
−45.802
113.378
105.214
0.77
92.97
C


ATOM
A88CL
O22
NMY
N2905
−46.568
114.487
105.541
0.77
92.97
O


ATOM
A88CM
C23
NMY
N2905
−45.672
112.489
106.449
0.77
92.97
C


ATOM
A88CN
N23
NMY
N2905
−49.383
112.238
105.534
0.77
92.97
N


TER


END

## Claims

1. A method to identify a compound that interferes with ribosomal function which comprises
(a) surface-immobilizing a ribosome having a FRET pair sensitive to transitioning between low FRET and high FRET states under translation competent conditions, wherein said FRET pair comprises a first fluorophore attached to a ribosomal protein of said ribosome and a second fluorophore attached a ribosomal protein of said ribosome;
(b) adding a test compound to said ribosome; and
(c) monitoring or detecting changes in FRET states using smFRET imaging techniques to identify a test compound capable of
(i) stabilizing said ribosome in an intermediate FRET state,
(ii) changing said ribosome's distribution into or out of an intermediate FRET state, or
(iii) changing said ribosome's rate of transition into or out of an intermediate FRET state.

2. The method of claim 1, wherein said first fluorophore is attached to ribosomal protein L1 and said second fluorophore is attached to ribosomal protein S13.

3. The method of claim 2, wherein the fluorophore attached to L1 is at (T202C) L1 and the fluorophore attached to S13 is at or near the amino terminus of S13.

4. The method of claim 1, wherein said compound is identified as a candidate antibiotic when said test compound
(i) stabilizes said ribosome in an intermediate FRET state or in a high FRET state,
(ii) increases said ribosome's distribution in intermediate or high FRET states,
(iii) increases said ribosome's rate of transition into intermediate or high FRET states, or
(iv) abolishes FRET.

5. The method of claim 1, wherein said intermediate FRET state comprises the P/pe tRNA binding state.

6. The method of claim 1, wherein said FRET pair consists of a donor-acceptor fluorophore pair or a donor-quencher fluorophore pair.

7. The method of claim 1, wherein said first fluorophore is attached to a ribosomal protein in a large ribosomal subunit and said second fluorophore is attached to a ribosomal protein in a small ribosomal subunit.