@text 
EXPLORING MOLECULAR STRUCTURE
EXERCISE 10
TRANSLATION
 
Kinemage 1     Yeast tRNA-Asp
Kinemage 2     E. coli glutaminyl-tRNA synthetase-tRNA complex
_________________________
 
In the first kinemage, the tertiary structure of a tRNA molecule is presented, including nonstandard base-pairing. The second kinemage explores the determinants for aminoacyl-tRNA synthetase binding. Also discussed are the problems of recognizing isoacceptor tRNA molecules and the conformational changes that must occur when aminoacyl-tRNA synthetase binds tRNA.
 
 
KINEMAGE 1 
Yeast tRNA-Asp
 
K1 View 1
 
In this kinemage, the tRNA molecule is displayed as a pseudobackbone: C-4' is connected directly to the 3'-phosphate group. The point of attachment of bases is indicated by a line from C-1' to C-4'. Examine the backbone of the L-shaped tRNA molecule. Trace the chain from the 5' end (residue 1) to the 3' end (residue 74). Residues 75 (cytidylate) and 76 (adenylate) at the 3' terminus have been omitted from this structure. (Adenylate 76 is the residue to which the amino acid becomes attached.)
 
Using a tRNA cloverleaf diagram as a guide, locate the acceptor stem, D arm, anticodon arm, variable arm, and T(psi)C arm. The bases in each of these groups can be turned on by clicking on the appropriate buttons under {bases}.
 
Before any crystal structures of tRNA had been determined, researchers treated tRNA molecules with nucleases to obtain structural information. Sites in the tRNA that were most susceptible to nuclease digestion were assumed to be the most exposed. Which regions do you predict would be most susceptible to nucleases?
 
Turn on the base pairs in each group (the first five buttons under {bases}). Look at the helices in the D arm (green) and acceptor stem (dark blue). Question: Are these similar to A-DNA or B-DNA? Rotate the molecule to look down the axis of each helix or switch to View2.
 
Answer: The arrangement of nucleotide bases within the helix indicates that tRNA adopts a conformation similar to that of A-DNA. (The structure of A-DNA is examined in Exercise 7).
 
K1 View 2
 
Select View2 from the VIEWS pull-down menu. The view down the acceptor-stem helix is striking; bases from three different groups (acceptor stem, variable arm, and T(psi)C arm) form the helix axis. Note how most of the bases in the tRNA are stacked, including the anticodon loop (residues 34-36), which is technically not part of a stem structure. Can you identify stacking interactions that occur between bases that are not adjacent in the primary structure? Rotate the image and look for bases of different colors parallel to each other and less than 5 angstroms apart. Some examples are residues 7 and 49 and residues 15 and 59. It may be useful to look at a cloverleaf diagram of a tRNA molecule for a better idea of the what these interactions involve. Question: What do the interactions accomplish?
 
Answer: Stacking interactions are energetically favorable, and interactions between non-adjacent base pairs help maintain the compact tertiary structure of tRNA.
 
Return to View1. The D arm (green) is a striking example of the versatility of ribonucleic acid structure. As it starts from the acceptor stem, the D arm dips down towards the anticodon loop, heads back towards the outside of the L, where it interacts with the T(psi)C arm (red), then comes back towards the first part of the D arm and continues into the anticodon stem. 
 
K1 View 3
 
Switch to View3 and turn off all bases except those in the D arm and the variable arm. This image shows a four-stranded helix in which the D arm provides three of the strands! The fourth strand is provided by the variable arm whose bases (orange) seem to intercalate between the D-arm bases. Rotate the image slightly around the x axis to see that the bases are parallel and are found in discrete planes to allow for hydrogen bonding. How many bases are in each planar group? Turn on the {H bonds} button and rotate the image to see some of the hydrogen bonds. The polynucleotide backbone must be flexible to accommodate these interactions.
 
Return to View3 and identify two nonstandard bases in the D arm: dihydroxyuracil at positions 16 and 19 (lower right corner). Adjust the view by clicking on {pickcenter}, selecting one of the residues, and increasing ZOOM and ZSLAB. (Remember to turn {pickcenter} off.) Rotate the image to examine the dihydroxyuracil (h2u) ring structure. How does it differ from the structure of other pyrimidines? 
 
Return to View1 and locate residues 16 and 19. Question: In structural terms, what is the effect of these two residues on the helix? In biological terms, why might these residues be here?
 
Answer: The rings are nonaromatic and thus cannot stack. They cause disruption of the helix and mark the approximate beginning and end of a stem structure. Biologically, the dihydroxyuracil rings are exposed and may help to distinguish the tRNA from other RNA molecules with other functions and shorter half-lives.
 
There are several nonstandard base pairs in the helices of this tRNA as well as in most tRNA molecules. Turn on the first five groups of bases and find a nonstandard base pair. Some examples are U5/G68 and G30/U40. Compare the geometry of the nonstandard pair and a Watson-Crick base pair. Question: What are possible functions for the mispaired bases?
 
Answer: The nonstandard base pairs may form a slight bulge, producing a bend in the RNA helix. Nonstandard base pairs may also be sites for recognition by tRNA-binding proteins.
 
In addition to nuclease digestion, another technique used to probe the tertiary structure of tRNA is to treat the tRNA with a cross-linking agent to bridge nucleotide bases found in close contact. Question: If only the secondary (cloverleaf) structure were known, how would cross-linking information help elucidate the tertiary structure of the tRNA shown in this exercise?
 
Answer: Cross-linking experiments would demonstrate interactions between the T(psi)C arm and the D arm, which are not evident from the cloverleaf structure.
 
Some tRNA molecules can recognize codons that differ in the 3' position due to so-called wobble in the 5' position of the anticodon. It is postulated that this position is more flexible and therefore less discriminating than the other two anticodon positions. Question: Do you see any structural evidence for this? (The anticodon is residues 34-36.)
 
Answer: Whereas residues 35 and 36 are close to the anticodon stem, residue 34 (the wobble position) protrudes farther and is less stabilized by stacking interactions with bases in the anticodon stem.
 
The variable arm (orange) contains only 4 nucleotides in this structure but may be as long as 21 nucleotides in other tRNA molecules. Question: What type of structure would a longer arm adopt and where would it fit relative to the tRNA L structure?
 
Answer: All tRNA structures are very compact, so a longer variable arm would probably be accommodated in a manner similar to the four-nucleotide variable arm shown here. The arm would most likely remain on the inside of the L. As we will see later, this arm is often implicated in aminoacyl-tRNA synthetase binding.
 
Aminoacyl-tRNA synthetases are ATP-dependent enzymes that catalyze the binding of an amino acid to the 2'- or 3'-hydroxyl group of the ribose at the 3' end of tRNA molecules. In experiments to identify the nucleotide residues in tRNA-Asp that are important for recognition by aspartyl-tRNA synthetase, individual residues were changed, and the resulting tRNA was tested for its ability to be aminoacylated. 
 
The residues found to be very important for aminoacylation can be highlighted by turning off the first five buttons under {bases} and turning on the {aa res} button. Question: What are these residues? In what part of the tRNA molecule are they found? 
 
Answer: The residues in tRNA-Asp that are important for aminoacylation are G73 in the acceptor stem, G10 and U25 at the end of the D arm, and G34, U35, and C36 of the anticodon. 
 
How might mutation of these residues block aminoacylation? 
 
Interestingly, the anticodon bases and residue 73 were found to adopt several different conformations in the crystal structure, which suggests that they are flexible and may undergo conformational changes--a type of induced fit--when tRNA binds to the synthetase.
 
Turn on View2 for another view of these residues.
 
The structure of the aspartyl-tRNA synthetase-tRNA complex has been solved. It was found that the synthetase binds on the inside of the tRNA L (on the left side of the molecule as shown in View2), interacting with the T(psi)C arm, the D arm, the variable arm, and the major groove of the anticodon helix. Question: Based on what you know about the structure of the major groove in A-DNA (double-stranded RNA has a similar conformation), does it seem likely that the synthetase recognizes specific bases? 
 
Answer: Because the major groove in A-DNA and double-stranded RNA is very narrow and deep, contacts between the protein and bases are difficult to make. Either the synthetase-tRNA contacts are not base specific and involve only the phosphate groups, or the conformational change in the tRNA induced by binding makes the bases more accessible.
 
In aminoacylation experiments with tRNA molecules containing altered bases, the binding of the tRNA substrate to the synthetase and the rate of catalysis were assessed. It was found that changes in residue 73 significantly affected synthetase binding and catalysis. Alteration of the catalytic rate makes sense because residue 73 is so near the site of amino acid attachment. Changes in the 10/25 base pair mostly affected the binding of the tRNA to the synthetase with little effect on catalysis. When the anticodon residues were changed, both synthetase binding and catalysis were significantly altered. The binding effects are compatible with other evidence that the anticodon is important for synthetase binding. Question: How can the effect on catalytic rate be explained, given that the aminoacylation site and the anticodon are about 80 angstroms apart?
 
Answer: The anticodon might affect synthetase catalytic activity via a conformational change in the protein induced by binding the anticodon. Alternatively, a conformational change in the tRNA induced by binding to the synthetase might place the acceptor end of the tRNA in a more favorable position for catalysis. 
 
In this example, the six nucleotides that are important for synthetase recognition determine which amino acid is attached to the tRNA. It was found that a yeast tRNA-Phe molecule could be aminoacylated with aspartic acid if the six residues were changed to those found in tRNA-Asp. It is also interesting that the anticodon is so important for recognition by some aminoacyl-tRNA synthetases, considering that one synthetase may recognize several isoacceptor tRNA molecules (tRNA molecules with different anticodons that bind a single amino acid).
 
To further explore the binding of aminoacyl-tRNA synthetase to tRNA, select Next from the KINEMAGE pull-down menu.
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KINEMAGE 2
E. coli glutaminyl-tRNA synthetase-tRNA complex
 
K2 View 1
 
In this image of a synthetase-tRNA complex, the tRNA structure (controlled by {tRNA}) has been simplified to a blue line joining the phosphate groups, and the protein (controlled by {protein}) is represented by a pink alpha-carbon trace. The amino acid (glutamine) is not shown. Note that the glutaminyl-tRNA synthetase spans the length of the tRNA molecule, interacting with the acceptor end, the inside of the L, and the anticodon loop. The acceptor stem is bound in a pocket of the synthetase. Question: Do you notice any structural differences between this tRNA and the yeast tRNA shown in the last kinemage?
 
Answer: In this kinemage, the acceptor stem is a hairpin structure, not straight as in tRNA-Asp. In addition, the first loop of the D arm doesnŐt dip towards the anticodon stem as much as in tRNA-Asp. But in general, the structures are very similar.
 
One way to probe DNA-protein or RNA-protein contacts is to treat the complex with chemical agents that cleave the phosphodiester backbone. These agents cleave only in areas that are not protected by bound protein. This technique is called footprinting. If this technique were used on the synthetase-tRNA complex shown here, what areas would be protected? Question: How might footprinting of tRNA-protein complexes be more complicated than DNA-protein footprinting?
 
Answer: The extensive secondary structure of the tRNA would complicate the tRNA-protein footprint, since some areas might be resistant to cleavage due to steric constraints rather than to actual protein contacts.
 
The areas of most extensive synthetase-tRNA interaction involve the anticodon arm and the acceptor stem. It is believed that two beta-barrel domains in the protein are responsible for recognizing the anticodon, and that the anticodon bases are presented to the protein, rather than stacked as in free tRNA. Unfortunately, much of the beta-barrel structure cannot be shown, due to its degree of disorder in the crystal from which this image was derived. 
 
K2 View 2
 
Switch to View2, which is analogous to View2 of the last kinemage. (In this case, the synthetase interacts with the right side of the tRNA as shown in this view, rather than the left as in the tRNA shown in Kinemage 1, View2.) Turn off {protein} and identify tRNA residues 10 and 25. Mark these residues by turning on {markers} (the last two points selected will be marked) and then turn {protein} back on. Rotate the image to the right. Question: Are residues 10 and 25, which were crucial for recognition by aspartyl-tRNA synthetase, in an area of tRNA-Gln that binds to the synthetase? 
 
Answer: Neither tRNA residue interacts closely with the synthetase.
 
Question: Does the glutaminyl-tRNA synthetase contact the anticodon stem in the major or minor groove? Does this differ from the recognition of tRNA-Asp by aspartyl-tRNA synthetase? 
 
Answer: The glutaminyl-tRNA synthetase contacts the minor groove, whereas the aspartyl-tRNA synthetase contacts the major groove. As in tRNA-Asp, the anticodon stem/loop in tRNA-Gln has been found to change conformation upon synthetase binding.
 
As you can see, different synthetases interact differently with their cognate tRNA molecules. There are two classes of synthetases, grouped according to structure and mechanism. Glutaminyl-tRNA synthetase is a class I synthetase, whereas aspartyl-tRNA synthetase is in class II. The amino acid specificity of each class of enzymes is constant in all organisms, so it seems that this aspect of protein synthesis is evolutionarily conserved.
 
Switch to View1. As mentioned earlier, one synthetase may recognize several different isoacceptor tRNA molecules. For example, methionyl-tRNA synthetase must recognize the elongator tRNA-Met as well as the initiator tRNA-Met (in eubacteria, the initiator methionine is formylated). The structure of tRNA-Gln shown here can be used as a model for the structures of the tRNA-Met molecules.
 
Turn off {markers} and {protein} and turn on the {Met diff} button to see how the two tRNA-Met molecules differ from each other. The differences are highlighted in orange. (If you have a black-and-white monitor, you can identify the differences by toggling {backbone} on and off.) In what parts of the tRNA molecule are the differences found? Why must the methionyl-tRNA synthetase ignore these areas during recognition of either tRNA? 
 
Question: Based on the contacts you have seen between tRNA-Gln and its synthetase, do you think that the methionyl-tRNA synthetase recognizes the initiator and elongator tRNA-Met molecules in the same fashion? You may want to turn {protein} on to answer this question.
 
Answer: Most of the differences between the two tRNA-Met molecules are in areas that are not bound by the synthetase, so it is reasonable to assume that recognition of either tRNA-Met molecule by methionyl-tRNA synthetase is similar to recognition of tRNA-Gln by its synthetase. In fact, both glutaminyl-tRNA synthetase and methionyl-tRNA synthetase are class I enzymes.
 
Question: Based on what you know about tRNA structure and the differences between the two tRNA-Met molecules, how might elongator tRNA molecules be recognized by the translational elongation factor EF-Tu?
 
Answer: EF-Tu must recognize all tRNA molecules except the initiator tRNA; therefore, it must recognize parts of tRNA structures that are common to all the elongator tRNA molecules and discriminate against the initiator tRNA. The T(psi)C arm, which is found in all tRNA molecules and contains several invariant residues, is a possible EF-Tu-binding site. The anticodon stem is a good candidate for a structure that could be used for discrimination between the elongator tRNAs and the initiator tRNA. A reasonable scenario for EF-Tu binding might involve both the T(psi)C arm and the anticodon arm. 
 
 
K2 View 3
 
Turn off {Met diff} and switch to View3 for a close-up view of the anticodon recognition region of glutaminyl-tRNA synthetase. The protein-tRNA contacts in the anticodon arm can be visualized by turning on the {anti recog} button. (If you have a black-and-white monitor, toggle {C alphas} on and off to see the marked residues in the protein, and toggle {backbone} on and off to see the marked residues in the tRNA.) Question: How far apart are the highlighted nucleotides (red) and amino acid residues (yellow)?
 
Answer: The distances separating the nucleotides and the amino acids are all greater than 6 angstroms. From this, we can infer that recognition probably involves movement of the tRNA anticodon arm or the protein or both. 
 
The end of the acceptor stem of the tRNA is bound in the protein active site, where ATP and glutamine also bind in order to charge the tRNA. Switch back to View1, turn off {anti recog}, and turn on the {HIGH} and {MSK} buttons. Which residues are highlighted? The residues can be identified easily when the {C alphas} button is turned off. The two sets of residues are highly conserved in the class I synthetases. They bind the phosphate groups of ATP (not shown) and are thought to be involved in catalyzing transfer of the amino acid to the end of the acceptor stem. 
 
K2 View 4
 
Turn on View4 to see a close-up view of the active site. Based on kinetic data, the anticodon-binding site and the active site of glutaminyl-tRNA synthetase are thought to communicate, as they do in yeast aspartyl-tRNA synthetase. Thus, the conformation of the active site depends on the conformation of the anticodon-binding site. Switch back to View1, turn on {anti recog}, and try to find a region of the protein that might mediate this communication.
 
One candidate region includes residues 517-520, which are in a loop in a beta sheet. The lower end of the loop is near the anticodon, and the upper end of the loop is close to the active-site domain.
 
Cross-linking and footprinting assays have helped identify the regions of tRNA that associate with ribosomal RNA during protein synthesis. In E. coli, the 16S rRNA of the 30S (small) subunit specifically binds the anticodon stem and loop, and in some cases, part of the T(psi)C arm. The 23S rRNA of the 50S (large) subunit specifically binds the 3' acceptor end (5'-CCA-3'). Turn off the {anti recog}, {HIGH}, and {MSK} buttons and turn on the {ribo recog} button under {tRNA} to see where the ribosome recognizes the tRNA. (If you have a black-and-white monitor, toggle {backbone} on and off.) How might these residues be involved in ribosome binding? This finding further establishes the importance of the RNA in the ribosome: rRNA recognizes tRNA during protein synthesis. Question: How might recognition of tRNA by rRNA differ from recognition of tRNA by protein?
 
Answer: Recognition of tRNA by rRNA presumably involves base-pair interactions. RNA, unlike proteins, can make highly complementary Watson-Crick base pairs (and possibly other types of base pairs) with other RNA molecules. Because RNA does not have positive charges as protein side chains do, electrostatic interactions with phosphate groups of the backbone are not likely to occur. Whereas nucleic-acid binding proteins may recognize either the phosphate backbone or specific sequences or both, rRNA must depend on the sequence of its tRNA substrate. However, due to the large number of base-pairing combinations possible between rRNA and tRNA, the sequence requirements need not be stringent.
_________________________
 
The kinemages in this exercise were designed by Mary A. Canady. Images of yeast tRNA-Asp are based on coordinates provided by E. Westhof, P. Dumas, and D. Moras (Brookhaven file 2TRA); images of glutaminyl-tRNA synthetase are based on coordinates provided by M. A. Rould, J. J. Perona, D. Soell, and T. A. Steitz (Brookhaven file 1GSG).
 
References
 
Ruff, M., Krishnaswamy, S., Boeglin, M., Poterszman, A., Mitschler, A., Podjarny, A., Rees, B., Thierry, J. C., and Moras, D. (1991). Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA-Asp. Science 252:1682-1689.
 
Putz, J., Puglisi, J. D., Florentz, C., and Giege, R. (1991). Identity elements for specific aminoacylation of yeast tRNA-Asp by cognate aspartyl-tRNA synthetase. Science 252:1696-1699.
 
Rould, M. A., Perona, J. J., and Steitz, T. A. (1991). Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature 352:213-218.
_________________________
 
@kinemage 1 
@caption 
Yeast tRNA-Asp. The pseudobackbone is shown in white. Specific regions of the molecule are color coded: amino acid acceptor stem (residues 1-7, 65-74), dark blue; D arm (residues 8-25), green; anticodon arm (residues 26-44), light blue; variable arm (residues 45-49), orange; and T(psi)C arm (residues 50-64), red.
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{c4* G 53}P 8.247 7.121 26.656 {c1* G 53}10.104 7.553 25.25
{c4* G 53}P 8.247 7.121 26.656 {p 5mu 54}7.189 10.584 27.762
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@group {bases} 
@vectorlist off {acceptor} color= blue
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{n4 C 63}14.932 5.731 19.091
{c4 C 63}P 15.375 5.447 20.317 {c5 C 63}16.488 6.156 20.84
{c6 C 63}16.888 5.819 22.081
{n1 C 63}P 16.273 4.833 22.799 {c6 C 63}16.888 5.819 22.081
@vectorlist off {aa res} color= hotpink
{c1* C 36}P 0.283 9.322 -32.89 {n1 C 36}0.105 10.773 -33.144
{c2 C 36}1.23 11.468 -33.533
{o2 C 36}2.3 10.881 -33.653
{c2 C 36}P 1.23 11.468 -33.533 {n3 C 36}1.101 12.805 -33.757
{c4 C 36}-0.098 13.446 -33.623
{n4 C 36}-0.166 14.755 -33.847
{c4 C 36}P -0.098 13.446 -33.623 {c5 C 36}-1.242 12.71 -33.204
{n1 C 36}P 0.105 10.773 -33.144 {c6 C 36}-1.095 11.401 -32.98
{c5 C 36}-1.242 12.71 -33.204
{c1* G 34}P -8.001 15.809 -38.227 {n9 G 34}-6.605 16.207 -38.496
{c8 G 34}-6.027 17.442 -38.392
{n7 G 34}-4.754 17.449 -38.676
{c5 G 34}-4.471 16.126 -39.005
{c6 G 34}-3.278 15.478 -39.408
{o6 G 34}-2.171 16.004 -39.573
{c6 G 34}P -3.278 15.478 -39.408 {n1 G 34}-3.401 14.128 -39.632
{c2 G 34}-4.588 13.473 -39.483
{n2 G 34}-4.582 12.163 -39.737
{c2 G 34}P -4.588 13.473 -39.483 {n3 G 34}-5.744 14.026 -39.109
{c4 G 34}-5.609 15.349 -38.885
{n9 G 34}P -6.605 16.207 -38.496 {c4 G 34}-5.609 15.349 -38.885
{c5 G 34}-4.471 16.126 -39.005
{c1* U 35}P -4.49 10.314 -35.446 {n1 U 35}-3.573 11.387 -35.88
{c2 U 35}-2.3 10.982 -36.254
{o2 U 35}-1.986 9.794 -36.239
{c2 U 35}P -2.3 10.982 -36.254 {n3 U 35}-1.408 11.941 -36.657
{c4 U 35}-1.747 13.264 -36.687
{o4 U 35}-0.855 14.074 -37.061
{c4 U 35}P -1.747 13.264 -36.687 {c5 U 35}-3.056 13.662 -36.284
{c6 U 35}-3.911 12.703 -35.895
{n1 U 35}-3.573 11.387 -35.88
{c1* G 73}P 42.029 -3.415 21.588 {n9 G 73}40.627 -3.692 21.244
{c8 G 73}39.92 -3.503 20.093
{n7 G 73}38.659 -3.841 20.183
{c5 G 73}38.511 -4.28 21.498
{c6 G 73}37.392 -4.766 22.216
{o6 G 73}36.236 -4.927 21.812
{c6 G 73}P 37.392 -4.766 22.216 {n1 G 73}37.644 -5.103 23.516
{c2 G 73}38.88 -4.975 24.084
{n2 G 73}38.966 -5.346 25.37
{c2 G 73}P 38.88 -4.975 24.084 {n3 G 73}39.963 -4.523 23.457
{c4 G 73}39.71 -4.192 22.171
{n9 G 73}P 40.627 -3.692 21.244 {c4 G 73}39.71 -4.192 22.171
{c5 G 73}38.511 -4.28 21.498
{c1* U 25}P 11.039 9.254 -12.618 {n1 U 25}9.877 9.632 -11.766
{c2 U 25}9.33 8.633 -10.988
{o2 U 25}9.803 7.499 -11.003
{c2 U 25}P 9.33 8.633 -10.988 {n3 U 25}8.259 8.95 -10.211
{c4 U 25}7.712 10.193 -10.166
{o4 U 25}6.728 10.354 -9.404
{c4 U 25}P 7.712 10.193 -10.166 {c5 U 25}8.29 11.212 -10.988
{n1 U 25}P 9.877 9.632 -11.766 {c6 U 25}9.348 10.888 -11.751
{c5 U 25}8.29 11.212 -10.988
{c1* G 10}P 8.241 1.384 -6.279 {n9 G 10}7.786 2.74 -6.578
{c8 G 10}6.74 3.449 -6.055
{n7 G 10}6.599 4.664 -6.548
{c5 G 10}7.638 4.745 -7.475
{c6 G 10}8.032 5.805 -8.327
{o6 G 10}7.509 6.905 -8.447
{c6 G 10}P 8.032 5.805 -8.327 {n1 G 10}9.108 5.515 -9.104
{c2 G 10}9.754 4.327 -9.075
{n2 G 10}10.787 4.232 -9.912
{c2 G 10}P 9.754 4.327 -9.075 {n3 G 10}9.428 3.307 -8.282
{c4 G 10}8.364 3.578 -7.505
{n9 G 10}P 7.786 2.74 -6.578 {c4 G 10}8.364 3.578 -7.505
{c5 G 10}7.638 4.745 -7.475
@vectorlist off {H bonds} color=yellow 
{n7 A 9}P U 8.435 10.404 -3.696 {n6 A 23}U 10.095 10.893 -4.138
{n3 U 12}P U 13.569 10.079 -5.427 {n1 A 23}U 12.55 11.737 -5.367
{n7 A 23}P U 8.625 13.579 -4.207 {n6 A 9}U 7.107 13.152 -3.507
{n7 G 22}P U 7.946 14.77 -0.275 {n6 A 46}U 6.704 13.587 0.559
{o6 G 22}P U 10.057 12.845 -0.954 {n1 A 46}U 8.7 12.231 0.087
{n1 G 22}P U 11.793 14.306 -2.035 {n3, psu 13}U 12.801 12.323 -1.777
{n2 G 45}P U 6.048 7.661 -7.195 {o6 G 10}U 7.156 7.088 -8.144
{n1 G 45}P U 5.247 10.029 -6.729 {o4 U 25}U 6.487 10.301 -8.969
{o4 psu 13}P U 13.764 14.048 -2.965 {n2 G 22}U 13.056 15.908 -2.985
{n7 A 14}P U 13.122 14.16 1.365 {n3 U 8}U 13.52 12.516 1.745
{n6 A 14}P U 10.612 13.651 2.751 {o2 U 8}U 11.423 12.094 2.855
{n1 A 15}P U 10.737 14.748 5.878 {n3 U 48}U 9.897 13.473 6.725
{o2 U 48}P U 11.439 11.85 6.304 {n6 A 15}U 12.49 13.253 5.476
{n3 U 11}P U 11.193 7.375 -7.05 {n1 A 24}U 11.058 9.048 -7.795
{o4 U 11}P U 9.374 7.703 -5.78 {n6 A 24}U 8.996 9.307 -6.807
@kinemage 2 
@caption 
E. coli glutaminyl-tRNA synthetase-tRNA complex. The alpha-carbon backbone of the protein is light pink; the tRNA is blue.
@2zoom 1.00 
@2zslab 200 
@2center 37.578 13.503 21.076 
@2matrix 
-0.108009 0.033411 0.993588 0.292559 0.956247 -0.000353 -0.950128 0.290645 -0.113058 
@3zoom 2.45 
@3zslab 300 
@3center 25.571 -10.409 22.351 
@3matrix 
0.907818 -0.121482 0.401384 0.029495 0.973250 0.227850 -0.418327 -0.195007 0.887116 
@4zoom 2.82 
@4zslab 375 
@4center 48.670 22.111 23.133 
@4matrix 
0.429584 0.533623 0.728494 -0.452264 0.825394 -0.337908 -0.781611 -0.184311 0.595914 
@onewidth 
@group {protein} 
@subgroup {C alphas} 
@vectorlist {backbone} nobutton color= pinktint 
{ca thr 8}P 22.968 28.414 13.89 {ca thr 8}22.968 28.414 13.89
{ca asn 9}25.481 30.117 16.105
{ca phe 10}26.251 33.689 17.101
{ca ile 11}28.725 34.128 14.209
{ca arg 12}26.066 33.123 11.639
{ca gln 13}23.564 35.533 13.155
{ca ile 14}26.245 38.223 12.691
{ca ile 15}26.88 37.208 9.069
{ca asp 16}23.144 37.047 8.181
{ca glu 17}22.733 40.472 9.782
{ca asp 18}25.639 41.929 7.785
{ca leu 19}24.26 40.606 4.546
{ca ala 20}20.789 41.946 5.463
{ca ser 21}22.194 45.409 6.195
{ca gly 22}24.001 45.4 2.901
{ca lys 23}27.292 45.688 4.824
{ca his 24}28.554 42.731 2.788
{ca thr 25}27.436 40.839 -0.28
{ca thr 26}29.789 37.882 0.254
{ca val 27}31.544 36.211 3.167
{ca his 28}35.226 35.555 2.88
{ca thr 29}36.926 33.688 5.742
{ca arg 30}40.361 32.098 6.274
{ca phe 31}41.855 29.299 8.343
{ca pro 32}45.359 30.574 9.31
{ca pro 33}47.456 27.901 11.022
{ca glu 34}51.064 28.516 11.924
{ca pro 35}53.1 25.592 10.393
{ca asn 36}54.71 24.483 13.675
{ca gly 37}52.934 21.218 14.268
{ca tyr 38}50.302 18.926 12.969
{ca leu 39}46.678 19.917 13.033
{ca his 40}44.448 18.448 15.76
{ca ile 41}40.68 18.024 16.469
{ca gly 42}40.487 21.596 17.89
{ca his 43}41.873 22.875 14.574
{ca ala 44}39.206 20.769 12.878
{ca lys 45}36.607 22.812 14.763
{ca ser 46}38.127 25.988 13.193
{ca ile 47}38.25 24.357 9.697
{ca cys 48}34.604 23.278 9.845
{ca leu 49}33.59 26.834 10.985
{ca asn 50}35.51 28.798 8.465
{ca phe 51}35.059 26.588 5.414
{ca gly 52}31.528 25.486 6.354
{ca ile 53}30.555 29.195 6.467
{ca ala 54}32.213 29.95 3.151
{ca gln 55}30.323 27.127 1.422
{ca asp 56}26.921 27.508 3.024
{ca tyr 57}26.931 31.227 2.238
{ca lys 58}28.18 33.062 -0.835
{ca gly 59}31.699 31.4 -0.861
{ca gln 60}35.497 31.614 -0.466
{ca cys 61}37.731 30.602 2.389
{ca asn 62}41.496 30.948 2.206
{ca leu 63}44.102 28.701 3.672
{ca arg 64}46.909 30.946 4.816
{ca phe 65}50.042 29.624 6.539
{ca asp 66}50.705 32.184 9.203
{ca asp 67}54.44 31.845 8.909
{ca thr 68}55.954 34.817 10.698
{ca asn 69}58.266 32.987 13.111
{ca pro 70}60.905 30.973 11.166
{ca val 71}62.656 29.273 14.163
{ca lys 72}59.359 27.591 15.167
{ca glu 73}58.292 26.381 11.708
{ca asp 74}59.066 23.677 9.182
{ca ile 75}58.113 22.761 5.591
{ca glu 76}56.971 19.315 6.832
{ca tyr 77}54.121 21.007 8.56
{ca val 78}52.863 23.013 5.589
{ca glu 79}52.536 19.814 3.535
{ca ser 80}50.74 17.859 6.283
{ca ile 81}48.302 20.694 7.049
{ca lys 82}47.276 20.945 3.373
{ca asn 83}46.749 17.199 3.459
{ca asp 84}44.523 17.162 6.547
{ca val 85}42.433 20.154 5.365
{ca glu 86}41.751 18.29 2.11
{ca trp 87}41.128 14.906 3.825
{ca leu 88}38.437 16.557 5.99
{ca gly 89}36.647 17.359 2.736
{ca phe 90}37.328 21.084 2.352
{ca his 91}38.856 23.197 -0.405
{ca trp 92}40.384 26.68 -0.235
{ca ser 93}40.076 29.638 -2.635
{ca gly 94}42.852 30.118 -5.077
{ca asn 95}46.318 29.201 -4.173
{ca val 96}47.528 28.445 -0.673
{ca arg 97}48.546 31.778 0.902
{ca tyr 98}51.396 32.622 3.228
{ca ser 99}51.911 35.704 5.476
{ca ser 100}55.435 35.646 3.968
{ca asp 101}53.852 36.521 0.646
{ca tyr 102}53.167 39.849 2.252
{ca phe 103}56.593 40.439 3.761
{ca asp 104}57.4 43.27 1.333
{ca gln 105}53.951 44.854 1.821
{ca leu 106}54.249 44.542 5.595
{ca his 107}57.661 46.283 5.559
{ca ala 108}56.145 49.079 3.448
{ca tyr 109}53.37 49.504 6.015
{ca ala 110}55.885 49.712 8.898
{ca ile 111}57.588 52.56 7.
{ca glu 112}54.219 54.295 6.661
{ca leu 113}53.775 53.989 10.428
{ca ile 114}57.291 55.441 10.988
{ca asn 115}56.527 58.347 8.627
{ca lys 116}53.454 59.207 10.655
{ca gly 117}55.451 58.985 13.912
{ca leu 118}53.389 55.984 15.095
{ca ala 119}56.336 53.599 15.296
{ca tyr 120}60.013 53.841 16.386
{ca val 121}63.023 51.576 16.863
{ca asp 122}63.606 50.901 20.466
{ca glu 123}66.827 49.581 21.932
{ca leu 124}65.624 48.516 25.349
{ca thr 125}66.946 44.952 25.823
{ca pro 126}64.55 41.919 25.935
{ca glu 127}64.564 42.024 29.731
{ca gln 128}64.177 45.799 29.878
{ca ile 129}61.053 45.939 27.645
{ca arg 130}59.324 43.668 30.234
{ca glu 131}60.633 45.874 33.088
{ca tyr 132}59.151 48.935 31.371
{ca arg 133}55.814 47.333 30.44
{ca gly 134}54.154 47.812 33.824
{ca thr 135}52.024 44.97 35.183
{ca leu 136}48.306 44.094 35.175
{ca thr 137}47.807 46.725 37.967
{ca gln 138}50.658 49.198 37.37
{ca pro 139}50.909 51.27 34.148
{ca gly 140}54.063 51.088 32.063
{ca lys 141}56.549 53.746 31.265
{ca asn 142}57.965 55.211 28.078
{ca ser 143}61.118 53.989 26.563
{ca pro 144}63.975 56.532 26.571
{ca tyr 145}64.248 55.959 22.798
{ca arg 146}60.534 56.622 22.183
{ca asp 147}60.795 60.13 20.721
{ca arg 148}63.435 59.559 18.059
{ca ser 149}62.778 61.609 14.899
{ca val 150}61.19 60.001 11.795
{ca glu 151}64.517 60.402 10.113
{ca glu 152}66.42 58.479 12.844
{ca asn 153}63.806 55.769 12.933
{ca leu 154}64.011 55.259 9.172
{ca ala 155}67.805 54.941 9.266
{ca leu 156}67.747 52.604 12.313
{ca phe 157}64.917 50.515 10.757
{ca glu 158}66.903 50.136 7.493
{ca lys 159}69.945 49.175 9.609
{ca met 160}67.719 46.534 11.22
{ca arg 161}66.652 45.315 7.809
{ca ala 162}70.296 45.177 6.587
{ca gly 163}71.593 43.147 9.56
{ca gly 164}73.628 45.854 11.306
{ca phe 165}72.077 44.993 14.731
{ca glu 166}72.38 41.736 16.633
{ca glu 167}69.295 39.804 17.714
{ca gly 168}67.697 41.395 20.71
{ca lys 169}69.555 44.676 20.264
{ca ala 170}66.649 46.569 18.649
{ca cys 171}63.053 46.115 17.54
{ca leu 172}60.332 48.249 15.957
{ca arg 173}57.438 49.198 18.216
{ca ala 174}54.153 50.972 17.713
{ca lys 175}53.837 54.255 19.609
{ca ile 176}50.482 53.754 21.296
{ca asp 177}49.917 54.193 25.023
{ca met 178}52.18 52.935 27.69
{ca ala 179}49.442 53.307 30.36
{ca ser 180}46.712 51.493 28.45
{ca pro 181}44.641 49.119 30.522
{ca phe 182}45.164 46.782 27.519
{ca ile 183}48.704 45.421 27.931
{ca val 184}48.893 44.601 24.142
{ca met 185}48.544 48.348 23.363
{ca arg 186}51.587 49.229 25.539
{ca asp 187}53.753 49.851 22.53
{ca pro 188}53.61 46.378 20.935
{ca val 189}56.583 45.324 18.835
{ca leu 190}55.861 45.132 15.159
{ca tyr 191}59.295 43.749 14.093
{ca arg 192}62.114 41.736 15.617
{ca ile 193}65.445 40.452 14.359
{ca lys 194}66.033 36.776 13.744
{ca phe 195}69.032 35.636 11.672
{ca ala 196}67.325 32.379 10.772
{ca glu 197}66.398 30.79 7.488
{ca his 198}62.738 30.848 6.624
{ca his 199}61.191 27.829 4.863
{ca gln 200}59.739 30.058 2.093
{ca thr 201}61.871 33.163 1.785
{ca gly 202}65.187 31.499 2.648
{ca asn 203}67.64 34.081 3.836
{ca lys 204}66.12 37.176 2.219
{ca trp 205}64.965 38.552 5.593
{ca cys 206}66.511 38.949 9.016
{ca ile 207}63.661 41.048 10.386
{ca tyr 208}60.338 39.274 10.801
{ca pro 209}56.897 40.746 11.534
{ca met 210}54.943 39.917 14.658
{ca tyr 211}51.558 38.288 14.598
{ca asp 212}49.438 41.351 15.504
{ca phe 213}50.953 43.448 12.793
{ca thr 214}50.846 40.609 10.207
{ca his 215}47.396 39.25 10.831
{ca cys 216}45.131 42.219 10.344
{ca ile 217}46.963 43.427 7.255
{ca ser 218}46.981 39.949 5.579
{ca asp 219}43.176 39.801 6.255
{ca ala 220}42.626 43.263 4.801
{ca leu 221}44.757 42.519 1.713
{ca glu 222}42.902 39.268 1.12
{ca gly 223}39.525 40.951 1.55
{ca ile 224}38.616 38.727 4.562
{ca thr 225}35.168 39.901 5.631
{ca his 226}35.004 38.312 9.076
{ca ser 227}38.179 37.023 10.899
{ca leu 228}37.212 34.208 13.225
{ca cys 229}39.615 33.338 15.92
{ca thr 230}39.596 31.979 19.42
{ca leu 231}38.78 33.828 22.666
{ca glu 232}42.273 34.712 23.89
{ca phe 233}42.529 37.139 20.963
{ca gln 234}39.776 39.419 22.318
{ca asp 235}42.272 41.949 23.779
{ca asn 236}44.381 41.678 20.642
{ca arg 237}41.404 42.879 18.606
{ca arg 238}42.147 46.408 19.811
{ca leu 239}45.609 46.329 18.197
{ca tyr 240}44.165 44.682 15.054
{ca asp 241}41.823 47.649 14.682
{ca trp 242}44.469 50.228 15.594
{ca val 243}46.889 48.954 12.873
{ca leu 244}44.169 49.062 10.265
{ca asp 245}42.94 52.519 11.347
{ca asn 246}46.402 54.008 10.853
{ca ile 247}47.669 52.719 7.535
{ca thr 248}46.402 53.403 4.014
{ca ile 249}44.327 50.239 3.525
{ca pro 250}40.889 50.314 1.816
{ca val 251}39.017 47.735 3.953
{ca his 252}38.683 46.864 7.631
{ca pro 253}37.806 43.139 8.251
{ca arg 254}36.137 42.532 11.662
{ca gln 255}37.267 39.884 14.184
{ca tyr 256}34.892 37.612 16.113
{ca glu 257}36.101 35.201 18.73
{ca phe 258}34.697 31.809 19.775
{ca ser 259}35.813 29.338 22.467
{ca arg 260}38.362 26.612 21.913
{ca leu 261}37.539 22.955 21.997
{ca asn 262}39.1 21.202 24.968
{ca leu 263}38.644 17.425 24.972
{ca glu 264}38.625 15.241 28.004
{ca tyr 265}41.654 12.97 28.596
{ca thr 266}43.892 14.668 26.093
{ca val 267}46.172 17.665 25.552
{ca met 268}45.588 20.008 22.565
{ca ser 269}48.67 22.111 23.133
{ca lys 270}51.156 21.782 20.274
{ca arg 271}53.991 22.307 22.777
{ca lys 272}52.799 19.315 24.789
{ca leu 273}51.932 17.194 21.725
{ca asn 274}55.415 17.976 20.441
{ca leu 275}56.97 16.796 23.746
{ca leu 276}55.072 13.521 23.396
{ca val 277}56.575 12.876 19.945
{ca thr 278}60.058 14.333 20.684
{ca asp 279}60.483 12.26 23.825
{ca lys 280}59.329 9.156 21.923
{ca his 281}56.356 8.462 24.215
{ca val 282}54.156 8.057 21.151
{ca glu 283}55.084 6.764 17.663
{ca gly 284}54.868 10.152 15.973
{ca trp 285}52.278 12.9 15.351
{ca asp 286}50.02 10.389 13.608
{ca asp 287}50.05 7.815 16.416
{ca pro 288}46.48 6.421 16.787
{ca arg 289}46.374 7.769 20.39
{ca met 290}47.111 11.347 19.361
{ca pro 291}44.308 13.973 19.003
{ca thr 292}45.788 15.076 15.654
{ca ile 293}43.669 14.74 12.495
{ca ser 294}46.249 12.265 11.074
{ca gly 295}46.239 10.181 14.285
{ca leu 296}42.431 10.158 14.254
{ca arg 297}42.569 9.074 10.571
{ca arg 298}45.083 6.234 11.257
{ca arg 299}42.967 5.165 14.274
{ca gly 300}40.063 4.773 11.825
{ca tyr 301}37.998 7.947 12.262
{ca thr 302}36.334 9.111 9.073
{ca ala 303}36.324 12.824 7.969
{ca ala 304}32.534 12.529 8.067
{ca ser 305}32.475 11.625 11.748
{ca ile 306}34.753 14.597 12.539
{ca arg 307}32.53 17.054 10.604
{ca glu 308}29.532 15.692 12.502
{ca phe 309}31.41 16.095 15.781
{ca cys 310}32.054 19.757 14.806
{ca lys 311}28.317 20.296 14.033
{ca arg 312}27.309 18.72 17.349
{ca ile 313}29.513 20.64 19.732
{ca gly 314}28.36 24.057 18.496
{ca val 315}30.204 27.413 18.324
{ca thr 316}29.841 29.759 21.316
{ca lys 317}31.822 31.864 23.778
{ca gln 318}31.444 29.43 26.697
{ca asp 319}34.622 27.684 27.884
{ca asn 320}33.91 23.961 27.515
{ca thr 321}35.393 20.509 27.751
{ca ile 322}33.814 17.836 25.701
{ca glu 323}33.671 14.294 26.923
{ca met 324}35.237 11.597 24.738
{ca ala 325}31.815 9.911 24.64
{ca ser 326}30.671 12.687 22.227
{ca leu 327}33.499 11.849 19.826
{ca glu 328}33.069 8.057 20.055
{ca ser 329}29.333 8.417 19.43
{ca cys 330}30.181 10.19 16.162
{ca ile 331}32.352 7.408 14.753
{ca arg 332}30.224 4.508 16.106
{ca glu 333}27.171 5.942 14.378
{ca asp 334}28.934 6.346 11.021
{ca leu 335}30.735 2.978 11.073
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{ca glu 384}38.628 -27.156 15.78
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{ca gly 406}26.814 -27.412 30.592
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{ca glu 408}24.691 -24.386 24.816
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{ca thr 436}29.541 -31.414 21.163
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{ca asp 438}23.951 -30.343 17.339
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{ca glu 494}47.527 0.912 29.087
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{ca glu 521}34.384 -6.498 19.643
{ca gly 522}34.421 -3.067 17.998
{ca tyr 523}35.37 -1.333 14.793
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{ca thr 532}50.771 -5.564 7.631
{ca ala 533}52.263 -7.616 4.702
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{ca arg 545}28.701 -0.224 23.612
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{ca gln 517}P 33.108 -5.142 12.613 {ca gln 517}33.108 -3.142 12.613
{ca gln 517}P 33.108 -4.142 11.613 {ca gln 517}33.108 -4.142 13.613
{ca glu 519}P 31.353 -8.505 15.603 {ca arg 520}30.962 -8.155 19.373
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{P C 34}P 16.951 -13.619 16.099 {P C 34}16.951 -13.619 18.099
{P U 35}P 20.81 -11.044 17.677 {P U 35}22.81 -11.044 17.677
{P U 35}P 21.81 -12.044 17.677 {P U 35}21.81 -10.044 17.677
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{P G 36}P 25.571 -11.409 22.351 {P G 36}25.571 -9.409 22.351
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{ca gly 42}40.487 21.596 17.89
{ca his 43}41.873 22.875 14.574
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{ca met 268}P 45.588 20.008 22.565 {ca ser 269}48.67 22.111 23.133
{ca lys 270}51.156 21.782 20.274
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{P G 3}39.236 48.103 35.528
{P G 4}36.914 46.54 30.191
{P G 5}34.669 42.835 26.221
{P U 6}30.652 37.76 26.658
{P A 7}27.342 33.146 28.532
{P 4SU 8}26.038 27.77 32.507
{P C 9}22.979 23.639 33.126
{P G 10}23.456 18.271 36.616
{P C 11}28.65 19.252 34.342
{P C 12}30.807 21.378 29.589
{P A 13}28.632 24.949 24.669
{P A 14}23.947 27.89 21.54
{P G 15}19.102 30.667 19.632
{P C 16}13.531 33.352 22.417
{P OMG 18}12.572 39.612 22.889
{P G 19}8.416 36.507 24.43
{P H2U 20}5.468 30.663 25.603
{P A 21}7.757 26.584 30.801
{P A 22}11.392 22.007 26.859
{P G 23}13.468 18.125 22.942
{P G 24}17.635 14.455 20.986
{P C 25}22.323 11.28 20.917
{P A 26}25.973 8.069 24.011
{P C 27}25.825 5.551 29.16
{P C 28}22.482 3.112 33.344
{P G 29}18.088 0.022 34.916
{P G 30}13.414 -3.211 32.268
{P A 31}10.696 -6.217 28.516
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{P C 34}16.951 -13.619 17.099
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{P 2MA 37}23.227 -4.146 24.038
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{P G 42}7.538 7.454 23.167
{P G 43}8.097 10.171 28.237
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{P A 45}13.688 16.412 34.897
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{P U 47}12.136 24.081 39.544
{P C 48}15.833 29.211 38.252
{P C 49}21.86 31.203 35.311
{P G 50}20.72 30.761 40.666
{P A 51}18.249 33.546 44.851
{P G 52}15.354 38.099 47.23
{P G 53}11.742 42.423 46.042
{P T 54}8.57 46.188 42.179
{P PSU 55}5.431 47.169 38.552
{P C 56}1.529 44.933 35.624
{P G 57}3.091 39.881 37.137
{P A 58}7.279 36.675 35.779
{P A 59}11.76 33.121 34.203
{P U 60}16.052 36.82 33.525
{P C 61}18.346 40.768 29.076
{P C 62}18.991 45.735 31.663
{P U 63}21.339 48.511 35.791
{P C 64}24.825 48.392 40.323
{P G 65}28.262 45.426 43.396
{P U 66}31.576 40.546 45.295
{P A 67}33.961 35.198 44.275
{P C 68}37.002 31.306 41.59
{P C 69}40.082 29.752 36.584
{P C 70}43.14 30.827 31.792
{P C 71}46.718 34.083 29.079
{P A 72}50.781 37.727 28.474
{P G 73}56.021 38.994 29.313
{P C 74}57.725 40.966 24.07
{P C 75}59.723 36.436 19.855
{P A 76}54.838 35.543 16.124
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{p G 4}P 36.914 46.54 30.191 {p G 5}34.669 42.835 26.221
{p U 6}30.652 37.76 26.658
{p C 11}P 28.65 19.252 34.342 {p C 12}30.807 21.378 29.589
{p G 15}P 19.102 30.667 19.632 {p C 16}13.531 33.352 22.417
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{p G 23}P U 13.468 17.125 22.942 {p G 23}U 13.468 19.125 22.942
{p G 23}P U 13.468 18.125 21.942 {p G 23}U 13.468 18.125 23.942
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{p C 28}22.482 3.112 33.344
{p G 29}18.088 0.022 34.916
{p G 30}13.414 -3.211 32.268
{p A 31}10.696 -6.217 28.516
{p OMU 32}10.581 -8.5 23.69
{p PSU 39}P 20.595 3.041 16.784 {p C 40}15.039 4.04 16.224
{p C 41}10.136 5.4 19.326
{p G 42}7.538 7.454 23.167
{p U 47}P 12.136 24.081 39.544 {p C 48}15.833 29.211 38.252
{p C 49}21.86 31.203 35.311
{p G 50}20.72 30.761 40.666
{p U 63}P U 20.339 48.511 35.791 {p U 63}U 22.339 48.511 35.791
{p U 63}P U 21.339 47.511 35.791 {p U 63}U 21.339 49.511 35.791
{p U 63}P U 21.339 48.511 34.791 {p U 63}U 21.339 48.511 36.791
{p G 65}P U 27.262 45.426 43.396 {p G 65}U 29.262 45.426 43.396
{p G 65}P U 28.262 44.426 43.396 {p G 65}U 28.262 46.426 43.396
{p G 65}P U 28.262 45.426 42.396 {p G 65}U 28.262 45.426 44.396
{p A 67}P 33.961 35.198 44.275 {p C 68}37.002 31.306 41.59
{p C 69}40.082 29.752 36.584
{p A 72}P U 49.781 37.727 28.474 {p A 72}U 51.781 37.727 28.474
{p A 72}P U 50.781 36.727 28.474 {p A 72}U 50.781 38.727 28.474
{p A 72}P U 50.781 37.727 27.474 {p A 72}U 50.781 37.727 29.474
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{P A 22}P 11.392 22.007 26.859 {P G 23}13.468 18.125 22.942
{P G 24}17.635 14.455 20.986
{P C 25}22.323 11.28 20.917
{P A 26}25.973 8.069 24.011
{P C 27}25.825 5.551 29.16
{P C 28}22.482 3.112 33.344
{P G 29}18.088 0.022 34.916
{P G 30}13.414 -3.211 32.268
{P A 31}10.696 -6.217 28.516
{P OMU 32}10.581 -8.5 23.69
{P U 33}12.667 -11.076 19.252
{P C 34}16.951 -13.619 17.099
{P U 35}21.81 -11.044 17.677
{P G 36}25.571 -10.409 22.351
{P 2MA 37}23.227 -4.146 24.038
{P PSU 38}23.668 0.22 20.743
{P PSU 39}20.595 3.041 16.784
{P C 40}15.039 4.04 16.224
{P C 41}10.136 5.4 19.326
{P G 42}7.538 7.454 23.167
{P G 43}8.097 10.171 28.237
{P C 44}10.502 12.857 32.974
{P A 45}13.688 16.412 34.897
{P U 46}13.695 20.734 38.108
{P U 47}12.136 24.081 39.544
{P C 48}15.833 29.211 38.252
{P C 49}21.86 31.203 35.311
{P G 57}P 3.091 39.881 37.137 {P A 58}7.279 36.675 35.779
{P C 74}P 57.725 40.966 24.07 {P C 75}59.723 36.436 19.855
{P A 76}54.838 35.543 16.124