# Patent

## Title
Screening methods using the crystal structure of ribosomal protein L11/GTPase activating region rRNA complex

## Abstract

The present invention is broadly directed to methods of screening ribosomal protein L11/GTPase activating region (GAR) RNA-modulating compounds by using information from the high-resolution structure of the L11/GAR complex. The methods are useful in identifying compounds useful for anti-bacterial treatments.

## Background
TECHNICAL FIELD OF THE INVENTION
The present invention relates to methods of screening for compounds that inhibit or activate bacterial growth by binding to the complex formed between ribosomal protein L11 and the 23S ribosomal RNA region that interacts with it in vivo.
BACKGROUND
The elongation cycle of protein synthesis is driven by two elongation factors that bind to nearly identical sites on the large (50S) ribosomal subunit (Spahn and Nierhaus, 1998; Wilson and Noller, 1998). EF-Tu delivers aminoacyl tRNAs to the ribosome, whereas EF-G catalyzes the translocation of the ribosome by one codon relative to the mRNA and the concomitant movement of the A and P site tRNAs. Both elongation factors are G proteins, and their interactions with the ribosome are coupled to the binding and hydrolysis of GTP. Like most G proteins, EF-Tu and EF-G are molecular switches that have limited inherent GTPase activity, and they rely on an accessory factor to stimulate activity at the appropriate time. This accessory factor is an integral part of the 50S ribosomal subunit and has usually been referred to as the “GTPase center,” but by analogy with the functionally equivalent GAP proteins that stimulate GTPase activity in G-proteins, it seems more appropriate to refer to it as the “GTPase activating region” (hereafter abbreviated as the GAR). Early work on the identification of the molecular components of the GAR implicated a complex between ribosomal protein L11 and a highly conserved 58-nucleotide stretch of 23S ribosomal RNA (rRNA), nucleotides 1051-1108 in Escherichia coli (Schmidt et al., 1981; Thompson et al., 1979). The L11-RNA complex is the target for a family of thiazole antibiotics that includes thiostrepton and micrococcin. Thiostrepton binds essentially irreversibly to 50S subunits (Sopori and Lengyel, 1972) and inhibits hydrolysis of GTP by EF-G (Pestka, 1970; Rodnina et al., 1997), while micrococcin binds to the same complex and stimulates GTP hydrolysis by EF-G (Cundliffe and Thompson, 1981).
Other components of the ribosome have also been implicated in stimulation of GTP hydrolysis by elongation factors. Classical work suggested that protein L7/L12, which together with L10 forms the “stalk” of the 50S subunit that lies adjacent to L11, is involved in stimulation of GTPase activity in EF-Tu (Donner et al., 1978). However, recently it has been shown that protein L7/L12, although essential for stalk formation, is not required for viability in yeast (Briones et al., 1998). The sarcin/ricin loop, a small, highly conserved stem-loop in the 23S rRNA that is known to be essential for ribosome function, has been footprinted by the elongation factors (Moazed et al., 1988), and is also considered a candidate for being part of the GAR. Therefore, it is not yet clear whether the L11-RNA complex per se should be considered the GAR, or whether the GAR should be defined as a more extensive region of the 50S subunit. In any event, it appears that the L11-RNA complex is at the heart of the GAR; the complex of L11 with its cognate RNA will be referred to herein as the GAR.
The GAR is one of the most thoroughly characterized RNA-protein complexes. The secondary structure of the RNA was first inferred from biochemical and genetic studies (Glotz et al., 1981; Noller et al., 1981). It consists of a junction of four double-helical stems (FIG. 1A). Approximately one-third of the residues in the GAR RNA are very highly conserved. The structure, thermodynamic stability, and ion-binding affinities of the RNA component have been extensively probed by a variety of biophysical and biochemical techniques; these data suggest that the 1067 and 1095 stem-loops are folded into a compact tertiary structure (Conn et al., 1998; Rosendahl and Douthwaite, 1994). Protein L11 consists of two domains: the C-terminal domain binds tightly to the RNA tertiary structure, while the N-terminal domain is required for the cooperative interaction with thiostrepton (Xing and Draper, 1996). The structure of the C-terminal domain has been determined by NMR techniques (Hinck et al., 1997; Markus et al., 1997). Footprinting studies (Rosendahl and Douthwaite, 1993) have identified regions of RNA involved in the interaction with L11, while NMR chemical shift measurements (Hinck et al., 1997) have identified an RNA-binding surface on the C-terminal domain of the protein.
It is an object of the invention to provide a detailed view of a functionally important protein-RNA complex in the ribosome.
It is also an object of the invention to provide a high-resolution structure of a ribosomal protein-RNA complex.
Yet another object of the invention is to provide new principles of RNA folding, of RNA-protein recognition, and of indirect RNA tertiary structure stabilization.
Yet another object of the invention is to solve the three dimensional structure of L11 complexed with GAR RNA and to determine its structure coordinates.
SUMMARY OF THE INVENTION
The present invention is broadly directed to methods of screening ribosomal protein L11/GTPase activating region (GAR) RNA-modulating compounds by using information from the high-resolution structure of the L11/GAR complex.
The invention encompasses use of the structure coordinates of an L11/GAR crystal to define the atomic details of regions of the L11/GAR complex, such as the GTPase activating region and one or more binding sites of accessory factors, which are target sites for inhibitors or activators.
The invention also encompasses use of the structure coordinates and atomic details of the L11/GAR RNA complex or its co-complexes to design, evaluate computationally, synthesize and use inhibitors or activators of the L11/GAR.
Structure coordinates for L11/GAR RNA complex according to Table II may be modified from this original set by mathematical manipulation. Such manipulations include, but are not limited to, crystallographic permutations, fractionalizations, or inversion of the raw structure coordinates, integer additions or subtractions to sets of the raw structure coordinates, and any combination of the above.
The crystal structure of the GAR allows the screening and design of novel classes of GAR inhibitory or activating compounds with great medical potential, for example, to prevent or stimulate growth of certain bacteria.
The invention encompasses a method for identifying a potential modulator of ribosomal protein L11/GAR activity, comprising the steps of: a) using a three-dimensional structure of the L11/GAR complex as defined by atomic coordinates of the L11/GAR according to FIG. 7; b) employing the three-dimensional structure to design or select the potential modulator; c) providing the potential modulator; and d) contacting the potential modulator with L11/GAR in the presence of an activity to determine the ability of the potential modulator to modulate the activity, for example, L11/GAR activity.
In one embodiment of the invention, the potential modulator is designed de novo.
In another embodiment of the invention, the potential modulator is designed from a known modulator.
In another embodiment of the invention, the step of employing the three-dimensional structure to design or select the compound comprises the steps of: a) identifying chemical entities or fragments capable of associating with the L11/GAR; and b) assembling the identified chemical entities or fragments into a single molecule to provide the structure of the potential modulator. Relative to this embodiment, the potential modulator may be designed de novo or designed from a known modulator.
The invention further encompasses a method for screening L11/GAR-binding compounds comprising the steps of: 1) incubating in vitro one or more compounds, a known L11/GAR binding activity and labeled RNA comprising GAR RNA; 2) separating that fraction of the labeled RNA bound to the known L11/GAR binding activity from that fraction of the labeled RNA not bound to the known L11/GAR binding activity; and 3) detecting labeled RNA, wherein a decrease in the level of the labeled RNA bound to the known L11 /GAR binding activity in the presence of one or more compounds indicates the binding of one or more of the compounds to L11/GAR.
The invention further encompasses a method for screening L11/GAR-binding compounds comprising the steps of: 1) incubating in vitro one or more compounds, a labeled known L11/GAR binding activity and an RNA comprising GAR RNA; 2) separating that fraction of the labeled known L11/GAR binding activity bound to the RNA from that fraction of the labeled known L11/GAR binding activity not bound to the RNA; and 3) detecting labeled known L11/GAR binding activity wherein a decrease in the level of the labeled known L11/GAR binding activity bound to the RNA in the presence of one or more compounds indicates that one or more of the compounds binds L11/GAR.
In one embodiment of the the method of screening L11/GAR-binding compounds, the known L11/GAR binding activity is an antibiotic. In another embodiment the antibiotic is micrococcin. In a preferred embodiment the antibiotic is thiostrepton.
In another embodiment of the method of screening L11/GAR-binding compounds, the RNA comprising GAR RNA is contained within a ribosome.
In another embodiment of the method of screening L11/GAR-binding compounds, a plurality of compounds is screened for L11/GAR binding in a plurality of separate, simultaneous assays.
The invention further encompasses a method for screening L11/GAR-binding compounds comprising the steps of: 1) incubating in vitro one or more compounds with a translationally competent cell extract and a translatable RNA; and 2) detecting translation, wherein a decrease in the level of translation indicates binding of one or more of the compounds to L11/GAR.
In one embodiment, the translatable RNA encodes an enzyme and the step of detecting translation comprises detecting the activity of the enzyme.
In a preferred embodiment, the enzyme is luciferase.
In another embodiment, the translatable RNA is poly-U, and the step of detecting translation detects the incorporation of labeled phenylalanine into polyphenylalanine.
In another embodiment, the translationally competent cell extract comprises isolated ribosomes.
The invention further encompasses a method for screening L11/GAR-binding compounds comprising the steps of: 1) incubating in vitro one or more compounds, isolated 70S ribosomes, isolated EF-G and gamma-labeled GTP; and 2) detecting GTP hydrolysis wherein a decrease in GTP hydrolysis indicates one or more of the compounds binds L11/GAR.
The invention further encompasses a method for screening anti-bacterial compounds comprising the steps of: 1) incubating in vitro one or more compounds, a known L11/GAR binding activity and labeled RNA comprising GAR RNA; 2) separating that fraction of the labeled RNA bound to the known L11/GAR binding activity from that fraction of the labeled RNA not bound to the known L11/GAR binding activity; and 3) detecting labeled RNA, wherein a decrease in the level of the labeled RNA bound to the known L11/GAR binding activity in the presence of one or more compounds indicates that one or more of the compounds has anti-bacterial properties.
The invention further encompasses a method for screening anti-bacterial compounds comprising the steps of: 1) incubating in vitro one or more compounds, a labeled known L11/GAR binding activity and an RNA comprising GAR RNA; 2) separating that fraction of the labeled known L11/GAR binding activity bound to the RNA from that fraction of the labeled known L11/GAR binding activity not bound to the RNA; and 3) detecting labeled known L11/GAR binding activity wherein a decrease in the level of the labeled known L11/GAR binding activity bound to the RNA in the presence of one or more compounds indicates that one or more of the compounds has anti-bacterial properties.
In one embodiment of the the method of screening anti-bacterial compounds, the known L11/GAR binding activity is an antibiotic. In another embodiment the antibiotic is micrococcin. In a preferred embodiment the antibiotic is thiostrepton.
In another embodiment of the method of screening anti-bacterial compounds, the RNA comprising GAR RNA is contained within a ribosome.
In another embodiment of the method of screening anti-bacterial compounds, a plurality of compounds is screened for L11/GAR binding in a plurality of separate, simultaneous assays.
The invention further encompasses a method for screening anti-bacterial compounds comprising the steps of: 1) incubating in vitro one or more compounds with a translationally competent cell extract and a translatable RNA; and 2) detecting translation, wherein a decrease in the level of translation indicates that one or more of the compounds has anti-bacterial properties.
In one embodiment, the translatable RNA encodes an enzyme and the step of detecting translation comprises detecting the activity of the enzyme.
In a preferred embodiment, the enzyme is luciferase.
In another embodiment, the translatable RNA is poly-U, and the step of detecting translation detects the incorporation of labeled phenylalanine into polyphenylalanine.
In another embodiment, the translationally competent cell extract comprises isolated ribosomes.
The invention further encompasses a method for screening anti-bacterial compounds comprising the steps of: 1) incubating in vitro one or more compounds, isolated 70S ribosomes, isolated EF-G and gamma-labeled GTP; and 2) detecting GTP hydrolysis wherein a decrease in GTP hydrolysis indicates that one or more of the compounds has anti-bacterial properties. Further features and advantages of the invention are embodied in the following description of the invention and in the claims.



BRIEF DESCRIPTION OF THE DRAWINGS
FIG. 1 shows an overview of the secondary and tertiary structure of the GTPase activating region RNA from Thermotoga maritima: a) RNA secondary structure derived from the crystal structure (RNA sequence is SEQ ID NO: 5). Lines indicate long-range base triples and the long-range 1088-1060 base pair; b) ribbon-and-stick schematic of the RNA tertiary structure (For clarity, protein L11 has been omitted from view); c) same as (b), but the view is down the major groove of the 1095 stem to emphasize the compactness to the RNA fold. FIGS. 1b and 1c were made with the program RIBBONS (Carson, 1991).
FIG. 2 shows selected details of the tertiary structure of the GTPase activating region RNA from Thermotoga maritima; in (a) and (b), the RNA backbone is represented by a ribbon and the phosphates are not shown: a) the ribose zipper that mediates the minor-groove to minor-groove association of the terminal stem and the 1082 hairpin loop (Hydrogen bonds are indicated by dotted lines); b) the major-groove to major-groove association of the 1067 and 1095 stem-loops, in a view emphasizing the high-five, S-turn, and dinucleotide platform motifs. The high-five motif consists of the long-range stacking of two bulged residues, U1061 and A1070. The S-turn comprises the inverted nucleotide U1060 and the bulged residue U1061. The dinucleotide platform motif consists of G1089 and U1090, on which the bulged residues G1071 and C1072 rest, as part of the long-range triples G1071-(G1091-C1100) and C1072-(C1092-G1099).
c) Geometries of the noncanonical base pairs and base triples. Top panel, the three major groove base triples in the core of the structure: G1089-(U1090-U1101), G1071-(G1091-C1100), and C1072-(C1092-G1099). Bottom left panel, the minor groove docking interactions (U1082-A1086)-(G1056-A1103) and A1085-(G1054-C1104). Bottom right panel, the long-range pair A1088-U1060. FIGS. 2a and 2b were made with RIBBONS (Carson, 1991); 2c with MOLSCRIPT (Kraulis, 1991).
FIG. 3. RNA-metal ion interactions in the tertiary structure of the GTPase activating region RNA from Thermotoga maritima: a) overview of the locations of the metal ions, showing that they are primarily in the interacting major grooves of the 1067 and 1095 stems. Magnesium ions are gold, cadmium ions are magenta, and the mercury ion is rose. b) close-up of the central cadmium ion that stabilizes sharp turns at the 1056-1057 and 1086-1087 phosphodiester linkages at the center of the 4-way junction. Direct ligation of the cadmium ion is indicated by solid lines, and second-shell ligation is indicated by dotted lines. FIG. 3a was made with RIBBONS (Carson, 1991), and FIG. 3b was made with MOLSCRIPT (Kraulis, 1991).
FIG. 4 shows the RNA-L11 complex within the GTPase activating region from Thermotoga maritima: a) alignment of four widely divergent L11 sequences (“E coli” is Escherichia coli, SEQ ID NO: 1; “T marit” is Thermotoga maritima, SEQ ID NO: 2; “Sulf ac” is Sulfolobus acidocaldarius, SEQ ID NO: 3; and “Sacc cor” is Saccharomyces cerevisiae, SEQ ID NO: 4), together with a schematic of the protein's secondary structure. The sidechains of residues shown in forward-slanting narrow hatch marks participate in the hydrophobic core in the crystal structure. Residues involved in RNA binding are shown with backward-slanting narrow hatch marks for side-chain contacts, backward slanting wide hatch marks for main-chain contacts or cross-hatched if both the side-chain and main-chain interact with RNA. Abbreviations: E. coli, Echerichia coli (eubacterium); T. marit, Thermotoga maritima (eubacterium); Sulf ac, Sulfolobus acidocaldarius (archaea); Sacc cer, Saccharomyces cerevisiae (eukaryote). The numbering is based on the Thermotoga maritima sequence present in the crystal structure. b) stereoview of the complex. The L11 N- and C-terminal domains are labled. Note that the N-terminal domain straddles the interface of the 1067 and 1095 stem-loops. c) orthogonal stereoview of the complex. This view emphasizes the relatively loose association of the L11 N-terminal domain with the RNA. FIGS 4b and 4c were made with RIBBONS (Carson, 1991).
FIG. 5 shows Protein-RNA recognition within the GTPase activating region from Thermotoga maritima: a) schematic of RNA-CTD interactions observed in the crystal structure. Unusual RNA conformational features are also indicated (see inset for key). Water molecules that mediate protein-RNA interactions are indicated by a “W”. b) Detail of the recognition of the conserved long-range A1088-U1060 pair by conserved L11 residues Gly 130 and Thr131 from helix 5, and by the N-terminus of helix 3. FIG. 5b was made with MOLSCRIPT (Kraulis, 1991).
FIG. 6 shows that the sites of mutations conferring resistance to thiostrepton and micrococcin are clustered around a cleft between the RNA and the proline-rich helix in the L11 N-terminal domain. Residues implicated in thiostrepton binding (A1067, A1095, and Pro22) are labeled. The position of Tyr61, which is protected by thiostrepton in protein footprinting experiments, is also indicated. Other labeled residues are those that confer micrococcin resistance (see text for details). The figure was made with RIBBONS (Carson, 1991).
Table II shows the atomic structure coordinates for the complex between ribosomal L11 protein and the GAR RNA as derived by X-ray diffraction from a crystal of L11 complexed with 23S rRNA nucleotides 1051-1108.



DETAILED DESCRIPTION OF THE INVENTION
The invention is based on the discovery of the crystal structure of the ribosomal GAR from the hyperthermophilic eubacterium Thermotoga maritima, which is disclosed herein
Definitions
As used herein, the term “binding site” or “binding pocket” refers to a region of a protein or protein/RNA complex which binds or interacts with a particular compound. It is understood that the composition of the protein or RNA residues and/or the protein or RNA backbone, as well as the interaction of such moieties with their solvent including ions defines the specificity of the binding pocket.
As used herein, the term “exposed residue” refers to an amino acid or RNA residue which is located on the surface of a protein, RNA or RNA/protein complex.
As used herein the term “N terminus” or “N terminal lobe” or “NTD” when used in reference to L11 means amino acids 1-70 of L11.
As used herein, the term “C terminus” or “C terminal lobe” or “CTD” when used in reference to L11 means amino acids 76-141 of L11.
As used herein, the term “tether” or “tether sequence” when used in reference to L11 means amino acids 71 to 75 of L11.
As used herein, the term “flexible” when applied to a protein or RNA domain means that that domain allows one or more domains adjoining or flanking it to move or flex in space relative to the flexible domain.
As used herein, the term “backbone” or “backbone residue” when applied to an RNA molecule refers to the sugar-phosphate moieties that are covalently linked to form an RNA polymer. When applied to a protein molecule, “backbone” or “backbone residue” refers to the alternating N—C—C—N moieties of amino acids that are covalently linked to form a peptide polymer.
As used herein, the term “interface” means the point or surface at which two or more domains of one or more molecules associate with each other.
As used herein, the term “GAR” refers to the region of the ribosome responsible for activating the GTPase activity of translation elongation factors. The term “GAR RNA” refers to nucleotides 1051 to 1108 of E. coli 23S rRNA or to its functional and structurally equivalent from any other bacterial rRNA. As used herein, GAR RNA refers to the nucleotides including and limited to (i.e., an RNA molecule consisting of GAR RNA) nucleotides 1051 to 1108 of E. Coli 23S rRNA (or the functionally and structurally equivalent region in other bacterial rRNAs); or it refers to that nucleotide region (1051 to 1108) within a longer nucleotide sequence (i.e., an RNA molecule consisting essentially of GAR RNA) where the GAR RNA (nucleotides 1051 to 1108) is the only active region in the longer sequence (in terms of binding and/or another activity), whether the extra sequence be a homologous sequence from the 23S rRNA (short of the complete sequence) or a heterologous sequence; or it refers to the 1051 to 1108 region within a complete functional 23S rRNA (i.e., an RNA molecule comprising the GAR RNA).
As used herein, the term “L11/GAR” refers to the portions of L 11 and GAR RNA which, when engaged in a complex, provide the L11/GAR binding site and/or activity, and preferably both the binding site and the activity. The term “L11/GAR” refers to a complex which consists of the ribosomal protein L11 and consists of the GAR RNA (nucleotides 1051 to 1108) in their native association; or it can refer to a complex consisting essentially of ribosomal protein L11 and consisting of or consisting essentially of or comprising GAR RNA (i.e., including other proteins which are inactive or do not otherwise affect the activity of the L11/GAR complex; or it can refer to a complex comprising ribosomal protein L11 and consisting of, consisting essentially of, or comprising GAR RNA. When ribosomal protein L11 is referred to, the complete protein is referred to; however, where an L11/GAR activity is referred to, the portion of L11 sufficient to provide the activity when associated in a complex with GAR ma be less than the complete L11 protein; “portion” referring to those combined L11 residues which provide for L11/GARcomplex formation and activity, the portions being one or more of the N-terminal, C-terminal or tether regions, as defined herein, or ant combination thereof.
“L11/GAR activity” may include one or more of the following: movement of the N-terminal lobe of L11; binding or displacement of thiostrepton or micrococcin; RNA translation, translation elongation, inhibition of amino acid addition, GTPase activity, and/or inhibition of elongation factor G (EF-G)-dependent GTP hydrolysis.
As used herein, the term “known L11/GAR binding activity” refers to an activity known in the art to associate with the L11/GAR either in vitro or in vivo. Known L11/GAR binding activities include, but are not limited to, the binding of agents such as thiostrepton and micrococcin.
As used herein, “stem loop” refers to a stretch of nucleic acid sequence on a single molecule comprising two lengths of sequence capable of forming hydrogen bonded base pairs with each other separated by a region which cannot participate in the same base pairing interaction, such that base pairing between the sequences capable of forming hydrogen bonded base pairs forms a loop of non-base paired nucleic acid consisting of the region which cannot participate in base pairing.
As used herein, the term “alpha helix” refers to a secondary structure arrangement of amino acids wherein hydrogen bonding between the C═O group of one peptide and the —NH group of the peptide bond four residues further down the same peptide polymer results in a right handed twist or helix formation.
As used herein, “four way junction” refers to a region in the tertiary structure of GAR RNA in which four helices interact simultaneously with each other, as defined by the crystal structure coordinates given in Table II.
As used herein, the term “translationally competent cell extract” refers to any fraction of a cell lysate, including a whole cell lysate, which is capable of directing the RNA-dependent polymerization of peptide bonds.
As used herein, the term “translatable RNA” refers to an RNA which, when incubated with factors necessary for translation can direct the synthesis of acid-precipitable protein.
As used herein, the term “decrease” when used in reference to a level of labeled RNA, a level of known L11/GAR binding activity, a level of translation, or a level of GTP hydrolysis means that the detected level is reduced by at least 10%, and preferably by 20% to 50% or more.
As used herein, the term “anti-bacterial properties” refers to the ability of a particular compound to inhibit the growth of bacteria. A compound can be said to have anti-bacterial properties if the rate of bacterial cell proliferation is reduced by at least 50%, and preferably by more than 50%.
As used herein, the term “naturally occurring amino acids” means the L-isomers of the naturally occurring amino acids. The naturally occurring amino acids are glycine (G, Gly), alanine (A, Ala), valine (V, Val), leucine (L, Leu), isoleucine (I, Ile), serine (S, Ser), methionine (M, Met), threonine (T, Thr), phenylalanine (F, Phe), tyrosine (Y, Tyr), tryptophan (W, Trp), cysteine (C, Cys), proline (P, Pro), histidine (H, His), aspartic acid (D, Asp), asparagine (N, Asn), glutamic acid (E, Glu), glutamine (Q, Gln), gamma-carboxyglutamic acid, arginine (R, Arg), ornithine and lysine (K, Lys). Unless specifically indicated, all amino acids referred to in this application are in the L-form.
As used herein, the term “unnatural amino acids” means amino acids that are not naturally found in proteins. Examples of unnatural amino acids used herein include racemic mixtures of selenocysteine and selenomethionine.
The term “positively charged amino acid” includes any naturally occurring or unnatural amino acid having a positively charged side chain under normal physiological conditions. Examples of positively charged naturally occurring amino acids are arginine, lysine and histidine.
The term “negatively charged amino acid” includes any naturally occurring or unnatural amino acid having a negatively charged side chain under normal physiological conditions. Examples of negatively charged naturally occurring amino acids are aspartic acid and glutamic acid.
The term “hydrophobic amino acid” means any amino acid having an uncharged, nonpolar side chain that is relatively insoluble in water. Examples of naturally occurring hydrophobic amino acids are alanine, leucine, isoleucine, valine, proline, phenylalanine, tryptophan and methionine.
The term “hydrophilic amino acid” means any amino acid having an uncharged, polar side chain that is relatively soluble in water. Examples of naturally occurring hydrophilic amino acids are serine, threonine, tyrosine, asparagine, glutamine, and cysteine.
As used herein, a “competitive” inhibitor is one that inhibits GAR activity by binding to the same kinetic form of the GAR as its accessory factors bind—thus directly competing with the accessory factors for the active site of the GAR. Competitive inhibition can be reversed completely by increasing the accessory factor concentration.
As used herein, the term “kinetic form” of the GAR means the condition of the GAR when either bound to an accessory factor or not, and in either its active or inactive state. That is, a kinetic form can be any conformation the GAR can assume under physiological conditions.
As used herein, the term “accessory factor” means an endogenous factor or protein that interacts with the L11/GAR. As used herein, EF-G is included in the term “accessory factor”.
As used herein, an “uncompetitive” inhibitor is one that inhibits GAR activity by binding to a different kinetic form of the GAR than do the accessory factors. Such inhibitors bind to GAR already bound with the accessory factor and not to the accessory factor-free GAR. Uncompetitive inhibition cannot be reversed completely by increasing the accessory factor concentration.
As used herein, the term “co-complex” means L11 protein in covalent or non-covalent association with GAR RNA. As used herein, a co-complex may also encompass accessory factors and/or inhibitors or activators complexed with L11 or L11/GAR RNA.
As used herein, the terms “associates with” or “interacts with” refers to a condition of proximity between a chemical entity or compound, or portions thereof, with another chemical entity, compound or portion thereof. The association or interaction may be non-covalent—wherein the juxtaposition is energetically favored by hydrogen bonding or van der Waals or electrostatic interactions—or it may be covalent.
The term “beta-sheet” refers to the conformation of a polypeptide chain stretched into an extended zig-zig conformation. Portions of polypeptide chains that run “parallel” all run in the same direction. Polypeptide chains that are “antiparallel” run in the opposite direction from the parallel chains.
As used herein, the term “target” means a region of the L11/GAR complex, as defined by the crystal structure coordinates of Table II, which when bound by a candidate inhibitor or activator results in inhibition or activation of L11/GAR function.
As used herein, the term “modulate” refers to a change, either an increase or a decrease in some activity.
As used herein, the term “modulator” means a compound that modulates some activity.
As used herein, the term “inhibits” or “decreases” means that a candidate modulator reduces the activity of the L11/GAR. A candidate modulator may be said to inhibit or decrease activity if the activity of L11/GAR as measured by inhibition of GTP hydrolysis and/or translational activity is reduced by more than 50% in the presence of 50 uM or less of inhibitor compared to values obtained in the absence of inhibitor. Candidate modulators will preferably inhibit by more than 50% the presence of 10 uM or less of inhibitor and most preferably in the presence of 1 uM or less of inhibitor.
As used herein, the term “activates” or “increases” means that a candidate modulator raises the activity of the L11/GAR. A candidate modulator may be said to activate or increase activity if the activity of L11/GAR as measured by an increase of GTP hydrolysis by more than 50% in the presence of 50 uM or less of activator compared to values obtained in the absence of activator. Candidate modulators will preferably activate by more than 50% in the presence of 10 uM or less of inhibitor and most preferably in the presence of 1 uM or less of inhibitor.
As used herein, the term “structure coordinates” refers to mathematical coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of an L11/GAR RNA complex in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are used to establish the positions of the individual atoms within the unit cell of the crystal.
As used herein, the term “heavy atom derivatization” refers to the method of producing a chemically modified form of a crystal of L11/GAR RNA. In practice, a crystal is soaked in a solution containing heavy metal atom salts, or organometallic compounds, e.g., methyl mercury nitrate, lead chloride, gold thiomalate, thimerosal or uranyl acetate, which can diffuse through the crystal and bind to the surface of the protein. The location(s) of the bound heavy metal atom(s) can be determined by X-ray diffraction analysis of the soaked crystal. This information, in turn, is used to generate the phase information used to construct three-dimensional structure of the protein or protein:RNA complex (Blundel, T. L. and N. L. Johnson, 1976, Protein Crystallography, Academic Press).
Those of skill in the art understand that a set of structure co-ordinates determined by X-ray crystallography is not without standard error. For the purpose of this invention, any set of structure coordinates for an L11/GAR RNA complex that has a root mean square deviation of protein backbone atoms (N, Cα, C and O) of less than 0.75 when superimposed on the structure coordinates of Table II, using backbone atoms, shall be considered identical.
The term “unit cell” refers to a basic parallelipiped shaped block. The entire volume of a crystal may be constructed by regular assembly of such blocks. Each unit cell comprises a complete representation of the unit of pattern, the repetition of which builds up the crystal. Using the structure coordinates of the L11/GAR RNA complex provided by this invention, molecular replacement may be used to determine the structure coordinates of a crystalline mutant or homologue of the L11/GAR RNA complex or of a different crystal form of the L11/GAR RNA complex.
Detailed Description of the High Resolution Structure of the L11/GAR Complex
The GAR RNA from the T. maritima 23S rRNA consists of nucleotides 1111-1168, which correspond to nucleotides 1051-1108 in the E. coli sequence. Hereafter, the E. coli numbering will be used in order to facilitate comparison with the available biochemical and genetic data. As described in detail in Example 1, crystals of the GAR RNA complexed with ribosomal protein L11 from T. maritima were prepared and used to solve the structure to 2.6 Å resolution using multi-wavelength anomalous diffraction on a mercury derivative of the crystal. Data collection, phasing and refinement statistics are shown in Table I. The asymmetric unit in the crystal consists of two 1:1 L11-RNA complexes stacked in a head-to-head manner. The two complexes are nearly identical except for a subtle bend in the terminal three base pairs of the RNA, and a difference in the degree of disorder of the two L11 N-terminal domains. Several observations strongly suggest that the conformation observed in the crystal structure is extremely similar to the structure of the GAR in situ in the ribosome. The RNA contains all of the predicted secondary structure; the two complexes in the asymmetric unit are virtually identical; and, most significantly, the structure explains most of the large body of experimental data on this system.
Structure of the GAR RNA
The predicted secondary structure of the GAR RNA (Glotz et al., 1981; Noller et al., 1981) is almost identical to that derived from the crystal structure (FIG. 1a). The RNA secondary structure contains four double-helical segments, referred to as the terminal stem (defined by nucleotides (nt) 1051-1056 base paired with nt 1103-1108), the 1067 stem-loop (defined by nt 1062-1076), the 1082 hairpin (defined by nt 1082-1086) and the 1095 stem-loop (defined by nt 1090-1101).
In the tertiary structure, the terminal stem stacks on the 1095 stem-loop, and the 1067 stem-loop stacks on the 1082 hairpin. Thus the four double-helical segments stack pairwise to form two extended helical subdomains. These two subdomains have irregular yet complementary shapes, so that the entire GAR RNA folds into a single compact globular domain (FIGS. 1b, c). The helical subdomains associate in a roughly parallel fashion, with the terminal stem packed against the 1082 hairpin, and the 1067 and 1095 stem-loops packed against each other. Bulged-out residues in the 1067 and 1095 stem-loops mediate long-range tertiary interactions between the two subdomains. The fold requires two sharp turns in the backbone at the 1056-1057 and 1086-1087 phosphodiester linkages in the center of the junction, where the chain crosses over from one helical subdomain to the other. The molecule also contains a relatively large number of well-ordered metal ions that are integral to the
A Ribose Zipper Joins the Terminal Stem and the 1082 Hairpin
The association of the terminal stem with the 1082 hairpin occurs via their minor grooves. This rather intimate packing is stabilized primarily by a dense network of hydrogen bonds between the riboses of nucleotides A1084-A1086 and C1104-A1106 (FIG. 2a). A similar structural motif has been observed in the P4-P6 domain of the group I intron, and has been referred to as a ribose zipper (Cate et al., 1996). At the center of the four-way junction, the 2′ OH of A1086 appears to be a particularly crucial component of the ribose zipper. It makes hydrogen bonds to A1103 N1 and G1056 2′OH, and also directly ligates a crucial central cadmium ion (see below). A1086 has an unusual syn conformation that is necessary for the very tight packing of its sugar against the G1056-A1103 pair, and for the reverse-Watson-Crick geometry of the U1082-A1086 pair (FIG. 2c). Another noteworthy feature of the ribose zipper is a minor groove A-(G-C) triple involving nucleotides A1085, G1055 and C1104 (FIG. 2c). This minor-groove triple has also been found previously in large RNA tertiary folds (Cate et al., 1996; Ferre-D'Amare et al., 1998).
Intimate Association of the 1067 and 1095 Stem-loops by Reciprocal Donation of Bulges
The interaction between the 1067 and the 1095 stem-loops occurs primarily in their major grooves and is mediated largely by a reciprocal donation of highly conserved bulged-out bases. This unusually intimate major-groove packing is the primary reason for the compactness of the overall fold, and it requires substantial distortions from regular helical geometry. This portion of the structure contains a large number of tertiary interactions, some of which are novel structural motifs.
The 1095 stem donates a bulged-out base, A1088, to a pocket created by a distortion in the 1067 stem (FIG. 1). A1088 forms a universally conserved reverse-Hoogsteen pair with U1060 (FIG. 2c). Because of steric constraints, A1088 must be in the syn conformation, which together with the reverse-Hoogsteen pairing geometry requires that U1060 must be flipped over. The inversion of U1060 is in turn facilitated by bulging out of the base of U1061. This inversion-bulge, or S-turn motif, has an S-shaped backbone conformation that has been observed previously (Szewczak et al., 1993; Wimberly, 1994; Wimberly et al., 1993). The insertion of A1088 also requires that residues A1077 and U1078 are unpaired and rotated out to open up the pocket. The unpaired conformation of these residues is stabilized by three hydrogen bonds to the sugar-phosphate backbone of the 1095 stem loop at A1088 and G1089. Two of these hydrogen bonds are to the base of A1077 which explains its universal conservation.
The reciprocal donation of a bulge from the 1067 stem-loop to the 1095 stem involves nucleotides G1071 and C1072, which form two novel interdomain base triples with the base pairs G1091-C1100 and C1092-G1099 respectively (FIGS. 2b, c). Within the 1095 stem loop, nucleotides G1089-(U1090-U1101) also form a triple (FIG. 2c), with G1089 acting as a stacking platform for the other two triples (FIG. 2b). The stacking of G1071 on G1089 is further stabilized by hydrogen bonds between the 1089 2′ OH and 1071 N3, and between the 1071 2′ OH and the 1089 phosphate. These three base triples explain the sequence conservation of all these residues. The 1072-(1092-1099) triple was previously predicted and subsequently experimentally confirmed, although the geometry proposed for the triple (Conn et al., 1998) differs from that seen in the crystal structure.
The 1067 and 1095 Hairpin Loops
The highly conserved 1067 hairpin loop consists of two parts, a hairpin portion (U1066-A1069) that stacks on the sheared U1065-A1073 pair, and a three-nucleotide bulge (A1070-C1072) that participates in two different long-range tertiary interactions. The hairpin portion has a conformation commonly found in small hairpin loops, with a U-turn motif (Quigley and Rich, 1976) at U1066 and regular stacking of A1067-G1068-A1069. A1069 stacks on A1073, and its 2′ OH hydrogen bonds to the N3 of U1065, thereby stabilizing the location of the 1069 sugar as well as the sheared geometry of the U1065-A1073 pair. The three-nucleotide bulge has a corkscrew-like conformation in which A1070 is bulged to one side, and G1071 and C1072 are bulged into the major groove of the 1095 stem-loop. A1070 makes a novel long-range stacking interaction with U1061 which will be referred to herein as a “high-five” motif (FIG. 2b), while 1071 and 1072 participate in the long-range base triples described above. The high-five motif makes several hydrogen-bonding and van der Waals interactions with the 1095 hairpin loop, thereby stabilizing the relative orientations of the two hairpins.
The 1095 hairpin loop is also very highly conserved, and has a regular conformation stabilized by a U-turn at U1094 and a sheared G1093-A1098 pair. Part of the base of G1093 stacks over the base of C1072, so that the long-range base triples are tightly wedged between an overhang from the sheared G-A pair on one side, and the G1089-(U1090-U1101) triple on the other side. The structure of the 1095 hairpin loop is very similar to an NMR-derived structure of a small stem-loop containing the same hairpin loop sequence (Fountain et al., 1996). The structural basis for the very high sequence conservation of several of the residues in the 1095 hairpin loop (i.e. A1095, A1096 and U/C1097) is not completely clear, but it may arise from interactions with the N-terminal domain of L11 (see below) or with other components of the ribosome.
Metal Ion Interactions with RNA
Three cadmium ions and at least seven magnesium ions are visible in the experimental electron density map. One of the cadmium ions stabilizes the association of the two complexes in the asymmetric unit, but the other two are integral to the RNA structure, and these two sites are probably occupied by magnesium ions in vivo. Most of the ions mediate the close approach of phosphates in the interacting major grooves of the 1067 and 1095 stems, and five of these ions stabilize the location and conformation of the 1070-1072 bulge between the 1067 and 1095 stems (FIG. 3a). A cadmium ion occupies a crucial location at the center of the four-way junction, where it makes either direct or water-mediated contacts with residues from all four double-helical stems (FIG. 3b). This ion appears to stabilize both of the sharp turns at the center of the junction, i.e. the 1056-1057 and 1086-1087 turns, and thereby plays an important role in determining the overall structure of the four-way junction.
Despite the accelerating pace of RNA structure determination, extremely little is known about RNA tertiary structure because only about five RNA folds have been determined. The crystal structure of the GAR RNA reveals an unexpectedly complex and compact fold that contains both well-known and novel structural motifs. The GAR RNA is in fact the most compact RNA structure yet reported, exposing only 138 Å2 of solvent accessible surface area per nucleotide (Nicholls et al., 1991). This extreme compactness is a result of extensive tertiary interactions along the entire length of the structure, in both the major and minor grooves. The other relatively compact known RNA folds exhibit primarily minor-groove packing (e.g., the P4-P6 domain of the group I intron) or primarily major-groove packing (e.g., tRNA), and are therefore less efficiently folded. It is probable that very efficient packing of RNA will be found to be common in the ribosome.
The crystal structure explains the molecular basis for a number of important mutagenesis results. In particular, the RNA residues most sensitive to mutation are involved in tertiary interactions. For example, mutation of any of the universally conserved residues within the A1085-G1055-C1104 triple, a crucial part of the ribose zipper joining the terminal stem and the 1082 hairpin, dramatically destabilizes the RNA structure and greatly reduces the affinity for L11 (Lu and Draper, 1995). Mutation of C1072 to U within the 1072-(1092-1099) triple destroys the RNA tertiary structure, which demonstrates the energetic importance of this triple. Finally, the unusual observation that U1061A and U1061G mutants are more stable (Lu and Draper, 1994; Lu and Draper, 1995) is explained by the 1061-1070 “high five” tertiary stacking motif, since purine stacking is more stable than pyrimidine stacking.
Stabilization of the RNA Tertiary Structure by Metal Ions
The crystal structure also reveals important new information about how metal ions interact with and stabilize unusual RNA structures. Biochemical experiments suggest that the GAR RNA contains relatively high affinity binding sites for two divalent cations (Bukhman and Draper, 1997) and one K+ or NH4+ ion (Wang et al., 1993). The crystal structure reveals no fewer than seven magnesium sites and two cadmium sites, most of which stabilize the close approach of phosphates in the interacting major grooves of the 1067 and 1095 stem-loops. The metal-ion stabilization of the 1070-1072 bulge conformation is qualitatively similar—though different in detail—to that seen in the A-rich bulge of the P4-P6 domain of the group I intron (Cate et al., 1996). The striking structural role played by the central cadmium ion suggests that this site corresponds to one of the thermodynamically important ions. While more experiments will be necessary to test this hypothesis, it is worth noting that this cadmium ion is one of the two sites in the structure that ligates a guanosine N7. Both Mn++ and Cd++ preferentially bind to guanosine N7, and it has been observed that Mn++ stabilizes the tertiary structure more than other divalent cations (Bukhman and Draper, 1997).
The Major-groove Dinucleotide Platform: a Generalization of the Adenosine Platform
The crystal structure also reveals a new variant of a known tertiary structure motif, the adenosine platform. In the structure of the P4-P6 domain, two successive adenines adopt a coplanar conformation—an adenosine platform—that serves as a stacking platform for a long-range tertiary interaction (Cate et al., 1996). In the GAR structure, two successive nucleotides, G1089 and U1090, adopt the same conformation seen in the adenosine platform (FIG. 2C). The two bases are coplanar, with a single N2-O4 hydrogen bond between them, and they also serve as a stacking platform, for the 1071-1072 bulge involved in base triples (FIG. 2B). There are, however, some differences between the GU platform seen here and the AA platform. In the P4-P6 structure, the motif is displayed in the minor groove rather than in the major groove, as is seen here. Moreover, in the P4-P6 structure it is the 3′ adenosine upon which the long-range stacking interaction occurs, while here G1071 rests upon the 5′residue of the motif, G1089. Finally, the tertiary stacking interaction occurs on opposite faces of the motif in the two structures. Despite these differences, the near-identity of the conformations and functions of the motifs in these two structures leads to the suggestion that the motif be referred to as a “dinucleotide platform”, since it is clearly not restricted to adenosines. The few available data suggest that a GU dinucleotide platform may generally be more stable than an AA platform for major groove display. In the GAR, residues 1089 and 1090 are strictly conserved as either GU or AA, but mutation from AA to GU results in a significant stabilization of the RNA tertiary structure (Lu and Draper, 1994; Lu and Draper 1995). The major-groove GU dinucleotide platform motif has also been found in small RNA structures lacking tertiary interactions (Szewczak et al., 1993; Wimberly et al., 1993), which suggests that in large structured RNAs, the GU dinucleotide platform may in some cases function as a pre-formed stacking platform supporting major-groove base triples.
Methylmercury as a Phasing Vehicle for RNA Crystal Structures
Surprisingly, the primary mercury site used in phasing is not near a cysteine of L11, but is located 2.4 Å from the N3 atom of U1061, consistent with a covalent mercury-uridine N3 bond. A similar, minor mercury site at U1078 is also visible in the anomalous difference Fourier map. Although most mercury adducts of pyrimidines have been obtained at the O4 or 5 positions of the base, a mercury 1-methylthymine adduct at N3 has been obtained at alkaline pH (Kosturko et al., 1974), and methylmercury salts have been shown to denature AT-rich DNA, consistent with reaction at thymine N3 (Gruenwedel and Davidson, 1966; Gruenwedel and Davidson, 1967). Uracil is often preferred at bulge sites in RNA, so many larger RNA structures may contain solvent-accessible uracils. Therefore, methylmercury derivatization of RNA under native conditions, either prior or subsequent to crystallization, may be a generally useful method for obtaining heavy atom derivatives of RNA crystals, without the laborious incorporation of sulfur-containing ribonucleotides.
The Structure of Ribosomal Protein L11
Ribosomal protein L11 consists of two globular domains connected by a linker region. The secondary structure and a sequence alignment of the protein are shown in FIG. 4a, and the tertiary fold is shown in FIGS. 4b and 4c in the context of the complex. As described below, there is some flexibility between the two domains, but the linker is short and it contains two conserved prolines (73 and 74) that provide inherent rigidity. Also, the domain interface consists primarily of conserved hydrophobic residues, notably Met52, Ile53, Pro55, Pro73 and Phe77. These observations suggest that relative orientation of the two domains has not been greatly perturbed by crystal packing requirements.
The structure of the L11 N-terminal domain (NTD) has not been previously reported. It consists of two helices packed against the concave surface of a three-stranded antiparallel beta sheet, with an overall β1-α1-α2-β2-β3 topology. The N-terminal 7 residues are disordered. One of the most distinctive and conserved regions of the L11 molecule is the proline-rich helix 1, which appears to have a crucial functional role, as described below. The electron density for this helix was weak, and the register of the sequence in this helix may be in error by one residue. The average main-chain B-factor for the domain is 72 Å2 (for comparison, the average B-factor of the C-terminal domain (CTD) is 24 Å2), indicating rigid body movement of the NTD within the crystal. This flexibility is consistent with the rather limited interactions seen between the NTD and other parts of the structure, and may have functional implications (see below).
The structure of the CTD is in good agreement with the previously determined NMR structures of the CTD, both in isolation (Markus et al., 1997; Xing et al., 1997) and in the context of the L11-RNA complex (Hinck et al., 1997). The domain consists of a three-helical bundle and a short parallel two-stranded β-ribbon, with an overall α3-β4-α4-α5-β5 topology. All five secondary structure elements contribute to a conserved hydrophobic core. The domain is characterized by two extended loops that are disordered in the absence of the RNA, but which have defined structures in the complex.
The RNA-protein Interaction
The two domains of L11 are very unequally associated with RNA. The CTD-RNA interface covers over 1700 Å2 of solvent accessible surface area, while the NTD-RNA interface is less than 100 Å2. This difference is consistent with the observation that the RNA-binding affinity of the CTD is essentially the same as that of the full-length protein (Xing and Draper, 1996).
The CTD binds the minor groove of the 1067 stem (FIGS. 4b, c), which is bent and flatter than the minor groove of a canonical A-form double helix. The RNA-binding surface of the CTD consists of one face of helix 5, the N-terminal end of helix 3, and loops 6 and 7 that flank helix 5. Helix 5 is positioned lengthwise in the minor groove, and the flanking loops 6 and 7 extend this minor groove binding surface and also interact with the sugar-phosphate backbones on either side of the groove. A summary of the CTD-RNA interactions observed in the crystal structure (FIG. 5a) emphasizes that the recognition of the RNA minor groove by L11 involves primarily interactions between the protein backbone and the RNA2′ OH moieties. Approximately half of the RNA-CTD hydrogen bonds involve a main-chain amide or carbonyl, and over half of the 2′OH groups in the CTD footprint are hydrogen-bonded to the protein. This preponderance of protein backbone-RNA backbone interactions indicates that overall shape complementarity between the RNA and protein must be an important determinant of specificity.
Although binding appears to depend less on electrostatic interactions than on shape complementarity, there are a number of important salt bridges between basic sidechains and phosphate groups: lysines 93, 126 and 133 and Arg94 interact with one side of the minor groove, and lysines 80, 87 and 112 with the other side. In the former group, the sidechains are splayed away from protein, and the hydrophobic part of the sidechain contributes to surface complementarity with the RNA. Sidechains at the N-terminus of α5 and within loop 7 make particularly intimate contact with the RNA, notably Ile127 and Asn117. Asn117 points directly into the minor groove making a number of hydrogen bonding interactions, and is one of the few sidechains that formally “reads” the local RNA sequence. Two of the most important recognition elements in the RNA are the universally conserved long-range pair U1060-A1088 and the surrounding RNA internal loop that distorts to accommodate the insertion of A1088. Significantly, the RNA footprint of helix 5 encompasses this entire region of distorted RNA. The importance of the U1060-A1088 pair for L11 specificity is shown by the extremely high conservation of Gly130 and Thr131 to which these bases are hydrogen-bonded (FIG. 5b).
The NTD bridges the interface between the 1067 and 1095 stem-loops, and it makes only a few specific interactions with the RNA (FIG. 4). Although its association with RNA is somewhat tenuous, which might be a result of its binding mode having been altered by crystal packing requirements, the high sequence conservation of the NTD residues interacting with RNA suggests that the binding mode observed in the crystal structure is relevant to the structure of the complex in solution. Moreover, as described above, the structure of the NTD-CTD interface also suggests that the orientation of the NTD has not been greatly perturbed by crystal packing. The NTD residues interacting with RNA include Lys10, Gln12, Gln30 and Lys71. Lys10 makes both main-chain and side-chain interactions with the RNA, and Gln30 probably interacts specifically with A1095. There is also electron density interacting with the Watson-Crick face of C1097, but it is not clear whether this density arises from the NTD; examination of an anomalous difference Fourier map reveals that some of this density must correspond to a mercury or cadmium site. Finally, although the proline-rich sequence in helix 1 is surface-exposed, highly conserved, and in the correct orientation for possible interactions with factors or antibiotics, it is close to but not in direct contact with RNA.
The Thiostrepton/micrococcin Binding Site
A1067 and A1095, at the ends of their respective stem-loops, have both been implicated in the binding of the antibiotics thiostrepton and micrococcin. Modification of A1067 by 2′-O methylation (Cundliffe and Thompson, 1979; Thompson et al., 1982) or transversion mutations at either site (Rosendahl and Douthwaite, 1994) confers thiostrepton resistance. It has also been shown that thiostrepton affects the reactivity of both A1067 and A1095, suggesting that these two sites are close together (Rosendahl and Douthwaite, 1994) as indeed they are in the crystal structure. As for the role of L11 in antibiotic binding, it is known that L11 is required for high affinity binding of thiostrepton to the RNA, and that binding of L11 and thiostrepton to the RNA is cooperative. Thiostrepton has a much weaker affinity for the RNA alone (Kd=0.4 μM), and it does not bind isolated L11 (Thompson et al., 1979). Two sites within the NTD of the protein have been implicated in this interaction: the mutations Pro22Ser and Pro22Thr confer thiostrepton resistance, while the antibiotic protects Tyr61 (Tyr62 in E. coli) in protein footprinting experiments (Porse et al., 1998). Recently, mutations that confer resistance to micrococcin have also been mapped to the NTD of L11 between residues 22 and 32 (Porse et al., 1999). All of these sites are located on a small surface of the NTD, near A1067 and A1095 on the RNA (FIG. 6). A prominent feature of this surface is the distinctive and highly conserved proline-rich helix, while Tyr61 is over 20 Å distant. The clustering of these sites of antibiotic resistance mutations, together with the cooperative binding data, strongly suggest that the antibiotics bind to the cleft between the RNA and the proline-rich helix 1 of the NTD.
The structure of the C-terminal domain (CTD) was previously determined by NMR in both the free (Markus et al., 1997; Xing et al., 1997) and RNA-bound (Hinck et al., 1997) forms. Our crystal structure of the CTD is similar to that of the RNA-bound form determined by NMR, except for the conformation of the large RNA-binding loop 6 which is poorly determined in the NMR studies (Hinck et al., 1997). The mean Cα root mean square difference (RMSD) for the crystal structure vs. NMR ensemble is 2.7 Å overall, or 1.6 Å when residues 86-97 of loop 6 are excluded. For comparison, the mean RMSD within the ensemble of NMR structures is 2.3 Å for main chain atoms.
Many ribosomal proteins show structural similarities to families of DNA- and RNA-binding proteins (Ramakrishnan and White, 1998). It was noted from the NMR structure that the CTD of L11 has a homeodomain-like fold (Markus et al., 1997; Xing et al., 1997), and further NMR studies on the complex suggested that the CTD uses the typical homeodomain helix to bind RNA (Hinck et al., 1997). Although the crystal structure reveals that this helix is indeed intimately associated with the RNA, its interaction does not bear any similarity to the base-specific recognition of a major groove by the homeodomains. Regarding the NTD, its overall α+β fold is similar to that seen in many other RNA-binding proteins (Ramakrishnan and White, 1998), but its β-α-α-β-β topology has not yet been observed in an RNA-binding protein.
RNA-protein Interaction
The L11-GAR RNA interaction has been probed by biochemical and NMR methods, and the crystal structure is in good agreement with the results of these studies, including a rather weak interaction between the RNA and the NTD. The RNA surface covered by the CTD corresponds fairly well to the residues protected by the binding of full-length L11 as shown by hydroxyl radical footprinting experiments (Rosendahl and Douthwaite, 1993). The RNA-binding surface of the CTD has been mapped by NMR chemical shift changes and relaxation studies (Hinck et al., 1997), and again the agreement with the crystal structure is excellent. The observation that L11 recognizes the RNA primarily by shape complementarity rather than by a sidechain-base reading of the RNA sequence is not surprising considering that the interaction occurs primarily via the minor groove. The interaction agrees with the prediction that relatively few highly conserved CTD residues would make specific sidechain contacts with RNA (Xing et al., 1997). However, the related prediction that RNA binding by the CTD would not involve extensive recognition of the RNA bases is incorrect, as most of the base pairs are recognized by either hydrogen bonding or hydrophobic interactions. However, most of these hydrogen bonds occur via main chain amides or carbonyls, rather than side chains. Finally, it is worth noting that L11 does not directly recognize the bulged-out nucleotides, which have previously been proposed as specificity determinants in ribosomal RNA-protein complexes.
Biochemical experiments have shown that L11 stabilizes the tertiary structure of the RNA, and that this is a property of the CTD (Draper and Xing, 1995; Xing and Draper, 1995). Since nearly all of the direct RNA-protein contacts within the complex are to the 1067 stem, the resulting stabilization of the RNA tertiary structure appears to be indirect. The binding of one face of helix 5 with both strands of the 1067 stem is extensive and universally conserved, and this interaction must be particularly important for stabilization of the RNA tertiary structure. Consistent with a crucial role in RNA binding, helix 5 contains most of the mutation sites that have the greatest adverse effect on binding affinity (T131V, G130A, K126A, and S134A) (Xing et al., 1997). As for the RNA-binding loops 6 and 7, both are disordered when not bound to RNA (Markus et al., 1997), but they are highly ordered in the complex, and their conformations match the groove surface perfectly. The loops contain conserved structural features, which are important in the complex and which may predispose them for RNA-binding. Although it makes many interactions with RNA and contains the other two sites most sensitive to mutation (G88P and P92G), the longer RNA-binding loop 6 is relatively poorly conserved between kingdoms, with the bacterial and archaeal loops differing significantly from the eukaryotic loops (FIG. 4A). This variability in the protein sequence correlates with variability between phylogenetic kingdoms in the base-pairing of the upper portion of the 1067 stem.
The NTD as a Molecular Switch
Prior to these structural studies, the molecular basis for cooperative binding within the RNA-L11-thiostrepton ternary complex was unknown. The crystal structure now provides a very straightforward explanation that also rationalizes the particular importance of the L11 NTD. The model also provides insights into how the GAR might function as a molecular switch.
The putative thiostrepton/micrococcin binding site is centered on a small gap between helix 1 of the NTD and the 1067/1095 region of the RNA (FIG. 6). The antibiotics are proposed to bind within this gap, possibly enlarging it somewhat, making specific interactions with the RNA on one side and further interactions with the NTD on the other side. In the absence of the NTD, the antibiotic's binding affinity would be greatly compromised, thus explaining the importance of the NTD for antibiotic binding (Xing and Draper, 1996). An alternative proposal, that thiostrepton binds directly only to the RNA and that this RNA conformation requires the presence of the NTD, is unlikely because the NTD does not appear to stabilize the RNA tertiary structure significantly, and because the NTD sites of resistance mutations are not in contact with the RNA. In a model that better accounts for previously known data and agrees with the crystal structure reported herein, the mechanism for the resistance to thiostrepton in Pro22 mutants would be a disruption of direct thiostrepton-Pro22 interaction. A similar mechanism must hold true for the micrococcin sites given the more recent data (Porse et al., 1999). Regarding the details of the interaction of thiostrepton and micrococcin with RNA, we note that these antibiotics contain an array of thiazole rings that resembles the array of prolines in the conserved proline-rich NTD helix.
The data disclosed herein suggests a potential mechanism of thiostrepton inhibition of factor-dependent GTPase activity involves restriction or “trapping” of one of the many conformational states that must occur during elongation (Cundliffe, 1986) by the antibiotic. In their analysis of the effects of the Pro22Ser and Pro22Thr mutations, Porse et al. (1998) suggest that thiostrepton binding may affect the ability of the L11 NTD to undergo a conformational change, an idea which merits closer examination in light of the crystal structure. In the structure, the CTD is rather firmly anchored to one of the two RNA subdomains, while the NTD is somewhat tenuously bound across the RNA subdomain-subdomain interface. Even in the absence of other data, this overall architecture suggests that the NTD may function as a molecular switch that reversibly associates with the GAR RNA during the elongation cycle. In light of the other data—in particular the cooperative binding of thiostrepton and full-length L11 to RNA, and the clustering of antibiotic resistance mutations to the cleft defined by A1067/A1095 and the proline-rich NTD helix—it appears even more likely that the NTD functions as a molecular switch, and that the thiazole antibiotics work by binding to the NTD-RNA interface, thereby preventing the NTD from switching between RNA-bound and RNA-free states. It is possible that the switch is coupled to, or triggered by, the binding of elongation factors. It is important to note that the NTD itself cannot provide the actual GTPase enhancing activity since L11 is not required for viability in E. coli (Stöffler et al., 1980). Therefore, the switch appears likely to function by controlling either the accessibility or the conformation of the GAR RNA.
This switch hypothesis could also explain why EF-Tu and IF2 do not footprint the 1067/1095 region of RNA, while EF-G does, even though all these factors interact with the sarcin/ricin loop (Moazed et al., 1988). The sarcin/ricin loop is known to bind to a nearby (Wilson and Noller, 1998) but distinct (Munishkin and Wool, 1997) site on EF-G. The EF-Tu-tRNA complex is similar in structure to EF-G, and the similarity is thought to be a case of molecular mimicry, with the factors binding to the same general region of the ribosome (Nissen et al., 1995). Thus the footprinting differences could be explained if EF-Tu and IF2 recognize a different conformation of the switch than EF-G does. This reasoning suggests that the two conformations of the GAR molecular switch correspond to different functional states of the ribosome.
The structure features a complex and very compact RNA fold stabilized by many bound metal ions, by a dense network of RNA tertiary interactions, and by extensive interactions with the protein. The overall architecture of the complex suggests that the N-terminal domain functions as a molecular switch, either by facilitating changes in the tertiary structure of the GAR RNA, or by controlling access to the RNA. Thiostrepton and micrococcin are proposed to bind to the NTD-RNA interface, thus locking the switch and disrupting GAR function.
Uses of the Crystal Structure Coordinates of the L11/GAR Complex
One approach enabled by the X-ray crystal structure disclosed herein is the use of the crystal coordinates for the rational design of GAR activity modulators, either de novo or by modification of known compounds. The modulators identified through use of the crystal structure coordinates will be useful for altering the rate of bacterial protein synthesis, and thereby the rate of bacterial cell growth. It is expected that, for example, an inhibitor of GAR function will inhibit bacterial cell proliferation, and will thus potentially have immediate medical usefulness.
One of skill in the art may use the structure data disclosed herein and the computer-modeling techniques described herein to develop models of target domains also selected through analysis of the crystal structure data (see below). These models can be used to provide a detailed analysis of the binding surfaces, including factors such as van der Waals contacts, electrostatic interactions and hydrogen-bonding opportunities. This information is then used with computer simulation techniques to map the favorable interaction positions for functional groups such as protons, hydroxyl groups, amine groups, divalent cations, aromatic and aliphatic functional groups, acetamide, methanol, etc. These groups may then be designed into a synthetic ligand.
The L11/GAR structure coordinates may be used to screen computationally small molecule data bases for chemical entities or compounds that may bind in whole, or in part, to the L11/GAR, to GAR, or to L11.
In addition, because the L11/GAR RNA complex may be crystallized in more than one crystal form (e.g, as a co-crystal with another factor, such as EF-G), the structure coordinates of the L11/GAR RNA, or portions thereof, as provided by this invention are useful to solve the structure of those other crystal forms of the L11/GAR RNA complex. One method that may be employed for this purpose is molecular replacement. In this method, the unknown crystal structure (i.e., that of the co-complex) may be determined using the L11/GAR complex structure coordinates of this invention as provided in FIG. 7. This method will provide an accurate structural form for the unknown crystal more quickly and efficiently than attempting to determine such information from first principles.
In addition, in accordance with this invention, the L11/GAR complex may be crystallized in co-complex with known GAR inhibitors (e.g., thiostrepton, micrococcin). The crystal structures of such complexes may then be solved by molecular replacement and compared with that of inhibitor-free L11/GAR complex. Critical sites for interaction of the known inhibitor with the L11/GAR may thus be identified at high resoultion. This information provides an additional tool for determining the most efficient binding interactions, for example, increased hydrophobic interactions, between L 11/GAR and a chemical entity or compound.
All of the complexes referred to above may be studied using well-known X-ray diffraction techniques and may be refined versus 2-3 Å resolution X-ray data to an R value of about 0.20 or less using computer software, such as X-PLOR (Yale University, ©1992, distributed by Molecular Simulations, Inc.). See, e.g., Blundel & Johnson, supra; Methods in Enzymology, 1985, vol. 114 & 115, H. W. Wyckoff et al., eds., Academic Press. The crystallographic information disclosed herein may thus be used to optimize known classes of L11/GAR inhibitors or activators.
Importantly, the X-ray crystal data disclosed herein also allows the design and synthesis of novel classes of L11/GAR inhibitors or activators (i.e., modulators). The design of compounds that bind to or modulate L11/GAR function according to this invention generally involves consideration of several factors. In particular, the compound must be capable of physically and structurally associating with L11/GAR. Non-covalent molecular interactions important in the functional association of L11/GAR with its accessory factors include hydrogen bonding, van der Waals, electrostatic and hydrophobic interactions.
It is recognized that although certain portions of the compound will not directly participate in this association with the L11/GAR, those portions may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of the binding site, or the spacing between functional groups of a compound comprising several chemical entities that directly interact with L11/GAR.
The potential modulating or binding effect of a chemical compound on the L11/GAR may be analyzed prior to its actual synthesis and testing by the use of computer modelling techniques. If the theoretical structure of the given compound suggests insufficient interaction and association between it and the L11/GAR, synthesis and testing of the compound is obviated. However, if computer modelling indicates a strong interaction, the molecule may then be synthesized and tested for its ability to bind to the L11/GAR domain and to inhibit using the assays described herein. In this manner, synthesis of inoperative compounds may be avoided.
A modulating or binding compound of the L11/GAR may be computationally evaluated and designed by means of a series of steps in which chemical entities or fragments are screened and selected for their ability to associate with the individual binding targets on the L11/GAR.
One skilled in the art may use one of several methods to screen chemical entities or fragments for their ability to associate with L11/GAR and more particularly with the individual binding domains comprising the L11/GAR active sites. This process may begin by visual inspection of, for example, the active site on the computer screen based on the L11/GAR RNA coordinates in FIG. 7. Selected fragments or chemical entities may then be positioned in a variety of orientations, or “docked”, within an individual binding target site of the L11/GAR as defined herein from analysis of the crystal structure data. Docking may be accomplished using software such as Quanta (Molecular Simulations, Inc., San Diego, Calif.) and Sybyl (Tripos, Inc., St. Louis, Mo.) followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARMM (Molecular Simulations, Inc., San Diego, Calif.) and AMBER (University of California at San Francisco).
Specialized computer programs may also assist in the process of selecting fragments or chemical entities. These include:

    1. GRID (Goodford, P. J., “A Computational Procedure for Determining Energetically Favorable Binding Sites on Biologically Important Macromolecules”, J. Med. Chem., 28, pp. 849-857 (1985)). GRID is available from Oxford University, Oxford, UK.
    2. MCSS (Miranker, A. and M. Karplus, “Functionality Maps of Binding Sites: A Multiple Copy Simultaneous Search Method.” Proteins: Structure. Function and Genetics, 11, pp. 29-34 (1991)). MCSS is available from Molecular Simulations, San Diego, Calif.
    3. AUTODOCK (Goodseil, D. S. and A. J. Olsen, “Automated Docking of Substrates to Proteins by Simulated Annealing”, Proteins: Structure. Function, and Genetics, 8, pp. 195-202 (1990)). AUTODOCK is available from Scripps Research Institute, La Jolla, Calif.
    4. DOCK (Kuntz, I. D. et al., “A Geometric Approach to Macromolecule-Ligand Interactions”, J. Mol. Biol., 161, pp. 269-288 (1982)). DOCK is available from University of California, San Francisco, Calif.
    5. CERIUS II (available from Molecular Simulations, Inc., San Diego, Calif.).
    6. Flexx (Rarey et al., 1996, J. Mol. Biol. 261: 470-489).


Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound or modulator. Assembly may proceed by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of the L11/GAR. This would be followed by manual model building using software such as Quanta or Sybyl.
Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include:

    1. CAVEAT (Bartlett, P. A. et al, “CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules”. In “Molecular Recognition in Chemical and Biological Problems”, Special Pub., Royal Chem. Soc., 78, pp. 182-196 (1989)). CAVEAT is available from the University of California, Berkeley, Calif.
    2. 3D Database systems such as MACCS-3D (MDL Information Systems, San Leandro, Calif.). This area is reviewed in Martin, Y. C., “3D Database Searching in Drug Design”, J. Med. Chem., 35, pp. 2145-2154 (1992)).
    3. HOOK (available from Molecular Simulations Inc., San Diego, Calif.).


Instead of proceeding to build an L11/GAR modulator in a step-wise fashion one fragment or chemical entity at a time as described above, modulatory L11/GAR binding compounds may be designed as a whole or “de novo” using either an empty active site or optionally including some portion(s) of a known inhibitor(s). These methods include:

    1. LUDI (Bohm, H.-J., “The Computer Program LUDI: A New Method for the De Novo Design of Enzyme Inhibitors”, J. Comp. Aid. Molec. Design, 6, pp. 61-78 (1992)). LUDI is available from Molecular Simulations, Inc., San Diego, Calif.
    2. LEGEND (Nishibata, Y. and A. Itai, Tetrahedron, 47, p. 8985 (1991)). LEGEND is available from Molecular Simulations, San Diego, Calif.
    3. LeapFrog (available from Tripos Associates, St. Louis, Mo.).


Other molecular modelling techniques may also be employed in accordance with this invention. See, e.g., Cohen, N. C. et al., “Molecular Modeling Software and Methods for Medicinal Chemistry”, J. Med. Chem., 33, pp. 883-894 (1990). See also, Navia, M. A. and M. A. Murcko, “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2, pp. 202-210 (1992); Hubbard, “Can Drugs Be Designed?”, Curr. Opin. Biotechnol., 8, pp. 696-700 (1997); and Afshar et al., “Structure-Based and Combinatorial Search for New RNA-Binding Drugs”, Curr. Opin. Biotechnol., 10, pp.59-63 (1999).
Once a compound has been designed or selected by the above methods, the efficiency with which that compound may bind to L11/GAR may be tested and optimized by computational evaluation. For example, a compound may be optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target site. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the modulator and the enzyme when the modulator is bound to L11/GAR preferably make a neutral or favorable contribution to the enthalpy of binding.
Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include:

    Gaussian 92, revision C [M. J. Frisch, Gaussian, Inc., Pittsburgh, Pa. ©1992]; AMBER, version 4.0 [P. A. Kollman, University of California at San Francisco, ©1994];
    QUANTA/CHARMM
    [Molecular Simulations, Inc., San Diego, Calif. ©.1994]; and Insight II/Discover (Biosysm Technologies Inc., San Diego, Calif. ©1994). These programs may be implemented, for instance, using a Silicon Graphics workstation, 02-R10000 or IBM RISC/6000 workstation model 550. Other hardware systems and software packages will be known to those skilled in the art.


Once an L11/GAR-binding compound has been optimally selected or designed, as described above, substitutions may then be made in some of its atoms or side groups in order to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation should be avoided. Such substituted chemical compounds may then be analyzed for efficiency of fit to L11/GAR by the same computer methods described in detail, above.
Targets for Modification of L11/GAR Function
The X-ray crystal structure co-ordinates disclosed herein may be used to define structural features of the L11/GAR which represent targets for inhibition or activation of the GTPase activity of the ribosome. The following regions of the L11/GAR, defined by the X-ray co-ordinate data, represent particularly useful targets for the development of inhibitory or activating compounds.
1. L11 N Terminus:GAR RNA Interface
The putative site for binding of the antibiotics thiostrepton and micrococcin to the GAR is between the N terminus of L11 and the interface between the 1067 and 1095 stem loops of the GAR RNA. The structural data as disclosed in Table II and described herein above suggest that the N terminal lobe of L11 behaves as a rigid body that flexes about the so-called “tether sequence” between the C terminal and N terminal lobes of the protein. Therefore, the binding pocket is not limited to those residues at the interface of the L11 N terminus and the GAR RNA that are in direct contact. The binding pocket can include all of the following:
A) all exposed residues from the L11 N terminus;
B) all exposed residues from the GAR RNA that are on its L11 binding surface, including A1070, U1061, A1095, A1096, C1097, and A1098;
C) L11 amino acid residues that are in direct contact with the GAR RNA, including K10, Q12, Q30 and K71;
D) L11 amino acid residues from the helical region between P20 and H31; and
E) the L11 β sheet between Q8 and P14, and neighboring I53.
Computer simulation techniques may be used to determine which parameters of the binding pocket may be exploited in designing or screening compounds that interact with the binding pocket. Such techniques allow for the construction of structural models that can then be used in designing inhibitory/activating compounds targeted to the L11/GAR binding pocket. These techniques may involve any of the software packages described above or known in the art, and include:
A) Interactive movement of the L11 N terminus as a rigid body with concurrent geometry optimization, using, for example, Quanta.
B) Molecular dynamics simulation of the GAR RNA-L11 complex using. For example, CHARMM and/or AMBER.
C) Normal mode dynamics simulation of the GAR RNA-L11 complex using, for example, CHARMM.
D) Molecular docking of thiostrepton and/or micrococcin to the models of the binding pocket.
2. The L11 Flexible Tether or the Flexible Tether:GAR RNA Interface
The flexible tether domain of L11 and the GAR RNA surfaces that the tether domain interacts with are defined by the crystal structure coordinates disclosed in Table II and discussed herein above. The X-ray crystal data suggest that the L11 N terminus may act as a molecular switch that triggers the GTPase activity. It is thought that thiostrepton and micrococcin act by modifying the interaction between the L11 N terminus and the GAR RNA. Therefore, the region tethering the N terminal and C terminal lobes of L11, (i.e., amino acids K71 through A75) represent a target for the development of compounds that inhibit or activate GAR function, as does the domain comprising the interface of the tether region with GAR RNA residues. The GAR RNA domain interacting with the tether includes U1061, the backbone of U1060, and G1059. Any molecule that could modify the relative positioning of the L11 NTD and CTD may disrupt the funtion of the molecular switch and thereby modulate the function of the GAR. For example, this could be performed by a molecule interacting with the L11 tether domain and/or the GAR in close contact with the tether. Any molecule that could interact with both the C terminal and N terminal lobes of L11 and stabilize one orientation of the lobes relative to the alternate orientation may disrupt the function of the molecular switch and thereby disrupt the function of the GAR.
Computer simulation techniques similar to those described above for modeling the L11 N terminus:GAR RNA interface may be used to determine which parameters of the 4 way junction and Cd++ coordination site may be exploited in designing or screening compounds that interact with or disrupt the junction/Cd++ coordination site and/or modify the activity of the GTPase.
3. The GAR RNA:EF-G Interface
The interaction of translational elongation factor EF-G with the ribosome has been mapped by directed hydroxyl radical probing (Wilson & Noller, 1998, Cell 92: 131-139). This approach indicated that GAR RNA residues in the region of A1070 and in the region of C1100 are involved in the binding of EF-G. A1070 is included in the GAR RNA:L11 N terminal interface discussed as a target above, but is nonetheless of interest in approaches aimed at disrupting or modifying EF-G binding.
The crystal structure coordinates disclosed in Table II and discussed herein above define the structure of the GAR RNA at C1100, and the RNA bases and L11 amino acid residues around it. This structure defines a novel target for the design and/or selection of molecules that can disrupt the GAR RNA:EF-G interaction.
Computer simulation techniques similar to those described above for modeling the L11 NTD: GAR RNA interface may be used to determine which parameters of the binding pocket may be exploited in designing or screening compounds that modify the relative positioning of L11 NTD and CTD and modify the activity of the GTPase.
4. RNA Folding/Stability
The X-ray crystal structure coordinates disclosed in Table II and discussed herein above define the structure of a novel “4 way junction” fold in the ribosomal RNA in the L11/GARcomplex. The data further reveal the importance of a Cd++ ion that occupies the center of the four way junction between bases 1056-1057 and 1086-1087. Because a ligand that can modify the folding of the RNA would be predicted to disrupt or otherwise modify the GTPase activity, this folded RNA structure represents a strong target for development of inhibitors or activators of the GTPase. Because the Cd++ ion likely stabilizes the unusual RNA fold, the region defined by those amino acid and RNA residues interacting with the Cd++ ion is particularly attractive as a target.
5. The L11 C Terminus:GAR RNA Interface
The domain comprising the interaction surface of the C terminal lobe of L11 and the GAR RNA is defined by the crystal structure data disclosed in Table II (X-ray co-ord's) and is described herein above. The crystal data indicate that the C terminus of L11 interacts very tightly with the GAR RNA. As such, the interaction may be difficult to disrupt. Computer simulation techniques similar to those described above for modeling the L11 N terminus:GAR RNA interface may be used to determine which parameters of the binding pocket may be exploited in designing or screening compounds that interact with the C terminal L11: GAR RNA interface domain and/or modify the activity of the GTPase.
The analysis of the various targets made possible by the crystal structure coordinate data disclosed herein, including the GAR RNA:L11 interface, the GAR RNA:L11: Micrococcin interface, the L11 N terminus:L11 C terminus interface (with or without GAR RNA), the GAR RNA:EF-G interface, and the GAR RNA:L11:EF-G interface, may be used to define specific features (e.g., a pattern of hydrogen bond donors and acceptors, a hydrophobic patch, etc.) of these targets. These features in turn define a three dimensional “pharmacophore” pattern. This pattern can then be used to screen virtual libraries of existing compounds, such as the Available Chemical Directory (MDL, Inc.) for compounds exhibiting the desired combination of chemical entities. In this screening, the quality of fit of such entities or compounds to the target site may be judged by a scoring function. The scoring function can account for shape complementarity (Katchalski-Katzir et al., 1992, Proc. Natl. Acad. Sci. USA, 89, pp.2195-2199.), estimated interaction energy (Meng et al., 1992, J.Comp. Chem., 13, pp. 505-524), surface accessibility, or a combination of these (see for example, Bohm, 1994, J. Comp. Aided Mol. Design, pp.243-256). A program such as Catalyst (MSI) can perform this task. Libraries of compounds can also be screened virtually using the coordinates of the targets and molecular docking programs such as DOCK (UCSF) or FLEXX.
Once one or more compounds have been identified as potential ligands using any of the methods described above, they may be screened for biological activity.
A variety of assays can be used to evaluate the activity of compounds designed to inhbit the activity of the L11/GAR. These include, but are not limited to: inhibition of bacterial growth, inhibition of in vitro protein synthesis using messenger RNA as a template, inhibition of the elongation phase of in vitro protein synthesis using polyU as a template, inhibition of GTP hydrolysis mediated by EF-G as described by Pestka (1970) and Rodnina et al. (1997); activation of GTP hydrolysis mediated by EF-G as described by Cundliffe and Thompson (1981). Binding of EF-G to both the L11/GAR complex and to the sarcin/ricin domain can be measured as described by Munishkin and Wool (1997, Proc. Natl. Acad. Sci. USA 94, 12280-12284; “The ribosome in pieces: Binding of elongation factor EF-G to oligoribonucleotides that mimic the sarcin/ricin and thiostrepton domains of 23S ribosomal RNA”).
In addition, compound interaction with the L11/GAR complex can be evaluated by direct binding assays. Filter binding assays that measure the ability of thiostrepton to cause retention of radiolabelled GAR RNA to nitrocellulose filters have been described by GuhaThakurta and Draper (1999; Biochemistry, 38, 3633-3640 “Protein-RNA sequence covariation in a ribosomal protein-rRNA complex”). As revealed herein, these assays can be modified to evaluate small molecules that competitively inhibit the binding of thiostrepton and/or micrococcin to the L11/GAR complex or to GAR. For molecules that do not themselves cause filter retention, the RNA may be labelled. For molecules that do cause filter retention, the RNA and/or RNA-protein complex can be immobilised on a solid support and the binding of radiolabelled thiostrepton or other known L11/GAR binding compound can be measured. Thiostrepton or micrococcin can be labelled metabolically by incorporation of 35S, 3H or 14C labelled precursors, or post-synthetically by modifcation of the molecule with radiolablled precursors. In addition thiostrepton or micrococcin can be labelled with another detectable group, including, but not limited to, fluorescent and luminescent groups.
Displacement assays can also be performed by using as reporter molecules any labelled molecule that binds to the L11/GAR complex or GAR RNA with an affinity of 50 uM or less. Suitable reporters include, but are not limited to, oligonucleotides, peptides and oligonucleotide-peptide conjugates.
Libraries for Screening According to the Invention
Inhibitors and/or activators identified according to the methods of the invention may be provided from libraries of compounds available from a number of sources or may be derived by combinatorial chemistry approaches known in the art. Such libraries include but are not limited to the available Chemical Directory, Maybridge, and natural product collections.
Compounds identified as ligands using the methods described herein may be further optimized to improve binding activity. Using the docked models of the known ligands thiostrepton and micrococcin, it is possible to identify structures of the ligand that may be altered to improve binding affinity. Similarly, features of a ligand that are identified as unimportant for binding may be excluded to reduce the molecular weight of the ligand.
EXAMPLES
In order that the invention described herein may be more fully understood, the following examples are set forth. It should be understood that these examples are for illustrative purposes only and are not to be construed as limiting this invention in any manner.
Example 1
Preparation and Analysis of L11/GAR RNA Crystal
A. Sample Preparation
The gene for T. maritima ribosomal protein L11 was cloned and overexpressed in E. coli using the T7-based expression system (Studier et al., 1990). The protein was purified b a combination of cation-exchange, hydroxylapatite and size-exclusion chromatography as reported for the purification of ribosomal protein S7 (Wimberly et al., 1997). For cocrystallization with RNA, the protein was dialysed into a buffer A containing 0.1 M KCl, 5 mM Na-cacodylate pH 6.0, 0.1 mM Na2EDTA, 1 mM DTT. A fragment of RNA corresponding to nucleotides 1111-1168 of T. maritima 23S rRNA was synthesized by in vitro run-off transcription from a linearized plasmid using T7 RNA polymerase. The plasmid contained the following elements: a T7 promoter, a self-cleaving hammerhead ribozyme to generate a homogeneous RNA 5′ end (Price et al., 1995), a template for the target RNA sequence, and a Pst I site used for plasmid linearization. RNA was purified on denaturing polyacrylamide slab gels, eluted, concentrated by ethanol precipitation, and dialyzed into buffer A. The RNA was reannealed by heating to 90° C. and slow cooling. L11 protein was added to yield a 1:1 RNA:protein mixture, which was concentrated to 0.15 mM in each component for crystallization experiments.
B. Crystallization and Structure Determination
Crystals of the complex were obtained at 4° C. using the hanging drop technique. The equimolar mixture of L11 and RNA in dialysis buffer A was mixed with an equal volume of well solution (25% glycerol, 15% PEG 4000, 0.2 M KCl, 50 mM MgCl2, 20 mM CdCl2, 1 mM DTT, 50 mM Tris pH 7.5 at 22° C.). The crystals were in the space group P212121, with cell dimensions of a=63.9 Å, b=84.3 Å and c=155.5 Å, and diffracted to better than 2.6 Å resolution using a synchrotron source. Diffraction data were collected under cryogenic conditions, and the crystals were flash-frozen by plunging into liquid nitrogen. For mercury derivatization, crystals were soaked for 24 hours in the well solution containing 1 mM CH3HgNO3 but lacking DTT. Efforts to obtain cocrystals of RNA with selenomethione-substituted L11 were unsuccessful, apparently because the preparation of selenomethionyl L11 used was at least partly misfolded.
The structure was solved using a multiwavelength anomalous diffraction (MAD) experiment (Hendrickson, 1991) on the methylmercury derivative. Straightforward isomorphous replacement was not possible because the derivative is not isomorphous with native crystals. Because the mercury L11 edge does not have a significant white line, data were collected at just two wavelengths, the inflection point of the mercury edge at 1.01 Å and a remote wavelength at 0.98 Å. This remote wavelength is near the maximum f′′ for accurate measurement of anomalous differences, and is also sufficiently remote from the inflection point to give useful isomorphous differences. Data were collected from a single flash-cooled crystal at beamline X12-C of the NSLS. To optimize measurement of anomalous differences, we used the inverse beam method in which pairs of sweeps separated by 180 degrees in were collected every 30 degrees. The data were integrated and scaled using the HKL suite of programs (Otwinowski and Minor, 1997).
Phasing was done by treating MAD as a special case of MIR (Ramakrishnan and Biou, 1997; Ramakrishnan et al., 1993). Local scaling of the data, determination of initial heavy atom sites, and initial phasing was done using the program SOLVE (Terwilliger and Berendzen, 1999). Subsequent phasing was done using the program SHARP (de la Fortelle and Bricogne, 1997). A significant improvement in phasing was obtained by including several well-ordered cadmium sites in a final round of SHARP heavy atom refinement. Each round of phasing was followed by density modification with Solomon (Abrahams and Leslie, 1996). The unaveraged, solvent-flattened map revealed virtually unbroken main-chain density for the RNA and the L11 C-terminal domains of both complexes in the asymmetric unit, which were easily built using the program O (Jones and Kjeldgaard, 1997). Twofold non-crystallographic symmetry (NCS) averaging followed by solvent flattening was then carried out using NCS and solvent masks based on the RNA and C-terminal domain coordinates. The resulting map was of high quality and revealed a few minor building errors, but the L11 N-terminal domain density was still of insufficient quality to permit unambiguous fitting. Interpretation of the density for the entire L11 N-terminal domain was possible only from iterative rounds of refinement and 2Fo-Fc maps. The final model was refined to an Rfree of 27% using the program X-PLOR (Brünger, 1988) using standard parameters for protein (Engh and Huber, 1991) and nucleic acid (Parkinson et al., 1996) structure refinement. Magnesium and cadmium ions were distinguished by inspection of an anomalous difference Fourier map. Magnesium ions were distinguished from ordered waters by inspection of 2Fo-Fc maps, in which an octahedral coordination of magnesium by water and RNA ligands was often visible. A Ramachandran plot of the protein revealed only three outliers, Lys93 in the C-terminal domain, which clearly has a positive phi angle in the original experimental map, and Ala21 and Val24 in the N-terminal domain, for which the side chains are very poorly defined. Details of the data collection, phasing and refinement are shown in Table I.
Example 2
Use of the Ribosomal Protein L11/GAR Crystal Structure Coordinates to Design a Modulator of GAR Activity
Example 1 illustrates the methods involved in generating a structure of the L11/GAR RNA complex at atomic resolution. The crystal structure data make clear, for example, that the N terminus of L11 can move within the context of the L11/GAR. Because the crystal structure data, in conjunction with available biochemical data, point to a molecular switch mechanism whereby the relative position of the L11 N terminal lobe determines the activity of the GAR, it is of interest to select or design compounds that can effect restriction of modification of this movement.
1. Modeling the movement and interactions of the L11 N terminal lobe.
One of skill in the art may use the crystal structure coordinates, along with the software package Quanta to interactively model the movement of the L11 N terminus as a rigid body relative to the other GAR surfaces. This model will provide information on the many possible interactions between the L11 N terminus and the other amino acid and nucleotide residues comprising the GAR, as well as solvent interactions.
To develop a more detailed picture of the molecular interactions involving the L11 N terminal lobe in the GAR, the software packages CHARMM and AMBER may be applied by one of skill in the art to the crystal structure coordinates. These will provide a molecular dynamics simulation of the N terminal lobe of L11 within the L11/GAR RNA complex.
Similarly, CHARMM may be used by one of skill in the art to provide a normal mode dynamics simulation of the L11 N terminal lobe within the L11/GAR context.
Finally, the crystal structure coordinates allow the use of software packages such as DOCK or to simulate docking of the known GAR modulators thiostrepton and micrococcin with the GAR, thereby providing a finely detailed description of those interactions within the GAR critical to its function.
Used in combination, the software approaches described above can manipulate the crystal structure coordinate data to provide a very high resolution three dimensional model of the L11 N terminal lobe and its interactions with other portions of the GAR including van der Waals contacts, electrostatic interactions and hydrogen bonding opportunities.
2. Design of a candidate modulator compound.
Once a detailed three dimensional model of the L11/GAR has been created as described above, one of skill in the art may use the grid-based software approaches GRID or CERIUS II, and MCSS techniques (see, for example, Castro et al., 1999, Medicinal Chem. Res. 9: 98-107) to map favorable interaction positions for functional groups such as protons, hydroxyl groups, anime groups, divalent cations, aromatic and aliphatic functional groups, acetamide, methanol, etc. Once a set of favorable groups for each position are predicted, one of skill in the art may take one of two different approaches to designing a modulator.
First, one may assemble the moieties predicted to interact with the various critical parts of the L11/GAR surfaces into a single molecule. This may be accomplished by one of skill in the art using the software packages CAVEAT, MACCS-3D or HOOK. One of skill in the art may then synthesize the selected compounds for in vitro and in vivo testing for effects on GAR activity.
Alternatively, one may screen a database, such as the MDL Available Chemical Directory to potentially find existing compounds that combine the required moieties in a favorable conformation for GAR binding. The software packages Catalyst, DOCK and FLEXX may be used to advantage for this purpose by one of skill in the art.
Example 3
Assaying the Activity of a Candidate Modulator by Displacement of Thiostrepton from the GAR
Thiostrepton binding to GTPase centre RNA can be monitored by a filter binding assays (Uchiumi et al., 1995, Biol. Chem., 270(50):29889-93; Draper et al., 1988, Methods Enzymol., 164:203-20). The filter binding assay can be transformed to a 96-well format using Millipore MHAB (mixed cellulose ester) 96-well plates. The dissociation constant for the thiostrepton/GTPase centre-59 mer complex of 1 uM is in good accordance with the literature. Additionally, filter binding can show the cooperativity in binding of thiostrepton and L11. Thermotoga maritima ribosomes are known to be sensitive to thiostrepton (Londei et al., 1988, J. Bacteriol., 170(9):4353-60), although 100-fold less than B. stearothermophilus ribosomes. The affinity of thiostrepton for Thermotoga GTPase center RNA in vitro has not yet been determined.
35S- or 32P-labelled RNA is prepared by transcription in the presence of radiolabelled nucleotides. The labelled RNAs are purified by gel electrophoresis or chromatography by reverse-phase. For filter binding assays the RNA are renatured and 3,000 to 10,000 cpm of RNA are used per assay. Association constants between RNA and thiostrepton in the presence or absence of inhbitor are determined in 100 ul reactions containing 10 mM Tris-HCl (pH 7.4), 3 mM MgCl2, 175 mM NH4Cl and 5% v/v DMSO. The reaction mixtures also contain between 2 and 10 uM thiostrepton and a range of inhibitor concentrations up to 50 uM. The RNA-thiostrepton-inhibitor mixtures are incubated for 15 min at room temperature (approximately 22° C.) prior to filtration through the nitrocellulose filter membranes.
For high-throughput screening, the assay can be performed in 96-well filter plates (Multiscreen HA filtration plates, Millipore) with nitrocellulose membranes incorporated into the bottom of each well and filtered using Multiscreen vacuum Manifold (Millipore). The filters are washed once with 100 ul buffer before determining their radioactivities using Microbeta Liquid Scintillation Counter (Wallac).
The relative amounts of RNA retained in the presence and absence of inhibitor can be determined by quantitation of the radioactivity on each filter. Compounds that reduce the amount of RNA retained on the filter in a concentration dependent manner are competitive inhibitors of thiostrepton binding to the RNA.
Example 4
Binding Assays with Radioactive Thiostrepton
Binding of [35S]-labelled thiostrepton to 23S RNA and ribosomes has been shown by gel filtration of RNA and RNA/L11 complexes together with thiostrepton as well as by charcoal (Norit) absorption of unbound [35S]thiostrepton (Thompson et al., 1979. Eur. J. Biochem., 98(1):261-5). Using equilibrium dialysis, the dissociation constant of thiostrepton/23S RNA has been determined as 0.23 uM (Thompson & Cundliffe, 1991, Biochimie 1991, 73(7-8):1131-5). The affinity to intact ribosomes is 100-1000fold higher (Pestka et al., 1976, Anal. Biochem., 71(1):137-42).
The ability of biotinylated GTPase centre-59 mer to bind thiostrepton (as shown by filter binding) gives a route for a displacement assay employing displacement of [3H]-labelled thiostrepton (Amersham) from an immobilised GTPase centre RNA/L11 complex or from ribosomes.
Example 5
Luciferase Translation Assay
Using an E. coli S30 lysate and luciferase mRNA (Promega E. coli S30 extract system for linear templates; Cat No: L1030) the active luciferase protein can be synthesised in vitro and the relative amount of luciferase generated is monitored in a bioluminescence assay. The mRNA is either provided by coupled transcription/translation using the linearized plasmid pBESTLucTM as a template or by adding purified luciferase mRNA.
The addition of ribosome-inactivating compounds or antibiotics directed to protein biosynthesis (thiostrepton, kanamycin, chloramphenicol and others) leads to a decrease in yield of active luciferase compared to the control. Compound and antibiotic titrations can be used to determine IC50 values (see Langer et al., 1996, Anal. Biochem., 243(1):150-3).
Example 6
Additional Translation Assays
An S30 transcription/translation system (Promega) can be used to incorporate [35S]methionine into protein translated from MS2 phage RNA. Translation yield is quantified after alkaline hydrolysis by acid precipitation of the synthesised peptides and scintillation counting. Whole-cell protein synthesis can be measured adding [14C]leucine to exponentially growing E. coli cells and measuring the incorporation into protein by alkaline hydrolysis and TCA precipitation (see Shinabarger et al., 1997, Antimicrob. Agents Chemother., 41(10):2132-6).
Example 7
Assay of Translation Elongation
Translation elongation is measured using isolated polysomes from E. coli MRE600 (Girbes et al., 1979, Methods Enzymol., 59:353-62), S100 extract from E. coli and poly(U) (Sigma) as a template (e.g. Grise-Miron et al., 1981, Biochim. Biophys. Acta, 656(1):103-10). Incorporation of [3H]phenylalanine into polyphenylalanine is quantified by acid precipitation and scintillation counting.
Example 8
In vitro EF-G-dependent GTP Hydrolysis
Thiostrepton acts on the tRNA translocation step of translation elongation and inhibits elongation factor G (EF-G)-dependent GTP hydrolysis (Pestka et al., 1970, Biochem. Biophys. Res. Commun., 40(3):667-74; Rodnina et al., 1997, Nature, 385:37-41). EF-G is known to contact the GTPase centre region of 23S RNA (Skold et al., 1983, Nucleic Acids Res., 11(14):4923-32; Moazed & Noller, 1986, Nature, 334:362-4). 70S ribosomes support GTP hydrolysis by EF-G in the absence of other factors normally necessary for protein synthesis. Uncoupled GTP hydrolysis and the inhibition by thiostrepton or other compounds can be measured in an assay containing purified ribosomes, purified EF-G and gamma-[32P]-GTP (Stark&Cundliffe, 1979, J. Mol. Biol., 134(4):767-9; Lill et al., 1988, EMBO J., 8(12):3933-8).
References


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TABLE I







Crystallographic statistics











Data collection
λ1 (1.008 Å)
λ2 (0.980 Å)







Reflections
 104,096
 107,907



Independent reflections
  25,927
  25,894



Completeness
 99% (98%)*
 98% (97%)*



Mean (I/sigma (I))
  20 (4.2)*
  20 (4.5)*



Rsym 
4.1% (17%)*
4.2% (17%)*



dmin (Å)
     2.6
     2.6



ƒ′ (Hg) (electrons)**
  −12.0
   −9.0



ƒ′′ (Hg) (electrons)**
     6.4
     8.0



ƒ′ (Cd) (electrons)**
   −0.42
   −0.46



ƒ′′ (Cd) (electrons)**
     2.3
     2.2

















λ1-λ2
λ1
λ2



Phasing
isomorphous
anomalous
anomalous







RCullis (centrics)
0.50
—
—



RKraut (acentrics)
0.09
0.025
0.023



Phasing power
1.25
1.54
1.52



(acentrics)



Mean figure of
0.39



merit (acentrics)



Mean figure of
0.23



merit (centrics)










Refinement




Number of atoms
4196 (2474 RNA, 1524 protein, 198




water & ions)



Rcryst/Rfree (5% of data)
0.228/0.253



RMS deviation from



ideal geometry



bond lengths
0.005 Å



bond angles
1.2 degrees







*Values in parentheses refer to the highest resolution shell. 



**Values after SHARP refinement. 














TABLE II







HEADER
RNA-PROTEIN COMPLEX 14-APR-99


ONHOLD
ONE-YEAR HOLD; EXPERIMENTAL DATA, ONE-YEAR HOLD


TITLE
CRYSTAL STRUCTURE OF THE RIBOSOMAL PROTEIN L11-RNA COMPLEX


COMPND
MOL_ID: 1;


COMPND 2
MOLECULE: 23S RIBOSOMAL RNA;


COMPND 3
CHAIN: C, D;


COMPND 4
FRAGMENT: FRAGMENT 1051-1108;


COMPND 5
MUTATION: U1108C;


COMPND 6
OTHER_DETAILS: COVALENT MERCURY LIGAND AT U1061;


COMPND 7
MOL_ID: 2;


COMPND 8
MOLECULE: RIBOSOMAL PROTEIN L11;


COMPND 9
CHAIN: A, B;


COMPND 10
ENGINEERED: YES;


COMPND 11
OTHER_DETAILS: COVALENT MERCURY LIGAND AT CYS39


SOURCE
MOL_ID: 1;


SOURCE 2
ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;


SOURCE 3
OTHER_DETAILS: IN VITRO TRANSCRIBED RNA;


SOURCE 4
MOL_ID: 2;


SOURCE 5
ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;


SOURCE 6
EXPRESSION_SYSTEM: ESCHERICHIA COLI;


SOURCE 7
EXPRESSION_SYSTEM_STRAIN: BL21(DE3);


SOURCE 8
EXPRESSION_SYSTEM_PLASMID: PET13A;


SOURCE 9
OTHER_DETAILS: RECOMBINANT PROTEIN


KEYWDS
RNA-PROTEIN COMPLEX, RNA, RIBOSOME, TRANSLOCATION,


KEYWDS 2
THIOSTREPTON


EXPDTA
X-RAY DIFFRACTION


AUTHOR
B. T. WIMBERLY, R. GUYMON, J. P. MCCUTCHEON, S. W. WHITE,


AUTHOR 2
V. RAMAKRISHNAN


REMARK 1


REMARK 1
REFERENCE 1


REMARK 1
AUTH Y. XING, D. DRAPER


REMARK 1
TITL COOPERATIVE INTERACTIONS OF RNA AND THIOSTREPTON


REMARK 1
TITL 2 ANTIBIOTIC WITH TWO DOMAINS OF RIBOSOMAL PROTEIN


REMARK 1
TITL 3 L11


REMARK 1
REF BIOCHEMISTRY  V. 35 1581 1996


REMARK 1
REFN ASTM BICHAW US ISSN 0006-2960 0033


REMARK 1
REFERENCE 2


REMARK 1
AUTH J. THOMPSON, F. SCHMIDT, E. CUNDLIFFE


REMARK 1
TITL SITE OF ACTION OF A RIBOSOMAL RNA METHYLASE


REMARK 1
TITL 2 CONFERRING RESISTANCE TO THIOSTREPTON


REMARK 1
REF J. BIOL.CHEM.  V. 257 7915 1982


REMARK 1
REFN ASTM JBCHA3 US ISSN 0021-9258  0071


REMARK 1
REFERENCE 3


REMARK 1
AUTH J. THOMPSON, E. CUNDLIFFE, M. STARK


REMARK 1
TITL BINDING OF THIOSTREPTON TO A COMPLEX OF 23S RNA


REMARK 1
TITL 2 WITH RIBOSOMAL PROTEIN L11


REMARK 1
REF EUR. J. BIOCHEM.  V. 98 261 1979


REMARK 1
REFN ASTM EJBCAI IX ISSN 0014-2956  0262


REMARK 2


REMARK 2
RESOLUTION. 2.57 ANGSTROMS.


REMARK 3


REMARK 3
REFINEMENT.


REMARK 3
PROGRAM: X-PLOR 3.851


REMARK 3
AUTHORS: BRUNGER


REMARK 3


REMARK 3
DATA USED IN REFINEMENT.


REMARK 3
RESOLUTION RANGE HIGH (ANGSTROMS): 2.57


REMARK 3
RESOLUTION RANGE LOW (ANGSTROMS): 20.0


REMARK 3
DATA CUTOFF  (SIGMA(F)): 0.0


REMARK 3
DATA CUTOFF HIGH  (ABS(F)): 1000000.0


REMARK 3
DATA CUTOFF LOW  (ABS(F)): 0.001


REMARK 3
COMPLETENESS (WORKING + TEST) (%): 95.5


REMARK 3
NUMBER OF REFLECTIONS:  49313


REMARK 3


REMARK 3
FIT TO DATA USED IN REFINEMENT.


REMARK 3
CROSS-VALIDATION METHOD:  THROUGHOUT


REMARK 3
FREE R VALUE TEST SET SELECTION: RANDOM


REMARK 3
R VALUE  (WORKING SET): 0.219


REMARK 3
FREE R VALUE  : 0.254


REMARK 3
FREE R VALUE TEST SET SIZE (%): 4.9


REMARK 3
FREE R VALUE TEST SET COUNT: 2398


REMARK 3
ESTIMATED ERROR OF FREE R VALUE: 0.005


REMARK 3


REMARK 3
FIT IN THE HIGHEST RESOLUTION BIN.


REMARK 3
TOTAL NUMBER OF BINS USED : 6


REMARK 3
BIN RESOLUTION RANGE HIGH (A): 2.57


REMARK 3
BIN RESOLUTION RANGE LOW (A): 2.73


REMARK 3
BIN COMPLETENESS (WORKING + TEST) (%): 86.2


REMARK 3
REFLECTIONS IN BIN (WORKING SET): 7101


REMARK 3
BIN R VALUE (WORKING SET): 0.386


REMARK 3
BIN FREE R VALUE  : 0.432


REMARK 3
BIN FREE R VALUE TEST SET SIZE (%): 4.5


REMARK 3
BIN FREE R VALUE TEST SET COUNT : 331


REMARK 3
ESTIMATED ERROR OF BIN FREE R VALUE: 0.024


REMARK 3


REMARK 3
NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.


REMARK 3
PROTEIN ATOMS : 1524


REMARK 3
NUCLEIC ACID ATOMS : 2474


REMARK 3
HETEROGEN ATOMS : 35


REMARK 3
SOLVENT ATOMS : 142


REMARK 3


REMARK 3
B VALUES.


REMARK 3
FROM WILSON PLOT (A**2): 58.8


REMARK 3
MEAN B VALUE (OVERALL, A**2): 42.8


REMARK 3
OVERALL ANISOTROPIC B VALUE.


REMARK 3
B11 (A**2): NULL


REMARK 3
B22 (A**2): NULL


REMARK 3
B33 (A**2): NULL


REMARK 3
B12 (A**2): NULL


REMARK 3
B13 (A**2): NULL


REMARK 3
B23 (A**2): NULL


REMARK 3


REMARK 3
ESTIMATED COORDINATE ERROR.


REMARK 3
ESD FROM LUZZATI PLOT (A): 0.32


REMARK 3
ESD FROM SIGMAA (A): 0.45


REMARK 3
LOW RESOLUTION CUTOFF (A): 5.00


REMARK 3


REMARK 3
CROSS-VALIDATED ESTIMATED COORDINATE ERROR.


REMARK 3
ESD FROM C-V LUZZATI PLOT (A): 0.39


REMARK 3
ESD FROM C-V SIGMAA (A): 0.50


REMARK 3


REMARK 3
RMS DEVIATIONS FROM IDEAL VALUES.


REMARK 3
BOND LENGTHS (A): 0.005


REMARK 3
BOND ANGLES (DEGREES): 1.0


REMARK 3
DIHEDRAL ANGLES (DEGREES): 28.8


REMARK 3
IMPROPER ANGLES (DEGREES): 1.40


REMARK 3


REMARK 3
ISOTROPIC THERMAL MODEL: RESTRAINED


REMARK 3


REMARK 3
ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA


REMARK 3
MAIN-CHAIN BOND (A**2): 3.59; 1.50


REMARK 3
MAIN-CHAIN ANGLE (A**2): 5.28; 2.00


REMARK 3
SIDE-CHAIN BOND (A**2): 6.59; 2.00


REMARK 3
SIDE-CHAIN ANGLE (A**2): 9.24; 2.50


REMARK 3


REMARK 3
NCS MODEL: RESTRAINTS


REMARK 3


REMARK 3
NCS RESTRAINTS.  RMS SIGMA/WEIGHT


REMARK 3
GROUP 1 POSITIONAL (A): 0.07; 50


REMARK 3
GROUP 1 B-FACTOR (A**2): 5.51; 2


REMARK 3
GROUP 2 POSITIONAL (A): 0.07; 50


REMARK 3
GROUP 2 B-FACTOR (A**2): 5.51; 2


REMARK 3


REMARK 3
PARAMETER FILE 1: DNA-RNA-MULTI-ENDO.PARAM


REMARK 3
PARAMETER FILE 2: PROTEIN_REP.PARAM


REMARK 3
TOPOLOGY FILE 1: DNA-RNA-MULTI-ENDO.TOP


REMARK 3
TOPOLOGY FILE 2: TOPHCSDX.PRO


REMARK 3
TOPOLOGY FILE 3: TOPH19.SOL


REMARK 3


REMARK 3
OTHER REFINEMENT REMARKS: NCS RESTRAINTS APPLIED TO RNA


REMARK 3
THROUGHOUT, NOT TO PROTEIN


REMARK 5


REMARK 5
WARNING


REMARK 5:
THIS IS LAYER 1 RELEASE.


REMARK 5


REMARK 5
PLEASE NOTE THAT THIS ENTRY WAS RELEASED AFTER DEPOSITOR


REMARK 5
CHECKING AND APPROVAL BUT WITHOUT PDB STAFF



INTERVENTION.


REMARK 5
AN AUXILIARY FILE, AUX.RPT, IS AVAILABLE FROM THE


REMARK 5
PDB FTP SERVER AND IS ACCESSIBLE THROUGH THE 3DB BROWSER.


REMARK 5
THE FILE CONTAINS THE OUTPUT OF THE PROGRAM WHAT_CHECK



AND


REMARK 5
OTHER DIAGNOSTICS.


REMARK 5


REMARK 5
NOMENCLATURE IN THIS ENTRY, INCLUDING HET RESIDUE NAMES


REMARK 5
AND HET ATOM NAMES, HAS NOT BEEN STANDARDIZED BY THE PDB


REMARK 5
PROCESSING STAFF. A LAYER 2 ENTRY WILL BE RELEASED SHORTLY


REMARK 5
AFTER THIS STANDARDIZATION IS COMPLETED AND APPROVED BY



THE


REMARK 5
DEPOSITOR. THE LAYER 2 ENTRY WILL BE TREATED AS A


REMARK 5
CORRECTION TO THIS ONE, WITH THE APPROPRIATE REVDAT



RECORD.


REMARK 5


REMARK 5
FURTHER INFORMATION INCLUDING VALIDATION CRITERIA USED IN


REMARK 5
CHECKING THIS ENTRY AND A LIST OF MANDATORY DATA FIELDS


REMARK 5
ARE AVAILABLE FROM THE PDB WEB SITE AT


REMARK 5
HTTP://WWW.PDB.BNL.GOV/.


REMARK 6


REMARK 6
THE ASYMMETRIC UNIT CONTAINS TWO L11-RNA COMPLEXES.



COMPLEX


REMARK 6
1 CONSISTS OF CHAINS A AND C, AND COMPLEX 2 CONSISTS OF


REMARK 6
CHAINS B AAND D. RESIDUES 1-7 AND 141 OF CHAIN A ARE


REMARK 6
DISORDERED. THE DENSITY FOR RESIDUES 8-70 OF CHAIN A WAS OF


REMARK 6
SIGNIFICANTLY LOWER QUALITY THAN THE DENSITY FOR THE


REMARK 6
REMAINDER OF THE ASYMMETRIC UNIT, AND THE QUALITY OF THE


REMARK 6
MODEL FOR THIS N-TERMINAL DOMAIN IS LOWER THAN THAT OF



THE


REMARK 6
C-TERMINAL DOMAIN (RESIDUES 71-140). RESIDUES 1-70 AND 141


REMARK 6
OF CHAIN B ARE DISORDERED. THE RNA IS NUMBERED WITH THE E.


REMARK 6
COLI NUMBERING TO FACILITATE COMPARISON WITH THE



EXTENSIVE


REMARK 6
BIOCHEMICAL DATA ON THE E. COLI RNA-L11 SYSTEM. THE E. COLI


REMARK 6
RNA NUMBERING IS ALSO USED IN THE PRIMARY REFERENCE


REMARK 6
DESCRIBING THIS STRUCTURE.


REMARK 7


REMARK 7
TER


REMARK 7
ASP: TERMINAL RESIDUE NOT SEEN IN MAPS


REMARK 7
ASP: TERMINAL RESIDUE NOT SEEN IN MAPS


REMARK 200


REMARK 200
EXPERIMENTAL DETAILS


REMARK 200
EXPERIMENT TYPE:  X-RAY DIFFRACTION


REMARK 200
DATE OF DATA COLLECTION : 24-SEP-1998


REMARK 200
TEMPERATURE (KELVIN): 100


REMARK 200
PH  : 8.3


REMARK 200
NUMBER OF CRYSTALS USED : 1


REMARK 200


REMARK 200
SYNCHROTRON (Y/N): Y


REMARK 200
RADIATION SOURCE : NSLS


REMARK 200
BEAMLINE  : X12C


REMARK 200
X-RAY GENERATOR MODEL : NULL


REMARK 200
MONOCHROMATIC OR LAUE (M/L): M


REMARK 200
WAVELENGTH OR RANGE (A): 0.98, 1.01


REMARK 200
MONOCHROMATOR  : SI CRYSTAL


REMARK 200
OPTICS  : MIRRORS


REMARK 200


REMARK 200
DETECTOR TYPE  : BRANDEIS 1K X 1 K CCD


REMARK 200
DETECTOR MANUFACTURER : NULL


REMARK 200
INTENSITY-INTEGRATION SOFTWARE: DENZO


REMARK 200
DATA SCALING SOFTWARE : SCALEPACK


REMARK 200


REMARK 200
NUMBER OF UNIQUE REFLECTIONS: 49313


REMARK 200
RESOLUTION RANGE HIGH (A): 2.57


REMARK 200
RESOLUTION RANGE LOW (A): 20.0


REMARK 200
REJECTION CRITERIA (SIGMA(I)): 0


REMARK 200


REMARK 200
OVERALL.


REMARK 200
COMPLETENESS FOR RANGE (%): 95.5


REMARK 200
DATA REDUNDANCY : 4.0


REMARK 200
R MERGE  (I): NULL


REMARK 200
R SYM  (I): 0.041


REMARK 200
< I/SIGMA(I)> FOR THE DATA SET: 20


REMARK 200


REMARK 200
IN THE HIGHEST RESOLUTION SHELL.


REMARK 200
HIGHEST RESOLUTION SHELL, RANGE HIGH (A): 2.57


REMARK 200
HIGHEST RESOLUTION SHELL, RANGE LOW (A): 2.73


REMARK 200
COMPLETENESS FOR SHELL (%): 86.2


REMARK 200
DATA REDUNDANCY IN SHELL: 3.4


REMARK 200
R MERGE FOR SHELL (I): NULL


REMARK 200
R SYM FOR SHELL (I): 0.17


REMARK 200
< I/SIGMA(I)> FOR SHELL : 4.3


REMARK 200


REMARK 200
DIFFRACTION PROTOCOL: MAD


REMARK 200
METHOD USED TO DETERMINE THE STRUCTURE: MAD


REMARK 200
SOFTWARE USED: NULL


REMARK 200
STARTING MODEL: NULL


REMARK 200


REMARK 200
REMARK: TWO WAVELENGTH HG MAD


REMARK 280


REMARK 280
CRYSTAL


REMARK 280
SOLVENT CONTENT, VS (%): 55


REMARK 280
MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.1


REMARK 280


REMARK 280
CRYSTALLIZATION CONDITIONS:


REMARK 280
25% GLYCEROL, 15% PEG 4000, 50 MM TRIS PH 7.5,


REMARK 280
50 MM MGCL2, 20 MM CDCL2, 0.2 M KCL,


REMARK 280
1 MM DITHIOTHREITOL, 4 DEGREES C


REMARK 290


REMARK 290
CRYSTALLOGRAPHIC SYMMETRY


REMARK 290
SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21


REMARK 290


REMARK 290
SYMOP SYMMETRY


REMARK 290
NNNMMM OPERATOR


REMARK 290
1555 X, Y, Z


REMARK 290
2555 1/2 − X, −Y, 1/2 + Z


REMARK 290
3555  −X, 1/2 + Y, 1/2 − Z


REMARK 290
4555 1/2 + X, 1/2 − Y, −Z


REMARK 290


REMARK 290
WHERE NNN -> OPERATOR NUMBER


REMARK 290
MMM -> TRANSLATION VECTOR


REMARK 290


REMARK 290
CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS


REMARK 290
THE FOLLOWING TRANSFORMATIONS OPERATE ON THE



ATOM/HETATM


REMARK 290
RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY


REMARK 290
RELATED MOLECULES.














REMARK 290
SMTRY1
1
1.000000
0.000000
0.000000
0.00000



REMARK 290
SMTRY2
1
0.000000
1.000000
0.000000
0.00000


REMARK 290
SMTRY3
1
0.000000
0.000000
1.000000
0.00000


REMARK 290
SMTRY1
2
−1.000000
0.000000
0.000000
31.94480


REMARK 290
SMTRY2
2
0.000000
−1.000000
0.000000
0.00000


REMARK 290
SMTRY3
2
0.000000
0.000000
1.000000
77.76050


REMARK 290
SMTRY1
3
−1.000000
0.000000
0.000000
0.00000


REMARK 290
SMTRY2
3
0.000000
1.000000
0.000000
42.13010


REMARK 290
SMTRY3
3
0.000000
0.000000
−1.000000
77.76050


REMARK 290
SMTRY1
4
1.000000
0.000000
0.000000
31.94480


REMARK 290
SMTRY2
4
0.000000
−1.000000
0.000000
42.13010


REMARK 290
SMTRY3
4
0.000000
0.000000
−1.000000
0.00000








REMARK 290



REMARK 290
REMARK: NULL


REMARK 295


REMARK 295
NON-CRYSTALLOGRAPHIC SYMMETRY


REMARK 295
THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS



BELOW


REMARK 295
DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG



ATOMS


REMARK 295
IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX


REMARK 295
TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD


REMARK 295
APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.


REMARK 295
CHAIN IDENTIFIERS GIVEN AS “?” REFER TO CHAINS FOR WHICH


REMARK 295
ATOMS ARE NOT FOUND IN THIS ENTRY.


REMARK 295


REMARK 295
 APPLIED TO  TRANSFORMED TO


REMARK 295
TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD


REMARK 295
SSS


REMARK 295
M 1 C 1051 . . . 1108 D 1051 . . . 1108 0.07


REMARK 295
M 2 A 71 . . . 140 B 71 . . . 140 0.99


REMARK 295


REMARK 295
WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS


REMARK 295


REMARK 295
REMARK:


REMARK 295
NCS RESTRAINTS NOT APPLIED TO PROTEIN


REMARK 465


REMARK 465
MISSING RESIDUES


REMARK 465
THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE


REMARK 465
EXPERIMENT. (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHA1N


REMARK 465
IDENTIFIER; SSSEQ = SEQUENCE NUMBER; I = INSERTION CODE):


REMARK 465


REMARK 465
M RES C SSSEQI


REMARK 465
ALA A 2


REMARK 465
LYS A 3


REMARK 465
LYS A 4


REMARK 465
VAL A 5


REMARK 465
ALA A 6


REMARK 465
ALA A 7


REMARK 465
ASP A 141


REMARK 465
ALA B 2 TO ILE B 70


REMARK 465
ASP B 141


REMARK 470


REMARK 470
MISSING ATOM


REMARK 470
THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M = MODEL



NUMBER;


REMARK 470
RES = RESIDUE NAME; C = CHAIN IDENTIFIER; SSEQ = SEQUENCE



NUMBER;


REMARK 470
I = INSERTION CODE):


REMARK 470
M RES CSSEQI ATOMS


REMARK 470
 G C1051 P O1P O2P


REMARK 470
 G D1051 P O1P O2P


REMARK 550


REMARK 550
SEGID


REMARK 550
RNA1, RNA2


REMARK 550
L111, L112


REMARK 600


REMARK 600
HETEROGEN


REMARK 600
THERE ARE A TOTAL OF 8 CADMIUM IONS IN THE STRUCTURE


REMARK 600


REMARK 600
THERE ARE A TOTAL OF 19 MAGNESIUM IONS IN THE STRUCTURE


REMARK 600


REMARK 600
THERE ARE A TOTAL OF 8 METHYLMERCURY


REMARK 600
IONS IN THE STRUCTURE.


REMARK 600
THE METHYL GROUP HAS NOT BEEN MODELLED


REMARK 600
FOR ANY OF THESE IONS.


REMARK 600
TWO OF THE IONS ARE COVALENTLY BOUND


REMARK 600
TO CYS A 39.


REMARK 600
ONE IS COVALENTLY BOUND TO U C 1061.


REMARK 600
ONE IS COVALENTLY BOUND TO U D 1061.


REMARK 600


REMARK 800


REMARK 800
SITE


REMARK 800
SITE_IDENTIFIER: TSR


REMARK 800
SITE_DESCRIPTION:


REMARK 800
PUTATIVE THIOSTREPTON/MICROCOCCIN BINDING SITE


REMARK 800


REMARK 800
SITE_IDENTIFIER: TSR


REMARK 800
SITE_DESCRIPTION:


REMARK 800
PUTATIVE THIOSTREPTON/MICROCOCCIN BINDING SITE


REMARK 800


REMARK 800
SITE_IDENTIFIER: TSR


REMARK 800
SITE_DESCRIPTION:


REMARK 800
PUTATIVE THIOSTREPTON/MICROCOCCIN BINDING SITE


REMARK 800


DBREF A
8 140 SWS P29395 RL11_THEMA 1 141


DBREF B
71 140 SWS P29395 RL11_THEMA 1 141


DBREF C
1051 1108 PDB  1051 1108


DBREF D
1051 1108 PDB  1051 1108


SEQADV
RES C 1108 GI M67498 1168 ENGINEERED MUTATION


SEQADV
RES D 1108 GI M67498 1168 ENGINEERED MUTATION











SEQRES
1
A
140
ALA LYS LYS VAL ALA ALA GLN ILE LYS LEU GLN LEU PRO


SEQRES
2
A
140
ALA GLY LYS ALA THR PRO ALA PRO PRO VAL GLY PRO ALA


SEQRES
3
A
140
LEU GLY GLN HIS GLY VAL ASN ILE MET GLU PHE CYS LYS


SEQRES
4
A
140
ARG PHE ASN ALA GLU THR ALA ASP LYS ALA GLY MET ILE


SEQRES
5
A
140
LEU PRO VAL VAL ILE THR VAL TYR GLU ASP LYS SER PHE


SEQRES
6
A
140
THR PHE ILE ILE LYS THR PRO PRO ALA SER PHE LEU LEU


SEQRES
7
A
140
LYS LYS ALA ALA GLY ILE GLU LYS GLY SER SER GLU PRO


SEQRES
8
A
140
LYS ARG LYS ILE VAL GLY LYS VAL THR ARG LYS GLN ILE


SEQRES
9
A
140
GLU GLU ILE ALA LYS THR LYS MET PRO ASP LEU ASN ALA


SEQRES
10 
A
140
ASN SER LEU GLU ALA ALA MET LYS ILE ILE GLU GLY THR


SEQRES
11 
A
140
ALA LYS SER MET GLY ILE GLU VAL VAL ASP


SEQRES
1
B
140
ALA LYS LYS VAL ALA ALA GLN ILE LYS LEU GLN LEU PRO


SEQRES
2
B
140
ALA GLY LYS ALA THR PRO ALA PRO PRO VAL GLY PRO ALA


SEQRES
3
B
140
LEU GLY GLN HIS GLY VAL ASN ILE MET GLU PHE CYS LYS


SEQRES
4
B
140
ARG PHE ASN ALA GLU THR ALA ASP LYS ALA GLY MET ILE


SEQRES
5
B
140
LEU PRO VAL VAL ILE THR VAL TYR GLU ASP LYS SER PHE


SEQRES
6
B
140
THR PHE ILE ILE LYS THR PRO PRO ALA SER PHE LEU LEU


SEQRES
7
B
140
LYS LYS ALA ALA GLY ILE GLU LYS GLY SER SER GLU PRO


SEQRES
8
B
140
LYS ARG LYS ILE VAL GLY LYS VAL THR ARG LYS GLN ILE


SEQRES
9
B
140
GLU GLU ILE ALA LYS THR LYS MET PRO ASP LEU ASN ALA


SEQRES
10 
B
140
ASN SER LEU GLU ALA ALA MET LYS ILE ILE GLU GLY THR


SEQRES
11 
B
140
ALA LYS SER MET GLY ILE GLU VAL VAL ASP


SEQRES
1
C
 58
G C U G G G A U G U U G G


SEQRES
2
C
 58
C U U A G A A G C A G C C


SEQRES
3
C
 58
A U C A U U U A A A G A G


SEQRES
4
C
 58
U G C G U A A C A G C U C


SEQRES
5
C
 58
A C C A G C


SEQRES
1
D
 58
G C U G G G A U G U U G G


SEQRES
2
D
 58
C U U A G A A G C A G C C


SEQRES
3
D
 58
A U C A U U U A A A G A G


SEQRES
4
D
 58
U G C G U A A C A G C U C


SEQRES
5
D
 58
A C C A G C











HET
CD
201
0



HET
CD
202
0


HET
CD
211
0


HET
CD
302
0


HET
CD
311
0


HET
CD
390
0


HET
CD
413
0


HET
CD
414
0
SEE REMARK 600


HET
MG
210
0


HET
MG
214
0


HET
MG
215
0


HET
MG
223
0


HET
MG
225
0


HET
MG
226
0


HET
MG
228
0


HET
MG
257
0


HET
MG
273
0


HET
MG
318
0


HET
MG
326
0


HET
MG
354
0


HET
MG
360
0


HET
MG
365
0


HET
MG
375
0


HET
MG
380
0


HET
MG
385
0


HET
MG
397
0


HET
MG
437
0
SEE REMARK 600


HET
HG
227
0


HET
HG
230
0


HET
HG
332
0


HET
HG
347
0


HET
HG
415
0


HET
HG
416
0


HET
HG
448
0


HET
HG
451
0
SEE REMARK 600









HETNAM
CD
CD


HETNAM
MG
MG


HETNAM
HG
MMC


HETSYN
CD
CADMIUM (II)


HETSYN
MG
MAGNESIUM (II)


HETSYN
HG
METHYLMERCURY ION








FORMUL 5
CD 8(CD1 2+)


FORMUL 6
MG 19(MG1 2+)


FORMUL 7
HG 8(C1 H3 HG1 1+)


FORMUL 8
HOH *142(H2 O1)

















HELIX 1
1
PRO
A
 26
GLN
A
 30
1
 5



HELIX 2
2
ILE
A
 35
ALA
A
 47
1
13


HELIX 3
3
ALA
A
 75
ALA
A
 83
1
 9


HELIX 4
4
ARG
A
102
ASP
A
115
1
14


HELIX 5
5
LEU
A
121
SER
A
134
1
14


HELIX 6
6
ALA
B
 75
ALA
B
 83
1
 9


HELIX 7
7
ARG
B
102
ASP
B
115
1
14


HELIX 8
8
LEU
B
121
MET
B
135
1
15
























SHEET 1
A
3
LLE
A
 9
PRO
A
 14
  0










SHEET 2
A
3
ILE
A
 53
VAL
A
 60
-1
N
ILE
A
 58
O
ILE
A
 9


SHEET 3
A
3
PHE
A
 66
ILE
A
 70
-1
N
ILE
A
 69
O
VAL
A
57


SHEET 1
B
2
GLY
A
 98
THR
A
101
  0


SHEET 2
B
2
ILE
A
137
VAL
A
140
  1
N
GLU
A
138
O
GLY
A
98


SHEET 1
C
2
GLY
B
 98
VAL
B
100
  0


SHEET 2
C
2
ILE
B
137
VAL
B
139
  1
N
GLU
B
138
O
GLY
B
98



















SITE 1
TSR
2
A
C
1067
A
C
1095






SITE 2
TSR
2
A
D
1067
A
D
1095


SITE 3
TSR
3
PRO
A
 22
PRO
A
 23
PRO
A
26














CRYST1
63.890
84.260
155.510
90.00
90.00
90.00
P 21 21 21 8












ORIGX1
1.000000
0.000000
0.000000
0.00000



ORIGX2
0.000000
1.000000
0.000000
0.00000


ORIGX3
0.000000
0.000000
1.000000
0.00000


SCALE1
0.015652
0.000000
0.000000
0.00000


SCALE2
0.000000
0.011868
0.000000
0.00000


SCALE3
0.000000
0.000000
0.006430
0.00000














MTRIX1
1
 0.974505
 0.101458
−0.200117
 −4.54330
1



MTRIX2
1
 0.097433
−0.994793
−0.029885
 −3.74880
1


MTRIX3
1
−0.202107
 0.009626
−0.979316
−50.69290
1


MTRIX1
2
 0.973477
 0.098780
−0.206364
 −4.89630
1


MTRIX2
2
 0.098758
−0.995057
−0.010432
 −2.89050
1


MTRIX3
2
−0.206374
−0.010225
−0.978420
−50.97240
1






















ATOM
1
N
GLN
A
8
−7.803
−11.096
−9.783
1.00
71.77
L111
N


ATOM
2
CA
GLN
A
8
−8.476
−9.887
−9.223
1.00
79.42
L111
C


ATOM
3
C
GLN
A
8
−8.010
−8.599
−9.897
1.00
80.19
L111
C


ATOM
4
O
GLN
A
8
−6.857
−8.190
−9.748
1.00
77.92
L111
O


ATOM
5
CB
GLN
A
8
−8.212
−9.788
−7.722
1.00
79.86
L111
C


ATOM
6
CG
GLN
A
8
−9.065
−8.752
−7.016
1.00
80.16
L111
C


ATOM
7
CD
GLN
A
8
−9.072
−8.948
−5.518
1.00
80.58
L111
C


ATOM
8
OE1
GLN
A
8
−8.020
−8.963
−4.881
1.00
82.16
L111
O


ATOM
9
NE2
GLN
A
8
−10.261
−9.104
−4.946
1.00
79.20
L111
N


ATOM
10
N
ILE
A
9
−8.916
−7.963
−10.634
1.00
81.13
L111
N


ATOM
11
CA
ILE
A
9
−8.604
−6.723
−11.337
1.00
80.39
L111
C


ATOM
12
C
ILE
A
9
−9.312
−5.530
−10.699
1.00
79.13
L111
C


ATOM
13
O
ILE
A
9
−10.338
−5.680
−10.036
1.00
78.96
L111
O


ATOM
14
CB
ILE
A
9
−9.013
−6.804
−12.834
1.00
77.02
L111
C


ATOM
15
CG1
ILE
A
9
−10.534
−6.778
−12.970
1.00
77.57
L111
C


ATOM
16
CG2
ILE
A
9
−8.482
−8.080
−13.452
1.00
74.06
L111
C


ATOM
17
CD1
ILE
A
9
−11.066
−5.495
−13.552
1.00
83.48
L111
C


ATOM
18
N
LYS
A
10
−8.752
−4.343
−10.900
1.00
80.87
L111
N


ATOM
19
CA
LYS
A
10
−9.330
−3.121
−10.360
1.00
77.55
L111
C


ATOM
20
C
LYS
A
10
−9.252
−2.011
−11.400
1.00
74.90
L111
C


ATOM
21
O
LYS
A
10
−8.308
−1.945
−12.191
1.00
69.61
L111
O


ATOM
22
CB
LYS
A
10
−8.590
−2.696
−9.089
1.00
78.72
L111
C


ATOM
23
CG
LYS
A
10
−7.080
−2.607
−9.243
1.00
76.53
L111
C


ATOM
24
CD
LYS
A
10
−6.482
−1.615
−8.256
1.00
76.55
L111
C


ATOM
25
CE
LYS
A
10
−6.047
−2.300
−6.968
1.00
78.93
L111
C


ATOM
26
NZ
LYS
A
10
−4.923
−1.584
−6.296
1.00
81.54
L111
N


ATOM
27
N
LEU
A
11
−10.261
−1.149
−11.403
1.00
72.26
L111
N


ATOM
28
CA
LEU
A
11
−10.311
−0.037
−12.342
1.00
77.13
L111
C


ATOM
29
C
LEU
A
11
−11.286
1.024
−11.852
1.00
78.99
L111
C


ATOM
30
O
LEU
A
11
−12.052
0.790
−10.915
1.00
78.52
L111
O


ATOM
31
CB
LEU
A
11
−10.744
−0.525
−13.728
1.00
77.54
L111
C


ATOM
32
CG
LEU
A
11
−11.051
−2.014
−13.906
1.00
72.58
L111
C


ATOM
33
CD1
LEU
A
11
−12.511
−2.199
−14.290
1.00
68.73
L111
C


ATOM
34
CD2
LEU
A
11
−10.128
−2.590
−14.969
1.00
73.75
L111
C


ATOM
35
N
GLN
A
12
−11.255
2.189
−12.489
1.00
80.79
L111
N


ATOM
36
CA
GLN
A
12
−12.144
3.284
−12.120
1.00
82.10
L111
C


ATOM
37
C
GLN
A
12
−13.115
3.582
−13.261
1.00
80.51
L111
C


ATOM
38
O
GLN
A
12
−12.791
4.320
−14.190
1.00
81.39
L111
O


ATOM
39
CB
GLN
A
12
−11.329
4.536
−11.789
1.00
81.65
L111
C


ATOM
40
CG
GLN
A
12
−10.068
4.267
−10.979
1.00
81.34
L111
C


ATOM
41
CD
GLN
A
12
−9.364
5.545
−10.556
1.00
88.15
L111
C


ATOM
42
OE1
GLN
A
12
−9.445
6.568
−11.239
1.00
89.05
L111
O


ATOM
43
NE2
GLN
A
12
−8.668
5.493
−9.425
1.00
90.09
L111
N


ATOM
44
N
LEU
A
13
−14.308
3.003
−13.184
1.00
80.02
L111
N


ATOM
45
CA
LEU
A
13
−15.320
3.197
−14.214
1.00
79.90
L111
C


ATOM
46
C
LEU
A
13
−16.345
4.256
−13.818
1.00
81.60
L111
C


ATOM
47
O
LEU
A
13
−16.761
4.331
−12.659
1.00
82.22
L111
O


ATOM
48
CB
LEU
A
13
−16.033
1.873
−14.502
1.00
73.75
L111
C


ATOM
49
CG
LEU
A
13
−15.191
0.615
−14.276
1.00
73.16
L111
C


ATOM
50
CD1
LEU
A
13
−16.100
−0.586
−14.059
1.00
74.99
L111
C


ATOM
51
CD2
LEU
A
13
−14.277
0.397
−15.470
1.00
68.58
L111
C


ATOM
52
N
PRO
A
14
−16.759
5.097
−14.783
1.00
80.42
L111
N


ATOM
53
CA
PRO
A
14
−17.745
6.151
−14.511
1.00
76.54
L111
C


ATOM
54
C
PRO
A
14
−19.065
5.553
−14.041
1.00
74.17
L111
C


ATOM
55
O
PRO
A
14
−19.364
4.396
−14.328
1.00
73.53
L111
O


ATOM
56
CB
PRO
A
14
−17.877
6.880
−15.846
1.00
74.99
L111
C


ATOM
57
CG
PRO
A
14
−17.358
5.919
−16.870
1.00
77.83
L111
C


ATOM
58
CD
PRO
A
14
−16.315
5.101
−16.188
1.00
76.88
L111
C


ATOM
59
N
ALA
A
15
−19.844
6.349
−13.317
1.00
75.75
L111
N


ATOM
60
CA
ALA
A
15
−21.128
5.917
−12.774
1.00
82.83
L111
C


ATOM
61
C
ALA
A
15
−21.947
5.008
−13.691
1.00
89.65
L111
C


ATOM
62
O
ALA
A
15
−21.711
3.800
−13.753
1.00
93.73
L111
O


ATOM
63
CB
ALA
A
15
−21.947
7.132
−12.387
1.00
88.09
L111
C


ATOM
64
N
GLY
A
16
−22.921
5.590
−14.387
1.00
94.26
L111
N


ATOM
65
CA
GLY
A
16
−23.761
4.810
−15.282
1.00
98.24
L111
C


ATOM
66
C
GLY
A
16
−23.218
4.696
−16.697
1.00
100.00
L111
C


ATOM
67
O
GLY
A
16
−23.672
5.395
−17.607
1.00
100.00
L111
O


ATOM
68
N
LYS
A
17
−22.239
3.813
−16.881
1.00
99.48
L111
N


ATOM
69
CA
LYS
A
17
−21.621
3.594
−18.187
1.00
98.41
L111
C


ATOM
70
C
LYS
A
17
−20.588
2.467
−18.117
1.00
99.13
L111
C


ATOM
71
O
LYS
A
17
−19.851
2.351
−17.134
1.00
100.00
L111
O


ATOM
72
CB
LYS
A
17
−20.951
4.883
−18.685
1.00
94.26
L111
C


ATOM
73
CG
LYS
A
17
−20.492
5.822
−17.580
1.00
96.55
L111
C


ATOM
74
CD
LYS
A
17
−21.088
7.220
−17.728
1.00
97.02
L111
C


ATOM
75
CE
LYS
A
17
−21.564
7.773
−16.385
1.00
96.31
L111
C


ATOM
76
NZ
LYS
A
17
−20.459
8.345
−15.556
1.00
90.28
L111
N


ATOM
77
N
ALA
A
18
−20.545
1.642
−19.163
1.00
98.71
L111
N


ATOM
78
CA
ALA
A
18
−19.615
0.517
−19.243
1.00
96.77
L111
C


ATOM
79
C
ALA
A
18
−19.707
−0.148
−20.614
1.00
96.63
L111
C


ATOM
80
O
ALA
A
18
−20.502
0.271
−21.453
1.00
98.42
L111
O


ATOM
81
CB
ALA
A
18
−19.932
−0.500
−18.152
1.00
95.01
L111
C


ATOM
82
N
THR
A
19
−18.872
−1.165
−20.837
1.00
96.19
L111
N


ATOM
83
CA
THR
A
19
−18.843
−1.936
−22.089
1.00
98.62
L111
C


ATOM
84
C
THR
A
19
−17.834
−1.538
−23.177
1.00
98.30
L111
C


ATOM
85
O
THR
A
19
−17.439
−2.379
−23.987
1.00
94.28
L111
O


ATOM
86
CB
THR
A
19
−20.250
−2.000
−22.756
1.00
100.00
L111
C


ATOM
87
OG1
THR
A
19
−21.255
−2.212
−21.753
1.00
100.00
L111
O


ATOM
88
CG2
THR
A
19
−20.311
−3.135
−23.772
1.00
99.76
L111
C


ATOM
89
N
PRO
A
20
−17.392
−0.267
−23.212
1.00
100.00
L111
N


ATOM
90
CA
PRO
A
20
−16.433
0.087
−24.268
1.00
100.00
L111
C


ATOM
91
C
PRO
A
20
−15.174
−0.778
−24.289
1.00
100.00
L111
C


ATOM
92
O
PRO
A
20
−14.692
−1.220
−23.246
1.00
100.00
L111
O


ATOM
93
CB
PRO
A
20
−16.117
1.561
−23.995
1.00
100.00
L111
C


ATOM
94
CG
PRO
A
20
−16.510
1.782
−22.568
1.00
100.00
L111
C


ATOM
95
CD
PRO
A
20
−17.690
0.887
−22.347
1.00
100.00
L111
C


ATOM
96
N
ALA
A
21
−14.650
−1.015
−25.487
1.00
100.00
L111
N


ATOM
97
CA
ALA
A
21
−13.450
−1.823
−25.640
1.00
100.00
L111
C


ATOM
98
C
ALA
A
21
−12.238
−1.115
−25.030
1.00
100.00
L111
C


ATOM
99
O
ALA
A
21
−11.622
−1.626
−24.097
1.00
100.00
L111
O


ATOM
100
CB
ALA
A
21
−13.204
−2.130
−27.121
1.00
100.00
L111
C


ATOM
101
N
PRO
A
22
−11.886
0.079
−25.542
1.00
100.00
L111
N


ATOM
102
CA
PRO
A
22
−10.725
0.773
−24.969
1.00
100.00
L111
C


ATOM
103
C
PRO
A
22
−10.740
0.904
−23.434
1.00
100.00
L111
C


ATOM
104
O
PRO
A
22
−9.793
0.478
−22.768
1.00
100.00
L111
O


ATOM
105
CB
PRO
A
22
−10.726
2.127
−25.683
1.00
100.00
L111
C


ATOM
106
CG
PRO
A
22
−11.439
1.862
−26.979
1.00
100.00
L111
C


ATOM
107
CD
PRO
A
22
−12.496
0.845
−26.645
1.00
100.00
L111
C


ATOM
108
N
PRO
A
23
−11.807
1.495
−22.853
1.00
100.00
L111
N


ATOM
109
CA
PRO
A
23
−11.880
1.650
−21.390
1.00
100.00
L111
C


ATOM
110
C
PRO
A
23
−11.941
0.338
−20.592
1.00
100.00
L111
C


ATOM
111
O
PRO
A
23
−11.025
0.026
−19.829
1.00
100.00
L111
O


ATOM
112
CB
PRO
A
23
−13.135
2.507
−21.173
1.00
99.53
L111
C


ATOM
113
CG
PRO
A
23
−13.446
3.100
−22.519
1.00
100.00
L111
C


ATOM
114
CD
PRO
A
23
−12.988
2.077
−23.513
1.00
100.00
L111
C


ATOM
115
N
VAL
A
24
−13.020
−0.423
−20.767
1.00
100.00
L111
N


ATOM
116
CA
VAL
A
24
−13.199
−1.689
−20.051
1.00
95.98
L111
C


ATOM
117
C
VAL
A
24
−12.711
−2.903
−20.844
1.00
94.54
L111
C


ATOM
118
O
VAL
A
24
−11.538
−3.272
−20.773
1.00
88.41
L111
O


ATOM
119
CB
VAL
A
24
−14.688
−1.923
−19.689
1.00
92.89
L111
C


ATOM
120
CG1
VAL
A
24
−14.809
−2.320
−18.232
1.00
90.90
L111
C


ATOM
121
CG2
VAL
A
24
−15.504
−0.668
−19.969
1.00
91.81
L111
C


ATOM
122
N
GLY
A
25
−13.636
−3.515
−21.584
1.00
95.43
L111
N


ATOM
123
CA
GLY
A
25
−13.343
−4.683
−22.401
1.00
94.07
L111
C


ATOM
124
C
GLY
A
25
−11.973
−5.312
−22.224
1.00
94.21
L111
C


ATOM
125
O
GLY
A
25
−11.738
−6.020
−21.243
1.00
93.12
L111
O


ATOM
126
N
PRO
A
26
−11.051
−5.081
−23.176
1.00
93.73
L111
N


ATOM
127
CA
PRO
A
26
−9.684
−5.606
−23.165
1.00
93.06
L111
C


ATOM
128
C
PRO
A
26
−9.110
−5.852
−21.774
1.00
94.47
L111
C


ATOM
129
O
PRO
A
26
−8.633
−6.947
−21.480
1.00
96.39
L111
O


ATOM
130
CB
PRO
A
26
−8.893
−4.546
−23.929
1.00
91.97
L111
C


ATOM
131
CG
PRO
A
26
−9.909
−3.882
−24.840
1.00
86.86
L111
C


ATOM
132
CD
PRO
A
26
−11.299
−4.278
−24.385
1.00
89.82
L111
C


ATOM
133
N
ALA
A
27
−9.167
−4.829
−20.927
1.00
95.87
L111
N


ATOM
134
CA
ALA
A
27
−8.647
−4.902
−19.561
1.00
96.04
L111
C


ATOM
135
C
ALA
A
27
−8.916
−6.234
−18.858
1.00
93.76
L111
C


ATOM
136
O
ALA
A
27
−8.098
−7.152
−18.912
1.00
89.80
L111
O


ATOM
137
CB
ALA
A
27
−9.218
−3.755
−18.730
1.00
98.77
L111
C


ATOM
138
N
LEU
A
28
−10.057
−6.326
−18.185
1.00
92.88
L111
N


ATOM
139
CA
LEU
A
28
−10.424
−7.543
−17.473
1.00
92.03
L111
C


ATOM
140
C
LEU
A
28
−10.935
−8.593
−18.454
1.00
91.54
L111
C


ATOM
141
O
LEU
A
28
−10.992
−9.782
−18.137
1.00
91.91
L111
O


ATOM
142
CB
LEU
A
28
−11.495
−7.237
−16.422
1.00
92.11
L111
C


ATOM
143
CG
LEU
A
28
−12.912
−6.897
−16.898
1.00
91.83
L111
C


ATOM
144
CD1
LEU
A
28
−13.728
−6.405
−15.711
1.00
87.53
L111
C


ATOM
145
CD2
LEU
A
28
−12.870
−5.837
−17.996
1.00
89.79
L111
C


ATOM
146
N
GLY
A
29
−11.304
−8.143
−19.650
1.00
90.13
L111
N


ATOM
147
CA
GLY
A
29
−11.794
−9.060
−20.661
1.00
88.78
L111
C


ATOM
148
C
GLY
A
29
−10.732
−10.074
−21.044
1.00
88.80
L111
C


ATOM
149
O
GLY
A
29
−11.022
−11.064
−21.716
1.00
86.10
L111
O


ATOM
150
N
GLN
A
30
−9.497
−9.826
−20.616
1.00
89.64
L111
N


ATOM
151
CA
GLN
A
30
−8.389
−10.726
−20.919
1.00
91.11
L111
C


ATOM
152
C
GLN
A
30
−7.986
−11.569
−19.712
1.00
91.31
L111
C


ATOM
153
O
GLN
A
30
−6.980
−12.277
−19.747
1.00
89.05
L111
O


ATOM
154
CB
GLN
A
30
−7.177
−9.932
−21.439
1.00
92.85
L111
C


ATOM
155
CG
GLN
A
30
−6.545
−8.965
−20.440
1.00
90.47
L111
C


ATOM
156
CD
GLN
A
30
−5.431
−8.119
−21.055
1.00
92.62
L111
C


ATOM
157
OE1
GLN
A
30
−4.260
−8.511
−21.057
1.00
93.46
L111
O


ATOM
158
NE2
GLN
A
30
−5.796
−6.955
−21.584
1.00
92.21
L111
N


ATOM
159
N
HIS
A
31
−8.776
−11.489
−18.646
1.00
94.67
L111
N


ATOM
160
CA
HIS
A
31
−8.505
−12.256
−17.432
1.00
94.53
L111
C


ATOM
161
C
HIS
A
31
−9.521
−13.393
−17.329
1.00
93.97
L111
C


ATOM
162
O
HIS
A
31
−9.323
−14.351
−16.582
1.00
94.95
L111
O


ATOM
163
CB
HIS
A
31
−8.594
−11.350
−16.193
1.00
92.77
L111
C


ATOM
164
CG
HIS
A
31
−7.423
−10.425
−16.028
1.00
90.32
L111
C


ATOM
165
ND1
HIS
A
31
−7.531
−9.056
−16.160
1.00
88.08
L111
N


ATOM
166
CD2
HIS
A
31
−6.126
−10.671
−15.729
1.00
86.03
L111
C


ATOM
167
CE1
HIS
A
31
−6.351
−8.500
−15.950
1.00
81.34
L111
C


ATOM
168
NE2
HIS
A
31
−5.480
−9.457
−15.686
1.00
84.77
L111
N


ATOM
169
N
GLY
A
32
−10.604
−13.278
−18.094
1.00
93.26
L111
N


ATOM
170
CA
GLY
A
32
−11.637
−14.299
−18.091
1.00
90.69
L111
C


ATOM
171
C
GLY
A
32
−13.032
−13.721
−17.950
1.00
90.58
L111
C


ATOM
172
O
GLY
A
32
−14.022
−14.353
−18.323
1.00
91.06
L111
O


ATOM
173
N
VAL
A
33
−13.107
−12.509
−17.415
1.00
89.92
L111
N


ATOM
174
CA
VAL
A
33
−14.376
−11.822
−17.196
1.00
90.50
L111
C


ATOM
175
C
VAL
A
33
−15.254
−11.711
−18.443
1.00
88.55
L111
C


ATOM
176
O
VAL
A
33
−14.753
−11.581
−19.560
1.00
88.34
L111
O


ATOM
177
CB
VAL
A
33
−14.135
−10.398
−16.652
1.00
92.08
L111
C


ATOM
178
CG1
VAL
A
33
−15.292
−9.976
−15.770
1.00
90.59
L111
C


ATOM
179
CG2
VAL
A
33
−12.830
−10.351
−15.873
1.00
93.31
L111
C


ATOM
180
N
ASN
A
34
−16.568
−11.766
−18.237
1.00
89.80
L111
N


ATOM
181
CA
ASN
A
34
−17.533
−11.650
−19.327
1.00
94.89
L111
C


ATOM
182
C
ASN
A
34
−18.128
−10.245
−19.290
1.00
96.48
L111
C


ATOM
183
O
ASN
A
34
−19.141
−10.008
−18.630
1.00
97.04
L111
O


ATOM
184
CB
ASN
A
34
−18.661
−12.681
−19.182
1.00
97.83
L111
C


ATOM
185
CG
ASN
A
34
−18.405
−13.683
−18.072
1.00
100.00
L111
C


ATOM
186
OD1
ASN
A
34
−19.205
−13.813
−17.141
1.00
100.00
L111
O


ATOM
187
ND2
ASN
A
34
−17.291
−14.405
−18.167
1.00
100.00
L111
N


ATOM
188
N
ILE
A
35
−17.486
−9.325
−20.006
1.00
98.20
L111
N


ATOM
189
CA
ILE
A
35
−17.898
−7.922
−20.071
1.00
97.32
L111
C


ATOM
190
C
ILE
A
35
−19.392
−7.651
−19.844
1.00
99.75
L111
C


ATOM
191
O
ILE
A
35
−19.776
−7.148
−18.788
1.00
100.00
L111
O


ATOM
192
CB
ILE
A
35
−17.478
−7.282
−21.426
1.00
95.15
L111
C


ATOM
193
CG1
ILE
A
35
−16.341
−8.094
−22.064
1.00
93.73
L111
C


ATOM
194
CG2
ILE
A
35
−17.066
−5.823
−21.213
1.00
87.68
L111
C


ATOM
195
CD1
ILE
A
35
−14.960
−7.824
−21.485
1.00
91.66
L111
C


ATOM
196
N
MET
A
36
−20.220
−7.980
−20.835
1.00
100.00
L111
N


ATOM
197
CA
MET
A
36
−21.672
−7.767
−20.773
1.00
99.82
L111
C


ATOM
198
C
MET
A
36
−22.294
−7.868
−19.376
1.00
97.54
L111
C


ATOM
199
O
MET
A
36
−23.032
−6.975
−18.950
1.00
95.12
L111
O


ATOM
200
CB
MET
A
36
−22.384
−8.752
−21.713
1.00
100.00
L111
C


ATOM
201
CG
MET
A
36
−23.911
−8.645
−21.709
1.00
100.00
L111
C


ATOM
202
SD
MET
A
36
−24.759
−10.248
−21.810
1.00
100.00
L111
S


ATOM
203
CE
MET
A
36
−25.601
−10.300
−20.213
1.00
97.00
L111
C


ATOM
204
N
GLU
A
37
−22.001
−8.960
−18.674
1.00
95.35
L111
N


ATOM
205
CA
GLU
A
37
−22.535
−9.190
−17.335
1.00
92.68
L111
C


ATOM
206
C
GLU
A
37
−22.124
−8.100
−16.349
1.00
93.66
L111
C


ATOM
207
O
GLU
A
37
−22.925
−7.672
−15.515
1.00
91.34
L111
O


ATOM
208
CB
GLU
A
37
−22.071
−10.552
−16.819
1.00
90.67
L111
C


ATOM
209
CG
GLU
A
37
−23.205
−11.512
−16.511
1.00
93.38
L111
C


ATOM
210
CD
GLU
A
37
−22.929
−12.372
−15.290
1.00
96.55
L111
C


ATOM
211
OE1
GLU
A
37
−22.044
−13.254
−15.365
1.00
91.81
L111
O


ATOM
212
OE2
GLU
A
37
−23.600
−12.163
−14.256
1.00
99.15
L111
O


ATOM
213
N
PHE
A
38
−20.872
−7.657
−16.449
1.00
94.99
L111
N


ATOM
214
CA
PHE
A
38
−20.335
−6.614
−15.575
1.00
95.14
L111
C


ATOM
215
C
PHE
A
38
−20.928
−5.243
−15.907
1.00
93.32
L111
C


ATOM
216
O
PHE
A
38
−21.382
−4.527
−15.017
1.00
92.65
L111
O


ATOM
217
CB
PHE
A
38
−18.802
−6.565
−15.693
1.00
93.51
L111
C


ATOM
218
CG
PHE
A
38
−18.139
−5.586
−14.748
1.00
96.97
L111
C


ATOM
219
CD1
PHE
A
38
−18.716
−5.269
−13.518
1.00
98.99
L111
C


ATOM
220
CD2
PHE
A
38
−16.935
−4.978
−15.094
1.00
96.40
L111
C


ATOM
221
CE1
PHE
A
38
−18.106
−4.355
−12.651
1.00
95.25
L111
C


ATOM
222
CE2
PHE
A
38
−16.318
−4.064
−14.233
1.00
96.95
L111
C


ATOM
223
CZ
PHE
A
38
−16.905
−3.754
−13.010
1.00
92.93
L111
C


ATOM
224
N
CYS
A
39
−20.925
−4.884
−17.187
1.00
94.43
L111
N


ATOM
225
CA
CYS
A
39
−21.461
−3.597
−17.632
1.00
95.64
L111
C


ATOM
226
C
CYS
A
39
−22.840
−3.321
−17.044
1.00
96.32
L111
C


ATOM
227
O
CYS
A
39
−23.051
−2.295
−16.392
1.00
95.48
L111
O


ATOM
228
CB
CYS
A
39
−21.540
−3.563
−19.159
1.00
93.89
L111
C


ATOM
229
SG
CYS
A
39
−19.986
−3.992
−19.971
1.00
100.00
L111
S


ATOM
230
N
LYS
A
40
−23.774
−4.239
−17.279
1.00
96.81
L111
N


ATOM
231
CA
LYS
A
40
−25.133
−4.101
−16.768
1.00
96.22
L111
C


ATOM
232
C
LYS
A
40
−25.135
−4.168
−15.240
1.00
95.74
L111
C


ATOM
233
O
LYS
A
40
−25.823
−3.389
−14.576
1.00
96.26
L111
O


ATOM
234
CB
LYS
A
40
−26.029
−5.205
−17.339
1.00
95.66
L111
C


ATOM
235
CG
LYS
A
40
−25.956
−5.344
−18.855
1.00
97.68
L111
C


ATOM
236
CD
LYS
A
40
−27.132
−6.148
−19.401
1.00
95.99
L111
C


ATOM
237
CE
LYS
A
40
−26.947
−6.475
−20.880
1.00
94.18
L111
C


ATOM
238
NZ
LYS
A
40
−28.171
−6.189
−21.684
1.00
88.70
L111
N


ATOM
239
N
ARG
A
41
−24.356
−5.097
−14.688
1.00
92.53
L111
N


ATOM
240
CA
ARG
A
41
−24.262
−5.260
−13.239
1.00
89.97
L111
C


ATOM
241
C
ARG
A
41
−23.694
−4.003
−12.582
1.00
90.13
L111
C


ATOM
242
O
ARG
A
41
−24.306
−3.433
−11.679
1.00
91.63
L111
O


ATOM
243
CB
ARG
A
41
−23.375
−6.459
−12.900
1.00
85.72
L111
C


ATOM
244
CG
ARG
A
41
−24.143
−7.710
−12.526
1.00
85.51
L111
C


ATOM
245
CD
ARG
A
41
−23.330
−8.594
−11.595
1.00
90.22
L111
C


ATOM
246
NE
ARG
A
41
−22.610
−9.641
−12.318
1.00
88.90
L111
N


ATOM
247
CZ
ARG
A
41
−21.670
−10.412
−11.778
1.00
87.28
L111
C


ATOM
248
NH1
ARG
A
41
−21.332
−10.257
−10.501
1.00
84.21
L111
N


ATOM
249
NH2
ARG
A
41
−21.070
−11.340
−12.511
1.00
80.87
L111
N


ATOM
250
N
PHE
A
42
−22.517
−3.583
−13.037
1.00
87.95
L111
N


ATOM
251
CA
PHE
A
42
−21.865
−2.393
−12.509
1.00
82.17
L111
C


ATOM
252
C
PHE
A
42
−22.838
−1.228
−12.587
1.00
83.84
L111
C


ATOM
253
O
PHE
A
42
−23.215
−0.648
−11.566
1.00
84.64
L111
O


ATOM
254
CB
PHE
A
42
−20.608
−2.074
−13.325
1.00
78.71
L111
C


ATOM
255
CG
PHE
A
42
−19.934
−0.792
−12.925
1.00
83.84
L111
C


ATOM
256
CD1
PHE
A
42
−19.109
−0.745
−11.802
1.00
84.59
L111
C


ATOM
257
CD2
PHE
A
42
−20.132
0.373
−13.662
1.00
83.65
L111
C


ATOM
258
CE1
PHE
A
42
−18.490
0.444
−11.417
1.00
79.21
L111
C


ATOM
259
CE2
PHE
A
42
−19.518
1.567
−13.289
1.00
77.97
L111
C


ATOM
260
CZ
PHE
A
42
−18.695
1.602
−12.162
1.00
81.55
L111
C


ATOM
261
N
ASN
A
43
−23.253
−0.906
−13.808
1.00
85.30
L111
N


ATOM
262
CA
ASN
A
43
−24.181
0.191
−14.053
1.00
86.52
L111
C


ATOM
263
C
ASN
A
43
−25.488
0.062
−13.284
1.00
85.43
L111
C


ATOM
264
O
ASN
A
43
−26.281
1.000
−13.240
1.00
85.51
L111
O


ATOM
265
CB
ASN
A
43
−24.476
0.296
−15.548
1.00
86.27
L111
C


ATOM
266
CG
ASN
A
43
−23.265
0.716
−16.344
1.00
92.38
L111
C


ATOM
267
OD1
ASN
A
43
−22.347
1.340
−15.811
1.00
96.74
L111
O


ATOM
268
ND2
ASN
A
43
−23.249
0.374
−17.627
1.00
99.06
L111
N


ATOM
269
N
ALA
A
44
−25.712
−1.098
−12.679
1.00
85.49
L111
N


ATOM
270
CA
ALA
A
44
−26.930
−1.319
−11.912
1.00
84.79
L111
C


ATOM
271
C
ALA
A
44
−26.900
−0.515
−10.618
1.00
85.21
L111
C


ATOM
272
O
ALA
A
44
−27.668
0.433
−10.452
1.00
84.84
L111
O


ATOM
273
CB
ALA
A
44
−27.092
−2.797
−11.603
1.00
86.85
L111
C


ATOM
274
N
GLU
A
45
−26.005
−0.893
−9.708
1.00
85.98
L111
N


ATOM
275
CA
GLU
A
45
−25.885
−0.211
−8.420
1.00
90.10
L111
C


ATOM
276
C
GLU
A
45
−25.222
1.158
−8.536
1.00
89.46
L111
C


ATOM
277
O
GLU
A
45
−25.388
2.010
−7.661
1.00
88.02
L111
O


ATOM
278
CB
GLU
A
45
−25.103
−1.076
−7.427
1.00
89.91
L111
C


ATOM
279
CG
GLU
A
45
−23.812
−1.641
−7.983
1.00
93.26
L111
C


ATOM
280
CD
GLU
A
45
−23.917
−3.118
−8.293
1.00
95.55
L111
C


ATOM
281
OE1
GLU
A
45
−24.558
−3.844
−7.503
1.00
94.41
L111
O


ATOM
282
OE2
GLU
A
45
−23.360
−3.551
−9.326
1.00
98.04
L111
O


ATOM
283
N
THR
A
46
−24.463
1.369
−9.608
1.00
89.00
L111
N


ATOM
284
CA
THR
A
46
−23.806
2.655
−9.810
1.00
91.97
L111
C


ATOM
285
C
THR
A
46
−24.849
3.680
−10.261
1.00
95.20
L111
C


ATOM
286
O
THR
A
46
−24.516
4.737
−10.806
1.00
95.92
L111
O


ATOM
287
CB
THR
A
46
−22.681
2.560
−10.865
1.00
90.40
L111
C


ATOM
288
OG1
THR
A
46
−23.232
2.170
−12.129
1.00
88.41
L111
O


ATOM
289
CG2
THR
A
46
−21.634
1.545
−10.429
1.00
87.67
L111
C


ATOM
290
N
ALA
A
47
−26.116
3.343
−10.031
1.00
95.70
L111
N


ATOM
291
CA
ALA
A
47
−27.237
4.208
−10.374
1.00
93.30
L111
C


ATOM
292
C
ALA
A
47
−27.464
5.142
−9.191
1.00
95.59
L111
C


ATOM
293
O
ALA
A
47
−27.681
6.341
−9.367
1.00
97.14
L111
O


ATOM
294
CB
ALA
A
47
−28.488
3.373
−10.634
1.00
85.02
L111
C


ATOM
295
N
ASP
A
48
−27.409
4.580
−7.985
1.00
98.95
L111
N


ATOM
296
CA
ASP
A
48
−27.589
5.360
−6.764
1.00
100.00
L111
C


ATOM
297
C
ASP
A
48
−26.667
6.582
−6.823
1.00
100.00
L111
C


ATOM
298
O
ASP
A
48
−27.065
7.697
−6.477
1.00
100.00
L111
O


ATOM
299
CB
ASP
A
48
−27.248
4.515
−5.526
1.00
100.00
L111
C


ATOM
300
CG
ASP
A
48
−27.577
3.038
−5.706
1.00
100.00
L111
C


ATOM
301
OD1
ASP
A
48
−28.633
2.721
−6.297
1.00
100.00
L111
O


ATOM
302
OD2
ASP
A
48
−26.777
2.191
−5.249
1.00
100.00
L111
O


ATOM
303
N
LYS
A
49
−25.434
6.356
−7.270
1.00
100.00
L111
N


ATOM
304
CA
LYS
A
49
−24.440
7.419
−7.394
1.00
99.10
L111
C


ATOM
305
C
LYS
A
49
−24.009
7.547
−8.859
1.00
98.06
L111
C


ATOM
306
O
LYS
A
49
−23.106
6.842
−9.318
1.00
95.26
L111
O


ATOM
307
CB
LYS
A
49
−23.226
7.105
−6.512
1.00
94.97
L111
C


ATOM
308
CG
LYS
A
49
−23.561
6.908
−5.037
1.00
92.57
L111
C


ATOM
309
CD
LYS
A
49
−22.956
5.619
−4.498
1.00
93.51
L111
C


ATOM
310
CE
LYS
A
49
−21.611
5.873
−3.827
1.00
94.40
L111
C


ATOM
311
NZ
LYS
A
49
−20.528
4.998
−4.365
1.00
88.97
L111
N


ATOM
312
N
ALA
A
50
−24.661
8.450
−9.587
1.00
95.33
L111
N


ATOM
313
CA
ALA
A
50
−24.360
8.653
−10.999
1.00
93.02
L111
C


ATOM
314
C
ALA
A
50
−23.680
9.985
−11.305
1.00
91.25
L111
C


ATOM
315
O
ALA
A
50
−23.898
10.986
−10.619
1.00
90.14
L111
O


ATOM
316
CB
ALA
A
50
−25.636
8.522
−11.819
1.00
96.51
L111
C


ATOM
317
N
GLY
A
51
−22.861
9.984
−12.353
1.00
89.39
L111
N


ATOM
318
CA
GLY
A
51
−22.153
11.186
−12.752
1.00
90.09
L111
C


ATOM
319
C
GLY
A
51
−20.709
11.173
−12.289
1.00
91.40
L111
C


ATOM
320
O
GLY
A
51
−19.828
11.733
−12.943
1.00
91.06
L111
O


ATOM
321
N
MET
A
52
−20.465
10.520
−11.158
1.00
91.81
L111
N


ATOM
322
CA
MET
A
52
−19.125
10.440
−10.591
1.00
88.05
L111
C


ATOM
323
C
MET
A
52
−18.347
9.218
−11.062
1.00
84.95
L111
C


ATOM
324
O
MET
A
52
−18.927
8.206
−11.455
1.00
85.89
L111
O


ATOM
325
CB
MET
A
52
−19.207
10.425
−9.065
1.00
85.66
L111
C


ATOM
326
CG
MET
A
52
−20.358
11.236
−8.503
1.00
86.98
L111
C


ATOM
327
SD
MET
A
52
−20.028
11.840
−6.840
1.00
94.43
L111
S


ATOM
328
CE
MET
A
52
−18.414
12.577
−7.060
1.00
92.32
L111
C


ATOM
329
N
ILE
A
53
−17.025
9.330
−11.021
1.00
80.70
L111
N


ATOM
330
CA
ILE
A
53
−16.145
8.242
−11.415
1.00
76.40
L111
C


ATOM
331
C
ILE
A
53
−15.856
7.437
−10.157
1.00
76.01
L111
C


ATOM
332
O
ILE
A
53
−15.214
7.937
−9.238
1.00
80.34
L111
O


ATOM
333
CB
ILE
A
53
−14.815
8.781
−11.987
1.00
72.67
L111
C


ATOM
334
CG1
ILE
A
53
−15.035
9.279
−13.421
1.00
73.66
L111
C


ATOM
335
CG2
ILE
A
53
−13.735
7.706
−11.897
1.00
69.87
L111
C


ATOM
336
CD1
ILE
A
53
−14.073
8.712
−14.461
1.00
67.81
L111
C


ATOM
337
N
LEU
A
54
−16.337
6.199
−10.110
1.00
77.62
L111
N


ATOM
338
CA
LEU
A
54
−16.123
5.355
−8.940
1.00
75.31
L111
C


ATOM
339
C
LEU
A
54
−15.263
4.129
−9.242
1.00
73.26
L111
C


ATOM
340
O
LEU
A
54
−15.468
3.448
−10.248
1.00
69.71
L111
O


ATOM
341
CB
LEU
A
54
−17.471
4.913
−8.354
1.00
74.18
L111
C


ATOM
342
CG
LEU
A
54
−18.446
4.186
−9.283
1.00
76.71
L111
C


ATOM
343
CD1
LEU
A
54
−19.398
3.339
−8.456
1.00
78.50
L111
C


ATOM
344
CD2
LEU
A
54
−19.221
5.196
−10.112
1.00
77.50
L111
C


ATOM
345
N
PRO
A
55
−14.277
3.841
−8.368
1.00
73.50
L111
N


ATOM
346
CA
PRO
A
55
−13.379
2.694
−8.531
1.00
73.63
L111
C


ATOM
347
C
PRO
A
55
−13.998
1.397
−8.010
1.00
72.99
L111
C


ATOM
348
O
PRO
A
55
−14.516
1.349
−6.895
1.00
76.87
L111
O


ATOM
349
CB
PRO
A
55
−12.139
3.096
−7.736
1.00
69.02
L111
C


ATOM
350
CG
PRO
A
55
−12.654
4.000
−6.669
1.00
66.68
L111
C


ATOM
351
CD
PRO
A
55
−13.950
4.617
−7.157
1.00
72.43
L111
C


ATOM
352
N
VAL
A
56
−13.945
0.349
−8.825
1.00
70.25
L111
N


ATOM
353
CA
VAL
A
56
−14.496
−0.942
−8.440
1.00
70.19
L111
C


ATOM
354
C
VAL
A
56
−13.399
−1.999
−8.486
1.00
70.07
L111
C


ATOM
355
O
VAL
A
56
−12.502
−1.937
−9.329
1.00
67.23
L111
O


ATOM
356
CB
VAL
A
56
−15.654
−1.361
−9.384
1.00
67.10
L111
C


ATOM
357
CG1
VAL
A
56
−15.246
−1.161
−10.828
1.00
67.75
L111
C


ATOM
358
CG2
VAL
A
56
−16.034
−2.808
−9.143
1.00
62.26
L111
C


ATOM
359
N
VAL
A
57
−13.459
−2.956
−7.565
1.00
72.09
L111
N


ATOM
360
CA
VAL
A
57
−12.472
−4.027
−7.527
1.00
73.93
L111
C


ATOM
361
C
VAL
A
57
−13.121
−5.341
−7.934
1.00
76.94
L111
C


ATOM
362
O
VAL
A
57
−13.788
−6.001
−7.131
1.00
78.31
L111
O


ATOM
363
CB
VAL
A
57
−11.849
−4.189
−6.127
1.00
68.90
L111
C


ATOM
364
CG1
VAL
A
57
−10.940
−5.410
−6.104
1.00
66.82
L111
C


ATOM
365
CG2
VAL
A
57
−11.058
−2.948
−5.767
1.00
67.57
L111
C


ATOM
366
N
ILE
A
58
−12.923
−5.702
−9.197
1.00
79.04
L111
N


ATOM
367
CA
ILE
A
58
−13.467
−6.930
−9.756
1.00
77.59
L111
C


ATOM
368
C
ILE
A
58
−12.611
−8.115
−9.319
1.00
77.59
L111
C


ATOM
369
O
ILE
A
58
−11.383
−8.023
−9.262
1.00
73.20
L111
O


ATOM
370
CB
ILE
A
58
−13.490
−6.863
−11.307
1.00
76.77
L111
C


ATOM
371
CG1
ILE
A
58
−14.689
−6.033
−11.773
1.00
79.34
L111
C


ATOM
372
CG2
ILE
A
58
−13.526
−8.267
−11.904
1.00
73.40
L111
C


ATOM
373
CD1
ILE
A
58
−15.970
−6.832
−11.963
1.00
82.47
L111
C


ATOM
374
N
THR
A
59
−13.270
−9.224
−8.999
1.00
82.32
L111
N


ATOM
375
CA
THR
A
59
−12.581
−10.444
−8.589
1.00
82.77
L111
C


ATOM
376
C
THR
A
59
−13.114
−11.602
−9.430
1.00
83.16
L111
C


ATOM
377
O
THR
A
59
−14.312
−11.888
−9.417
1.00
78.62
L111
O


ATOM
378
CB
THR
A
59
−12.815
−10.761
−7.091
1.00
81.80
L111
C


ATOM
379
OG1
THR
A
59
−12.872
−9.539
−6.341
1.00
79.00
L111
O


ATOM
380
CG2
THR
A
59
−11.682
−11.629
−6.552
1.00
74.95
L111
C


ATOM
381
N
VAL
A
60
−12.221
−12.256
−10.168
1.00
84.63
L111
N


ATOM
382
CA
VAL
A
60
−12.603
−13.377
−11.022
1.00
85.45
L111
C


ATOM
383
C
VAL
A
60
−12.140
−14.723
−10.466
1.00
85.80
L111
C


ATOM
384
O
VAL
A
60
−10.947
−14.934
−10.228
1.00
83.46
L111
O


ATOM
385
CB
VAL
A
60
−12.030
−13.211
−12.445
1.00
85.69
L111
C


ATOM
386
CG1
VAL
A
60
−12.984
−12.383
−13.295
1.00
80.95
L111
C


ATOM
387
CG2
VAL
A
60
−10.653
−12.563
−12.380
1.00
84.62
L111
C


ATOM
388
N
TYR
A
61
−13.098
−15.629
−10.272
1.00
86.41
L111
N


ATOM
389
CA
TYR
A
61
−12.827
−16.965
−9.747
1.00
88.03
L111
C


ATOM
390
C
TYR
A
61
−12.459
−17.915
−10.877
1.00
89.54
L111
C


ATOM
391
O
TYR
A
61
−12.885
−17.721
−12.015
1.00
93.25
L111
O


ATOM
392
CB
TYR
A
61
−14.056
−17.486
−8.998
1.00
87.73
L111
C


ATOM
393
CG
TYR
A
61
−14.589
−16.487
−7.999
1.00
91.62
L111
C


ATOM
394
CD1
TYR
A
61
−13.873
−16.187
−6.837
1.00
89.76
L111
C


ATOM
395
CD2
TYR
A
61
−15.772
−15.788
−8.244
1.00
89.94
L111
C


ATOM
396
CE1
TYR
A
61
−14.316
−15.214
−5.947
1.00
89.76
L111
C


ATOM
397
CE2
TYR
A
61
−16.225
−14.810
−7.358
1.00
92.12
L111
C


ATOM
398
CZ
TYR
A
61
−15.489
−14.526
−6.214
1.00
92.07
L111
C


ATOM
399
OH
TYR
A
61
−15.910
−13.543
−5.347
1.00
94.51
L111
O


ATOM
400
N
GLU
A
62
−11.666
−18.936
−10.557
1.00
89.59
L111
N


ATOM
401
CA
GLU
A
62
−11.218
−19.921
−11.541
1.00
86.30
L111
C


ATOM
402
C
GLU
A
62
−12.248
−20.245
−12.626
1.00
84.38
L111
C


ATOM
403
O
GLU
A
62
−11.886
−20.480
−13.779
1.00
83.12
L111
O


ATOM
404
CB
GLU
A
62
−10.798
−21.217
−10.835
1.00
86.59
L111
C


ATOM
405
CG
GLU
A
62
−11.842
−21.781
−9.872
1.00
98.78
L111
C


ATOM
406
CD
GLU
A
62
−12.709
−22.865
−10.502
1.00
100.00
L111
C


ATOM
407
OE1
GLU
A
62
−12.149
−23.866
−11.007
1.00
100.00
L111
O


ATOM
408
OE2
GLU
A
62
−13.952
−22.711
−10.490
1.00
100.00
L111
O


ATOM
409
N
ASP
A
63
−13.527
−20.246
−12.261
1.00
83.04
L111
N


ATOM
410
CA
ASP
A
63
−14.593
−20.554
−13.210
1.00
83.65
L111
C


ATOM
411
C
ASP
A
63
−15.045
−19.360
−14.066
1.00
89.63
L111
C


ATOM
412
O
ASP
A
63
−16.153
−19.364
−14.609
1.00
90.46
L111
O


ATOM
413
CB
ASP
A
63
−15.795
−21.132
−12.461
1.00
80.07
L111
C


ATOM
414
CG
ASP
A
63
−16.738
−20.061
−11.968
1.00
79.27
L111
C


ATOM
415
OD1
ASP
A
63
−16.275
−19.146
−11.254
1.00
85.70
L111
O


ATOM
416
OD2
ASP
A
63
−17.941
−20.130
−12.298
1.00
76.37
L111
O


ATOM
417
N
LYS
A
64
−14.188
−18.347
−14.185
1.00
91.01
L111
N


ATOM
418
CA
LYS
A
64
−14.481
−17.150
−14.976
1.00
89.76
L111
C


ATOM
419
C
LYS
A
64
−15.585
−16.261
−14.398
1.00
89.42
L111
C


ATOM
420
O
LYS
A
64
−15.809
−15.149
−14.882
1.00
91.74
L111
O


ATOM
421
CB
LYS
A
64
−14.833
−17.540
−16.418
1.00
92.48
L111
C


ATOM
422
CG
LYS
A
64
−13.737
−17.237
−17.436
1.00
92.64
L111
C


ATOM
423
CD
LYS
A
64
−12.362
−17.682
−16.936
1.00
89.88
L111
C


ATOM
424
CE
LYS
A
64
−11.520
−18.269
−18.060
1.00
87.02
L111
C


ATOM
425
NZ
LYS
A
64
−12.331
−18.548
−19.280
1.00
89.34
L111
N


ATOM
426
N
SER
A
65
−16.280
−16.748
−13.373
1.00
88.30
L111
N


ATOM
427
CA
SER
A
65
−17.336
−15.966
−12.738
1.00
87.60
L111
C


ATOM
428
C
SER
A
65
−16.668
−14.827
−11.979
1.00
90.25
L111
C


ATOM
429
O
SER
A
65
−15.443
−14.800
−11.857
1.00
94.42
L111
O


ATOM
430
CB
SER
A
65
−18.138
−16.830
−11.766
1.00
83.90
L111
C


ATOM
431
OG
SER
A
65
−19.255
−16.115
−11.265
1.00
86.12
L111
O


ATOM
432
N
PHE
A
66
−17.459
−13.895
−11.456
1.00
89.68
L111
N


ATOM
433
CA
PHE
A
66
−16.872
−12.769
−10.737
1.00
86.65
L111
C


ATOM
434
C
PHE
A
66
−17.824
−11.963
−9.852
1.00
84.85
L111
C


ATOM
435
O
PHE
A
66
−19.049
−12.065
−9.956
1.00
84.96
L111
O


ATOM
436
CB
PHE
A
66
−16.207
−11.819
−11.740
1.00
83.79
L111
C


ATOM
437
CG
PHE
A
66
−17.166
−11.224
−12.736
1.00
84.15
L111
C


ATOM
438
CD1
PHE
A
66
−17.849
−10.044
−12.446
1.00
84.23
L111
C


ATOM
439
CD2
PHE
A
66
−17.402
−11.851
−13.955
1.00
85.47
L111
C


ATOM
440
CE1
PHE
A
66
−18.756
−9.496
−13.358
1.00
83.49
L111
C


ATOM
441
CE2
PHE
A
66
−18.307
−11.312
−14.875
1.00
85.83
L111
C


ATOM
442
CZ
PHE
A
66
−18.985
−10.132
−14.574
1.00
81.40
L111
C


ATOM
443
N
THR
A
67
−17.223
−11.166
−8.975
1.00
83.77
L111
N


ATOM
444
CA
THR
A
67
−17.937
−10.279
−8.065
1.00
79.66
L111
C


ATOM
445
C
THR
A
67
−17.102
−9.009
−8.062
1.00
79.21
L111
C


ATOM
446
O
THR
A
67
−16.005
−8.985
−8.623
1.00
78.86
L111
O


ATOM
447
CB
THR
A
67
−17.990
−10.835
−6.630
1.00
77.12
L111
C


ATOM
448
OG1
THR
A
67
−16.660
−11.101
−6.169
1.00
71.17
L111
O


ATOM
449
CG2
THR
A
67
−18.807
−12.112
−6.585
1.00
76.03
L111
C


ATOM
450
N
PHE
A
68
−17.603
−7.954
−7.439
1.00
77.92
L111
N


ATOM
451
CA
PHE
A
68
−16.850
−6.711
−7.409
1.00
76.33
L111
C


ATOM
452
C
PHE
A
68
−17.396
−5.750
−6.379
1.00
74.52
L111
C


ATOM
453
O
PHE
A
68
−18.609
−5.594
−6.241
1.00
74.74
L111
O


ATOM
454
CB
PHE
A
68
−16.871
−6.046
−8.789
1.00
79.76
L111
C


ATOM
455
CG
PHE
A
68
−18.255
−5.772
−9.311
1.00
78.43
L111
C


ATOM
456
CD1
PHE
A
68
−18.994
−6.781
−9.922
1.00
77.56
L111
C


ATOM
457
CD2
PHE
A
68
−18.821
−4.506
−9.193
1.00
77.06
L111
C


ATOM
458
CE1
PHE
A
68
−20.276
−6.532
−10.409
1.00
79.65
L111
C


ATOM
459
CE2
PHE
A
68
−20.103
−4.247
−9.677
1.00
76.90
L111
C


ATOM
460
CZ
PHE
A
68
−20.831
−5.263
−10.285
1.00
77.56
L111
C


ATOM
461
N
ILE
A
69
−16.491
−5.105
−5.656
1.00
73.94
L111
N


ATOM
462
CA
ILE
A
69
−16.885
−4.142
−4.644
1.00
70.90
L111
C


ATOM
463
C
ILE
A
69
−16.752
−2.736
−5.218
1.00
71.09
L111
C


ATOM
464
O
ILE
A
69
−15.773
−2.420
−5.901
1.00
68.28
L111
O


ATOM
465
CB
ILE
A
69
−16.010
−4.273
−3.377
1.00
65.36
L111
C


ATOM
466
CG1
ILE
A
69
−14.550
−3.966
−3.709
1.00
63.63
L111
C


ATOM
467
CG2
ILE
A
69
−16.119
−5.682
−2.820
1.00
61.98
L111
C


ATOM
468
CD1
ILE
A
69
−13.850
−3.146
−2.650
1.00
54.75
L111
C


ATOM
469
N
ILE
A
70
−17.753
−1.903
−4.962
1.00
68.20
L111
N


ATOM
470
CA
ILE
A
70
−17.740
−0.530
−5.443
1.00
65.88
L111
C


ATOM
471
C
ILE
A
70
−17.350
0.388
−4.283
1.00
61.84
L111
C


ATOM
472
O
ILE
A
70
−17.975
0.367
−3.222
1.00
60.58
L111
O


ATOM
473
CB
ILE
A
70
−19.126
−0.135
−6.022
1.00
66.46
L111
C


ATOM
474
CG1
ILE
A
70
−19.030
−0.026
−7.545
1.00
67.64
L111
C


ATOM
475
CG2
ILE
A
70
−19.608
1.187
−5.432
1.00
69.87
L111
C


ATOM
476
CD1
ILE
A
70
−19.695
−1.163
−8.283
1.00
63.00
L111
C


ATOM
477
N
LYS
A
71
−16.301
1.179
−4.489
1.00
55.49
L111
N


ATOM
478
CA
LYS
A
71
−15.820
2.092
−3.463
1.00
49.56
L111
C


ATOM
479
C
LYS
A
71
−16.181
3.531
−3.773
1.00
51.89
L111
C


ATOM
480
O
LYS
A
71
−16.814
3.826
−4.787
1.00
58.09
L111
O


ATOM
481
CB
LYS
A
71
−14.301
1.996
−3.325
1.00
41.23
L111
C


ATOM
482
CG
LYS
A
71
−13.736
0.617
−3.549
1.00
45.62
L111
C


ATOM
483
CD
LYS
A
71
−12.280
0.573
−3.134
1.00
47.82
L111
C


ATOM
484
CE
LYS
A
71
−12.066
−0.371
−1.962
1.00
53.59
L111
C


ATOM
485
NZ
LYS
A
71
−10.785
−1.130
−2.085
1.00
54.56
L111
N


ATOM
486
N
THR
A
72
−15.763
4.424
−2.883
1.00
51.64
L111
N


ATOM
487
CA
THR
A
72
−16.005
5.851
−3.034
1.00
48.54
L111
C


ATOM
488
C
THR
A
72
−15.040
6.390
−4.088
1.00
47.19
L111
C


ATOM
489
O
THR
A
72
−13.919
5.896
−4.227
1.00
51.43
L111
O


ATOM
490
CB
THR
A
72
−15.758
6.584
−1.711
1.00
49.44
L111
C


ATOM
491
OG1
THR
A
72
−14.374
6.469
−1.356
1.00
56.76
L111
O


ATOM
492
CG2
THR
A
72
−16.598
5.975
−0.602
1.00
49.50
L111
C


ATOM
493
N
PRO
A
73
−15.463
7.409
−4.850
1.00
43.35
L111
N


ATOM
494
CA
PRO
A
73
−14.603
7.989
−5.890
1.00
39.98
L111
C


ATOM
495
C
PRO
A
73
−13.260
8.487
−5.357
1.00
38.40
L111
C


ATOM
496
O
PRO
A
73
−13.153
8.908
−4.206
1.00
41.41
L111
O


ATOM
497
CB
PRO
A
73
−15.449
9.117
−6.483
1.00
40.56
L111
C


ATOM
498
CG
PRO
A
73
−16.536
9.360
−5.490
1.00
44.56
L111
C


ATOM
499
CD
PRO
A
73
−16.775
8.071
−4.781
1.00
42.40
L111
C


ATOM
500
N
PRO
A
74
−12.217
8.453
−6.198
1.00
36.48
L111
N


ATOM
501
CA
PRO
A
74
−10.882
8.904
−5.788
1.00
35.21
L111
C


ATOM
502
C
PRO
A
74
−10.881
10.296
−5.162
1.00
32.68
L111
C


ATOM
503
O
PRO
A
74
−11.778
11.102
−5.406
1.00
30.40
L111
O


ATOM
504
CB
PRO
A
74
−10.066
8.856
−7.082
1.00
37.87
L111
C


ATOM
505
CG
PRO
A
74
−10.787
7.880
−7.956
1.00
31.11
L111
C


ATOM
506
CD
PRO
A
74
−12.244
8.000
−7.601
1.00
35.28
L111
C


ATOM
507
N
ALA
A
75
−9.868
10.570
−4.348
1.00
31.58
L111
N


ATOM
508
CA
ALA
A
75
−9.763
11.862
−3.698
1.00
29.59
L111
C


ATOM
509
C
ALA
A
75
−9.517
12.901
−4.774
1.00
34.00
L111
C


ATOM
510
O
ALA
A
75
−10.210
13.915
−4.837
1.00
37.52
L111
O


ATOM
511
CB
ALA
A
75
−8.618
11.856
−2.694
1.00
34.28
L111
C


ATOM
512
N
SER
A
76
−8.532
12.638
−5.627
1.00
30.09
L111
N


ATOM
513
CA
SER
A
76
−8.211
13.561
−6.702
1.00
31.31
L111
C


ATOM
514
C
SER
A
76
−9.467
13.929
−7.483
1.00
31.25
L111
C


ATOM
515
O
SER
A
76
−9.661
15.091
−7.825
1.00
36.66
L111
O


ATOM
516
CB
SER
A
76
−7.169
12.951
−7.643
1.00
32.45
L111
C


ATOM
517
OG
SER
A
76
−7.473
11.608
−7.957
1.00
36.38
L111
O


ATOM
518
N
PHE
A
77
−10.323
12.946
−7.752
1.00
31.85
L111
N


ATOM
519
CA
PHE
A
77
−11.564
13.194
−8.489
1.00
34.16
L111
C


ATOM
520
C
PHE
A
77
−12.502
14.125
−7.734
1.00
38.37
L111
C


ATOM
521
O
PHE
A
77
−12.919
15.160
−8.251
1.00
41.67
L111
O


ATOM
522
CB
PHE
A
77
−12.307
11.894
−8.769
1.00
33.17
L111
C


ATOM
523
CG
PHE
A
77
−13.623
12.095
−9.468
1.00
40.76
L111
C


ATOM
524
CD1
PHE
A
77
−13.667
12.357
−10.837
1.00
47.11
L111
C


ATOM
525
CD2
PHE
A
77
−14.818
12.034
−8.761
1.00
42.42
L111
C


ATOM
526
CE1
PHE
A
77
−14.880
12.554
−11.492
1.00
38.82
L111
C


ATOM
527
CE2
PHE
A
77
−16.041
12.230
−9.409
1.00
42.68
L111
C


ATOM
528
CZ
PHE
A
77
−16.069
12.491
−10.777
1.00
38.85
L111
C


ATOM
529
N
LEU
A
78
−12.852
13.743
−6.514
1.00
39.27
L111
N


ATOM
530
CA
LEU
A
78
−13.732
14.568
−5.703
1.00
42.01
L111
C


ATOM
531
C
LEU
A
78
−13.162
15.986
−5.625
1.00
44.64
L111
C


ATOM
532
O
LEU
A
78
−13.892
16.967
−5.777
1.00
45.86
L111
O


ATOM
533
CB
LEU
A
78
−13.861
13.966
−4.303
1.00
42.80
L111
C


ATOM
534
CG
LEU
A
78
−14.640
12.646
−4.258
1.00
47.12
L111
C


ATOM
535
CD1
LEU
A
78
−14.485
11.973
−2.899
1.00
38.14
L111
C


ATOM
536
CD2
LEU
A
78
−16.108
12.925
−4.548
1.00
50.88
L111
C


ATOM
537
N
LEU
A
79
−11.851
16.081
−5.406
1.00
43.07
L111
N


ATOM
538
CA
LEU
A
79
−11.164
17.367
−5.309
1.00
34.91
L111
C


ATOM
539
C
LEU
A
79
−11.352
18.182
−6.580
1.00
35.68
L111
C


ATOM
540
O
LEU
A
79
−11.701
19.355
−6.522
1.00
36.29
L111
O


ATOM
541
CB
LEU
A
79
−9.676
17.150
−5.056
1.00
32.85
L111
C


ATOM
542
CG
LEU
A
79
−9.326
16.833
−3.603
1.00
29.72
L111
C


ATOM
543
CD1
LEU
A
79
−7.848
16.529
−3.480
1.00
33.33
L111
C


ATOM
544
CD2
LEU
A
79
−9.703
18.013
−2.730
1.00
29.46
L111
C


ATOM
545
N
LYS
A
80
−11.113
17.558
−7.727
1.00
39.06
L111
N


ATOM
546
CA
LYS
A
80
−11.292
18.235
−9.006
1.00
38.30
L111
C


ATOM
547
C
LYS
A
80
−12.692
18.832
−8.990
1.00
39.56
L111
C


ATOM
548
O
LYS
A
80
−12.872
20.036
−9.144
1.00
44.34
L111
O


ATOM
549
CB
LYS
A
80
−11.191
17.239
−10.163
1.00
32.02
L111
C


ATOM
550
CG
LYS
A
80
−9.805
17.066
−10.750
1.00
32.26
L111
C


ATOM
551
CD
LYS
A
80
−9.758
15.821
−11.628
1.00
37.75
L111
C


ATOM
552
CE
LYS
A
80
−8.410
15.660
−12.313
1.00
49.50
L111
C


ATOM
553
NZ
LYS
A
80
−8.046
14.224
−12.490
1.00
54.98
L111
N


ATOM
554
N
LYS
A
81
−13.681
17.969
−8.789
1.00
39.53
L111
N


ATOM
555
CA
LYS
A
81
−15.070
18.386
−8.754
1.00
38.23
L111
C


ATOM
556
C
LYS
A
81
−15.268
19.576
−7.832
1.00
41.10
L111
C


ATOM
557
O
LYS
A
81
−15.797
20.603
−8.242
1.00
50.63
L111
O


ATOM
558
CB
LYS
A
81
−15.949
17.230
−8.290
1.00
40.15
L111
C


ATOM
559
CG
LYS
A
81
−17.433
17.521
−8.367
1.00
56.64
L111
C


ATOM
560
CD
LYS
A
81
−18.209
16.317
−8.878
1.00
68.16
L111
C


ATOM
561
CE
LYS
A
81
−19.133
15.761
−7.799
1.00
76.64
L111
C


ATOM
562
NZ
LYS
A
81
−18.420
15.535
−6.502
1.00
78.09
L111
N


ATOM
563
N
ALA
A
82
−14.836
19.435
−6.585
1.00
45.28
L111
N


ATOM
564
CA
ALA
A
82
−14.976
20.500
−5.598
1.00
43.40
L111
C


ATOM
565
C
ALA
A
82
−14.384
21.832
−6.056
1.00
49.00
L111
C


ATOM
566
O
ALA
A
82
−15.003
22.884
−5.892
1.00
53.59
L111
O


ATOM
567
CB
ALA
A
82
−14.330
20.076
−4.290
1.00
42.16
L111
C


ATOM
568
N
ALA
A
83
−13.183
21.790
−6.621
1.00
48.31
L111
N


ATOM
569
CA
ALA
A
83
−12.527
23.004
−7.089
1.00
44.61
L111
C


ATOM
570
C
ALA
A
83
−13.115
23.458
−8.416
1.00
44.02
L111
C


ATOM
571
O
ALA
A
83
−12.693
24.467
−8.978
1.00
50.26
L111
O


ATOM
572
CB
ALA
A
83
−11.042
22.764
−7.236
1.00
40.08
L111
C


ATOM
573
N
GLY
A
84
−14.086
22.699
−8.912
1.00
42.49
L111
N


ATOM
574
CA
GLY
A
84
−14.727
23.029
−10.169
1.00
37.87
L111
C


ATOM
575
C
GLY
A
84
−13.804
22.971
−11.370
1.00
39.67
L111
C


ATOM
576
O
GLY
A
84
−14.127
23.511
−12.424
1.00
50.03
L111
O


ATOM
577
N
ILE
A
85
−12.654
22.323
−11.226
1.00
37.41
L111
N


ATOM
578
CA
ILE
A
85
−11.715
22.219
−12.334
1.00
37.65
L111
C


ATOM
579
C
ILE
A
85
−11.826
20.868
−13.037
1.00
41.62
L111
C


ATOM
580
O
ILE
A
85
−12.532
19.974
−12.571
1.00
45.50
L111
O


ATOM
581
CB
ILE
A
85
−10.261
22.429
−11.863
1.00
37.93
L111
C


ATOM
582
CG1
ILE
A
85
−9.905
21.408
−10.784
1.00
32.73
L111
C


ATOM
583
CG2
ILE
A
85
−10.088
23.845
−11.336
1.00
42.04
L111
C


ATOM
584
CD1
ILE
A
85
−8.435
21.395
−10.442
1.00
22.67
L111
C


ATOM
585
N
GLU
A
86
−11.126
20.728
−14.159
1.00
45.67
L111
N


ATOM
586
CA
GLU
A
86
−11.156
19.499
−14.948
1.00
47.13
L111
C


ATOM
587
C
GLU
A
86
−9.874
18.675
−14.831
1.00
47.71
L111
C


ATOM
588
O
GLU
A
86
−9.882
17.460
−15.044
1.00
48.51
L111
O


ATOM
589
CB
GLU
A
86
−11.408
19.839
−16.421
1.00
57.79
L111
C


ATOM
590
CG
GLU
A
86
−12.374
18.896
−17.128
1.00
77.13
L111
C


ATOM
591
CD
GLU
A
86
−13.815
19.383
−17.078
1.00
86.58
L111
C


ATOM
592
OE1
GLU
A
86
−14.025
20.594
−16.849
1.00
90.24
L111
O


ATOM
593
OE2
GLU
A
86
−14.734
18.553
−17.268
1.00
89.81
L111
O


ATOM
594
N
LYS
A
87
−8.771
19.335
−14.499
1.00
39.94
L111
N


ATOM
595
CA
LYS
A
87
−7.499
18.645
−14.366
1.00
38.76
L111
C


ATOM
596
C
LYS
A
87
−6.699
19.204
−13.204
1.00
34.61
L111
C


ATOM
597
O
LYS
A
87
−6.981
20.291
−12.715
1.00
46.69
L111
O


ATOM
598
CB
LYS
A
87
−6.686
18.784
−15.656
1.00
41.37
L111
C


ATOM
599
CG
LYS
A
87
−7.279
18.057
−16.847
1.00
47.04
L111
C


ATOM
600
CD
LYS
A
87
−6.550
18.426
−18.128
1.00
53.23
L111
C


ATOM
601
CE
LYS
A
87
−5.833
17.224
−18.724
1.00
60.76
L111
C


ATOM
602
NZ
LYS
A
87
−6.109
15.961
−17.979
1.00
61.63
L111
N


ATOM
603
N
GLY
A
88
−5.703
18.452
−12.759
1.00
34.29
L111
N


ATOM
604
CA
GLY
A
88
−4.871
18.914
−11.669
1.00
33.53
L111
C


ATOM
605
C
GLY
A
88
−3.718
19.688
−12.261
1.00
35.94
L111
C


ATOM
606
O
GLY
A
88
−3.422
19.547
−13.445
1.00
37.03
L111
O


ATOM
607
N
SER
A
89
−3.065
20.511
−11.453
1.00
35.86
L111
N


ATOM
608
CA
SER
A
89
−1.941
21.285
−11.951
1.00
31.79
L111
C


ATOM
609
C
SER
A
89
−0.968
20.358
−12.658
1.00
33.45
L111
C


ATOM
610
O
SER
A
89
−0.868
19.185
−12.317
1.00
36.12
L111
O


ATOM
611
CB
SER
A
89
−1.227
21.987
−10.801
1.00
30.17
L111
C


ATOM
612
OG
SER
A
89
0.141
22.195
−11.114
1.00
29.65
L111
O


ATOM
613
N
SER
A
90
−0.260
20.881
−13.651
1.00
36.82
L111
N


ATOM
614
CA
SER
A
90
0.716
20.083
−14.372
1.00
35.62
L111
C


ATOM
615
C
SER
A
90
1.981
20.112
−13.530
1.00
35.74
L111
C


ATOM
616
O
SER
A
90
2.879
19.287
−13.692
1.00
37.58
L111
O


ATOM
617
CB
SER
A
90
0.976
20.682
−15.758
1.00
37.33
L111
C


ATOM
618
OG
SER
A
90
1.955
21.708
−15.701
1.00
51.94
L111
O


ATOM
619
N
GLU
A
91
2.034
21.083
−12.625
1.00
33.32
L111
N


ATOM
620
CA
GLU
A
91
3.166
21.246
−11.726
1.00
38.55
L111
C


ATOM
621
C
GLU
A
91
2.619
21.648
−10.362
1.00
37.86
L111
C


ATOM
622
O
GLU
A
91
2.553
22.832
−10.026
1.00
36.53
L111
O


ATOM
623
CB
GLU
A
91
4.115
22.317
−12.262
1.00
42.92
L111
C


ATOM
624
CG
GLU
A
91
4.927
21.857
−13.457
l.00
56.44
L111
C


ATOM
625
CD
GLU
A
91
6.025
22.832
−13.841
1.00
69.04
L111
C


ATOM
626
OE1
GLU
A
91
6.223
23.832
−13.113
1.00
67.53
L111
O


ATOM
627
OE2
GLU
A
91
6.692
22.593
−14.876
1.00
73.04
L111
O


ATOM
628
N
PRO
A
92
2.199
20.652
−9.561
1.00
39.75
L111
N


ATOM
629
CA
PRO
A
92
1.643
20.871
−8.222
1.00
37.71
L111
C


ATOM
630
C
PRO
A
92
2.536
21.749
−7.365
1.00
33.98
L111
C


ATOM
631
O
PRO
A
92
3.760
21.633
−7.418
1.00
31.75
L111
O


ATOM
632
CB
PRO
A
92
1.505
19.459
−7.655
1.00
34.90
L111
C


ATOM
633
CG
PRO
A
92
1.371
18.596
−8.852
1.00
30.25
L111
C


ATOM
634
CD
PRO
A
92
2.246
19.219
−9.898
1.00
39.42
L111
C


ATOM
635
N
LYS
A
93
1.910
22.625
−6.584
1.00
30.90
L111
N


ATOM
636
CA
LYS
A
93
2.620
23.544
−5.703
1.00
36.65
L111
C


ATOM
637
C
LYS
A
93
3.250
24.695
−6.477
1.00
36.64
L111
C


ATOM
638
O
LYS
A
93
3.181
25.841
−6.044
1.00
45.57
L111
O


ATOM
639
CB
LYS
A
93
3.699
22.800
−4.907
1.00
42.76
L111
C


ATOM
640
CG
LYS
A
93
4.532
23.681
−3.993
1.00
47.27
L111
C


ATOM
641
CD
LYS
A
93
4.991
22.907
−2.768
1.00
53.52
L111
C


ATOM
642
CE
LYS
A
93
5.915
23.744
−1.894
1.00
54.40
L111
C


ATOM
643
NZ
LYS
A
93
7.235
23.085
−1.673
1.00
61.73
L111
N


ATOM
644
N
ARG
A
94
3.864
24.394
−7.616
1.00
35.63
L111
N


ATOM
645
CA
ARG
A
94
4.486
25.432
−8.430
1.00
29.80
L111
C


ATOM
646
C
ARG
A
94
3.408
26.252
−9.125
1.00
32.19
L111
C


ATOM
647
O
ARG
A
94
3.593
27.443
−9.371
1.00
36.21
L111
O


ATOM
648
CB
ARG
A
94
5.418
24.817
−9.475
1.00
21.41
L111
C


ATOM
649
CG
ARG
A
94
6.818
24.559
−8.966
1.00
26.71
L111
C


ATOM
650
CD
ARG
A
94
7.779
24.180
−10.088
1.00
28.16
L111
C


ATOM
651
NE
ARG
A
94
9.002
23.582
−9.551
1.00
40.63
L111
N


ATOM
652
CZ
ARG
A
94
10.016
23.133
−10.289
1.00
42.98
L111
C


ATOM
653
NH1
ARG
A
94
9.965
23.212
−11.610
1.00
45.19
L111
N


ATOM
654
NH2
ARG
A
94
11.085
22.606
−9.704
1.00
48.46
L111
N


ATOM
655
N
LYS
A
95
2.284
25.612
−9.440
1.00
28.46
L111
N


ATOM
656
CA
LYS
A
95
1.177
26.298
−10.104
1.00
30.94
L111
C


ATOM
657
C
LYS
A
95
−0.145
25.834
−9.542
1.00
28.39
L111
C


ATOM
658
O
LYS
A
95
−0.511
24.679
−9.700
1.00
40.28
L111
O


ATOM
659
CB
LYS
A
95
1.169
26.024
−11.614
1.00
36.77
L111
C


ATOM
660
CG
LYS
A
95
2.531
25.791
−12.244
1.00
49.47
L111
C


ATOM
661
CD
LYS
A
95
2.426
25.746
−13.765
1.00
48.94
L111
C


ATOM
662
CE
LYS
A
95
3.782
25.970
−14.420
1.00
50.63
L111
C


ATOM
663
NZ
LYS
A
95
3.730
25.733
−15.886
1.00
46.96
L111
N


ATOM
664
N
ILE
A
96
−0.872
26.728
−8.892
1.00
30.02
L111
N


ATOM
665
CA
ILE
A
96
−2.162
26.357
−8.337
1.00
31.34
L111
C


ATOM
666
C
ILE
A
96
−3.209
26.537
−9.425
1.00
35.19
L111
C


ATOM
667
O
ILE
A
96
−3.286
27.593
−10.048
1.00
42.96
L111
O


ATOM
668
CB
ILE
A
96
−2.502
27.231
−7.115
1.00
33.87
L111
C


ATOM
669
CG1
ILE
A
96
−1.379
27.115
−6.079
1.00
33.04
L111
C


ATOM
670
CG2
ILE
A
96
−3.840
26.812
−6.518
1.00
28.64
L111
C


ATOM
671
CD1
ILE
A
96
−0.892
25.695
−5.843
i.00
35.36
L111
C


ATOM
672
N
VAL
A
97
−4.008
25.504
−9.664
1.00
32.56
L111
N


ATOM
673
CA
VAL
A
97
−5.022
25.570
−10.704
1.00
29.74
L111
C


ATOM
674
C
VAL
A
97
−6.427
25.650
−10.148
1.00
36.58
L111
C


ATOM
675
O
VAL
A
97
−7.399
25.737
−10.905
1.00
38.60
L111
O


ATOM
676
CB
VAL
A
97
−4.930
24.351
−11.648
1.00
38.47
L111
C


ATOM
677
CG1
VAL
A
97
−3.502
24.185
−12.123
1.00
37.01
L111
C


ATOM
678
CG2
VAL
A
97
−5.403
23.086
−10.940
1.00
37.97
L111
C


ATOM
679
N
GLY
A
98
−6.531
25.623
−8.823
1.00
35.02
L111
N


ATOM
680
CA
GLY
A
98
−7.836
25.690
−8.192
1.00
35.16
L111
C


ATOM
681
C
GLY
A
98
−7.744
25.779
−6.683
1.00
38.01
L111
C


ATOM
682
O
GLY
A
98
−6.648
25.832
−6.117
1.00
38.34
L111
O


ATOM
683
N
LYS
A
99
−8.896
25.801
−6.023
1.00
35.14
L111
N


ATOM
684
CA
LYS
A
99
−8.911
25.883
−4.575
1.00
40.57
L111
C


ATOM
685
C
LYS
A
99
−10.230
25.403
−3.991
1.00
42.95
L111
C


ATOM
686
O
LYS
A
99
−11.264
25.396
−4.663
1.00
42.23
L111
O


ATOM
687
CB
LYS
A
99
−8.634
27.320
−4.130
1.00
50.99
L111
C


ATOM
688
CG
LYS
A
99
−9.850
28.231
−4.172
1.00
60.57
L111
C


ATOM
689
CD
LYS
A
99
−9.469
29.678
−3.885
1.00
65.97
L111
C


ATOM
690
CE
LYS
A
99
−10.646
30.614
−4.127
1.00
63.49
L111
C


ATOM
691
NZ
LYS
A
99
−10.216
31.886
−4.768
1.00
65.04
L111
N


ATOM
692
N
VAL
A
100
−10.180
24.992
−2.731
1.00
40.70
L111
N


ATOM
693
CA
VAL
A
100
−11.361
24.511
−2.036
1.00
41.33
L111
C


ATOM
694
C
VAL
A
100
−11.330
24.980
−0.592
1.00
41.84
L111
C


ATOM
695
O
VAL
A
100
−10.263
25.188
−0.012
1.00
40.91
L111
O


ATOM
696
CB
VAL
A
100
−11.440
22.973
−2.057
1.00
42.37
L111
C


ATOM
697
CG1
VAL
A
100
−11.840
22.498
−3.442
1.00
43.81
L111
C


ATOM
698
CG2
VAL
A
100
−10.102
22.377
−1.651
1.00
37.38
L111
C


ATOM
699
N
THR
A
101
−12.511
25.145
−0.016
1.00
43.68
L111
N


ATOM
700
CA
THR
A
101
−12.629
25.595
1.355
1.00
42.43
L111
C


ATOM
701
C
THR
A
101
−12.362
24.454
2.321
1.00
45.89
L111
C


ATOM
702
O
THR
A
101
−12.495
23.284
1.963
1.00
46.60
L111
O


ATOM
703
CB
THR
A
101
−14.026
26.153
1.610
1.00
45.72
L111
C


ATOM
704
OG1
THR
A
101
−15.005
25.154
1.293
1.00
40.56
L111
O


ATOM
705
CG2
THR
A
101
−14.260
27.380
0.738
1.00
42.52
L111
C


ATOM
706
N
ARG
A
102
−11.981
24.799
3.545
1.00
49.33
L111
N


ATOM
707
CA
ARG
A
102
−11.701
23.797
4.565
1.00
49.44
L111
C


ATOM
708
C
ARG
A
102
−12.925
22.925
4.792
1.00
49.34
L111
C


ATOM
709
O
ARG
A
102
−12.807
21.744
5.115
1.00
53.45
L111
O


ATOM
710
CB
ARG
A
102
−11.301
24.469
5.879
1.00
51.60
L111
C


ATOM
711
CG
ARG
A
102
−10.126
23.806
6.574
1.00
64.32
L111
C


ATOM
712
CD
ARG
A
102
−10.579
23.003
7.777
1.00
72.71
L111
C


ATOM
713
NE
ARG
A
102
−10.495
23.786
9.006
1.00
86.85
L111
N


ATOM
714
CZ
ARG
A
102
−10.080
23.304
10.174
1.00
96.04
L111
C


ATOM
715
NH1
ARG
A
102
−9.710
22.033
10.275
1.00
95.91
L111
N


ATOM
716
NH2
ARG
A
102
−10.033
24.095
11.242
1.00
96.71
L111
N


ATOM
717
N
LYS
A
103
−14.103
23.514
4.626
1.00
50.48
L111
N


ATOM
718
CA
LYS
A
103
−15.341
22.774
4.811
1.00
51.76
L111
C


ATOM
719
C
LYS
A
103
−15.441
21.718
3.719
1.00
51.34
L111
C


ATOM
720
O
LYS
A
103
−15.884
20.600
3.966
1.00
59.36
L111
O


ATOM
721
CB
LYS
A
103
−16.545
23.721
4.751
1.00
53.67
L111
C


ATOM
722
CG
LYS
A
103
−17.839
23.135
5.319
1.00
62.90
L111
C


ATOM
723
CD
LYS
A
103
−17.717
22.781
6.806
1.00
65.48
L111
C


ATOM
724
CE
LYS
A
103
−18.840
21.841
7.257
1.00
63.76
L111
C


ATOM
725
NZ
LYS
A
103
−19.077
21.884
8.732
1.00
58.26
L111
N


ATOM
726
N
GLN
A
104
−15.013
22.073
2.512
1.00
51.89
L111
N


ATOM
727
CA
GLN
A
104
−15.052
21.145
1.388
1.00
44.08
L111
C


ATOM
728
C
GLN
A
104
−14.161
19.939
1.664
1.00
42.43
L111
C


ATOM
729
O
GLN
A
104
−14.519
18.804
1.347
1.00
40.53
L111
O


ATOM
730
CB
GLN
A
104
−14.602
21.850
0.110
1.00
42.64
L111
C


ATOM
731
CG
GLN
A
104
−15.663
22.751
−0.484
1.00
35.82
L111
C


ATOM
732
CD
GLN
A
104
−15.242
23.354
−1.804
1.00
44.67
L111
C


ATOM
733
OE1
GLN
A
104
−14.303
24.154
−1.867
1.00
37.53
L111
O


ATOM
734
NE2
GLN
A
104
−15.936
22.975
−2.873
1.00
35.39
L111
N


ATOM
735
N
ILE
A
105
−12.998
20.186
2.254
1.00
39.32
L111
N


ATOM
736
CA
ILE
A
105
−12.088
19.103
2.584
1.00
35.57
L111
C


ATOM
737
C
ILE
A
105
−12.846
18.187
3.525
1.00
41.32
L111
C


ATOM
738
O
ILE
A
105
−12.770
16.965
3.411
1.00
46.00
L111
O


ATOM
739
CB
ILE
A
105
−10.832
19.624
3.298
1.00
33.68
L111
C


ATOM
740
CG1
ILE
A
105
−9.873
20.242
2.277
1.00
32.96
L111
C


ATOM
741
CG2
ILE
A
105
−10.154
18.495
4.061
1.00
34.33
L111
C


ATOM
742
CD1
ILE
A
105
−9.501
19.321
1.131
1.00
34.42
L111
C


ATOM
743
N
GLU
A
106
−13.584
18.800
4.448
1.00
47.08
L111
N


ATOM
744
CA
GLU
A
106
−14.382
18.068
5.428
1.00
53.52
L111
C


ATOM
745
C
GLU
A
106
−15.411
17.186
4.719
1.00
55.13
L111
C


ATOM
746
O
GLU
A
106
−15.606
16.027
5.087
1.00
59.36
L111
O


ATOM
747
CB
GLU
A
106
−15.094
19.051
6.381
1.00
50.72
L111
C


ATOM
748
CG
GLU
A
106
−15.480
18.464
7.748
1.00
55.56
L111
C


ATOM
749
CD
GLU
A
106
−16.029
19.504
8.734
1.00
62.03
L111
C


ATOM
750
OE1
GLU
A
106
−15.308
20.476
9.054
1.00
63.26
L111
O


ATOM
751
OE2
GLU
A
106
−17.182
19.345
9.199
1.00
53.90
L111
O


ATOM
752
N
GLU
A
107
−16.061
17.731
3.695
1.00
51.75
L111
N


ATOM
753
CA
GLU
A
107
−17.071
16.982
2.954
1.00
52.07
L111
C


ATOM
754
C
GLU
A
107
−16.476
15.755
2.282
1.00
50.13
L111
C


ATOM
755
O
GLU
A
107
−16.990
14.642
2.417
1.00
49.53
L111
O


ATOM
756
CB
GLU
A
107
−17.720
17.871
1.891
1.00
56.84
L111
C


ATOM
757
CG
GLU
A
107
−17.859
19.328
2.293
1.00
73.20
L111
C


ATOM
758
CD
GLU
A
107
−18.843
20.088
1.422
1.00
81.27
L111
C


ATOM
759
OE1
GLU
A
107
−19.271
19.540
0.382
1.00
84.05
L111
O


ATOM
760
OE2
GLU
A
107
−19.187
21.237
1.779
1.00
86.15
L111
O


ATOM
761
N
ILE
A
108
−15.391
15.973
1.549
1.00
46.89
L111
N


ATOM
762
CA
ILE
A
108
−14.719
14.900
0.844
1.00
39.41
L111
C


ATOM
763
C
ILE
A
108
−14.222
13.854
1.829
1.00
40.77
L111
C


ATOM
764
O
ILE
A
108
−14.441
12.658
1.637
1.00
43.65
L111
O


ATOM
765
CB
ILE
A
108
−13.542
15.447
0.019
1.00
38.05
L111
C


ATOM
766
CG1
ILE
A
108
−14.072
16.428
−1.032
1.00
36.44
L111
C


ATOM
767
CG2
ILE
A
108
−12.796
14.305
−0.649
1.00
41.19
L111
C


ATOM
768
CD1
ILE
A
108
−13.004
17.084
−1.882
1.00
31.78
L111
C


ATOM
769
N
ALA
A
109
−13.561
14.303
2.891
1.00
40.57
L111
N


ATOM
770
CA
ALA
A
109
−13.053
13.380
3.895
1.00
42.41
L111
C


ATOM
771
C
ALA
A
109
−14.205
12.546
4.429
1.00
44.77
L111
C


ATOM
772
O
ALA
A
109
−14.051
11.356
4.685
1.00
48.40
L111
O


ATOM
773
CB
ALA
A
109
−12.393
14.140
5.032
1.00
38.72
L111
C


ATOM
774
N
LYS
A
110
−15.365
13.174
4.589
1.00
47.97
L111
N


ATOM
775
CA
LYS
A
110
−16.537
12.474
5.099
1.00
44.59
L111
C


ATOM
776
C
LYS
A
110
−17.027
11.474
4.066
1.00
45.30
L111
C


ATOM
777
O
LYS
A
110
−17.377
10.342
4.401
1.00
44.67
L111
O


ATOM
778
CB
LYS
A
110
−17.651
13.469
5.422
1.00
45.45
L111
C


ATOM
779
CG
LYS
A
110
−17.991
13.562
6.902
1.00
47.29
L111
C


ATOM
780
CD
LYS
A
110
−17.733
14.963
7.448
1.00
51.84
L111
C


ATOM
781
CE
LYS
A
110
−18.991
15.558
8.070
1.00
53.58
L111
C


ATOM
782
NZ
LYS
A
110
−18.712
16.257
9.356
1.00
55.16
L111
N


ATOM
783
N
THR
A
111
−17.043
11.902
2.807
1.00
44.49
L111
N


ATOM
784
CA
THR
A
111
−17.492
11.060
1.705
1.00
42.63
L111
C


ATOM
785
C
THR
A
111
−16.635
9.810
1.548
1.00
44.42
L111
C


ATOM
786
O
THR
A
111
−17.149
8.707
1.375
1.00
44.77
L111
O


ATOM
787
CB
THR
A
111
−17.452
11.830
0.376
1.00
40.13
L111
C


ATOM
788
OG1
THR
A
111
−18.545
12.754
0.325
1.00
46.15
L111
O


ATOM
789
CG2
THR
A
111
−17.552
10.871
−0.799
1.00
43.65
L111
C


ATOM
790
N
LYS
A
112
−15.323
9.995
1.609
1.00
42.25
L111
N


ATOM
791
CA
LYS
A
112
−14.382
8.898
1.448
1.00
42.77
L111
C


ATOM
792
C
LYS
A
112
−14.081
8.127
2.732
1.00
43.93
L111
C


ATOM
793
O
LYS
A
112
−13.321
7.157
2.713
1.00
47.28
L111
O


ATOM
794
CB
LYS
A
112
−13.072
9.442
0.873
1.00
44.33
L111
C


ATOM
795
CG
LYS
A
112
−13.129
9.772
−0.607
1.00
40.93
L111
C


ATOM
796
CD
LYS
A
112
−11.806
9.474
−1.281
1.00
35.66
L111
C


ATOM
797
CE
LYS
A
112
−11.377
8.032
−1.062
1.00
31.03
L111
C


ATOM
798
NZ
LYS
A
112
−11.960
7.113
−2.076
1.00
28.57
L111
N


ATOM
799
N
MET
A
113
−14.673
8.554
3.842
1.00
42.32
L111
N


ATOM
800
CA
MET
A
113
−14.436
7.911
5.132
1.00
41.26
L111
C


ATOM
801
C
MET
A
113
−14.492
6.379
5.116
1.00
39.35
L111
C


ATOM
802
O
MET
A
113
−13.619
5.717
5.688
1.00
39.20
L111
O


ATOM
803
CB
MET
A
113
−15.410
8.457
6.177
1.00
39.84
L111
C


ATOM
804
CG
MET
A
113
−14.931
8.283
7.609
1.00
45.81
L111
C


ATOM
805
SD
MET
A
113
−13.481
9.269
8.040
1.00
47.31
L111
S


ATOM
806
CE
MET
A
113
−14.261
10.787
8.610
1.00
49.60
L111
C


ATOM
807
N
PRO
A
114
−15.524
5.793
4.484
1.00
32.93
L111
N


ATOM
808
CA
PRO
A
114
−15.582
4.328
4.458
1.00
29.51
L111
C


ATOM
809
C
PRO
A
114
−14.301
3.703
3.912
1.00
35.05
L111
C


ATOM
810
O
PRO
A
114
−13.918
2.609
4.314
1.00
41.74
L111
O


ATOM
811
CB
PRO
A
114
−16.791
4.013
3.575
1.00
27.80
L111
C


ATOM
812
CG
PRO
A
114
−17.214
5.307
2.967
1.00
23.57
L111
C


ATOM
813
CD
PRO
A
114
−16.678
6.411
3.811
1.00
31.92
L111
C


ATOM
814
N
ASP
A
115
−13.629
4.408
3.008
1.00
38.82
L111
N


ATOM
815
CA
ASP
A
115
−12.399
3.898
2.419
1.00
36.41
L111
C


ATOM
816
C
ASP
A
115
−11.138
4.462
3.069
1.00
36.55
L111
C


ATOM
817
O
ASP
A
115
−10.025
4.080
2.713
1.00
40.35
L111
O


ATOM
818
CB
ASP
A
115
−12.385
4.193
0.919
1.00
48.68
L111
C


ATOM
819
CG
ASP
A
115
−13.453
3.418
0.162
1.00
57.41
L111
C


ATOM
820
OD1
ASP
A
115
−13.653
2.221
0.464
1.00
51.55
L111
O


ATOM
821
OD2
ASP
A
115
−14.090
4.009
−0.737
1.00
58.21
L111
O


ATOM
822
N
LEU
A
116
−11.311
5.368
4.024
1.00
38.89
L111
N


ATOM
823
CA
LEU
A
116
−10.178
5.969
4.720
1.00
33.57
L111
C


ATOM
824
C
LEU
A
116
−9.916
5.199
6.007
1.00
32.97
L111
C


ATOM
825
O
LEU
A
116
−10.817
4.567
6.547
1.00
40.69
L111
O


ATOM
826
CB
LEU
A
116
−10.482
7.427
5.055
1.00
38.53
L111
C


ATOM
827
CG
LEU
A
116
−9.930
8.533
4.156
1.00
37.13
L111
C


ATOM
828
CD1
LEU
A
116
−9.839
8.062
2.720
1.00
34.98
L111
C


ATOM
829
CD2
LEU
A
116
−10.837
9.742
4.261
1.00
33.33
L111
C


ATOM
830
N
ASN
A
117
−8.686
5.256
6.501
1.00
32.67
L111
N


ATOM
831
CA
ASN
A
117
−8.336
4.549
7.725
1.00
33.28
L111
C


ATOM
832
C
ASN
A
117
−8.052
5.502
8.889
1.00
39.76
L111
C


ATOM
833
O
ASN
A
117
−7.373
5.140
9.851
1.00
36.63
L111
O


ATOM
834
CB
ASN
A
117
−7.117
3.666
7.475
1.00
23.35
L111
C


ATOM
835
CG
ASN
A
117
−5.872
4.470
7.208
1.00
24.02
L111
C


ATOM
836
OD1
ASN
A
117
−5.949
5.659
6.916
1.00
31.18
L111
O


ATOM
837
ND2
ASN
A
117
−4.714
3.828
7.306
1.00
18.87
L111
N


ATOM
838
N
ALA
A
118
−8.572
6.720
8.799
1.00
41.20
L111
N


ATOM
839
CA
ALA
A
118
−8.363
7.710
9.846
1.00
41.18
L111
C


ATOM
840
C
ALA
A
118
−9.297
7.443
11.018
1.00
43.82
L111
C


ATOM
841
O
ALA
A
118
−10.455
7.069
10.827
1.00
45.81
L111
O


ATOM
842
CB
ALA
A
118
−8.604
9.103
9.296
1.00
41.30
L111
C


ATOM
843
N
ASN
A
119
−8.793
7.644
12.230
1.00
42.07
L111
N


ATOM
844
CA
ASN
A
119
−9.589
7.419
13.429
1.00
42.41
L111
C


ATOM
845
C
ASN
A
119
−10.370
8.660
13.847
1.00
48.14
L111
C


ATOM
846
O
ASN
A
119
−11.141
8.625
14.807
1.00
53.14
L111
O


ATOM
847
CB
ASN
A
119
−8.684
6.981
14.575
1.00
37.27
L111
C


ATOM
848
CG
ASN
A
119
−8.180
5.575
14.400
1.00
33.45
L111
C


ATOM
849
OD1
ASN
A
119
−8.886
4.714
13.876
1.00
31.47
L111
O


ATOM
850
ND2
ASN
A
119
−6.951
5.328
14.837
1.00
38.73
L111
N


ATOM
851
N
SER
A
120
−10.168
9.756
13.125
1.00
48.44
L111
N


ATOM
852
CA
SER
A
120
−10.851
11.005
13.430
1.00
43.86
L111
C


ATOM
853
C
SER
A
120
−11.091
11.809
12.163
1.00
45.90
L111
C


ATOM
854
O
SER
A
120
−10.321
11.715
11.208
1.00
53.71
L111
O


ATOM
855
CB
SER
A
120
−10.010
11.834
14.401
1.00
38.80
L111
C


ATOM
856
OG
SER
A
120
−8.642
11.834
14.030
1.00
32.06
L111
O


ATOM
857
N
LEU
A
121
−12.157
12.601
12.156
1.00
46.97
L111
N


ATOM
858
CA
LEU
A
121
−12.476
13.429
11.000
1.00
44.83
L111
C


ATOM
859
C
LEU
A
121
−11.297
14.333
10.678
1.00
45.31
L111
C


ATOM
860
O
LEU
A
121
−11.078
14.693
9.526
1.00
52.25
L111
O


ATOM
861
CB
LEU
A
121
−13.705
14.291
11.277
1.00
39.77
L111
C


ATOM
862
CG
LEU
A
121
−13.904
15.469
10.325
1.00
41.18
L111
C


ATOM
863
CD1
LEU
A
121
−14.063
14.958
8.900
1.00
41.06
L111
C


ATOM
864
CD2
LEU
A
121
−15.128
16.260
10.751
1.00
41.00
L111
C


ATOM
865
N
GLU
A
122
−10.542
14.701
11.705
1.00
46.54
L111
N


ATOM
866
CA
GLU
A
122
−9.383
15.562
11.522
1.00
47.46
L111
C


ATOM
867
C
GLU
A
122
−8.327
14.834
10.702
1.00
45.12
L111
C


ATOM
868
O
GLU
A
122
−7.781
15.383
9.747
1.00
51.65
L111
O


ATOM
869
CB
GLU
A
122
−8.807
15.962
12.881
1.00
45.32
L111
C


ATOM
870
CG
GLU
A
122
−9.646
16.987
13.629
1.00
57.78
L111
C


ATOM
871
CD
GLU
A
122
−10.643
16.353
14.588
1.00
63.03
L111
C


ATOM
872
OE1
GLU
A
122
−10.380
15.234
15.075
1.00
64.43
L111
O


ATOM
873
OE2
GLU
A
122
−11.690
16.979
14.857
1.00
69.35
L111
O


ATOM
874
N
ALA
A
123
−8.045
13.593
11.083
1.00
41.17
L111
N


ATOM
875
CA
ALA
A
123
−7.062
12.786
10.381
1.00
38.97
L111
C


ATOM
876
C
ALA
A
123
−7.516
12.566
8.944
1.00
41.17
L111
C


ATOM
877
O
ALA
A
123
−6.701
12.562
8.022
1.00
41.16
L111
O


ATOM
878
CB
ALA
A
123
−6.891
11.452
11.081
1.00
36.50
L111
C


ATOM
879
N
ALA
A
124
−8.822
12.389
8.760
1.00
36.64
L111
N


ATOM
880
CA
ALA
A
124
−9.390
12.168
7.432
1.00
36.26
L111
C


ATOM
881
C
ALA
A
124
−9.133
13.362
6.533
1.00
35.14
L111
C


ATOM
882
O
ALA
A
124
−8.742
13.207
5.379
1.00
41.09
L111
O


ATOM
883
CB
ALA
A
124
−10.886
11.914
7.533
1.00
32.82
L111
C


ATOM
884
N
MET
A
125
−9.358
14.555
7.072
1.00
38.73
L111
N


ATOM
885
CA
MET
A
125
−9.158
15.785
6.322
1.00
34.84
L111
C


ATOM
886
C
MET
A
125
−7.686
15.968
6.003
1.00
31.87
L111
C


ATOM
887
O
MET
A
125
−7.330
16.458
4.938
1.00
42.09
L111
O


ATOM
888
CB
MET
A
125
−9.671
16.977
7.126
1.00
35.51
L111
C


ATOM
889
CG
MET
A
125
−11.072
16.769
7.695
1.00
40.88
L111
C


ATOM
890
SD
MET
A
125
−12.008
18.287
7.948
1.00
45.99
L111
S


ATOM
891
CE
MET
A
125
−10.675
19.462
8.286
1.00
44.96
L111
C


ATOM
892
N
LYS
A
126
−6.831
15.567
6.930
1.00
28.09
L111
N


ATOM
893
CA
LYS
A
126
−5.397
15.684
6.730
1.00
28.15
L111
C


ATOM
894
C
LYS
A
126
−5.007
14.801
5.551
1.00
30.29
L111
C


ATOM
895
O
LYS
A
126
−4.107
15.129
4.781
1.00
32.85
L111
O


ATOM
896
CB
LYS
A
126
−4.652
15.229
7.989
1.00
34.95
L111
C


ATOM
897
CG
LYS
A
126
−4.010
16.351
8.781
1.00
28.05
L111
C


ATOM
898
CD
LYS
A
126
−4.465
16.328
10.229
1.00
31.31
L111
C


ATOM
899
CE
LYS
A
126
−3.431
15.676
11.140
1.00
39.80
L111
C


ATOM
900
NZ
LYS
A
126
−2.064
16.271
11.016
1.00
45.29
L111
N


ATOM
901
N
ILE
A
127
−5.691
13.669
5.417
1.00
32.92
L111
N


ATOM
902
CA
ILE
A
127
−5.414
12.748
4.325
1.00
29.89
L111
C


ATOM
903
C
ILE
A
127
−5.820
13.405
3.014
1.00
30.60
L111
C


ATOM
904
O
ILE
A
127
−5.024
13.492
2.086
1.00
36.08
L111
O


ATOM
905
CB
ILE
A
127
−6.179
11.423
4.501
1.00
23.98
L111
C


ATOM
906
CG1
ILE
A
127
−5.591
10.649
5.689
1.00
33.32
L111
C


ATOM
907
CG2
ILE
A
127
−6.074
10.590
3.234
1.00
26.83
L111
C


ATOM
908
CD1
ILE
A
127
−6.427
9.465
6.152
1.00
25.44
L111
C


ATOM
909
N
ILE
A
128
−7.060
13.875
2.947
1.00
30.31
L111
N


ATOM
910
CA
ILE
A
128
−7.559
14.543
1.756
1.00
27.70
L111
C


ATOM
911
C
ILE
A
128
−6.681
15.730
1.359
1.00
30.19
L111
C


ATOM
912
O
ILE
A
128
−6.406
15.939
0.181
1.00
37.83
L111
O


ATOM
913
CB
ILE
A
128
−8.980
15.065
1.974
1.00
29.26
L111
C


ATOM
914
CG1
ILE
A
128
−9.911
13.906
2.325
1.00
27.20
L111
C


ATOM
915
CG2
ILE
A
128
−9.454
15.802
0.731
1.00
29.10
L111
C


ATOM
916
CD1
ILE
A
128
−9.915
12.793
1.304
1.00
21.41
L111
C


ATOM
917
N
GLU
A
129
−6.245
16.507
2.342
1.00
27.35
L111
N


ATOM
918
CA
GLU
A
129
−5.412
17.669
2.065
1.00
28.43
L111
C


ATOM
919
C
GLU
A
129
−4.116
17.249
1.418
1.00
25.38
L111
C


ATOM
920
O
GLU
A
129
−3.554
17.983
0.613
1.00
33.17
L111
O


ATOM
921
CB
GLU
A
129
−5.092
18.429
3.348
1.00
39.34
L111
C


ATOM
922
CG
GLU
A
129
−6.223
19.289
3.870
1.00
49.18
L111
C


ATOM
923
CD
GLU
A
129
−6.093
19.546
5.355
1.00
57.36
L111
C


ATOM
924
OE1
GLU
A
129
−4.942
19.571
5.849
1.00
62.27
L111
O


ATOM
925
OE2
GLU
A
129
−7.136
19.716
6.024
1.00
61.09
L111
O


ATOM
926
N
GLY
A
130
−3.634
16.071
1.785
1.00
24.18
L111
N


ATOM
927
CA
GLY
A
130
−2.394
15.591
1.210
1.00
21.91
L111
C


ATOM
928
C
GLY
A
130
−2.536
15.392
−0.285
1.00
23.19
L111
C


ATOM
929
O
GLY
A
130
−1.597
15.625
−1.042
1.00
21.99
L111
O


ATOM
930
N
THR
A
131
−3.720
14.962
−0.705
1.00
22.49
L111
N


ATOM
931
CA
THR
A
131
−4.005
14.723
−2.111
1.00
25.94
L111
C


ATOM
932
C
THR
A
131
−4.160
16.049
−2.849
1.00
28.86
L111
C


ATOM
933
O
THR
A
131
−3.629
16.229
−3.946
1.00
31.66
L111
O


ATOM
934
CB
THR
A
131
−5.292
13.896
−2.270
1.00
27.10
L111
C


ATOM
935
OG1
THR
A
131
−5.078
12.577
−1.747
1.00
26.23
L111
O


ATOM
936
CG2
THR
A
131
−5.694
13.808
−3.734
1.00
27.07
L111
C


ATOM
937
N
ALA
A
132
−4.887
16.979
−2.241
1.00
27.56
L111
N


ATOM
938
CA
ALA
A
132
−5.096
18.292
−2.835
1.00
26.64
L111
C


ATOM
939
C
ALA
A
132
−3.753
18.974
−3.058
1.00
28.30
L111
C


ATOM
940
O
ALA
A
132
−3.524
19.602
−4.084
1.00
30.29
L111
O


ATOM
941
CB
ALA
A
132
−5.954
19.134
−1.922
1.00
32.54
L111
C


ATOM
942
N
LYS
A
133
−2.866
18.843
−2.082
1.00
29.52
L111
N


ATOM
943
CA
LYS
A
133
−1.545
19.443
−2.158
1.00
27.21
L111
C


ATOM
944
C
LYS
A
133
−0.754
18.848
−3.311
1.00
30.72
L111
C


ATOM
945
O
LYS
A
133
0.190
19.458
−3.813
1.00
34.77
L111
O


ATOM
946
CB
LYS
A
133
−0.784
19.205
−0.846
1.00
30.61
L111
C


ATOM
947
CG
LYS
A
133
−0.843
20.371
0.138
1.00
38.23
L111
C


ATOM
948
CD
LYS
A
133
−0.782
19.897
1.581
1.00
35.27
L111
C


ATOM
949
CE
LYS
A
133
0.653
19.826
2.079
1.00
45.39
L111
C


ATOM
950
NZ
LYS
A
133
0.737
19.680
3.568
1.00
50.50
L111
N


ATOM
951
N
SER
A
134
−1.141
17.650
−3.729
1.00
31.51
L111
N


ATOM
952
CA
SER
A
134
−0.441
16.966
−4.807
1.00
33.04
L111
C


ATOM
953
C
SER
A
134
−0.969
17.300
−6.202
1.00
30.13
L111
C


ATOM
954
O
SER
A
134
−0.345
16.952
−7.198
1.00
27.50
L111
O


ATOM
955
CB
SER
A
134
−0.510
15.452
−4.588
1.00
31.88
L111
C


ATOM
956
OG
SER
A
134
−1.741
14.927
−5.055
1.00
23.70
L111
O


ATOM
957
N
MET
A
135
−2.107
17.977
−6.276
1.00
26.88
L111
N


ATOM
958
CA
MET
A
135
−2.691
18.308
−7.563
1.00
25.82
L111
C


ATOM
959
C
MET
A
135
−2.887
19.801
−7.783
1.00
31.45
L111
C


ATOM
960
O
MET
A
135
−3.737
20.209
−8.581
1.00
30.19
L111
O


ATOM
961
CB
MET
A
135
−4.029
17.597
−7.711
1.00
27.23
L111
C


ATOM
962
CG
MET
A
135
−4.974
17.857
−6.574
1.00
22.80
L111
C


ATOM
963
SD
MET
A
135
−6.230
16.597
−6.491
1.00
37.09
L111
S


ATOM
964
CE
MET
A
135
−7.008
16.793
−8.089
1.00
41.07
L111
C


ATOM
965
N
GLY
A
136
−2.105
20.613
−7.078
1.00
27.82
L111
N


ATOM
966
CA
GLY
A
136
−2.215
22.050
−7.228
1.00
22.84
L111
C


ATOM
967
C
GLY
A
136
−3.569
22.630
−6.854
1.00
27.99
L111
C


ATOM
968
O
GLY
A
136
−4.068
23.538
−7.515
1.00
33.90
L111
O


ATOM
969
N
ILE
A
137
−4.181
22.099
−5.806
1.00
27.75
L111
N


ATOM
970
CA
ILE
A
137
−5.458
22.621
−5.345
1.00
29.45
L111
C


ATOM
971
C
ILE
A
137
−5.207
23.141
−3.934
1.00
37.77
L111
C


ATOM
972
O
ILE
A
137
−4.722
22.409
−3.066
1.00
42.44
L111
O


ATOM
973
CB
ILE
A
137
−6.553
21.535
−5.334
1.00
29.74
L111
C


ATOM
974
CG1
ILE
A
137
−6.755
20.994
−6.751
1.00
30.99
L111
C


ATOM
975
CG2
ILE
A
137
−7.864
22.117
−4.842
1.00
21.17
L111
C


ATOM
976
CD1
ILE
A
137
−7.883
19.989
−6.877
1.00
23.63
L111
C


ATOM
977
N
GLU
A
138
−5.508
24.419
−3.723
1.00
40.79
L111
N


ATOM
978
CA
GLU
A
138
−5.299
25.058
−2.435
1.00
39.24
L111
C


ATOM
979
C
GLU
A
138
−6.528
25.003
−1.549
1.00
43.73
L111
C


ATOM
980
O
GLU
A
138
−7.640
24.799
−2.031
1.00
48.97
L111
O


ATOM
981
CB
GLU
A
138
−4.903
26.506
−2.644
1.00
41.53
L111
C


ATOM
982
CG
GLU
A
138
−3.466
26.787
−2.294
1.00
59.35
L111
C


ATOM
983
CD
GLU
A
138
−3.094
28.228
−2.556
1.00
67.14
L111
C


ATOM
984
OE1
GLU
A
138
−3.950
28.970
−3.098
1.00
59.01
L111
O


ATOM
985
OE2
GLU
A
138
−1.950
28.613
−2.220
1.00
67.00
L111
O


ATOM
986
N
VAL
A
139
−6.316
25.193
−0.251
1.00
48.03
L111
N


ATOM
987
CA
VAL
A
139
−7.404
25.171
0.725
1.00
52.55
L111
C


ATOM
988
C
VAL
A
139
−7.561
26.549
1.370
1.00
53.32
L111
C


ATOM
989
O
VAL
A
139
−6.578
27.164
1.782
1.00
54.50
L111
O


ATOM
990
CB
VAL
A
139
−7.144
24.122
1.838
1.00
47.09
L111
C


ATOM
991
CG1
VAL
A
139
−7.486
22.741
1.332
1.00
46.28
L111
C


ATOM
992
CG2
VAL
A
139
−5.689
24.171
2.281
1.00
54.07
L111
C


ATOM
993
N
VAL
A
140
−8.799
27.028
1.454
1.00
57.53
L111
N


ATOM
994
CA
VAL
A
140
−9.076
28.334
2.045
1.00
58.40
L111
C


ATOM
995
C
VAL
A
140
−10.295
28.298
2.970
1.00
64.90
L111
C


ATOM
966
O
VAL
A
140
−11.243
27.540
2.674
1.00
63.16
L111
O


ATOM
997
CB
VAL
A
140
−9.321
29.394
0.950
1.00
56.76
L111
C


ATOM
998
CG1
VAL
A
140
−8.207
29.343
−0.082
1.00
48.47
L111
C


ATOM
999
CG2
VAL
A
140
−10.667
29.156
0.288
1.00
56.93
L111
C


ATOM
1000
OXT
VAL
A
140
−10.290
29.036
3.980
1.00
72.53
L111
O


TER
1001

VAL
A
140


ATOM
1002
N
LYS
B
71
−21.043
−5.854
−42.905
1.00
63.31
L112
N


ATOM
1003
CA
LYS
B
71
−20.335
−6.681
−43.925
1.00
62.12
L112
C


ATOM
1004
C
LYS
B
71
−20.331
−8.162
−43.563
1.00
64.08
L112
C


ATOM
1005
O
LYS
B
71
−20.688
−8.546
−42.446
1.00
64.38
L112
O


ATOM
1006
CB
LYS
B
71
−18.892
−6.202
−44.080
1.00
58.09
L112
C


ATOM
1007
CG
LYS
B
71
−18.753
−4.928
−44.883
1.00
57.55
L112
C


ATOM
1008
CD
LYS
B
71
−17.414
−4.877
−45.584
1.00
59.51
L112
C


ATOM
1009
CE
LYS
B
71
−17.502
−4.091
−46.883
1.00
73.52
L112
C


ATOM
1010
NZ
LYS
B
71
−16.276
−3.277
−47.136
1.00
74.38
L112
N


ATOM
1011
N
THR
B
72
−19.922
−8.992
−44.517
1.00
60.82
L112
N


ATOM
1012
CA
THR
B
72
−19.866
−10.432
−44.305
1.00
53.90
L112
C


ATOM
1013
C
THR
B
72
−18.602
−10.793
−43.534
1.00
45.75
L112
C


ATOM
1014
O
THR
B
72
−17.573
−10.123
−43.661
1.00
42.26
L112
O


ATOM
1015
CB
THR
B
72
−19.881
−11.190
−45.647
1.00
54.39
L112
C


ATOM
1016
OG1
THR
B
72
−20.261
−10.291
−46.695
1.00
53.11
L112
O


ATOM
1017
CG2
THR
B
72
−20.877
−12.340
−45.603
1.00
54.95
L112
C


ATOM
1018
N
PRO
B
73
−18.664
−11.860
−42.721
1.00
37.48
L112
N


ATOM
1019
CA
PRO
B
73
−17.507
−12.290
−41.935
1.00
34.20
L112
C


ATOM
1020
C
PRO
B
73
−16.302
−12.518
−42.828
1.00
36.67
L112
C


ATOM
1021
O
PRO
B
73
−16.441
−12.715
−44.034
1.00
42.32
L112
O


ATOM
1022
CB
PRO
B
73
−17.977
−13.578
−41.271
1.00
35.95
L112
C


ATOM
1023
CG
PRO
B
73
−19.465
−13.478
−41.261
1.00
38.50
L112
C


ATOM
1024
CD
PRO
B
73
−19.831
−12.733
−42.504
1.00
38.65
L112
C


ATOM
1025
N
PRO
B
74
−15.097
−12.500
−42.247
1.00
30.98
L112
N


ATOM
1026
CA
PRO
B
74
−13.896
−12.712
−43.056
1.00
29.22
L112
C


ATOM
1027
C
PRO
B
74
−13.949
−14.071
−43.737
1.00
30.46
L112
C


ATOM
1028
O
PRO
B
74
−14.664
−14.971
−43.292
1.00
34.58
L112
O


ATOM
1029
CB
PRO
B
74
−12.755
−12.620
−42.042
1.00
26.89
L112
C


ATOM
1030
CG
PRO
B
74
−13.334
−11.909
−40.876
1.00
16.14
L112
C


ATOM
1031
CD
PRO
B
74
−14.773
−12.302
−40.828
1.00
24.82
L112
C


ATOM
1032
N
ALA
B
75
−13.196
−14.217
−44.819
1.00
26.98
L112
N


ATOM
1033
CA
ALA
B
75
−13.162
−15.472
−45.540
1.00
21.93
L112
C


ATOM
1034
C
ALA
B
75
−12.623
−16.534
−44.597
1.00
29.69
L112
C


ATOM
1035
O
ALA
B
75
−13.190
−17.619
−44.481
1.00
33.14
L112
O


ATOM
1036
CB
ALA
B
75
−12.264
−15.346
−46.760
1.00
29.99
L112
C


ATOM
1037
N
SER
B
76
−11.530
−16.210
−43.912
1.00
29.96
L112
N


ATOM
1038
CA
SER
B
76
−10.911
−17.143
−42.978
1.00
31.14
L112
C


ATOM
1039
C
SER
B
76
−11.908
−17.595
−41.918
1.00
36.21
L112
C


ATOM
1040
O
SER
B
76
−11.922
−18.760
−41.517
1.00
38.58
L112
O


ATOM
1041
CB
SER
B
76
−9.700
−16.496
−42.305
1.00
28.76
L112
C


ATOM
1042
OG
SER
B
76
−10.103
−15.622
−41.266
1.00
33.61
L112
O


ATOM
1043
N
PHE
B
77
−12.748
−16.674
−41.465
1.00
35.12
L112
N


ATOM
1044
CA
PHE
B
77
−13.731
−17.018
−40.457
1.00
36.06
L112
C


ATOM
1045
C
PHE
B
77
−14.684
−18.047
−41.025
1.00
38.63
L112
C


ATOM
1046
O
PHE
B
77
−14.874
−19.116
−40.448
1.00
43.61
L112
O


ATOM
1047
CB
PHE
B
77
−14.518
−15.787
−40.025
1.00
44.62
L112
C


ATOM
1048
CG
PHE
B
77
−15.644
−16.097
−39.080
1.00
47.58
L112
C


ATOM
1049
CD1
PHE
B
77
−15.388
−16.347
−37.733
1.00
44.42
L112
C


ATOM
1050
CD2
PHE
B
77
−16.959
−16.151
−39.536
1.00
44.81
L112
C


ATOM
1051
CE1
PHE
B
77
−16.424
−16.646
−36.855
1.00
40.74
L112
C


ATOM
1052
CE2
PHE
B
77
−18.003
−16.449
−38.667
1.00
42.72
L112
C


ATOM
1053
CZ
PHE
B
77
−17.736
−16.697
−37.322
1.00
44.82
L112
C


ATOM
1054
N
LEU
B
78
−15.288
−17.719
−42.161
1.00
37.81
L112
N


ATOM
1055
CA
LEU
B
78
−16.228
−18.625
−42.810
1.00
36.34
L112
C


ATOM
1056
C
LEU
B
78
−15.574
−19.970
−43.100
1.00
31.89
L112
C


ATOM
1057
O
LEU
B
78
−16.204
−21.017
−42.980
1.00
35.90
L112
O


ATOM
1058
CB
LEU
B
78
−16.743
−17.998
−44.105
1.00
34.71
L112
C


ATOM
1059
CG
LEU
B
78
−17.603
−16.750
−43.895
1.00
33.80
L112
C


ATOM
1060
CD1
LEU
B
78
−18.030
−16.182
−45.238
1.00
29.39
L112
C


ATOM
1061
CD2
LEU
B
78
−18.817
−17.113
−43.052
1.00
29.74
L112
C


ATOM
1062
N
LEU
B
79
−14.302
−19.936
−43.474
1.00
26.28
L112
N


ATOM
1063
CA
LEU
B
79
−13.566
−21.153
−43.765
1.00
31.61
L112
C


ATOM
1064
C
LEU
B
79
−13.420
−22.002
−42.498
1.00
39.25
L112
C


ATOM
1065
O
LEU
B
79
−13.727
−23.194
−42.508
1.00
40.69
L112
O


ATOM
1066
CB
LEU
B
79
−12.192
−20.799
−44.344
1.00
31.36
L112
C


ATOM
1067
CG
LEU
B
79
−12.229
−20.369
−45.816
1.00
25.54
L112
C


ATOM
1068
CD1
LEU
B
79
−10.852
−19.971
−46.314
1.00
21.73
L112
C


ATOM
1069
CD2
LEU
B
79
−12.763
−21.520
−46.635
1.00
23.94
L112
C


ATOM
1070
N
LYS
B
80
−12.960
−21.384
−41.411
1.00
44.27
L112
N


ATOM
1071
CA
LYS
B
80
−12.794
−22.078
−40.131
1.00
39.57
L112
C


ATOM
1072
C
LYS
B
80
−14.075
−22.822
−39.785
1.00
35.79
L112
C


ATOM
1073
O
LYS
B
80
−14.049
−23.993
−39.418
1.00
37.45
L112
O


ATOM
1074
CB
LYS
B
80
−12.500
−21.077
−39.008
1.00
44.26
L112
C


ATOM
1075
CG
LYS
B
80
−11.028
−20.840
−38.710
1.00
46.47
L112
C


ATOM
1076
CD
LYS
B
80
−10.839
−19.591
−37.850
1.00
45.33
L112
C


ATOM
1077
CE
LYS
B
80
−9.377
−19.388
−37.474
1.00
50.24
L112
C


ATOM
1078
NZ
LYS
B
80
−9.071
−17.963
−37.174
1.00
50.61
L112
N


ATOM
1079
N
LYS
B
81
−15.197
−22.122
−39.907
1.00
34.23
L112
N


ATOM
1080
CA
LYS
B
81
−16.508
−22.682
−39.609
1.00
39.48
L112
C


ATOM
1081
C
LYS
B
81
−16.845
−23.880
−40.485
1.00
42.52
L112
C


ATOM
1082
O
LYS
B
81
−17.253
−24.929
−39.991
1.00
49.15
L112
O


ATOM
1083
CB
LYS
B
81
−17.580
−21.607
−39.787
1.00
41.03
L112
C


ATOM
1084
CG
LYS
B
81
−18.306
−21.234
−38.510
1.00
52.41
L112
C


ATOM
1085
CD
LYS
B
81
−19.812
−21.200
−38.730
1.00
68.51
L112
C


ATOM
1086
CE
LYS
B
81
−20.234
−19.983
−39.549
1.00
73.66
L112
C


ATOM
1087
NZ
LYS
B
81
−20.152
−20.217
−41.023
1.00
71.12
L112
N


ATOM
1088
N
ALA
B
82
−16.678
−23.722
−41.792
1.00
45.81
L112
N


ATOM
1089
CA
ALA
B
82
−16.979
−24.800
−42.725
1.00
44.23
L112
C


ATOM
1090
C
ALA
B
82
−16.154
−26.049
−42.431
1.00
40.55
L112
C


ATOM
1091
O
ALA
B
82
−16.662
−27.165
−42.503
1.00
39.77
L112
O


ATOM
1092
CB
ALA
B
82
−16.729
−24.336
−44.149
1.00
42.43
L112
C


ATOM
1093
N
ALA
B
83
−14.882
−25.855
−42.101
1.00
35.34
L112
N


ATOM
1094
CA
ALA
B
83
−13.990
−26.967
−41.807
1.00
33.10
L112
C


ATOM
1095
C
ALA
B
83
−14.259
−27.559
−40.431
1.00
40.90
L112
C


ATOM
1096
O
ALA
B
83
−13.797
−28.659
−40.123
1.00
42.00
L112
O


ATOM
1097
CB
ALA
B
83
−12.544
−26.514
−41.898
1.00
30.83
L112
C


ATOM
1098
N
GLY
B
84
−15.000
−26.823
−39.605
1.00
43.37
L112
N


ATOM
1099
CA
GLY
B
84
−15.320
−27.292
−38.267
1.00
40.61
L112
C


ATOM
1100
C
GLY
B
84
−14.164
−27.194
−37.287
1.00
41.90
L112
C


ATOM
1101
O
GLY
B
84
−14.061
−27.997
−36.361
1.00
45.63
L112
O


ATOM
1102
N
ILE
B
85
−13.283
−26.222
−37.495
1.00
40.72
L112
N


ATOM
1103
CA
ILE
B
85
−12.141
−26.025
−36.612
1.00
39.23
L112
C


ATOM
1104
C
ILE
B
85
−12.283
−24.664
−35.944
1.00
44.21
L112
C


ATOM
1105
O
ILE
B
85
−13.168
−23.884
−36.304
1.00
48.06
L112
O


ATOM
1106
CB
ILE
B
85
−10.801
−26.081
−37.388
1.00
34.91
L112
C


ATOM
1107
CG1
ILE
B
85
−10.738
−24.959
−38.423
1.00
34.57
L112
C


ATOM
1108
CG2
ILE
B
85
−10.657
−27.425
−38.076
1.00
33.20
L112
C


ATOM
1109
CD1
ILE
B
85
−9.477
−24.973
−39.258
1.00
32.16
L112
C


ATOM
1110
N
GLU
B
86
−11.422
−24.380
−34.972
1.00
45.20
L112
N


ATOM
1111
CA
GLU
B
86
−11.484
−23.108
−34.266
1.00
43.68
L112
C


ATOM
1112
C
GLU
B
86
−10.261
−22.245
−34.544
1.00
41.68
L112
C


ATOM
1113
O
GLU
B
86
−10.258
−21.049
−34.257
1.00
47.94
L112
O


ATOM
1114
CB
GLU
B
86
−11.632
−23.347
−32.760
1.00
46.15
L112
C


ATOM
1115
CG
GLU
B
86
−10.322
−23.581
−32.020
1.00
65.68
L112
C


ATOM
1116
CD
GLU
B
86
−10.394
−23.163
−30.561
1.00
76.24
L112
C


ATOM
1117
OE1
GLU
B
86
−11.440
−23.417
−29.922
1.00
79.61
L112
O


ATOM
1118
OE2
GLU
B
86
−9.409
−22.580
−30.054
1.00
77.24
L112
O


ATOM
1119
N
LYS
B
87
−9.222
−22.850
−35.103
1.00
33.13
L112
N


ATOM
1120
CA
LYS
B
87
−8.011
−22.109
−35.416
1.00
40.07
L112
C


ATOM
1121
C
LYS
B
87
−7.423
−22.570
−36.741
1.00
40.26
L112
C


ATOM
1122
O
LYS
B
87
−7.610
−23.712
−37.150
1.00
46.66
L112
O


ATOM
1123
CB
LYS
B
87
−6.973
−22.293
−34.306
1.00
43.57
L112
C


ATOM
1124
CG
LYS
B
87
−7.240
−21.468
−33.057
1.00
57.30
L112
C


ATOM
1125
CD
LYS
B
87
−6.210
−21.759
−31.970
1.00
60.56
L112
C


ATOM
1126
CE
LYS
B
87
−5.750
−20.483
−31.279
1.00
59.04
L112
C


ATOM
1127
NZ
LYS
B
87
−6.112
−19.261
−32.054
1.00
64.31
L112
N


ATOM
1128
N
GLY
B
88
−6.725
−21.671
−37.418
1.00
34.46
L112
N


ATOM
1129
CA
GLY
B
88
−6.110
−22.038
−38.672
1.00
33.11
L112
C


ATOM
1130
C
GLY
B
88
−4.818
−22.742
−38.333
1.00
31.13
L112
C


ATOM
1131
O
GLY
B
88
−4.402
−22.747
−37.180
1.00
34.45
L112
O


ATOM
1132
N
SER
B
89
−4.183
−23.345
−39.325
1.00
31.44
L112
N


ATOM
1133
CA
SER
B
89
−2.935
−24.043
−39.093
1.00
29.45
L112
C


ATOM
1134
C
SER
B
89
−1.871
−23.027
−38.709
1.00
37.64
L112
C


ATOM
1135
O
SER
B
89
−1.904
−21.889
−39.167
1.00
39.44
L112
O


ATOM
1136
CB
SER
B
89
−2.519
−24.789
−40.357
1.00
30.04
L112
C


ATOM
1137
OG
SER
B
89
−1.138
−25.097
−40.339
1.00
30.69
L112
O


ATOM
1138
N
SER
B
90
−0.932
−23.437
−37.863
1.00
34.79
L112
N


ATOM
1139
CA
SER
B
90
0.145
−22.556
−37.434
1.00
36.73
L112
C


ATOM
1140
C
SER
B
90
1.250
−22.593
−38.480
1.00
37.59
L112
C


ATOM
1141
O
SER
B
90
2.173
−21.778
−38.474
1.00
38.46
L112
O


ATOM
1142
CB
SER
B
90
0.698
−23.023
−36.092
1.00
42.80
L112
C


ATOM
1143
OG
SER
B
90
1.368
−24.265
−36.234
1.00
57.39
L112
O


ATOM
1144
N
GLU
B
91
1.153
−23.565
−39.373
1.00
40.27
L112
N


ATOM
1145
CA
GLU
B
91
2.122
−23.726
−40.445
1.00
44.62
L112
C


ATOM
1146
C
GLU
B
91
1.352
−24.125
−41.697
1.00
42.72
L112
C


ATOM
1147
O
GLU
B
91
1.316
−25.295
−42.067
1.00
49.13
L112
O


ATOM
1148
CB
GLU
B
91
3.135
−24.812
−40.085
1.00
47.12
L112
C


ATOM
1149
CG
GLU
B
91
4.520
−24.289
−39.768
1.00
58.48
L112
C


ATOM
1150
CD
GLU
B
91
5.431
−25.364
−39.208
1.00
65.15
L112
C


ATOM
1151
OE1
GLU
B
91
5.935
−26.197
−39.997
1.00
68.92
L112
O


ATOM
1152
OE2
GLU
B
91
5.643
−25.374
−37.976
1.00
74.00
L112
O


ATOM
1153
N
PRO
B
92
0.699
−23.154
−42.352
1.00
40.19
L112
N


ATOM
1154
CA
PRO
B
92
−0.071
−23.435
−43.566
1.00
40.89
L112
C


ATOM
1155
C
PRO
B
92
0.736
−24.213
−44.603
1.00
42.71
L112
C


ATOM
1156
O
PRO
B
92
1.955
−24.035
−44.720
1.00
32.77
L112
O


ATOM
1157
CB
PRO
B
92
−0.467
−22.049
−44.062
1.00
43.77
L112
C


ATOM
1158
CG
PRO
B
92
−0.489
−21.217
−42.818
1.00
42.90
L112
C


ATOM
1159
CD
PRO
B
92
0.642
−21.729
−41.987
1.00
35.83
L112
C


ATOM
1160
N
LYS
B
93
0.043
−25.074
−45.346
1.00
45.71
L112
N


ATOM
1161
CA
LYS
B
93
0.656
−25.905
−46.380
1.00
42.76
L112
C


ATOM
1162
C
LYS
B
93
1.431
−27.073
−45.773
1.00
42.07
L112
C


ATOM
1163
O
LYS
B
93
1.296
−28.210
−46.223
1.00
47.50
L112
O


ATOM
1164
CB
LYS
B
93
1.588
−25.068
−47.267
1.00
46.12
L112
C


ATOM
1165
CG
LYS
B
93
1.163
−24.984
−48.735
1.00
52.73
L112
C


ATOM
1166
CD
LYS
B
93
−0.145
−24.214
−48.924
1.00
53.15
L112
C


ATOM
1167
CE
LYS
B
93
0.025
−23.038
−49.883
1.00
56.74
L112
C


ATOM
1168
NZ
LYS
B
93
0.637
−23.435
−51.187
1.00
65.38
L112
N


ATOM
1169
N
ARG
B
94
2.232
−26.790
−44.748
1.00
39.69
L112
N


ATOM
1170
CA
ARG
B
94
3.028
−27.815
−44.077
1.00
28.33
L112
C


ATOM
1171
C
ARG
B
94
2.200
−28.678
−43.134
1.00
27.71
L112
C


ATOM
1172
O
ARG
B
94
2.515
−29.841
−42.919
1.00
39.31
L112
O


ATOM
1173
CB
ARG
B
94
4.159
−27.172
−43.282
1.00
22.60
L112
C


ATOM
1174
CG
ARG
B
94
5.305
−26.668
−44.121
1.00
29.42
L112
C


ATOM
1175
CD
ARG
B
94
6.358
−26.019
−43.246
1.00
31.23
L112
C


ATOM
1176
NE
ARG
B
94
7.463
−25.486
−44.033
1.00
42.70
L112
N


ATOM
1177
CZ
ARG
B
94
8.628
−25.108
−43.516
1.00
56.07
L112
C


ATOM
1178
NH1
ARG
B
94
8.833
−25.207
−42.207
1.00
58.35
L112
N


ATOM
1179
NH2
ARG
B
94
9.584
−24.628
−44.304
1.00
57.97
L112
N


ATOM
1180
N
LYS
B
95
1.146
−28.110
−42.568
1.00
27.38
L112
N


ATOM
1181
CA
LYS
B
95
0.301
−28.850
−41.645
1.00
29.34
L112
C


ATOM
1182
C
LYS
B
95
−1.150
−28.482
−41.891
1.00
30.96
L112
C


ATOM
1183
O
LYS
B
95
−1.551
−27.342
−41.680
1.00
36.81
L112
O


ATOM
1184
CB
LYS
B
95
0.688
−28.513
−40.200
1.00
39.33
L112
C


ATOM
1185
CG
LYS
B
95
0.177
−29.500
−39.158
1.00
54.73
L112
C


ATOM
1186
CD
LYS
B
95
−0.879
−28.870
−38.249
1.00
67.65
L112
C


ATOM
1187
CE
LYS
B
95
−0.393
−28.746
−36.801
1.00
74.12
L112
C


ATOM
1188
NZ
LYS
B
95
−0.959
−27.548
−36.096
1.00
63.57
L112
N


ATOM
1189
N
ILE
B
96
−1.937
−29.446
−42.345
1.00
32.10
L112
N


ATOM
1190
CA
ILE
B
96
−3.347
−29.195
−42.614
1.00
32.15
L112
C


ATOM
1191
C
ILE
B
96
−4.165
−29.436
−41.353
1.00
33.56
L112
C


ATOM
1192
O
ILE
B
96
−4.075
−30.496
−40.739
1.00
42.84
L112
O


ATOM
1193
CB
ILE
B
96
−3.863
−30.103
−43.759
1.00
28.05
L112
C


ATOM
1194
CG1
ILE
B
96
−3.017
−29.876
−45.014
1.00
11.50
L112
C


ATOM
1195
CG2
ILE
B
96
−5.330
−29.814
−44.048
1.00
19.38
L112
C


ATOM
1196
CD1
ILE
B
96
−2.904
−28.429
−45.429
1.00
19.93
L112
C


ATOM
1197
N
VAL
B
97
−4.964
−28.448
−40.973
1.00
32.84
L112
N


ATOM
1198
CA
VAL
B
97
−5.776
−28.552
−39.770
1.00
29.62
L112
C


ATOM
1199
C
VAL
B
97
−7.232
−28.853
−40.066
1.00
29.20
L112
C


ATOM
1200
O
VAL
B
97
−8.015
−29.112
−39.156
1.00
36.19
L112
O


ATOM
1201
CB
VAL
B
97
−5.717
−27.246
−38.949
1.00
28.85
L112
C


ATOM
1202
CG1
VAL
B
97
−4.288
−26.945
−38.556
1.00
28.11
L112
C


ATOM
1203
CG2
VAL
B
97
−6.291
−26.094
−39.760
1.00
28.49
L112
C


ATOM
1204
N
GLY
B
98
−7.605
−28.811
−41.337
1.00
34.31
L112
N


ATOM
1205
CA
GLY
B
98
−8.988
−29.072
−41.685
1.00
28.21
L112
C


ATOM
1206
C
GLY
B
98
−9.152
−29.147
−43.181
1.00
30.18
L112
C


ATOM
1207
O
GLY
B
98
−8.192
−28.965
−43.923
1.00
30.67
L112
O


ATOM
1208
N
LYS
B
99
−10.373
−29.402
−43.627
1.00
29.50
L112
N


ATOM
1209
CA
LYS
B
99
−10.634
−29.516
−45.046
1.00
32.51
L112
C


ATOM
1210
C
LYS
B
99
−12.080
−29.187
−45.374
1.00
36.44
L112
C


ATOM
1211
O
LYS
B
99
−12.976
−29.448
−44.575
1.00
35.95
L112
O


ATOM
1212
CB
LYS
B
99
−10.315
−30.937
−45.507
1.00
39.97
L112
C


ATOM
1213
CG
LYS
B
99
−10.933
−32.025
−44.639
1.00
41.83
L112
C


ATOM
1214
CD
LYS
B
99
−11.335
−33.237
−45.469
1.00
51.41
L112
C


ATOM
1215
CE
LYS
B
99
−10.486
−34.453
−45.134
1.00
53.02
L112
C


ATOM
1216
NZ
LYS
B
99
−11.298
−35.553
−44.538
1.00
66.17
L112
N


ATOM
1217
N
VAL
B
100
−12.298
−28.609
−46.555
1.00
40.79
L112
N


ATOM
1218
CA
VAL
B
100
−13.642
−28.263
−47.010
1.00
40.95
L112
C


ATOM
1219
C
VAL
B
100
−13.871
−28.788
−48.419
1.00
41.23
L112
C


ATOM
1220
O
VAL
B
100
−12.927
−28.948
−49.199
1.00
37.76
L112
O


ATOM
1221
CB
VAL
B
100
−13.877
−26.742
−47.033
1.00
42.14
L112
C


ATOM
1222
CG1
VAL
B
100
−14.062
−26.228
−45.623
1.00
47.48
L112
C


ATOM
1223
CG2
VAL
B
100
−12.714
−26.049
−47.719
1.00
46.52
L112
C


ATOM
1224
N
THR
B
101
−15.134
−29.054
−48.737
1.00
43.68
L112
N


ATOM
1225
CA
THR
B
101
−15.505
−29.556
−50.052
1.00
44.90
L112
C


ATOM
1226
C
THR
B
101
−15.572
−28.401
−51.030
1.00
46.97
L112
C


ATOM
1227
O
THR
B
101
−15.847
−27.266
−50.641
1.00
49.23
L112
O


ATOM
1228
CB
THR
B
101
−16.882
−30.228
−50.037
1.00
44.59
L112
C


ATOM
1229
OG1
THR
B
101
−17.875
−29.262
−49.670
1.00
47.42
L112
O


ATOM
1230
CG2
THR
B
101
−16.904
−31.382
−49.050
1.00
37.18
L112
C


ATOM
1231
N
ARG
B
102
−15.319
−28.692
−52.301
1.00
47.23
L112
N


ATOM
1232
CA
ARG
B
102
−15.376
−27.664
−53.324
1.00
42.99
L112
C


ATOM
1233
C
ARG
B
102
−16.760
−27.046
−53.255
1.00
39.27
L112
C


ATOM
1234
O
ARG
B
102
−16.947
−25.888
−53.609
1.00
51.83
L112
O


ATOM
1235
CB
ARG
B
102
−15.140
−28.272
−54.708
1.00
50.12
L112
C


ATOM
1236
CG
ARG
B
102
−14.295
−27.405
−55.639
1.00
58.67
L112
C


ATOM
1237
CD
ARG
B
102
−12.884
−27.964
−55.821
1.00
61.68
L112
C


ATOM
1238
NE
ARG
B
102
−12.827
−29.413
−55.632
1.00
63.94
L112
N


ATOM
1239
CZ
ARG
B
102
−11.703
−30.124
−55.623
1.00
67.71
L112
C


ATOM
1240
NH1
ARG
B
102
−10.534
−29.517
−55.793
1.00
66.40
L112
N


ATOM
1241
NH2
ARG
B
102
−11.747
−31.442
−55.443
1.00
60.88
L112
N


ATOM
1242
N
LYS
B
103
−17.730
−27.823
−52.786
1.00
37.67
L112
N


ATOM
1243
CA
LYS
B
103
−19.096
−27.333
−52.664
1.00
41.92
L112
C


ATOM
1244
C
LYS
B
103
−19.160
−26.308
−51.547
1.00
44.83
L112
C


ATOM
1245
O
LYS
B
103
−19.856
−25.298
−51.649
1.00
49.24
L112
O


ATOM
1246
CB
LYS
B
103
−20.056
−28.483
−52.354
1.00
49.35
L112
C


ATOM
1247
CG
LYS
B
103
−21.265
−28.079
−51.510
1.00
57.47
L112
C


ATOM
1248
CD
LYS
B
103
−22.244
−27.221
−52.298
1.00
66.45
L112
C


ATOM
1249
CE
LYS
B
103
−23.683
−27.670
−52.075
1.00
76.17
L112
C


ATOM
1250
NZ
LYS
B
103
−24.099
−27.557
−50.645
1.00
75.72
L112
N


ATOM
1251
N
GLN
B
104
−18.434
−26.578
−50.471
1.00
44.97
L112
N


ATOM
1252
CA
GLN
B
104
−18.412
−25.662
−49.347
1.00
43.50
L112
C


ATOM
1253
C
GLN
B
104
−17.766
−24.359
−49.796
1.00
37.68
L112
C


ATOM
1254
O
GLN
B
104
−18.268
−23.277
−49.500
1.00
38.95
L112
O


ATOM
1255
CB
GLN
B
104
−17.640
−26.279
−48.181
1.00
47.34
L112
C


ATOM
1256
CG
GLN
B
104
−18.442
−27.328
−47.425
1.00
42.38
L112
C


ATOM
1257
CD
GLN
B
104
−17.693
−27.890
−46.237
1.00
42.53
L112
C


ATOM
1258
OE1
GLN
B
104
−16.603
−28.446
−46.380
1.00
35.56
L112
O


ATOM
1259
NE2
GLN
B
104
−18.275
−27.745
−45.050
1.00
36.61
L112
N


ATOM
1260
N
ILE
B
105
−16.660
−24.471
−50.525
1.00
30.76
L112
N


ATOM
1261
CA
ILE
B
105
−15.962
−23.296
−51.026
1.00
35.17
L112
C


ATOM
1262
C
ILE
B
105
−16.931
−22.427
−51.811
1.00
39.38
L112
C


ATOM
1263
O
ILE
B
105
−16.880
−21.202
−51.736
1.00
44.28
L112
O


ATOM
1264
CB
ILE
B
105
−14.808
−23.678
−51.962
1.00
26.23
L112
C


ATOM
1265
CG1
ILE
B
105
−13.674
−24.314
−51.159
1.00
35.32
L112
C


ATOM
1266
CG2
ILE
B
105
−14.320
−22.442
−52.714
1.00
30.76
L112
C


ATOM
1267
CD1
ILE
B
105
−12.778
−23.317
−50.444
1.00
30.65
L112
C


ATOM
1268
N
GLU
B
106
−17.815
−23.074
−52.563
1.00
44.23
L112
N


ATOM
1269
CA
GLU
B
106
−18.800
−22.367
−53.366
1.00
48.57
L112
C


ATOM
1270
C
GLU
B
106
−19.776
−21.590
−52.488
1.00
50.45
L112
C


ATOM
1271
O
GLU
B
106
−20.083
−20.430
−52.769
1.00
52.09
L112
O


ATOM
1272
CB
GLU
B
106
−19.563
−23.358
−54.249
1.00
56.57
L112
C


ATOM
1273
CG
GLU
B
106
−20.814
−22.786
−54.920
1.00
65.87
L112
C


ATOM
1274
CD
GLU
B
106
−21.335
−23.664
−56.053
1.00
68.27
L112
C


ATOM
1275
OE1
GLU
B
106
−20.505
−24.254
−56.781
1.00
62.09
L112
O


ATOM
1276
OE2
GLU
B
106
−22.573
−23.762
−56.214
1.00
66.69
L112
O


ATOM
1277
N
GLU
B
107
−20.258
−22.222
−51.422
1.00
48.38
L112
N


ATOM
1278
CA
GLU
B
107
−21.204
−21.567
−50.523
1.00
50.26
L112
C


ATOM
1279
C
GLU
B
107
−20.610
−20.317
−49.890
1.00
50.25
L112
C


ATOM
1280
O
GLU
B
107
−21.311
−19.332
−49.661
1.00
52.98
L112
O


ATOM
1281
CB
GLU
B
107
−21.648
−22.527
−49.425
1.00
52.51
L112
C


ATOM
1282
CG
GLU
B
107
−22.481
−23.685
−49.921
1.00
72.08
L112
C


ATOM
1283
CD
GLU
B
107
−22.371
−24.896
−49.016
1.00
86.41
L112
C


ATOM
1284
OE1
GLU
B
107
−21.249
−25.188
−48.545
1.00
91.57
L112
O


ATOM
1285
OE2
GLU
B
107
−23.405
−25.554
−48.772
1.00
92.70
L112
O


ATOM
1286
N
ILE
B
108
−19.315
−20.355
−49.602
1.00
46.38
L112
N


ATOM
1287
CA
ILE
B
108
−18.667
−19.206
−48.999
1.00
43.09
L112
C


ATOM
1288
C
ILE
B
108
−18.525
−18.099
−50.030
1.00
42.47
L112
C


ATOM
1289
O
ILE
B
108
−18.815
−16.937
−49.748
1.00
47.10
L112
O


ATOM
1290
CB
ILE
B
108
−17.272
−19.565
−48.449
1.00
42.76
L112
C


ATOM
1291
CG1
ILE
B
108
−17.407
−20.613
−47.345
1.00
35.09
L112
C


ATOM
1292
CG2
ILE
B
108
−16.592
−18.317
−47.891
1.00
31.13
L112
C


ATOM
1293
CD1
ILE
B
108
−16.084
−21.041
−46.747
1.00
41.11
L112
C


ATOM
1294
N
ALA
B
109
−18.081
−18.464
−51.229
1.00
38.62
L112
N


ATOM
1295
CA
ALA
B
109
−17.900
−17.486
−52.293
1.00
38.24
L112
C


ATOM
1296
C
ALA
B
109
−19.208
−16.761
−52.539
1.00
37.79
L112
C


ATOM
1297
O
ALA
B
109
−19.222
−15.562
−52.807
1.00
37.18
L112
O


ATOM
1298
CB
ALA
B
109
−17.436
−18.172
−53.562
1.00
38.10
L112
C


ATOM
1299
N
LYS
B
110
−20.309
−17.497
−52.437
1.00
38.29
L112
N


ATOM
1300
CA
LYS
B
110
−21.626
−16.917
−52.647
1.00
42.58
L112
C


ATOM
1301
C
LYS
B
110
−21.945
−15.951
−51.518
1.00
45.99
L112
C


ATOM
1302
O
LYS
B
110
−22.468
−14.858
−51.747
1.00
55.26
L112
O


ATOM
1303
CB
LYS
B
110
−22.689
−18.016
−52.702
1.00
39.40
L112
C


ATOM
1304
CG
LYS
B
110
−22.558
−18.947
−53.898
1.00
51.26
L112
C


ATOM
1305
CD
LYS
B
110
−23.911
−19.512
−54.329
1.00
60.46
L112
C


ATOM
1306
CE
LYS
B
110
−23.897
−19.968
−55.790
1.00
63.75
L112
C


ATOM
1307
NZ
LYS
B
110
−24.464
−21.340
−55.985
1.00
64.25
L112
N


ATOM
1308
N
THR
B
111
−21.620
−16.357
−50.297
1.00
40.79
L112
N


ATOM
1309
CA
THR
B
111
−21.876
−15.527
−49.134
1.00
38.24
L112
C


ATOM
1310
C
THR
B
111
−21.088
−14.231
−49.196
1.00
42.37
L112
C


ATOM
1311
O
THR
B
111
−21.644
−13.152
−48.998
1.00
48.64
L112
O


ATOM
1312
CB
THR
B
111
−21.490
−16.256
−47.845
1.00
42.62
L112
C


ATOM
1313
OG1
THR
B
111
−22.140
−17.531
−47.812
1.00
49.22
L112
O


ATOM
1314
CG2
THR
B
111
−21.899
−15.441
−46.630
1.00
41.08
L112
C


ATOM
1315
N
LYS
B
112
−19.794
−14.346
−49.479
1.00
41.09
L112
N


ATOM
1316
CA
LYS
B
112
−18.900
−13.194
−49.544
1.00
38.50
L112
C


ATOM
1317
C
LYS
B
112
−18.910
−12.449
−50.879
1.00
43.09
L112
C


ATOM
1318
O
LYS
B
112
−18.246
−11.424
−51.018
1.00
40.13
L112
O


ATOM
1319
CB
LYS
B
112
−17.467
−13.640
−49.240
1.00
35.11
L112
C


ATOM
1320
CG
LYS
B
112
−17.124
−13.715
−47.764
1.00
33.43
L112
C


ATOM
1321
CD
LYS
B
112
−16.011
−12.742
−47.409
1.00
29.28
L112
C


ATOM
1322
CE
LYS
B
112
−16.567
−11.530
−46.680
1.00
35.42
L112
C


ATOM
1323
NZ
LYS
B
112
−15.524
−10.509
−46.385
1.00
31.34
L112
N


ATOM
1324
N
MET
B
113
−19.654
−12.957
−51.857
1.00
50.88
L112
N


ATOM
1325
CA
MET
B
113
−19.709
−12.331
−53.180
1.00
51.11
L112
C


ATOM
1326
C
MET
B
113
−19.879
−10.807
−53.156
1.00
49.15
L112
C


ATOM
1327
O
MET
B
113
−19.130
−10.081
−53.813
1.00
50.15
L112
O


ATOM
1328
CB
MET
B
113
−20.824
−12.962
−54.022
1.00
51.18
L112
C


ATOM
1329
CG
MET
B
113
−20.717
−12.654
−55.515
1.00
47.98
L112
C


ATOM
1330
SD
MET
B
113
−19.263
−13.400
−56.298
1.00
49.73
L112
S


ATOM
1331
CE
MET
B
113
−18.549
−11.969
−57.088
1.00
52.43
L112
C


ATOM
1332
N
PRO
B
114
−20.870
−10.301
−52.409
1.00
42.31
L112
N


ATOM
1333
CA
PRO
B
114
−21.051
−8.849
−52.369
1.00
41.88
L112
C


ATOM
1334
C
PRO
B
114
−19.781
−8.079
−51.997
1.00
44.88
L112
C


ATOM
1335
O
PRO
B
114
−19.589
−6.945
−52.439
1.00
51.97
L112
O


ATOM
1336
CB
PRO
B
114
−22.171
−8.646
−51.345
1.00
38.22
L112
C


ATOM
1337
CG
PRO
B
114
−22.290
−9.946
−50.621
1.00
43.79
L112
C


ATOM
1338
CD
PRO
B
114
−21.870
−11.000
−51.588
1.00
46.66
L112
C


ATOM
1339
N
ASP
B
115
−18.912
−8.690
−51.197
1.00
46.07
L112
N


ATOM
1340
CA
ASP
B
115
−17.673
−8.030
−50.785
1.00
45.61
L112
C


ATOM
1341
C
ASP
B
115
−16.506
−8.353
−51.709
1.00
42.88
L112
C


ATOM
1342
O
ASP
B
115
−15.435
−7.758
−51.598
1.00
47.89
L112
O


ATOM
1343
CB
ASP
B
115
−17.292
−8.429
−49.355
1.00
51.51
L112
C


ATOM
1344
CG
ASP
B
115
−18.431
−8.252
−48.368
1.00
50.88
L112
C


ATOM
1345
OD1
ASP
B
115
−19.514
−7.787
−48.779
1.00
57.98
L112
O


ATOM
1346
OD2
ASP
B
115
−18.240
−8.582
−47.178
1.00
59.37
L112
O


ATOM
1347
N
LEU
B
116
−16.713
−9.298
−52.618
1.00
40.70
L112
N


ATOM
1348
CA
LEU
B
116
−15.669
−9.698
−53.553
1.00
37.46
L112
C


ATOM
1349
C
LEU
B
116
−15.698
−8.849
−54.819
1.00
37.00
L112
C


ATOM
1350
O
LEU
B
116
−16.757
−8.385
−55.242
1.00
38.81
L112
O


ATOM
1351
CB
LEU
B
116
−15.851
−11.169
−53.939
1.00
40.60
L112
C


ATOM
1352
CG
LEU
B
116
−15.289
−12.293
−53.065
1.00
35.62
L112
C


ATOM
1353
CD1
LEU
B
116
−14.872
−11.765
−51.707
1.00
42.51
L112
C


ATOM
1354
CD2
LEU
B
116
−16.347
−13.368
−52.923
1.00
33.28
L112
C


ATOM
1355
N
ASN
B
117
−14.535
−8.653
−55.429
1.00
32.39
L112
N


ATOM
1356
CA
ASN
B
117
−14.467
−7.886
−56.662
1.00
32.20
L112
C


ATOM
1357
C
ASN
B
117
−14.427
−8.835
−57.867
1.00
37.64
L112
C


ATOM
1358
O
ASN
B
117
−14.193
−8.415
−59.001
1.00
35.01
L112
O


ATOM
1359
CB
ASN
B
117
−13.235
−6.984
−56.655
1.00
24.31
L112
C


ATOM
1360
CG
ASN
B
117
−11.952
−7.762
−56.709
1.00
29.72
L112
C


ATOM
1361
OD1
ASN
B
117
−11.914
−8.941
−56.354
1.00
32.78
L112
O


ATOM
1362
ND2
ASN
B
117
−10.883
−7.110
−57.154
1.00
25.55
L112
N


ATOM
1363
N
ALA
B
118
−14.662
−10.117
−57.608
1.00
39.75
L112
N


ATOM
1364
CA
ALA
B
118
−14.665
−11.130
−58.656
1.00
41.80
L112
C


ATOM
1365
C
ALA
B
118
−15.862
−10.910
−59.567
1.00
45.30
L112
C


ATOM
1366
O
ALA
B
118
−16.863
−10.330
−59.156
1.00
53.58
L112
O


ATOM
1367
CB
ALA
B
118
−14.734
−12.512
−58.043
1.00
30.65
L112
C


ATOM
1368
N
ASN
B
119
−15.760
−11.381
−60.804
1.00
46.03
L112
N


ATOM
1369
CA
ASN
B
119
−16.840
−11.216
−61.766
1.00
48.46
L112
C


ATOM
1370
C
ASN
B
119
−17.574
−12.516
−62.081
1.00
50.16
L112
C


ATOM
1371
O
ASN
B
119
−18.557
−12.512
−62.817
1.00
55.94
L112
O


ATOM
1372
CB
ASN
B
119
−16.287
−10.625
−63.061
1.00
49.26
L112
C


ATOM
1373
CG
ASN
B
119
−16.023
−9.137
−62.958
1.00
50.05
L112
C


ATOM
1374
OD1
ASN
B
119
−16.747
−8.407
−62.269
1.00
48.95
L112
O


ATOM
1375
ND2
ASN
B
119
−14.981
−8.674
−63.646
1.00
48.05
L112
N


ATOM
1376
N
SER
B
120
−17.096
−13.624
−61.527
1.00
51.92
L112
N


ATOM
1377
CA
SER
B
120
−17.711
−14.924
−61.771
1.00
47.70
L112
C


ATOM
1378
C
SER
B
120
−17.599
−15.828
−60.555
1.00
50.21
L112
C


ATOM
1379
O
SER
B
120
−16.614
−15.770
−59.823
1.00
58.54
L112
O


ATOM
1380
CB
SER
B
120
−17.034
−15.609
−62.964
1.00
46.48
L112
C


ATOM
1381
OG
SER
B
120
−15.617
−15.558
−62.866
1.00
29.64
L112
O


ATOM
1382
N
LEU
B
121
−18.607
−16.670
−60.346
1.00
49.76
L112
N


ATOM
1383
CA
LEU
B
121
−18.591
−17.600
−59.225
1.00
44.29
L112
C


ATOM
1384
C
LEU
B
121
−17.276
−18.369
−59.261
1.00
42.13
L112
C


ATOM
1385
O
LEU
B
121
−16.669
−18.628
−58.229
1.00
45.70
L112
O


ATOM
1386
CB
LEU
B
121
−19.760
−18.578
−59.327
1.00
41.45
L112
C


ATOM
1387
CG
LEU
B
121
−19.784
−19.676
−58.262
1.00
41.89
L112
C


ATOM
1388
CD1
LEU
B
121
−19.585
−19.051
−56.890
1.00
40.55
L112
C


ATOM
1389
CD2
LEU
B
121
−21.102
−20.431
−58.320
1.00
32.73
L112
C


ATOM
1390
N
GLU
B
122
−16.842
−18.722
−60.465
1.00
39.88
L112
N


ATOM
1391
CA
GLU
B
122
−15.593
−19.447
−60.666
1.00
40.08
L112
C


ATOM
1392
C
GLU
B
122
−14.444
−18.620
−60.091
1.00
38.04
L112
C


ATOM
1393
O
GLU
B
122
−13.606
−19.135
−59.355
1.00
43.79
L112
O


ATOM
1394
CB
GLU
B
122
−15.377
−19.699
−62.170
1.00
47.41
L112
C


ATOM
1395
CG
GLU
B
122
−14.120
−20.496
−62.548
1.00
66.40
L112
C


ATOM
1396
CD
GLU
B
122
−14.105
−20.935
−64.023
1.00
79.56
L112
C


ATOM
1397
OE1
GLU
B
122
−15.061
−21.614
−64.461
1.00
83.56
L112
O


ATOM
1398
OE2
GLU
B
122
−13.137
−20.604
−64.747
1.00
80.21
L112
O


ATOM
1399
N
ALA
B
123
−14.416
−17.332
−60.422
1.00
37.15
L112
N


ATOM
1400
CA
ALA
B
123
−13.369
−16.432
−59.946
1.00
31.33
L112
C


ATOM
1401
C
ALA
B
123
−13.466
−16.220
−58.440
1.00
32.49
L112
C


ATOM
1402
O
ALA
B
123
−12.458
−16.207
−57.736
1.00
32.50
L112
O


ATOM
1403
CB
ALA
B
123
−13.472
−15.096
−60.655
1.00
28.73
L112
C


ATOM
1404
N
ALA
B
124
−14.689
−16.042
−57.958
1.00
26.80
L112
N


ATOM
1405
CA
ALA
B
124
−14.937
−15.835
−56.545
1.00
22.39
L112
C


ATOM
1406
C
ALA
B
124
−14.365
−16.994
−55.736
1.00
30.24
L112
C


ATOM
1407
O
ALA
B
124
−13.632
−16.790
−54.773
1.00
32.38
L112
O


ATOM
1408
CB
ALA
B
124
−16.434
−15.714
−56.304
1.00
19.73
L112
C


ATOM
1409
N
MET
B
125
−14.695
−18.214
−56.147
1.00
38.83
L112
N


ATOM
1410
CA
MET
B
125
−14.232
−19.422
−55.468
1.00
34.24
L112
C


ATOM
1411
C
MET
B
125
−12.718
−19.546
−55.464
1.00
30.68
L112
C


ATOM
1412
O
MET
B
125
−12.142
−20.147
−54.562
1.00
39.64
L112
O


ATOM
1413
CB
MET
B
125
−14.839
−20.659
−56.125
1.00
37.17
L112
C


ATOM
1414
CG
MET
B
125
−16.346
−20.783
−55.948
1.00
34.83
L112
C


ATOM
1415
SD
MET
B
125
−16.993
−22.386
−56.480
1.00
44.61
L112
S


ATOM
1416
CE
MET
B
125
−15.586
−23.063
−57.397
1.00
33.28
L112
C


ATOM
1417
N
LYS
B
126
−12.074
−18.991
−56.480
1.00
26.30
L112
N


ATOM
1418
CA
LYS
B
126
−10.622
−19.038
−56.558
1.00
27.93
L112
C


ATOM
1419
C
LYS
B
126
−10.072
−18.083
−55.503
1.00
30.79
L112
C


ATOM
1420
O
LYS
B
126
−8.932
−18.220
−55.056
1.00
35.96
L112
O


ATOM
1421
CB
LYS
B
126
−10.146
−18.601
−57.946
1.00
32.20
L112
C


ATOM
1422
CG
LYS
B
126
−10.107
−19.703
−58.994
1.00
27.48
L112
C


ATOM
1423
CD
LYS
B
126
−8.844
−19.598
−59.850
1.00
40.52
L112
C


ATOM
1424
CE
LYS
B
126
−9.159
−19.142
−61.268
1.00
32.95
L112
C


ATOM
1425
NZ
LYS
B
126
−9.919
−20.188
−62.011
1.00
51.40
L112
N


ATOM
1426
N
ILE
B
127
−10.895
−17.110
−55.114
1.00
31.30
L112
N


ATOM
1427
CA
ILE
B
127
−10.511
−16.117
−54.111
1.00
30.96
L112
C


ATOM
1428
C
ILE
B
127
−10.523
−16.741
−52.718
1.00
28.53
L112
C


ATOM
1429
O
ILE
B
127
−9.570
−16.587
−51.952
1.00
27.30
L112
O


ATOM
1430
CB
ILE
B
127
−11.469
−14.899
−54.139
1.00
27.50
L112
C


ATOM
1431
CG1
ILE
B
127
−11.203
−14.064
−55.391
1.00
29.44
L112
C


ATOM
1432
CG2
ILE
B
127
−11.268
−14.038
−52.902
1.00
28.00
L112
C


ATOM
1433
CD1
ILE
B
127
−12.047
−12.810
−55.482
1.00
31.68
L112
C


ATOM
1434
N
ILE
B
128
−11.608
−17.439
−52.396
1.00
20.75
L112
N


ATOM
1435
CA
ILE
B
128
−11.731
−18.104
−51.111
1.00
18.60
L112
C


ATOM
1436
C
ILE
B
128
−10.637
−19.152
−50.969
1.00
23.21
L112
C


ATOM
1437
O
ILE
B
128
−9.936
−19.202
−49.960
1.00
34.11
L112
O


ATOM
1438
CB
ILE
B
128
−13.084
−18.796
−50.975
1.00
17.63
L112
C


ATOM
1439
CG1
ILE
B
128
−14.208
−17.807
−51.280
1.00
17.94
L112
C


ATOM
1440
CG2
ILE
B
128
−13.236
−19.348
−49.581
1.00
23.67
L112
C


ATOM
1441
CD1
ILE
B
128
−14.138
−16.529
−50.469
1.00
20.35
L112
C


ATOM
1442
N
GLU
B
129
−10.488
−19.985
−51.989
1.00
23.93
L112
N


ATOM
1443
CA
GLU
B
129
−9.473
−21.025
−51.982
1.00
27.79
L112
C


ATOM
1444
C
GLU
B
129
−8.116
−20.447
−51.612
1.00
28.96
L112
C


ATOM
1445
O
GLU
B
129
−7.332
−21.079
−50.907
1.00
34.08
L112
O


ATOM
1446
CB
GLU
B
129
−9.379
−21.666
−53.359
1.00
43.68
L112
C


ATOM
1447
CG
GLU
B
129
−9.007
−23.129
−53.344
1.00
54.25
L112
C


ATOM
1448
CD
GLU
B
129
−9.708
−23.894
−54.445
1.00
67.26
L112
C


ATOM
1449
OE1
GLU
B
129
−10.697
−23.356
−54.998
1.00
58.57
L112
O


ATOM
1450
OE2
GLU
B
129
−9.272
−25.027
−54.754
1.00
76.46
L112
O


ATOM
1451
N
GLY
B
130
−7.836
−19.248
−52.108
1.00
29.13
L112
N


ATOM
1452
CA
GLY
B
130
−6.571
−18.609
−51.809
1.00
23.84
L112
C


ATOM
1453
C
GLY
B
130
−6.440
−18.423
−50.315
1.00
27.27
L112
C


ATOM
1454
O
GLY
B
130
−5.372
−18.629
−49.735
1.00
29.16
L112
O


ATOM
1455
N
THR
B
131
−7.536
−18.031
−49.680
1.00
19.93
L112
N


ATOM
1456
CA
THR
B
131
−7.521
−17.839
−48.242
1.00
27.52
L112
C


ATOM
1457
C
THR
B
131
−7.337
−19.204
−47.579
1.00
28.05
L112
C


ATOM
1458
O
THR
B
131
−6.453
−19.383
−46.741
1.00
33.97
L112
O


ATOM
1459
CB
THR
B
131
−8.832
−17.187
−47.758
1.00
25.95
L112
C


ATOM
1460
OG1
THR
B
131
−8.954
−15.883
−48.335
1.00
19.66
L112
O


ATOM
1461
CG2
THR
B
131
−8.836
−17.050
−46.255
1.00
29.87
L112
C


ATOM
1462
N
ALA
B
132
−8.164
−20.167
−47.977
1.00
23.92
L112
N


ATOM
1463
CA
ALA
B
132
−8.101
−21.523
−47.436
1.00
21.36
L112
C


ATOM
1464
C
ALA
B
132
−6.704
−22.108
−47.505
1.00
21.61
L112
C


ATOM
1465
O
ALA
B
132
−6.253
−22.768
−46.575
1.00
34.50
L112
O


ATOM
1466
CB
ALA
B
132
−9.060
−22.428
−48.182
1.00
19.47
L112
C


ATOM
1467
N
LYS
B
133
−6.015
−21.870
−48.610
1.00
25.84
L112
N


ATOM
1468
CA
LYS
B
133
−4.674
−22.405
−48.779
1.00
29.20
L112
C


ATOM
1469
C
LYS
B
133
−3.693
−21.721
−47.851
1.00
27.88
L112
C


ATOM
1470
O
LYS
B
133
−2.642
−22.270
−47.530
1.00
37.04
L112
O


ATOM
1471
CB
LYS
B
133
−4.213
−22.232
−50.230
1.00
33.18
L112
C


ATOM
1472
CG
LYS
B
133
−5.011
−23.052
−51.235
1.00
37.46
L112
C


ATOM
1473
CD
LYS
B
133
−4.884
−22.487
−52.640
1.00
50.67
L112
C


ATOM
1474
CE
LYS
B
133
−3.636
−23.010
−53.343
1.00
51.75
L112
C


ATOM
1475
NZ
LYS
B
133
−3.389
−22.329
−54.654
1.00
54.53
L112
N


ATOM
1476
N
SER
B
134
−4.042
−20.518
−47.416
1.00
36.66
L112
N


ATOM
1477
CA
SER
B
134
−3.168
−19.747
−46.539
1.00
36.64
L112
C


ATOM
1478
C
SER
B
134
−3.344
−20.080
−45.066
1.00
33.11
L112
C


ATOM
1479
O
SER
B
134
−2.635
−19.541
−44.223
1.00
37.50
L112
O


ATOM
1480
CB
SER
B
134
−3.414
−18.252
−46.741
1.00
34.18
L112
C


ATOM
1481
OG
SER
B
134
−4.603
−17.857
−46.080
1.00
23.48
L112
O


ATOM
1482
N
MET
B
135
−4.281
−20.964
−44.748
1.00
29.84
L112
N


ATOM
1483
CA
MET
B
135
−4.509
−21.312
−43.357
1.00
23.70
L112
C


ATOM
1484
C
MET
B
135
−4.602
−22.808
−43.089
1.00
29.55
L112
C


ATOM
1485
O
MET
B
135
−5.283
−23.242
−42.161
1.00
23.32
L112
O


ATOM
1486
CB
MET
B
135
−5.768
−20.618
−42.857
1.00
22.94
L112
C


ATOM
1487
CG
MET
B
135
−7.034
−21.139
−43.448
1.00
17.81
L112
C


ATOM
1488
SD
MET
B
135
−8.303
−19.898
−43.327
1.00
34.08
L112
S


ATOM
1489
CE
MET
B
135
−9.264
−20.525
−41.959
1.00
35.79
L112
C


ATOM
1490
N
GLY
B
136
−3.914
−23.592
−43.910
1.00
35.43
L112
N


ATOM
1491
CA
GLY
B
136
−3.911
−25.030
−43.728
1.00
27.07
L112
C


ATOM
1492
C
GLY
B
136
−5.245
−25.737
−43.854
1.00
28.44
L112
C


ATOM
1493
O
GLY
B
136
−5.524
−26.683
−43.120
1.00
30.60
L112
O


ATOM
1494
N
ILE
B
137
−6.088
−25.289
−44.770
1.00
27.95
L112
N


ATOM
1495
CA
ILE
B
137
−7.357
−25.966
−44.963
1.00
31.48
L112
C


ATOM
1496
C
ILE
B
137
−7.358
−26.505
−46.389
1.00
36.97
L112
C


ATOM
1497
O
ILE
B
137
−7.192
−25.752
−47.350
1.00
43.45
L112
O


ATOM
1498
CB
ILE
B
137
−8.547
−25.019
−44.736
1.00
31.35
L112
C


ATOM
1499
CG1
ILE
B
137
−8.702
−24.756
−43.233
1.00
30.66
L112
C


ATOM
1500
CG2
ILE
B
137
−9.826
−25.634
−45.302
1.00
23.26
L112
C


ATOM
1501
CD1
ILE
B
137
−9.853
−23.843
−42.859
1.00
19.47
L112
C


ATOM
1502
N
GLU
B
138
−7.516
−27.820
−46.508
1.00
34.70
L112
N


ATOM
1503
CA
GLU
B
138
−7.523
−28.504
−47.793
1.00
24.78
L112
C


ATOM
1504
C
GLU
B
138
−8.909
−28.509
−48.402
1.00
30.83
L112
C


ATOM
1505
O
GLU
B
138
−9.911
−28.509
−47.685
1.00
25.06
L112
O


ATOM
1506
CB
GLU
B
138
−7.065
−29.949
−47.617
1.00
33.57
L112
C


ATOM
1507
CG
GLU
B
138
−5.717
−30.270
−48.240
1.00
53.60
L112
C


ATOM
1508
CD
GLU
B
138
−5.435
−31.769
−48.293
1.00
61.48
L112
C


ATOM
1509
OE1
GLU
B
138
−6.286
−32.555
−47.810
1.00
52.54
L112
O


ATOM
1510
OE2
GLU
B
138
−4.359
−32.152
−48.818
1.00
61.92
L112
O


ATOM
1511
N
VAL
B
139
−8.962
−28.518
−49.733
1.00
36.08
L112
N


ATOM
1512
CA
VAL
B
139
−10.234
−28.552
−50.450
1.00
32.76
L112
C


ATOM
1513
C
VAL
B
139
−10.392
−29.933
−51.077
1.00
35.50
L112
C


ATOM
1514
O
VAL
B
139
−9.434
−30.484
−51.624
1.00
35.56
L112
O


ATOM
1515
CB
VAL
B
139
−10.293
−27.477
−51.557
1.00
24.66
L112
C


ATOM
1516
CG1
VAL
B
139
−11.653
−27.507
−52.234
1.00
22.09
L112
C


ATOM
1517
CG2
VAL
B
139
−10.044
−26.102
−50.959
1.00
19.96
L112
C


ATOM
1518
N
VAL
B
140
−11.593
−30.499
−50.978
1.00
39.97
L112
N


ATOM
1519
CA
VAL
B
140
−11.862
−31.825
−51.534
1.00
47.65
L112
C


ATOM
1520
C
VAL
B
140
−13.287
−31.934
−52.091
1.00
51.84
L112
C


ATOM
1521
O
VAL
B
140
−13.610
−32.955
−52.740
1.00
48.50
L112
O


ATOM
1522
CB
VAL
B
140
−11.651
−32.933
−50.467
1.00
46.88
L112
C


ATOM
1523
CG1
VAL
B
140
−11.479
−34.280
−51.152
1.00
53.45
L112
C


ATOM
1524
CG2
VAL
B
140
−10.421
−32.628
−49.615
1.00
37.90
L112
C


ATOM
1525
OXT
VAL
B
140
−14.071
−30.988
−51.877
1.00
56.26
L112
O


TER
1526

VAL
B
140


ATOM
1527
O5*
G
C
1051
24.335
−12.173
6.313
1.00
73.26
RNA1
O


ATOM
1528
C5*
G
C
1051
22.929
−12.367
6.147
1.00
60.23
RNA1
C


ATOM
1529
C4*
G
C
1051
22.454
−13.612
6.854
1.00
60.92
RNA1
C


ATOM
1530
O4*
G
C
1051
22.709
−13.474
8.275
1.00
63.63
RNA1
O


ATOM
1531
C3*
G
C
1051
20.961
−13.878
6.747
1.00
62.37
RNA1
C


ATOM
1532
O3*
G
C
1051
20.640
−14.594
5.557
1.00
56.24
RNA1
O


ATOM
1533
C2*
G
C
1051
20.665
−14.668
8.018
1.00
60.79
RNA1
C


ATOM
1534
O2*
G
C
1051
20.939
−16.050
7.900
1.00
63.11
RNA1
O


ATOM
1535
C1*
G
C
1051
21.637
−14.032
9.016
1.00
57.61
RNA1
C


ATOM
1536
N9
G
C
1051
21.014
−12.959
9.786
1.00
54.68
RNA1
N


ATOM
1537
C8
G
C
1051
21.204
−11.607
9.624
1.00
57.52
RNA1
C


ATOM
1538
N7
G
C
1051
20.474
−10.887
10.430
1.00
63.57
RNA1
N


ATOM
1539
C5
G
C
1051
19.766
−11.817
11.176
1.00
60.31
RNA1
C


ATOM
1540
C6
G
C
1051
18.808
−11.631
12.205
1.00
65.69
RNA1
C


ATOM
1541
O6
G
C
1051
18.372
−10.568
12.669
1.00
71.42
RNA1
O


ATOM
1542
N1
G
C
1051
18.347
−12.847
12.698
1.00
61.97
RNA1
N


ATOM
1543
C2
G
C
1051
18.751
−14.081
12.257
1.00
58.15
RNA1
C


ATOM
1544
N2
G
C
1051
18.193
−15.135
12.861
1.00
61.86
RNA1
N


ATOM
1545
N3
G
C
1051
19.636
−14.269
11.294
1.00
58.41
RNA1
N


ATOM
1546
C4
G
C
1051
20.099
−13.101
10.802
1.00
56.62
RNA1
C


ATOM
1547
P
C
C
1052
19.126
−14.611
5.015
1.00
50.79
RNA1
P


ATOM
1548
O1P
C
C
1052
18.620
−13.217
4.973
1.00
58.55
RNA1
O


ATOM
1549
O2P
C
C
1052
19.094
−15.438
3.784
1.00
67.52
RNA1
O


ATOM
1550
O5*
C
C
1052
18.323
−15.374
6.155
1.00
48.31
RNA1
O


ATOM
1551
C5*
C
C
1052
18.502
−16.781
6.372
1.00
35.63
RNA1
C


ATOM
1552
C4*
C
C
1052
17.510
−17.267
7.392
1.00
38.42
RNA1
C


ATOM
1553
O4*
C
C
1052
17.824
−16.686
8.682
1.00
47.16
RNA1
O


ATOM
1554
C3*
C
C
1052
16.087
−16.825
7.117
1.00
44.09
RNA1
C


ATOM
1555
O3*
C
C
1052
15.438
−17.673
6.200
1.00
49.32
RNA1
O


ATOM
1556
C2*
C
C
1052
15.449
−16.814
8.499
1.00
46.87
RNA1
C


ATOM
1557
O2*
C
C
1052
14.978
−18.071
8.935
1.00
46.62
RNA1
O


ATOM
1558
C1*
C
C
1052
16.623
−16.360
9.368
1.00
48.30
RNA1
C


ATOM
1559
N1
C
C
1052
16.588
−14.902
9.601
1.00
47.59
RNA1
N


ATOM
1560
C2
C
C
1052
15.778
−14.405
10.629
1.00
47.88
RNA1
C


ATOM
1561
O2
C
C
1052
15.145
−15.205
11.338
1.00
45.47
RNA1
O


ATOM
1562
N3
C
C
1052
15.706
−13.069
10.824
1.00
51.51
RNA1
N


ATOM
1563
C4
C
C
1052
16.406
−12.242
10.045
1.00
47.87
RNA1
C


ATOM
1564
N4
C
C
1052
16.289
−10.929
10.263
1.00
45.35
RNA1
N


ATOM
1565
C5
C
C
1052
17.252
−12.720
9.006
1.00
42.28
RNA1
C


ATOM
1566
C6
C
C
1052
17.314
−14.043
8.821
1.00
43.16
RNA1
C


ATOM
1567
P
U
C
1053
14.314
−17.067
5.236
1.00
53.77
RNA1
P


ATOM
1568
O1P
U
C
1053
14.776
−15.724
4.784
1.00
61.48
RNA1
O


ATOM
1569
O2P
U
C
1053
13.984
−18.106
4.231
1.00
67.30
RNA1
O


ATOM
1570
O5*
U
C
1053
13.059
−16.888
6.196
1.00
51.10
RNA1
O


ATOM
1571
C5*
U
C
1053
12.448
−18.032
6.809
1.00
47.98
RNA1
C


ATOM
1572
C4*
U
C
1053
11.467
−17.603
7.868
1.00
47.08
RNA1
C


ATOM
1573
O4*
U
C
1053
12.170
−16.895
8.917
1.00
48.31
RNA1
O


ATOM
1574
C3*
U
C
1053
10.382
−16.641
7.423
1.00
49.60
RNA1
C


ATOM
1575
O3*
U
C
1053
9.295
−17.321
6.812
1.00
61.44
RNA1
O


ATOM
1576
C2*
U
C
1053
9.993
−15.961
8.730
1.00
50.47
RNA1
C


ATOM
1577
O2*
U
C
1053
9.119
−16.731
9.531
1.00
43.66
RNA1
O


ATOM
1578
C1*
U
C
1053
11.339
−15.875
9.443
1.00
44.87
RNA1
C


ATOM
1579
N1
U
C
1053
12.003
−14.575
9.247
1.00
55.73
RNA1
N


ATOM
1580
C2
U
C
1053
11.564
−13.505
10.018
1.00
53.37
RNA1
C


ATOM
1581
O2
U
C
1053
10.644
−13.591
10.824
1.00
47.71
RNA1
O


ATOM
1582
N3
U
C
1053
12.240
−12.328
9.807
1.00
43.32
RNA1
N


ATOM
1583
C4
U
C
1053
13.281
−12.110
8.928
1.00
42.60
RNA1
C


ATOM
1584
O4
U
C
1053
13.827
−11.008
8.906
1.00
44.05
RNA1
O


ATOM
1585
C5
U
C
1053
13.666
−13.253
8.157
1.00
39.63
RNA1
C


ATOM
1586
C6
U
C
1053
13.032
−14.415
8.336
1.00
51.41
RNA1
C


ATOM
1587
P
G
C
1054
8.426
−16.576
5.682
1.00
62.77
RNA1
P


ATOM
1588
O1P
G
C
1054
9.391
−15.966
4.732
1.00
48.23
RNA1
O


ATOM
1589
O2P
G
C
1054
7.391
−17.524
5.177
1.00
63.46
RNA1
O


ATOM
1590
O5*
G
C
1054
7.673
−15.417
6.482
1.00
57.93
RNA1
O


ATOM
1591
C5*
G
C
1054
6.589
−15.737
7.376
1.00
58.01
RNA1
C


ATOM
1592
C4*
G
C
1054
6.160
−14.521
8.162
1.00
54.61
RNA1
C


ATOM
1593
O4*
G
C
1054
7.279
−14.019
8.937
1.00
57.89
RNA1
O


ATOM
1594
C3*
G
C
1054
5.693
−13.296
7.392
1.00
56.27
RNA1
C


ATOM
1595
O3*
G
C
1054
4.352
−13.378
6.946
1.00
61.66
RNA1
O


ATOM
1596
C2*
G
C
1054
5.851
−12.189
8.425
1.00
52.95
RNA1
C


ATOM
1597
O2*
G
C
1054
4.779
−12.130
9.346
1.00
49.43
RNA1
O


ATOM
1598
C1*
G
C
1054
7.119
−12.626
9.148
1.00
47.41
RNA1
C


ATOM
1599
N9
G
C
1054
8.274
−11.911
8.616
1.00
41.21
RNA1
N


ATOM
1600
C8
G
C
1054
9.205
−12.347
7.703
1.00
35.70
RNA1
C


ATOM
1601
N7
G
C
1054
10.100
−11.440
7.414
1.00
39.32
RNA1
N


ATOM
1602
C5
G
C
1054
9.741
−10.342
8.190
1.00
34.83
RNA1
C


ATOM
1603
C6
G
C
1054
10.333
−9.051
8.304
1.00
30.48
RNA1
C


ATOM
1604
O6
G
C
1054
11.333
−8.604
7.728
1.00
27.46
RNA1
O


ATOM
1605
N1
G
C
1054
9.635
−8.245
9.199
1.00
30.56
RNA1
N


ATOM
1606
C2
G
C
1054
8.511
−8.623
9.898
1.00
43.91
RNA1
C


ATOM
1607
N2
G
C
1054
7.967
−7.703
10.717
1.00
37.62
RNA1
N


ATOM
1608
N3
G
C
1054
7.957
−9.818
9.803
1.00
43.41
RNA1
N


ATOM
1609
C4
G
C
1054
8.619
−10.620
8.938
1.00
41.38
RNA1
C


ATOM
1610
P
G
C
1055
3.878
−12.469
5.704
1.00
66.88
RNA1
P


ATOM
1611
O1P
G
C
1055
4.889
−12.575
4.612
1.00
48.03
RNA1
O


ATOM
1612
O2P
G
C
1055
2.452
−12.820
5.440
1.00
64.70
RNA1
O


ATOM
1613
O5*
G
C
1055
3.943
−10.971
6.248
1.00
63.61
RNA1
O


ATOM
1614
C5*
G
C
1055
3.012
−10.512
7.237
1.00
53.95
RNA1
C


ATOM
1615
C4*
G
C
1055
3.371
−9.125
7.706
1.00
46.33
RNA1
C


ATOM
1616
O4*
G
C
1055
4.737
−9.107
8.201
1.00
45.69
RNA1
O


ATOM
1617
C3*
G
C
1055
3.363
−8.001
6.687
1.00
40.52
RNA1
C


ATOM
1618
O3*
G
C
1055
2.066
−7.500
6.421
1.00
47.06
RNA1
O


ATOM
1619
C2*
G
C
1055
4.212
−6.943
7.377
1.00
42.04
RNA1
C


ATOM
1620
O2*
G
C
1055
3.475
−6.224
8.348
1.00
43.70
RNA1
O


ATOM
1621
C1*
G
C
1055
5.264
−7.798
8.076
1.00
31.41
RNA1
C


ATOM
1622
N9
G
C
1055
6.501
−7.839
7.307
1.00
24.39
RNA1
N


ATOM
1623
C8
G
C
1055
7.026
−8.888
6.592
1.00
29.37
RNA1
C


ATOM
1624
N7
G
C
1055
8.158
−8.591
6.005
1.00
32.88
RNA1
N


ATOM
1625
C5
G
C
1055
8.388
−7.266
6.352
1.00
23.47
RNA1
C


ATOM
1626
C6
G
C
1055
9.458
−6.393
6.013
1.00
28.67
RNA1
C


ATOM
1627
O6
G
C
1055
10.450
−6.622
5.314
1.00
27.35
RNA1
O


ATOM
1628
N1
G
C
1055
9.292
−5.136
6.584
1.00
24.95
RNA1
N


ATOM
1629
C2
G
C
1055
8.235
−4.763
7.377
1.00
26.92
RNA1
C


ATOM
1630
N2
G
C
1055
8.255
−3.513
7.838
1.00
28.71
RNA1
N


ATOM
1631
N3
G
C
1055
7.234
−5.561
7.696
1.00
22.90
RNA1
N


ATOM
1632
C4
G
C
1055
7.375
−6.789
7.155
1.00
29.13
RNA1
C


ATOM
1633
P
G
C
1056
1.758
−6.834
4.989
1.00
49.25
RNA1
P


ATOM
1634
O1P
G
C
1056
1.991
−7.883
3.963
1.00
42.81
RNA1
O


ATOM
1635
O2P
G
C
1056
0.428
−6.158
5.065
1.00
37.09
RNA1
O


ATOM
1636
O5*
G
C
1056
2.899
−5.734
4.819
1.00
32.92
RNA1
O


ATOM
1637
C5*
G
C
1056
2.796
−4.457
5.476
1.00
35.07
RNA1
C


ATOM
1638
C4*
G
C
1056
3.939
−3.563
5.065
1.00
31.58
RNA1
C


ATOM
1639
O4*
G
C
1056
5.187
−4.183
5.457
1.00
35.44
RNA1
O


ATOM
1640
C3*
G
C
1056
4.089
−3.329
3.575
1.00
34.14
RNA1
C


ATOM
1641
O3*
G
C
1056
3.270
−2.275
3.113
1.00
39.89
RNA1
O


ATOM
1642
C2*
G
C
1056
5.567
−3.005
3.429
1.00
33.87
RNA1
C


ATOM
1643
O2*
G
C
1056
5.865
−1.651
3.704
1.00
36.26
RNA1
O


ATOM
1644
C1*
G
C
1056
6.184
−3.915
4.489
1.00
31.52
RNA1
C


ATOM
1645
N9
G
C
1056
6.611
−5.191
3.922
1.00
35.38
RNA1
N


ATOM
1646
C8
G
C
1056
5.874
−6.350
3.845
1.00
33.57
RNA1
C


ATOM
1647
N7
G
C
1056
6.516
−7.326
3.265
1.00
40.73
RNA1
N


ATOM
1648
C5
G
C
1056
7.752
−6.782
2.941
1.00
37.74
RNA1
C


ATOM
1649
C6
G
C
1056
8.875
−7.367
2.290
1.00
41.95
RNA1
C


ATOM
1650
O6
G
C
1056
8.999
−8.519
1.852
1.00
52.67
RNA1
O


ATOM
1651
N1
G
C
1056
9.925
−6.460
2.169
1.00
34.10
RNA1
N


ATOM
1652
C2
G
C
1056
9.899
−5.160
2.611
1.00
28.22
RNA1
C


ATOM
1653
N2
G
C
1056
11.011
−4.444
2.407
1.00
29.23
RNA1
N


ATOM
1654
N3
G
C
1056
8.860
−4.603
3.211
1.00
30.05
RNA1
N


ATOM
1655
C4
G
C
1056
7.829
−5.466
3.344
1.00
33.38
RNA1
C


ATOM
1656
P
A
C
1057
2.647
−2.350
1.636
1.00
36.51
RNA1
P


ATOM
1657
O1P
A
C
1057
2.944
−1.053
0.973
1.00
50.45
RNA1
O


ATOM
1658
O2P
A
C
1057
3.064
−3.614
0.988
1.00
31.54
RNA1
O


ATOM
1659
O5*
A
C
1057
1.085
−2.420
1.900
1.00
24.51
RNA1
O


ATOM
1660
C5*
A
C
1057
0.516
−3.490
2.659
1.00
23.76
RNA1
C


ATOM
1661
C4*
A
C
1057
−0.421
−2.936
3.703
1.00
25.17
RNA1
C


ATOM
1662
O4*
A
C
1057
0.346
−2.384
4.802
1.00
26.26
RNA1
O


ATOM
1663
C3*
A
C
1057
−1.282
−1.776
3.240
1.00
26.38
RNA1
C


ATOM
1664
O3*
A
C
1057
−2.429
−2.174
2.517
1.00
39.01
RNA1
O


ATOM
1665
C2*
A
C
1057
−1.612
−1.068
4.542
1.00
23.04
RNA1
C


ATOM
1666
O2*
A
C
1057
−2.658
−1.705
5.241
1.00
26.68
RNA1
O


ATOM
1667
C1*
A
C
1057
−0.304
−1.230
5.310
1.00
20.72
RNA1
C


ATOM
1668
N9
A
C
1057
0.587
−0.081
5.125
1.00
25.31
RNA1
N


ATOM
1669
C8
A
C
1057
1.840
−0.055
4.550
1.00
24.58
RNA1
C


ATOM
1670
N7
A
C
1057
2.393
1.135
4.537
1.00
16.48
RNA1
N


ATOM
1671
C5
A
C
1057
1.445
1.949
5.143
1.00
18.96
RNA1
C


ATOM
1672
C6
A
C
1057
1.428
3.322
5.438
1.00
21.91
RNA1
C


ATOM
1673
N6
A
C
1057
2.445
4.150
5.174
1.00
18.97
RNA1
N


ATOM
1674
N1
A
C
1057
0.322
3.824
6.029
1.00
28.79
RNA1
N


ATOM
1675
C2
A
C
1057
−0.688
2.991
6.317
1.00
26.99
RNA1
C


ATOM
1676
N3
A
C
1057
−0.786
1.681
6.104
1.00
27.54
RNA1
N


ATOM
1677
C4
A
C
1057
0.326
1.215
5.505
1.00
19.03
RNA1
C


ATOM
1678
P
U
C
1058
−2.943
−1.256
1.300
1.00
33.80
RNA1
P


ATOM
1679
O1P
U
C
1058
−1.733
−0.731
0.608
1.00
32.34
RNA1
O


ATOM
1680
O2P
U
C
1058
−3.967
−1.996
0.524
1.00
30.00
RNA1
O


ATOM
1681
O5*
U
C
1058
−3.665
−0.043
2.030
1.00
29.35
RNA1
O


ATOM
1682
C5*
U
C
1058
−4.955
−0.218
2.627
1.00
31.01
RNA1
C


ATOM
1683
C4*
U
C
1058
−5.530
1.120
3.008
1.00
33.02
RNA1
C


ATOM
1684
O4*
U
C
1058
−4.686
1.734
4.018
1.00
32.59
RNA1
O


ATOM
1685
C3*
U
C
1058
−5.554
2.156
1.902
1.00
34.36
RNA1
C


ATOM
1686
O3*
U
C
1058
−6.626
2.018
0.993
1.00
36.65
RNA1
O


ATOM
1687
C2*
U
C
1058
−5.596
3.459
2.680
1.00
27.20
RNA1
C


ATOM
1688
O2*
U
C
1058
−6.886
3.727
3.188
1.00
26.74
RNA1
O


ATOM
1689
C1*
U
C
1058
−4.652
3.139
3.831
1.00
24.15
RNA1
C


ATOM
1690
N1
U
C
1058
−3.267
3.546
3.532
1.00
18.02
RNA1
N


ATOM
1691
C2
U
C
1058
−2.971
4.898
3.590
1.00
19.91
RNA1
C


ATOM
1692
O2
U
C
1058
−3.802
5.750
3.879
1.00
30.16
RNA1
O


ATOM
1693
N3
U
C
1058
−1.671
5.219
3.300
1.00
13.57
RNA1
N


ATOM
1694
C4
U
C
1058
−0.655
4.353
2.965
1.00
20.26
RNA1
C


ATOM
1695
O4
U
C
1058
0.470
4.801
2.729
1.00
30.19
RNA1
O


ATOM
1696
C5
U
C
1058
−1.035
2.981
2.926
1.00
12.30
RNA1
C


ATOM
1697
C6
U
C
1058
−2.296
2.631
3.205
1.00
13.08
RNA1
C


ATOM
1698
P
G
C
1059
−6.470
2.631
−0.484
1.00
30.00
RNA1
P


ATOM
1699
O1P
G
C
1059
−5.071
2.397
−0.938
1.00
16.05
RNA1
O


ATOM
1700
O2P
G
C
1059
−7.607
2.157
−1.311
1.00
33.73
RNA1
O


ATOM
1701
O5*
G
C
1059
−6.635
4.196
−0.256
1.00
30.83
RNA1
O


ATOM
1702
C5*
G
C
1059
−7.854
4.731
0.279
1.00
22.74
RNA1
C


ATOM
1703
C4*
G
C
1059
−7.798
6.231
0.278
1.00
24.79
RNA1
C


ATOM
1704
O4*
G
C
1059
−6.727
6.667
1.149
1.00
28.49
RNA1
O


ATOM
1705
C3*
G
C
1059
−7.475
6.869
−1.060
1.00
26.72
RNA1
C


ATOM
1706
O3*
G
C
1059
−8.642
7.007
−1.857
1.00
34.13
RNA1
O


ATOM
1707
C2*
G
C
1059
−6.884
8.214
−0.657
1.00
28.17
RNA1
C


ATOM
1708
O2*
G
C
1059
−7.880
9.178
−0.371
1.00
38.10
RNA1
O


ATOM
1709
C1*
G
C
1059
−6.157
7.860
0.640
1.00
23.13
RNA1
C


ATOM
1710
N9
G
C
1059
−4.721
7.665
0.480
1.00
15.04
RNA1
N


ATOM
1711
C8
G
C
1059
−4.064
6.490
0.206
1.00
17.72
RNA1
C


ATOM
1712
N7
G
C
1059
−2.766
6.634
0.130
1.00
21.45
RNA1
N


ATOM
1713
C5
G
C
1059
−2.552
7.989
0.360
1.00
9.82
RNA1
C


ATOM
1714
C6
G
C
1059
−1.344
8.740
0.392
1.00
23.72
RNA1
C


ATOM
1715
O6
G
C
1059
−0.177
8.344
0.216
1.00
19.54
RNA1
O


ATOM
1716
N1
G
C
1059
−1.585
10.082
0.661
1.00
19.14
RNA1
N


ATOM
1717
C2
G
C
1059
−2.822
10.638
0.874
1.00
19.08
RNA1
C


ATOM
1718
N2
G
C
1059
−2.837
11.957
1.125
1.00
16.35
RNA1
N


ATOM
1719
N3
G
C
1059
−3.955
9.953
0.844
1.00
20.08
RNA1
N


ATOM
1720
C4
G
C
1059
−3.746
8.641
0.582
1.00
20.00
RNA1
C


ATOM
1721
P
U
C
1060
−8.509
7.045
−3.456
1.00
31.42
RNA1
P


ATOM
1722
O1P
U
C
1060
−9.692
6.330
−3.996
1.00
31.37
RNA1
O


ATOM
1723
O2P
U
C
1060
−8.243
8.446
−3.872
1.00
36.54
RNA1
O


ATOM
1724
O5*
U
C
1060
−7.195
6.198
−3.754
1.00
22.64
RNA1
O


ATOM
1725
C5*
U
C
1060
−7.016
5.523
−5.009
1.00
22.76
RNA1
C


ATOM
1726
C4*
U
C
1060
−5.589
5.064
−5.145
1.00
18.28
RNA1
C


ATOM
1727
O4*
U
C
1060
−4.739
6.232
−5.160
1.00
20.83
RNA1
O


ATOM
1728
C3*
U
C
1060
−5.079
4.166
−4.022
1.00
28.38
RNA1
C


ATOM
1729
O3*
U
C
1060
−4.142
3.234
−4.559
1.00
34.99
RNA1
O


ATOM
1730
C2*
U
C
1060
−4.336
5.141
−3.110
1.00
28.41
RNA1
C


ATOM
1731
O2*
U
C
1060
−3.277
4.523
−2.401
1.00
41.53
RNA1
O


ATOM
1732
C1*
U
C
1060
−3.794
6.157
−4.115
1.00
23.82
RNA1
C


ATOM
1733
N1
U
C
1060
−3.613
7.518
−3.587
1.00
15.63
RNA1
N


ATOM
1734
C2
U
C
1060
−2.336
7.922
−3.245
1.00
18.51
RNA1
C


ATOM
1735
O2
U
C
1060
−1.353
7.193
−3.325
1.00
21.06
RNA1
O


ATOM
1736
N3
U
C
1060
−2.245
9.216
−2.800
1.00
13.56
RNA1
N


ATOM
1737
C4
U
C
1060
−3.271
10.129
−2.661
1.00
21.90
RNA1
C


ATOM
1738
O4
U
C
1060
−3.015
11.281
−2.293
1.00
25.73
RNA1
O


ATOM
1739
C5
U
C
1060
−4.559
9.632
−3.018
1.00
7.65
RNA1
C


ATOM
1740
C6
U
C
1060
−4.686
8.377
−3.455
1.00
23.41
RNA1
C


ATOM
1741
P
U
C
1061
−4.622
2.136
−5.633
1.00
28.90
RNA1
P


ATOM
1742
O1P
U
C
1061
−3.994
0.840
−5.253
1.00
34.87
RNA1
O


ATOM
1743
O2P
U
C
1061
−6.093
2.222
−5.792
1.00
16.57
RNA1
O


ATOM
1744
O5*
U
C
1061
−3.946
2.631
−6.983
1.00
24.02
RNA1
O


ATOM
1745
C5*
U
C
1061
−2.514
2.667
−7.117
1.00
25.58
RNA1
C


ATOM
1746
C4*
U
C
1061
−2.122
3.503
−8.311
1.00
31.26
RNA1
C


ATOM
1747
O4*
U
C
1061
−2.694
2.914
−9.507
1.00
36.66
RNA1
O


ATOM
1748
C3*
U
C
1061
−2.584
4.961
−8.290
1.00
33.14
RNA1
C


ATOM
1749
O3*
U
C
1061
−1.601
5.740
−8.967
1.00
23.50
RNA1
O


ATOM
1750
C2*
U
C
1061
−3.831
4.934
−9.167
1.00
32.29
RNA1
C


ATOM
1751
O2*
U
C
1061
−4.100
6.183
−9.775
1.00
33.30
RNA1
O


ATOM
1752
C1*
U
C
1061
−3.414
3.896
−10.205
1.00
40.61
RNA1
C


ATOM
1753
N1
U
C
1061
−4.461
3.257
−11.015
1.00
50.51
RNA1
N


ATOM
1754
C2
U
C
1061
−4.299
3.335
−12.387
1.00
62.28
RNA1
C


ATOM
1755
O2
U
C
1061
−3.330
3.880
−12.914
1.00
62.30
RNA1
O


ATOM
1756
N3
U
C
1061
−5.303
2.754
−13.123
1.00
73.69
RNA1
N


ATOM
1757
C4
U
C
1061
−6.427
2.110
−12.641
1.00
67.10
RNA1
C


ATOM
1758
O4
U
C
1061
−7.260
1.668
−13.440
1.00
68.66
RNA1
O


ATOM
1759
C5
U
C
1061
−6.515
2.056
−11.210
1.00
54.52
RNA1
C


ATOM
1760
C6
U
C
1061
−5.552
2.617
−10.463
1.00
45.73
RNA1
C


ATOM
1761
P
G
C
1062
−0.570
6.637
−8.138
1.00
27.54
RNA1
P


ATOM
1762
O1P
G
C
1062
−0.356
5.986
−6.813
1.00
24.54
RNA1
O


ATOM
1763
O2P
G
C
1062
0.600
6.908
−9.017
1.00
15.00
RNA1
O


ATOM
1764
O5*
G
C
1062
−1.358
8.001
−7.930
1.00
14.13
RNA1
O


ATOM
1765
C5*
G
C
1062
−2.396
8.125
−6.939
1.00
22.88
RNA1
C


ATOM
1766
C4*
G
C
1062
−2.448
9.547
−6.435
1.00
15.45
RNA1
C


ATOM
1767
O4*
G
C
1062
−1.246
9.824
−5.677
1.00
24.75
RNA1
O


ATOM
1768
C3*
G
C
1062
−2.438
10.568
−7.550
1.00
12.59
RNA1
C


ATOM
1769
O3*
G
C
1062
−3.742
10.823
−8.006
1.00
33.25
RNA1
O


ATOM
1770
C2*
G
C
1062
−1.783
11.777
−6.911
1.00
19.71
RNA1
C


ATOM
1771
O2*
G
C
1062
−2.709
12.520
−6.141
1.00
23.78
RNA1
O


ATOM
1772
C1*
G
C
1062
−0.751
11.111
−5.999
1.00
16.39
RNA1
C


ATOM
1773
N9
G
C
1062
0.564
10.927
−6.611
1.00
14.13
RNA1
N


ATOM
1774
C8
G
C
1062
1.229
9.734
−6.776
1.00
24.14
RNA1
C


ATOM
1775
N7
G
C
1062
2.388
9.866
−7.361
1.00
25.47
RNA1
N


ATOM
1776
C5
G
C
1062
2.495
11.229
−7.605
1.00
26.26
RNA1
C


ATOM
1777
C6
G
C
1062
3.527
11.966
−8.235
1.00
31.66
RNA1
C


ATOM
1778
O6
G
C
1062
4.572
11.542
−8.758
1.00
28.31
RNA1
O


ATOM
1779
N1
G
C
1062
3.246
13.328
−8.243
1.00
23.22
RNA1
N


ATOM
1780
C2
G
C
1062
2.108
13.904
−7.739
1.00
23.93
RNA1
C


ATOM
1781
N2
G
C
1062
2.025
15.238
−7.844
1.00
18.71
RNA1
N


ATOM
1782
N3
G
C
1062
1.125
13.226
−7.174
1.00
19.22
RNA1
N


ATOM
1783
C4
G
C
1062
1.384
11.902
−7.137
1.00
21.18
RNA1
C


ATOM
1784
P
G
C
1063
−3.983
11.091
−9.564
1.00
32.90
RNA1
P


ATOM
1785
O1P
G
C
1063
−3.162
10.105
−10.324
1.00
29.07
RNA1
O


ATOM
1786
O2P
G
C
1063
−5.446
11.159
−9.776
1.00
28.95
RNA1
O


ATOM
1787
O5*
G
C
1063
−3.361
12.534
−9.798
1.00
32.11
RNA1
O


ATOM
1788
C5*
G
C
1063
−4.042
13.712
−9.342
1.00
23.86
RNA1
C


ATOM
1789
C4*
G
C
1063
−3.302
14.944
−9.798
1.00
22.38
RNA1
C


ATOM
1790
O4*
G
C
1063
−1.983
14.950
−9.201
1.00
24.88
RNA1
O


ATOM
1791
C3*
G
C
1063
−3.019
15.022
−11.287
1.00
26.89
RNA1
C


ATOM
1792
O3*
G
C
1063
−4.110
15.506
−12.042
1.00
33.17
RNA1
O


ATOM
1793
C2*
G
C
1063
−1.806
15.936
−11.343
1.00
25.82
RNA1
C


ATOM
1794
O2*
G
C
1063
−2.149
17.294
−11.168
1.00
34.75
RNA1
O


ATOM
1795
C1*
G
C
1063
−1.035
15.472
−10.118
1.00
14.96
RNA1
C


ATOM
1796
N9
G
C
1063
−0.093
14.412
−10.461
1.00
16.28
RNA1
N


ATOM
1797
C8
G
C
1063
−0.201
13.070
−10.178
1.00
17.00
RNA1
C


ATOM
1798
N7
G
C
1063
0.820
12.373
−10.602
1.00
23.95
RNA1
N


ATOM
1799
C5
G
C
1063
1.644
13.309
−11.212
1.00
13.66
RNA1
C


ATOM
1800
C6
G
C
1063
2.898
13.151
−11.857
1.00
19.46
RNA1
C


ATOM
1801
O6
G
C
1063
3.555
12.117
−12.032
1.00
27.29
RNA1
O


ATOM
1802
N1
G
C
1063
3.385
14.363
−12.326
1.00
19.82
RNA1
N


ATOM
1803
C2
G
C
1063
2.749
15.571
−12.201
1.00
24.09
RNA1
C


ATOM
1804
N2
G
C
1063
3.385
16.631
−12.718
1.00
33.27
RNA1
N


ATOM
1805
N3
G
C
1063
1.579
15.731
−11.609
1.00
25.48
RNA1
N


ATOM
1806
C4
G
C
1063
1.091
14.569
−11.137
1.00
16.05
RNA1
C


ATOM
1807
P
C
C
1064
−4.385
14.882
−13.495
1.00
32.63
RNA1
P


ATOM
1808
O1P
C
C
1064
−4.311
13.399
−13.376
1.00
34.14
RNA1
O


ATOM
1809
O2P
C
C
1064
−5.610
15.520
−14.047
1.00
34.53
RNA1
O


ATOM
1810
O5*
C
C
1064
−3.124
15.351
−14.340
1.00
25.39
RNA1
O


ATOM
1811
C5*
C
C
1064
−2.841
16.743
−14.483
1.00
20.47
RNA1
C


ATOM
1812
C4*
C
C
1064
−1.510
16.945
−15.158
1.00
22.15
RNA1
C


ATOM
1813
O4*
C
C
1064
−0.455
16.348
−14.362
1.00
25.83
RNA1
O


ATOM
1814
C3*
C
C
1064
−1.320
16.321
−16.528
1.00
29.48
RNA1
C


ATOM
1815
O3*
C
C
1064
−1.921
17.088
−17.565
1.00
35.84
RNA1
O


ATOM
1816
C2*
C
C
1064
0.199
16.267
−16.648
1.00
29.04
RNA1
C


ATOM
1817
O2*
C
C
1064
0.774
17.500
−17.036
1.00
28.73
RNA1
O


ATOM
1818
C1*
C
C
1064
0.611
15.958
−15.212
1.00
21.28
RNA1
C


ATOM
1819
N1
C
C
1064
0.899
14.525
−15.020
1.00
19.09
RNA1
N


ATOM
1820
C2
C
C
1064
2.155
14.044
−15.409
1.00
27.83
RNA1
C


ATOM
1821
O2
C
C
1064
2.977
14.836
−15.897
1.00
32.73
RNA1
O


ATOM
1822
N3
C
C
1064
2.442
12.734
−15.247
1.00
23.67
RNA1
N


ATOM
1823
C4
C
C
1064
1.535
11.915
−14.716
1.00
22.40
RNA1
C


ATOM
1824
N4
C
C
1064
1.871
10.635
−14.564
1.00
29.03
RNA1
N


ATOM
1825
C5
C
C
1064
0.246
12.374
−14.314
1.00
9.70
RNA1
C


ATOM
1826
C6
C
C
1064
−0.027
13.674
−14.482
1.00
20.34
RNA1
C


ATOM
1827
P
U
C
1065
−2.537
16.339
−18.853
1.00
31.56
RNA1
P


ATOM
1828
O1P
U
C
1065
−3.488
15.293
−18.407
1.00
29.35
RNA1
O


ATOM
1829
O2P
U
C
1065
−3.011
17.398
−19.774
1.00
46.70
RNA1
O


ATOM
1830
O5*
U
C
1065
−1.266
15.617
−19.495
1.00
22.04
RNA1
O


ATOM
1831
C5*
U
C
1065
−0.138
16.392
−19.935
1.00
25.90
RNA1
C


ATOM
1832
C4*
U
C
1065
1.022
15.492
−20.286
1.00
32.86
RNA1
C


ATOM
1833
O4*
U
C
1065
1.493
14.818
−19.094
1.00
35.71
RNA1
O


ATOM
1834
C3*
U
C
1065
0.721
14.374
−21.270
1.00
35.55
RNA1
C


ATOM
1835
O3*
U
C
1065
0.799
14.834
−22.609
1.00
37.39
RNA1
O


ATOM
1836
C2*
U
C
1065
1.793
13.340
−20.939
1.00
36.11
RNA1
C


ATOM
1837
O2*
U
C
1065
3.047
13.612
−21.536
1.00
27.98
RNA1
O


ATOM
1838
C1*
U
C
1065
1.917
13.505
−19.423
1.00
33.40
RNA1
C


ATOM
1839
N1
U
C
1065
1.088
12.543
−18.676
1.00
17.15
RNA1
N


ATOM
1840
C2
U
C
1065
1.653
11.323
−18.364
1.00
21.75
RNA1
C


ATOM
1841
O2
U
C
1065
2.789
11.015
−18.700
1.00
24.53
RNA1
O


ATOM
1842
N3
U
C
1065
0.841
10.472
−17.652
1.00
12.86
RNA1
N


ATOM
1843
C4
U
C
1065
−0.454
10.708
−17.245
1.00
22.54
RNA1
C


ATOM
1844
O4
U
C
1065
−1.068
9.829
−16.631
1.00
33.30
RNA1
O


ATOM
1845
C5
U
C
1065
−0.972
11.988
−17.617
1.00
18.28
RNA1
C


ATOM
1846
C6
U
C
1065
−0.202
12.840
−18.300
1.00
12.72
RNA1
C


ATOM
1847
P
U
C
1066
−0.290
14.345
−23.688
1.00
38.85
RNA1
P


ATOM
1848
O1P
U
C
1066
−1.664
14.499
−23.126
1.00
18.29
RNA1
O


ATOM
1849
O2P
U
C
1066
0.064
15.034
−24.964
1.00
40.95
RNA1
O


ATOM
1850
O5*
U
C
1066
0.014
12.790
−23.851
1.00
36.40
RNA1
O


ATOM
1851
C5*
U
C
1066
1.288
12.346
−24.350
1.00
35.84
RNA1
C


ATOM
1852
C4*
U
C
1066
1.461
10.870
−24.107
1.00
38.35
RNA1
C


ATOM
1853
O4*
U
C
1066
1.463
10.613
−22.679
1.00
39.66
RNA1
O


ATOM
1854
C3*
U
C
1066
0.359
9.974
−24.652
1.00
44.84
RNA1
C


ATOM
1855
O3*
U
C
1066
0.570
9.660
−26.021
1.00
45.33
RNA1
O


ATOM
1856
C2*
U
C
1066
0.473
8.739
−23.769
1.00
44.55
RNA1
C


ATOM
1857
O2*
U
C
1066
1.511
7.884
−24.213
1.00
33.40
RNA1
O


ATOM
1858
C1*
U
C
1066
0.859
9.357
−22.421
1.00
39.47
RNA1
C


ATOM
1859
N1
U
C
1066
−0.301
9.556
−21.535
1.00
27.32
RNA1
N


ATOM
1860
C2
U
C
1066
−0.598
8.548
−20.630
1.00
27.94
RNA1
C


ATOM
1861
O2
U
C
1066
0.086
7.545
−20.506
1.00
31.42
RNA1
O


ATOM
1862
N3
U
C
1066
−1.722
8.759
−19.869
1.00
19.18
RNA1
N


ATOM
1863
C4
U
C
1066
−2.556
9.854
−19.905
1.00
25.49
RNA1
C


ATOM
1864
O4
U
C
1066
−3.565
9.870
−19.194
1.00
36.42
RNA1
O


ATOM
1865
C5
U
C
1066
−2.168
10.867
−20.840
1.00
19.93
RNA1
C


ATOM
1866
C6
U
C
1066
−1.082
10.689
−21.604
1.00
23.45
RNA1
C


ATOM
1867
P
A
C
1067
−0.690
9.514
−27.002
1.00
46.85
RNA1
P


ATOM
1868
O1P
A
C
1067
−1.666
10.598
−26.712
1.00
36.17
RNA1
O


ATOM
1869
O2P
A
C
1067
−0.149
9.350
−28.374
1.00
52.36
RNA1
O


ATOM
1870
O5*
A
C
1067
−1.379
8.151
−26.562
1.00
45.01
RNA1
O


ATOM
1871
C5*
A
C
1067
−2.763
7.888
−26.874
1.00
42.12
RNA1
C


ATOM
1872
C4*
A
C
1067
−3.108
6.464
−26.511
1.00
37.93
RNA1
C


ATOM
1873
O4*
A
C
1067
−2.272
5.567
−27.279
1.00
37.30
RNA1
O


ATOM
1874
C3*
A
C
1067
−2.805
6.123
−25.068
1.00
39.89
RNA1
C


ATOM
1875
O3*
A
C
1067
−3.905
6.462
−24.244
1.00
44.47
RNA1
O


ATOM
1876
C2*
A
C
1067
−2.505
4.632
−25.107
1.00
27.28
RNA1
C


ATOM
1877
O2*
A
C
1067
−3.664
3.829
−25.084
1.00
44.22
RNA1
O


ATOM
1878
C1*
A
C
1067
−1.845
4.494
−26.472
1.00
20.11
RNA1
C


ATOM
1879
N9
A
C
1067
−0.389
4.519
−26.443
1.00
16.55
RNA1
N


ATOM
1880
C8
A
C
1067
0.450
5.516
−26.872
1.00
13.35
RNA1
C


ATOM
1881
N7
A
C
1067
1.722
5.206
−26.785
1.00
21.36
RNA1
N


ATOM
1882
C5
A
C
1067
1.715
3.927
−26.244
1.00
6.97
RNA1
C


ATOM
1883
C6
A
C
1067
2.746
3.037
−25.917
1.00
18.48
RNA1
C


ATOM
1884
N6
A
C
1067
4.046
3.301
−26.105
1.00
25.96
RNA1
N


ATOM
1885
N1
A
C
1067
2.400
1.845
−25.391
1.00
13.59
RNA1
N


ATOM
1886
C2
A
C
1067
1.102
1.575
−25.214
1.00
28.55
RNA1
C


ATOM
1887
N3
A
C
1067
0.041
2.326
−25.488
1.00
23.97
RNA1
N


ATOM
1888
C4
A
C
1067
0.423
3.503
−26.009
1.00
16.34
RNA1
C


ATOM
1889
P
G
C
1068
−3.632
7.060
−22.783
1.00
39.02
RNA1
P


ATOM
1890
O1P
G
C
1068
−2.666
8.189
−22.930
1.00
31.97
RNA1
O


ATOM
1891
O2P
G
C
1068
−4.955
7.282
−22.122
1.00
23.85
RNA1
O


ATOM
1892
O5*
G
C
1068
−2.872
5.872
−22.052
1.00
29.64
RNA1
O


ATOM
1893
C5*
G
C
1068
−3.560
4.650
−21.753
1.00
26.14
RNA1
C


ATOM
1894
C4*
G
C
1068
−2.611
3.675
−21.128
1.00
30.68
RNA1
C


ATOM
1895
O4*
G
C
1068
−1.612
3.299
−22.105
1.00
33.92
RNA1
O


ATOM
1896
C3*
G
C
1068
−1.821
4.231
−19.956
1.00
37.79
RNA1
C


ATOM
1897
O3*
G
C
1068
−2.586
4.140
−18.752
1.00
40.54
RNA1
O


ATOM
1898
C2*
G
C
1068
−0.564
3.368
−19.963
1.00
31.49
RNA1
C


ATOM
1899
O2*
G
C
1068
−0.774
2.123
−19.322
1.00
38.55
RNA1
O


ATOM
1900
C1*
G
C
1068
−0.364
3.120
−21.463
1.00
28.77
RNA1
C


ATOM
1901
N9
G
C
1068
0.605
3.989
−22.123
1.00
18.63
RNA1
N


ATOM
1902
C8
G
C
1068
0.381
5.255
−22.612
1.00
21.10
RNA1
C


ATOM
1903
N7
G
C
1068
1.437
5.779
−23.177
1.00
18.47
RNA1
N


ATOM
1904
C5
G
C
1068
2.419
4.808
−23.047
1.00
12.57
RNA1
C


ATOM
1905
C6
G
C
1068
3.776
4.807
−23.476
1.00
23.53
RNA1
C


ATOM
1906
O6
G
C
1068
4.402
5.696
−24.076
1.00
26.90
RNA1
O


ATOM
1907
N1
G
C
1068
4.417
3.616
−23.140
1.00
26.41
RNA1
N


ATOM
1908
C2
G
C
1068
3.831
2.561
−22.479
1.00
23.88
RNA1
C


ATOM
1909
N2
G
C
1068
4.625
1.500
−22.232
1.00
22.10
RNA1
N


ATOM
1910
N3
G
C
1068
2.564
2.546
−22.085
1.00
17.30
RNA1
N


ATOM
1911
C4
G
C
1068
1.924
3.695
−22.396
1.00
15.61
RNA1
C


ATOM
1912
P
A
C
1069
−2.674
5.408
−17.758
1.00
35.85
RNA1
P


ATOM
1913
O1P
A
C
1069
−2.982
6.639
−18.536
1.00
34.22
RNA1
O


ATOM
1914
O2P
A
C
1069
−3.551
5.029
−16.625
1.00
34.69
RNA1
O


ATOM
1915
O5*
A
C
1069
−1.186
5.532
−17.220
1.00
22.83
RNA1
O


ATOM
1916
C5*
A
C
1069
−0.570
4.437
−16.545
1.00
16.26
RNA1
C


ATOM
1917
C4*
A
C
1069
0.859
4.768
−16.237
1.00
21.94
RNA1
C


ATOM
1918
O4*
A
C
1069
1.694
4.585
−17.417
1.00
35.64
RNA1
O


ATOM
1919
C3*
A
C
1069
1.093
6.209
−15.768
1.00
37.69
RNA1
C


ATOM
1920
O3*
A
C
1069
2.058
6.196
−14.714
1.00
40.68
RNA1
O


ATOM
1921
C2*
A
C
1069
1.737
6.855
−16.996
1.00
39.67
RNA1
C


ATOM
1922
O2*
A
C
1069
2.583
7.960
−16.731
1.00
43.60
RNA1
O


ATOM
1923
C1*
A
C
1069
2.567
5.680
−17.491
1.00
37.65
RNA1
C


ATOM
1924
N9
A
C
1069
3.223
5.772
−18.793
1.00
33.82
RNA1
N


ATOM
1925
C8
A
C
1069
2.972
6.600
−19.858
1.00
28.66
RNA1
C


ATOM
1926
N7
A
C
1069
3.878
6.527
−20.805
1.00
37.91
RNA1
N


ATOM
1927
C5
A
C
1069
4.758
5.554
−20.349
1.00
34.14
RNA1
C


ATOM
1928
C6
A
C
1069
5.949
5.022
−20.886
1.00
38.86
RNA1
C


ATOM
1929
N6
A
C
1069
6.490
5.420
−22.038
1.00
44.62
RNA1
N


ATOM
1930
N1
A
C
1069
6.577
4.054
−20.180
1.00
40.40
RNA1
N


ATOM
1931
C2
A
C
1069
6.041
3.661
−19.017
1.00
35.55
RNA1
C


ATOM
1932
N3
A
C
1069
4.939
4.093
−18.408
1.00
28.51
RNA1
N


ATOM
1933
C4
A
C
1069
4.342
5.053
−19.133
1.00
31.82
RNA1
C


ATOM
1934
P
A
C
1070
1.715
6.875
−13.302
1.00
33.11
RNA1
P


ATOM
1935
O1P
A
C
1070
3.039
7.134
−12.680
1.00
18.08
RNA1
O


ATOM
1936
O2P
A
C
1070
0.734
7.989
−13.469
1.00
18.52
RNA1
O


ATOM
1937
O5*
A
C
1070
0.968
5.723
−12.497
1.00
30.46
RNA1
O


ATOM
1938
C5*
A
C
1070
1.690
4.589
−11.998
1.00
21.05
RNA1
C


ATOM
1939
C4*
A
C
1070
0.844
3.851
−11.000
1.00
30.01
RNA1
C


ATOM
1940
O4*
A
C
1070
−0.391
3.424
−11.634
1.00
25.30
RNA1
O


ATOM
1941
C3*
A
C
1070
1.479
2.612
−10.390
1.00
36.56
RNA1
C


ATOM
1942
O3*
A
C
1070
1.078
2.564
−9.026
1.00
37.18
RNA1
O


ATOM
1943
C2*
A
C
1070
0.847
1.469
−11.185
1.00
37.06
RNA1
C


ATOM
1944
O2*
A
C
1070
0.739
0.256
−10.463
1.00
48.87
RNA1
O


ATOM
1945
C1*
A
C
1070
−0.539
2.028
−11.495
1.00
32.98
RNA1
C


ATOM
1946
N9
A
C
1070
−1.107
1.501
−12.735
1.00
42.72
RNA1
N


ATOM
1947
C8
A
C
1070
−0.659
1.702
−14.019
1.00
49.93
RNA1
C


ATOM
1948
N7
A
C
1070
−1.380
1.098
−14.929
1.00
50.90
RNA1
N


ATOM
1949
C5
A
C
1070
−2.366
0.452
−14.198
1.00
55.33
RNA1
C


ATOM
1950
C6
A
C
1070
−3.435
−0.367
−14.582
1.00
59.78
RNA1
C


ATOM
1951
N6
A
C
1070
−3.697
−0.683
−15.850
1.00
68.95
RNA1
N


ATOM
1952
N1
A
C
1070
−4.235
−0.857
−13.608
1.00
56.29
RNA1
N


ATOM
1953
C2
A
C
1070
−3.965
−0.536
−12.340
1.00
41.79
RNA1
C


ATOM
1954
N3
A
C
1070
−2.987
0.222
−11.854
1.00
44.24
RNA1
N


ATOM
1955
C4
A
C
1070
−2.212
0.692
−12.847
1.00
46.56
RNA1
C


ATOM
1956
P
G
C
1071
2.022
1.866
−7.940
1.00
29.75
RNA1
P


ATOM
1957
O1P
G
C
1071
1.299
1.985
−6.653
1.00
39.09
RNA1
O


ATOM
1958
O2P
G
C
1071
2.436
0.526
−8.435
1.00
39.01
RNA1
O


ATOM
1959
O5*
G
C
1071
3.325
2.769
−7.901
1.00
19.92
RNA1
O


ATOM
1960
C5*
G
C
1071
3.295
4.113
−7.406
1.00
16.74
RNA1
C


ATOM
1961
C4*
G
C
1071
4.704
4.562
−7.133
1.00
23.89
RNA1
C


ATOM
1962
O4*
G
C
1071
5.222
3.769
−6.044
1.00
22.65
RNA1
O


ATOM
1963
C3*
G
C
1071
5.633
4.285
−8.302
1.00
25.19
RNA1
C


ATOM
1964
O3*
G
C
1071
5.646
5.390
−9.187
1.00
38.67
RNA1
O


ATOM
1965
C2*
G
C
1071
6.974
4.006
−7.639
1.00
21.49
RNA1
C


ATOM
1966
O2*
G
C
1071
7.729
5.164
−7.347
1.00
30.27
RNA1
O


ATOM
1967
C1*
G
C
1071
6.533
3.335
−6.340
1.00
18.58
RNA1
C


ATOM
1968
N9
G
C
1071
6.500
1.878
−6.393
1.00
22.64
RNA1
N


ATOM
1969
C8
G
C
1071
5.389
1.076
−6.272
1.00
20.39
RNA1
C


ATOM
1970
N7
G
C
1071
5.672
−0.196
−6.315
1.00
31.29
RNA1
N


ATOM
1971
C5
G
C
1071
7.048
−0.236
−6.482
1.00
14.55
RNA1
C


ATOM
1972
C6
G
C
1071
7.922
−1.342
−6.582
1.00
28.22
RNA1
C


ATOM
1973
O6
G
C
1071
7.647
−2.549
−6.512
1.00
31.85
RNA1
O


ATOM
1974
N1
G
C
1071
9.239
−0.934
−6.762
1.00
15.53
RNA1
N


ATOM
1975
C2
G
C
1071
9.660
0.371
−6.818
1.00
20.27
RNA1
C


ATOM
1976
N2
G
C
1071
10.977
0.567
−6.997
1.00
25.10
RNA1
N


ATOM
1977
N3
G
C
1071
8.853
1.411
−6.707
1.00
19.36
RNA1
N


ATOM
1978
C4
G
C
1071
7.570
1.035
−6.546
1.00
11.18
RNA1
C


ATOM
1979
P
C
C
1072
5.597
5.137
−10.767
1.00
27.21
RNA1
P


ATOM
1980
O1P
C
C
1072
4.563
4.110
−11.043
1.00
30.50
RNA1
O


ATOM
1981
O2P
C
C
1072
5.512
6.459
−11.426
1.00
25.77
RNA1
O


ATOM
1982
O5*
C
C
1072
7.022
4.506
−11.073
1.00
15.96
RNA1
O


ATOM
1983
C5*
C
C
1072
8.198
5.315
−11.019
1.00
23.11
RNA1
C


ATOM
1984
C4*
C
C
1072
9.419
4.471
−11.280
1.00
32.01
RNA1
C


ATOM
1985
O4*
C
C
1072
9.601
3.533
−10.192
1.00
36.03
RNA1
O


ATOM
1986
C3*
C
C
1072
9.365
3.597
−12.522
1.00
30.99
RNA1
C


ATOM
1987
O3*
C
C
1072
9.711
4.326
−13.688
1.00
33.23
RNA1
O


ATOM
1988
C2*
C
C
1072
10.362
2.496
−12.188
1.00
29.75
RNA1
C


ATOM
1989
O2*
C
C
1072
11.703
2.904
−12.371
1.00
34.64
RNA1
O


ATOM
1990
C1*
C
C
1072
10.121
2.314
−10.692
1.00
29.06
RNA1
C


ATOM
1991
N1
C
C
1072
9.151
1.242
−10.401
1.00
21.88
RNA1
N


ATOM
1992
C2
C
C
1072
9.623
−0.062
−10.229
1.00
22.42
RNA1
C


ATOM
1993
O2
C
C
1072
10.852
−0.281
−10.328
1.00
27.87
RNA1
O


ATOM
1994
N3
C
C
1072
8.735
−1.053
−9.964
1.00
9.91
RNA1
N


ATOM
1995
C4
C
C
1072
7.430
−0.780
−9.883
1.00
19.29
RNA1
C


ATOM
1996
N4
C
C
1072
6.591
−1.789
−9.644
1.00
23.91
RNA1
N


ATOM
1997
C5
C
C
1072
6.925
0.538
−10.048
1.00
13.70
RNA1
C


ATOM
1998
C6
C
C
1072
7.812
1.510
−10.304
1.00
24.95
RNA1
C


ATOM
1999
P
A
C
1073
8.702
4.336
−14.936
1.00
33.99
RNA1
P


ATOM
2000
O1P
A
C
1073
8.504
2.919
−15.333
1.00
35.83
RNA1
O


ATOM
2001
O2P
A
C
1073
7.512
5.181
−14.614
1.00
22.96
RNA1
O


ATOM
2002
O5*
A
C
1073
9.551
5.050
−16.074
1.00
31.36
RNA1
O


ATOM
2003
C5*
A
C
1073
10.772
4.462
−16.571
1.00
35.37
RNA1
C


ATOM
2004
C4*
A
C
1073
11.245
5.227
−17.781
1.00
39.45
RNA1
C


ATOM
2005
O4*
A
C
1073
10.229
5.143
−18.815
1.00
39.78
RNA1
O


ATOM
2006
C3*
A
C
1073
11.400
6.713
−17.522
1.00
40.87
RNA1
C


ATOM
2007
O3*
A
C
1073
12.673
7.017
−16.987
1.00
44.46
RNA1
O


ATOM
2008
C2*
A
C
1073
11.147
7.327
−18.890
1.00
38.57
RNA1
C


ATOM
2009
O2*
A
C
1073
12.279
7.252
−19.738
1.00
41.89
RNA1
O


ATOM
2010
C1*
A
C
1073
10.054
6.409
−19.426
1.00
27.18
RNA1
C


ATOM
2011
N9
A
C
1073
8.713
6.872
−19.081
1.00
23.78
RNA1
N


ATOM
2012
C8
A
C
1073
7.835
6.282
−18.209
1.00
31.10
RNA1
C


ATOM
2013
N7
A
C
1073
6.685
6.903
−18.112
1.00
30.54
RNA1
N


ATOM
2014
C5
A
C
1073
6.819
7.979
−18.974
1.00
22.89
RNA1
C


ATOM
2015
C6
A
C
1073
5.948
9.015
−19.319
1.00
24.05
RNA1
C


ATOM
2016
N6
A
C
1073
4.711
9.130
−18.836
1.00
24.67
RNA1
N


ATOM
2017
N1
A
C
1073
6.391
9.940
−20.193
1.00
27.06
RNA1
N


ATOM
2018
C2
A
C
1073
7.627
9.815
−20.684
1.00
28.92
RNA1
C


ATOM
2019
N3
A
C
1073
8.539
8.879
−20.442
1.00
33.22
RNA1
N


ATOM
2020
C4
A
C
1073
8.066
7.979
−19.568
1.00
24.70
RNA1
C


ATOM
2021
P
G
C
1074
12.790
8.131
−15.846
1.00
37.49
RNA1
P


ATOM
2022
O1P
G
C
1074
11.994
7.638
−14.698
1.00
42.76
RNA1
O


ATOM
2023
O2P
G
C
1074
14.226
8.458
−15.661
1.00
37.27
RNA1
O


ATOM
2024
O5*
G
C
1074
12.052
9.389
−16.488
1.00
32.12
RNA1
O


ATOM
2025
C5*
G
C
1074
12.636
10.074
−17.611
1.00
30.38
RNA1
C


ATOM
2026
C4*
G
C
1074
11.776
11.239
−18.042
1.00
29.26
RNA1
C


ATOM
2027
O4*
G
C
1074
10.505
10.762
−18.552
1.00
28.39
RNA1
O


ATOM
2028
C3*
G
C
1074
11.393
12.245
−16.972
1.00
30.49
RNA1
C


ATOM
2029
O3*
G
C
1074
12.431
13.170
−16.697
1.00
40.29
RNA1
O


ATOM
2030
C2*
G
C
1074
10.152
12.899
−17.566
1.00
32.10
RNA1
C


ATOM
2031
O2*
G
C
1074
10.452
13.891
−18.528
1.00
36.08
RNA1
O


ATOM
2032
C1*
G
C
1074
9.491
11.714
−18.268
1.00
26.45
RNA1
C


ATOM
2033
N9
G
C
1074
8.479
11.075
−17.435
1.00
22.10
RNA1
N


ATOM
2034
C8
G
C
1074
8.576
9.862
−16.794
1.00
21.18
RNA1
C


ATOM
2035
N7
G
C
1074
7.490
9.539
−16.145
1.00
28.77
RNA1
N


ATOM
2036
C5
G
C
1074
6.628
10.604
−16.362
1.00
15.54
RNA1
C


ATOM
2037
C6
G
C
1074
5.300
10.815
−15.917
1.00
22.89
RNA1
C


ATOM
2038
O6
G
C
1074
4.589
10.071
−15.240
1.00
28.81
RNA1
O


ATOM
2039
N1
G
C
1074
4.802
12.038
−16.351
1.00
26.73
RNA1
N


ATOM
2040
C2
G
C
1074
5.487
12.937
−17.126
1.00
24.75
RNA1
C


ATOM
2041
N2
G
C
1074
4.828
14.058
−17.440
1.00
20.91
RNA1
N


ATOM
2042
N3
G
C
1074
6.724
12.748
−17.560
1.00
19.40
RNA1
N


ATOM
2043
C4
G
C
1074
7.228
11.568
−17.144
1.00
19.49
RNA1
C


ATOM
2044
P
C
C
1075
12.535
13.826
−15.232
1.00
35.74
RNA1
P


ATOM
2045
O1P
C
C
1075
12.251
12.757
−14.239
1.00
37.48
RNA1
O


ATOM
2046
O2P
C
C
1075
13.814
14.574
−15.147
1.00
35.45
RNA1
O


ATOM
2047
O5*
C
C
1075
11.326
14.864
−15.223
1.00
29.10
RNA1
O


ATOM
2048
C5*
C
C
1075
11.373
16.035
−16.052
1.00
20.72
RNA1
C


ATOM
2049
C4*
C
C
1075
10.144
16.884
−15.848
1.00
27.73
RNA1
C


ATOM
2050
O4*
C
C
1075
8.980
16.162
−16.316
1.00
25.49
RNA1
O


ATOM
2051
C3*
C
C
1075
9.804
17.254
−14.413
1.00
29.84
RNA1
C


ATOM
2052
O3*
C
C
1075
10.548
18.355
−13.924
1.00
32.76
RNA1
O


ATOM
2053
C2*
C
C
1075
8.311
17.537
−14.490
1.00
32.29
RNA1
C


ATOM
2054
O2*
C
C
1075
8.018
18.838
−14.963
1.00
33.04
RNA1
O


ATOM
2055
C1*
C
C
1075
7.860
16.488
−15.508
1.00
30.74
RNA1
C


ATOM
2056
N1
C
C
1075
7.407
15.259
−14.836
1.00
23.00
RNA1
N


ATOM
2057
C2
C
C
1075
6.083
15.178
−14.407
1.00
25.39
RNA1
C


ATOM
2058
O2
C
C
1075
5.320
16.133
−14.627
1.00
27.71
RNA1
O


ATOM
2059
N3
C
C
1075
5.666
14.063
−13.764
1.00
20.56
RNA1
N


ATOM
2060
C4
C
C
1075
6.518
13.054
−13.553
1.00
24.69
RNA1
C


ATOM
2061
N4
C
C
1075
6.067
11.975
−12.911
1.00
22.56
RNA1
N


ATOM
2062
C5
C
C
1075
7.870
13.108
−13.991
1.00
16.20
RNA1
C


ATOM
2063
C6
C
C
1075
8.269
14.217
−14.622
1.00
23.77
RNA1
C


ATOM
2064
P
C
C
1076
10.912
18.423
−12.358
1.00
42.91
RNA1
P


ATOM
2065
O1P
C
C
1076
11.372
17.085
−11.911
1.00
24.52
RNA1
O


ATOM
2066
O2P
C
C
1076
11.781
19.612
−12.113
1.00
41.73
RNA1
O


ATOM
2067
O5*
C
C
1076
9.491
18.679
−11.696
1.00
32.86
RNA1
O


ATOM
2068
C5*
C
C
1076
8.768
19.870
−11.997
1.00
27.46
RNA1
C


ATOM
2069
C4*
C
C
1076
7.458
19.893
−11.255
1.00
30.86
RNA1
C


ATOM
2070
O4*
C
C
1076
6.570
18.885
−11.798
1.00
34.77
RNA1
O


ATOM
2071
C3*
C
C
1076
7.500
19.581
−9.769
1.00
26.66
RNA1
C


ATOM
2072
O3*
C
C
1076
7.913
20.668
−8.961
1.00
36.57
RNA1
O


ATOM
2073
C2*
C
C
1076
6.062
19.172
−9.499
1.00
32.47
RNA1
C


ATOM
2074
O2*
C
C
1076
5.198
20.290
−9.410
1.00
32.97
RNA1
O


ATOM
2075
C1*
C
C
1076
5.735
18.385
−10.765
1.00
34.29
RNA1
C


ATOM
2076
N1
C
C
1076
6.012
16.945
−10.577
1.00
22.34
RNA1
N


ATOM
2077
C2
C
C
1076
5.036
16.150
−9.959
1.00
24.18
RNA1
C


ATOM
2078
O2
C
C
1076
3.977
16.680
−9.577
1.00
25.15
RNA1
O


ATOM
2079
N3
C
C
1076
5.271
14.825
−9.784
1.00
20.85
RNA1
N


ATOM
2080
C4
C
C
1076
6.428
14.295
−10.185
1.00
21.45
RNA1
C


ATOM
2081
N4
C
C
1076
6.611
12.987
−9.994
1.00
19.48
RNA1
N


ATOM
2082
C5
C
C
1076
7.446
15.083
−10.805
1.00
18.25
RNA1
C


ATOM
2083
C6
C
C
1076
7.196
16.389
−10.984
1.00
25.90
RNA1
C


ATOM
2084
P
A
C
1077
8.725
20.374
−7.602
1.00
34.53
RNA1
P


ATOM
2085
O1P
A
C
1077
9.776
19.366
−7.891
1.00
32.29
RNA1
O


ATOM
2086
O2P
A
C
1077
9.115
21.689
−7.025
1.00
55.02
RNA1
O


ATOM
2087
O5*
A
C
1077
7.641
19.691
−6.652
1.00
22.72
RNA1
O


ATOM
2088
C5*
A
C
1077
6.447
20.399
−6.283
1.00
17.11
RNA1
C


ATOM
2089
C4*
A
C
1077
5.461
19.477
−5.601
1.00
26.56
RNA1
C


ATOM
2090
O4*
A
C
1077
5.058
18.423
−6.514
1.00
34.54
RNA1
O


ATOM
2091
C3*
A
C
1077
5.916
18.724
−4.357
1.00
32.85
RNA1
C


ATOM
2092
O3*
A
C
1077
5.872
19.511
−3.175
1.00
37.36
RNA1
O


ATOM
2093
C2*
A
C
1077
4.913
17.576
−4.297
1.00
36.94
RNA1
C


ATOM
2094
O2*
A
C
1077
3.661
17.943
−3.748
1.00
32.73
RNA1
O


ATOM
2095
C1*
A
C
1077
4.723
17.255
−5.778
1.00
32.51
RNA1
C


ATOM
2096
N9
A
C
1077
5.612
16.160
−6.172
1.00
27.14
RNA1
N


ATOM
2097
C8
A
C
1077
6.830
16.224
−6.802
1.00
22.59
RNA1
C


ATOM
2098
N7
A
C
1077
7.406
15.054
−6.959
1.00
28.95
RNA1
N


ATOM
2099
C5
A
C
1077
6.500
14.158
−6.405
1.00
23.18
RNA1
C


ATOM
2100
C6
A
C
1077
6.524
12.758
−6.252
1.00
29.03
RNA1
C


ATOM
2101
N6
A
C
1077
7.543
11.984
−6.643
1.00
32.89
RNA1
N


ATOM
2102
N1
A
C
1077
5.454
12.174
−5.669
1.00
23.42
RNA1
N


ATOM
2103
C2
A
C
1077
4.443
12.948
−5.259
1.00
10.65
RNA1
C


ATOM
2104
N3
A
C
1077
4.309
14.266
−5.338
1.00
26.74
RNA1
N


ATOM
2105
C4
A
C
1077
5.385
14.821
−5.930
1.00
26.08
RNA1
C


ATOM
2106
P
U
C
1078
6.978
19.284
−2.026
1.00
29.17
RNA1
P


ATOM
2107
O1P
U
C
1078
8.330
19.420
−2.616
1.00
22.94
RNA1
O


ATOM
2108
O2P
U
C
1078
6.586
20.141
−0.877
1.00
41.57
RNA1
O


ATOM
2109
O5*
U
C
1078
6.828
17.754
−1.608
1.00
29.90
RNA1
O


ATOM
2110
C5*
U
C
1078
5.706
17.287
−0.830
1.00
21.78
RNA1
C


ATOM
2111
C4*
U
C
1078
5.789
15.785
−0.649
1.00
21.19
RNA1
C


ATOM
2112
O4*
U
C
1078
5.732
15.157
−1.957
1.00
29.99
RNA1
O


ATOM
2113
C3*
U
C
1078
7.075
15.241
−0.031
1.00
27.77
RNA1
C


ATOM
2114
O3*
U
C
1078
7.057
15.184
1.390
1.00
36.77
RNA1
O


ATOM
2115
C2*
U
C
1078
7.094
13.812
−0.554
1.00
34.85
RNA1
C


ATOM
2116
O2*
U
C
1078
6.229
12.972
0.191
1.00
32.65
RNA1
O


ATOM
2117
C1*
U
C
1078
6.532
13.986
−1.963
1.00
28.35
RNA1
C


ATOM
2118
N1
U
C
1078
7.611
14.137
−2.955
1.00
21.70
RNA1
N


ATOM
2119
C2
U
C
1078
8.275
12.987
−3.352
1.00
27.00
RNA1
C


ATOM
2120
O2
U
C
1078
7.975
11.872
−2.946
1.00
29.58
RNA1
O


ATOM
2121
N3
U
C
1078
9.305
13.189
−4.238
1.00
24.66
RNA1
N


ATOM
2122
C4
U
C
1078
9.728
14.393
−4.760
1.00
26.71
RNA1
C


ATOM
2123
O4
U
C
1078
10.714
14.417
−5.504
1.00
44.05
RNA1
O


ATOM
2124
C5
U
C
1078
8.978
15.530
−4.320
1.00
18.54
RNA1
C


ATOM
2125
C6
U
C
1078
7.970
15.368
−3.459
1.00
19.12
RNA1
C


ATOM
2126
P
C
C
1079
7.168
16.527
2.260
1.00
28.61
RNA1
P


ATOM
2127
O1P
C
C
1079
7.780
16.107
3.544
1.00
34.30
RNA1
O


ATOM
2128
O2P
C
C
1079
7.770
17.644
1.487
1.00
31.33
RNA1
O


ATOM
2129
O5*
C
C
1079
5.641
16.867
2.520
1.00
13.04
RNA1
O


ATOM
2130
C5*
C
C
1079
4.851
15.965
3.271
1.00
17.43
RNA1
C


ATOM
2131
C4*
C
C
1079
3.398
16.246
3.064
1.00
19.74
RNA1
C


ATOM
2132
O4*
C
C
1079
2.954
15.688
1.803
1.00
26.36
RNA1
O


ATOM
2133
C3*
C
C
1079
2.556
15.540
4.098
1.00
25.66
RNA1
C


ATOM
2134
O3*
C
C
1079
2.525
16.312
5.278
1.00
37.56
RNA1
O


ATOM
2135
C2*
C
C
1079
1.217
15.382
3.394
1.00
27.27
RNA1
C


ATOM
2136
O2*
C
C
1079
0.452
16.573
3.416
1.00
25.00
RNA1
O


ATOM
2137
C1*
C
C
1079
1.672
15.091
1.963
1.00
17.88
RNA1
C


ATOM
2138
N1
C
C
1079
1.795
13.641
1.677
1.00
17.52
RNA1
N


ATOM
2139
C2
C
C
1079
0.629
12.878
1.441
1.00
19.34
RNA1
C


ATOM
2140
O2
C
C
1079
−0.488
13.427
1.500
1.00
24.52
RNA1
O


ATOM
2141
N3
C
C
1079
0.748
11.561
1.159
1.00
15.18
RNA1
N


ATOM
2142
C4
C
C
1079
1.955
10.994
1.111
1.00
20.12
RNA1
C


ATOM
2143
N4
C
C
1079
2.018
9.691
0.814
1.00
14.62
RNA1
N


ATOM
2144
C5
C
C
1079
3.150
11.734
1.359
1.00
16.35
RNA1
C


ATOM
2145
C6
C
C
1079
3.025
13.040
1.635
1.00
14.99
RNA1
C


ATOM
2146
P
A
C
1080
2.747
15.593
6.692
1.00
32.18
RNA1
P


ATOM
2147
O1P
A
C
1080
3.901
14.668
6.598
1.00
27.65
RNA1
O


ATOM
2148
O2P
A
C
1080
2.748
16.674
7.711
1.00
42.21
RNA1
O


ATOM
2149
O5*
A
C
1080
1.413
14.745
6.853
1.00
24.30
RNA1
O


ATOM
2150
C5*
A
C
1080
0.157
15.421
6.836
1.00
25.92
RNA1
C


ATOM
2151
C4*
A
C
1080
−0.967
14.459
6.593
1.00
27.37
RNA1
C


ATOM
2152
O4*
A
C
1080
−0.902
13.924
5.248
1.00
35.15
RNA1
O


ATOM
2153
C3*
A
C
1080
−1.028
13.223
7.462
1.00
26.09
RNA1
C


ATOM
2154
O3*
A
C
1080
−1.528
13.489
8.759
1.00
36.10
RNA1
O


ATOM
2155
C2*
A
C
1080
−1.956
12.331
6.651
1.00
33.11
RNA1
C


ATOM
2156
O2*
A
C
1080
−3.309
12.717
6.787
1.00
32.80
RNA1
O


ATOM
2157
C1*
A
C
1080
−1.510
12.643
5.223
1.00
26.83
RNA1
C


ATOM
2158
N9
A
C
1080
−0.538
11.650
4.767
1.00
16.76
RNA1
N


ATOM
2159
C8
A
C
1080
0.838
11.722
4.719
1.00
20.21
RNA1
C


ATOM
2160
N7
A
C
1080
1.411
10.609
4.319
1.00
8.53
RNA1
N


ATOM
2161
C5
A
C
1080
0.340
9.754
4.073
1.00
7.38
RNA1
C


ATOM
2162
C6
A
C
1080
0.273
8.414
3.649
1.00
15.76
RNA1
C


ATOM
2163
N6
A
C
1080
1.348
7.660
3.376
1.00
25.46
RNA1
N


ATOM
2164
N1
A
C
1080
−0.952
7.859
3.514
1.00
17.62
RNA1
N


ATOM
2165
C2
A
C
1080
−2.029
8.606
3.785
1.00
16.21
RNA1
C


ATOM
2166
N3
A
C
1080
−2.095
9.868
4.192
1.00
17.28
RNA1
N


ATOM
2167
C4
A
C
1080
−0.861
10.389
4.323
1.00
7.47
RNA1
C


ATOM
2168
P
U
C
1081
−1.136
12.505
9.973
1.00
29.01
RNA1
P


ATOM
2169
O1P
U
C
1081
0.273
12.088
9.807
1.00
19.32
RNA1
O


ATOM
2170
O2P
U
C
1081
−1.558
13.151
11.237
1.00
36.17
RNA1
O


ATOM
2171
O5*
U
C
1081
−2.072
11.248
9.708
1.00
27.53
RNA1
O


ATOM
2172
C5*
U
C
1081
−3.469
11.439
9.421
1.00
34.97
RNA1
C


ATOM
2173
C4*
U
C
1081
−4.093
10.146
8.967
1.00
39.34
RNA1
C


ATOM
2174
O4*
U
C
1081
−3.488
9.719
7.725
1.00
36.64
RNA1
O


ATOM
2175
C3*
U
C
1081
−3.908
8.982
9.922
1.00
36.77
RNA1
C


ATOM
2176
O3*
U
C
1081
−4.954
9.001
10.888
1.00
49.64
RNA1
O


ATOM
2177
C2*
U
C
1081
−4.001
7.774
9.001
1.00
31.27
RNA1
C


ATOM
2178
O2*
U
C
1081
−5.344
7.418
8.739
1.00
35.76
RNA1
O


ATOM
2179
C1*
U
C
1081
−3.375
8.311
7.713
1.00
27.99
RNA1
C


ATOM
2180
N1
U
C
1081
−1.959
7.966
7.513
1.00
16.45
RNA1
N


ATOM
2181
C2
U
C
1081
−1.659
6.684
7.082
1.00
15.53
RNA1
C


ATOM
2182
O2
U
C
1081
−2.511
5.822
6.912
1.00
24.70
RNA1
O


ATOM
2183
N3
U
C
1081
−0.328
6.446
6.856
1.00
6.42
RNA1
N


ATOM
2184
C4
U
C
1081
0.717
7.335
7.015
1.00
17.75
RNA1
C


ATOM
2185
O4
U
C
1081
1.850
7.005
6.656
1.00
12.74
RNA1
O


ATOM
2186
C5
U
C
1081
0.332
8.627
7.495
1.00
15.50
RNA1
C


ATOM
2187
C6
U
C
1081
−0.961
8.890
7.724
1.00
17.69
RNA1
C


ATOM
2188
P
U
C
1082
−4.709
8.375
12.348
1.00
43.16
RNA1
P


ATOM
2189
O1P
U
C
1082
−3.513
9.034
12.942
1.00
33.87
RNA1
O


ATOM
2190
O2P
U
C
1082
−6.019
8.423
13.060
1.00
35.46
RNA1
O


ATOM
2191
O5*
U
C
1082
−4.357
6.855
12.050
1.00
39.66
RNA1
O


ATOM
2192
C5*
U
C
1082
−5.388
5.949
11.643
1.00
36.85
RNA1
C


ATOM
2193
C4*
U
C
1082
−4.834
4.563
11.500
1.00
35.35
RNA1
C


ATOM
2194
O4*
U
C
1082
−4.024
4.471
10.301
1.00
27.83
RNA1
O


ATOM
2195
C3*
U
C
1082
−3.895
4.106
12.600
1.00
42.67
RNA1
C


ATOM
2196
O3*
U
C
1082
−4.544
3.677
13.786
1.00
48.43
RNA1
O


ATOM
2197
C2*
U
C
1082
−3.130
2.979
11.925
1.00
41.00
RNA1
C


ATOM
2198
O2*
U
C
1082
−3.847
1.757
11.941
1.00
43.11
RNA1
O


ATOM
2199
C1*
U
C
1082
−3.000
3.510
10.496
1.00
29.73
RNA1
C


ATOM
2200
N1
U
C
1082
−1.691
4.146
10.281
1.00
21.48
RNA1
N


ATOM
2201
C2
U
C
1082
−0.650
3.342
9.826
1.00
24.74
RNA1
C


ATOM
2202
O2
U
C
1082
−0.781
2.155
9.573
1.00
35.44
RNA1
O


ATOM
2203
N3
U
C
1082
0.552
3.980
9.678
1.00
16.73
RNA1
N


ATOM
2204
C4
U
C
1082
0.825
5.303
9.921
1.00
20.16
RNA1
C


ATOM
2205
O4
U
C
1082
1.963
5.730
9.715
1.00
29.48
RNA1
O


ATOM
2206
C5
U
C
1082
−0.293
6.069
10.378
1.00
15.77
RNA1
C


ATOM
2207
C6
U
C
1082
−1.485
5.479
10.536
1.00
20.32
RNA1
C


ATOM
2208
P
U
C
1083
−3.685
3.548
15.138
1.00
44.11
RNA1
P


ATOM
2209
O1P
U
C
1083
−3.013
4.855
15.416
1.00
33.72
RNA1
O


ATOM
2210
O2P
U
C
1083
−4.550
2.923
16.170
1.00
44.56
RNA1
O


ATOM
2211
O5*
U
C
1083
−2.554
2.515
14.732
1.00
26.53
RNA1
O


ATOM
2212
C5*
U
C
1083
−1.204
2.710
15.133
1.00
27.01
RNA1
C


ATOM
2213
C4*
U
C
1083
−0.310
1.810
14.328
1.00
35.50
RNA1
C


ATOM
2214
O4*
U
C
1083
0.049
2.450
13.077
1.00
37.83
RNA1
O


ATOM
2215
C3*
U
C
1083
1.014
1.490
14.985
1.00
42.54
RNA1
C


ATOM
2216
O3*
U
C
1083
0.829
0.394
15.868
1.00
53.77
RNA1
O


ATOM
2217
C2*
U
C
1083
1.899
1.142
13.797
1.00
40.40
RNA1
C


ATOM
2218
O2*
U
C
1083
1.676
−0.184
13.354
1.00
50.14
RNA1
O


ATOM
2219
C1*
U
C
1083
1.383
2.112
12.733
1.00
31.81
RNA1
C


ATOM
2220
N1
U
C
1083
2.176
3.350
12.641
1.00
27.07
RNA1
N


ATOM
2221
C2
U
C
1083
3.403
3.291
11.995
1.00
27.98
RNA1
C


ATOM
2222
O2
U
C
1083
3.842
2.278
11.491
1.00
38.26
RNA1
O


ATOM
2223
N3
U
C
1083
4.101
4.471
11.959
1.00
27.06
RNA1
N


ATOM
2224
C4
U
C
1083
3.711
5.686
12.480
1.00
29.89
RNA1
C


ATOM
2225
O4
U
C
1083
4.463
6.660
12.376
1.00
35.97
RNA1
O


ATOM
2226
C5
U
C
1083
2.432
5.676
13.120
1.00
28.35
RNA1
C


ATOM
2227
C6
U
C
1083
1.726
4.538
13.180
1.00
34.18
RNA1
C


ATOM
2228
P
A
C
1084
1.531
0.409
17.308
1.00
46.22
RNA1
P


ATOM
2229
O1P
A
C
1084
1.502
1.811
17.819
1.00
47.82
RNA1
O


ATOM
2230
O2P
A
C
1084
0.915
−0.683
18.102
1.00
45.99
RNA1
O


ATOM
2231
O5*
A
C
1084
3.037
0.024
16.984
1.00
32.44
RNA1
O


ATOM
2232
C5*
A
C
1084
4.103
0.403
17.854
1.00
26.01
RNA1
C


ATOM
2233
C4*
A
C
1084
5.395
−0.104
17.293
1.00
30.31
RNA1
C


ATOM
2234
O4*
A
C
1084
5.314
−1.544
17.185
1.00
39.98
RNA1
O


ATOM
2235
C3*
A
C
1084
5.631
0.378
15.881
1.00
31.04
RNA1
C


ATOM
2236
O3*
A
C
1084
6.308
1.611
15.926
1.00
35.76
RNA1
O


ATOM
2237
C2*
A
C
1084
6.448
−0.741
15.252
1.00
34.39
RNA1
C


ATOM
2238
O2*
A
C
1084
7.825
−0.635
15.548
1.00
29.53
RNA1
O


ATOM
2239
C1*
A
C
1084
5.872
−1.970
15.956
1.00
36.40
RNA1
C


ATOM
2240
N9
A
C
1084
4.827
−2.698
15.230
1.00
38.88
RNA1
N


ATOM
2241
C8
A
C
1084
3.464
−2.577
15.388
1.00
38.21
RNA1
C


ATOM
2242
N7
A
C
1084
2.770
−3.432
14.677
1.00
33.92
RNA1
N


ATOM
2243
C5
A
C
1084
3.737
−4.151
13.984
1.00
35.92
RNA1
C


ATOM
2244
C6
A
C
1084
3.648
−5.222
13.069
1.00
34.35
RNA1
C


ATOM
2245
N6
A
C
1084
2.493
−5.781
12.695
1.00
38.02
RNA1
N


ATOM
2246
N1
A
C
1084
4.802
−5.704
12.551
1.00
36.24
RNA1
N


ATOM
2247
C2
A
C
1084
5.960
−5.145
12.935
1.00
38.72
RNA1
C


ATOM
2248
N3
A
C
1084
6.173
−4.143
13.790
1.00
34.15
RNA1
N


ATOM
2249
C4
A
C
1084
5.007
−3.689
14.291
1.00
36.93
RNA1
C


ATOM
2250
P
A
C
1085
5.839
2.793
14.965
1.00
32.91
RNA1
P


ATOM
2251
O1P
A
C
1085
4.351
2.768
14.939
1.00
23.95
RNA1
O


ATOM
2252
O2P
A
C
1085
6.554
4.030
15.366
1.00
36.15
RNA1
O


ATOM
2253
O5*
A
C
1085
6.414
2.342
13.557
1.00
34.02
RNA1
O


ATOM
2254
C5*
A
C
1085
7.826
2.172
13.384
1.00
35.68
RNA1
C


ATOM
2255
C4*
A
C
1085
8.100
1.383
12.136
1.00
40.49
RNA1
C


ATOM
2256
O4*
A
C
1085
7.592
0.035
12.283
1.00
46.64
RNA1
O


ATOM
2257
C3*
A
C
1085
7.426
1.921
10.889
1.00
37.28
RNA1
C


ATOM
2258
O3*
A
C
1085
8.249
2.933
10.322
1.00
38.08
RNA1
O


ATOM
2259
C2*
A
C
1085
7.311
0.685
10.002
1.00
36.45
RNA1
C


ATOM
2260
O2*
A
C
1085
8.496
0.425
9.278
1.00
44.66
RNA1
O


ATOM
2261
C1*
A
C
1085
7.122
−0.432
11.032
1.00
36.77
RNA1
C


ATOM
2262
N9
A
C
1085
5.743
−0.875
11.198
1.00
24.80
RNA1
N


ATOM
2263
C8
A
C
1085
4.754
−0.265
11.923
1.00
28.92
RNA1
C


ATOM
2264
N7
A
C
1085
3.606
−0.896
11.888
1.00
28.93
RNA1
N


ATOM
2265
C5
A
C
1085
3.857
−2.000
11.087
1.00
22.34
RNA1
C


ATOM
2266
C6
A
C
1085
3.040
−3.060
10.664
1.00
26.52
RNA1
C


ATOM
2267
N6
A
C
1085
1.749
−3.175
11.000
1.00
26.24
RNA1
N


ATOM
2268
N1
A
C
1085
3.596
−4.006
9.874
1.00
25.01
RNA1
N


ATOM
2269
C2
A
C
1085
4.889
−3.875
9.532
1.00
27.90
RNA1
C


ATOM
2270
N3
A
C
1085
5.758
−2.920
9.864
1.00
23.94
RNA1
N


ATOM
2271
C4
A
C
1085
5.171
−2.002
10.654
1.00
23.81
RNA1
C


ATOM
2272
P
A
C
1086
7.578
4.220
9.636
1.00
38.44
RNA1
P


ATOM
2273
O1P
A
C
1086
6.238
4.440
10.244
1.00
21.00
RNA1
O


ATOM
2274
O2P
A
C
1086
8.578
5.315
9.641
1.00
32.04
RNA1
O


ATOM
2275
O5*
A
C
1086
7.359
3.750
8.133
1.00
44.64
RNA1
O


ATOM
2276
C5*
A
C
1086
8.465
3.286
7.337
1.00
27.97
RNA1
C


ATOM
2277
C4*
A
C
1086
7.965
2.407
6.217
1.00
34.03
RNA1
C


ATOM
2278
O4*
A
C
1086
7.509
1.138
6.753
1.00
34.69
RNA1
O


ATOM
2279
C3*
A
C
1086
6.759
2.929
5.455
1.00
38.31
RNA1
C


ATOM
2280
O3*
A
C
1086
7.095
3.913
4.484
1.00
30.65
RNA1
O


ATOM
2281
C2*
A
C
1086
6.166
1.659
4.850
1.00
40.89
RNA1
C


ATOM
2282
O2*
A
C
1086
6.734
1.284
3.610
1.00
37.38
RNA1
O


ATOM
2283
C1*
A
C
1086
6.488
0.616
5.925
1.00
29.88
RNA1
C


ATOM
2284
N9
A
C
1086
5.326
0.253
6.739
1.00
26.28
RNA1
N


ATOM
2285
C8
A
C
1086
4.885
−1.015
7.018
1.00
26.71
RNA1
C


ATOM
2286
N7
A
C
1086
3.748
−1.049
7.675
1.00
32.50
RNA1
N


ATOM
2287
C5
A
C
1086
3.437
0.289
7.869
1.00
23.83
RNA1
C


ATOM
2288
C6
A
C
1086
2.346
0.926
8.486
1.00
32.24
RNA1
C


ATOM
2289
N6
A
C
1086
1.320
0.274
9.042
1.00
40.46
RNA1
N


ATOM
2290
N1
A
C
1086
2.340
2.275
8.508
1.00
27.06
RNA1
N


ATOM
2291
C2
A
C
1086
3.359
2.928
7.943
1.00
26.31
RNA1
C


ATOM
2292
N3
A
C
1086
4.435
2.444
7.329
1.00
27.72
RNA1
N


ATOM
2293
C4
A
C
1086
4.413
1.102
7.323
1.00
23.09
RNA1
C


ATOM
2294
P
G
C
1087
6.254
5.281
4.430
1.00
30.97
RNA1
P


ATOM
2295
O1P
G
C
1087
4.896
4.969
3.921
1.00
19.34
RNA1
O


ATOM
2296
O2P
G
C
1087
6.402
5.980
5.734
1.00
46.09
RNA1
O


ATOM
2297
O5*
G
C
1087
7.006
6.141
3.329
1.00
29.62
RNA1
O


ATOM
2298
C5*
G
C
1087
8.108
6.998
3.667
1.00
28.45
RNA1
C


ATOM
2299
C4*
G
C
1087
8.911
7.283
2.428
1.00
31.27
RNA1
C


ATOM
2300
O4*
G
C
1087
9.604
6.075
2.060
1.00
35.33
RNA1
O


ATOM
2301
C3*
G
C
1087
8.034
7.656
1.244
1.00
31.37
RNA1
C


ATOM
2302
O3*
G
C
1087
7.978
9.077
1.163
1.00
19.46
RNA1
O


ATOM
2303
C2*
G
C
1087
8.776
7.064
0.049
1.00
32.80
RNA1
C


ATOM
2304
O2*
G
C
1087
9.745
7.961
−0.462
1.00
29.59
RNA1
O


ATOM
2305
C1*
G
C
1087
9.484
5.854
0.674
1.00
27.32
RNA1
C


ATOM
2306
N9
G
C
1087
8.899
4.525
0.520
1.00
19.62
RNA1
N


ATOM
2307
C8
G
C
1087
7.596
4.129
0.735
1.00
23.90
RNA1
C


ATOM
2308
N7
G
C
1087
7.429
2.836
0.618
1.00
9.45
RNA1
N


ATOM
2309
C5
G
C
1087
8.685
2.359
0.273
1.00
16.55
RNA1
C


ATOM
2310
C6
G
C
1087
9.128
1.036
0.007
1.00
25.58
RNA1
C


ATOM
2311
O6
G
C
1087
8.476
−0.016
0.029
1.00
25.76
RNA1
O


ATOM
2312
N1
G
C
1087
10.483
1.004
−0.307
1.00
13.38
RNA1
N


ATOM
2313
C2
G
C
1087
11.309
2.103
−0.354
1.00
25.58
RNA1
C


ATOM
2314
N2
G
C
1087
12.595
1.870
−0.653
1.00
21.09
RNA1
N


ATOM
2315
N3
G
C
1087
10.906
3.341
−0.116
1.00
22.18
RNA1
N


ATOM
2316
C4
G
C
1087
9.596
3.394
0.191
1.00
16.33
RNA1
C


ATOM
2317
P
A
C
1088
6.677
9.862
1.669
1.00
23.48
RNA1
P


ATOM
2318
O1P
A
C
1088
6.035
9.121
2.788
1.00
34.67
RNA1
O


ATOM
2319
O2P
A
C
1088
7.106
11.267
1.858
1.00
30.75
RNA1
O


ATOM
2320
O5*
A
C
1088
5.683
9.810
0.434
1.00
34.79
RNA1
O


ATOM
2321
C5*
A
C
1088
6.166
10.084
−0.886
1.00
33.74
RNA1
C


ATOM
2322
C4*
A
C
1088
5.808
8.952
−1.804
1.00
29.37
RNA1
C


ATOM
2323
O4*
A
C
1088
4.376
8.744
−1.752
1.00
30.18
RNA1
O


ATOM
2324
C3*
A
C
1088
6.153
9.200
−3.261
1.00
27.75
RNA1
C


ATOM
2325
O3*
A
C
1088
6.465
7.951
−3.847
1.00
19.39
RNA1
O


ATOM
2326
C2*
A
C
1088
4.848
9.717
−3.842
1.00
20.69
RNA1
C


ATOM
2327
O2*
A
C
1088
4.730
9.462
−5.224
1.00
39.54
RNA1
O


ATOM
2328
C1*
A
C
1088
3.821
8.926
−3.035
1.00
19.38
RNA1
C


ATOM
2329
N9
A
C
1088
2.553
9.623
−2.868
1.00
12.67
RNA1
N


ATOM
2330
C8
A
C
1088
1.291
9.132
−3.089
1.00
19.49
RNA1
C


ATOM
2331
N7
A
C
1088
0.338
9.996
−2.842
1.00
19.80
RNA1
N


ATOM
2332
C5
A
C
1088
1.019
11.134
−2.432
1.00
11.03
RNA1
C


ATOM
2333
C6
A
C
1088
0.578
12.406
−2.033
1.00
14.84
RNA1
C


ATOM
2334
N6
A
C
1088
−0.708
12.768
−1.988
1.00
13.38
RNA1
N


ATOM
2335
N1
A
C
1088
1.517
13.309
−1.680
1.00
16.35
RNA1
N


ATOM
2336
C2
A
C
1088
2.807
12.952
−1.736
1.00
16.68
RNA1
C


ATOM
2337
N3
A
C
1088
3.343
11.792
−2.099
1.00
19.47
RNA1
N


ATOM
2338
C4
A
C
1088
2.383
10.917
−2.440
1.00
11.60
RNA1
C


ATOM
2339
P
G
C
1089
7.282
7.896
−5.216
1.00
26.48
RNA1
P


ATOM
2340
O1P
G
C
1089
7.768
9.270
−5.525
1.00
30.79
RNA1
O


ATOM
2341
O2P
G
C
1089
6.437
7.171
−6.198
1.00
18.45
RNA1
O


ATOM
2342
O5*
G
C
1089
8.548
7.011
−4.853
1.00
14.93
RNA1
O


ATOM
2343
C5*
G
C
1089
9.568
7.515
−3.971
1.00
29.50
RNA1
C


ATOM
2344
C4*
G
C
1089
10.362
6.367
−3.400
1.00
26.25
RNA1
C


ATOM
2345
O4*
G
C
1089
9.469
5.554
−2.600
1.00
34.26
RNA1
O


ATOM
2346
C3*
G
C
1089
10.981
5.439
−4.439
1.00
20.63
RNA1
C


ATOM
2347
O3*
G
C
1089
12.197
4.922
−3.925
1.00
28.79
RNA1
O


ATOM
2348
C2*
G
C
1089
9.965
4.305
−4.531
1.00
28.82
RNA1
C


ATOM
2349
O2*
G
C
1089
10.543
3.072
−4.908
1.00
40.76
RNA1
O


ATOM
2350
C1*
G
C
1089
9.439
4.238
−3.099
1.00
19.76
RNA1
C


ATOM
2351
N9
G
C
1089
8.069
3.749
−2.988
1.00
15.09
RNA1
N


ATOM
2352
C8
G
C
1089
6.930
4.499
−2.817
1.00
17.24
RNA1
C


ATOM
2353
N7
G
C
1089
5.848
3.773
−2.729
1.00
20.25
RNA1
N


ATOM
2354
C5
G
C
1089
6.301
2.466
−2.857
1.00
14.36
RNA1
C


ATOM
2355
C6
G
C
1089
5.590
1.243
−2.839
1.00
23.53
RNA1
C


ATOM
2356
O6
G
C
1089
4.368
1.060
−2.704
1.00
38.04
RNA1
O


ATOM
2357
N1
G
C
1089
6.442
0.156
−2.998
1.00
10.56
RNA1
N


ATOM
2358
C2
G
C
1089
7.801
0.235
−3.159
1.00
16.75
RNA1
C


ATOM
2359
N2
G
C
1089
8.456
−0.931
−3.305
1.00
18.05
RNA1
N


ATOM
2360
N3
G
C
1089
8.475
1.369
−3.178
1.00
14.70
RNA1
N


ATOM
2361
C4
G
C
1089
7.668
2.437
−3.022
1.00
10.92
RNA1
C


ATOM
2362
P
U
C
1090
13.585
5.675
−4.221
1.00
43.14
RNA1
P


ATOM
2363
O1P
U
C
1090
13.436
6.453
−5.476
1.00
42.35
RNA1
O


ATOM
2364
O2P
U
C
1090
14.010
6.371
−2.971
1.00
42.92
RNA1
O


ATOM
2365
O5*
U
C
1090
14.587
4.467
−4.490
1.00
39.62
RNA1
O


ATOM
2366
C5*
U
C
1090
15.989
4.585
−4.207
1.00
45.78
RNA1
C


ATOM
2367
C4*
U
C
1090
16.693
3.275
−4.492
1.00
55.27
RNA1
C


ATOM
2368
O4*
U
C
1090
16.237
2.246
−3.570
1.00
55.21
RNA1
O


ATOM
2369
C3*
U
C
1090
16.455
2.661
−5.862
1.00
53.66
RNA1
C


ATOM
2370
O3*
U
C
1090
17.267
3.222
−6.875
1.00
51.89
RNA1
O


ATOM
2371
C2*
U
C
1090
16.781
1.194
−5.637
1.00
48.18
RNA1
C


ATOM
2372
O2*
U
C
1090
18.172
0.949
−5.690
1.00
54.31
RNA1
O


ATOM
2373
C1*
U
C
1090
16.271
0.979
−4.213
1.00
41.15
RNA1
C


ATOM
2374
N1
U
C
1090
14.922
0.387
−4.190
1.00
41.07
RNA1
N


ATOM
2375
C2
U
C
1090
14.823
−0.998
−4.283
1.00
36.51
RNA1
C


ATOM
2376
O2
U
C
1090
15.792
−1.730
−4.388
1.00
37.99
RNA1
O


ATOM
2377
N3
U
C
1090
13.542
−1.493
−4.256
1.00
24.06
RNA1
N


ATOM
2378
C4
U
C
1090
12.374
−0.772
−4.150
1.00
29.36
RNA1
C


ATOM
2379
O4
U
C
1090
11.297
−1.373
−4.078
1.00
32.44
RNA1
O


ATOM
2380
C5
U
C
1090
12.554
0.649
−4.068
1.00
27.73
RNA1
C


ATOM
2381
C6
U
C
1090
13.788
1.167
−4.087
1.00
33.24
RNA1
C


ATOM
2382
P
G
C
1091
16.725
3.245
−8.383
1.00
58.06
RNA1
P


ATOM
2383
O1P
G
C
1091
15.277
3.599
−8.351
1.00
49.18
RNA1
O


ATOM
2384
O2P
G
C
1091
17.668
4.074
−9.177
1.00
62.85
RNA1
O


ATOM
2385
O5*
G
C
1091
16.838
1.724
−8.851
1.00
59.36
RNA1
O


ATOM
2386
C5*
G
C
1091
18.123
1.141
−9.135
1.00
62.76
RNA1
C


ATOM
2387
C4*
G
C
1091
18.029
−0.370
−9.212
1.00
62.76
RNA1
C


ATOM
2388
O4*
G
C
1091
17.448
−0.882
−7.980
1.00
57.83
RNA1
O


ATOM
2389
C3*
G
C
1091
17.168
−0.998
−10.302
1.00
67.15
RNA1
C


ATOM
2390
O3*
G
C
1091
17.800
−1.073
−11.581
1.00
73.47
RNA1
O


ATOM
2391
C2*
G
C
1091
16.911
−2.391
−9.736
1.00
63.68
RNA1
C


ATOM
2392
O2*
G
C
1091
17.997
−3.276
−9.939
1.00
66.38
RNA1
O


ATOM
2393
C1*
G
C
1091
16.766
−2.098
−8.243
1.00
52.76
RNA1
C


ATOM
2394
N9
G
C
1091
15.354
−1.954
−7.902
1.00
42.68
RNA1
N


ATOM
2395
C8
G
C
1091
14.638
−0.795
−7.717
1.00
43.79
RNA1
C


ATOM
2396
N7
G
C
1091
13.368
−1.009
−7.490
1.00
42.36
RNA1
N


ATOM
2397
C5
G
C
1091
13.243
−2.392
−7.512
1.00
31.07
RNA1
C


ATOM
2398
C6
G
C
1091
12.100
−3.220
−7.342
1.00
32.80
RNA1
C


ATOM
2399
O6
G
C
1091
10.926
−2.886
−7.133
1.00
29.29
RNA1
O


ATOM
2400
N1
G
C
1091
12.427
−4.567
−7.442
1.00
27.53
RNA1
N


ATOM
2401
C2
G
C
1091
13.687
−5.057
−7.676
1.00
37.58
RNA1
C


ATOM
2402
N2
G
C
1091
13.806
−6.387
−7.734
1.00
43.37
RNA1
N


ATOM
2403
N3
G
C
1091
14.754
−4.300
−7.840
1.00
37.83
RNA1
N


ATOM
2404
C4
G
C
1091
14.461
−2.989
−7.748
1.00
34.74
RNA1
C


ATOM
2405
P
C
C
1092
16.901
−1.334
−12.902
1.00
78.16
RNA1
P


ATOM
2406
O1P
C
C
1092
15.717
−0.429
−12.869
1.00
76.90
RNA1
O


ATOM
2407
O2P
C
C
1092
17.813
−1.307
−14.079
1.00
77.44
RNA1
O


ATOM
2408
O5*
C
C
1092
16.360
−2.822
−12.721
1.00
69.64
RNA1
O


ATOM
2409
C5*
C
C
1092
17.277
−3.929
−12.693
1.00
63.11
RNA1
C


ATOM
2410
C4*
C
C
1092
16.536
−5.243
−12.604
1.00
59.28
RNA1
C


ATOM
2411
O4*
C
C
1092
15.859
−5.364
−11.322
1.00
50.31
RNA1
O


ATOM
2412
C3*
C
C
1092
15.433
−5.487
−13.621
1.00
60.54
RNA1
C


ATOM
2413
O3*
C
C
1092
15.910
−5.898
−14.893
1.00
61.03
RNA1
O


ATOM
2414
C2*
C
C
1092
14.614
−6.580
−12.949
1.00
56.00
RNA1
C


ATOM
2415
O2*
C
C
1092
15.155
−7.875
−13.128
1.00
59.60
RNA1
O


ATOM
2416
C1*
C
C
1092
14.704
−6.175
−11.477
1.00
46.68
RNA1
C


ATOM
2417
N1
C
C
1092
13.500
−5.411
−11.103
1.00
45.69
RNA1
N


ATOM
2418
C2
C
C
1092
12.311
−6.125
−10.845
1.00
48.75
RNA1
C


ATOM
2419
O2
C
C
1092
12.334
−7.367
−10.877
1.00
35.22
RNA1
O


ATOM
2420
N3
C
C
1092
11.175
−5.443
−10.568
1.00
40.06
RNA1
N


ATOM
2421
C4
C
C
1092
11.191
−4.109
−10.529
1.00
43.65
RNA1
C


ATOM
2422
N4
C
C
1092
10.043
−3.483
−10.269
1.00
38.14
RNA1
N


ATOM
2423
C5
C
C
1092
12.386
−3.357
−10.759
1.00
43.83
RNA1
C


ATOM
2424
C6
C
C
1092
13.508
−4.043
−11.036
1.00
48.70
RNA1
C


ATOM
2425
P
G
C
1093
15.082
−5.497
−16.210
1.00
59.69
RNA1
P


ATOM
2426
O1P
G
C
1093
14.954
−4.014
−16.213
1.00
64.26
RNA1
O


ATOM
2427
O2P
G
C
1093
15.706
−6.182
−17.376
1.00
68.36
RNA1
O


ATOM
2428
O5*
G
C
1093
13.629
−6.109
−15.961
1.00
39.18
RNA1
O


ATOM
2429
C5*
G
C
1093
13.440
−7.525
−15.810
1.00
34.94
RNA1
C


ATOM
2430
C4*
G
C
1093
12.017
−7.828
−15.395
1.00
40.12
RNA1
C


ATOM
2431
O4*
G
C
1093
11.737
−7.199
−14.117
1.00
45.67
RNA1
O


ATOM
2432
C3*
G
C
1093
10.929
−7.304
−16.315
1.00
43.53
RNA1
C


ATOM
2433
O3*
G
C
1093
10.687
−8.168
−17.410
1.00
48.03
RNA1
O


ATOM
2434
C2*
G
C
1093
9.720
−7.183
−15.391
1.00
41.69
RNA1
C


ATOM
2435
O2*
G
C
1093
8.996
−8.389
−15.229
1.00
27.92
RNA1
O


ATOM
2436
C1*
G
C
1093
10.381
−6.769
−14.075
1.00
38.16
RNA1
C


ATOM
2437
N9
G
C
1093
10.350
−5.318
−13.870
1.00
36.77
RNA1
N


ATOM
2438
C8
G
C
1093
11.401
−4.431
−13.970
1.00
34.83
RNA1
C


ATOM
2439
N7
G
C
1093
11.048
−3.190
−13.762
1.00
32.06
RNA1
N


ATOM
2440
C5
G
C
1093
9.685
−3.259
−13.505
1.00
27.72
RNA1
C


ATOM
2441
C6
G
C
1093
8.752
−2.231
−13.223
1.00
27.54
RNA1
C


ATOM
2442
O6
G
C
1093
8.947
−1.013
−13.160
1.00
34.45
RNA1
O


ATOM
2443
N1
G
C
1093
7.475
−2.743
−13.014
1.00
19.53
RNA1
N


ATOM
2444
C2
G
C
1093
7.136
−4.075
−13.075
1.00
19.64
RNA1
C


ATOM
2445
N2
G
C
1093
5.851
−4.382
−12.830
1.00
17.24
RNA1
N


ATOM
2446
N3
G
C
1093
7.993
−5.040
−13.352
1.00
21.92
RNA1
N


ATOM
2447
C4
G
C
1093
9.241
−4.566
−13.554
1.00
25.99
RNA1
C


ATOM
2448
P
U
C
1094
10.214
−7.545
−18.808
1.00
48.86
RNA1
P


ATOM
2449
O1P
U
C
1094
11.019
−6.314
−19.033
1.00
51.40
RNA1
O


ATOM
2450
O2P
U
C
1094
10.225
−8.631
−19.820
1.00
62.99
RNA1
O


ATOM
2451
O5*
U
C
1094
8.700
−7.137
−18.549
1.00
35.14
RNA1
O


ATOM
2452
C5*
U
C
1094
7.726
−8.151
−18.319
1.00
39.65
RNA1
C


ATOM
2453
C4*
U
C
1094
6.342
−7.561
−18.289
1.00
45.60
RNA1
C


ATOM
2454
O4*
U
C
1094
6.086
−6.907
−17.022
1.00
47.84
RNA1
O


ATOM
2455
C3*
U
C
1094
6.030
−6.503
−19.328
1.00
46.03
RNA1
C


ATOM
2456
O3*
U
C
1094
5.775
−7.078
−20.601
1.00
56.79
RNA1
O


ATOM
2457
C2*
U
C
1094
4.829
−5.786
−18.713
1.00
44.04
RNA1
C


ATOM
2458
O2*
U
C
1094
3.588
−6.431
−18.943
1.00
37.76
RNA1
O


ATOM
2459
C1*
U
C
1094
5.168
−5.844
−17.219
1.00
44.47
RNA1
C


ATOM
2460
N1
U
C
1094
5.770
−4.589
−16.742
1.00
26.87
RNA1
N


ATOM
2461
C2
U
C
1094
4.909
−3.585
−16.329
1.00
22.09
RNA1
C


ATOM
2462
O2
U
C
1094
3.691
−3.719
−16.288
1.00
25.93
RNA1
O


ATOM
2463
N3
U
C
1094
5.519
−2.419
−15.962
1.00
13.38
RNA1
N


ATOM
2464
C4
U
C
1094
6.869
−2.159
−15.947
1.00
36.16
RNA1
C


ATOM
2465
O4
U
C
1094
7.263
−1.036
−15.621
1.00
36.16
RNA1
O


ATOM
2466
C5
U
C
1094
7.696
−3.256
−16.357
1.00
27.39
RNA1
C


ATOM
2467
C6
U
C
1094
7.131
−4.404
−16.729
1.00
19.00
RNA1
C


ATOM
2468
P
A
C
1095
6.404
−6.394
−21.913
1.00
56.22
RNA1
P


ATOM
2469
O1P
A
C
1095
7.761
−5.866
−21.571
1.00
36.24
RNA1
O


ATOM
2470
O2P
A
C
1095
6.257
−7.345
−23.045
1.00
62.45
RNA1
O


ATOM
2471
O5*
A
C
1095
5.420
−5.169
−22.156
1.00
37.34
RNA1
O


ATOM
2472
C5*
A
C
1095
5.858
−3.993
−22.836
1.00
26.88
RNA1
C


ATOM
2473
C4*
A
C
1095
4.732
−3.002
−22.897
1.00
25.01
RNA1
C


ATOM
2474
O4*
A
C
1095
3.576
−3.668
−23.451
1.00
31.13
RNA1
O


ATOM
2475
C3*
A
C
1095
4.254
−2.489
−21.555
1.00
30.12
RNA1
C


ATOM
2476
O3*
A
C
1095
5.068
−1.403
−21.134
1.00
47.22
RNA1
O


ATOM
2477
C2*
A
C
1095
2.797
−2.116
−21.824
1.00
32.85
RNA1
C


ATOM
2478
O2*
A
C
1095
2.630
−0.839
−22.418
1.00
29.79
RNA1
O


ATOM
2479
C1*
A
C
1095
2.395
−3.179
−22.845
1.00
21.93
RNA1
C


ATOM
2480
N9
A
C
1095
1.649
−4.328
−22.333
1.00
17.01
RNA1
N


ATOM
2481
C8
A
C
1095
2.142
−5.568
−21.985
1.00
21.36
RNA1
C


ATOM
2482
N7
A
C
1095
1.211
−6.424
−21.627
1.00
21.32
RNA1
N


ATOM
2483
C5
A
C
1095
0.031
−5.696
−21.729
1.00
10.86
RNA1
C


ATOM
2484
C6
A
C
1095
−1.315
−6.037
−21.498
1.00
23.82
RNA1
C


ATOM
2485
N6
A
C
1095
−1.717
−7.254
−21.118
1.00
35.80
RNA1
N


ATOM
2486
N1
A
C
1095
−2.249
−5.076
−21.679
1.00
30.20
RNA1
N


ATOM
2487
C2
A
C
1095
−1.844
−3.861
−22.076
1.00
23.15
RNA1
C


ATOM
2488
N3
A
C
1095
−0.610
−3.423
−22.337
1.00
20.47
RNA1
N


ATOM
2489
C4
A
C
1095
0.289
−4.399
−22.143
1.00
9.00
RNA1
C


ATOM
2490
P
A
C
1096
5.554
−1.325
−19.607
1.00
33.71
RNA1
P


ATOM
2491
O1P
A
C
1096
5.985
−2.689
−19.209
1.00
38.06
RNA1
O


ATOM
2492
O2P
A
C
1096
6.505
−0.198
−19.472
1.00
30.42
RNA1
O


ATOM
2493
O5*
A
C
1096
4.203
−0.950
−18.856
1.00
19.71
RNA1
O


ATOM
2494
C5*
A
C
1096
3.610
0.332
−19.065
1.00
17.59
RNA1
C


ATOM
2495
C4*
A
C
1096
2.176
0.335
−18.609
1.00
25.20
RNA1
C


ATOM
2496
O4*
A
C
1096
1.399
−0.548
−19.452
1.00
36.18
RNA1
O


ATOM
2497
C3*
A
C
1096
1.916
−0.155
−17.197
1.00
31.52
RNA1
C


ATOM
2498
O3*
A
C
1096
2.158
0.858
−16.224
1.00
40.13
RNA1
O


ATOM
2499
C2*
A
C
1096
0.458
−0.589
−17.277
1.00
29.94
RNA1
C


ATOM
2500
O2*
A
C
1096
−0.436
0.497
−17.220
1.00
33.53
RNA1
O


ATOM
2501
C1*
A
C
1096
0.392
−1.181
−18.684
1.00
28.76
RNA1
C


ATOM
2502
N9
A
C
1096
0.682
−2.615
−18.662
1.00
29.57
RNA1
N


ATOM
2503
C8
A
C
1096
1.915
−3.230
−18.760
1.00
20.07
RNA1
C


ATOM
2504
N7
A
C
1096
1.862
−4.536
−18.673
1.00
16.60
RNA1
N


ATOM
2505
C5
A
C
1096
0.506
−4.803
−18.515
1.00
21.73
RNA1
C


ATOM
2506
C6
A
C
1096
−0.207
−6.004
−18.372
1.00
21.62
RNA1
C


ATOM
2507
N6
A
C
1096
0.376
−7.207
−18.386
1.00
30.29
RNA1
N


ATOM
2508
N1
A
C
1096
−1.551
−5.928
−18.222
1.00
19.53
RNA1
N


ATOM
2509
C2
A
C
1096
−2.130
−4.715
−18.234
1.00
19.83
RNA1
C


ATOM
2510
N3
A
C
1096
−1.565
−3.512
−18.377
1.00
21.31
RNA1
N


ATOM
2511
C4
A
C
1096
−0.231
−3.630
−18.511
1.00
13.07
RNA1
C


ATOM
2512
P
C
C
1097
2.770
0.451
−14.795
1.00
34.58
RNA1
P


ATOM
2513
O1P
C
C
1097
3.901
−0.488
−15.013
1.00
24.95
RNA1
O


ATOM
2514
O2P
C
C
1097
3.010
1.716
−14.062
1.00
42.37
RNA1
O


ATOM
2515
O5*
C
C
1097
1.558
−0.333
−14.115
1.00
33.44
RNA1
O


ATOM
2516
C5*
C
C
1097
1.711
−1.664
−13.564
1.00
27.30
RNA1
C


ATOM
2517
C4*
C
C
1097
0.347
−2.298
−13.386
1.00
34.16
RNA1
C


ATOM
2518
O4*
C
C
1097
−0.067
−2.943
−14.625
1.00
37.39
RNA1
O


ATOM
2519
C3*
C
C
1097
0.219
−3.406
−12.354
1.00
33.88
RNA1
C


ATOM
2520
O3*
C
C
1097
0.093
−2.924
−11.025
1.00
36.37
RNA1
O


ATOM
2521
C2*
C
C
1097
−1.041
−4.120
−12.816
1.00
36.19
RNA1
C


ATOM
2522
O2*
C
C
1097
−2.214
−3.415
−12.457
1.00
31.86
RNA1
O


ATOM
2523
C1*
C
C
1097
−0.865
−4.089
−14.334
1.00
35.36
RNA1
C


ATOM
2524
N1
C
C
1097
−0.146
−5.311
−14.780
1.00
29.78
RNA1
N


ATOM
2525
C2
C
C
1097
−0.859
−6.537
−14.895
1.00
31.29
RNA1
C


ATOM
2526
O2
C
C
1097
−2.097
−6.552
−14.732
1.00
30.74
RNA1
O


ATOM
2527
N3
C
C
1097
−0.175
−7.667
−15.188
1.00
27.52
RNA1
N


ATOM
2528
C4
C
C
1097
1.146
−7.616
−15.390
1.00
35.55
RNA1
C


ATOM
2529
N4
C
C
1097
1.788
−8.764
−15.640
1.00
38.53
RNA1
N


ATOM
2530
C5
C
C
1097
1.874
−6.389
−15.338
1.00
27.77
RNA1
C


ATOM
2531
C6
C
C
1097
1.197
−5.275
−15.036
1.00
24.47
RNA1
C


ATOM
2532
P
A
C
1098
1.072
−3.493
−9.886
1.00
38.47
RNA1
P


ATOM
2533
O1P
A
C
1098
2.477
−3.131
−10.212
1.00
22.01
RNA1
O


ATOM
2534
O2P
A
C
1098
0.484
−3.068
−8.588
1.00
56.40
RNA1
O


ATOM
2535
O5*
A
C
1098
0.959
−5.079
−10.023
1.00
40.54
RNA1
O


ATOM
2536
C5*
A
C
1098
−0.328
−5.740
−9.972
1.00
47.03
RNA1
C


ATOM
2537
C4*
A
C
1098
−0.192
−7.201
−10.348
1.00
50.05
RNA1
C


ATOM
2538
O4*
A
C
1098
0.276
−7.310
−11.720
1.00
43.04
RNA1
O


ATOM
2539
C3*
A
C
1098
0.819
−8.007
−9.544
1.00
59.35
RNA1
C


ATOM
2540
O3*
A
C
1098
0.289
−8.467
−8.305
1.00
57.94
RNA1
O


ATOM
2541
C2*
A
C
1098
1.170
−9.146
−10.496
1.00
54.42
RNA1
C


ATOM
2542
O2*
A
C
1098
0.229
−10.203
−10.479
1.00
63.88
RNA1
O


ATOM
2543
C1*
A
C
1098
1.125
−8.440
−11.851
1.00
42.41
RNA1
C


ATOM
2544
N9
A
C
1098
2.456
−7.982
−12.247
1.00
29.98
RNA1
N


ATOM
2545
C8
A
C
1098
2.967
−6.709
−12.213
1.00
32.72
RNA1
C


ATOM
2546
N7
A
C
1098
4.222
−6.633
−12.588
1.00
34.32
RNA1
N


ATOM
2547
C5
A
C
1098
4.557
−7.942
−12.902
1.00
34.44
RNA1
C


ATOM
2548
C6
A
C
1098
5.751
−8.533
−13.363
1.00
43.55
RNA1
C


ATOM
2549
N6
A
C
1098
6.879
−7.852
−13.597
1.00
39.58
RNA1
N


ATOM
2550
N1
A
C
1098
5.746
−9.866
−13.579
1.00
48.91
RNA1
N


ATOM
2551
C2
A
C
1098
4.615
−10.549
−13.348
1.00
42.95
RNA1
C


ATOM
2552
N3
A
C
1098
3.435
−10.108
−12.916
1.00
35.82
RNA1
N


ATOM
2553
C4
A
C
1098
3.474
−8.782
−12.708
1.00
35.65
RNA1
C


ATOM
2554
P
G
C
1099
1.238
−8.516
−7.006
1.00
52.26
RNA1
P


ATOM
2555
O1P
G
C
1099
1.696
−7.137
−6.706
1.00
52.99
RNA1
O


ATOM
2556
O2P
G
C
1099
0.511
−9.287
−5.970
1.00
54.62
RNA1
O


ATOM
2557
O5*
G
C
1099
2.513
−9.346
−7.481
1.00
43.47
RNA1
O


ATOM
2558
C5*
G
C
1099
2.413
−10.749
−7.772
1.00
41.68
RNA1
C


ATOM
2559
C4*
G
C
1099
3.735
−11.273
−8.271
1.00
42.05
RNA1
C


ATOM
2560
O4*
G
C
1099
4.033
−10.671
−9.554
1.00
43.83
RNA1
O


ATOM
2561
C3*
G
C
1099
4.938
−10.934
−7.409
1.00
48.09
RNA1
C


ATOM
2562
O3*
G
C
1099
5.100
−11.821
−6.317
1.00
58.27
RNA1
O


ATOM
2563
C2*
G
C
1099
6.089
−10.992
−8.402
1.00
50.43
RNA1
C


ATOM
2564
O2*
G
C
1099
6.588
−12.296
−8.639
1.00
57.02
RNA1
O


ATOM
2565
C1*
G
C
1099
5.426
−10.432
−9.660
1.00
44.89
RNA1
C


ATOM
2566
N9
G
C
1099
5.639
−8.989
−9.729
1.00
45.65
RNA1
N


ATOM
2567
C8
G
C
1099
4.714
−7.993
−9.515
1.00
38.56
RNA1
C


ATOM
2568
N7
G
C
1099
5.228
−6.796
−9.584
1.00
41.94
RNA1
N


ATOM
2569
C5
G
C
1099
6.569
−7.014
−9.873
1.00
34.92
RNA1
C


ATOM
2570
C6
G
C
1099
7.631
−6.094
−10.053
1.00
42.48
RNA1
C


ATOM
2571
O6
G
C
1099
7.601
−4.857
−9.985
1.00
44.46
RNA1
O


ATOM
2572
N1
G
C
1099
8.829
−6.746
−10.336
1.00
41.82
RNA1
N


ATOM
2573
C2
G
C
1099
8.982
−8.108
−10.437
1.00
42.77
RNA1
C


ATOM
2574
N2
G
C
1099
10.211
−8.548
−10.736
1.00
31.50
RNA1
N


ATOM
2575
N3
G
C
1099
8.001
−8.974
−10.262
1.00
31.12
RNA1
N


ATOM
2576
C4
G
C
1099
6.832
−8.362
−9.984
1.00
33.36
RNA1
C


ATOM
2577
P
C
C
1100
5.772
−11.286
−4.956
1.00
62.31
RNA1
P


ATOM
2578
O1P
C
C
1100
5.270
−9.914
−4.687
1.00
56.23
RNA1
O


ATOM
2579
O2P
C
C
1100
5.583
−12.348
−3.934
1.00
65.10
RNA1
O


ATOM
2580
O5*
C
C
1100
7.320
−11.188
−5.316
1.00
45.54
RNA1
O


ATOM
2581
C5*
C
C
1100
8.052
−12.366
−5.670
1.00
43.72
RNA1
C


ATOM
2582
C4*
C
C
1100
9.458
−12.015
−6.069
1.00
40.97
RNA1
C


ATOM
2583
O4*
C
C
1100
9.429
−11.213
−7.276
1.00
44.70
RNA1
O


ATOM
2584
C3*
C
C
1100
10.249
−11.173
−5.087
1.00
43.30
RNA1
C


ATOM
2585
O3*
C
C
1100
10.817
−11.913
−4.022
1.00
57.32
RNA1
O


ATOM
2586
C2*
C
C
1100
11.306
−10.543
−5.980
1.00
45.40
RNA1
C


ATOM
2587
O2*
C
C
1100
12.407
−11.390
−6.236
1.00
41.08
RNA1
O


ATOM
2588
C1*
C
C
1100
10.508
−10.293
−7.258
1.00
40.42
RNA1
C


ATOM
2589
N1
C
C
1100
9.968
−8.923
−7.239
1.00
34.22
RNA1
N


ATOM
2590
C2
C
C
1100
10.851
−7.860
−7.450
1.00
34.09
RNA1
C


ATOM
2591
O2
C
C
1100
12.043
−8.112
−7.698
1.00
30.44
RNA1
O


ATOM
2592
N3
C
C
1100
10.390
−6.595
−7.377
1.00
32.20
RNA1
N


ATOM
2593
C4
C
C
1100
9.102
−6.369
−7.112
1.00
36.06
RNA1
C


ATOM
2594
N4
C
C
1100
8.695
−5.101
−7.023
1.00
42.37
RNA1
N


ATOM
2595
C5
C
C
1100
8.173
−7.432
−6.920
1.00
31.00
RNA1
C


ATOM
2596
C6
C
C
1100
8.643
−8.681
−6.995
1.00
29.98
RNA1
C


ATOM
2597
P
U
C
1101
11.026
−11.199
−2.592
1.00
60.70
RNA1
P


ATOM
2598
O1P
U
C
1101
9.727
−10.588
−2.196
1.00
50.26
RNA1
O


ATOM
2599
O2P
U
C
1101
11.694
−12.160
−1.673
1.00
70.90
RNA1
O


ATOM
2600
O5*
U
C
1101
12.055
−10.024
−2.904
1.00
44.87
RNA1
O


ATOM
2601
C5*
U
C
1101
13.364
−10.316
−3.411
1.00
39.54
RNA1
C


ATOM
2602
C4*
U
C
1101
14.139
−9.041
−3.619
1.00
45.93
RNA1
C


ATOM
2603
O4*
U
C
1101
13.487
−8.234
−4.635
1.00
53.56
RNA1
O


ATOM
2604
C3*
U
C
1101
14.232
−8.111
−2.424
1.00
45.04
RNA1
C


ATOM
2605
O3*
U
C
1101
15.241
−8.491
−1.503
1.00
55.35
RNA1
O


ATOM
2606
C2*
U
C
1101
14.519
−6.767
−3.078
1.00
45.97
RNA1
C


ATOM
2607
O2*
U
C
1101
15.875
−6.620
−3.450
1.00
43.86
RNA1
O


ATOM
2608
C1*
U
C
1101
13.668
−6.856
−4.341
1.00
43.43
RNA1
C


ATOM
2609
N1
U
C
1101
12.349
−6.220
−4.172
1.00
40.87
RNA1
N


ATOM
2610
C2
U
C
1101
12.289
−4.831
−4.234
1.00
35.67
RNA1
C


ATOM
2611
O2
U
C
1101
13.277
−4.130
−4.420
1.00
34.43
RNA1
O


ATOM
2612
N3
U
C
1101
11.032
−4.294
−4.067
1.00
27.89
RNA1
N


ATOM
2613
C4
U
C
1101
9.851
−4.983
−3.852
1.00
38.34
RNA1
C


ATOM
2614
O4
U
C
1101
8.792
−4.355
−3.727
1.00
30.79
RNA1
O


ATOM
2615
C5
U
C
1101
9.993
−6.408
−3.801
1.00
38.67
RNA1
C


ATOM
2616
C6
U
C
1101
11.204
−6.965
−3.959
1.00
40.99
RNA1
C


ATOM
2617
P
C
C
1102
15.110
−8.040
0.038
1.00
56.93
RNA1
P


ATOM
2618
O1P
C
C
1102
13.690
−8.220
0.458
1.00
45.32
RNA1
O


ATOM
2619
O2P
C
C
1102
16.195
−8.697
0.810
1.00
59.07
RNA1
O


ATOM
2620
O5*
C
C
1102
15.415
−6.479
0.002
1.00
47.10
RNA1
O


ATOM
2621
C5*
C
C
1102
16.687
−6.002
−0.447
1.00
40.92
RNA1
C


ATOM
2622
C4*
C
C
1102
16.706
−4.495
−0.480
1.00
41.54
RNA1
C


ATOM
2623
O4*
C
C
1102
15.809
−4.001
−1.511
1.00
45.86
RNA1
O


ATOM
2624
C3*
C
C
1102
16.235
−3.772
0.769
1.00
43.22
RNA1
C


ATOM
2625
O3*
C
C
1102
17.189
−3.732
1.814
1.00
49.70
RNA1
O


ATOM
2626
C2*
C
C
1102
15.910
−2.389
0.227
1.00
45.44
RNA1
C


ATOM
2627
O2*
C
C
1102
17.061
−1.587
0.031
1.00
39.52
RNA1
O


ATOM
2628
C1*
C
C
1102
15.294
−2.733
−1.125
1.00
41.32
RNA1
C


ATOM
2629
N1
C
C
1102
13.822
−2.807
−1.006
1.00
35.07
RNA1
N


ATOM
2630
C2
C
C
1102
13.091
−1.607
−0.999
1.00
35.73
RNA1
C


ATOM
2631
O2
C
C
1102
13.700
−0.530
−1.134
1.00
40.70
RNA1
O


ATOM
2632
N3
C
C
1102
11.748
−1.649
−0.843
1.00
24.21
RNA1
N


ATOM
2633
C4
C
C
1102
11.131
−2.821
−0.703
1.00
25.56
RNA1
C


ATOM
2634
N4
C
C
1102
9.805
−2.813
−0.534
1.00
27.04
RNA1
N


ATOM
2635
C5
C
C
1102
11.844
−4.056
−0.726
1.00
25.22
RNA1
C


ATOM
2636
C6
C
C
1102
13.175
−4.004
−0.880
1.00
29.24
RNA1
C


ATOM
2637
P
A
C
1103
16.678
−3.598
3.336
1.00
46.37
RNA1
P


ATOM
2638
O1P
A
C
1103
15.453
−4.431
3.507
1.00
34.79
RNA1
O


ATOM
2639
O2P
A
C
1103
17.841
−3.806
4.238
1.00
53.23
RNA1
O


ATOM
2640
O5*
A
C
1103
16.223
−2.077
3.443
1.00
50.88
RNA1
O


ATOM
2641
C5*
A
C
1103
17.095
−1.012
3.017
1.00
45.92
RNA1
C


ATOM
2642
C4*
A
C
1103
16.368
0.307
3.082
1.00
42.03
RNA1
C


ATOM
2643
O4*
A
C
1103
15.249
0.282
2.164
1.00
42.45
RNA1
O


ATOM
2644
C3*
A
C
1103
15.748
0.629
4.431
1.00
46.34
RNA1
C


ATOM
2645
O3*
A
C
1103
16.697
1.231
5.297
1.00
50.61
RNA1
O


ATOM
2646
C2*
A
C
1103
14.604
1.568
4.068
1.00
40.60
RNA1
C


ATOM
2647
O2*
A
C
1103
15.018
2.911
3.913
1.00
43.99
RNA1
O


ATOM
2648
C1*
A
C
1103
14.163
1.007
2.714
1.00
35.23
RNA1
C


ATOM
2649
N9
A
C
1103
13.007
0.114
2.815
1.00
24.56
RNA1
N


ATOM
2650
C8
A
C
1103
12.964
−1.259
2.771
1.00
12.09
RNA1
C


ATOM
2651
N7
A
C
1103
11.755
−1.754
2.912
1.00
21.27
RNA1
N


ATOM
2652
C5
A
C
1103
10.949
−0.629
3.052
1.00
11.33
RNA1
C


ATOM
2653
C6
A
C
1103
9.566
−0.469
3.247
1.00
17.54
RNA1
C


ATOM
2654
N6
A
C
1103
8.699
−1.485
3.341
1.00
18.44
RNA1
N


ATOM
2655
N1
A
C
1103
9.091
0.792
3.351
1.00
23.77
RNA1
N


ATOM
2656
C2
A
C
1103
9.947
1.810
3.270
1.00
20.47
RNA1
C


ATOM
2657
N3
A
C
1103
11.262
1.789
3.093
1.00
25.40
RNA1
N


ATOM
2658
C4
A
C
1103
11.706
0.525
2.990
1.00
22.14
RNA1
C


ATOM
2659
P
C
C
1104
16.907
0.637
6.771
1.00
47.34
RNA1
P


ATOM
2660
O1P
C
C
1104
17.274
−0.801
6.656
1.00
47.39
RNA1
O


ATOM
2661
O2P
C
C
1104
17.809
1.572
7.493
1.00
49.59
RNA1
O


ATOM
2662
O5*
C
C
1104
15.454
0.717
7.410
1.00
32.80
RNA1
O


ATOM
2663
C5*
C
C
1104
14.847
1.985
7.660
1.00
32.89
RNA1
C


ATOM
2664
C4*
C
C
1104
13.409
1.804
8.055
1.00
33.67
RNA1
C


ATOM
2665
O4*
C
C
1104
12.654
1.301
6.924
1.00
36.61
RNA1
O


ATOM
2666
C3*
C
C
1104
13.151
0.793
9.157
1.00
44.60
RNA1
C


ATOM
2667
O3*
C
C
1104
13.379
1.321
10.455
1.00
47.83
RNA1
O


ATOM
2668
C2*
C
C
1104
11.699
0.409
8.912
1.00
41.50
RNA1
C


ATOM
2669
O2*
C
C
1104
10.802
1.363
9.443
1.00
39.51
RNA1
O


ATOM
2670
C1*
C
C
1104
11.635
0.426
7.382
1.00
35.38
RNA1
C


ATOM
2671
N1
C
C
1104
11.881
−0.915
6.818
1.00
26.79
RNA1
N


ATOM
2672
C2
C
C
1104
10.807
−1.804
6.699
1.00
30.49
RNA1
C


ATOM
2673
O2
C
C
1104
9.672
−1.426
7.039
1.00
25.17
RNA1
O


ATOM
2674
N3
C
C
1104
11.031
−3.049
6.216
1.00
35.06
RNA1
N


ATOM
2675
C4
C
C
1104
12.264
−3.412
5.850
1.00
35.48
RNA1
C


ATOM
2676
N4
C
C
1104
12.440
−4.649
5.381
1.00
39.73
RNA1
N


ATOM
2677
C5
C
C
1104
13.370
−2.524
5.948
1.00
26.28
RNA1
C


ATOM
2678
C6
C
C
1104
13.137
−1.298
6.432
1.00
26.38
RNA1
C


ATOM
2679
P
C
C
1105
13.943
0.357
11.610
1.00
45.15
RNA1
P


ATOM
2680
O1P
C
C
1105
14.937
−0.579
11.008
1.00
37.59
RNA1
O


ATOM
2681
O2P
C
C
1105
14.345
1.217
12.749
1.00
50.66
RNA1
O


ATOM
2682
O5*
C
C
1105
12.669
−0.496
12.036
1.00
27.84
RNA1
O


ATOM
2683
C5*
C
C
1105
11.541
0.141
12.636
1.00
26.44
RNA1
C


ATOM
2684
C4*
C
C
1105
10.431
−0.855
12.852
1.00
36.80
RNA1
C


ATOM
2685
O4*
C
C
1105
9.967
−1.354
11.569
1.00
46.02
RNA1
O


ATOM
2686
C3*
C
C
1105
10.793
−2.111
13.623
1.00
39.57
RNA1
C


ATOM
2687
O3*
C
C
1105
10.794
−1.905
15.026
1.00
48.60
RNA1
O


ATOM
2688
C2*
C
C
1105
9.713
−3.084
13.169
1.00
42.79
RNA1
C


ATOM
2689
O2*
C
C
1105
8.473
−2.848
13.811
1.00
36.52
RNA1
O


ATOM
2690
C1*
C
C
1105
9.576
−2.714
11.693
1.00
39.01
RNA1
C


ATOM
2691
N1
C
C
1105
10.448
−3.539
10.827
1.00
31.92
RNA1
N


ATOM
2692
C2
C
C
1105
10.029
−4.832
10.461
1.00
29.04
RNA1
C


ATOM
2693
O2
C
C
1105
8.934
−5.259
10.875
1.00
27.41
RNA1
O


ATOM
2694
N3
C
C
1105
10.831
−5.584
9.672
1.00
26.50
RNA1
N


ATOM
2695
C4
C
C
1105
12.005
−5.100
9.255
1.00
26.95
RNA1
C


ATOM
2696
N4
C
C
1105
12.768
−5.879
8.473
1.00
32.01
RNA1
N


ATOM
2697
C5
C
C
1105
12.453
−3.798
9.614
1.00
31.44
RNA1
C


ATOM
2698
C6
C
C
1105
11.652
−3.059
10.389
1.00
27.18
RNA1
C


ATOM
2699
P
A
C
1106
11.685
−2.860
15.964
1.00
49.11
RNA1
P


ATOM
2700
O1P
A
C
1106
12.987
−3.106
15.282
1.00
36.36
RNA1
O


ATOM
2701
O2P
A
C
1106
11.676
−2.277
17.331
1.00
55.01
RNA1
O


ATOM
2702
O5*
A
C
1106
10.861
−4.222
15.988
1.00
33.45
RNA1
O


ATOM
2703
C5*
A
C
1106
9.507
−4.255
16.482
1.00
40.30
RNA1
C


ATOM
2704
C4*
A
C
1106
8.910
−5.628
16.280
1.00
55.66
RNA1
C


ATOM
2705
O4*
A
C
1106
8.774
−5.892
14.859
1.00
57.89
RNA1
O


ATOM
2706
C3*
A
C
1106
9.747
−6.785
16.804
1.00
61.21
RNA1
C


ATOM
2707
O3*
A
C
1106
9.552
−7.004
18.196
1.00
63.93
RNA1
O


ATOM
2708
C2*
A
C
1106
9.287
−7.945
15.928
1.00
60.31
RNA1
C


ATOM
2709
O2*
A
C
1106
8.040
−8.478
16.344
1.00
54.72
RNA1
O


ATOM
2710
C1*
A
C
1106
9.104
−7.244
14.582
1.00
50.43
RNA1
C


ATOM
2711
N9
A
C
1106
10.327
−7.245
13.772
1.00
40.12
RNA1
N


ATOM
2712
C8
A
C
1106
11.297
−6.265
13.730
1.00
43.18
RNA1
C


ATOM
2713
N7
A
C
1106
12.279
−6.522
12.899
1.00
35.92
RNA1
N


ATOM
2714
C5
A
C
1106
11.940
−7.754
12.356
1.00
35.80
RNA1
C


ATOM
2715
C6
A
C
1106
12.574
−8.570
11.401
1.00
32.97
RNA1
C


ATOM
2716
N6
A
C
1106
13.721
−8.242
10.791
1.00
42.58
RNA1
N


ATOM
2717
N1
A
C
1106
11.984
−9.744
11.088
1.00
28.98
RNA1
N


ATOM
2718
C2
A
C
1106
10.831
−10.065
11.694
1.00
37.34
RNA1
C


ATOM
2719
N3
A
C
1106
10.132
−9.379
12.601
1.00
37.05
RNA1
N


ATOM
2720
C4
A
C
1106
10.746
−8.218
12.893
1.00
37.35
RNA1
C


ATOM
2721
P
G
C
1107
10.770
−7.554
19.093
1.00
58.93
RNA1
P


ATOM
2722
O1P
G
C
1107
12.057
−7.023
18.562
1.00
36.85
RNA1
O


ATOM
2723
O2P
G
C
1107
10.406
−7.307
20.512
1.00
61.45
RNA1
O


ATOM
2724
O5*
G
C
1107
10.741
−9.124
18.823
1.00
57.72
RNA1
O


ATOM
2725
C5*
G
C
1107
9.559
−9.898
19.117
1.00
58.74
RNA1
C


ATOM
2726
C4*
G
C
1107
9.678
−11.278
18.520
1.00
65.40
RNA1
C


ATOM
2727
O4*
G
C
1107
9.633
−11.183
17.073
1.00
61.43
RNA1
O


ATOM
2728
C3*
G
C
1107
10.983
−11.999
18.818
1.00
66.79
RNA1
C


ATOM
2729
O3*
G
C
1107
10.969
−12.653
20.079
1.00
66.96
RNA1
O


ATOM
2730
C2*
G
C
1107
11.110
−12.966
17.647
1.00
65.40
RNA1
C


ATOM
2731
O2*
G
C
1107
10.392
−14.174
17.833
1.00
59.25
RNA1
O


ATOM
2732
C1*
G
C
1107
10.509
−12.142
16.504
1.00
56.87
RNA1
C


ATOM
2733
N9
G
C
1107
11.541
−11.428
15.759
1.00
46.90
RNA1
N


ATOM
2734
C8
G
C
1107
11.980
−10.140
15.964
1.00
49.14
RNA1
C


ATOM
2735
N7
G
C
1107
12.952
−9.797
15.163
1.00
45.19
RNA1
N


ATOM
2736
C5
G
C
1107
13.159
−10.921
14.374
1.00
43.33
RNA1
C


ATOM
2737
C6
G
C
1107
14.092
−11.155
13.326
1.00
44.94
RNA1
C


ATOM
2738
O6
G
C
1107
14.953
−10.387
12.869
1.00
41.91
RNA1
O


ATOM
2739
N1
G
C
1107
13.958
−12.437
12.803
1.00
44.05
RNA1
N


ATOM
2740
C2
G
C
1107
13.048
−13.374
13.227
1.00
48.45
RNA1
C


ATOM
2741
N2
G
C
1107
13.071
−14.553
12.597
1.00
49.02
RNA1
N


ATOM
2742
N3
G
C
1107
12.177
−13.169
14.198
1.00
48.55
RNA1
N


ATOM
2743
C4
G
C
1107
12.289
−11.932
14.725
1.00
47.37
RNA1
C


ATOM
2744
P
C
C
1108
12.345
−12.840
20.886
1.00
71.15
RNA1
P


ATOM
2745
O1P
C
C
1108
13.100
−11.558
20.849
1.00
59.46
RNA1
O


ATOM
2746
O2P
C
C
1108
12.015
−13.463
22.194
1.00
75.00
RNA1
O


ATOM
2747
O5*
C
C
1108
13.155
−13.893
20.010
1.00
72.84
RNA1
O


ATOM
2748
C5*
C
C
1108
12.697
−15.251
19.876
1.00
75.04
RNA1
C


ATOM
2749
C4*
C
C
1108
13.581
−16.004
18.914
1.00
76.03
RNA1
C


ATOM
2750
O4*
C
C
1108
13.459
−15.420
17.592
1.00
73.82
RNA1
O


ATOM
2751
C3*
C
C
1108
15.073
−15.954
19.208
1.00
77.22
RNA1
C


ATOM
2752
O3*
C
C
1108
15.576
−16.622
20.377
1.00
76.14
RNA1
O


ATOM
2753
C2*
C
C
1108
15.696
−16.220
17.844
1.00
77.82
RNA1
C


ATOM
2754
O2*
C
C
1108
15.731
−17.593
17.507
1.00
80.53
RNA1
O


ATOM
2755
C1*
C
C
1108
14.705
−15.511
16.916
1.00
74.18
RNA1
C


ATOM
2756
N1
C
C
1108
15.147
−14.151
16.545
1.00
69.37
RNA1
N


ATOM
2757
C2
C
C
1108
15.946
−13.987
15.400
1.00
64.11
RNA1
C


ATOM
2758
O2
C
C
1108
16.232
−14.979
14.713
1.00
63.69
RNA1
O


ATOM
2759
N3
C
C
1108
16.383
−12.750
15.074
1.00
59.38
RNA1
N


ATOM
2760
C4
C
C
1108
16.047
−11.702
15.829
1.00
57.06
RNA1
C


ATOM
2761
N4
C
C
1108
16.508
−10.503
15.472
1.00
58.03
RNA1
N


ATOM
2762
C5
C
C
1108
15.224
−11.837
16.984
1.00
61.31
RNA1
C


ATOM
2763
C6
C
C
1108
14.801
−13.066
17.303
1.00
67.15
RNA1
C


TER
2764

C
C
1108


ATOM
2765
O5*
G
D
1051
13.368
11.108
−58.535
1.00
55.60
RNA2
O


ATOM
2766
C5*
G
D
1051
14.100
12.302
−58.210
1.00
63.32
RNA2
C


ATOM
2767
C4*
G
D
1051
13.550
13.505
−58.939
1.00
61.69
RNA2
C


ATOM
2768
O4*
G
D
1051
13.809
13.364
−60.359
1.00
66.02
RNA2
O


ATOM
2769
C3*
G
D
1051
12.043
13.659
−58.835
1.00
59.67
RNA2
C


ATOM
2770
O3*
G
D
1051
11.661
14.349
−57.659
1.00
53.26
RNA2
O


ATOM
2771
C2*
G
D
1051
11.684
14.404
−60.113
1.00
58.82
RNA2
C


ATOM
2772
O2*
G
D
1051
11.873
15.801
−60.015
1.00
62.26
RNA2
O


ATOM
2773
C1*
G
D
1051
12.691
13.815
−61.102
1.00
58.27
RNA2
C


ATOM
2774
N9
G
D
1051
12.147
12.672
−61.833
1.00
55.11
RNA2
N


ATOM
2775
C8
G
D
1051
12.505
11.352
−61.693
1.00
57.64
RNA2
C


ATOM
2776
N7
G
D
1051
11.830
10.552
−62.472
1.00
63.74
RNA2
N


ATOM
2777
C5
G
D
1051
10.976
11.393
−63.171
1.00
59.62
RNA2
C


ATOM
2778
C6
G
D
1051
10.002
11.100
−64.162
1.00
54.61
RNA2
C


ATOM
2779
O6
G
D
1051
9.687
9.999
−64.634
1.00
56.94
RNA2
O


ATOM
2780
N1
G
D
1051
9.366
12.254
−64.606
1.00
52.85
RNA2
N


ATOM
2781
C2
G
D
1051
9.629
13.525
−64.157
1.00
48.26
RNA2
C


ATOM
2782
N2
G
D
1051
8.910
14.509
−64.707
1.00
49.20
RNA2
N


ATOM
2783
N3
G
D
1051
10.531
13.811
−63.237
1.00
51.58
RNA2
N


ATOM
2784
C4
G
D
1051
11.163
12.707
−62.791
1.00
56.30
RNA2
C


ATOM
2785
P
C
D
1052
10.243
14.024
−56.983
1.00
59.48
RNA2
P


ATOM
2786
O1P
C
D
1052
10.050
12.549
−57.013
1.00
61.66
RNA2
O


ATOM
2787
O2P
C
D
1052
10.183
14.741
−55.688
1.00
73.92
RNA2
O


ATOM
2788
O5*
C
D
1052
9.194
14.690
−57.976
1.00
41.41
RNA2
O


ATOM
2789
C5*
C
D
1052
9.295
16.081
−58.307
1.00
47.28
RNA2
C


ATOM
2790
C4*
C
D
1052
8.298
16.442
−59.376
1.00
45.31
RNA2
C


ATOM
2791
O4*
C
D
1052
8.683
15.855
−60.645
1.00
50.63
RNA2
O


ATOM
2792
C3*
C
D
1052
6.892
15.933
−59.137
1.00
47.61
RNA2
C


ATOM
2793
O3*
C
D
1052
6.174
16.759
−58.247
1.00
56.07
RNA2
O


ATOM
2794
C2*
C
D
1052
6.301
15.896
−60.540
1.00
49.42
RNA2
C


ATOM
2795
O2*
C
D
1052
5.816
17.144
−60.990
1.00
40.34
RNA2
O


ATOM
2796
C1*
C
D
1052
7.518
15.487
−61.371
1.00
50.98
RNA2
C


ATOM
2797
N1
C
D
1052
7.546
14.031
−61.621
1.00
53.95
RNA2
N


ATOM
2798
C2
C
D
1052
6.704
13.502
−62.611
1.00
53.59
RNA2
C


ATOM
2799
O2
C
D
1052
5.974
14.271
−63.253
1.00
52.10
RNA2
O


ATOM
2800
N3
C
D
1052
6.705
12.169
−62.838
1.00
59.04
RNA2
N


ATOM
2801
C4
C
D
1052
7.499
11.370
−62.120
1.00
65.70
RNA2
C


ATOM
2802
N4
C
D
1052
7.459
10.056
−62.374
1.00
66.17
RNA2
N


ATOM
2803
C5
C
D
1052
8.369
11.880
−61.110
1.00
59.37
RNA2
C


ATOM
2804
C6
C
D
1052
8.363
13.202
−60.898
1.00
55.97
RNA2
C


ATOM
2805
P
U
D
1053
5.067
16.101
−57.298
1.00
63.43
RNA2
P


ATOM
2806
O1P
U
D
1053
5.641
14.831
−56.780
1.00
62.31
RNA2
O


ATOM
2807
O2P
U
D
1053
4.576
17.128
−56.343
1.00
74.13
RNA2
O


ATOM
2808
O5*
U
D
1053
3.889
15.763
−58.312
1.00
57.11
RNA2
O


ATOM
2809
C5*
U
D
1053
3.199
16.820
−58.990
1.00
48.12
RNA2
C


ATOM
2810
C4*
U
D
1053
2.185
16.257
−59.953
1.00
50.31
RNA2
C


ATOM
2811
O4*
U
D
1053
2.860
15.628
−61.074
1.00
49.75
RNA2
O


ATOM
2812
C3*
U
D
1053
1.277
15.164
−59.421
1.00
50.89
RNA2
C


ATOM
2813
O3*
U
D
1053
0.202
15.634
−58.629
1.00
56.33
RNA2
O


ATOM
2814
C2*
U
D
1053
0.818
14.477
−60.698
1.00
50.72
RNA2
C


ATOM
2815
O2*
U
D
1053
−0.225
15.175
−61.357
1.00
48.82
RNA2
O


ATOM
2816
C1*
U
D
1053
2.091
14.528
−61.540
1.00
43.49
RNA2
C


ATOM
2817
N1
U
D
1053
2.881
13.292
−61.391
1.00
42.34
RNA2
N


ATOM
2818
C2
U
D
1053
2.501
12.182
−62.141
1.00
40.65
RNA2
C


ATOM
2819
O2
U
D
1053
1.564
12.193
−62.926
1.00
43.48
RNA2
O


ATOM
2820
N3
U
D
1053
3.258
11.057
−61.935
1.00
32.60
RNA2
N


ATOM
2821
C4
U
D
1053
4.329
10.920
−61.079
1.00
48.03
RNA2
C


ATOM
2822
O4
U
D
1053
4.880
9.822
−60.973
1.00
58.30
RNA2
O


ATOM
2823
C5
U
D
1053
4.670
12.106
−60.352
1.00
43.77
RNA2
C


ATOM
2824
C6
U
D
1053
3.954
13.222
−60.528
1.00
44.26
RNA2
C


ATOM
2825
P
G
D
1054
−0.300
14.738
−57.393
1.00
63.07
RNA2
P


ATOM
2826
O1P
G
D
1054
0.909
14.253
−56.659
1.00
56.57
RNA2
O


ATOM
2827
O2P
G
D
1054
−1.342
15.504
−56.670
1.00
55.48
RNA2
O


ATOM
2828
O5*
G
D
1054
−0.993
13.484
−58.088
1.00
55.82
RNA2
O


ATOM
2829
C5*
G
D
1054
−2.203
13.659
−58.842
1.00
63.34
RNA2
C


ATOM
2830
C4*
G
D
1054
−2.607
12.376
−59.540
1.00
61.66
RNA2
C


ATOM
2831
O4*
G
D
1054
−1.612
11.993
−60.529
1.00
57.48
RNA2
O


ATOM
2832
C3*
G
D
1054
−2.785
11.116
−58.707
1.00
58.52
RNA2
C


ATOM
2833
O3*
G
D
1054
−4.027
11.063
−58.021
1.00
50.20
RNA2
O


ATOM
2834
C2*
G
D
1054
−2.702
10.021
−59.766
1.00
54.72
RNA2
C


ATOM
2835
O2*
G
D
1054
−3.915
9.849
−60.469
1.00
57.84
RNA2
O


ATOM
2836
C1*
G
D
1054
−1.657
10.588
−60.723
1.00
42.15
RNA2
C


ATOM
2837
N9
G
D
1054
−0.347
10.004
−60.453
1.00
43.98
RNA2
N


ATOM
2838
C8
G
D
1054
0.686
10.525
−59.707
1.00
48.29
RNA2
C


ATOM
2839
N7
G
D
1054
1.715
9.721
−59.624
1.00
48.90
RNA2
N


ATOM
2840
C5
G
D
1054
1.340
8.607
−60.367
1.00
43.87
RNA2
C


ATOM
2841
C6
G
D
1054
2.037
7.396
−60.634
1.00
37.83
RNA2
C


ATOM
2842
O6
G
D
1054
3.167
7.050
−60.252
1.00
35.95
RNA2
O


ATOM
2843
N1
G
D
1054
1.279
6.539
−61.428
1.00
42.56
RNA2
N


ATOM
2844
C2
G
D
1054
0.013
6.807
−61.901
1.00
45.28
RNA2
C


ATOM
2845
N2
G
D
1054
−0.567
5.854
−62.647
1.00
42.14
RNA2
N


ATOM
2846
N3
G
D
1054
−0.642
7.925
−61.659
1.00
40.97
RNA2
N


ATOM
2847
C4
G
D
1054
0.074
8.774
−60.892
1.00
45.06
RNA2
C


ATOM
2848
P
G
D
1055
−4.174
10.115
−56.729
1.00
60.11
RNA2
P


ATOM
2849
O1P
G
D
1055
−3.012
10.347
−55.817
1.00
52.31
RNA2
O


ATOM
2850
O2P
G
D
1055
−5.562
10.287
−56.226
1.00
45.31
RNA2
O


ATOM
2851
O5*
G
D
1055
−4.016
8.633
−57.297
1.00
61.25
RNA2
O


ATOM
2852
C5*
G
D
1055
−5.060
8.044
−58.084
1.00
49.39
RNA2
C


ATOM
2853
C4*
G
D
1055
−4.631
6.705
−58.643
1.00
46.06
RNA2
C


ATOM
2854
O4*
G
D
1055
−3.395
6.848
−59.392
1.00
46.04
RNA2
O


ATOM
2855
C3*
G
D
1055
−4.322
5.571
−57.678
1.00
46.58
RNA2
C


ATOM
2856
O3*
G
D
1055
−5.478
4.904
−57.197
1.00
44.61
RNA2
O


ATOM
2857
C2*
G
D
1055
−3.512
4.627
−58.556
1.00
50.61
RNA2
C


ATOM
2858
O2*
G
D
1055
−4.337
3.844
−59.397
1.00
57.17
RNA2
O


ATOM
2859
C1*
G
D
1055
−2.719
5.604
−59.419
1.00
37.93
RNA2
C


ATOM
2860
N9
G
D
1055
−1.364
5.764
−58.905
1.00
28.75
RNA2
N


ATOM
2861
C8
G
D
1055
−0.813
6.849
−58.266
1.00
28.74
RNA2
C


ATOM
2862
N7
G
D
1055
0.437
6.662
−57.928
1.00
31.82
RNA2
N


ATOM
2863
C5
G
D
1055
0.725
5.377
−58.371
1.00
24.53
RNA2
C


ATOM
2864
C6
G
D
1055
1.924
4.619
−58.293
1.00
28.90
RNA2
C


ATOM
2865
O6
G
D
1055
3.010
4.943
−57.807
1.00
32.85
RNA2
O


ATOM
2866
N1
G
D
1055
1.771
3.360
−58.862
1.00
26.15
RNA2
N


ATOM
2867
C2
G
D
1055
0.615
2.884
−59.432
1.00
32.58
RNA2
C


ATOM
2868
N2
G
D
1055
0.658
1.635
−59.922
1.00
28.69
RNA2
N


ATOM
2869
N3
G
D
1055
−0.505
3.580
−59.514
1.00
26.67
RNA2
N


ATOM
2870
C4
G
D
1055
−0.377
4.809
−58.971
1.00
28.85
RNA2
C


ATOM
2871
P
G
D
1056
−5.427
4.178
−55.764
1.00
41.37
RNA2
P


ATOM
2872
O1P
G
D
1056
−5.088
5.212
−54.752
1.00
49.91
RNA2
O


ATOM
2873
O2P
G
D
1056
−6.660
3.370
−55.603
1.00
41.24
RNA2
O


ATOM
2874
O5*
G
D
1056
−4.173
3.205
−55.857
1.00
31.72
RNA2
O


ATOM
2875
C5*
G
D
1056
−4.288
1.915
−56.458
1.00
26.06
RNA2
C


ATOM
2876
C4*
G
D
1056
−2.992
1.163
−56.310
1.00
30.23
RNA2
C


ATOM
2877
O4*
G
D
1056
−1.926
1.929
−56.923
1.00
33.12
RNA2
O


ATOM
2878
C3*
G
D
1056
−2.520
0.944
−54.886
1.00
25.25
RNA2
C


ATOM
2879
O3*
G
D
1056
−3.091
−0.214
−54.323
1.00
32.82
RNA2
O


ATOM
2880
C2*
G
D
1056
−1.015
0.792
−55.044
1.00
30.19
RNA2
C


ATOM
2881
O2*
G
D
1056
−0.631
−0.515
−55.418
1.00
28.72
RNA2
O


ATOM
2882
C1*
G
D
1056
−0.728
1.769
−56.181
1.00
29.85
RNA2
C


ATOM
2883
N9
G
D
1056
−0.326
3.081
−55.682
1.00
33.20
RNA2
N


ATOM
2884
C8
G
D
1056
−1.142
4.165
−55.453
1.00
31.51
RNA2
C


ATOM
2885
N7
G
D
1056
−0.496
5.205
−55.003
1.00
40.50
RNA2
N


ATOM
2886
C5
G
D
1056
0.825
4.784
−54.926
1.00
37.25
RNA2
C


ATOM
2887
C6
G
D
1056
1.985
5.481
−54.505
1.00
45.50
RNA2
C


ATOM
2888
O6
G
D
1056
2.078
6.654
−54.106
1.00
54.00
RNA2
O


ATOM
2889
N1
G
D
1056
3.122
4.677
−54.584
1.00
42.27
RNA2
N


ATOM
2890
C2
G
D
1056
3.138
3.372
−55.020
1.00
38.28
RNA2
C


ATOM
2891
N2
G
D
1056
4.337
2.765
−55.040
1.00
33.41
RNA2
N


ATOM
2892
N3
G
D
1056
2.060
2.712
−55.413
1.00
35.91
RNA2
N


ATOM
2893
C4
G
D
1056
0.947
3.474
−55.341
1.00
31.74
RNA2
C


ATOM
2894
P
A
D
1057
−3.445
−0.241
−52.765
1.00
34.80
RNA2
P


ATOM
2895
O1P
A
D
1057
−2.899
−1.503
−52.213
1.00
40.31
RNA2
O


ATOM
2896
O2P
A
D
1057
−3.058
1.055
−52.152
1.00
39.35
RNA2
O


ATOM
2897
O5*
A
D
1057
−5.027
−0.331
−52.754
1.00
19.58
RNA2
O


ATOM
2898
C5*
A
D
1057
−5.823
0.724
−53.304
1.00
24.68
RNA2
C


ATOM
2899
C4*
A
D
1057
−6.915
0.144
−54.161
1.00
26.68
RNA2
C


ATOM
2900
O4*
A
D
1057
−6.359
−0.301
−55.425
1.00
40.11
RNA2
O


ATOM
2901
C3*
A
D
1057
−7.560
−1.100
−53.585
1.00
30.27
RNA2
C


ATOM
2902
O3*
A
D
1057
−8.559
−0.816
−52.635
1.00
35.52
RNA2
O


ATOM
2903
C2*
A
D
1057
−8.090
−1.811
−54.820
1.00
30.75
RNA2
C


ATOM
2904
O2*
A
D
1057
−9.317
−1.270
−55.268
1.00
24.78
RNA2
O


ATOM
2905
C1*
A
D
1057
−6.991
−1.506
−55.834
1.00
16.37
RNA2
C


ATOM
2906
N9
A
D
1057
−5.973
−2.559
−55.883
1.00
21.50
RNA2
N


ATOM
2907
C8
A
D
1057
−4.626
−2.445
−55.613
1.00
18.28
RNA2
C


ATOM
2908
N7
A
D
1057
−3.962
−3.566
−55.754
1.00
23.67
RNA2
N


ATOM
2909
C5
A
D
1057
−4.935
−4.484
−56.140
1.00
21.49
RNA2
C


ATOM
2910
C6
A
D
1057
−4.872
−5.852
−56.447
1.00
17.73
RNA2
C


ATOM
2911
N6
A
D
1057
−3.748
−6.569
−56.412
1.00
22.33
RNA2
N


ATOM
2912
N1
A
D
1057
−6.019
−6.470
−56.797
1.00
29.29
RNA2
N


ATOM
2913
C2
A
D
1057
−7.150
−5.753
−56.829
1.00
30.01
RNA2
C


ATOM
2914
N3
A
D
1057
−7.337
−4.465
−56.559
1.00
24.69
RNA2
N


ATOM
2915
C4
A
D
1057
−6.177
−3.879
−56.219
1.00
18.45
RNA2
C


ATOM
2916
P
U
D
1058
−8.746
−1.807
−51.399
1.00
30.93
RNA2
P


ATOM
2917
O1P
U
D
1058
−7.361
−2.213
−50.993
1.00
24.94
RNA2
O


ATOM
2918
O2P
U
D
1058
−9.669
−1.203
−50.402
1.00
29.08
RNA2
O


ATOM
2919
O5*
U
D
1058
−9.464
−3.068
−52.042
1.00
30.31
RNA2
O


ATOM
2920
C5*
U
D
1058
−10.859
−3.043
−52.331
1.00
28.81
RNA2
C


ATOM
2921
C4*
U
D
1058
−11.349
−4.440
−52.592
1.00
31.83
RNA2
C


ATOM
2922
O4*
U
D
1058
−10.668
−4.953
−53.765
1.00
33.24
RNA2
O


ATOM
2923
C3*
U
D
1058
−11.031
−5.471
−51.520
1.00
33.13
RNA2
C


ATOM
2924
O3*
U
D
1058
−11.925
−5.479
−50.425
1.00
32.98
RNA2
O


ATOM
2925
C2*
U
D
1058
−11.084
−6.772
−52.299
1.00
29.12
RNA2
C


ATOM
2926
O2*
U
D
1058
−12.414
−7.204
−52.513
1.00
29.74
RNA2
O


ATOM
2927
C1*
U
D
1058
−10.455
−6.348
−53.622
1.00
26.32
RNA2
C


ATOM
2928
N1
U
D
1058
−9.008
−6.614
−53.638
1.00
21.34
RNA2
N


ATOM
2929
C2
U
D
1058
−8.608
−7.932
−53.803
1.00
24.87
RNA2
C


ATOM
2930
O2
U
D
1058
−9.402
−8.853
−53.938
1.00
31.94
RNA2
O


ATOM
2931
N3
U
D
1058
−7.253
−8.136
−53.799
1.00
8.92
RNA2
N


ATOM
2932
C4
U
D
1058
−6.273
−7.188
−53.647
1.00
22.44
RNA2
C


ATOM
2933
O4
U
D
1058
−5.088
−7.533
−53.685
1.00
18.08
RNA2
O


ATOM
2934
C5
U
D
1058
−6.759
−5.848
−53.482
1.00
22.73
RNA2
C


ATOM
2935
C6
U
D
1058
−8.080
−5.614
−53.488
1.00
18.95
RNA2
C


ATOM
2936
P
G
D
1059
−11.432
−6.089
−49.022
1.00
29.43
RNA2
P


ATOM
2937
O1P
G
D
1059
−9.995
−5.757
−48.812
1.00
18.78
RNA2
O


ATOM
2938
O2P
G
D
1059
−12.431
−5.724
−47.993
1.00
38.92
RNA2
O


ATOM
2939
O5*
G
D
1059
−11.490
−7.659
−49.247
1.00
34.42
RNA2
O


ATOM
2940
C5*
G
D
1059
−12.729
−8.312
−49.534
1.00
29.33
RNA2
C


ATOM
2941
C4*
G
D
1059
−12.525
−9.801
−49.573
1.00
27.67
RNA2
C


ATOM
2942
O4*
G
D
1059
−11.608
−10.126
−50.645
1.00
28.30
RNA2
O


ATOM
2943
C3*
G
D
1059
−11.883
−10.411
−48.339
1.00
32.02
RNA2
C


ATOM
2944
O3*
G
D
1059
−12.840
−10.666
−47.314
1.00
37.54
RNA2
O


ATOM
2945
C2*
G
D
1059
−11.260
−11.691
−48.887
1.00
27.34
RNA2
C


ATOM
2946
O2*
G
D
1059
−12.207
−12.736
−48.993
1.00
21.26
RNA2
O


ATOM
2947
C1*
G
D
1059
−10.838
−11.258
−50.289
1.00
18.26
RNA2
C


ATOM
2948
N9
G
D
1059
−9.425
−10.920
−50.414
1.00
11.76
RNA2
N


ATOM
2949
C8
G
D
1059
−8.846
−9.686
−50.262
1.00
10.37
RNA2
C


ATOM
2950
N7
G
D
1059
−7.552
−9.700
−50.455
1.00
15.12
RNA2
N


ATOM
2951
C5
G
D
1059
−7.260
−11.026
−50.747
1.00
5.51
RNA2
C


ATOM
2952
C6
G
D
1059
−6.022
−11.652
−51.055
1.00
15.78
RNA2
C


ATOM
2953
O6
G
D
1059
−4.892
−11.145
−51.124
1.00
17.40
RNA2
O


ATOM
2954
N1
G
D
1059
−6.184
−13.009
−51.300
1.00
12.54
RNA2
N


ATOM
2955
C2
G
D
1059
−7.377
−13.685
−51.256
1.00
23.87
RNA2
C


ATOM
2956
N2
G
D
1059
−7.326
−14.997
−51.540
1.00
21.07
RNA2
N


ATOM
2957
N3
G
D
1059
−8.536
−13.119
−50.962
1.00
20.56
RNA2
N


ATOM
2958
C4
G
D
1059
−8.404
−11.794
−50.723
1.00
17.53
RNA2
C


ATOM
2959
P
U
D
1060
−12.363
−10.713
−45.780
1.00
31.30
RNA2
P


ATOM
2960
O1P
U
D
1060
−13.473
−10.167
−44.963
1.00
29.83
RNA2
O


ATOM
2961
O2P
U
D
1060
−11.840
−12.074
−45.484
1.00
37.29
RNA2
O


ATOM
2962
O5*
U
D
1060
−11.129
−9.708
−45.745
1.00
25.29
RNA2
O


ATOM
2963
C5*
U
D
1060
−10.735
−9.064
−44.527
1.00
22.54
RNA2
C


ATOM
2964
C4*
U
D
1060
−9.378
−−8.435
−44.692
1.00
22.65
RNA2
C


ATOM
2965
O4*
U
D
1060
−8.401
−9.481
−44.882
1.00
24.56
RNA2
O


ATOM
2966
C3*
U
D
1060
−9.238
−7.481
−45.870
1.00
26.03
RNA2
C


ATOM
2967
O3*
U
D
1060
−8.303
−6.454
−45.522
1.00
41.53
RNA2
O


ATOM
2968
C2*
U
D
1060
−8.608
−8.361
−46.946
1.00
31.11
RNA2
C


ATOM
2969
O2*
U
D
1060
−7.808
−7.616
−47.841
1.00
45.38
RNA2
O


ATOM
2970
C1*
U
D
1060
−7.735
−9.299
−46.110
1.00
26.61
RNA2
C


ATOM
2971
N1
U
D
1060
−7.519
−10.632
−46.690
1.00
21.85
RNA2
N


ATOM
2972
C2
U
D
1060
−6.291
−10.898
−47.261
1.00
23.55
RNA2
C


ATOM
2973
O2
U
D
1060
−5.402
−10.063
−47.355
1.00
21.48
RNA2
O


ATOM
2974
N3
U
D
1060
−6.141
−12.182
−47.726
1.00
25.97
RNA2
N


ATOM
2975
C4
U
D
1060
−7.076
−13.199
−47.691
1.00
28.32
RNA2
C


ATOM
2976
O4
U
D
1060
−6.778
−14.311
−48.139
1.00
27.53
RNA2
O


ATOM
2977
C5
U
D
1060
−8.329
−12.837
−47.107
1.00
18.41
RNA2
C


ATOM
2978
C6
U
D
1060
−8.507
−11.600
−46.642
1.00
21.87
RNA2
C


ATOM
2979
P
U
D
1061
−8.630
−5.419
−44.325
1.00
28.91
RNA2
P


ATOM
2980
O1P
U
D
1061
−8.173
−4.091
−44.810
1.00
33.68
RNA2
O


ATOM
2981
O2P
U
D
1061
−10.037
−5.590
−43.863
1.00
15.62
RNA2
O


ATOM
2982
O5*
U
D
1061
−7.649
−5.888
−43.161
1.00
19.70
RNA2
O


ATOM
2983
C5*
U
D
1061
−6.225
−5.745
−43.301
1.00
18.21
RNA2
C


ATOM
2984
C4*
U
D
1061
−5.514
−6.526
−42.225
1.00
27.99
RNA2
C


ATOM
2985
O4*
U
D
1061
−5.894
−5.996
−40.927
1.00
36.85
RNA2
O


ATOM
2986
C3*
U
D
1061
−5.800
−8.028
−42.181
1.00
29.80
RNA2
C


ATOM
2987
O3*
U
D
1061
−4.608
−8.696
−41.772
1.00
33.59
RNA2
O


ATOM
2988
C2*
U
D
1061
−6.812
−8.151
−41.043
1.00
33.22
RNA2
C


ATOM
2989
O2*
U
D
1061
−6.748
−9.417
−40.415
1.00
27.78
RNA2
O


ATOM
2990
C1*
U
D
1061
−6.313
−7.055
−40.102
1.00
42.74
RNA2
C


ATOM
2991
N1
U
D
1061
−7.205
−6.543
−39.046
1.00
44.96
RNA2
N


ATOM
2992
C2
U
D
1061
−6.737
−6.649
−37.742
1.00
53.51
RNA2
C


ATOM
2993
O2
U
D
1061
−5.650
−7.143
−37.464
1.00
44.65
RNA2
O


ATOM
2994
N3
U
D
1061
−7.579
−6.157
−36.776
1.00
60.76
RNA2
N


ATOM
2995
C4
U
D
1061
−8.811
−5.585
−36.961
1.00
51.80
RNA2
C


ATOM
2996
O4
U
D
1061
−9.435
−5.195
−35.977
1.00
48.61
RNA2
O


ATOM
2997
C5
U
D
1061
−9.240
−5.508
−38.333
1.00
40.80
RNA2
C


ATOM
2998
C6
U
D
1061
−8.440
−5.979
−39.307
1.00
43.37
RNA2
C


ATOM
2999
P
G
D
1062
−3.700
−9.466
−42.848
1.00
33.56
RNA2
P


ATOM
3000
O1P
G
D
1062
−3.835
−8.777
−44.158
1.00
35.31
RNA2
O


ATOM
3001
O2P
G
D
1062
−2.353
−9.644
−42.252
1.00
21.04
RNA2
O


ATOM
3002
O5*
G
D
1062
−4.367
−10.905
−42.956
1.00
30.74
RNA2
O


ATOM
3003
C5*
G
D
1062
−5.563
−11.128
−43.737
1.00
36.95
RNA2
C


ATOM
3004
C4*
G
D
1062
−5.583
−12.554
−44.235
1.00
30.45
RNA2
C


ATOM
3005
O4*
G
D
1062
−4.531
−12.739
−45.222
1.00
26.47
RNA2
O


ATOM
3006
C3*
G
D
1062
−5.264
−13.550
−43.139
1.00
20.89
RNA2
C


ATOM
3007
O3*
G
D
1062
−6.428
−13.905
−42.431
1.00
31.67
RNA2
O


ATOM
3008
C2*
G
D
1062
−4.625
−14.707
−43.894
1.00
23.56
RNA2
C


ATOM
3009
O2*
G
D
1062
−5.589
−15.567
−44.466
1.00
18.76
RNA2
O


ATOM
3010
C1*
G
D
1062
−3.854
−13.963
−44.988
1.00
16.90
RNA2
C


ATOM
3011
N9
G
D
1062
−2.473
−13.642
−44.620
1.00
13.03
RNA2
N


ATOM
3012
C8
G
D
1062
−1.919
−12.387
−44.523
1.00
19.49
RNA2
C


ATOM
3013
N7
G
D
1062
−0.660
−12.404
−44.173
1.00
13.70
RNA2
N


ATOM
3014
C5
G
D
1062
−0.362
−13.749
−44.024
1.00
14.04
RNA2
C


ATOM
3015
C6
G
D
1062
0.850
−14.379
−43.651
1.00
24.18
RNA2
C


ATOM
3016
O6
G
D
1062
1.933
−13.852
−43.356
1.00
29.04
RNA2
O


ATOM
3017
N1
G
D
1062
0.723
−15.765
−43.634
1.00
22.87
RNA2
N


ATOM
3018
C2
G
D
1062
−0.427
−16.456
−43.927
1.00
30.15
RNA2
C


ATOM
3019
N2
G
D
1062
−0.349
−17.795
−43.849
1.00
24.93
RNA2
N


ATOM
3020
N3
G
D
1062
−1.570
−15.878
−44.269
1.00
30.88
RNA2
N


ATOM
3021
C4
G
D
1062
−1.466
−14.531
−44.300
1.00
16.88
RNA2
C


ATOM
3022
P
G
D
1063
−6.322
−14.242
−40.874
1.00
28.41
RNA2
P


ATOM
3023
O1P
G
D
1063
−5.463
−13.199
−40.266
1.00
27.32
RNA2
O


ATOM
3024
O2P
G
D
1063
−7.701
−14.468
−40.367
1.00
29.73
RNA2
O


ATOM
3025
O5*
G
D
1063
−5.523
−15.617
−40.821
1.00
30.17
RNA2
O


ATOM
3026
C5*
G
D
1063
−6.184
−16.864
−41.087
1.00
24.95
RNA2
C


ATOM
3027
C4*
G
D
1063
−5.241
−18.011
−40.832
1.00
20.87
RNA2
C


ATOM
3028
O4*
G
D
1063
−4.075
−17.850
−41.677
1.00
27.19
RNA2
O


ATOM
3029
C3*
G
D
1063
−4.659
−18.092
−39.434
1.00
26.89
RNA2
C


ATOM
3030
O3*
G
D
1063
−5.539
−18.706
−38.508
1.00
40.50
RNA2
O


ATOM
3031
C2*
G
D
1063
−3.373
−18.869
−39.659
1.00
23.40
RNA2
C


ATOM
3032
O2*
G
D
1063
−3.601
−20.256
−39.810
1.00
29.18
RNA2
O


ATOM
3033
C1*
G
D
1063
−2.919
−18.297
−40.994
1.00
21.30
RNA2
C


ATOM
3034
N9
G
D
1063
−2.022
−17.158
−40.820
1.00
18.48
RNA2
N


ATOM
3035
C8
G
D
1063
−2.309
−15.827
−41.016
1.00
13.94
RNA2
C


ATOM
3036
N7
G
D
1063
−1.283
−15.044
−40.798
1.00
19.66
RNA2
N


ATOM
3037
C5
G
D
1063
−0.260
−15.909
−40.428
1.00
17.05
RNA2
C


ATOM
3038
C6
G
D
1063
1.093
−15.646
−40.066
1.00
24.81
RNA2
C


ATOM
3039
O6
G
D
1063
1.680
−14.559
−39.999
1.00
27.63
RNA2
O


ATOM
3040
N1
G
D
1063
1.776
−16.819
−39.756
1.00
29.06
RNA2
N


ATOM
3041
C2
G
D
1063
1.234
−18.080
−39.781
1.00
24.76
RNA2
C


ATOM
3042
N2
G
D
1063
2.051
−19.081
−39.433
1.00
26.32
RNA2
N


ATOM
3043
N3
G
D
1063
−0.018
−18.340
−40.119
1.00
25.89
RNA2
N


ATOM
3044
C4
G
D
1063
−0.702
−17.217
−40.429
1.00
24.85
RNA2
C


ATOM
3045
P
C
D
1064
−5.606
−18.145
−37.003
1.00
33.12
RNA2
P


ATOM
3046
O1P
C
D
1064
−5.740
−16.669
−37.090
1.00
33.72
RNA2
O


ATOM
3047
O2P
C
D
1064
−6.628
−18.934
−36.261
1.00
34.10
RNA2
O


ATOM
3048
O5*
C
D
1064
−4.159
−18.476
−36.424
1.00
27.13
RNA2
O


ATOM
3049
C5*
C
D
1064
−3.695
−19.826
−36.395
1.00
16.79
RNA2
C


ATOM
3050
C4*
C
D
1064
−2.235
−19.884
−36.032
1.00
25.70
RNA2
C


ATOM
3051
O4*
C
D
1064
−1.436
−19.190
−37.022
1.00
29.89
RNA2
O


ATOM
3052
C3*
C
D
1064
−1.813
−19.250
−34.720
1.00
29.70
RNA2
C


ATOM
3053
O3*
C
D
1064
−2.095
−20.085
−33.611
1.00
37.04
RNA2
O


ATOM
3054
C2*
C
D
1064
−0.315
−19.047
−34.923
1.00
30.06
RNA2
C


ATOM
3055
O2*
C
D
1064
0.445
−20.216
−34.696
1.00
28.38
RNA2
O


ATOM
3056
C1*
C
D
1064
−0.251
−18.704
−36.409
1.00
30.33
RNA2
C


ATOM
3057
N1
C
D
1064
−0.140
−17.251
−36.627
1.00
20.71
RNA2
N


ATOM
3058
C2
C
D
1064
1.114
−16.655
−36.474
1.00
24.44
RNA2
C


ATOM
3059
O2
C
D
1064
2.086
−17.365
−36.175
1.00
30.49
RNA2
O


ATOM
3060
N3
C
D
1064
1.237
−15.325
−36.654
1.00
26.69
RNA2
N


ATOM
3061
C4
C
D
1064
0.170
−14.591
−36.976
1.00
20.50
RNA2
C


ATOM
3062
N4
C
D
1064
0.347
−13.279
−37.141
1.00
22.60
RNA2
N


ATOM
3063
C5
C
D
1064
−1.120
−15.169
−37.143
1.00
10.11
RNA2
C


ATOM
3064
C6
C
D
1064
−1.229
−16.492
−36.962
1.00
23.85
RNA2
C


ATOM
3065
P
U
D
1065
−2.513
−19.420
−32.214
1.00
35.56
RNA2
P


ATOM
3066
O1P
U
D
1065
−3.615
−18.460
−32.467
1.00
26.06
RNA2
O


ATOM
3067
O2P
U
D
1065
−2.716
−20.527
−31.248
1.00
43.50
RNA2
O


ATOM
3068
O5*
U
D
1065
−1.209
−18.600
−31.807
1.00
27.70
RNA2
O


ATOM
3069
C5*
U
D
1065
0.044
−19.282
−31.609
1.00
30.92
RNA2
C


ATOM
3070
C4*
U
D
1065
1.168
−18.287
−31.469
1.00
30.67
RNA2
C


ATOM
3071
O4*
U
D
1065
1.332
−17.559
−32.713
1.00
39.57
RNA2
O


ATOM
3072
C3*
U
D
1065
0.951
−17.209
−30.423
1.00
36.18
RNA2
C


ATOM
3073
O3*
U
D
1065
1.285
−17.667
−29.123
1.00
36.24
RNA2
O


ATOM
3074
C2*
U
D
1065
1.843
−16.076
−30.921
1.00
38.21
RNA2
C


ATOM
3075
O2*
U
D
1065
3.207
−16.224
−30.578
1.00
34.14
RNA2
O


ATOM
3076
C1*
U
D
1065
1.692
−16.216
−32.437
1.00
34.96
RNA2
C


ATOM
3077
N1
U
D
1065
0.645
−15.327
−32.968
1.00
22.93
RNA2
N


ATOM
3078
C2
U
D
1065
1.028
−14.066
−33.377
1.00
24.04
RNA2
C


ATOM
3079
O2
U
D
1065
2.187
−13.674
−33.325
1.00
20.47
RNA2
O


ATOM
3080
N3
U
D
1065
0.008
−13.276
−33.849
1.00
17.91
RNA2
N


ATOM
3081
C4
U
D
1065
−1.325
−13.612
−33.954
1.00
25.02
RNA2
C


ATOM
3082
O4
U
D
1065
−2.125
−12.793
−34.424
1.00
30.88
RNA2
O


ATOM
3083
C5
U
D
1065
−1.640
−14.934
−33.511
1.00
26.71
RNA2
C


ATOM
3084
C6
U
D
1065
−0.670
−15.727
−33.046
1.00
28.23
RNA2
C


ATOM
3085
P
U
D
1066
0.342
−17.279
−27.876
1.00
35.54
RNA2
P


ATOM
3086
O1P
U
D
1066
−1.089
−17.498
−28.212
1.00
19.51
RNA2
O


ATOM
3087
O2P
U
D
1066
0.927
−17.960
−26.692
1.00
43.24
RNA2
O


ATOM
3088
O5*
U
D
1066
0.552
−15.708
−27.728
1.00
32.79
RNA2
O


ATOM
3089
C5*
U
D
1066
1.867
−15.163
−27.509
1.00
39.57
RNA2
C


ATOM
3090
C4*
U
D
1066
1.853
−13.664
−27.695
1.00
41.26
RNA2
C


ATOM
3091
O4*
U
D
1066
1.606
−13.339
−29.088
1.00
50.01
RNA2
O


ATOM
3092
C3*
U
D
1066
0.773
−12.909
−26.935
1.00
46.81
RNA2
C


ATOM
3093
O3*
U
D
1066
1.137
−12.653
−25.587
1.00
47.16
RNA2
O


ATOM
3094
C2*
U
D
1066
0.645
−11.626
−27.743
1.00
45.38
RNA2
C


ATOM
3095
O2*
U
D
1066
1.671
−10.702
−27.422
1.00
47.24
RNA2
O


ATOM
3096
C1*
U
D
1066
0.848
−12.142
−29.168
1.00
44.66
RNA2
C


ATOM
3097
N1
U
D
1066
−0.437
−12.423
−29.835
1.00
36.02
RNA2
N


ATOM
3098
C2
U
D
1066
−1.001
−11.401
−30.583
1.00
31.01
RNA2
C


ATOM
3099
O2
U
D
1066
−0.450
−10.325
−30.752
1.00
24.12
RNA2
O


ATOM
3100
N3
U
D
1066
−2.231
−11.687
−31.131
1.00
26.04
RNA2
N


ATOM
3101
C4
U
D
1066
−2.939
−12.872
−31.028
1.00
32.10
RNA2
C


ATOM
3102
O4
U
D
1066
−4.082
−12.941
−31.501
1.00
32.26
RNA2
O


ATOM
3103
C5
U
D
1066
−2.276
−13.895
−30.271
1.00
27.27
RNA2
C


ATOM
3104
C6
U
D
1066
−1.080
−13.644
−29.712
1.00
35.51
RNA2
C


ATOM
3105
P
A
D
1067
0.011
−12.695
−24.442
1.00
41.56
RNA2
P


ATOM
3106
O1P
A
D
1067
−0.869
−13.868
−24.667
1.00
35.90
RNA2
O


ATOM
3107
O2P
A
D
1067
0.710
−12.532
−23.138
1.00
61.37
RNA2
O


ATOM
3108
O5*
A
D
1067
−0.877
−11.403
−24.702
1.00
37.80
RNA2
O


ATOM
3109
C5*
A
D
1067
−2.175
−11.275
−24.099
1.00
33.78
RNA2
C


ATOM
3110
C4*
A
D
1067
−2.689
−9.870
−24.284
1.00
40.27
RNA2
C


ATOM
3111
O4*
A
D
1067
−1.791
−8.952
−23.617
1.00
40.68
RNA2
O


ATOM
3112
C3*
A
D
1067
−2.714
−9.402
−25.727
1.00
40.11
RNA2
C


ATOM
3113
O3*
A
D
1067
−3.918
−9.794
−26.362
1.00
46.79
RNA2
O


ATOM
3114
C2*
A
D
1067
−2.560
−7.892
−25.606
1.00
33.18
RNA2
C


ATOM
3115
O2*
A
D
1067
−3.785
−7.245
−25.315
1.00
34.55
RNA2
O


ATOM
3116
C1*
A
D
1067
−1.637
−7.782
−24.394
1.00
30.38
RNA2
C


ATOM
3117
N9
A
D
1067
−0.216
−7.636
−24.699
1.00
18.52
RNA2
N


ATOM
3118
C8
A
D
1067
0.791
−8.539
−24.462
1.00
19.03
RNA2
C


ATOM
3119
N7
A
D
1067
1.987
−8.090
−24.769
1.00
23.17
RNA2
N


ATOM
3120
C5
A
D
1067
1.748
−6.814
−25.262
1.00
12.64
RNA2
C


ATOM
3121
C6
A
D
1067
2.605
−5.811
−25.748
1.00
16.33
RNA2
C


ATOM
3122
N6
A
D
1067
3.934
−5.945
−25.831
1.00
21.10
RNA2
N


ATOM
3123
N1
A
D
1067
2.046
−4.651
−26.154
1.00
17.93
RNA2
N


ATOM
3124
C2
A
D
1067
0.714
−4.518
−26.077
1.00
24.51
RNA2
C


ATOM
3125
N3
A
D
1067
−0.197
−5.388
−25.642
1.00
23.41
RNA2
N


ATOM
3126
C4
A
D
1067
0.393
−6.528
−25.240
1.00
22.32
RNA2
C


ATOM
3127
P
G
D
1068
−3.863
−10.352
−27.861
1.00
37.45
RNA2
P


ATOM
3128
O1P
G
D
1068
−2.775
−11.365
−27.915
1.00
32.87
RNA2
O


ATOM
3129
O2P
G
D
1068
−5.247
−10.719
−28.265
1.00
30.61
RNA2
O


ATOM
3130
O5*
G
D
1068
−3.399
−9.084
−28.697
1.00
34.59
RNA2
O


ATOM
3131
C5*
G
D
1068
−4.254
−7.938
−28.794
1.00
32.91
RNA2
C


ATOM
3132
C4*
G
D
1068
−3.550
−6.828
−29.521
1.00
39.65
RNA2
C


ATOM
3133
O4*
G
D
1068
−2.460
−6.334
−28.708
1.00
34.36
RNA2
O


ATOM
3134
C3*
G
D
1068
−2.908
−7.218
−30.840
1.00
41.96
RNA2
C


ATOM
3135
O3*
G
D
1068
−3.874
−7.194
−31.893
1.00
38.73
RNA2
O


ATOM
3136
C2*
G
D
1068
−1.811
−6.168
−30.989
1.00
37.55
RNA2
C


ATOM
3137
O2*
G
D
1068
−2.315
−4.944
−31.487
1.00
54.39
RNA2
O


ATOM
3138
C1*
G
D
1068
−1.382
−5.951
−29.535
1.00
22.83
RNA2
C


ATOM
3139
N9
G
D
1068
−0.226
−6.739
−29.134
1.00
20.42
RNA2
N


ATOM
3140
C8
G
D
1068
−0.246
−8.011
−28.616
1.00
22.08
RNA2
C


ATOM
3141
N7
G
D
1068
0.944
−8.464
−28.328
1.00
22.50
RNA2
N


ATOM
3142
C5
G
D
1068
1.803
−7.433
−28.683
1.00
10.90
RNA2
C


ATOM
3143
C6
G
D
1068
3.211
−7.347
−28.595
1.00
18.64
RNA2
C


ATOM
3144
O6
G
D
1068
4.011
−8.196
−28.176
1.00
32.91
RNA2
O


ATOM
3145
N1
G
D
1068
3.679
−6.123
−29.060
1.00
12.16
RNA2
N


ATOM
3146
C2
G
D
1068
2.894
−5.115
−29.547
1.00
13.74
RNA2
C


ATOM
3147
N2
G
D
1068
3.543
−4.013
−29.960
1.00
20.53
RNA2
N


ATOM
3148
N3
G
D
1068
1.575
−5.179
−29.629
1.00
16.63
RNA2
N


ATOM
3149
C4
G
D
1068
1.100
−6.360
−29.184
1.00
16.14
RNA2
C


ATOM
3150
P
A
D
1069
−3.995
−8.447
−32.902
1.00
27.21
RNA2
P


ATOM
3151
O1P
A
D
1069
−4.082
−9.718
−32.124
1.00
34.28
RNA2
O


ATOM
3152
O2P
A
D
1069
−5.070
−8.102
−33.864
1.00
29.02
RNA2
O


ATOM
3153
O5*
A
D
1069
−2.601
−8.445
−33.661
1.00
13.61
RNA2
O


ATOM
3154
C5*
A
D
1069
−2.231
−7.337
−34.472
1.00
12.04
RNA2
C


ATOM
3155
C4*
A
D
1069
−0.867
−7.557
−35.055
1.00
21.87
RNA2
C


ATOM
3156
O4*
A
D
1069
0.149
−7.322
−34.046
1.00
32.63
RNA2
O


ATOM
3157
C3*
A
D
1069
−0.590
−8.954
−35.628
1.00
35.90
RNA2
C


ATOM
3158
O3*
A
D
1069
0.162
−8.819
−36.833
1.00
43.63
RNA2
O


ATOM
3159
C2*
A
D
1069
0.352
−9.560
−34.592
1.00
35.57
RNA2
C


ATOM
3160
O2*
A
D
1069
1.241
−10.526
−35.127
1.00
44.23
RNA2
O


ATOM
3161
C1*
A
D
1069
1.127
−8.311
−34.199
1.00
42.00
RNA2
C


ATOM
3162
N9
A
D
1069
2.031
−8.358
−33.054
1.00
38.32
RNA2
N


ATOM
3163
C8
A
D
1069
2.071
−9.207
−31.976
1.00
30.76
RNA2
C


ATOM
3164
N7
A
D
1069
3.141
−9.059
−31.233
1.00
35.91
RNA2
N


ATOM
3165
C5
A
D
1069
3.827
−8.017
−31.841
1.00
33.30
RNA2
C


ATOM
3166
C6
A
D
1069
5.053
−7.392
−31.552
1.00
39.74
RNA2
C


ATOM
3167
N6
A
D
1069
5.850
−7.751
−30.540
1.00
50.68
RNA2
N


ATOM
3168
N1
A
D
1069
5.443
−6.375
−32.353
1.00
41.06
RNA2
N


ATOM
3169
C2
A
D
1069
4.649
−6.022
−33.371
1.00
43.25
RNA2
C


ATOM
3170
N3
A
D
1069
3.483
−6.540
−33.747
1.00
36.03
RNA2
N


ATOM
3171
C4
A
D
1069
3.131
−7.548
−32.935
1.00
31.57
RNA2
C


ATOM
3172
P
A
D
1070
−0.353
−9.514
−38.183
1.00
39.29
RNA2
P


ATOM
3173
O1P
A
D
1070
0.847
−9.589
−39.057
1.00
23.58
RNA2
O


ATOM
3174
O2P
A
D
1070
−1.128
−10.747
−37.873
1.00
27.46
RNA2
O


ATOM
3175
O5*
A
D
1070
−1.376
−8.452
−38.783
1.00
32.87
RNA2
O


ATOM
3176
C5*
A
D
1070
−0.906
−7.233
−39.388
1.00
32.49
RNA2
C


ATOM
3177
C4*
A
D
1070
−2.018
−6.594
−40.179
1.00
35.94
RNA2
C


ATOM
3178
O4*
A
D
1070
−3.134
−6.304
−39.296
1.00
34.73
RNA2
O


ATOM
3179
C3*
A
D
1070
−1.665
−5.292
−40.885
1.00
39.27
RNA2
C


ATOM
3180
O3*
A
D
1070
−2.329
−5.275
−42.147
1.00
42.75
RNA2
O


ATOM
3181
C2*
A
D
1070
−2.248
−4.225
−39.960
1.00
39.48
RNA2
C


ATOM
3182
O2*
A
D
1070
−2.656
−3.052
−40.635
1.00
46.91
RNA2
O


ATOM
3183
C1*
A
D
1070
−3.468
−4.935
−39.379
1.00
38.47
RNA2
C


ATOM
3184
N9
A
D
1070
−3.821
−4.467
−38.038
1.00
42.60
RNA2
N


ATOM
3185
C8
A
D
1070
−3.112
−4.646
−36.878
1.00
43.81
RNA2
C


ATOM
3186
N7
A
D
1070
−3.690
−4.133
−35.822
1.00
45.93
RNA2
N


ATOM
3187
C5
A
D
1070
−4.854
−3.570
−36.318
1.00
44.50
RNA2
C


ATOM
3188
C6
A
D
1070
−5.898
−2.873
−35.697
1.00
50.91
RNA2
C


ATOM
3189
N6
A
D
1070
−5.936
−2.617
−34.390
1.00
62.29
RNA2
N


ATOM
3190
N1
A
D
1070
−6.915
−2.441
−36.474
1.00
49.05
RNA2
N


ATOM
3191
C2
A
D
1070
−6.870
−2.698
−37.783
1.00
37.67
RNA2
C


ATOM
3192
N3
A
D
1070
−5.940
−3.344
−38.485
1.00
40.26
RNA2
N


ATOM
3193
C4
A
D
1070
−4.946
−3.761
−37.683
1.00
42.22
RNA2
C


ATOM
3194
P
G
D
1071
−1.684
−4.476
−43.382
1.00
30.55
RNA2
P


ATOM
3195
O1P
G
D
1071
−2.623
−4.642
−44.520
1.00
33.24
RNA2
O


ATOM
3196
O2P
G
D
1071
−1.310
−3.114
−42.932
1.00
42.96
RNA2
O


ATOM
3197
O5*
G
D
1071
−0.331
−5.246
−43.697
1.00
21.65
RNA2
O


ATOM
3198
C5*
G
D
1071
−0.333
−6.592
−44.214
1.00
29.38
RNA2
C


ATOM
3199
C4*
G
D
1071
1.026
−6.907
−44.779
1.00
23.80
RNA2
C


ATOM
3200
O4*
G
D
1071
1.238
−6.061
−45.928
1.00
28.20
RNA2
O


ATOM
3201
C3*
G
D
1071
2.141
−6.557
−43.811
1.00
30.81
RNA2
C


ATOM
3202
O3*
G
D
1071
2.441
−7.666
−42.979
1.00
41.31
RNA2
O


ATOM
3203
C2*
G
D
1071
3.288
−6.132
−44.719
1.00
22.22
RNA2
C


ATOM
3204
O2*
G
D
1071
4.080
−7.199
−45.191
1.00
28.60
RNA2
O


ATOM
3205
C1*
G
D
1071
2.532
−5.498
−45.883
1.00
21.88
RNA2
C


ATOM
3206
N9
G
D
1071
2.369
−4.053
−45.773
1.00
20.68
RNA2
N


ATOM
3207
C8
G
D
1071
1.186
−3.366
−45.636
1.00
17.70
RNA2
C


ATOM
3208
N7
G
D
1071
1.347
−2.072
−45.623
1.00
24.21
RNA2
N


ATOM
3209
C5
G
D
1071
2.716
−1.895
−45.742
1.00
13.42
RNA2
C


ATOM
3210
C6
G
D
1071
3.478
−0.710
−45.794
1.00
24.45
RNA2
C


ATOM
3211
O6
G
D
1071
3.078
0.460
−45.758
1.00
34.15
RNA2
O


ATOM
3212
N1
G
D
1071
4.841
−0.981
−45.904
1.00
15.33
RNA2
N


ATOM
3213
C2
G
D
1071
5.395
−2.241
−45.961
1.00
23.28
RNA2
C


ATOM
3214
N2
G
D
1071
6.734
−2.306
−46.052
1.00
12.46
RNA2
N


ATOM
3215
N3
G
D
1071
4.686
−3.356
−45.925
1.00
19.68
RNA2
N


ATOM
3216
C4
G
D
1071
3.363
−3.109
−45.817
1.00
12.68
RNA2
C


ATOM
3217
P
C
D
1072
2.695
−7.430
−41.419
1.00
33.36
RNA2
P


ATOM
3218
O1P
C
D
1072
1.653
−6.490
−40.920
1.00
33.81
RNA2
O


ATOM
3219
O2P
C
D
1072
2.864
−8.759
−40.777
1.00
35.75
RNA2
O


ATOM
3220
O5*
C
D
1072
4.090
−6.677
−41.393
1.00
20.85
RNA2
O


ATOM
3221
C5*
C
D
1072
5.294
−7.370
−41.724
1.00
18.04
RNA2
C


ATOM
3222
C4*
C
D
1072
6.458
−6.420
−41.676
1.00
27.13
RNA2
C


ATOM
3223
O4*
C
D
1072
6.309
−5.437
−42.729
1.00
37.39
RNA2
O


ATOM
3224
C3*
C
D
1072
6.577
−5.591
−40.408
1.00
33.89
RNA2
C


ATOM
3225
O3*
C
D
1072
7.216
−6.295
−39.352
1.00
27.21
RNA2
O


ATOM
3226
C2*
C
D
1072
7.364
−4.376
−40.882
1.00
36.24
RNA2
C


ATOM
3227
O2*
C
D
1072
8.753
−4.637
−40.967
1.00
40.82
RNA2
O


ATOM
3228
C1*
C
D
1072
6.803
−4.182
−42.291
1.00
32.40
RNA2
C


ATOM
3229
N1
C
D
1072
5.704
−3.196
−42.347
1.00
21.10
RNA2
N


ATOM
3230
C2
C
D
1072
6.015
−1.860
−42.594
1.00
22.51
RNA2
C


ATOM
3231
O2
C
D
1072
7.206
−1.541
−42.755
1.00
32.30
RNA2
O


ATOM
3232
N3
C
D
1072
5.016
−0.947
−42.647
1.00
18.99
RNA2
N


ATOM
3233
C4
C
D
1072
3.750
−1.327
−42.456
1.00
23.03
RNA2
C


ATOM
3234
N4
C
D
1072
2.795
−0.389
−42.506
1.00
21.64
RNA2
N


ATOM
3235
C5
C
D
1072
3.405
−2.681
−42.204
1.00
18.92
RNA2
C


ATOM
3236
C6
C
D
1072
4.404
−3.575
−42.160
1.00
22.99
RNA2
C


ATOM
3237
P
A
D
1073
6.502
−6.360
−37.915
1.00
37.37
RNA2
P


ATOM
3238
O1P
A
D
1073
6.300
−4.954
−37.487
1.00
30.80
RNA2
O


ATOM
3239
O2P
A
D
1073
5.328
−7.287
−37.972
1.00
26.29
RNA2
O


ATOM
3240
O5*
A
D
1073
7.614
−6.996
−36.980
1.00
33.33
RNA2
O


ATOM
3241
C5*
A
D
1073
8.842
−6.293
−36.711
1.00
45.87
RNA2
C


ATOM
3242
C4*
A
D
1073
9.614
−7.024
−35.651
1.00
39.23
RNA2
C


ATOM
3243
O4*
A
D
1073
8.804
−7.060
−34.451
1.00
42.33
RNA2
O


ATOM
3244
C3*
A
D
1073
9.847
−8.484
−35.996
1.00
42.31
RNA2
C


ATOM
3245
O3*
A
D
1073
11.022
−8.666
−36.753
1.00
46.57
RNA2
O


ATOM
3246
C2*
A
D
1073
9.902
−9.161
−34.638
1.00
40.15
RNA2
C


ATOM
3247
O2*
A
D
1073
11.169
−9.047
−34.018
1.00
50.42
RNA2
O


ATOM
3248
C1*
A
D
1073
8.866
−8.350
−33.866
1.00
29.91
RNA2
C


ATOM
3249
N9
A
D
1073
7.532
−8.935
−33.963
1.00
24.96
RNA2
N


ATOM
3250
C8
A
D
1073
6.453
−8.438
−34.648
1.00
25.01
RNA2
C


ATOM
3251
N7
A
D
1073
5.373
−9.170
−34.534
1.00
31.09
RNA2
N


ATOM
3252
C5
A
D
1073
5.770
−10.224
−33.727
1.00
16.48
RNA2
C


ATOM
3253
C6
A
D
1073
5.085
−11.338
−33.237
1.00
25.59
RNA2
C


ATOM
3254
N6
A
D
1073
3.804
−11.589
−33.504
1.00
28.23
RNA2
N


ATOM
3255
N1
A
D
1073
5.765
−12.201
−32.456
1.00
25.23
RNA2
N


ATOM
3256
C2
A
D
1073
7.053
−11.951
−32.200
1.00
27.30
RNA2
C


ATOM
3257
N3
A
D
1073
7.811
−10.937
−32.608
1.00
31.09
RNA2
N


ATOM
3258
C4
A
D
1073
7.099
−10.097
−33.375
1.00
27.01
RNA2
C


ATOM
3259
P
G
D
1074
11.030
−9.753
−37.924
1.00
43.98
RNA2
P


ATOM
3260
O1P
G
D
1074
9.978
−9.343
−38.892
1.00
47.14
RNA2
O


ATOM
3261
O2P
G
D
1074
12.435
−9.917
−38.384
1.00
36.10
RNA2
O


ATOM
3262
O5*
G
D
1074
10.556
−11.084
−37.192
1.00
30.43
RNA2
O


ATOM
3263
C5*
G
D
1074
11.408
−11.715
−36.230
1.00
29.08
RNA2
C


ATOM
3264
C4*
G
D
1074
10.753
−12.951
−35.675
1.00
27.13
RNA2
C


ATOM
3265
O4*
G
D
1074
9.559
−12.586
−34.940
1.00
25.79
RNA2
O


ATOM
3266
C3*
G
D
1074
10.260
−13.964
−36.689
1.00
34.21
RNA2
C


ATOM
3267
O3*
G
D
1074
11.289
−14.803
−37.175
1.00
42.20
RNA2
O


ATOM
3268
C2*
G
D
1074
9.202
−14.730
−35.908
1.00
33.31
RNA2
C


ATOM
3269
O2*
G
D
1074
9.747
−15.738
−35.080
1.00
37.22
RNA2
O


ATOM
3270
C1*
G
D
1074
8.598
−13.621
−35.049
1.00
21.21
RNA2
C


ATOM
3271
N9
G
D
1074
7.387
−13.070
−35.648
1.00
27.34
RNA2
N


ATOM
3272
C8
G
D
1074
7.235
−11.852
−36.268
1.00
27.08
RNA2
C


ATOM
3273
N7
G
D
1074
6.017
−11.640
−36.688
1.00
25.47
RNA2
N


ATOM
3274
C5
G
D
1074
5.325
−12.787
−36.327
1.00
19.99
RNA2
C


ATOM
3275
C6
G
D
1074
3.966
−13.130
−36.504
1.00
30.58
RNA2
C


ATOM
3276
O6
G
D
1074
3.063
−12.460
−37.021
1.00
35.90
RNA2
O


ATOM
3277
N1
G
D
1074
3.687
−14.396
−35.992
1.00
36.16
RNA2
N


ATOM
3278
C2
G
D
1074
4.597
−15.219
−35.379
1.00
34.56
RNA2
C


ATOM
3279
N2
G
D
1074
4.134
−16.400
−34.936
1.00
34.63
RNA2
N


ATOM
3280
N3
G
D
1074
5.868
−14.906
−35.205
1.00
31.20
RNA2
N


ATOM
3281
C4
G
D
1074
6.159
−13.683
−35.695
1.00
23.24
RNA2
C


ATOM
3282
P
C
D
1075
11.130
−15.471
−38.624
1.00
45.43
RNA2
P


ATOM
3283
O1P
C
D
1075
10.527
−14.447
−39.520
1.00
54.78
RNA2
O


ATOM
3284
O2P
C
D
1075
12.430
−16.096
−38.995
1.00
41.18
RNA2
O


ATOM
3285
O5*
C
D
1075
10.046
−16.607
−38.379
1.00
33.77
RNA2
O


ATOM
3286
C5*
C
D
1075
10.384
−17.767
−37.609
1.00
31.73
RNA2
C


ATOM
3287
C4*
C
D
1075
9.233
−18.737
−37.587
1.00
31.50
RNA2
C


ATOM
3288
O4*
C
D
1075
8.122
−18.137
−36.879
1.00
31.95
RNA2
O


ATOM
3289
C3*
C
D
1075
8.653
−19.112
−38.940
1.00
34.59
RNA2
C


ATOM
3290
O3*
C
D
1075
9.390
−20.130
−39.596
1.00
42.98
RNA2
O


ATOM
3291
C2*
C
D
1075
7.239
−19.539
−38.581
1.00
30.88
RNA2
C


ATOM
3292
O2*
C
D
1075
7.175
−20.852
−38.064
1.00
24.97
RNA2
O


ATOM
3293
C1*
C
D
1075
6.902
−18.546
−37.472
1.00
31.01
RNA2
C


ATOM
3294
N1
C
D
1075
6.223
−17.355
−38.013
1.00
26.90
RNA2
N


ATOM
3295
C2
C
D
1075
4.831
−17.388
−38.173
1.00
32.07
RNA2
C


ATOM
3296
O2
C
D
1075
4.206
−18.407
−37.825
1.00
31.32
RNA2
O


ATOM
3297
N3
C
D
1075
4.204
−16.313
−38.700
1.00
31.52
RNA2
N


ATOM
3298
C4
C
D
1075
4.908
−15.237
−39.059
1.00
24.70
RNA2
C


ATOM
3299
N4
C
D
1075
4.246
−14.208
−39.592
1.00
23.21
RNA2
N


ATOM
3300
C5
C
D
1075
6.320
−15.169
−38.892
1.00
20.78
RNA2
C


ATOM
3301
C6
C
D
1075
6.932
−16.239
−38.370
1.00
26.55
RNA2
C


ATOM
3302
P
C
D
1076
9.458
−20.140
−41.200
1.00
41.54
RNA2
P


ATOM
3303
O1P
C
D
1076
9.719
−18.749
−41.663
1.00
42.90
RNA2
O


ATOM
3304
O2P
C
D
1076
10.363
−21.241
−41.628
1.00
43.49
RNA2
O


ATOM
3305
O5*
C
D
1076
7.973
−20.524
−41.614
1.00
36.12
RNA2
O


ATOM
3306
C5*
C
D
1076
7.448
−21.808
−41.272
1.00
35.93
RNA2
C


ATOM
3307
C4*
C
D
1076
6.024
−21.941
−41.742
1.00
36.70
RNA2
C


ATOM
3308
O4*
C
D
1076
5.179
−21.022
−41.003
1.00
41.67
RNA2
O


ATOM
3309
C3*
C
D
1076
5.735
−21.611
−43.198
1.00
33.47
RNA2
C


ATOM
3310
O3*
C
D
1076
6.076
−22.654
−44.099
1.00
41.74
RNA2
O


ATOM
3311
C2*
C
D
1076
4.240
−21.334
−43.160
1.00
38.53
RNA2
C


ATOM
3312
O2*
C
D
1076
3.483
−22.530
−43.103
1.00
31.60
RNA2
O


ATOM
3313
C1*
C
D
1076
4.107
−20.590
−41.831
1.00
39.34
RNA2
C


ATOM
3314
N1
C
D
1076
4.199
−19.124
−42.018
1.00
25.11
RNA2
N


ATOM
3315
C2
C
D
1076
3.048
−18.421
−42.397
1.00
28.28
RNA2
C


ATOM
3316
O2
C
D
1076
1.978
−19.045
−42.536
1.00
22.07
RNA2
O


ATOM
3317
N3
C
D
1076
3.127
−17.083
−42.605
1.00
27.17
RNA2
N


ATOM
3318
C4
C
D
1076
4.293
−16.452
−42.451
1.00
27.03
RNA2
C


ATOM
3319
N4
C
D
1076
4.330
−15.136
−42.681
1.00
24.90
RNA2
N


ATOM
3320
C5
C
D
1076
5.475
−17.140
−42.056
1.00
21.98
RNA2
C


ATOM
3321
C6
C
D
1076
5.384
−18.460
−41.849
1.00
26.59
RNA2
C


ATOM
3322
P
A
D
1077
6.603
−22.281
−45.575
1.00
39.40
RNA2
P


ATOM
3323
O1P
A
D
1077
7.618
−21.198
−45.455
1.00
25.39
RNA2
O


ATOM
3324
O2P
A
D
1077
6.965
−23.549
−46.255
1.00
45.75
RNA2
O


ATOM
3325
O5*
A
D
1077
5.308
−21.688
−46.290
1.00
35.32
RNA2
O


ATOM
3326
C5*
A
D
1077
4.132
−22.496
−46.434
1.00
30.36
RNA2
C


ATOM
3327
C4*
A
D
1077
2.948
−21.659
−46.863
1.00
39.87
RNA2
C


ATOM
3328
O4*
A
D
1077
2.657
−20.660
−45.852
1.00
36.52
RNA2
O


ATOM
3329
C3*
A
D
1077
3.067
−20.856
−48.149
1.00
35.06
RNA2
C


ATOM
3330
O3*
A
D
1077
2.842
−21.640
−49.313
1.00
33.77
RNA2
O


ATOM
3331
C2*
A
D
1077
1.981
−19.801
−47.965
1.00
41.16
RNA2
C


ATOM
3332
O2*
A
D
1077
0.677
−20.271
−48.264
1.00
33.46
RNA2
O


ATOM
3333
C1*
A
D
1077
2.078
−19.520
−46.466
1.00
37.76
RNA2
C


ATOM
3334
N9
A
D
1077
2.924
−18.352
−46.211
1.00
25.78
RNA2
N


ATOM
3335
C8
A
D
1077
4.243
−18.300
−45.836
1.00
18.19
RNA2
C


ATOM
3336
N7
A
D
1077
4.722
−17.081
−45.756
1.00
17.18
RNA2
N


ATOM
3337
C5
A
D
1077
3.639
−16.275
−46.087
1.00
18.35
RNA2
C


ATOM
3338
C6
A
D
1077
3.492
−14.874
−46.208
1.00
24.31
RNA2
C


ATOM
3339
N6
A
D
1077
4.486
−13.996
−46.008
1.00
25.10
RNA2
N


ATOM
3340
N1
A
D
1077
2.277
−14.401
−46.558
1.00
22.28
RNA2
N


ATOM
3341
C2
A
D
1077
1.285
−15.278
−46.776
1.00
17.11
RNA2
C


ATOM
3342
N3
A
D
1077
1.302
−16.604
−46.702
1.00
22.31
RNA2
N


ATOM
3343
C4
A
D
1077
2.522
−17.044
−46.352
1.00
17.88
RNA2
C


ATOM
3344
P
U
D
1078
3.650
−21.306
−50.662
1.00
27.11
RNA2
P


ATOM
3345
O1P
U
D
1078
5.104
−21.343
−50.374
1.00
20.77
RNA2
O


ATOM
3346
O2P
U
D
1078
3.091
−22.176
−51.728
1.00
43.45
RNA2
O


ATOM
3347
O5*
U
D
1078
3.288
−19.785
−50.981
1.00
30.32
RNA2
O


ATOM
3348
C5*
U
D
1078
1.985
−19.408
−51.478
1.00
30.56
RNA2
C


ATOM
3349
C4*
U
D
1078
1.896
−17.901
−51.631
1.00
32.53
RNA2
C


ATOM
3350
O4*
U
D
1078
2.062
−17.283
−50.329
1.00
27.97
RNA2
O


ATOM
3351
C3*
U
D
1078
2.967
−17.244
−52.497
1.00
36.01
RNA2
C


ATOM
3352
O3*
U
D
1078
2.620
−17.183
−53.871
1.00
42.75
RNA2
O


ATOM
3353
C2*
U
D
1078
2.990
−15.821
−51.961
1.00
36.74
RNA2
C


ATOM
3354
O2*
U
D
1078
1.935
−15.045
−52.493
1.00
40.26
RNA2
O


ATOM
3355
C1*
U
D
1078
2.744
−16.048
−50.472
1.00
35.91
RNA2
C


ATOM
3356
N1
U
D
1078
4.015
−16.102
−49.729
1.00
25.89
RNA2
N


ATOM
3357
C2
U
D
1078
4.637
−14.892
−49.423
1.00
35.33
RNA2
C


ATOM
3358
O2
U
D
1078
4.167
−13.800
−49.730
1.00
30.93
RNA2
O


ATOM
3359
N3
U
D
1078
5.830
−15.008
−48.749
1.00
28.65
RNA2
N


ATOM
3360
C4
U
D
1078
6.455
−16.177
−48.357
1.00
30.34
RNA2
C


ATOM
3361
O4
U
D
1078
7.555
−16.119
−47.795
1.00
39.15
RNA2
O


ATOM
3362
C5
U
D
1078
5.749
−17.376
−48.699
1.00
25.89
RNA2
C


ATOM
3363
C6
U
D
1078
4.584
−17.300
−49.355
1.00
28.67
RNA2
C


ATOM
3364
P
C
D
1079
2.674
−18.503
−54.775
1.00
37.89
RNA2
P


ATOM
3365
O1P
C
D
1079
2.944
−18.013
−56.153
1.00
39.80
RNA2
O


ATOM
3366
O2P
C
D
1079
3.558
−19.539
−54.176
1.00
37.02
RNA2
O


ATOM
3367
O5*
C
D
1079
1.167
−18.996
−54.704
1.00
15.08
RNA2
O


ATOM
3368
C5*
C
D
1079
0.145
−18.192
−55.288
1.00
23.37
RNA2
C


ATOM
3369
C4*
C
D
1079
−1.208
−18.608
−54.795
1.00
19.59
RNA2
C


ATOM
3370
O4*
C
D
1079
−1.438
−18.079
−53.467
1.00
27.26
RNA2
O


ATOM
3371
C3*
C
D
1079
−2.308
−17.995
−55.628
1.00
31.62
RNA2
C


ATOM
3372
O3*
C
D
1079
−2.525
−18.767
−56.789
1.00
35.58
RNA2
O


ATOM
3373
C2*
C
D
1079
−3.484
−17.941
−54.667
1.00
27.16
RNA2
C


ATOM
3374
O2*
C
D
1079
−4.148
−19.180
−54.551
1.00
30.55
RNA2
O


ATOM
3375
C1*
C
D
1079
−2.774
−17.609
−53.357
1.00
19.20
RNA2
C


ATOM
3376
N1
C
D
1079
−2.738
−16.155
−53.087
1.00
15.42
RNA2
N


ATOM
3377
C2
C
D
1079
−3.891
−15.525
−52.594
1.00
14.73
RNA2
C


ATOM
3378
O2
C
D
1079
−4.922
−16.196
−52.423
1.00
22.43
RNA2
O


ATOM
3379
N3
C
D
1079
−3.853
−14.203
−52.319
1.00
15.70
RNA2
N


ATOM
3380
C4
C
D
1079
−2.730
−13.512
−52.513
1.00
19.14
RNA2
C


ATOM
3381
N4
C
D
1079
−2.733
−12.219
−52.194
1.00
18.52
RNA2
N


ATOM
3382
C5
C
D
1079
−1.550
−14.119
−53.033
1.00
14.27
RNA2
C


ATOM
3383
C6
C
D
1079
−1.598
−15.430
−53.303
1.00
9.72
RNA2
C


ATOM
3384
P
A
D
1080
−2.665
−18.025
−58.200
1.00
33.84
RNA2
P


ATOM
3385
O1P
A
D
1080
−1.604
−16.982
−58.302
1.00
29.98
RNA2
O


ATOM
3386
O2P
A
D
1080
−2.762
−19.085
−59.240
1.00
51.18
RNA2
O


ATOM
3387
O5*
A
D
1080
−4.078
−17.315
−58.069
1.00
18.89
RNA2
O


ATOM
3388
C5*
A
D
1080
−5.228
−18.109
−57.802
1.00
23.14
RNA2
C


ATOM
3389
C4*
A
D
1080
−6.362
−17.256
−57.316
1.00
29.15
RNA2
C


ATOM
3390
O4*
A
D
1080
−6.077
−16.724
−55.997
1.00
31.88
RNA2
O


ATOM
3391
C3*
A
D
1080
−6.704
−16.028
−58.131
1.00
27.12
RNA2
C


ATOM
3392
O3*
A
D
1080
−7.427
−16.344
−59.312
1.00
35.45
RNA2
O


ATOM
3393
C2*
A
D
1080
−7.520
−15.221
−57.129
1.00
24.68
RNA2
C


ATOM
3394
O2*
A
D
1080
−8.839
−15.710
−57.002
1.00
23.19
RNA2
O


ATOM
3395
C1*
A
D
1080
−6.774
−15.502
−55.826
1.00
22.08
RNA2
C


ATOM
3396
N9
A
D
1080
−5.817
−14.431
−55.545
1.00
19.19
RNA2
N


ATOM
3397
C8
A
D
1080
−4.460
−14.391
−55.773
1.00
21.24
RNA2
C


ATOM
3398
N7
A
D
1080
−3.911
−13.232
−55.485
1.00
17.04
RNA2
N


ATOM
3399
C5
A
D
1080
−4.974
−12.465
−55.021
1.00
10.07
RNA2
C


ATOM
3400
C6
A
D
1080
−5.061
−11.132
−54.578
1.00
15.82
RNA2
C


ATOM
3401
N6
A
D
1080
−4.019
−10.295
−54.529
1.00
19.09
RNA2
N


ATOM
3402
N1
A
D
1080
−6.271
−10.680
−54.183
1.00
20.36
RNA2
N


ATOM
3403
C2
A
D
1080
−7.317
−11.517
−54.229
1.00
15.92
RNA2
C


ATOM
3404
N3
A
D
1080
−7.362
−12.783
−54.626
1.00
14.17
RNA2
N


ATOM
3405
C4
A
D
1080
−6.145
−13.200
−55.023
1.00
9.63
RNA2
C


ATOM
3406
P
U
D
1081
−7.413
−15.312
−60.548
1.00
31.28
RNA2
P


ATOM
3407
O1P
U
D
1081
−6.027
−14.791
−60.717
1.00
8.76
RNA2
O


ATOM
3408
O2P
U
D
1081
−8.089
−15.971
−61.696
1.00
35.73
RNA2
O


ATOM
3409
O5*
U
D
1081
−8.356
−14.144
−60.021
1.00
18.56
RNA2
O


ATOM
3410
C5*
U
D
1081
−9.643
−14.457
−59.459
1.00
22.44
RNA2
C


ATOM
3411
C4*
U
D
1081
−10.276
−13.222
−58.867
1.00
34.63
RNA2
C


ATOM
3412
O4*
U
D
1081
−9.471
−12.728
−57.771
1.00
31.00
RNA2
O


ATOM
3413
C3*
U
D
1081
−10.406
−12.045
−59.817
1.00
37.02
RNA2
C


ATOM
3414
O3*
U
D
1081
−11.605
−12.172
−60.569
1.00
43.64
RNA2
O


ATOM
3415
C2*
U
D
1081
−10.429
−10.844
−58.874
1.00
32.75
RNA2
C


ATOM
3416
O2*
U
D
1081
−11.714
−10.603
−58.330
1.00
30.48
RNA2
O


ATOM
3417
C1*
U
D
1081
−9.499
−11.311
−57.756
1.00
21.25
RNA2
C


ATOM
3418
N1
U
D
1081
−8.115
−10.826
−57.857
1.00
8.85
RNA2
N


ATOM
3419
C2
U
D
1081
−7.839
−9.537
−57.429
1.00
18.01
RNA2
C


ATOM
3420
O2
U
D
1081
−8.706
−8.754
−57.039
1.00
20.38
RNA2
O


ATOM
3421
N3
U
D
1081
−6.515
−9.190
−57.477
1.00
4.56
RNA2
N


ATOM
3422
C4
U
D
1081
−5.463
−9.977
−57.902
1.00
19.29
RNA2
C


ATOM
3423
O4
U
D
1081
−4.306
−9.560
−57.785
1.00
17.28
RNA2
O


ATOM
3424
C5
U
D
1081
−5.838
−11.273
−58.364
1.00
8.37
RNA2
C


ATOM
3425
C6
U
D
1081
−7.118
−11.640
−58.331
1.00
9.01
RNA2
C


ATOM
3426
P
U
D
1082
−11.700
−11.511
−62.026
1.00
37.21
RNA2
P


ATOM
3427
O1P
U
D
1082
−10.555
−11.984
−62.849
1.00
30.04
RNA2
O


ATOM
3428
O2P
U
D
1082
−13.101
−11.726
−62.489
1.00
36.07
RNA2
O


ATOM
3429
O5*
U
D
1082
−11.463
−9.962
−61.755
1.00
48.61
RNA2
O


ATOM
3430
C5*
U
D
1082
−12.470
−9.172
−61.107
1.00
49.13
RNA2
C


ATOM
3431
C4*
U
D
1082
−12.043
−7.729
−61.052
1.00
45.78
RNA2
C


ATOM
3432
O4*
U
D
1082
−11.006
−7.553
−60.054
1.00
41.16
RNA2
O


ATOM
3433
C3*
U
D
1082
−11.417
−7.176
−62.317
1.00
45.00
RNA2
C


ATOM
3434
O3*
U
D
1082
−12.349
−6.822
−63.321
1.00
44.91
RNA2
O


ATOM
3435
C2*
U
D
1082
−10.633
−5.979
−61.801
1.00
41.47
RNA2
C


ATOM
3436
O2*
U
D
1082
−11.449
−4.837
−61.628
1.00
38.13
RNA2
O


ATOM
3437
C1*
U
D
1082
−10.147
−6.497
−60.448
1.00
34.17
RNA2
C


ATOM
3438
N1
U
D
1082
−8.767
−6.998
−60.524
1.00
21.76
RNA2
N


ATOM
3439
C2
U
D
1082
−7.752
−6.093
−60.271
1.00
27.58
RNA2
C


ATOM
3440
O2
U
D
1082
−7.961
−4.925
−59.983
1.00
39.33
RNA2
O


ATOM
3441
N3
U
D
1082
−6.482
−6.599
−60.370
1.00
17.32
RNA2
N


ATOM
3442
C4
U
D
1082
−6.125
−7.886
−60.687
1.00
19.81
RNA2
C


ATOM
3443
O4
U
D
1082
−4.925
−8.184
−60.736
1.00
21.01
RNA2
O


ATOM
3444
C5
U
D
1082
−7.228
−8.767
−60.933
1.00
16.38
RNA2
C


ATOM
3445
C6
U
D
1082
−8.483
−8.304
−60.843
1.00
16.69
RNA2
C


ATOM
3446
P
U
D
1083
−11.820
−6.597
−64.817
1.00
43.63
RNA2
P


ATOM
3447
O1P
U
D
1083
−11.131
−7.845
−65.255
1.00
40.26
RNA2
O


ATOM
3448
O2P
U
D
1083
−12.950
−6.055
−65.619
1.00
45.21
RNA2
O


ATOM
3449
O5*
U
D
1083
−10.714
−5.466
−64.618
1.00
33.40
RNA2
O


ATOM
3450
C5*
U
D
1083
−9.461
−5.509
−65.306
1.00
21.92
RNA2
C


ATOM
3451
C4*
U
D
1083
−8.508
−4.519
−64.689
1.00
33.84
RNA2
C


ATOM
3452
O4*
U
D
1083
−7.824
−5.125
−63.563
1.00
30.68
RNA2
O


ATOM
3453
C3*
U
D
1083
−7.392
−4.060
−65.607
1.00
39.61
RNA2
C


ATOM
3454
O3*
U
D
1083
−7.851
−2.983
−66.405
1.00
47.78
RNA2
O


ATOM
3455
C2*
U
D
1083
−6.301
−3.633
−64.635
1.00
38.07
RNA2
C


ATOM
3456
O2*
U
D
1083
−6.517
−2.326
−64.141
1.00
48.19
RNA2
O


ATOM
3457
C1*
U
D
1083
−6.486
−4.647
−63.504
1.00
32.72
RNA2
C


ATOM
3458
N1
U
D
1083
−5.568
−5.793
−63.608
1.00
23.49
RNA2
N


ATOM
3459
C2
U
D
1083
−4.251
−5.604
−63.225
1.00
27.40
RNA2
C


ATOM
3460
O2
U
D
1083
−3.823
−4.541
−62.823
1.00
42.53
RNA2
O


ATOM
3461
N3
U
D
1083
−3.447
−6.710
−63.335
1.00
31.74
RNA2
N


ATOM
3462
C4
U
D
1083
−3.809
−7.963
−63.784
1.00
30.45
RNA2
C


ATOM
3463
O4
U
D
1083
−2.962
−8.863
−63.823
1.00
30.78
RNA2
O


ATOM
3464
C5
U
D
1083
−5.183
−8.081
−64.168
1.00
19.97
RNA2
C


ATOM
3465
C6
U
D
1083
−5.995
−7.019
−64.069
1.00
27.83
RNA2
C


ATOM
3466
P
A
D
1084
−7.438
−2.912
−67.949
1.00
45.35
RNA2
P


ATOM
3467
O1P
A
D
1084
−7.390
−4.295
−68.485
1.00
47.07
RNA2
O


ATOM
3468
O2P
A
D
1084
−8.323
−1.906
−68.587
1.00
48.86
RNA2
O


ATOM
3469
O5*
A
D
1084
−5.952
−2.353
−67.903
1.00
30.12
RNA2
O


ATOM
3470
C5*
A
D
1084
−5.051
−2.560
−68.990
1.00
25.41
RNA2
C


ATOM
3471
C4*
A
D
1084
−3.717
−1.960
−68.652
1.00
29.72
RNA2
C


ATOM
3472
O4*
A
D
1084
−3.876
−0.534
−68.496
1.00
39.52
RNA2
O


ATOM
3473
C3*
A
D
1084
−3.174
−2.444
−67.326
1.00
26.49
RNA2
C


ATOM
3474
O3*
A
D
1084
−2.405
−3.601
−67.544
1.00
36.34
RNA2
O


ATOM
3475
C2*
A
D
1084
−2.346
−1.271
−66.828
1.00
33.86
RNA2
C


ATOM
3476
O2*
A
D
1084
−1.043
−1.267
−67.373
1.00
28.54
RNA2
O


ATOM
3477
C1*
A
D
1084
−3.138
−0.086
−67.379
1.00
30.15
RNA2
C


ATOM
3478
N9
A
D
1084
−4.093
0.522
−66.459
1.00
28.36
RNA2
N


ATOM
3479
C8
A
D
1084
−5.439
0.258
−66.342
1.00
28.20
RNA2
C


ATOM
3480
N7
A
D
1084
−6.058
1.041
−65.494
1.00
25.56
RNA2
N


ATOM
3481
C5
A
D
1084
−5.050
1.861
−65.004
1.00
22.38
RNA2
C


ATOM
3482
C6
A
D
1084
−5.061
2.922
−64.088
1.00
27.67
RNA2
C


ATOM
3483
N6
A
D
1084
−6.165
3.359
−63.482
1.00
38.68
RNA2
N


ATOM
3484
N1
A
D
1084
−3.884
3.530
−63.815
1.00
34.84
RNA2
N


ATOM
3485
C2
A
D
1084
−2.776
3.091
−64.434
1.00
37.58
RNA2
C


ATOM
3486
N3
A
D
1084
−2.641
2.106
−65.322
1.00
27.16
RNA2
N


ATOM
3487
C4
A
D
1084
−3.830
1.530
−65.569
1.00
29.13
RNA2
C


ATOM
3488
P
A
D
1085
−2.533
−4.824
−66.531
1.00
33.05
RNA2
P


ATOM
3489
O1P
A
D
1085
−3.976
−4.945
−66.187
1.00
26.54
RNA2
O


ATOM
3490
O2P
A
D
1085
−1.809
−5.987
−67.103
1.00
37.42
RNA2
O


ATOM
3491
O5*
A
D
1085
−1.708
−4.311
−65.275
1.00
37.64
RNA2
O


ATOM
3492
C5*
A
D
1085
−0.321
−3.983
−65.415
1.00
34.30
RNA2
C


ATOM
3493
C4*
A
D
1085
0.137
−3.193
−64.225
1.00
40.98
RNA2
C


ATOM
3494
O4*
A
D
1085
−0.509
−1.900
−64.217
1.00
45.08
RNA2
O


ATOM
3495
C3*
A
D
1085
−0.209
−3.817
−62.888
1.00
33.48
RNA2
C


ATOM
3496
O3*
A
D
1085
0.816
−4.734
−62.538
1.00
33.50
RNA2
O


ATOM
3497
C2*
A
D
1085
−0.260
−2.614
−61.955
1.00
33.78
RNA2
C


ATOM
3498
O2*
A
D
1085
1.022
−2.252
−61.488
1.00
36.97
RNA2
O


ATOM
3499
C1*
A
D
1085
−0.762
−1.506
−62.885
1.00
29.69
RNA2
C


ATOM
3500
N9
A
D
1085
−2.183
−1.205
−62.769
1.00
20.61
RNA2
N


ATOM
3501
C8
A
D
1085
−3.232
−1.910
−63.299
1.00
32.48
RNA2
C


ATOM
3502
N7
A
D
1085
−4.406
−1.388
−63.038
1.00
31.65
RNA2
N


ATOM
3503
C5
A
D
1085
−4.110
−0.263
−62.285
1.00
23.98
RNA2
C


ATOM
3504
C6
A
D
1085
−4.922
0.724
−61.710
1.00
27.87
RNA2
C


ATOM
3505
N6
A
D
1085
−6.253
0.732
−61.813
1.00
35.25
RNA2
N


ATOM
3506
N1
A
D
1085
−4.315
1.716
−61.023
1.00
23.17
RNA2
N


ATOM
3507
C2
A
D
1085
−2.975
1.709
−60.936
1.00
28.66
RNA2
C


ATOM
3508
N3
A
D
1085
−2.102
0.838
−61.439
1.00
29.00
RNA2
N


ATOM
3509
C4
A
D
1085
−2.742
−0.137
−62.110
1.00
24.43
RNA2
C


ATOM
3510
P
A
D
1086
0.438
−6.094
−61.782
1.00
32.76
RNA2
P


ATOM
3511
O1P
A
D
1086
−0.961
−6.454
−62.137
1.00
17.94
RNA2
O


ATOM
3512
O2P
A
D
1086
1.532
−7.068
−62.001
1.00
30.14
RNA2
O


ATOM
3513
O5*
A
D
1086
0.451
−5.671
−60.253
1.00
42.21
RNA2
O


ATOM
3514
C5*
A
D
1086
1.644
−5.155
−59.645
1.00
32.88
RNA2
C


ATOM
3515
C4*
A
D
1086
1.288
−4.326
−58.440
1.00
36.41
RNA2
C


ATOM
3516
O4*
A
D
1086
0.612
−3.114
−58.860
1.00
29.39
RNA2
O


ATOM
3517
C3*
A
D
1086
0.303
−4.967
−57.481
1.00
36.90
RNA2
C


ATOM
3518
O3*
A
D
1086
0.922
−5.900
−56.613
1.00
33.24
RNA2
O


ATOM
3519
C2*
A
D
1086
−0.287
−3.768
−56.748
1.00
42.63
RNA2
C


ATOM
3520
O2*
A
D
1086
0.470
−3.347
−55.630
1.00
53.18
RNA2
O


ATOM
3521
C1*
A
D
1086
−0.267
−2.692
−57.839
1.00
38.42
RNA2
C


ATOM
3522
N9
A
D
1086
−1.590
−2.432
−58.407
1.00
27.17
RNA2
N


ATOM
3523
C8
A
D
1086
−2.195
−1.210
−58.569
1.00
27.28
RNA2
C


ATOM
3524
N7
A
D
1086
−3.431
−1.285
−59.001
1.00
32.05
RNA2
N


ATOM
3525
C5
A
D
1086
−3.644
−2.647
−59.160
1.00
25.72
RNA2
C


ATOM
3526
C6
A
D
1086
−4.765
−3.385
−59.572
1.00
30.69
RNA2
C


ATOM
3527
N6
A
D
1086
−5.930
−2.832
−59.910
1.00
37.15
RNA2
N


ATOM
3528
N1
A
D
1086
−4.650
−4.731
−59.619
1.00
26.67
RNA2
N


ATOM
3529
C2
A
D
1086
−3.484
−5.284
−59.271
1.00
27.74
RNA2
C


ATOM
3530
N3
A
D
1086
−2.360
−4.697
−58.860
1.00
32.46
RNA2
N


ATOM
3531
C4
A
D
1086
−2.510
−3.363
−58.824
1.00
28.26
RNA2
C


ATOM
3532
P
G
D
1087
0.286
−7.364
−56.455
1.00
31.77
RNA2
P


ATOM
3533
O1P
G
D
1087
−0.973
−7.249
−55.682
1.00
28.82
RNA2
O


ATOM
3534
O2P
G
D
1087
0.266
−8.020
−57.788
1.00
46.35
RNA2
O


ATOM
3535
O5*
G
D
1087
1.337
−8.122
−55.545
1.00
32.87
RNA2
O


ATOM
3536
C5*
G
D
1087
2.401
−8.899
−56.109
1.00
29.23
RNA2
C


ATOM
3537
C4*
G
D
1087
3.449
−9.109
−55.061
1.00
33.39
RNA2
C


ATOM
3538
O4*
G
D
1087
4.062
−7.829
−54.802
1.00
39.61
RNA2
O


ATOM
3539
C3*
G
D
1087
2.847
−9.568
−53.742
1.00
26.85
RNA2
C


ATOM
3540
O3*
G
D
1087
2.937
−10.985
−53.689
1.00
26.33
RNA2
O


ATOM
3541
C2*
G
D
1087
3.745
−8.914
−52.696
1.00
29.63
RNA2
C


ATOM
3542
O2*
G
D
1087
4.887
−9.702
−52.418
1.00
30.88
RNA2
O


ATOM
3543
C1*
G
D
1087
4.196
−7.635
−53.412
1.00
31.58
RNA2
C


ATOM
3544
N9
G
D
1087
3.534
−6.370
−53.099
1.00
24.38
RNA2
N


ATOM
3545
C8
G
D
1087
2.184
−6.105
−53.015
1.00
13.22
RNA2
C


ATOM
3546
N7
G
D
1087
1.926
−4.837
−52.821
1.00
6.56
RNA2
N


ATOM
3547
C5
G
D
1087
3.176
−4.240
−52.743
1.00
11.78
RNA2
C


ATOM
3548
C6
G
D
1087
3.536
−2.887
−52.546
1.00
26.38
RNA2
C


ATOM
3549
O6
G
D
1087
2.796
−1.905
−52.394
1.00
28.30
RNA2
O


ATOM
3550
N1
G
D
1087
4.919
−2.723
−52.537
1.00
19.38
RNA2
N


ATOM
3551
C2
G
D
1087
5.836
−3.736
−52.697
1.00
26.46
RNA2
C


ATOM
3552
N2
G
D
1087
7.138
−3.390
−52.661
1.00
19.48
RNA2
N


ATOM
3553
N3
G
D
1087
5.509
−4.997
−52.881
1.00
20.61
RNA2
N


ATOM
3554
C4
G
D
1087
4.176
−5.176
−52.894
1.00
16.45
RNA2
C


ATOM
3555
P
A
D
1088
1.639
−11.888
−53.962
1.00
30.91
RNA2
P


ATOM
3556
O1P
A
D
1088
0.713
−11.203
−54.900
1.00
35.03
RNA2
O


ATOM
3557
O2P
A
D
1088
2.152
−13.234
−54.286
1.00
39.93
RNA2
O


ATOM
3558
O5*
A
D
1088
0.937
−11.965
−52.543
1.00
35.70
RNA2
O


ATOM
3559
C5*
A
D
1088
1.728
−12.195
−51.367
1.00
40.71
RNA2
C


ATOM
3560
C4*
A
D
1088
1.473
−11.114
−50.352
1.00
31.86
RNA2
C


ATOM
3561
O4*
A
D
1088
0.051
−11.035
−50.098
1.00
31.43
RNA2
O


ATOM
3562
C3*
A
D
1088
2.134
−11.354
−49.008
1.00
28.62
RNA2
C


ATOM
3563
O3*
A
D
1088
2.454
−10.092
−48.453
1.00
22.01
RNA2
O


ATOM
3564
C2*
A
D
1088
1.032
−12.007
−48.192
1.00
19.87
RNA2
C


ATOM
3565
O2*
A
D
1088
1.196
−11.783
−46.811
1.00
35.87
RNA2
O


ATOM
3566
C1*
A
D
1088
−0.209
−11.301
−48.739
1.00
17.80
RNA2
C


ATOM
3567
N9
A
D
1088
−1.421
−12.106
−48.687
1.00
8.11
RNA2
N


ATOM
3568
C8
A
D
1088
−2.654
−11.733
−48.221
1.00
11.14
RNA2
C


ATOM
3569
N7
A
D
1088
−3.559
−12.675
−48.317
1.00
26.75
RNA2
N


ATOM
3570
C5
A
D
1088
−2.873
−13.743
−48.883
1.00
15.31
RNA2
C


ATOM
3571
C6
A
D
1088
−3.272
−15.045
−49.241
1.00
15.70
RNA2
C


ATOM
3572
N6
A
D
1088
−4.511
−15.516
−49.067
1.00
17.72
RNA2
N


ATOM
3573
N1
A
D
1088
−2.343
−15.856
−49.789
1.00
9.16
RNA2
N


ATOM
3574
C2
A
D
1088
−1.099
−15.388
−49.957
1.00
14.79
RNA2
C


ATOM
3575
N3
A
D
1088
−0.603
−14.189
−49.657
1.00
18.20
RNA2
N


ATOM
3576
C4
A
D
1088
−1.555
−13.405
−49.117
1.00
14.12
RNA2
C


ATOM
3577
P
G
D
1089
3.501
−9.994
−47.248
1.00
27.70
RNA2
P


ATOM
3578
O1P
G
D
1089
4.147
−11.322
−47.068
1.00
28.27
RNA2
O


ATOM
3579
O2P
G
D
1089
2.776
−9.361
−46.117
1.00
25.52
RNA2
O


ATOM
3580
O5*
G
D
1089
4.606
−8.988
−47.785
1.00
22.53
RNA2
O


ATOM
3581
C5*
G
D
1089
5.471
−9.357
−48.871
1.00
30.86
RNA2
C


ATOM
3582
C4*
G
D
1089
5.959
−8.118
−49.573
1.00
24.73
RNA2
C


ATOM
3583
O4*
G
D
1089
4.810
−7.428
−50.122
1.00
31.53
RNA2
O


ATOM
3584
C3*
G
D
1089
6.676
−7.119
−48.676
1.00
23.96
RNA2
C


ATOM
3585
O3*
G
D
1089
7.692
−6.491
−49.437
1.00
35.59
RNA2
O


ATOM
3586
C2*
G
D
1089
5.581
−6.109
−48.333
1.00
26.26
RNA2
C


ATOM
3587
O2*
G
D
1089
6.055
−4.799
−48.099
1.00
39.73
RNA2
O


ATOM
3588
C1*
G
D
1089
4.742
−6.120
−49.602
1.00
26.61
RNA2
C


ATOM
3589
N9
G
D
1089
3.339
−5.773
−49.400
1.00
22.30
RNA2
N


ATOM
3590
C8
G
D
1089
2.265
−6.629
−49.311
1.00
19.61
RNA2
C


ATOM
3591
N7
G
D
1089
1.123
−6.007
−49.184
1.00
20.16
RNA2
N


ATOM
3592
C5
G
D
1089
1.468
−4.661
−49.171
1.00
20.55
RNA2
C


ATOM
3593
C6
G
D
1089
0.653
−3.505
−49.059
1.00
26.65
RNA2
C


ATOM
3594
O6
G
D
1089
−0.582
−3.435
−48.934
1.00
34.44
RNA2
O


ATOM
3595
N1
G
D
1089
1.415
−2.339
−49.098
1.00
18.23
RNA2
N


ATOM
3596
C2
G
D
1089
2.782
−2.292
−49.218
1.00
22.47
RNA2
C


ATOM
3597
N2
G
D
1089
3.341
−1.065
−49.215
1.00
23.99
RNA2
N


ATOM
3598
N3
G
D
1089
3.551
−3.365
−49.325
1.00
21.65
RNA2
N


ATOM
3599
C4
G
D
1089
2.832
−4.504
−49.293
1.00
15.76
RNA2
C


ATOM
3600
P
U
D
1090
9.177
−7.107
−49.459
1.00
46.88
RNA2
P


ATOM
3601
O1P
U
D
1090
9.375
−7.944
−48.246
1.00
47.63
RNA2
O


ATOM
3602
O2P
U
D
1090
9.376
−7.711
−50.800
1.00
46.50
RNA2
O


ATOM
3603
O5*
U
D
1090
10.098
−5.811
−49.333
1.00
47.06
RNA2
O


ATOM
3604
C5*
U
D
1090
11.428
−5.782
−49.876
1.00
48.58
RNA2
C


ATOM
3605
C4*
U
D
1090
12.040
−4.407
−49.703
1.00
55.86
RNA2
C


ATOM
3606
O4*
U
D
1090
11.307
−3.422
−50.482
1.00
58.42
RNA2
O


ATOM
3607
C3*
U
D
1090
12.027
−3.835
−48.296
1.00
57.85
RNA2
C


ATOM
3608
O3*
U
D
1090
13.074
−4.330
−47.488
1.00
54.72
RNA2
O


ATOM
3609
C2*
U
D
1090
12.152
−2.336
−48.538
1.00
56.90
RNA2
C


ATOM
3610
O2*
U
D
1090
13.486
−1.912
−48.750
1.00
55.53
RNA2
O


ATOM
3611
C1*
U
D
1090
11.345
−2.164
−49.823
1.00
47.41
RNA2
C


ATOM
3612
N1
U
D
1090
9.971
−1.713
−49.552
1.00
39.04
RNA2
N


ATOM
3613
C2
U
D
1090
9.769
−0.350
−49.369
1.00
41.49
RNA2
C


ATOM
3614
O2
U
D
1090
10.675
0.475
−49.415
1.00
47.92
RNA2
O


ATOM
3615
N3
U
D
1090
8.468
0.014
−49.123
1.00
33.29
RNA2
N


ATOM
3616
C4
U
D
1090
7.371
−0.820
−49.033
1.00
35.37
RNA2
C


ATOM
3617
O4
U
D
1090
6.255
−0.333
−48.820
1.00
43.33
RNA2
O


ATOM
3618
C5
U
D
1090
7.660
−2.210
−49.227
1.00
26.33
RNA2
C


ATOM
3619
C6
U
D
1090
8.916
−2.599
−49.476
1.00
31.79
RNA2
C


ATOM
3620
P
G
D
1091
12.865
−4.400
−45.899
1.00
63.03
RNA2
P


ATOM
3621
O1P
G
D
1091
11.489
−4.915
−45.629
1.00
48.47
RNA2
O


ATOM
3622
O2P
G
D
1091
14.047
−5.119
−45.346
1.00
63.48
RNA2
O


ATOM
3623
O5*
G
D
1091
12.909
−2.874
−45.434
1.00
53.82
RNA2
O


ATOM
3624
C5*
G
D
1091
14.160
−2.173
−45.369
1.00
60.37
RNA2
C


ATOM
3625
C4*
G
D
1091
13.939
−0.687
−45.231
1.00
57.35
RNA2
C


ATOM
3626
O4*
G
D
1091
13.057
−0.232
−46.291
1.00
51.52
RNA2
O


ATOM
3627
C3*
G
D
1091
13.275
−0.168
−43.964
1.00
64.14
RNA2
C


ATOM
3628
O3*
G
D
1091
14.165
−0.050
−42.851
1.00
71.95
RNA2
O


ATOM
3629
C2*
G
D
1091
12.766
1.197
−44.414
1.00
59.80
RNA2
C


ATOM
3630
O2*
G
D
1091
13.774
2.190
−44.402
1.00
67.83
RNA2
O


ATOM
3631
C1*
G
D
1091
12.345
0.913
−45.854
1.00
48.17
RNA2
C


ATOM
3632
N9
G
D
1091
10.912
0.647
−45.911
1.00
35.24
RNA2
N


ATOM
3633
C8
G
D
1091
10.281
−0.571
−45.991
1.00
35.20
RNA2
C


ATOM
3634
N7
G
D
1091
8.979
−0.474
−45.954
1.00
29.59
RNA2
N


ATOM
3635
C5
G
D
1091
8.739
0.890
−45.858
1.00
21.43
RNA2
C


ATOM
3636
C6
G
D
1091
7.518
1.604
−45.771
1.00
32.33
RNA2
C


ATOM
3637
O6
G
D
1091
6.364
1.159
−45.749
1.00
43.19
RNA2
O


ATOM
3638
N1
G
D
1091
7.731
2.976
−45.699
1.00
28.62
RNA2
N


ATOM
3639
C2
G
D
1091
8.961
3.582
−45.701
1.00
39.37
RNA2
C


ATOM
3640
N2
G
D
1091
8.965
4.920
−45.626
1.00
34.96
RNA2
N


ATOM
3641
N3
G
D
1091
10.107
2.925
−45.772
1.00
32.50
RNA2
N


ATOM
3642
C4
G
D
1091
9.920
1.594
−45.848
1.00
25.53
RNA2
C


ATOM
3643
P
C
D
1092
13.560
0.093
−41.358
1.00
80.57
RNA2
P


ATOM
3644
O1P
C
D
1092
12.499
−0.941
−41.171
1.00
72.16
RNA2
O


ATOM
3645
O2P
C
D
1092
14.702
0.146
−40.409
1.00
77.36
RNA2
O


ATOM
3646
O5*
C
D
1092
12.841
1.520
−41.356
1.00
67.00
RNA2
O


ATOM
3647
C5*
C
D
1092
13.608
2.728
−41.517
1.00
47.50
RNA2
C


ATOM
3648
C4*
C
D
1092
12.721
3.950
−41.413
1.00
46.89
RNA2
C


ATOM
3649
O4*
C
D
1092
11.785
3.999
−42.524
1.00
47.64
RNA2
O


ATOM
3650
C3*
C
D
1092
11.825
4.069
−40.193
1.00
48.58
RNA2
C


ATOM
3651
O3*
C
D
1092
12.485
4.523
−39.029
1.00
50.53
RNA2
O


ATOM
3652
C2*
C
D
1092
10.775
5.069
−40.650
1.00
46.94
RNA2
C


ATOM
3653
O2*
C
D
1092
11.196
6.411
−40.524
1.00
56.76
RNA2
O


ATOM
3654
C1*
C
D
1092
10.610
4.694
−42.122
1.00
44.37
RNA2
C


ATOM
3655
N1
C
D
1092
9.429
3.823
−42.282
1.00
40.91
RNA2
N


ATOM
3656
C2
C
D
1092
8.155
4.415
−42.217
1.00
43.01
RNA2
C


ATOM
3657
O2
C
D
1092
8.072
5.647
−42.083
1.00
41.14
RNA2
O


ATOM
3658
N3
C
D
1092
7.056
3.632
−42.298
1.00
33.92
RNA2
N


ATOM
3659
C4
C
D
1092
7.188
2.312
−42.444
1.00
39.14
RNA2
C


ATOM
3660
N4
C
D
1092
6.075
1.577
−42.496
1.00
35.85
RNA2
N


ATOM
3661
C5
C
D
1092
8.469
1.685
−42.538
1.00
31.59
RNA2
C


ATOM
3662
C6
C
D
1092
9.552
2.471
−42.458
1.00
35.03
RNA2
C


ATOM
3663
P
G
D
1093
11.977
4.012
−37.593
1.00
51.96
RNA2
P


ATOM
3664
O1P
G
D
1093
11.975
2.526
−37.626
1.00
48.41
RNA2
O


ATOM
3665
O2P
G
D
1093
12.764
4.724
−36.553
1.00
64.77
RNA2
O


ATOM
3666
O5*
G
D
1093
10.458
4.492
−37.515
1.00
35.20
RNA2
O


ATOM
3667
C5*
G
D
1093
10.122
5.886
−37.581
1.00
24.69
RNA2
C


ATOM
3668
C4*
G
D
1093
8.630
6.056
−37.704
1.00
29.37
RNA2
C


ATOM
3669
O4*
G
D
1093
8.164
5.435
−38.930
1.00
34.30
RNA2
O


ATOM
3670
C3*
G
D
1093
7.808
5.387
−36.620
1.00
33.91
RNA2
C


ATOM
3671
O3*
G
D
1093
7.738
6.175
−35.452
1.00
53.14
RNA2
O


ATOM
3672
C2*
G
D
1093
6.454
5.194
−37.289
1.00
36.57
RNA2
C


ATOM
3673
O2*
G
D
1093
5.628
6.344
−37.254
1.00
23.38
RNA2
O


ATOM
3674
C1*
G
D
1093
6.871
4.878
−38.726
1.00
33.38
RNA2
C


ATOM
3675
N9
G
D
1093
6.940
3.436
−38.961
1.00
31.32
RNA2
N


ATOM
3676
C8
G
D
1093
8.073
2.656
−39.054
1.00
27.97
RNA2
C


ATOM
3677
N7
G
D
1093
7.812
1.389
−39.243
1.00
30.70
RNA2
N


ATOM
3678
C5
G
D
1093
6.424
1.326
−39.280
1.00
27.66
RNA2
C


ATOM
3679
C6
G
D
1093
5.563
0.215
−39.451
1.00
30.04
RNA2
C


ATOM
3680
O6
G
D
1093
5.866
−0.977
−39.608
1.00
42.76
RNA2
O


ATOM
3681
N1
G
D
1093
4.222
0.596
−39.422
1.00
21.84
RNA2
N


ATOM
3682
C2
G
D
1093
3.770
1.881
−39.247
1.00
13.29
RNA2
C


ATOM
3683
N2
G
D
1093
2.437
2.046
−39.237
1.00
19.33
RNA2
N


ATOM
3684
N3
G
D
1093
4.564
2.926
−39.091
1.00
16.91
RNA2
N


ATOM
3685
C4
G
D
1093
5.869
2.579
−39.115
1.00
23.30
RNA2
C


ATOM
3686
P
U
D
1094
7.627
5.455
−34.022
1.00
46.64
RNA2
P


ATOM
3687
O1P
U
D
1094
8.556
4.303
−34.026
1.00
32.38
RNA2
O


ATOM
3688
O2P
U
D
1094
7.774
6.516
−32.989
1.00
56.93
RNA2
O


ATOM
3689
O5*
U
D
1094
6.124
4.934
−33.989
1.00
26.86
RNA2
O


ATOM
3690
C5*
U
D
1094
5.051
5.877
−33.932
1.00
35.20
RNA2
C


ATOM
3691
C4*
U
D
1094
3.735
5.172
−33.742
1.00
45.98
RNA2
C


ATOM
3692
O4*
U
D
1094
3.308
4.545
−34.978
1.00
50.88
RNA2
O


ATOM
3693
C3*
U
D
1094
3.692
4.055
−32.717
1.00
39.85
RNA2
C


ATOM
3694
O3*
U
D
1094
3.600
4.551
−31.387
1.00
48.03
RNA2
O


ATOM
3695
C2*
U
D
1094
2.457
3.270
−33.154
1.00
40.06
RNA2
C


ATOM
3696
O2*
U
D
1094
1.243
3.843
−32.701
1.00
44.52
RNA2
O


ATOM
3697
C1*
U
D
1094
2.527
3.400
−34.678
1.00
45.26
RNA2
C


ATOM
3698
N1
U
D
1094
3.134
2.217
−35.313
1.00
38.99
RNA2
N


ATOM
3699
C2
U
D
1094
2.294
1.148
−35.606
1.00
29.79
RNA2
C


ATOM
3700
O2
U
D
1094
1.083
1.180
−35.422
1.00
31.88
RNA2
O


ATOM
3701
N3
U
D
1094
2.920
0.043
−36.124
1.00
17.61
RNA2
N


ATOM
3702
C4
U
D
1094
4.262
−0.105
−36.384
1.00
31.42
RNA2
C


ATOM
3703
O4
U
D
1094
4.679
−1.193
−36.785
1.00
23.03
RNA2
O


ATOM
3704
C5
U
D
1094
5.062
1.053
−36.093
1.00
28.82
RNA2
C


ATOM
3705
C6
U
D
1094
4.485
2.147
−35.584
1.00
23.80
RNA2
C


ATOM
3706
P
A
D
1095
4.523
3.907
−30.234
1.00
43.63
RNA2
P


ATOM
3707
O1P
A
D
1095
5.870
3.607
−30.802
1.00
36.61
RNA2
O


ATOM
3708
O2P
A
D
1095
4.416
4.772
−29.033
1.00
64.56
RNA2
O


ATOM
3709
O5*
A
D
1095
3.794
2.535
−29.896
1.00
28.91
RNA2
O


ATOM
3710
C5*
A
D
1095
4.511
1.451
−29.281
1.00
29.01
RNA2
C


ATOM
3711
C4*
A
D
1095
3.579
0.291
−29.049
1.00
27.64
RNA2
C


ATOM
3712
O4*
A
D
1095
2.506
0.741
−28.191
1.00
38.10
RNA2
O


ATOM
3713
C3*
A
D
1095
2.890
−0.216
−30.302
1.00
32.19
RNA2
C


ATOM
3714
O3*
A
D
1095
3.698
−1.186
−30.964
1.00
40.82
RNA2
O


ATOM
3715
C2*
A
D
1095
1.575
−0.772
−29.769
1.00
37.08
RNA2
C


ATOM
3716
O2*
A
D
1095
1.705
−2.077
−29.240
1.00
37.59
RNA2
O


ATOM
3717
C1*
A
D
1095
1.278
0.195
−28.623
1.00
27.61
RNA2
C


ATOM
3718
N9
A
D
1095
0.397
1.313
−28.956
1.00
26.65
RNA2
N


ATOM
3719
C8
A
D
1095
0.753
2.601
−29.290
1.00
20.45
RNA2
C


ATOM
3720
N7
A
D
1095
−0.273
3.404
−29.463
1.00
27.16
RNA2
N


ATOM
3721
C5
A
D
1095
−1.376
2.587
−29.246
1.00
16.61
RNA2
C


ATOM
3722
C6
A
D
1095
−2.765
2.837
−29.271
1.00
25.70
RNA2
C


ATOM
3723
N6
A
D
1095
−3.303
4.034
−29.520
1.00
29.59
RNA2
N


ATOM
3724
N1
A
D
1095
−3.596
1.799
−29.023
1.00
28.34
RNA2
N


ATOM
3725
C2
A
D
1095
−3.060
0.599
−28.761
1.00
25.38
RNA2
C


ATOM
3726
N3
A
D
1095
−1.775
0.240
−28.702
1.00
28.20
RNA2
N


ATOM
3727
C4
A
D
1095
−0.977
1.292
−28.955
1.00
21.18
RNA2
C


ATOM
3728
P
A
D
1096
3.829
−1.151
−32.569
1.00
34.70
RNA2
P


ATOM
3729
O1P
A
D
1096
4.017
0.256
−32.992
1.00
37.33
RNA2
O


ATOM
3730
O2P
A
D
1096
4.838
−2.167
−32.962
1.00
24.34
RNA2
O


ATOM
3731
O5*
A
D
1096
2.383
−1.617
−33.047
1.00
20.77
RNA2
O


ATOM
3732
C5*
A
D
1096
1.913
−2.930
−32.724
1.00
19.81
RNA2
C


ATOM
3733
C4*
A
D
1096
0.421
−3.021
−32.910
1.00
22.36
RNA2
C


ATOM
3734
O4*
A
D
1096
−0.262
−2.200
−31.934
1.00
23.18
RNA2
O


ATOM
3735
C3*
A
D
1096
−0.119
−2.546
−34.243
1.00
23.44
RNA2
C


ATOM
3736
O3*
A
D
1096
0.028
−3.536
−35.249
1.00
37.12
RNA2
O


ATOM
3737
C2*
A
D
1096
−1.575
−2.237
−33.914
1.00
26.79
RNA2
C


ATOM
3738
O2*
A
D
1096
−2.392
−3.387
−33.889
1.00
29.84
RNA2
O


ATOM
3739
C1*
A
D
1096
−1.458
−1.686
−32.493
1.00
23.36
RNA2
C


ATOM
3740
N9
A
D
1096
−1.373
−0.228
−32.496
1.00
24.90
RNA2
N


ATOM
3741
C8
A
D
1096
−0.240
0.551
−32.560
1.00
30.09
RNA2
C


ATOM
3742
N7
A
D
1096
−0.485
1.838
−32.573
1.00
29.53
RNA2
N


ATOM
3743
C5
A
D
1096
−1.870
1.914
−32.507
1.00
21.47
RNA2
C


ATOM
3744
C6
A
D
1096
−2.751
3.005
−32.479
1.00
23.47
RNA2
C


ATOM
3745
N6
A
D
1096
−2.348
4.281
−32.511
1.00
30.56
RNA2
N


ATOM
3746
N1
A
D
1096
−4.075
2.741
−32.411
1.00
23.77
RNA2
N


ATOM
3747
C2
A
D
1096
−4.471
1.460
−32.368
1.00
24.81
RNA2
C


ATOM
3748
N3
A
D
1096
−3.736
0.349
−32.383
1.00
22.60
RNA2
N


ATOM
3749
C4
A
D
1096
−2.429
0.650
−32.454
1.00
13.49
RNA2
C


ATOM
3750
P
C
D
1097
0.158
−3.087
−36.781
1.00
28.43
RNA2
P


ATOM
3751
O1P
C
D
1097
1.274
−2.107
−36.889
1.00
25.96
RNA2
O


ATOM
3752
O2P
C
D
1097
0.208
−4.341
−37.575
1.00
39.67
RNA2
O


ATOM
3753
O5*
C
D
1097
−1.234
−2.357
−37.037
1.00
17.23
RNA2
O


ATOM
3754
C5*
C
D
1097
−1.317
−1.078
−37.691
1.00
20.94
RNA2
C


ATOM
3755
C4*
C
D
1097
−2.742
−0.584
−37.636
1.00
29.32
RNA2
C


ATOM
3756
O4*
C
D
1097
−3.029
−0.045
−36.315
1.00
40.36
RNA2
O


ATOM
3757
C3*
C
D
1097
−3.106
0.550
−38.569
1.00
29.37
RNA2
C


ATOM
3758
O3*
C
D
1097
−3.388
0.082
−39.870
1.00
44.58
RNA2
O


ATOM
3759
C2*
C
D
1097
−4.341
1.126
−37.895
1.00
33.92
RNA2
C


ATOM
3760
O2*
C
D
1097
−5.487
0.330
−38.113
1.00
32.32
RNA2
O


ATOM
3761
C1*
C
D
1097
−3.945
1.037
−36.423
1.00
34.10
RNA2
C


ATOM
3762
N1
C
D
1097
−3.265
2.289
−36.012
1.00
31.44
RNA2
N


ATOM
3763
C2
C
D
1097
−4.047
3.417
−35.683
1.00
27.94
RNA2
C


ATOM
3764
O2
C
D
1097
−5.285
3.313
−35.669
1.00
29.21
RNA2
O


ATOM
3765
N3
C
D
1097
−3.427
4.588
−35.390
1.00
30.98
RNA2
N


ATOM
3766
C4
C
D
1097
−2.090
4.658
−35.404
1.00
44.95
RNA2
C


ATOM
3767
N4
C
D
1097
−1.519
5.838
−35.133
1.00
50.64
RNA2
N


ATOM
3768
C5
C
D
1097
−1.275
3.522
−35.698
1.00
39.09
RNA2
C


ATOM
3769
C6
C
D
1097
−1.897
2.370
−35.988
1.00
32.35
RNA2
C


ATOM
3770
P
A
D
1098
−2.688
0.785
−41.132
1.00
43.71
RNA2
P


ATOM
3771
O1P
A
D
1098
−1.216
0.563
−41.059
1.00
24.08
RNA2
O


ATOM
3772
O2P
A
D
1098
−3.449
0.343
−42.334
1.00
56.53
RNA2
O


ATOM
3773
O5*
A
D
1098
−2.952
2.337
−40.908
1.00
42.07
RNA2
O


ATOM
3774
C5*
A
D
1098
−4.281
2.842
−40.702
1.00
41.90
RNA2
C


ATOM
3775
C4*
A
D
1098
−4.225
4.295
−40.292
1.00
49.33
RNA2
C


ATOM
3776
O4*
A
D
1098
−3.523
4.414
−39.025
1.00
47.73
RNA2
O


ATOM
3777
C3*
A
D
1098
−3.462
5.219
−41.229
1.00
50.90
RNA2
C


ATOM
3778
O3*
A
D
1098
−4.263
5.645
−42.324
1.00
54.47
RNA2
O


ATOM
3779
C2*
A
D
1098
−3.057
6.363
−40.303
1.00
47.39
RNA2
C


ATOM
3780
O2*
A
D
1098
−4.104
7.289
−40.085
1.00
53.57
RNA2
O


ATOM
3781
C1*
A
D
1098
−2.781
5.621
−38.995
1.00
36.88
RNA2
C


ATOM
3782
N9
A
D
1098
−1.365
5.289
−38.851
1.00
28.68
RNA2
N


ATOM
3783
C8
A
D
1098
−0.744
4.078
−39.051
1.00
36.76
RNA2
C


ATOM
3784
N7
A
D
1098
0.560
4.120
−38.906
1.00
27.01
RNA2
N


ATOM
3785
C5
A
D
1098
0.813
5.442
−38.575
1.00
32.11
RNA2
C


ATOM
3786
C6
A
D
1098
2.004
6.136
−38.311
1.00
39.08
RNA2
C


ATOM
3787
N6
A
D
1098
3.217
5.578
−38.364
1.00
35.79
RNA2
N


ATOM
3788
N1
A
D
1098
1.907
7.447
−37.996
1.00
37.08
RNA2
N


ATOM
3789
C2
A
D
1098
0.692
8.013
−37.969
1.00
35.02
RNA2
C


ATOM
3790
N3
A
D
1098
−0.498
7.470
−38.214
1.00
31.17
RNA2
N


ATOM
3791
C4
A
D
1098
−0.366
6.169
−38.516
1.00
35.12
RNA2
C


ATOM
3792
P
G
D
1099
−3.598
5.799
−43.783
1.00
57.31
RNA2
P


ATOM
3793
O1P
G
D
1099
−3.062
4.481
−44.215
1.00
60.32
RNA2
O


ATOM
3794
O2P
G
D
1099
−4.589
6.508
−44.640
1.00
60.85
RNA2
O


ATOM
3795
O5*
G
D
1099
−2.349
6.753
−43.537
1.00
41.11
RNA2
O


ATOM
3796
C5*
G
D
1099
−2.543
8.130
−43.169
1.00
50.07
RNA2
C


ATOM
3797
C4*
G
D
1099
−1.216
8.782
−42.888
1.00
47.05
RNA2
C


ATOM
3798
O4*
G
D
1099
−0.626
8.173
−41.712
1.00
46.92
RNA2
O


ATOM
3799
C3*
G
D
1099
−0.174
8.588
−43.975
1.00
54.47
RNA2
C


ATOM
3800
O3*
G
D
1099
−0.305
9.517
−45.036
1.00
55.05
RNA2
O


ATOM
3801
C2*
G
D
1099
1.139
8.720
−43.217
1.00
48.61
RNA2
C


ATOM
3802
O2*
G
D
1099
1.553
10.057
−43.029
1.00
55.32
RNA2
O


ATOM
3803
C1*
G
D
1099
0.781
8.073
−41.878
1.00
40.34
RNA2
C


ATOM
3804
N9
G
D
1099
1.140
6.659
−41.891
1.00
34.55
RNA2
N


ATOM
3805
C8
G
D
1099
0.293
5.577
−41.965
1.00
33.18
RNA2
C


ATOM
3806
N7
G
D
1099
0.926
4.437
−42.047
1.00
37.87
RNA2
N


ATOM
3807
C5
G
D
1099
2.270
4.787
−42.007
1.00
28.79
RNA2
C


ATOM
3808
C6
G
D
1099
3.437
3.978
−42.083
1.00
36.73
RNA2
C


ATOM
3809
O6
G
D
1099
3.519
2.747
−42.210
1.00
46.32
RNA2
O


ATOM
3810
N1
G
D
1099
4.596
4.744
−42.006
1.00
30.92
RNA2
N


ATOM
3811
C2
G
D
1099
4.630
6.113
−41.873
1.00
40.47
RNA2
C


ATOM
3812
N2
G
D
1099
5.847
6.678
−41.812
1.00
23.42
RNA2
N


ATOM
3813
N3
G
D
1099
3.549
6.876
−41.805
1.00
31.10
RNA2
N


ATOM
3814
C4
G
D
1099
2.415
6.152
−41.883
1.00
28.17
RNA2
C


ATOM
3815
P
C
D
1100
0.097
9.071
−46.522
1.00
56.56
RNA2
P


ATOM
3816
O1P
C
D
1100
−0.323
7.657
−46.716
1.00
63.87
RNA2
O


ATOM
3817
O2P
C
D
1100
−0.407
10.115
−47.447
1.00
69.36
RNA2
O


ATOM
3818
O5*
C
D
1100
1.688
9.106
−46.507
1.00
39.12
RNA2
O


ATOM
3819
C5*
C
D
1100
2.380
10.337
−46.298
1.00
32.71
RNA2
C


ATOM
3820
C4*
C
D
1100
3.863
10.098
−46.207
1.00
40.37
RNA2
C


ATOM
3821
O4*
C
D
1100
4.155
9.281
−45.042
1.00
45.57
RNA2
O


ATOM
3822
C3*
C
D
1100
4.502
9.335
−47.356
1.00
48.34
RNA2
C


ATOM
3823
O3*
C
D
1100
4.774
10.136
−48.495
1.00
58.69
RNA2
O


ATOM
3824
C2*
C
D
1100
5.771
8.784
−46.718
1.00
42.72
RNA2
C


ATOM
3825
O2*
C
D
1100
6.840
9.707
−46.670
1.00
45.27
RNA2
O


ATOM
3826
C1*
C
D
1100
5.289
8.466
−45.303
1.00
36.28
RNA2
C


ATOM
3827
N1
C
D
1100
4.897
7.048
−45.234
1.00
33.17
RNA2
N


ATOM
3828
C2
C
D
1100
5.910
6.083
−45.177
1.00
37.72
RNA2
C


ATOM
3829
O2
C
D
1100
7.090
6.461
−45.104
1.00
37.78
RNA2
O


ATOM
3830
N3
C
D
1100
5.582
4.772
−45.201
1.00
34.10
RNA2
N


ATOM
3831
C4
C
D
1100
4.299
4.409
−45.268
1.00
36.21
RNA2
C


ATOM
3832
N4
C
D
1100
4.024
3.103
−45.330
1.00
35.52
RNA2
N


ATOM
3833
C5
C
D
1100
3.242
5.369
−45.283
1.00
32.04
RNA2
C


ATOM
3834
C6
C
D
1100
3.583
6.665
−45.263
1.00
33.05
RNA2
C


ATOM
3835
P
U
D
1101
4.754
9.460
−49.951
1.00
59.64
RNA2
P


ATOM
3836
O1P
U
D
1101
3.464
8.731
−50.077
1.00
53.79
RNA2
O


ATOM
3837
O2P
U
D
1101
5.117
10.490
−50.957
1.00
73.54
RNA2
O


ATOM
3838
O5*
U
D
1101
5.931
8.390
−49.894
1.00
44.03
RNA2
O


ATOM
3839
C5*
U
D
1101
7.275
8.809
−49.652
1.00
37.19
RNA2
C


ATOM
3840
C4*
U
D
1101
8.197
7.620
−49.625
1.00
44.44
RNA2
C


ATOM
3841
O4*
U
D
1101
7.844
6.748
−48.520
1.00
47.50
RNA2
O


ATOM
3842
C3*
U
D
1101
8.140
6.710
−50.836
1.00
49.53
RNA2
C


ATOM
3843
O3*
U
D
1101
8.892
7.203
−51.930
1.00
55.95
RNA2
O


ATOM
3844
C2*
U
D
1101
8.681
5.396
−50.286
1.00
46.03
RNA2
C


ATOM
3845
O2*
U
D
1101
10.091
5.371
−50.196
1.00
46.23
RNA2
O


ATOM
3846
C1*
U
D
1101
8.097
5.396
−48.875
1.00
41.37
RNA2
C


ATOM
3847
N1
U
D
1101
6.840
4.627
−48.800
1.00
33.41
RNA2
N


ATOM
3848
C2
U
D
1101
6.935
3.238
−48.784
1.00
34.44
RNA2
C


ATOM
3849
O2
U
D
1101
8.011
2.640
−48.812
1.00
33.60
RNA2
O


ATOM
3850
N3
U
D
1101
5.730
2.575
−48.737
1.00
17.93
RNA2
N


ATOM
3851
C4
U
D
1101
4.466
3.143
−48.705
1.00
36.01
RNA2
C


ATOM
3852
O4
U
D
1101
3.465
2.411
−48.702
1.00
25.00
RNA2
O


ATOM
3853
C5
U
D
1101
4.457
4.577
−48.714
1.00
24.85
RNA2
C


ATOM
3854
C6
U
D
1101
5.610
5.251
−48.760
1.00
26.88
RNA2
C


ATOM
3855
P
C
D
1102
8.485
6.763
−53.418
1.00
41.89
RNA2
P


ATOM
3856
O1P
C
D
1102
7.001
6.821
−53.510
1.00
43.20
RNA2
O


ATOM
3857
O2P
C
D
1102
9.312
7.542
−54.372
1.00
53.94
RNA2
O


ATOM
3858
O5*
C
D
1102
8.938
5.240
−53.483
1.00
38.14
RNA2
O


ATOM
3859
C5*
C
D
1102
10.317
4.889
−53.306
1.00
37.05
RNA2
C


ATOM
3860
C4*
C
D
1102
10.494
3.390
−53.332
1.00
45.27
RNA2
C


ATOM
3861
O4*
C
D
1102
9.855
2.793
−52.168
1.00
52.28
RNA2
O


ATOM
3862
C3*
C
D
1102
9.872
2.637
−54.498
1.00
54.50
RNA2
C


ATOM
3863
O3*
C
D
1102
10.597
2.706
−55.716
1.00
57.12
RNA2
O


ATOM
3864
C2*
C
D
1102
9.784
1.219
−53.949
1.00
52.66
RNA2
C


ATOM
3865
O2*
C
D
1102
11.017
0.522
−54.000
1.00
56.57
RNA2
O


ATOM
3866
C1*
C
D
1102
9.401
1.482
−52.493
1.00
46.15
RNA2
C


ATOM
3867
N1
C
D
1102
7.932
1.399
−52.330
1.00
28.20
RNA2
N


ATOM
3868
C2
C
D
1102
7.331
0.128
−52.307
1.00
22.69
RNA2
C


ATOM
3869
O2
C
D
1102
8.053
−0.881
−52.366
1.00
35.31
RNA2
O


ATOM
3870
N3
C
D
1102
5.988
0.028
−52.219
1.00
9.49
RNA2
N


ATOM
3871
C4
C
D
1102
5.246
1.129
−52.135
1.00
16.43
RNA2
C


ATOM
3872
N4
C
D
1102
3.922
0.979
−52.052
1.00
15.53
RNA2
N


ATOM
3873
C5
C
D
1102
5.825
2.433
−52.133
1.00
15.77
RNA2
C


ATOM
3874
C6
C
D
1102
7.158
2.521
−52.229
1.00
21.76
RNA2
C


ATOM
3875
P
A
D
1103
9.806
2.525
−57.105
1.00
47.42
RNA2
P


ATOM
3876
O1P
A
D
1103
8.514
3.264
−57.011
1.00
38.37
RNA2
O


ATOM
3877
O2P
A
D
1103
10.747
2.818
−58.216
1.00
57.18
RNA2
O


ATOM
3878
O5*
A
D
1103
9.456
0.974
−57.138
1.00
48.19
RNA2
O


ATOM
3879
C5*
A
D
1103
10.493
−0.015
−56.995
1.00
51.39
RNA2
C


ATOM
3880
C4*
A
D
1103
9.894
−1.397
−56.965
1.00
45.50
RNA2
C


ATOM
3881
O4*
A
D
1103
8.978
−1.488
−55.847
1.00
45.01
RNA2
O


ATOM
3882
C3*
A
D
1103
9.053
−1.764
−58.178
1.00
51.96
RNA2
C


ATOM
3883
O3*
A
D
1103
9.867
−2.246
−59.243
1.00
53.83
RNA2
O


ATOM
3884
C2*
A
D
1103
8.095
−2.817
−57.622
1.00
48.46
RNA2
C


ATOM
3885
O2*
A
D
1103
8.635
−4.125
−57.578
1.00
47.52
RNA2
O


ATOM
3886
C1*
A
D
1103
7.882
−2.316
−56.192
1.00
43.28
RNA2
C


ATOM
3887
N9
A
D
1103
6.646
−1.549
−56.032
1.00
30.89
RNA2
N


ATOM
3888
C8
A
D
1103
6.477
−0.189
−55.914
1.00
25.35
RNA2
C


ATOM
3889
N7
A
D
1103
5.222
0.179
−55.797
1.00
26.03
RNA2
N


ATOM
3890
C5
A
D
1103
4.519
−1.019
−55.836
1.00
17.17
RNA2
C


ATOM
3891
C6
A
D
1103
3.149
−1.314
−55.759
1.00
19.87
RNA2
C


ATOM
3892
N6
A
D
1103
2.193
−0.387
−55.623
1.00
16.79
RNA2
N


ATOM
3893
N1
A
D
1103
2.784
−2.616
−55.828
1.00
26.16
RNA2
N


ATOM
3894
C2
A
D
1103
3.737
−3.548
−55.965
1.00
23.04
RNA2
C


ATOM
3895
N3
A
D
1103
5.055
−3.394
−56.049
1.00
30.58
RNA2
N


ATOM
3896
C4
A
D
1103
5.384
−2.090
−55.977
1.00
28.62
RNA2
C


ATOM
3897
P
C
D
1104
9.699
−1.627
−60.718
1.00
44.57
RNA2
P


ATOM
3898
O1P
C
D
1104
9.942
−0.162
−60.644
1.00
47.15
RNA2
O


ATOM
3899
O2P
C
D
1104
10.506
−2.463
−61.648
1.00
47.11
RNA2
O


ATOM
3900
O5*
C
D
1104
8.160
−1.850
−61.042
1.00
36.26
RNA2
O


ATOM
3901
C5*
C
D
1104
7.642
−3.172
−61.211
1.00
34.08
RNA2
C


ATOM
3902
C4*
C
D
1104
6.144
−3.130
−61.321
1.00
33.02
RNA2
C


ATOM
3903
O4*
C
D
1104
5.569
−2.739
−60.048
1.00
35.45
RNA2
O


ATOM
3904
C3*
C
D
1104
5.595
−2.113
−62.301
1.00
36.26
RNA2
C


ATOM
3905
O3*
C
D
1104
5.633
−2.561
−63.643
1.00
42.96
RNA2
O


ATOM
3906
C2*
C
D
1104
4.183
−1.890
−61.780
1.00
35.20
RNA2
C


ATOM
3907
O2*
C
D
1104
3.297
−2.916
−62.185
1.00
38.85
RNA2
O


ATOM
3908
C1*
C
D
1104
4.408
−1.952
−60.268
1.00
31.46
RNA2
C


ATOM
3909
N1
C
D
1104
4.636
−0.606
−59.702
1.00
26.13
RNA2
N


ATOM
3910
C2
C
D
1104
3.528
0.178
−59.334
1.00
24.36
RNA2
C


ATOM
3911
O2
C
D
1104
2.386
−0.295
−59.447
1.00
21.42
RNA2
O


ATOM
3912
N3
C
D
1104
3.735
1.428
−58.865
1.00
27.00
RNA2
N


ATOM
3913
C4
C
D
1104
4.981
1.900
−58.745
1.00
31.66
RNA2
C


ATOM
3914
N4
C
D
1104
5.140
3.147
−58.292
1.00
37.50
RNA2
N


ATOM
3915
C5
C
D
1104
6.120
1.119
−59.087
1.00
19.85
RNA2
C


ATOM
3916
C6
C
D
1104
5.906
−0.115
−59.554
1.00
26.62
RNA2
C


ATOM
3917
P
C
D
1105
5.825
−1.489
−64.826
1.00
42.78
RNA2
P


ATOM
3918
O1P
C
D
1105
6.805
−0.460
−64.381
1.00
36.29
RNA2
O


ATOM
3919
O2P
C
D
1105
6.074
−2.246
−66.084
1.00
51.04
RNA2
O


ATOM
3920
O5*
C
D
1105
4.397
−0.802
−64.932
1.00
18.59
RNA2
O


ATOM
3921
C5*
C
D
1105
3.253
−1.574
−65.316
1.00
29.02
RNA2
C


ATOM
3922
C4*
C
D
1105
2.021
−0.711
−65.320
1.00
36.00
RNA2
C


ATOM
3923
O4*
C
D
1105
1.741
−0.275
−63.965
1.00
45.01
RNA2
O


ATOM
3924
C3*
C
D
1105
2.122
0.582
−66.111
1.00
43.97
RNA2
C


ATOM
3925
O3*
C
D
1105
1.919
0.405
−67.505
1.00
50.57
RNA2
O


ATOM
3926
C2*
C
D
1105
1.060
1.451
−65.447
1.00
42.61
RNA2
C


ATOM
3927
O2*
C
D
1105
−0.259
1.147
−65.873
1.00
33.02
RNA2
O


ATOM
3928
C1*
C
D
1105
1.225
1.048
−63.983
1.00
40.14
RNA2
C


ATOM
3929
N1
C
D
1105
2.173
1.938
−63.273
1.00
34.85
RNA2
N


ATOM
3930
C2
C
D
1105
1.704
3.161
−62.765
1.00
30.45
RNA2
C


ATOM
3931
O2
C
D
1105
0.516
3.473
−62.939
1.00
29.26
RNA2
O


ATOM
3932
N3
C
D
1105
2.558
3.975
−62.106
1.00
32.19
RNA2
N


ATOM
3933
C4
C
D
1105
3.836
3.622
−61.956
1.00
39.46
RNA2
C


ATOM
3934
N4
C
D
1105
4.644
4.466
−61.298
1.00
41.48
RNA2
N


ATOM
3935
C5
C
D
1105
4.346
2.391
−62.471
1.00
36.86
RNA2
C


ATOM
3936
C6
C
D
1105
3.488
1.587
−63.114
1.00
34.30
RNA2
C


ATOM
3937
P
A
D
1106
2.559
1.463
−68.538
1.00
47.42
RNA2
P


ATOM
3938
O1P
A
D
1106
3.960
1.743
−68.117
1.00
33.03
RNA2
O


ATOM
3939
O2P
A
D
1106
2.297
0.944
−69.905
1.00
51.03
RNA2
O


ATOM
3940
O5*
A
D
1106
1.674
2.772
−68.323
1.00
38.12
RNA2
O


ATOM
3941
C5*
A
D
1106
0.283
2.777
−68.706
1.00
43.96
RNA2
C


ATOM
3942
C4*
A
D
1106
−0.340
4.129
−68.452
1.00
51.41
RNA2
C


ATOM
3943
O4*
A
D
1106
−0.379
4.381
−67.026
1.00
57.25
RNA2
O


ATOM
3944
C3*
A
D
1106
0.391
5.331
−69.029
1.00
56.31
RNA2
C


ATOM
3945
O3*
A
D
1106
0.086
5.559
−70.396
1.00
55.12
RNA2
O


ATOM
3946
C2*
A
D
1106
−0.076
6.467
−68.126
1.00
56.95
RNA2
C


ATOM
3947
O2*
A
D
1106
−1.351
6.970
−68.478
1.00
57.32
RNA2
O


ATOM
3948
C1*
A
D
1106
−0.169
5.761
−66.776
1.00
49.81
RNA2
C


ATOM
3949
N9
A
D
1106
1.065
5.896
−66.003
1.00
39.90
RNA2
N


ATOM
3950
C8
A
D
1106
2.098
4.994
−65.902
1.00
41.00
RNA2
C


ATOM
3951
N7
A
D
1106
3.070
5.388
−65.116
1.00
41.71
RNA2
N


ATOM
3952
C5
A
D
1106
2.652
6.635
−64.672
1.00
37.31
RNA2
C


ATOM
3953
C6
A
D
1106
3.238
7.572
−63.805
1.00
36.44
RNA2
C


ATOM
3954
N6
A
D
1106
4.419
7.389
−63.208
1.00
40.12
RNA2
N


ATOM
3955
N1
A
D
1106
2.563
8.720
−63.570
1.00
38.29
RNA2
N


ATOM
3956
C2
A
D
1106
1.380
8.904
−64.178
1.00
37.00
RNA2
C


ATOM
3957
N3
A
D
1106
0.726
8.097
−65.014
1.00
37.07
RNA2
N


ATOM
3958
C4
A
D
1106
1.423
6.965
−65.219
1.00
37.01
RNA2
C


ATOM
3959
P
G
D
1107
1.186
6.251
−71.341
1.00
60.89
RNA2
P


ATOM
3960
O1P
G
D
1107
2.513
5.650
−71.037
1.00
51.64
RNA2
O


ATOM
3961
O2P
G
D
1107
0.665
6.218
−72.732
1.00
66.72
RNA2
O


ATOM
3962
O5*
G
D
1107
1.226
7.763
−70.838
1.00
59.43
RNA2
O


ATOM
3963
C5*
G
D
1107
0.098
8.639
−71.043
1.00
70.93
RNA2
C


ATOM
3964
C4*
G
D
1107
0.341
9.984
−70.392
1.00
70.62
RNA2
C


ATOM
3965
O4*
G
D
1107
0.347
9.841
−68.945
1.00
70.80
RNA2
O


ATOM
3966
C3*
G
D
1107
1.673
10.648
−70.701
1.00
69.85
RNA2
C


ATOM
3967
O3*
G
D
1107
1.703
11.337
−71.937
1.00
68.76
RNA2
O


ATOM
3968
C2*
G
D
1107
1.852
11.589
−69.519
1.00
71.85
RNA2
C


ATOM
3969
O2*
G
D
1107
1.134
12.799
−69.666
1.00
74.63
RNA2
O


ATOM
3970
C1*
G
D
1107
1.278
10.751
−68.377
1.00
66.31
RNA2
C


ATOM
3971
N9
G
D
1107
2.356
9.990
−67.753
1.00
61.03
RNA2
N


ATOM
3972
C8
G
D
1107
2.765
8.710
−68.056
1.00
64.56
RNA2
C


ATOM
3973
N7
G
D
1107
3.811
8.330
−67.371
1.00
62.08
RNA2
N


ATOM
3974
C5
G
D
1107
4.100
9.417
−66.555
1.00
59.12
RNA2
C


ATOM
3975
C6
G
D
1107
5.134
9.600
−65.598
1.00
54.80
RNA2
C


ATOM
3976
O6
G
D
1107
6.035
8.812
−65.270
1.00
51.34
RNA2
O


ATOM
3977
N1
G
D
1107
5.056
10.854
−65.001
1.00
50.79
RNA2
N


ATOM
3978
C2
G
D
1107
4.109
11.810
−65.287
1.00
54.33
RNA2
C


ATOM
3979
N2
G
D
1107
4.199
12.959
−64.606
1.00
51.64
RNA2
N


ATOM
3980
N3
G
D
1107
3.146
11.653
−66.176
1.00
49.03
RNA2
N


ATOM
3981
C4
G
D
1107
3.201
10.443
−66.769
1.00
58.09
RNA2
C


ATOM
3982
P
C
D
1108
3.118
11.599
−72.654
1.00
71.56
RNA2
P


ATOM
3983
O1P
C
D
1108
3.923
10.353
−72.579
1.00
60.79
RNA2
O


ATOM
3984
O2P
C
D
1108
2.828
12.209
−73.977
1.00
78.78
RNA2
O


ATOM
3985
O5*
C
D
1108
3.837
12.677
−71.723
1.00
69.28
RNA2
O


ATOM
3986
C5*
C
D
1108
3.274
13.992
−71.536
1.00
65.61
RNA2
C


ATOM
3987
C4*
C
D
1108
4.139
14.809
−70.605
1.00
60.04
RNA2
C


ATOM
3988
O4*
C
D
1108
4.193
14.171
−69.304
1.00
61.74
RNA2
O


ATOM
3989
C3*
C
D
1108
5.598
14.965
−71.001
1.00
60.53
RNA2
C


ATOM
3990
O3*
C
D
1108
5.901
15.783
−72.134
1.00
66.71
RNA2
O


ATOM
3991
C2*
C
D
1108
6.282
15.272
−69.677
1.00
63.96
RNA2
C


ATOM
3992
O2*
C
D
1108
6.155
16.631
−69.306
1.00
69.72
RNA2
O


ATOM
3993
C1*
C
D
1108
5.457
14.420
−68.706
1.00
64.54
RNA2
C


ATOM
3994
N1
C
D
1108
6.098
13.130
−68.372
1.00
61.20
RNA2
N


ATOM
3995
C2
C
D
1108
7.127
13.116
−67.417
1.00
59.89
RNA2
C


ATOM
3996
O2
C
D
1108
7.454
14.179
−66.867
1.00
54.39
RNA2
O


ATOM
3997
N3
C
D
1108
7.739
11.946
−67.119
1.00
60.31
RNA2
N


ATOM
3998
C4
C
D
1108
7.359
10.821
−67.728
1.00
62.68
RNA2
C


ATOM
3999
N4
C
D
1108
7.999
9.689
−67.411
1.00
63.03
RNA2
N


ATOM
4000
C5
C
D
1108
6.308
10.803
−68.693
1.00
64.65
RNA2
C


ATOM
4001
C6
C
D
1108
5.711
11.968
−68.982
1.00
64.25
RNA2
C


TER
4002

C
D
1108


HETATM
4003
CD
CD

201
4.250
−2.291
−5.735
0.91
77.47
CD


HETATM
4004
CD
CD

202
5.716
1.827
1.431
0.91
32.35
CD


HETATM
4005
O
HOH

205
7.540
−4.792
−0.436
1.00
19.29
O


HETATM
4006
O
HOH

209
8.097
9.026
−9.315
1.00
27.99
O


HETATM
4007
MG
MG

210
7.174
1.073
−14.750
1.00
31.99
MG


HETATM
4008
CD
CD

211
3.380
6.488
−27.905
0.91
47.98
CD


HETATM
4009
O
HOH

213
−0.304
4.175
−0.867
1.00
38.63
O


HETATM
4010
MG
MG

214
−17.505
21.323
11.148
1.00
36.28
MG


HETATM
4011
MG
MG

215
−1.702
7.910
−11.196
1.00
23.07
MG


HETATM
4012
O
HOH

216
−3.510
9.209
−16.056
1.00
43.93
O


HETATM
4013
O
HOH

217
−4.416
−0.858
−2.563
1.00
53.29
O


HETATM
4014
O
HOH

218
6.288
−5.327
−3.385
1.00
23.44
O


HETATM
4015
O
HOH

221
−1.778
1.682
−3.132
1.00
35.80
O


HETATM
4016
O
HOH

222
−6.849
10.117
−5.442
1.00
24.81
O


HETATM
4017
MG
MG

223
14.749
−5.902
12.250
1.00
36.97
MG


HETATM
4018
MG
MG

225
19.765
−8.266
10.030
1.00
41.29
MG


HETATM
4019
MG
MG

226
4.983
5.583
−14.224
1.00
17.24
MG


HETATM
4020
HG
HG

227
10.163
10.934
−4.731
0.10
21.14
HG


HETATM
4021
MG
MG

228
0.368
−4.197
15.065
1.00
49.67
MG


HETATM
4022
HG
HG

230
−4.955
2.266
−15.287
0.41
65.01
HG


HETATM
4023
O
HOH

232
17.184
−8.123
12.078
1.00
46.90
O


HETATM
4024
O
HOH

233
5.132
−9.156
11.493
1.00
39.77
O


HETATM
4025
O
HOH

235
−2.182
2.520
−0.424
1.00
32.75
O


HETATM
4026
O
HOH

236
3.337
3.950
−2.832
1.00
22.74
O


HETATM
4027
O
HOH

237
−0.294
3.992
−4.949
1.00
41.19
O


HETATM
4028
O
HOH

238
3.987
7.706
−7.271
1.00
22.33
O


HETATM
4029
O
HOH

239
−2.682
1.061
−25.220
1.00
28.52
O


HETATM
4030
O
HOH

241
−0.901
−1.716
11.637
1.00
34.24
O


HETATM
4031
O
HOH

243
13.905
−12.456
1.182
1.00
61.18
O


HETATM
4032
O
HOH

244
−6.595
6.151
4.226
1.00
33.67
O


HETATM
4033
O
HOH

245
−10.614
11.084
18.691
1.00
47.29
O


HETATM
4034
O
HOH

246
2.153
6.645
−5.263
1.00
42.17
O


HETATM
4035
O
HOH

254
1.596
7.517
−28.596
1.00
20.43
O


HETATM
4036
O
HOH

255
5.496
5.982
−27.129
1.00
15.56
O


HETATM
4037
O
HOH

256
5.082
7.342
−29.082
1.00
15.30
O


HETATM
4038
MG
MG

257
4.272
8.284
−11.053
1.00
18.63
MG


HETATM
4039
O
HOH

258
5.759
9.095
−9.332
1.00
22.95
O


HETATM
4040
O
HOH

259
5.439
8.750
−13.001
1.00
29.22
O


HETATM
4041
O
HOH

260
3.112
6.893
−9.834
1.00
15.63
O


HETATM
4042
O
HOH

261
2.565
9.752
−11.319
1.00
21.45
O


HETATM
4043
O
HOH

262
2.003
−1.889
−6.293
1.00
39.08
O


HETATM
4044
O
HOH

263
6.523
−2.887
−3.470
1.00
31.47
O


HETATM
4045
O
HOH

264
5.691
−4.152
−6.413
1.00
49.36
O


HETATM
4046
O
HOH

265
13.164
−1.037
−13.541
1.00
53.81
O


HETATM
4047
O
HOH

266
1.658
−4.440
−6.534
1.00
54.55
O


HETATM
4048
O
HOH

267
4.147
−0.985
−10.097
1.00
21.21
O


HETATM
4049
O
HOH

268
7.729
0.998
−17.041
1.00
32.76
O


HETATM
4050
O
HOH

269
9.473
0.412
−15.439
1.00
22.86
O


HETATM
4051
O
HOH

270
5.281
1.436
−15.928
1.00
30.01
O


HETATM
4052
O
HOH

271
5.086
−1.392
−12.878
1.00
29.98
O


HETATM
4053
O
HOH

272
5.284
18.973
−15.526
1.00
29.56
O


HETATM
4054
MG
MG

273
5.268
8.632
9.371
1.00
35.80
MG


HETATM
4055
O
HOH

274
4.009
8.265
7.258
1.00
21.81
O


HETATM
4056
O
HOH

275
6.536
8.905
7.475
1.00
34.86
O


HETATM
4057
O
HOH

276
3.058
8.060
9.657
1.00
31.13
O


HETATM
4058
O
HOH

277
5.081
6.362
8.463
1.00
31.02
O


HETATM
4059
O
HOH

278
3.600
10.499
8.517
1.00
50.03
O


HETATM
4060
CD
CD

302
0.011
−4.071
−53.380
0.91
31.52
CD


HETATM
4061
O
HOH

305
1.845
2.702
−51.597
1.00
14.19
O


HETATM
4062
CD
CD

311
4.100
−9.327
−24.111
0.91
76.29
CD


HETATM
4063
O
HOH

313
−1.010
−7.500
−47.833
1.00
40.72
O


HETATM
4064
MG
MG

318
1.219
3.097
−48.942
1.00
17.48
MG


HETATM
4065
O
HOH

322
−10.157
−13.890
−44.431
1.00
41.81
O


HETATM
4066
MG
MG

326
2.778
−7.878
−38.005
1.00
11.66
MG


HETATM
4067
O
HOH

327
9.652
−2.170
−38.994
1.00
44.35
O


HETATM
4068
HG
HG

332
−7.089
−5.545
−35.006
0.60
82.38
HG


HETATM
4069
O
HOH

333
1.493
−12.458
−57.479
1.00
39.19
O


HETATM
4070
O
HOH

335
−4.211
7.242
−62.792
1.00
49.93
O


HETATM
4071
O
HOH

336
−7.759
−5.212
−49.585
1.00
35.75
O


HETATM
4072
O
HOH

338
−3.953
−6.679
−45.543
1.00
38.41
O


HETATM
4073
O
HOH

339
0.508
−10.010
−44.801
1.00
28.38
O


HETATM
4074
O
HOH

340
−8.610
1.401
−65.472
1.00
31.42
O


HETATM
4075
O
HOH

343
5.058
−10.891
−43.391
1.00
29.07
O


HETATM
4076
O
HOH

345
5.817
−19.070
−33.612
1.00
35.77
O


HETATM
4077
O
HOH

346
8.758
−14.281
−46.244
1.00
40.41
O


HETATM
4078
HG
HG

347
6.715
−12.669
−48.448
0.20
54.24
HG


HETATM
4079
O
HOH

349
5.113
−13.530
−54.095
1.00
42.05
O


HETATM
4080
O
HOH

352
6.195
−6.263
−57.438
1.00
39.69
O


HETATM
4081
O
HOH

353
12.125
3.149
−49.649
1.00
38.23
O


HETATM
4082
MG
MG

354
11.145
8.122
−61.981
1.00
29.67
MG


HETATM
4083
O
HOH

355
10.792
7.517
−64.576
1.00
68.09
O


HETATM
4084
O
HOH

356
12.630
7.721
−60.264
1.00
42.56
O


HETATM
4085
O
HOH

357
13.374
7.731
−62.491
1.00
44.36
O


HETATM
4086
O
HOH

358
8.902
7.560
−61.857
1.00
47.98
O


HETATM
4087
MG
MG

360
6.237
6.431
−66.914
1.00
28.74
MG


HETATM
4088
O
HOH

361
6.408
4.325
−65.550
1.00
56.01
O


HETATM
4089
O
HOH

362
8.361
5.765
−66.746
1.00
36.18
O


HETATM
4090
O
HOH

363
4.653
5.030
−68.186
1.00
40.11
O


HETATM
4091
O
HOH

364
7.146
6.368
−64.453
1.00
50.71
O


HETATM
4092
MG
MG

365
4.856
8.795
−57.034
1.00
57.29
MG


HETATM
4093
O
HOH

367
5.981
7.693
−58.709
1.00
45.32
O


HETATM
4094
O
HOH

368
2.602
9.503
−57.044
1.00
34.21
O


HETATM
4095
O
HOH

369
−3.740
−7.741
−49.878
1.00
34.52
O


HETATM
4096
O
HOH

371
−4.630
−7.088
−47.848
1.00
47.42
O


HETATM
4097
O
HOH

372
−1.660
−6.106
−49.542
1.00
29.15
O


HETATM
4098
O
HOH

373
−6.163
−7.124
−50.377
1.00
43.85
O


HETATM
4099
O
HOH

374
−4.330
−5.161
−49.766
1.00
36.71
O


HETATM
4100
MG
MG

375
−4.006
−10.777
−39.969
1.00
19.68
MG


HETATM
4101
O
HOH

376
−3.858
−12.278
−36.949
1.00
28.95
O


HETATM
4102
O
HOH

377
−2.097
−12.249
−40.683
1.00
38.24
O


HETATM
4103
O
HOH

378
−5.782
−11.177
−38.567
1.00
48.85
O


HETATM
4104
O
HOH

379
−3.396
−9.585
−37.760
1.00
53.51
O


HETATM
4105
MG
MG

380
1.544
−10.560
−40.973
1.00
15.03
MG


HETATM
4106
O
HOH

381
0.239
−9.278
−41.992
1.00
24.23
O


HETATM
4107
O
HOH

382
3.079
−11.151
−39.552
1.00
29.52
O


HETATM
4108
O
HOH

383
2.890
−11.254
−42.623
1.00
28.59
O


HETATM
4109
O
HOH

384
0.497
−12.218
−40.320
1.00
24.46
O


HETATM
4110
MG
MG

385
4.975
−3.399
−36.540
1.00
26.05
MG


HETATM
4111
O
HOH

386
4.351
−3.722
−38.893
1.00
47.91
O


HETATM
4112
O
HOH

387
6.538
−3.279
−34.525
1.00
52.58
O


HETATM
4113
O
HOH

388
6.829
−2.324
−37.582
1.00
23.58
O


HETATM
4114
O
HOH

389
2.776
−4.208
−36.379
1.00
47.45
O


HETATM
4115
CD
CD

390
−0.220
−0.169
−45.971
1.00
66.34
CD


HETATM
4116
O
HOH

391
1.204
0.456
−48.678
1.00
26.12
O


HETATM
4117
O
HOH

392
−2.039
−0.298
−44.457
1.00
74.79
O


HETATM
4118
O
HOH

394
−2.332
−1.375
−46.858
1.00
55.72
O


HETATM
4119
O
HOH

395
0.735
−1.415
−41.666
1.00
23.21
O


HETATM
4120
O
HOH

396
−2.289
1.508
−46.080
1.00
38.73
O


HETATM
4121
MG
MG

397
−1.117
−10.966
−60.412
1.00
36.18
MG


HETATM
4122
O
HOH

399
−2.144
−9.538
−58.861
1.00
29.70
O


HETATM
4123
O
HOH

400
1.112
−10.642
−59.923
1.00
66.19
O


HETATM
4124
O
HOH

401
−3.291
−10.503
−60.904
1.00
35.31
O


HETATM
4125
O
HOH

402
−2.294
−12.413
−59.078
1.00
39.66
O


HETATM
4126
O
HOH

403
−1.467
−8.797
−61.459
1.00
53.05
O


HETATM
4127
O
HOH

404
−12.040
−30.139
−41.430
1.00
41.13
O


HETATM
4128
O
HOH

405
−2.445
−24.982
−35.646
1.00
41.49
O


HETATM
4129
O
HOH

406
−12.232
−9.609
−53.785
1.00
19.82
O


HETATM
4130
O
HOH

407
−10.736
−14.577
−49.559
1.00
27.37
O


HETATM
4131
O
HOH

408
−18.946
−19.067
−62.962
1.00
48.41
O


HETATM
4132
O
HOH

409
−19.414
−10.463
−60.502
1.00
52.79
O


HETATM
4133
O
HOH

410
−6.651
−19.456
−54.939
1.00
26.78
O


HETATM
4134
O
HOH

411
−2.899
−18.491
−49.891
1.00
31.34
O


HETATM
4135
O
HOH

412
−4.041
−25.738
−47.368
1.00
61.51
O


HETATM
4136
CD
CD

413
−13.027
8.492
10.933
0.10
33.43
CD


HETATM
4137
CD
CD

414
−11.592
5.003
−2.412
0.10
14.13
CD


HETATM
4138
HG
HG

415
−23.456
−2.491
−20.626
0.10
35.19
HG


HETATM
4139
HG
HG

416
−17.183
−2.624
−19.816
0.10
45.02
HG


HETATM
4140
O
HOH

418
−0.113
29.557
−9.189
1.00
36.18
O


HETATM
4141
O
HOH

419
−1.958
16.568
4.135
1.00
22.82
O


HETATM
4142
O
HOH

420
0.874
15.995
−1.216
1.00
36.22
O


HETATM
4143
O
HOH

421
−0.098
21.800
−5.101
1.00
35.12
O


HETATM
4144
O
HOH

422
−1.412
23.130
−2.906
1.00
36.67
O


HETATM
4145
O
HOH

423
−3.317
24.792
0.592
1.00
45.31
O


HETATM
4146
O
HOH

424
0.019
9.295
−10.598
1.00
36.37
O


HETATM
4147
O
HOH

425
−2.568
8.364
−13.958
1.00
50.92
O


HETATM
4148
O
HOH

426
−2.689
18.373
−24.066
1.00
34.21
O


HETATM
4149
O
HOH

427
7.170
6.156
−29.910
1.00
17.29
O


HETATM
4150
O
HOH

428
8.929
4.171
−22.749
1.00
41.67
O


HETATM
4151
O
HOH

429
12.036
0.863
−14.965
1.00
42.52
O


HETATM
4152
O
HOH

431
−1.202
8.279
12.504
1.00
41.33
O


HETATM
4153
O
HOH

432
8.485
7.265
7.104
1.00
46.57
O


HETATM
4154
O
HOH

434
4.018
10.172
4.758
1.00
37.32
O


HETATM
4155
O
HOH

435
18.225
−9.006
−2.120
1.00
60.80
O


HETATM
4156
MG
MG

437
11.760
−10.915
4.311
1.00
47.79
MG


HETATM
4157
O
HOH

438
12.113
−10.561
1.951
1.00
58.11
O


HETATM
4158
O
HOH

440
14.043
−10.435
3.845
1.00
43.62
O


HETATM
4159
O
HOH

441
9.524
−10.398
4.381
1.00
41.20
O


HETATM
4160
O
HOH

442
11.946
−13.321
4.538
1.00
65.98
O


HETATM
4161
O
HOH

443
12.227
−8.461
4.164
1.00
61.70
O


HETATM
4162
O
HOH

444
1.040
4.817
−2.689
1.00
32.93
O


HETATM
4163
O
HOH

445
4.226
0.914
2.202
1.00
3.57
O


HETATM
4164
O
HOH

446
6.340
−0.071
1.151
1.00
19.50
O


HETATM
4165
O
HOH

447
4.234
3.232
1.596
1.00
12.18
O


HETATM
4166
HG
HG

448
−4.015
−8.066
−15.150
0.10
21.04
HG


HETATM
4167
O
HOH

450
−4.907
−3.163
−52.117
1.00
24.48
O


HETATM
4168
HG
HG

451
−5.485
5.932
−35.358
0.10
26.20
HG


HETATM
4169
O
HOH

452
−4.427
1.650
−44.668
1.00
47.88
O


HETATM
4170
O
HOH

453
−6.126
−4.197
−47.630
1.00
40.28
O


HETATM
4171
O
HOH

454
−14.902
−5.184
−53.399
1.00
41.04
O


HETATM
4172
O
HOH

455
2.198
−31.615
−45.895
1.00
38.45
O


HETATM
4173
O
HOH

456
−0.111
−29.053
−48.914
1.00
37.64
O


HETATM
4174
O
HOH

457
5.023
−28.677
−39.390
1.00
42.30
O


HETATM
4175
O
HOH

459
−8.700
−0.565
−36.045
1.00
32.85
O


HETATM
4176
O
HOH

460
−1.593
−4.423
−51.572
1.00
28.40
O


HETATM
4177
O
HOH

461
−1.729
−3.181
−53.813
1.00
2.00
O


HETATM
4178
O
HOH

462
−1.294
−5.593
−53.672
1.00
22.25
O


HETATM
4179
O
HOH

463
0.388
−1.958
−53.133
1.00
27.43
O







MASTER  320 0 35 8 7 0 3 12 4175 4 0 32


END

## Claims

1. A method for identifying a potential modulator of ribosomal protein L11/GAR activity, comprising the steps of:
a) providing the atomic co-ordinates of the L11 GTPase Activating Region (L11/GAR) in Table II, thereby defining a three-dimensional structure of the L11/GAR; 
b) using said three dimensional structure of the L11/GAR to design or select a potential modulator by computer modeling; 
c) providing said potential modulator; and 
d) physically contacting said potential modulator with L11/GAR to determine the ability of said potential modulator to modulate L11/GAR activity, wherein a modulator of L11/GAR activity is identified.

2. The method according to claim 1, wherein said potential modulator is designed de novo.

3. The method according to claim 1, wherein said potential modulator is designed from a known modulator.

4. The method according to claim 1, wherein said step of employing said three-dimensional structure to design or select said potential modulator comprises the steps of:
a) identifying chemical entities or fragments with the potential to bind said L11/GAR; and 
b) assembling the identified chemical entities or fragments into a single molecule to provide the structure of said potential modulator.

5. The method according to claim 4, wherein said potential modulator is designed de novo.

6. The method according to claim 4, wherein said potential modulator is designed from a known modulator.