WO2010064019A1 - Structure and uses of embryonic ectoderm development (eed) polypeptide - Google Patents

Structure and uses of embryonic ectoderm development (eed) polypeptide Download PDF

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WO2010064019A1
WO2010064019A1 PCT/GB2009/002822 GB2009002822W WO2010064019A1 WO 2010064019 A1 WO2010064019 A1 WO 2010064019A1 GB 2009002822 W GB2009002822 W GB 2009002822W WO 2010064019 A1 WO2010064019 A1 WO 2010064019A1
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atom
asp
hoh
lys
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French (fr)
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Steven J. Gamblin
Miriam Sharpe
Neil Justin
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Medical Research Council
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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • C07K14/4702—Regulators; Modulating activity

Definitions

  • PcG proteins were first identified in Drosophila as long-term repressors of homeotic (Hox) gene expression during development. They have since been implicated in the silencing of genes important for cell proliferation and differentiation and embryonic development in mammals [4-6]. It appears that PcG proteins are able to maintain silenced epigenetic states through posttranslational modifications and structural changes to the underlying chromatin structure (reviewed in Ringrose & Paro[l ] and Levine et a/. [2]).
  • the Polycomb Repressive Complex2 (PRC2) complex of PcG proteins was found to have an intrinsic histone methylation activity specific for lysine residue 27 of histone H3 (H3K27) [7-1 1 ].
  • the composition of this complex varies, but the core components present in all PRC2 complexes isolated so far include Embryonic Ectoderm Development (EED), EZH2 (Enhancer of Zeste-2) and SUZ 12 (Supressor of Zeste 12) or homologs of these proteins (reviewed in [12, 13].
  • the invention provides crystalline EED polypeptide, said polypeptide being bound to a tri-methyllysine histone peptide or an analogue thereof.
  • the invention relates to an EED polypeptide having the structure defined by the structural coordinates as shown herein.
  • the invention relates to a method for identifying a candidate modulator of EED polypeptide activity, said method comprising
  • the invention relates to a method as described above wherein the structural coordinates of at least the aromatic cage of EED are selected.
  • the invention relates to a method as described above wherein each of the structural coordinates of presented herein are selected.
  • the invention in another aspect, relates to a method for identifying a candidate therapeutic agent, said method comprising application of rational drug design to the crystal structure of EED.
  • the invention in another aspect, relates to a method of manufacturing a modulator of a EED polypeptide, said method comprising identifying a candidate modulator as described above, and synthesising a quantity of said modulator.
  • the invention relates to use of the atomic coordinates as shown herein in the modelling of a EED polypeptide.
  • the invention relates to a method for the design of one or more ligands of a EED polypeptide, said method comprising the use of coordinates presented herein.
  • a molecular modelling apparatus is suitably a computer programmed with the appropriate tools for molecular modelling.
  • Rational design of candidate agents likely to be able to interact with the target protein may be based upon structural studies of the molecular shapes of the target protein as disclosed herein. These will provide guidance as to which amino acid residues form molecular contact regions.
  • the candidate therapeutic agent (or candidate modulator or molecular entity of interest (interchangeably referred to as 'agent' below)) may be an organic compound or other chemical.
  • the agent may be a compound, which is obtainable from or produced by any suitable source, whether natural or artificial.
  • the agent may be an amino acid molecule, a polypeptide, or a chemical derivative thereof, or a combination thereof.
  • the agent may even be a polynucleotide molecule - which may be ⁇ sense or an anti-sense molecule.
  • the agent may be an antibody.
  • the agent may be designed or obtained from a library of compounds, which may comprise peptides, as well as other compounds, such as small organic molecules.
  • the agent may be a natural substance, a biological macromolecule, or an extract made from biological materials such as bacteria, fungi, or animal (particularly mammalian) cells or tissues, an organic or an inorganic molecule, a synthetic agent, a semi-synthetic agent, a structural or functional mimetic, a peptide, a peptidomimetic, a derivatised agent, a peptide cleaved from a whole protein, or a peptide synthesised synthetically (such as, by way of example, either using a peptide synthesiser or by recombinant techniques or combinations thereof, a recombinant agent, an antibody, a natural or a non-natural agent, a fusion protein or equivalent thereof and mutants, derivatives or combinations thereof).
  • the agent will be an organic compound.
  • the organic compounds will comprise two or more hydrocarbyl groups.
  • hydrocarbyl group means a group comprising at least C and H and may optionally comprise one or more other suitable substituents. Examples of such substituents may include halo-, alkoxy-, nitro-, an alkyl group, a cyclic group etc.
  • substituents may include halo-, alkoxy-, nitro-, an alkyl group, a cyclic group etc.
  • a combination of substituents may form a cyclic group. If the hydrocarbyl group comprises more than one C then those carbons need not necessarily be linked to each other. For example, at least two of the carbons may be linked via a suitable element or group.
  • the hydrocarbyl group may contain hetero atoms. Suitable hetero atoms will be apparent to those skilled in the art and include, for instance, sulphur, nitrogen and oxygen.
  • the agent comprises at least one cyclic group.
  • the cyclic group may be a polycyclic group, such as a non-fused polycyclic group.
  • the agent comprises at least the one of said cyclic groups linked to another hydrocarbyl group.
  • the agent may be in the form of a pharmaceutically acceptable salt - such as an acid addition salt or a base salt - or a solvate thereof, including a hydrate thereof.
  • suitable salts see Berge et a/, (1977) J. Pharm. Sci. 66, 1-19.
  • Mutating has it normal meaning in the art and may refer to the substitution or truncation or deletion of the residue, motif or domain referred to. Mutation may be effected at the polypeptide level e.g. by synthesis of a polypeptide having the mutated sequence, or may be effected at the nucleotide level e.g. by making a nucleic acid encoding the mutated sequence, which nucleic acid may be subsequently translated to produce the mutated polypeptide. Where no amino acid is specified as the replacement amino acid for a given mutation site, suitably alanine (A) is used.
  • A alanine
  • a fragment is suitably at least 10 amino acids in length, suitably at least 25 amino acids, suitably at least 50 amino acids, suitably at least 100 amino acids, suitably at least 200 amino acids, suitably the majority of the EED polypeptide of interest.
  • a fragment comprises a whole motif or a whole domain of the EED polypeptide of interest.
  • a fragment comprises at least 10 amino acids either side of the given mutation of interest.
  • a fragment comprises at least 10 amino acids each side of the two or more mutations, and suitably further comprises the intervening amino acid sequence too.
  • the fragment comprises the amino acids between said mutation and said end (e.g. the N- or C- terminus).
  • the invention relates to an EED family polypeptide comprising one or more of the mutations described herein.
  • Polycomb Group (PcG) proteins play an essential role in maintaining the silencing of genes required for development through posttranslational modifications and changes to chromatin structure (reviewed in Ringrose & Paro[l] and Levine et al.[2]).
  • the silencing activity of Polycomb Repressive Complex 2 (PRC2) is dependent on its ability to tri-methylate lysine 27 of histone H3. Although this modification is catalysed by the SET domain of the EZH2 subunit of PRC2, methylation activity requires at least two other subunits of the complex; SUZ 12 and EED.
  • EED is a WD40-repeat-containing protein which forms a propeller-like structure in which each of seven WD40-repeats corresponds to a ⁇ -sheet-'blade'[16].
  • WD40- repeat proteins form a large family which participate in very diverse cellular functions, often acting at a molecular level as a rigid scaffold on which protein-protein interactions can occur, coordinating downstream events[19].
  • EED binds to four different histone-derived peptides containing trimethylation marks associated with gene repression, and present the crystal structures of EED in complex with these peptides.
  • ⁇ EED forms a ⁇ -propeller molecule with un-accounted electron density in a central depression on one side of the protein ( Figure Ia).
  • Conditions used to grow the ⁇ EED crystals included a non-detergent sulfobetaine (NDSB-195).
  • NDSB-195 An NDSB- 195 molecule was successfully built into the map at the site of the unoccupied electron density ( Figure Ib).
  • the protein-bound quarternary amine of the sulfobetaine molecule is structurally similar to a trimethylated lysine side chain[20]; in addition, the residues making up the sulfobetaine binding site in ⁇ EED consists of three aromatic side chains, strongly resembling the 'aromatic cages' used by other protein domains to recognise methylated lysine residues, such as the PHD domain[21, 22], the chromodomain[23] and the double tudor domain[24]. From this evidence we inferred that EED might bind to trimethylated lysine residues such as those found on the N- terminal tails of histone proteins.
  • histone lysine residues There are a number of histone lysine residues that are known to be methylated in vivo. The most commonly studied of these include lysine residue 4 of histone H3 (H3K4), H3K9, H3K27, H3K36, H3K79 and H4K20.
  • H3K4 histone H3
  • H3K9 histone H3
  • H3K27 histone H3
  • H3K36 histone H3K79
  • H4K20 histone H3
  • HlK26me3 since methylation of the linker histone H 1.4 at lysine 26 appears to be important for transcriptional repression by EZH2[25]
  • Dissociation constants for the unlabelled peptides were determined using competition assays in which the dansyl-labelled peptide plus EED was titrated with an unlabelled peptide (see Figure 2).
  • ⁇ EED binds most tightly to H3K9me3, H4K20me3 and HlK26me3 peptides with Kd values of 9.7 to 19.1 ⁇ M, and slightly less tightly to H3K27me3 (45.6 ⁇ M), but does not bind to a appreciably to H3K4me3, H3K36me3 or H3K79me3.
  • ⁇ EED was also shown to have a clear binding preference for the trimethylated state compared with variously methylated or unmethylated H1K26 or H3K27 peptides.
  • Each blade is an antiparallel ⁇ -sheet, typically made up of four ⁇ -strands labelled A to D. Loops A-B and C-D form the bottom surface of the propeller, and loops B-C and D-A form the top surface, which also contains the tri-methylated lysine-binding pocket.
  • Blade 7 contains both the N terminus (leading into strand D) and the C terminus (strand C).
  • the peptides in the four co-crystal structures bind in a similar manner.
  • the aromatic cage that recognises the trimethylated lysine residue in each peptide is the only known example of a methyllysine-binding aromatic cage found on a ⁇ -propeller domain. It consists of three aromatic sidechains arranged in a half-box-like cage (F97, Y 148, Y365). The trimethylammonium group of the lysine is inserted into this cage and is stabilised by van der Waals and cation- ⁇ interactions ( Figure lc,d).
  • a fourth aromatic sidechain (W364) stabilises the 'stem' of the lysine sidechain via hydrophobic interactions.
  • the WDR5 component of MLL-family methyltransferase complexes also a ⁇ - propeller, has been demonstrated to bind the MLL methylation target H3K4 in various methylation states[26, 27].
  • WDR5 binds to unmodified H3K4, or mono-, di-, or tri-methylated H3K4 with a similar Kd (4.5 - 6.8 uM) [26].
  • the protein mainly recognises the residues surrounding H3K4, and appears to "present" the H3K4 side chain, projecting it out into the solvent for further methylation[28-31].
  • EED does not present the methylation target to the rest of the PRC2 complex. Instead, the aromatic cage of EED mediates tri-methyl lysine recognition, with some less- specific interaction occurring with the immediately surrounding residues.
  • the "aromatic cage” motif where two to four aromatic amino acids form a hydrophobic environment, is commonly used by proteins to recognise methylated lysine residues[21, 22, 24] and has been found in chromodomains, tudor domains and plant homeodomain (PHD) finger domains.
  • the chromodomains from Heterochromatin Protein 1 (HPl), and the Polycomb (PC) subunit of another PcG complex, PRCl recognise methylated H3K27[32, 33], and H3K9[23, 34], respectively, both displaying a higher affinity towards the tri-methylated state over mono- and di-methylations[33].
  • a double chromodomain from the CHDl chromo- ATPase/helicase-DNA-binding 1 nucleosome remodeling complex recognises histone
  • H3 tri-methylated at K4[35], along with the double6.1 domain from the JMJD2A histone demethylase[24], and the zinc-binding PHD finger, found in the proteins BPTF (bromodomain and PHD domain transcription factor) and ING2 (inhibitor of growth 2)
  • H3K9, H3K27 and H4K20 appear to correlate with gene repression [4, 5, 36-41], although in the Barski et al. study[37], highly localized H3K9me3 peaks were also found in some active genes and the H4K20me3 mark was not associated with either active or silent promoters. Trimethylated H3K9, H3K27 and H4K20 residues have also been associated with silenced chromatin in Drosophila[42].
  • H3K4me3 and H3K36me3 signals correlated with gene activation, but H3K79me3 was associated with repression.
  • EED is likely facilitating the PRC complex to carry out trimethylation of H3K27, spreading and amplifying this signal for repression across the area of chromatin.
  • the structure of EED presented here with a small molecule mimetic of tri-methyllysine offers important opportunities for new therapeutic approaches. Indeed, it may well be that the small molecule binding site we have identified, together with the interactions that it forms with NDSB- 195, provide key insights into the development of compounds that bind with high affinity to this site that would reduce the patterns of H3K27 observed in certain cancer types.
  • Determination of the 3D structure of EED provides important information about the likely active sites of EED, particularly when comparisons are made with similar enzymes. This information may then be used for rational design of EED inhibitors or interactors, e.g. by computational techniques which identify possible binding ligands for the active sites, by enabling linked-fragment approaches to drug design, and by enabling the identification and location of bound ligands using X-ray crystallographic analysis. These techniques are discussed in more detail below.
  • EED inhibitors may also be designed in the this way. More specifically, a ligand (e.g. a potential inhibitor) of EED may be designed that complements the functionalities of the EED active site(s), such as the aromatic cage. The ligand can then be synthesised, formed into a complex with EED, and the complex then analysed by X-ray crystallography to identify the actual position of the bound ligand.
  • a ligand e.g. a potential inhibitor
  • the ligand can then be synthesised, formed into a complex with EED, and the complex then analysed by X-ray crystallography to identify the actual position of the bound ligand.
  • the structure and/or functional groups of the ligand can then be adjusted, if necessary, in view of the results of the X-ray analysis, and the synthesis and analysis sequence repeated until an optimised ligand is obtained.
  • Related approaches to structure-based drug design are also discussed in Bohacek et al., Medicinal Research Reviews, Vol.16, (1996), 3-50.
  • EED inhibitors or activators
  • automated ligand-receptor docking programs discussed e.g. by Jones et al. in Current Opinion in Biotechnology, Vol.6, (1995), 652-656) which require accurate information on the atomic coordinates of target molecules may be used to design EED inhibitors (or activators).
  • Linked-fragment approaches to drug design also require accurate information on the atomic coordinates of target molecules.
  • a first stage of the drug design program may involve computer-based in silico screening of compound databases (such as the Cambridge Structural Database) with the aim of identifying compounds which interact with the active site or sites of the target bio-molecule. Screening selection criteria may be based on pharmacokinetic properties such as metabolic stability and toxicity.
  • determination of the EED structure allows the architecture and chemical nature of each active site to be identified, which in turn allows the geometric and functional constraints of a descriptor for the potential inhibitor to be derived. The descriptor is, therefore, a type of virtual 3-D pharmacophore, which can also be used as selection criteria or filter for database screening.
  • the invention relates to the selection and/or design and/or screening for inhibitors or activators or molecules capable of interfering with or binding to EED polypeptides.
  • the invention relates to screening for inhibitors of EED polypeptides.
  • Figure 1 Structural basis of EED binding to NDSB-195 and methylated histone peptides.
  • FIG. 1 EED binds repressive trimethylated histione peptides.
  • A Sequence of peptides used for binding experiments. Tight binding peptides are marked by red boxes while weak binding peptides are shown by blue boxes.
  • B Table showing affinities of peptides for EED wt and mutants.
  • C,D Fluorescent competition experiments showing traces for H3K9me3, H3K27me3, H3K79me3 and H4k20me3 (C) and HlK26me3, HlK26me2, HlK26mel, and HlK26meO (D).
  • ⁇ EED DNA was amplified using PCR from a vector supplied by D. Reinberg, and then cloned into a pGEX-4T vector (Amersham Biosciences) encoding an N-terminal glutathione-S-transferase (GST) fusion protein followed by ⁇ thrombin cleavage site.
  • GST glutathione-S-transferase
  • Wild type and mutant ⁇ EED were subsequently transformed into Escherichia coli BL21(DE3) (Novagen) for nonl ⁇ beled and selenomethionine-enriched ⁇ EED protein expression.
  • Cells were grown in Terrific Broth media for nonlabeled expression or in SelenoMet Medium (Molecular Dimensions) for selenomethionine-enriched expression.
  • Cells were grown at 30 0 C and 210 rpm until they reached an absorbance at 600 nm (A 60O ) of 0.5, when the temperature was decreased to 18°C. When the cells reached an A 60O of approximately 0.8, they were induced with 0.3 mM final concentration of isopropyl- ⁇ -D-thiogalactoside.
  • cells were harvested by centrifugation at 4000 x g for 20 min, resuspended in a buffer solution of 100 mM Tris-HCl pH 8.0, 300 mM NaCl and 10 mM DTT and lysed by sonication on ice.
  • the supernatant fraction obtained by centrifugation of the lysate at 20 000 x g for 45 min was loaded onto glutathione sepharose 4B beads (GE Healthcare) and washed using the lysis buffer solution.
  • Proteins were then cleaved from GST with human ⁇ -thrombin (Haematologic Technologies, Inc.), further purified using size exclusion chromatography (Superdex 200, GE Healthcare) in buffer containing 50 mM Tris-HCl pH 8.7, 150 mM NaCl and 3 mM TCEP, and then snap frozen using liquid nitrogen and stored at -8O 0 C for later use.
  • Peptides were synthesised and purified by reversed phase HPLC at the University of Bristol Peptide Synthesis Facility. Peptide masses were verified by mass spectrometry.
  • Crystallography For crystallisation trials, protein solutions were prepared as either ⁇ EED alone at 2.5 mg/ml or as a complex solution at 1.5 mg/ml with peptide at a 7-fold higher molar concentration. All protein solutions contained TCEP at 15 mM concentration. Crystals were grown at 18°C using the vapour diffusion technique in hanging drops. Drops were prepared by mixing equal volumes of ⁇ EED protein alone with reservoir solution containing 4.0-4.1 M formate and 0.6-0.7 M NDSB-195, or by mixing equal volumes of ⁇ EED protein complex with 3.7-3.9 M formate solution. Crystals were transferred into mother liquor with 5 to 10% glycerol prior to flash cooling in liquid nitrogen.
  • Diffraction data for the ⁇ EED-only native and selenomethionine crystals were collected at the Daresbury synchrotron on beamline 10.1 at the peak wavelength for selenium.
  • Diffraction data for the protein complex crystals were collected using an in-house MicroMax 007HF rotating anode coupled to a RaxisIV 4 ⁇ detector. Data were integrated using Denzo and scaled with Scalepack[44]. Phases for the selenomethionine-substitued ⁇ EED structure were generated and extended using the single wavelength anomalous dispersion (SAD) method and SOLVE[45] and RESOLVE[46] programs.
  • SAD single wavelength anomalous dispersion
  • Phases from RESOLVE were used to autobuild a model with ARP/wARP[47] in warpNtrace mode.
  • the protein complex crystal structures were solved by molecular replacement using AMoRe[48] and the selenomethionine-substitued ⁇ EED structure as the search model.
  • Standard refinement was carried out with refmac5[49] and CNS[50] together with manual model building with Coot[51].
  • Figures were created with Pymol (DeL ⁇ no Scientific; http://pymol.sourceforge.net/). Binding studies.
  • Czermin, B., et al., Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell, 2002. 111 (2): p. 185-96.
  • the invention makes use of the following atomic co-ordinates which describe, among other things, the crystal structure of a domain of the EED protein and the co-ordinates for the EED complexes with the additive (add1-renum2) and H3K27me3 (refmac17) peptide.
  • ATOM lie O MET A 180 7.314 38.917 26.105 1.00 18.57 A O

Abstract

The invention relates to a crystalline EED polypeptide, said polypeptide being bound to a tri-methyllysine histone peptide or an analogue thereof. The invention also relates to methods.

Description

Structure and Uses of Embryonic Ectoderm Development (EED) Polypeptide
Background to the Invention
Polycomb Group (PcG) proteins were first identified in Drosophila as long-term repressors of homeotic (Hox) gene expression during development. They have since been implicated in the silencing of genes important for cell proliferation and differentiation and embryonic development in mammals [4-6]. It appears that PcG proteins are able to maintain silenced epigenetic states through posttranslational modifications and structural changes to the underlying chromatin structure (reviewed in Ringrose & Paro[l ] and Levine et a/. [2]).
The Polycomb Repressive Complex2 (PRC2) complex of PcG proteins was found to have an intrinsic histone methylation activity specific for lysine residue 27 of histone H3 (H3K27) [7-1 1 ]. The composition of this complex varies, but the core components present in all PRC2 complexes isolated so far include Embryonic Ectoderm Development (EED), EZH2 (Enhancer of Zeste-2) and SUZ 12 (Supressor of Zeste 12) or homologs of these proteins (reviewed in [12, 13].
Summary of the Invention
An aromatic cage on EED mediates recognition of repressive trimethyllysine histone marks important for PRC2 function.
The invention relates in particular to the aspects set out in the accompanying claims.
Detailed Description of the Invention
In one aspect the invention provides crystalline EED polypeptide, said polypeptide being bound to a tri-methyllysine histone peptide or an analogue thereof.
In another aspect, the invention relates to an EED polypeptide having the structure defined by the structural coordinates as shown herein.
In another aspect, the invention relates to a method for identifying a candidate modulator of EED polypeptide activity, said method comprising
(i) providing a molecular modelling apparatus with a set of structural coordinates of an EED polypeptide selected from those shown herein;
(ii) providing said molecular modelling apparatus with a set of structural coordinates of a molecular entity of interest; and
(iii) determining whether the molecular entity of interest is expected to bind to or to affect the structure of said EED polypeptide, wherein an expectation of binding or affecting the structure of said EED polypeptide identifies said molecular entity of interest as a candidate modulator of EED polypeptide activity.
In another aspect, the invention relates to a method as described above wherein the structural coordinates of at least the aromatic cage of EED are selected.
In another aspect, the invention relates to a method as described above wherein each of the structural coordinates of presented herein are selected.
In another aspect, the invention relates to a method for identifying a candidate therapeutic agent, said method comprising application of rational drug design to the crystal structure of EED.
In another aspect, the invention relates to a method of manufacturing a modulator of a EED polypeptide, said method comprising identifying a candidate modulator as described above, and synthesising a quantity of said modulator.
In another aspect, the invention relates to use of the atomic coordinates as shown herein in the modelling of a EED polypeptide.
In another aspect, the invention relates to a method for the design of one or more ligands of a EED polypeptide, said method comprising the use of coordinates presented herein.
A molecular modelling apparatus is suitably a computer programmed with the appropriate tools for molecular modelling.
Rational design of candidate agents likely to be able to interact with the target protein may be based upon structural studies of the molecular shapes of the target protein as disclosed herein. These will provide guidance as to which amino acid residues form molecular contact regions.
The candidate therapeutic agent (or candidate modulator or molecular entity of interest (interchangeably referred to as 'agent' below)) may be an organic compound or other chemical. The agent may be a compound, which is obtainable from or produced by any suitable source, whether natural or artificial. The agent may be an amino acid molecule, a polypeptide, or a chemical derivative thereof, or a combination thereof. The agent may even be a polynucleotide molecule - which may be α sense or an anti-sense molecule. The agent may be an antibody. The agent may be designed or obtained from a library of compounds, which may comprise peptides, as well as other compounds, such as small organic molecules. By way of example, the agent may be a natural substance, a biological macromolecule, or an extract made from biological materials such as bacteria, fungi, or animal (particularly mammalian) cells or tissues, an organic or an inorganic molecule, a synthetic agent, a semi-synthetic agent, a structural or functional mimetic, a peptide, a peptidomimetic, a derivatised agent, a peptide cleaved from a whole protein, or a peptide synthesised synthetically (such as, by way of example, either using a peptide synthesiser or by recombinant techniques or combinations thereof, a recombinant agent, an antibody, a natural or a non-natural agent, a fusion protein or equivalent thereof and mutants, derivatives or combinations thereof). Typically, the agent will be an organic compound. Typically, the organic compounds will comprise two or more hydrocarbyl groups. Here, the term "hydrocarbyl group" means a group comprising at least C and H and may optionally comprise one or more other suitable substituents. Examples of such substituents may include halo-, alkoxy-, nitro-, an alkyl group, a cyclic group etc. In addition to the possibility of the substituents being a cyclic group, a combination of substituents may form a cyclic group. If the hydrocarbyl group comprises more than one C then those carbons need not necessarily be linked to each other. For example, at least two of the carbons may be linked via a suitable element or group. Thus, the hydrocarbyl group may contain hetero atoms. Suitable hetero atoms will be apparent to those skilled in the art and include, for instance, sulphur, nitrogen and oxygen. For some applications, preferably the agent comprises at least one cyclic group. The cyclic group may be a polycyclic group, such as a non-fused polycyclic group. For some applications, the agent comprises at least the one of said cyclic groups linked to another hydrocarbyl group. The agent may be in the form of a pharmaceutically acceptable salt - such as an acid addition salt or a base salt - or a solvate thereof, including a hydrate thereof. For a review on suitable salts see Berge et a/, (1977) J. Pharm. Sci. 66, 1-19.
Mutating has it normal meaning in the art and may refer to the substitution or truncation or deletion of the residue, motif or domain referred to. Mutation may be effected at the polypeptide level e.g. by synthesis of a polypeptide having the mutated sequence, or may be effected at the nucleotide level e.g. by making a nucleic acid encoding the mutated sequence, which nucleic acid may be subsequently translated to produce the mutated polypeptide. Where no amino acid is specified as the replacement amino acid for a given mutation site, suitably alanine (A) is used. A fragment is suitably at least 10 amino acids in length, suitably at least 25 amino acids, suitably at least 50 amino acids, suitably at least 100 amino acids, suitably at least 200 amino acids, suitably the majority of the EED polypeptide of interest. Suitably a fragment comprises a whole motif or a whole domain of the EED polypeptide of interest. Suitably a fragment comprises at least 10 amino acids either side of the given mutation of interest. When more than one mutation is discussed, suitably a fragment comprises at least 10 amino acids each side of the two or more mutations, and suitably further comprises the intervening amino acid sequence too. Where a mutation is within 10 amino acids of the end of the polypeptide then suitably the fragment comprises the amino acids between said mutation and said end (e.g. the N- or C- terminus).
In another aspect, the invention relates to an EED family polypeptide comprising one or more of the mutations described herein.
Biological Context
Polycomb Group (PcG) proteins play an essential role in maintaining the silencing of genes required for development through posttranslational modifications and changes to chromatin structure (reviewed in Ringrose & Paro[l] and Levine et al.[2]). The silencing activity of Polycomb Repressive Complex 2 (PRC2) is dependent on its ability to tri-methylate lysine 27 of histone H3. Although this modification is catalysed by the SET domain of the EZH2 subunit of PRC2, methylation activity requires at least two other subunits of the complex; SUZ 12 and EED. We have determined the crystal structure of the EED subunit of PRC2 and identified an aromatic cage at one end of its beta-propeller structure and shown that it specifically binds tri-methyl lysine residues. Our binding studies show that EED recognises tri -methylated H1K26, H3K9, H4K20 and H3K27 - all considered repressive marks. It does not bind to H3K4, H3K36 or H3K79 - marks that are associated with active chromatin. The crystal structures of EED in complex with tri-methyllysine histone peptides explain how the protein targets repressive but not active marks. From the X-ray structure we have designed' a point mutation in the aromatic cage of EED that reduces methyl-lysine binding, without destabilising the structure. The occurrence of a mutation in Drosophila that is adjacent to the aromatic cage, that severely disrupts development ([3]), suggest an essential role for the methyl-lysine binding site on EED in PRC2 function. EZH2 contains the evolutionarily conserved SET (Su[V AR]3-9, Ezh2, Trithorax) domain which is responsible for the histone methylation activity of the PRC2 complex. EED is not predicted to have any catalytic activity, but has been found to interact directly with EZH2 [14-16]. The presence of both EED and SUZ12 is required for the methyltransferase activity of EZH2, as well as stability of the complex [15, 17, 18]. EED is a WD40-repeat-containing protein which forms a propeller-like structure in which each of seven WD40-repeats corresponds to a β-sheet-'blade'[16]. WD40- repeat proteins form a large family which participate in very diverse cellular functions, often acting at a molecular level as a rigid scaffold on which protein-protein interactions can occur, coordinating downstream events[19].
Here we show that EED binds to four different histone-derived peptides containing trimethylation marks associated with gene repression, and present the crystal structures of EED in complex with these peptides.
We initially expressed and purified full-length mammalian EED (441 residues). As trials failed to yield crystals of full-length material, we produced a truncated protein designed from the results of limited proteolysis and sequence analysis, encompassing the seven WD-40 repeat domain or residues 77 to 441 (ΔEED). Crystals were obtained from both native and selenomethionine (SeMet)-substituted ΔEED that produced diffraction data extending to 2.1 and 1.9 A Bragg spacing, respectively. The SeMet- stubstituted structure was solved using the single anomalous dispersion technique, and this was used as a model for molecular replacement to solve the native structure. ΔEED forms a β-propeller molecule with un-accounted electron density in a central depression on one side of the protein (Figure Ia). Conditions used to grow the ΔEED crystals included a non-detergent sulfobetaine (NDSB-195). An NDSB- 195 molecule was successfully built into the map at the site of the unoccupied electron density (Figure Ib). The protein-bound quarternary amine of the sulfobetaine molecule is structurally similar to a trimethylated lysine side chain[20]; in addition, the residues making up the sulfobetaine binding site in ΔEED consists of three aromatic side chains, strongly resembling the 'aromatic cages' used by other protein domains to recognise methylated lysine residues, such as the PHD domain[21, 22], the chromodomain[23] and the double tudor domain[24]. From this evidence we inferred that EED might bind to trimethylated lysine residues such as those found on the N- terminal tails of histone proteins. There are a number of histone lysine residues that are known to be methylated in vivo. The most commonly studied of these include lysine residue 4 of histone H3 (H3K4), H3K9, H3K27, H3K36, H3K79 and H4K20. We measured the relative binding affinity of ΔEED to trimethylated versions of these lysine residues and also HlK26me3 (since methylation of the linker histone H 1.4 at lysine 26 appears to be important for transcriptional repression by EZH2[25]) in synthetic peptides. We synthesised a trimethylated H1K26 peptide that was labelled with a fluorescent dansyl molecule at the C-terminus. Dissociation constants for the unlabelled peptides were determined using competition assays in which the dansyl-labelled peptide plus EED was titrated with an unlabelled peptide (see Figure 2). ΔEED binds most tightly to H3K9me3, H4K20me3 and HlK26me3 peptides with Kd values of 9.7 to 19.1 μM, and slightly less tightly to H3K27me3 (45.6 μM), but does not bind to a appreciably to H3K4me3, H3K36me3 or H3K79me3. ΔEED was also shown to have a clear binding preference for the trimethylated state compared with variously methylated or unmethylated H1K26 or H3K27 peptides.
Co-crystallisation of ΔEED in complex with HlK26me3, H3K27me3, H3K9me3 and H4K20me3 peptides produced crystals that diffracted from 2.1 to 2.75 A resolution and the structures were solved by molecular replacement using the native ΔEED structure as a model. Relevant crystallographic statistics are given in Supplementary Table 1.
The WD40-repeats of ΔEED fold into a seven-bladed β-propeller domain with a central pocket on either side of the propeller (Fig. 1), as seen previously 16]. Each blade is an antiparallel β-sheet, typically made up of four β-strands labelled A to D. Loops A-B and C-D form the bottom surface of the propeller, and loops B-C and D-A form the top surface, which also contains the tri-methylated lysine-binding pocket. Blade 7 contains both the N terminus (leading into strand D) and the C terminus (strand C). Another notable feature is the extended 4CD loop, which follows the edge of the propeller, comprising an α-helix, a random coil turn and a β-strand that forms strand E of blade 3. This extended loop is missing from WDR5, the closest structural homolog to EED in the Protein Data Bank, and it is not yet clear what function it may provide.
The peptides in the four co-crystal structures bind in a similar manner. The aromatic cage that recognises the trimethylated lysine residue in each peptide is the only known example of a methyllysine-binding aromatic cage found on a β-propeller domain. It consists of three aromatic sidechains arranged in a half-box-like cage (F97, Y 148, Y365). The trimethylammonium group of the lysine is inserted into this cage and is stabilised by van der Waals and cation-π interactions (Figure lc,d). A fourth aromatic sidechain (W364) stabilises the 'stem' of the lysine sidechain via hydrophobic interactions.
In order to confirm the role of the aromatic cage in binding trimethylated peptides, a series of four site-directed ΔEED mutants were created. In the case of Y 148 A the mutant protein was insoluble, hi contrast, F97A, Y365A and W364A did produce well-behaved, soluble protein. For two of these mutants we measured affinities for methyllysine histone peptides by ITC, Y365A did not produce any detectable binding while F97A gave a Kd of 70 uM.
The WDR5 component of MLL-family methyltransferase complexes, also a β- propeller, has been demonstrated to bind the MLL methylation target H3K4 in various methylation states[26, 27]. WDR5 binds to unmodified H3K4, or mono-, di-, or tri-methylated H3K4 with a similar Kd (4.5 - 6.8 uM) [26]. The protein mainly recognises the residues surrounding H3K4, and appears to "present" the H3K4 side chain, projecting it out into the solvent for further methylation[28-31]. hi contrast, EED does not present the methylation target to the rest of the PRC2 complex. Instead, the aromatic cage of EED mediates tri-methyl lysine recognition, with some less- specific interaction occurring with the immediately surrounding residues.
Further Applications of the Invention
The "aromatic cage" motif, where two to four aromatic amino acids form a hydrophobic environment, is commonly used by proteins to recognise methylated lysine residues[21, 22, 24] and has been found in chromodomains, tudor domains and plant homeodomain (PHD) finger domains. The chromodomains from Heterochromatin Protein 1 (HPl), and the Polycomb (PC) subunit of another PcG complex, PRCl, recognise methylated H3K27[32, 33], and H3K9[23, 34], respectively, both displaying a higher affinity towards the tri-methylated state over mono- and di-methylations[33]. A double chromodomain from the CHDl (chromo- ATPase/helicase-DNA-binding 1) nucleosome remodeling complex recognises histone
H3 tri-methylated at K4[35], along with the double Tudor domain from the JMJD2A histone demethylase[24], and the zinc-binding PHD finger, found in the proteins BPTF (bromodomain and PHD domain transcription factor) and ING2 (inhibitor of growth 2)
[21, 22].
Various histone modifications have been associated with either silenced or active chromatin states. In mammalian cells, trimethylation of H3K9, H3K27 and H4K20 appears to correlate with gene repression [4, 5, 36-41], although in the Barski et al. study[37], highly localized H3K9me3 peaks were also found in some active genes and the H4K20me3 mark was not associated with either active or silent promoters. Trimethylated H3K9, H3K27 and H4K20 residues have also been associated with silenced chromatin in Drosophila[42]. By contrast, other trimethylated marks have been associated with gene expression: high levels of trimethylated H3K4, H3K9, H3K36, and H3K79 have been found in transcribed regions[43]. In the Barski et al. study[37], H3K4me3 and H3K36me3 signals correlated with gene activation, but H3K79me3 was associated with repression.
Interestingly, in a study on the interaction of the two Drosophila Polycomb Group proteins ESC and E(Z), Tie and colleagues reported on the phenotype of esc9, an M236K mutation isolated from classical genetic screens in Drosophila, which abolished transcriptional silencing by ESC (the Drosophila homologue of EED) in vivo. The equivalent residue in our structure lies adjacent to W364 of the aromatic cage described above and its mutation is likely to dirupt the aromatic cage structure. This genetic result strongly implicated and essential role for the aromatic cage of EED in recognition of repressive tri-methyl lysine marks and the methylation activity of the PRC2 complex. Thus, by binding these repression-associated trimethylated histones, EED is likely facilitating the PRC complex to carry out trimethylation of H3K27, spreading and amplifying this signal for repression across the area of chromatin. Given the interest in the overexpression of PRC2 in certain cancers, with its concomitant increase in H3K27 tri-methylation, the structure of EED presented here with a small molecule mimetic of tri-methyllysine offers important opportunities for new therapeutic approaches. Indeed, it may well be that the small molecule binding site we have identified, together with the interactions that it forms with NDSB- 195, provide key insights into the development of compounds that bind with high affinity to this site that would reduce the patterns of H3K27 observed in certain cancer types. Analysis of the sequences of other WD40 repeat containing proteins fails to reveal any similar pattern of conservation of aromatic and/or hydrophobic residues associated these proteins. It seems therefore that the aromatic binding cage described here may well be unique to EED like proteins associated with PRC2 and as such offers the potential for very high selectivity of action of compounds developed from the NDSB- 195 to bind into this site.
Structure Based Design
Determination of the 3D structure of EED provides important information about the likely active sites of EED, particularly when comparisons are made with similar enzymes. This information may then be used for rational design of EED inhibitors or interactors, e.g. by computational techniques which identify possible binding ligands for the active sites, by enabling linked-fragment approaches to drug design, and by enabling the identification and location of bound ligands using X-ray crystallographic analysis. These techniques are discussed in more detail below.
An iterative approach to ligand design based on repeated sequences of computer modelling, protein-ligand complex formation and X-ray analysis may be employed. EED inhibitors may also be designed in the this way. More specifically, a ligand (e.g. a potential inhibitor) of EED may be designed that complements the functionalities of the EED active site(s), such as the aromatic cage. The ligand can then be synthesised, formed into a complex with EED, and the complex then analysed by X-ray crystallography to identify the actual position of the bound ligand. The structure and/or functional groups of the ligand can then be adjusted, if necessary, in view of the results of the X-ray analysis, and the synthesis and analysis sequence repeated until an optimised ligand is obtained. Related approaches to structure-based drug design are also discussed in Bohacek et al., Medicinal Research Reviews, Vol.16, (1996), 3-50.
As a result of the determination of the EED 3D structure, more purely computational techniques for rational drug design may also be used to design EED inhibitors (or activators). For example, automated ligand-receptor docking programs (discussed e.g. by Jones et al. in Current Opinion in Biotechnology, Vol.6, (1995), 652-656) which require accurate information on the atomic coordinates of target molecules may be used to design EED inhibitors (or activators). Linked-fragment approaches to drug design also require accurate information on the atomic coordinates of target molecules. The idea behind these approaches is to determine (computationally or experimentally) the binding locations of plural ligands to a target molecule, and then construct a molecular scaffold to connect the ligands together in such a way that their relative binding positions are preserved. The connected ligands thus form a potential lead compound that can be further refined using e.g. iterative technique(s). For a virtual linked-fragment approach see Verlinde et al., J. of Computer- Aided Molecular Design, 6, (1992), 131-147, and for NMR and X- ray approaches see Shuker et al., Science, 274, (1996), 1531-1534 and Stout et al., Structure, 6, (1998), 839-848. The use of these approaches to design EED inhibitors is made possible by the determination of the EED structure.
Many of the techniques and approaches to structure-based drug design described above rely at some stage on X-ray analysis to identify the binding position of a ligand in a ligand-protein complex. A common way of doing this is to perform X-ray crystallography on the complex, produce a difference Fourier electron density map, and associate a particular pattern of electron density with the ligand. However, in order to produce the map it is necessary to know beforehand the protein 3D structure (or at least the protein structure factors). Therefore, determination of the EED structure also allows difference Fourier electron density maps of EED-ligand complexes to be produced, which can greatly assist the process of rational drug design.
The approaches to structure-based drug design described above all require initial identification of possible compounds for interaction with the target molecule (in this case EED). Sometimes these compounds are known e.g. from the research literature. However, when they are not, or when novel compounds are wanted, a first stage of the drug design program may involve computer-based in silico screening of compound databases (such as the Cambridge Structural Database) with the aim of identifying compounds which interact with the active site or sites of the target bio-molecule. Screening selection criteria may be based on pharmacokinetic properties such as metabolic stability and toxicity. However, determination of the EED structure allows the architecture and chemical nature of each active site to be identified, which in turn allows the geometric and functional constraints of a descriptor for the potential inhibitor to be derived. The descriptor is, therefore, a type of virtual 3-D pharmacophore, which can also be used as selection criteria or filter for database screening.
The invention relates to the selection and/or design and/or screening for inhibitors or activators or molecules capable of interfering with or binding to EED polypeptides. In particular the invention relates to screening for inhibitors of EED polypeptides.
The invention is now described by way of example in which reference is made to the following drawings.
Brief Description of the Drawings
Figure Legends
Figure 1. Structural basis of EED binding to NDSB-195 and methylated histone peptides.
A..Ribbons representation of EED in complex with histone peptide containing trimethylated H3K9. EED is shown in grey with the peptide in yellow. The positions of the four residues that form the hydrophobic box are indicated by blue circles. B Stick representation of NDSB-195 (yellow) in complex with hydrophobic cage residues of EED (blue) C. Close up view of the aromatic cage with the four residues that form it labelled. D. Electrostatic surface representation of the cage with bound histone peptide (yellow). Negatively charged residues are coloured red while positive ones are blue.
Figure 2. EED binds repressive trimethylated histione peptides. A. Sequence of peptides used for binding experiments. Tight binding peptides are marked by red boxes while weak binding peptides are shown by blue boxes. B. Table showing affinities of peptides for EED wt and mutants. C,D. Fluorescent competition experiments showing traces for H3K9me3, H3K27me3, H3K79me3 and H4k20me3 (C) and HlK26me3, HlK26me2, HlK26mel, and HlK26meO (D).
EXAMPLES Methods
Protein Expression and Purification ΔEED DNA was amplified using PCR from a vector supplied by D. Reinberg, and then cloned into a pGEX-4T vector (Amersham Biosciences) encoding an N-terminal glutathione-S-transferase (GST) fusion protein followed by α thrombin cleavage site. Site-directed mutants of ΔEED were generated with the ExSite protocol (Stratagene).
Wild type and mutant ΔEED were subsequently transformed into Escherichia coli BL21(DE3) (Novagen) for nonlαbeled and selenomethionine-enriched ΔEED protein expression. Cells were grown in Terrific Broth media for nonlabeled expression or in SelenoMet Medium (Molecular Dimensions) for selenomethionine-enriched expression. Cells were grown at 300C and 210 rpm until they reached an absorbance at 600 nm (A60O) of 0.5, when the temperature was decreased to 18°C. When the cells reached an A60O of approximately 0.8, they were induced with 0.3 mM final concentration of isopropyl-β-D-thiogalactoside. After a further incubation of 16 hours at 18°C, cells were harvested by centrifugation at 4000 x g for 20 min, resuspended in a buffer solution of 100 mM Tris-HCl pH 8.0, 300 mM NaCl and 10 mM DTT and lysed by sonication on ice. The supernatant fraction obtained by centrifugation of the lysate at 20 000 x g for 45 min was loaded onto glutathione sepharose 4B beads (GE Healthcare) and washed using the lysis buffer solution. Proteins were then cleaved from GST with human α-thrombin (Haematologic Technologies, Inc.), further purified using size exclusion chromatography (Superdex 200, GE Healthcare) in buffer containing 50 mM Tris-HCl pH 8.7, 150 mM NaCl and 3 mM TCEP, and then snap frozen using liquid nitrogen and stored at -8O0C for later use.
Peptides were synthesised and purified by reversed phase HPLC at the University of Bristol Peptide Synthesis Facility. Peptide masses were verified by mass spectrometry.
Crystallography For crystallisation trials, protein solutions were prepared as either ΔEED alone at 2.5 mg/ml or as a complex solution at 1.5 mg/ml with peptide at a 7-fold higher molar concentration. All protein solutions contained TCEP at 15 mM concentration. Crystals were grown at 18°C using the vapour diffusion technique in hanging drops. Drops were prepared by mixing equal volumes of ΔEED protein alone with reservoir solution containing 4.0-4.1 M formate and 0.6-0.7 M NDSB-195, or by mixing equal volumes of ΔEED protein complex with 3.7-3.9 M formate solution. Crystals were transferred into mother liquor with 5 to 10% glycerol prior to flash cooling in liquid nitrogen. Diffraction data for the ΔEED-only native and selenomethionine crystals were collected at the Daresbury synchrotron on beamline 10.1 at the peak wavelength for selenium. Diffraction data for the protein complex crystals were collected using an in-house MicroMax 007HF rotating anode coupled to a RaxisIV4^ detector. Data were integrated using Denzo and scaled with Scalepack[44]. Phases for the selenomethionine-substitued ΔEED structure were generated and extended using the single wavelength anomalous dispersion (SAD) method and SOLVE[45] and RESOLVE[46] programs. Phases from RESOLVE were used to autobuild a model with ARP/wARP[47] in warpNtrace mode. The protein complex crystal structures were solved by molecular replacement using AMoRe[48] and the selenomethionine-substitued ΔEED structure as the search model. Standard refinement was carried out with refmac5[49] and CNS[50] together with manual model building with Coot[51]. Figures were created with Pymol (DeLαno Scientific; http://pymol.sourceforge.net/). Binding studies. All fluorescence emission spectra were measured using a dansyl labelled peptide (sequence: KKKARKSAGAA-dansyl) at 20° C in 50 mM Tris-HCl pH 8.7, 150 mM NaCl and 3 mM TCEP using a SPEX FluoroMax fluorimeter. Binding of dansyl peptide to EED was monitored by titrating EED into 5 μM peptide (excitation 330nm, emission 537nm). Dissociation constants for the unlabelled histone peptides were determined using a competition assay by adding excess peptide to a complex of 35uM EED with 35 uM dansyl peptide. The subsequent decrease in fluorescence was monitored. The affinity of Δ77EED for various histone peptides was also measured using isothermal titration calorimetry (ITC) at 20 or 210C by injecting the peptide in question at 400 μM into the ITC cell containing Δ77EED at 40 μM (buffer as above). References
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Supplementary Table 1. Crystallographic statistics.
Table 1 Data collection and refinement statistics of ΔEED co-crystallised with histone- derived peptides
Hl K26me3 H3K9me3 H3K27me3 H4K20me3
Data collection
Space group P2i2i2i P2ι2i2i P2i2i2i P2i2,2i
Cell dimensions a, b, c (λ) 57.5, 85.2, 57.6, 85.1 , 57.8, 85.2, 57.7, 85.2,
91.1 91.3 90.8 91.2 a, β, χ {°) m 90, 90, 90 90, 90, 90 90, 90, 90 90, 90, 90
Resolution (A) 30.0-2.65 50.0-2.45 50.0-2.75 50.0-2.10
(2.74-2.65)* (2.54-2.45)* (2.85-2.75)* (2.18-2.10)*
Rsym Or Kmerge 0.1 19 (0.389) 0.1 17 (0.352) 0.103 (0.443) 0.109 (0.321 ) l/σl 1 1.3 (3.2) 9.9 (3.1 ) 9.2 (2.2) 1 1.4 (4.7)
Completeness 98.1 (98.8) 95.5 (97.8) 95.7(97.7) 98.9 (99.1 )
(%)
Redundancy 4.2 (4.0) 4.1 (4.0) 2.8 (2.8) 4.6 (4.6)
Refinement
Resolution (A) 30.00 - 2.65 50.00 - 2.45 50.00 - 2.75 50.00 - 2.10
No. reflections 12670 15472 1 1058 25288
R work/ Rfree 0.180/0.259 0.181 /0.244 0.194/0.256 0.166/0.204
No. atoms
Protein (chain 2947 2903 2915 291 1
A)
Ligand (chain 53 41 39 70
B) Water 166 230 75 400
B-factors
Protein 17.42 16.53 32.62 16.30
Ligand/ion 37.04 27.58 75.23 36.74
Water 16.42 21.04 25.33 31.02
R.m.s deviations
Bond lengths 0.009 0.010 0.008 0.009
(A)
Bond angles (°) 1.215 1.287 1.107 1.209
Number of crystals for each structure should be noted in footnote. *Highest resolution shell is shown in parenthesis.
Table 2 Data collection, phasing and refinement statistics of ΔEED/NDSB-195
Native SeMet
Data collection
Space group P2i2i2ι P2i2i2i
Cell dimensions a, b, c (A) 57.7, 85.0, 90.8 57. 9, 85.3, 90. 9 cc, β, y {°) 90, 90, 90 90, 90, 90
Peak
Wavelength (A) 0.97900 0.97900
Resolution (A) 30.0-1.95 30.0-1.90
(2.02-1.95)* (1.97-1.90)
Rsym Of Rmerge 0.091 (0.426) 0.1 12 (0.500) l/σl 14.5 (2.1) 14.3 (1.8)
Completeness (%) 98.5 (91.0) 95.1 (71.4)
Redundancy 4.4 (3.2) 6.5 (2.7)
Refinement
Resolution (A) 30-1.95
No. reflections 31442
R work/ Rfree 0.197 / 0.232
No. atoms 3145
Protein 2895
Ligand/ion 12
Water 238
Average B factor 21.72
R.m.s deviations
Bond lengths 0.021 (A) Bond angles (°) 1.680
Number of xtals for each structure should be noted in footnote. ""Highest resolution shell is shown in parenthesis.
The invention makes use of the following atomic co-ordinates which describe, among other things, the crystal structure of a domain of the EED protein and the co-ordinates for the EED complexes with the additive (add1-renum2) and H3K27me3 (refmac17) peptide.
Atomic Co-ordinates for Addl-Renum2:
REMARK Written by O version 12.0.0 REMARK Wed Aug 20 14:12:44 2008
CRYSTl 57 . 803 85. 337 91 . 231 90.00 90.00 90.00
ORIGXl 1.000000 0.000000 0.000000 0.00000
ORI GX2 0.000000 1.000000 0.000000 0.00000
0RIGX3 0.000000 0.000000 1.000000 0.00000
SCALEl 0.017300 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011718 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010961 0.00000
ATOM 1 N TYR A 80 -13.318 7. 322 20.832 1.00 42.09 A N
ATOM 2 CA TYR A 80 -12.817 8. 712 20.589 1 .00 42. 19 A C ATOM 3 CB TYR A 80 11.494 8.964 21.340 1.00 42.86 A C
ATOM 4 CG TYR A 80 11.669 9.143 22.826 1.00 42.88 A C
ATOM 5 CDl TYR A 80 12.463 10.176 23.326 1.00 44.14 A C
ATOM 6 CEl TYR A 80 12.638 10.361 24.707 1.00 45.51 A C
ATOM 7 CZ TYR A 80 12.004 9.513 25.602 1.00 44.58 A C
ATOM 8 OH TYR A 80 12.187 9.714 26.966 1.00 43.66 A O
ATOM 9 CE2 TYR A 80 11.199 8.472 25.117 1.00 44.49 A C
ATOM 10 CD2 TYR A 80 11.041 8.294 23.729 1.00 42.28 A C
ATOM 11 C TYR A 80 12.601 8.901 19.098 1.00 41.55 A C
ATOM 12 O TYR A 80 12.041 8.016 18.441 1.00 41.90 A O
ATOM 13 N SER A 81 13.065 10.042 18.577 1.00 40.10 A N
ATOM 14 CA SER A 81 12.988 10.386 17.137 1.00 38.15 A C
ATOM 15 CB SER A 81 14.294 10.061 16.396 1.00 38.22 A C
ATOM 16 OG SER A 81 14.706 8.727 16.637 1.00 42.51 A O
ATOM 17 C SER A 81 12.708 11.877 16.979 1.00 35.05 A C
ATOM 18 O SER A 81 13.420 12.724 17.505 1.00 36.07 A O
ATOM 19 N PHE A 82 11.674 12.170 16.222 1.00 31.45 A N
ATOM 20 CA PHE A 82 11.191 13.512 16.042 1.00 21.11 A C
ATOM 21 CB PHE A 82 -9.785 13.630 16.604 1.00 27.77 A C
ATOM 22 CG PHE A 82 -9.714 13.625 18.099 1.00 26.95 A C
ATOM 23 CDl PHE A 82 -9.681 14.816 18.791 1.00 25.31 A C
ATOM 24 CEl PHE A 82 -9.594 14.833 20.179 1.00 29.01 A C
ATOM 25 CZ PHE A 82 -9.511 13.615 20.892 1.00 29.56 A C
ATOM 26 CE2 PHE A 82 -9.524 12.412 20.205 1.00 30.39 A C
ATOM 27 CD2 PHE A 82 -9.636 12.419 18.809 1.00 28.80 A C
ATOM 28 C PHE A 82 11.090 13.693 14.563 1.00 26.15 A C
ATOM 29 O PHE A 82 10.752 12.742 13.873 1.00 24.15 A O
ATOM 30 N LYS A 83 11.354 14.914 14.092 1.00 24.07 A N
ATOM 31 CA LYS A 83 11.215 15.258 12.681 1.00 24.56 A C
ATOM 32 CB LYS A 83 12.615 15.662 12.174 1.00 24.90 A C
ATOM 33 CG LYS A 83 12.736 16.713 11.055 1.00 28.65 A C
ATOM 34 CD LYS A 83 14.134 17.397 11.169 1.00 28.53 A C
ATOM 35 CE LYS A 83 14.350 17.842 12.659 1.00 34.99 A C
ATOM 36 NZ LYS A 83 15.436 18.822 12.971 1.00 35.18 A N
ATOM 37 C LYS A 83 10.152 16.385 12.525 1.00 22.03 A C
ATOM 38 O LYS A 83 10.173 17.340 13.261 1.00 21.38 A O
ATOM 39 N CYS A 84 -9.219 16.257 11.593 1.00 21.19 A N
ATOM 40 CA CYS A 84 -8.227 17.306 11.401 1.00 21.17 A C
ATOM 41 CB CYS A 84 -7.008 16.802 10.632 1.00 19.27 A C
ATOM 42 SG CYS A 84 -5.801 18.129 10.396 1.00 22.37 A S
ATOM 43 C CYS A 84 -8.861 18.517 10.677 1.00 20.94 A C
ATOM 44 O CYS A 84 -9.364 18.369 9.555 1.00 20.85 A O
ATOM 45 N VAL A 85 -8.825 19.694 11.316 1.00 20.56 A N
ATOM 46 CA VAL A 85 -9.579 20.855 10.851 1.00 20.99 A C
ATOM 47 CB VAL A 85 10.596 21.419 11.909 1.00 21.12 A C
ATOM 48 CGl VAL A 85 11.760 20.440 12.131 1.00 20.14 A C
ATOM 49 CG2 VAL A 85 -9.890 21.835 13.257 1.00 19.65 A C
ATOM 50 C VAL A 85 -8.725 22.011 10.363 1.00 22.02 A C
ATOM 51 O VAL A 85 -9.248 '22.948 9.761 1.00 23.12 A O
ATOM 52 N ASN A 86 -7.428 21.955 10.607 1.00 21.56 A N
ATOM 53 CA ASN A 86 -6.518 23.007 10.159 1.00 22.36 A C
ATOM 54 CB ASN A 86 -6.854 24.292 10.939 1.00 22.59 A C
ATOM 55 CG ASN A 86 -6.297 25.577 10.283 1.00 24.37 A C
ATOM 56 ODl ASN A 86 -5.723 25.541 9.185 1.00 22.88 A O
ATOM 57 ND2 ASN A 86 -6.482 26.715 10.968 1.00 20.36 A N
ATOM 58 C ASN A 86 -5.079 22.573 10.406 1.00 22.56 A C
ATOM 59 O ASN A 86 -4.829 21.621 11.151 1.00 21.65 A O
ATOM 60 N SER A 87 -4.138 23.264 9.772 1.00 22.86 A N
ATOM 61 CA SER A 87 -2.724 23.082 10.010 1.00 22.87 A C
ATOM 62 CB SER A 87 -2.159 21.912 9.198 1.00 23.13 A C
ATOM 63 OG SER A 87 -2.203 22.123 7.801 1.00 23.56 A O
ATOM 64 C SER A 87 -2.030 24.388 9.630 1.00 23.88 A C
ATOM 65 O SER A 87 -2.578 25.165 8.833 1.00 23.70 A O
ATOM 66 N LEU A 88 -0.871 24.659 10.227 1.00 24.48 A N
ATOM 67 CA LEU A 88 -0.010 25.762 9.748 1.00 25.94 A C
ATOM 68 CB LEU A 88 -0.439 27.124 10.295 1.00 26.86 A C
ATOM 69 CG LEU A 88 -0.455 27.375 11.793 1.00 29.37 A C
ATOM 70 CDl LEU A 88 0.712 28.319 12.132 1.00 34.27 A C
ATOM 71 CD2 LEU A 88 -1.744 28.054 12.165 1.00 31.94 A C
ATOM 72 C LEU A 88 1.467 25.489 9.975 1.00 25.52 A C
ATOM 73 O LEU A 88 1.824 24.499 10.577 1.00 24.12 A O
ATOM 74 N LYS A 89 2.322 26.369 9.462 1.00 25.19 A N
ATOM 75 CA LYS A 89 3.738 26.202 9.582 1.00 25.93 A C
ATOM 76 CB LYS A 89 4.313 25.798 8.213 1.00 25.88 A C
ATOM 77 CG LYS A 89 5.736 25.287 8.283 1.00 28.34 A C
ATOM 78 CD LYS A 89 6.204 24.609 6.960 1.00 29.84 A C
ATOM 79 CE LYS A 89 5.140 23.671 6.363 1.00 36.46 A C ATOM 80 NZ LYS A 89 5.743 22.432 5.783 1.00 40.09 A N
ATOM 81 C LYS A 89 4.322 27.532 10.041 1.00 25.64 A C
ATOM 82 O LYS A 89 3.953 28.587 9.478 1.00 25.32 A O
ATOM 83 N GLϋ A 90 5.206 27.503 11.039 1.00 23.57 A N
ATOM 84 CA GLO A 90 5.874 28.744 11.476 1.00 24.21 A C
ATOM 85 CB GLO A 90 6.377 28.615 12.914 1.00 23.74 A C
ATOM 86 CG GLO A 90 5.203 28.373 13.922 1.00 20.99 A C
ATOM 87 CD GLO A 90 5.567 28.571 15.383 1.00 22.61 A C
ATOM 88 OEl GLO A 90 6.795 28.660 15.730 1.00 19.65 A O
ATOM 89 OE2 GLO A 90 4.604 28.594 16.200 1.00 20.45 A O
ATOM 90 C GLO A 90 7.030 29.084 10.515 1.00 25.87 A C
ATOM 91 O GLO A 90 7.645 28.176 9.959 1.00 25.16 A O
ATOM 92 N ASP A 91 7.333 30.371 10.352 1.00 27.05 A N
ATOM 93 CA ASP A 91 8.367 30.846 9.371 1.00 28.28 A C
ATOM 94 CB ASP A 91 8.332 32.387 9.244 1.00 29.04 A C
ATOM 95 CG ASP A 91 8.662 33.117 10.588 1.00 31.37 A C
ATOM 96 ODl ASP A 91 9.473 32.615 11.396 1.00 35.39 A O
ATOM 97 OD2 ASP A 91 8.090 34.200 10.857 1.00 36.03 A O
ATOM 98 C ASP A 91 9.816 30.439 9.650 1.00 27.99 A C
ATOM 99 O ASP A 91 10.662 30.572 8.782 1.00 27.86 A O
ATOM 100 N HIS A 92 10.142 30.004 10.859 1.00 27.57 A N
ATOM 101 CA HIS A 92 11.542 29.732 11.165 1.00 26.92 A C
ATOM 102 CB HIS A 92 11.784 29.794 12.665 1.00 26.63 A C
ATOM 103 CG HIS A 92 10.801 29.001 13.457 1.00 24.72 A C
ATOM 104 NDl HIS A 92 10.838 27.621 13.519 1.00 22.19 A N
ATOM 105 CEl HIS A 92 9.871 27.193 14.312 1.00 19.56 A C
ATOM 106 NE2 HIS A 92 9.202 28.246 14.756 1.00 20.88 A N
ATOM 107 CD2 HIS A 92 9.764 29.389 14.240 1.00 23.11 A C
ATOM 108 C HIS A 92 12.073 28.407 10.591 1.00 27.99 A C
ATOM 109 O HIS A 92 13.294 28.184 10.581 1.00 28.31 A O
ATOM 110 N ASN A 93 11.153 27.534 10.158 1.00 28.22 A N
ATOM 111 CA ASN A 93 11.478 26.189 9.660 1.00 28.32 A C
ATOM 112 CB ASN A 93 12.000 26.273 8.196 1.00 29.36 A C
ATOM 113 CG ASN A 93 10.985 26.933 7.242 1.00 33.76 A C
ATOM 114 ODl ASN A 93 11.348 27.804 6.420 1.00 38.74 A O
ATOM 115 ND2 ASN A 93 9.708 26.534 7.352 1.00 35.96 A N
ATOM 116 C ASN A 93 12.374 25.296 10.566 1.00 27.06 A C
ATOM 117 O ASN A 93 13.010 24.356 10.075 1.00 27.82 A O
ATOM 118 N GLN A 94 12.423 25.580 11.877 1.00 24.69 A N
ATOM 119 CA GLN A 94 13.124 24.743 12.848 1.00 23.06 A C
ATOM 120 CB GLN A 94 13.843 25.632 13.872 1.00 22.96 A C
ATOM 121 CG GLN A 94 14.713 26.714 13.261 1.00 28.56 A C
ATOM 122 CD GLN A 94 15.734 26.150 12.293 1.00 35.12 A C
ATOM 123 OEl GLN A 94 16.611 25.373 12.690 1.00 36.84 A O
ATOM 124 NE2 GLN A 94 15.616 26.522 10.996 1.00 36.70 A N
ATOM 125 C GLN A 94 12.122 23.845 13.570 1.00 21.09 A C
ATOM 126 O GLN A 94 10.919 24.143 13.549 1.00 19.27 A O
ATOM 127 N PRO A 95 12.588 22.737 14.205 1.00 19.50 A N
ATOM 128 CA PRO A 95 11.561 21.982 14.924 1.00 19.35 A C
ATOM 129 CB PRO A 95 12.355 20.852 15.569 1.00 19.16 A C
ATOM 130 CG PRO A 95 13.566 20.685 14.694 1.00 19.60 A C
ATOM 131 CD PRO A 95 13.913 22.091 14.320 1.00 20.08 A C
ATOM 132 C PRO A 95 10.753 22.756 15.998 1.00 18.13 A C
ATOM 133 O PRO A 95 11.283 23.633 16.729 1.00 18.15 A O
ATOM 134 N LEO A 96 9.477 22.429 16.068 1.00 17.33 A N
ATOM 135 CA LEO A 96 8.653 22.806 17.229 1.00 17.20 A C
ATOM 136 CB LEO A 96 7.222 23.096 16.833 1.00 16.11 A C
ATOM 137 CG LEO A 96 6.966 24.384 16.049 1.00 16.26 A C
ATOM 138 CDl LEO A 96 5.466 24.478 15.757 1.00 12.89 A C
ATOM 139 CD2 LEO A 96 7.468 25.630 16.796 1.00 15.55 A C
ATOM 140 C LEO A 96 8.763 21.639 18.197 1.00 17.09 A C
ATOM 141 O LEO A 96 8.276 20.538 17.924 1.00 17.81 A O
ATOM 142 N PHE A 97 9.509 21.857 19.275 1.00 15.71 A N
ATOM 143 CA PHE A 97 9.735 20.800 20.245 1.00 14.59 A C
ATOM 144 CB PHE A 97 11.062 21.065 20.972 1.00 14.07 A C
ATOM 145 CG PHE A 97 12.303 20.777 20.129 1.00 16.66 A C
ATOM 146 CDl PHE A 97 12.588 19.464 19.703 1.00 16.41 A C
ATOM 147 CEl PHE A 97 13.770 19.187 18.946 1.00 19.12 A C
ATOM 148 CZ PHE A 97 14.658 20.232 18.654 1.00 17.77 A C
ATOM 149 CE2 PHE A 97 14.394 21.549 19.116 1.00 16.58 A C
ATOM 150 CD2 PHE A 97 13.217 21.808 19.833 1.00 13.26 A C
ATOM 151 C PHE A 97 8.577 20.644 21.244 1.00 15.04 A C
ATOM 152 O PHE A 97 8.339 19.547 21.765 1.00 14.39 A O
ATOM 153 N GLY A 98 7.857 21.721 21.514 1.00 13.48 A N
ATOM 154 CA GLY A 98 6.909 21.700 22.626 1.00 13.70 A C
ATOM 155 C GLY A 98 5.620 22.427 22.262 1.00 13.03 A C
ATOM 156 O GLY A 98 5.659 23.394 21.491 1.00 13.16 A O ATOM 157 N VAL A 99 4.516 21.985 22.874 1.00 11.82 A N
ATOM 158 CA VAL A 99 3.196 22.642 22.832 1.00 12.64 A C
ATOM 159 CB VAL A 99 2.360 22.186 21.573 1.00 10.02 A C
ATOM 160 CGl VAL A 99 2.208 20.640 21.556 1.00 9.68 A C
ATOM 161 CG2 VAL A 99 1.022 22.900 21.503 1.00 12.81 A C
ATOM 162 C VAL A 99 2.425 22.411 24.188 1.00 13.28 A C
ATOM 163 O VAL A 99 2.494 21.308 24.799 1.00 13.56 A O
ATOM 164 N GLN A 100 1.727 23.443 24.666 1.00 12.29 A N
ATOM 165 CA GLN A 100 0.964 23.381 25.918 1.00 12.59 A C
ATOM 166 CB GLN A 100 1.805 23.831 27.162 1.00 11.82 A C
ATOM 167 CG GLN A 100 3.089 23.029 27.381 1.00 12.91 A C
ATOM 168 CD GLN A 100 2.855 21.658 27.983 1.00 13.15 A C
ATOM 169 OEl GLN A 100 1.751 21.355 28.433 1.00 13.66 A O
ATOM 170 NE2 GLN A 100 3.902 20.801 27.964 1.00 13.00 A N
ATOM 171 C GLN A 100 -0.257 24.311 25.802 1.00 13.26 A C
ATOM 172 O GLN A 100 -0.100 25.543 25.610 1.00 12.81 A O
ATOM 173 N PHE A 101 -1.460 23.729 25.877 1.00 12.44 A N
ATOM 174 CA PHE A 101 -2.643 24.547 26.125 1.00 13.26 A C
ATOM 175 CB PHE A 101 -3.943 23.722 26.036 1.00 11.79 A C
ATOM 176 CG PHE A 101 -4.571 23.682 24.642 1.00 13.57 A C
ATOM 177 CDl PHE A 101 -5.405 24.707 24.216 1.00 11.67 A C
ATOM 178 CEl PHE A 101 -6.018 24.677 22.946 1.00 15.76 A C
ATOM 179 CZ PHE A 101 -5.755 23.596 22.075 1.00 14.99 A C
ATOM 180 CE2 PHE A 101 -4.916 22.572 22.477 1.00 13.47 A C
ATOM 181 CD2 PHE A 101 -4.315 22.612 23.781 1.00 13.46 A C
ATOM 182 C PHE A 101 -2.529 25.152 27.531 1.00 13.56 A C
ATOM 183 O PHE A 101 -2.006 24.521 28.472 1.00 13.24 A O
ATOM 184 N ASN A 102 -3.006 26.376 27.691 1.00 15.03 A N
ATOM 185 CA ASN A 102 -3.155 26.921 29.020 1.00 16.24 A C
ATOM 186 CB ASN A 102 -3.238 28.446 29.005 1.00 15.78 A C
ATOM 187 CG ASN A 102 -3.421 29.003 30.406 1.00 17.87 A C
ATOM 188 ODl ASN A 102 -2.988 28.398 31.378 1.00 18.96 A O
ATOM 189 ND2 ASN A 102 -4.065 30.139 30.513 1.00 21.22 A N
ATOM 190 C ASN A 102 -4.397 26.340 29.783 1.00 17.49 A C
ATOM 191 O ASN A 102 -5.534 26.620 29.413 1.00 17.89 A O
ATOM 192 N TRP A 103 -4.184 25.519 30.806 1.00 18.61 A N
ATOM 193 CA TRP A 103 -5.342 25.056 31.641 1.00 22.61 A C
ATOM 194 CB TRP A 103 -5.195 23.607 32.105 1.00 20.98 A C
ATOM 195 CG TRP A 103 -5.027 22.586 31.004 1.00 19.27 A C
ATOM 196 CDl TRP A 103 -5.268 22.752 29.644 1.00 19.51 A C
ATOM 197 NEl TRP A 103 -4.985 21.569 28.961 1.00 17.47 A N
ATOM 198 CE2 TRP A 103 -4.604 20.612 29.876 1.00 19.65 A C
ATOM 199 CD2 TRP A 103 -4.628 21.211 31.173 1.00 20.17 A C
ATOM 200 CE3 TRP A 103 -4.277 20.428 32.288 1.00 19.87 A C
ATOM 201 CZ3 TRP A 103 -3.914 19.066 32.063 1.00 19.74 A C
ATOM 202 CH2 TRP A 103 -3.905 18.521 30.769 1.00 19.90 A C
ATOM 203 CZ2 TRP A 103 -4.246 19.272 29.671 1.00 19.68 A C
ATOM 204 C TRP A 103 -5.585 25.953 32.869 1.00 25.88 A C
ATOM 205 O TRP A 103 -6.590 25.777 33.578 1.00 27.48 A O
ATOM 206 N HIS A 104 -4.663 26.893 33.113 1.00 29.80 A N
ATOM 207 CA HIS A 104 -4.626 27.700 34.353 1.00 34.09 A C
ATOM 208 CB HIS A 104 -3.186 28.026 34.766 1.00 33.93 A C
ATOM 209 CG HIS A 104 -2.508 26.970 35.591 1.00 37.02 A C
ATOM 210 NDl HIS A 104 -1.898 25.864 35.037 1.00 36.68 A N
ATOM 211 CEl HIS A 104 -1.374 25.125 36.000 1.00 37.67 A C
ATOM 212 NE2 HIS A 104 -1.606 25.720 37.158 1.00 39.26 A N
ATOM 213 CD2 HIS A 104 -2.306 26.878 36.932 1.00 37.78 A C
ATOM 214 C HIS A 104 -5.298 29.017 34.076 1.00 36.93 A C
ATOM 215 O HIS A 104 -4.640 30.056 34.156 1.00 37.67 A O
ATOM 216 N SER A 105 -6.576 28.973 33.686 1.00 40.27 A N
ATOM 217 CA SER A 105 -7.441 30.175 33.542 1.00 43.17 A C
ATOM 218 CB SER A 105 -6.694 31.506 33.850 1.00 44.25 A C
ATOM 219 OG SER A 105 -7.422 32.388 34.747 1.00 45.66 A O
ATOM 220 C SER A 105 -8.199 30.274 32.199 1.00 43.71 A C
ATOM 221 O SER A 105 -9.309 30.802 32.185 1.00 43.68 A O
ATOM 222 N LYS A 106 -7.591 29.780 31.101 1.00 44.70 A N
ATOM 223 CA LYS A 106 -8.116 29.911 29.701 1.00 44.67 A C
ATOM 224 CB LYS A 106 -6.988 30.230 28.677 1.00 45.39 A C
ATOM 225 CG LYS A 106 -6.573 31.722 28.544 1.00 46.29 A C
ATOM 226 CD LYS A 106 -5.040 31.926 28.320 1.00 45.33 A C
ATOM 227 CE LYS A 106 -4.669 33.422 28.277 1.00 46.58 A C
ATOM 228 NZ LYS A 106 -3.231 33.759 27.921 1.00 45.27 A N
ATOM 229 C LYS A 106 -8.871 28.665 29.226 1.00 44.71 A C
ATOM 230 O LYS A 106 -8.487 27.529 29.528 1.00 44.85 A O
ATOM 231 N LEU A 111 -9.729 29.418 24.088 1.00 25.68 A N
ATOM 232 CA LEU A 111 -8.751 28.334 24.213 1.00 23.93 A C
ATOM 233 CB LEU A 111 -9.296 27.057 23.531 1.00 24.95 A C ATOM 234 CG LEU A 111 10.558 26.383 24.105 1.00 26.31 A C
ATOM 235 CDl LED A 111 10.653 24.958 23.578 1.00 31.57 A C
ATOM 236 CD2 LEO A 111 10.557 26.354 25.635 1.00 33.69 A C
ATOM 237 C LEU A 111 -7.353 28.724 23.628 1.00 22.98 A C
ATOM 238 O LED A 111 -7.200 28.845 22.398 1.00 22.11 A O
ATOM 239 N VAL A 112 -6.353 28.907 24.499 1.00 19.53 A N
ATOM 240 CA VAL A 112 -5.024 29.415 24.125 1.00 17.34 A C
ATOM 241 CB VAL A 112 -4.694 30.733 24.916 1.00 18.36 A C
ATOM 242 CGl VAL A 112 -3.223 31.152 24.812 1.00 18.94 A C
ATOM 243 CG2 VAL A 112 -5.613 31.913 24.457 1.00 19.90 A C
ATOM .244 C VAL A 112 -3.938 28.328 24.314 1.00 16.07 A C
ATOM 245 O VAL A 112 -3.895 27.634 25.340 1.00 14.18 A O
ATOM 246 N PHE A 113 -3.075 28.185 23.322 1.00 15.35 A N
ATOM 247 CA PHE A 113 -1.916 27.314 23.429 1.00 15.78 A C
ATOM 248 CB PHE A 113 -2.137 25.974 22.658 1.00 15.54 A C
ATOM 249 CG PHE A 113 -2.113 26.090 21.158 1.00 15.82 A C
ATOM 250 CDl PHE A 113 -0.891 25.949 20.434 1.00 13.59 A C
ATOM 251 CEl PHE A 113 -0.887 26.030 19.031 1.00 17.63 A C
ATOM 252 CZ PHE A 113 -2.109 26.228 18.328 1.00 16.28 A C
ATOM 253 CE2 PHE A 113 -3.324 26.363 19.034 1.00 16.03 A C
ATOM 254 CD2 PHE A 113 -3.316 26.305 20.445 1.00 16.91 A C
ATOM 255 C PHE A 113 -0.579 27.999 23.051 1.00 16.18 A C
ATOM 256 O PHE A 113 -0.552 28.928 22.207 1.00 15.24 A O
ATOM 257 N ALA A 114 0.516 27.534 23.678 1.00 15.52 A N
ATOM 258 CA ALA A 114 1.867 27.988 23.353 1.00 14.34 A C
ATOM 259 CB ALA A 114 2.659 28.286 24.648 1.00 13.25 A C
ATOM 260 C ALA A 114 2.622 26.945 22.505 1.00 14.19 A C
ATOM 261 O ALA A 114 2.467 25.734 22.692 1.00 13.63 A O
ATOM 262 N THR A 115 3.444 27.403 21.568 1.00 14.18 A N
ATOM 263 CA THR A 115 4.374 26.491 20.874 1.00 13.93 A C
ATOM 264 CB THR A 115 4.194 26.471 19.345 1.00 13.74 A C
ATOM 265 OGl THR A 115 4.487 27.779 18.865 1.00 13.11 A O
ATOM 266 CG2 THR A 115 2.744 26.127 18.965 1.00 14.27 A C
ATOM 267 C THR A 115 5.767 26.994 21.158 1.00 14.44 A C
ATOM 268 O THR A 115 5.948 28.191 21.345 1.00 14.37 A O
ATOM 269 N VAL A 116 6.749 26.085 21.205 1.00 16.21 A N
ATOM 270 CA VAL A 116 8.144 26.461 21.486 1.00 17.24 A C
ATOM 271 CB VAL A 116 8.655 26.127 22.949 1.00 18.08 A C
ATOM 272 CGl VAL A 116 8.047 27.075 23.964 1.00 20.05 A C
ATOM 273 CG2 VAL A 116 8.304 24.707 23.345 1.00 19.01 A C
ATOM 274 C VAL A 116 9.043 25.813 20.433 1.00 16.85 A C
ATOM 275 O VAL A 116 8.974 24.626 20.190 1.00 15.89 A O
ATOM 276 N GLY A 117 9.876 26.625 19.805 1.00 17.45 A N
ATOM 277 CA GLY A 117 10.786 26.135 18.796 1.00 17.71 A C
ATOM 278 C GLY A 117 11.665 27.303 18.397 1.00 18.69 A C
ATOM 279 O GLY A 117 11.340 28.468 18.691 1.00 19.38 A O
ATOM 280 N SER A 118 12.789 26.992 17.751 1.00 18.53 A N
ATOM 281 CA SER A 118 13.804 27.991 17.438 1.00 19.07 A C
ATOM 282 CB SER A 118 13.289 28.925 16.341 1.00 19.14 A C
ATOM 283 OG SER A 118 14.274 • 29.815 15.928 1.00 17.19 A O
ATOM 284 C SER A 118 14.165 28.709 18.743 1.00 18.56 A C
ATOM 285 O SER A 118 14.195 28.069 19.807 1.00 19.62 A O
ATOM 286 N ASN A 119 14.366 30.026 18.698 1.00 18.24 A N
ATOM 287 CA ASN A 119 14.512 30.818 19.917 1.00 17.29 A C
ATOM 288 CB ASN A 119 15.716 31.783 19.812 1.00 17.84 A C
ATOM 289 CG ASN A 119 15.502 32.883 18.775 1.00 17.65 A C
ATOM 290 ODl ASN A 119 16.138 33.971 18.807 1.00 19.58 A O
ATOM 291 ND2 ASN A 119 14.626 32.605 17.833 1.00 22.24 A N
ATOM 292 C ASN A 119 13.264 31.582 20.321 1.00 17.24 A C
ATOM 293 O ASN A 119 13.357 32.704 20.853 1.00 18.09 A O
ATOM 294 N ARG A 120 12.090 31.002 20.077 1.00 17.54 A N
ATOM 295 CA ARG A 120 10.846 31.705 20.392 1.00 16.78 A C
ATOM 296 CB ARG A 120 10.256 32.376 19.154 1.00 17.98 A C
ATOM 297 CG ARG A 120 9.510 31.459 18.253 1.00 18.38 A C
ATOM 298 CD ARG A 120 8.918 32.251 17.119 1.00 20.57 A C
ATOM 299 NE ARG A 120 9.880 32.617 16.077 1.00 18.60 A N
ATOM 300 CZ ARG A 120 9.593 32.809 14.780 1.00 19.13 A C
ATOM 301 NHl ARG A 120 8.359 32.654 14.312 1.00 19.01 A N
ATOM 302 NH2 ARG A 120 10.575 33.150 13.923 1.00 21.21 A N
ATOM 303 C ARG A 120 9.778 30.856 21.080 1.00 16.05 A C
ATOM 304 O ARG A 120 9.878 29.629 21.147 1.00 16.07 A O
ATOM 305 N VAL A 121 8.808 31.545 21.652 1.00 14.61 A N
ATOM 306 CA VAL A 121 7.584 30.937 22.103 1.00 14.37 A C
ATOM 307 CB VAL A 121 7.488 30.767 23.650 1.00 14.69 A C
ATOM 308 CGl VAL A 121 7.705 32.075 24.348 1.00 15.29 A C
ATOM 309 CG2 VAL A 121 6.096 30.133 24.029 1.00 17.13 A C
ATOM 310 C VAL A 121 6.442 31.760 21.507 1.00 14.05 A C ATOM 311 O VAL A 121 6.512 32.993 21.464 1.00 14.25 A O
ATOM 312 N THR A 122 5.456 31.057 20.968 1.00 13.98 A N
ATOM 313 CA THR A 122 4.310 31.667 20.261 1.00 14.92 A C
ATOM 314 CB THR A 122 4.331 31.342 18.742 1.00 14.81 A C
ATOM 315 OGl THR A 122 5.615 31.695 18.186 1.00 17.56 A O
ATOM 316 CG2 THR A 122 3.222 32.145 17.974 1.00 14.80 A C
ATOM 317 C THR A 122 2.937 31.264 20.840 1.00 14.50 A C
ATOM 318 O THR A 122 2.662 30.067 21.091 1.00 13.73 A O
ATOM 319 N LEU A 123 2.095 32.269 21.030 1.00 13.95 A N
ATOM 320 CA LEU A 123 0.729 32.060 21.513 1.00 16.73 A C
ATOM 321 CB LEU A 123 0.399 33.107 22.586 1.00 16.45 A C
ATOM 322 CG LEU A 123 0.571 32.644 24.028 1.00 22.02 A C
ATOM 323 CDl LEU A 123 1.710 31.676 24.290 1.00 19.81 A C
ATOM 324 CD2 LEU A 123 0.477 33.718 25.123 1.00 19.78 A C
ATOM 325 C LEU A 123 -0.274 32.118 20.341 1.00 15.11 A C
ATOM 326 O LEU A 123 -0.152 32.985 19.465 1.00 16.30 A O
ATOM 327 N TYR A 124 -1.197 31.161 20.324 1.00 15.35 A N
ATOM 328 CA TYR A 124 -2.329 31.070 19.370 1.00 15.85 A C
ATOM 329 CB TYR A 124 -2.194 29.846 18.465 1.00 15.25 A C
ATOM 330 CG TYR A 124 -0.929 29.804 17.624 1.00 16.37 A C
ATOM 331 CDl TYR A 124 -0.932 30.343 16.328 1.00 14.69 A C
ATOM 332 CEl TYR A 124 0.169 30.334 15.541 1.00 14.41 A C
ATOM 333 CZ TYR A 124 1.351 29.771 16.020 1.00 15.09 A C
ATOM 334 OH TYR A 124 2.433 29.791 15.152 1.00 17.74 A O
ATOM 335 CE2 TYR A 124 1.417 29.214 17.311 1.00 16.33 A C
ATOM 336 CD2 TYR A 124 0.270 29.246 18.124 1.00 10.82 A C
ATOM 337 C TYR A 124 -3.641 30.897 20.136 1.00 17.43 A C
ATOM 338 O TYR A 124 -3.689 30.306 21.240 1.00 16.30 A O
ATOM 339 N GLU A 125 -4.729 31.344 19.522 1.00 17.50 A N
ATOM 340 CA GLU A 125 -6.022 31.162 20.163 1.00 18.64 A C
ATOM 341 CB GLU A 125 -6.555 32.540 20.509 1.00 17.79 A C
ATOM 342 CG GLU A 125 -7.879 32.620 21.225 1.00 19.71 A C
ATOM 343 CD GLU A 125 -8.174 34.099 21.519 1.00 21.42 A C
ATOM 344 OEl GLU A 125 -7.649 34.628 22.499 1.00 17.98 A O
ATOM ' 345 OE2 GLU A 125 -8.883 34.744 20.742 1.00 17.38 A O
ATOM 346 C GLU A 125 -6.935 30.360 19.206 1.00 19.37 A C
ATOM 347 O GLU A 125 -7.083 30.704 18.020 1.00 19.27 A O
ATOM 348 N CYS A 126 -7.521 29.267 19.706 1.00 19.35 A N
ATOM 349 CA CYS A 126 -8.491 28.484 18.887 1.00 20.61 A C
ATOM 350 CB CYS A 126 -8.614 27.044 19.388 1.00 19.10 A C
ATOM 351 SG CYS A 126 -7.029 26.204 19.425 1.00 19.70 A S
ATOM 352 C CYS A 126 -9.908 29.112 18.737 1.00 20.36 A C
ATOM 353 O CYS A 126 10.546 29.530 19.728 1.00 20.69 A O
ATOM 354 N HIS A 127 10.356 29.175 17.491 1.00 21.87 A N
ATOM 355 CA HIS A 127 11.702 29.665 17.142 1.00 22.61 A C
ATOM 356 CB HIS A 127 11.614 31.038 16.512 1.00 21.97 A C
ATOM 357 CG HIS A 127 11.182 32.093 17.476 1.00 24.14 A C
ATOM 358 NDl HIS A 127 12.056 32.717 18.350 1.00 24.43 A N
ATOM 359 CEl HIS A 127 11.383 33.588 19.086 1.00 23.53 A C
ATOM 360 NE2 HIS A 127 10.110 33.556 18.719 1.00 21.66 A N
ATOM 361 CD2 HIS A 127 -9.955 32.618 17.727 1.00 22.58 A C
ATOM 362 C HIS A 127 12.454 28.666 16.264 1.00 23.97 A C
ATOM 363 O HIS A 127 11.891 27.629 15.862 1.00 22.72 A O
ATOM 364 N SER A 128 13.738 28.957 15.976 1.00 25.68 A N
ATOM 365 CA SER A 128 14.569 28.023 15.183 1.00 27.11 A C
ATOM 366 CB SER A 128 16.071 28.374 15.262 1.00 28.04 A C
ATOM 367 OG SER A 128 16.276 29.771 15.311 1.00 29.28 A O
ATOM 368 C SER A 128 14.082 27.878 13.740 1.00 27.18 A C
ATOM 369 O SER A 128 13.194 28.617 13.312 1.00 27.35 A O
ATOM 370 N GLN A 129 14.651 26.918 13.011 1.00 27.97 A N
ATOM 371 CA GLN A 129 14.227 26.561 11.639 1.00 28.79 A C
ATOM 372 CB GLN A 129 14.790 27.529 10.581 1.00 30.08 A C
ATOM 373 CG GLN A 129 16.339 27.534 10.502 1.00 35.11 A C
ATOM 374 CD GLN A 129 16.986 28.534 11.463 1.00 40.37 A C
ATOM 375 OEl GLN A 129 16.553 29.689 11.554 1.00 43.48 A O
ATOM 376 NE2 GLN A 129 18.034 28.096 12.178 1.00 40.65 A N
ATOM 377 C GLN A 129 12.707 26.345 11.519 1.00 27.60 A C
ATOM 378 O GLN A 129 12.037 26.704 10.508 1.00 26.75 A O
ATOM 379 N GLY A 130 12.192 25.735 12.590 1.00 26.97 A N
ATOM 380 CA GLY A 130 10.792 25.376 12.756 1.00 25.21 A C
ATOM 381 C GLY A 130 -9.769 26.502 12.111 1.00 24.54 A C
ATOM 382 O GLY A 130 -8.573 26.228 12.647 1.00 24.65 A O
ATOM 383 N GLU A 131 10.212 27.756 12.908 1.00 22.91 A N
ATOM 384 CA GLU A 131 -9.268 28.890 12.931 1.00 22.34 A C
ATOM 385 CB GLU A 131 -9.976 30.239 12.975 1.00 22.35 A C
ATOM 386 CG GLU A 131 -8.956 31.389 13.028 1.00 23.61 A C
ATOM 387 CD GLU A 131 -9.555 32.753 13.312 1.00 26.46 A C ATOM 388 OEl GLU A 131 10.717 32.818 13.805 1.00 26.30 A O
ATOM 389 OE2 GLU A 131 -8.835 33.761 13.037 1.00 26.19 A O
ATOM 390 C GLU A 131 -8.301 28.807 14.118 1.00 21.80 A C
ATOM 391 O GLU A 131 -8.721 28.641 15.288 1.00 20.46 A O
ATOM 392 N ILE A 132 -7.019 28.906 13.782 1.00 21.54 A N
ATOM 393 CA ILE A 132 -5.927 29.136 14.736 1.00 22.80 A C
ATOM 394 CB ILE A 132 -4.778 28.108 14.505 1.00 23.52 A C
ATOM 395 CGl ILE A 132 -5.319 26.664 14.379 1.00 24.85 A C
ATOM 396 CDl ILE A 132 -4.355 25.695 13.573 1.00 25.20 A C
ATOM 397 CG2 ILE A 132 -3.742 28.157 15.658 1.00 24.33 A C
ATOM 398 C ILE A 132 -5.388 30.574 14.554 1.00 21.46 A C
ATOM 399 O ILE A 132 -4.596 30.814 13.640 1.00 21.74 A O
ATOM 400 N ARG A 133 -5.804 31.494 15.429 1.00 19.89 A N
ATOM 401 CA ARG A 133 -5.457 32.907 15.386 1.00 18.90 A C
ATOM 402 CB ARG A 133 -6.581 33.723 16.041 1.00 20.32 A C
ATOM 403 CG ARG A 133 -6.567 35.260 15.682 1.00 19.20 A C
ATOM 404 CD ARG A 133 -7.821 36.023 16.211 1.00 22.41 A C
ATOM 405 NE ARG A 133 -9.052 35.429 15.655 1.00 25.16 A N
ATOM 406 CZ ARG A 133 10.295 35.644 16.094 1.00 28.32 A C
ATOM 407 NHl ARG A 133 10.535 36.473 17.110 1.00 25.98 A N
ATOM 408 NH2 ARG A 133 11.314 35.005 15.509 1.00 24.76 A N
ATOM 409 C ARG A 133 -4.106 33.211 16.078 1.00 18.14 A C
ATOM 410 O ARG A 133 -3.947 32.952 17.292 1.00 15.02 A O
ATOM 411 N LEU A 134 -3.136 33.713 15.285 1.00 16.37 A N
ATOM 412 CA LEU A 134 -1.812 34.097 15.782 1.00 15.92 A C
ATOM 413 CB LEU A 134 -0.797 34.366 14.616 1.00 15.67 A C
ATOM 414 CG LEU A 134 0.634 34.852 14.871 1.00 15.00 A C
ATOM 415 CDl LEU A 134 1.389 33.799 15.766 1.00 13.90 A C
ATOM 416 CD2 LEU A 134 1.386 35.101 13.494 1.00 16.58 A C
ATOM 417 C LEU A 134 -1.932 35.313 16.662 1.00 16.24 A C
ATOM 418 O LEU A 134 -2.526 36.310 16.257 1.00 15.14 A O
ATOM 419 N LEU A 135 -1.389 35.211 17.878 1.00 15.22 A N
ATOM 420 CA LEU A 135 -1.340 36.326 18.800 1.00 15.80 A C
ATOM 421 CB LEU A 135 -1.765 35.900 20.236 1.00 15.89 A C
ATOM 422 CG LEU A 135 -3.132 35.191 20.373 1.00 17.75 A C
ATOM 423 CDl LEU A 135 -3.563 34.820 21.837 1.00 17.67 A C
ATOM 424 CD2 LEU A 135 -4.338 35.960 19.603 1.00 14.74 A C
ATOM 425 C LEU A 135 0.028 37.031 18.769 1.00 16.08 A C
ATOM 426 O LEU A 135 0.214 37.999 18.012 1.00 16.13 A O
ATOM 427 N GLN A 136 0.972 36.582 19.609 1.00 15.28 A N
ATOM 428 CA GLN A 136 2.199 37.307 19.801 1.00 15.77 A C
ATOM 429 CB GLN A 136 2.010 38.432 20.844 1.00 15.96 A C
ATOM 430 CG GLN A 136 3.219 39.482 20.995 1.00 16.67 A C
ATOM 431 CD GLN A 136 3.008 40.475 22.156 1.00 14.70 A C
ATOM 432 OEl GLN A 136 2.121 40.284 22.989 1.00 13.93 A O
ATOM. 433 NE2 GLN A 136 3.825 41.511 22.223 1.00 10.74 A N
ATOM 434 C GLN A 136 3.275 36.297 20.238 1.00 17.02 A C
ATOM 435 O GLN A 136 2.951 35.296 20.884 1.00 16.81 A O
ATOM 436 N SER A 137 4.527 36.578 19.883 1.00 15.88 A N
ATOM 437 CA SER A 137 5.697 35.774 20.310 1.00 16.18 A C
ATOM 438 CB SER A 137 6.556 35.408 19.085 1.00 15.64 A C
ATOM 439 OG SER A 137 5.827 34.485 18.266 1.00 14.91 A O
ATOM 440 C SER A 137 6.612 36.507 21.288 1.00 15.24 A C
ATOM 441 O SER A 137 6.752 37.729 21.253 1.00 15.12 A O
ATOM 442 N TYR A 138 7.287 35.731 22.104 1.00 15.52 A N
ATOM 443 CA TYR A 138 8.548 36.157 22.733 1.00 16.20 A C
ATOM 444 CB TYR A 138 8.604 35.720 24.188 1.00 16.66 A C
ATOM 445 CG TYR A 138 9.932 35.977 24.839 1.00 17.70 A C
ATOM 446 CDl TYR A 138 10.228 37.221 25.387 1.00 17.11 A C
ATOM 447 CEl TYR A 138 11.442 37.474 25.963 1.00 19.50 A C
ATOM 448 CZ TYR A 138 12.416 36.472 26.001 1.00 21.38 A C
ATOM 449 OH TYR A 138 13.662 36.721 26.581 1.00 23.56 A O
ATOM 450 CE2 TYR A 138 12.147 35.217 25.467 1.00 21.02 A C
ATOM 451 CD2 TYR A 138 10.907 34.979 24.886 1.00 18.72 A C
ATOM 452 C TYR A 138 9.728 35.571 21.927 1.00 16.95 A C
ATOM 453 O TYR A 138 9.780 34.342 21.668 1.00 16.75 A O
ATOM 454 N VAL A 139 10.649 36.450 21.521 1.00 16.36 A N
ATOM 455 CA VAL A 139 11.860 36.063 20.780 1.00 18.14 A C
ATOM 456 CB VAL A 139 11.967 36.774 19.411 1.00 17.85 A C
ATOM 457 CGl VAL A 139 13.303 36.398 18.678 1.00 18.43 A C
ATOM 458 CG2 VAL A 139 10.759 36.420 18.579 1.00 17.31 A C
ATOM 459 C VAL A 139 13.068 36.370 21.659 1.00 19.11 A C
ATOM 460 O VAL A 139 13.258 37.505 22.073 1.00 18.67 A O
ATOM 461 N ASP A 140 13.851 35.352 22.007 1.00 20.25 A N
ATOM 462 CA ASP A 140 15.042 35.598 22.840 1.00 22.43 A C
ATOM 463 CB ASP A 140 15.676 34.273 23.198 1.00 22.46 A C
ATOM 464 CG ASP A 140 16.536 34.364 24.437 1.00 23.38 A C ATOM 465 ODl ASP A 140 17.744 34.640 24.318 1.00 24.44 A O
ATOM 466 OD2 ASP A 140 16.020 34.108 25.524 1.00 21.05 A O
ATOM 467 C ASP A 140 16.117 36.505 22.168 1.00 23.17 A C
ATOM 468 O ASP A 140 16.396 36.357 20.993 1.00 24.16 A O
ATOM 469 N ALA A 141 16.739 37.414 22.926 1.00 25.58 A N
ATOM 470 CA ALA A 141 17.848 38.263 22.391 1.00 25.98 A C
ATOM 471 CB ALA A 141 18.345 39.251 23.465 1.00 27.98 A C
ATOM 472 C ALA A 141 19.022 37.453 21.816 1.00 26.62 A C
ATOM 473 O ALA A 141 19.677 37.874 20.853 1.00 26.48 A O
ATOM 474 N ASP A 142 19.261 36.272 22.384 1.00 25.87 A N
ATOM 475 CA ASP A 142 20.258 35.374 21.844 1.00 26.96 A C
ATOM 476 CB ASP A 142 20.727 34.452 22.970 1.00 27.08 A C
ATOM 477 CG ASP A 142 21.961 33.643 22.620 1.00 28.69 A C
ATOM 478 ODl ASP A 142 22.229 33.386 21.436 1.00 30.82 A O
ATOM 479 OD2 ASP A 142 22.650 33.230 23.578 1.00 32.51 A O
ATOM 480 C ASP A 142 19.643 34.588 20.683 1.00 27.33 A C
ATOM 481 O ASP A 142 18.807 33.691 20.923 1.00 26.43 A O
ATOM 482 N ALA A 143 20.089 34.873 19.447 1.00 27.01 A N
ATOM 483 CA ALA A 143 19.695 34.094 18.263 1.00 27.50 C
ATOM 484 CB ALA A 143 20.189 34.738 16.963 1.00 28.73 A C
ATOM 485 C ALA A 143 20.139 32.635 18.309 1.00 27.48 A C
ATOM 486 O ALA A 143 19.628 31.829 17.530 1.00 27.72 A O
ATOM 487 N ASP A 144 21.058 32.299 19.221 1.00 27.15 A N
ATOM 488 CA ASP A 144 21.521 30.904 19.403 1.00 27.36 A C
ATOM 489 CB ASP A 144 23.005 30.880 19.779 1.00 28.99 A C
ATOM 490 CG ASP A 144 23.902 31.302 18.622 1.00 34.70 A C
ATOM 491 ODl ASP A 144 23.660 30.844 17.463 1.00 40.01 A O
ATOM 492 OD2 ASP A 144 24.844 32.091 18.879 1.00 37.59 A O
ATOM 493 C ASP A 144 20.769 30.077 20.457 1.00 25.21 A C
ATOM 494 O ASP A 144 21.022 28.887 20.583 1.00 24.32 A O
ATOM 495 N GLϋ A 145 19.916 30.722 21.259 1.00 23.43 A N
ATOM 496 CA GLU A 145 19.011 30.016 22.184 1.00 21.83 A C
ATOM 497 CB GLϋ A 145 18.162 31.020 23.001 1.00 21.26 A C
ATOM 498 CG GLO A 145 17.058 30.373 23.947 1.00 22.29 A C
ATOM 499 CD GLϋ A 145 17.625 29.536 25.097 1.00 19.76 A C
ATOM 500 OEl GLU A 145 18.184 28.434 24.832 1.00 17.74 A O
ATOM 501 OE2 GLϋ A 145 17.502 29.972 26.285 1.00 21.46 A O
ATOM 502 C GLU A 145 18.092 29.087 21.387 1.00 20.62 A C
ATOM 503 O GLϋ A 145 17.715 29.383 20.244 1.00 20.83 A O
ATOM 504 N ASN A 146 17.770 27.947 21.971 1.00 20.30 A N
ATOM 505 CA ASN A 146 16.801 27.029 21.396 1.00 20.23 A C
ATOM 506 CB ASN A 146 17.514 25.841 20.753 1.00 21.17 A C
ATOM 507 CG ASN A 146 16.617 25.045 19.809 1.00 25.81 A C
ATOM 508 ODl ASN A 146 15.341 25.213 19.765 1.00 28.51' A O
ATOM 509 ND2 ASN A 146 17.262 24.146 19.040 1.00 27.74 A N
ATOM 510 C ASN A 146 15.911 26.549 22.527 1.00 18.95 A C
ATOM 511 O ASN A 146 16.376 25.791 23.411 1.00 18.14 A O
ATOM 512 N PHE A 147 14.659 27.016 22.516 1.00 18.04 A N
ATOM 513 CA PHE A 147 13.684 26.651 23.548 1.00 16.39 A C
ATOM 514 CB PHE A 147 12.511 27.660 23.662 1.00 15.07 A C
ATOM 515 CG PHE A 147 12.923 29.032 24.225 1.00 16.54 A C
ATOM 516 CDl PHE A 147 13.660 29.119 25.403 1.00 13.46 A C
ATOM 517 CEl PHE A 147 14.010 30.331 25.945 1.00 14.11 A C
ATOM 518 CZ PHE A 147 13.694 31.473 25.297 1.00 12.47 A C
ATOM 519 CE2 PHE A 147 12.956 31.443 24.094 1.00 11.15 A C
ATOM 520 CD2 PHE A 147 12.584 30.207 23.567 1.00 15.73 A C
ATOM 521 C PHE A 147 13.177 25.267 23.236 1.00 16.17 A C
ATOM 522 O PHE A 147 12.847 24.951 22.061 1.00 16.84 A O
ATOM 523 N TYR A 148 13.122 24.448 24.291 1.00 16.18 A N
ATOM 524 CA TYR A 148 12.698 23.046 24.220 1.00 15.72 A C
ATOM 525 CB TYR A 148 13.724 22.183 24.968 1.00 16.49 A C
ATOM 526 CG TYR A 148 15.145 22.129 24.398 1.00 16.55 A C
ATOM 527 CDl TYR A 148 15.437 22.564 23.105 1.00 17.59 A C
ATOM 528 CEl TYR A 148 16.726 22.485 22.574 1.00 19.27 A C
ATOM 529 CZ TYR A 148 17.759 22.021 23.370 1.00 19.53 A C
ATOM 530 OH TYR A 148 19.030 21.933 22.845 1.00 20.45 A O
ATOM 531 CE2 TYR A 148 17.507 21.565 24.678 1.00 20.04 A C
ATOM 532 CD2 TYR A 148 16.199 21.630 25.187 1.00 17.24 A C
ATOM 533 C TYR A 148 11.323 22.770 24.836 1.00 15.33 A C
ATOM 534 O TYR A 148 10.615 21.791 24.442 1.00 15.07 A O
ATOM 535 N THR A 149 10.939 23.594 25.812 1.00 13.98 A N
ATOM 536 CA THR A 149 9.741 23.297 26.608 1.00 14.25 A C
ATOM 537 CB THR A 149 10.006 22.131 27.650 1.00 14.68 A C
ATOM 538 OGl THR A 149 8.770 21.449 27.985 1.00 19.63 A O
ATOM 539 CG2 THR A 149 10.736 22.625 28.940 1.00 14.36 A C
ATOM 540 C THR A 149 9.145 24.543 27.261 1.00 13.63 A C
ATOM 541 O THR A 149 9.826 25.555 27.410 1.00 13.96 A O ATOM 542 N CYS A 150 7.873 24.462 27.657 1.00 12.42 A N
ATOM 543 CA CYS A 150 7.243 25.529 28.409 1.00 13.51 A C
ATOM 544 CB CYS A 150 6.573 26.595 27.499 1.00 13.25 A C
ATOM 545 SG CYS A 150 5.190 25.882 26.538 1.00 16.17 A S
ATOM 546 C CYS A 150 6.218 24.913 29.358 1.00 11.93 A C
ATOM 547 O CYS A 150 5.861 23.733 29.229 1.00 13.06 A O
ATOM 548 N ALA A 151 5.738 25.727 30.285 1.00 11.65 A N
ATOM 549 CA ALA A 151 4.793 25.258 31.326 1.00 13.02 A C
ATOM 550 CB ALA A 151 5.530 24.570 32.443 1.00 11.37 A C
ATOM 551 C ALA A 151 4.027 26.465 31.868 1.00 11.95 A C
ATOM 552 O ALA A 151 4.618 27.561 32.115 1.00 11.73 A O
ATOM 553 N TRP A 152 2.732 26.270 32.055 1.00 12.08 A N
ATOM 554 CA TRP A 152 1.859 27.337 32.574 1.00 11.85 A C
ATOM 555 CB TRP A 152 0.476 27.301 31.883 1.00 11.10 A C
ATOM 556 CG TRP A 152 0.424 27.482 30.353 1.00 11.84 A C
ATOM 557 CDl TRP A 152 0.531 26.495 29.370 1.00 14.71 A C
ATOM 558 NEl TRP A 152 0.367 27.052 28.120 1.00 12.02 A N
ATOM 559 CE2 TRP A 152 0.143 28.401 28.260 1.00 11.09 A C
ATOM 560 CD2 TRP A 152 0.147 28.700 29.650 1.00 12.84 A ' C
ATOM 561 CE3 TRP A 152 0.066 30.019 30.057 1.00 12.92 A C
ATOM 562 CZ3 TRP A 152 0.261 31.029 29.041 1.00 13.19 A C
ATOM 563 CH2 TRP A 152 0.296 30.683 27.686 1.00 15.38 A C
ATOM 564 CZ2 TRP A 152 0.062 29.381 27.273 1.00 14.52 A C
ATOM 565 C TRP A 152 1.638 27.264 34.076 1.00 11.98 A C
ATOM 566 O TRP A 152 1.606 26.179 34.688 1.00 11.80 A O
ATOM 567 N THR A 153 1.374 28.430 34.655 1.00 12.68 A N
ATOM 568 CA THR A 153 1.027 28.568 36.057 1.00 14.35 A C
ATOM 569 CB THR A 153 2.306 28.513 36.968 1.00 12.62 A C
ATOM 570 OGl THR A 153 1.901 28.302 38.304 1.00 11.14 A O
ATOM 571 CG2 THR A 153 3.205 29.834 36.862 1.00 13.08 A C
ATOM 572 C THR A 153 0.251 29.881 36.259 1.00 15.97 A C
ATOM 573 O THR A 153 0.103 30.529 35.271 1.00 15.76 A O
ATOM 574 N TYR A 154 0.071 30.207 37.523 1.00 18.26 A N
ATOM 575 CA TYR A 154 0.639 31.508 37.906 1.00 20.67 A C
ATOM 576 CB TYR A 154 1.712 31.338 39.010 1.00 22.49 A C
ATOM 577 CG TYR A 154 2.989 30.739 38.573 1.00 25.03 A C
ATOM 578 CDl TYR A 154 3.837 31.450 37.720 1.00 28.85 A C
ATOM 579 CEl TYR A 154 5.080 30.943 37.316 1.00 29.91 A C
ATOM 580 CZ TYR A 154 5.490 29.712 37.753 1.00 29.48 A C
ATOM 581 OH TYR A 154 6.732 29.286 37.316 1.00 32.61 A O
ATOM 582 CE2 TYR A 154 4.677 28.948 38.623 1.00 31.24 A C
ATOM 583 CD2 TYR A 154 3.400 29.491 39.039 1.00 29.32 A C
ATOM 584 C TYR A 154 0.399 32.364 38.547 1.00 21.62 A C
ATOM 585 O TYR A 154 1.227 31.858 39.337 1.00 19.83 A O
ATOM 586 N ASP A 155 0.305 33.668 38.316 1.00 23.14 A N
ATOM 587 CA ASP A 155 1.091 34.633 39.102 1.00 27.52 A C
ATOM 588 CB ASP A 155 1.226 35.978 38.341 1.00 28.25 A C
ATOM 589 CG ASP A 155 2.307 36.936 38.942 1.00 32.33 A C
ATOM 590 ODl ASP A 155 2.333 37.125 40.183 1.00 33.24 A O
ATOM 591 OD2 ASP A 155 3.111 37.527 38.158 1.00 35.98 A O
ATOM 592 C ASP A 155 0.354 34.770 40.432 1.00 29.97 A C
ATOM 593 O ASP A 155 0.846 35.077 40.454 1.00 30.78 A O
ATOM 594 N SER A 156 1.040 34.470 41.537 1.00 32.13 A N
ATOM 595 CA SER A 156 0.453 34.659 42.873 1.00 34.87 A C
ATOM 596 CB SER A 156 1.210 33.853 43.946 1.00 34.65 A C
ATOM 597 OG SER A 156 2.592 34.149 43.907 1.00 34.36 A O
ATOM 598 C SER A 156 0.328 36.159 43.268 1.00 35.67 A C
ATOM 599 O SER A 156 0.578 36.517 44.045 1.00 36.13 A O
ATOM 600 N ASN A 157 1.222 37.014 42.717 1.00 36.34 A N
ATOM 601 CA ASN A 157 1.189 38.494 42.894 1.00 37.09 A C
ATOM 602 CB ASN A 157 2.572 39.153 42.652 1.00 38.00 A C
ATOM 603 CG ASN A 157 3.703 38.505 43.452 1.00 42.76 A C
ATOM 604 ODl ASN A 157 3.525 38.096 44.616 1.00 46.81 A O
ATOM 605 ND2 ASN A 157 4.895 38.422 42.831 1.00 45.88 A N
ATOM 606 C ASN A 157 0.152 39.225 42.026 1.00 37.19 A C
ATOM 607 O ASN A 157 0.448 40.215 42.466 1.00 37.95 A O
ATOM 608 N THR A 158 0.060 38.767 40.795 1.00 36.06 A N
ATOM 609 CA THR A 158 1.000 39.473 39.904 1.00 35.26 A C
ATOM 610 CB THR A 158 0.315 40.008 38.572 1.00 35.59 A C
ATOM 611 OGl THR A 158 0.018 38.911 37.709 1.00 34.01 A O
ATOM 612 CG2 THR A 158 0.933 40.837 38.873 1.00 34.34 A C
ATOM 613 C THR A 158 2.260 38.692 39.555 1.00 34.84 A C
ATOM 614 O THR A 158 3.084 39.218 38.808 1.00 36.39 A O
ATOM 615 N SER A 159 2.433 37.479 40.111 1.00 33.71 A N
ATOM 616 CA SER A 159 3.505 36.494 39.723 1.00 31.45 A C
ATOM 617 CB SER A 159 4.863 37.020 40.145 1.00 32.41 A C
ATOM 618 OG SER A 159 5.230 38.112 39.316 1.00 32.24 A O ATOM 619 C SER A 159 -3.577 36.005 38.234 1.00 30.64 A C
ATOM 620 O SER A 159 -4.316 35.069 37.898 1.00 31.00 A O
ATOM 621 N HIS A 160 -2.796 36.610 37.357 1.00 27.38 A N
ATOM 622 CA HIS A 160 -2.834 36.291 35.935 1.00 26.41 A C
ATOM 623 CB HIS A 160 -2.232 31.ill 35.165 1.00 27.55 A C
ATOM 624 CG HIS A 160 -3.124 38.683 35.102 1.00 33.34 A C
ATOM 625 NDl HIS A 160 -2.635 39.975 35.160 1.00 38.16 A N
ATOM 626 CEl HIS A 160 -3.641 40.829 35.081 1.00 40.43 A C
ATOM 627 NE2 HIS A 160 -4.764 40.140 34.961 1.00 40.76 A N
ATOM 628 CD2 HIS A 160 -4.471 38.795 34.984 1.00 38.49 A C
ATOM 629 C HIS A 160 -2.065 34.996 35.565 1.00 22.91 A C
ATOM 630 O HIS A 160 -1.207 34.574 36.285 1.00 20.94 A O
ATOM 631 N PRO A 161 -2.368 34.379 34.412 1.00 22.56 A N
ATOM 632 CA PRO A 161 -1.561 33.232 33.983 1.00 20.96 A C
ATOM 633 CB PRO A 161 -2.320 32.703 32.759 1.00 21.47 A C
ATOM 634 CG PRO A 161 -3.735 33.309 32.916 1.00 23.21 A C
ATOM 635 CD PRO A 161 -3.448 34.665 33.454 1.00 22.73 A C
ATOM 636 C PRO A 161 -0.121 33.675 33.636 1.00 19.38 A C
ATOM 637 O PRO A 161 0.092 34.832 33.300 1.00 18.72 A O
ATOM 638 N LEO A 162 0.859 32.800 33.857 1.00 16.77 A N
ATOM 639 CA LED A 162 2.251 33.055 33.519 1.00 15.19 A C
ATOM 640 CB LEU A 162 3.147 33.135 34.784 1.00 15.08 A C
ATOM 641 CG LED A 162 3.078 34.322 35.717 1.00 17.87 A C
ATOM 642 CDl LED A 162 3.900 34.013 36.954 1.00 18.02 A C
ATOM 643 CD2 LED A 162 3.625 35.535 34.904 1.00 19.28 A C
ATOM 644 C LEO A 162 2.760 31.853 32.691 1.00 14.45 A C
ATOM 645 O LEO A 162 2.286 30.739 32.855 1.00 12.14 A O
ATOM 646 N LEO A 163 3.825 32.070 31.938 1.00 13.39 A N
ATOM 647 CA LEO A 163 4.417 30.990 31.132 1.00 13.95 A C
ATOM 648 CB LEO A 163 4.147 31.228 29.634 1.00 14.38 A C
ATOM 649 CG LEO A 163 4.581 30.199 28.571 1.00 14.75 A C
ATOM 650 CDl LEO A 163 3.918 28.781 28.719 1.00 16.50 A C
ATOM 651 CD2 LEO A 163 4.280 30.835 27.206 1.00 16.84 A C
ATOM 652 C LEO A 163 5.884 30.900 31.387 1.00 14.36 A C
ATOM 653 O LEO A 163 6.595 31.885 31.212 1.00 17.24 A O
ATOM 654 N ALA A 164 6.350 29.741 31.840 1.00 13.37 A N
ATOM 655 CA ALA A 164 7.760 29.483 32.021 1.00 12.29 A C
ATOM 656 CB ALA A 164 7.968 28.567 33.256 1.00 13.43 A C
ATOM 657 C ALA A 164 8.317 28.810 30.748 1.00 13.13 A C
ATOM 658 O ALA A 164 7.738 27.840 30.276 1.00 13.15 A O
ATOM 659 N VAL A 165 9.439 29.309 30.208 1.00 12.05 A N
ATOM 660 CA VAL A 165 10.085 28.694 29.009 1.00 13.18 A C
ATOM 661 CB VAL A 165 9.863 29.590 27.703 1.00 14.00 A C
ATOM 662 CGl VAL A 165 10.586 30.934 27.788 1.00 13.21 A C
ATOM 663 CG2 VAL A 165 10.314 28.849 26.453 1.00 16.46 A C
ATOM 664 C VAL A 165 11.572 28.443 29.314 1.00 13.54 A C
ATOM 665 O VAL A 165 12.234 29.209 30.083 1.00 13.26 A O
ATOM 666 N ALA A 166 12.128 27.374 28.756 1.00 13.99 A N
ATOM 667 CA ALA A 166 13.571 27.145 28.864 1.00 15.02 A C
ATOM 668 CB ALA A 166 13.934 26.540 30.271 1.00 14.06 A C
ATOM 669 C ALA A 166 14.028 26.209 27.734 1.00 15.71 A C
ATOM 670 O ALA A 166 13.199 25.537 27.083 1.00 15.03 A O
ATOM 671 N GLY A 167 15.331 26.177 27.500 1.00 15.93 A N
ATOM 672 CA GLY A 167 15.943 25.273 26.494 1.00 16.91 A C
ATOM 673 C GLY A 167 17.466 25.182 26.588 1.00 17.17 A C
ATOM 674 O GLY A 167 17.989 25.024 27.689 1.00 17.91 A O
ATOM 675 N SER A 168 18.167 25.307 25.448 1.00 16.57 A N
ATOM 676 CA SER A 168 19.630 25.010 25.362 1.00 17.95 A C
ATOM 677 CB SER A 168 20.156 25.041 23.905 1.00 17.23 A C
ATOM 678 OG SER A 168 19.912 26.290 23.277 1.00 20.88 A O
ATOM 679 C SER A 168 20.525 25.832 26.303 1.00 18.45 A C
ATOM 680 O SER A 168 21.427 25.268 26.932 1.00 17.80 A O
ATOM 681 N ARG A 169 20.233 27.131 26.463 1.00 19.53 A N
ATOM 682 CA ARG A 169 21.052 27.996 27.323 1.00 21.63 A C
ATOM 683 CB ARG A 169 20.746 29.482 27.091 1.00 21.60 A C
ATOM 684 CG ARG A 169 21.224 30.073 25.753 1.00 24.39 A C
ATOM 685 CD ARG A 169 20.726 31.580 25.612 1.00 26.16 A C
ATOM 686 NE ARG A 169 21.487 32.559 26.438 1.00 31.61 A N
ATOM 687 CZ ARG A 169 21.108 33.819 26.673 1.00 35.99 A C
ATOM 688 NHl ARG A 169 19.972 34.296 26.155 1.00 37.56 A N
ATOM 689 NH2 ARG A 169 21.869 34.619 27.422 1.00 38.81 A N
ATOM 690 C ARG A 169 20.909 27.688 28.834 1.00 21.18 A C
ATOM 691 O ARG A 169 21.698 28.208 29.644 1.00 19.94 A O
ATOM 692 N GLY A 170 19.903 26.874 29.204 1.00 19.87 A N
ATOM 693 CA GLY A 170 19.677 26.530 30.603 1.00 20.03 A C
ATOM 694 C GLY A 170 19.244 27.748 31.420 1.00 19.97 A C
ATOM 695 O GLY A 170 19.568 27.872 32.603 1.00 20.47 A O ATOM 696 N ILE A 171 18.482 28.637 30.786 1.00 19.46 A N
ATOM 697 CA ILE A 171 17.894 29.789 31.468 1.00 19.60 A C
ATOM 698 CB ILE A 171 18.375 31.173 30.869 1.00 20.19 A C
ATOM 699 CGl ILE A 171 19.922 31.324 30.885 1.00 23.68 A C
ATOM 700 CDl ILE A 171 20.463 32.544 30.022 1.00 22.14 A C
ATOM 701 CG2 ILE A 171 17.734 32.354 31.581 1.00 21.25 A C
ATOM 702 C ILE A 171 16.364 29.659 31.427 1.00 18.19 A C
ATOM 703 O ILE A 171 15.774 29.430 30.354 1.00 19.29 A O
ATOM 704 N ILE A 172 15.743 29.749 32.600 1.00 16.74 A N
ATOM 705 CA ILE A 172 14.276 29.774 32.739 1.00 15.64 A C
ATOM 706 CB ILE A 172 13.785 29.141 34.116 1.00 15.81 A C
ATOM 707 CGl ILE A 172 14.231 27.670 34.230 1.00 13.66 A C
ATOM 708 CDl ILE A 172 14.268 27.076 35.753 1.00 14.40 A C
ATOM 709 CG2 ILE A 172 12.235 29.184 34.190 1.00 14.77 A C
ATOM 710 C ILE A 172 13.781 31.216 32.563 1.00 15.92 A C
ATOM 711 O ILE A 172 14.233 32.125 33.284 1.00 14.68 A O
ATOM 712 N ARG A 173 12.925 31.437 31.560 1.00 14.93 A N
ATOM 713 CA ARG A 173 12.312 32.744 31.357 1.00 15.28 A C
ATOM 714 CB ARG A 173 12.232 33.121 29.895 1.00 15.64 A C
ATOM 715 CG ARG A 173 13.551 33.153 29.067 1.00 20.13 A C
ATOM 716 CD ARG A 173 14.507 34.223 29.577 1.00 23.97 A C
ATOM 717 NE ARG A 173 15.792 34.147 28.897 1.00 27.93 A N
ATOM 718 CZ ARG A 173 16.849 34.903 29.193 1.00 33.49 A C
ATOM 719 NHl ARG A 173 16.769 35.841 30.149 1.00 31.80 A N
ATOM 720 NH2 ARG A 173 18.002 34.719 28.540 1.00 31.86 A N
ATOM 721 C ARG A 173 10.881 32.684 31.922 1.00 15.58 A C
ATOM 722 O ARG A 173 10.129 31.780 31.567 1.00 13.83 A O
ATOM 723 N ILE A 174 10.511 33.648 32.762 1.00 14.65 A N
ATOM 724 CA ILE A 174 9.095 33.797 33.196 1.00 14.72 A C
ATOM 725 CB ILE A 174 8.947 34.049 34.699 1.00 15.20 A C
ATOM 726 CGl ILE A 174 9.749 32.953 35.488 1.00 13.63 A C
ATOM 727 CDl ILE A 174 9.237 31.521 35.313 1.00 13.69 A C
ATOM 728 CG2 ILE A 174 7.440 34.028 35.080 1.00 14.16 A C
ATOM 729 C ILE A 174 8.495 34.911 32.365 1.00 14.78 A C
ATOM 730 O ILE A 174 8.955 36.073 32.419 1.00 13.16 A O
ATOM 731 N ILE A 175 7.527 34.517 31.538 1.00 14.73 A N
ATOM 732 CA ILE A 175 6.903 35.383 30.506 1.00 15.18 A C
ATOM 733 CB ILE A 175 6.940 34.683 29.129 1.00 15.64 A C
ATOM 734 CGl ILE A 175 8.392 34.437 28.710 1.00 18.68 A C
ATOM 735 CDl ILE A 175 8.468 33.478 27.604 1.00 28.36 A C
ATOM 736 CG2 ILE A 175 6.220 35.515 27.974 1.00 15.24 A C
ATOM 737 C ILE A 175 5.446 35.690 30.890 1.00 14.26 A C
ATOM 738 O ILE A 175 4.657 34.770 31.190 1.00 13.90 A O
ATOM 739 N ASN A 176 5.115 36.966 30.896 1.00 14.84 A N
ATOM 740 CA ASN A 176 3.745 37.449 30.967 1.00 15.20 A C
ATOM 741 CB ASN A 176 3.793 38.959 31.214 1.00 15.99 A
ATOM 742 CG ASN A 176 2.421 39.609 31.333 1.00 17.10 A C
ATOM 743 ODl ASN A 176 1.378 39.099 30.848 1.00 20.09 A O
ATOM 744 ND2 ASN A 176 2.406 40.778 31.980 1.00 18.67 A N
ATOM 745 C ASN A 176 3.094 37.169 29.605 1.00 16.31 A C
ATOM 746 O ASN A 176 3.468 37.821 28.611 1.00 15.53 A O
ATOM 747 N PRO A 177 2.124 36.226 29.536 1.00 16.65 A N
ATOM 748 CA PRO A 177 1.523 35.870 28.228 1.00 17.24 A C
ATOM 749 CB PRO A 177 0.684 34.609 28.533 1.00 17.69 A C
ATOM 750 CG PRO A 177 0.396 34.680 30.023 1.00 17.03 A C
ATOM 751 CD PRO A 177 1.522 35.476 30.662 1.00 17.03 A C
ATOM 752 C PRO A 177 0.637 36.934 27.568 1.00 18.14 A C
ATOM 753 O PRO A 177 0.359 36.851 26.342 1.00 19.79 A O
ATOM 754 N ILE A 178 0.151 37.880 28.344 1.00 17.26 A N
ATOM 755 CA ILE A 178 -0.586 39.007 27.787 1.00 17.49 A C
ATOM 756 CB ILE A 178 -1.252 39.884 28.894 1.00 16.73 A C
ATOM 757 CGl ILE A 178 -2.004 38.983 29.876 1.00 18.82 A C
ATOM 758 CDl ILE A 178 -2.826 39.677 31.013 1.00 20.55 A C
ATOM 759 CG2 ILE A 178 -2.140 40.993 28.219 1.00 16.21 A C
ATOM 760 C ILE A 178 0.284 39.873 26.864 1.00 16.89 A C
ATOM 761 O ILE A 178 -0.039 40.041 25.681 1.00 15.24 A O
ATOM 762 N THR A 179 1.398 40.368 27.395 1.00 16.34 A N
ATOM 763 CA THR A 179 2.286 41.266 26.674 1.00 16.15 A C
ATOM 764 CB THR A 179 2.807 42.314 27.620 1.00 16.65 A C
ATOM 765 OGl rTHR A 179 3.499 41.653 28.685 1.00 16.69 A O
ATOM 766 CG2 THR A 179 1.616 43.156 28.246 1.00 15.61 A C
ATOM 767 C THR A 179 3.490 40.555 26.045 1.00 16.70 A C
ATOM 768 O THR A 179 4.229 41.147 25.258 1.00 16.74 A O
ATOM 769 N MET A 180 3.680 39.275 26.373 1.00 16.40 A N
ATOM 770 CA MET A 180 4.908 38.542 26.046 1.00 17.44 A C
ATOM 111 CB MET A 180 4.993 38.209 24.547 1.00 17.19 A C
ATOM 772 CG MET A 180 3.775 37.407 24.019 1.00 16.19 A C ATOM 773 SD MET A 180 3.537 35.854 24.950 1.00 17.47 A S
ATOM 774 CE MET A 180 4.678 34.744 24.126 1.00 15.68 A C
ATOM 775 C MET A 180 6.209 39.182 26.608 1.00 18.08 A C
ATOM lie O MET A 180 7.314 38.917 26.105 1.00 18.57 A O
ATOM 111 N GLN A 181 6.070 40.023 27.636 1.00 18.32 A N
ATOM 778 CA GLN A 181 7.232 40.559 28.371 1.00 18.97 A C
ATOM 779 CB GLN A 181 6.847 41.675 29.330 1.00 19.97 A C
ATOM 780 CG GLN A 181 6.344 42.957 28.737 1.00 20.71 A C
ATOM 781 CD GLN A 181 5.694 43.836 29.826 1.00 20.78 A C
ATOM 782 OEl GLN A 181 4.539 43.631 30.188 1.00 19.66 A O
ATOM 783 NE2 GLN A 181 6.467 44.775 30.378 1.00 21.92 A N
ATOM 784 C GLN A 181 7.859 39.481 29.227 1.00 19.59 A C
ATOM 785 O GLN A 181 7.153 38.632 29.805 1.00 16.87 A O
ATOM 786 N CYS A 182 9.185 39.502 29.296 1.00 20.24 A N
ATOM 787 CA CYS A 182 9.909 38.593 30.192 1.00 21.58 A C
ATOM 788 CB CYS A 182 11.294 38.211 29.635 1.00 21.84 A C
ATOM 789 SG CYS A 182 12.263 37.202 30.810 1.00 24.76 A S
ATOM 790 C CYS A 182 9.991 39.291 31.548 1.00 22.03 A C
ATOM 791 O CYS A 182 10.527 40.416 31.656 1.00 20.40 A O
ATOM 792 N ILE A 183 9.393 38.672 32.565 1.00 20.51 A N
ATOM 793 CA ILE A 183 9.268 39.361 33.829 1.00 22.00 A C
ATOM 794 CB ILE A 183 7.884 39.175 34.594 1.00 22.53 A C
ATOM 795 CGl ILE A 183 7.554 37.766 35.009 1.00 24.62 A C
ATOM 796 CDl ILE A 183 5.979 37.644 35.272 1.00 25.37 A C
ATOM 797 CG2 ILE A 183 6.720 39.641 33.749 1.00 21.50 A C
ATOM 798 C ILE A 183 10.482 39.131 34.711 1.00 21.32 A C
ATOM 799 O ILE A 183 10.895 40.051 35.404 1.00 20.48 A O
ATOM 800 N LYS A 184 11.066 37.926 34.609 1.00 19.41 A N
ATOM 801 CA LYS A 184 12.256 37.508 35.388 1.00 19.40 A C
ATOM 802 CB LYS A 184 11.930 37.378 36.883 1.00 20.42 A C
ATOM 803 CG LYS A 184 10.769 36.424 37.253 1.00 18.02 A C
ATOM 804 CD LYS A 184 10.326 36.731 38.678 1.00 22.10 A C
ATOM 805 CE LYS A 184 9.185 35.796 39.240 1.00 24.02 A C
ATOM 806 NZ LYS A 184 8.870 36.168 40.744 1.00 23.58 A N
ATOM 807 C LYS A 184 12.833 36.193 34.861 1.00 19.60 A C
ATOM 808 O LYS A 184 12.180 35.500 34.048 1.00 18.30 A O
ATOM 809 N HIS A 185 14.056 35.842 35.301 1.00 18.34 A N
ATOM 810 CA HIS A 185 14.687 34.630 34.831 1.00 18.33 A C
ATOM 811 CB HIS A 185 15.592 34.900 33.604 1.00 18.47 A C
ATOM 812 CG HIS A 185 16.824 35.690 33.932 1.00 24.84 A C
ATOM 813 NDl HIS A 185 16.869 37.064 33.843 1.00 29.93 A N
ATOM 814 CEl HIS A 185 18.069 37.486 34.198 1.00 32.78 A C
ATOM 815 NE2 HIS A 185 18.798 36.436 34.530 1.00 32.95 A N
ATOM 816 CD2 HIS A 185 18.040 35.301 34.379 1.00 28.29 A C
ATOM 817 C HIS A 185 15.474 33.954 35.942 1.00 17.43 A C
ATOM 818 O HIS A 185 15.857 34.579 36.946 1.00 17.16 A O
ATOM 819 N TYR A 186 15.722 32.675 35.758 1.00 16.77 A N
ATOM 820 CA TYR A 186 16.511 31.895 36.694 1.00 17.55 A C
ATOM 821 CB TYR A 186 15.651 30.884 37.458 1.00 16.59 A C
ATOM 822 CG TYR A 186 14.482 31.517 38.165 1.00 19.84 A C
ATOM 823 CDl TYR A 186 14.672 32.216 39.368 1.00 19.94 A C
ATOM 824 CEl TYR A 186 13.574 32.824 40.017 1.00 20.82 A C
ATOM 825 CZ TYR A 186 12.303 32.739 39.424 1.00 17.60 A C
ATOM 826 OH TYR A 186 11.264 33.326 40.042 1.00 19.82 A O
ATOM 827 CE2 TYR A 186 12.094 32.070 38.238 1.00 20.14 A C
ATOM 828 CD2 TYR A 186 13.178 31.461 37.605 1.00 17.69 A C
ATOM 829 C TYR A 186 17.632 31.156 35.985 1.00 18.49 A C
ATOM 830 O TYR A 186 17.419 30.550 34.947 1.00 18.95 A O
ATOM 831 N VAL A 187 18.818 31.201 36.568 1.00 20.26 A N
ATOM 832 CA VAL A 187 19.986 30.523 36.030 1.00 23.17 A C
ATOM 833 CB VAL A 187 21.138 31.487 35.710 1.00 23.38 A C
ATOM 834 CGl VAL A 187 22.249 30.699 34.978 1.00 26.74 A C
ATOM 835 CG2 VAL A 187 20.664 32.602 34.800 1.00 23.66 A C
ATOM 836 C VAL A 187 20.431 29.535 37.105 1.00 23.86 A C
ATOM 837 O VAL A 187 20.518 29.889 38.285 1.00 23.04 A O
ATOM 838 N GLY A 188 20.638 28.295 36.674 1.00 26.15 A N
ATOM 839 CA GLY A 188 21.103 27.190 37.509 1.00 28.05 A C
ATOM 840 C GLY A 188 22.600 27.256 37.437 1.00 29.31 A C
ATOM 841 O GLY A 188 23.174 28.263 37.860 1.00 29.27 A O
ATOM 842 N HIS A 189 23.225 26.211 36.907 1.00 29.96 A N
ATOM 843 CA HIS A 189 24.608 26.328 36.364 1.00 31.97 A C
ATOM 844 CB HIS A 189 25.466 25.078 36.648 1.00 32.78 A C
ATOM 845 CG HIS A 189 25.663 24.798 38.100 1.00 35.81 A C
ATOM 846 NDl HIS A 189 25.995 25.780 39.011 1.00 40.73 A N
ATOM 847 CEl HIS A 189 26.101 25.244 40.214 1.00 41.82 A C
ATOM 848 NE2 HIS A 189 25.853 23.948 40.117 1.00 43.84 A N
ATOM 849 CD2 HIS A 189 25.583 23.642 38.802 1.00 40.53 A C ATOM 850 C HIS A 189 24.706 26.715 34.849 1.00 31.72 A C
ATOM 851 O HIS A 189 25.821 26.925 34.318 1.00 31.89 A O
ATOM 852 N GLY A 190 23.565 26.809 34.162 1.00 30.09 A N
ATOM 853 CA GLY A 190 23.581 27.283 32.759 1.00 29.33 A C
ATOM 854 C GLY A 190 23.727 26.199 31.687 1.00 27.15 A C
ATOM 855 O GLY A 190 24.181 26.471 30.584 1.00 27.47 A O
ATOM 856 N ASN A 191 23.310 24.975 32.023 1.00 25.76 A N
ATOM 857 CA ASN A 191 23.355 23.768 31.135 1.00 22.71 A C
ATOM 858 CB ASN A 191 23.956 22.666 31.953 1.00 22.28 A C
ATOM 859 CG ASN A 191 25.239 23.127 32.643 1.00 24.04 A C
ATOM 860 ODl ASN A 191 26.204 23.476 31.966 1.00 24.23 A O
ATOM 861 ND2 ASN A 191 25.240 23.168 33.962 1.00 22.60 A N
ATOM 862 C ASN A 191 21.935 23.395 30.711 1.00 21.03 A C
ATOM 863 O ASN A 191 20.999 23.710 31.476 1.00 20.38 A O
ATOM 864 N ALA A 192 21.768 22.771 29.536 1.00 18.56 A N
ATOM 865 CA ALA A 192 20.446 22.729 28.856 1.00 18.14 A C
ATOM 866 CB ALA A 192 20.482 21.891 27.589 1.00 16.24 A C
ATOM 867 C ALA A 192 19.331 22.220 29.770 1.00 16.15 A C
ATOM 868 O ALA A 192 19.526 21.238 30.502 1.00 15.22 A O
ATOM 869 N ILE A 193 18.168 22.872 29.697 1.00 15.48 A N
ATOM 870 CA ILE A 193 16.982 22.405 30.459 1.00 13.93 A C
ATOM 871 CB ILE A 193 16.259 23.592 31.167 1.00 13.27 A C
ATOM 872 CGl ILE A 193 17.161 24.176 32.298 1.00 15.18 A C
ATOM 873 CDl ILE A 193 16.724 25.493 32.778 1.00 13.56 A C
ATOM 874 CG2 ILE A 193 14.860 23.163 31.747 1.00 13.46 A C
ATOM 875 C ILE A 193 16.055 21.642 29.504 1.00 13.55 A C
ATOM 876 O ILE A 193 15.565 22.186 28.482 1.00 14.27 A O
ATOM 877 N ASN A 194 15.826 20.375 29.821 1.00 13.47 A N
ATOM 878 CA ASN A 194 15.024 19.463 28.991 1.00 13.03 A C
ATOM 879 CB ASN A 194 15.646 18.056 29.105 1.00 12.79 A C
ATOM 880 CG ASN A 194 17.009 17.971 28.417 1.00 14.53 A C
ATOM 881 ODl ASN A 194 17.269 18.665 27.404 1.00 18.96 A O
ATOM 882 ND2 ASN A 194 17.897 17.116 28.955 1.00 12.55 A N
ATOM 883 C ASN A 194 13.508 19.405 29.314 1.00 13.67 A C
ATOM 884 O ASN A 194 12.714 19.014 28.466 1.00 14.70 A O
ATOM 885 N GLU A 195 13.125 19.769 30.540 1.00 13.34 A N
ATOM 886 CA GLU A 195 11.726 19.778 30.976 1.00 14.44 A C
ATOM 887 CB GLU A 195 11.233 18.361 31.360 1.00 14.23 A C
ATOM 888 CG GLO A 195 9.706 18.182 31.518 1.00 16.82 A C
ATOM 889 CD GLϋ A 195 8.922 18.619 30.287 1.00 23.47 A C
ATOM 890 OEl GLU A 195 8.467 17.728 29.487 1.00 23.15 A O
ATOM 891 OE2 GLU A 195 8.796 19.870 30.112 1.00 23.07 A O
ATOM 892 C GLU A 195 11.477 20.773 32.125 1.00 13.89 A C
ATOM 893 O GLU A 195 12.368 21.003 32.972 1.00 13.51 A O
ATOM 894 N LEU A 196 10.285 21.377 32.091 1.00 12.15 A N
ATOM 895 CA LEU A 196 9.682 22.153 33.182 1.00 13.05 A C
ATOM 896 CB LEU A 196 9.533 23.622 32.740 1.00 12.03 A C
ATOM 897 CG LEU A 196 10.828 24.330 32.367 1.00 10.70 A C
ATOM 898 CDl LEU A 196 10.557 25.610 31.580 1.00 12.28 A C
ATOM 899 CD2 LEU A 196 11.744 24.523 33.658 1.00 8.35 A C
ATOM 900 C LEU A 196 8.323 21.601 33.603 1.00 12.47 A C
ATOM 901 O LEU A 196 7.475 21.248 32.748 1.00 14.39 A O
ATOM 902 N LYS A 197 8.070 21.564 34.903 1.00 13.40 A N
ATOM 903 CA LYS A 197 6.750 21.227 35.407 1.00 13.69 A C
ATOM 904 CB LYS A 197 6.633 19.716 35.751 1.00 13.51 A C
ATOM 905 CG LYS A 197 6.767 18.747 34.609 1.00 15.35 A C
ATOM 906 CD LYS A 197 5.477 18.683 33.784 1.00 16.06 A C
ATOM 907 CE LYS A 197 5.590 17.652 32.680 1.00 17.77 A C
ATOM 908 NZ LYS A 197 5.612 16.265 33.324 1.00 23.16 A N
ATOM 909 C LYS A 197 6.391 22.033 36.672 1.00 14.43 A C
ATOM 910 O LYS A 197 7.214 22.200 37.600 1.00 12.89 A O
ATOM 911 N PHE A 198 5.145 22.494 36.734 1.00 13.80 A N
ATOM 912 CA PHE A 198 4.663 23.175 37.945 1.00 13.78 A C
ATOM 913 CB PHE A 198 3.756 24.358 37.588 1.00 14.15 A C
ATOM 914 CG PHE A 198 4.504 25.587 37.166 1.00 12.15 A C
ATOM 915 CDl PHE A 198 5.018 26.464 38.142 1.00 14.53 A C
ATOM 916 CEl PHE A 198 5.727 27.617 37.769 1.00 13.00 A C
ATOM 917 CZ PHE A 198 5.926 27.924 36.423 1.00 8.57 A C
ATOM 918 CE2 PHE A 198 5.372 27.051 35.413 1.00 11.00 A C
ATOM 919 CD2 PHE A 198 4.684 25.892 35.805 1.00 12.91 A C
ATOM 920 C PHE A 198 3.936 22.196 38.840 1.00 14.02 A C
ATOM 921 O PHE A 198 3.237 21.308 38.340 1.00 15.39 A O
ATOM 922 N HIS A 199 4.123 22.356 40.154 1.00 13.81 A N
ATOM 923 CA HIS A 199 3.494 21.571 41.226 1.00 15.42 A C
ATOM 924 CB HIS A 199 3.965 22.143 42.580 1.00 14.26 A C
ATOM 925 CG HIS A 199 3.607 21.334 43.795 1.00 14.22 A C
ATOM 926 NDl HIS A 199 2.350 21.333 44.345 1.00 15.15 A N ATOM 927 CEl HIS A 199 2.337 20.562 45.424 1.00 15.73 A C
ATOM 928 NE2 HIS A 199 3.565 20.115 45.626 1.00 15.74 A N
ATOM 929 CD2 HIS A 199 4.385 20.608 44.642 1.00 14.42 A C
ATOM 930 C HIS A 199 1.952 21.638 41.039 1.00 16.39 A C
ATOM 931 O HIS A 199 1.424 22.701 40.634 1.00 16.51 A O
ATOM 932 N PRO A 200 1.244 20.495 41.250 1.00 16.39 A N
ATOM 933 CA PRO A 200 -0.200 20.467 40.988 1.00 17.81 A C
ATOM 934 CB PRO A 200 -0.542 18.968 41.061 1.00 16.45 A C
ATOM 935 CG PRO A 200 0.539 18.423 41.951 1.00 17.80 A C
ATOM 936 CD PRO A 200 1.749 19.152 41.591 1.00 14.79 A C
ATOM 937 C PRO A 200 -1.025 21.275 42.001 1.00 17.69 A C
ATOM 938 O PRO A 200 -2.138 21.661 41.667 1.00 18.78 A O
ATOM 939 N ARG A 201 -0.478 21.543 43.185 1.00 18.19 A N
ATOM 940 CA ARG A 201 -1.213 22.295 44.225 1.00 19.09 A C
ATOM 941 CB ARG A 201 -1.291 21.498 45.507 1.00 21.68 A C
ATOM 942 CG ARG A 201 -1.768 20.023 45.341 1.00 21.35 A C
ATOM 943 CD ARG A 201 -3.266 19.930 45.367 1.00 26.44 A C
ATOM 944 NE ARG A 201 -3.767 18.922 46.324 1.00 33.82 A N
ATOM 945 CZ ARG A 201 -4.417 17.816 45.999 1.00 37.98 A C
ATOM 946 NHl ARG A 201 -4.652 17.518 44.705 1.00 40.83 A N
ATOM 947 NH2 ARG A 201 -4.848 17.009 46.976 1.00 40.14 A N
ATOM 948 C ARG A 201 -0.652 23.669 44.517 1.00 18.46 A C
ATOM 949 O ARG A 201 -1.382 24.571 44.961 1.00 18.95 A O
ATOM 950 N ASP A 202 0.631 23.870 44.223 1.00 16.02 A N
ATOM 951 CA ASP A 202 1.270 25.138 44.532 1.00 14.76 A C
ATOM 952 CB ASP A 202 2.413 24.925 45.539 1.00 14.84 A C
ATOM 953 CG ASP A 202 3.053 26.246 45.985 1.00 15.80 A C
ATOM 954 ODl ASP A 202 2.845 27.280 45.313 1.00 11.00 A O
ATOM 955 OD2 ASP A 202 3.729 26.243 47.032 1.00 16.88 A O
ATOM 956 C ASP A 202 1.835 25.702 43.247 1.00 13.78 A C
ATOM 957 O ASP A 202 2.834 25.227 42.747 1.00 12.68 A O
ATOM 958 N PRO A 203 1.169 26.708 42.696 1.00 15.67 A N
ATOM 959 CA PRO A 203 1.537 27.310 41.405 1.00 15.11 A C
ATOM 960 CB PRO A 203 0.427 28.355 41.189 1.00 15.82 A C
ATOM 961 CG PRO A 203 0.008 28.715 42.630 1.00 18.95 A C
ATOM 962 CD PRO A 203 0.002 27.376 43.319 1.00 14.39 A C
ATOM 963 C PRO A 203 2.933 28.019 41.402 1.00 15.42 A C
ATOM 964 O PRO A 203 3.430 28.365 40.317 1.00 15.32 A O
ATOM 965 N ASN A 204 3.533 28.257 42.583 1.00 14.42 A N
ATOM 966 CA ASN A 204 4.889 28.859 42.681 1.00 15.08 A C
ATOM 967 CB ASN A 204 5.075 29.658 43.988 1.00 14.34 A C
ATOM 968 CG ASN A 204 4.032 30.733 44.172 1.00 16.97 A C
ATOM 969 ODl ASN A 204 3.264 30.728 45.155 1.00 21.15 A O
ATOM 970 ND2 ASN A 204 3.968 31.631 43.228 1.00 15.94 A N
ATOM 971 C ASN A 204 6.052 27.865 42.562 1.00 14.07 A C
ATOM 972 O ASN A 204 7.203 28.290 42.461 1.00 14.54 A O
ATOM 973 N LEU A 205 5.770 26.564 42.626 1.00 14.65 A N
ATOM 974 CA LEU A 205 6.857 25.562 42.747 1.00 14.45 A C
ATOM 975 CB LEU A 205 6.589 24.480 43.823 1.00 12.86 A C
ATOM 976 CG LEU A 205 6.391 24.948 45.273 1.00 11.94 A C
ATOM 977 CDl LEU A 205 6.139 23.744 46.146 1.00 12.90 A C
ATOM 978 CD2 LEU A 205 7.630 25.706 45.749 1.00 15.86 A C
ATOM 979 C LEU A 205 7.129 24.934 41.371 1.00 14.44 A C
ATOM 980 O LEU A 205 6.321 24.126 40.832 1.00 15.39 A O
ATOM 981 N LEU A 206 8.242 25.370 40.799 1.00 14.81 A N
ATOM 982 CA LEU A 206 8.650 24.968 39.454 1.00 13.60 A C
ATOM 983 CB LEU A 206 9.008 26.192 38.619 1.00 13.47 A C
ATOM 984 CG LEU A 206 9.603 25.921 37.213 1.00 12.36 A C
ATOM 985 CDl LEU A 206 8.595 25.143 36.299 1.00 11.61 A C
ATOM 986 CD2 LEU A 206 10.043 27.252 36.608 1.00 14.73 A C
ATOM 987 C LEU A 206 9.818 24.013 39.522 1.00 14.04 A C
ATOM 988 O LEU A 206 10.864 24.320 40.159 1.00 14.29 A O
ATOM 989 N LEU A 207 9.629 22.859 38.865 1.00 13.32 A N
ATOM 990 CA LEU A 207 10.662 21.817 38.716 1.00 12.31 A C
ATOM 991 CB LEU A 207 10.050 20.428 38.921 1.00 11.22 A C
ATOM 992 CG LEU A 207 10.944 19.207 38.913 1.00 12.88 A C
ATOM 993 CDl LEU A 207 11.807 19.228 40.213 1.00 11.94 A C
ATOM 994 CD2 LEU A 207 10.128 17.899 38.796 1.00 13.22 A C
ATOM 995 C LEU A 207 11.287 21.921 37.317 1.00 13.45 A C
ATOM 996 O LEU A 207 10.568 21.978 36.298 1.00 10.67 A O
ATOM 997 N SER A 208 12.626 21.971 37.272 1.00 13.12 A N
ATOM 998 CA SER A 208 13.362 21.945 35.990 1.00 12.78 A C
ATOM 999 CB SER A 208 14.199 23.215 35.804 1.00 13.11 A C
ATOM 1000 OG SER A 208 15.100 23.380 36.944 1.00 16.92 A O
ATOM 1001 C SER A 208 14.257 20.703 36.005 1.00 14.12 A C
ATOM 1002 O SER A 208 14.808 20.322 37.058 1.00 13.88 A , O
ATOM 1003 N VAL A 209 14.424 20.070 34.839 1.00 14.29 A N ATOM 1004 CA VAL A 209 15.321 18.906 34.717 .00 14.83 A C
ATOM 1005 CB VAL A 209 14.538 17.566 34.429 .00 15.09 A C
ATOM 1006 CGl VAL A 209 13.166 17.553 35.157 .00 16.40 A C
ATOM 1007 CG2 VAL A 209 14.379 17.302 32.992 .00 17.59 A C
ATOM 1008 C VAL A 209 16.411 19.212 33.678 .00 13.84 A C
ATOM 1009 O VAL A 209 16.120 19.830 32.662 .00 13.15 A O
ATOM 1010 N SER A 210 17.658 18.816 33.949 .00 13.72 A N
ATOM 1011 CA SER A 210 18.783 19.348 33.151 .00 14.69 A C
ATOM 1012 CB SER A 210 19.581 20.396 33.985 .00 14.58 A C
ATOM 1013 OG SER A 210 20.719 20.848 33.271 .00 15.72 A O
ATOM 1014 C SER A 210 19.741 18.320 32.546 .00 15.54 A C
ATOM 1015 O SER A 210 20.004 17.224 33.119 .00 15.10 A O
ATOM 1016 N LYS A 211 20.318 18.735 31.416 .00 16.33 A N
ATOM 1017 CA LYS A 211 21.422 18.046 30.791 .00 17.44 A C
ATOM 1018 CB LYS A 211 21.830 18.820 29.517 1.00 17.68 A C
ATOM 1019 CG LYS A 211 23.039 18.222 28.754 1.00 17.44 A C
ATOM 1020 CD LYS A 211 23.358 19.050 27.511 19.86 A C
ATOM 1021 CE LYS A 211 24.587 18.436 26.743 23.09 A C
ATOM 1022 NZ LYS A 211 24.590 18.843 25.302 28.05 A N
ATOM 1023 C LYS A 211 22.632 17.839 31.742 17.77 A C
ATOM 1024 O LYS A 211 23.463 16.923 31.535 18.79 A O
ATOM 1025 N ASP A 212 22.703 18.637 32.797 16.38 A N
ATOM 1026 CA ASP A 212 23.794 18.508 33.810 16.99 A C
ATOM 1027 CB ASP A 212 24.129 19.881 34.420 16.48 A C
ATOM 1028 CG ASP A 212 23.080 20.377 35.440 1.00 19.81 A C
ATOM 1029 ODl ASP A 212 22.157 19.640 35.838 20.91 A O
ATOM 1030 OD2 ASP A 212 23.186 21.537 35.895 23.57 A O
ATOM 1031 C ASP A 212 23.583 17.441 34.896 15.55 A C
ATOM 1032 O ASP A 212 24.320 17.401 35.878 16.08 A O
ATOM 1033 N HIS A 213 22.595 16.572 34.697 16.17 A N
ATOM 1034 CA HIS A 213 22.306 15.369 35.544 16.27 A C
ATOM 1035 CB HIS A 213 23.554 14.530 35.977 16.55 A C
ATOM 1036 CG HIS A 213 24.563 14.289 34.888 18.36 A C
ATOM 1037 NDl HIS A 213 25.761 13.639 35.117 20.05 A N
ATOM 1038 CEl HIS A 213 26.448 13.562 33.986 21.38 A C
ATOM 1039 NE2 HIS A 213 25.741 14.140 33.027 21.55 A N
ATOM 1040 CD2 HIS A 213 24.563 14.618 33.569 19.48 A C
ATOM 1041 C HIS A 213 21.432 15.663 36.768 15.89 A C
ATOM 1042 O HIS A 213 21.082 14.753 37.536 18.28 A O
ATOM 1043 N ALA A 214 21.089 16.927 36.963 15.53 A N
ATOM 1044 CA ALA A 214 20.322 17.349 38.145 14.68 A C
ATOM 1045 CB ALA A 214 21.089 18.465 38.886 13.54 A C
ATOM 1046 C ALA A 214 18.856 17.786 37.873 14.15 A C
ATOM 1047 O ALA A 214 18.552 18.253 36.758 14.73 A O
ATOM 1048 N LEU A 215 17.962 17.609 38.873 1.00 13.61 A N
ATOM 1049 CA LEU A 215 16.679 18.340 38.908 .00 14.11 A C
ATOM 1050 CB LEU A 215 15.443 17.451 39.308 .00 13.40 A C
ATOM 1051 CG LEU A 215 15.132 16.230 38.391 .00 16.74 A C
ATOM 1052 CDl LEU A 215 15.934 15.005 38.836 .00 17.25 A C
ATOM 1053 CD2 LED A 215 13.616 15.855 38.485 .00 16.72 A C
ATOM 1054 C LEU A 215 16.830 19.507 39.882 .00 14.03 A C
ATOM 1055 O LEU A 215 17.588 19.410 40.854 .00 14.42 A O
ATOM 1056 N ARG A 216 16.133 20.615 39.621 .00 14.73 A N
ATOM 1057 CA ARG A 216 16.103 21.734 40.581 1.00 16.16 A C
ATOM 1058 CB ARG A 216 16.933 22.921 40.072 1.00 15.21 A C
ATOM 1059 CG ARG A 216 18.470 22.665 40.051 14.87 A C
ATOM 1060 CD ARG A 216 19.243 23.708 39.178 20.09 A C
ATOM 1061 NE ARG A 216 20.650 23.280 39.189 23.04 A N
ATOM 1062 CZ ARG A 216 21.187 22.392 38.325 26.20 A C
ATOM 1063 NHl ARG A 216 20.489 21.921 37.254 20.88 A N
ATOM 1064 NH2 ARG A 216 22.446 22.004 38.520 19.06 A N
ATOM 1065 C ARG A 216 14.652 22.160 40.852 16.33 A C
ATOM 1066 O ARG A 216 13.834 22.241 39.894 16.02 A O
ATOM 1067 N LEU A 217 14.331 22.417 42.117 14.92 A N
ATOM 1068 CA LEU A 217 13.016 22.931 42.483 14.54 A C
ATOM 1069 CB LEU A 217 12.409 22.113 43.622 13.11 A C
ATOM 1070 CG LEU A 217 11.057 22.520 44.208 13.00 A C
ATOM 1071 CDl LEU A 217 9.895 22.268 43.200 14.61 A C
ATOM 1072 CD2 LEU A 217 10.713 21.851 45.518 15.51 A C
ATOM 1073 C LEU A 217 13.139 24.414 42.884 15.36 A C
ATOM 1074 O LEU A 217 13.907 24.754 43.813 13.76 A O
ATOM 1075 N TRP A 218 12.361 25.260 42.222 14.25 A N
ATOM 1076 CA TRP A 218 12.388 26.705 42.443 14.50 A C
ATOM 1077 CB TRP A 218 12.610 27.436 41.123 15.02 A C
ATOM 1078 CG TRP A 218 13.772 26.967 40.274 15.29 A C
ATOM 1079 CDl TRP A 218 13.786 25.907 39.396 15.28 A C
ATOM 1080 NEl TRP A 218 15.029 25.797 38.804 1.00 18.71 A N ATOM 1081 CE2 TRP A 218 15.827 26.815 39.250 1.00 15.67 A C
ATOM 1082 CD2 TRP A 218 15.067 27.575 40.188 1.00 15.14 A C
ATOM 1083 CE3 TRP A 218 15.663 28.669 40.813 1.00 14.16 A C
ATOM 1084 CZ3 TRP A 218 16.976 28.982 40.488 1.00 17.33 A C
ATOM 1085 CH2 TRP A 218 17.699 28.208 39.562 1.00 15.51 A C
ATOM 1086 CZ2 TRP A 218 17.146 27.123 38.935 1.00 18.29 A C
ATOM 1087 C TRP A 218 11.052 27.212 43.035 1.00 14.89 A C
ATOM 1088 O TRP A 218 9.961 26.730 42.676 1.00 13.23 A O
ATOM 1089 N ASN A 219 11.155 28.249 43.865 1.00 13.85 A N
ATOM 1090 CA ASN A 219 10.020 28.958 44.355 1.00 13.99 A C
ATOM 1091 CB ASN A 219 10.092 29.098 45.878 1.00 14.01 A C
ATOM 1092 CG ASN A 219 8.889 29.833 46.469 1.00 14.23 A C
ATOM 1093 ODl ASN A 219 8.259 30.663 45.791 1.00 14.01 A O
ATOM 1094 ND2 ASN A 219 8.577 29.543 47.749 1.00 11.10 A N
ATOM 1095 C ASN A 219 10.001 30.305 43.648 1.00 13.82 A C
ATOM 1096 O ASN A 219 10.851 31.172 43.894 1.00 14.21 A O
ATOM 1097 N ILE A 220 9.039 30.469 42.748 1.00 13.65 A N
ATOM 1098 CA ILE A 220 9.017 31.633 41.854 1.00 13.89 A C
ATOM 1099 CB ILE A 220 8.491 31.302 40.385 1.00 13.42 A C
ATOM 1100 CGl ILE A 220 7.000 30.957 40.360 1.00 14.26 A C
ATOM 1101 CDl ILE A 220 6.352 31.223 38.975 1.00 11.23 A C
ATOM 1102 CG2 ILE A 220 9.328 30.222 39.660 1.00 13.38 A C
ATOM 1103 C ILE A 220 8.246 32.810 42.473 1.00 14.77 A C
ATOM 1104 O ILE A 220 8.126 33.856 41.856 1.00 16.07 A O
ATOM 1105 N GLN A 221 7.724 32.640 43.683 1.00 14.60 A N
ATOM 1106 CA GLN A 221 7.237 33.787 44.466 1.00 15.23 A C
ATOM 1107 CB GLN A 221 6.235 33.370 45.560 1.00 14.55 A C
ATOM 1108 CG GLN A 221 5.795 34.586 46.305 1.00 21.28 A C
ATOM 1109 CD GLN A 221 4.411 34.447 46.838 1.00 31.36 A C
ATOM 1110 OEl GLN A 221 3.454 34.938 46.230 1.00 36.73 A O
ATOM 1111 NE2 GLN A 221 4.278 33.795 47.991 1.00 30.94 A N
ATOM 1112 C GLN A 221 8.402 34.526 45.134 1.00 15.13 A C
ATOM 1113 O GLN A 221 8.495 35.729 45.041 1.00 16.25 A O
ATOM 1114 N THR A 222 9.281 33.790 45.806 1.00 14.92 A N
ATOM 1115 CA THR A 222 10.406 34.412 46.513 1.00 14.79 A C
ATOM 1116 CB THR A 222 10.597 33.824 47.928 1.00 14.54 A C
ATOM 1117 OGl THR A 222 10.796 32.393 47.872 1.00 13.27 A O
ATOM 1118 CG2 THR A 222 9.383 34.126 48.803 1.00 13.51 A C
ATOM 1119 C THR A 222 11.719 34.352 45.719 1.00 14.97 A C
ATOM 1120 O THR A 222 12.731 34.799 46.222 1.00 15.87 A O
ATOM 1121 N ASP A 223 11.701 33.768 44.505 1.00 15.33 A N
ATOM 1122 CA ASP A 223 12.895 33.673 43.623 1.00 15.45 A C
ATOM 1123 CB ASP A 223 13.366 35.077 43.181 1.00 16.80 A C
ATOM 1124 CG ASP A 223 12.287 35.846 42.442 1.00 17.51 A C
ATOM 1125 ODl ASP A 223 11.509 35.232 41.689 1.00 21.76 A O
ATOM 1126 OD2 ASP A 223 12.223 37.069 42.604 1.00 21.89 A O
ATOM 1127 C ASP A 223 14.064 32.912 44.260 1.00 15.72 A C
ATOM 1128 O ASP A 223 15.242 33.372 44.221 1.00 15.78 A O
ATOM 1129 N THR A 224 13.737 31.760 44.842 1.00 15.26 A N
ATOM 1130 CA THR A 224 14.666 30.928 45.609 1.00 15.58 A C
ATOM 1131 CB THR A 224 14.253 30.752 47.091 1.00 15.24 A C
ATOM 1132 OGl THR A 224 12.873 30.428 47.214 1.00 14.82 A O
ATOM 1133 CG2 THR A 224 14.556 32.017 47.952 1.00 16.12 A C
ATOM 1134 C THR A 224 14.815 29.535 44.951 1.00 15.68 A C
ATOM 1135 O THR A 224 13.810 28.941 44.460 1.00 14.86 A O
ATOM 1136 N LEϋ A 225 16.063 29.062 44.875 1.00 15.29 A N
ATOM 1137 CA LEU A 225 16.348 27.643 44.622 1.00 14.63 A C
ATOM 1138 CB LED A 225 17.816 27.468 44.192 1.00 14.04 A C
ATOM 1139 CG LEU A 225 18.280 26.056 43.770 1.00 15.04 A C
ATOM 1140 CDl LEU A 225 17.318 25.380 42.800 1.00 17.69 A C
ATOM 1141 CD2 LEU A 225 19.745 26.048 43.218 1.00 16.85 A C
ATOM 1142 C LEU A 225 16.050 26.850 45.895 1.00 14.72 A C
ATOM 1143 O LEU A 225 16.815 26.917 46.879 1.00 14.55 A O
ATOM 1144 N VAL A 226 14.970 26.070 45.909 1.00 13.05 A N
ATOM 1145 CA VAL A 226 14.616 25.298 47.109 1.00 12.02 A C
ATOM 1146 CB VAL A 226 13.111 24.871 47.155 1.00 13.42 A C
ATOM 1147 CGl VAL A 226 12.766 24.059 48.464 1.00 12.13 A C
ATOM 1148 CG2 VAL A 226 12.141 26.074 46.978 1.00 11.13 A C
ATOM 1149 C VAL A 226 15.477 24.033 47.309 1.00 13.98 A C
ATOM 1150 O VAL A 226 15.931 23.774 48.436 1.00 13.16 A O
ATOM 1151 N ALA A 227 15.691 23.261 46.223 1.00 13.41 A N
ATOM 1152 CA ALA A 227 16.442 22.024 46.296 1.00 14.21 A C
ATOM 1153 CB ALA A 227 15.528 20.865 46.820 1.00 12.70 A C
ATOM 1154 C ALA A 227 17.054 21.667 44.916 1.00 15.18 A C
ATOM 1155 O ALA A 227 16.497 22.039 43.852 1.00 14.79 A O
ATOM 1156 N ILE A 228 18.182 20.934 44.971 1.00 14.88 A N
ATOM 1157 CA ILE A 228 18.881 20.308 43.858 1.00 15.08 A C ATOM 1158 CB ILE A 228 20.355 20.738 43.746 1.00 16.21 A C
ATOM 1159 CGl ILE A 228 20.481 22.273 43.816 1.00 15.42 A C
ATOM 1160 CDl ILE A 228 21.895 22.763 44.282 1.00 18.14 A C
ATOM 1161 CG2 ILE A 228 21.002 20.163 42.397 1.00 17.76 A C
ATOM 1162 C ILE A 228 18.815 18.798 44.096 1.00 15.57 A C
ATOM 1163 O ILE A 228 19.246 18.303 45.150 1.00 14.64 A O
ATOM 1164 N PHE A 229 18.251 18.073 43.148 1.00 14.80 A N
ATOM 1165 CA PHE A 229 18.177 16.617 43.237 1.00 16.58 A C
ATOM 1166 CB PHE A 229 16.761 16.116 42.881 1.00 16.88 A C
ATOM 1167 CG PHE A 229 15.693 16.707 43.735 1.00 15.76 A C
ATOM 1168 CDl PHE A 229 15.256 16.045 44.880 1.00 17.41 A C
ATOM 1169 CEl PHE A 229 14.229 16.615 45.718 1.00 16.85 A C
ATOM 1170 CZ PHE A 229 13.686 17.864 45.371 1.00 17.57 A C
ATOM 1171 CE2 PHE A 229 14.115 18.510 44.203 1.00 14.67 A C
ATOM 1172 CD2 PHE A 229 15.124 17.936 43.399 1.00 17.31 A C
ATOM 1173 C PHE A 229 19.220 16.014 42.318 1.00 17.45 A C
ATOM 1174 O PHE A 229 19.087 16.081 41.115 1.00 17.54 A O
ATOM 1175 N GLY A 230 20.274 15.424 42.894 1.00 18.68 A N
ATOM 1176 CA GLY A 230 21.448 15.053 42.103 1.00 20.50 A C
ATOM 1177 C GLY A 230 22.608 14.698 43.008 1.00 23.50 A C
ATOM 1178 O GLY A 230 22.617 15.044 44.214 1.00 24.18 A O
ATOM 1179 N GLY A 231 23.607 14.034 42.449 1.00 23.70 A N
ATOM 1180 CA GLY A 231 24.855 13.882 43.188 1.00 25.41 A C
ATOM 1181 C GLY A 231 25.133 12.424 43.407 1.00 26.30 A C
ATOM 1182 O GLY A 231 25.128 11.654 42.446 1.00 25.79 A O
ATOM 1183 N VAL A 232 25.350 12.052 44.670 1.00 27.14 A N
ATOM 1184 CA VAL A 232 25.838 10.689 45.009 1.00 27.84 A C
ATOM 1185 CB VAL A 232 25.876 10.386 46.520 1.00 27.99 A C
ATOM 1186 CGl VAL A 232 26.388 8.886 46.769 1.00 27.53 A C
ATOM 1187 CG2 VAL A 232 26.769 11.435 47.243 1.00 24.98 A C
ATOM 1188 C VAL A 232 25.054 9.580 44.335 1.00 28.24 A C
ATOM 1189 O VAL A 232 25.653 8.732 43.688 1.00 30.05 A O
ATOM 1190 N GLO A 233 23.736 9.533 44.498 1.00 28.42 A N
ATOM 1191 CA GLU A 233 22.969 8.490 43.761 1.00 26.21 A C
ATOM 1192 CB GLU A 233 22.546 7.391 44.733 1.00 27.06 A C
ATOM 1193 CG GLU A 233 23.761 6.587 45.339 1.00 27.54 A C
ATOM 1194 CD GLU A 233 24.453 5.606 44.338 1.00 32.03 A C
ATOM 1195 OEl GLU A 233 23.771 5.079 43.436 1.00 35.47 A O
ATOM 1196 OE2 GLU A 233 25.686 5.357 44.435 1.00 32.86 A O
ATOM 1197 C GLU A 233 21.849 9.047 42.828 1.00 25.29 A C
ATOM 1198 O GLU A 233 20.782 8.434 42.662 1.00 24.25 A O
ATOM 1199 N GLY A 234 22.123 10.201 42.212 1.00 23.55 A N
ATOM 1200 CA GLY A 234 21.210 10.793 41.241 1.00 22.16 A C
ATOM 1201 C GLY A 234 21.533 10.294 39.858 1.00 21.71 A C
ATOM 1202 O GLY A 234 22.343 9.363 39.685 1.00 21.31 A O
ATOM 1203 N HIS A 235 20.931 10.928 38.850 1.00 20.01 A N
ATOM 1204 CA HIS A 235 21.194 10.555 37.493 1.00 18.47 A C
ATOM 1205 CB HIS A 235 20.257 11.305 36.514 1.00 18.74 A C
ATOM 1206 CG HIS A 235 18.823 10.888 36.639 1.00 17.10 A C
ATOM 1207 NDl HIS A 235 18.322 9.741 36.054 1.00 16.88 A N
ATOM 1208 CEl HIS A 235 17.041 9.609 36.375 1.00 16.93 A C
ATOM 1209 NE2 HIS A 235 16.691 10.643 37.122 1.00 16.05 A N
ATOM 1210 CD2 HIS A 235 17.788 11.453 37.313 1.00 14.30 A C
ATOM 1211 C HIS A 235 22.679 10.694 37.116 1.00 19.46 A C
ATOM 1212 O HIS A 235 23.352 11.618 37.573 1.00 17.74 A O
ATOM 1213 N ARG A 236 23.163 9.741 36.312 1.00 19.98 A N
ATOM 1214 CA ARG A 236 24.563 9.719 35.811 1.00 21.41 A C
ATOM 1215 CB ARG A 236 25.132 8.307 35.863 1.00 22.27 A C
ATOM 1216 CG ARG A 236 25.043 7.642 37.200 1.00 26.80 A C
ATOM 1217 CD ARG A 236 26.168 8.107 38.077 1.00 35.73 A C
ATOM 1218 NE ARG A 236 25.836 7.813 39.469 1.00 41.52 A N
ATOM 1219 CZ ARG A 236 25.653 8.741 40.411 1.00 42.11 A C
ATOM 1220 NHl ARG A 236 25.809 10.037 40.139 1.00 41.68 A N
ATOM 1221 NH2 ARG A 236 25.331 8.357 41.627 1.00 42.18 A N
ATOM 1222 C ARG A 236 24.711 10.224 34.398 1.00 20.91 A C
ATOM 1223 O ARG A 236 25.792 10.141 33.824 1.00 21.72 A O
ATOM 1224 N ASP A 237 23.629 10.754 33.818 1.00 20.41 A N
ATOM 1225 CA ASP A 237 23.656 11.338 32.470 1.00 19.20 A C
ATOM 1226 CB ASP A 237 23.528 10.243 31.401 1.00 19.95 A C
ATOM 1227 CG ASP A 237 24.050 10.685 30.032 1.00 19.34 A C
ATOM 1228 ODl ASP A 237 24.143 11.901 29.675 1.00 21.14 A O
ATOM 1229 OD2 ASP A 237 24.348 9.781 29.257 1.00 24.82 A O
ATOM 1230 C ASP A 237 22.474 12.338 32.403 1.00 18.63 A C
ATOM 1231 O ASP A 237 21.790 12.506 33.415 1.00 17.33 A O
ATOM 1232 N GLU A 238 22.236 12.981 31.248 1.00 19.04 A N
ATOM 1233 CA GLU A 238 21.135 13.989 31.108 1.00 19.03 A C
ATOM 1234 CB GLU A 238 20.827 14.363 29.668 1.00 19.41 A C ATOM 1235 CG GLU A 238 21.970 14.905 28.870 1.00 22.04 A C
ATOM 1236 CD GLU A 238 21.514 15.553 27.560 1.00 22.70 A C
ATOM 1237 OEl GLD A 238 20.421 16.199 27.476 1.00 23.15 A O
ATOM 1238 OE2 GLO A 238 22.296 15.457 26.605 1.00 20.65 A O
ATOM 1239 C GLO A 238 19.825 13.509 31.707 1.00 18.35 A C
ATOM, 1240 O GLO A 238 19.412 12.374 31.455 1.00 17.60 A O
ATOM 1241 N VAL A 239 19.162 14.374 32.488 1.00 17.91 A N
ATOM 1242 CA VAL A 239 17.757 14.115 32.875 1.00 17.09 A C
ATOM 1243 CB VAL A 239 17.384 14.726 34.240 1.00 17.28 A C
ATOM 1244 CGl VAL A 239 16.047 14.134 34.759 1.00 16.93 A C
ATOM 1245 CG2 VAL A 239 18.492 14.417 35.251 1.00 16.56 A C
ATOM 1246 C VAL A 239 16.872 14.643 31.710 1.00 16.80 A C
ATOM 1247 O VAL A 239 17.054 15.764 31.269 1.00 17.24 A O
ATOM 1248 N LEU A 240 15.964 13.811 31.209 1.00 15.60 A N
ATOM 1249 CA LEU A 240 15.084 14.178 30.067 1.00 15.02 A C
ATOM 1250 CB LEU A 240 15.038 13.021 29.060 1.00 14.43 A C
ATOM 1251 CG LEU A 240 16.422 12.685 28.450 1.00 16.30 A C
ATOM 1252 CDl LEU A 240 16.433 11.395 27.603 1.00 16.29 A C
ATOM 1253 CD2 LEU A 240 16.967 13.901 27.645 1.00 15.04 A C
ATOM 1254 C LEU A 240 13.654 14.565 30.436 1.00 13.70 A C
ATOM 1255 O LEU A 240 12.985 15.331 29.706 1.00 12.21 A O
ATOM 1256 N SER A 241 13.168 13.970 31.519 1.00 14.27 A N
ATOM 1257 CA SER A 241 11.790 14.158 31.927 1.00 14.86 A C
ATOM 1258 CB SER A 241 10.847 13.222 31.071 1.00 15.37 A C
ATOM 1259 OG SER A 241 9.484 13.492 31.339 1.00 15.13 A O
ATOM 1260 C SER A 241 11.585 14.025 33.422 1.00 14.25 A C
ATOM 1261 O SER A 241 12.425 13.461 34.167 1.00 13.93 A O
ATOM 1262 N ALA A 242 10.459 14.553 33.890 1.00 14.66 A N
ATOM 1263 CA ALA A 242 10.030 14.330 35.272 1.00 14.27 A C
ATOM 1264 CB ALA A 242 10.910 15.153 36.296 1.00 12.79 A C
ATOM 1265 C ALA A 242 8.556 14.654 35.435 1.00 15.53 A C
ATOM 1266 O ALA A 242 7.968 15.336 34.593 1.00 15.01 A O
ATOM 1267 N ASP A 243 7.961 14.152 36.512 1.00 14.99 A N
ATOM 1268 CA ASP A 243 6.565 14.426 36.788 1.00 15.49 A C
ATOM 1269 CB ASP A 243 5.660 13.411 36.010 1.00 15.52 A C
ATOM 1270 CG ASP A 243 4.195 13.816 35.957 1.00 18.13 A C
ATOM 1271 ODl ASP A 243 3.906 14.979 35.603 1.00 18.43 A O
ATOM 1272 OD2 ASP A 243 3.299 12.943 36.179 1.00 15.79 A O
ATOM 1273 C ASP A 243 6.256 14.362 38.294 1.00 14.13 A C
ATOM 1274 O ASP A 243 6.677 13.453 39.005 1.00 10.89 A O
ATOM 1275 N TYR A 244 5.463 15.334 38.750 1.00 13.96 A N
ATOM 1276 CA TYR A 244 4.855 15.277 40.076 1.00 15.04 A C
ATOM 1277 CB TYR A 244 4.283 16.643 40.414 1.00 12.97 A C
ATOM 1278 CG TYR A 244 5.230 17.818 40.640 1.00 14.34 A C
ATOM 1279 CDl TYR A 244 5.844 18.007 41.908 1.00 10.88 A C
ATOM 1280 CEl TYR A 244 6.613 19.096 42.165 1.00 14.61 A C
ATOM 1281 CZ TYR A 244 6.818 20.061 41.194 1.00 13.66 A C
ATOM 1282 OH TYR A 244 7.547 21.193 41.529 1.00 15.16 A O
ATOM 1283 CE2 TYR A 244 6.259 19.933 39.941 1.00 15.58 A C
ATOM 1284 CD2 TYR A 244 5.433 18.795 39.655 1.00 13.13 A C
ATOM 1285 C TYR A 244 3.708 14.268 40.122 1.00 15.32 A C
ATOM 1286 O TYR A 244 2.943 14.163 39.151 1.00 14.84 A O
ATOM 1287 N ASP A 245 3.531 13.552 41.236 1.00 15.84 A N
ATOM 1288 CA ASP A 245 2.256 12.798 41.411 1.00 17.53 A C
ATOM 1289 CB ASP A 245 2.309 11.781 42.555 1.00 17.32 A C
ATOM 1290 CG ASP A 245 2.361 12.451 43.947 1.00 20.01 A C
ATOM 1291 ODl ASP A 245 2.801 13.624 44.070 1.00 18.22 A O
ATOM 1292 OD2 ASP A 245 1.955 11.787 44.920 1.00 24.23 A O
ATOM 1293 C ASP A 245 1.081 13.762 41.658 1.00 17.98 A C
ATOM 1294 O ASP A 245 1.251 14.976 41.670 1.00 16.28 A O
ATOM 1295 N LEO A 246 -0.114 13.191 41.849 1.00 19.30 A N
ATOM 1296 CA LEO A 246 -1.360 13.941 41.935 1.00 20.22 A C
ATOM 1297 CB LEO A 246 -2.528 12.981 42.271 1.00 20.98 A C
ATOM 1298 CG LEO A 246 -3.887 13.670 42.255 1.00 21.99 A C
ATOM 1299 CDl LEO A 246 -4.150 14.369 40.918 1.00 24.62 A C
ATOM 1300 CD2 LEU A 246 -5.030 12.725 42.651 1.00 21.53 A C
ATOM 1301 C LEU A 246 -1.315 15.010 43.011 1.00 20.03 A C
ATOM 1302 O LEU A 246 -1.752 16.156 42.823 1.00 18.29 A O
ATOM 1303 N LEU A 247 -0.800 14.613 44.164 1.00 21.53 A N
ATOM 1304 CA LEU A 247 -0.780 15.507 45.310 1.00 22.90 A C
ATOM 1305 CB LEO A 247 -0.924 14.681 46.585 1.00 24.04 A C
ATOM 1306 CG LEO A 247 -1.915 13.507 46.570 1.00 27.20 A C
ATOM 1307 CDl LEO A 247 -1.564 12.478 47.667 1.00 31.21 A C
ATOM 1308 CD2 LEO A 247 -3.333 13.974 46.723 1.00 30.13 A C
ATOM 1309 C LEO A 247 0.453 16.417 45.365 1.00 21.86 A C
ATOM 1310 O LEU A 247 0.482 17.373 46.155 1.00 22.66 A O
ATOM 1311 N GLY A 248 1.447 16.158 44.524 1.00 19.86 A N ATOM 1312 CA GLY A 248 2.762 16.827 44.630 1.00 19.70 A C
ATOM 1313 C GLY A 248 3.575 16.428 45.879 1.00 19.55 A C
ATOM 1314 O GLY A 248 4.298 17.247 46.451 1.00 19.32 A O
ATOM 1315 N GLU A 249 3.419 15.184 46.316 1.00 18.60 A N
ATOM 1316 CA GLϋ A 249 4.186 14.629 47.410 1.00 18.88 A C
ATOM 1317 CB GLU A 249 3.331 13.603 48.161 1.00 18.86 A C
ATOM 1318 CG GLϋ A 249 2.215 14.312 48.980 1.00 20.32 A C
ATOM 1319 CD GLU A 249 1.302 13.393 49.798 1.00 21.20 A C
ATOM 1320 OEl GLU A 249 1.212 12.167 49.562 1.00 27.96 A O
ATOM 132. OE2 GLU A 249 0.642 13.942 50.694 1.00 27.70 A O
ATOM 1322 C GLU A 249 5.513 13.998 46.950 1.00 18.48 A C
ATOM 1323 O GLU A 249 6.460 13.841 47.748 1.00 17.66 A O
ATOM 1324 N LYS A 250 5.578 13.641 45.674 1.00 18.08 A N
ATOM 1325 CA LYS A 250 6.744 12.952 45.102 1.00 18.07 A C
ATOM 1326 CB LYS A 250 6.690 11.439 45.397 1.00 18.08 A C
ATOM 1327 CG LYS A 250 5.350 10.780 45.083 1.00 18.28 A C
ATOM 1328 CD LYS A 250 5.260 9.358 45.666 1.00 17.42 A C
ATOM 1329 CE LYS A 250 3.947 8.660 45.296 1.00 17.77 A C
ATOM 1330 NZ LYS A 250 2.767 9.167 46.032 1.00 11.11 A N
ATOM 1331 C LYS A 250 6.898 13.218 43.610 1.00 17.58 A C
ATOM 1332 O LYS A 250 5.926 13.583 42.902 1.00 16.91 A O
ATOM 1333 N ILE A 251 8.139 13.047 43.143 1.00 16.84 A N
ATOM 1334 CA ILE A 251 8.534 13.279 41.758 1.00 15.88 A C
ATOM 1335 CB ILE A 251 9.622 14.391 41.658 1.00 15.83 A C
ATOM 1336 CGl ILE A 251 9.099 15.750 42.162 1.00 15.08 A C
ATOM 1337 CDl ILE A 251 10.277 16.712 42.559 1.00 15.77 A C
ATOM 1338 CG2 ILE A 251 10.220 14.503 40.202 1.00 16.20 A C
ATOM 1339 C ILE A 251 9.158 12.005 41.233 1.00 15.76 A C
ATOM 1340 O ILE A 251 10.014 11.424 41.890 1.00 16.41 A O
ATOM 1341 N MET A 252 8.741 11.572 40.046 1.00 15.15 A N
ATOM 1342 CA MET A 252 9.525 10.569 39.329 1.00 14.97 A C
ATOM 1343 CB MET A 252 8.615 9.437 38.754 1.00 15.04 A C
ATOM 1344 CG MET A 252 9.367 8.149 38.273 1.00 14.49 A C
ATOM 1345 SD MET A 252 10.085 7.175 39.645 1.00 18.86 A S
ATOM 1346 CE MET A 252 8.596 6.443 40.295 1.00 17.97 A C
ATOM 1347 C MET A 252 10.274 11.274 38.203 1.00 15.64 A C
ATOM 1348 O MET A 252 9.671 12.038 37.399 1.00 14.42 A O
ATOM 1349 N SER A 253 11.567 10.977 38.098 1.00 15.59 A N
ATOM 1350 CA SER A 253 12.411 11.502 37.009 1.00 15.69 A C
ATOM 1351 CB SER A 253 13.552 12.354 37.586 1.00 16.88 A C
ATOM 1352 OG SER A 253 14.420 11.569 38.424 1.00 15.38 A O
ATOM 1353 C SER A 253 12.996 10.359 36.161 1.00 14.94 A C
ATOM 1354 O SER A 253 13.062 9.238 36.618 1.00 14.98 A O
ATOM 1355 N CYS A 254 13.490 10.666 34.964 1.00 15.20 A N
ATOM 1356 CA CYS A 254 14.056 9.675 34.068 1.00 15.84 A C
ATOM 1357 CB CYS A 254 12.944 8.944 33.291 1.00 14.83 A C
ATOM 1358 SG CYS A 254 12.062 9.984 32.170 1.00 17.37 A S
ATOM 1359 C CYS A 254 15.047 10.282 33.078 1.00 15.74 A C
ATOM 1360 O CYS A 254 15.027 11.495 32.804 1.00 14.54 A O
ATOM 1361 N GLY A 255 15.913 9.442 32.509 1.00 15.70 A N
ATOM 1362 CA GLY A 255 16.960 10.026 31.694 1.00 16.37 A C
ATOM 1363 C GLY A 255 17.723 9.136 30.749 1.00 16.67 A C
ATOM 1364 O GLY A 255 17.302 8.011 30.442 1.00 14.94 A O
ATOM 1365 N MET A 256 18.848 9.684 30.301 1.00 17.89 A N
ATOM 1366 CA MET A 256 19.756 9.036 29.357 1.00 21.21 A C
ATOM 1367 CB MET A 256 20.733 10.033 28.775 1.00 21.08 A C
ATOM 1368 CG MET A 256 20.176 10.804 27.625 1.00 24.64 A C
ATOM 1369 SD MET A 256 21.387 11.815 26.720 1.00 29.50 A S
ATOM 1370 CE MET A 256 22.925 10.993 26.934 1.00 34.88 A C
ATOM 1371 C MET A 256 20.531 7.886 29.982 1.00 20.85 A C
ATOM 1372 O MET A 256 21.007 7.037 29.254 1.00 20.92 A O
ATOM 1373 N ASP A 257 20.614 7.857 31.313 1.00 20.08 A N
ATOM 1374 CA ASP A 257 21.181 6.715 32.014 1.00 21.12 A C
ATOM 1375 CB ASP A 257 21.706 7.121 33.407 1.00 20.74 A C
ATOM 1376 CG ASP A 257 20.597 7.618 34.357 1.00 22.73 A C
ATOM 1377 ODl ASP A 257 19.396 7.555 33.986 1.00 20.94 A O
ATOM 1378 OD2 ASP A 257 20.931 8.085 35.473 1.00 19.64 A O
ATOM 1379 C ASP A 257 20.250 5.469 32.056 1.00 20.17 A C
ATOM 1380 O ASP A 257 20.584 4.482 32.710 1.00 21.28 A O
ATOM 1381 N HIS A 258 19.128 5.507 31.321 1.00 19.79 A N
ATOM 1382 CA HIS A 258 18.103 4.425 31.281 1.00 21.00 A C
ATOM 1383 CB HIS A 258 18.666 3.022 30.960 1.00 21.12 A C
ATOM 1384 CG HIS A 258 19.582 2.957 29.775 1.00 22.36 A C
ATOM 1385 NDl HIS A 258 19.969 1.756 29.224 1.00 23.10 A N
ATOM 1386 CEl HIS A 258 20.775 1.980 28.194 1.00 22.80 A C
ATOM 1387 NE2 HIS A 258 20.927 3.284 28.061 1.00 23.93 A N
ATOM 1388 CD2 HIS A 258 20.185 3.922 29.030 1.00 25.25 A C ATOM 1389 C HIS A 258 17.339 4.257 32.596 1.00 20.74 A C
ATOM 1390 O HIS A 258 16.503 3.352 32.701 1.00 22.52 A O
ATOM 1391 N SER A 259 17.614 5.082 33.607 00 20.67 A N
ATOM 1392 CA SER A 259 16.930 4.935 34.891 00 20.63 A C
ATOM 1393 CB SER A 259 17.935 4.980 36.074 00 22.49 A C
ATOM 1394 OG SER A 259 18.041 6.278 36.622 00 24.15 A O
ATOM 1395 C SER A 259 15.725 5.866 35.164 00 20.63 A C
ATOM 1396 O SER A 259 15.623 7.001 34.625 00 20.65 A O
ATOM 1397 N LEO A 260 14.807 5.345 35.989 00 19.28 A N
ATOM 1398 CA LEO A 260 13.697 6.088 36.600 00 18.60 A C
ATOM 1399 CB LEO A 260 12.368 5.397 36.302 00 17.68 A C
ATOM 1400 CG LEU A 260 11.990 5.499 34.810 00 18.93 A C
ATOM 1401 CDl LEO A 260 11.872 4.084 34.096 00 20.32 A C
ATOM 1402 CD2 LEU A 260 10.760 6.407 34.560 00 18.11 A C
ATOM 1403 C LEU A 260 13.950 6.184 38.122 00 18.48 A C
ATOM 1404 O LEU A 260 14.203 5.153 38.791 00 17.85 A O
ATOM 1405 N LYS A 261 13.860 7.414 38.667 00 16.20 A N
ATOM 1406 CA LYS A 261 14.135 7.657 40.058 00 16.70 A C
ATOM 1407 CB LYS A 261 15.507 8.384 40.228 00 15.92 A C
ATOM 1408 CG LYS A 261 16.746 7.568 39.706 00 16.51 A C
ATOM 1409 CD LYS A 261 18.061 8.362 39.895 00 16.28 A C
ATOM 1410 CE LYS A 261 19.209 7.734 39.103 1.00 20.56 A C
ATOM 1411 NZ LYS A 261 19.593 6.451 39.783 1.00 22.10 A N
ATOM 1412 C LYS A 261 13.031 8.456 40.734 1.00 15.42 A C
ATOM 1413 O LYS A 261 12.521 9.425 40.169 1.00 14.01 A O
ATOM 1414 N LEO A 262 12.673 8.012 41.938 1.00 16.02 A N
ATOM 1415 CA LEU A 262 11.656 8.628 42.794 1.00 16.16 A C
ATOM 1416 CB LEU A 262 10.886 7.535 43.560 16.14 A C
ATOM 1417 CG LEU A 262 9.750 7.959 44.498 16.75 A C
ATOM 1418 CDl LEU A 262 8.590 8.644 43.715 15.29 A C
ATOM 1419 CD2 LEU A 262 9.196 6.732 45.337 17.10 A C
ATOM 1420 C LEU A 262 12.324 9.593 43.782 16.87 A C
ATOM 1421 O LEU A 262 13.364 9.269 44.401 18.22 A O
ATOM 1422 N TRP A 263 11.746 10.770 43.940 15.86 A N
ATOM 1423 CA TRP A 263 12.201 11.687 44.969 15.69 A C
ATOM 1424 CB TRP A 263 12.924 12.869 44.329 15.86 A C
ATOM 1425 CG TRP A 263 13.903 12.543 43.260 15.54 A C
ATOM 1426 CDl TRP A 263 13.634 12.287 41.916 15.12 A C
ATOM 1427 NEl TRP A 263 14.815 12.060 41.245 13.33 A N
ATOM 1428 CE2 TRP A 263 15.866 12.182 42.121 14.62 A C
ATOM 1429 CD2 TRP A 263 15.336 12.479 43.398 15.38 A C
ATOM 1430 CE3 TRP A 263 16.223 12.640 44.488 1.00 16.11 A C
ATOM 1431 CZ3 TRP A 263 17.589 12.479 44.260 .00 14.83 A C
ATOM 1432 CH2 TRP A 263 18.093 12.210 42.975 .00 14.01 A C
ATOM 1433 CZ2 TRP A 263 17.253 12.037 41.893 .00 14.47 A C
ATOM 1434 C TRP A 263 11.006 12.210 45.744 .00 16.67 A C
ATOM 1435 O TRP A 263 10.187 12.979 45.178 .00 16.68 A O
ATOM 1436 N ARG A 264 10.896 11.819 47.021 .00 16.83 A N
ATOM 1437 CA ARG A 264 9.791 12.237 47.876 .00 18.69 A C
ATOM 1438 CB ARG A 264 9.626 11.263 49.064 .00 19.61 A C
ATOM 1439 CG ARG A 264 9.339 9.807 48.663 .00 19.95 A C
ATOM 1440 CD ARG A 264 9.202 8.923 49.945 1.00 20.94 A C
ATOM 1441 NE ARG A 264 8.961 7.512 49.616 1.00 23.80 A N
ATOM 1442 CZ ARG A 264 7.807 7.039 49.136 00 23.06 A C
ATOM 1443 NHl ARG A 264 6.788 7.860 48.912 00 22.43 A N
ATOM 1444 NH2 ARG A 264 7.667 5.741 48.882 00 21.60 A N
ATOM 1445 C ARG A 264 10.007 13.673 48.407 00 18.36 A C
ATOM 1446 O ARG A 264 11.066 13.962 48.949 00 19.02 A O
ATOM 1447 N ILE A 265 8.992 14.541 48.285 00 17.47 A N
ATOM 1448 CA ILE A 265 9.121 15.959 48.693 00 17.22 A C
ATOM 1449 CB ILE A 265 9.031 16.976 47.492 00 17.64 A C
ATOM 1450 CGl ILE A 265 7.699 16.868 46.724 00 17.31 A C
ATOM 1451 CDl ILE A 265 7.507 18.002 45.697 00 17.89 A C
ATOM 1452 CG2 ILE A 265 10.239 16.827 46.533 00 14.06 A C
ATOM 1453 C ILE A 265 8.183 16.300 49.851 00 16.61 A C
ATOM 1454 O ILE A 265 8.031 17.441 50.239 00 16.17 A O
ATOM 1455 N ASN A 266 7.560 15.273 50.401 00 18.02 A N
ATOM 1456 CA ASN A 266 6.786 15.388 51.643 00 19.62 A C
ATOM 1457 CB ASN A 266 5.461 14.620 51.530 00 20.61 A C
ATOM 1458 CG ASN A 266 5.656 13.117 51.395 00 18.50 A C
ATOM 1459 ODl ASN A 266 6.699 12.631 50.929 00 18.78 A O
ATOM 1460 ND2 ASN A 266 4.645 12.362 51.821 00 20.70 A N
ATOM 1461 C ASN A 266 7.553 14.867 52.856 00 19.53 A C
ATOM 1462 O ASN A 266 6.937 14.599 53.877 00 20.13 A O
ATOM 1463 N SER A 267 8.867 14.690 52.746 00 21.49 A N
ATOM 1464 CA SER A 267 9.714 14.480 53.949 00 22.80 A C
ATOM 1465 CB SER A 267 11.162 14.211 53.555 1.00 23.17 A C ATOM 1466 OG SER A 267 11.721 15.331 52.882 1.00 23.19 A O
ATOM 1467 C SER A 267 9.674 15.722 54.864 1.00 23.82 A C
ATOM 1468 O SER A 267 9.371 16.830 54.404 1.00 22.77 A O
ATOM 1469 N LYS A 268 9.972 15.555 56.157 1.00 24.30 A N
ATOM 1470 CA LYS A 268 10.051 16.733 57.062 1.00 24.34 A C
ATOM 1471 CB LYS A 268 10.442 16.334 58.487 1.00 25.43 A C
ATOM 1472 CG LYS A 268 9.446 15.359 59.131 1.00 31.07 A C
ATOM 1473 CD LYS A 268 10.116 14.636 60.316 1.00 36.23 A C
ATOM 1474 CE LYS A 268 9.933 13.108 60.299 1.00 39.02 A C
ATOM 1475 NZ LYS A 268 10.459 12.584 61.604 1.00 39.15 A N
ATOM 1476 C LYS A 268 11.050 17.746 56.531 1.00 22.60 A C
ATOM 1477 O LYS A 268 10.774 18.947 56.525 1.00 22.13 A O
ATOM 1478 N ARG A 269 12.182 17.227 56.059 1.00 22.63 A N
ATOM 1479 CA ARG A 269 13.284 18.009 55.479 1.00 22.25 A C
ATOM 1480 CB ARG A 269 14.494 17.134 55.066 1.00 20.98 A C
ATOM 1481 CG ARG A 269 15.598 17.900 54.339 1.00 23.67 A C
ATOM 1482 CD ARG A 269 16.729 16.999 53.839 1.00 24.17 A C
ATOM 1483 NE ARG A 269 17.828 17.721 53.172 1.00 31.04 A N
ATOM 1484 CZ ARG A 269 18.925 17.128 52.679 1.00 33.66 A C
ATOM 1485 NHl ARG A 269 19.066 15.811 52.779 1.00 35.90 A N
ATOM 1486 NH2 ARG A 269 19.883 17.834 52.073 1.00 35.34 A N
ATOM 1487 C ARG A 269 12.751 18.892 54.319 1.00 20.42 A C
ATOM 1488 O ARG A 269 12.862 20.097 54.411 1.00 18.83 A O
ATOM 1489 N MET A 270 12.153 18.282 53.291 1.00 19.52 A N
ATOM 1490 CA MET A 270 11.545 19.025 52.165 1.00 19.80 A C
ATOM 1491 CB MET A 270 11.272 18.092 50.957 1.00 20.14 A C
ATOM 1492 CG MET A 270 12.542 17.675 50.201 1.00 21.67 A C
ATOM 1493 SD MET A 270 13.464 19.080 49.530 1.00 24.84 A S
ATOM 1494 CE MET A 270 12.187 20.043 48.693 1.00 22.27 A C
ATOM 1495 C MET A 270 10.340 19.959 52.503 1.00 19.49 A C
ATOM 1496 O MET A 270 10.299 21.095 52.025 1.00 17.95 A O
ATOM 1497 N MET A 271 9.397 19.530 53.351 1.00 20.44 A N
ATOM 1498 CA MET A 271 8.298 20.424 53.750 1.00 21.93 A C
ATOM 1499 CB MET A 271 7.256 19.697 54.609 1.00 22.16 A C
ATOM 1500 CG MET A 271 6.501 18.567 53.857 1.00 23.68 A C
ATOM 1501 SD MET A 271 5.313 17.593 54.852 1.00 29.04 A S
ATOM 1502 CE MET A 271 6.304 16.839 56.173 1.00 27.40 A C
ATOM 1503 C MET A 271 8.862 21.643 54.488 1.00 21.07 A C
ATOM 1504 O MET A 271 8.407 22.776 54.306 1.00 21.02 A O
ATOM 1505 N ASN A 272 9.906 21.411 55.284 1.00 21.03 A N
ATOM 1506 CA ASN A 272 10.491 22.490 56.042 1.00 21.42 A C
ATOM 1507 CB ASN A 272 11.430 21.943 57.123 1.00 22.54 A C
ATOM 1508 CG ASN A 272 12.076 23.041 57.946 1.00 28.02 A C
ATOM 1509 ODl ASN A 272 11.390 23.809 58.658 1.00 32.54 A O
ATOM 1510 ND2 ASN A 272 13.405 23.147 57.835 1.00 34.16 A N
ATOM 1511 C ASN A 272 11.215 23.469 55.100 1.00 19.61 A C
ATOM 1512 O ASN A 272 11.161 24.684 55.339 1.00 19.75 A O
ATOM 1513 N ALA A 273 11.905 22.929 54.087 1.00 16.84 A N
ATOM 1514 CA ALA A 273 12.698 23.729 53.128 1.00 16.98 A C
ATOM 1515 CB ALA A 273 13.598 22.848 52.243 1.00 15.86 A C
ATOM 1516 C ALA A 273 11.766 24.581 52.255 1.00 15.67 A C
ATOM 1517 O ALA A 273 12.091 25.730 51.944 1.00 15.19 A O
ATOM 1518 N ILE A 274 10.611 24.029 51.878 1.00 16.83 A N
ATOM 1519 CA ILE A 274 9.578 24.790 51.122 1.00 15.94 A C
ATOM 1520 CB ILE A 274 8.417 23.863 50.545 1.00 16.38 A C
ATOM 1521 CGl ILE A 274 8.965 22.956 49.442 1.00 14.59 A C
ATOM 1522 CDl ILE A 274 8.237 21.605 49.285 1.00 16.69 A C
ATOM 1523 CG2 ILE A 274 7.234 24.724 50.000 1.00 16.67 A C
ATOM 1524 C ILE A 274 9.052 25.944 51.976 1.00 16.51 A C
ATOM 1525 O ILE A 274 8.948 27.098 51.504 1.00 14.03 A O
ATOM 1526 N LYS A 275 8.756 25.630 53.245 1.00 17.65 A N
ATOM 1527 CA LYS A 275 8.269 26.639 54.189 1.00 19.34 A C
ATOM 1528 CB LYS A 275 7.860 25.998 55.521 1.00 20.11 A C
ATOM 1529 CG LYS A 275 7.449 26.968 56.573 1.00 23.79 A C
ATOM 1530 CD LYS A 275 7.137 26.236 57.892 1.00 34.88 A C
ATOM 1531 CE LYS A 275 8.370 25.493 58.514 1.00 38.34 A C
ATOM 1532 NZ LYS A 275 9.580 26.373 58.814 1.00 40.84 A N
ATOM 1533 C LYS A 275 9.300 27.784 54.350 1.00 18.19 A C
ATOM 1534 O LYS A 275 8.927 28.958 54.316 1.00 19.33 A O
ATOM 1535 N GLU A 276 10.587 27.442 54.479 1.00 18.52 A N
ATOM 1536 CA GLU A 276 11.659 28.457 54.582 1.00 17.12 A C
ATOM 1537 CB GLU A 276 13.009 27.799 54.981 1.00 17.90 A C
ATOM 1538 CG GLU A 276 13.013 27.207 56.416 1.00 19.42 A C
ATOM 1539 CD GLU A 276 12.900 28.302 57.538 1.00 22.75 A C
ATOM ' 1540 OEl GLU A 276 13.191 29.493 57.305 1.00 22.29 A O
ATOM 1541 OE2 GLU A 276 12.457 27.966 58.646 1.00 27.86 A O
ATOM 1542 C GLU A 276 11.789 29.316 53.319 1.00 16.88 A C ATOM 1543 O GLU A 276 12.015 30.553 53.385 00 15.63 A O
ATOM 1544 N SER A 277 11.606 28.690 52.153 00 15.57 A N
ATOM 1545 CA SER A 277 11.647 29.425 50.865 00 15.54 A C
ATOM 1546 CB SER A 277 11.500 28.452 49.650 00 14.87 A C
ATOM 1547 OG SER A 277 10.167 28.050 49.439 00 12.99 A O
ATOM 1548 C SER A 277 10.608 30.540 50.837 00 15.61 A C
ATOM 1549 O SER A 277 10.883 31.622 50.332 00 15.04 A O
ATOM 1550 N TYR A 278 9.437 30.281 51.425 00 16.11 A N
ATOM 1551 CA TYR A 278 8.351 31.292 51.558 00 17.66 A C
ATOM 1552 CB TYR A 278 7.009 30.610 51.907 00 18.71 A C
ATOM 1553 CG TYR A 278 6.314 30.111 50.677 00 18.71 A C
ATOM 1554 CDl TYR A 278 6.203 28.732 50.422 00 15.31 A C
ATOM 1555 CEl TYR A 278 5.588 28.281 49.257 00 16.25 A C
ATOM 1556 CZ TYR A 278 5.059 29.212 48.334 00 16.89 A C
ATOM 1557 OH TYR A 278 4.441 28.752 47.169 00 18.65 A O
ATOM 1558 CE2 TYR A 278 5.172 30.565 48.561 00 18.67 A C
ATOM 1559 CD2 TYR A 278 5.806 31.016 49.732 00 16.37 A C
ATOM 1560 C TYR A 278 8.650 32.379 52.592 00 18.69 A C
ATOM 1561 O TYR A 278 8.196 33.504 52.459 00 18.48 A O
ATOM 1562 N ASP A 279 9.469 32.042 53.588 00 20.35 A N
ATOM 1563 CA ASP A 279 9.848 32.984 54.652 00 21.28 A C
ATOM 1564 CB ASP A 279 10.136 32.228 55.971 00 21.71 A C
ATOM 1565 CG ASP A 279 8.843 31.747 56.699 00 27.95 A C
ATOM 1566 ODl ASP A 279 7.711 32.213 56.379 00 34.45 A O
ATOM 1567 OD2 ASP A 279 8.948 30.857 57.588 00 34.64 A O
ATOM 1568 C ASP A 279 11.060 33.847 54.238 00 20.73 A C
ATOM 1569 O ASP A 279 11.489 34.698 55.003 1.00 22.13 A O
ATOM 1570 N TYR A 280 11.622 33.609 53.052 1.00 19.59 A N
ATOM 1571 CA TYR A 280 12.866 34.241 52.661 .00 18.75 A C
ATOM 1572 CB TYR A 280 13.736 33.305 51.813 .00 18.69 A C
ATOM 1573 CG TYR A 280 15.080 33.960 51.465 .00 18.53 A C
ATOM 1574 CDl TYR A 280 16.083 34.051 52.423 .00 15.73 A C
ATOM 1575 CEl TYR A 280 17.315 34.662 52.143 .00 18.29 A C
ATOM 1576 CZ TYR A 280 17.543 35.207 50.893 .00 17.23 A C
ATOM 1577 OH TYR A 280 18.763 35.800 50.640 ,00 16.38 A O
ATOM 1578 CE2 TYR A 280 16.564 35.129 49.903 .00 16.29 A C
ATOM 1579 CD2 TYR A 280 15.329 34.500 50.201 ,00 17.73 A C
ATOM 1580 C TYR A 280 12.612 35.524 51.900 ,00 20.05 A C
ATOM 1581 O TYR A 280 11.971 35.501 50.834 ,00 17.58 A O
ATOM 1582 N ASN A 281 13.104 36.645 52.440 .00 20.48 A N
ATOM 1583 CA ASN A 281 13.073 37.932 51.727 .00 22.44 A C
ATOM 1584 CB- ASN A 281 12.013 38.899 52.320 1.00 23.14 A C
ATOM 1585 CG ASN A 281 11.976 40.255 51.613 1.00 23.98 A C
ATOM 1586 ODl ASN A 281 12.800 40.551 50.738 .00 25.16 A O
ATOM 1587 ND2 ASN A 281 11.011 41.099 52.004 .00 28.02 A N
ATOM 1588 C ASN A 281 14.442 38.570 51.815 .00 22.92 A C
ATOM 1589 O ASN A 281 14.797 39.040 52.886 .00 22.51 A O
ATOM 1590 N PRO A 282 15.208 38.585 50.691 .00 23.44 A N
ATOM 1591 CA PRO A 282 16.595 39.041 50.727 .00 24.22 A C
ATOM 1592 CB PRO A 282 17.047 38.902 49.276 .00 23.21 A C
ATOM 1593 CG PRO A 282 15.757 38.952 48.479 .00 24.10 A C
ATOM 1594 CD PRO A 282 14.801 38.216 49.323 1.00 23.73 A C
ATOM 1595 C PRO A 282 16.728 40.493 51.219 1.00 25.01 A C
ATOM 1596 O PRO A 282 17.778 40.873 51.746 25.54 A O
ATOM 1597 N ASN A 283 15.664 41.281 51.082 25.87 A N
ATOM 1598 CA ASN A 283 15.674 42.650 51.607 27.26 A C
ATOM 1599 CB ASN A 283 14.551 43.491 50.989 28.38 A C
ATOM 1600 CG ASN A 283 14.640 43.578 49.446 32.61 A C
ATOM 1601 ODl ASN A 283 13.608 43.665 48.766 1.00 37.15 A O
ATOM 1602 ND2 ASN A 283 15.862 43.572 48.899 .00 32.85 A N
ATOM 1603 C ASN A 283 15.652 42.764 53.145 .00 26.57 A C
ATOM 1604 O ASN A 283 16.085 43.779 53.685 .00 27.03 A O
ATOM 1605 N LYS A 284 15.182 41.718 53.823 .00 26.01 A N
ATOM 1606 CA LYS A 284 14.987 41.704 55.280 .00 25.84 A C
ATOM 1607 CB LYS A 284 13.608 41.106 55.638 .00 26.71 A C
ATOM 1608 CG LYS A 284 12.377 41.744 54.958 .00 32.00 A C
ATOM 1609 CD LYS A 284 12.385 43.265 55.006 .00 36.51 A C
ATOM 1610 CE LYS A 284 10.970 43.845 55.062 .00 40.98 A C
ATOM 1611 NZ LYS A 284 10.486 44.042 56.508 .00 42.68 A N
ATOM 1612 C LYS A 284 16.060 40.911 56.051 .00 24.83 A C
ATOM 1613 O LYS A 284 15.941 40.741 57.289 1.00 24.90 A O
ATOM 1614 N THR A 285 17.076 40.399 55.345 1.00 23.39 A N
ATOM 1615 CA THR A 285 18.073 39.496 55.972 21.32 A C
ATOM 1616 CB THR A 285 17.614 38.012 55.959 21.44 A C
ATOM 1617 OGl THR A 285 18.518 37.212 56.745 20.07 A O
ATOM 1618 CG2 THR A 285 17.463 37.451 54.484 18.91 A C
ATOM 1619 C THR A 285 19.451 39.621 55.366 1.00 20.58 A C ATOM 1620 O THR A 285 19.604 40.168 54.290 1.00 19.41 A O
ATOM 1621 N ASN A 286 20.456 39.096 56.076 1.00 19.76 A N
ATOM 1622 CA ASN A 286 21.834 39.058 55.578 1.00 19.43 A C
ATOM 1623 CB ASN A 286 22.809 39.417 56.707 1.00 19.00 A C
ATOM 1624 CG ASN A 286 22.536 40.785 57.278 1.00 19.56 A C
ATOM 1625 ODl ASN A 286 22.168 40.926 58.448 1.00 23.82 A O
ATOM 1626 ND2 ASN A 286 22.677 41.794 56.456 1.00 15.86 A N
ATOM 1627 C ASN A 286 22.219 37.715 54.951 1.00 19.47 A C
ATOM 1628 O ASN A 286 23.185 37.620 54.178 1.00 20.43 A O
ATOM 1629 N ARG A 287 21.459 36.678 55.257 1.00 17.97 A N
ATOM 1630 CA ARG A 287 21.805 35.349 54.718 1.00 18.11 A C
ATOM 1631 CB ARG A 287 21.157 34.238 55.579 1.00 17.50 A C
ATOM 1632 CG ARG A 287 19.613 34.156 55.432 1.00 18.36 A C
ATOM 1633 CD ARG A 287 18.908 33.436 56.599 1.00 16.91 A C
ATOM 1634 NE ARG A 287 17.473 33.709 56.653 1.00 18.51 A N
ATOM 1635 CZ ARG A 287 16.483 32.989 56.086 1.00 19.48 A C
ATOM 1636 NHl ARG A 287 16.706 31.859 55.393 1.00 18.11 A N
ATOM 1637 NH2 ARG A 287 15.220 33.384 56.278 1.00 18.28 A N
ATOM 1638 C ARG A 287 21.431 35.205 53.208 1.00 18.85 A C
ATOM 1639 O ARG A 287 20.491 35.875 52.705 1.00 19.34 A O
ATOM 1640 N PRO A 288 22.159 34.328 52.490 1.00 18.72 A N
ATOM 1641 CA PRO A 288 21.693 33.759 51.229 1.00 18.51 A C
ATOM 1642 CB PRO A 288 22.964 33.129 50.623 1.00 17.56 A C
ATOM 1643 CG PRO A 288 23.814 32.758 51.826 1.00 18.07 A C
ATOM 1644 CD PRO A 288 23.468 33.769 52.913 1.00 19.74 A C
ATOM 1645 C PRO A 288 20.654 32.692 51.568 1.00 17.71 A C
ATOM 1646 O PRO A 288 20.539 32.293 52.733 1.00 18.20 A O
ATOM 1647 N PHE A 289 19.841 32.268 50.594 1.00 16.50 A N
ATOM 1648 CA PHE A 289 18.900 31.208 50.885 1.00 15.50 A C
ATOM 1649 CB PHE A 289 17.654 31.248 49.950 1.00 15.08 A C
ATOM 1650 CG PHE A 289 16.665 30.174 50.306 1.00 12.72 A C
ATOM 1651 CDl PHE A 289 15.901 30.295 51.476 1.00 13.28 A C
ATOM 1652 CEl PHE A 289 15.028 29.298 51.900 1.00 17.37 A C
ATOM 1653 CZ PHE A 289 14.926 28.119 51.115 1.00 14.78 A C
ATOM 1654 CE2 PHE A 289 15.709 27.993 49.959 1.00 14.50 A C
ATOM 1655 CD2 PHE A 289 16.582 29.005 49.560 1.00 15.86 A C
ATOM 1656 C PHE A 289 19.656 29.914 50.703 1.00 15.89 A C
ATOM 1657 O PHE A 289 20.333 29.757 49.667 1.00 16.76 A O
ATOM 1658 N ILE A 290 19.602 29.002 51.673 1.00 15.57 A N
ATOM 1659 CA ILE A 290 20.403 27.815 51.537 1.00 16.93 A C
ATOM 1660 CB ILE A 290 21.076 27.381 52.843 1.00 18.37 A C
ATOM 1661 CGl ILE A 290 22.200 28.390 53.185 1.00 20.46 A C
ATOM 1662 CDl ILE A 290 22.224 28.784 54.559 1.00 28.20 A C
ATOM 1663 CG2 ILE A 290 21.754 26.011 52.646 1.00 15.81 A C
ATOM 1664 C ILE A 290 19.539 26.721 50.884 1.00 17.26 A C
ATOM 1665 O ILE A 290 18.489 26.390 51.411 1.00 16.67 A O
ATOM 1666 N SER A 291 19.988 26.194 49.740 1.00 17.87 A N
ATOM 1667 CA SER A 291 19.273 25.114 49.022 1.00 19.53 A C
ATOM 1668 CB SER A 291 19.795 25.040 47.566 1.00 19.86 A C
ATOM 1669 OG SER A 291 19.773 26.352 46.959 1.00 22.87 A O
ATOM 1670 C SER A 291 19.519 23.758 49.685 1.00 19.61 A C
ATOM 1671 O SER A 291 20.616 23.533 50.230 1.00 20.08 A O
ATOM 1672 N GLN A 292 18.558 22.843 49.578 1.00 19.36 A N
ATOM 1673 CA GLN A 292 18.792 21.418 49.965 1.00 20.24 A C
ATOM 1674 CB GLN A 292 17.500 20.641 50.253 1.00 19.69 A C
ATOM 1675 CG GLN A 292 16.533 21.255 51.267 1.00 21.11 A C
ATOM 1676 CD GLN A 292 17.230 21.605 52.624 1.00 25.43 A C
ATOM 1677 OEl GLN A 292 17.781 20.714 53.293 1.00 23.59 A O
ATOM 1678 NE2 GLN A 292 17.204 22.890 53.008 1.00 19.81 A N
ATOM 1679 C GLN A 292 19.554 20.709 48.859 1.00 20.52 A C
ATOM 1680 O GLN A 292 19.248 20.874 47.672 1.00 18.69 A O
ATOM 1681 N LYS A 293 20.603 19.968 49.230 1.00 20.86 A N
ATOM 1682 CA LYS A 293 21.255 19.091 48.259 1.00 21.95 A C
ATOM 1683 CB LYS A 293 22.793 19.229 48.281 1.00 23.33 A C
ATOM 1684 CG LYS A 293 23.341 20.447 47.498 1.00 24.91 A C
ATOM 1685 CD LYS A 293 22.947 21.841 48.113 1.00 26.98 A C
ATOM 1686 CE LYS A 293 23.777 22.232 49.366 1.00 30.00 A C
ATOM 1687 NZ LYS A 293 23.426 23.610 49.827 1.00 31.10 A N
ATOM 1688 C LYS A 293 20.779 17.672 48.577 1.00 22.03 A C
ATOM 1689 O LYS A 293 21.125 17.114 49.599 1.00 21.63 A O
ATOM 1690 N ILE A 294 19.900 17.146 47.726 1.00 21.12 A N
ATOM 1691 CA ILE A 294 19.334 15.813 47.916 1.00 20.01 A C
ATOM 1692 CB ILE A 294 17.829 15.793 47.588 1.00 20.09 A C
ATOM 1693 CGl ILE A 294 17.089 16.955 48.301 1.00 18.76 A C
ATOM 1694 CDl ILE A 294 17.081 16.878 49.786 1.00 21.27 A C
ATOM 1695 CG2 ILE A 294 17.209 14.391 47.856 1.00 19.40 A C
ATOM 1696 C ILE A 294 20.121 14.854 47.013 1.00 20.58 A C ATOM 1697 O ILE A 294 19.986 14.880 45.792 1.00 19.70 A O
ATOM 1698 N HIS A 295 20.975 14.042 47.630 1.00 19.65 A N
ATOM 1699 CA HIS A 295 21.902 13.150 46.896 1.00 20.92 A C
ATOM 1700 CB HIS A 295 23.235 13.047 47.688 1.00 21.33 A C
ATOM 1701 CG HIS A 295 24.122 14.255 47.574 1.00 22.07 A C
ATOM 1702 NDl HIS A 295 25.072 14.393 46.585 1.00 22.03 A N
ATOM 1703 CEl HIS A 295 25.705 15.541 46.741 1.00 23.94 A C
ATOM 1704 NE2 HIS A 295 25.249 16.125 47.836 1.00 22.94 A N
ATOM 1705 CD2 HIS A 295 24.267 15.335 48.385 1.00 24.55 A C
ATOM 1706 C HIS A 295 21.343 11.728 46.677 1.00 20.79 A C
ATOM 1707 O HIS A 295 21.921 10.939 45.929 1.00 21.15 A O
ATOM 1708 N PHE A 296 20.241 11.397 47.347 1.00 20.80 A N
ATOM 1709 CA PHE A 296 19.726 10.005 47.399 1.00 21.45 A C
ATOM 1710 CB PHE A 296 19.991 9.377 48.784 1.00 22.16 A C
ATOM 1711 CG PHE A 296 21.440 9.327 49.115 1.00 20.80 A C
ATOM 1712 CDl PHE A 296 22.254 8.351 48.533 1.00 24.39 A C
ATOM 1713 CEl PHE A 296 23.635 8.314 48.782 1.00 23.48 A C
ATOM 1714 CZ PHE A 296 24.221 9.310 49.610 1.00 24.69 A C
ATOM 1715 CE2 PHE A 296 23.427 10.308 50.166 1.00 22.55 A C
ATOM 1716 CD2 PHE A 296 22.026 10.316 49.891 1.00 23.07 A C
ATOM 1717 C PHE A 296 18.238 9.916 47.066 1.00 21.43 A C
ATOM 1718 O PHE A 296 17.389 10.429 47.824 1.00 21.24 A O
ATOM 1719 N PRO A 297 17.924 9.282 45.928 1.00 21.91 A N
ATOM 1720 CA PRO A 297 16.529 9.074 45.566 1.00 21.44 A C
ATOM 1721 CB PRO A 297 16.604 8.613 44.106 1.00 21.97 A C
ATOM 1722 CG PRO A 297 17.945 7.963 43.959 1.00 22.73 A C
ATOM 1723 CD PRO A 297 18.868 8.733 44.918 1.00 21.26 A C
ATOM 1724 C PRO A 297 15.868 8.016 46.466 1.00 22.80 A C
ATOM 1725 O PRO A 297 16.545 7.172 47.050 1.00 23.31 A O
ATOM 1726 N ASP A 298 14.550 8.057 46.553 1.00 23.05 A N
ATOM 1727 CA ASP A 298 13.761 7.150 47.436 1.00 23.34 A C
ATOM 1728 CB ASP A 298 12.526 7.906 47.935 1.00 22.41 A C
ATOM 1729 CG ASP A 298 12.904 9.085 48.841 1.00 25.88 A C
ATOM 1730 ODl ASP A 298 13.222 8.839 50.039 1.00 26.50 A O
ATOM 1731 OD2 ASP A 298 12.950 10.239 48.344 1.00 23.50 A O
ATOM 1732 C ASP A 298 13.373 5.790 46.789 1.00 22.35 A C
ATOM 1733 O ASP A 298 12.754 4.914 47.441 1.00 22.95 A O
ATOM 1734 N PHE A 299 13.786 5.615 45.536 1.00 22.14 A N
ATOM 1735 CA PHE A 299 13.602 4.391 44.750 1.00 21.44 A C
ATOM 1736 CB PHE A 299 12.100 4.023 44.522 1.00 21.06 A C
ATOM 1737 CG PHE A 299 11.894 2.927 43.510 1.00 21.03 A C
ATOM 1738 CDl PHE A 299 11.976 1.581 43.893 1.00 21.25 A C
ATOM 1739 CEl PHE A 299 11.814 0.539 42.938 1.00 23.56 A C
ATOM 1740 CZ PHE A 299 11.594 0.862 41.586 1.00 21.54 A C
ATOM 1741 CE2 PHE A 299 11.526 2.216 41.207 1.00 23.47 A C
ATOM 1742 CD2 PHE A 299 11.661 3.231 42.162 1.00 20.56 A C
ATOM 1743 C PHE A 299 14.306 4.683 43.446 1.00 21.84 A C
ATOM 1744 O PHE A 299 14.385 5.852 43.011 1.00 21.16 A O
ATOM 1745 N SER A 300 14.868 3.633 42.832 1.00 20.97 A N
ATOM 1746 CA SER A 300 15.483 3.752 41.516 1.00 21.38 A C
ATOM 1747 CB SER A 300 16.967 4.104 41.645 1.00 22.27 A C
ATOM 1748 OG SER A 300 17.504 4.382 40.373 1.00 20.47 A O
ATOM 1749 C SER A 300 15.350 2.438 40.748 1.00 22.40 A C
ATOM 1750 O SER A 300 15.480 1.367 41.349 1.00 23.25 A O
ATOM 1751 N THR A 301 15.140 2.506 39.434 1.00 22.13 A N
ATOM 1752 CA THR A 301 15.211 1.279 38.597 1.00 22.35 A C
ATOM 1753 CB THR A 301 13.809 0.537 38.491 1.00 21.97 A C
ATOM 1754 OGl THR A 301 13.922 -0.633 37.662 1.00 21.37 A O
ATOM 1755 CG2 THR A 301 12.705 1.489 37.902 1.00 21.00 A C
ATOM 1756 C THR A 301 15.813 1.537 37.215 1.00 22.78 A C
ATOM 1757 O THR A 301 15.622 2.604 36.652 1.00 22.23 A O
ATOM 1758 N ARG A 302 16.544 0.548 36.682 1.00 23.57 A N
ATOM 1759 CA ARG A 302 16.941 0.504 35.276 1.00 25.73 A C
ATOM 1760 CB ARG A 302 18.478 0.482 35.114 l.'oo 25.99 A C
ATOM 1761 CG ARG A 302 19.198 1.708 35.677 1.00 29.53 A C
ATOM 1762 CD ARG A 302 20.759 1.628 35.548 1.00 30.26 A C
ATOM 1763 NE ARG A 302 21.286 2.143 34.279 1.00 39.25 A N
ATOM 1764 CZ ARG A 302 21.657 1.395 33.229 1.00 43.84 A C
ATOM 1765 NHl ARG A 302 21.547 0.066 33.260 1.00 45.12 A N
ATOM 1766 NH2 ARG A 302 22.131 1.982 32.121 1.00 46.95 A N
ATOM 1767 C ARG A 302 16.330 -0.690 34.503 1.00 25.26 A C
ATOM 1768 O ARG A 302 16.774 -0.999 33.394 1.00 25.48 A O
ATOM 1769 N ASP A 303 15.292 -1.304 35.080 1.00 24.90 A N
ATOM 1770 CA ASP A 303 14.730 -2.581 34.624 1.00 25.97 A C
ATOM 1771 CB ASP A 303 14.333 -3.419 35.823 1.00 26.85 A C
ATOM 1772 CG ASP A 303 15.476 -4.199 36.400 1.00 33.99 A C
ATOM 1773 ODl ASP A 303 16.610 -4.155 35.836 1.00 38.21 A O ATOM 1774 OD2 ASP A 303 15.227 -4.869 37.446 1.00 39.23 A O
ATOM 1775 C ASP A 303 13.455 -2.420 33.801 1.00 24.63 A C
ATOM 1776 O ASP A 303 12.715 -3.395 33.634 1.00 24.37 A O
ATOM 1777 N ILE A 304 13.178 -1.198 33.347 1.00 21.98 A N
ATOM 1778 CA ILE A 304 11.951 -0.918 32.597 1.00 21.69 A C
ATOM 1779 CB ILE A 304 11.194 0.373 33.044 1.00 20.96 A C
ATOM 1780 CGl ILE A 304 10.863 0.310 34.524 1.00 20.77 A C
ATOM 1781 CDl ILE A 304 9.868 -0.821 34.862 1.00 18.82 A C
ATOM 1782 CG2 ILE A 304 9.867 0.532 32.223 1.00 20.20 A C
ATOM 1783 C ILE A 304 12.312 -0.839 31.129 1.00 21.13 A C
ATOM 1784 O ILE A 304 11.750 -1.586 30.325 1.00 21.78 A O
ATOM 1785 N HIS A 305 13.254 0.040 30.788 1.00 20.25 A N
ATOM 1786 CA HIS A 305 13.642 0.236 29.384 1.00 20.48 A C
ATOM 1787 CB HIS A 305 13.423 1.705 28.987 1.00 18.92 A C
ATOM 1788 CG HIS A 305 12.008 2.176 29.171 1.00 17.93 A C
ATOM 1789 NDl HIS A 305 11.601 2.918 30.257 1.00 20.24 A N
ATOM 1790 CEl HIS A 305 10.314 3.176 30.160 1.00 16.30 A C
ATOM 1791 NE2 HIS A 305 9.863 2.611 29.051 1.00 20.17 A N
ATOM 1792 CD2 HIS A 305 10.901 1.990 28.413 1.00 14.36 A C
ATOM 1793 C HIS A 305 15.102 -0.213 29.128 1.00 21.65 A C
ATOM 1794 O HIS A 305 15.866 -0.391 30.078 1.00 22.33 A O
ATOM 1795 N ARG A 306 15.498 -0.367 27.863 1.00 23.56 A N
ATOM 1796 CA ARG A 306 16.888 -0.722 27.556 1.00 25.93 A C
ATOM 1797 CB ARG A 306 16.953 -1.997 26.721 1.00 27.44 A C
ATOM 1798 CG ARG A 306 16.163 -3.171 27.316 1.00 31.98 A C
ATOM 1799 CD ARG A 306 16.441 -3.375 28.797 1.00 41.84 A C
ATOM 1800 NE ARG A 306 15.506 -4.335 29.405 1.00 46.87 A N
ATOM 1801 CZ ARG A 306 15.365 -4.551 30.713 1.00 49.04 A C
ATOM 1802 NHl ARG A 306 16.098 -3.879 31.602 1.00 49.46 A N
ATOM 1803 NH2 ARG A 306 14.478 -5.449 31.132 1.00 49.87 A N
ATOM 1804 C ARG A 306 17.637 0.407 26.861 1.00 25.92 A C
ATOM 1805 O ARG A 306 18.667 0.179 26.219 1.00 25.60 A O
ATOM 1806 N ASN A 307 17.097 1.620 26.964 1.00 25.18 A N
ATOM 1807 CA ASN A 307 17.710 2.798 26.369 1.00 25.08 A C
ATOM 1808 CB ASN A 307 17.426 2.877 24.875 1.00 25.52 A C
ATOM 1809 CG ASN A 307 18.641 3.309 24.092 1.00 27.33 A C
ATOM 1810 ODl ASN A 307 19.235 4.381 24.326 1.00 30.33 A O
ATOM 1811 ND2 ASN A 307 19.037 2.471 23.173 1.00 29.88 A N
ATOM 1812 C ASN A 307 17.233 4.050 27.089 1.00 24.93 A C
ATOM 1813 O ASN A 307 16.555 3.915 28.133 1.00 24.43 A O
ATOM 1814 N TYR A 308 17.618 5.228 26.575 1.00 24.16 A N
ATOM 1815 CA TYR A 308 17.196 6.561 27.135 1.00 24.55 A C
ATOM 1816 CB TYR A 308 17.312 7.702 26.101 i!oo 25.50 A C
ATOM 1817 CG TYR A 308 18.685 8.043 25.568 1.00 30.13 A C
ATOM 1818 CDl TYR A 308 19.846 7.463 26.103 1.00 29.71 A C
ATOM 1819 CEl TYR A 308 21.123. 7.780 25.576 1.00 33.00 A C
ATOM 1820 CZ TYR A 308 21.234' 8.700 24.540 1.00 31.67 A C
ATOM 1821 OH TYR A 308 22.488 9.032 24.043 1.00 32.29 A O
ATOM 1822 CE2 TYR A 308 20.089 9.314 24.009 1.00 33.61 A C
ATOM 1823 CD2 TYR A 308 18.824 8.983 24.525 1.00 30.19 A C
ATOM 1824 C TYR A 308 15.726 6.591 27.499 1.00 22.28 A C
ATOM 1825 O TYR A 308 14.871 6.240 26.697 1.00 22.34 A O
ATOM 1826 N VAL A 309 15.398 7.099 28.667 1.00 20.23 A N
ATOM 1827 CA VAL A 309 13.996 7.150 29.021 1.00 18.09 A C
ATOM 1828 CB VAL A 309 13.750 6.615 30.433 1.00 18.62 A C
ATOM 1829 CGl VAL A 309 12.233 6.526 30.717 1.00 16.92 A C
ATOM 1830 CG2 VAL A 309 14.461 5.218 30.626 1.00 17.80 A C
ATOM 1831 C VAL A 309 13.649 8.627 28.838 1.00 17.77 A C
ATOM 1832 O VAL A 309 14.190 9.457 29.545 1.00 17.28 A O
ATOM 1833 N ASP A 310 12.833 8.946 27.826 1.00 16.05 A N
ATOM 1834 CA ASP A 310 12.603 10.355 27.430 1.00 16.25 A C
ATOM 1835 CB ASP A 310 12.955 10.566 25.935 1.00 15.66 A C
ATOM 1836 CG ASP A 310 11.940 9.881 24.967 1.00 17.45 A C
ATOM 1837 ODl ASP A 310 11.215 8.976 25.431 1.00 16.40 A O
ATOM 1838 OD2 ASP A 310 11.904 10.208 23.749 1.00 15.80 A O
ATOM 1839 C ASP A 310 11.245 10.990 27.798 1.00 15.29 A C
ATOM 1840 O ASP A 310 10.978 12.163 27.464 1.00 13.65 A O
ATOM 1841 N CYS A 311 10.395 10.246 28.515 1.00 14.82 A N
ATOM 1842 CA CYS A 311 9.093 10.806 28.948 1.00 14.30 A C
ATOM 1843 CB CYS A 311 8.072 10.866 27.775 1.00 14.39 A C
ATOM 1844 SG CYS A 311 6.620 11.922 28.095 1.00 14.51 A S
ATOM 1845 C CYS A 311 8.516 9.968 30.061 1.00 14.94 A C
ATOM 1846 O CYS A 311 8.577 8.740 29.977 1.00 14.84 A O
ATOM 1847 N VAL A 312 8.001 10.627 31.109 1.00 13.72 A N
ATOM 1848 CA VAL A 312 7.417 9.915 32.270 1.00 14.56 A C
ATOM 1849 CB VAL A 312 8.458 9.697 33.405 1.00 14.05 A C
ATOM 1850 CGl VAL A 312 8.904 11.037 33.968 1.00 13.35 A C ATOM 1851 CG2 VAL A 312 7.887 8.811 34.507 1.00 12.74 A C
ATOM 1852 C VAL A 312 6.200 10.672 32.804 1.00 15.31 A C
ATOM 1853 O VAL A 312 6.119 11.911 32.728 1.00 15.15 A O
ATOM 1854 N ARG A 313 5.244 9.896 33.356 1.00 15.90 A N
ATOM 1855 CA ARG A 313 4.016 10.419 33.951 1.00 17.42 A C
ATOM 1856 CB ARG A 313 2.900 10.511 32.910 1.00 18.40 A C
ATOM 1857 CG ARG A 313 1.648 11.191 33.416 1.00 25.32 A C
ATOM 1858 CD ARG A 313 1.769 12.677 33.155 1.00 33.73 A C
ATOM 1859 NE ARG A 313 0.519 13.427 33.224 1.00 31.54 A N
ATOM 1860 CZ ARG A 313 0.074 13.789 34.356 1.00 34.53 A C
ATOM 1861 NHl ARG A 313 0.471 13.468 35.521 1.00 36.07 A N
ATOM 1862 NH2 ARG A 313 1.209 14.470 34.321 1.00 29.42 A N
ATOM 1863 C ARG A 313 3.521 9.517 35.064 1.00 16.48 A C
ATOM 1864 O ARG A 313 3.613 8.291 34.990 1.00 16.44 A O
ATOM 1865 N TRP A 314 2.991 10.123 36.094 1.00 15.43 A N
ATOM 1866 CA TRP A 314 2.219 9.330 37.035 1.00 16.51 A C
ATOM 1867 CB TRP A 314 2.046 10.075 38.357 1.00 15.88 A C
ATOM 1868 CG TRP A 314 3.295 10.178 39.137 1.00 18.17 A C
ATOM 1869 CDl TRP A 314 4.262 11.165 39.046 1.00 16.39 A C
ATOM 1870 NEl TRP A 314 5.287 10.880 39.918 1.00 17.39 A N
ATOM 1871 CE2 TRP A 314 5.027 9.692 40.562 1.00 17.32 A C
ATOM 1872 CD2 TRP A 314 3.796 9.201 40.065 1.00 17.71 A C
ATOM 1873 CE3 TRP A 314 3.295 7.988 40.563 1.00 16.40 A C
ATOM 1874 CZ3 TRP A 314 4.055 7.282 41.511 1.00 15.56 A C
ATOM 1875 CH2 TRP A 314 5.261 7.792 41.981 1.00 17.38 A C
ATOM 1876 CZ2 TRP A 314 5.776 8.998 41.525 1.00 16.22 A C
ATOM 1877 C TRP A 314 0.821 9.055 36.468 1.00 16.85 A C
ATOM 1878 O TRP A 314 0.234 9.936 35.818 1.00 16.91 A O
ATOM 1879 N LED A 315 0.302 7.858 36.728 1.00 16.60 A N
ATOM 1880 CA LEU A 315 1.138 7.552 36.521 1.00 17.78 A C
ATOM 1881 CB LEU A 315 1.346 6.521 35.381 1.00 16.61 A C
ATOM 1882 CG LEU A 315 2.774 6.106 34.935 1.00 16.98 A C
ATOM 1883 CDl LEU A 315 3.541 7.295 34.324 1.00 16.18 A C
ATOM 1884 CD2 LEU A 315 2.710 4.983 33.886 1.00 19.04 A C
ATOM 1885 C LEU A 315 1.671 7.035 37.864 1.00 17.31 A C
ATOM 1886 O LEU A 315 1.666 5.818 38.128 1.00 17.12 A O
ATOM 1887 N GLY A 316 2.072 7.951 38.729 1.00 17.35 A N
ATOM 1888 CA GLY A 316 2.337 7.561 40.123 1.00 18.38 A C
ATOM 1889 C GLY A 316 1.058 7.124 40.848 1.00 18.84 A C
ATOM 1890 O GLY A 316 0.116 7.891 40.933 1.00 18.79 A O
ATOM 1891 N ASP A 317 1.027 5.890 41.349 1.00 18.19 A N
ATOM 1892 CA ASP A 317 0.188 5.326 41.946 1.00 18.81 A C
ATOM 1893 CB ASP A 317 0.172 4.392 43.107 1.00 19.38 A C
ATOM 1894 CG ASP A 317 0.884 5.100 44.289 1.00 24.54 A C
ATOM 1895 ODl ASP A 317 0.813 6.346 44.432 1.00 23.82 A O
ATOM 1896 OD2 ASP A 317 1.483 4.360 45.113 1.00 28.15 A O
ATOM 1897 C ASP A 317 1.044 4.515 40.918 1.00 18.66 A C
ATOM 1898 O ASP A 317 2.097 3.996 41.268 1.00 18.92 A O
ATOM 1899 N LEU A 318 0.562 4.364 39.687 1.00 17.28 A N
ATOM 1900 CA LEU A 318 1.309 3.674 38.637 1.00 16.37 A C
ATOM 1901 CB LEU A 318 0.383 2.949 37.664 1.00 15.69 A C
ATOM 1902 CG LEU A 318 0.568 1.919 38.278 1.00 17.36 A C
ATOM 1903 CDl LEU A 318 1.341 1.174 37.180 1.00 18.24 A C
ATOM 1904 CD2 LEU A 318 0.224 0.888 39.115 1.00 19.17 A C
ATOM 1905 C LEU A 318 2.129 4.678 37.858 1.00 15.94 A C
ATOM 1906 O LEU A 318 1.910 5.885 37.973 1.00 15.31 A O
ATOM 1907 N ILE A 319 3.065 4.172 37.061 1.00 16.07 A N
ATOM 1908 CA ILE A 319 3.905 5.012 36.191 1.00 16.62 A C
ATOM 1909 CB ILE A 319 5.437 4.825 36.476 1.00 16.30 A C
ATOM 1910 CGl ILE A 319 5.760 5.092 37.953 1.00 17.10 A C
ATOM 1911 CDl ILE A 319 5.553 6.569 38.284 1.00 15.34 A C
ATOM 1912 CG2 ILE A 319 6.249 5.756 35.566 1.00 15.36 A C
ATOM 1913 C ILE A 319 3.678 4.666 34.714 1.00 17.73 A C
ATOM 1914 O ILE A 319 3.650 3.475 34.358 1.00 17.91 A O
ATOM 1915 N LEU A 320 3.582 5.694 33.871 1.00 16.37 A N
ATOM 1916 CA LEU A 320 3.766 5.513 32.449 1.00 16.94 A C
ATOM 1917 CB LEU A 320 2.624 6.143 31.636 1.00 16.76 A C
ATOM 1918 CG LEU A 320 1.177 5.728 31.859 1.00 19.50 A C
ATOM 1919 CDl LEU A 320 0.338 6.756 31.132 1.00 19.18 A C
ATOM 1920 CD2 LEU A 320 0.915 4.324 31.304 1.00 17.27 A C
ATOM 1921 C LEU A 320 5.086 6.114 31.991 1.00 16.85 A C
ATOM 1922 O LEU A 320 5.348 7.291 32.236 1.00 17.36 A O
ATOM 1923 N SER A 321 5.906 5.323 31.302 1.00 15.73 A N
ATOM 1924 CA SER A 321 7.152 5.840 30.767 1.00 16.09 A C
ATOM 1925 CB SER A 321 8.347 5.647 31.772 1.00 15.22 A C
ATOM 1926 OG SER A 321 8.552 4.271 32.102 1.00 15.33 A O
ATOM 1927 C SER A 321 7.491 5.247 29.411 1.00 16.12 A C ATOM 1928 O SER A 321 7.018 4.162 29.035 1.00 16.22 A O
ATOM 1929 N LYS A 322 8.332 5.956 28.676 1.00 16.63 A N
ATOM 1930 CA LYS A 322 8.794 5.476 27.394 1.00 17.53 A C
ATOM 1931 CB LYS A 322 7.955 6.052 26.198 1.00 17.88 A C
ATOM 1932 CG LYS A 322 7.965 7.588 26.018 1.00 18.29 A C
ATOM 1933 CD LYS A 322 7.304 8.007 24.673 1.00 15.16 A C
ATOM 1934 CE LYS A 322 8.169 7.623 23.426 1.00 14.45 A C
ATOM 1935 NZ LYS A 322 9.468 8.370 23.370 1.00 18.65 A N
ATOM 1936 C LYS A 322 10.289 5.704 27.142 1.00 18.49 A C
ATOM 1937 O LYS A 322 10.926 6.593 27.732 1.00 18.13 A O
ATOM 1938 N SER A 323 10.803 4.884 26.241 1.00 17.96 A N
ATOM 1939 CA SER A 323 12.120 5.030 25.623 1.00 19.50 A C
ATOM 1940 CB SER A 323 12.995 3.805 26.010 1.00 19.88 A C
ATOM 1941 OG SER A 323 14.319 3.870 25.473 1.00 20.47 A O
ATOM 1942 C SER A 323 11.929 5.177 24.093 1.00 19.32 A C
ATOM 1943 O SER A 323 10.819 5.518 23.640 1.00 18.67 A O
ATOM 1944 N CYS A 324 12.982 4.927 23.301 1.00 20.12 A N
ATOM 1945 CA CYS A 324 12.882 4.867 21.823 1.00 20.89 A C
ATOM 1946 CB CYS A 324 14.172 5.421 21.164 1.00 20.76 A C
ATOM 1947 SG CYS A 324 15.683 4.665 21.910 1.00 25.57 A S
ATOM 1948 C CYS A 324 12.667 3.461 21.278 1.00 20.81 A C
ATOM 1949 O CYS A 324 13.036 3.187 20.154 1.00 21.13 A O
ATOM 1950 N GLU A 325 12.061 2.574 22.044 1.00 20.92 A N
ATOM 1951 CA GLO A 325 11.851 1.191 21.599 1.00 21.77 A C
ATOM 1952 CB GLU A 325 12.307 0.207 22.676 1.00 23.17 A C
ATOM 1953 CG GLU A 325 13.777 0.325 23.042 1.00 27.96 A C
ATOM 1954 CD GLU A 325 14.193 -0.665 24.112 1.00 33.66 A C
ATOM 1955 OEl GLU A 325 13.330 -1.444 24.567 1.00 30.97 A O
ATOM 1956 OE2 GLU A 325 15.381 -0.662 24.494 1.00 26.72 A O
ATOM 1957 C GLU A 325 10.382 0.926 21.199 1.00 20.91 A C
ATOM 1958 O GLU A 325 9.921 -0.214 21.253 1.00 21.14 A O
ATOM 1959 N ASN A 326 9.683 1.988 20.765 1.00 19.41 A N
ATOM 1960 CA ASN A 326 8.300 1.977 20.233 1.00 18.77 A C
ATOM 1961 CB ASN A 326 8.295 1.295 18.872 1.00 19.02 A C
ATOM 1962 CG ASN A 326 8.955 2.134 17.802 1.00 22.14 A C
ATOM 1963 ODl ASN A 326 8.767 3.352 17.737 1.00 29.07 A O
ATOM 1964 ND2 ASN A 326 9.749 1.501 16.940 1.00 18.85 A N
ATOM 1965 C ASN A 326 7.315 1.324 21.236 1.00 17.39 A C
ATOM 1966 O ASN A 326 6.566 0.416 20.869 1.00 16.41 A O
ATOM 1967 N ALA A 327 7.324 1.767 22.517 1.00 16.77 A N
ATOM 1968 CA ALA A 327 6.471 1.290 23.632 1.00 16.46 A C
ATOM 1969 CB ALA A 327 6.991 -0.049 24.195 1.00 17.75 A C
ATOM 1970 C ALA A 327 6.365 2.299 24.770 1.00 16.87 A C
ATOM 1971 O ALA A 327 7.376 2.873 25.234 1.00 15.62 A O
ATOM 1972 N ILE A 328 5.133 2.497 25.222 1.00 16.82 A N
ATOM 1973 CA ILE A 328 4.893 3.063 26.557 1.00 16.23 A C
ATOM 1974 CB ILE A 328 3.707 4.058 26.510 1.00 16.61 A C
ATOM 1975 CGl ILE A 328 4.043 5.250 25.566 1.00 15.49 A C
ATOM 1976 CDl ILE A 328 2.819 6.022 25.115 1.00 12.96 A C
ATOM 1977 CG2 ILE A 328 3.357 4.567 27.900 1.00 16.07 A C
ATOM 1978 C ILE A 328 4.679 1.899 27.559 1.00 16.57 A C
ATOM 1979 O ILE A 328 3.801 1.060 27.366 1.00 16.99 A O
ATOM 1980 N VAL A 329 5.523 1.806 28.585 1.00 15.32 A N
ATOM 1981 CA VAL A 329 5.341 0.779 29.622 1.00 14.91 A C
ATOM 1982 CB VAL A 329 6.715 0.232 30.127 1.00 15.50 A C
ATOM 1983 CGl VAL A 329 6.517 -0.866 31.170 1.00 12.97 A C
ATOM 1984 CG2 VAL A 329 7.573 -0.350 28.910 1.00 15.54 A C
ATOM 1985 C VAL A 329 4.534 1.359 30.821 1.00 14.36 A C
ATOM 1986 O VAL A 329 4.863 2.444 31.342 1.00 14.87 A O
ATOM 1987 N CYS A 330 3.503 0.641 31.229 1.00 15.12 A N
ATOM 1988 CA CYS A 330 2.827 0.916 32.481 1.00 15.43 A C
ATOM 1989 CB CYS A 330 1.304 0.820 32.335 1.00 14.59 A C
ATOM 1990 SG CYS A 330 0.391 1.303 33.871 1.00 18.11 A S
ATOM 1991 C CYS A 330 3.360 -0.013 33.601 1.00 16.45 A C
ATOM 1992 O CYS A 330 3.263 -1.243 33.507 1.00 15.68 A O
ATOM 1993 N TRP A 331 3.902 0.577 34.669 1.00 15.78 A N
ATOM 1994 CA TRP A 331 4.601 -0.205 35.706 1.00 16.55 A C
ATOM 1995 CB TRP A 331 6.103 -0.361 35.361 1.00 16.90 A C
ATOM 1996 CG TRP A 331 6.876 0.951 35.347 1.00 18.35 A C
ATOM 1997 CDl TRP A 331 6.959 1.872 34.300 1.00 18.14 A C
ATOM 1998 NEl TRP A 331 7.785 2.921 34.667 1.00 16.16 A N
ATOM 1999 CE2 TRP A 331 8.235 2.707 35.951 1.00 17.59 A C
ATOM 2000 CD2 TRP A 331 7.703 1.484 36.407 1.00 17.73 A C
ATOM 2001 CE3 TRP A 331 8.014 1.053 37.702 1.00 16.31 A C
ATOM 2002 CZ3 TRP A 331 8.863 1.810 38.476 1.00 17.36 A C
ATOM 2003 CH2 TRP A 331 9.366 3.049 38.004 1.00 18.12 A C
ATOM 2004 CZ2 TRP A 331 9.069 3.505 36.757 1.00 18.03 A C ATOM 2005 C TRP A 331 4.461 0.427 37.085 1.00 16.74 A C
ATOM 2006 O TRP A 331 4.083 1.591 37.199 1.00 15.57 A O
ATOM 2007 N LYS A 332 4.845 -0.326 38.120 1.00 17.36 A N
ATOM 2008 CA LYS A 332 4.946 0.220 39.502 1.00 18.06 A C
ATOM 2009 CB LYS A 332 3.672 -0.084 40.340 1.00 16.93 A C
ATOM 2010 CG LYS A 332 3.392 -1.609 40.484 1.00 15.82 A C
ATOM 2011 CD LYS A 332 2.191 -1.930 41.406 1.00 19.08 A C
ATOM 2012 CE LYS A 332 2.562 -1.836 42.893 1.00 19.54 A C
ATOM 2013 NZ LYS A 332 1.324 -1.986 43.669 1.00 22.52 A N
ATOM 2014 C LYS A 332 6.198 -0.292 40.243 1.00 18.16 A C
ATOM 2015 O LYS A 332 6.637 -1.434 40.028 1.00 18.85 A O
ATOM 2016 N PRO A 333 6.776 0.540 41.132 1.00 19.24 A N
ATOM 2017 CA PRO A 333 7.822 0.010 42.034 1.00 18.83 A C
ATOM 2018 CB PRO A 333 8.163 1.214 42.917 1.00 19.27 A C
ATOM 2019 CG PRO A 333 7.775 2.448 42.097 1.00 19.23 A C
ATOM 2020 CD PRO A 333 6.511 1.983 41.369 1.00 18.48 A C
ATOM 2021 C PRO A 333 7.318 -1.138 42.913 1.00 18.33 A C
ATOM 2022 O PRO A 333 6.173 -1.144 43.284 1.00 18.04 A O
ATOM 2023 N GLY A 334 8.181 -2.087 43.259 1.00 19.75 A N
ATOM 2024 CA GLY A 334 7.807 -3.200 44.115 1.00 20.60 A C
ATOM 2025 C GLY A 334 6.987 -4.294 43.411 1.00 23.23 A C
ATOM 2026 O GLY A 334 6.909 -4.358 42.179 1.00 21.41 A O
ATOM 2027 N LYS A 335 6.399 -5.158 44.230 1.00 25.02 A N
ATOM 2028 CA LYS A 335 5.635 -6.315 43.792 1.00 28.57 A C
ATOM 2029 CB LYS A 335 5.787 -7.474 44.800 1.00 27.78 A C
ATOM 2030 CG LYS A 335 7.062 -8.267 44.594 1.00 31.82 A C
ATOM 2031 CD LYS A 335 7.177 -9.498 45.534 1.00 32.30 A C
ATOM 2032 CE LYS A 335 8.543 -10.169 45.377 1.00 38.16 A C
ATOM 2033 NZ LYS A 335 8.865 -10.389 43.915 1.00 40.37 A N
ATOM 2034 C LYS A 335 4.179 -5.890 43.648 1.00 28.47 A C
ATOM 2035 O LYS A 335 3.813 -4.801 44.092 1.00 28.86 A O
ATOM 2036 N MET A 336 3.357 -6.740 43.034 1.00 29.92 A N
ATOM 2037 CA MET A 336 2.018 -6.342 42.563 1.00 31.76 A C
ATOM 2038 CB MET A 336 1.262 -7.563 42.005 1.00 32.50 A C
ATOM 2039 CG MET A 336 0.172 -7.287 41.526 1.00 34.89 A C
ATOM 2040 SD MET A 336 0.170 -6.157 40.110 1.00 37.65 A S
ATOM 2041 CE MET A 336 1.929 -5.808 39.881 1.00 38.26 A C
ATOM 2042 C MET A 336 1.170 -5.686 43.660 1.00 32.43 A C
ATOM 2043 O MET A 336 0.322 -4.813 43.405 1.00 31.95 A O
ATOM 2044 N GLU A 337 1.384 -6.144 44.878 1.00 32.23 A N
ATOM 2045 CA GLU A 337 0.537 -5.745 45.973 1.00 33.18 A C
ATOM 2046 CB GLU A 337 0.204 -6.997 46.799 1.00 34.38 A C
ATOM 2047 CG GLU A 337 1.416 -7.600 47.597 1.00 38.18 A C
ATOM 2048 CD GLU A 337 2.402 -8.481 46.773 1.00 43.86 A C
ATOM 2049 OEl GLU A 337 2.162 -8.767 45.560 1.00 42.25 A O
ATOM 2050 OE2 GLU A 337 3.435 -8.899 47.376 1.00 46.44 A O
ATOM 2051 C GLU A 337 1.152 -4.636 46.867 1.00 32.38 A C
ATOM 2052 O GLU A 337 0.531 -4.248 47.853 1.00 32.28 A O
ATOM 2053 N ASP A 338 2.359 -4.153 46.539 1.00 31.41 A N
ATOM 2054 CA ASP A 338 3.050 -3.142 47.360 1.00 30.51 A C
ATOM 2055 CB ASP A 338 4.561 -3.136 47.069 1.00 29.97 A C
ATOM 2056 CG ASP A 338 5.271 -4.433 47.501 1.00 30.11 A C
ATOM 2057 ODl ASP A 338 4.718 -5.211 48.318 1.00 34.26 A O
ATOM 2058 OD2 ASP A 338 6.380 -4.676 47.008 1.00 25.73 A O
ATOM 2059 C ASP A 338 2.487 -1.714 47.188 1.00 30.79 A C
ATOM 2060 O ASP A 338 2.401 -1.200 46.053 1.00 30.15 A O
ATOM 2061 N ASP A 339 2.130 -1.073 48.309 1.00 30.48 A N
ATOM 2062 CA ASP A 339 1.720 0.343 48.317 1.00 31.02 A C
ATOM 2063 CB ASP A 339 1.085 0.749 49.662 1.00 32.36 A C
ATOM 2064 CG ASP A 339 0.456 2.160 49.621 1.00 37.37 A C
ATOM 2065 ODl ASP A 339 0.381 2.449 48.729 1.00 44.52 A O
ATOM 2066 OD2 ASP A 339 0.794 3.001 50.468 1.00 41.19 A O
ATOM 2067 C ASP A 339 2.935 1.236 48.014 1.00 29.39 A C
ATOM 2068 O ASP A 339 4.024 1.024 48.564 1.00 27.83 A O
ATOM 2069 N ILE A 340 2.734 2.215 47.123 1.00 29.03 A N
ATOM 2070 CA ILE A 340 3.791 3.160 46.715 1.00 28.26 A C
ATOM 2071 CB ILE A 340 3.275 4.197 45.630 1.00 28.01 A C
ATOM 2072 CGl ILE A 340 4.424 5.038 45.087 1.00 27.48 A C
ATOM 2073 CDl ILE A 340 5.366 4.295 44.227 1.00 27.16 A C
ATOM 2074 CG2 ILE A 340 2.109 5.089 46.149 1.00 25.78 A C
ATOM 2075 C ILE A 340 4.470 3.859 47.923 1.00 28.59 A C
ATOM 2076 O ILE A 340 5.687 4.077 47.924 1.00 28.97 A O
ATOM 2077 N ASP A 341 3.687 4.166 48.952 1.00 28.63 A N
ATOM 2078 CA ASP A 341 4.207 4.893 50.112 1.00 29.97 A C
ATOM 2079 CB ASP A 341 3.111 5.741 50.728 1.00 30.32 A C
ATOM 2080 CG ASP A 341 2.797 6.968 49.885 1.00 32.09 A C
ATOM 2081 ODl ASP A 341 3.679 7.435 49.115 1.00 33.76 A O ATOM 2082 OD2 ASP A 341 1.665 7.458 49.979 1.00 34.02 A O
ATOM 2083 C ASP A 341 4.950 4.045 51.159 1.00 30.34 A C
ATOM 2084 O ASP A 341 5.529 4.581 52.097' 1.00 29.60 A O
ATOM 2085 N LYS A 342 4.956 2.726 50.953 1.00 31.22 A N
ATOM 2086 CA LYS A 342 5.726 1.796 51.781 1.00 33.07 A C
ATOM 2087 CB LYS A 342 4.872 0.612 52.246 1.00 33.30 A C
ATOM 2088 CG LYS A 342 3.756 0.966 53.238 1.00 36.15 A C
ATOM 2089 CD LYS A 342 2.960 -0.318 53.620 1.00 36.50 A C
ATOM 2090 CE LYS A 342 1.582 0.021 54.187 1.00 42.07 A C
ATOM 2091 NZ LYS A 342 0.948 1.166 53.428 1.00 43.50 A N
ATOM 2092 C LYS A 342 6.980 1.294 51.073 1.00 32.25 A C
ATOM 2093 O LYS A 342 7.800 0.570 51.685 1.00 32.30 A O
ATOM 2094 N ILE A 343 7.138 1.682 49.800 1.00 30.86 A N
ATOM 2095 CA ILE A 343 8.374 1.426 49.047 1.00 30.22 A C
ATOM 2096 CB ILE A 343 8.243 1.903 47.541 1.00 29.89 A C
ATOM 2097 CGl ILE A 343 7.100 1.173 46.822 1.00 27.59 A C
ATOM 2098 CDl ILE A 343 7.378 -0.336 46.614 1.00 23.56 A C
ATOM 2099 CG2 ILE A 343 9.550 1.704 46.783 1.00 27.32 A C
ATOM 2100 C ILE A 343 9.602 2.110 49.708 1.00 31.03 A C
ATOM 2101 O ILE A 343 9.577 3.317 49.944 1.00 30.04 A O
ATOM 2102 N LYS A 344 10.667 1.338 49.972 1.00 31.09 A N
ATOM 2103 CA LYS A 344 11.940 1.865 50.538 1.00 32.49 A C
ATOM 2104 CB LYS A 344 12.412 0.921 51.646 1.00 32.41 A C
ATOM 2105 CG LYS A 344 11.333 0.683 52.731 1.00 34.24 A C
ATOM 2106 CD LYS A 344 11.830 -0.339 53.781 1.00 35.86 A C
ATOM 2107 CE LYS A 344 11.279 -0.029 55.201 1.00 42.71 A C
ATOM 2108 NZ LYS A 344 12.067 , 1.067 55.928 1.00 45.29 A N
ATOM 2109 C LYS A 344 13.025 2.016 49.452 1.00 31.19 A C
ATOM 2110 O LYS A 344 12.909 1.371 48.412 1.00 31.60 A O
ATOM 2111 N PRO A 345 14.085 2.850 49.672 1.00 30.89 A N
ATOM 2112 CA PRO A 345 15.134 3.058 48.650 1.00 29.97 A C
ATOM 2113 CB PRO A 345 16.147 3.969 49.378 1.00 30.71 A C
ATOM 2114 CG PRO A 345 15.366 4.647 50.386 1.00 30.80 A C
ATOM 2115 CD PRO A 345 14.369 3.673 50.872 1.00 31.12 A C
ATOM 2116 C PRO A 345 15.862 1.811 48.160 1.00 29.79 A C
ATOM 2117 O PRO A 345 16.454 1.826 47.070 1.00 28.84 A O
ATOM 2118 N SER A 346 15.854 0.749 48.968 1.00 29.68 A N
ATOM 2119 CA SER A 346 16.542 -0.501 48.611 1.00 31.19 A C
ATOM 2120 CB SER A 346 16.998 -1.265 49.882 1.00 31.96 A C
ATOM 2121 OG SER A 346 15.985 -1.314 50.892 1.00 33.66 A O
ATOM 2122 C SER A 346 15.705 -1.437 47.699 1.00 30.84 A C
ATOM 2123 O SER A 346 16.193 -2.503 47.294 1.00 31.49 A O
ATOM 2124 N GLU A 347 14.470 -1.038 47.390 1.00 30.07 A N
ATOM 2125 CA GLU A 347 13.545 -1.882 46.613 1.00 29.69 A C
ATOM 2126 CB GLO A 347 12.218 -1.167 46.350 1.00 29.26 A C
ATOM 2127 CG GLϋ A 347 11.187 -2.016 45.585 1.00 29.17 A C
ATOM 2128 CD GLU A 347 10.824 -3.331 46.290 1.00 30.57 A C
ATOM 2129 OEl GLU A 347 10.336 -3.325 47.434 1.00 31.39 A O
ATOM 2130 OE2 GLU A 347 10.995 -4.384 45.680 1.00 32.23 A O
ATOM 2131 C GLU A 347 14.201 -2.330 45.321 1.00 28.50 A C
ATOM 2132 O GLU A 347 14.648 -1.505 44.537 1.00 28.41 O
ATOM 2133 N SER A 348 14.297 -3.647 45.149 1.00 28.65 A N
ATOM 2134 CA SER A 348 14.892 -4.257 43.966 1.00 29.38 A C
ATOM 2135 CB SER A 348 15.696 -5.501 44.367 1.00 30.06 A C
ATOM 2136 OG SER A 348 16.926 -5.097 44.921 1.00 34.01 A O
ATOM 2137 C SER A 348 13.868 -4.678 42.905 1.00 28.02 A C
ATOM 2138 O SER A 348 14.250 -5.009 41.789 1.00 27.73 A O
ATOM 2139 N ASN A 349 12.594 -4.708 43.270 1.00 26.88 A N
ATOM 2140 CA ASN A 349 11.563 -5.189 42.334 1.00 26.82 A C
ATOM 2141 CB ASN A 349 10.624 -6.211 42.982 1.00 27.06 A C
ATOM 2142 CG ASN A 349 11.365 -7.479 43.467 1.00 32.97 A C
ATOM 2143 ODl ASN A 349 11.191 -7.900 44.630 1.00 37.38 A O
ATOM 2144 ND2 ASN A 349 12.216 -8.066 42.592 1.00 32.63 A N
ATOM 2145 C ASN A 349 10.735 -4.098 41.680 1.00 24.90 A C
ATOM 2146 O ASN A 349 10.466 -3.060 42.299 1.00 25.27 A O
ATOM 2147 N VAL A 350 10.321 -4.365 40.440 1.00 23.83 A N
ATOM 2148 CA VAL A 350 9.270 -3.589 39/751 1.00 22.32 A C
ATOM 2149 CB VAL A 350 9.814 -2.729 38.567 1.00 21.15 A C
ATOM 2150 CGl VAL A 350 10.674 -1.598 39.077 1.00 21.45 A C
ATOM 2151 CG2 VAL A 350 10.558 -3.573 37.491 1.00 22.51 A C
ATOM 2152 C VAL A 350 8.178 -4.545 39.248 1.00 22.65 A C
ATOM 2153 O VAL A 350 8.419 -5.767 39.173 1.00 22.74 A O
ATOM 2154 N THR A 351 7.005 -4.007 38.886 1.00 21.00 A N
ATOM 2155 CA THR A 351 5.915 -4.822 38.338 1.00 22.44 A C
ATOM 2156 CB THR A 351 4.744 -4.980 39.321 1.00 21.82 A C
ATOM 2157 OGl THR A 351 5.205 -5.672 40.490 1.00 26.59 A O
ATOM 2158 CG2 THR A 351 3.614 -5.798 38.711 1.00 23.30 A C ATOM 2159 C THR A 351 5.391 -4.188 37.049 1.00 22.20 A C
ATOM 2160 O THR A 351 5.012 -3.013 37.064 1.00 23.19 A O
ATOM 2161 N ILE A 352 5.375 -4.958 35.967 1.00 20.57 A N
ATOM 2162 CA ILE A 352 4.830 -4.482 34.670 1.00 20.82 A C
ATOM 2163 CB ILE A 352 5.635 -5.107 33.442 1.00 21.27 A C
ATOM 2164 CGl ILE A 352 7.158 -4.963 33.644 1.00 21.29 A C
ATOM 2165 CDl ILE A 352 7.602 -3.590 33.839 1.00 23.57 A C
ATOM 2166 CG2 ILE A 352 5.180 -4.523 32.072 1.00 18.98 A C
ATOM 2167 C ILE A 352 3.344 -4.783 34.549 1.00 20.69 A C
ATOM 2168 O ILE A 352 2.932 -5.939 34.644 1.00 19.27 A O
ATOM 2169 N LEO A 353 2.534 -3.740 34.348 1.00 21.20 A N
ATOM 2170 CA LEU A 353 1.082 -3.924 34.258 1.00 21.91 A C
ATOM 2171 CB LED A 353 0.313 -2.939 35.153 1.00 21.70 A C
ATOM 2172 CG LED A 353 0.246 -3.413 36.627 1.00 26.87 A C
ATOM 2173 CDl LEO A 353 1.236 -2.600 37.470 1.00 28.53 A C
ATOM 2174 CD2 LEO A 353 1.175 -3.266 37.161 1.00 31.42 A C
ATOM 2175 C LEO A 353 0.543 -3.908 32.828 1.00 20.78 A C
ATOM 2176 O LEO A 353 0.603 -4.290 32.594 1.00 22.31 A O
ATOM 2177 N GLY A 354 1.380 -3.482 31.887 1.00 19.12 A N
ATOM 2178 CA GLY A 354 0.965 -3.353 30.515 1.00 18.16 A C
ATOM 2179 C GLY A 354 2.035 -2.682 29.680 1.00 17.04 A C
ATOM 2180 O GLY A 354 2.987 -2.084 30.189 1.00 15.91 A O
ATOM 2181 N ARG A 355 1.853 -2.765 28.371 1.00 15.76 A N
ATOM 2182 CA ARG A 355 2.749 -2.103 27.429 1.00 15.21 A C
ATOM 2183 CB ARG A 355 3.944 -2.984 27.048 1.00 14.11 A C
ATOM 2184 CG ARG A 355 5.124 -2.134 26.538 1.00 15.07 A C
ATOM 2185 CD ARG A 355 6.321 -2.968 26.122 1.00 17.88 A C
ATOM 2186 NE ARG A 355 6.082 -3.654 24.843 1.00 18.55 A N
ATOM 2187 CZ ARG A 355 6.680 -4.797 24.522 1.00 19.02 A C
ATOM 2188 NHl ARG A 355 7.502 -5.370 25.419 1.00 13.87 A N
ATOM 2189 NH2 ARG A 355 6.442 -5.377 23.344 1.00 15.90 A N
ATOM 2190 C ARG A 355 1.954 -1.742 26.210 1.00 14.72 A C
ATOM 2191 O ARG A 355 1.245 -2.596 25.666 1.00 15.27 A O
ATOM 2192 N PHE A 356 2.026 -0.477 25.815 1.00 14.25 A N
ATOM 2193 CA PHE A 356 1.315 0.021 24.641 1.00 14.09 A C
ATOM 2194 CB PHE A 356 0.681 1.379 24.948 1.00 13.66 A C
ATOM 2195 CG PHE A 356 0.196 1.397 26.168 1.00 15.21 A C
ATOM 2196 CDl PHE A 356 1.011 0.290 26.505 1.00 15.03 A C
ATOM 2197 CEl PHE A 356 1.867 0.334 27.637 1.00 14.77 A C
ATOM 2198 CZ PHE A 356 1.892 1.512 28.452 1.00 14.75 A C
ATOM 2199 CE2 PHE A 356 1.101 2.602 28.116 1.00 18.38 A C
ATOM 2200 CD2 PHE A 356 0.252 2.546 26.956 1.00 16.45 A C
ATOM 2201 C PHE A 356 2.308 0.211 23.494 1.00 15.42 A C
ATOM 2202 O PHE A 356 3.116 1.134 23.534 1.00 15.86 A O
ATOM 2203 N ASP A 357 2.275 -0.699 22.512 1.00 14.84 A N
ATOM 2204 CA ASP A 357 3.182 -0.632 21.360 1.00 16.13 A C
ATOM 2205 CB ASP A 357 3.511 -2.039 20.854 1.00 15.82 A C
ATOM 2206 CG ASP A 357 4.339 -2.842 21.866 1.00 20.24 A C
ATOM 2207 ODl ASP A 357 4.857 -2.240 22.818 1.00 19.19 A O
ATOM 2208 OD2 ASP A 357 4.468 -4.063 21.736 1.00 22.53 A O
ATOM 2209 C ASP A 357 2.608 0.259 20.223 1.00 14.74 A C
ATOM 2210 O ASP A 357 1.403 0.494 20.128 1.00 14.87 A O
ATOM 2211 N TYR A 358 3.518 0.754 19.393 1.00 15.21 A N
ATOM 2212 CA TYR A 358 3.201 1.601 18.265 1.00 15.47 A C
ATOM 2213 CB TYR A 358 2.928 3.050 18.717 1.00 15.29 A C
ATOM 2214 CG TYR A 358 3.945 3.541 19.744 1.00 15.56 A C
ATOM 2215 CDl TYR A 358 5.141 4.135 19.353 1.00 16.04 A C
ATOM 2216 CEl TYR A 358 6.068 4.603 20.300 1.00 17.64 A C
ATOM 2217 CZ TYR A 358 5.803 4.451 21.650 1.00 16.93 A C
ATOM 2218 OH TYR A 358 6.717 4.903 22.584 1.00 15.77 A O
ATOM 2219 CE2 TYR A 358 4.616 3.889 22.053 1.00 15.98 A C
ATOM 2220 CD2 TYR A 358 3.689 3.429 21.091 1.00 15.77 A C
ATOM 2221 C TYR A 358 4.410 1.508 17.315 1.00 16.10 A C
ATOM 2222 O TYR A 358 5.286 0.667 17.510 1.00 16.56 A O
ATOM 2223 N SER A 359 4.434 2.334 16.281 1.00 16.76 A N
ATOM 2224 CA SER A 359 5.461 2.196 15.242 1.00 17.76 A C
ATOM 2225 CB SER A 359 4.842 1.717 13.902 1.00 17.90 A C
ATOM 2226 OG SER A 359 4.309 0.414 14.077 1.00 20.98 A O
ATOM 2227 C SER A 359 6.184 3.464 15.011 1.00 17.61 A C
ATOM 2228 O SER A 359 5.597 4.548 15.202 1.00 15.35 A O
ATOM 2229 N GLN A 360 7.449 3.312 14.547 1.00 19.02 A N
ATOM 2230 CA GLN A 360 8.226 4.392 13.884 1.00 20.58 A C
ATOM 2231 CB GLN A 360 7.617 4.773 12.505 1.00 20.39 A C
ATOM 2232 CG GLN A 360 7.750 3.650 11.422 1.00 22.08 A C
ATOM 2233 CD GLN A 360 6.938 3.973 10.200 1.00 22.80 A C
ATOM 2234 OEl GLN A 360 5.720 3.880 10.205 1.00 25.47 A O
ATOM 2235 NE2 GLN A 360 7.615 4.438 9.157 1.00 25.26 A N ATOM 2236 C GLN A 360 8.396 5.625 14.804 1.00 21.38 A C
ATOM 2237 O GLN A 360 8.096 6.793 14.425 1.00 19.16 A O
ATOM 2238 N CYS A 361 8.935 5.348 15.996 1.00 21.40 A N
ATOM 2239 CA CYS A 361 9.155 6.373 17.006 1.00 22.47 A C
ATOM 2240 CB CYS A 361 7.906 6.527 17.908 1.00 22.30 A C
ATOM 2241 SG CYS A 361 8.013 7.956 19.009 1.00 23.13 A S
ATOM 2242 C CYS A 361 10.393 5.970 17.814 1.00 23.11 A C
ATOM 2243 O CYS A 361 10.330 5.707 19.051 1.00 22.95 A O
ATOM 2244 N ASP A 362 11.518 5.900 17.098 1.00 24.54 A N
ATOM 2245 CA ASP A 362 12.788 5.453 17.673 1.00 25.77 A C
ATOM 2246 CB ASP A 362 13.282 4.206 16.935 1.00 28.31 A C
ATOM 2247 CG ASP A 362 13.330 4.410 15.427 1.00 32.17 A C
ATOM 2248 ODl ASP A 362 14.037 5.343 14.994 1.00 35.23 A O
ATOM 2249 OD2 ASP A 362 12.642 3.658 14.685 1.00 38.45 A O
ATOM 2250 C ASP A 362 13.856 6.548 17.691 1.00 25.40 A C
ATOM 2251 O ASP A 362 15.018 6.314 18.066 1.00 24.31 A O
ATOM 2252 N ILE A 363 13.465 7.762 17.320 1.00 24.56 A N
ATOM 2253 CA ILE A 363 14.302 8.929 17.654 1.00 23.83 A C
ATOM 2254 CB ILE A 363 14.138 10.057 16.599 1.00 23.53 A C
ATOM 2255 CGl ILE A 363 12.685 10.543 16.532 1.00 22.60 A C
ATOM 2256 CDl ILE A 363 12.529 11.921 15.844 1.00 23.73 A C
ATOM 2257 CG2 ILE A 363 14.680 9.605 15.223 1.00 24.61 A C
ATOM 2258 C ILE A 363 13.968 9.386 19.096 1.00 23.44 A C
ATOM 2259 O ILE A 363 12.903 9.064 19.606 1.00 23.32 A O
ATOM 2260 N TRP A 364 14.875 10.079 19.777 1.00 22.99 A N
ATOM 2261 CA TRP A 364 14.615 10.426 21.169 1.00 23.16 A C
ATOM 2262 CB TRP A 364 15.810 10.146 22.114 1.00 25.34 A C
ATOM 2263 CG TRP A 364 17.060 10.958 21.896 1.00 28.80 A C
ATOM 2264 CDl TRP A 364 18.026 10.739 20.949 1.00 31.59 A C
ATOM 2265 NEl TRP A 364 19.022 11.676 21.064 1.00 32.31 A N
ATOM 2266 CE2 TRP A 364 18.733 12.519 22.108 1.00 31.38 A C
ATOM 2267 CD2 TRP A 364 17.506 12.098 22.663 1.00 31.03 A C
ATOM 2268 CE3 TRP A 364 16.984 12.797 23.760 1.00 30.42 A C
ATOM 2269 CZ3 TRP A 364 17.706 13.890 24.263 1.00 31.04 A C
ATOM 2270 CH2 TRP A 364 18.917 14.291 23.678 1.00 30.15 A C
ATOM 2271 CZ2 TRP A 364 19.449 13.619 22.607 1.00 30.88 A C
ATOM 2272 C TRP A 364 14.067 11.848 21.319 1.00 20.68 A C
ATOM 2273 O TRP A 364 14.113 12.640 20.369 1.00 20.06 A O
ATOM 2274 N TYR A 365 13.521 12.113 22.500 1.00 18.67 A N
ATOM 2275 CA TYR A 365 12.752 13.348 22.840 1.00 17.47 A C
ATOM 2276 CB TYR A 365 13.615 14.596 22.691 1.00 16.68 A C
ATOM 2277 CG TYR A 365 13.210 15.801 23.559 1.00 17.72 A C
ATOM 2278 CDl TYR A 365 13.464 15.816 24.941 1.00 17.31 A C
ATOM 2279 CEl TYR A 365 13.102 16.933 25.746 1.00 17.62 A C
ATOM 2280 CZ TYR A 365 12.537 18.037 25.143 1.00 16.73 A C
ATOM 2281 OH TYR A 365 12.196 19.138 25.902 1.00 17.89 A O
ATOM 2282 CE2 TYR A 365 12.317 18.055 23.754 1.00 16.21 A C
ATOM 2283 CD2 TYR A 365 12.636 16.945 22.979 1.00 15.89 A C
ATOM 2284 C TYR A 365 11.421 13.421 22.013 1.00 17.43 A C
ATOM 2285 O TYR A 365 11.195 14.333 21.199 1.00 16.80 A O
ATOM 2286 N MET A 366 10.569 12.417 22.255 1.00 16.42 A N
ATOM 2287 CA MET A 366 9.253 12.286 21.625 1.00 15.72 A C
ATOM 2288 CB MET A 366 9.220 11.092 20.631 1.00 16.16 A C
ATOM 2289 CG MET A 366 10.237 11.228 19.439 1.00 17.19 A C
ATOM 2290 SD MET A 366 9.687 12.524 18.257 1.00 17.60 A S
ATOM 2291 CE MET A 366 8.520 11.548 17.289 1.00 16.78 A C
ATOM 2292 C MET A 366 8.318 12.099 22.817 1.00 15.01 A C
ATOM 2293 O MET A 366 8.342 11.075 23.482 1.00 14.42 A O
ATOM 2294 N ARG A 367 7.504 13.115 23.107 1.00 13.53 A N
ATOM 2295 CA ARG A 367 6.806 13.151 24.394 1.00 14.62 A C
ATOM 2296 CB ARG A 367 7.068 14.522 25.082 1.00 14.58 A C
ATOM 2297 CG ARG A 367 8.523 14.728 25.496 1.00 16.39 A C
ATOM 2298 CD ARG A 367 8.747 16.161 26.137 1.00 17.15 A C
ATOM 2299 NE ARG A 367 8.899 17.249 25.160 1.00 18.82 A N
ATOM 2300 CZ ARG A 367 9.008 18.558 25.474 1.00 20.84 A C
ATOM 2301 NHl ARG A 367 8.977 18.970 26.740 1.00 19.01 A N
ATOM 2302 NH2 ARG A 367 9.111 19.481 24.507 1.00 20.76 A N
ATOM 2303 C ARG A 367 5.318 12.832 24.266 1.00 14.16 A C
ATOM 2304 O ARG A 367 4.640 13.319 23.379 1.00 14.88 A O
ATOM 2305 N PHE A 368 4.817 11.956 25.104 1.00 14.35 A N
ATOM 2306 CA PHE A 368 3.398 11.740 25.168 1.00 13.58 A C
ATOM 2307 CB PHE A 368 3.097 10.263 25.521 1.00 13.40 A C
ATOM 2308 CG PHE A 368 3.630 9.788 26.898 1.00 15.40 A C
ATOM 2309 CDl PHE A 368 2.988 10.161 28.091 1.00 15.87 A C
ATOM 2310 CEl PHE A 368 3.431 9.691 29.330 1.00 17.27 A C
ATOM 2311 CZ PHE A 368 4.545 8.880 29.422 1.00 14.09 A C
ATOM 2312 CE2 PHE A 368 5.204 8.489 28.236 1.00 19.12 A C ATOM 2313 CD2 PHE A 368 4.731 8.923 26.988 1.00 15.09 A C
ATOM 2314 C PHE A 368 2.740 12.759 26.135 1.00 13.91 A C
ATOM 2315 O PHE A 368 3.414 13.418 26.960 1.00 12.66 A O
ATOM 2316 N SER A 369 1.421 12.899 26.036 1.00 14.07 A N
ATOM 2317 CA SER A 369 0.693 13.755 26.982 1.00 15.59 A C
ATOM 2318 CB SER A 369 0.512 15.148 26.342 1.00 14.12 A C
ATOM 2319 OG SER A 369 -0.668 15.164 25.500 1.00 20.44 A O
ATOM 2320 C SER A 369 -0.637 13.102 27.377 1.00 15.61 A C
ATOM 2321 O SER A 369 -1.095 12.186 26.713 1.00 16.33 A O
ATOM 2322 N THR A 370 -1.264 13.551 28.470 1.00 16.90 A N
ATOM 2323 CA THR A 370 -2.628 13.115 28.820 1.00 16.09 A C
ATOM 2324 CB THR A 370 -2.728 12.476 30.233 1.00 16.07 A C
ATOM 2325 OGl THR A 370 -2.204 13.401 31.193 1.00 19.74 A O
ATOM 2326 CG2 THR A 370 -1.959 11.084 30.317 1.00 15.61 A C
ATOM 2327 C THR A 370 -3.530 14.320 28.837 1.00 16.70 A C
ATOM 2328 O THR A 370 -3.047 15.420 28.996 1.00 17.47 A O
ATOM 2329 N ASP A 371 -4.828 14.101 28.730 1.00 15.48 A N
ATOM 2330 CA ASP A 371 -5.838 15.172 28.954 1.00 16.87 A C
ATOM 2331 CB ASP A 371 -7.199 14.682 28.493 1.00 16.55 A C
ATOM 2332 CG ASP A 371 -7.685 13.519 29.333 1.00 19.11 A C
ATOM 2333 ODl ASP A 371 -6.924 12.563 29.561 1.00 19.58 A O
ATOM 2334 OD2 ASP A 371 -8.782 13.587 29.852 1.00 23.45 A O
ATOM 2335 C ASP A 371 -5.890 15.522 30.464 1.00 15.47 A C
ATOM 2336 O ASP A 371 -5.172 14.920 31.282 1.00 13.79 A O
ATOM 2337 N PHE A 372 -6.698 16.532 30.800 1.00 15.85 A N
ATOM 2338 CA PHE A 372 -6.826 17.058 32.166 1.00 16.96 A C
ATOM 2339 CB PHE A 372 -7.799 18.250 32.235 1.00 17.91 A C
ATOM 2340 CG PHE A 372 -8.121 18.692 33.650 1.00 19.80 A C
ATOM 2341 CDl PHE A 372 -7.396 19.715 34.250 1.00 20.60 A C
ATOM 2342 CEl PHE A 372 -7.683 20.122 35.579 1.00 21.90 A C
ATOM 2343 CZ PHE A 372 -8.689 19.479 36.312 1.00 20.54 A C
ATOM 2344 CE2 PHE A 372 -9.419 18.440 35.734 1.00 20.32 A C
ATOM 2345 CD2 PHE A 372 -9.132 18.059 34.388 1.00 18.88 A C
ATOM 2346 C PHE A 372 -7.248 15.959 33.143 1.00 15.88 A C
ATOM 2347 O PHE A 372 -6.639 15.824 34.209 1.00 16.02 A O
ATOM 2348 N TRP A 373 -8.218 15.135 32.737 1.00 15.84 A N
ATOM 2349 CA TRP A 373 -8.788 14.098 33.625 1.00 16.38 A C
ATOM 2350 CB TRP A 373 10.243 13.811 33.238 1.00 16.55 A C
ATOM 2351 CG TRP A 373 11.109 15.008 33.441 1.00 19.67 A C
ATOM 2352 CDl TRP A 373 11.583 15.895 32.485 1.00 21.70 A C
ATOM 2353 NEl TRP A 373 12.317 16.905 33.109 1.00 18.94 A N
ATOM 2354 CE2 TRP A 373 12.308 16.688 34.468 1.00 21.71 A C
ATOM 2355 CD2 TRP A 373 11.560 15.504 34.714 1.00 18.88 A C
ATOM 2356 CE3 TRP A 373 11.397 15.059 36.034 1.00 19.46 A C
ATOM 2357 CZ3 TRP A 373 12.003 15.789 37.070 1.00 20.06 A C
ATOM 2358 CH2 TRP, A 373 12.744 16.959 36.796 1.00 20.95 A C
ATOM 2359 CZ2 TRP A 373 12.914 17.426 35.513 1.00 21.14 A C
ATOM 2360 C TRP A 373 -7.988 12.804 33.637 1.00 15.39 A C
ATOM 2361 O TRP A 373 -8.234 11.911 34.463 1.00 16.15 A O
ATOM 2362 N GLN A 374 -7.023 12.707 32.731 1.00 15.42 A N
ATOM 2363 CA GLN A 374 -6.265 11.430 32.512 1.00 15.10 A C
ATOM 2364 CB GLN A 374 -5.359 11.045 33.667 1.00 13.37 A C
ATOM 2365 CG GLN A 374 -4.408 12.133 34.132 1.00 15.13 A C
ATOM 2366 CD GLN A 374 -3.320 11.475 35.019 1.00 19.60 A C
ATOM 2367 OEl GLN A 374 -2.141 11.412 34.653 1.00 21.89 A O
ATOM 2368 NE2 GLN A 374 -3.703 11.098 36.223 1.00 19.79 A N
ATOM 2369 C GLN A 374 -7.129 10.260 32.090 1.00 15.46 A C
ATOM 2370 O GLN A 374 -6.827 9.080 32.406 1.00 17.05 A O
ATOM 2371 N LYS A 375 -8.140 10.580 31.294 1.00 16.03 A N
ATOM 2372 CA LYS A 375 -8.896 9.584 30.556 1.00 17.04 A C
ATOM 2373 CB LYS A 375 10.256 10.144 30.165 1.00 17.17 A C
ATOM 2374 CG LYS A 375 11.126 10.553 31.347 1.00 19.65 A C
ATOM 2375 CD LYS A 375 12.327 11.307 30.794 1.00 22.22 A C
ATOM 2376 CE LYS A 375 13.284 11.673 31.929 1.00 27.03 A C
ATOM 2377 NZ LYS A 375 14.267 12.574 31.330 1.00 28.46 A N
ATOM 2378 C LYS A 375 -8.209 9.161 29.253 1.00 17.81 A C
ATOM 2379 O LYS A 375 -8.481 8.079 28.725 1.00 16.74 A O
ATOM 2380 N MET A 376 -7.361 10.033 28.714 1.00 18.65 A N
ATOM 2381 CA MET A 376 -6.726 9.731 27.452 1.00 20.07 A C
ATOM 2382 CB MET A 376 -7.611 10.'122 26.252 1.00 20.71 A C
ATOM 2383 CG MET A 376 -7.620 11.471 25.719 1.00 23.76 A C
ATOM 2384 SD MET A 376 -9.158 11.684 24.732 1.00 25.70 A S
ATOM 2385 CE MET A 376 -9.844 12.980 25.706 1.00 25.61 A C
ATOM 2386 C MET A 376 -5.242 10.107 27.368 1.00 19.19 A C
ATOM 2387 O MET A 376 -4.762 10.952 28.119 1.00 17.50 A O
ATOM 2388 N LEU A 377 -4.528 9.367 26.523 1.00 17.55 A N
ATOM 2389 CA LED A 377 -3.075 9.395 26.388 1.00 17.02 A C ATOM 2390 CB LEU A 377 -2.478 8.075 26.969 1.00 17.62 A C
ATOM 2391 CG LEU A 377 -1.016 7.654 26.758 1.00 18.19 A C
ATOM 2392 CDl LEU A 377 -0.110 8.676 27.359 1.00 20.40 A C
ATOM 2393 CD2 LEU A 377 -0.688 6.222 27.359 1.00 15.88 A C
ATOM 2394 C LEU A 377 -2.770 9.552 24.872 1.00 15.93 A C
ATOM 2395 O LEU A 377 -3.295 8.803 24.045 1.00 15.16 A O
ATOM 2396 N ALA A 378 -1.974 10.556 24.507 1.00 16.09 A N
ATOM 2397 CA ALA A 378 -1.691 10.875 23.090 1.00 15.10 A C
ATOM 2398 CB ALA A 378 -2.301 12.218 22.719 1.00 15.22 A C
ATOM 2399 C ALA A 378 -0.166 10.920 22.857 1.00 16.06 A C
ATOM 2400 O ALA A 378 0.539 11.576 23.618 1.00 15.03 A O
ATOM 2401 N LEO A 379 0.298 10.258 21.785 1.00 15.00 A N
ATOM 2402 CA LEU A 379 1.686 10.280 21.326 1.00 15.20 A C
ATOM 2403 CB LEU A 379 2.411 8.983 21.793 1.00 14.36 A C
ATOM 2404 CG LED A 379 3.859 8.854 21.289 1.00 14.81 A C
ATOM 2405 CDl LEO A 379 4.783 10.006 21.789 1.00 13.92 A C
ATOM 2406 CD2 LEO A 379 4.437 7.534 21.669 1.00 16.80 A C
ATOM 2407 C LEO A 379 1.784 10.361 19.802 1.00 15.24 A C
ATOM 2408 O LEO A 379 1.084 9.618 19.088 1.00 15.39 A O
ATOM 2409 N GLY A 380 2.600 11.293 19.301 1.00 15.84 A N
ATOM 2410 CA GLY A 380 3.000 11.299 17.888 1.00 17.36 A C
ATOM 2411 C GLY A 380 4.242 10.478 17.563 1.00 17.24 A C
ATOM 2412 O GLY A 380 5.123 10.272 18.420 1.00 17.59 A O
ATOM 2413 N ASN A 381 4.314 9.981 16.332 1.00 16.39 A N
ATOM 2414 CA ASN A 381 5.532 9.288 15.891 1.00 17.21 A C
ATOM 2415 CB ASN A 381 5.261 7.797 15.461 1.00 15.34 A C
ATOM 2416 CG ASN A 381 4.662 7.661 14.064 1.00 17.34 A C
ATOM 2417 ODl ASN A 381 4.497 8.652 13.348 1.00 15.23 A O
ATOM 2418 ND2 ASN A 381 4.377 6.406 13.654 1.00 13.48 A N
ATOM 2419 C ASN A 381 6.331 10.114 14.872 1.00 17.26 A C
ATOM 2420 O ASN A 381 5.941 11.248 14.515 1.00 18.19 A O
ATOM 2421 N GLN A 382 7.470 9.565 14.451 1.00 17.95 A N
ATOM 2422 CA GLN A 382 8.396 10.294 13.567 1.00 19.27 A C
ATOM 2423 CB GLN A 382 9.834 9.709 13.674 1.00 18.62 A C
ATOM 2424 CG GLN A 382 9.972 8.387 12.940 1.00 20.86 A C
ATOM 2425 CD GLN A 382 10.915 7.381 13.596 1.00 21.75 A C
ATOM 2426 OEl GLN A 382 11.350 7.547 14.735 1.00 24.83 A O
ATOM 2427 NE2 GLN A 382 11.210 6.291 12.867 1.00 20.57 A N
ATOM 2428 C GLN A 382 7.919 10.489 12.094 1.00 19.05 A C
ATOM 2429 O GLN A 382 8.595 11.170 11.303 1.00 20.42 A O
ATOM 2430 N VAL A 383 6.775 9.924 11.725 1.00 19.01 A N
ATOM 2431 CA VAL A 383 6.222 10.107 10.370 1.00 19.23 A C
ATOM 2432 CB VAL A 383 6.208 8.779 9.475 1.00 19.69 A C
ATOM 2433 CGl VAL A 383 7.572 8.430 9.071 1.00 21.84 A C
ATOM 2434 CG2 VAL A 383 5.542 7.603 10.197 1.00 19.76 A C
ATOM 2435 C VAL A 383 4.832 10.727 10.336 1.00 18.45 A C
ATOM 2436 O VAL A 383 4.097 10.567 9.339 1.00 18.65 A O
ATOM 2437 N GLY A 384 4.482 11.435 11.407 1.00 17.23 A N
ATOM 2438 CA GLY A 384 3.248 12.227 11.493 1.00 16.80 A C
ATOM 2439 C GLY A 384 1.948 11.521 11.800 1.00 15.79 A C
ATOM 2440 O GLY A 384 0.870 12.109 11.636 1.00 17.74 A O
ATOM 2441 N LYS A 385 2.053 10.291 12.291 1.00 16.54 A N
ATOM 2442 CA LYS A 385 0.921 9.521 12.784 1.00 16.11 A C
ATOM 2443 CB LYS A 385 1.171 8.028 12.524 1.00 14.73 A C
ATOM 2444 CG LYS A 385 0.007 7.112 12.944 1.00 16.44 A C
ATOM 2445 CD LYS A 385 0.219 5.673 12.394 1.00 17.52 A C
ATOM 2446 CE LYS A 385 -0.956 4.765 12.736 1.00 19.06 A C
ATOM 2447 NZ LYS A 385 -0.759 3.381 12.065 1.00 18.23 A N
ATOM 2448 C LYS A 385 0.669 9.756 14.311 1.00 16.39 A C
ATOM 2449 O LYS A 385 1.606 9.708 15.124 1.00 17.15 A O
ATOM 2450 N LEU A 386 -0.591 9.946 14.695 1.00 16.28 A N
ATOM 2451 CA LEU A 386 -0.938 10.123 16.141 1.00 17.00 A C
ATOM 2452 CB LEU A 386 -1.922 11.263 16.342 1.00 15.90 A C
ATOM 2453 CG LEU A 386 -1.373 12.679 16.368 1.00 18.44 A C
ATOM 2454 CDl LEO A 386 -2.535 13.726 16.341 1.00 18.60 A C
ATOM 2455 CD2 LEU A 386 -0.530 12.848 17.627 1.00 14.47 A C
ATOM 2456 C LEU A 386 -1.606 8.885 16.668 1.00 17.15 A C
ATOM 2457 O LEU A 386 -2.469 8.321 15.979 1.00 17.03 A O
ATOM 2458 N TYR A 387 -1.245 8.501 17.896 1.00 15.52 A N
ATOM 2459 CA TYR A 387 -1.827 7.370 18.600 1.00 15.15 A C
ATOM 2460 CB TYR A 387 -0.760 6.379 19.062 1.00 14.98 A C
ATOM 2461 CG TYR A 387 -0.015 5.646 17.938 1.00 13.90 A C
ATOM 2462 CDl TYR A 387 -0.405 4.386 17.530 1.00 12.30 A C
ATOM 2463 CEl TYR A 387 0.262 3.727 16.482 1.00 17.31 A C
ATOM 2464 CZ TYR A 387 1.346 4.346 15.862 1.00 15.26 A C
ATOM 2465 OH TYR A 387 2.050 3.766 14.844 1.00 17.39 A O
ATOM 2466 CE2 TYR A 387 1.731 5.611 16.250 1.00 16.34 A C ATOM 2467 CD2 TYR A 387 1.044 6.246 17.281 1.00 15.97 A C
ATOM 2468 C TYR A 387 -2.513 7.973 19.838 1.00 15.68 A C
ATOM 2469 O TYR A 387 -1.899 8.793 20.570 1.00 14.14 A O
ATOM 2470 N VAL A 388 -3.798 7.644 20.011 1.00 14.50 A N
ATOM 2471 CA VAL A 388 -4.549 8.055 21.216 1.00 15.22 A C
ATOM 2472 CB VAL A 388 -5.658 9.064 20.825 1.00 15.42 A C
ATOM 2473 CGl VAL A 388 -6.487 9.475 22.038 1.00 12.53 A C
ATOM 2474 CG2 VAL A 388 -5.016 10.273 20.166 1.00 14.92 A C
ATOM 2475 C VAL A 388 -5.109 6.843 21.995 1.00 16.03 A C
ATOM 2476 O VAL A 388 -5.877 6.026 21.411 1.00 16.78 A O
ATOM 2477 N TRP A 389 -4.726 6.694 23.274 1.00 14.28 A N
ATOM 2478 CA TRP A 389 -5.205 5.565 24.048 1.00 14.90 A C
ATOM 2479 CB TRP A 389 -4.071 4.857 24.790 1.00 14.45 A C
ATOM 2480 CG TRP A 389 -3.085 4.058 23.868 1.00 14.13 ' A C
ATOM 2481 CDl TRP A 389 -3.150 2.731 23.534 1.00 13.52 A C
ATOM 2482 NEl TRP A 389 -2.062 2.397 22.729 1.00 13.32 A N
ATOM 2483 CE2 TRP A 389 -1.278 3.503 22.561 1.00 13.15 A C
ATOM 2484 CD2 TRP A 389 -1.878 4.562 23.270 1.00 14.77 A C
ATOM 2485 CE3 TRP A 389 -1.247 5.825 23.266 1.00 14.90 A C
ATOM ' 2486 CZ3 TRP A 389 -0.055 5.975 22.559 1.00 12.88 A C
ATOM 2487 CH2 TRP A 389 0.519 4.899 21.879 1.00 14.67 A C
ATOM 2488 CZ2 TRP A 389 -0.076 3.655 21.859 1.00 12.79 A C
ATOM 2489 C TRP A 389 -6.291 6.009 25.062 1.00 15.35 A C
ATOM 2490 O TRP A 389 -6.089 6.961 25.792 1.00 16.32 A O
ATOM 2491 N ASP A 390 -7.388 5.261 25.095 1.00 15.39 A N
ATOM 2492 CA ASP A 390 -8.512 5.427 26.033 1.00 16.22 A C
ATOM 2493 CB ASP A 390 -9.785 4.922 25.337 1.00 16.17 A C
ATOM 2494 CG ASP A 390 -11.036 4.936 26.242 1.00 21.61 A C
ATOM 2495 ODl ASP A 390 -10.995 5.420 27.392 1.00 19.23 A O
ATOM 2496 OD2 ASP A 390 -12.080 4.432 25.765 1.00 23.37 A O
ATOM 2497 C ASP A 390 -8.181 4.652 27.320 1.00 16.10 A C
ATOM 2498 O ASP A 390 -8.129 3.399 27.326 1.00 14.22 A O
ATOM 2499 N LEU A 391 -7.932 5.406 28.401 1.00 15.20 A N
ATOM 2500 CA LEU A 391 -7.469 4.833 29.672 1.00 15.68 A C
ATOM 2501 CB LEU A 391 -6.467 5.764 30.362 1.00 15.56 A C
ATOM 2502 CG LEU A 391 -5.207 6.189 29.577 1.00 15.38 A C
ATOM 2503 CDl LEU A 391 -4.354 7.138 30.444 1.00 17.58 A C
ATOM 2504 CD2 LEU A 391 -4.385 4.995 29.104 1.00 14.55 A C
ATOM 2505 C LEU A 391 -8.625 4.485 30.620 1.00 15.99 A C
ATOM 2506 O LEU A 391 -8.419 3.934 31.713 1.00 16.24 A O
ATOM 2507 N GLU A 392 -9.843 4.764 30.163 1.00 16.61 A N
ATOM 2508 CA GLU A 392 -11.026 4.525 30.958 1.00 16.96 A C
ATOM 2509 CB GLU A 392 -12.123 5.502 30.568 1.00 17.85 A C
ATOM 2510 CG GLU A 392 -13.265 5.547 31.595 1.00 20.72 A C
ATOM 2511 CD GLU A 392 -13.035 6.558 32.709 1.00 24.09 A C
ATOM 2512 OEl GLϋ A 392 -11.869 6.931 32.957 1.00 22.95 A O
ATOM 2513 OE2 GLU A 392 -14.030 6.959 33.360 1.00 26.56 A O
ATOM 2514 C GLU A 392 -11.515 3.068 30.839 1.00 16.47 A C
ATOM 2515 O GLU A 392 -12.557 2.808 30.239 1.00 16.05 A O
ATOM 2516 N VAL A 393 -10.751 2.159 31.444 1.00 16.21 A N
ATOM 2517 CA VAL A 393 -10.943 0.704 31.406 1.00 16.78 A C
ATOM 2518 CB VAL A 393 -10.116 -0.005 30.223 1.00 17.07 A C
ATOM 2519 CGl VAL A 393 -10.704 0.333 28.861 1.00 17.30 A C
ATOM 2520 CG2 VAL A 393 -8.676 0.363 30.233 1.00 18.13 A C
ATOM 2521 C VAL A 393 -10.457 0.200 32.772 1.00 17.88 A C
ATOM 2522 O VAL A 393 -9.855 0.965 33.502 1.00 16.59 A O
ATOM 2523 N GLU A 394 -10.714 -1.064 33.124 1.00 18.75 A N
ATOM 2524 CA GLU A 394 -10.503 -1.534 34.498 1.00 20.31 A C
ATOM 2525 CB GLU A 394 -11.306 -2.812 34.792 1.00 21.72 A C
ATOM 2526 CG GLU A 394 -12.628 -2.854 34.121 1.00 27.44 A C
ATOM 2527 CD GLU A 394 -13.493 -4.018 34.581 1.00 34.97 A C
ATOM 2528 OEl GLU A 394 -12.935 -5.091 34.945 1.00 36.87 A O
ATOM 2529 OE2 GLU A 394 -14.733 -3.841 34.579 1.00 39.24 A O
ATOM 2530 C GLU A 394 -9.057 -1.774 34.875 1.00 20.27 A C
ATOM 2531 O GLU A 394 -8.714 -1.675 36.054 1.00 19.84 A O
ATOM 2532 N ASP A 395 -8.214 -2.065 33.870 1.00 18.67 A N
ATOM 2533 CA ASP A 395 -6.820 -2.375 34.073 1.00 17.89 A C
ATOM 2534 CB ASP A 395 -6.590 -3.915 34.121 1.00 17.63 A C
ATOM 2535 CG ASP A 395 -7.299 -4.561 35.323 1.00 19.54 A C
ATOM 2536 ODl ASP A 395 -6.753 -4.507 36.442 1.00 17.08 A O
ATOM 2537 OD2 ASP A 395 -8.393 -5.093 35.136 1.00 20.58 A O
ATOM 2538 C ASP A 395 -6.020 -1.713 32.930 1.00 16.75 A C
ATOM 2539 O ASP A 395 -6.550 -1.474 31.847 1.00 16.25 A O
ATOM 2540 N PRO A 396 -4.787 -1.316 33.216 1.00 16.08 A N
ATOM 2541 CA PRO A 396 -3.942 -0.569 32.266 1.00 16.55 A C
ATOM 2542 CB PRO A 396 -2.585 -0.516 33.012 1.00 15.75 A C
ATOM 2543 CG PRO A 396 -3.029 -0.462 34.457 1.00 17.01 A C ATOM 2544 CD PRO A 396 -4.128 -1.480 34.525 1.00 16.32 A C
ATOM 2545 C PRO A 396 -3.813 -1.272 30.892 1.00 16.01 A C
ATOM 2546 O PRO A 396 -3.955 -0.614 29.846 1.00 15.85 A O
ATOM 2547 N HIS A 397 -3.614 -2.598 30.913 1.00 15.07 A N
ATOM 2548 CA HIS A 397 -3.457 -3.407 29.656 1.00 15.36 A C
ATOM 2549 CB HIS A 397 -2.858 -4.803 29.932 1.00 13.71 A C
ATOM 2550 CG HIS A 397 -3.844 -5.820 30.394 1.00 15.33 A C
ATOM 2551 NDl HIS A 397 -4.398 -5.804 31.664 1.00 15.63 A N
ATOM 2552 CEl HIS A 397 -5.255 -6.813 31.777 1.00 15.61 A C
ATOM 2553 NE2 HIS A 397 -5.272 -7.481 30.633 1.00 19.65 A N
ATOM 2554 CD2 HIS A 397 -4.416 -6.868 29.741 1.00 15.64 A C
ATOM 2555 C HIS A 397 -4.693 -3.435 28.716 1.00 15.42 A C
ATOM 2556 O HIS A 397 -4.586 -3.824 27.562 1.00 14.53 A O
ATOM 2557 N LYS A 398 -5.844 -3.000 29.218 1.00 14.18 A N
ATOM 2558 CA LYS A 398 -7.070 -3.020 28.455 1.00 15.58 A C
ATOM 2559 CB LYS A 398 -8.273 -3.342 29.407 1.00 15.72 A C
ATOM 2560 CG LYS A 398 -8.106 -4.723 30.074 1.00 16.30 A C
ATOM 2561 CD LYS A 398 -9.260 -5.077 31.060 1.00 16.98 A C
ATOM 2562 CE LYS A 398 -8.949 -6.362 31.886 1.00 18.52 A C
ATOM 2563 NZ LYS A 398 10.096 -6.550 32.923 1.00 19.71 A N
ATOM 2564 C LYS A 398 -7.260 -1.702 27.674 1.00 15.42 A C
ATOM 2565 O LYS A 398 -8.246 -1.554 26.987 1.00 16.42 A O
ATOM 2566 N ALA A 399 -6.309 -0.773 27.758 1.00 14.80 A N
ATOM 2567 CA ALA A 399 -6.412 0.522 27.046 1.00 16.27 A C
ATOM 2568 CB ALA A 399 -5.089 1.310 27.155 1.00 15.13 A C
ATOM 2569 C ALA A 399 -6.795 0.341 25.562 1.00 17.02 A C
ATOM 2570 O ALA A 399 -6.253 -0.548 24.876 1.00 18.48 A O
ATOM 2571 N LYS A 400 -7.663 1.215 25.061 1.00 17.01 A N
ATOM 2572 CA LYS A 400 -8.121 1.177 23.664 1.00 18.98 A C
ATOM 2573 CB LYS A 400 -9.643 1.233 23.562 1.00 18.40 A C
ATOM 2574 CG LYS A 400 10.384 0.232 24.408 1.00 22.83 A C
ATOM 2575 CD LYS A 400 11.906 0.489 24.353 1.00 25.33 A C
ATOM 2576 CE LYS A 400 12.472 0.936 25.715 1.00 33.54 A C
ATOM 2577 NZ LYS A 400 13.804 0.276 26.115 1.00 36.58 A N
ATOM 2578 C LYS A 400 -7.502 2.265 22.780 1.00 17.50 A C
ATOM 2579 O LYS A 400 -7.652 3.463 23.038 1.00 16.84 A O
ATOM 2580 N CYS A 401 -6.823 1.815 21.725 1.00 17.57 A N
ATOM 2581 CA CYS A 401 -6.123 2.689 20.823 1.00 17.63 A C
ATOM 2582 CB CYS A 401 -4.860 2.004 20.345 1.00 18.06 A C
ATOM 2583 SG CYS A 401 -3.757 3.151 19.493 1.00 16.81 A S
ATOM 2584 C CYS A 401 -6.949 3.148 19.601 1.00 19.07 A C
ATOM 2585 O CYS A 401 -7.601 2.323 18.888 1.00 17.83 A O
ATOM 2586 N THR A 402 -6.910 4.457 19.356 1.00 18.79 A N
ATOM 2587 CA THR A 402 -7.351 5.004 18.090 1.00 21.49 A C
ATOM 2588 CB THR A 402 -8.657 5.873 18.189 1.00 22.41 A C
ATOM 2589 OGl THR A 402 -8.911 6.455 16.899 1.00 28.72 A O
ATOM 2590 CG2 THR A 402 -8.494 7.008 19.100 1.00 20.89 A C
ATOM 2591 C THR A 402 -6.170 5.712 17.414 1.00 21.13 A C
ATOM 2592 O THR A 402 -5.310 6.308 18.121 1.00 20.74 A O
ATOM 2593 N THR A 403 -6.097 5.627 16.072 1.00 19.53 A N
ATOM 2594 CA THR A 403 -5.039 6.351 15.326 1.00 19.69 A C
ATOM 2595 CB THR A 403 -4.152 5.397 14.460 1.00 19.42 A C
ATOM 2596 OGl THR A 403 -5.028 4.581 13.668 1.00 21.66 A O
ATOM 2597 CG2 THR A 403 -3.278 4.481 15.330 1.00 17.79 A C
ATOM 2598 C THR A 403 -5.563 7.461 14.404 1.00 19.66 A C
ATOM 2599 O THR A 403 -6.633 7.342 13.758 1.00 18.02 A O
ATOM 2600 N LEU A 404 -4.777 8.519 14.312 1.00 18.92 A N
ATOM 2601 CA LEU A 404 -5.141 9.730 13.556 1.00 19.42 A C
ATOM 2602 CB LEU A 404 -5.379 10.920 14.516 1.00 18.65 A C
ATOM 2603 CG LEU A 404 -6.381 10.747 15.671 1.00 20.78 A C
ATOM 2604 CDl LEU A 404 -6.336 11.964 16.582 1.00 20.29 A C
ATOM 2605 CD2 LEU A 404 -7.823 10.489 15.211 1.00 21.30 A C
ATOM 2606 C LEU A 404 -4.029 10.061 12.561 1.00 19.47 A C
ATOM 2607 O LEU A 404 -2.866 10.296 12.955 1.00 19.20 A O
ATOM 2608 N THR A 405 -4.386 10.047 11.260 1.00 19.74 A N
ATOM 2609 CA THR A 405 -3.463 10.322 10.163 1.00 19.64 A C
ATOM 2610 CB THR A 405 -3.075 9.030 9.377 1.00 20.68 A C
ATOM 2611 OGl THR A 405 -4.254 8.359 8.896 1.00 20.26 A O
ATOM 2612 CG2 THR A 405 -2.357 8.084 10.284 1.00 22.26 A C
ATOM 2613 C THR A 405 -4.023 11.361 9.176 1.00 19.54 A C
ATOM 2614 O THR A 405 -5.217 11.472 8.984 1.00 18.46 A O
ATOM 2615 N HIS A 406 -3.133 12.140 8.594 1.00 21.54 A N
ATOM 2616 CA HIS A 406 -3.441 13.069 7.510 1.00 22.59 A C
ATOM 2617 CB HIS A 406 -3.461 14.518 7.997 1.00 22.68 A C
ATOM 2618 CG HIS A 406 -4.142 15.463 7.052 1.00 25.13 A C
ATOM 2619 NDl HIS A 406 -3.503 16.005 5.952 1.00 25.15 A N
ATOM 2620 CEl HIS A 406 -4.348 16.779 5.289 1.00 28.61 A C ATOM 2621 NE2 HIS A 406 -5.514 16.759 5.920 1.00 30.72 A N
ATOM 2622 CD2 HIS A 406 -5.407 15.955 7.033 1.00 25.93 A C
ATOM 2623 C HIS A 406 -2.373 12.903 6.453 1.00 23.32 A C
ATOM 2624 O HIS A 406 -1.171 12.882 6.766 1.00 21.94 A O
ATOM 2625 N HIS A 407 -2.819 12.835 5.196 1.00 24.27 A N
ATOM 2626 CA HIS A 407 -1.926 12.633 4.037 1.00 26.31 A C
ATOM 2627 CB HIS A 407 -2.754 12.375 2.744 1.00 27.76 A C
ATOM 2628 CG HIS A 407 -3.279 13.616 2.068 1.00 32.98 A C
ATOM 2629 NDl HIS A 407 -4.482 14.206 2.410 1.00 37.27 A N
ATOM 2630 CEl HIS A 407 -4.700 15.255 1.631 1.00 37.34 A C
ATOM 2631 NE2 HIS A 407 -3.692 15.359 0.782 1.00 36.91 A N
ATOM 2632 CD2 HIS A 407 -2.791 14.344 1.028 1.00 36.26 A C
ATOM 2633 C HIS A 407 -0.840 13.732 3.869 1.00 25.75 A C
ATOM 2634 O HIS A 407 0.221 13.470 3.308 1.00 25.93 A O
ATOM 2635 N LYS A 408 -1.081 14.922 4.406 1.00 24.70 A N
ATOM 2636 CA LYS A 408 -0.096 15.993 4.346 1.00 26.14 A C
ATOM 2637 CB LYS A 408 -0.756 17.313 3.918 1.00 26.78 A C
ATOM 2638 CG LYS A 408 -1.044 17.311 2.374 1.00 30.77 A C
ATOM 2639 CD LYS A 408 -2.034 18.383 1.961 1.00 36.30 A C
ATOM 2640 CE LYS A 408 -1.847 18.752 0.495 1.00 39.00 A C
ATOM 2641 NZ LYS A 408 -2.449 20.100 0.225 1.00 41.89 A N
ATOM 2642 C LYS A 408 0.748 16.144 5.609 1.00 25.51 A C
ATOM 2643 O LYS A 408 1.693 16.943 5.632 1.00 26.37 A O
ATOM 2644 N CYS A 409 0.415 15.350 6.632 1.00 24.14 A N
ATOM 2645 CA CYS A 409 1.150 15.345 7.897 1.00 22.84 A C
ATOM 2646 CB CYS A 409 0.194 15.320 9.105 1.00 23.05 A C
ATOM 2647 SG CYS A 409 1.075 15.445 10.684 1.00 23.19 A S
ATOM 2648 C CYS A 409 2.174 14.188 7.924 1.00 22.15 A C
ATOM 2649 O CYS A 409 1.837 13.029 8.247 1.00 21.73 A O
ATOM 2650 N GLY A 410 3.411 14.512 7.536 1.00 21.15 A N
ATOM 2651 CA GLY A 410 4.432 13.519 7.398 1.00 20.36 A C
ATOM 2652 C GLY A 410 5.724 13.705 8.192 1.00 20.30 A C
ATOM 2653 O GLY A 410 6.615 12.837 8.119 1.00 21.62 A O
ATOM 2654 N ALA A 411 5.861 14.830 8.907 1.00 18.82 A N
ATOM 2655 CA ALA A 411 7.056 15.096 9.741 1.00 18.33 A C
ATOM 2656 CB ALA A 411 7.381 16.559 9.723 1.00 17.63 A C
ATOM 2657 C ALA A 411 6.921 14.594 11.193 1.00 17.91 A C
ATOM 2658 O ALA A 411 5.803 14.370 11.670 1.00 19.12 A O
ATOM 2659 N ALA A 412 8.048 14.392 11.885 1.00 17.76 A N
ATOM 2660 CA ALA A 412 7.985 13.868 13.241 1.00 17.36 A C
ATOM 2661 CB ALA A 412 9.408 13.634 13.848 1.00 17.07 A C
ATOM 2662 C ALA A 412 7.157 14.792 14.126 1.00 16.72 A C
ATOM 2663 O ALA A 412 7.383 16.016 14.126 1.00 17.06 A O
ATOM 2664 N ILE A 413 6.229 14.208 14.874 1.00 14.37 A N
ATOM 2665 CA ILE A 413 5.462 14.952 15.912 1.00 15.03 A C
ATOM 2666 CB ILE A 413 4.015 14.365 16.086 1.00 15.57 A C
ATOM 2667 CGl ILE A 413 3.153 14.643 14.850 1.00 12.49 A C
ATOM 2668 CDl ILE A 413 1.995 13.652 14.647 1.00 15.12 A C
ATOM 2669 CG2 ILE A 413 3.276 14.986 17.324 1.00 15.57 A C
ATOM 2670 C ILE A 413 6.242 14.881 17.230 1.00 14.77 A C
ATOM 2671 O ILE A 413 6.485 13.785 17.744 1.00 15.49 A O
ATOM 2672 N ARG A 414 6.618 16.029 17.803 1.00 14.40 A N
ATOM 2673 CA ARG A 414 7.462 16.030 19.007 1.00 14.86 A C
ATOM 2674 CB ARG A 414 8.433 17.245 19.112 1.00 15.14 A C
ATOM 2675 CG ARG A 414 9.385 17.650 17.915 1.00 17.71 A C
ATOM 2676 CD ARG A 414 10.340 16.647 17.258 1.00 26.54 A C
ATOM 2677 NE ARG A 414 11.277 15.995 18.134 1.00 24.11 A N
ATOM 2678 CZ ARG A 414 12.408 15.359 17.810 1.00 21.38 A C
ATOM 2679 NHl ARG A 414 12.934 15.332 16.587 1.00 28.35 A N
ATOM 2680 NH2 ARG A 414 13.082 14.767 18.790 1.00 19.26 A N
ATOM 2681 C ARG A 414 6.618 16.033 20.280 1.00 15.05 A C
ATOM 2682 O ARG A 414 6.994 15.454 21.278 1.00 15.23 A O
ATOM 2683 N GLN A 415 5.512 16.743 20.257 1.00 14.55 A N
ATOM 2684 CA GLN A 415 4.654 16.803 21.437 1.00 14.86 A C
ATOM 2685 CB GLN A 415 5.142 17.923 22.413 1.00 13.95 A C
ATOM 2686 CG GLN A 415 4.496 17.758 23.815 1.00 14.70 A C
ATOM 2687 CD GLN A 415 5.148 18.613 24.890 1.00 16.74 A C
ATOM 2688 OEl GLN A 415 5.366 19.806 24.684 1.00 13.18 A O
ATOM 2689 NE2 GLN A 415 5.415 18.007 26.064 1.00 15.01 A N
ATOM 2690 C GLN A 415 3.196 17.040 21.015 1.00 15.02 A C
ATOM 2691 O GLN A 415 2.959 17.513 19.897 1.00 13.28 A O
ATOM 2692 N THR A 416 2.237 16.714 21.911 1.00 14.02 A N
ATOM 2693 CA THR A 416 0.827 16.932 21.691 1.00 15.26 A C
ATOM 2694 CB THR A 416 0.030 15.589 21.489 1.00 15.35 A C
ATOM 2695 OGl THR A 416 0.185 14.792 22.664 1.00 18.19 A O
ATOM 2696 CG2 THR A 416 0.582 14.761 20.333 1.00 17.27 A C
ATOM 2697 C THR A 416 0.286 17.632 22.953 1.00 14.17 A C ATOM 2698 O THR A 416 0.888 17.522 24.032 1.00 14.45 A O
ATOM 2699 N SER A 417 -0.816 18.350 22.832 1.00 13.78 A N
ATOM 2700 CA SER A 417 -1.504 18.922 24.026 1.00 14.22 A C
ATOM 2701 CB SER A 417 -0.976 20.350 24.361 1.00 12.96 A C
ATOM 2702 OG SER A 417 -1.568 20.921 25.531 1.00 11.80 A O
ATOM 2703 C SER A 417 -3.021 18.943 23.799 .00 14.97 A C
ATOM 2704 O SER A 417 -3.499 19.318 22.729 .00 16.35 A O
ATOM 2705 N PHE A 418 -3.778 18.556 24.825 .00 16.23 A N
ATOM 2706 CA PHE A 418 -5.240 18.637 24.835 .00 16.10 A C
ATOM 2707 CB PHE A 418 -5.817 17.488 25.678 .00 15.45 A C
ATOM 2708 CG PHE A 418 -5.823 16.134 24.987 .00 17.73 A C
ATOM 2709 CDl PHE A 418 -6.836 15.815 24.049 .00 16.28 A C
ATOM 2710 CEl PHE A 418 -6.874 14.531 23.436 .00 14.41 A C
ATOM 2711 CZ PHE A 418 -5.911 13.574 23.769 .00 15.02 A C
ATOM 2712 CE2 PHE A 418 -4.890 13.870 24.711 1.00 14.31 A C
ATOM 2713 CD2 PHE A 418 -4.890 15.139 25.345 1.00 13.10 A C
ATOM 2714 C PHE A 418 -5.670 19.948 25.489 16.57 A C
ATOM 2715 O PHE A 418 -5.085 20.394 26.509 14.66 A O
ATOM 2716 N SER A 419 -6.701 20.572 24.913 16.33 A N
ATOM 2717 CA SER A 419 -7.374 21.697 25.564 16.55 A C
ATOM 2718 CB SER A 419 -8.474 22.279 24.676 16.47 A C
ATOM 2719 OG SER A 419 -9.530 21.335 24.421 16.76 A O
ATOM 2720 C SER A 419 -7.947 21.226 26.935 16.93 A C
ATOM 2721 O SER A 419 -8.123 20.042 27.124 15.76 A O
ATOM 2722 N ARG A 420 -8.214 22.155 27.864 19.30 A N
ATOM 2723 CA ARG A 420 -8.760 21.818 29.193 21.94 A C
ATOM 2724 CB ARG A 420 -8.920 23.086 30.017 22.55 A C
ATOM 2725 CG ARG A 420 -9.160 22.833 31.501 22.52 A C
ATOM 2726 CD ARG A 420 -9.277 24.137 32.276 25.39 A C
ATOM 2727 NE ARG A 420 -9.576 23.915 33.688 34.94 A N
ATOM 2728 CZ ARG A 420 -9.426 22.751 34.308 37.85 A C
ATOM 2729 NHl ARG A 420 -8.978 21.697 33.641 39.44 A N
ATOM 2730 NH2 ARG A 420 -9.704 22.647 35.600 35.28 A N
ATOM 2731 C ARG A 420 -10.116 21.070 29.144 23.03 A C
ATOM 2732 O ARG A 420 -10.407 20.265 30.019 21.69 A O
ATOM 2733 N ASP A 421 -10.939 21.339 28.111 23.85 A N
ATOM 2734 CA ASP A 421 -12.264 20.719 27.994 25.73 A C
ATOM 2735 CB ASP A 421 -13.309 21.712 27.427 26.85 A C
ATOM 2736 CG ASP A 421 -12.984 22.178 26.017 27.17 A C
ATOM 2737 ODl ASP A 421 -12.021 21.688 25.438 25.56 A O
ATOM 2738 OD2 ASP A 421 -13.721 23.022 25.465 36.20 A O
ATOM 2739 C ASP A 421 -12.220 19.422 27.187 26.29 A C
ATOM 2740 O ASP A 421 -13.266 18.812 26.931 26.45 A O
ATOM 2741 N SER A 422 -10.995 19.024 26.813 25.32 A N
ATOM 2742 CA SER A 422 -10.685 17.830 26.017 24.91 A C
ATOM 2743 CB SER A 422 -11.075 16.551 26.778 25.52 A C
ATOM 2744 OG SER A 422 -10.636 16.562 28.147 25.64 A O
ATOM 2745 C SER A 422 -11.252 17.808 24.538 23.98 A C
ATOM 2746 O SER A 422 -11.270 16.760 23.883 24.21 A O
ATOM 2747 N SER A 423 -11.639 18.961 24.015 1.00 22.89 A N
ATOM 2748 CA SER A 423 -12.353 19.049 22.721 00 21.82 A C
ATOM 2749 CB SER A 423 -13.400 20.175 22.111 00 20.53 A C
ATOM 2750 OG SER A 423 -12.760 21.438 22.684 00 23.42 A O
ATOM 2751 C SER A 423 -11.401 19.268 21.528 00 20.67 A C
ATOM 2752 O SER A 423 -11.809 19.087 20.349 00 20.64 A O
ATOM 2753 N ILE A 424 -10.151 19.652 21.831 00 17.48 A N
ATOM 2754 CA ILE A 424 -9.127 19.930 20.808 00 16.73 A C
ATOM 2755 CB ILE A 424 -8.904 21.460 20.594 00 16.37 A C
ATOM 2756 CGl ILE A 424 -10.247 22.199 20.394 00 16.84 A C
ATOM 2757 CDl ILE A 424 -10.125 23.687 20.001 00 18.45 A C
ATOM 2758 CG2 ILE A 424 -7.806 21.765 19.537 00 15.76 A C
ATOM 2759 C ILE A 424 -7.819 19.267 21.155 00 16.09 A C
ATOM 2760 O ILE A 424 -7.365 19.277 22.315 00 16.65 A O
ATOM 2761 N LEU A 425 -7.205 18.691 20.140 00 16.23 A N
ATOM 2762 CA LEU A 425 -5.869 18.154 20.236 00 16.06 A C
ATOM 2763 CB LEϋ A 425 -5.930 16.642 20.015 00 16.04 A C
ATOM 2764 CG LEU A 425 -4.636 15.839 19.962 00 17.10 A C
ATOM 2765 CDl LEU A 425 -3.973 15.861 21.393 1.00 18.95 A C
ATOM 2766 CD2 LEU A 425 -4.916 14.388 19.526 15.84 A C
ATOM 2767 C LEU A 425 -4.,883 18.816 19.234 15.55 A C
ATOM 2768 O LEU A 425 -5..118 18.778 18.040 16.38 A O
ATOM 2769 N ILE A 426 -3.806 19.417 19.741 14.78 A N
ATOM 2770 CA ILE A 426 -2.726 19.984 18.918 14.61 A C
ATOM 2771 CB ILE A 426 -2.345 21.451 19.362 15.31 A C
ATOM 2772 CGl ILE A 426 -3.571 22.398 19.439 15.23 A C
ATOM 2773 CDl ILE A 426 -4.230 22.840 18.101 14.28 A C
ATOM 2774 CG2 ILE A 426 -1.158 21.990 18.547 1.00 11.11 A C ATOM 2775 C ILE A 426 -1.460 19.121 18.917 00 14.98 A C
ATOM 2776 O ILE A 426 -0.983 18.689 19.986. 00 14.74 A O
ATOM 2777 N ALA A 427 -0.917 18.868 17.715 00 14.28 A N
ATOM 2778 CA ALA A 427 0.365 18.186 17.518 00 13.98 A C
ATOM 2779 CB ALA A 427 0.155 16.898 16.697 00 13.58 A C
ATOM 2780 C ALA A 427 1.316 19.174 16.785 00 14.19 A C
ATOM 2781 O ALA A 427 0.898 19.928 15.885 00 14.55 A O
ATOM 2782 N VAL A 428 2.566 19.236 17.230 00 14.31 A N
ATOM 2783 CA VAL A 428 3.574 20.097 16.605 00 14.12 A C
ATOM 2784 CB VAL A 428 4.082 21.251 17.535 00 13.17 A C
ATOM 2785 CGl VAL A 428 2.936 22.190 17.909 00 13.58 A C
ATOM 2786 CG2 VAL A 428 4.766 20.716 18.773 00 13.24 A C
ATOM 2787 C VAL A 428 4.752 19.246 16.133 00 14.63 A C
ATOM 2788 O VAL A 428 5.044 18.178 16.712 00 15.06 A O
ATOM 2789 N CYS A 429 5.446 19.729 15.107 1.00 14.28 A N
ATOM 2790 CA CYS A 429 6.278 18.863 14.277 16.89 A C
ATOM 2791 CB CYS A 429 5.619 18.643 12.909 16.88 A C
ATOM 2792 SG CYS A 429 4.111 17.697 12.972 18.25 A S
ATOM 2793 C CYS A 429 7.660 19.424 14.031 17.55 A C
ATOM 2794 O CYS A 429 7.846 20.616 14.195 17.89 A O
ATOM 2795 N ASP A 430 8.581 18.545 13.601 17.74 A N
ATOM 2796 CA ASP A 430 9.982 18.853 13.252 18.91 A C
ATOM 2797 CB ASP A 430 10.813 17.560 13.012 18.41 A C
ATOM 2798 CG ASP A 430 11.631 17.174 14.205 21.68 A C
ATOM 2799 ODl ASP A 430 11.371 17.744 15.263 1.00 25.14 A O
ATOM 2800 OD2 ASP A 430 12.513 16.289 14.146 25.59 A O
ATOM 2801 C ASP A 430 10.164 19.823 12.070 19.24 A C
ATOM 2802 O ASP A 430 11.206 20.468 11.952 19.12 A O
ATOM 2803 N ASP A 431 9.148 19.932 11.232 19.51 A N
ATOM 2804 CA ASP A 431 9.176 20.853 10.111 20.82 A C
ATOM 2805 CB ASP A 431 8.550 20.190 8.861 21.39 A C
ATOM 2806 CG ASP A 431 7.043 20.000 8.989 24.31 A C
ATOM 2807 ODl ASP A 431 6.490 20.053 10.135 26.51 A O
ATOM 2808 OD2 ASP A 431 6.395 19.782 7.955 25.92 A O
ATOM 2809 C ASP A 431 8.488 22.194 10.445 20.47 A C
ATOM 2810 O ASP A 431 8.178 22.959 9.526 20.28 A O
ATOM 2811 N ALA A 432 8.269 22.461 11.752 19.74 A N
ATOM 2812 CA ALA A 432 7.600 23.693 12.262 19.70 A C
ATOM 2813 CB ALA A 432 8.377 25.013 11.787 20.33 A C
ATOM 2814 C ALA A 432 6.074 23.803 12.014 18.56 A C
ATOM 2815 O ALA A 432 5.465 24.909 12.131 18.70 A O
ATOM 2816 N SER A 433 5.447 22.668 11.690 17.25 A N
ATOM 2817 CA SER A 433 4.028 22.635 11.351 16.25 A C
ATOM 2818 CB SER A 433 3.694 21.635 10.229 16.24 A C
ATOM 2819 OG SER A 433 3.933 20.263 10.535 17.75 A O
ATOM 2820 C SER A 433 3.229 22.344 12.643 16.44 A C
ATOM 2821 O SER A 433 3.747 21.655 13.565 15.90 A O
ATOM 2822 N ILE A 434 2.031 22.911 12.695 14.53 A N
ATOM 2823 CA ILE A 434 1.060 22.714 13.786 15.31 A C
ATOM 2824 CB ILE A 434 0.721 24.071 14.452 1.00 14.14 A C
ATOM 2825 CGl ILE A 434 2.010 24.676 15.068 15.29 A C
ATOM 2826 CDl ILE A 434 1.949 26.176 15.343 14.83 A C
ATOM 2827 CG2 ILE A 434 -0.489 23.967 15.501 13.71 A C
ATOM 2828 C ILE A 434 -0.171 22.089 13.194 15.19 A C
ATOM 2829 O ILE A 434 -0.634 22.530 12.107 15.88 A O
ATOM 2830 N TRP A 435 -0.709 21.088 13.893 •14.63 A N
ATOM 2831 CA TRP A 435 -1.898 20.319 13.444 15.50 A C
ATOM 2832 CB TRP A 435 -1 503 18.872 13.078 15.80 A C
ATOM 2833 CG TRP A 435 -0.507 18.881 11.944 17.53 A C
ATOM 2834 CDl TRP A 435 0.850 19.105 12.016 19.07 A C
ATOM 2835 NEl TRP A 435 1.404 19.066 10.747 1.00 18.54 A N
ATOM 2836 CE2 TRP A 435 0.393 18.868 9.836 20.71 A C
ATOM 2837 CD2 TRP A 435 -0.818 18.742 10.558 19.93 A C
ATOM 2838 CE3 TRP A 435 -2.018 18.520 9.849 20.42 A C
ATOM 2839 CZ3 TRP A 435 -1.980 18.423 8.457 1.00 18.14 A C
ATOM 2840 CH2 TRP A 435 -0.764 18.564 7.757 20.97 A C
ATOM 2841 CZ2 TRP A 435 0.438 18.792 8.425 21.45 A C
ATOM 2842 C TRP A 435 -3.016 20.339 14.464 14.98 A C
ATOM 2843 O TRP A 435 -2.812 19.998 15.646 15.49 A O
ATOM 2844 N ARG A 436 -4.199 20.742 14.022 14.38 A N
ATOM 2845 CA ARG A 436 -5.340 20.864 14.918 16.75 A C
ATOM 2846 CB ARG A 436 -5.965 22.270 14.830 16.62 A C
ATOM 2847 CG ARG A 436 -7.161 22.449 15.802 18.47 A C
ATOM 2848 CD ARG A 436 -7.907 23.788 15.588 18.38 A C
ATOM 2849 NE ARG A 436 -9.265 23.720 16.201 19.48 A N
ATOM 2850 CZ ARG A 436 -10.036 24.773 16.426 19.98 A C
ATOM 2851 NHl ARG A 436 -9.620 25.990 16.080 1.00 16.32 A N ATOM 2852 NH2 ARG A 436 11.239 24.605 16.970 1.00 24.60 A N
ATOM 2853 C ARG A 436 -6.430 19.819 14.694 1.00 16.86 A C
ATOM 2854 O ARG A 436 -6.976 19.703 13.569 1.00 17.83 A O
ATOM 2855 N TRP A 437 -6.754 19.082 15.747 1.00 16.17 A N
ATOM 2856 CA TRP A 437 -7.714 17.980 15.673 1.00 17.22 A C
ATOM 2857 CB TRP A 437 -7.056 16.610 15.994 1.00 16.28 A C
ATOM 2858 CG TRP A 437 -6.003 16.175 15.006 1.00 17.13 A C
ATOM 2859 CDl TRP A 437 -4.697 16.559 14.964 1.00 16.54 A C
ATOM 2860 NEl TRP A 437 -4.042 15.928 13.940 1.00 16.81 A N
ATOM 2861 CE2 TRP A 437 -4.935 15.134 13.265 1.00 17.35 A C
ATOM 2862 CD2 TRP A 437 -6.191 15.272 13.909 1.00 18.30 A C
ATOM 2863 CE3 TRP A 437 -7.286 14.514 13.448 1.00 15.53 A C
ATOM 2864 CZ3 TRP A 437 -7.097 13.677 12.341 1.00 17.51 A C
ATOM 2865 CH2 TRP A 437 -5.841 13.584 11.687 1.00 17.01 A C
ATOM 2866 CZ2 TRP A 437 -4.744 14.282 12.139 1.00 17.26 A C
ATOM 2867 C TRP A 437 -8.870 18.224 16.616 1.00 17.53 A C
ATOM 2868 O TRP A 437 -8.669 18.351 17.832 1.00 16.70 A O
ATOM 2869 N ASP A 438 10.081 18.290 16.071 1.00 18.39 A N
ATOM 2870 CA ASP A 438 11.253 18.610 16.918 1.00 20.49 A C
ATOM 2871 CB ASP A 438 12.164 19.674 16.282 1.00 20.99 A C
ATOM 2872 CG ASP A 438 11.607 21.100 16.409 1.00 22.23 A C
ATOM 2873 ODl ASP A 438 10.392 21.270 16.710 1.00 21.69 A O
ATOM 2874 OD2 ASP A 438 12.390 22.054 16.216 1.00 23.58 A O
ATOM 2875 C ASP A 438 12.035 17.351 17.161 1.00 22.83 A C
ATOM 2876 O ASP A 438 12.217 16.539 16.248 1.00 23.25 A O
ATOM 2877 N ARG A 439 12.523 17.203 18.381 1.00 25.96 A N
ATOM 2878 CA ARG A 439 13.209 15.989 18.764 1.00 30.16 A C
ATOM 2879 CB ARG A 439 13.193 15.841 20.294 1.00 30.04 A C
ATOM 2880 CG ARG A 439 13.634 14.493 20.778 1.00 34.17 A C
ATOM 2881 CD ARG A 439 12.934 14.061 22.037 1.00 37.64 A C
ATOM 2882 NE ARG A 439 13.863 13.283 22.841 1.00 43.73 A N
ATOM 2883 CZ ARG A 439 14.084 13.466 24.140 1.00 46.28 A C
ATOM 2884 NHl ARG A 439 13.419 14.392 24.816 1.00 45.02 A N
ATOM 2885 NH2 ARG A 439 14.971 12.698 24.770 1.00 49.54 A N
ATOM 2886 C ARG A 439 14.628 15.973 18.196 1.00 32.45 A C
ATOM 2887 O ARG A 439 15.346 16.977 18.277 1.00 32.54 A O
ATOM 2888 N LEU A 440 14.997 14.842 17.579 1.00 35.67 A N
ATOM 2889 CA LEU A 440 16.423 14.519 17.266 1.00 37.77 A C
ATOM 2890 CB LEU A 440 16.737 14.569 15.754 1.00 38.09 A C
ATOM 2891 CG LEU A 440 15.808 14.094 14.625 1.00 38.76 A C
ATOM 2892 CDl LEU A 440 15.720 12.578 14.551 1.00 40.12 A C
ATOM 2893 CD2 LEU A 440 16.295 14.663 13.278 1.00 39.28 A C
ATOM 2894 C LEU A 440 16.867 13.181 17.860 1.00 38.20 A C
ATOM 2895 O LEU A 440 17.474 13.140 18.935 1.00 39.36 A O
ATOM 2896 O HOH W 441 16.174 24.796 51.203 1.00 11.61 W O
ATOM 2897 O HOH W 442 1.725 18.952 26.162 1.00 11.89 W O
ATOM 2898 O HOH W 443 19.574 13.543 39.430 1.00 13.92 W O
ATOM 2899 O HOH W 444 10.091 2.424 24.589 1.00 19.04 W O
ATOM 2900 O HOH W 445 5.947 21.294 30.428 1.00 10.79 W O
ATOM 2901 O HOH W 446 19.245 30.713 54.448 1.00 14.09 W O
ATOM 2902 O HOH W 447 -2.922 -4.306 33.538 1.00 19.77 W O
ATOM 2903 O HOH W 448 9.432 4.791 21.411 1.00 19.02 W O
ATOM 2904 O HOH W 449 17.035 28.352 28.211 1.00 14.07 W O
ATOM 2905 O HOH W 450 6.975 29.339 18.433 1.00 16.88 W O
ATOM 2906 O HOH W 451 -1.790 24.467 32.309 1.00 27.87 W O
ATOM 2907 O HOH W 452 11.199 5.299 49.489 1.00 29.45 W O
ATOM 2908 O HOH W 453 5.978 32.230 12.073 1.00 27.28 W O
ATOM 2909 O HOH W 454 9.521 16.479 22.574 1.00 23.64 W O
ATOM 2910 O HOH W 455 14.878 1.210 32.744 1.00 20.33 W O
ATOM 2911 O HOH W 456 -6.461 33.695 11.759 1.00 20.08 W O
ATOM 2912 O HOH W 457 13.780 24.177 17.343 1.00 19.64 W O
ATOM 2913 O HOH W 458 10.622 41.546 27.904 1.00 25.92 W O
ATOM 2914 O HOH W 459 6.267 21.712 26.433 1.00 14.93 W O
ATOM 2915 O HOH W 460 0.483 15.816 29.995 1.00 22.33 W O
ATOM 2916 O HOH W 461 -0.848 -0.123 21.836 1.00 20.33 W O
ATOM 2917 O HOH W 462 1.650 23.669 31.234 1.00 12.55 W O
ATOM 2918 O HOH W 463 -9.216 29.484 35.423 1.00 40.19 W O
ATOM 2919 O HOH W 464 -2.228 17.297 27.018 1.00 14.56 W O
ATOM 2920 O HOH W 465 4.366 15.833 27.419 1.00 15.75 W O
ATOM 2921 O HOH W 466 12.644 -2.422 31.067 1.00 28.90 W O
ATOM 2922 O HOH W 467 18.131 30.836 45.699 1.00 12.33 W O
ATOM 2923 O HOH W 468 15.263 1.163 44.550 1.00 24.06 W O
ATOM 2924 O HOH W 469 3.934 -8.282 33.303 1.00 18.45 W O
ATOM 2925 O HOH W 470 18.834 -1.029 30.781 1.00 41.32 W O
ATOM 2926 O HOH W 471 6.032 18.837 28.974 1.00 15.83 W O
ATOM 2927 O HOH W 472 -1.654 12.829 12.425 1.00 15.42 W O
ATOM 2928 O HOH W 473 -7.315 9.300 10.605 1.00 24.43 W O ATOM 2929 O HOH W 474 -8.115 17.730 28.691 1.00 22.76 W O
ATOM 2930 O HOH W 475 -1.418 15.437 13.266 1.00 20.59 W O
ATOM 2931 O HOH W 476 26.031 18.151 49.433 1.00 16.80 W O
ATOM 2932 O HOH W 477 6.880 41.699 24.479 1.00 16.76 W O
ATOM 2933 O HOH W 478 17.418 32.561 26.955 1.00 37.63 W O
ATOM 2934 O HOH W 479 3.509 4.993 11.125 1.00 22.20 W O
ATOM 2935 O HOH W 480 13.725 31.294 55.250 1.00 21.87 W O
ATOM 2936 O HOH W 481 10.584 14.787 10.478 1.00 22.60 W O
ATOM 2937 O HOH W 482 5.681 19.145 50.570 1.00 28.73 W O
ATOM 2938 O HOH W 483 6.082 10.495 49.193 1.00 17.87 W O
ATOM 2939 O HOH W 484 -1.846 10.710 38.392 1.00 24.49 W O
ATOM 2940 O HOH W 485 14.955 21.563 55.927 1.00 26.13 W O
ATOM 2941 O HOH W 486 10.174 39.322 21.922 1.00 19.20 W O
ATOM 2942 O HOH W 487 3.918 17.069 9.637 1.00 19.77 W O
ATOM 2943 O HOH W 488 3.481 24.628 49.134 1.00 20.83 W O
ATOM 2944 O HOH W 489 3.331 21.775 34.456 1.00 12.84 W O
ATOM 2945 O HOH W 490 16.308 23.603 16.535 1.00 28.85 W O
ATOM 2946 O HOH W 491 8.437 0.522 13.790 1.00 28.26 W O
ATOM 2947 O HOH W 492 -9.338 14.175 9.556 1.00 27.10 W O
ATOM 2948 O HOH W 493 -7.778 6.568 33.351 1.00 39.76 W O
ATOM 2949 O HOH W 494 21.449 20.230 52.051 1.00 25.54 W O
ATOM 2950 O HOH W 495 3.499 32.649 40.702 1.00 20.77 W O
ATOM 2951 O HOH W 496 13.690 -5.560 47.246 1.00 32.64 W O
ATOM 2952 O HOH W 497 23.256 13.579 39.786 1.00 19.59 W O
ATOM 2953 O HOH W 498 12.716 33.648 16.358 1.00 22.83 W O
ATOM 2954 O HOH W 499 19.644 18.508 26.016 1.00 26.05 W O
ATOM 2955 O HOH W 500 5.867 32.426 15.451 1.00 17.01 W O
ATOM 2956 O HOH W 501 15.559 35.531 46.702 1.00 25.59 W O
ATOM 2957 O HOH W 502 3.506 10.218 48.942 1.00 24.09 W O
ATOM 2958 O HOH W 503 19.048 32.727 39.237 1.00 33.90 W O
ATOM 2959 O HOH W 504 4.180 -9.167 42.080 1.00 37.08 W O
ATOM 2960 O HOH W 505 10.820 6.198 9.824 1.00 31.72 W O
ATOM 2961 O HOH W 506 11.407 29.131 9.804 1.00 39.05 W O
ATOM 2962 O HOH W 507 2.749 -2.722 50.828 1.00 30.05 W O
ATOM 2963 O HOH W 508 13.427 31.491 13.279 1.00 23.96 W O
ATOM 2964 O HOH W 509 20.255 5.704 42.546 1.00 34.46 W O
ATOM 2965 O HOH W 510 -7.403 24.827 27.417 1.00 23.38 W O
ATOM 2966 O HOH W 511 13.572 36.836 55.201 1.00 28.64 W O
ATOM 2967 O HOH W 512 20.187 33.617 48.113 1.00 26.04 W O
ATOM 2968 O HOH W 513 7.581 40.087 22.139 1.00 14.79 W O
ATOM 2969 O HOH W 514 19.612 42.897 52.773 1.00 29.67 W O
ATOM 2970 O HOH W 515 14.863 31.739 17.258 1.00 36.67 W O
ATOM 2971 O HOH W 516 11.291 8.024 21.230 1.00 27.42 W O
ATOM 2972 O HOH W 517 -3.195 3.967 40.999 1.00 28.41 W O
ATOM 2973 O HOH W 518 6.680 10.892 6.179 1.00 33.87 W O
ATOM 2974 O HOH W 519 4.194 17.170 36.964 1.00 18.50 W O
ATOM 2975 O HOH W 520 13.968 14.774 51.636 1.00 33.26 W O
ATOM 2976 O HOH W 521 26.703 12.874 37.763 1.00 30.66 W O
ATOM 2977 O HOH W 522 4.084 17.261 49.809 1.00 27.00 W O
ATOM 2978 O HOH W 523 15.107 -1.267 41.841 1.00 26.55 W O
ATOM 2979 O HOH W 524 13.653 14.349 48.580 1.00 29.92 W O
ATOM 2980 O HOH W 525 13.405 25.640 59.769 1.00 35.69 W O
ATOM 2981 O HOH W 526 14.136 -2.651 39.478 1.00 25.37 W O
ATOM 2982 O HOH W 527 -0.559 10.448 41.081 1.00 28.26 W O
ATOM 2983 O HOH W 528 11.874 17.986 29.888 1.00 25.89 W O
ATOM 2984 O HOH W 529 23.574 32.221 28.092 1.00 37.76 W O
ATOM 2985 O HOH W 530 13.602 23.823 14.354 1.00 34.81 W O
ATOM 2986 O HOH W 531 4.655 16.765 5.856 1.00 30.48 W O
ATOM 2987 O HOH W 532 10.684 -1.459 49.589 1.00 30.96 W O
ATOM 2988 O HOH W 533 23.831 25.701 28.016 1.00 26.03 W O
ATOM 2989 O HOH W 534 9.522 23.683 7.375 1.00 27.36 W O
ATOM 2990 O HOH W 535 8.995 -6.211 47.436 1.00 36.50 W O
ATOM 2991 O HOH W 536 14.421 19.513 19.108 1.00 37.42 W O
ATOM 2992 O HOH W 537 15.054 11.747 47.852 1.00 27.61 W O
ATOM 2993 O HOH W 538 -3.048 15.552 32.864 1.00 20.36 W O
ATOM 2994 O HOH W 539 26.466 24.159 27.298 1.00 45.22 W O
ATOM 2995 O HOH W 540 10.304 -6.018 36.649 1.00 41.64 W O
ATOM 2996 O HOH W 541 5.886 23.115 53.281 1.00 21.05 W O
ATOM 2997 O HOH W 542 16.402 36.077 16.668 1.00 35.16 W O
ATOM 2998 O HOH W 543 7.917 10.981 52.974 1.00 29.07 W O
ATOM 2999 O HOH W 544 13.726 14.563 29.751 1.00 37.11 W O
ATOM 3000 O HOH W 545 7.525 19.318 5.519 1.00 28.60 W O
ATOM 3001 O HOH W 546 12.710 -6.349 30.767 1.00 31.18 W O
ATOM 3002 O HOH W 547 17.183 0.125 22.598 1.00 37.37 W O
ATOM 3003 O HOH W 548 11.035 14.261 29.035 1.00 26.04 W O
ATOM 3004 O HOH W 549 11.680 -11.705 44.903 1.00 47.37 W O
ATOM 3005 O HOH W 550 8.803 -8.483 40.878 1.00 36.78 W O ATOM 3006 O HOH W 551 20.446 38.462 51.517 1.00 30.08 W O
ATOM 3007 O HOH W 552 -6.723 35.101 38.442 1.00 42.46 W O
ATOM 3008 O HOH W 553 0.190 2.110 45.607 1.00 31.03 W O
ATOM 3009 O HOH W 554 0.993 8.445 43.739 1.00 31.92 W O
ATOM 3010 O HOH W 555 22.905 6.519 39.811 1.00 32.70 W O
ATOM 3011 O HOH W 556 4.732 42.091 33.201 1.00 30.40 W O
ATOM 3012 O HOH W 557 15.053 29.779 11.161 1.00 39.23 W O
ATOM 3013 O HOH W 558 17.822 33.633 46.581 1.00 28.06 W O
ATOM 3014 O HOH W 559 3.570 19.502 7.238 1.00 29.19 W O
ATOM 3015 O HOH W 560 11.213 9.604 14.105 1.00 36.12 W O
ATOM 3016 O HOH W 561 15.591 38.178 36.904 1.00 23.49 W O
ATOM 3017 O HOH W 562 17.344 -1.862 38.207 1.00 25.35 W O
ATOM 3018 O HOH W 563 23.551 30.022 29.703 1.00 41.80 W O
ATOM 3019 O HOH W 564 6.011 5.822 6.704 1.00 32.54 W O
ATOM 3020 O HOH W 565 1.106 37.578 46.063 1.00 46.33 W O
ATOM 3021 O HOH W 566 16.296 -4.874 47.940 1.00 43.65 W O
ATOM 3022 O HOH W 567 -9.499 0.560 19.865 1.00 38.41 W O
ATOM 3023 O HOH W 568 -3.567 28.061 7.563 1.00 44.72 W O
ATOM 3024 O HOH W 569 0.892 37.495 33.854 1.00 35.48 W O
ATOM 3025 O HOH W 570 0.643 16.338 38.982 1.00 25.93 W O
ATOM 3026 O HOH W 571 6.284 34.843 50.253 1.00 39.54 W O
ATOM 3027 O HOH W 572 1.059 27.878 6.906 1.00 35.28 W O
ATOM 3028 O HOH W 573 2.775 19.556 35.791 1.00 33.85 W O
ATOM 3029 O HOH W 574 13.648 -5.104 38.935 1.00 36.40 W O
ATOM 3030 O HOH W 575 26.227 14.124 30.407 1.00 42.26 W O
ATOM 3031 O HOH W 576 -7.176 13.270 8.218 1.00 32.68 W O
ATOM 3032 O HOH W 577 2.149 13.790 53.150 1.00 35.35 W O
ATOM 3033 O HOH W 578 20.699 20.010 24.218 1.00 32.56 W O
ATOM 3034 O HOH W 579 13.167 21.516 10.462 1.00 32.70 W O
ATOM 3035 O HOH W 580 -3.546 3.757 37.894 1.00 26.55 W O
ATOM 3036 O HOH W 581 22.270 16.752 24.422 1.00 34.25 W O
ATOM 3037 ■ O HOH W 582 10.973 37.540 49.029 1.00 37.16 W O
ATOM 3038 O HOH W 583 17.797 0.549 43.261 1.00 31.04 W O
ATOM 3039 O HOH W 584 22.474 36.886 19.103 1.00 37.33 W O
ATOM 3040 O HOH W 585 -0.097 13.113 38.497 1.00 23.71 W O
ATOM 3041 O HOH W 586 18.502 -1.812 44.953 1.00 40.92 W O
ATOM 3042 O HOH W 587 17.107 25.197 14.025 1.00 40.70 W O
ATOM 3043 O HOH W 588 9.199 12.356 8.422 1.00 37.30 W O
ATOM 3044 O HOH W 589 3.027 33.922 50.857 1.00 39.66 W O
ATOM 3045 O HOH W 590 15.057 7.137 19.063 1.00 42.83 W O
ATOM 3046 O HOH W 591 19.454 4.381 44.812 1.-00 29.16 W O
ATOM 3047 O HOH W 592 15.102 17.412 14.050 1.00 35.36 W O
ATOM 3048 O HOH W 593 24.437 6.890 29.778 1.00 45.67 W O
ATOM 3049 O HOH W 594 0.179 4.396 52.443 1.00 43.27 W O
ATOM 3050 O HOH W 595 7.895 -2.252 21.358 1.00 27.61 W O
ATOM 3051 O HOH W 596 13.576 40.664 36.855 1.00 36.44 W O
ATOM 3052 O HOH W 597 22.566 17.911 45.186 1.00 42.64 W O
ATOM 3053 O HOH W 598 11.722 -6.868 39.269 1.00 25.17 W O
ATOM 3054 O HOH W 599 -1.805 3.900 9.492 1.00 39.43 W O
ATOM 3055 O HOH W 600 -9.258 25.217 7.679 1.00 39.30 W O
ATOM 3056 O HOH W 601 -2.060 6.101 47.584 1.00 43.73 W O
ATOM 3057 O HOH W 602 13.597 -3.462 50.301 1.00 35.13 W O
ATOM 3058 O HOH W 603 22.023 4.325 26.082 1.00 46.13 W O
ATOM 3059 O HOH W 604 25.841 16.401 41.584 1.00 41.58 W O
ATOM 3060 O HOH W 605 2.134 2.591 11.344 1.00 34.74 W O
ATOM 3061 O HOH W 606 10.295 35.676 11.867 1.00 35.33 W O
ATOM 3062 O HOH W 607 12.569 6.774 13.849 1.00 51.40 W O
ATOM 3063 O HOH W 608 11.133 -4.806 32.098 1.00 32.33 W O
ATOM 3064 O HOH W 609 1.602 14.935 37.380 1.00 35.23 W O
ATOM 3065 O HOH W 610 -4.279 16.702 35.319 1.00 30.01 W O
ATOM 3066 O HOH W 611 -1.171 21.883 29.242 1.00 35.64 W O
ATOM 3067 O HOH W 612 13.990 23.562 21.893 1.00 34.34 W O
ATOM 3068 O HOH W 613 -2.454 31.709 12.076 1.00 33.98 W O
ATOM 3069 O HOH W 614 4.079 "21.950 49.627 1.00 29.43 W O
ATOM 3070 O HOH W 615 7.440 37.569 43.180 1.00 32.37 W O
ATOM 3071 O HOH W 616 14.664 31.746 13.719 1.00 46.05 W O
ATOM 3072 O HOH W 617 16.963 34.164 41.354 1.00 46.28 W O
ATOM 3073 O HOH W 618 20.441 30.863 47.323 1.00 28.64 W O
ATOM 3074 O HOH W 619 3.298 41.136 35.590 1.00 32.39 W O
ATOM 3075 O HOH W 620 11.620 20.242 32.567 1.00 37.27 W O
ATOM 3076 O HOH W 621 2.104 6.433 9.090 1.00 37.17 W O
ATOM 3077 O HOH W 622 11.632 25.694 29.721 1.00 40.17 W O
ATOM 3078 O HOH W 623 24.930 35.364 18.336 1.00 42.44 W O
ATOM 3079 O HOH W 624 11.072 31.310 6.268 1.00 47.04 W O
ATOM 3080 O HOH W 625 2.032 18.577 38.041 1.00 44.99 W O
ATOM 3081 O HOH W 626 -7.041 2.975 12.044 1.00 42.47 W O
ATOM 3082 O HOH W 627 17.119 35.367 43.676 1.00 40.23 W O ATOM 3083 O HOH W 628 -2.326 1.340 41.994 1.00 38.22 W O
ATOM 3084 O HOH W 629 19.613 22.870 20.353 1.00 38.78 W O
ATOM 3085 O HOH W 630 19.038 31.505 42.870 1.00 41.57 W O
ATOM 3086 O HOH W 631 17.971 29.026 17.682 1.00 43.85 W O
ATOM 3087 O HOH W 632 8.060 38.055 46.930 1.00 39.91 W O
ATOM 3088 O HOH W 633 22.529 40.626 51.428 1.00 40.37 W O
ATOM 3089 O HOH W 634 9.855 38.379 42.281 1.00 40.98 W O
ATOM 3090 O HOH W 635 -4.921 26.267 6.886 1.00 52.88 W O
ATOM 3091 O HOH W 636 19.018 -3.109 33.413 1.00 45.33 W O
ATOM 3092 O HOH W 637 22.370 4.542 41.470 1.00 54.11 W O
ATOM 3093 O HOH W 638 15.624 -6.953 35.910 1.00 47.75 W O
ATOM 3094 O HOH W 639 16.342 20.779 25.945 1.00 51.16 W O
ATOM 3095 O HOH W 640 8.014 9.706 59.764 1.00 59.45 W O
ATOM 3096 O HOH W 641 -9.569 -4.370 38.210 1.00 48.24 W O
ATOM 3097 O HOH W 642 5.988 -1.958 17.436 1.00 33.06 W O
ATOM 3098 O HOH W 643 11.819 25.963 7.395 1.00 39.21 W O
ATOM 3099 O HOH W 644 18.785 -6.639 45.425 1.00 35.14 W O
ATOM 3100 O HOH W 645 10.395 8.906 59.308 1.00 42.40 W O
ATOM 3101 O HOH W 646 28.144 6.166 43.834 1.00 35.24 W O
ATOM 3102 O HOH W 647 23.063 42.296 53.745 1.00 42.90 W O
ATOM 3103 O HOH W 648 18.326 2.714 52.130 1.00 49.32 W O
ATOM 3104 O HOH W 649 16.565 26.338 8.544 1.00 49.54 W O
ATOM 3105 O HOH W 650 0.873 42.487 35.316 1.00 40.44 W O
ATOM 3106 O HOH W 651 15.257 17.632 24.499 1.00 49.51 W O
ATOM 3107 O HOH W 652 17.092 4.440 45.766 1.00 37.57 W O
ATOM 3108 O HOH W 653 16.099 4.734 20.050 1.00 50.63 W O
ATOM 3109 O HOH W 654 16.870 29.108 15.406 1.00 42.53 W O
ATOM 3110 O HOH W 655 -9.873 35.388 9.432 1.00 38.89 W O
ATOM 3111 O HOH W 656 8.251 6.983 5.454 1.00 45.19 W O
ATOM 3112 O HOH W 657 25.180 20.518 42.407 1.00 26.36 W O
ATOM 3113 O HOH W 658 -6.439 9.600 8.076 1.00 27.09 W O
ATOM 3114 O HOH W 659 10.775 40.056 19.080 1.00 21.39 W O
ATOM 3115 O HOH W 660 5.540 34.489 40.294 1.00 24.10 W O
ATOM 3116 O HOH W 661 11.134 10.530 52.732 1.00 33.63 W O
ATOM 3117 O HOH W 662 24.273 16.938 39.624 1.00 40.25 W O
ATOM 3118 O HOH W 663 9.177 40.282 39.507 1.00 38.26 W O
ATOM 3119 O HOH W 664 14.991 36.141 39.669 1.00 40.90 W O
ATOM 3120 O HOH W 665 4.616 26.047 52.983 1.00 38.73 W O
ATOM 3121 O HOH W 666 20.658 33.371 44.069 1.00 43.02 W O
ATOM 3122 O HOH W 667 -7.286 34.675 33.577 1.00 45.34 W O
ATOM 3123 O HOH W 668 -4.076 24.122 5.901 1.00 37.43 W O
ATOM 3124 O HOH W 669 5.059 9.172 59.435 1.00 36.89 W O
ATOM 3125 O HOH W 670 -7.555 0.456 12.166 1.00 41.23 W O
ATOM 3126 O HOH W 671 13.735 10.714 53.701 1.00 38.21 W O
ATOM 3127 O HOH W 672 1.374 -5.703 53.202 1.00 42.29 W O
ATOM 3128 O HOH W 673 30.739 5.755 42.220 1.00 39.67 W O
ATOM 3129 O HOH W 674 3.067 -7.687 52.071 1.00 51.26 W O
ATOM 3130 O HOH W 675 6.265 18.509 58.957 1.00 42.84 W O
ATOM 3131 O HOH W 676 8.303 19.925 58.325 1.00 40.51 W O
ATOM 3132 O HOH W 677 6.795 22.048 57.837 1.00 38.53 W O
ATOM 3133 O HOH W 678 6.131 -6.519 52.559 1.00 44.08 W O
ATOM 3134 02 NDS B 679 18.194 15.192 17.891 1.00 52.24 B O
ATOM 3135 Sl NDS B 679 16.774 15.110 18.331 1.00 52.77 B S
ATOM 3136 03 NDS B 679 16.118 13.879 17.757 1.00 46.50 B O
ATOM 3137 Ol NDS B 679 16.100 16.368 17.901 1.00 50.36 B O
ATOM 3138 C4 NDS B 679 16.807 15.034 20.012 1.00 48.17 B C
ATOM 3139 C3 NDS B 679 17.167 16.393 20.621 1.00 46.74 B C
ATOM 3140 C2 NDS B 679 16.685 16.503 22.061 1.00 46.57 B C
ATOM 3141 Nl NDS B 679 16.937 17.763 22.822 1.00 46.19 B N
ATOM 3142 Cl NDS B 679 16.812 17.450 24.253 1.00 44.08 B C
ATOM 3143 C7 NDS B 679 18.277 18.328 22.586 1.00 46.25 B C
ATOM 3144 C5 NDS B 679 15.869 18.719 22.523 1.00 47.33 B C
ATOM 3145 C6 NDS B 679 16.394 19.814 21.613 1.00 50.94 B C
END
Atomic Co-ordinates for refmac17
HEADER XX-XXX-XX COMPND REMARK REMARK REFINEMENT . REMARK PROGRAM REFMAC 5.2.0019 REMARK AUTHORS MORSHUDOV, VAGIN, DODSON REMARK REMARK REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK REMARK DATA USED IN REFINEMENT. REMARK RESOLUTION RANGE HIGH (ANGSTROMS) 2.75 REMARK RESOLUTION RANGE LOW (ANGSTROMS) 50.00 REMARK DATA CUTOFF (SIGMA(F)) NONE REMARK COMPLETENESS FOR RANGE (%) 95.92 REMARK NUMBER OF REFLECTIONS 11058 REMARK REMARK FIT TO DATA USED IN REFINEMENT. REMARK CROSS-VALIDATION METHOD THROUGHOUT REMARK FREE R VALUE TEST SET SELECTION RANDOM REMARK R VALUE (WORKING + TEST SET) 0.19640 REMARK R VALUE (WORKING SET) 0.19359 REMARK FREE R VALUE 0.25563 REMARK FREE R VALUE TEST SET SIZE (%) 4.7 REMARK FREE R VALUE TEST SET COUNT 544 REMARK REMARK FIT IN THE HIGHEST RESOLUTION BIN. REMARK TOTAL NUMBER OF BINS USED 20 REMARK BIN RESOLUTION RANGE HIGH 2.750 REMARK BIN RESOLUTION RANGE LOW 2.821 REMARK REFLECTION IN BIN (WORKING SET) 816 REMARK BIN COMPLETENESS (WORKING+TEST) (%) 98.84 REMARK BIN R VALUE (WORKING SET) 0.302 REMARK BIN FREE R VALUE SET COUNT 37 REMARK BIN FREE R VALUE 0.347 REMARK REMARK NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK ALL ATOMS : 3029 REMARK REMARK B VALUES. REMARK FROM WILSON PLOT (A**2) NULL REMARK MEAN B VALUE (OVERALL, A**2) 27.793 REMARK OVERALL ANISOTROPIC B VALUE. REMARK BIl (A**2) 1.31 REMARK B22 (A**2) -2.07 REMARK B33 (A**2) 0.76 REMARK B12 (A**2) 0.00 REMARK B13 (A**2) 0.00 REMARK B23 (A**2) 0.00 REMARK REMARK ESTIMATED OVERALL COORDINATE ERROR. REMARK ESU BASED ON R VALUE (A) NULL REMARK ESU BASED ON FREE R VALUE (A) 0.379 REMARK ESU BASED ON MAXIMUM LIKELIHOOD (A) 0.245 REMARK ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2) 12.566 REMARK REMARK CORRELATION COEFFICIENTS. REMARK CORRELATION COEFFICIENT FO-FC : 0.934 REMARK CORRELATION COEFFICIENT FO-FC FREE : 0.889 REMARK REMARK RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK BOND LENGTHS REFINED ATOMS (A) 3028 008 0.021 REMARK BOND LENGTHS OTHERS (A) 2059 001 0.020 REMARK BOND ANGLES REFINED ATOMS (DEGREES) 4102 107 1.930 REMARK BOND ANGLES OTHERS (DEGREES) 4992 816 3.000 REMARK TORSION ANGLES, PERIOD 1 (DEGREES) 363 410 5.000 REMARK TORSION ANGLES, PERIOD 2 (DEGREES) 149 36.539 23.758 REMARK TORSION ANGLES, PERIOD 3 (DEGREES) 517 15.572 15.000 REMARK TORSION ANGLES, PERIOD 4 (DEGREES) 20 18.823 15.000 REMARK CHIRAL-CENTER RESTRAINTS (A**3) 439 0.067 0.200 REMARK GENERAL PLANES REFINED ATOMS (A) 3359 0.003 0.020 REMARK GENERAL PLANES OTHERS (A) 638 0.001 0 . 020 REMARK NON-BONDED CONTACTS REFINED ATOMS (A) 596 0.185 0 .200 REMARK NON-BONDED CONTACTS OTHERS (A) 2244 0.191 0 . 200 REMARK NON-BONDED TORSION REFINED ATOMS (A) 1435 0.179 0 . 200 REMARK NON-BONDED TORSION OTHERS (A) 1641 085 0 . 200 REMARK H-BOND (X... Y) REFINED ATOMS (A) 144 154 0 .200 REMARK SYMMETRY VDW REFINED ATOMS (A) 28 143 0 . 200 REMARK SYMMETRY VDW OTHERS (A) 64 203 0 .200 REMARK SYMMETRY H-BOND REFINED ATOMS (A) 6 248 0 .200 REMARK REMARK ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK MAIN-CHAIN BOND REFINED ATOMS <A**2) 2344 0.604 500 REMARK MAIN-CHAIN BOND OTHER ATOMS (A**2) 735 0.054 ,500 REMARK MAIN-CHAIN ANGLE REFINED ATOMS (A**2) 2935 0.678 ,000 REMARK SIDE-CHAIN BOND REFINED ATOMS (A**2) 1446 0.745 ,000 REMARK SIDE-CHAIN ANGLE REFINED ATOMS (A**2) 1167 1.193 4.500 REMARK REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3
CRYSTl 57. 739 84.977 90." 710 90.00 90.00 90.00 P 21 21 21
SCALEl 0.017319 0 .000000 0.000000 0.00000
SCALE2 0.000000 0 .011768 0.000000 0.00000
SCALE3 0.000000 0 .000000 0.011024 0.00000
ATOM 1 N TYR A 80 -17.815 13.035 17.934 1.00 50.23 N
ATOM 2 CA TYR A 80 -17.064 12.828 19.209 1.00 50.23 C
ATOM 4 CB TYR A 80 -17.981 12.228 20.286 1.00 50.87 C
ATOM 7 CG TYR A 80 -18.453 10.813 20.003 1.00 51.50 C
ATOM 8 CDl TYR A 80 -19.616 10.576 19.264 1.00 51.79 C
ATOM 10 CEl TYR A 80 -20.051 9.278 19.008 1.00 51.64 C
ATOM 12 CZ TYR A 80 -19.324 8.201 19.499 1.00 51.71 C
ATOM 13 OH TYR A 80 -19.742 6.917 19.253 1.00 51.68 O
ATOM 15 CE2 TYR A 80 -18.173 8.407 20.242 1.00 51.83 C
ATOM 17 CD2 TYR A 80 -17.744 9.707 20.492 1.00 52.00 C
ATOM 19 C TYR A 80 -15.781 11.980 19.016 1.00 50.04 C
ATOM 20 O TYR A 80 -15.208 11.468 19.990 1.00 50.06 O
ATOM 24 N SER A 81 -15.353 11.844 17.757 1.00 49.42 N
ATOM 25 CA SER A 81 -13.999 11.401 17.396 1.00 48.74 C
ATOM 27 CB SER A 81 -14.065 10.300 16.342 1.00 48.84 C
ATOM 30 OG SER A 81 -14.633 10.795 15.140 1.00 48.60 O
ATOM 32 C SER A 81 -13.256 12.610 16.835 1.00 48.18 C
ATOM 33 O SER A 81 -13.821 13.701 16.782 1.00 48.53 O
ATOM 35 N PHE A 82 -12.014 12.429 16.394 1.00 47.33 N
ATOM 36 CA PHE A 82 -11.197 13.567 15.967 1.00 46.78 C
ATOM 38 CB PHE A 82 -9.787 13.464 16.540 1.00 46.62 C
ATOM 41 CG PHE A 82 -9.717 13.776 18.001 1.00 46.17 C
ATOM 42 CDl PHE A 82 -9.854 15.076 18.444 1.00 46.23 C
ATOM 44 CEl PHE A 82 -9.798 15.373 19.793 1.00 46.78 C
ATOM 46 CZ PHE A 82 -9.603 14.357 20.716 1.00 46.54 C
ATOM 48 CE2 PHE A 82 -9.468 13.057 20.282 1.00 46.14 C
ATOM 50 CD2 PHE A 82 -9.528 12.771 18.932 1.00 45.94 C
ATOM 52 C PHE A 82 -11.131 13.764 14.457 1.00 46.33 C
ATOM 53 O PHE A 82 -10.945 12.809 13.705 1.00 46.24 O
ATOM 55 N LYS A 83 -11.267 15.026 14.045 1.00 45.95 N
ATOM 56 CA LYS A 83 -11.215 15.457 12.646 1.00 45.32 C
ATOM 58 CB LYS A 83 -12.606 15.965 12.228 1.00 45.67 C
ATOM 61 CG LYS A 83 -12.717 16.587 10.812 1.00 46.62 C
ATOM 64 CD LYS A 83 -12.580 15.539 9.684 1.00 48.22 C
ATOM 67 CE LYS A 83 -13.801 14.597 9.592 1.00 48.20 C
ATOM 70 NZ LYS A 83 -13.737 13.690 8.410 1.00 47.66 N
ATOM 74 C LYS A 83 -10.169 16.578 12.484 1.00 44.57 C
ATOM 75 O LYS A 83 -10.239 17.604 13.161 1.00 44.32 O
ATOM 77 N CYS A 84 -9.202 16.372 11.593 1.00 43.77 N
ATOM 78 CA CYS A 84 -8.186 17.384 11.299 1.00 43.23 C
ATOM 80 CB CYS A 84 -7.150 16.822 10.319 1.00 43.12 C
ATOM 83 SG CYS A 84 -5.700 17.862 10.012 1.00 43.84 S
ATOM 85 C CYS A 84 -8.900 18.579 10.694 1.00 42.47 C
ATOM 86 O CYS A 84 -9.567 18.427 9.684 1.00 42.35 O
ATOM 88 N VAL A 85 -8.796 19.749 11.327 1.00 41.85 N
ATOM 89 CA VAL A 85 -9.557 20.938 10.892 1.00 41.41 C
ATOM 91 CB VAL A 85 -10.524 21.455 11.990 1.00 41.17 C
ATOM 93 CGl VAL A 85 -11.535 20.377 12.357 1.00 40.77 C
ATOM 97 CG2 VAL A 85 -9.762 21.932 13.220 1.00 41.13 C
ATOM 101 C VAL A 85 -8.711 22.115 10.398 1.00 41.05 C
ATOM 102 O VAL A 85 -9.250 23.050 9.821 1.00 41.19 O
ATOM 104 N ASN A 86 -7.401 22.076 10.614 1.00 40.63 N
ATOM 105 CA ASN A 86 -6.524 23.163 10.200 1.00 40.27 C
ATOM 107 CB ASN A 86 -6.866 24.447 10.961 1.00 40.25 C
ATOM 110 CG ASN A 86 -6.333 25.706 10.284 1.00 40.42 C ATOM 111 ODl ASN A 86 -5.621 25.649 9.278 1.00 40.47 O
ATOM 112 ND2 ASN A 86 -6.684 26.856 10.842 1.00 39.49 N
ATOM 115 C ASN A 86 -5.074 22.815 10.472 1.00 39.98 C
ATOM 116 O ASN A 86 -4.770 21.959 11.303 1.00 39.94 O
ATOM 118 N SER A 87 -4.179 23.491 9.770 1.00 39.75 N
ATOM 119 CA SER A 87 -2.766 23.375 10.037 1.00 39.69 C
ATOM 121 CB SER A 87 -2.172 22.205 9.258 1.00 39.80 C
ATOM 124 OG SER A 87 -1.959 22.543 7.902 1.00 39.54 O
ATOM 126 C SER A 87 -2.087 24.658 9.635 1.00 39.60 C
ATOM 127 O SER A 87 -2.658 25.453 8.890 1.00 39.78 O
ATOM 129 N LEϋ A 88 -0.879 24.868 10.145 1.00 39.50 N
ATOM 130 CA LEU A 88 -0.049 25.988 9.713 1.00 39.55 C
ATOM 132 CB LEϋ A 88 -0.552 27.312 10.298 1.00 39.45 C
ATOM 135 CG LEϋ A 88 -0.571 27.521 11.811 1.00 39.62 C
ATOM 137 CDl LEϋ A 88 0.759 28.089 12.297 1.00 39.44 C
ATOM 141 CD2 LEU A 88 -1.710 28.462 12.188 1.00 39.45 C
ATOM 145 C LEU A 88 1.406 25.743 10.071 1.00 39.64 C
ATOM 146 O LEU A 88 1.714 24.799 10.792 1.00 39.88 O
ATOM 148 N LYS A 89 2.297 26.584 9.552 1.00 39.68 N
ATOM 149 CA LYS A 89 3.733 26.437 9.788 1.00 39.61 C
ATOM 151 CB LYS A 89 4.411 25.938 8.511 1.00 39.63 C
ATOM 154 CG LYS A 89 5.765 25.268 8.727 1.00 40.01 C
ATOM 157 CD LYS A 89 6.494 25.012 7.395 1.00 40.55 C
ATOM 160 CE LYS A 89 5.757 24.008 6.496 1.00 41.37 C
ATOM 163 NZ LYS A 89 5.537 22.693 7.175 1.00 41.91 N
ATOM 167 C LYS A 89 4.357 27.760 10.268 1.00 39.47 C
ATOM 168 O LYS A 89 3.848 28.841 9.972 1.00 39.60 O
ATOM 170 N GLU A 90 5.445 27.660 11.027 1.00 39.17 N
ATOM 171 CA GLU A 90 6.143 28.831 11.556 1.00 38.79 C
ATOM 173 CB GLU A 90 6.571 28.577 13.002 1.00 38.61 C
ATOM 176 CG GLU A 90 5.398 28.286 13.932 1.00 37.87 C
ATOM 179 CD GLU A 90 5.718 28.489 15.411 1.00 37.54 C
ATOM 180 OEl GLU A 90 6.885 28.764 15.753 1.00 35.56 O
ATOM 181 OE2 GLU A 90 4.790 28.372 16.235 1.00 35.13 O
ATOM 182 C GLU A 90 7.350 29.179 10.675 1.00 38.90 C
ATOM 183 O GLU A 90 8.017 28.287 10.144 1.00 39.00 O
ATOM 185 N ASP A 91 7.628 30.475 10.527 1.00 38.90 N
ATOM 186 CA ASP A 91 8.616 30.941 9.543 1.00 38.89 C
ATOM 188 CB ASP A 91 8.616 32.485 9.399 1.00 39.04 C
ATOM 191 CG ASP A 91 8.905 33.226 10.710 1.00 40.02 C
ATOM 192 ODl ASP A 91 9.889 32.885 11.398 1.00 41.12 O
ATOM 193 OD2 ASP A 91 8.159 34.178 11.042 1.00 40.80 O
ATOM 194 C ASP A 91 10.022 30.381 9.793 1.00 38.77 C
ATOM 195 O ASP A 91 10.678 29.932 8.860 1.00 39.01 O
ATOM 197 N HIS A 92 10.459 30.367 11.051 1.00 38.64 N
ATOM 198 CA HIS A 92 11.803 29.883 11.409 1.00 38.48 C
ATOM 200 CB HIS A 92 11.971 29.814 12.932 1.00 38.35 C
ATOM 203 CG HIS A 92 10.920 28.996 13.611 1.00 38.52 C
ATOM 204 NDl HIS A 92 10.904 27.620 13.568 1.00 38.02 N
ATOM 206 CEl HIS A 92 9.854 27.173 14.231 1.00 38.95 C
ATOM 208 NE2 HIS A 92 9.191 28.210 14.709 1.00 39.36 N
ATOM 210 CD2 HIS A 92 9.834 29.362 14.332 1.00 39.05 C
ATOM 212 C HIS A 92 12.144 28.519 10.796 1.00 38.43 C
ATOM 213 O HIS A 92 13.318 28.206 10.601 1.00 38.31 O
ATOM 215 N ASN A 93 11.117 27.711 10.525 1.00 38.30 N
ATOM 216 CA ASN A 93 11.275 26.375 9.944 1.00 38.19 C
ATOM 218 CB ASN A 93 11.781 26.477 8.503 1.00 38.30 C
ATOM 221 CG ASN A 93 10.654 26.655 7.512 1.00 39.47 C
ATOM 222 ODl ASN A 93 9.703 25.863 7.487 1.00 41.06 O
ATOM 223 ND2 ASN A 93 10.751 27.692 6.679 1.00 39.88 N
ATOM 226 C ASN A 93 12.126 25.378 10.751 1.00 37.99 C
ATOM 227 O ASN A 93 12.456 24.303 10.251 1.00 38.17 O
ATOM 229 N GLN A 94 12.459 25.722 11.994 1.00 37.61 N
ATOM 230 CA GLN A 94 13.093 24.781 12.918 1.00 37.21 C
ATOM 232 CB GLN A 94 13.891 25.527 13.996 1.00 37.48 C
ATOM 235 CG GLN A 94 14.908 26.539 13.452 1.00 37.99 C
ATOM 238 CD GLN A 94 15.689 26.005 12.256 1.00 39.04 C
ATOM 239 OEl GLN A 94 16.666 25.267 12.408 1.00 39.44 O
ATOM 240 NE2 GLN A 94 15.255 26.378 11.058 1.00 39.35 N
ATOM 243 C GLN A 94 12.021 23.912 13.566 1.00 36.73 C
ATOM 244 O GLN A 94 10.835 24.236 13.507 1.00 36.79 O
ATOM 246 N PRO A 95 12.426 22.782 14.160 1.00 36.06 N
ATOM 247 CA PRO A 95 11.453 21.943 14.843 1.00 35.63 C
ATOM 249 CB PRO A 95 12.305 20.778 15.375 1.00 35.81 C
ATOM 252 CG PRO A 95 13.522 20.774 14.553 1.00 35.85 C
ATOM 255 CD PRO A 95 13.776 22.195 14.202 1.00 36.04 C
ATOM 258 C PRO A 95 10.756 22.642 16.011 1.00 35.16 C ATOM 259 O PRO A 95 11.407 23.324 16.813 1.00 35.29 O
ATOM 260 N LEU- A 96 9.441 22.465 16.093 1.00 34.37 N
ATOM 261 CA LED A 96 8.690 22.814 17.291 1.00 33.82 C
ATOM 263 CB LEU A 96 7.219 23.084 16.949 1.00 33.65 C
ATOM 266 CG LEU A 96 6.934 24.336 16.105 1.00 33.11 C
ATOM 268 CDl LEU A 96 5.507 24.321 15.582 1.00 32.17 C
ATOM 272 CD2 LEU A 96 7.213 25.618 16.882 1.00 32.38 C
ATOM 276 C LEU A 96 8.816 21.650 18.287 1.00 33.45 C
ATOM 277 O LEU A 96 8.365 20.537 18.017 1.00 33.54 O
ATOM 279 N PHE A 97 9.444 21.910 19.430 1.00 32.85 N
ATOM 280 CA PHE A 97 9.748 20.864 20.401 1.00 32.32 C
ATOM 282 CB PHE A 97 11.082 21.159 21.093 1.00 32.48 C
ATOM 285 CG PHE A 97 12.284 20.886 20.231 1.00 32.86 C
ATOM 286 CDl PHE A 97 12.531 19.604 19.746 1.00 33.18 C
ATOM 288 CEl PHE A 97 13.635 19.348 18.954 1.00 32.61 C
ATOM 290 CZ PHE A 97 14.516 20.373 18.648 1.00 32.52 C
ATOM 292 CE2 PHE A 97 14.290 21.645 19.128 1.00 32.56 C
ATOM 294 CD2 PHE A 97 13.178 21.900 19.916 1.00 32.94 C
ATOM 296 C PHE A 97 8.670 20.686 21.463 1.00 31.89 C
ATOM 297 O PHE A 97 8.624 19.654 22.133 1.00 32.14 O
ATOM 299 N GLY A 98 7.821 21.690 21.643 1.00 31.10 N
ATOM 300 CA GLY A 98 6.808 21.629 22.684 1.00 30.37 C
ATOM 303 C GLY A 98 5.552 22.372 22.304 1.00 29.74 C
ATOM 304 O GLY A 98 5.594 23.309 21.515 1.00 29.81 O
ATOM 306 N VAL A 99 4.429 21.932 22.853 1.00 28.89 N
ATOM 307 CA VAL A 99 3.187 22.664 22.735 1.00 28.55 C
ATOM 309 CB VAL A 99 2.365 22.206 21.509 1.00 28.66 C
ATOM 311 CGl VAL A 99 2.102 20.696 21.544 1.00 28.16 C
ATOM 315 CG2 VAL A 99 1.060 22.998 21.422 1.00 28.81 C
ATOM 319 C VAL A 99 2.397 22.480 24.018 1.00 27.98 C
ATOM 320 O VAL A 99 2.339 21.385 24.553 1.00 28.20 O
ATOM 322 N GLN A 100 1.820 23.555 24.533 1.00 27.51 N
ATOM 323 CA GLN A 100 1.031 23.480 25.760 1.00 27.29 C
ATOM 325 CB GLN A 100 1.856 23.939 26.958 1.00 27.19 C
ATOM 328 CG GLN A 100 3.069 23.086 27.276 1.00 27.38 C
ATOM 331 CD GLN A 100 2.731 21.737 27.885 1.00 26.82 C
ATOM 332 OEl GLN A 100 1.596 21.475 28.303 1.00 25.14 O
ATOM 333 NE2 GLN A 100 3.734 20.872 27.949 1.00 27.19 N
ATOM 336 C GLN A 100 -0.214 24.349 25.685 1.00 26.78 C
ATOM 337 O GLN A 100 -0.130 25.549 25.431 1.00 26.27 O
ATOM 339 N PHE A 101 -1.368 23.738 25.906 1.00 26.41 N
ATOM 340 CA PHE A 101 -2.561 24.506 26.152 1.00 26.53 C
ATOM 342 CB PHE A 101 -3.809 23.644 26.083 1.00 26.05 C
ATOM 345 CG PHE A 101 -4.430 23.600 24.731 1.00 25.73 C
ATOM 346 CDl PHE A 101 -5.224 24.643 24.294 1.00 24.95 C
ATOM 348 CEl PHE A 101 -5.804 24.606 23.041 1.00 25.31 C
ATOM 350 CZ PHE A 101 -5.595 23.512 22.212 1.00 25.29 C
ATOM 352 CE2 PHE A 101 -4.807 22.465 22.640 1.00 25.25 C
ATOM 354 CD2 PHE A 101 -4.226 22.512 23.891 1.00 25.73 C
ATOM 356 C PHE A 101 -2.454 25.091 27.528 1.00 26.74 C
ATOM 357 O PHE A 101 -1.843 24.504 28.409 1.00 26.69 O
ATOM 359 N ASN A 102 -3.060 26.258 27.696 1.00 27.52 N
ATOM 360 CA ASN A 102 -3.215 26.887 28.996 1.00 28.07 C
ATOM 362 CB ASN A 102 -3.276 28.397 28.812 1.00 27.70 C
ATOM 365 CG ASN A 102 -3.529 29.128 30.094 1.00 27.36 C
ATOM 366 ODl ASN A 102 -2.983 28.780 31.139 1.00 27.53 O
ATOM 367 ND2 ASN A 102 -4.362 30.159 30.027 1.00 25.62 N
ATOM 370 C ASN A 102 -4.493 26.375 29.677 1.00 28.82 C
ATOM 371 O ASN A 102 -5.596 26.821 29.354 1.00 28.89 O
ATOM 373 N TRP A 103 -4.344 25.442 30.615 1.00 29.76 N
ATOM 374 CA TRP A 103 -5.489 24.896 31.362 1.00 30.45 C
ATOM " 376 CB TRP A 103 -5.173 23.494 31.899 1.00 29.87 C
ATOM 379 CG TRP A 103 -5.068 22.441 30.864 1.00 29.37 C
ATOM 380 CDl TRP A 103 -5.441 22.531 29.560 1.00 29.50 C
ATOM 382 NEl TRP A 103 -5.206 21.346 28.914 1.00 29.34 N
ATOM 384 CE2 TRP A 103 -4.694 20.450 29.809 1.00 29.43 C
ATOM 385 CD2 TRP A 103 -4.596 21.108 31.052 1.00 29.40 C
ATOM 386 CE3 TRP A 103 -4.093 20.404 32.150 1.00 29.27 C
ATOM 388 CZ3 TRP A 103 -3.708 19.090 31.975 1.00 29.35 C
ATOM 390 CH2 TRP A 103 -3.817 18.463 30.725 1.00 29.63 C
ATOM 392 CZ2 TRP A 103 -4.308 19.126 29.632 1.00 29.41 C
ATOM 394 C TRP A 103 -5.932 25.789 32.521 1.00 31.37 C
ATOM 395 O TRP A 103 -6.844 25.435 33.256 1.00 31.26 O
ATOM 397 N HIS A 104 -5.288 26.939 32.690 1.00 32.85 N
ATOM 398 CA HIS A 104 -5.688 27.906 33.705 1.00 33.99 C
ATOM 400 CB HIS A 104 -4.458 28.481 34.387 1.00 33.86 C
ATOM 403 CG HIS A 104 -3.431 27.451 34.718 1.00 34.21 C ATOM 404 NDl HIS A 104 -3.471 26.705 35.876 1.00 33.91 N
ATOM 406 CEl HIS A 104 -2.450 25.868 35.891 1.00 34.37 C
ATOM 408 NE2 HIS A 104 -1.755 26.038 34.780 1-.00 34.84 N
ATOM 410 CD2 HIS A 104 -2.349 27.021 34.028 1.00 34.31 C
ATOM 412 C HIS A 104 -6.501 29.040 33.094 1.00 35.33 C
ATOM 413 O HIS A 104 -6.822 30.010 33.784 1.00 35.91 O
ATOM 415 N SER A 105 -6.835 28.933 31.806 1.00 36.64 N
ATOM 416 CA SER A 105 -7.583 29.996 31.139 1.00 37.49 C
ATOM 418 CB SER A 105 -7.657 29.788 29.610 1.00 37.62 C
ATOM 421 OG SER A 105 -8.735 28.954 29.222 1.00 37.71 O
ATOM 423 C SER A 105 -8.966 30.079 31.783 1.00 38.54 C
ATOM 424 O SER A 105 -9.531 29.060 32.192 1.00 38.72 O
ATOM 426 N LYS A 106 -9.484 31.303 31.888 1.00 39.81 N
ATOM 427 CA LYS A 106 10.709 31.580 32.636 1.00 40.13 C
ATOM 429 CB LYS A 106 10.742 33.058 33.035 1.00 40.36 C
ATOM 432 CG LYS A 106 11.793 33.416 34.107 1.00 40.73 C
ATOM 435 CD LYS A 106 11.671 34.886 34.563 1.00 40.82 C
ATOM 438 CE LYS A 106 11.730 35.875 33.384 1.00 41.17 C
ATOM 441 NZ LYS A 106 11.704 37.298 33.837 1.00 41.57 N
ATOM 445 C LYS A 106 11.968 31.223 31.842 1.00 40.64 C
ATOM 446 O LYS A 106 11.970 31.209 30.600 1.00 40.48 O
ATOM 448 N GLO A 107 13.036 30.934 32.583 1.00 41.28 N
ATOM 449 CA GLU A 107 14.363 30.676 32.003 1.00 41.40 C
ATOM 451 CB GLO A 107 15.438 30.678 33.106 1.00 41.59 C
ATOM 454 CG GLU A 107 16.837 30.218 32.662 1.00 41.75 C
ATOM 457 CD GLU A 107 17.879 30.253 33.802 1.00 42.45 C
ATOM 458 OEl GLU A 107 18.996 29.736 33.597 1.00 43.32 O
ATOM 459 OE2 GLU A 107 17.598 30.806 34.899 1.00 43.82 O
ATOM 460 C GLU A 107 14.695 31.740 30.959 1.00 41.43 C
ATOM 461 O GLU A 107 14.759 32.932 31.282 1.00 41.49 O
ATOM 463 N GLY A 108 14.862 31.308 29.707 1.00 41.26 N
ATOM 464 CA GLY A 108 15.325 32.195 28.634 1.00 40.84 C
ATOM 467 C GLY A 108 14.249 32.762 27.723 1.00 40.65 C
ATOM 468 O GLY A 108 14.558 33.209 26.613 1.00 40.72 O
ATOM 470 N ASP A 109 12.994 32.773 28.183 1.00 40.17 N
ATOM 471 CA ASP A 109 11.876 33.184 27.328 1.00 39.58 C
ATOM 473 CB ASP A 109 10.643 33.540 28.156 1.00 39.90 C
ATOM 476 CG ASP A 109 10.869 34.747 29.044 1.00 40.84 C
ATOM 477 ODl ASP A 109 11.538 35.698 28.588 1.00 41.55 O
ATOM 478 OD2 ASP A 109 10.382 34.744 30.198 1.00 42.95 O
ATOM 479 C ASP A 109 11.567 32.039 26.378 1.00 38.92 C
ATOM 480 O ASP A 109 11.735 30.874 26.745 1.00 39.14 O
ATOM 482 N PRO A 110 11.126 32.351 25.149 1.00 37.95 N
ATOM 483 CA PRO A 110 10.963 31.250 24.202 1.00 37.24 C
ATOM 485 CB PRO A 110 10.725 31.963 22.848 1.00 37.41 C
ATOM 488 CG PRO A 110 11.077 33.413 23.088 1.00 37.66 C
ATOM 491 CD PRO A 110 10.763 33.642 24.541 1.00 38.04 C
ATOM 494 C PRO A 110 -9.786 30.346 24.566 1.00 36.39 C
ATOM 495 O PRO A 110 -8.971 30.685 25.434 1.00 36.26 O
ATOM 496 N LEU A 111 -9.716 29.202 23.898 1.00 35.26 N
ATOM 497 CA LEU A 111 -8.686 28.216 24.165 1.00 34.35 C
ATOM 499 CB LEU A 111 -9.134 26.838 23.659 1.00 34.44 C
ATOM 502 CG LEU A 111 10.159 26.063 24.505 1.00 34.36 C
ATOM 504 CDl LEU A 111 10.835 24.966 23.665 1.00 33.42 C
ATOM 508 CD2 LEU A 111 11.203 26.983 25.144 1.00 34.52 C
ATOM 512 C LEU A 111 -7.357 28.660 23.526 1.00 33.57 C
ATOM 513 O LEU A 111 -7.247 28.814 22.296 1.00 33.62 O
ATOM 515 N VAL A 112 -6.358 28.870 24.380 1.00 32.34 N
ATOM 516 CA VAL A 112 -5.067 29.391 23.976 1.00 31.39 C
ATOM 518 CB VAL A 112 -4.750 30.698 24.736 1.00 31.43 C
ATOM 520 CGl VAL A 112 -3.281 31.131 24.532 1.00 31.21 C
ATOM 524 CG2 VAL A 112 -5.718 31.796 24.305 1.00 31.23 C
ATOM 528 C VAL A 112 -3.993 28.358 24.264 1.00 30.39 C
ATOM 529 O VAL A 112 -4.000 27.726 25.319 1.00 29.69 O
ATOM 531 N PHE A 113 -3.080 28.186 23.313 1.00 29.53 N
ATOM 532 CA PHE A 113 -1.950 27.300 23.497 1.00 29.22 C
ATOM 534 CB PHE A 113 -2.178 25.985 22.755 1.00 28.95 C
ATOM 537 CG PHE A 113 -2.151 26.102 21.257 1.00 29.09 C
ATOM 538 CDl PHE A 113 -0.963 25.925 20.552 1.00 28.87 C
ATOM 540 CEl PHE A 113 -0.935 26.011 19.168 1.00 28.39 C
ATOM 542 CZ PHE A 113 -2.099 26.263 18.472 1.00 28.74 C
ATOM 544 CE2 PHE A 113 -3.292 26.433 19.153 1.00 28.83 C
ATOM 546 CD2 PHE A 113 -3.317 26.344 20.544 1.00 29.26 C
ATOM 548 C PHE A 113 -0.633 27.943 23.073 1.00 28.75 C
ATOM 549 O PHE A 113 -0.606 28.838 22.242 1.00 28.48 O
ATOM 551 N ALA A 114 0.458 27.475 23.667 1.00 28.46 N
ATOM 552 CA ALA A 114 1.790 27.952 23.330 1.00 28.19 C ATOM 554 CB ALA A 114 2.518 28.373 24.587 1.00 28.18 C
ATOM 558 C ALA A 114 2.569 26.863 22.601 1.00 27.71 C
ATOM 559 O ALA A 114 2.388 25.689 22.884 1.00 27.60 O
ATOM 561 N THR A 115 3.401 27.264 21.641 1.00 27.48 N
ATOM 562 CA THR A 115 4.366 26.378 20.988 1.00 27.50 C
ATOM 564 CB THR A 115 4.233 26.384 19.440 1.00 27.33 C
ATOM 566 OGl THR A 115 4.507 27.694 18.937 1.00 27.43 O
ATOM 568 CG2 THR A 115 2.846 25.974 18.989 1.00 27.33 C
ATOM 572 C THR A 115 5.750 26.901 21.321 1.00 27.46 C
ATOM 573 O THR A 115 5.916 28.099 21.528 1.00 27.44 O
ATOM 575 N VAL A 116 6.743 26.015 21.362 1.00 27.64 N
ATOM 576 CA VAL A 116 8.148 26.420 21.527 1.00 27.72 C
ATOM 578 CB VAL A 116 8.675 26.128 22.939 1.00 27.68 C
ATOM 580 CGl VAL A 116 8.159 27.165 23.904 1.00 28.31 C
ATOM 584 CG2 VAL A 116 8.268 24.738 23.387 1.00 27.97 C
ATOM 588 C VAL A 116 9.050 25.722 20.521 1.00 27.71 C
ATOM 589 O VAL A 116 8.910 24.529 20.280 1.00 27.64 O
ATOM 591 N GLY A 117 9.986 26.484 19.957 1.00 28.08 N
ATOM 592 CA GLY A 117 10.896 26.015 18.908 1.00 28.13 C
ATOM 595 C GLY A 117 11.745 27.168 18.400 1.00 28.26 C
ATOM 596 O GLY A 117 11.334 28.322 18.482 1.00 28.09 O
ATOM 598 N SER A 118 12.929 26.858 17.867 1.00 28.69 N
ATOM 599 CA SER A 118 13.927 27.882 17.528 1.00 28.61 C
ATOM 601 CB SER A 118 13.413 28.796 16.420 1.00 28.76 C
ATOM 604 OG SER A 118 14.424 29.672 15.990 1.00 29.20 O
ATOM 606 C SER A 118 14.221 28.662 18.808 1.00 28.80 C
ATOM 607 O SER A 118 14.217 28.068 19.890 1.00 29.05 O
ATOM 609 N ASN A 119 14.451 29.972 18.718 1.00 28.70 N
ATOM 610 CA ASN A 119 14.623 30.779 19.933 1.00 28.52 C
ATOM 612 CB ASN A 119 15.839 31.704 19.811 1.00 28.58 C
ATOM 615 CG ASN A 119 15.637 32.816 18.812 1.00 28.23 C
ATOM 616 ODl ASN A 119 14.892 32.672 17.840 1.00 25.88 O
ATOM 617 ND2 ASN A 119 16.317 33.935 19.043 1.00 28.13 N
ATOM 620 C ASN A 119 13.374 31.583 20.304 1.00 28.46 C
ATOM 621 O ASN A 119 13.481 32.678 20.871 1.00 28.16 O
ATOM 623 N ARG A 120 12.193 31.041 19.998 1.00 28.33 N
ATOM 624 CA ARG A 120 10.954 31.748 20.306 1.00 28.45 C
ATOM 626 CB ARG A 120 10.397 32.414 19.045 1.00 28.42 C
ATOM 629 CG ARG A 120 9.407 31.571 18.265 1.00 29.16 C
ATOM 632 CD ARG A 120 8.913 32.297 17.016 1.00 29.92 C
ATOM 635 NE ARG A 120 9.988 32.546 16.055 1.00 31.05 N
ATOM 637 CZ ARG A 120 9.803 32.970 14.807 1.00 31.22 C
ATOM 638 NHl ARG A 120 8.585 33.182 14.328 1.00 31.77 N
ATOM 641 NH2 ARG A 120 10.853 33.167 14.026 1.00 31.73 N
ATOM 644 C ARG A 120 9.871 30.887 20.963 1.00 28.06 C
ATOM 645 O ARG A 120 9.896 29.659 20.893 1.00 27.80 O
ATOM 647 N VAL A 121 8.926 31.568 21.609 1.00 27.81 N
ATOM 648 CA VAL A 121 7.681 30.954 22.074 1.00 27.78 C
ATOM 650 CB VAL A 121 7.590 30.877 23.635 1.00 27.68 C
ATOM 652 CGl VAL A 121 8.082 32.147 24.285 1.00 27.75 C
ATOM 656 CG2 VAL A 121 6.172 30.561 24.091 1.00 27.72 C
ATOM 660 C VAL A 121 6.539 31.756 21.463 1.00 27.46 C
ATOM 661 O VAL A 121 6.596 32.969 21.447 1.00 27.57 O
ATOM 663 N THR A 122 5.538 31.074 20.912 1.00 27.41 N
ATOM 664 CA THR A 122 4.421 31.739 20.248 1.00 27.64 C
ATOM 666 CB THR A 122 4.385 31.438 18.741 1.00 27.60 C
ATOM 668 OGl THR A 122 5.658 31.732 18.150 1.00 27.62 O
ATOM 670 CG2 THR A 122 3.293 32.269 18.064 1.00 27.38 C
ATOM 674 C THR A 122 3.095 31.272 20.826 1.00 27.77 C
ATOM 675 O THR A 122 2.911 30.088 21.075 1.00 27.70 O
ATOM 677 N LEU A 123 2.170 32.208 21.019 1.00 28.04 N
ATOM 678 CA LEU A 123 0.839 31.897 21.529 1.00 28.16 C
ATOM 680 CB LEU A 123 0.461 32.847 22.672 1.00 27.99 C
ATOM 683 CG LEU A 123 0.968 32.490 24.076 1.00 27.96 C
ATOM 685 CDl LEU A 123 2.433 32.088 24.046 1.00 27.96 C
ATOM 689 CD2 LEU A 123 0.733 33.638 25.066 1.00 27.73 C
ATOM 693 C LEU A 123 -0.183 31.993 20.397 1.00 28.42 C
ATOM 694 O LEU A 123 -0.170 32.942 19.613 1.00 28.23 O
ATOM 696 N TYR A 124 -1.055 30.995 20.318 1.00 28.83 N
ATOM 697 CA TYR A 124 -2.156 30.987 19.372 1.00 29.36 C
ATOM 699 CB TYR A 124 -2.028 29.807 18.429 1.00 29.15 C
ATOM 702 CG TYR A 124 -0.749 29.797 17.654 1.00 28.95 C
ATOM 703 CDl TYR A 124 -0.683 30.353 16.389 1.00 28.99 C
ATOM 705 CEl TYR A 124 0.496 30.344 15.664 1.00 28.92 C
ATOM 707 CZ TYR A 124 1.627 29.776 16.203 1.00 28.88 C
ATOM 708 OH TYR A 124 2.793 29.772 15.476 1.00 29.05 O
ATOM 710 CE2 TYR A 124 1.591 29.214 17.464 1.00 29.38 C ATOM 712 CD2 TYR A 124 0.402 29.225 18.182 1.00 29.30 C
ATOM 714 C TYR A 124 -3.473 30.879 20.125 1.00 29.97 C
ATOM 715 O TYR A 124 -3.520 30.385 21.252 1.00 29.98 O
ATOM 717 N GLU A 125 -4.543 31.346 19.494 1.00 30.73 N
ATOM 718 CA GLO A 125 -5.869 31.261 20.078 1.00 31.17 C
ATOM 720 CB GLO A 125 -6.458 32.651 20.230 1.00 31.08 C
ATOM 723 CG GLO A 125 -7.686 32.685 21.080 1.00 31.15 C
ATOM 726 CD GLO A 125 -8.085 34.092 21.443 1.00 31.65 C
ATOM 727 OEl GLO A 125 -7.773 34.511 22.574 1.00 32.92 O
ATOM 728 OE2 GLO A 125 -8.700 34.785 20.601 1.00 32.40 O
ATOM 729 C GLO A 125 -6.731 30.420 19.162 1.00 31.68 C
ATOM 730 O GLO A 125 -6.685 30.594 17.941 1.00 31.80 O
ATOM 732 N CYS A 126 -7.494 29.496 19.745 1.00 32.26 N
ATOM 733 CA CYS A 126 -8.368 28.617 18.964 1.00 32.77 C
ATOM 735 CB CYS A 126 -8.441 27.228 19.592 1.00 32.86 C
ATOM 738 SG CYS A 126 -6.855 26.387 19.683 1.00 32.86 S
ATOM 740 C CYS A 126 -9.773 29.208 18.844 1.00 33.24 C
ATOM 741 O CYS A 126 10.295 29.789 19.800 1.00 33.13 O
ATOM 743 N HIS A 127 10.358 29.058 17.655 1.00 33.77 N
ATOM 744 CA HIS A 127 11.683 29.589 17.327 1.00 34.15 C
ATOM 746 CB HIS A 127 11.560 30.980 16.702 1.00 34.13 C
ATOM 749 CG HIS A 127 11.111 32.039 17.660 1.00 34.19 C
ATOM 750 NDl HIS A 127 11.988 32.744 18.455 1.00 33.34 N
ATOM 752 CEl HIS A 127 11.314 33.611 19.188 1.00 33.19 C
ATOM 754 NE2 HIS A 127 10.031 33.494 18.897 1.00 33.47 N
ATOM 756 CD2 HIS A 127 -9.876 32.517 17.946 1.00 34.11 C
ATOM 758 C HIS A 127 12.389 28.656 16.344 1.00 34.61 C
ATOM 759 O HIS A 127 11.746 27.854 15.663 1.00 34.59 O
ATOM 761 N SER A 128 13.710 28.775 16.258 1.00 35.04 N
ATOM 762 CA SER A 128 14.511 27.866 15.433 1.00 35.33 C
ATOM 764 CB SER A 128 15.996 28.149 15.629 1.00 35.50 C
ATOM 767 OG SER A 128 16.245 29.534 15.464 1.00 36.72 O
ATOM 769 C SER A 128 14.138 27.957 13.953 1.00 35.43 C
ATOM 770 O SER A 128 13.418 28.864 13.541 1.00 35.62 O
ATOM 772 N GLN A 129 14.633 27.000 13.169 1.00 35.49 N
ATOM 773 CA GLN A 129 14.204 26.800 11.782 1.00 35.63 C
ATOM lib CB GLN A 129 14.492 28.026 10.893 1.00 36.02 C
ATOM 778 CG GLN A 129 15.972 28.260 10.557 1.00 36.91 C
ATOM 781 CD GLN A 129 16.830 28.447 11.795 1.00 38.26 C
ATOM 782 OEl GLN A 129 17.172 27.479 12.478 1.00 39.81 O
ATOM 783 NE2 GLN A 129 17.174 29.693 12.097 1.00 38.98 N
ATOM 786 C GLN A 129 12.722 26.440 11.723 1.00 35.63 C
ATOM 787 O GLN .A 129 12.055 26.700 10.715 1.00 35.63 O
ATOM 789 N GLY A 130 12.219 25.834 12.803 1.00 35.49 N
ATOM 790 CA GLY A 130 10.820 25.420 12.891 1.00 35.25 C
ATOM 793 C GLY A 130 -9.814 26.559 12.816 1.00 35.14 C
ATOM 794 O GLY A 130 -8.658 26.340 12.475 1.00 35.20 O
ATOM 796 N GLO A 131 10.237 27.773 13.150 1.00 34.93 N
ATOM 797 CA GLU A 131 -9.369 28.930 13.009 1.00 34.68 C
ATOM 799 CB GLO A 131 10.190 30.214 13.045 1.00 34.90 C
ATOM 802 CG GLO A 131 -9.419 31.453 12.564 1.00 35.09 C
ATOM 805 CD GLO A 131 -9.811 32.729 13.296 1.00 35.32 C
ATOM 806 OEl GLO A 131 10.965 32.815 13.793 1.00 36.07 O
ATOM 807 OE2 GLO A 131 -8.951 33.641 13.373 1.00 35.65 O
ATOM 808 C GLU A 131 -8.323 28.962 14.119 1.00 34.38 C
ATOM 809 O GLU A 131 -8.646 28.760 15.290 1.00 34.25 O
ATOM 811 N ILE A 132 -7.075 29.236 13.738 1.00 34.03 N
ATOM 812 CA ILE A 132 -5.956 29.323 14.682 1.00 33.55 C
ATOM 814 CB ILE A 132 -4.855 28.296 14.345 1.00 33.54 C
ATOM 816 CGl ILE A 132 -5.401 26.865 14.424 1.00 33.41 C
ATOM 819 CDl ILE A 132 -4.381 25.791 14.038 1.00 33.32 C
ATOM 823 CG2 ILE A 132 -3.679 28.455 15.305 1.00 34.02 C
ATOM 827 C ILE A 132 -5.355 30.733 14.661 1.00 33.15 C
ATOM 828 O ILE A 132 -4.520 31.048 13.814 1.00 33.38 O
ATOM 830 N ARG A 133 -5.765 31.573 15.602 1.00 32.45 N
ATOM 831 CA ARG A 133 -5.410 32.988 15.561 1.00 32.03 C
ATOM 833 CB ARG A 133 -6.515 33.803 16.236 1.00 32.09 C
ATOM 836 CG ARG A 133 -6.565 35.264 15.844 1.00 32.51 C
ATOM 839 CD ARG A 133 -7.797 35.937 16.451 1.00 33.09 C
ATOM 842 NE ARG A 133 -9.023 35.582 15.728 1.00 34.35 N
ATOM 844 CZ ARG A 133 10.264 35.745 16.193 1.00 34.45 C
ATOM 845 NHl ARG A 133 10.493 36.274 17.388 1.00 34.82 N
ATOM 848 NH2 ARG A 133 11.294 35.372 15.450 1.00 34.88 N
ATOM 851 C ARG A 133 -4.040 33.270 16.203 1.00 31.43 C
ATOM 852 O ARG A 133 -3.884 33.194 17.428 1.00 31.32 O
ATOM 854 N LEU A 134 -3.055 33.591 15.362 1.00 30.63 N
ATOM 855 CA LEO A 134 -1.721 34.008 15.815 1.00 30.11 C ATOM 857 CB LED A 134 -0.794 34.246 14.611 1.00 29.88 C
ATOM 860 CG LEU A 134 0.659 34.652 14.883 1.00 29.99 C
ATOM 862 CDl LEU A 134 1.347 33.613 15.748 1.00 29.44 C
ATOM 866 CD2 LEU A 134 1.442 34.863 13.595 1.00 29.33 C
ATOM 870 C LEU A 134 -1.818 35.283 16.640 1.00 29.60 C
ATOM 871 O LEU A 134 -2.433 36.250 16.209 1.00 29.30 O
ATOM 873 N LEU A 135 -1.223 35.269 17.830 1.00 29.49 N
ATOM 874 CA LEU A 135 -1.214 36.433 18.719 1.00 29.44 C
ATOM 876 CB LEU A 135 -1.688 36.061 20.139 1.00 29.27 C
ATOM 879 CG LEU A 135 -2.993 35.260 20.309 1.00 29.53 C
ATOM 881 CDl LEU A 135 -3.310 35.057 21.786 1.00 28.47 C
ATOM 885 CD2 LEU A 135 -4.192 35.894 19.596 1.00 29.12 C
ATOM 889 C LEU A 135 0.181 37.087 18.742 1.00 29.30 C
ATOM 890 O LEU A 135 0.438 38.029 17.994 1.00 29.60 O
ATOM 892 N GLN A 136 1.092 36.579 19.563 1.00 29.17 N
ATOM 893 CA GLN A 136 2.341 37.283 19.829 1.00 29.14 C
ATOM 895 CB GLN A 136 2.087 38.360 20.893 1.00 29.22 C
ATOM 898 CG GLN A 136 3.161 39.443 21.021 1.00 29.19 C
ATOM 901 CD GLN A 136 2.890 40.414 22.173 1.00 28.89 C
ATOM 902 OEl GLN A 136 1.925 40.265 22.921 1.00 27.83 O
ATOM 903 NE2 GLN A 136 3.748 41.415 22.313 1.00 28.97 N
ATOM 906 C GLN A 136 3.418 36.310 20.304 1.00 29.09 C
ATOM 907 O GLN A 136 3.136 35.403 21.087 1.00 29.08 O
ATOM 909 N SER A 137 4.645 36.495 19.826 1.00 28.99 N
ATOM 910 CA SER A 137 5.760 35.660 20.251 1.00 29.07 C
ATOM 912 CB SER A 137 6.577 35.216 19.051 1.00 29.01 C
ATOM 915 OG SER A 137 5.840 34.319 18.247 1.00 29.83 O
ATOM 917 C SER A 137 6.676 36.379 21.211 1.00 29.05 C
ATOM 918 O SER A 137 6.662 37.604 21.300 1.00 29.04 O
ATOM 920 N TYR A 138 7.454 35.600 21.953 1.00 29.31 N
ATOM 921 CA TYR A 138 8.641 36.106 22.632 1.00 29.61 C
ATOM 923 CB TYR A 138 8.635 35.764 24.125 1.00 29.56 C
ATOM 926 CG TYR A 138 9.969 36.018 24.793 1.00 29.34 C
ATOM 927 CDl TYR A 138 10.266 37.246 25.362 1.00 29.29 C
ATOM 929 CEl TYR A 138 11.499 37.483 25.959 1.00 29.35 C
ATOM 931 CZ TYR A 138 12.446 36.486 25.979 1.00 29.53 C
ATOM 932 OH TYR A 138 13.682 36.693 26.562 1.00 30.08 O
ATOM 934 CE2 TYR A 138 12.168 35.264 25.417 1.00 29.76 C
ATOM 936 CD2 TYR A 138 10.939 35.037 24.829 1.00 29.36 C
ATOM 938 C TYR A 138 9.852 35.480 21.944 1.00 29.85 C
ATOM 939 O TYR A 138 9.930 34.261 21.821 1.00 29.86 O
ATOM 941 N VAL A 139 10.778 36.316 21.480 1.00 30.25 N
ATOM 942 CA VAL A 139 12.004 35.849 20.833 1.00 30.59 C
ATOM 944 CB VAL A 139 12.208 36.509 19.460 1.00 30.46 C
ATOM 946 CGl VAL A 139 13.344 35.812 18.701 1.00 29.88 C
ATOM 950 CG2 VAL A 139 10.902 36.488 18.659 1.00 29.63 C
ATOM 954 C VAL A 139 13.192 36.194 21.714 1.00 31.02 C
ATOM 955 O VAL A 139 13.371 37.350 22.077 1.00 31.21 O
ATOM 957 N ASP A 140 13.998 35.197 22.059 1.00 31.60 N
ATOM 958 CA ASP A 140 15.140 35.422 22.937 1.00 32.04 C
ATOM 960 CB ASP A 140 15.775 34.086 23.349 1.00 32.05 C
ATOM 963 CG ASP A 140 16.635 34.204 24.594 1.00 32.11 C
ATOM 964 ODl ASP A 140 17.560 35.038 24.581 1.00 33.80 O
ATOM 965 OD2 ASP A 140 16.402 33.462 25.580 1.00 32.55 O
ATOM 966 C ASP A 140 16.163 36.330 22.240 1.00 32.46 C
ATOM 967 O ASP A 140 16.451 36.148 21.062 1.00 32.62 O
ATOM 969 N ALA A 141 16.692 37.313 22.968 1.00 33.09 N
ATOM 970 CA ALA A 141 17.741 38.200 22.442 1.00 33.47 C
ATOM 972 CB ALA A 141 18.276 39.125 23.546 1.00 33.45 C
ATOM 976 C ALA A 141 18.881 37.391 21.814 1.00 33.88 C
ATOM 977 O ALA A 141 19.379 37.743 20.742 1.00 34.27 O
ATOM 979 N ASP A 142 19.271 36.300 22.469 1.00 34.06 N
ATOM 980 CA ASP A 142 20.230 35.357 21.898 1.00 34.23 C
ATOM 982 CB ASP A 142 20.748 34.428 22.999 1.00 34.42 C
ATOM 985 CG ASP A 142 21.818 33.466 22.512 1.00 34.64 C
ATOM 986 ODl ASP A 142 21.952 33.280 21.278 1.00 34.53 O
ATOM 987 OD2 ASP A 142 22.518 32.890 23.382 1.00 35.07 O
ATOM 988 C ASP A 142 19.624 34.534 20.734 1.00 34.43 C
ATOM 989 O ASP A 142 18.722 33.707 20.937 1.00 34.55 O
ATOM 991 N ALA A 143 20.139 34.762 19.522 1.00 34.43 N
ATOM 992 CA ALA A 143 19.716 34.017 18.324 1.00 34.45 C
ATOM 994 CB ALA A 143 20.344 34.614 17.076 1.00 34.16 C
ATOM 998 C ALA A 143 20.056 32.529 18.411 1.00 34.63 C
ATOM 999 O ALA A 143 19.405 31.710 17.761 1.00 34.48 O
ATOM 1001 N ASP A 144 21.076 32.193 19.209 1.00 34.82 N
ATOM 1002 CA ASP A 144 21.510 30.801 19.408 1.00 34.84 C
ATOM 1004 CB ASP A 144 23.009 30.743 19.735 1.00 35.32 C ATOM 1007 CG ASP A 144 23.883 31.110 18.548 00 36.74 C
ATOM 1008 ODl ASP A 144 23.424 30.988 17.386 00 38.35 O
ATOM 1009 OD2 ASP A 144 25.044 31.509 18.783 00 39.47 O
ATOM 1010 C ASP A 144 20.749 30.043 20.495 00 34.65 C
ATOM 1011 O ASP A 144 21.004 28.856 20.700 00 34.52 O
ATOM 1013 N GLU A 145 19.837 30.714 21.201 00 34.20 N
ATOM 1014 CA GLU A 145 18.955 30.025 22.146 00 33.81 C
ATOM 1016 CB GLU A 145 18.089 31.025 22.922 1.00 33.78 C
ATOM 1019 CG GLU A 145 17.004 30.417 23.814 33.78 C
ATOM 1022 CD GLU A 145 17.557 29.572 24.956 33.46 C
ATOM 1023 OEl GLU A 145 18.083 28.466 24.695 32.20 O
ATOM 1024 OE2 GLU A 145 17.433 30.011 26.122 33.34 O
ATOM 1025 C GLU A 145 18.066 29.068 21.376 33.11 C
ATOM 1026 O GLU A 145 17.699 29.317 20.230 32.87 O
ATOM 1028 N ASN A 146 17.724 27.961 22.005 32.64 N
ATOM 1029 CA ASN A 146 16.753 27.066 21.422 32.00 C
ATOM 1031 CB ASN A 146 17.457 25.938 20.664 32.43 C
ATOM 1034 CG ASN A 146 16.499 25.127 19.792 33.30 C
ATOM 1035 ODl ASN A 146 15.263 25.285 19.864 1.00 34.95 O
ATOM 1036 ND2 ASN A 146 17.065 24.240 18.968 .00 34.20 N
ATOM 1039 C ASN A 146 15.844 26.520 22.510 .00 31.62 C
ATOM 1040 O ASN A 146 16.263 25.686 23.320 .00 31.86 O
ATOM 1042 N PHE A 147 14.606 27.004 22.534 .00 30.83 N
ATOM 1043 CA PHE A 147 13.635 26.567 23.527 .00 30.19 C
ATOM 1045 CB PHE A 147 12.460 27.537 23.613 .00 29.93 C
ATOM 1048 CG PHE A 147 12.840 28.888 24.140 .00 29.99 C
ATOM 1049 CDl PHE A 147 13.489 29.011 25.364 .00 29.97 C
ATOM 1051 CEl PHE A 147 13.845 30.247 25.855 .00 29.78 C
ATOM 1053 CZ PHE A 147 13.550 31.386 25.128 1.00 29.61 C
ATOM 1055 CE2 PHE A 147 12.906 31.278 23.912 1.00 29.62 C
ATOM 1057 CD2 PHE A 147 12.555 30.034 23.422 1.00 29.68 C
ATOM 1059 C PHE A 147 13.148 25.169 23.206 1.00 29.72 C
ATOM 1060 O PHE A 147 12.748 24.884 22.075 1.00 29.43 O
ATOM 1062 N TYR A 148 13.215 24.307 24.220 1.00 29.37 N
ATOM 1063 CA TYR A 148 12.836 22.901 24.119 29.01 C
ATOM 1065 CB TYR A 148 13.900 22.022 24.801 29.27 C
ATOM 1068 CG TYR A 148 15.290 22.042 24.176 29.51 C
ATOM 1069 CDl TYR A 148 15.517 22.583 22.911 29.61 C
ATOM 1071 CEl TYR A 148 16.774 22.578 22.346 29.61 C
ATOM 1073 CZ TYR A 148 17.832 22.013 23.028 30.36 C
ATOM 1074 OH TYR A 148 19.092 22.016 22.452 30.07 O
ATOM 1076 CE2 TYR A 148 17.631 21.455 24.285 29.85 C
ATOM 1078 CD2 TYR A 148 16.369 21.468 24.841 29.80 C
ATOM 1080 C TYR A 148 11.485 22.618 24.774 28.51 C
ATOM 1081 O TYR A 148 10.796 21.659 24.409 28.47 O
ATOM 1083 N THR A 149 11.104 23.451 25.735 27.79 N
ATOM 1084 CA THR A 149 10.018 23.107 26.631 27.56 C
ATOM 1086 CB THR A 149 10.560 22.269 27.812 1.00 27.58 C
ATOM 1088 OGl THR A 149 9.470 21.717 28.560 27.88 O
ATOM 1090 CG2 THR A 149 11.439 23.125 28.725 27.01 C
ATOM 1094 C THR A 149 9.354 24.344 27.187 26.98 C
ATOM 1095 O THR A 149 9.969 25.390 27.291 27.08 O
ATOM 1097 N CYS A 150 8.091 24.215 27.551 26.66 N
ATOM 1098 CA CYS A 150 7.410 25.268 28.276 00 26.62 C
ATOM 1100 CB CYS A 150 6.868 26.310 27.307 00 26.60 C
ATOM 1103 SG CYS A 150 5.368 25.809 26.473 00 26.98 S
ATOM 1105 C CYS A 150 6.287 24.701 29.138 00 26.42 C
ATOM 1106 O CYS A 150 5.881 23.554 28.962 00 26.66 O
ATOM 1108 N ALA A 151 5.804 25.508 30.077 00 26.33 N
ATOM 1109 CA ALA A 151 4.755 25.093 31.006 00 26.32 C
ATOM 1111 CB ALA A 151 5.354 24.341 32.177 00 26.05 C
ATOM 1115 C ALA A 151 3.976 26.302 31.504 00 26.25 C
ATOM 1116 O ALA A 151 4.508 27.402 31.588 00 26.32 O
ATOM 1118 N TRP A 152 2.712 26.085 31.837 00 26.44 N
ATOM 1119 CA TRP A 152 1.839 27.157 32.283 00 26.49 C
ATOM 1121 CB TRP A 152 0.473 27.054 31.602 00 26.18 C
ATOM 1124 CG TRP A 152 0.456 27.385 30.154 00 25.49 C
ATOM 1125 CDl TRP A 152 0.686 26.534 29.128 00 25.25 C
ATOM 1127 NEl TRP A 152 0.557 27.191 27.929 00 25.41 N
ATOM 1129 CE2 TRP A 152 0.232 28.498 28.169 00 25.48 C
ATOM 1130 CD2 TRP A 152 0.149 28.656 29.567 00 25.60 C
ATOM 1131 CE3 TRP A 152 -0.179 29.917 30.086 00 25.50 C
ATOM 1133 CZ3 TRP A 152 -0.411 30.966 29.194 00 25.39 C
ATOM 1135 CH2 TRP A 152 -0.324 30.774 27.804 00 25.15 C
ATOM 1137 CZ2 TRP A 152 -0.003 29.553 27.274 25.65 C
ATOM 1139 C TRP A 152 1.621 27.084 33.781 26.88 C
ATOM 1140 O TRP A 152 1.463 26.006 34.345 1.00 26.86 O ATOM 1142 N THR A 153 1.609 28.243 34.412 1.00 27.46 N
ATOM 1143 CA THR A 153 1.093 28.381 35.756 1.00 28.52 C
ATOM 1145 CB THR A 153 2.216 28.413 36.806 1.00 28.27 C
ATOM 1147 OGl THR A 153 1.664 28.215 38.107 1.00 27.68 O
ATOM 1149 CG2 THR A 153 2.973 29.743 36.776 1.00 27.89 C
ATOM 1153 C THR A 153 0.328 29.689 35.737 1.00 29.24 C
ATOM 1154 O THR A 153 0.007 30.182 34.662 1.00 29.54 O
ATOM 1156 N TYR A 154 0.048 30.244 36.911 1.00 30.13 N
ATOM 1157 CA TYR A 154 0.511 31.588 37.014 1.00 30.83 C
ATOM 1159 CB TYR A 154 2.041 31.529 37.130 1.00 31.20 C
ATOM 1162 CG TYR A 154 2.478 30.534 38.162 1.00 31.22 C
ATOM 1163 CDl TYR A 154 2.804 29.239 37.796 1.00 31.62 C
ATOM 1165 CEl TYR A 154 3.172 28.307 38.737 1.00 31.59 C
ATOM 1167 CZ TYR A 154 3.195 28.665 40.069 1.00 31.53 C
ATOM 1168 OH TYR A 154 3.556 27.734 41.004 1.00 31.68 O
ATOM 1170 CE2 TYR A 154 2.862 29.946 40.463 1.00 31.31 C
ATOM 1172 CD2 TYR A 154 2.501 30.869 39.512 1.00 31.10 C
ATOM 1174 C TYR A 154 0.081 32.263 38.237 1.00 31.39 C
ATOM 1175 O TYR A 154 0.512 31.586 39.162 1.00 31.49 O
ATOM 1177 N ASP A 155 0.097 33.592 38.233 1.00 32.27 N
ATOM 1178 CA ASP A 155 0.577 34.378 39.362 1.00 32.66 C
ATOM 1180 CB ASP A 155 0.665 35.845 38.960 1.00 32.82 C
ATOM 1183 CG ASP A 155 1.113 36.750 40.095 1.00 33.17 C
ATOM 1184 ODl ASP A 155 0.584 36.647 41.220 1.00 35.44 O
ATOM 1185 OD2 ASP A 155 1.981 37.606 39.844 1.00 35.38 O
ATOM 1186 C ASP A 155 0.376 34.193 40.528 1.00 33.08 C
ATOM 1187 O ASP A 155 1.566 34.440 40.406 1.00 32.92 O
ATOM 1189 N SER A 156 0.168 33.782 41.668 1.00 34.02 N
ATOM 1190 CA SER A 156 0.635 33.335 42.812 1.00 34.79 C
ATOM 1192 CB SER A 156 0.257 32.615 43.827 1.00 35.04 C
ATOM 1195 OG SER A 156 1.168 33.524 44.430 1.00 35.82 O
ATOM 1197 C SER A 156 1.414 34.436 43.553 1.00 35.51 C
ATOM 1198 O SER A 156 2.205 34.123 44.468 1.00 36.05 O
ATOM 1200 N ASN A 157 1.176 35.700 43.188 1.00 35.67 N
ATOM 1201 CA ASN A 157 1.897 36.839 43.775 1.00 35.65 C
ATOM 1203 CB ASN A 157 0.898 37.813 44.412 1.00 35.95 C
ATOM 1206 CG ASN A 157 0.169 37.207 45.610 1.00 36.57 C
ATOM 1207 ODl ASN A 157 0.772 36.531 46.450 1.00 37.24 O
ATOM 1208 ND2 ASN A 157 1.135 37.455 45.695 1.00 37.47 N
ATOM 1211 C ASN A 157 2.786 37.575 42.762 1.00 35.68 C
ATOM 1212 O ASN A 157 3.948 37.890 43.054 1.00 35.73 O
ATOM 1214 N THR A 158 2.241 37.828 41.571 1.00 35.40 N
ATOM 1215 CA THR A 158 2.955 38.581 40.539 1.00 35.07 C
ATOM 1217 CB THR A 158 1.987 39.229 39.537 1.00 35.14 C
ATOM 1219 OGl THR A 158 1.676 38.291 38.498 1.00 35.19 O
ATOM 1221 CG2 THR A 158 0.697 39.688 40.234 1.00 35.52 C
ATOM 1225 C THR A 158 3.896 37.676 39.754 1.00 34.69 C
ATOM 1226 O THR A 158 4.728 38.155 38.980 1.00 34.66 O
ATOM 1228 N SER A 159 3.730 36.368 39.925 1.00 34.29 N
ATOM 1229 CA SER A 159 4.498 35.367 39.182 1.00 34.02 C
ATOM 1231 CB SER A 159 6.012 35.604 39.320 1.00 34.21 C
ATOM 1234 OG SER A 159 6.634 35.783 38.058 1.00 33.92 O
ATOM 1236 C SER A 159 4.132 35.246 37.712 1.00 33.74 C
ATOM 1237 O SER A 159 4.592 34.322 37.049 1.00 33.96 O
ATOM 1239 N HIS A 160 3.316 36.153 37.193 1.00 33.17 N
ATOM 1240 CA HIS A 160 3.017 36.127 35.171 1.00 32.84 C
ATOM 1242 CB HIS A 160 2.414 37.461 35.345 1.00 33.55 C
ATOM 1245 CG HIS A 160 3.380 38.600 35.465 1.00 35.87 C
ATOM 1246 NDl HIS A 160 3.083 39.771 36.131 1.00 38.09 N
ATOM 1248 CEl HIS A 160 4.134 40.574 36.094 1.00 38.34 C
ATOM 1250 NE2 HIS A 160 5.106 39.962 35.436 1.00 38.06 N
ATOM 1252 CD2 HIS A 160 4.664 38.722 35.042 1.00 37.51 C
ATOM 1254 C HIS A 160 2.116 34.941 35.426 1.00 31.99 C
ATOM 1255 O HIS A 160 1.279 34.534 36.223 1.00 31.66 O
ATOM 1257 N PRO A 161 2.289 34.383 34.220 1.00 30.97 N
ATOM 1258 CA PRO A 161 1.491 33.238 33.830 1.00 30.24 C
ATOM 1260 CB PRO A 161 2.137 32.794 32.517 1.00 30.31 C
ATOM 1263 CG PRO A 161 2.678 34.043 31.951 1.00 30.66 C
ATOM 1266 CD PRO A 161 3.184 34.811 33.133 1.00 30.99 C
ATOM 1269 C PRO A 161 0.053 33.653 33.593 1.00 29.39 C
ATOM 1270 O PRO A 161 0.238 34.833 33.398 1.00 29.40 O
ATOM 1271 N LEO A 162 0.839 32.678 33.641 1.00 28.43 N
ATOM 1272 CA LEU A 162 2.243 32.902 33.374 1.00 27.68 C
ATOM 1274 CB LEU A 162 3.028 33.038 34.671 1.00 27.40 C
ATOM 1277 CG LED A 162 2.733 34.260 35.534 1.00 26.59 C
ATOM 1279 CDl LEU A 162 3.545 34.171 36.811 1.00 24.81 C
ATOM 1283 CD2 LEU A 162 3.028 35.538 34.766 1.00 25.19 C ATOM 1287 C LEU A 162 2.740 31.710 32.624 1.00 26.42 C
ATOM 1288 O LEϋ A 162 2.222 30.611 32.787 1.00 26.37 O
ATOM 1290 N LEU A 163 3.758 31.930 31.814 1.00 25.40 N
ATOM 1291 CA LEϋ A 163 4.330 30.882 31.001 1.00 24.72 C
ATOM 1293 CB LEϋ A 163 4.073 31.206 29.545 1.00 24.64 C
ATOM 1296 CG LEU A 163 4.459 30.175 28.498 1.00 25.22 C
ATOM 1298 CDl LEϋ A 163 3.851 28.796 28.770 1.00 24.52 C
ATOM 1302 CD2 LEU A 163 4.021 ■30.718 27.138 1.00 25.21 C
ATOM 1306 C LEϋ A 163 5.819 30.797 31.271 1.00 24.23 C
ATOM 1307 O LEU A 163 6.516 31.803 31.229 1.00 24.03 O
ATOM 1309 N ALA A 164 6.300 29.598 31.576 1.00 23.92 N
ATOM 1310 CA ALA A 164 7.727 29.364 31.748 1.00 23.84 C
ATOM 1312 CB ALA A 164 7.976 28.500 32.963 1.00 23.63 C
ATOM 1316 C ALA A 164 8.280 28.696 30.495 1.00 23.57 C
ATOM 1317 O ALA A 164 7.668 27.792 29.959 1.00 23.18 O
ATOM 1319 N VAL A 165 9.429 29.165 30.028 1.00 23.75 N
ATOM 1320 CA VAL A 165 10.147 28.540 28.912 1.00 23.88 C
ATOM 1322 CB VAL A 165 10.059 29.390 27.619 1.00 23.87 C
ATOM 1324 CGl VAL A 165 8.636 29.404 27.095 1.00 24.19 C
ATOM 1328 CG2 VAL A 165 10.547 30.809 27.864 1.00 23.19 C
ATOM 1332 C VAL A 165 11.619 28.306 29.270 1.00 23.93 C
ATOM 1333 O VAL A 165 12.194 29.006 30.102 1.00 23.82 O
ATOM 1335 N ALA A 166 12.223 27.310 28.639 1.00 24.09 N
ATOM 1336 CA ALA A 166 13.623 26.990 28.885 1.00 24.28 C
ATOM 1338 CB ALA A 166 13.788 26.275 30.220 1.00 23.94 C
ATOM 1342 C ALA A 166 14.122 26.125 27.744 1.00 24.48 C
ATOM 1343 O ALA A 166 13.327 25.501 27.044 1.00 24.60 O
ATOM 1345 N GLY A 167 15.433 26.091 27.553 1.00 24.75 N
ATOM 1346 CA GLY A 167 15.998 25.384 26.425 1.00 25.10 C
ATOM 1349 C GLY A 167 17.487 25.170 26.547 1.00 25.46 C
ATOM 1350 O GLY A 167 18.002 24.965 27.650 1.00 25.44 O
ATOM 1352 N SER A 168 18.168 25.238 25.405 1.00 25.69 N
ATOM 1353 CA SER A 168 19.572 24.865 25.306 1.00 26.07 C
ATOM 1355 CB SER A 168 20.055 24.998 23.864 1.00 26.15 C
ATOM 1358 OG SER A 168 19.513 26.154 23.258 1.00 27.23 O
ATOM 1360 C SER A 168 20.475 25.663 26.233 1.00 26.25 C
ATOM 1361 O SER A 168 21.403 25.102 26.818 1.00 26.38 O
ATOM 1363 N ARG A 169 20.202 26.958 26.384 1.00 26.55 N
ATOM 1364 CA ARG A 169 21.024 27.819 27.252 1.00 26.91 C
ATOM 1366 CB ARG A 169 20.660 29.292 27.062 1.00 26.97 C
ATOM 1369 CG ARG A 169 21.089 29.866 25.717 1.00 28.96 C
ATOM 1372 CD ARG A 169 20.607 31.333 25.541 1.00 29.64 C
ATOM 1375 NE ARG A 169 21.477 32.339 26.182 1.00 31.63 N
ATOM 1377 CZ ARG A 169 21.146 33.623 26.375 1.00 32.20 C
ATOM 1378 NHl ARG A 169 19.957 34.092 26.004 1.00 33.57 N
ATOM 1381 NH2 ARG A 169 22.004 34.455 26.951 1.00 32.85 N
ATOM 1384 C ARG A 169 20.950 27.478 28.747 1.00 26.40 C
ATOM 1385 O ARG A 169 21.805 27.906 29.512 1.00 26.37 O
ATOM 1387 N GLY A 170 19.933 26.726 29.160 1.00 26.06 N
ATOM 1388 CA GLY A 170 19.767 26.362 30.559 1.00 25.92 C
ATOM 1391 C GLY A 170 19.254 27.506 31.412 1.00 25.70 C
ATOM 1392 O GLY A 170 19.504 27.532 32.607 1.00 26.00 O
ATOM 1394 N ILE A 171 18.542 28.449 30.796 1.00 25.67 N
ATOM 1395 CA ILE A 171 17.899 29.568 31.501 1.00 25.58 C
ATOM 1397 CB ILE A 171 18.233 30.920 30.849 1.00 25.62 C
ATOM 1399 CGl ILE A 171 19.722 31.244 30.990 1.00 25.81 C
ATOM 1402 CDl ILE A 171 20.224 32.228 29.924 1.00 26.16 C
ATOM 1406 CG2 ILE A 171 17.374 32.039 31.467 1.00 25.62 C
ATOM 1410 C ILE A 171 16.372 29.443 31.467 1.00 25.27 C
ATOM 1411 O ILE A 171 15.782 29.225 30.405 1.00 25.00 O
ATOM 1413 N ILE A 172 15.744 29.604 32.628 1.00 24.89 N
ATOM 1414 CA ILE A 172 14.298 29.620 32.722 1.00 24.91 C
ATOM 1416 CB ILE A 172 13.793 29.084 34.071 1.00 24.64 C
ATOM 1418 CGl ILE A 172 14.180 27.616 34.246 1.00 24.39 C
ATOM 1421 CDl ILE A 172 13.808 27.031 35.587 1.00 24.30 C
ATOM 1425 CG2 ILE A 172 12.289 29.226 34.150 1.00 24.73 C
ATOM 1429 C ILE A 172 13.844 31.053 32.564 1.00 24.97 C
ATOM 1430 O ILE A 172 14.365 31.938 33.224 1.00 24.85 O
ATOM 1432 N ARG A 173 12.875 31.265 31.684 1.00 25.21 N
ATOM 1433 CA ARG A 173 12.289 32.568 31.455 1.00 25.52 C
ATOM 1435 CB ARG A 173 12.277 32.879 29.970 1.00 26.12 C
ATOM 1438 CG ARG A 173 13.611 32.802 29.289 1.00 27.94 C
ATOM 1441 CD ARG A 173 14.377 34.073 29.465 1.00 31.24 C
ATOM 1444 NE ARG A 173 15.661 33.979 28.791 1.00 32.83 N
ATOM 1446 CZ ARG A 173 16.630 34.883 28.880 1.00 34.45 C
ATOM 1447 NHl ARG A 173 16.475 35.980 29.627 1.00 34.91 N
ATOM 1450 NH2 ARG A 173 17.768 34.683 28.217 1.00 35.10 N ATOM 1453 C ARG A 173 10.848 32.540 31.910 1.00 25.47 C
ATOM 1454 O ARG A 173 10.095 31.666 31.495 1.00 25.24 O
ATOM 1456 N ILE A 174 10.458 33.502 32.740 1.00 25.48 N
ATOM 1457 CA ILE A 174 9.066 33.655 33.124 1.00 25.47 C
ATOM 1459 CB ILE A 174 8.935 33.997 34.602 1.00 25.55 C
ATOM 1461 CGl ILE A 174 9.584 32.899 35.453 1.00 26.41 C
ATOM 1464 CDl ILE A 174 8.938 31.513 35.299 1.00 26.53 C
ATOM 1468 CG2 ILE A 174 7.482 34.128 34.980 1.00 25.54 C
ATOM 1472 C ILE A 174 8.436 34.741 32.268 1.00 25.47 C
ATOM 1473 O ILE A 174 8.700 35.928 32.457 1.00 25.48 O
ATOM 1475 N ILE A 175 7.608 34.320 31.314 1.00 25.58 N
ATOM 1476 CA ILE A 175 6.990 35.230 30.361 1.00 25.58 C
ATOM 1478 CB ILE A 175 6.875 34.603 28.965 1.00 25.40 C
ATOM 1480 CGl ILE A 175 8.207 33.996 28.506 1.00 24.88 C
ATOM 1483 CDl ILE A 175 9.260 34.997 28.211 1.00 24.46 C
ATOM 1487 CG2 ILE A 175 6.365 35.648 27.969 1.00 25.40 C
ATOM 1491 C ILE A 175 5.577 35.597 30.798 1.00 25.76 C
ATOM 1492 O ILE A 175 4.757 34.723 31.058 1.00 25.90 O
ATOM 1494 N ASN A 176 5.295 36.891 30.876 1.00 26.05 N
ATOM 1495 CA ASN A 176 3.923 37.374 30.962 1.00 25.96 C
ATOM 1497 CB ASN A 176 3.920 38.866 31.298 1.00 26.21 C
ATOM 1500 CG ASN A 176 2.539 39.491 31.252 1.00 26.50 C
ATOM 1501 ODl ASN A 176 1.594 38.930 30.696 1.00 28.95 O
ATOM 1502 ND2 ASN A 176 2.422 40.678 31.831 1.00 26.95 N
ATOM 1505 C ASN A 176 3.309 37.134 29.599 1.00 26.07 C
ATOM 1506 O ASN A 176 3.759 37.716 28.628 1.00 26.17 O
ATOM 1508 N PRO A 177 2.290 36.263 29.510 1.00 26.20 N
ATOM 1509 CA PRO A 177 1.780 35.904 28.202 1.00 26.17 C
ATOM 1511 CB PRO A 177 1.041 34.597 28.476 1.00 25.96 C
ATOM 1514 CG PRO A 177 0.551 34.733 29.832 1.00 25.87 C
ATOM 1517 CD PRO A 177 1.554 35.566 30.577 1.00 26.27 C
ATOM 1520 C PRO A 177 0.841 36.947 27.589 1.00 26.39 C
ATOM 1521 O PRO A 177 0.532 36.851 26.403 1.00 26.97 O
ATOM 1522 N ILE A 178 0.379 37.922 28.367 1.00 26.30 N
ATOM 1523 CA ILE A 178 -0.413 39.012 27.794 1.00 26.41 C
ATOM 1525 CB ILE A 178 -1.023 39.930 28.882 1.00 26.48 C
ATOM 1527 CGl ILE A 178 -2.125 39.181 29.643 1.00 26.46 C
ATOM 1530 CDl ILE A 178 -2.719 39.947 30.810 1.00 26.24 C
ATOM 1534 CG2 ILE A 178 -1.573 41.200 28.255 1.00 26.09 C
ATOM 1538 C ILE A 178 0.464 39.839 26.852 1.00 26.51 C
ATOM 1539 O ILE A 178 0.192 39.921 25.655 1.00 26.37 O
ATOM 1541 N THR A 179 1.528 40.414 27.415 1.00 26.59 N
ATOM 1542 CA THR A 179 2.460 41.294 26.700 1.00 26.43 C
ATOM 1544 CB THR A 179 3.101 42.273 27.684 1.00 26.48 C
ATOM 1546 OGl THR A 179 3.902 41.540 28.622 1.00 26.20 O
ATOM 1548 CG2 THR A 179 2.030 43.066 28.426 1.00 26.39 C
ATOM 1552 C THR A 179 3.618 40.554 26.027 1.00 26.47 C
ATOM 1553 O THR A 179 4.327 41.121 25.199 1.00 26.37 O
ATOM 1555 N MET A 180 3.801 39.292 26.403 1.00 26.66 N
ATOM 1556 CA MET A 180 5.004 38.508 26.092 1.00 26.71 C
ATOM 1558 CB MET A 180 5.084 38.159 24.601 1.00 26.46 C
ATOM 1561 CG MET A 180 3.889 37.340 24.082 1.00 25.99 C
ATOM 1564 SD MET A 180 3.646 35.704 24.836 1.00 25.05 S
ATOM 1565 CE MET A 180 4.720 34.649 23.859 1.00 23.05 C
ATOM 1569 C MET A 180 6.298 39.158 26.612 1.00 26.93 C
ATOM 1570 O MET A 180 7.379 38.922 26.071 1.00 27.09 O
ATOM 1572 N GLN A 181 6.188 39.941 27.686 1.00 27.10 N
ATOM 1573 CA GLN A 181 7.365 40.424 28.406 1.00 27.45 C
ATOM 1575 CB GLN A 181 6.993 41.559 29.352 1.00 27.53 C
ATOM 1578 CG GLN A 181 6.738 42.889 28.701 1.00 27.84 C
ATOM 1581 CD GLN A 181 6.052 43.852 29.652 1.00 27.86 C
ATOM 1582 OEl GLN A 181 4.888 43.669 29.997 1.00 28.04 O
ATOM 1583 NE2 GLN A 181 6.771 44.878 30.082 1.00 28.59 N
ATOM 1586 C GLN A 181 7.967 39.309 29.253 1.00 27.63 C
ATOM 1587 O GLN A 181 7.233 38.546 29.889 1.00 27.58 O
ATOM 1589 N CYS A 182 9.299 39.243 29.285 1.00 27.90 N
ATOM 1590 CA CYS A 182 10.029 38.358 30.210 1.00 27.91 C
ATOM 1592 CB CYS A 182 11.439 38.063 29.666 1.00 27.89 C
ATOM 1595 SG CYS A 182 12.598 37.243 30.818 1.00 28.81 S
ATOM 1597 C CYS A 182 10.109 39.001 31.603 1.00 27.86 C
ATOM 1598 O CYS A 182 10.944 39.864 31.837 1.00 27.89 O
ATOM 1600 N ILE A 183 9.236 38.588 32.518 1.00 27.95 N
ATOM 1601 CA ILE A 183 9.225 39.135 33.877 1.00 28.06 C
ATOM 1603 CB ILE A 183 8.159 38.468 34.753 1.00 27.93 C
ATOM 1605 CGl ILE A 183 6.763 38.905 34.343 1.00 27.87 C
ATOM 1608 CDl ILE A 183 5.683 38.164 35.085 1.00 27.72 C
ATOM 1612 CG2 ILE A 183 8.387 38.817 36.214 1.00 28.08 C ATOM 1616 C ILE A 183 10.554 38.923 34.600 00 28.39 C
ATOM 1617 O ILE A 183 11.101 39.855 35.191 00 28.41 O
ATOM 1619 N LYS A 184 11.046 37.683 34.560 00 28.74 N
ATOM 1620 CA LYS A 184 12.234 37.267 35.315 00 28.70 C
ATOM 1622 CB LYS A 184 11.900 37.123 36.797 00 28.64 C
ATOM 1625 CG LYS A 184 10.750 36.194 37.096 00 28.45 C
ATOM 1628 CD LYS A 184 10.434 36.234 38.570 00 28.71 C
ATOM 1631 CE LYS A 184 9.121 35.549 38.889 00 28.67 C
ATOM 1634 NZ LYS A 184 8.798 35.702 40.330 00 28.88 N
ATOM 1638 C LYS A 184 12.810 35.952 34.812 00 28.74 C
ATOM 1639 O LYS A 184 12.124 35.179 34.140 00 28.42 O
ATOM 1641 N HIS A 185 14.071 35.702 35.158 00 28.92 N
ATOM 1642 CA HIS A 185 14.754 34.495 34.715 00 29.30 C
ATOM 1644 CB HIS A 185 15.657 34.789 33.497 00 29.43 C
ATOM 1647 CG HIS A 185 16.943 35.486 33.827 00 30.04 C
ATOM 1648 NDl HIS A 185 17.045 36.857 33.939 00 30.45 N
ATOM 1650 CEl HIS A 185 18.294 37.181 34.217 00 30.16 C
ATOM 1652 NE2 HIS A 185 19.010 36.072 34.278 00 30.12 N
ATOM 1654 CD2 HIS A 185 18.190 34.999 34.030 00 30.29 C
ATOM 1656 C HIS A 185 15.516 33.818 35.845 00 29.38 C
ATOM 1657 O HIS A 185 15.740 34.414 36.895 00 29.53 O
ATOM 1659 N TYR A 186 15.871 32.554 35.638 00 29.56 N
ATOM 1660 CA TYR A 186 16.664 31.806 36.612 00 29.86 C
ATOM 1662 CB TYR A 186 15.796 30.790 37.348 00 29.53 C
ATOM 1665 CG TYR A 186 14.589 31.401 38.017 00 29.44 C
ATOM 1666 CDl TYR A 186 14.721 32.143 39.178 00 29.59 C
ATOM 1668 CEl TYR A 186 13.613 32.714 39.795 00 29.38 C
ATOM 1670 CZ TYR A 186 12.360 32.542 39.246 00 29.00 C
ATOM 1671 OH TYR A 186 11.267 33.103 39.858 00 29.12 O
ATOM 1673 CE2 TYR A 186 12.203 31.809 38.093 00 28.82 C
ATOM 1675 CD2 TYR A 186 13.314 31.241 37.487 00 29.07 C
ATOM 1677 C TYR A 186 17.818 31.097 35.921 00 30.16 C
ATOM 1678 O TYR A 186 17.664 30.578 34.823 00 30.15 O
ATOM 1680 N VAL A 187 18.982 31.100 36.560 00 30.84 N
ATOM 1681 CA VAL A 187 20.147 30.388 36.039 00 31.27 C
ATOM 1683 CB VAL A 187 21.235 31.353 35.523 00 31.12 C
ATOM 1685 CGl VAL A 187 22.155 30.626 34.555 00 30.96 C
ATOM 1689 CG2 VAL A 187 20.613 32.574 34.851 00 30.70 C
ATOM 1693 C VAL A 187 20.751 29.512 37.133 00 31.88 C
ATOM 1694 O VAL A 187 20.459 29.682 38.316 00 32.05 O
ATOM 1696 N GLY A 188 21.598 28.578 36.719 00 32.65 N
ATOM 1697 CA GLY A 188 22.293 27.677 37.628 00 33.05 C
ATOM 1700 C GLY A 188 22.668 26.414 36.886 00 33.65 C
ATOM 1701 O GLY A 188 23.837 26.026 36.858 00 33.59 O
ATOM 1703 N HIS A 189 21.662 25.792 36.262 00 34.46 N
ATOM 1704 CA HIS A 189 21.823 24.514 35.539 1.00 34.58 C
ATOM 1706 CB HIS A 189 20.587 24.193 34.655 00 35.24 C
ATOM 1709 CG HIS A 189 19.455 23.499 35.374 00 36.43 C
ATOM 1710 NDl HIS A 189 19.590 22.264 35.977 00 38.12 N
ATOM 1712 CEl HIS A 189 18.430 21.894 36.497 00 37.95 C
ATOM 1714 NE2 HIS A 189 17.540 22.836 36.239 00 38.04 N
ATOM 1716 CD2 HIS A 189 18.152 23.849 35.535 00 37.63 C
ATOM 1718 C HIS A 189 23.100 24.511 34.680 00 34.63 C
ATOM 1719 O HIS A 189 23.388 25.481 33.956 00 34.74 O
ATOM 1721 N GLY A 190 23.853 23.412 34.778 00 34.24 N
ATOM 1722 CA GLY A 190 25.100 23.226 34.032 00 33.66 C
ATOM 1725 C GLY A 190 24.934 23.227 32.520 00 33.25 C
ATOM 1726 O GLY A 190 25.909 23.392 31.780 00 33.42 O
ATOM 1728 N ASN A 191 23.704 23.049 32.052 00 32.53 N
ATOM 1729 CA ASN A 191 23.447 22.986 30.627 00 31.75 C
ATOM 1731 CB ASN A 191 24.111 21.719 30.043 00 32.14 C
ATOM 1734 CG ASN A 191 24.348 21.804 28.535 00 33.03 C
ATOM 1735 ODl ASN A 191 24.410 20.775 27.857 00 34.57 O
ATOM 1736 ND2 ASN A 191 24.479 23.024 28.004 00 33.88 N
ATOM 1739 C ASN A 191 21.941 23.015 30.359 00 30.80 C
ATOM 1740 O ASN A 191 21.170 23.526 31.177 00 30.25 O
ATOM 1742 N ALA A 192 21.528 22.452 29.226 00 29.87 N
ATOM 1743 CA ALA A 192 20.180 22.644 28.701 00 29.05 C
ATOM 1745 CB ALA A 192 20.061 21.988 27.331 00 28.95 C
ATOM 1749 C ALA A 192 19.098 22.111 29.627 00 27.94 C
ATOM 1750 O ALA A 192 19.288 21.122 30.326 00 27.59 O
ATOM 1752 N ILE A 193 17.962 22.788 29.619 00 26.93 N
ATOM 1753 CA ILE A 193 16.777 22.309 30.308 00 26.57 C
ATOM 1755 CB ILE A 193 15.980 23.466 30.930 00 26.09 C
ATOM 1757 CGl ILE A 193 16.780 24.083 32.076 1.00 25.76 C
ATOM 1760 CDl ILE A 193 16.340 25.466 32.454 1.00 25.91 C
ATOM 1764 CG2 ILE A 193 14.636 22.983 31.414 1.00 26.07 C ATOM 1768 C ILE A 193 15.940 21.555 29.275 1.00 26.16 C
ATOM 1769 O ILE A 193 15.499 22.126 28.272 1.00 25.85 O
ATOM 1771 N ASN A 194 15.755 20.264 29.511 1.00 25.73 N
ATOM 1772 CA ASN A 194 14.976 19.441 28.616 1.00 25.70 C
ATOM 1774 CB ASN A 194 15.464 17.995 28.660 1.00 25.98 C
ATOM 1777 CG ASN A 194 16.891 17.844 28.153 1.00 26.59 C
ATOM 1778 ODl ASN A 194 17.763 17.328 28.864 1.00 27.56 O
ATOM 1779 ND2 ASN A 194 17.138 18.299 26.921 1.00 25.90 N
ATOM 1782 C ASN A 194 13.499 19.492 28.950 1.00 25.44 C
ATOM 1783 O ASN A 194 12.675 19.220 28.094 1.00 25.41 O
ATOM 1785 N GLU A 195 13.149 19.837 30.186 1.00 25.40 N
ATOM 1786 CA GLϋ A 195 11.733 19.938 30.545 1.00 25.11 C
ATOM 1788 CB GLU A 195 11.145 18.541 30.705 1.00 25.13 C
ATOM 1791 CG GLU A 195 9.638 18.531 30.677 1.00 25.94 C
ATOM 1794 CD GLU A 195 9.106 17.200 30.232 1.00 27.35 C
ATOM 1795 OEl GLU A 195 9.545 16.179 30.813 1.00 30.08 O
ATOM 1796 OE2 GLU A 195 8.263 17.169 29.301 1.00 30.75 O
ATOM 1797 C GLU A 195 11.389 20.759 31.794 1.00 24.27 C
ATOM 1798 O GLU A 195 12.159 20.816 32.752 1.00 23.73 O
ATOM 1800 N LEU A 196 10.195 21.362 31.752 1.00 23.59 N
ATOM 1801 CA LEU A 196 9.606 22.111 32.869 1.00 23.04 C
ATOM 1803 CB LEU A 196 9.471 23.579 32.489 1.00 22.73 C
ATOM 1806 CG LEU A 196 10.771 24.308 32.192 1.00 22.19 C
ATOM 1808 CDl LEU A 196 10.459 25.644 31.512 1.00 21.34 C
ATOM 1812 CD2 LEU A 196 11.573 24.479 33.475 1.00 20.50 C
ATOM 1816 C LEU A 196 8.215 21.589 33.257 1.00 22.38 C
ATOM 1817 O LEU A 196 7.418 21.233 32.390 1.00 21.99 O
ATOM 1819 N LYS A 197 7.937 21.575 34.561 1.00 21.95 N
ATOM 1820 CA LYS A 197 6.643 21.160 35.109 1.00 21.86 C
ATOM 1822 CB LYS A 197 6.651 19.677 35.486 1.00 21.85 C
ATOM 1825 CG LYS A 197 6.765 18.700 34.334 1.00 21.89 C
ATOM 1828 CD LYS A 197 5.532 18.675 33.457 1.00 21.83 C
ATOM 1831 CE LYS A 197 5.584 17.490 32.500 1.00 22.23 C
ATOM 1834 NZ LYS A 197 5.456 16.171 33.202 1.00 22.52 N
ATOM 1838 C LYS A 197 6.314 21.940 36.378 1.00 21.67 C
ATOM 1839 O LYS A 197 7.196 22.167 37.212 1.00 21.76 O
ATOM 1841 N PHE A 198 5.040 22.299 36.542 1.00 21.30 N
ATOM 1842 CA PHE A 198 4.560 22.951 37.768 1.00 20.92 C
ATOM 1844 CB PHE A 198 3.633 24.115 37.426 1.00 20.56 C
ATOM 1847 CG PHE A 198 4.353 25.345 37.020 1.00 20.32 C
ATOM 1848 CDl PHE A 198 4.868 26.206 37.985 1.00 20.17 C
ATOM 1850 CEl PHE A 198 5.552 27.351 37.617 1.00 20.28 C
ATOM 1852 CZ PHE A 198 5.733 27.632 36.271 1.00 19.96 C
ATOM 1854 CE2 PHE A 198 5.225 26.767 35.306 1.00 19.52 C
ATOM 1856 CD2 PHE A 198 4.547 25.637 35.683 1.00 19.05 C
ATOM 1858 C PHE A 198 3.823 22.004 38.709 1.00 20.68 C
ATOM 1859 O PHE A 198 3.047 21.149 38.285 1.00 20.38 O
ATOM 1861 N HIS A 199 4.055 22.194 40.000 1.00 20.69 N
ATOM 1862 CA HIS A 199 3.326 21.474 41.045 1.00 20.76 C
ATOM 1864 CB HIS A 199 3.657 22.098 42.400 1.00 20.60 C
ATOM 1867 CG HIS A 199 3.442 21.191 43.560 1.00 20.60 C
ATOM 1868 NDl HIS A 199 2.202 20.974 44.114 1.00 21.46 N
ATOM 1870 CEl HIS A 199 2.315 20.131 45.126 1.00 21.91 C
ATOM 1872 NE2 HIS A 199 3.587 19.794 45.247 1.00 21.62 N
ATOM 1874 CD2 HIS A 199 4.312 20.449 44.281 1.00 21.39 C
ATOM 1876 C HIS A 199 1.805 21.526 40.790 1.00 20.93 C
ATOM 1877 O HIS A 199 1.262 22.591 40.464 1.00 21.04 O
ATOM 1879 N PRO A 200 1.111 20.381 40.938 1.00 20.79 N
ATOM 1880 CA PRO A 200 -0.335 20.330 40.692 1.00 20.66 C
ATOM 1882 CB PRO A 200 -0.651 18.839 40.822 1.00 20.55 C
ATOM 1885 CG PRO A 200 0.397 18.305 41.700 1.00 20.60 C
ATOM 1888 CD PRO A 200 1.634 19.068 41.350 1.00 20.70 C
ATOM 1891 C PRO A 200 -1.181 21.119 41.691 1.00 20.74 C
ATOM 1892 O PRO A 200 -2.360 21.335 41.452 1.00 20.78 O
ATOM 1893 N ARG A 201 -0.584 21.527 42.804 1.00 20.88 N
ATOM 1894 CA ARG A 201 -1.310 22.199 43.872 1.00 21.02 C
ATOM 1896 CB ARG A 201 -1.285 21.343 45.133 1.00 21.71 C
ATOM 1899 CG ARG A 201 -1.662 19.897 44.894 1.00 23.59 C
ATOM 1902 CD ARG A 201 -3.146 19.721 44.816 1.00 26.55 C
ATOM 1905 NE ARG A 201 -3.681 19.229 46.087 1.00 28.31 N
ATOM 1907 CZ ARG A 201 -4.352 18.085 46.250 1.00 29.59 C
ATOM 1908 NHl ARG A 201 -4.622 17.285 45.215 1.00 30.99 N
ATOM 1911 NH2 ARG A 201 -4.785 17.741 47.461 1.00 29.48 N
ATOM 1914 C ARG A 201 -0.733 23.555 44.216 1.00 20.71 C
ATOM 1915 O ARG A 201 -1.459 24.416 44.697 1.00 21.01 O
ATOM 1917 N ASP A 202 0.567 23.735 44.008 1.00 20.22 N
ATOM 1918 CA ASP A 202 1.236 24.991 44.309 1.00 19.86 C ATOM 1920 CB ASP A 202 2.385 24.758 45.277 1.00 19.77 C
ATOM 1923 CG ASP A 202 3.035 26.045 45.729 1.00 20.43 C
ATOM 1924 ODl ASP A 202 2.874 27.077 45.042 1.00 20.75 O
ATOM 1925 OD2 ASP A 202 3.721 26.027 46.776 1.00 21.16 O
ATOM 1926 C ASP A 202 1.748 25.583 43.007 1.00 19.45 C
ATOM 1927 O ASP A 202 2.634 25.017 42.381 1.00 19.07 O
ATOM 1929 N PRO A 203 1.201 26.738 42.596 1.00 19.36 N
ATOM 1930 CA PRO A 203 1.550 27.295 41.288 1.00 19.35 C
ATOM 1932 CB PRO A 203 0.488 28.380 41.066 1.00 19.25 C
ATOM 1935 CG PRO A 203 -0.470 28.256 42.199 1.00 19.54 C
ATOM 1938 CD PRO A 203 0.253 27.606 43.307 1.00 19.33 C
ATOM 1941 C PRO A 203 2.945 27.913 41.213 1.00 19.27 C
ATOM 1942 O PRO A 203 3.396 28.255 40.121 1.00 19.18 O
ATOM 1943 N ASN A 204 3.605 28.056 42.360 1.00 19.30 N
ATOM 1944 CA ASN A 204 4.927 28.663 42.442 1.00 19.44 C
ATOM 1946 CB ASN A 204 5.096 29.354 43.793 1.00 19.41 C
ATOM 1949 CG ASN A 204 3.986 30.323 44.083 1.00 19.20 C
ATOM 1950 ODl ASN A 204 3.588 31.091 43.218 1.00 19.39 O
ATOM 1951 ND2 ASN A 204 3.475 30.293 45.301 1.00 19.32 N
ATOM 1954 C ASN A 204 6.057 27.661 42.278 1.00 19.46 C
ATOM 1955 O ASN A 204 7.196 28.049 42.029 1.00 19.32 O
ATOM 1957 N LEO A 205 5.748 26.380 42.426 1.00 19.59 N
ATOM 1958 CA LEU A 205 6.784 25.368 42.465 1.00 19.94 C
ATOM 1960 CB LEU A 205 6.411 24.274 43.457 1.00 19.89 C
ATOM 1963 CG LEU A 205 6.327 24.759 44.912 1.00 19.72 C
ATOM 1965 CDl LEU A 205 5.964 23.613 45.859 1.00 18.94 C
ATOM 1969 CD2 LEU A 205 7.628 25.418 45.347 1.00 19.43 C
ATOM 1973 C LEU A 205 7.062 24.810 41.072 1.00 20.25 C
ATOM 1974 O LEU A 205 6.314 24.004 40.540 1.00 20.57 O
ATOM 1976 N LEU A 206 8.159 25.277 40.491 1.00 20.57 N
ATOM 1977 CA LEU A 206 8.557 24.923 39.153 1.00 20.66 C
ATOM 1979 CB LEU A 206 9.042 26.177 38.421 1.00 20.51 C
ATOM 1982 CG LEU A 206 9.446 26.010 36.954 1.00 20.63 C
ATOM 1984 CDl LEU A 206 8.343 25.319 36.163 1.00 19.55 C
ATOM 1988 CD2 LEU A 206 9.824 27.357 36.317 1.00 20.13 C
ATOM 1992 C LEU A 206 9.677 23.905 39.256 1.00 21.05 C
ATOM 1993 O LEU A 206 10.675 24.142 39.933 1.00 21.32 O
ATOM 1995 N LEU A 207 9.507 22.766 38.594 1.00 21.51 N
ATOM 1996 CA LEU A 207 10.550 21.740 38.537 1.00 21.85 C
ATOM 1998 CB LEU A 207 9.951 20.363 38.802 1.00 21.92 C
ATOM 2001 CG LEU A 207 10.832 19.135 38.597 1.00 21.81 C
ATOM 2003 CDl LEU A 207 11.911 19.042 39.677 1.00 21.82 C
ATOM 2007 CD2 LEU A 207 9.939 17.908 38.594 1.00 21.87 C
ATOM 2011 C LEU A 207 11.214 21.759 37.169 1.00 22.12 C
ATOM 2012 O LEU A 207 10.527 21.783 36.156 1.00 22.09 O
ATOM 2014 N SER A 208 12.544 21.756 37.145 1.00 22.48 N
ATOM 2015 CA SER A 208 13.295 21.734 35.895 1.00 22.92 C
ATOM 2017 CB SER A 208 14.198 22.955 35.811 1.00 22.95 C
ATOM 2020 OG SER A 208 15.106 22.950 36.892 1.00 23.67 O
ATOM 2022 C SER A 208 14.143 20.471 35.819 1.00 23.26 C
ATOM 2023 O SER A 208 14.696 20.030 36.834 1.00 23.67 O
ATOM 2025 N VAL A 209 14.238 19.889 34.627 1.00 23.31 N
ATOM 2026 CA VAL A 209 15.098 18.731 34.406 1.00 23.57 C
ATOM 2028 CB VAL A 209 14.314 17.512 33.881 1.00 23.41 C
ATOM 2030 CGl VAL A 209 12.885 17.510 34.427 1.00 22.80 C
ATOM 2034 CG2 VAL A 209 14.316 17.471 32.362 1.00 23.04 C
ATOM 2038 C VAL A 209 16.176 19.152 33.412 1.00 24.08 C
ATOM 2039 O VAL A 209 15.900 19.907 32.472 1.00 24.40 O
ATOM 2041 N SER A 210 17.406 18.689 33.612 1.00 24.44 N
ATOM 2042 CA SER A 210 18.515 19.229 32.836 1.00 24.73 C
ATOM 2044 CB SER A 210 19.307 20.244 33.666 1.00 24.74 C
ATOM 2047 OG SER A 210 20.483 20.660 32.980 1.00 24.36 O
ATOM 2049 C SER A 210 19.479 18.207 32.267 1.00 25.09 C
ATOM 2050 O SER A 210 19.654 17.103 32.789 1.00 25.20 O
ATOM 2"052 N LYS A 211 20.115 18.642 31.184 1.00 25.63 N
ATOM 2053 CA LYS A 211 21.209 17.936 30.532 1.00 25.72 C
ATOM 2055 CB LYS A 211 21.646 18.750 29.306 1.00 25.95 C
ATOM 2058 CG LYS A 211 22.793 18.176 28.492 1.00 26.25 C
ATOM 2061 CD LYS A 211 22.631 18.540 27.008 1.00 26.63 C
ATOM 2064 CE LYS A 211 23.874 18.214 26.178 1.00 26.96 C
ATOM 2067 NZ LYS A 211 23.967 19.106 24.971 1.00 26.45 N
ATOM 2071 C LYS A 211 22.382 17.715 31.487 1.00 25.65 C
ATOM 2072 O LYS A 211 23.250 16.890 31.220 1.00 25.47 O
ATOM 2074 N ASP A 212 22.384 18.433 32.612 1.00 25.67 N
ATOM 2075 CA ASP A 212 23.467 18.335 33.591 1.00 25.50 C
ATOM 2077 CB ASP A 212 23.719 19.697 34.269 1.00 25.67 C
ATOM 2080 CG ASP A 212 22.599 20.119 35.225 1.00 26.06 C ATOM 2081 ODl ASP A 212 21.786 19.279 35.669 1.00 26.78 O
ATOM 2082 OD2 ASP A 212 22.540 21.325 35.535 1.00 26.60 O
ATOM 2083 C ASP A 212 23.228 17.265 34.636 1.00 25.18 C
ATOM 2084 O ASP A 212 23.872 17.274 35.678 1.00 25.10 O
ATOM 2086 N HIS A 213 22.307 16.345 34.364 1.00 25.00 N
ATOM 2087 CA HIS A 213 22.016 15.225 35.277 1.00 25.07 C
ATOM 2089 CB HIS A 213 23.307 14.574 35.816 1.00 25.03 C
ATOM 2092 CG HIS A 213 24.290 14.166 34.756 1.00 25.31 C
ATOM 2093 NDl HIS A 213 24.232 14.626 33.456 1.00 25.83 N
ATOM 2095 CEl HIS A 213 25.227 14.104 32.759 1.00 24.93 C
ATOM 2097 NE2 HIS A 213 25.933 13.328 33.562 1.00 24.46 N
ATOM 2099 CD2 HIS A 213 25.377 13.358 34.818 1.00 24.82 C
ATOM 2101 C HIS A 213 21.116 15.597 36.472 1.00 24.83 C
ATOM 2102 O HIS A 213 20.718 14.720 37.237 1.00 24.74 O
ATOM 2104 N ALA A 214 20.777 16.875 36.628 1.00 24.56 N
ATOM 2105 CA ALA A 214 20.100 17.328 37.839 1.00 24.43 C
ATOM 2107 CB ALA A 214 20.866 18.465 38.469 1.00 24.05 C
ATOM 2111 C ALA A 214 18.658 17.754 37.587 1.00 24.33 C
ATOM 2112 O ALA A 214 18.319 18.251 36.512 1.00 24.17 O
ATOM 2114 N LEO A 215 17.821 17.517 38.594 1.00 24.24 N
ATOM 2115 CA LED A 215 16.547 18.184 38.732 1.00 24.25 C
ATOM 2117 CB LEU A 215 15.477 17.219 39.227 1.00 24.52 C
ATOM 2120 CG LEO A 215 15.082 16.095 38.268 1.00 25.41 C
ATOM 2122 CDl LEO A 215 15.979 14.880 38.453 1.00 26.42 C
ATOM 2126 CD2 LEO A 215 13.624 15.719 38.492 1.00 24.98 C
ATOM 2130 C LEO A 215 16.697 19.310 39.750 1.00 24.01 C
ATOM 2131 O LEO A 215 17.399 19.170 40.757 1.00 23.39 O
ATOM 2133 N ARG A 216 16.031 20.428 39.480 1.00 23.88 N
ATOM 2134 CA ARG A 216 15.982 21.538 40.419 1.00 23.64 C
ATOM 2136 CB ARG A 216 16.788 22.726 39.895 1.00 23.83 C
ATOM 2139 CG ARG A 216 18.293 22.515 39.879 1.00 24.47 C
ATOM 2142 CD ARG A 216 19.024 23.725 39.292 1.00 25.61 C
ATOM 2145 NE ARG A 216 20.486 23.603 39.375 1.00 26.50 N
ATOM 2147 CZ ARG A 216 21.306 24.487 39.961 1.00 28.39 C
ATOM 2148 NHl ARG A 216 20.860 25.591 40.563 1.00 29.35 N
ATOM 2151 NH2 ARG A 216 22.613 24.256 39.964 1.00 29.06 N
ATOM 2154 C ARG A 216 14.532 21.933 40.628 1.00 22.93 C
ATOM 2155 O ARG A 216 13.747 21.938 39.688 1.00 23.03 O
ATOM 2157 N LEO A 217 14.186 22.240 41.871 1.00 22.27 N
ATOM 2158 CA LEO A 217 12.864 22.719 42.223 1.00 21.84 C
ATOM 2160 CB LEO A 217 12.286 21.886 43.366 1.00 21.90 C
ATOM 2163 CG LEO A 217 10.861 22.241 43.814 1.00 22.13 C
ATOM 2165 CDl LEO A 217 9.895 22.094 42.651 1.00 22.63 C
ATOM 2169 CD2 LEU A 217 10.408 21.375 44.979 1.00 21.93 C
ATOM 2173 C LEO A 217 12.971 24.162 42.668 1.00 21.36 C
ATOM 2174 O LEU A 217 13.632 24.456 43.670 1.00 21.41 O
ATOM 2176 N TRP A 218 12.303 25.050 41.934 1.00 20.70 N
ATOM 2177 CA TRP A 218 12.328 26.481 42.207 1.00 20.19 C
ATOM 2179 CB TRP A 218 12.590 27.251 40.922 1.00 19.98 C
ATOM 2182 CG TRP A 218 13.774 26.788 40.124 1.00 19.88 C
ATOM 2183 CDl TRP A 218 13.829 25.716 39.289 1.00 19.96 C
ATOM 2185 NEl TRP A 218 15.074 25.624 38.719 1.00 19.66 N
ATOM 2187 CE2 TRP A 218 15.846 26.653 39.175 1.00 18.83 C
ATOM 2188 CD2 TRP A 218 15.060 27.411 40.058 1.00 19.40 C
ATOM 2189 CE3 TRP A 218 15.622 28.537 40.662 1.00 19.96 C
ATOM 2191 CZ3 TRP A 218 16.927 28.857 40.367 1.00 19.92 C
ATOM 2193 CH2 TRP A 218 17.681 28.080 39.484 1.00 19.50 C
ATOM 2195 CZ2 TRP A 218 17.159 26.977 38.884 1.00 19.45 C
ATOM 2197 C TRP A 218 10.999 26.958 42.775 1.00 19.87 C
ATOM 2198 O TRP A 218 9.949 26.413 42.450 1.00 19.55 O
ATOM 2200 N ASN A 219 11.059 27.984 43.623 1.00 19.69 N
ATOM 2201 CA ASN A 219 9.877 28.714 44.092 1.00 19.48 C
ATOM 2203 CB ASN A 219 9.901 28.864 45.626 1.00 19.56 C
ATOM 2206 CG ASN A 219 8.758 29.730 46.170 1.00 19.51 C
ATOM 2207 ODl ASN A 219 8.349 30.719 45.553 1.00 17.82 O
ATOM 2208 ND2 ASN A 219 8.256 29.363 47.349 1.00 18.94 N
ATOM 2211 C ASN A 219 9.878 30.072 43.418 1.00 19.10 C
ATOM 2212 O ASN A 219 10.652 30.963 43.782 1.00 18.96 O
ATOM 2214 N ILE A 220 9.000 30.233 42.441 1.00 19.08 N
ATOM 2215 CA ILE A 220 9.022 31.426 41.616 1.00 19.14 C
ATOM 2217 CB ILE A 220 8.576 31.123 40.161 1.00 19.23 C
ATOM 2219 CGl ILE A 220 7.059 30.922 40.048 1.00 19.11 C
ATOM 2222 CDl ILE A 220 6.567 30.857 38.604 1.00 18.36 C
ATOM 2226 CG2 ILE A 220 9.320 29.887 39.626 1.00 18.79 C
ATOM 2230 C ILE A 220 8.244 32.588 42.238 1.00 19.21 C
ATOM 2231 O ILE A 220 8.191 33.668 41.672 1.00 19.37 O
ATOM 2233 N GLN A 221 7.660 32.380 43.411 1.00 19.63 N ATOM 2234 CA GLN A 221 7.102 33.495 44.178 .00 19.75 C
ATOM 2236 CB GLN A 221 6.196 33.009 45.308 .00 19.98 C
ATOM 2239 CG GLN A 221 5.914 34.047 46.377 .00 20.37 C
ATOM 2242 CD GLN A 221 4.481 34.494 46.387 .00 22.29 C
ATOM 2243 OEl GLN A 221 4.088 35.370 45.607 .00 23.49 O
ATOM 2244 NE2 GLN A 221 3.681 33.907 47.283 .00 21.90 N
ATOM 2247 C GLN A 221 8.240 34.302 44.764 .00 19.98 C
ATOM 2248 O GLN A 221 8.349 35.483 44.477 .00 20".67 O
ATOM 2250 N THR A 222 9.078 33.651 45.577 .00 19.81 N
ATOM 2251 CA THR A 222 10.224 34.289 46.229 .00 19.44 C
ATOM 2253 CB THR A 222 10.412 33.746 47.669 .00 19.19 C
ATOM 2255 OGl THR A 222 10.787 32.365 47.637 .00 18.85 O
ATOM 2257 CG2 THR A 222 9.140 33.873 48.432 .00 18.74 C
ATOM 2261 C THR A 222 11.532 34.121 45.437 .00 19.55 C
ATOM 2262 O THR A 222 12.611 34.475 45.925 .00 19.53 O
ATOM 2264 N ASP A 223 11.439 33.577 44.224 .00 19.65 N
ATOM 2265 CA ASP A 223 12.601 33.417 43.342 .00 19.73 C
ATOM 2267 CB ASP A 223 13.123 34.769 42.857 .00 19.47 C
ATOM 2270 CG ASP A 223 12.087 35.573 42.112 .00 19.81 C
ATOM 2271 ODl ASP A 223 11.192 34.997 41.446 .00 18.84 O
ATOM 2272 OD2 ASP A 223 12.183 36.811 42.191 .00 21.42 O
ATOM 2273 C ASP A 223 13.725 32.708 44.060 .00 19.93 C
ATOM 2274 O ASP A 223 14.817 33.249 44.174 1.00 19.93 O
ATOM 2276 N THR A 224 13.453 31.500 44.545 1.00 20.13 N
ATOM 2277 CA THR A 224 14.421 30.755 45.337 1.00 20.25 C
ATOM 2279 CB THR A 224 13.984 30.720 46.814 1.00 20.36 C
ATOM 2281 OGl THR A 224 12.618 30.287 46.907 1.00 20.55 O
ATOM 2283 CG2 THR A 224 14.099 32.107 47.435 1.00 19.92 C
ATOM 2287 C THR A 224 14.581 29.334 44.797 20.57 C
ATOM 2288 O THR A 224 13.601 28.697 44.409 20.58 O
ATOM 2290 N LEU A 225 15.821 28.856 44.738 20.80 N
ATOM 2291 CA LEU A 225 16.094 27.481 44.370 21.06 C
ATOM 2293 CB LEU A 225 17.520 27.331 43.851 21.15 C
ATOM 2296 CG LEU A 225 17.958 25.917 43.451 21.20 C
ATOM 2298 CDl LEU A 225 17.315 25.506 42.136 22.15 C
ATOM 2302 CD2 LEU A 225 19.452 25.840 43.328 21.02 C
ATOM 2306 C LEU A 225 15.926 26.649 45.616 21.34 C
ATOM 2307 O LEU A 225 16.767 26.692 46.495 21.57 O
ATOM 2309 N VAL A 226 14.848 25.886 45.702 21.88 N
ATOM 2310 CA VAL A 226 14.557 25.160 46.932 22.32 C
ATOM 2312 CB VAL A 226 13.087 24.733 47.026 22.34 C
ATOM 2314 CGl VAL A 226 12.794 24.181 48.429 21.67 C
ATOM 2318 CG2 VAL A 226 12.168 25.904 46.691 1.00 22.14 C
ATOM 2322 C VAL A 226 15.431 23.919 47.095 23.04 C
ATOM 2323 O VAL A 226 15.897 23.625 48.204 23.24 O
ATOM 2325 N ALA A 227 15.648 23.187 46.003 23.51 N
ATOM 2326 CA ALA A 227 16.382 21.926 46.083 23.74 C
ATOM 2328 CB ALA A 227 15.468 20.818 46.657 1.00 23.37 C
ATOM 2332 C ALA A 227 16.989 21.494 44.735 00 24.11 C
ATOM 2333 O ALA A 227 16.511 21.867 43.667 00 23.82 O
ATOM 2335 N ILE A 228 18.068 20.722 44.820 00 24.63 N
ATOM 2336 CA ILE A 228 18.687 20.100 43.671 00 25.03 C
ATOM 2338 CB ILE A 228 20.133 20.578 43.472 00 24.90 C
ATOM 2340 CGl ILE A 228 20.213 22.101 43.627 00 25.18 C
ATOM 2343 CDl ILE A 228 21.609 22.666 43.545 00 24.84 C
ATOM 2347 CG2 ILE A 228 20.636 20.157 42.101 00 24.38 C
ATOM 2351 C ILE A 228 18.677 18.602 43.922 00 25.61 C
ATOM 2352 O ILE A 228 19.053 18.150 45.000 00 25.59 O
ATOM 2354 N PHE A 229 18.218 17.841 42.935 00 26.40 N
ATOM 2355 CA PHE A 229 18.178 16.390 43.024 1.00 26.92 C
ATOM 2357 CB PHE A 229 16.782 15.844 42.732 1.00 26.73 C
ATOM 2360 CG PHE A 229 15.681 16.554 43.463 1.00 26.15 C
ATOM 2361 CDl PHE A 229 15.112 15.996 44.593 1.00 25.77 C
ATOM 2363 CEl PHE A 229 14.092 16.643 45.266 1.00 26.18 C
ATOM 2365 CZ PHE A 229 13.629 17.859 44.806 1.00 26.30 C
ATOM 2367 CE2 PHE A 229 14.186 18.424 43.670 .00 26.31 C
ATOM 2369 CD2 PHE A 229 15.203 17.772 43.005 .00 25.66 C
ATOM 2371 C PHE A 229 19.144 15.887 41.991 .00 27.50 C
ATOM 2372 O PHE A 229 18.956 16.111 40.805 .00 27.32 O
ATOM 2374 N GLY A 230 20.188 15.216 42.453 .00 28.85 N
ATOM 2375 CA GLY A 230 21.328 14.859 41.606 .00 29.80 C
ATOM 2378 C GLY A 230 22.308 14.039 42.411 1.00 30.70 C
ATOM 2379 O GLY A 230 21.891 13.273 43.257 1.00 31.23 O
ATOM 2381 N GLY A 231 23.604 14.198 42.162 1.00 31.79 N
ATOM 2382 CA GLY A 231 24.628 13.421 42.875 1.00 32.47 C
ATOM 2385 C GLY A 231 24.911 12.104 42.183 1.00 33.31 C
ATOM 2386 O GLY A 231 24.314 11.811 41.145 1.00 33.85 O ATOM 2388 N VAL A 232 25.805 11.300 42.762 .00 34.16 N
ATOM 2389 CA VAL A 232 26.277 10.054 42.118 ,00 34.64 C
ATOM 2391 CB VAL A 232 27.440 9.390 42.912 .00 34.96 C
ATOM 2393 CGl VAL A 232 27.884 8.087 42.231 ,00 34.77 C
ATOM 2397 CG2 VAL A 232 28.628 10.364 43.066 .00 35.43 C
ATOM 2401 C VAL A 232 25.152 9.024 41.937 ,00 35.15 C
ATOM 2402 O VAL A 232 25.048 8.391 40.876 .00 35.34 O
ATOM 2404 N GLU A 233 24.325 8.867 42.975 ,00 35.40 N
ATOM 2405 CA GLU A 233 23.146 7.998 42.925 ,00 35.53 C
ATOM 2407 CB GLU A 233 22.794 7.483 44.325 ,00 35.81 C
ATOM 2410 CG GLU A 233 23.891 6.607 44.937 ,00 37.00 C
ATOM 2413 CD GLU A 233 24.307 5.462 44.017 ,00 38.58 C
ATOM 2414 OEl GLU A 233 23.413 4.700 43.589 00 39.39 O
ATOM 2415 OE2 GLU A 233 25.517 5.329 43.715 00 39.59 O
ATOM 2416 C GLU A 233 21.944 8.698 42.293 ,00 35.57 C
ATOM 2417 O GLU A 233 20.880 8.092 42.135 00 35.52 O
ATOM 2419 N GLY A 234 22.114 9.972 41.939 1.00 35.37 N
ATOM 2420 CA GLY A 234 21.190 10.640 41.044 00 35.38 C
ATOM 2423 C GLY A 234 21.379 10.088 39.643 00 35.43 C
ATOM 2424 O GLY A 234 21.986 9.023 39.461 .00 35.39 O
ATOM 2426 N HIS A 235 20.873 10.818 38.650 00 35.37 N
ATOM 2427 CA HIS A 235 21.040 10.430 37.243 .00 35.29 C
ATOM 2429 CB HIS A 235 20.116 11.260 36.337 00 35.13 C
ATOM 2432 CG HIS A 235 18.672 10.871 36.428 00 34.33 C
ATOM 2433 NDl HIS A 235 18.161 9.763 35.791 1.00 33.44 N
ATOM 2435 CEl HIS A 235 16.870 9.667 36.049 1.00 33.48 C
ATOM 2437 NE2 HIS A 235 16.526 10.673 36.831 1.00 33.56 N
ATOM 2439 CD2 HIS A 235 17.634 11.443 37.080 1.00 33.66 C
ATOM 2441 C HIS A 235 22.490 10.561 36.760 1.00 35.26 C
ATOM 2442 O HIS A 235 23.105 11.616 36.899 1.00 35.44 O
ATOM 2444 N ARG A 236 23.015 9.493 36.166 1.00 35.26 N
ATOM 2445 CA ARG A 236 24.381 9.490 35.630 1.00 35.31 C
ATOM 2447 CB ARG A 236 24.976 8.081 35.726 35.65 C
ATOM 2450 CG ARG A 236 24.999 7.519 37.142 36.26 C
ATOM 2453 CD ARG A 236 25.577 6.102 37.183 37.42 C
ATOM 2456 NE ARG A 236 25.645 5.583 38.556 1.00 39.20 N
ATOM 2458 CZ ARG A 236 26.582 5.905 39.459 1.00 40.95 C
ATOM 2459 NHl ARG A 236 27.566 6.752 39.150 1.00 41.76 N
ATOM 2462 NH2 ARG A 236 26.537 5.379 40.688 1.00 40.90 N
ATOM 2465 C ARG A 236 24.471 10.002 34.184 1.00 34.72 C
ATOM 2466 O ARG A 236 25.487 9.801 33.527 1.00 34.61 O
ATOM 2468 N ASP A 237 23.417 10.666 33.697 1.00 34.28 N
ATOM 2469 CA ASP A 237 23.382 11.234 32.336 1.00 33.88 C
ATOM 2471 CB ASP A 237 23.224 10.110 31.302 33.77 C
ATOM 2474 CG ASP A 237 23.774 10.475 29.936 34.04 C
ATOM 2475 ODl ASP A 237 23.942 11.673 29.632 33.84 O
ATOM 2476 OD2 ASP A 237 24.021 9.547 29.144 35.24 O
ATOM 2477 C ASP A 237 22.235 12.253 32.226 33.28 C
ATOM 2478 O ASP A 237 21.581 12.551 33.218 32.96 O
ATOM 2480 N GLU A 238 22.003 12.797 31.032 33.16 N
ATOM 2481 CA GLU A 238 20.945 13.791 30.823 33.20 C
ATOM 2483 CB GLU A 238 20.686 14.027 29.348 33.12 C
ATOM 2486 CG GLU A 238 21.766 14.723 28.600 33.75 C
ATOM 2489 CD GLU A 238 21.219 15.486 27.403 34.12 C
ATOM 2490 OEl GLU A 238 20.160 16.140 27.561 35.46 O
ATOM 2491 OE2 GLU A 238 21.852 15.453 26.320 34.92 O
ATOM 2492 C GLU A 238 19.622 13.331 31.390 32.96 C
ATOM 2493 O GLU A 238 19.194 12.205 31.127 32.99 O
ATOM 2495 N VAL A 239 18.960 14.211 32.135 32.57 N
ATOM 2496 CA VAL A 239 17.592 13.949 32.573 32.10 C
ATOM 2498 CB VAL A 239 17.299 14.554 33.959 32.17 C
ATOM 2500 CGl VAL A 239 15.965 14.032 34.485 31.86 C
ATOM 2504 CG2 VAL A 239 18.428 14.217 34.927 1.00 31.94 C
ATOM 2508 C VAL A 239 16.658 14.530 31.508 1.00 31.69 C
ATOM 2509 O VAL A 239 16.783 15.705 31.129 1.00 31.64 O
ATOM 2511 N LEU A 240 15.753 13.695 31.001 1.00 30.91 N
ATOM 2512 CA LEU A 240 14.910 14.077 29.869 1.00 30.41 C
ATOM 2514 CB LEU A 240 14.908 12.975 28.801 1.00 30.53 C
ATOM 2517 CG LEU A 240 16.234 12.741 28.055 1.00 31.43 C
ATOM 2519 CDl LEU A 240 16.018 11.798 26.862 1.00 32.26 C
ATOM 2523 CD2 LEU A 240 16.873 14.048 27.580 31.90 C
ATOM 2527 C LEU A 240 13.481 14.435 30.276 29.66 C
ATOM 2528 O LEU A 240 12.870 15.302 29.666 29.36 O
ATOM 2530 N SER A 241 12.951 13.786 31.306 28.96 N
ATOM 2531 CA SER A 241 11.580 14.046 31.719 28.37 C
ATOM 2533 CB SER A 241 10.609 13.203 30.877 28.47 C
ATOM 2536 OG SER A 241 9.314 13.774 30.823 1.00 28.04 O ATOM 2538 C SER A 241 11.360 13.769 33.198 1.00 27.87 C
ATOM 2539 O SER A 241 12.018 12.901 33.781 1.00 28.01 O
ATOM 2541 N ALA A 242 10.426 14.520 33.786 1.00 27.04 N
ATOM 2542 CA ALA A 242 10.015 14.337 35.179 1.00 26.21 C
ATOM 2544 CB ALA A 242 10.845 15.218 36.099 1.00 26.12 C
ATOM 2548 C ALA A 242 8.540 14.669 35.315 1.00 25.36 C
ATOM 2549 O ALA A 242 7.990 15.395 34.489 1.00 24.93 O
ATOM 2551 N ASP A 243 7.905 14.132 36.353 1.00 24.71 N
ATOM 2552 CA ASP A 243 6.476 14.361 36.590 1.00 24.42 C
ATOM 2554 CB ASP A 243 5.626 13.356 35.788 1.00 24.47 C
ATOM 2557 CG ASP A 243 4.146 13.767 35.685 1.00 24.71 C
ATOM 2558 ODl ASP A 243 3.862 14.874 35.180 1.00 25.36 O
ATOM 2559 OD2 ASP A 243 3.262 12.977 36.090 1.00 24.27 O
ATOM 2560 C ASP A 243 6.135 14.263 38.080 1.00 23.84 C
ATOM 2561 O ASP A 243 6.618 13.374 38.774 1.00 23.65 O
ATOM 2563 N TYR A 244 5.317 15.196 38.562 1.00 23.27 N
ATOM 2564 CA TYR A 244 4.728 15.096 39.888 1.00 23.04 C
ATOM 2566 CB TYR A 244 4.126 16.428 40.325 1.00 22.41 C
ATOM 2569 CG TYR A 244 5.055 17.600 40.491 1.00 21.51 C
ATOM 2570 CDl TYR A 244 5.708 17.828 41.688 1.00 21.73 C
ATOM 2572 CEl TYR A 244 6.526 18.938 41.865 1.00 21.38 C
ATOM 2574 CZ TYR A 244 6.680 19.838 40.837 1.00 21.37 C
ATOM 2575 OH TYR A 244 7.490 20.944 40.992 1.00 21.31 O
ATOM 2577 CE2 TYR A 244 6.019 19.639 39.650 1.00 21.40 C
ATOM 2579 CD2 TYR A 244 5.203 18.531 39.491 1.00 20.97 C
ATOM 2581 C TYR A 244 3.573 14.086 39.871 1.00 23.00 C
ATOM 2582 O TYR A 244 2.802 14.029 38.901 1.00 23.17 O
ATOM 2584 N ASP A 245 3.424 13.329 40.956 1.00 22.96 N
ATOM 2585 CA ASP A 245 2.191 12.594 41.206 1.00 23.02 C
ATOM 2587 CB ASP A 245 2.335 11.644 42.392 1.00 22.85 C
ATOM 2590 CG ASP Ά 245 2.313 12.359 43.733 1.00 22.74 C
ATOM 2591 ODl ASP A 245 2.554 13.580 43.779 1.00 23.17 O
ATOM 2592 OD2 ASP A 245 2.062 11.692 44.757 1.00 21.45 O
ATOM 2593 C ASP A 245 1.073 13.591 41.464 1.00 23.22 C
ATOM 2594 O ASP A 245 1.319 14.788 41.588 1.00 23.08 O
ATOM 2596 N LEU A 246 -0.148 13.083 41.564 1.00 23.82 N
ATOM 2597 CA LEU A 246 -1.359 13.913 41.568 1.00 23.98 C
ATOM 2599 CB LEU A 246 -2.601 13.004 41.537 1.00 24.12 C
ATOM 2602 CG LEU A 246 -3.982 13.469 42.020 1.00 24.41 C
ATOM 2604 CDl LEU A 246 -5.101 12.880 41.181 1.00 24.30 C
ATOM 2608 CD2 LEU A 246 -4.181 13.094 43.492 1.00 25.71 C
ATOM 2612 C LEU A 246 -1.407 14.926 42.716 1.00 24.15 C
ATOM 2613 O LEU A 246 -1.751 16.080 42.508 1.00 24.18 O
ATOM 2615 N LEU A 247 -1.035 14.508 43.916 1.00 24.59 N
ATOM 2616 CA LEU A 247 -0.969 15.433 45.056 1.00 24.93 C
ATOM 2618 CB LEU A 247 -1.072 14.654 46.375 1.00 25.09 C
ATOM 2621 CG LEU A 247 -2.305 13.763 46.535 1.00 25.70 C
ATOM 2623 CDl LEU A 247 -2.339 13.120 47.909 1.00 25.93 C
ATOM 2627 CD2 LEU A 247 -3.566 14.572 46.297 1.00 26.34 C
ATOM 2631 C LEU A 247 0.317 16.263 45.082 1.00 24.96 C
ATOM 2632 O LEU A 247 0.485 17.116 45.946 1.00 24.99 O
ATOM 2634 N GLY A 248 1.236 16.003 44.163 1.00 25.13 N
ATOM 2635 CA GLY A 248 2.520 16.688 44.176 1.00 25.50 C
ATOM 2638 C GLY A 248 3.328 16.384 45.428 1.00 25.79 C
ATOM 2639 O GLY A 248 3.976 17.273 45.980 1.00 26.00 O
ATOM 2641 N GLU A 249 3.293 15.123 45.861 1.00 25.93 N
ATOM 2642 CA GLU A 249 4.058 14.646 47.020 1.00 26.08 C
ATOM 2644 CB GLU A 249 3.205 13.686 47.843 1.00 25.99 C
ATOM 2647 CG GLU A 249 2.274 14.394 48.784 1.00 26.66 C
ATOM 2650 CD GLU A 249 1.229 13.476 49.380 1.00 27.10 C
ATOM 2651 OEl GLU A 249 1.426 12.235 49.350 1.00 28.35 O
ATOM 2652 OE2 GLU A 249 0.203 14.009 49.869 1.00 28.45 O
ATOM 2653 C GLU A 249 5.365 13.944 46.647 1.00 25.97 C
ATOM 2654 O GLU A 249 6.219 13.714 47.506 1.00 25.96 O
ATOM 2656 N LYS A 250 5.511 13.590 45.377 1.00 25.90 N
ATOM 2657 CA LYS A 250 6.702 12.903 44.907 1.00 25.92 C
ATOM 2659 CB LYS A 250 6.585 11.401 45.154 1.00 25.81 C
ATOM 2662 CG LYS A 250 5.264 10.799 44.667 1.00 26.01 C
ATOM 2665 CD LYS A 250 5.141 9.314 44.995 1.00 25.66 C
ATOM 2668 CE LYS A 250 3.723 8.806 44.786 1.00 24.69 C
ATOM 2671 NZ LYS A 250 2.860 9.116 45.942 1.00 23.08 N
ATOM 2675 C LYS A 250 6.892 13.172 43.424 1.00 25.98 C
ATOM 2676 O LYS A 250 5.940 13.477 42.711 1.00 25.74 O
ATOM 2678 N ILE A 251 8.139 13.074 42.986 1.00 26.19 N
ATOM 2679 CA ILE A 251 8.506 13.254 41.600 1.00 26.28 C
ATOM 2681 CB ILE A 251 9.619 14.307 41.448 1.00 26.21 C
ATOM 2683 CGl ILE A 251 9.175 15.667 42.001 1.00 26.20 C ATOM 2686 CDl ILE A 251 10.255 16.758 41.905 1.00 25.56 C
ATOM 2690 CG2 ILE A 251 10.024 14.443 39.993 1.00 26.15 C
ATOM 2694 C ILE A 251 9.047 11.928 41.095 1.00 26.56 C
ATOM 2695 O ILE A 251 9.715 11.203 41.829 1.00 26.44 O
ATOM 2697 N MET A 252 8.745 11.612 39.843 1.00 27.00 N
ATOM 2698 CA MET A 252 9.418 10.539 39.141 1.00 27.41 C
ATOM 2700 CB MET A 252 8.402 9.531 38.599 1.00 27.44 C
ATOM 2703 CG MET A 252 9.027 8.257 38.022 1.00 27.46 C
ATOM 2706 SD MET A 252 9.877 7.210 39.242 1.00 27.25 S
ATOM 2707 CE MET A 252 8.520 6.250 39.895 1.00 26.82 C
ATOM 2711 C MET A 252 10.203 11.167 38.000 1.00 27.91 C
ATOM 2712 O MET A 252 9.655 11.953 37.230 1.00 28.09 O
ATOM 2714 N SER A 253 11.486 10.829 37.894 1.00 28.47 N
ATOM 2715 CA SER A 253 12.342 11.360 36.830 1.00 28.87 C
ATOM 2717 CB SER A 253 13.535 12.085 37.440 1.00 29.01 C
ATOM 2720 OG SER A 253 14.362 11.170 38.141 1.00 29.89 O
ATOM 2722 C SER A 253 12.842 10.245 35.921 1.00 29.07 C
ATOM 2723 O SER A 253 12.785 9.080 36.275 1.00 28.85 O
ATOM 2725 N CYS A 254 13.341 10.613 34.747 1.00 29.63 N
ATOM 2726 CA CYS A 254 13.852 9.632 33.796 1.00 30.12 C
ATOM 2728 CB CYS A 254 12.697 8.990 33.026 1.00 30.28 C
ATOM 2731 SG CYS A 254 11.889 10.068 31.821 1.00 31.02 S
ATOM 2733 C CYS A 254 14.836 10.287 32.840 1.00 30.37 C
ATOM 2734 O CYS A 254 14.765 11.494 32.627 1.00 30.53 O
ATOM 2736 N GLY A 255 15.753 9.500 32.274 1.00 30.64 N
ATOM 2737 CA GLY A 255 16.785 10.053 31.395 1.00 30.96 C
ATOM 2740 C GLY A 255 17.632 9.081 30.577 1.00 31.35 C
ATOM 2741 O GLY A 255 17.273 7.914 30.380 1.00 31.21 O
ATOM 2743 N MET A 256 18.779 9.583 30.110 1.00 31.72 N
ATOM 2744 CA MET A 256 19.628 8.864 29.164 1.00 31.78 C
ATOM 2746 CB MET A 256 20.595 9.825 28.480 1.00 31.85 C
ATOM 2749 CG MET A 256 19.928 10.696 27.452 1.00 32.18 C
ATOM 2752 SD MET A 256 21.093 11.738 26.573 1.00 32.53 S
ATOM 2753 CE MET A 256 20.036 12.356 25.266 1.00 32.55 C
ATOM 2757 C MET A 256 20.405 7.715 29.778 1.00 31.95 C
ATOM 2758 O ' MET A 256 20.927 6.869 29.049 1.00 32.23 O
ATOM 2760 N ASP A 257 20.484 7.672 31.105 1.00 31.96 N
ATOM 2761 CA ASP A 257 21.055 6.519 31.798 1.00 31.92 C
ATOM 2763 CB ASP A 257 21.656 6.956 33.148 1.00 31.88 C
ATOM 2766 CG ASP A 257 20.610 7.523 34.115 1.00 31.72 C
ATOM 2767 ODl ASP A 257 19.522 7.914 33.649 1.00 32.50 O
ATOM 2768 OD2 ASP A 257 20.869 7.570 35.337 1.00 29.66 O
ATOM 2769 C ASP A 257 20.008 5.388 31.965 1.00 32.15 C
ATOM 2770 O ASP A 257 20.051 4.627 32.933 1.00 32.45 O
ATOM 2772 N HIS A 258 19.055 5.300 31.031 1.00 32.34 N
ATOM 2773 CA HIS A 258 18.065 4.209 30.969 1.00 32.29 C
ATOM 2775 CB HIS A 258 18.736 2.869 30.601 1.00 32.51 C
ATOM 2778 CG HIS A 258 19.510 2.885 29.314 1.00 33.25 C
ATOM 2779 NDl HIS A 258 19.990 4.042 28.732 1.00 35.08 N
ATOM 2781 CEl HIS A 258 20.651 3.741 27.626 1.00 34.48 C
ATOM 2783 NE2 HIS A 258 20.628 2.428 27.476 1.00 34.16 N
ATOM 2785 CD2 HIS A 258 19.928 1.869 28.520 1.00 33.37 C
ATOM 2787 C HIS A 258 17.274 4.020 32.270 1.00 32.22 C
ATOM 2788 O HIS A 258 16.629 2.988 32.447 1.00 32.54 O
ATOM 2790 N SER A 259 17.301 5.005 33.167 1.00 32.07 N
ATOM 2791 CA SER A 259 16.732 4.838 34.513 1.00 31.97 C
ATOM 2793 CB SER A 259 17.812 5.035 35.576 1.00 32.09 C
ATOM 2796 OG SER A 259 18.216 6.393 35.634 1.00 32.30 O
ATOM 2798 C SER A 259 15.570 5.785 34.836 1.00 31.88 C
ATOM 2799 O SER A 259 15.523 6.927 34.369 1.00 31.69 O
ATOM 2801 N LEU A 260 14.653 5.284 35.664 1.00 31.49 N
ATOM 2802 CA LEU A 260 13.560 6.062 36.221 1.00 31.00 C
ATOM 2804 CB LED A 260 12.227 5.443 35.811 1.00 30.94 C
ATOM 2807 CG LEU A 260 11.829 5.693 34.351 1.00 30.92 C
ATOM 2809 CDl LEU A 260 11.600 4.379 33.590 1.00 30.66 C
ATOM 2813 CD2 LEU A 260 10.604 6.611 34.257 1.00 30.25 C
ATOM 2817 C LEU A 260 13.706 6.086 37.752 1.00 30.87 C
ATOM 2818 O LEU A 260 13.873 5.034 38.377 1.00 30.94 O
ATOM 2820 N LYS A 261 13.633 7.284 38.341 1.00 30.32 N
ATOM 2821 CA LYS A 261 13.970 7.498 39.748 1.00 29.82 C
ATOM 2823 CB LYS A 261 15.321 8.216 39.845 1.00 29.96 C
ATOM 2826 CG LYS A 261 16.511 7.304 39.615 1.00 30.21 C
ATOM 2829 CD LYS A 261 17.797 8.071 39.342 1.00 30.21 C
ATOM 2832 CE LYS A 261 18.963 7.115 39.133 1.00 30.31 C
ATOM 2835 NZ LYS A 261 19.350 6.443 40.412 1.00 31.17 N
ATOM 2839 C LYS A 261 12.909 8.300 40.506 1.00 29.31 C
ATOM 2840 O LYS A 261 12.378 9.297 40.003 1.00 28.95 O ATOM 2842 N LEU A 262 12.628 7.864 41.731 1.00 28.69 N
ATOM 2843 CA LEU A 262 11.619 8.497 42.565 1.00 28.31 C
ATOM 2845 CB LEU A 262 10.823 7.445 43.331 1.00 28.28 C
ATOM 2848 CG LEU A 262 9.595 7.996 44.050 1.00 28.56 C
ATOM 2850 CDl LEU A 262 8.585 8.399 43.003 1.00 28.88 C
ATOM 2854 CD2 LEU A 262 8.991 6.999 45.038 1.00 28.31 C
ATOM 2858 C LEU A 262 12.272 9.430 43.563 1.00 27.98 C
ATOM 2859 O LEU A 262 13.285 9.096 44.170 1.00 28.31 O
ATOM 2861 N TRP A 263 11.680 10.598 43.740 1.00 27.33 N
ATOM 2862 CA TRP A 263 12.138 11.528 44.739 1.00 26.95 C
ATOM 2864 CB TRP A 263 12.798 12.724 44.085 1.00 26.39 C
ATOM 2867 CG TRP A 263 13.763 12.419 43.004 1.00 25.73 C
ATOM 2868 CDl TRP A 263 13.479 12.202 41.689 1.00 25.37 C
ATOM 2870 NEl TRP A 263 14.634 12.000 40.982 1.00 25.08 N
ATOM 2872 CE2 TRP A 263 15.698 12.094 41.836 1.00 25.47 C
ATOM 2873 CD2 TRP A 263 15.183 12.366 43.123 1.00 25.34 C
ATOM 2874 CE3 TRP A 263 16.073 12.509 44.194 1.00 25.29 C
ATOM 2876 CZ3 TRP A 263 17.432 12.380 43.949 1.00 25.60 C
ATOM 2878 CH2 TRP A 263 17.916 12.106 42.654 1.00 25.63 C
ATOM 2880 CZ2 TRP A 263 17.067 11.960 41.589 1.00 25.51 C
ATOM 2882 C TRP A 263 10.930 12.011 45.486 1.00 26.75 C
ATOM 2883 O TRP A 263 10.077 12.656 44.902 1.00 26.96 O
ATOM 2885 N ARG A 264 10.837 11.703 46.767 1.00 26.81 N
ATOM 2886 CA ARG A 264 9.720 12.184 47.557 1.00 27.24 C
ATOM 2888 CB ARG A 264 9.534 11.320 48.793 1.00 27.47 C
ATOM 2891 CG ARG A 264 9.282 9.865 48.463 1.00 28.24 C
ATOM 2894 CD ARG A 264 9.210 8.998 49.716 1.00 28.51 C
ATOM 2897 NE ARG A 264 9.172 7.574 49.373 1.00 29.38 N
ATOM 2899 CZ ARG A 264 8.103 6.919 48.916 1.00 29.87 C
ATOM 2900 NHl ARG A 264 6.945 7.545 48.726 1.00 30.16 N
ATOM 2903 NH2 ARG A 264 8.195 5.620 48.639 1.00 30.37 N
ATOM 2906 C ARG A 264 9.978 13.632 47.950 1.00 27.14 C
ATOM 2907 O ARG A 264 11.120 14.021 48.158 1.00 27.26 O
ATOM 2909 N ILE A 265 8.922 14.436 48.010 1.00 27.17 N
ATOM 2910 CA ILE A 265 9.031 15.818 48.473 1.00 27.15 C
ATOM 2912 CB ILE A 265 8.825 16.822 47.311 1.00 27.11 C
ATOM 2914 CGl ILE A 265 7.361 16.850 46.837 1.00 27.19 C
ATOM 2917 CDl ILE A 265 7.057 17.944 45.817 1.00 26.54 C
ATOM 2921 CG2 ILE A 265 9.762 16.479 46.159 1.00 26.55 C
ATOM 2925 C ILE A 265 8.074 16.126 49.628 1.00 27.27 C
ATOM 2926 O ILE A 265 7.918 17.273 50.013 1.00 27.13 O
ATOM 2928 N ASN A 266 7.456 15.092 50.185 1.00 27.52 N
ATOM 2929 CA ASN A 266 6.580 15.242 51.336 1.00 27.76 C
ATOM 2931 CB ASN A 266 5.318 14.380 51.167 1.00 27.79 C
ATOM 2934 CG ASN A 266 5.629 12.897 50.996 1.00 27.69 C
ATOM 2935 ODl ASN A 266 6.696 12.518 50.507 1.00 28.09 O
ATOM 2936 ND2 ASN A 266 4.687 12.055 51.386 1.00 27.31 N
ATOM 2939 C ASN A 266 7.284 14.905 52.644 1.00 27.94 C
ATOM 2940 O ASN A 266 6.659 14.933 53.696 1.00 28.20 O
ATOM 2942 N SER A 267 8.570 14.572 52.577 1.00 28.20 N
ATOM 2943 CA SER A 267 9.397 14.420 53.775 1.00 28.60 C
ATOM 2945 CB SER A 267 10.810 13.985 53.380 1.00 28.66 C
ATOM 2948 OG SER A 267 11.486 15.011 52.660 1.00 28.03 O
ATOM 2950 C SER A 267 9.486 15.755 54.532 1.00 29.05 C
ATOM 2951 O SER A 267 9.385 16.822 53.914 1.00 29.06 O
ATOM 2953 N LYS A 268 9.688 15.703 55.853 1.00 29.48 N
ATOM 2954 CA LYS A 268 9.827 16.951 56.646 1.00 29.75 C
ATOM 2956 CB LYS A 268 9.931 16.747 58.171 1.00 30.17 C
ATOM 2959 CG LYS A 268 10.411 15.397 58.681 1.00 32.13 C
ATOM 2962 CD LYS A 268 9.296 14.593 59.406 1.00 33.51 C
ATOM 2965 CE LYS A 268 7.964 14.567 58.638 1.00 34.34 C
ATOM 2968 NZ LYS A 268 7.144 13.366 58.997 1.00 34.69 N
ATOM 2972 C LYS A 268 10.993 17.801 56.164 1.00 29.58 C
ATOM 2973 O LYS A 268 10.898 19.026 56.136 1.00 29.40 O
ATOM 2975 N ARG A 269 12.074 17.152 55.759 1.00 29.39 N
ATOM 2976 CA ARG A 269 13.188 17.868 55.159 1.00 29.50 C
ATOM 2978 CB ARG A 269 14.238 16.889 54.636 1.00 29.26 C
ATOM 2981 CG ARG A 269 15.582 17.528 54.480 1.00 29.52 C
ATOM 2984 CD ARG A 269 16.552 16.706 53.651 1.00 30.00 C
ATOM 2987 NE ARG A 269 17.560 17.578 53.053 1.00 30.43 N
ATOM 2989 CZ ARG A 269 18.640 17.171 52.385 1.00 31.08 C
ATOM 2990 NHl ARG A 269 18.915 15.880 52.225 1.00 30.91 N
ATOM 2993 NH2 ARG A 269 19.469 18.082 51.884 1.00 31.47 N
ATOM 2996 C ARG A 269 12.701 18.795 54.032 1.00 29.49 C
ATOM 2997 O ARG A 269 12.919 20.006 54.076 1.00 29.69 O
ATOM 2999 N MET A 270 12.006 18.231 53.050 1.00 29.42 N
ATOM 3000 CA MET A 270 11.541 19.009 51.902 1.00 29.31 C ATOM 3002 CB MET A 270 11.211 18.091 50.729 1.00 29.31 C
ATOM 3005 CG MET A 270 12.445 17.580 49.998 1.00 29.17 C
ATOM 3008 SD MET A 270 13.401 18.849 49.139 1.00 29.14 S
ATOM 3009 CE MET A 270 12.127 19.655 48.160 1.00 27.52 C
ATOM 3013 C MET A 270 10.348 19.909 52.206 1.00 29.21 C
ATOM 3014 O MET A 270 10.271 21.017 51.682 1.00 29.07 O
ATOM 3016 N MET A 271 9.417 19.444 53.034 1.00 29.16 N
ATOM 3017 CA MET A 271 8.299 20.291 53.442 1.00 29.39 C
ATOM 3019 CB MET A 271 7.336 19.531 54.341 1.00 29.36 C
ATOM 3022 CG MET A 271 6.534 18.470 53.628 1.00 30.14 C
ATOM 3025 SD MET A 271 5.451 17.562 54.767 1.00 31.69 S
ATOM 3026 CE MET A 271 6.606 16.834 55.948 1.00 30.65 C
ATOM 3030 C MET A 271 8.814 21.512 54.186 1.00 28.99 C
ATOM 3031 O MET A 271 8.278 22.602 54.056 1.00 28.91 O
ATOM 3033 N ASN A 272 9.860 21.309 54.976 1.00 29.08 N
ATOM 3034 CA ASN A 272 10.488 22.389 55.724 1.00 28.68 C
ATOM 3036 CB ASN A 272 11.441 21.799 56.773 1.00 28.90 C
ATOM 3039 CG ASN A 272 12.261 22.849 57.475 1.00 29.84 C
ATOM 3040 ODl ASN A 272 11.727 23.669 58.236 1.00 32.29 O
ATOM 3041 ND2 ASN A 272 13.576 22.840 57.225 1.00 30.64 N
ATOM 3044 C ASN A 272 11.227 23.333 54.777 1.00 28.11 C
ATOM 3045 O ASN A 272 11.190 24.541 54.948 1.00 27.84 O
ATOM 3047 N ALA A 273 11.887 22.769 53.774 1.00 27.64 N
ATOM 3048 CA ALA A 273 12.609 23.563 52.789 1.00 27.55 C
ATOM 3050 CB ALA A 273 13.387 22.648 51.834 1.00 27.45 C
ATOM 3054 C ALA A 273 11.660 24.474 52.007 1.00 27.37 C
ATOM 3055 O ALA A 273 11.997 25.619 51.701 1.00 27.18 O
ATOM 3057 N ILE A 274 10.472 23.964 51.686 1.00 27.14 N
ATOM 3058 CA ILE A 274 9.471 24.750 50.968 1.00 27.09 C
ATOM 3060 CB ILE A 274 8.339 23.863 50.397 1.00 26.92 C
ATOM 3062 CGl ILE A 274 8.897 22.931 49.304 1.00 26.87 C
ATOM 3065 CDl ILE A 274 8.035 21.737 48.982 1.00 26.18 C
ATOM 3069 CG2 ILE A 274 7.228 24.725 49.826 1.00 26.60 C
ATOM 3073 C ILE A 274 8.903 25.819 51.890 1.00 27.20 C
ATOM 3074 O ILE A 274 8.690 26.960 51.469 1.00 26.84 O
ATOM 3076 N LYS A 275 8.675 25.453 53.149 1.00 27.62 N
ATOM 3077 CA LYS A 275 8.249 26.422 54.149 1.00 28.03 C
ATOM 3079 CB LYS A 275 8.158 25.785 55.535 1.00 27.95 C
ATOM 3082 CG LYS A 275 7.541 26.694 56.582 1.00 28.46 C
ATOM 3085 CD LYS A 275 7.448 26.025 57.976 1.00 29.80 C
ATOM 3088 CE LYS A 275 8.619 26.390 58.924 1.00 31.79 C
ATOM 3091 NZ LYS A 275 9.918 25.693 58.596 1.00 32.71 N
ATOM 3095 C LYS A 275 9.241 27.580 54.163 1.00 28.08 C
ATOM 3096 O LYS A 275 8.862 28.730 53.960 1.00 28.23 O
ATOM 3098 N GLϋ A 276 10.515 27.265 54.363 1.00 28.11 N
ATOM 3099 CA ,GLU A 276 11.552 28.286 54.400 1.00 28.18 C
ATOM 3101 CB GLϋ A 276 12.933 27.667 54.648 1.00 28.14 C
ATOM 3104 CG GLO A 276 13.100 27.035 56.030 1.00 27.84 C
ATOM 3107 CD GLϋ A 276 12.961 28.024 57.175 1.00 27.55 C
ATOM 3108 OEl GLϋ A 276 13.303 29.220 57.016 1.00 26.65 O
ATOM 3109 OE2 GLϋ A 276 12.499 27.593 58.245 1.00 28.11 O
ATOM 3110 C GLϋ A 276 11.569 29.113 53.119 1.00 28.43 C
ATOM 3111 O GLU A 276 11.647 30.342 53.185 1.00 28.85 O
ATOM 3113 N SER A 277 11.475 28.457 51.962 1.00 28.44 N
ATOM 3114 CA SER A 277 11.478 29.171 50.673 1.00 28.37 C
ATOM 3116 CB SER A 277 11.193 28.227 49.502 1.00 28.35 C
ATOM 3119 OG SER A 277 9.802 27.983 49.373 1.00 27.93 O
ATOM 3121 C SER A 277 10.449 30.292 50.660 1.00 28.38 C
ATOM 3122 O SER A 277 10.699 31.359 50.101 1.00 28.32 O
ATOM 3124 N TYR A 278 9.293 30.040 51.271 1.00 28.47 N
ATOM 3125 CA TYR A 278 8.238 31.046 51.340 1.00 28.90 C
ATOM 3127 CB TYR A 278 6.881 30.404 51.633 1.00 28.34 C
ATOM 3130 CG TYR A 278 6.190 29.922 50.386 1.00 27.87 C
ATOM 3131 CDl TYR A 278 5.982 28.572 50.156 1.00 27.68 C
ATOM 3133 CEl TYR A 278 5.350 28.129 48.999 1.00 28.01 C
ATOM 3135 CZ TYR A 278 4.924 29.047 48.053 1.00 28.01 C
ATOM 3136 OH TYR A 278 4.295 28.618 46.907 1.00 27.74 O
ATOM 3138 CE2 TYR A 278 5.130 30.393 48.256 1.00 28.03 C
ATOM 3140 CD2 TYR A 278 5.761 30.823 49.419 1.00 28.21 C
ATOM 3142 C TYR A 278 8.536 32.169 52.333 1.00 29.32 C
ATOM 3143 O TYR A 278 8.023 33.270 52.185 1.00 29.20 O
ATOM 3145 N ASP A 279 9.375 31.898 53.326 1.00 30.17 N
ATOM 3146 CA ASP A 279 9.808 32.937 54.261 1.00 30.74 C
ATOM 3148 CB ASP A 279 10.183 32.323 55.605 1.00 31.09 C
ATOM 3151 CG ASP A 279 9.131 32.568 56.647 1.00 32.91 C
ATOM 3152 ODl ASP A 279 9.144 33.680 57.239 1.00 35.07 O
ATOM 3153 OD2 ASP A 279 8.281 31.663 56.849 1.00 34.06 O ATOM 3154 C ASP A 279 10.962 33.815 53.771 1.00 31.03 C
ATOM 3155 O ASP A 279 11.162 34.910 54.300 1.00 31.12 O
ATOM 3157 N TYR A 280 11.715 33.361 52.773 1.00 31.19 N
ATOM 3158 CA TYR A 280 12.915 34.084 52.372 1.00 31.51 C
ATOM 3160 CB TYR A 280 13.831 33.212 51.511 1.00 31.21 C
ATOM 3163 CG TYR A 280 15.155 33.875 51.189 1.00 30.99 C
ATOM 3164 CDl TYR A 280 16.187 33.889 52.120 1.00 30.57 C
ATOM 3166 CEl TYR A 280 17.394 34.507 51.834 1.00 31.10 C
ATOM 3168 CZ TYR A 280 17.572 35.123 50.604 1.00 30.75 C
ATOM 3169 OH TYR A 280 18.763 35.731 50.317 1.00 30.78 O
ATOM 3171 CE2 TYR A 280 16.560 35.128 49.664 1.00 30.20 C
ATOM 3173 CD2 TYR A 280 15.367 34.503 49.955 1.00 30.29 C
ATOM 3175 C TYR A 280 12.591 35.378 51.636 1.00 31.98 C
ATOM 3176 O TYR A 280 11.937 35.360 50.596 1.00 32.27 O
ATOM 3178 N ASN A 281 13.051 36.496 52.196 1.00 32.67 N
ATOM 3179 CA ASN A 281 13.048 37.788 51.514 1.00 32.96 C
ATOM 3181 CB ASN A 281 11.987 38.707 52.118 1.00 33.04 C
ATOM 3184 CG ASN A 281 11.912 40.059 51.423 1.00 33.11 C
ATOM 3185 ODl ASN A 281 12.563 40.300 50.393 1.00 33.13 O
ATOM 3186 ND2 ASN A 281 11.110 40.952 51.988 1.00 33.76 N
ATOM 3189 C ASN A 281 14.434 38.441 51.627 1.00 33.41 C
ATOM 3190 O ASN A 281 14.836 38.879 52.716 1.00 33.36 O
ATOM 3192 N PRO A 282 15.166 38.521 50.503 1.00 33.85 N
ATOM 3193 CA PRO A 282 16.556 38.986 50.562 1.00 34.13 C
ATOM 3195 CB PRO A 282 17.031 38.901 49.105 1.00 34.05 C
ATOM 3198 CG PRO A 282 15.803 38.793 48.281 1.00 34.06 C
ATOM 3201 CD PRO A 282 14.743 38.189 49.131 1.00 33.95 C
ATOM 3204 C PRO A 282 16.718 40.404 51.113 1.00 34.52 C
ATOM 3205 O PRO A 282 17.746 40.713 51.719 1.00 34.76 O
ATOM 3206 N ASN A 283 15.713 41.251 50.917 1.00 34.91 N
ATOM 3207 CA ASN A 283 15.734 42.607 51.483 1.00 35.11 C
ATOM 3209 CB ASN A 283 14.606 43.446 50.899 1.00 35.29 C
ATOM 3212 CG ASN A 283 14.648 43.480 49.395 1.00 36.28 C
ATOM 3213 ODl ASN A 283 15.689 43.203 48.794 1.00 37.26 O
ATOM 3214 ND2 ASN A 283 13.519 43.799 48.773 1.00 37.28 N
ATOM 3217 C ASN A 283 15.643 42.624 53.003 1.00 35.18 C
ATOM 3218 O ASN A 283 16.236 43.484 53.649 1.00 35.64 O
ATOM 3220 N LYS A 284 14.929 41.657 53.565 1.00 34.99 N
ATOM 3221 CA LYS A 284 14.724 41.574 55.007 1.00 34.90 C
ATOM 3223 CB LYS A 284 13.281 41.122 55.265 1.00 35.48 C
ATOM 3226 CG LYS A 284 12.227 42.189 54.910 1.00 36.90 C
ATOM 3229 CD LYS A 284 11.715 42.939 56.166 1.00 38.94 C
ATOM 3232 CE LYS A 284 11.813 44.458 56.014 1.00 39.78 C
ATOM 3235 NZ LYS A 284 11.092 44.978 54.812 1.00 39.93 N
ATOM 3239 C LYS A 284 15.716 40.634 55.717 1.00 34.50 C
ATOM 3240 O LYS A 284 15.469 40.217 56.850 1.00 34.40 O
ATOM 3242 N THR A 285 16.833 40.306 55.060 1.00 34.08 N
ATOM 3243 CA THR A 285 17.844 39.396 55.634 1.00 33.39 C
ATOM 3245 CB THR A 285 17.377 37.924 55.586 1.00 33.28 C
ATOM 3247 OGl THR A 285 18.286 37.112 56.336 1.00 32.94 O
ATOM 3249 CG2 THR A 285 17.317 37.413 54.153 1.00 32.94 C
ATOM 3253 C THR A 285 19.205 39.491 54.937 1.00 32.89 C
ATOM 3254 O THR A 285 19.315 39.992 53.819 1.00 32.63 O
ATOM 3256 N ASN A 286 20.235 38.990 55.611 1.00 32.48 N
ATOM 3257 CA ASN A 286 21.601 38.984 55.070 1.00 32.16 C
ATOM 3259 CB ASN A 286 22.602 39.398 56.139 1.00 32.17 C
ATOM 3262 CG ASN A 286 22.298 40.752 56.723 1.00 33.04 C
ATOM 3263 ODl ASN A 286 22.089 40.874 57.931 1.00 35.20 O
ATOM 3264 ND2 ASN A 286 22.250 41.779 55.872 1.00 32.80 N
ATOM 3267 C ASN A 286 22.040 37.638 54.525 1.00 31.64 C
ATOM 3268 O ASN A 286 23.089 37.540 53.900 1.00 31.57 O
ATOM 3270 N ARG A 287 21.256 36.598 54.771 1.00 31.27 N
ATOM 3271 CA ARG A 287 21.625 35.266 54.323 1.00 30.97 C
ATOM 3273 CB ARG A 287 20.953 34.189 55.185 1.00 30.96 C
ATOM 3276 CG ARG A 287 19.460 34.002 54.946 1.00 30.83 C
ATOM 3279 CD ARG A 287 18.784 33.304 56.135 1.00 31.14 C
ATOM 3282 NE ARG A 287 17.332 33.518 56.146 1.00 31.49 N
ATOM 3284 CZ ARG A 287 16.404 32.587 55.920 1.00 31.33 C
ATOM 3285 NHl ARG A 287 16.731 31.327 55.653 1.00 32.06 N
ATOM 3288 NH2 ARG A 287 15.121 32.930 55.961 1.00 31.03 N
ATOM 3291 C ARG A 287 21.246 35.071 52.864 1.00 30.54 C
ATOM 3292 O ARG A 287 20.306 35.692 52.379 1.00 30.66 O
ATOM 3294 N PRO A 288 21.982 34.201 52.163 1.00 29.94 N
ATOM 3295 CA PRO A 288 21.502 33.687 50.899 1.00 29.58 C
ATOM 3297 CB PRO A 288 22.770 33.147 50.247 1.00 29.56 C
ATOM 3300 CG PRO A 288 23.585 32.672 51.391 1.00 29.83 C
ATOM 3303 CD PRO A 288 23.280 33.611 52.536 1.00 29.94 C ATOM 3306 C PRO A 288 20.552 32.552 51.230 1.00 29.21 C
ATOM 3307 O PRO A 288 20.606 32.018 52.345 1.00 29.21 O
ATOM 3308 N PHE A 289 19.687 32.179 50.300 00 28.62 N
ATOM 3309 CA PHE A 289 18.827 31.039 50.547 00 28.35 C
ATOM 3311 CB PHE A 289 17.584 31.068 49.667 00 28.19 C
ATOM 3314 CG PHE A 289 16.594 30.010 50.032 00 28.41 C
ATOM 3315 CDl PHE A 289 15.852 30.121 51.203 00 27.95 C
ATOM 3317 CEl PHE A 289 14.964 29.131 51.573 00 28.08 C
ATOM 3319 CZ PHE A 289 14.820 28.005 50.778 00 28.03 C
ATOM 3321 CE2 PHE A 289 15.570 27.878 49.618 00 28.16 C
ATOM 3323 CD2 PHE A 289 16.454 28.871 49.253 00 28.05 C
ATOM 3325 C PHE A 289 19.606 29.746 50.319 00 28.05 C
ATOM 3326 O PHE A 289 20.195 29.561 49.260 00 28.09 O
ATOM 3328 N ILE A 290 19.610 28.852 51.306 00 27.78 N
ATOM 3329 CA ILE A 290 20.314 27.578 51.159 00 27.83 C
ATOM 3331 CB ILE A 290 20.853 27.034 52.508 00 27.76 C
ATOM 3333 CGl ILE A 290 22.109 27.800 52.931 00 27.42 C
ATOM 3336 CDl ILE A 290 21.856 29.232 53.311 00 27.23 C
ATOM 3340 CG2 ILE A 290 21.214 25.558 52.399 00 27.26 C
ATOM 3344 C ILE A 290 19.417 26.532 50.509 00 27.84 C
ATOM 3345 O ILE A 290 18.355 26.204 51.040 00 27.68 O
ATOM 3347 N SER A 291 19.864 26.014 49.363 00 27.92 N
ATOM 3348 CA SER A 291 19.177 24.934 48.663 1.00 27.98 C
ATOM 3350 CB SER A 291 19.666 24.847 47.223 .00 28.08 C
ATOM 3353 OG SER A 291 19.491 26.082 46.550 .00 28.98 O
ATOM 3355 C SER A 291 19.465 23.611 49.319 .00 27.94 C
ATOM 3356 O SER A 291 20.563 23.401 49.809 .00 27.98 O
ATOM 3358 N < GLN A 292 18.491 22.707 49.303 .00 28.26 N
ATOM 3359 CA GLN A 292 18.738 21.311 49.695 1.00 28.24 C
ATOM 3361 CB GLN A 292 17.446 20.542 49.981 1.00 28.09 C
ATOM 3364 CG GLN A 292 16.433 21.270 50.852 1.00 29.02 C
ATOM 3367 CD GLN A 292 16.929 21.527 52.259 1.00 30.18 C
ATOM 3368 OEl GLN A 292 17.380 20.608 52.931 1.00 31.89 O
ATOM 3369 NE2 GLN A 292 16.820 22.770 52.724 1.00 29.22 N
ATOM 3372 C GLN A 292 19.491 20.624 48.561 1.00 28.08 C
ATOM 3373 O GLN A 292 19.311 20.954 47.390 00 27.69 O
ATOM 3375 N LYS A 293 20.365 19.697 48.928 00 28.37 N
ATOM 3376 CA LYS A 293 21.035 18.832 47.963 00 28.50 C
ATOM 3378 CB LYS A 293 22.560 18.913 48.093 00 28.86 C
ATOM 3381 CG LYS A 293 23.170 20.246 47.657 00 29.83 C
ATOM 3384 CD LYS A 293 23.036 21.346 48.736 00 30.37 C
ATOM 3387 CE LYS A 293 23.549 22.691 48.221 00 30.29 C
ATOM 3390 NZ LYS A 293 22.928 23.857 48.889 00 30.52 N
ATOM 3394 C LYS A 293 20.554 17.419 48.249 00 28.29 C
ATOM 3395 O LYS A 293 20.937 16.825 49.251 00 28.02 O
ATOM 3397 N ILE A 294 19.687 16.906 47.387 00 28.03 N
ATOM 3398 CA ILE A 294 19.169 15.563 47.538 00 28.16 C
ATOM 3400 CB ILE A 294 17.660 15.503 47.229 00 27.75 C
ATOM 3402 CGl ILE A 294 16.907 16.629 47.961 00 26.69 C
ATOM 3405 CDl ILE A 294 17.044 16.630 49.448 00 24.05 C
ATOM 3409 CG2 ILE A 294 17.099 14.133 47.581 00 27.52 C
ATOM 3413 C ILE A 294 19.962 14.671 46.590 00 28.37 C
ATOM 3414 O ILE A 294 19.840 14.786 45.373 00 28.25 O
ATOM 3416 N HIS A 295 20.802 13.805 47.153 00 28.93 N
ATOM 3417 CA HIS A 295 21.674 12.927 46.348 00 29.17 C
ATOM 3419 CB HIS A 295 23.123 12.961 46.867 00 29.36 C
ATOM 3422 CG HIS A 295 23.842 14.245 46.586 00 29.97 C
ATOM 3423 NDl HIS A 295 24.861 14.712 47.384 00 29.63 N
ATOM 3425 CEl HIS A 295 25.302 15.862 46.908 00 30.98 C
ATOM 3427 NE2 HIS A 295 24.604 16.161 45.827 00 31.75 N
ATOM 3429 CD2 HIS A 295 23.681 15.166 45.605 00 31.33 C
ATOM 3431 C HIS A 295 21.194 11.481 46.281 00 29.07 C
ATOM 3432 O HIS A 295 21.872 10.635 45.694 00 28.73 O
ATOM 3434 N PHE A 296 20.031 11.202 46.874 00 29.39 N
ATOM 3435 CA PHE A 296 19.519 9.837 46.970 00 29.70 C
ATOM 3437 CB PHE A 296 19.836 9.255 48.349 00 29.76 C
ATOM 3440 CG PHE A 296 21.306 9.208 48.643 1.00 29.73 C
ATOM 3441 CDl PHE A 296 22.134 8.348 47.935 29.45 C
ATOM 3443 CEl PHE A 296 23.499 8.316 48.175 29.90 C
ATOM 3445 CZ PHE A 296 24.057 9.165 49.122 30.09 C
ATOM 3447 CE2 PHE A 296 23.246 10.034 49.831 30.10 C
ATOM 3449 CD2 PHE A 296 21.873 10.057 49.588 30.13 C
ATOM 3451 C PHE A 296 18.026 9.760 46.675 1.00 29.87 C
ATOM 3452 O PHE A 296 17.219 10.265 47.450 1.00 30.21 O
ATOM 3454 N PRO A 297 17.653 9.150 45.537 1.00 30.14 N
ATOM 3455 CA PRO A 297 16.238 8.900 45.266 1.00 30.52 C
ATOM 3457 CB PRO A 297 16.245 8.376 43.828 1.00 30.72 C ATOM 3460 CG PRO A 297 17.613 7.826 43.626 1.00 30.42 C
ATOM 3463 CD PRO A 297 18.516 8.691 44.432 1.00 29.92 C
ATOM 3466 C PRO A 297 15.658 7.846 46.192 1.00 30.77 C
ATOM 3467 O PRO A 297 16.399 7.025 46.709 1.00 30.80 O
ATOM 3468 N ASP A 298 14.342 7.856 46.382 1.00 31.28 N
ATOM 3469 CA ASP A 298 13.687 6.869 47.256 1.00 31.62 C
ATOM 3471 CB ASP A 298 12.481 7.484 47.950 1.00 31.79 C
ATOM 3474 CG ASP A 298 12.740 8.890 48.389 1.00 31.91 C
ATOM 3475 ODl ASP A 298 13.031 9.093 49.581 1.00 31.72 O
ATOM 3476 OD2 ASP A 298 12.688 9.780 47.514 1.00 32.54 O
ATOM 3477 C ASP A 298 13.268 5.607 46.504 1.00 31.81 C
ATOM 3478 O ASP A 298 12.654 4.718 47.085 1.00 31.66 O
ATOM 3480 N PHE A 299 13.579 5.562 45.212 1.00 32.16 N
ATOM 3481 CA PHE A 299 13.507 4.346 44.415 1.00 32.55 C
ATOM 3483 CB PHE A 299 12.060 3.879 44.205 1.00 32.63 C
ATOM 3486 CG PHE A 299 11.913 2.827 43.131 1.00 32.51 C
ATOM 3487 CDl PHE A 299 12.025 1.482 43.437 1.00 32.85 C
ATOM 3489 CEl PHE A 299 11.905 0.508 42.440 1.00 32.92 C
ATOM 3491 CZ PHE A 299 11.679 0.882 41.124 1.00 32.54 C
ATOM 3493 CE2 PHE A 299 11.572 2.221 40.804 1.00 32.77 C
ATOM 3495 CD2 PHE A 299 11.689 3.189 41.804 1.00 33.10 C
ATOM 3497 C PHE A 299 14.171 4.603 43.061 1.00 32.93 C
ATOM 3498 O PHE A 299 14.197 5.740 42.584 1.00 32.99 O
ATOM 3500 N SER A 300 14.695 3.539 42.452 1.00 33.17 N
ATOM 3501 CA SER A 300 15.301 3.616 41.137 1.00 33.59 C
ATOM 3503 CB SER A 300 16.744 4.097 41.262 1.00 33.62 C
ATOM 3506 OG SER A 300 17.366 4.205 39.991 1.00 33.47 O
ATOM 3508 C SER A 300 15.266 2.262 40.428 1.00 34.11 C
ATOM 3509 O SER A 300 15.318 1.209 41.064 1.00 34.47 O
ATOM 3511 N THR A 301 15.180 2.306 39.103 1.00 34.62 N
ATOM 3512 CA THR A 301 15.197 1.109 38.268 1.00 34.98 C
ATOM 3514 CB THR A 301 13.776 0.494 38.154 1.00 34.92 C
ATOM 3516 OGl THR A 301 13.782 -0.620 37.254 1.00 34.71 O
ATOM 3518 CG2 THR A 301 12.772 1.529 37.660 1.00 35.06 C
ATOM 3522 C THR A 301 15.752 1.464 36.880 1.00 35.45 C
ATOM 3523 O THR A 301 15.456 2.531 36.338 1.00 35.34 O
ATOM 3525 N ARG A 302 16.596 0.588 36.339 1.00 36.09 N
ATOM 3526 CA ARG A 302 17.006 0.654 34.933 1.00 36.82 C
ATOM 3528 CB ARG A 302 18.517 0.444 34.785 1.00 36.81 C
ATOM 3531 CG ARG A 302 19.381 1.647 35.160 1.00 37.85 C
ATOM 3534 CD ARG A 302 20.867 1.269 35.177 1.00 38.69 C
ATOM 3537 NE ARG A 302 21.259 0.560 33.952 1.00 40.48 N
ATOM 3539 CZ ARG A 302 21.587 1.143 32.794 1.00 41.44 C
ATOM 3540 NHl ARG A 302 21.594 2.468 32.675 1.00 42.51 N
ATOM 3543 NH2 ARG A 302 21.917 0.396 31.742 1.00 41.17 N
ATOM 3546 C ARG A 302 16.278 -0.451 34.191 1.00 36.95 C
ATOM 3547 O ARG A 302 16.611 -0.767 33.055 1.00 36.95 O
ATOM 3549 N ASP A 303 15.247 -0.998 34.831 1.00 37.41 N
ATOM 3550 CA ASP A 303 14.725 -2.308 34.493 1.00 37.83 C
ATOM 3552 CB ASP A 303 14.534 -3.097 35.787 1.00 38.16 C
ATOM 3555 CG ASP A 303 14.979 -4.524 35.655 1.00 39.66 C
ATOM 3556 ODl ASP A 303 16.026 -4.862 36.257 1.00 41.56 O
ATOM 3557 OD2 ASP A 303 14.306 -5.293 34.927 1.00 41.15 O
ATOM 3558 C ASP A 303 13.411 -2.261 33.714 1.00 38.02 C
ATOM 3559 O ASP A 303 12.604 -3.184 33.805 1.00 38.15 O
ATOM 3561 N ILE A 304 13.209 -1.196 32.942 1.00 38.12 N
ATOM 3562 CA ILE A 304 11.958 -0.980 32.206 1.00 38.22 C
ATOM 3564 CB ILE A 304 11.199 0.268 32.733 1.00 38.21 C
ATOM 3566 CGl ILE A 304 10.675 0.016 34.147 1.00 38.32 C
ATOM 3569 CDl ILE A 304 9.679 -1.106 34.242 1.00 38.27 C
ATOM 3573 CG2 ILE A 304 10.047 0.644 31.813 1.00 37.96 C
ATOM 3577 C ILE A 304 12.228 -0.799 30.726 1.00 38.20 C
ATOM 3578 O ILE A 304 11.580 -1.422 29.894 1.00 37.67 O
ATOM 3580 N HIS A 305 13.178 0.075 30.410 1.00 38.56 N
ATOM 3581 CA HIS A 305 13.566 0.324 29.035 1.00 38.88 C
ATOM 3583 CB HIS A 305 13.380 1.806 28.704 1.00 38.72 C
ATOM 3586 CG HIS A 305 11.996 2.306 28.979 1.00 38.28 C
ATOM 3587 NDl HIS A 305 10.946 2.107 28.110 - 1.00 38.14 N
ATOM 3589 CEl HIS A 305 9.848 2.638 28.616 1.00 37.98 C
ATOM 3591 NE2 HIS A 305 10.146 3.171 29.786 1.00 38.21 N
ATOM 3593 CD2 HIS A 305 11.482 2.971 30.040 1.00 38.28 C
ATOM 3595 C HIS A 305 15.008 -0.130 28.818 1.00 39.28 C
ATOM 3596 O HIS A 305 15.764 -0.317 29.776 1.00 39.48 O
ATOM 3598 N ARG A 306 15.363 -0.346 27.553 1.00 39.78 N
ATOM 3599 CA ARG A 306 16.725 -0.722 27.170 1.00 39.83 C
ATOM 3601 CB ARG A 306 16.708 -1.957 26.250 1.00 40.19 C
ATOM 3604 CG ARG A 306 16.631 -3.309 26.975 1.00 41.79 C ATOM 3607 CD ARG A 306 17.864 -3.596 27.868 1.00 44.80 C
ATOM 3610 NE ARG A 306 17.619 -3.309 29.298 1.00 46.49 N
ATOM 3612 CZ ARG A 306 18.165 -2.317 30.026 1.00 46.70 C
ATOM 3613 NHl ARG A 306 19.040 -1.443 29.512 1.00 46.22 N
ATOM 3616 NH2 ARG A 306 17.826 -2.195 31.306 1.00 45.99 N
ATOM 3619 C ARG A 306 17.465 0.454 26.509 1.00 39.77 C
ATOM 3620 O ARG A 306 18.587 0.299 26.013 1.00 39.85 O
ATOM 3622 N ASN A 307 16.845 1.631 26.519 1.00 39.40 N
ATOM 3623 CA ASN A 307 17.444 2.814 25.918 1.00 39.23 C
ATOM 3625 CB ASN A 307 17.056 2.906 24.435 1.00 39.37 C
ATOM 3628 CG ASN A 307 18.184 3.446 23.556 1.00 40.29 C
ATOM 3629 ODl ASN A 307 18.876 4.414 23.910 1.00 41.47 O
ATOM 3630 ND2 ASN A 307 18.360 2.829 22.391 1.00 40.86 N
ATOM 3633 C ASN A 307 17.004 4.060 26.688 1.00 38.92 C
ATOM 3634 O ASN A 307 16.389 3.946 27.757 1.00 39.14 O
ATOM 3636 N TYR A 308 17.337 5.236 26.155 1.00 38.41 N
ATOM 3637 CA TYR A 308 16.947 6.512 26.754 1.00 37.96 C
ATOM 3639 CB TYR A 308 17.254 7.688 25.810 1.00 38.23 C
ATOM 3642 CG TYR A 308 18.711 7.874 25.413 1.00 38.58 C
ATOM 3643 CDl TYR A 308 19.046 8.605 24.272 1.00 38.51 C
ATOM 3645 CEl TYR A 308 20.377 8.789 23.897 1.00 39.03 C
ATOM 3647 CZ TYR A 308 21.390 8.230 24.663 1.00 39.18 C
ATOM 3648 OH TYR A 308 22.703 8.399 24.294 1.00 38.93 O
ATOM 3650 CE2 TYR A 308 21.087 7.498 25.801 1.00 39.25 C
ATOM 3652 CD2 TYR A 308 19.754 7.322 26.169 1.00 39.46 C
ATOM 3654 C TYR A 308 15.456 6.525 27.072 1.00 37.41 C
ATOM 3655 O TYR A 308 14.635 6.235 26.201 1.00 37.57 O
ATOM 3657 N VAL A 309 15.113 6.852 28.317 1.00 36.48 N
ATOM 3658 CA VAL A 309 13.722 7.029 28.710 1.00 35.71 C
ATOM 3660 CB VAL A 309 13.458 6.520 30.135 1.00 35.57 C
ATOM 3662 CGl VAL A 309 11.973 6.481 30.404 1.00 35.23 C
ATOM 3666 CG2 VAL A 309 14.077 5.134 30.332 1.00 35.30 C
ATOM 3670 C VAL A 309 13.417 8.516 28.593 1.00 35.01 C
ATOM 3671 O VAL A 309 13.878 9.310 29.410 1.00 34.64 O
ATOM 3673 N ASP A 310 12.647 8.880 27.565 1.00 34.41 N
ATOM 3674 CA ASP A 310 12.474 10.282 27.173 1.00 34.11 C
ATOM 3676 CB ASP A 310 12.712 10.437 25.658 1.00 34.27 C
ATOM 3679 CG ASP A 310 11.607 9.813 24.803 1.00 34.74 C
ATOM 3680 ODl ASP A 310 10.898 8.906 25.285 1.00 35.86 O
ATOM 3681 OD2 ASP A 310 11.459 10.225 23.632 1.00' 34.67 O
ATOM 3682 C ASP A 310 11.136 10.935 27.560 1.00 33.59 C
ATOM 3683 O ASP A 310 10.850 12.052 27.137 1.00 33.67 O
ATOM 3685 N CYS A 311 10.321 10.263 28.362 1.00 33.08 N
ATOM 3686 CA CYS A 311 9.024 10.815 28.731 1.00 32.75 C
ATOM 3688 CB CYS A 311 8.115 10.877 27.506 1.00 32.82 C
ATOM 3691 SG CYS A 311 6.530 11.699 27.784 1.00 33.32 S
ATOM 3693 C CYS A 311 8.373 9.969 29.815 1.00 32.27 C
ATOM 3694 O CYS A 311 8.314 8.754 29.681 1.00 32.19 O
ATOM 3696 N VAL A 312 7.907 10.616 30.885 1.00 31.87 N
ATOM 3697 CA VAL A 312 7.265 9.934 32.017 1.00 31.75 C
ATOM 3699 CB VAL A 312 8.259 9.667 33.202 1.00 31.63 C
ATOM 3701 CGl VAL A 312 8.496 10.919 34.021 1.00 31.46 C
ATOM 3705 CG2 VAL A 312 7.735 8.559 34.098 1.00 31.53 C
ATOM 3709 C VAL A 312 6.047 10.715 32.526 1.00 31.53 C
ATOM 3710 O VAL A 312 5.937 11.927 32.341 1.00 31.48 O
ATOM 3712 N ARG A 313 5.136 9.991 33.164 1.00 31.38 N
ATOM 3713 CA ARG A 313 3.897 10.545 33.680 1.00 31.27 C
ATOM 3715 CB ARG A 313 2.865 10.670 32.562 1.00 31.82 C
ATOM 3718 CG ARG A 313 2.499 12.094 32.207 1.00 33.27 C
ATOM 3721 CD ARG A 313 1.535 12.689 33.224 1.00 35.61 C
ATOM 3724 NE ARG A 313 0.788 13.835 32.701 1.00 35.61 N
ATOM 3726 CZ ARG A 313 -0.223 14.420 33.344 1.00 37.53 C
ATOM 3727 NHl ARG A 313 -0.601 13.969 34.546 1.00 37.53 N
ATOM 3730 NH2 ARG A 313 -0.857 15.461 32.793 1.00 38.01 N
ATOM 3733 C ARG A 313 3.352 9.627 34.749 1.00 30.78 C
ATOM 3734 O ARG A 313 3.544 8.420 34.685 1.00 30.62 O
ATOM 3736 N TRP A 314 2.672 10.202 35.731 1.00 30.38 N
ATOM 3737 CA TRP A 314 1.942 9.407 36.709 1.00 30.15 C
ATOM 3739 CB TRP A 314 1.882 10.125 38.057 1.00 29.82 C
ATOM 3742 CG TRP A 314 3.173 10.133 38.789 1.00 29.52 C
ATOM 3743 CDl TRP A 314 4.160 11.069 38.698 1.00 29.58 C
ATOM 3745 NEl TRP A 314 5.199 10.746 39.539 1.00 29.65 N
ATOM 3747 CE2 TRP A 314 4.896 9.580 40.189 1.00 29.61 C
ATOM 3748 CD2 TRP A 314 3.622 9.165 39.741 1.00 29.01 C
ATOM 3749 CE3 TRP A 314 3.073 7.988 40.257 1.00 28.94 C
ATOM 3751 CZ3 TRP A 314 3.798 7.270 41.188 1.00 29.45 C
ATOM 3753 CH2 TRP A 314 5.067 7.712 41.622 1.00 29.60 C ATOM 3755 CZ2 TRP A 314 5.628 8.863 41.137 1.00 29.37 C
ATOM 3757 C TRP A 314 0.526 9.125 36.214 1.00 29.85 C
ATOM 3758 O TRP A 314 -0.134 10.000 35.654 1.00 29.79 O
ATOM 3760 N LEU A 315 0.081 7.890 36.405 1.00 29.74 N
ATOM 3761 CA LED A 315 -1.326 7.541 36.274 1.00 29.66 C
ATOM 3763 CB LED A 315 -1.527 6.467 35.203 1.00 29.71 C
ATOM 3766 CG LED A 315 -2.980 6.187 34.800 1.00 29.73 C
ATOM 3768 CDl LEU A 315 -3.554 7.368 34.022 1.00 29.93 C
ATOM 3772 CD2 LED A 315 -3.073 4.919 33.980 1.00 29.34 C
ATOM 3776 C LEU A 315 -1.753 7.036 37.640 1.00 29.55 C
ATOM 3777 O LEU A 315 -1.701 5.837 37.915 1.00 29.72 O
ATOM 3779 N GLY A 316 -2.144 7.962 38.506 1.00 29.43 N
ATOM 3780 CA GLY A 316 -2.397 7.633 39.898 1.00 29.46 C
ATOM 3783 C GLY A 316 -1.104 7.147 40.517 1.00 29.35 C
ATOM 3784 O GLY A 316 -0.071 7.787 40.370 1.00 29.02 O
ATOM 3786 N ASP A 317 -1.161 5.998 41.182 1.00 29.51 N
ATOM 3787 CA ASP A 317 0.024 5.380 41.761 1.00 29.67 C
ATOM 3789 CB ASP A 317 -0.367 4.458 42.917 1.00 30.00 C
ATOM 3792 CG ASP A 317 -1.082 5.191 44.048 1.00 31.31 C
ATOM 3793 ODl ASP A 317 -0.902 6.418 44.200 1.00 32.87 O
ATOM 3794 OD2 ASP A 317 -1.825 4.524 44.799 1.00 33.55 O
ATOM 3795 C ASP A 317 0.853 4.591 40.738 1.00 29.63 C
ATOM 3796 O ASP A 317 1.924 4.097 41.081 1.00 29.81 O
ATOM 3798 N LEU A 318 0.369 4.470 39.501 1.00 29.44 N
ATOM 3799 CA LEU A 318 1.121 3.811 38.431 1.00 29.32 C
ATOM 3801 CB LEU A 318 0.176 3.048 37.513 1.00 29.31 C
ATOM 3804 CG LEU A 318 -0.593 1.883 38.130 1.00 29.48 C
ATOM 3806 CDl LEU A 318 -1.515 1.260 37.086 1.00 29.07 C
ATOM " 3810 CD2 LEU A 318 0.360 0.843 38.698 1.00 28.95 C
ATOM 3814 C LEU A 318 1.918 4.797 37.587 1.00 29.32 C
ATOM 3815 O LEU A 318 1.646 5.997 37.591 1.00 29.35 O
ATOM 3817 N ILE A 319 2.889 4.269 36.844 1.00 29.34 N
ATOM 3818 CA ILE A 319 3.750 5.068 35.958 1.00 29.29 C
ATOM 3820 CB ILE A 319 5.241 4.860 36.290 1.00 29.10 C
ATOM 3822 CGl ILE A 319 5.544 5.308 37.720 1.00 29.25 C
ATOM 3825 CDl ILE A 319 5.467 6.811 37.923 1.00 29.61 C
ATOM 3829 CG2 ILE A 319 6.117 5.615 35.296 1.00 29.13 C
ATOM 3833 C ILE A 319 3.576 4.691 34.481 1.00 29.28 C
ATOM 3834 O ILE A 319 3.566 3.508 34.134 1.00 29.49 O
ATOM 3836 N LEU A 320 3.450 5.700 33.624 1.00 29.15 N
ATOM 3837 CA LEU A 320 3.593 5.520 32.186 1.00 29.30 C
ATOM 3839 CB LEU A 320 2.432 6.167 31.440 1.00 29.06 C
ATOM 3842 CG LEU A 320 1.091 5.449 31.569 1.00 28.59 C
ATOM 3844 CDl LEU A 320 -0.050 6.421 31.285 1.00 28.94 C
ATOM 3848 CD2 LEU A 320 1.031 4.247 30.657 1.00 27.07 C
ATOM 3852 C LEU A 320 4.901 6.160 31.746 1.00 29.47 C
ATOM 3853 O LEU A 320 5.144 7.317 32.050 1.00 29.72 O
ATOM 3855 N SER A 321 5.742 5.413 31.039 1.00 29.66 N
ATOM 3856 CA SER A 321 7.000 5.956 30.532 1.00 29.98 C
ATOM 3858 CB SER A 321 8.149 5.636 31.492 1.00 29.87 C
ATOM 3861 OG SER A 321 8.449 4.255 31.496 1.00 29.29 O
ATOM 3863 C SER A 321 7.310 5.402 29.154 1.00 30.33 C
ATOM 3864 O SER A 321 6.761 4.382 28.757 1.00 30.65 O
ATOM 3866 N LYS A 322 8.184 6.072 28.418 1.00 30.79 N
ATOM 3867 CA LYS A 322 8.621 5.538 27.141 1.00 31.18 C
ATOM 3869 CB LYS A 322 7.781 6.074 25.968 1.00 31.29 C
ATOM 3872 CG LYS A 322 7.905 7.567 25.699 1.00 31.62 C
ATOM 3875 CD LYS A 322 7.216 7.985 24.403 1.00 31.30 C
ATOM 3878 CE LYS A 322 8.094 7.769 23.185 1.00 30.99 C
ATOM 3881 NZ LYS A 322 9.217 8.737 23.113 1.00 30.44 N
ATOM 3885 C LYS A 322 10.085 5.796 26.904 1.00 31.96 C
ATOM 3886 O LYS A 322 10.710 6.613 27.571 1.00 31.58 O
ATOM 3888 N SER A 323 10.605 5.054 25.942 1.00 33.22 N
ATOM 3889 CA SER A 323 11.954 5.188 25.453 1.00 34.54 C
ATOM 3891 CB SER A 323 12.725 3.902 25.761 1.00 34.45 C
ATOM 3894 OG SER A 323 13.934 3.818 25.038 1.00 34.40 O
ATOM 3896 C SER A 323 11.799 5.401 23.961 1.00 35.20 C
ATOM 3897 O SER A 323 10.722 5.806 23.518 1.00 35.60 O
ATOM 3899 N CYS A 324 12.842 5.122 23.182 1.00 36.00 N
ATOM 3900 CA CYS A 324 12.755 5.220 21.720 1.00 36.57 C
ATOM 3902 CB CYS A 324 14.015 5.898 21.141 1.00 36.99 C
ATOM 3905 SG CYS A 324 15.628 5.135 21.587 1.00 38.33 S
ATOM 3907 C CYS A 324 12.531 3.851 21.073 1.00 36.97 C
ATOM 3908 O CYS A 324 13.011 3.596 19.962 1.00 37.47 O
ATOM 3910 N GLU A 325 11.781 2.984 21.750 1.00 37.01 N
ATOM 3911 CA GLU A 325 11.631 1.598 21.313 1.00 37.01 C
ATOM 3913 CB GLU A 325 12.008 0.653 22.453 1.00 37.00 C ATOM 3916 CG GLU A 325 13.381 0.920 23.044 1.00 37.35 C
ATOM 3919 CD GLU A 325 13.700 0.012 24.217 1.00 37.45 C
ATOM 3920 OEl GLO A 325 13.650 0.488 25.375 1.00 36.98 O
ATOM ' 3921 OE2 GLO A 325 13.993 -1.181 23.975 1.00 38.49 O
ATOM 3922 C GLO A 325 10.209 1.304 20.827 1.00 37.16 C
ATOM 3923 O GLU A 325 9.795 0.142 20.784 1.00 37.16 O
ATOM 3925 N ASN A 326 9.471 2.357 20.453 1.00 37.20 N
ATOM 3926 CA ASN A 326 8.097 2.228 19.931 1.00 36.97 C
ATOM 3928 CB ASN A 326 8.089 1.384 18.642 1.00 37.25 C
ATOM 3931 CG ASN A 326 8.881 2.030 17.505 1.00 38.41 C
ATOM 3932 ODl ASN A 326 8.363 2.894 16.785 1.00 40.00 O
ATOM 3933 ND2 ASN A 326 10.131 1.593 17.322 1.00 38.75 N
ATOM 3936 C ASN A 326 7.079 1.660 20.946 "1.00 36.72 C
ATOM 3937 O ASN A 326 6.138 0.959 20.561 1.00 36.81 O
ATOM 3939 N ALA A 327 7.261 1.977 22.230 1.00 36.12 N
ATOM 3940 CA ALA A 327 6.396 1.447 23.287 1.00 35.69 C
ATOM 3942 CB ALA A 327 6.897 0.092 23.724 1.00 35.60 C
ATOM 3946 C ALA A 327 6.291 2.373 24.500 1.00 35.22 C
ATOM 3947 O ALA A 327 7.285 2.913 24.966 1.00 34.86 O
ATOM 3949 N ILE A 328 5.071 2.550 24.992 1.00 34.88 N
ATOM 3950 CA ILE A 328 4.825 3.206 26.265 1.00 34.95 C
ATOM 3952 CB ILE A 328 3.601 4.148 26.191 1.00 34.81 C
ATOM 3954 CGl ILE A 328 3.927 5.392 25.359 1.00 35.08 C
ATOM 3957 CDl ILE A 328 2.714 6.240 24.993 1.00 34.81 C
ATOM 3961 CG2 ILE A 328 3.166 4.571 27.577 1.00 34.65 C
ATOM 3965 C ILE A 328 4.547 2.101 27.281 1.00 34.82 C
ATOM 3966 O ILE A 328 3.555 1.400 27.155 1.00 34.72 O
ATOM 3968 N VAL A 329 5.419 1.939 28.273 1.00 34.85 N
ATOM 3969 CA VAL A 329 5.215 0.929 29.315 1.00 35.07 C
ATOM 3971 CB VAL A 329 6.554 0.373 29.886 1.00 34.89 C
ATOM 3973 CGl VAL A 329 6.293 -0.633 31.008 1.00 33.84 C
ATOM 3977 CG2 VAL A 329 7.384 -0.264 28.786 1.00 34.41 C
ATOM 3981 C VAL A 329 4.411 1.531 30.454 1.00 35.24 C
ATOM 3982 O VAL A 329 4.629 2.674 30.826 1.00 35.01 O
ATOM 3984 N CYS A 330 3.472 0.756 30.984 1.00 35.82 N
ATOM 3985 CA CYS A 330 2.765 1.111 32.197 1.00 36.37 C
ATOM 3987 CB CYS A 330 1.264 0.943 32.027 1.00 36.35 C
ATOM 3990 SG CYS A 330 0.353 1.258 33.554 1.00 36.37 S
ATOM 3992 C CYS A 330 3.257 0.176 33.282 1.00 36.99 C
ATOM 3993 O CYS A 330 3.285 -1.042 33.091 1.00 37.15 O
ATOM 3995 N TRP A 331 3.646 0.734 34.422 1.00 37.61 N
ATOM 3996 CA TRP A 331 4.297 -0.065 35.450 1.00 38.11 C
ATOM 3998 CB TRP A 331 5.742 -0.339 35.027 1.00 38.41 C
ATOM 4001 CG TRP A 331 6.565 0.913 34.956 1.00 38173 C
ATOM 4002 CDl TRP A 331 6.636 1.794 33.916 1.00 38.78 C
ATOM 4004 NEl TRP A 331 7.483 2.826 34.232 1.00 38.67 N
ATOM 4006 CE2 TRP A 331 7.974 2.627 35.495 1.00 38.60 C
ATOM 4007 CD2 TRP A 331 7.415 1.432 35.981 1.00 38.84 C
ATOM 4008 CE3 TRP A 331 7.758 0.998 37.266 1.00 38.99 C
ATOM 4010 CZ3 TRP A 331 8.640 1.760 38.015 1.00 38.77 C
ATOM 4012 CH2 TRP A 331 9.183 2.944 37.505 1.00 38.84 C
ATOM 4014 CZ2 TRP A 331 8.862 3.395 36.249 1.00 39.01 C
ATOM 4016 C TRP A 331 4.286 0.605 36.818 1.00 38.44 C
ATOM 4017 O TRP A 331 3.855 1.741 36.970 1.00 38.35 O
ATOM 4019 N LYS A 332 4.766 -0.122 37.814 1.00 39.07 N
ATOM 4020 CA LYS A 332 4.907 0.418 39.153 1.00 39.74 C
ATOM 4022 CB LYS A 332 3.639 0.186 39.969 1.00 39.52 C
ATOM 4025 CG LYS A 332 3.231 -1.261 40.023 1.00 39.41 C
ATOM 4028 CD LYS A 332 2.085 -1.489 40.982 1.00 39.60 C
ATOM 4031 CE LYS A 332 2.565 -1.629 42.415 1.00 39.67 C
ATOM 4034 NZ LYS A 332 1.559 -2.327 43.260 1.00 39.20 N
ATOM 4038 C LYS A 332 6.090 -0.231 39.860 1.00 40.40 C
ATOM 4039 O LYS A 332 6.491 -1.345 39.512 1.00 40.35 O
ATOM 4041 N PRO A 333 6.664 0.474 40.846 1.00 41.28 N
ATOM 4042 CA PRO A 333 7.704 -0.122 41.685 1.00 41.74 C
ATOM 4044 CB PRO A 333 8.191 1.058 42.544 1.00 41.83 C
ATOM 4047 CG PRO A 333 7.659 2.297 41.871 1.00 41.72 C
ATOM 4050 CD PRO A 333 6.396 1.879 41.211 1.00 41.32 C
ATOM 4053 C PRO A 333 7.172 -1.246 42.575 1.00 42.25 C
ATOM 4054 O PRO A 333 6.002 -1.228 42.972 1.00 42.23 O
ATOM 4055 N GLY A 334 8.034 -2.213 42.874 1.00 42.88 N
ATOM 4056 CA GLY A 334 7.678 -3.335 43.732 1.00 43.45 C
ATOM 4059 C GLY A 334 6.737 -4.327 43.077 1.00 43.86 C
ATOM 4060 O GLY A 334 6.388 -4.197 41.906 1.00 43.74 O
ATOM 4062 N LYS A 335 6.324 -5.319 43.855 1.00 44.50 N
ATOM 4063 CA LYS A 335 5.418 -6.362 43.383 1.00 45.16 C
ATOM 4065 CB LYS A 335 5.476 -7.564 44.326 1.00 45.12 C ATOM 4068 CG LYS A 335 6.871 -8.154 44.436 1.00 45.04 C
ATOM 4071 CD LYS A 335 6.890 -9.394 45.297 1.00 45.26 C
ATOM 4074 CE LYS A 335 8.177 -10.174 45.106 1.00 45.73 C
ATOM 4077 NZ LYS A 335 8.395 -10.554 43.675 1.00 46.38 N
ATOM 4081 C LYS A 335 3.985 -5.834 43.250 1.00 45.76 C
ATOM 4082 O LYS A 335 3.705 -4.685 43.605 1.00 45.82 O
ATOM 4084 N MET A 336 3.091 -6.673 42.727 1.00 46.47 N
ATOM 4085 CA MET A 336 1.712 -6.263 42.409 1.00 46.87 C
ATOM 4087 CB MET A 336 0.944 -7.445 41.788 1.00 47.17 C
ATOM 4090 CG MET A 336 -0.505 -7.152 41.368 1.00 47.16 C
ATOM 4093 SD MET A 336 -0.632 -6.082 39.917 1.00 49.34 S
ATOM 4094 CE MET A 336 -2.261 -5.332 40.144 1.00 47.99 C
ATOM 4098 C MET A 336 0.949 -5.722 43.632 1.00 47.30 C
ATOM 4099 O MET A 336 0.195 -4.755 43.522 1.00 47.32 O
ATOM 4101 N GLϋ A 337 1.151 -6.347 44.787 1.00 47.62 N
ATOM 4102 CA GLD A 337 0.449 -5.961 46.017 1.00 47.86 C
ATOM 4104 CB GLϋ A 337 0.327 -7.174 46.970 1.00 48.21 C
ATOM 4107 CG GLϋ A 337 1.654 -7.701 47.589 1.00 49.03 C
ATOM 4110 CD GLϋ A 337 2.416 -8.679 46.687 1.00 50.40 C
ATOM 4111 OEl GLϋ A 337 2.374 -8.525 45.446 1.00 51.22 O
ATOM 4112 OE2 GLϋ A 337 3.070 -9.600 47.225 1.00 51.64 O
ATOM 4113 C GLU A 337 1.077 -4.759 46.761 1.00 47.90 C
ATOM 4114 O GLD A 337 0.466 -4.235 47.696 1.00 47.84 O
ATOM 4116 N ASP A 338 2.277 -4.329 46.352 1.00 47.89 N
ATOM 4117 CA ASP A 338 3.031 -3.280 47.079 1.00 47.88 C
ATOM 4119 CB ASP A 338 4.515 -3.276 46.657 1.00 47.81 C
ATOM 4122 CG ASP A 338 5.279 -4.524 47.114 1.00 47.62 C
ATOM 4123 ODl ASP A 338 4.715 -5.371 47.847 1.00 47.20 O
ATOM 4124 OD2 ASP A 338 6.465 -4.648 46.735 1.00 46.77 O
ATOM 4125 C ASP A 338 2.451 -1.860 46.902 1.00 47.93 C
ATOM 4126 O ASP A 338 2.220 -1.410 45.777 1.00 47.74 O
ATOM 4128 N ASP A 339 2.233 -1.162 48.021 1.00 48.16 N
ATOM 4129 CA ASP A 339 1.788 0.241 48.010 1.00 47.92 C
ATOM 4131 CB ASP A 339 1.169 0.639 49.359 1.00 48.15 C
ATOM 4134 CG ASP A 339 0.687 2.094 49.382 1.00 48.70 C
ATOM 4135 ODl ASP A 339 -0.433 2.368 48.888 1.00 49.98 O
ATOM 4136 OD2 ASP A 339 1.433 2.964 49.891 1.00 49.88 O
ATOM 4137 C ASP A 339 2.958 1.167 47.704 1.00 47.71 C
ATOM 4138 O ASP A 339 4.069 0.970 48.209 1.00 47.64 O
ATOM 4140 N ILE A 340 2.691 2.188 46.894 1.00 47.54 N
ATOM 4141 CA ILE A 340 3.720 3.140 46.456 1.00 47.36 C
ATOM 4143 CB ILE A 340 3.122 4.163 45.434 1.00 47.07 C
ATOM 4145 CGl ILE A 340 4.217 5.020 44.800 1.00 46.58 C
ATOM 4148 CDl ILE A 340 5.286 4.229 44.109 1.00 46.06 C
ATOM 4152 CG2 ILE A 340 2.050 5.036 46.082 1.00 46.81 C
ATOM 4156 C ILE A 340 4.417 3.851 47.637 1.00 47.41 C
ATOM 4157 O ILE A 340 5.646 4.007 47.644 1.00 47.21 O
ATOM 4159 N ASP A 341 3.639 4.232 48.650 1.00 47.44 N
ATOM 4160 CA ASP A 341 4.170 4.979 49.797 1.00 47.39 C
ATOM 4162 CB ASP A 341 3.034 5.703 50.527 1.00 47.26 C
ATOM 4165 CG ASP A 341 2.347 6.733 49.648 1.00 47.03 C
ATOM 4166 ODl ASP A 341 3.070 7.467 48.944 1.00 46.87 O
ATOM 4167 OD2 ASP A 341 1.096 6.809 49.650 1.00 46.34 O
ATOM 4168 C ASP A 341 4.973 4.118 50.778 1.00 47.46 C
ATOM 4169 O ASP A 341 5.619 4.650 51.685 1.00 47.28 O
ATOM 4171 N LYS A 342 4.943 2.798 50.594 1.00 47.52 N
ATOM 4172 CA LYS A 342 5.732 1.889 51.421 1.00 47.61 C
ATOM 4174 CB LYS A 342 4.866 0.702 51.864 1.00 47.71 C
ATOM 4177 CG LYS A 342 3.625 1.103 52.666 1.00 48.00 C
ATOM 4180 CD LYS A 342 3.319 0.110 53.795 1.00 48.09 C
ATOM 4183 CE LYS A 342 4.226 0.346 55.010 1.00 48.49 C
ATOM 4186 NZ LYS A 342 3.891 -0.530 56.173 1.00 48.19 N
ATOM 4190 C LYS A 342 7.019 1.394 50.730 1.00 47.51 C
ATOM 4191 O LYS A 342 7.713 0.518 51.251 1.00 47.46 O
ATOM 4193 N ILE A 343 7.357 1.965 49.576 1.00 47.43 N
ATOM 4194 CA ILE A 343 8.545 1.523 48.834 1.00 47.34 C
ATOM 4196 CB ILE A 343 8.462 1.923 47.328 1.00 47.30 C
ATOM 4198 CGl ILE A 343 7.248 1.260 46.659 1.00 47.02 C
ATOM 4201 CDl ILE A 343 7.342 -0.244 46.523 1.00 46.39 C
ATOM 4205 CG2 ILE A 343 9.750 1.552 46.584 1.00 47.22 C
ATOM 4209 C ILE A 343 9.841 2.076 49.460 1.00 47.29 C
ATOM 4210 O ILE A 343 9.946 3.275 49.748 1.00 47.27 O
ATOM 4212 N LYS A 344 10.816 1.192 49.673 1.00 47.05 N
ATOM 4213 CA LYS A 344 12.151 1.600 50.122 1.00 46.78 C
ATOM 4215 CB LYS A 344 12.763 0.547 51.056 1.00 46.96 C
ATOM 4218 CG LYS A 344 12.517 0.803 52.538 1.00 47.94 C
ATOM 4221 CD LYS A 344 11.024 0.837 52.910 1.00 49.21 C ATOM 4224 CE LYS A 344 10.307 -0.479 52.598 1.00 50.05 C
ATOM 4227 NZ LYS A 344 11.063 -1.684 53.055 1.00 50.53 N
ATOM 4231 C LYS A 344 13.063 1.826 48.910 1.00 46.39 C
ATOM 4232 O LYS A 344 12.830 1.248 47.849 1.00 46.10 O
ATOM 4234 N PRO A 345 14.095 2.683 49.057 1.00 45.99 N
ATOM 4235 CA PRO A 345 15.069 2.882 47.971 1.00 45.74 C
ATOM 4237 CB PRO A 345 16.002 3.978 48.516 1.00 45.68 C
ATOM 4240 CG PRO A 345 15.763 4.032 49.975 1.00 45.75 C
ATOM 4243 CD PRO A 345 14.373 3.548 50.219 1.00 45.86 C
ATOM 4246 C PRO A 345 15.861 1.634 47.550 1.00 45.34 C
ATOM 4247 O PRO A 345 16.386 1.598 46.439 1.00 45.28 O
ATOM 4248 N SER A 346 15.940 0.626 48.412 1.00 45.03 N
ATOM 4249 CA SER A 346 16.624 -0.624 48.071 1.00 44.91 C
ATOM 4251 CB SER A 346 16.926 -1.430 49.340 1.00 44.91 C
ATOM 4254 OG SER A 346 15.729 -1.807 50.004 1.00 44.79 O
ATOM 4256 C SER A 346 15.818 -1.496 47.102 1.00 44.67 C
ATOM 4257 O SER A 346 16.386 -2.375 46.451 1.00 44.68 O
ATOM 4259 N GLU A 347 14.508 -1.242 47.022 1.00 44.42 N
ATOM 4260 CA GLO A 347 13.548 -2.047 46.239 1.00 44.31 C
ATOM 4262 CB GLU A 347 12.201 -1.316 46.174 1.00 44.24 C
ATOM 4265 CG GLU A 347 11.161 -1.935 45.255 1.00 44.26 C
ATOM 4268 CD GLU A 347 10.748 -3.316 45.691 1.00 43.92 C
ATOM 4269 OEl GLU A 347 10.154 -3.441 46.777 1.00 43.37 O
ATOM 4270 OE2 GLU A 347 11.005 -4.276 44.939 1.00 44.19 O
ATOM 4271 C GLU A 347 14.021 -2.409 44.822 1.00 44.22 C
ATOM 4272 O GLU A 347 14.394 -1.530 44.038 1.00 44.20 O
ATOM 4274 N SER A 348 13.967 -3.709 44.508 1.00 44.08 N
ATOM 4275 CA SER A 348 14.541 -4.267 43.273 1.00 43.88 C
ATOM 4277 CB SER A 348 15.392 -5.495 43.604 1.00 43.95 C
ATOM 4280 OG SER A 348 16.506 -5.143 44.405 1.00 44.76 O
ATOM 4282 C SER A 348 13.517 -4.676 42.219 1.00 43.56 C
ATOM 4283 O SER A 348 13.896 -4.943 41.084 1.00 43.42 O
ATOM 4285 N ASN A 349 12.239 -4.747 42.591 1.00 43.24 N
ATOM 4286 CA ASN A 349 11.190 -5.215 41.681 1.00 43.02 C
ATOM 4288 CB ASN A 349 10.224 -6.160 42.413 1.00 43.16 C
ATOM 4291 CG ASN A 349 10.893 -7.440 42.882 1.00 43.54 C
ATOM 4292 ODl ASN A 349 11.882 -7.888 42.301 1.00 45.07 O
ATOM 4293 ND2 ASN A 349 10.349 -8.039 43.932 1.00 43.23 N
ATOM 4296 C ASN A 349 10.385 -4.083 41.036 1.00 42.77 C
ATOM 4297 O ASN A 349 10.206 -3.012 41.620 1.00 42.89 O
ATOM 4299 N VAL A 350 9.909 -4.346 39.822 1.00 42.26 N
ATOM 4300 CA VAL A 350 8.957 -3.491 39.127 1.00 41.76 C
ATOM 4302 CB VAL A 350 9.626 -2.689 37.989 1.00 41.61 C
ATOM 4304 CGl VAL A 350 10.670 -1.744 38.550 1.00 41.26 C
ATOM 4308 CG2 VAL A 350 10.251 -3.619 36.966 1.00 40.75 C
ATOM 4312 C VAL A 350 7.885 -4.405 38.552 1.00 41.53 C
ATOM 4313 O VAL A 350 8.171 -5.551 38.211 1.00 41.57 O
ATOM 4315 N THR A 351 6.657 -3.907 38.445 1.00 41.18 N
ATOM 4316 CA THR A 351 5.540 -4.708 37.951 1.00 40.92 C
ATOM 4318 CB THR A 351 4.409 -4.786 38.989 1.00 40.80 C
ATOM 4320 OGl THR A 351 4.873 -5.503 40.135 1.00 40.64 O
ATOM 4322 CG2 THR A 351 3.190 -5.496 38.414 1.00 40.84 C
ATOM 4326 C THR A 351 4.994 -4.106 36.670 1.00 40.82 C
ATOM 4327 O THR A 351 4.432 -3.011 36.695 1.00 41.08 O
ATOM 4329 N ILE A 352 5.145 -4.831 35.560 1.00 40.51 N
ATOM 4330 CA ILE A 352 4.685 -4.360 34.250 1.00 40.15 C
ATOM 4332 CB ILE A 352 5.453 -5.036 33.097 1.00 40.09 C
ATOM 4334 CGl ILE A 352 6.977 -4.832 33.234 1.00 39.48 C
ATOM 4337 CDl ILE A 352 7.411 -3.499 33.797 1.00 38.20 C
ATOM 4341 CG2 ILE A 352 4.913 -4.550 31.746 1.00 40.40 C
ATOM 4345 C ILE A 352 3.205 -4.655 34.054 1.00 39.97 C
ATOM 4346 O ILE A 352 2.815 -5.811 33.888 1.00 40.21 O
ATOM 4348 N LEU A 353 2.389 -3.606 34.057 1.00 39.61 N
ATOM 4349 CA LEU A 353 0.937 -3.749 33.912 1.00 39.31 C
ATOM 4351 CB LEU A 353 0.221 -2.671 34.729 1.00 39.24 C
ATOM 4354 CG LEU A 353 0.168 -2.974 36.223 1.00 39.13 C
ATOM 4356 CDl LEU A 353 -0.087 -1.714 36.999 1.00 39.47 C
ATOM 4360 CD2 LEU A 353 -0.907 -3.998 36.506 1.00 38.96 C
ATOM 4364 C LEU A 353 0.459 -3.705 32.459 1.00 38.91 C
ATOM 4365 O LEU A 353 -0.716 -3.931 32.183 1.00 38.69 O
ATOM 4367 N GLY A 354 1.361 -3.422 31.532 1.00 38.69 N
ATOM 4368 CA GLY A 354 0.978 -3.305 30.136 1.00 38.74 C
ATOM 4371 C GLY A 354 1.964 -2.497 29.329 1.00 38.51 C
ATOM 4372 O GLY A 354 2.828 -1.827 29.878 1.00 38.22 O
ATOM 4374 N ARG A 355 1.820 -2.569 28.014 1.00 38.69 N
ATOM 4375 CA ARG A 355 2.692 -1.859 27.104 1.00 38.89 C
ATOM 4377 CB ARG A 355 3.963 -2.656 26.832 1.00 38.85 C ATOM 4380 CG ARG A 355 5.065 -1.800 26.229 1.00 39.13 C
ATOM 4383 CD ARG A 355 6.248 -2.630 25.821 1.00 39.27 C
ATOM 4386 NE ARG A 355 5.972 -3.410 24.617 1.00 39.43 N
ATOM 4388 CZ ARG A 355 6.410 -4.649 24.401 1.00 40.27 C
ATOM 4389 NHl ARG A 355 7.112 -5.303 25.323 1.00 40.93 N
ATOM 4392 NH2 ARG A 355 6.105 -5.265 23.267 1.00 40.21 N
ATOM 4395 C ARG A 355 1.965 -1.590 25.800 1.00 38.90 C
ATOM 4396 O ARG A 355 1.476 -2.510 25.155 1.00 38.86 O
ATOM 4398 N PHE A 356 1.910 -0.321 25.418 1.00 39.17 N
ATOM 4399 CA PHE A 356 1.184 0.105 24.239 1.00 39.42 C
ATOM 4401 CB PHE A 356 0.425 1.401 24.522 1.00 39.40 C
ATOM 4404 CG PHE A 356 -0.357 1.391 25.809 1.00 39.35 C
ATOM 4405 CDl PHE A 356 -1.100 0.281 26.183 1.00 39.47 C
ATOM 4407 CEl PHE A 356 -1.823 0.283 27.357 1.00 39.38 C
ATOM 4409 CZ PHE A 356 -1.823 1.407 28.166 1.00 39.55 C
ATOM 4411 CE2 PHE A 356 -1.099 2.522 27.798 1.00 39.15 C
ATOM 4413 CD2 PHE A 356 -0.373 2.511 26.629 1.00 39.30 C
ATOM 4415 C PHE A 356 2.157 0.330 23.099 1.00 39.56 C
ATOM 4416 O PHE A 356 2.901 1.302 23.106 1.00 39.44 O
ATOM 4418 N ASP A 357 2.146 -0.571 22.123 1.00 40.10 N
ATOM 4419 CA ASP A 357 3.065 -0.487 20.992 1.00 40.66 C
ATOM 4421 CB ASP A 357 3.328 -1.870 20.403 1.00 40.57 C
ATOM 4424 CG ASP A 357 4.211 -2.719 21.284 1.00 40.60 C
ATOM 4425 ODl ASP A 357 4.761 -2.200 22.275 1.00 40.08 O
ATOM 4426 OD2 ASP A 357 4.357 -3.913 20.971 1.00 40.92 O
ATOM 4427 C ASP A 357 2.552 0.436 19.898 1.00 41.15 C
ATOM 4428 O ASP A 357 1.356 0.731 19.808 1.00 41.02 O
ATOM 4430 N TYR A 358 3.489 0.890 19.073 1.00 41.81 N
ATOM 4431 CA TYR A 358 3.190 1.763 17.945 1.00 42.41 C
ATOM 4433 CB TYR A 358 2.944 3.202 18.420 1.00 42.55 C
ATOM 4436 CG TYR A 358 3.916 3.700 19.461 1.00 42.42 C
ATOM 4437 CDl TYR A 358 5.010 4.472 19.109 1.00 42.47 C
ATOM 4439 CEl TYR A 358 5.894 4.935 20.074 1.00 42.92 C
ATOM 4441 CZ TYR A 358 5.689 4.627 21.400 1.00 42.92 C
ATOM 4442 OH TYR A 358 6.570 5.088 22.357 1.00 42.89 O
ATOM 4444 CE2 TYR A 358 4.605 3.861 21.769 1.00 42.74 C
ATOM 4446 CD2 TYR A 358 3.728 3.408 20.804 1.00 42.45 C
ATOM 4448 C TYR A 358 4.331 1.680 16.933 1.00 42.88 C
ATOM 4449 O TYR A 358 5.261 0.892 17.109 1.00 42.76 O
ATOM 4451 N SER A 359 4.251 2.474 15.871 1.00 43.53 N
ATOM 4452 CA SER A 359 5.189 2.366 14.769 1.00 44.12 C
ATOM 4454 CB SER A 359 4.436 1.931 13.510 1.00 44.09 C
ATOM 4457 OG SER A 359 3.771 0.692 13.716 1.00 43.74 O
ATOM 4459 C SER A 359 5.951 3.668 14.506 1.00 44.75 C
ATOM 4460 O SER A 359 5.415 4.762 14.695 1.00 44.83 O
ATOM 4462 N GLN A 360 7.206 3.523 14.074 1.00 45.52 N
ATOM 4463 CA GLN A 360 8.048 4.634 13.605 1.00 46.10 C
ATOM 4465 CB GLN A 360 7.567 5.150 12.238 1.00 46.19 C
ATOM 4468 CG GLN A 360 7.943 4.221 11.089 1.00 46.30 C
ATOM 4471 CD GLN A 360 6.993 4.302 9.904 1.00 46.41 C
ATOM 4472 OEl GLN A 360 5.776 4.411 10.069 1.00 46.57 O
ATOM 4473 NE2 GLN A 360 7.550 4.224 8.697 1.00 46.77 N
ATOM 4476 C GLN A 360 8.158 5.758 14.634 1.00 46.60 C
ATOM 4477 O GLN A 360 7.585 6.836 14.487 1.00 46.54 O
ATOM 4479 N CYS A 361 8.914 5.473 15.682 1.00 47.27 N
ATOM 4480 CA CYS A 361 9.114 6.406 16.770 1.00 47.46 C
ATOM 4482 CB CYS A 361 7.923 6.321 17.726 1.00 47.69 C
ATOM 4485 SG CYS A 361 7.759 7.687 18.909 1.00 47.90 S
ATOM 4487 C CYS A 361 10.420 6.027 17.463 1.00 47.76 C
ATOM 4488 O CYS A 361 10.483 5.897 18.694 1.00 47.89 O
ATOM 4490 N ASP A 362 11.464 5.851 16.652 1.00 47.89 N
ATOM 4491 CA ASP A 362 12.769 5.419 17.159 1.00 47.95 C
ATOM 4493 CB ASP A 362 13.257 4.139 16.441 1.00 48.13 C
ATOM 4496 CG ASP A 362 12.832 4.071 14.979 1.00 48.80 C
ATOM 4497 ODl ASP A 362 13.171 4.995 14.214 1.00 49.92 O
ATOM 4498 OD2 ASP A 362 12.164 3.086 14.594 1.00 49.38 O
ATOM 4499 C ASP A 362 13.806 6.564 17.146 1.00 48.03 C
ATOM 4500 O ASP A 362 15.017 6.326 17.070 1.00 48.38 O
ATOM 4502 N ILE A 363 13.312 7.803 17.241 1.00 47.78 N
ATOM 4503 CA ILE A 363 14.140 8.973 17.584 1.00 47.31 C
ATOM 4505 CB ILE A 363 14.052 10.101 16.508 1.00 47.46 C
ATOM 4507 CGl ILE A 363 12.638 10.698 16.420 1.00 47.15 C
ATOM 4510 CDl ILE A 363 12.584 12.012 15.695 1.00 47.05 C
ATOM 4514 CG2 ILE A 363 14.506 9.573 15.141 1.00 47.17 C
ATOM 4518 C ILE A 363 13.710 9.510 18.959 1.00 47.05 C
ATOM 4519 O ILE A 363 12.536 9.393 19.331 1.00 47.08 O
ATOM 4521 N TRP A 364 14.649 10.095 19.707 1.00 46.56 N ATOM 4522 CA TRP A 364 14.349 10.578 21.069 1.00 46.01 C
ATOM 4524 CB TRP A 364 15.507 10.301 22.054 1.00 46.63 C
ATOM 4527 CG TRP A 364 16.799 11.063 21.833 1.00 47.25 C
ATOM 4528 CDl TRP A 364 17.829 10.715 20.999 1.00 47.50 C
ATOM 4530 NEl TRP A 364 18.848 11.640 21.089 1.00 47.53 N
ATOM 4532 CE2 TRP A 364 18.500 12.601 22.003 1.00 47.66 C
ATOM 4533 CD2 TRP A 364 17.217 12.267 22.503 1.00 48.00 C
ATOM 4534 CE3 TRP A 364 16.627 13.101 23.469 1.00 47.78 C
ATOM 4536 CZ3 TRP A 364 17.326 14.235 23.897 1.00 47.53 C
ATOM 4538 CH2 TRP A 364 18.601 14.539 23.376 1.00 47.54 C
ATOM 4540 CZ2 TRP A 364 19.202 13.737 22.434 1.00 47.57 C
ATOM 4542 C TRP A 364 13.892 12.038 21.125 1.00 45.22 C
ATOM 4543 O TRP A 364 14.098 12.811 20.190 1.00 45.06 O
ATOM 4545 N TYR A 365 13.270 12.382 22.249 1.00 44.25 N
ATOM 4546 CA TYR A 365 12.523 13.636 22.437 1.00 43.58 C
ATOM 4548 CB TYR A 365 13.368 14.871 22.103 1.00 43.68 C
ATOM 4551 CG TYR A 365 13.061 16.010 23.037 1.00 43.60 C
ATOM 4552 CDl TYR A 365 13.733 16.136 24.249 1.00 43.84 C
ATOM 4554 CEl TYR A 365 13.447 17.166 25.128 1.00 43.86 C
ATOM 4556 CZ TYR A 365 12.467 18.085 24.804 1.00 44.12 C
ATOM 4557 OH TYR A 365 12.178 19.116 25.672 1.00 43.88 O
ATOM 4559 CE2 TYR A 365 11.775 17.976 23.606 1.00 44.26 C
ATOM 4561 CD2 TYR A 365 12.071 16.936 22.735 1.00 44.02 C
ATOM 4563 C TYR A 365 11.170 13.638 21.691 1.00 42.69 C
ATOM 4564 O TYR A 365 10.815 14.584 20.989 1.00 42.29 O
ATOM 4566 N MET A 366 10.432 12.548 21.883 1.00 41.78 N
ATOM 4567 CA MET A 366 9.079 12.381 21.384 1.00 41.15 C
ATOM 4569 CB MET A 366 8.992 11.150 20.480 1.00 41.40 C
ATOM 4572 CG MET A 366 9.908 11.206 19.259 1.00 41.82 C
ATOM 4575 SD MET A 366 9.320 12.358 18.001 1.00 41.93 S
ATOM 4576 CE MET A 366 8.250 11.279 17.038 1.00 41.79 C
ATOM 4580 C MET A 366 8.200 12.180 22.601 1.00 40.30 C
ATOM 4581 O MET A 366 8.311 11.173 23.290 1.00 40.38 O
ATOM 4583 N ARG A 367 7.336 13.146 22.866 1.00 39.36 N
ATOM 4584 CA ARG A 367 6.594 13.189 24.112 1.00 38.62 C
ATOM 4586 CB ARG A 367 6.696 14.584 24.729 1.00 39.21 C
ATOM 4589 CG ARG A 367 7.843 14.763 25.675 1.00 39.96 C
ATOM 4592 CD ARG A 367 9.147 14.916 24.946 1.00 42.15 C
ATOM 4595 NE ARG R 367 10.256 15.003 25.893 1.00 42.84 N
ATOM 4597 CZ ARG A 367 10.555 16.082 26.619 1.00 43.86 C
ATOM 4598 NHl ARG A 367 9.849 17.207 26.516 1.00 44.18 N
ATOM 4601 NH2 ARG A 367 11.583 16.037 27.451 1.00 44.21 N
ATOM 4604 C ARG A 367 5.127 12.869 23.916 1.00 37.65 C
ATOM 4605 O ARG A 367 4.470 13.432 23.041 1.00 37.56 O
ATOM 4607 N PHE A 368 4.608 11.986 24.759 1.00 36.42 N
ATOM 4608 CA PHE A 368 3.169 11.795 24.854 1.00 35.63 C
ATOM 4610 CB PHE A 368 2.834 10.346 25.198 1.00 35.32 C
ATOM 4613 CG PHE A 368 3.386 9.878 26.520 1.00 35.25 C
ATOM 4614 CDl PHE A 368 2.703 10.122 27.697 1.00 35.01 C
ATOM 4616 CEl PHE A 368 3.191 9.683 28.908 1.00 34.64 C
ATOM 4618 CZ PHE A 368 4.363 8.986 28.962 1.00 34.59 C
ATOM 4620 CE2 PHE A 368 5.058 8.724 27.801 1.00 35.14 C
ATOM 4622 CD2 PHE A 368 4.566 9.162 26.582 1.00 35.26 C
ATOM 4624 C PHE A 368 2.582 12.762 25.888 1.00 34.78 C
ATOM 4625 O PHE A 368 3.285 13.234 26.773 1.00 34.56 O
ATOM 4627 N SER A 369 1.304 13.083 25.753 1.00 33.91 N
ATOM 4628 CA SER A 369 0.625 13.903 26.743 1.00 33.43 C
ATOM 4630 CB SER A 369 0.420 15.326 26.227 1.00 33.24 C
ATOM 4633 OG SER A 369 -0.565 15.372 25.215 1.00 33.55 O
ATOM 4635 C SER A 369 -0.704 13.257 27.075 1.00 32.83 C
ATOM 4636 O SER A 369 -1.108 12.300 26.421 1.00 32.58 O
ATOM 4638 N THR A 370 -1.362 13.765 28.113 1.00 32.42 N
ATOM 4639 CA THR A 370 -2.707 13.320 28.473 1.00 32.11 C
ATOM 4641 CB THR A 370 -2.733 12.468 29.751 1.00 32.05 C
ATOM 4643 OGl THR A 370 -2.406 13.284 30.883 1.00 32.23 O
ATOM 4645 CG2 THR A 370 -1.755 11.304 29.641 1.00 31.60 C
ATOM 4649 C THR A 370 -3.600 14.517 28.690 1.00 31.67 C
ATOM 4650 O THR A 370 -3.129 15.648 28.798 1.00 31.19 O
ATOM 4652 N ASP A 371 -4.898 14.257 28.744 1.00 31.44 N
ATOM 4653 CA ASP A 371 -5.863 15.313 28.977 1.00 31.40 C
ATOM 4655 CB ASP A 371 -7.236 14.938 28.410 1.00 31.37 C
ATOM 4658 CG ASP A 371 -7.882 13.784 29.148 1.00 31.41 C
ATOM 4659 ODl ASP A 371 -7.216 12.748 29.336 1.00 30.30 O
ATOM 4660 OD2 ASP A 371 -9.064 13.921 29.536 1.00 33.32 O
ATOM 4661 C ASP A 371 -5.926 15.580 30.471 1.00 31.09 C
ATOM 4662 O ASP A 371 -5.363 14.831 31.268 1.00 31.10 O
ATOM 4664 N PHE A 372 -6.599 16.658 30.839 1.00 31.01 N ATOM 4665 CA PHE A 372 -6.742 17.051 32.238 1.00 31.12 C
ATOM 4667 CB PHE A 372 -7.667 18.272 32.333 1.00 31.21 C
ATOM 4670 CG PHE A 372 -8.041 18.652 33.740 1.00 31.29 C
ATOM 4671 CDl PHE A 372 -7.247 19.521 34.474 1.00 31.36 C
ATOM 4673 CEl PHE A 372 -7.598 19.877 35.772 1.00 31.26 C
ATOM 4675 CZ PHE A 372 -8.757 19.361 36.344 1.00 31.45 C
ATOM 4677 CE2 PHE A 372 -9.558 18.495 35.618 1.00 31.19 C
ATOM 4679 CD2 PHE A 372 -9.201 18.151 34.324 1.00 31.31 C
ATOM 4681 C PHE A 372 -7.252 15.916 33.148 1.00 31.05 C
ATOM 4682 O PHE A 372 -6.779 15.770 34.274 1.00 31.14 O
ATOM 4684 N TRP A 373 -8.202 15.119 32.666 1.00 30.81 N
ATOM 4685 CA TRP A 373 -8.800 14.066 33.491 1.00 30.74 C
ATOM 4687 CB TRP A 373 10.234 13.786 33.044 1.00 31.13 C
ATOM 4690 CG TRP A 373 11.102 14.960 33.248 1.00 31.38 C
ATOM 4691 CDl TRP A 373 11.535 15.832 32.297 1.00 31.37 C
ATOM 4693 NEl TRP A 373 12.299 16.812 32.874 1.00 31.48 N
ATOM 4695 CE2 TRP A 373 12.354 16.598 34.227 1.00 31.61 C
ATOM 4696 CD2 TRP A 373 11.605 15.436 34.498 1.00 31.43 C
ATOM 4697 CE3 TRP A 373 11.502 14.989 35.823 1.00 31.70 C
ATOM 4699 CZ3 TRP A 373 12.153 15.707 36.826 1.00 31.48 C
ATOM 4701 CH2 TRP A 373 12.895 16.860 36.524 1.00 31.50 C
ATOM 4703 CZ2 TRP A 373 13.004 17.324 35.236 1.00 31.64 C
ATOM 4705 C TRP A 373 -8.019 12.771 33.464 1.00 30.54 C
ATOM 4706 O TRP A 373 -8.257 11.899 34.302 1.00 30.32 O
ATOM 4708 N GLN A 374 -7.098 12.665 32.504 1.00 30.21 N
ATOM 4709 CA GLN A 374 -6.368 11.437 32.194 1.00 30.03 C
ATOM 4711 CB GLN A 374 -5.529 10.963 33.378 1.00 29.77 C
ATOM 4714 CG GLN A 374 -4.567 12.014 33.874 1.00 29.75 C
ATOM 4717 CD GLN A 374 -3.560 11.472 34.863 1.00 29.66 C
ATOM 4718 OEl GLN A 374 -3.913 10.974 35.931 1.00 28.69 O
ATOM 4719 NE2 GLN A 374 -2.289 11.574 34.510 1.00 30.62 N
ATOM 4722 C GLN A 374 -7.286 10.329 31.697 1.00 30.03 C
ATOM 4723 O GLN A 374 -6.986 9.158 31.870 1.00 29.90 O
ATOM 4725 N LYS A 375 -8.393 10.702 31.057 1.00 30.32 N
ATOM 4726 CA LYS A 375 -9.228 9.733 30.345 1.00 30.70 C
ATOM 4728 CB LYS A 375 10.546 10.364 29.882 1.00 30.62 C
ATOM 4731 CG LYS A 375 11.459 10.846 30.991 1.00 31.15 C
ATOM 4734 CD LYS A 375 12.764 11.395 30.414 1.00 31.21 C
ATOM 4737 CE LYS A 375 13.738 11.816 31.498 1.00 31.45 C
ATOM 4740 NZ LYS A 375 13.225 12.986 32.270 1.00 32.27 N
ATOM 4744 C LYS A 375 -8.495 9.176 29.111 1.00 30.91 C
ATOM 4745 O LYS A 375 -8.847 8.102 28.600 1.00 31.03 O
ATOM 4747 N MET A 376 -7.494 9.903 28.617 1.00 30.81 N
ATOM 4748 CA MET A 376 -6.815 9.466 27.417 1.00 30.97 C
ATOM 4750 CB MET A 376 -7.633 9.851 26.187 1.00 31.13 C
ATOM 4753 CG MET A 376 -8.192 11.243 26.217 1.00 31.32 C
ATOM 4756 SD MET A 376 -9.177 11.536 24.746 1.00 31.64 S
ATOM 4757 CE MET A 376 -9.937 13.111 25.163 1.00 32.00 C
ATOM 4761 C MET A 376 -5.382 9.945 27.266 1.00 30.84 C
ATOM 4762 O MET A 376 -4.946 10.894 27.909 1.00 30.86 O
ATOM 4764 N LEU A 377 -4.672 9.244 26.390 1.00 30.85 N
ATOM 4765 CA LEU A 377 -3.249 9.406 26.175 1.00 30.93 C
ATOM 4767 CB LEU A 377 -2.535 8.152 26.681 1.00 30.94 C
ATOM 4770 CG LEU A 377 -1.051 7.959 26.390 1.00 30.97 C
ATOM 4772 CDl LEU A 377 -0.280 9.220 26.725 1.00 31.37 C
ATOM 4776 CD2 LEU A 377 -0.528 6.768 27.185 1.00 31.06 C
ATOM 4780 C LEU A 377 -2.997 9.609 24.684 1.00 30.88 C
ATOM 4781 O LEU A 377 -3.589 8.926 23.854 1.00 30.80 O
ATOM 4783 N ALA A 378 -2.127 10.558 24.353 1.00 31.14 N
ATOM 4784 CA ALA A 378 -1.876 10.938 22.963 1.00 31.32 C
ATOM 4786 CB ALA A 378 -2.448 12.311 22.695 1.00 31.27 C
ATOM 4790 C ALA A 378 -0.380 10.923 22.657 1.00 31.38 C
ATOM 4791 O ALA A 378 0.411 11.540 23.375 1.00 31.28 O
ATOM 4793 N LEU A 379 -0.004 10.203 21.603 1.00 31.45 N
ATOM 4794 CA LEU A 379 1.379 10.161 21.136 1.00 31.71 C
ATOM 4796 CB LEU A 379 2.063 8.864 21.567 1.00 31.62 C
ATOM 4799 CG LEU A 379 3.525 8.682 21.138 1.00 31.28 C
ATOM 4801 CDl LEU A 379 4.341 9.952 21.329 1.00 31.09 C
ATOM 4805 CD2 LEU A 379 4.164 7.527 21.898 1.00 31.27 C
ATOM 4809 C LEU A 379 1.422 10.256 19.626 1.00 32.02 C
ATOM 4810 O LEU A 379 0.693 9.549 18.939 1.00 32.17 O
ATOM 4812 N GLY A 380 2.277 11.138 19.119 1.00 32.49 N
ATOM 4813 CA GLY A 380 2.534 11.250 17.686 1.00 32.74 C
ATOM 4816 C GLY A 380 3.848 10.568 17.360 1.00 32.95 C
ATOM 4817 O GLY A 380 4.775 10.611 18.158 1.00 32.93 O
ATOM 4819 N ASN A 381 3.935 9.945 16.189 1.00 33.43 N
ATOM 4820 CA ASN A 381 5.143 9.215 15.795 1.00 33.75 C ATOM 4822 CB ASN A 381 4.756 7.820 15.286 1.00 33.72 C
ATOM 4825 CG ASN A 381 4.430 7.793 13.814 1.00 33.31 C
ATOM 4826 ODl ASN A 381 4.107 8.811 13.210 1.00 33.32 O
ATOM 4827 ND2 ASN A 381 4.510 6.615 13.226 1.00 33.38 N
ATOM 4830 C ASN A 381 5.999 9.998 14.780 1.00 34.19 C
ATOM 4831 O ASN A 381 5.619 11.091 14.357 1.00 34.64 O
ATOM 4833 N GLN A 382 7.142 9.441 14.383 1.00 34.64 N
ATOM 4834 CA GLN A 382 8.144 10.202 13.606 1.00 34.74 C
ATOM 4836 CB GLN A 382 9.567 9.602 13.768 1.00 35.05 C
ATOM 4839 CG GLN A 382 9.925 8.409 12.866 1.00 35.31 C
ATOM 4842 CD GLN A 382 11.099 7.560 13.408 1.00 35.71 C
ATOM 4843 OEl GLN A 382 11.793 7.944 14.360 1.00 36.90 O
ATOM 4844 NE2 GLN A 382 11.314 6.396 12.793 1.00 36.51 N
ATOM 4847 C GLN A 382 7.803 10.448 12.124 1.00 34.67 C
ATOM 4848 O GLN A 382 8.506 11.215 11.460 1.00 35.02 O
ATOM 4850 N VAL A 383 6.742 9.819 11.613 1.00 34.33 N
ATOM 4851 CA VAL A 383 6.243 10.098 10.250 1.00 33.94 C
ATOM 4853 CB VAL A 383 6.194 8.823 9.345 1.00 33.79 C
ATOM 4855 CGl VAL A 383 7.582 8.236 9.169 1.00 32.90 C
ATOM 4859 CG2 VAL A 383 5.217 7.787 9.903 1.00 33.13 C
ATOM 4863 C VAL A 383 4.854 10.721 10.294 1.00 33.79 C
ATOM 4864 O VAL A 383 4.110 10.647 9.323 1.00 33.52 O
ATOM 4866 N GLY A 384 4.508 11.328 11.429 1.00 33.87 N
ATOM 4867 CA GLY A 384 3.281 12.127 11.549 1.00 33.85 C
ATOM 4870 C GLY A 384 1.986 11.342 11.653 1.00 33.77 C
ATOM 4871 O GLY A 384 0.992 11.693 11.024 1.00 34.03 O
ATOM 4873 N LYS A 385 2.003 10.282 12.452 1.00 33.74 N
ATOM 4874 CA LYS A 385 0.808 9.515 12.779 1.00 33.52 C
ATOM 4876 CB LYS A 385 1.064 8.045 12.493 1.00 33.49 C
ATOM 4879 CG LYS A 385 -0.175 7.190 12.460 1.00 33.93 C
ATOM 4882 CD LYS A 385 0.214 5.722 12.393 1.00 34.00 C
ATOM 4885 CE LYS A 385 -0.981 4.815 12.170 1.00 34.22 C
ATOM 4888 NZ LYS A 385 -0.617 3.393 12.444 1.00 35.03 N
ATOM 4892 C LYS A 385 0.467 9.714 14.266 1.00 33.31 C
ATOM 4893 O LYS A 385 1.355 9.653 15.126 1.00 33.09 O
ATOM 4895 N LEU A 386 -0.813 9.947 14.556 1.00 32.95 N
ATOM 4896 CA LEO A 386 -1.277 10.204 15.925 1.00 32.70 C
ATOM 4898 CB LEU A 386 -2.245 11.400 15.980 1.00 32.91 C
ATOM 4901 CG LEU A 386 -1.734 12.777 16.430 1.00 33.15 C
ATOM 4903 CDl LEU A 386 -2.904 13.755 16.502 1.00 33.12 C
ATOM 4907 CD2 LEU A 386 -1.002 12.711 17.772 1.00 33.60 C
ATOM 4911 C LEU A 386 -1.972 8.995 16.518 1.00 32.28 C
ATOM 4912 O LEU A 386 -2.893 8.447 15.924 1.00 32.19 O
ATOM 4914 N TYR A 387 -1.532 8.611 17.709 1.00 31.93 N
ATOM 4915 CA TYR A 387 -2.133 7.526 18.461 1.00 31.64 C
ATOM 4917 CB TYR A 387 -1.037 6.582 18.966 1.00 31.71 C
ATOM 4920 CG TYR A 387 -0.349 5.788 17.872 1.00 31.71 C
ATOM 4921 CDl TYR A 387 -0.725 4.476 17.596 1.00 32.19 C
ATOM 4923 CEl TYR A 387 -0.104 3.735 16.588 1.00 32.24 C
ATOM 4925 CZ TYR A 387 0.904 4.308 15.843 1.00 32.21 C
ATOM 4926 OH TYR A 387 1.519 3.574 14.849 1.00 32.07 O
ATOM 4928 CE2 TYR A 387 1.298 5.611 16.100 1.00 32.22 C
ATOM 4930 CD2 TYR A 387 0.670 6.344 17.110 1.00 31.94 C
ATOM 4932 C TYR A 387 -2.880 8.132 19.639 1.00 31.24 C
ATOM 4933 O TYR A 387 -2.314 8.939 20.369 1.00 31.29 O
ATOM 4935 N VAL A 388 -4.144 7.763 19.825 1.00 30.78 N
ATOM 4936 CA VAL A 388 -4.857 8.142 21.049 1.00 30.70 C
ATOM 4938 CB VAL A 388 -5.994 9.130 20.800 1.00 30.49 C
ATOM 4940 CGl VAL A 388 -6.669 9.460 22.118 1.00 30.10 C
ATOM 4944 CG2 VAL A 388 -5.465 10.392 20.142 1.00 30.79 C
ATOM 4948 C VAL A 388 -5.430 6.937 21.780 1.00 30.46 C
ATOM 4949 O VAL A 388 -6.228 6.188 21.221 1.00 30.44 O
ATOM 4951 N TRP A 389 -5.032 6.773 23.038 1.00 30.29 N
ATOM 4952 CA TRP A 389 -5.484 5.652 23.846 1.00 30.34 C
ATOM 4954 CB TRP A 389 -4.323 5.052 24.622 1.00 30.51 C
ATOM 4957 CG TRP A 389 -3.360 4.295 23.782 1.00 30.81 C
ATOM 4958 CDl TRP A 389 -3.413 2.972 23.468 1.00 30.94 C
ATOM 4960 NEl TRP A 389 -2.339 2.629 22.679 1.00 30.90 N
ATOM 4962 CE2 TRP A 389 -1.564 3.740 22.481 1.00 30.57 C
ATOM 4963 CD2 TRP A 389 -2.180 4.810 23.159 1.00 30.94 C
ATOM 4964 CE3 TRP A 389 -1.587 6.076 23.103 1.00 31.21 C
ATOM 4966 CZ3 TRP A 389 -0.406 6.228 22.385 1.00 31.07 C
ATOM 4968 CH2 TRP A 389 0.181 5.142 21.727 1.00 30.74 C
ATOM 4970 CZ2 TRP A 389 -0.384 3.894 21.763 1.00 30.55 C
ATOM 4972 C TRP A 389 -6.566 6.068 24.833 1.00 30.23 C
ATOM 4973 O TRP A 389 -6.422 7.068 25.533 1.00 29.73 O
ATOM 4975 N ASP A 390 -7.637 5.276 24.875 1.00 30.08 N ATOM 4976 CA ASP A 390 -8.717 5.442 25.837 1.00 29.95 C
ATOM 4978 CB ASP A 390 10.017 4.893 25.249 1.00 29.86 C
ATOM 4981 CG ASP A 390 11.139 4.829 26.257 1.00 30.23 C
ATOM 4982 ODl ASP A 390 11.110 5.617 27.222 1.00 30.03 O
ATOM 4983 OD2 ASP A 390 12.052 3.986 26.077 1.00 31.53 O
ATOM 4984 C ASP A 390 -8.347 4.700 27.122 1.00 29.92 C
ATOM 4985 O ASP A 390 -8.367 3.468 27.170 1.00 29.86 O
ATOM 4987 N LED A 391 -8.012 5.457 28.162 1.00 29.87 N
ATOM 4988 CA LED A 391 -7.624 4.874 29.451 1.00 29.86 C
ATOM 4990 CB LEU A 391 -6.701 5.836 30.197 1.00 29.68 C
ATOM 4993 CG LED A 391 -5.424 6.209 29.439 1.00 29.37 C
ATOM 4995 CDl LED A 391 -4.490 7.021 30.327 1.00 28.30 C
ATOM 4999 CD2 LED A 391 -4.718 4.960 28.885 1.00 28.40 C
ATOM 5003 C LED A 391 -8.813 4.510 30.339 1.00 29.81 C
ATOM 5004 O LED A 391 -8.637 3.915 31.409 1.00 29.54 O
ATOM 5006 N GLϋ A 392 10.015 4.846 29.877 1.00 30.04 N
ATOM 5007 CA GLU A 392 11.233 4.620 30.624 1.00 30.27 C
ATOM 5009 CB GLU A 392 12.340 5.546 30.102 1.00 30.19 C
ATOM 5012 CG GLU A 392 13.455 5.839 31.117 1.00 30.59 C
ATOM 5015 CD GLU A 392 12.993 6.641 32.351 1.00 30.76 C
ATOM 5016 OEl GLU A 392 11.846 7.142 32.381 1.00 29.61 O
ATOM 5017 OE2 GLU A 392 13.797 6.763 33.296 1.00 30.99 O
ATOM 5018 C GLU A 392 11.634 3.149 30.544 1.00 30.46 C
ATOM 5019 O GLU A 392 12.643 2.795 29.933 1.00 30.51 O
ATOM 5021 N VAL A 393 10.823 2.307 31.182 1.00 30.82 N
ATOM 5022 CA VAL A 393 10.959 0.848 31.126 1.00 31.22 C
ATOM 5024 CB VAL A 393 10.171 0.235 29.928 1.00 31.11 C
ATOM 5026 CGl VAL A 393 10.833 0.602 28.608 1.00 30.23 C
ATOM 5030 CG2 VAL A 393 -8.703 0.674 29.948 1.00 30.06 C
ATOM 5034 C VAL A 393 10.444 0.254 32.439 1.00 31.82 C
ATOM 5035 O VAL A 393 -9.551 0.825 33.060 1.00 32.20 O
ATOM 5037 N GLU A 394 10.999 -0.887 32.849 1.00 32.25 N
ATOM 5038 CA GLU A 394 10.777 -1.433 34.195 1.00 32.55 C
ATOM 5040 CB GLU A 394 11.465 -2.778 34.345 1.00 32.65 C
ATOM 5043 CG GLU A 394 12.989 -2.700 34.376 1.00 33.78 C
ATOM 5046 CD GLU A 394 13.658 -3.964 33.846 1.00 34.62 C
ATOM 5047 OEl GLU A 394 12.940 -4.822 33.259 1.00 37.38 O
ATOM 5048 OE2 GLU A 394 14.903 -4.089 34.001 1.00 36.64 O
ATOM 5049 C GLU A 394 -9.315 -1.604 34.539 1.00 32.51 C
ATOM 5050 O GLU A 394 -8.905 -1.314 35.659 1.00 32.82 O
ATOM 5052 N ASP A 395 -8.536 -2.082 33.576 1.00 32.51 N
ATOM 5053 CA ASP A 395 -7.107 -2.306 33.772 1.00 32.47 C
ATOM 5055 CB ASP A 395 -6.802 -3.804 33.786 1.00 32.50 C
ATOM 5058 CG ASP A 395 -7.413 -4.511 34.988 1.00 32.84 C
ATOM 5059 ODl ASP A 395 -6.988 -4.231 36.126 1.00 33.22 O
ATOM 5060 OD2 ASP A 395 -8.323 -5.344 34.801 1.00 33.39 O
ATOM 5061 C ASP A 395 -6.317 -1.607 32.670 1.00 32.39 C
ATOM 5062 O ASP A 395 -6.843 -1.384 31.580 1.00 32.49 O
ATOM 5064 N PRO A 396 -5.051 -1.253 32.949 1.00 32.36 N
ATOM 5065 CA PRO A 396 -4.246 -0.513 31.969 1.00 32.39 C
ATOM 5067 CB PRO A 396 -2.887 -0.348 32.671 1.00 32.42 C
ATOM 5070 CG PRO A 396 -3.156 -0.553 34.110 1.00 32.42 C
ATOM 5073 CD PRO A 396 -4.300 -1.513 34.190 1.00 32.41 C
ATOM 5076 C PRO A 396 -4.063 -1.211 30.614 1.00 32.35 C
ATOM 5077 O PRO A 396 -4.036 -0.538 29.585 1.00 32.24 O
ATOM 5078 N HIS A 397 -3.945 -2.537 30.606 1.00 32.36 N
ATOM 5079 CA HIS A 397 -3.710 -3.265 29.350 1.00 32.44 C
ATOM 5081 CB HIS A 397 -3.126 -4.655 29.629 1.00 32.52 C
ATOM 5084 CG HIS A 397 -4.130 -5.654 30.108 1.00 32.84 C
ATOM 5085 NDl HIS A 397 -4.656 -5.634 31.381 1.00 33.20 N
ATOM 5087 CEl HIS A 397 -5.504 -6.638 31.518 1.00 33.10 C
ATOM 5089 NE2 HIS A 397 -5.547 -7.307 30.380 1.00 33.00 N
ATOM 5091 CD2 HIS A 397 -4.693 -6.713 29.483 1.00 33.08 C
ATOM 5093 C HIS A 397 -4.944 -3.363 28.430 1.00 32.33 C
ATOM 5094 O HIS A 397 -4.819 -3.772 27.279 1.00 32.14 O
ATOM 5096 N LYS A 398 -6.117 -2.979 28.934 1.00 32.34 N
ATOM 5097 CA LYS A 398 -7.360 -2.998 28.156 1.00 32.40 C
ATOM 5099 CB LYS A 398 -8.538 -3.315 29.080 1.00 32.23 C
ATOM 5102 CG LYS A 398 -8.400 -4.629 29.818 1.00 32.44 C
ATOM 5105 CD LYS A 398 -9.474 -4.800 30.881 1.00 32.44 C
ATOM 5108 CE LYS A 398 -9.213 -6.037 31.736 1.00 32.60 C
ATOM 5111 NZ LYS A 398 10.036 -6.058 32.985 1.00 32.98 N
ATOM 5115 C LYS A 398 -7.641 -1.680 27.412 1.00 32.50 C
ATOM 5116 O LYS A 398 -8.756 -1.472 26.914 1.00 32.49 O
ATOM 5118 N ALA A 399 -6.638 -0.805 27.318 1.00 32.62 N
ATOM 5119 CA ALA A 399 -6.825 0.542 26.765 1.00 32.78 C
ATOM 5121 CB ALA A 399 -5.602 1.409 27.064 1.00 32.49 C ATOM 5125 C ALA A 399 -7.097 0.494 25.259 1.00 32.87 C
ATOM 5126 O ALA A 399 -6.397 -0.208 24.532 1.00 32.78 O
ATOM 5128 N LYS A 400 -8.105 1.240 24.801 1.00 33.11 N
ATOM 5129 CA LYS A 400 -8.546 1.183 23.398 1.00 33.43 C
ATOM 5131 CB LYS A 400 -10.062 1.390 23.270 1.00 33.35 C
ATOM 5134 CG LYS A 400 -10.927 0.668 24.301 1.00 33.66 C
ATOM 5137 CD LYS A 400 -12.415 0.776 23.939 1.00 33.86 C
ATOM 5140 CE LYS A 400 -13.327 0.097 24.966 1.00 33.96 C
ATOM 5143 NZ LYS A 400 -13.546 0.960 26.161 1.00 34.72 N
ATOM 5147 C LYS A 400 -7.831 2.231 22.559 1.00 33.47 C
ATOM 5148 O LYS A 400 -8.053 3.418 22.727 1.00 33.56 O
ATOM 5150 N CYS A 401 -6.979 1.782 21.648 1.00 34.03 N
ATOM 5151 CA CYS A 401 -6.241 2.680 20.775 1.0.0 34.56 C
ATOM 5153 CB CYS A 401 -4.917 2.057 20.346 1.00 34.40 C
ATOM 5156 SG CYS A 401 -3.914 3.159 19.319 1.00 33.93 S
ATOM 5158 C CYS A 401 -7.037 3.033 19.530 1.00 35.15 C
ATOM 5159 O CYS A 401 -7.819 2.234 19.018 1.00 35.26 O
ATOM 5161 N THR A 402 -6.829 4.247 19.047 1.00 35.81 N
ATOM 5162 CA THR A 402 -7.425 4.688 17.806 1.00 36.45 C
ATOM 5164 CB THR A 402 -8.111 5.406 18.045 1.00 36.53 C
ATOM 5166 OGl THR A 402 -8.642 6.811 17.797 1.00 36.38 O
ATOM 5168 CG2 THR A 402 -9.310 5.160 19.486 1.00 36.35 C
ATOM 5172 C THR A 402 -6.398 5.617 17.186 1.00 37.05 C
ATOM 5173 O THR A 402 -5.709 6.336 17.901 1.00 37.18 O
ATOM 5175 N THR A 403 -6.265 5.579 15.869 1.00 37.89 N
ATOM 5176 CA THR A 403 -5.212 6.333 15.202 1.00 38.71 C
ATOM 5178 CB THR A 403 -4.308 5.411 14.355 1.00 38.71 C
ATOM 5180 OGl THR A 403 -5.064 4.285 13.894 1.00 38.74 O
ATOM 5182 CG2 THR A 403 -3.140 4.909 15.185 1.00 38.56 C
ATOM 5186 C THR A 403 -5.779 7.447 14.337 1.00 39.42 C
ATOM 5187 O THR A 403 -6.913 7.373 13.881 1.00 39.47 O
ATOM 5189 N LEU A 404 -4.972 8.483 14.128 1.00 40.49 N
ATOM 5190 CA LEU A 404 -5.357 9.635 13.320 1.00 41.36 C
ATOM 5192 CB LEU A 404 -5.579 10.859 14.212 1.00 41.25 C
ATOM 5195 CG LEU A 404 -6.705 10.799 15.246 1.00 40.92 C
ATOM 5197 CDl LEU A 404 -6.559 11.949 16.231 1.00 40.47 C
ATOM 5201 CD2 LEU A 404 -8.070 10.826 14.580 1.00 40.00 C
ATOM 5205 C LEU A 404 -4.265 9.945 12.298 1.00 42.27 C
ATOM 5206 O LEU A 404 -3.087 10.047 12.647 1.00 42.27 O
ATOM 5208 N THR A 405 -4.651 10.078 11.031 1.00 43.56 N
ATOM 5209 CA THR A 405 -3.702 10.476 9.995 1.00 44.27 C
ATOM 5211 CB THR A 405 -3.053 9.266 9.280 1.00 44.22 C
ATOM 5213 OGl THR A 405 -2.842 8.198 10.210 1.00 43.90 O
ATOM 5215 CG2 THR A 405 -1.705 9.671 8.678 1.00 44.03 C
ATOM 5219 C THR A 405 -4.358 11.376 8.960 1.00 45.15 C
ATOM 5220 O THR A 405 -5.560 11.283 8.704 1.00 45.05 O
ATOM 5222 N HIS A 406 -3.541 12.259 8.398 1.00 46.57 N
ATOM 5223 CA HIS A 406 -3.921 13.127 7.297 1.00 47.22 C
ATOM 5225 CB HIS A 406 -4.034 14.575 7.772 1.00 47.67 C
ATOM 5228 CG HIS A 406 -4.484 15.525 6.706 1.00 48.14 C
ATOM 5229 NDl HIS A 406 -3.637 16.445 6.120 1.00 50.60 N
ATOM 5231 CEl HIS A 406 -4.305 17.140 5.214 1.00 50.64 C
ATOM 5233 NE2 HIS A 406 -5.552 16.699 5.185 1.00 50.52 N
ATOM 5235 CD2 HIS A 406 -5.689 15.688 6.107 1.00 49.88 C
ATOM 5237 C HIS A 406 -2.827 13.009 6.248 1.00 47.99 C
ATOM 5238 O HIS A 406 -1.640 13.050 6.587 1.00 48.16 O
ATOM 5240 N HIS A 407 -3.218 12.854 4.983 1.00 48.74 N
ATOM 5241 CA HIS A 407 -2.247 12.599 3.903 1.00 49.13 C
ATOM 5243 CB HIS A 407 -2.939 12.458 2.534 1.00 49.73 C
ATOM 5246 CG HIS A 407 -3.518 13.735 2.004 1.00 50.83 C
ATOM 5247 NDl HIS A 407 -4.794 14.160 2.314 1.00 52.40 N
ATOM 5249 CEl HIS A 407 -5.035 15.309 1.706 1.00 52.52 C
ATOM 5251 NE2 HIS A 407 -3.962 15.644 1.010 1.00 52.69 N
ATOM 5253 CD2 HIS A 407 -2.999 14.676 1.178 1.00 51.98 C
ATOM 5255 C HIS A 407 -1.169 13.675 3.830 1.00 49.32 C
ATOM 5256 O HIS A 407 0.012 13.367 3.627 1.00 49.22 O
ATOM 5258 N LYS A 408 -1.576 14.928 4.033 1.00 49.37 N
ATOM 5259 CA LYS A 408 -0.669 16.066 3.851 1.00 49.35 C
ATOM 5261 CB LYS A 408 -1.466 17.330 3.472 1.00 49.62 C
ATOM 5264 CG LYS A 408 -0.753 18.240 2.456 1.00 50.00 C
ATOM 5267 CD LYS A 408 -1.599 18.477 1.198 1.00 49.94 C
ATOM 5270 CE LYS A 408 -0.770 19.088 0.073 1.00 50.05 C
ATOM 5273 NZ LYS A 408 0.433 18.272 -0.286 1.00 49.88 N
ATOM 5277 C LYS A 408 0.221 16.316 5.079 1.00 49.25 C
ATOM 5278 O LYS A 408 0.967 17.299 5.115 1.00 49.26 O
ATOM 5280 N CYS A 409 0.155 15.410 6.060 1.00 49.00 N
ATOM 5281 CA CYS A 409 0.915 15.526 7.303 1.00 48.34 C ATOM 5283 CB CYS A 409 -0.046 15.441 8.490 1.00 48.56 C
ATOM 5286 SG CYS A 409 0.767 15.695 10.080 1.00 50.02 S
ATOM 5288 C CYS A 409 1.966 14.412 7.406 1.00 47.78 C
ATOM 5289 O CYS A 409 1.603 13.242 7.582 1.00 48.07 O
ATOM 5291 N GLY A 410 3.253 14.770 7.309 1.00 46.66 N
ATOM 5292 CA GLY A 410 4.334 13.770 7.201 1.00 45.75 C
ATOM 5295 C GLY A 410 5.611 13.965 8.011 1.00 44.94 C
ATOM 5296 O GLY A 410 6.482 13.094 7.998 1.00 44.86 O
ATOM 5298 N ALA A 411 5.738 15.091 8.713 1.00 43.97 N
ATOM 5299 CA ALA A 411 6.917 15.367 9.542 1.00 43.04 C
ATOM 5301 CB ALA A 411 7.147 16.881 9.672 1.00 43.01 C
ATOM 5305 C ALA A 411 6.726 14.738 10.911 1.00 42.18 C
ATOM 5306 O ALA A 411 5.594 14.473 11.320 1.00 42.07 O
ATOM 5308 N ALA A 412 7.833 14.504 11.614 1.00 41.15 N
ATOM 5309 CA ALA A 412 7.798 13.910 12.956 1.00 40.31 C
ATOM 5311 CB ALA A 412 9.214 13.656 13.460 1.00 40.24 C
ATOM 5315 C ALA A 412 7.061 14.822 13.925 1.00 39.45 C
ATOM 5316 O ALA A 412 7.182 16.037 13.831 1.00 39.57 O
ATOM 5318 N ILE A 413 6.296 14.230 14.840 1.00 38.36 N
ATOM 5319 CA ILE A 413 5.575 14.980 15.873 1.00 37.73 C
ATOM 5321 CB ILE A 413 4.132 14.'467 16.040 1.00 37.64 C
ATOM 5323 CGl ILE A 413 3.328 14.705 14.761 1.00 37.19 C
ATOM 5326 CDl ILE A 413 2.084 13.883 14.678 1.00 37.29 C
ATOM 5330 CG2 ILE A 413 3.458 15.153 17.215 1.00 37.76 C
ATOM 5334 C ILE A 413 6.302 14.871 17.216 1.00 37.12 C
ATOM 5335 O ILE A 413 6.488 13.768 17.741 1.00 36.88 O
ATOM 5337 N ARG A 414 6.692 16.020 17.768 1.00 36.46 N
ATOM 5338 CA ARG A 414 7.486 16.088 19.008 1.00 35.81 C
ATOM 5340 CB ARG A 414 8.353 17.349 19.005 1.00 36.09 C
ATOM 5343 CG ARG A 414 9.440 17.348 17.954 1.00 36.51 C
ATOM 5346 CD ARG A 414 10.584 16.463 18.381 1.00 37.44 C
ATOM 5349 NE ARG A 414 11.588 16.327 17.335 1.00 37.33 N
ATOM 5351 CZ ARG A 414 12.566 15.427 17.359 1.00 38.40 C
ATOM 5352 NHl ARG A 414 13.419 15.369 16.346 1.00 38.58 N
ATOM 5355 NH2 ARG A 414 12.717 14.600 18.393 1.00 38.70 N
ATOM 5358 C ARG A 414 6.637 16.085 20.277 1.00 34.95 C
ATOM 5359 O ARG A 414 7.059 15.565 21.313 1.00 34.41 O
ATOM 5361 N GLN A 415 5.461 16.699 20.204 1.00 34.04 N
ATOM 5362 CA GLN A 415 4.574 16.752 21.349 1.00 33.85 C
ATOM 5364 CB GLN A 415 5.035 17.820 22.362 1.00 33.64 C
ATOM 5367 CG GLN A 415 4.429 17.614 23.757 1.00 33.62 C
ATOM 5370 CD GLN A 415 5.031 18.495 24.816 1.00 33.65 C
ATOM 5371 OEl GLN A 415 5.328 19.659 24.576 1.00 33.98 O
ATOM 5372 NE2 GLN A 415 5.195 17.950 26.012 1.00 33.89 N
ATOM 5375 C GLN A 415 3.126 16.997 20.936 1.00 33.37 C
ATOM 5376 O GLN A 415 2.858 17.545 19.872 1.00 33.29 O
ATOM 5378 N THR A 416 2.209 16.557 21.794 1.00 32.96 N
ATOM 5379 CA THR A 416 0.788 16.769 21.628 1.00 32.71 C
ATOM 5381 CB THR A 416 0.052 15.426 21.538 1.00 32.84 C
ATOM 5383 OGl THR A 416 0.557 14.524 22.544 1.00 32.98 O
ATOM 5385 CG2 THR A 416 0.239 14.817 20.149 1.00 32.69 C
ATOM 5389 C THR A 416 0.257 17.534 22.825 1.00 32.35 C
ATOM 5390 O THR A 416 0.890 17.558 23.878 1.00 32.27 O
ATOM 5392 N SER A 417 -0.907 18.152 22.668 1.00 32.06 N
ATOM 5393 CA SER A 417 -1.545 18.852 23.778 1.00 32.13 C
ATOM 5395 CB SER A 417 -1.011 20.289 23.888 1.00 32.05 C
ATOM 5398 OG SER A 417 -1.372 20.906 25.117 1.00 31.09 O
ATOM 5400 C SER A 417 -3.062 18.851 23.607 1.00 32.06 C
ATOM 5401 O SER A 417 -3.565 19.175 22.538 1.00 31.90 O
ATOM 5403 N PHE A 418 -3.777 18.456 24.659 1.00 32.20 N
ATOM 5404 CA PHE A 418 -5.234 18.546 24.696 1.00 32.46 C
ATOM 5406 CB PHE A 418 -5.843 17.429 25.544 1.00 32.69 C
ATOM 5409 CG PHE A 418 -5.706 16.063 24.941 1.00 33.02 C
ATOM 5410 CDl PHE A 418 -6.662 15.583 24.058 1.00 32.99 C
ATOM 5412 CEl PHE A 418 -6.538 14.319 23.502 1.00 33.12 C
ATOM 5414 CZ PHE A 418 -5.445 13.519 23.828 1.00 33.24 C
ATOM 5416 CE2 PHE A 418 -4.485 13.988 24.712 1.00 33.03 C
ATOM 5418 CD2 PHE A 418 -4.620 15.250 25.263 1.00 33.28 C
ATOM 5420 C PHE A 418 -5.638 19.861 25.316 1.00 32.54 C
ATOM 5421 O PHE A 418 -4.918 20.408 26.152 1.00 32.40 O
ATOM 5423 N SER A 419 -6.797 20.367 24.914 1.00 32.62 N
ATOM 5424 CA SER A 419 -7.397 21.487 25.613 1.00 32.81 C
ATOM 5426 CB SER A 419 -8.542 22.089 24.804 1.00 32.74 C
ATOM 5429 OG SER A 419 -9.545 21.120 24.566 1.00 33.22 O
ATOM 5431 C SER A 419 -7.915 20.968 26.943 1.00 32.91 C
ATOM 5432 O SER A 419 -8.011 19.756 27.153 1.00 32.71 O
ATOM 5434 N ARG A 420 -8.244 21.891 27.840 1.00 33.30 N ATOM 5435 CA ARG A 420 -8.794 21.536 29.148 1.00 33.46 C
ATOM 5437 CB ARG A 420 -8.987 22.787 30.011 1.00 33.70 C
ATOM 5440 CG ARG A 420 -8.972 22.502 31.506 1.00 33.69 C
ATOM 5443 CD ARG A 420 -9.710 23.567 32.286 1.00 34.47 C
ATOM 5446 NE ARG A 420 -9.335 23.568 33.698 1.00 35.67 N
ATOM 5448 CZ ARG A 420 -9.701 22.644 34.591 1.00 37.10 C
ATOM 5449 NHl ARG A 420 10.470 21.609 34.249 1.00 37.27 N
ATOM 5452 NH2 ARG A 420 -9.294 22.759 35.854 1.00 37.38 N
ATOM 5455 C ARG A 420 10.119 20.765 29.032 1.00 33.39 C
ATOM 5456 O ARG A 420 10.367 19.849 29.813 1.00 33.34 O
ATOM 5458 N ASP A 421 10.956 21.135 28.057 1.00 33.37 N
ATOM 5459 CA ASP A 421 12.219 20.418 27.786 1.00 33.25 C
ATOM 5461 CB ASP A 421 13.250 21.351 27.131 1.00 33.37 C
ATOM 5464 CG ASP A 421 12.786 21.896 25.789 1.00 34.36 C
ATOM 5465 ODl ASP A 421 12.205 21.120 25.006 1.00 35.76 O
ATOM 5466 OD2 ASP A 421 12.998 23.100 25.514 1.00 35.39 O
ATOM 5467 C ASP A 421 12.041 19.159 26.922 1.00 33.06 C
ATOM 5468 O ASP A 421 13.009 18.445 26.686 1.00 33.10 O
ATOM 5470 N SER A 422 10.820 18.921 26.433 1.00 32.70 N
ATOM 5471 CA SER A 422 10.471 17.754 25.599 1.00 32.38 C
ATOM 5473 CB SER A 422 10.836 16.438 26.304 1.00 32.47 C
ATOM 5476 OG SER A 422 10.391 16.433 27.652 1.00 33.05 O
ATOM 5478 C SER A 422 11.066 17.768 24.179 1.00 32.05 C
ATOM 5479 O SER A 422 10.896 16.802 23.430 1.00 32.15 O
ATOM 5481 N SER A 423 11.730 18.856 23.792 1.00 31.49 N
ATOM 5482 CA SER A 423 12.395 18.909 22.495 1.00 31.12 C
ATOM 5484 CB SER A 423 13.503 19.961 22.491 1.00 30.93 C
ATOM 5487 OG SER A 423 12.976 21.258 22.652 1.00 30.10 O
ATOM 5489 C SER A 423 11.418 19.178 21.360 1.00 31.00 C
ATOM 5490 O SER A 423 11.755 18.956 20.197 1.00 30.99 O
ATOM 5492 N ILE A 424 10.220 19.662 21.700 1.00 30.84 N
ATOM 5493 CA ILE A 424 -9.181 19.980 20.715 1.00 30.70 C
ATOM 5495 CB ILE A 424 -8.908 21.504 20.647 1.00 30.58 C
ATOM 5497 CGl ILE A 424 10.172 22.265 20.245 1.00 30.47 C
ATOM 5500 CDl ILE A 424 10.009 23.767 20.266 1.00 30.45 C
ATOM 5504 CG2 ILE A 424 -7.800 21.809 19.657 1.00 30.51 C
ATOM 5508 C ILE A 424 -7.873 19.260 21.054 1.00 30.69 C
ATOM 5509 O ILE A 424 -7.507 19.133 22.228 1.00 30.76 O
ATOM 5511 N LEU A 425 -7.181 18.794 20.015 1.00 30.59 N
ATOM 5512 CA LEU A 425 -5.870 18.168 20.155 1.00 30.54 C
ATOM 5514 CB LEU A 425 -5.945 16.667 19.865 1.00 30.69 C
ATOM 5517 CG LEU A 425 -4.609 15.915 19.966 1.00 30.61 C
ATOM 5519 CDl LEU A 425 -4.056 16.031 21.379 1.00 30.24 C
ATOM 5523 CD2 LEU A 425 -4.757 14.453 19.556 1.00 30.53 C
ATOM 5527 C LEU A 425 -4.892 18.801 19.188 1.00 30.42 C
ATOM 5528 O LED A 425 -5.049 18.672 17.979 1.00 30.36 O
ATOM 5530 N ILE A 426 -3.879 19.474 19.725 1.00 30.40 N
ATOM 5531 CA ILE A 426 -2.856 20.100 18.910 1.00 30.41 C
ATOM 5533 CB ILE A 426 -2.467 21.488 19.456 1.00 30.34 C
ATOM 5535 CGl ILE A 426 -3.643 22.468 19.312 1.00 30.25 C
ATOM 5538 CDl ILE A 426 -4.102 22.728 17.868 1.00 29.35 C
ATOM 5542 CG2 ILE A 426 -1.216 22.021 18.742 1.00 30.32 C
ATOM 5546 C ILE A 426 -1.632 19.207 18.880 1.00 30.43 C
ATOM 5547 O ILE A 426 -1.239 18.671 19.912 1.00 30.48 O
ATOM 5549 N ALA A 427 -1.055 19.044 17.687 1.00 30.65 N
ATOM 5550 CA ALA A 427 0.219 18.337 17.486 1.00 30.66 C
ATOM 5552 CB ALA A 427 -0.008 17.068 16.688 1.00 30.53 C
ATOM 5556 C ALA A 427 1.208 19.255 16.755 1.00 30.64 C
ATOM 5557 O ALA A 427 0.824 19.967 15.825 1.00 30.31 O
ATOM 5559 N VAL A 428 2.471 19.243 17.177 1.00 30.74 N
ATOM 5560 CA VAL A 428 3.494 20.093 16.554 1.00 31.12 C
ATOM 5562 CB VAL A 428 4.007 21.184 17.523 1.00 30.99 C
ATOM 5564 CGl VAL A 428 2.886 22.163 17.846 1.00 30.55 C
ATOM 5568 CG2 VAL A 428 4.593 20.570 18.779 1.00 29.98 C
ATOM 5572 C VAL A 428 4.674 19.285 16.009 1.00 31.39 C
ATOM 5573 O VAL A 428 5.082 18.295 16.612 1.00 31.58 O
ATOM 5575 N CYS A 429 5.237 19.731 14.887 1.00 31.69 N
ATOM 5576 CA CYS A 429 6.170 18.904 14.121 1.00 32.11 C
ATOM 5578 CB CYS A 429 5.567 18.600 12.756 1.00 32.04 C
ATOM 5581 SG CYS A 429 3.916 17.971 12.893 1.00 32.14 S
ATOM 5583 C CYS A 429 7.570 19.467 13.927 1.00 32.39 C
ATOM 5584 O CYS A 429 7.858 20.613 14.276 1.00 32.41 O
ATOM 5586 N ASP A 430 8.427 18.625 13.348 1.00 32.85 N
ATOM 5587 CA ASP A 430 9.824 18.958 13.089 1.00 33.26 C
ATOM 5589 CB ASP A 430 10.638 17.689 12.871 1.00 33.69 C
ATOM 5592 CG ASP A 430 11.285 17.223 14.125 1.00 35.64 C
ATOM 5593 ODl ASP A 430 10.576 17.179 15.155 1.00 39.05 O ATOM 5594 OD2 ASP A 430 12.497 16.928 14.094 1.00 38.17 O
ATOM 5595 C ASP A 430 10.042 19.883 11.907 1.00 33.30 C
ATOM 5596 O ASP A 430 11.140 20.410 11.730 1.00 33.37 O
ATOM 5598 N ASP A 431 9.009 20.057 11.091 1.00 33.24 N
ATOM 5599 CA ASP A 431 9.046 21.019 9.997 1.00 33.25 C
ATOM 5601 CB ASP A 431 8.274 20.461 8.792 1.00 33.27 C
ATOM 5604 CG ASP A 431 6.804 20.239 9.092 1.00 34.06 C
ATOM 5605 ODl ASP A 431 6.353 20.611 10.194 1.00 35.93 O
ATOM 5606 OD2 ASP A 431 6.092 19.692 8.232 1.00 35.20 O
ATOM 5607 C ASP A 431 8.478 22.382 10.438 1.00 33.15 C
ATOM 5608 O ASP A 431 8.244 23.255 9.598 1.00 33.46 O
ATOM 5610 N ALA A 432 8.263 22.545 11.749 1.00 32.84 N
ATOM 5611 CA ALA A 432 7.642 23.734 12.345 1.00 32.56 C
ATOM 5613 CB ALA A 432 8.350 25.017 11.898 1.00 32.35 C
ATOM 5617 C ALA A 432 6.135 23.838 12.086 1.00 32.49 C
ATOM 5618 O ALA A 432 5.560 24.922 12.224 1.00 32.75 O
ATOM 5620 N SER A 433 5.486 22.727 11.740 1.00 32.17 N
ATOM 5621 CA SER A 433 4.046 22.760 11.457 1.00 31.98 C
ATOM 5623 CB SER A 433 3.671 21.776 10.341 1.00 31.97 C
ATOM 5626 OG SER A 433 3.980 20.435 10.685 1.00 31.66 O
ATOM 5628 C SER A 433 3.199 22.490 12.701 1.00 31.77 C
ATOM 5629 O SER A 433 3.632 21.822 13.633 1.00 31.63 O
ATOM 5631 N ILE A 434 1.983 23.018 12.688 1.00 31.67 N
ATOM 5632 CA ILE A 434 1.035 22.877 13.778 1.00 31.76 C
ATOM 5634 CB ILE A 434 0.683 24.254 14.395 1.00 31.66 C
ATOM 5636 CGl ILE A 434 1.958 24.988 14.838 1.00 31.76 C
ATOM 5639 CDl ILE A 434 1.719 26.375 15.443 1.00 31.58 C
ATOM 5643 CG2 ILE A 434 -0.283 24.095 15.569 1.00 31.36 C
ATOM 5647 C ILE A 434 -0.214 22.238 13.191 1.00 31.88 C
ATOM 5648 O ILE A 434 -0.677 22.653 12.138 1.00 31.76 O
ATOM 5650 N TRP A 435 -0.749 21.227 13.868 1.00 32.32 N
ATOM 5651 CA TRP A 435 -1.889 20.466 13.367 1.00 32.55 C
ATOM 5653 CB TRP A 435 -1.436 19.064 12.978 1.00 33.33 C
ATOM 5656 CG TRP A 435 -0.527 19.113 11.813 1.00 33.92 C
ATOM 5657 CDl TRP A 435 0.815 19.365 11.827 1.00 34.51 C
ATOM 5659 NEl TRP A 435 1.307 19.372 10.548 1.00 34.77 N
ATOM 5661 CE2 TRP A 435 0.278 19.123 9.677 1.00 35.07 C
ATOM 5662 CD2 TRP A 435 -0.896 18.964 10.445 1.00 34.44 C
ATOM 5663 CE3 TRP A 435 -2.105 18.700 9.790 1.00 34.91 C
ATOM 5665 CZ3 TRP A 435 -2.105 18.607 8.398 1.00 34.81 C
ATOM 5667 CH2 TRP A 435 -0.915 18.771 7.660 1.00 34.70 C
ATOM 5669 CZ2 TRP A 435 0.283 19.025 8.281 1.00 34.70 C
ATOM 5671 C TRP A 435 -2.971 20.397 14.418 1.00 32.59 C
ATOM 5672 O TRP A 435 -2.705 20.027 15.555 1.00 32.62 O
ATOM 5674 N ARG A 436 -4.189 20.761 14.032 1.00 32.49 N
ATOM 5675 CA ARG A 436 -5.289 20.869 14.973 1.00 32.53 C
ATOM 5677 CB ARG A 436 -5.910 22.259 14.899 1.00 32.51 C
ATOM 5680 CG ARG A 436 -7.143 22.410 15.778 1.00 32.52 C
ATOM 5683 CD ARG A 436 -7.812 23.743 15.584 1.00 32.40 C
ATOM 5686 NE ARG A 436 -9.045 23.850 16.357 1.00 32.14 N
ATOM 5688 CZ ARG A 436 -9.789 24.949 16.411 1.00 32.81 C
ATOM 5689 NHl ARG A 436 -9.422 26.042 15.753 1.00 33.29 N
ATOM 5692 NH2 ARG A 436 10.897 24.964 17.137 1.00 33.01 N
ATOM 5695 C ARG A 436 -6.369 19.848 14.694 1.00 32.61 C
ATOM 5696 O ARG A 436 -7.015 19.898 13.647 1.00 32.88 O
ATOM 5698 N TRP A 437 -6.593 18.959 15.656 1.00 32.65 N
ATOM 5699 CA TRP A 437 -7.641 17.944 15.564 1.00 32.64 C
ATOM 5701 CB TRP A 437 -7.036 16.567 15.848 1.00 32.36 C
ATOM 5704 CG TRP A 437 -6.024 16.119 14.815 1.00 32.19 C
ATOM 5705 CDl TRP A 437 -4.717 16.500 14.723 1.00 32.18 C
ATOM 5707 NEl TRP A 437 -4.112 15.879 13.658 1.00 31.91 N
ATOM 5709 CE2 TRP A 437 -5.030 15.075 13.037 1.00 32.09 C
ATOM 5710 CD2 TRP A 437 -6.246 15.195 13.743 1.00 32.21 C
ATOM 5711 CE3 TRP A 437 -7.358 14.458 13.309 1.00 32.05 C
ATOM 5713 CZ3 TRP A 437 -7.223 13.638 12.199 1.00 32.13 C
ATOM 5715 CH2 TRP A 437 -5.998 13.539 11.516 1.00 32.33 C
ATOM 5717 CZ2 TRP A 437 -4.894 14.249 11.916 1.00 32.26 C
ATOM 5719 C TRP A 437 -8.771 18.257 16.554 1.00 32.52 C
ATOM 5720 O TRP A 437 -8.526 18.377 17.743 1.00 32.32 O
ATOM 5722 N ASP A 438 10.000 18.396 16.059 1.00 32.81 N
ATOM 5723 CA ASP A 438 11.159 18.689 16.918 1.00 33.39 C
ATOM 5725 CB ASP A 438 11.980 19.861 16.368 1.00 33.45 C
ATOM 5728 CG ASP A 438 11.331 21.208 16.629 1.00 34.35 C
ATOM 5729 ODl ASP A 438 10.105 21.248 16.853 1.00 36.97 O
ATOM 5730 OD2 ASP A 438 12.043 22.231 16.613 1.00 34.77 O
ATOM 5731 C ASP A 438 12.071 17.485 17.083 1.00 33.57 C
ATOM 5732 O ASP A 438 12.272 16.718 16.148 1.00 33.42 O ATOM 5734 N ARG A 439 -12.639 17.352 18.277 1.00 34.22 N
ATOM 5735 CA ARG A 439 -13.480 16.215 18.627 1.00 34.25 C
ATOM 5737 CB ARG A 439 -13.800 16.252 20.117 1.00 34.57 C
ATOM 5740 CG ARG A 439 -14.306 14.933 20.672 1.00 35.47 C
ATOM 5743 CD ARG A 439 -13.142 13.999 21.009 1.00 38.09 C
ATOM 5746 NE ARG A 439 -13.362 13.212 22.221 1.00 38.92 N
ATOM 5748 CZ ARG A 439 -13.453 13.719 23.455 1.00 40.47 C
ATOM 5749 NHl ARG A 439 -13.388 15.034 23.674 1.00 41.39 N
ATOM 5752 NH2 ARG A 439 -13.633 12.908 24.490 1.00 40.86 N
ATOM 5755 C ARG A 439 -14.784 16.210 17.831 1.00 34.41 C
ATOM 5756 O ARG A 439 -15.636 17.086 18.011 1.00 34.44 O
ATOM 5758 N ALA B 25 20.680 5.892 20.193 1.00 75.32 N
ATOM 5759 CA ALA B 25 19.626 6.550 19.378 1.00 75.38 C
ATOM 5761 CB ALA B 25 18.286 6.439 20.073 1.00 75.26 C
ATOM 5765 C ALA B 25 19.992 8.012 19.158 1.00 75.48 C
ATOM 5766 O ALA B 25 20.702 8.598 19.980 1.00 75.47 O
ATOM 5770 N ARG B 26 19.515 8.592 18.050 1.00 75.63 N
ATOM 5771 CA ARG B 26 19.737 10.018 17.748 1.00 75.55 C
ATOM 5773 CB ARG B 26 20.539 10.187 16.440 1.00 75.69 C
ATOM 5776 CG ARG B 26 21.035 11.625 16.149 1.00 75.91 C
ATOM 5779 CD ARG B 26 21.848 12.238 17.312 1.00 76.39 C
ATOM 5782 NE ARG B 26 21.649 13.688 17.429 1.00 76.54 N
ATOM 5784 CZ ARG B 26 21.915 14.422 18.516 1.00 76.65 C
ATOM 5785 NHl ARG B 26 22.392 13.864 19.626 1.00 76.72 N
ATOM 5788 NH2 ARG B 26 21.695 15.734 18.497 1.00 76.62 N
ATOM 5791 C ARG B 26 18.421 10.822 17.707 1.00 75.47 C
ATOM 5792 O ARG B 26 17.348 10.272 17.441 1.00 75.38 O
ATOM 5794 N M3L B 27 18.528 12.123 17.996 1.00 75.36 N
ATOM 5795 CA M3L B 27 17.375 13.029 18.105 1.00 75.25 C
ATOM 5797 CB M3L B 27 17.831 14.409 18.606 1.00 75.11 C
ATOM 5800 CG M3L B 27 16.800 15.095 19.501 1.00 74.57 C
ATOM 5803 CD M3L B 27 17.323 16.434 20.025 1.00 73.87 C
ATOM 5806 CE M3L B 27 16.275 17.150 20.887 1.00 73.61 C
ATOM 5809 NZ M3L B 27 16.825 18.209 21.770 1.00 73.33 N
ATOM 5810 CM3 M3L B 27 17.419 17.624 22.981 1.00 72.84 C
ATOM 5814 CM2 M3L B 27 17.845 19.014 21.084 1.00 73.06 C
ATOM 5818 CMl M3L B 27 15.734 19.107 22.179 1.00 72.92 C
ATOM 5822 C M3L B 27 16.625 13.167 16.809 1.00 75.25 C
ATOM 5823 O M3L B 27 15.396 13.152 16.802 1.00 75.15 O
ATOM 5825 N SER B 28 17.360 13.303 15.704 1.00 75.33 N
ATOM 5826 CA SER B 28 16.769 13.363 14.359 1.00 75.39 C
ATOM 5828 CB SER B 28 17.303 14.583 13.601 1.00 75.38 C
ATOM 5831 OG SER B 28 17.554 15.669 14.472 1.00 75.43 O
ATOM 5833 C SER B 28 17.040 12.104 13.517 1.00 75.47 C
ATOM 5834 O SER B 28 16.518 11.995 12.407 1.00 75.48 O
ATOM 5836 N ALA B 29 17.844 11.173 14;050 1.00 75.55 N
ATOM 5837 CA ALA B 29 18.310 9.960 13^342 1.00 75.50 C
ATOM 5839 CB ALA B 29 17.898 8.703 14.109 1.00 75.47 C
ATOM 5843 C ALA B 29 17.854 9.855 11.889 1.00 75.59 C
ATOM 5844 O ALA B 29 18.532 10.335 10.978 1.00 75.66 O
ATOM 5846 O HOH W 1 3.353 21.644 34.241 1.00 14.62 O
ATOM 5849 O HOH W 2 7.058 21.129 27.066 1.00 20.36 O
ATOM 5852 O HOH W 3 19.997 41.953 52.474 1.00 28.73 O
ATOM 5855 O HOH W 4 0.411 0.910 14.141 1.00 21.41 O
ATOM 5858 O HOH W 5 17.929 30.534 45.458 1.00 17.06 O
ATOM 5861 O HOH W 6 0.812 23.686 7.172 1.00 21.81 O
ATOM 5864 O HOH W 7 -4.349 26.593 7.215 1.00 36.06 O
ATOM 5867 O HOH W 8 -2.743 3.988 40.707 1.00 27.09 O
ATOM 5870 O HOH W 9 17.062 28.301 28.083 1.00 15.07 O
ATOM 5873 O HOH W 10 -0.451 12.730 37.561 1.00 30.51 O
ATOM 5876 O HOH W 11 8.409 10.991 52.227 1.00 17.27 O
ATOM 5879 O HOH W 12 21.378 5.915 37.446 1.00 51.02 O
ATOM 5882 O HOH W 13 1.584 23.650 30.831 1.00 18.65 O
ATOM 5885 O HOH W 14 19.498 13.476 39.043 1.00 11.62 O
ATOM 5888 O HOH W 15 19.169 1.884 38.589 1.00 25.64 O
ATOM 5891 O HOH W 16 -0.070 16.181 29.845 1.00 38.28 O
ATOM 5894 O HOH H 17 7.804 39.957 22.382 1.00 21.57 O
ATOM 5897 O HOH W 18 -1.932 24.524 31.494 1.00 14.86 O
ATOM 5900 O HOH W 19 6.741 19.077 28.908 1.00 27.33 O
ATOM 5903 O HOH W 20 1.584 19.154 25.946 1.00 15.44 O
ATOM 5906 O HOH W 21 21.183 20.247 51.905 1.00 29.30 O
ATOM 5909 O HOH W 22 22.448 26.500 47.592 1.00 11.40 O
ATOM 5912 O HOH W 23 14.973 1.128 44.312 1.00 26.32 O
ATOM 5915 O HOH W 24 9.125 19.706 24.941 1.00 35.61 O
ATOM 5918 O HOH W 25 -1.613 5.601 47.375 1.00 35.42 O
ATOM 5921 O HOH W 26 3.024 24.428 48.658 1.00 24.03 O
ATOM 5924 O HOH W 27 -9.682 11.923 36.588 1.00 11.51 O ATOM 5927 O HOH W 28 19.348 18.010 25.757 1.00 29.00 O
ATOM 5930 O HOH W 29 4.612 14.104 31.176 1.00 15.95 O
ATOM 5933 O HOH W 30 9.055 5.142 21.135 1.00 26.41 O
ATOM 5936 O HOH W 31 23.745 30.388 23.817 1.00 39.10 O
ATOM 5939 O HOH W 32 3.726 21.498 31.659 1.00 16.45 O
ATOM 5942 O HOH W 33 -2.400 17.226 26.781 1.00 15.75 O
ATOM 5945 O HOH W 34 24.203 18.397 44.408 1.00 22.15 O
ATOM 5948 O HOH W 35 9.345 -2.230 25.782 1.00 14.66 O
ATOM 5951 O HOH W 36 -3.380 34.782 27.069 1.00 16.55 O
ATOM 5954 O HOH W 37 13.535 30.840 54.915 1.00 16.79 O
ATOM 5957 O HOH W 38 14.689 37.917 32.171 1.00 29.55 O
ATOM 5960 O HOH W 39 4.366 13.167 54.933 1.00 36.74 O
ATOM 5963 O HOH W 40 15.098 17.053 14.893 1.00 41.83 O
ATOM 5966 O HOH W 41 5.909 10.723 48.610 1.00 25.82 O
ATOM 5969 O HOH W 42 10.872 7.836 21.048 1.00 41.46 O
ATOM 5972 O HOH W 43 3.594 13.440 20.565 1.00 26.85 O
ATOM 5975 O HOH W 44 15.983 35.791 39.839 1.00 32.50 O
ATOM 5978 O HOH W 45 14.395 40.271 32.889 1.00 31.82 O
ATOM 5981 O HOH W 46 5.815 21.442 30.150 1.00 20.89 O
ATOM 5984 O HOH W 47 0.453 -2.961 22.598 1.00 24.17 O
ATOM 5987 O HOH W 48 9.538 36.680 55.300 1.00 34.91 O
ATOM 5990 O HOH W 49 15.769 35.480 46.089 1.00 29.57 O
ATOM 5993 O HOH W 50 -6.715 40.540 37.977 1.00 30.82 O
ATOM 5996 O HOH W 51 -7.599 9.644 10.676 1.00 29.13 O
ATOM 5999 O HOH W 52 0.167 22.912 37.173 1.00 20.99 O
ATOM 6002 O HOH W 53 -0.846 21.099 30.646 1.00 28.73 O
ATOM 6005 O HOH W 54 -2.725 36.726 25.426 1.00 22.68 O
ATOM 6008 O HOH W 55 12.645 -2.170 31.241 1.00 24.05 O
ATOM 6011 O HOH W 56 9.260 29.630 57.855 1.00 26.88 O
ATOM 6014 O HOH W 57 6.478 33.036 55.496 1.00 27.76 O
ATOM 6017 O HOH W 58 -8.689 5.167 14.850 1.00 22.10 O
ATOM 6020 O HOH W 59 26.976 10.136 31.006 1.00 24.23 O
ATOM 6023 O HOH W 60 12.771 33.081 16.560 1.00 26.21 O
ATOM 6026 O HOH W 61 16.046 24.742 50.740 1.00 21.24 O
ATOM 6029 O HOH W 62 -2.627 -4.370 33.613 1.00 27.77 O
ATOM 6032 O HOH W 63 26.688 11.847 45.297 1.00 37.40 O
ATOM 6035 O HOH W 64 -0.983 0.278 21.364 1.00 23.08 O
ATOM 6038 O HOH W 65 6.761 29.375 18.462 1.00 25.09 O
ATOM 6041 O HOH W 66 5.504 -8.000 35.963 1.00 37.35 O
ATOM 6044 O HOH W 67 3.653 -8.089 32.888 1.00 25.88 O
ATOM 6047 O HOH W 68 -0.166 37.820 24.370 1.00 12.82 O
ATOM 6050 O HOH W 69 13.285 31.596 13.274 1.00 22.31 O
ATOM 6053 O HOH W 70 13.722 35.547 17.414 1.00 29.99 O
ATOM 6056 O HOH W 71 21.366 21.805 37.746 1.00 21.11 O
ATOM 6059 O HOH W 72 25.803 24.664 37.204 1.00 27.30 O
ATOM 6062 O HOH W 73 18.840 32.517 39.127 1.00 28.68 O
ATOM 6065 O HOH W 74 24.449 10.183 45.134 1.00 21.37 O
ATOM 6068 O HOH W 75 10.932 26.757 33.739 1.00 17.63 O

Claims

1. A crystalline EED polypeptide, said polypeptide being bound to a tri- methyllysine histone peptide or an analogue thereof.
2. EED polypeptide having the structure defined by the structural coordinates as shown herein.
3. A method for identifying a candidate modulator of EED polypeptide activity, said method comprising
(i) providing a molecular modelling apparatus with a set of structural coordinates of an EED polypeptide selected from those shown herein;
(ii) providing said molecular modelling apparatus with a set of structural coordinates of a molecular entity of interest; and
(iii) determining whether the molecular entity of interest is expected to bind to or to affect the structure of said EED polypeptide, wherein an expectation of binding or affecting the structure of said EED polypeptide identifies said molecular entity of interest as a candidate modulator of EED polypeptide activity.
4. A method according to claim 3 wherein the structural coordinates of at least the aromatic cage of EED are selected.
5. A method according to claim 3 wherein each of the structural coordinates of presented herein are selected.
6. A method for identifying a candidate therapeutic agent, said method comprising application of rational drug design to the crystal structure of EED.
7. A method of manufacturing a modulator of a EED polypeptide, said method comprising identifying a candidate modulator according to any of claims 3 to 6, and synthesising a quantity of said modulator.
8. Use of the atomic coordinates as shown herein in the modelling of a EED polypeptide.
9. A method for the design of one or more ligands of a EED polypeptide, said method comprising the use of coordinates presented herein.
10. A method or product substantially as described herein. ,
PCT/GB2009/002822 2008-12-05 2009-12-03 Structure and uses of embryonic ectoderm development (eed) polypeptide WO2010064019A1 (en)

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