Title:
Modulating nuclear receptor coactivator binding
Kind Code:
A1


Abstract:
The present invention comprises cocrystal of a nuclear receptor comprising a molecule bound to the coactivator binding site of said nuclear receptor. The present invention further comprises a machine-readable data storage medium encoded with machine readable data corresponding to the structure coordinates of amino acids of a nuclear receptor coactivator binding site which, when using a machine programmed with instructions for using said data, is capable of displaying a graphical three-dimensional representation of a molecular complex of a compound bound to a nuclear receptor coactivator binding site.



Inventors:
Baxter, John D. (San Francisco, CA, US)
Darimont, Beatrice (Eugene, OR, US)
Feng, Weijun (Hayward, CA, US)
Fletterick, Robert J. (Hillsborough, CA, US)
Kushner, Peter J. (San Francisco, CA, US)
Wagner, Richard L. (San Francisco, CA, US)
West, Brian L. (San Francisco, CA, US)
Yamamoto, Keith R. (San Francisco, CA, US)
Application Number:
11/274682
Publication Date:
07/06/2006
Filing Date:
11/14/2005
Assignee:
Regents of the University of California
Primary Class:
Other Classes:
257/E21.266, 530/350, 257/E21.218
International Classes:
C07K14/72; G01N33/53; C07K14/47; C07K14/705; C12N15/09; G01N33/00; G01N33/15; G01N33/50; G01N33/68; G06F17/30; G06F17/50; G06G7/48; H01L21/3065; H01L21/314; H01L21/336
View Patent Images:



Primary Examiner:
DEJONG, ERIC S
Attorney, Agent or Firm:
VLP Law Group LLP (Palo Alto, CA, US)
Claims:
What is claimed is:

1. A cocrystal of a nuclear receptor comprising a molecule bound to the coactivator binding site of said nuclear receptor.

2. The cocrystal of claim 1, wherein said nuclear receptor is a thyroid receptor.

3. The cocrystal of claim 2, wherein said thyroid receptor is human.

4. The cocrystal of claim 3, wherein said molecule is peptide.

5. The cocrystal of claim 4, wherein said peptide comprises a NR-box amino acid sequence or derivative thereof.

6. The cocrystal of claim 4 wherein the peptide comprises a nuclear receptor box sequence.

7. The cocrystal of claim 4 wherein the peptide consists of a portion of GRIP1 comprising a nuclear receptor box 2 sequence, wherein the portion is given by SEQ ID NO: 6.

8. The cocrystal of claim 7 wherein the peptide consists of a sequence selected from the group consisting of: residues 11-23 of SEQ ID NO: 6, residues 12-24 of SEQ ID NO: 6, residues 14-24 of SEQ ID NO: 6, residues 14-22 of SEQ ID NO: 6, and residues 7-23 of SEQ ID NO: 6.

9. The cocrystal of claim 6 wherein the nuclear receptor box sequence is ILHRLL.

10. The cocrystal of claim 6 wherein the peptide consists of a portion of GRIP1 comprising a nuclear receptor box 3 sequence, wherein the portion is given by SEQ ID NO: 7.

11. The cocrystal of claim 3 wherein the peptide comprises a sequence selected from the group consisting of: residues 9-21 of SEQ ID NO: 7, residues 8-24 of SEQ ID NO: 7, residues 5-24 of SEQ ID NO: 7.

12. The cocrystal of claim 6 wherein the nuclear receptor box sequence is LLRYLL.

13. The cocrystal of claim 4 wherein the peptide has sequence SEQ ID NO: 31.

14. A machine-readable data storage medium, comprising a data storage material encoded with machine readable data which, when using a machine programmed with instructions for using said data, is capable of displaying a graphical three-dimensional representation of a molecular complex of a compound bound to a nuclear receptor coactivator binding site comprising structure coordinates of amino acids corresponding to human thyroid receptor amino acids selected from the group consisting of helix 3 residues Ile280, Thr281, Val283, Val284, Ala287, and Lys288, helix 4 residue Phe293, helix 5 residues Gln301, Ile302, Leu305, Lys306, helix 6 residue Cys309, and helix 12 residues Pro453, Leu454, Glu457, Val458 and Phe459, or a homologue of said molecular complex, wherein said homologue comprises a coactivator binding site that has a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.

15. The machine readable storage medium of claim 14, wherein said nuclear receptor is a thyroid receptor.

16. The machine readable storage medium of claim 15, wherein said thyroid receptor is human.

17. The machine readable storage medium of claim 16, wherein said molecule is peptide.

18. The machine readable storage medium of claim 17, wherein said peptide comprises a NR-box amino acid sequence, or derivative thereof.

19. The machine-readable data storage medium according to claim 14, wherein said molecular complex is defined by the set of structure coordinates depicted in Appendix 1, or a homologue of said molecular complex, said homologue having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.

20. A machine-readable data storage medium comprising a data storage material encoded with a first set of machine readable data which, when combined with a second set of machine readable data, using a machine programmed with instructions for using said first set of data and said second set of data, can determine at least a portion of the structure coordinates corresponding to the second set of machine readable data, wherein: said first set of data comprises a Fourier transform of at least a portion of the structural coordinates selected from the group consisting of coordinates depicted in Appendix 1; and said second set of data comprises an X-ray diffraction pattern of a molecule or molecular complex.

Description:

CLAIM OF PRIORITY

This application is a divisional of, and claims the benefit of priority to, U.S. application Ser. No. 09/281,717, filed Mar. 30, 1999, now U.S. Pat. No. 6,965,850, which claims priority under Title 35, United States Code § 119(e) of U.S. provisional application 60/079,956 filed Mar. 30, 1998, and 60/113,146, filed Dec. 16, 1998, all of which are incorporated by reference herein in their entirety.

ACKNOWLEDGEMENTS

This invention was supported in part by grants from the National Institutes of Health: Grant Nos. DK 51083, DK 51281, and P41-RR01081 and from the Army of the United States: Grant No. AIBS#562. The U.S. Government may have rights in this invention.

FIELD OF THE INVENTION

The present invention relates to nuclear receptor coactivator binding, and achieving modulation of the same.

BACKGROUND

Cells contain receptors that can elicit a biological response by binding various molecules including proteins, hormones and/or drugs. Nuclear receptors represent a super family of proteins that are hormone/ligand-activated transcription factors that enhance or repress transcription in a cell type-, ligand- and promoter-dependent manner. The nuclear receptor family includes receptors for glucocorticoids (GRs), androgens (ARs), mineralocorticoids (MRs), progestins (PRs), estrogens (ERs), thyroid hormones (TRs), vitamin D (VDRs), retinoids (RARs and RXRs), peroxisomes (XPARs and PPARs) and icosanoids (IRs). The so-called “orphan receptors” for which ligands have not been identified are also part of the nuclear receptor superfamily, as they are structurally homologous to the classic nuclear receptors, such as steroid and thyroid receptors.

Although overall sequence conservation between nuclear receptors varies between different families of receptors, sequence conservation between functional regions, or modules, of the receptors is high. For example, nuclear receptors can be organized into functional modules comprising an N-terminal transcriptional activation domain, a central DNA binding domain (DBD), and a C-terminal ligand binding domain (LBD). The LBD of nuclear receptors represents a hormone/ligand dependent molecular switch. Binding of hormone to a nuclear receptor's LBD changes its ability to modulate transcription of DNA, although they may have transcription-independent actions. Nuclear receptors also bind proteins, such as chaperone complexes, corepressors, or coactivators, that are involved in receptor function. Hormone binding by a nuclear receptor can increase or decrease binding affinity to these proteins, and can influence or mediate the multiple actions of the nuclear receptors on transcription. For example, nuclear receptors can stimulate transcription in response to hormone binding by recruiting coactivator proteins to promoters of responsive genes (Glass et al., Curr. Opin. Cell Biol. (1997) 9:222-32); and Horwitz et al., Mol. Endocrinol. (1996) 10:1167-77).

Coactivators of the p160 family mediate activity of a transcriptional activation domain, called AF2, that is part of the nuclear receptor's LBD. A few receptor mutants deficient in coactivator-dependent activation have been isolated (TR: Collingwood et al. Proc. Natl. Acad. Sci. (1997) 94:248-253; VDR: Jurutka et al., J. Biol. Chem. (1997) 227:14592-14599, Masayama et al., Mol. Endocrinol. (1997) 11:1507-1517; ER and RAR: Henttu et al., Mol. Cell Biol. (1997) 17:1832-1839). While these studies support the physiological relevance of the observed interaction, the structural and functional nature of the site to which coactivators bind has not been defined.

The medical importance of nuclear receptors is significant. They have been implicated in breast cancer, prostate cancer, cardiac arrhythmia, infertility, osteoporosis, hyperthyroidism, hypercholesterolemia, obesity and other conditions. However, limited treatments are available and current agonist/antagonist drugs used to target nuclear receptors are ligands that bind to the receptor's LBD buried deep within the receptor. Although additional targets on nuclear receptors are desired for drug development, the structural and functional basis of such sites, including the coactivator binding site, has not been described.

Accordingly, a need exists for identification and characterization of the coactivator binding sites of nuclear receptors, and molecules that affect their interaction with cellular coactivator proteins. This would provide a major new target for iterative drug design, synthesis, and selection. It also would be advantageous to devise methods and compositions for reducing the time required to discover compounds that target the coactivator binding site of nuclear receptors and administer them to organisms to modulate physiological processes regulated by nuclear receptors.

Relevant Literature

Wagner et al., (Nature (1995) 378:690-697) disclose the crystal structure of rat TR-alpha LBD. Various references disclose mutations in carboxyl-terminal helices of nuclear receptors (Henttu et al., supra; O'Donnell et al., Mol. Endocrinol. (1991) 5:94-99; Whitfield et al., Mol. Endocrinol. (1995) 9:1166-79; Saatcioglu et al., Mol. Cell Biol. (1997) 17:4687-95; Collingwood et al., supra; Kamei et al., Cell (1996) 85:403-14). Hong et al. (Proc. Natl. Acad. Sci. USA (1996) 93(10):498-49452) and Hong et al. (Mol. Cell. Biol. (1997) 17:2735-2744) disclose cloning and expression of GRIP1 coactivator. Torchia et al., (Nature (1997) 387:677-84), Le Douarin et al., (EMBO J (1996) 15:6701-6715) and Heery et al. (Nature (1997) 387:733-736) disclose sequence alignment of various coactivator proteins showing a (SEQ ID NO: 1) LxxLL motif.

SUMMARY OF THE INVENTION

The present invention relates to identification and manipulation of the coactivator binding site of nuclear receptors. Identification of this site permits design and obtention of compounds that bind to the coactivator binding site of nuclear receptors and modulate coactivator binding to the receptor. The compounds include agonists and antagonists that modulate nuclear receptor activity by promoting (agonists) or blocking (antagonists) hormone-dependent coactivator binding to the receptor, particularly antagonists. The compounds of the invention can be receptor-, cell- and/or tissue-specific.

The present invention also includes protein cocrystals of nuclear receptors with a molecule bound to the coactivator binding site and methods for making them. The cocrystals provide means to obtain atomic modeling information of the specific amino acids and their atoms forming the coactivator binding site and that interact with molecules that bind to the site, such as coactivator. The cocrystals also provide modeling information regarding the coactivator nuclear receptor interaction, as well as the structure of coactivators bound thereto.

The present invention further provides methods for identifying and designing small molecules that bind to the coactivator binding site using atomic models of nuclear receptors. The method involves modeling test compounds that fit spatially into a nuclear receptor coactivator binding site of interest using an atomic structural model comprising a nuclear receptor coactivator binding site or portion thereof, screening the test compounds in a biological assay characterized by binding of a test compound to a nuclear receptor coactivator binding site, and identifying a test compound that modulates coactivator binding to the nuclear receptor.

The invention also includes compositions and methods for identifying coactivator binding sites of nuclear receptors. The methods involve examining the surface of a nuclear receptor of interest to identify residues that modulate coactivator binding. The residues can be identified by homology to the coactivator binding site of human TR described herein. Overlays and superpositioning with a three dimensional model of a nuclear receptor LBD, or a portion thereof that contains a coactivator binding site, also can be used for this purpose. Additionally, alignment and/or modeling can be used as a guide for the placement of mutations on the LBD surface to characterize the nature of the site in the context of a cell.

Also provided is a method of modulating the activity of a nuclear receptor. The method can be in vitro or in vivo. The method comprises administering, in vitro or in vivo, a sufficient amount of a compound that binds to the coactivator binding site. Preferred compounds bind to the site with greater affinity than coactivator proteins found in a cell of interest. Binding at this site, the compound can compete for binding of coactivator proteins, thereby inhibiting gene transcription, or in some cases promoting it, even when hormone is or is not bound.

The invention further includes a method for identifying an agonist or antagonist of coactivator binding to a nuclear receptor. The method comprises providing the atomic coordinates comprising a nuclear receptor coactivator binding site or portion thereof to a computerized modeling system; modeling compounds which fit spatially into the nuclear receptor coactivator binding site; and identifying in an assay for nuclear receptor activity a compound that increases or decreases activity of the nuclear receptor through binding the coactivator binding site.

Also provided is a machine-readable data storage medium with information for constructing and manipulating an atomic model comprising a coactivator binding site or portion thereof. The medium comprises a data storage material encoded with machine readable data which, when using a machine programmed with instructions for using said data, is capable of displaying a graphical three-dimensional representation of a molecule or molecular complex for a nuclear receptor coactivator binding site.

Also provided is a method of identifying a compound that selectively modulates the activity of one type of nuclear receptor compared to other nuclear receptors. The method is exemplified by modeling test compounds that fit spatially and preferentially into a nuclear receptor coactivator binding site of interest using an atomic structural model of a nuclear receptor coactivator binding site, selecting a compound that interacts with one or more residues of the coactivator binding site unique in the context of that site, and identifying in an assay for coactivator binding activity a compound that selectively binds to the coactivator binding site compared to other nuclear receptors. The unique features involved in receptor-selective coactivator binding can be identified by comparing atomic models of different receptors or isoforms of the same type of receptor.

The invention finds use in the selection and characterization of peptide, peptidomimetic, as well as other small molecule compounds, such as small organic molecules, identified by the methods of the invention, particularly new lead compounds useful in treating nuclear receptor-based disorders.

BRIEF DESCRIPTION OF THE DRAWINGS

The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee.

FIG. 1 shows the specific effects of mutations on hTRβ1 transcriptional activation in HeLa cells and correlation with effects on binding to GST-GRIP1. T3 dependent activation of transcription of a reporter gene, expressed as the percentage of WT is plotted for each mutant. GST-GRIP1 binding, analyzed by autoradiography after separation using 10% SDS-PAGE, was also expressed as the percentage of WT and plotted for each mutant. The GST-GRIP1 used included GRIP1 amino acids 721-1121; the same results were obtained using a GST-GRIP1 construct including GRIP1 amino acids 563-1121 (data not shown).

FIG. 2 shows that overexpression of full-length GRIP1 rescues loss of transcriptional activation by hTRβ1 mutants. Indicated amounts of the expression vector for full-length GRIP1, pSG5-GRIP1, is included in the cotransfections, which otherwise are performed as in FIG. 1. The WT or different representative hTRβ1 mutants are indicated.

FIG. 3 shows specific hERα surface mutants cause loss of transcriptional activation in HeLa cells in parallel with their loss of in vitro GRIP1 binding. The fold E2 activation, expressed as the percentage of WT, and the phosphorimager quantitation of in vitro binding of [35S]-labeled hERα WT and mutants to GST-GRIP1 (GRIP1 amino acids 721-1121) also expressed as the percentage of WT is plotted for each mutant.

FIG. 4 shows a plot of the fold E2 activation observed when the indicated amounts of the full-length GRIP1 expression vector, pSG5-GRIP1, are added to the co-transfection experiment, which otherwise is performed as for FIG. 3. The WT or different hERα mutants are indicated. The data represent the averages of three independent experiments, with standard deviations less than 10%.

FIG. 5 shows a CPK model of the TRα-LBD, indicating the LBD surface locations of mutations made in the full-length hTRβ1. Mutated residues having no effect on GRP1 binding or effect on activation in HeLa cells are shaded gray. Mutated residues with diminished GRIP1 and SRC-1a binding and diminished activation in HeLa cells are colored to reflect chemical properties of the residues: red, blue (purple), and green indicate acidic, basic, and hydrophobic residues, respectively. The main chain structures of the TRα- and TRβ-LBDs are the same (data not shown).

FIG. 6 shows sequence alignment of amino acid residues of members of the p160 coactivator family. Single amino acid designations are used. Members of the p160 coactivator family interact with the nuclear receptors through conserved (SEQ ID NO: 1) LxxLL motifs.

FIG. 7 (comprising FIGS. 7a and 7b) shows binding affinity assays of GST-GRIP1 constructs with NR-boxes 1, 2, and/or 3 and their interaction with TR LBD. GRIP-1 NR boxes 1, 2 and 3 interact differently with TRβ LBD. Single letter designations are used for the amino acids (FIG. 7a).

FIG. 8 (comprising FIGS. 8a and 8b) shows binding affinity assays of GST-GRIP1 constructs with NR-boxes 1,2, and/or 3 and their interaction with TR and GR LBDs. TR and GR differ in their interactions with GRIP-1.

FIG. 9 (comprising FIGS. 9a and 9b) shows binding affinity assays for NR-box 2- and 3-peptides and GRIP1 and their interaction with TR LBD. NR box 2- and 3-containing peptides (FIG. 9b) reproduce the affinity and specificity of the NR interaction domain (FIG. 9a).

FIG. 10 (comprising FIGS. 10a, 10b and 10c) shows binding affinity assays for NR-box 2- and 3-peptides and their interaction with TR LBD. Sequences adjacent to the (SEQ ID NO: 1) LxxLL motif modulate the affinity of NR-box-TRP LBD interactions.

FIG. 11 shows binding affinity assays for mutant GRIP1 and NR-box 2- and 3-peptides and their interaction with TR LBD. The individual leucine residues of the (SEQ ID NO: 1) LxxLL motif are crucial for binding of the GRIP-1 NR interaction domain to TRP LBD.

FIG. 12 shows the contents of the asymmetric unit of the crystallized hTRβ LBD:GRIP1 NR-box 2 peptide complex. The crystal lattice consists of a repeating unit containing a 2:2 complex of hTR LBD and GRIP1 site 2 peptide. Positions of the two GRIP1 site 2 peptides are boxed, in green (site 1), and red (site 2), with the peptides drawn as a C-alpha trace. The two NCS related monomers of the hTR LBD are shown as a secondary structure ribbon drawing, with monomer 1 in light grey, and monomer 2 in dark grey. The side chains of the hydrophobic residues I689, L690, L693, L694 of the GRIP1 NR-box 2 peptides are drawn to emphasize those interactions observed in both bound peptides.

FIG. 13 shows a ribbon diagram depicting the interaction of the GRIP1 NR-box 2 peptide with the hTRβ LBD. The GRIP1 NR-box 2 peptide (dark grey) forms three turns of α-helix, and binds the hTR LBD (light gray) in a hydrophobic cleft defined by helices H3, H4, H5, and H12. Portions of the hTRβ LBD, and the neighboring monomer, are omitted for clarity.

FIG. 14 shows interface between the GRIP1 NR-box 2 peptide and the hTRβ LBD. Side chains of residues of the hTRβ LBD within 4.5 Å of the GRIP-1 NR-box 2 peptide are labeled. The color of the individual side chains reflects the chemical nature of the residue: acidic residues are red, basic residue are blue, aliphatic residues are green, aromatic residues are brown, and polar residues are orange. The peptide is depicted as a C-alpha trace with the side chains of (SEQ ID NO: 2) ILxxLL motif shown explicitly.

FIG. 15 shows residues in the hTRβ LBD that are necessary for transactivation. The transactivation mutations are mapped onto the interface between the GRIP1 NR-box 2 peptide and the hTRβ LBD.

FIG. 16 shows molecular surface of the hTR LBD. The side chains of the leucines resides fit within a hydrophobic groove formed from helices H3, H5, and H12, while the side chain of the non-conserved isoleucine residue packs against the outside edge of the groove. The remainder of the peptide is shown as main chain.

FIG. 17 shows complementarity between the (SEQ ID NO: 1) LxxLL motif and the surface of the hTR LBD. The side chains of the (SEQ ID NO: 2) ILxxLL motif are shown in a CPK representation, with the main chain of the peptide drawn as a C-alpha trace. The three leucince residues fit into pockets of the coactivator binding site of the hTRβ LBD, depicted as mesh, while the isoleucine residue rests on the edge of the site's cleft.

FIG. 18 shows the coactivator binding site cleft, one side of which is formed by conformationally hormone-responsive residues. On the left is a view of the TR-LBD molecular surface showing the concave surfaces in gray. The cavity is shown at the center of the figure. On the right is shown a CPK model of the TR-LBD, overlaid with a molecular surface view, which is restricted to a 12 Å radius of the hydrophobic cavity. Mutated residues of the coactivator binding site that are hormone-insensitive (V284, K288, I302 and K306) are located on one side of the cleft and are colored yellow. Mutated CBS residues likely undergo a conformational change upon hormone binding (L454 and E457) are located on the opposite side of the cleft and are colored red.

FIG. 19 shows alignment of amino acid sequences (single letter amino acid designations) containing residues that form the coactivator binding sites of several nuclear receptors. The boxes represent residues of alpha-helix (H3, H4, H5, H6 and H12); lower case letters “h” and “q” represent hydrophobic and polar residues, respectively.

DESCRIPTION OF SPECIFIC EMBODIMENTS

The present invention provides methods and compositions for identifying compounds that modulate nuclear receptor activity. The compounds can be nuclear receptor agonists or antagonists that bind to the coactivator binding site (and that act as mimetics to the coactivator in this regard), and promote (agonists) or block (antagonists) binding of the coactivator to the target nuclear receptor. Compounds that bind to the coactivator binding site also are provided. The compounds can be natural or synthetic. Preferred compounds are small organic molecules, peptides and peptidomimetics (e.g., cyclic peptides, peptide analogs, or constrained peptides).

As described in the Examples, mutagenesis and coactivator binding studies, coupled with analysis of atomic models derived from cocrystals, reveals for the first time a previously unknown structure for nuclear receptors, the coactivator binding site. By “coactivator binding site” is intended a structural segment or segments of nuclear receptor polypeptide chain folded in such a way so as to give the proper geometry and amino acid residue conformation for binding a coactivator. This is the physical arrangement of protein atoms in three-dimensional space forming a coactivator binding site pocket or cavity. Residues forming the site are amino acids corresponding to (i.e., the same as or equivalent to) human TR residues of C-terminal helix 3 (Ile280, Thr281, Val283, Val284, Ala287, and Lys288), helix 4 (Phe293), helix 5 (Gln301, Ile302, Leu305, Lys306), helix 6 (Cys309), and helix 12 (Leu454, Glu457, Val458 and Phe459). The coactivator binding site is highly conserved among the nuclear receptor super family (FIG. 19). Thus, this site corresponds to a surprisingly small cluster of residues on the surface of the LBD that form a prominent hydrophobic cleft. The hydrophobic cleft is formed by hydrophobic residues corresponding to human TR residues of C-terminal helix 3 (Ile280, Val283, Val284, and Ala287), helix 4 (Phe293), helix 5 (Ile302 and Leu305), helix 6 (Cys309), and helix 12 (Leu454, Val458 and Phe459). The hydrophobic cleft of the coactivator binding site also is highly conserved among the nuclear receptor super family (FIG. 19).

The invention also includes compositions and methods for identifying coactivator binding sites of nuclear receptors. The methods involve examining the surface of a nuclear receptor of interest to identify residues that modulate coactivator binding. The residues can be identified by homology to the coactivator binding site of human TR described herein. A preferred method is alignment with the residues of any nuclear receptor corresponding to (i.e., equivalent to) human TR residues of the C-terminal helix 3 (Ile280, Thr281, Val283, Val284, Ala287, and Lys288), helix 4 (Phe293), helix 5 (Gln301, Ile302, Leu302, Lys306), helix 6 (Cys309), and helix 12 (Pro453, Leu454, Glu457, Val458 and Phe459). Overlays and superpositioning with a three-dimensional model of a nuclear receptor LBD, or a portion thereof that contains a coactivator binding site, also can be used for this purpose. For example, three-dimensional structures of TR, RAR, RXR and ER LBDs can be used for this purpose. For example, nuclear receptors identifiable by homology alignment include normal nuclear receptors or proteins structurally related to nuclear receptors found in humans, natural mutants of nuclear receptors found in humans, normal or mutant receptors found in animals, as well as non-mammalian organisms such as pests or infectious organisms, or viruses.

Alignment and/or modeling also can be used as a guide for the placement of mutations on the LBD surface to characterize the nature of the site in the context of a cell. Selected residues are mutated to preserve global receptor structure and solubility. To destroy the coactivator binding interaction, preferred mutations are to charged residues (e.g., Arg, Lys, or Glu) on the basis that bulky, surface charged residues might disrupt coactivator binding, yet preserve global receptor structure and solubility. Mutants can be tested for coactivator binding as well as the relative change in strength of the binding interaction. Ligand-dependent coactivator interaction assays also can be tested for this purpose, such as those described herein.

Compounds that bind to the coactivator binding site of nuclear receptors can be identified by computational modeling and/or screening. For example, coactivator agonists or antagonists can be identified by providing atomic coordinates comprising a nuclear receptor coactivator binding site or portion thereof to a computerized modeling system, modeling them, and identifying compounds that fit spatially into the coactivator binding site. By a “portion thereof” is intended the atomic coordinates corresponding to a sufficient number of residues or their atoms of the coactivator binding site that interact with a compound capable of binding to the site. This includes receptor residues having an atom within 4.5 Å of a bound compound or fragment thereof. For instance, human TR residues Val284, Phe293, Ile302, Leu305 and Leu454 contain side chain atoms that are within 4.5 Å, and interact with, hydrophobic residues of a (SEQ ID NO: 1) LxxLL motif of an NR-box 2 coactivator peptide. As another example, an atomic structural model utilized for computational modeling and/or screening of compounds that bind to the coactivator binding site may include a portion of atomic coordinates of amino acid residues corresponding to the site composed of residues of human thyroid receptor selected from Val284, Lys288, Ile302, Lys306, Leu454 and Glu457, or their structural and functional equivalents found in other receptors. Thus, for example, the atomic coordinates provided to the modeling system can contain atoms of the nuclear receptor LBD, part of the LBD such as atoms corresponding to the coactivator binding site or a subset of atoms useful in the modeling and design of compounds that bind to a coactivator binding site.

The atomic coordinates of a compound that fits into the coactivator binding site also can be used for modeling to identify compounds or fragments that bind the site. By “modeling” is intended quantitative and qualitative analysis of molecular structure/function based on atomic structural information and receptor-coactivator agonists/antagonists interaction models. This includes conventional numeric-based molecular dynamic and energy minimization models, interactive computer graphic models, modified molecular mechanics models, distance geometry and other structure-based constraint models. Modeling is preferably performed using a computer and may be further optimized using known methods. By “fits spatially” is intended that the three-dimensional structure of a compound is accommodated geometrically by a cavity or pocket of a nuclear receptor coactivator binding site.

Compounds of particular interest fit spatially and preferentially into the coactivator binding site. By “fits spatially and preferentially” is intended that a compound possesses a three-dimensional structure and conformation for selectively interacting with a nuclear receptor coactivator binding site. Compounds that fit spatially and preferentially into the coactivator binding site interact with amino acid residues forming the hydrophobic cleft of this site. In particular, the hydrophobic cleft of the coactivator binding site comprises a small cluster of hydrophobic residues. The site also contains polar or charged residues at its periphery. The present invention also includes a method for identifying a compound capable of selectively modulating coactivator binding to different nuclear receptors. The method comprises the steps of modeling test compounds that fit spatially and preferentially into the coactivator binding site of a nuclear receptor of interest using an atomic structural model of a nuclear receptor, screening the test compounds in a biological assay for nuclear receptor activity characterized by preferential binding of a test compound to the coactivator binding site of a nuclear receptor, and identifying a test compound that selectively modulates the activity of a nuclear receptor. Such receptor-specific compounds are selected that exploit differences between the coactivator binding sites of one type of receptor versus a second type of receptor, such as the differences depicted in FIG. 19.

The invention also is applicable to generating new compounds that distinguish nuclear receptor isoforms. This can facilitate generation of either tissue-specific or function-specific compounds. For instance, GR subfamily members have usually one receptor encoded by a single gene, although there are exceptions. For example, there are two PR isoforms, A and B, translated from the same mRNA by alternate initiation from different AUG codons. There are two GR forms, one of which does not bind ligand. This method is especially applicable to the TR subfamily which usually has several receptors that are encoded by at least two (TR: α, β) or three (RAR, RXR, and PPAR: α, β, γ) genes or have alternate RNA splicing.

The receptor-specific compounds of the invention preferably interact with conformationally constrained residues of the coactivator binding site that are conserved among one type of receptor compared to a second type of receptor. “Conformationally constrained” is intended to refer to the three-dimensional structure of a chemical or moiety thereof having certain rotations about its bonds fixed by various local geometric and physical-chemical constraints. Conformationally constrained structural features of a coactivator binding site include residues that have their natural flexible conformations fixed by various geometric and physical-chemical constraints, such as local backbone, local side chain, and topological constraints. These types of constraints are exploited to restrict positioning of atoms involved in receptor-coactivator recognition and binding.

For instance, comparison of sequences of the GR and TR coactivator interaction surface shows a highly negatively charged sequence at the C-terminal end of TR helix 12 (E460 and D461) that is neutral in the equivalent positions in GR helix 12 (GR residues 1788 and N759, corresponding to TR residue positions 460 and 461, as depicted in FIG. 19). As described in the Examples, the cocrystal of the hTRβ LBD complexed with the GRIP1 NR-box 2 peptide shows that TR residues E460 and D461 interact with positively charged residues of the NR-box 2 peptide. Also, when comparing the RAR LBD structure to that of the TR LBD, conformation of helix 12 differs slightly, whereas helices 3, 4, 5 and 6 are substantially the same. Thus, differences in helix 12, particularly charge differences at the C-terminal end of the helix, may modulate preferential interaction of TR for NR-box 2 containing coactivators. As further demonstrated in the Examples, GR and GB differ in their specificity for different NR-boxes containing the conserved (SEQ ID NO: 1) LxxLL motif found in members of the p160 family of coactivator proteins. As also demonstrated in the Examples, GR but not TR is able to interact with peptides containing the hydrophobic interaction motifs of p53 (SEQ ID NO: 3; FxxLW) and VP16 (SEQ ID NO: 4; FxxAL). Thus, TR exhibits preferential interaction with NR-box peptides comprising the (SEQ ID NO: 1) LxxLL motif, but GR does not discriminate and can bind peptides containing a generic amphipathic helix motif. Accordingly, these real differences among the various nuclear receptors can be exploited in the identification and design of compounds that modulate coactivator binding to one nuclear receptor compared to another.

For modeling, docking algorithms and computer programs that employ them can be used to identify compounds that fit into the coactivator binding site. For example, docking programs can be one of which does not bind ligand. This method is especially applicable to the TR subfamily which usually has several receptors that are encoded by at least two (TB: α, β) or three (RAR, RXR, and PPAR: α, β, γ) genes or have alternate RNA splicing.

The receptor-specific compounds of the invention preferably interact with conformationally constrained residues of the coactivator binding site that are conserved among one type of receptor compared to a second type of receptor. “Conformationally constrained” is intended to refer to the three-dimensional structure of a chemical or moiety thereof having certain rotations about its bonds fixed by various local geometric and physical-chemical constraints. Conformationally constrained structural features of a coactivator binding site include residues that have their natural flexible conformations fixed by various geometric and physical-chemical constraints, such as local backbone, local side chain, and topological constraints. These types of constraints are exploited to restrict positioning of atoms involved in receptor-coactivator recognition and binding.

For instance, comparison of sequences of the GR and TR coactivator interaction surface shows a highly negatively charged sequence at the C-terminal end of TR helix 12 (E460 and D461) that is neutral in the equivalent positions in GR helix 12 (GR residues 1788 and N759, corresponding to TR residue positions 460 and 461, as depicted in FIG. 19). As described in the Examples, the cocrystal of the hTRβ LBD complexed with the GRIP1 NR-box 2 peptide shows that TR residues E460 and D461 interact with positively charged residues of the NR-box 2 peptide. Also, when comparing the RAR LBD structure to that of the TR LBD, conformation of helix 12 differs slightly, whereas helices 3, 4, 5 and 6 are substantially the same. Thus, differences in helix 12, particularly charge differences at the C-terminal end of the helix, may modulate preferential interaction of TR for NR-box 2 containing coactivators. As further demonstrated in the Examples, TR and GR differ in theft specificity for different NR-boxes containing the conserved (SEQ ID NO: 1) LxxLL motif found in members of the p160 family of coactivator proteins. As also demonstrated in the Examples, GR but not TR is able to interact with peptides containing the hydrophobic interaction motifs of p53 (SEQ ID NO: 3; FxxLW) and VP16 (SEQ ID NO: 4; FxxAL). Thus, TR exhibits preferential interaction with NR-box peptides comprising the (SEQ ID NO: 1) LXXLL motif, but GR does not discriminate and can bind peptides containing a generic amphipathic helix motif. Accordingly, these real differences among the various nuclear receptors can be exploited in the identification and design of compounds that modulate coactivator binding to one nuclear receptor compared to another.

For modeling, docking algorithms and computer programs that employ them can be used to identify compounds that fit into the coactivator binding site. For example, docking programs can be used to predict how a small molecule of interest can interact with the nuclear receptor coactivator binding site. Fragment-based docking also can be used in building molecules de novo inside the coactivator binding site, by placing chemical fragments that complement the site to optimize intermolecular interactions. The techniques can be used to optimize the geometry of the binding interactions. This design approach has been made possible by identification of the coactivator binding site structure thus, the principles of molecular recognition can now be used to design a compound which is complementary to the structure of this site. Compounds fitting the coactivator binding site serve as a starting point for an iterative design, synthesis and test cycle in which new compounds are selected and optimized for desired properties including affinity, efficacy, and selectivity. For example, the compounds can be subjected to addition modification, such as replacement and/or addition of R-group substituents of a core structure identified for a particular class of binding compounds, modeling and/or activity screening if desired, and then subjected to additional rounds of testing.

Computationally small molecule databases can be screened for chemical entities or compounds that can bind in whole, or in part, to a nuclear receptor coactivator binding site of interest. In this screening, the quality of fit of such entities or compounds to the binding site may be judged either by shape complementarity (DesJalais et al., J. Med. Chem. (1988) 31:722-729) or by estimated interaction energy (Meng et al., J. Comp. Chem. (1992) 13:505-524). The molecule databases include any virtual or physical database, such as electronic and physical compound library databases, and are preferably used in developing compounds that modulate coactivator binding.

Compounds can be designed intelligently by exploiting available structural and functional information by gaining an understanding of the quantitative structure-activity relationship (QSAR), using that understanding to design new compound libraries, particularly focused libraries having chemical diversity of one or more particular groups of a core structure, and incorporating any structural data into that iterative design process. For example, one skilled in the art may use one of several methods to screen chemical entities or fragments for their ability to associate with the coactivator binding site of a nuclear receptor of interest. This process may begin by visual inspection of, for example, the coactivator binding site on the computer screen. Selected fragments or chemical entities may then be positioned into all or part of the site. Docking may be accomplished using software such as Quanta and Sybyl, followed by energy minimization and molecular dynamics with standard molecular mechanics force-fields, such as CHARMM and AMBER.

For example, compounds and/or fragments can be designed to fill up the hydrophobic cleft, the pocket deep within the cleft, the upper end of the site, and/or the lower end of the site. Residues comprising a coactivator binding site, when defined by the user as those residues having an atom within 4.5 Å of an atom of a bound chemical entity, can be modeled to look for energetic contributions and interaction with the bound chemical entity. For example, a compound or fragment can be designed to contain hydrophobic groups that interact with hydrophobic residues of the coactivator binding site. As described in the examples, human TR. residues V284, Phe293, Ile302, Leu305 and Leu454 contain side chain atoms that are within 4.5 Å, and interact with, hydrophobic residues of a (SEQ ID NO: 1) LxxLL motif of an NR-box 2 coactivator peptide. Thus, for example, peptides and/or peptide mimetics having a hxxhh motif, where “h” is a hydrophobic residue and x is any residue, can be constructed. Small organic molecules that mimic one or more of these particular interactions also can be designed, for example, by including one or more R-groups that are hydrophobic and fit into the site.

Specialized computer programs may also assist in the process of selecting chemical entity fragments or whole compounds. These include: GRID (Goodford, J. Med. Chem. (1985) 28:849-857; available from Oxford University, Oxford, UK); MCSS (Miranker et al., Proteins: Structure, Function and Genetics, (1991) 11:29-34; available from Molecular Simulations, Burlington, Mass.); AUTODOCK (Goodsell et al., Proteins: Structure, Function and Genetics (1990) 8:195-202; available from Scripps Research Institute, La Jolla, Calif.); and DOCK (Kuntz et al, J. Mol. Biol. (1982) 161:269-288; available from University of California, San Francisco, Calif.).

Additional commercially available computer databases for small molecular compounds include Cambridge Structural Database and Fine Chemical Database (Rusinko, Chem. Des. Auto. News (1993) 8:44-47).

Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound. Assembly may be proceeded by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of a nuclear receptor. This can be followed by manual model building using software such as Quanta or Sybyl.

Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include: CAVEAT (Bartlett et al., “CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules”, In: Molecular Recognition in Chemical and Biological Problems”, Special Pub., Royal Chem. Soc. (1989) 78:182-196; CAVEAT is available from the University of California, Berkeley, Calif.); 3D Database systems such as MACCS-3D (MDL Information Systems, San Leandro, Calif.; reviewed in Martin, J. Med. Chem. (1992) 35:2145-2154); and HOOK (available from Molecular Simulations, Burlington, Mass.).

In addition to building a compound in a step-wise fashion, one fragment or chemical entity at a time as described above, compounds that bind to a coactivator binding site of interest also may be designed as a whole or de novo using either an empty coactivator binding site or optionally including some portion(s) of a molecule known to binds to the site, such as an NR-box type peptide. These methods include: LUDI (Bohm, J. Comp. Aid. Molec. Design (1992) 6:61-78; LUDI is available from Biosym Technologies, San Diego, Calif.); LEGEND (Nishibata et al., Tetrahedron (1991) 47:8985; LEGEND is available from Molecular Simulations, Burlington, Mass.); and LeapFrog (available from Tripos Associates, St. Louis, Mo.).

Other molecular modeling techniques may also be employed in accordance with this invention. See, for example, Cohen et al., J. Med. Chem. (1990) 33:883-894); Navia et al., Curr. Opin. Struct. Biol. (1992) 2:202-210). For example, where the structures of test compounds are known, a model of the test compound may be superimposed over the model of the structure of the invention. Numerous methods and techniques are known in the art for performing this step, any of which may be used. See, for example, Farmer, “Drug Design,” Ariens, E. J., ed., 10:119-143 (Academic Press, New York, 1980); U.S. Pat. No. 5,331,573; U.S. Pat. No. 5,500,807; Verlinde, Structure, (1994) 2:577-587); and Kuntz et al., Science, (1992) 257:1078-1082). The model building techniques and computer evaluation systems described herein are not a limitation on the present invention.

Using these computer modeling systems a large number of compounds may be quickly and easily examined and expensive and lengthy biochemical testing avoided. Moreover, the need for actual synthesis of many compounds can be substantially reduced and/or effectively eliminated.

Compounds identified through modeling can be screened in an assay characterized by binding of the compound to a coactivator binding site of interest for coactivator binding activity, such as a biologically based assay. Screening can be in vitro and/or in vivo. Preferred assays include cell-free competition assays and cell culture based assays. The biological screening preferably centers on activity-based response models, binding assays (which measure how well a compound binds to the receptor), and bacterial, yeast and animal cell lines (which measure the biological effect of a compound in a cell). The assays can be automated for high capacity—high throughput screening (HTS) in which large numbers of compounds can be tested to identify compounds with the desired activity.

As an example, in vitro binding assays can be performed in which compounds are tested for their ability to block the binding of a coactivator protein, fragment, fusion or peptide thereof, to a coactivator binding site of interest. For cell and tissue culture assays, they may be performed to assess a compound's ability to block function of cellular coactivators, such as members of the p160 family of coactivator proteins, such as SRC-1, AIB1 RAC3, p/CIP, and GRIP1 and its homologues TIF 2 and NcoA-2, and those that exhibit receptor and/or isoform-specific binding affinity. In a preferred embodiment, compounds of the invention bind to a nuclear receptor coactivator binding site with greater affinity than the cellular coactivator proteins. Tissue profiling and appropriate animal models also can be used to select compounds. Different cell types and tissues also can be used for these biological screening assays. Suitable assays for such screening are described herein and in Shibata et al. (Recent Prog. Horm. Res. 52:141-164 (1997)); Tagami et al., (Mol. Cell Biol. (1997) 17(5):2642-2648); Zhu et al. (J. Biol. Chem. (1997) 272(14):9048-9054); Lin et al. (Mol. Cell Biol. (1997) 17(10):6131-6138); Kakizawa et al. (J. Biol. Chem. (1997) 272(38):23799-23804); and Chang et al. (Proc. Natl. Acad. Sci. USA (1997) 94(17):9040-9045), which references are incorporated herein in their entirety by reference. For example, coactivators or binding fragments thereof can be expressed and/or assayed for binding as for GRIP1 (Hong et al., MCB supra; and Hong et al., PNAS supra) and/or SRC-1 (Spencer et al., Nature (1997) 389:194-198; Onate et al., Science (1995) 270:1354-1357), incorporated by reference.

The compounds selected can have agonist and/or antagonistic properties. The compounds also include those that exhibit new properties with varying mixtures of agonist and antagonist activities, depending on the effects of altering coactivator binding in the context of different activities of nuclear receptors, either hormone-dependent or hormone-independent, which are mediated by proteins other than coactivators, and which interact with the receptors at locations other than the coactivator binding site. The compounds also include those, which through their binding to receptor locations that are conformationally sensitive to hormone binding, have allosteric effects on the receptor by stabilizing or destabilizing the hormone-bound conformation of the receptor, or by directly inducing the same, similar, or different conformational changes induced in the receptor by the binding of hormone.

Of particular interest is use of such compounds in a method of modulating nuclear receptor activity in a mammal by administering to a mammal in need thereof a sufficient amount of a compound that fits spatially and preferentially into a coactivator binding site of a nuclear receptor “of interest. By “modulating” is intended increasing or decreasing activity of a nuclear receptor. For example, pre-clinical candidate compounds can be tested in appropriate animal models in order to measure efficacy, absorption, pharmacokinetics and toxicity following standard techniques known in the art. Compounds exhibiting desired properties are then tested in clinical trials for use in treatment of various nuclear receptor-based disorders. These include ER-based disorders, such as postmenopausal symptoms and cancer resulting from loss of estrogen production, and osteoporosis and cardiovascular disease stemming from traditional estrogen replacement therapy. Others include TR-based disorders including cardiovascular disease, metabolic disorders, hyperthyroidism, glaucoma and skin disorders. GR-based disorders include Type II diabetes and inflammatory conditions such as rheumatic diseases.

The invention also provides for cocrystals made from nuclear receptor ligand binding domains with a molecule bound to the coactivator binding site. As exemplified in the Examples, TR LBDs are co-crystallized with a peptide molecule comprising a coactivator NR-box 2 peptide sequence bound to the coactivator binding site, and the hormone/ligand T3.

Crystals are made from purified nuclear receptor LBDs that are usually expressed by a cell culture, such as E. coli. Preferably, different crystals (cocrystals) for the same nuclear receptor are separately made using different coactivators-type molecules, such as protein fragments, fusions or small peptides. The coactivator-type molecules preferably contain NR-box sequences necessary for binding to the coactivator binding site, or derivatives of NR-box sequences. Other molecules can be used in co-crystallization, such as small organics that bind to the coactivator or hormone binding site(s). Heavy atom substitutions can be included in the LBD and/or a co-crystallizing molecule.

After the three dimensional structure of the cocrystal is determined, the structural information can be used in computational methods to design synthetic compounds for the nuclear receptor, and further structure-activity relationships can be determined through routine testing using the assays described herein and known in the art.

Since nuclear receptor LBDs may crystallize in more than one crystal form, the structure coordinates of such receptors or portions thereof, as provided in Appendix 1, are particularly useful for solving the structure of those other crystal forms of nuclear receptors. They may also be used to solve the structure of mutants or co-complexes of nuclear receptors having sufficient structural similarity.

One method that may be employed for this purpose is molecular replacement. In this method, the unknown crystal structure, may be determined using the structure coordinates of this invention as provided in Appendix 1. This method will provide an accurate structural form for the unknown crystal more quickly and efficiently than attempting to determine such information ab initio.

Atomic coordinate information gleaned from the crystals of the invention can be stored. In a preferred embodiment, the information is provided in the form of a machine-readable data storage medium. This medium contains information for constructing and/or manipulating an atomic model of a coactivator binding site or portion thereof. For example, the machine readable data for the coactivator binding site comprises structure coordinates of amino acids corresponding to human TR amino acids selected from C-terminal helix 3 (Ile280, Thr281, Val283, Val284, Ala287, and Lys288), helix 4 (Phe293), helix 5 (Gln301, Ile302, Leu305, Lys306), helix 6 (Cys309), and helix 12 (Pro453, Leu454, Glu457, Val458 and Phe459), or a homologue of the molecule or molecular complex comprising the site. The homologues comprise a coactivator binding site that has a root mean square deviation from the backbone atoms of the amino acids of not more than 1.5 Å. A preferred molecule or complex represents a compound bound to the coactivator binding site.

The machine-readable data storage medium can be used for interactive drug design and molecular replacement studies. For example, a data storage material is encoded with a first set of machine-readable data that can be combined with a second set of machine-readable data. For molecular replacement, the first set of data can comprise a Fourier transform of at least a portion of the structural coordinates of the nuclear receptor or portion thereof of interest, and the second data set comprises an X-ray diffraction pattern of the molecule or molecular complex of interest. Using a machine programmed with instructions for using the first and second data sets a portion or all of the structure coordinates corresponding to the second data can be determined.

Protein for crystals and assays described herein can be produced using expression and purification techniques described herein and known in the art. For example, high level expression of nuclear receptor LBDs can be obtained in suitable expression hosts such as E. coli. Expression of LBDs in E. coli, for example, includes the TR LBD and other nuclear receptors, including members of the steroid/thyroid receptor superfamily, such as the receptors ER, AR, MR, PR, RAR, RXR and VDR. Yeast and other eukaryotic expression systems can be used with nuclear receptors that bind heat shock proteins as these nuclear receptors are generally more difficult to express in bacteria, with the exception of ER, which can be expressed in bacteria. Representative nuclear receptors or their ligand binding domains have been cloned and sequenced: human RAR-α, human RAR-γ, human RXR-α, human RXR-α, human PPAR-α, human PPAR-β, human PPAR-γ, human VDR, human ER (as described in Seielstad et al., Molecular Endocrinol., (1995) 9:647-658, incorporated herein by reference), human GR, human PR, human MR, and human AR. The LBD for each of these receptors has been identified.

Coactivator proteins can be expressed using techniques known in the art, particularly members of the p160 family of coactivator proteins that have been cloned and/or expressed previously, such as SRC-1, AIB1, RAC3, p/CIP, and GRIP1 and its homologues TIF 2 and NcoA-2. A preferred method for expression of coactivator protein is to express a fragment that retains transcriptional activation activity using the “yeast 2-hybrid” method as described by Hong et al. (PNAS supra and MCB supra), for GRIP1 expression, which reference is herein incorporated by reference.

The proteins can be expressed alone, as fragments of the mature or full-length sequence, or as fusions to heterologous sequences. For example, TR can be expressed without any portion of the DBD or amino-terminal domain. Portions of the DBD or amino-terminus can be included if further structural information with amino acids adjacent the LBD is desired. Generally, for the TR the LBD used for crystals will be less than 300 amino acids in length. Preferably, the TR LBD will be at least 150 amino acids in length, more preferably at least 200 amino acids in length, and most preferably at least 250 amino acids in length. For example the LBD used for crystallization can comprise amino acids spanning from Met 122 to Val 410 of the rat TR-α or Glu 202 to Asp 461 of the human TR-β.

Typically the LBDs are purified to homogeneity for crystallization. Purity of LBDs can be measured with sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), mass spectrometry (MS) and hydrophobic high performance liquid chromatography (HPLC). The purified LBD for crystallization should be at least 97.5% pure, preferably at least 99.0% pure, more preferably at least 99.5% pure.

Initially, purification of the unliganded receptor can be obtained by conventional techniques, such as hydrophobic interaction chromatography (HPLC), ion exchange chromatography (HPLC), and heparin affinity chromatography.

To achieve higher purification for improved crystals of nuclear receptors, especially the TR subfamily and TR, the receptors can be ligand-shift-purified using a column that separates the receptor according to charge, such as an ion exchange or hydrophobic interaction column, and then bind the eluted receptor with a ligand, especially an agonist. The ligand induces a change in the receptor's surface charge such that when re-chromatographed on the same column, ligand-bound receptor is separated from unliganded receptor. Usually saturating concentrations of ligand are used in the column and the protein can be preincubated with the ligand prior to passing it over the column. The structural studies detailed herein indicate the general applicability of this technique for obtaining super-pure nuclear receptor LBDs for crystallization.

Purification can also be accomplished by use of a purification handle or “tag,” such as with at least one histidine amino acid engineered to reside on the end of the protein, such as on the N-terminus, and then using a nickel or cobalt chelation column for purification. (Janknecht et al., Proc. Natl. Acad. Sci. USA, (1991) 88:8972-8976) incorporated by reference.

Typically purified LBD, such as TR LBD, is equilibrated at a saturating concentration of ligand at a temperature that preserves the integrity of the protein. Ligand equilibration can be established between 2 and 37° C., although the receptor tends to be more stable in the 2-20° C. range. Preferably crystals are made with the hanging drop methods detailed herein. Regulated temperature control is desirable to improve crystal stability and quality. Temperatures between 4 and 25° C. are generally used and it is often preferable to test crystallization over a range of temperatures. The crystals are then subjected to vapor diffusion and bombarded with x-rays to obtain x-ray diffraction pattern following standard procedures.

For co-crystallization with a peptide that binds to the coactivator binding site, various concentrations of peptides containing a sequence that binds to a coactivator binding site of a nuclear receptor of interest can be used in microcrystallization trials, and the appropriate peptides selected for further crystallization. Any number of techniques, including those assays described herein can assay peptides for binding to the coactivator binding site of a nuclear receptor of interest. In a preferred embodiment, a NR-box 2 sequence-containing peptide is used for crystallization with TR LBD. A preferred peptide contains a NR-box (SEQ ID NO: 1) LxxLL motif, and suitable flanking sequences necessary for binding and forming complex with coactivator binding site of the nuclear receptor of interest, such as a TR LBD. The binding peptides are then tested in crystallization trials at various concentrations and ratios of concentrations with a nuclear receptor of interest, for example, as described herein and in the Examples. For crystallization trials with TR LBD, the hanging drop vapor diffusion method is preferred. Conditions of pH, solvent and solute components and concentrations and temperature can be adjusted, for instance, as described in the Examples. In the handing drop method, to obtain suitable crystals for x-ray diffraction analysis, seeding of prepared drops with microcrystals of the complex can be used. Collection of structural information can be determined by molecular replacement using the structure of TR LBD determined herein or previously by Wagner et al., supra. The structure is refined following standard techniques known in the art.

There are many uses and advantages provided by the present invention. For example, the methods and compositions described herein are useful for identifying peptides, peptidomimetics or small natural or synthetic organic molecules that modulate nuclear receptor activity. The compounds are useful in treating nuclear receptor-based disorders. Methods and compositions of the invention also find use in characterizing structure/function relationships of natural and synthetic coactivator compounds.

The following examples illustrate various aspects of this invention. These examples do not limit the scope of this invention.

EXAMPLES

Example 1

Expression and Purification of Wild-Type and Mutant Nuclear Receptors and Coactivators

A. Human TRβ LBD

Human TRβ LBD (His6-E202-D461) was expressed and purified as described (Shiau et al., Gene (1996) 179(2):205-10). Briefly, the protein was expressed from pET (e.g., pET3 and pET28) in BL21DE3 at 14° C., induced at OD (600 nm) 0.7 with 1 mM IPTG and incubation was extended for 24 hours. Cells were harvested and lysed in 50 mM sodium-phosphate buffer (pH 8.0), 0.3M NaCl, 10% glycerol, 25 mM β-merceptoethanol and 0.1 mM PMSF as described above. The lysate was cleared by ultracentrifugation (Ti45, 36000 rpm, 1 h, 4° C.), loaded on a Talon column equilibrated in the sodium phosphate buffer described above, washed with 12 mM imidazole and eluted with an imidazole gradient (12-300 mM). TRβ LBD containing fractions were loaded in 0.6M ammonium sulfate on a TSK-phenyl hydrophobic interaction column and eluted with a reverse ammonium sulfate gradient [0.6-0 M] in 50% glycerol and 10% acetonitrile. Fractions containing TRβ LBD were tested for hormone binding, pooled and incubated with a 3-fold molar excess of T3 (Sigma). The hydrophobic interaction run was repeated with liganded receptor under the same conditions. Liganded receptor, which elutes earlier than unliganded receptor, was collected and buffer changed to 20 mM Hepes pH7.0, 3 mM DTT and 0.1 μM T3 using NAP columns (Pharmacia). For crystallization, the protein was concentrated by ultrafiltration (Millipore UFV2BGC 10 concentrators) to a final concentration of 9 mg/ml. The yield was about 9.5 mg protein per liter bacterial culture.

B. Human TR Mutants

Thirty-seven thyroid receptor mutants were created by synthesizing double-stranded oligonucleotides which encode the mutant sequence and which have ends allowing them to be ligated as a cassette using pairs of the NsiI, PstI, SstI, AlwNI, Apol, PflMI, BstXI, BseRI, BsmFI, PvuII, NspI, SmaI, PmlI, BglII and BsmI restriction sites of the hTRβ1 cDNA sequence, or the 3′ plasmid polylinker SalI, or BamHI restriction sites. The hTRβ sequences thus mutated were subcloned into the pCMX vector encoding the full-length 461 amino acid hTRβ1 sequence. Some of the mutations of the hTRβ1 in the CMX vector and all three mutations of the hERα in the pSG5-ER-HEGO vector (Tora et al., EMBO (1989) 8:1981) were created using Quick Change Site-Directed Mutagenesis Kits (Stratagene). The mutated sequences were verified by DNA sequencing using Sequenase Kits (Stratagene).

C. Human ERα LBD

The human ERα-LBD 297-554 was overexpressed as described previously (Seielstad, et al., supra) in BL21(DE3)pLysS cells transformed with a modified pET-23d-ERG vector that contained the sequence Met-Asp-Pro fused to residues 297 to 554 of the hERα (provided by Paul Sigler of Yale University). Clarified bacterial lysates were adjusted to 3 M in urea and 0.7 M in NaCl and then applied to a 10-ml column of estradiol-Sepharose (Greene, et al., Proc. Natl. Acad. Sci. USA (1980) 77:5115-5119; Landel, et al., Mol. Endocrinol. (1994) 8:1407-1419; Landel, et al., J. Steroid Biochem. Molec. Biol. (1997) 63:59-73).

To carboxymethylate the solvent-accessible cysteines, the bound hERα-LBD was treated with 5 mM iodoacetic acid in 10 mM Tris, pH 8.1, 250 mM NaSCN (Hegy, et al., Steroids (1996) 61:367-373). Protein was eluted with 3×10-5 M ligand (either DES or OHT) in 30-100 ml of 50 mM Tris, 1 mM EDTA, 1 mM DTT and 250 mM NaSCN, pH 8.5. The yield of hERα-LBD was typically close to 100% (Seielstad, et al., Biochemistry (1995) 34:12605-12615). The affinity-purified material was concentrated and exchanged into 20 mM Tris, 1 mM EDTA, 4 mM DTT, pH 8.1 by ultrafiltration. The protein was bound to a Resource Q column (Pharmacia) and then eluted with a linear gradient of 25-350 mM NaCl in 20 mM Tris, pH 8.1, 1 mM DTT. The hERα-LBD ligand complexes eluted at 150-200 mM NaCl. Pooled fractions were concentrated by ultrafiltration and analyzed by SDS-PAGE, native PAGE, and electrospray ionization mass spectrometry.

D. Human ER Mutants

To test the importance of the NR box peptide/LBD interface observed in the crystal, a series of site-directed mutations were introduced into the ERα LBD. These mutations were designed either to simultaneously perturb the structural integrity and the nonpolar character of the floor of the binding groove (Ile 358->Arg, Val 376->Arg and Leu 539->Arg) or to prevent the formation of the capping interactions (Lys 362->Ala and Glu 542->Lys). Fusions of glutathione-S-transferase (GST) to the wild-type and mutant LBDs were analyzed for their ability to bind 35S-labeled GRIP1 in the absence of ligand or in the presence of DES or OHT.

35S-labeled GRIP1 was incubated with either immobilized GST, immobilized wild type GST-hERα LBD, or immobilized mutant GST-LBDs in the absence of ligand or in the presence of DES or OHT. The bound GRIP1 was quantitated after SDS-PAGE. I358R, mutant LBD containing a Ile->Arg substitution at residue 358; K362A, mutant LBD containing a Lys->Ala substitution at residue 362; V376R, mutant LBD containing a Val->Arg substitution at residue 376; L539R, mutant LBD containing a Leu->Arg substitution at residue 539; E542K, mutant LBD containing a Glu->Lys substitution at residue 542.

In the absence of ligand or in the presence of OHT, fusions to the wild-type protein and all of the mutant LBDs showed no detectable binding to GRIP1. The Ile 358->Arg, Val 376->Arg and Leu 539->Arg mutants were all unable to interact with coactivator in the presence of agonist, confirming the importance of the packing interactions observed in the crystal. Disruption of either the N- or C-terminal capping interaction also compromised GRIP1 binding in the presence of agonist. Only the wild-type GST-LBD was able to recognize the coactivator in the presence of DES.

E. Human ER LBD-GST Fusion Protein

A fusion between glutathione-S-transferase (GST) and amino acids 282-595 of hERα was constructed by subcloning the EcoRI fragment from pSG5 ERα-LBD (Lopez et al., submitted manuscript) into pGEX-3× (Pharmacia). The Ile 358->Arg, Lys 362->Ala, and Leu 539->Arg mutations were introduced into the GST-LBD construct using the QuikChange Kit (Stratagene) according to the manufacturer's instructions. The Val 376->Arg and Glu 542->Lys mutations were created in the GST-LBD construct by subcloning the BsmI/HindIII fragments of derivatives of pSG5-ER-HEGO (Tora, et al., supra) into which these mutations had already been introduced. All constructs were verified by automated sequencing (University of Chicago Cancer Research Center DNA Sequencing Facility).

F. Radiolabeled Full-Length Receptors and Coactivator Proteins

Wild-type (WT) or mutant pCMV-hTRβ1 vector and the pSG5-GRIP1 and pCMX-SRC-1a vectors were used to produce radiolabeled full-length receptors and coactivator proteins using the TNT coupled Reticulocyte Lysate System (Promega) and [35S]-Met (DuPont). GST-GRIP1 (amino acids 721-1221), GST-GRIP1 (amino acids 563-1121), GST-SRC-1a (amino acids 381-882), GSThTRβ1 (full-length, WT or mutants, WT provided by C. Costa), and the GST-hRXRα (full-length provided by. C. Costa), fusion proteins were produced in E. coli strain HB101 as per the manufacturer's protocol (Pharmacia Biotech).

G. Coactivator GRIP1 563-767 His6 GST Fusion Protein

GRIP1 563-767 was cloned as a Bam HI-Xho I fragment derived from pGEX-2TK GRIP1 563-1121 into the corresponding sites of pGEX-4T1. A His6-tag was added by inserting a Xho I-Nae I fragment of pET23a into Xho I-Bsa AI sites of this pGEX-4T1 construct yielding pGEX GRIP1 563-767His6. Mutants of GRIP1 563-767 were generated by PCR or single stranded mutagenesis using oligonucleotides carrying the mutations and a pSG5 GRIP1 vector as template. The mutations were confirmed by sequence analysis and integrated into pGEX GRIP1 563-767His6 as NgoMI-Xho I fragments. The GRIP1 563-767 His6 GST fusion protein was expressed in HB101 at 37° C. Protein expression was induced with 1 mM IPTG at an optical density (600 nm) of 0.7 and extended for 4 hours after induction. Cells were harvested by centrifugation, resuspended in sonication buffer (20 mM Tris HCl pH 8.0, 0.1 M NaCl, 110% glycerol, 0.1 mM PMSF and protease inhibitors (Complete, EDTA free, Boehringer Mannheim)). The resuspended cells were freeze-thawed once, incubated on ice with 0.1 mg/ml lysozyme for 20 minutes and lysed per sonication. The lysate was cleared by ultracentrifugation (Ti 45, 36000 rpm, 1 h 4° C.), the supernatant filtered (Costar 0.2 μm top filter) and loaded on a Talon column (Clontech). The column was washed with 10 column volumes of sonication buffer supplemented with 12 mM imidazole and eluted with an imidazole gradient [12-100 mM]. At this step the fusion proteins are about 95% pure. Imidazole was removed by gelfiltration on NAP columns (Pharmacia), and protein concentrations determined using the Biorad protein assay. Equal concentrations of the different derivatives of the fusion fragment were incubated with glutathione agarose (1 h, 4° C.) which was equilibrated in binding buffer (sonication buffer supplemented with 1 mM DTT, 1 mM EDTA and 0.01% NP-40). Beads were washed with at least 20 volumes of this buffer, diluted in binding buffer with 20% glycerol to 40%, frozen in aliqots and stored at −70° C.

H. Coactivator GRIP1 563-767 His6

GRIP1 563-767 was cloned as a Bam HI-Xho I fragment derived fron pGEX GRIP1 563-767His6 into corresponding cloning sites of pET23a yielding pETGRIP1 563-767His6. The fragment was expressed in BL21DE3. Expression, cell lysis and Talon purification was identical as described for GST GRIP1 563-767His6. The protein eluted from a Talon column in two fractions, one at 12 mM and one between 40 and 70 mM imidazole. In the earlier eluting fraction the fragment was associated with a 70 kDa protein which was removed by a MonoQ run in 50 mM Tris HCl pH7.5, 10% glycerol, 1 mM EDTA, 1 mM DTT, 0.1 mM PMSF and protease inhibitors. GRIP1 563-767His6 eluted in the flow through and was concentrated by ultrafiltration. At this step the protein was more than 95% pure.

Example 2

Peptide Synthesis

Coactivator peptides were obtained using standard techniques. All peptides were HPLC purified and analyzed by mass spectroscopy. Peptide concentrations were either determined spectroscopically using the tyrosine signal (A276=1450 M−1 cm−1) or by amino acid analysis following standard techniques.

Example 3

Binding Assays with Nuclear Receptors and Coactivators

A. GST-GRIP Pull-Down Assays and Peptide Competition Assays

Binding experiments were performed by mixing glutathione beads containing 10 μg of GST fusion proteins (Coomassie Plus Protein Assay Reagent, Pierce) with 1-2 μl of the [35S]-labeled wild-type or mutant hTRβ1 (25 fmoles, 4000 cpm of receptor), or coactivators in 150 μl of binding buffer (20 mM HEPES, 150 mM KCl, 25 mM MgCl2, 10% glycerol, 1 mM dithiothreitol, 0.2 mM phenylmethylsulfonyl fluoride, and protease inhibitors) containing 2 mg/ml BSA for 1.5 hrs in the presence or absence of 1 μM T3. Beads were washed 3 times with 1 ml of binding buffer and the bound proteins were separated using 10% SDS-PAGE and visualized by autoradiography. Binding was quantitated by phosphorimaging using ImageQuant (Molecular Dynamics).

For in vitro binding studies GR, TR and their derivatives were translated in the presence of [35S]methionine using the TNT Coupled Reticulocyte System (Promega). Separate translations were performed in the presence and absence of 10 μM dexamethasone or 1 μM RU486 for GR and 10 μM triiodothyronine for TR. Expression was quantified by phosphoimager analysis (BAS2000, Fuji). For all binding assays 50 μl of a 20% bead suspension containing either 1.6 or 4.0 μM bound purified GST GRIP1 fragment (either 568-767 or 563-1121) was incubated with 0.2 μl or 1.4 μl in vitro transcribed and translated TR or GR, respectively. Binding was performed in the binding buffer described above supplemented with 20 μg/ml BSA and appropriate hormone. The chosen GST GRIP1 fragment concentrations were sufficient to bind either 70 or 100% of the TR derivatives. The reaction was incubated at 4° C. under rotation for 2 hours. In case of competition experiments, the appropriate concentration of peptides were added to the reaction before addition of receptors. However, no differences in the results were noted by adding the peptides after half of the incubation of the GST GRIP1 fragment with nuclear receptors. This demonstrates that equilibrium is reached under the chosen conditions. Beads were washed five times with 200 μl binding buffer+BSA at 4° C. before elution of the bound proteins in 20 μl SDS loading buffer. Eluted beads and input labeled protein were subjected to SDS-PAGE. The fraction of bound nuclear receptors was determined by phosphoimager analysis.

B. GST-hTRβ1 Pull-Down Assays

Assay and analysis was performed as for Example 3A. In vitro binding of [35S]-labeled full-length GRIP1, [35S]-labeled full-length SRC-1a, and [35S]-labeled full-length hRXRα, to GSThTRβ1 wild-type (WT) and mutants was performed. Mutants V284R, K288A, I302R, L454R, and E457K all bound to hRXRα with an affinity equivalent to wild type hTR. All of these mutants showed decreased ability to bind GRIP1 and SRC-1a, as expected from the results of Example 3A. The same results were obtained when a GST-SRC1 construct including SRC-1a amino acids 381-882 was tested for binding of [35S]-Met-labeled full-length hTRβ1 WT and mutants (data not shown).

C. GST-hERα LBD Pull-Down Assays

The wild-type and mutant GST-hERα LBDs were expressed in BL21(DE3) cells. Total ligand binding activity was determined by a controlled pore glass bead assay (Greene, et al., Mol. Endocrinol. (1988) 2:714-726) and protein levels were monitored by western blotting with a monoclonal antibody to hERα (H222). Cleared extracts containing the GST-hERα LBDs were incubated in buffer alone (50 mM Tris, pH 7.4, 150 mM NaCl, 2 mM EDTA, 1 mM DTT, 0.5% NP-40 and a protease inhibitor cocktail) or with 1 μM of either DES or OHT for 1 hour at 4° C. Extract samples containing thirty pmol of GST-LBD were then incubated with 10 μl glutathioneSepharose-4B beads (Pharmacia) for 1 hour at 4° C. Beads were washed five times with 20 mM HEPES, pH 7.4, 400 mM NaCl, and 0.05% NP-40. 35S-labeled GRIP1 was synthesized by in vitro transcription and translation using the TNT Coupled Reticulocyte Lysate System (Promega) according to the manufacturer's instructions and pSG5-GRIP1 as the template. Immobilized GSThERα LBDs were incubated for 2.5 hours with 2.5 μl aliquots of crude translation reaction mixture diluted in 300 μl of Tris-buffered saline (TBS). After five washes in TBS containing 0.05% NP-40, proteins were eluted by boiling the beads for 10 minutes in sample buffer. Bound 35S-GRIP1 was quantitated by fluorography following SDS-PAGE.

D. Electrophoretic Mobility Shift Assays

GRIP1, a mouse p160 coactivator, recognizes the ERα LBD in a ligand-dependent manner. The binding of agonists to the Erα LBD promotes recruitment of GRIP1, whereas binding of antagonists prevents this interaction (Norris, et al., J. Biol. Chem. (1998) 273:6679-88). While agonist-bound receptor will bind to all three of the NR boxes from GRIP1, ERα strongly prefers NR-box 2 (Ding, et al., Mol. Endocrinol. (1998) 12:302-13).

An electrophoretic mobility shift assay was used to directly assess the ability of the NR-box 2 peptide to bind the purified ERα LBD in the presence of either DES or OHT. Eight microgram samples of purified hERα-LBD bound to either DES or OHT were incubated in the absence of the peptide, i.e., buffer alone, or in the presence of either a 2-fold or 10-fold molar excess of the GRIP1 NR-box 2 peptide. The binding reactions were performed on ice for 45 minutes in 10 μl of buffer containing 20 mM Tris, pH 8.1, 1 mM DTT, and 200 mM NaCl and then subjected to 6% native PAGE. Gels were stained with GELCODE Blue Stain reagent (Pierce).

In the presence of the NR-box 2 peptide, the migration of the DES-hERα-LBD complex was retarded. In contrast, peptide addition had no effect on the mobility of the OHT-hERα-LBD complex. Hence, this peptide fragment of GRIP1 possesses the ligand-dependent receptor binding activity characteristic of the full-length protein.

Example: 4

Transfection Assays with TR and hERα

HeLa cell transfection and assay conditions are described (Webb et al., Mol. Endocrinol. (1995) 9:443). For TR assays, 5 μg of the reporter p(DR-4)2-TK-LUC consisting of two copies of the DR-4 element (a direct repeat of the consensus TR response element (TRE) spaced by 4 base pairs) placed upstream of a minimal (−32/+45) thymidine kinase gene promoter linked to luciferase (LUC) coding sequences were used. A reporter containing palindromic TREs gave the same results (data not shown). Also, 2 μg of the hTRβ1 expression vector, pCMX-TR (WT or mutant), and 0.5 μg transfection control vector, pJ3LacZ, which contains the SV40 promoter linked to the β-galactosidase gene, were used. Other cells co-transfected with vector or receptor constructs can be used for same purpose. Alternative cells expressing sufficient levels of an endogenous receptor(s), or cells selected that express a single reporter, can be used for transfection assays, including MCF-7 cells expressing ER (Webb et al., supra), and GC cells expressing TR (Norman et al., J. Biol. Chem. (1989) 264:12063-12073).

For hERα assays, 5 μg of estrogen responsive reporter plasmid encoding chloramphenicol acetyltransferase (CAT), pERE-collTATA (Sadovsky, et al., Mol Cell Biol. (1995) 15:1554), 0.5 μg expression vector encoding full-length hERα, pSG5-er HEGO (WT or mutants), and 2 μg of pj3lacz, were used. For the experiments of FIGS. 2 and 4, 0.5 μg of a full-length GRIP1 expression vector, pSG5-GRIP1, was also included in the transfection. Transfected cells were treated with or without 1 μM T3 or E2, as indicated. After culturing for 24 hrs, the LUC or CAT activities were assayed and the β-galactosidase activities were also assayed to correct for differences in transfection efficiencies. The triplicate points were averaged and standard deviations were less than 10%.

Example 5

Hormone Binding Assays for Wild-Type and Mutant TRs

The T3 binding affinity constants (Kd) for in vitro-translated WT and mutant TRs were measured using [125I] 3,5,3′ triiodo-L-thyronine ([125I]T3) in gel filtration binding assays as described (Apriletti et al., Protein Expr. Purif. (1995) 6:363). Both the Kd and standard error (S.E.) values were calculated using the Prism computer program (GraphPad Software, Inc.). Mutations are indicated by the single-letter amino acid abbreviations, with the native residue name, followed by the primary sequence position number, and then the mutated residue name. The affinity of the WT TR is 81±12 pM. The relative affinity was determined by dividing the WT Kd by each mutant Kd. The 37 mutants tested with their relative affinities are: E217R (123%), E227R (109%), K242E (92%), E267R (117%), H271R (123%), T277R (7%), T281R (145%), V284R (105%), D285A (89%), K288A (98%), C294K (94%), E295R (118%), C298A (87%), C298R (141%), E299A (171%), I302A (86%), I302R (99%), K306A (6%), K306E (6%), P384R (164%), A387R (107%), E390R (151%), E393R (146%), L400R (95%), H413R (109%), H416R (153%), M423R (156%), R429A (48%), S437R (170%), L440R (174%), V444R (89%), T448R (234%), E449R (36%), P453E (32%), L454R (26%), L456R (46%), E457K (71%).

Example 6

Coactivator Binding Assays for Wild-Type and Mutant Trs

Wild type (WT) TR and most of the TR mutants liganded to 3,5,3′-triiodo-L-thyronine (T3) bind equally well to the coactivator, GRIP1. In all cases, GRIP1 binding was hormone-dependent (data not shown). Mutations L454R and E457K in surface residues of helix 12 abolish GRIP1 binding (FIG. 1). Mutations in two residues of helix 3, V284R and K288A, and two residues of helix 5, I302R and K306A, also impair binding (FIG. 1). Five mutations with diminished GRIP1 binding (V284R, K288A, I302R, L454R, and E457K) also show decreased binding to another coactivator, SRC-1a (data not shown). Thus, these results show that two different coactivators recognize the same TR surface residues.

Example 7

TR Residues Involved in Ligand-Dependent Transcription Activation in Context of a Cell

Residues involved in ligand-mediated transcription activation were identified by testing the TR mutants of Example 8 in HeLa cells. T3 increased reporter gene activity 5-fold in cells expressing either WT TR or mutated TRs showing normal GRIP1 binding (representative mutants are shown in FIG. 1. By contrast, TR mutants with diminished or absent GRIP1 binding (V284R, K288A, I302R, K306A, L454R, and E457K) show a diminished or absent response to T3 which correlates with the GRIP1 binding defect. Overexpression of GRIP1 increases activation by the WT TR and rescues activation by TR mutants roughly in proportion to the severity of the defect of GRIP1 binding and activation (FIG. 2). These results suggest that the same residues are required for coactivator binding, function of the endogenous coactivator(s) in HeLa cells, and responsiveness of TRs to GRIP1.

Example 8

Effect of TR Mutations on Other Receptor Functions

The effects of the mutations on other receptor functions also were examined. All of the mutants bound radiolabeled thyroid hormone (Kd values, 6%-234% that for native receptor); occasional lower values were expected because some residues have partially buried side chains. None of the residues that decrease GRIP1 binding affected TR binding to a GST-RXR fusion protein or to DNA using three different DNA half-site arrangements and testing with or without added RXR (data not shown). Some mutations that affect GRIP1 binding occur in a region spanning helices 3-5, which has been suggested as important for TR/RXR heterodimerization (O'Donnell et al., supra; Lee et al., Mol. Endocrinol. (1992) 6:1867-1873). In contrast, however, the above results indicate that these residues do not contribute to TR/RXR heterodimerization. Further, TRs mutated in the CBS residues retain the ability of WT TR of T3-dependent inhibition of the activity of the Jun and Fos transcription factors at an AP-1 site (Saatcioglu et al., supra), suggesting that the CBS residues do not participate in TR actions mediated through these proteins. These data indicate that the mutational effects are specific, the amount of input labeled TR in the different reactions is comparable, and the levels of expression of the mutant TRs are comparable to those of WT receptors.

Example 9

Coactivator Binding Site in ER

Three separate mutations (K362A, V376R, and E542K) were created in human estrogen receptor-α (hERα) which align to three of the effective positions in hTRβ1 (K288A, I302R, and E457K). All three mutations diminish GRIP1 binding and abolish transcriptional activation (FIG. 3), and mutant V376R, with 10% residual GRIP1 binding, was rescued partially by overexpression of GRIP1 (FIG. 4). As a control, the ER mutants demonstrated a normal hormone-dependent ability to activate a vitellogenin-LUC hybrid reporter gene, GL45, which responds to the ER amino-terminal activation function (Berry et al., EMBO J. (1990) 9:2811-2818) (data not shown). The finding that similar residues are required for GRIP1 binding and transcription activation activity in the TR and ER suggests that the coactivator binding site residues are similar in different nuclear receptors.

Example 10

Coactivator NR-Box Binding Affinity for TR

To study the interaction between nuclear receptors and GRIP1 in vitro, a fragment of GRIP1 (563-767) was purified that contains all three NR-boxes (FIGS. 6 and 7). The fragment was found to be highly soluble and, in agreement with a secondary structure prediction using PhD, displays a mainly alpha-helical far UV-CD spectrum (data not shown). Three of the four helices predicted for the fragment include the NR-boxes at their C-terminus, suggesting that these boxes are part of amphipathic alpha-helices. These results show that the NR-boxes of GRIP1 are contained in a soluble, alpha-helical 24 kD fragment.

Binding assays show that GRIP1 NR-boxes 1, 2 and 3, interact differentially with hTRβ LBD (FIG. 7). A GST-fusion of the GRIP1 (563-767) fragment strongly binds TR (kD or EC50) in a ligand depend fashion. Replacement of the hydrophobic residues of NR-box 3 with alanine does not reduce binding of TR significantly, whereas similar replacement of NR-box 2 results in loss of TR binding of about 50%. By titrating the amount of GRIP1 fragment, about a 4-fold stronger binding of TR for NR-box 2 (EC50=1.0 μM) over NR-box 3 (EC50=4.0 μM) was estimated. In the absence of functional NR-boxes 2 and 3, almost no binding to TR was detected suggesting that under these experimental conditions NR-box 1 is not a cognate binding site for TR. Full length TR or TR-LBD bound GRIP1 equally. These results show that TR recognizes GRIP1 NR-box 2 and 3, with preference for NR-box 2.

Example 11

Coactivator NR-Box Binding Affinity for GR

GR also was found to bind GRIP1 (563-767) in a ligand-dependent manner (FIG. 8). However, in contrast to TR, extension of GRIP1 (563-767) to residue 1121 increases binding to GR about 3-fold suggesting an additional binding site on GRIP1 for GR. Binding of the larger fragment remains ligand-dependent; no interaction can be observed in the presence of the GR partial antagonist RU486. These results are in agreement with in vivo 2-hybrid GR GRIP1 interaction studies. In the presence of ligand no difference was detected in the binding of GRIP1 by full length GR or a deletion mutant of GR that lacks the N-terminal activation domain AF-1. However in the absence of ligand, binding of GR to GRIP1 (563-1121) increased by about 10-fold indicating that sequences in the GR. N-terminus are able to suppress binding of unliganded GR to this additional binding site in GRIP1. Additionally, GR did not bind to a GRIP1 (563-767) mutant in which both NR-box 2 and 3 are replaced by alanines, and binds most strongly to a fragment that lacks a functional NR-box 2. As with TR, GR does not recognize NR-box 1. In contrast to TR, the GR prefers NR-box 3 to NR-box 2. These results demonstrate that GR prefers binding to NR-box 3 and interacts with an additional GRIP1 site within the CREB (cAMP-response-element binding protein)-binding protein (CBP) binding site.

Example 12

Coactivator Peptide Binding Affinity for TR

To investigate whether the preference of TR for NR-box 2 is dependent on the sequence or structural context of the NR-boxes, competition studies on the interaction of GRIP1 with hTRβ LBD were performed using coactivator peptides containing different NR-boxes (NR-box 2 peptide (residues 11-23 of SEQ ID NO: 6) EKHKILHRLLQDS, and NR-box 3 peptide (residues 9-21 of SEQ ID NO: 7) ENALLRYLLDKDD) (FIG. 9). Consistent with the interaction of hTRβ LBDP with GRIP1 (563-767) NR-box mutants, a peptide containing NR-box 1 competes the interaction of GRIP1 with hTRβ LBD only at very high concentrations (EC50=130 μM). Peptides containing either NR-box 2 or 3 compete GRIP1 (563-767) efficiently and display the preference of hTRβ LBD for NR-box 2 (EC50 (NR-box 2)=1.5 μM, EC50 (NR-box 3)=4 μM). The apparent affinities (EC50) for peptides of NR-box 2 and 3 are comparable with the analogous GRIP1 (563-767) NR-box mutants suggesting that the preference of it for NR-boxes is solely dependent on the sequence and independent of the structural context of the NR-boxes.

Peptides of NR-box 2 or 3 compete with GRIP1 (563-767) containing functional NR-boxes 2 and 3 or a mutant of this fragment that contains only a functional NR-box 2 with comparable affinity. Thus, while TR can bind both NR-box 2 and 3, in a GRIP1 coactivator peptide fragment containing both boxes, TR preferentially binds NR-box 2.

These results show the preference of TR for NR-box 2 is sequence dependent.

The same types of assays for TR competition are performed to assess coactivator peptide binding affinity for GR The peptide concentrations are normalized relative to TR for obtaining comparable dose response curves.

Example 13

Binding Affinity of TR for Extended Coactivator Peptides

Sequence identity between all three central NR-boxes of the p160 coactivator family is limited to the conserved leucine residues of the (SEQ ID NO: 1) LxxLL motif (FIG. 6). However, the sequence conservation of a particular NR-box can extend into neighboring residues. To investigate the contribution of these neighboring residues to affinity and specificity of the different NR-boxes for TR, the ability of peptides containing individual NR-boxes with different lengths of adjacent sequences to compete with the interaction of GRIP1 (563-767) with hTRβ LBD were compared (FIGS. 10a, 10b, and 10c).

A peptide (FIG. 10b) consisting of the minimal motif of NR-box 3 (residues 12-17 of SEQ ID NO: 7; LLRYLL) does not compete with the TR LBD interaction with GRIP1 (563-767). A peptide consisting of the NR-box 2 (residues 15-20 of SEQ ID NO: 6; ILHRLL) also does not sufficiently compete the interaction (data not shown). Extending peptides containing a (SEQ ID NO: 1) LxxLL motif to include adjacent residues increased affinity for both NR-box motifs and magnified the preference of TR for NR-box 2 (NR-box 2 peptides in FIG. 10a: (residues 11-23 SEQ ID NO: 6) EKHKILHRLLQDS and (residues 7-23 of SEQ ID NO: 6) TSLKEKHKILHRLLQDS; and NR-box 3 peptides in FIG. 10b (residues 8-24 of SEQ ID NO: 7) KENALLRYLLDKDDTKD and (residues 5-24 of SEQ ID NO: 7) PKKKENALLRYLLDKDDTKD). A chimeric peptide containing the NR-box 3 motif in the context of the NR-box 2 flanking sequences (SEQ ID NO: 29; TSLKEKHKLLRYLLQDSS) binds like a NR-box 2 peptide (FIG. 10c).

These results demonstrates that preference of TR for NR-box 2 is at least partially due to features of the bound peptide (residues 15-20 of SEQ ID NO: 6; ILHRLL), but that their affinity and specificity is modulated by adjacent sequences.

Example 14

Binding Affinity of TR and GR for Mutant Coactivator

A. TR affinity for ILxxLL Motif Residues

To investigate the role of the hydrophobic residues in NR-box 2, individual residues of the (residues 15-20 of SEQ ID NO: 6) ILHRLL motif were replaced by alanine in the background of GRIP1 (563-767) containing a non-functional NR-box 3 (FIG. 11a). Surprisingly, replacement of any of the conserved leucines prevents binding to TR almost completely. Only replacement of the nonconserved isoleucine exhibited a lessened but still severe impact on the affinity of NR-box 2 for TR. As replacement of a single leucine by alanine is sufficient to overcome the interaction of both the remaining hydrophobic residues and adjacent sequences with hTRβ LBD, it appears that their contribution to the affinity of NR-box 2 for hTRβ LBD is cooperative rather than additive.

Similar results were obtained by competing the interaction of hTRβ LBD with the GRIP1 (563-767) NR-box 3 mutant using peptides in which either IL, HR or LL of the NR-box 2 motif are replaced by alanines (FIG. 11b). Whereas the peptides containing the IL or LL replacement failed to interact with the hTRβ LBD even at very high concentrations, in agreement with a proposed alpha-helical structure of the motif, replacement of the “HR spacer” by alanines showed a marginal effect on the affinity of the peptide for TR-LBD.

Replacement of single leucine residues of NR-box 2 by phenylalanine reduced the affinity of NR-box 2 peptides for TR LBD about 100-fold, replacement of the isoleucine about 10-fold (FIG. 11c). Therefore, the interaction of TR with GRIP1 relies not simply on the hydrophobicity of the (SEQ ID NO: 1) LxxLL motif, but also on positive contributions by the leucine residues themselves.

These results demonstrate that single mutations of the conserved leucines in the (SEQ ID NO: 1) LxxLL motif strongly reduce affinity of GRIP1 for hTRβ LBD.

Collectively, the above examples demonstrate that peptides containing NR-boxes, particularly NR-box 2, reproduce the affinity and specificity of the interaction of GRIP1 (563-767) with hTRβ LBD.

B. TR Affinity of FxxLW and FxxAL Motif Residues

The three conserved leucines of the NR-box 2 (SEQ ID NO: 2) ILxxLL motif are embedded in the hydrophobic cleft of the hTRβ LBD:NR-box 2 interaction surface, whereas the non conserved isoleucine is located on the rim of this cleft where structural changes can be more easily accommodated (See Example 18). In agreement with this structure, replacement of this residue by alanine or phenylalanine reduced binding to hTRβ LBD to a less extent than the comparable mutations of the conserved leucine residues. The surface generated by the three conserved leucines (L690, L693, L694) of the NR-box 2 peptide (residues 12-24 of SEQ ID NO: 6) 686-KHKILHRLLQDSS-698 is highly complementary to the corresponding binding site in the hTRβ LBD (FIGS. 16 and 17). Comparison of this binding site to other nuclear receptors shows that it contains a structural motif that is unique, highly conserved and present in all known structures of nuclear receptor LBDs (Wurtz et al., Nat Struct Biol. (1996) 3:87-94; Wagner et al., supra; Renaud et al., Nature (1995) 378:681-689; Bourguet et al., Nature (1995) 375:377-382; and Brzozowski et al., Nature (1997) 389:753-758).

Interaction of highly conserved hydrophobic motifs, which are part of amphipathic alphahelices, with complementary hydrophobic surfaces resembles a feature observed for the interaction of several other transcriptional activators with their target proteins (p53:MDM2, VP16:TAFII31 or CREB:KIX-CBP). However, the motifs of p53 (FxxLW), VP16 (FxxAL) and CREB (YxxIL) differ from the (SEQ ID NO: 1) LxxLL motif of nuclear receptor coactivators. A Fxxxh motif may be generally involved in interaction with TAFII31, where “h” represents any hydrophobic residue. Though with respect to the known structures, complementarity of the interacting hydrophobic surfaces identified here seem to be a common feature of these interactions, cross-reactions between different motifs are possible. For instance, VP16, p53, and p65 (FxxFL) are able to functionally interact with TAFII31, or p53 and E2F1-DP1 (FxxLL) both interact with MDM2. These interactions are sensitive to mutations in the Fxxxh motif. Therefore it appears that either complementarity of the hydrophobic surfaces is not an absolute requirement or that induced fitting of the interacting surfaces is possible.

Based on these observations, studies were performed to determine whether GRIP1 interacts with TAFII31 or MDM2. However, no interaction was detected. GRIP1 mutants changing NR-box 2 (SEQ ID NO: 1; LxxLL) to VP16 (SEQ ID NO: 4; FxxAL) or p53 (SEQ ID NO: 3; FxxLW) like binding sites also failed to bind TAFII31 or MDM2 demonstrating that the presence of the correct binding site is not sufficient to create binding (data not shown). Moreover, peptides containing the VP16 or p53 binding sites are not able to compete the interaction of GRIP1 with TR, even in very high concentration, but do compete the interaction with GR (data not shown). The affinity of this interaction is weak, but comparable to affinity of a peptide of NR-box 2 that, in the context of a GRIP1 mutant lacking NR-box 3, binds GR in vivo (Ding et al., supra). This binding is only about ten times less than a peptide containing NR-box 3, GR's primary binding site.

As shown above, GR binds GRIP1 (563-767) with about one-fifth the affinity than a comparable amount of TR. Thus, the high concentration of NR-box 3 peptide required to compete the interaction of GR with GRIP1 (563-767) may rather reflect a weak affinity of GR for the peptide rather than a particular strong interaction of GR with GRIP1 (563-767).

These results suggest that at least on the peptide level, other hydrophobic motifs besides (SEQ ID NO: 1) LxxLL can interact with the coactivator binding site, but that it is receptor dependent.

C. TR Affinity for Residues Adjacent to ILxxLL Motif

Peptides containing a FxxLL motif bind TR but with two orders of magnitude lower affinity than a (SEQ ID NO: 1) LxxLL motif (FIG. 11). To test whether the additional changes in the hydrophobic motif or adjacent sequences of the VP16 peptide prevent its binding to TR, a chimeric peptide containing the NR box-2 motif (SEQ ID NO: 1) LxxLL in the context of the VP16 sequence was constructed. This peptide binds to TR but with an about 100-fold lower affinity than the original NR-box 2 peptide. Thus, the inability to bind the VP16 peptide appears to be due to the combination of an imperfect hydrophobic motif and the incompatibility of TR to adjacent sequences of the VP16 motif

As the interaction of the chimeric peptide with GR was comparable to the original NR-box 2 and VP16 peptides, this incompatibility appears due to TR-specific features in the NR-box interaction surface. These results show sequences adjacent the NR-box motif LxxLL can reduce binding of NR-box 2 to TR, but not GR.

Example 15

Crystallization and Structure Determination of NR LBD Complexes

A. Crystallization of hTRβ LBD with T3 and GRIP1 NR-Box 2 Peptide

Several peptides containing GRIP1 NR-box 2 were tested in crystallization trials with the hTRβ LBD. The complex of the hTRβ LBD with the GRIP1 NR-box 2 peptide 686-KHKILHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6) produced crystals that were dependent on both the presence and the concentration of the peptide. Without the peptide, the hTRβ LBD precipitated immediately. However, nucleation was erratic, but could be overcome through seeding of prepared drops with microcrystals of the hTRβ LBD:GRIP1 NR-box 2 peptide complex. Structure of the hTRβ LBD:GRIP1 NR-box 2 peptide complex was determined by molecular replacement using the structure of the hTRβ LBD determined previously (Wagner et al., supra) and refined to a resolution of 3.6 Å (Table 1). The refined model consists of residues K211-P254 and V264-D461 of monomer 1 of the hTRβ LBD, residues K211-P254 and G261-D461 of monomer 2 of the hTRβ LBD, and the GRIP1 NR-box 2 peptides (residues 14-24 of SEQ ID NO: 6) 688-KILHRLLQDSS-698, and (residues 14-22 of SEQ ID NO: 6) 688-KILHRLLQD-696 (Appendix 1). The structure in Appendix 1 consists of: a portion of each of two molecules of hTRβ, chain A (SEQ ID NO: 52) and chain B (SEQ ID NO: 53); two molecules of T3, chain J and chain K; and two molecules of GRIP-1 peptide, chain X (SEQ ID NO: 54) and chain Y (SEQ ID NO: 55).

Briefly, the complex between the hTRβ LBD and the GRIP1 NR-box 2 peptide 686-KHKJLHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6) was prepared by mixing (equal) volumes of a solution of 9 mg/ml hTRβ LBD in 20 mM HEPES pH 7.4 with a solution of 14 mM GRIP1 in 0.4 mM ammonium acetate pH 4.72, and incubating the mixture on ice for 1 hour. Crystals were obtained after 2 days at 4° C. using hanging drop vapor diffusion from a drop containing 1.51 μl of hTRβ LBD:GRIP1 complex, prepared as described, and 0.5 μl 15% PEG 4K, 0.2M sodium citrate pH 4.9, suspended above a reservoir containing 10% PEG 4K, 0.1M ammonium acetate, and 0.05 M sodium citrate (pH 5.6). After allowing the drop to equilibrate for 1 hour, 0.211 of 10-3 to 10-5 dilutions of microcrystals in reservoir buffer were introduced to provide nucleation. Crystals are of space group P3121 (a=95.2, b=95.2, c=137.6) and contain two molecules of the hTRβ LBD and two molecules of the GRIP1 NR-box 2 peptide 686-KHKILHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6).

TABLE 1
Data collection, phasing, and refinement statistics
Data collection
ResolutionReflections
Data set(Å)measureduniqueCoverage(%)Rsym
Native3.635565849096.30.007
Rotation Search
Correlation coefficient
Euler angles (°)Highest
Search modelΘ1Θ2Θ3Highest peakfalse peak
hTR β LBDM160.1280.68241.9016.3
M29.9387.70180.615.914.2
Translation search
Fractional coordinatesTranslation function
xyzHighest peak (o)Highest false peak (o)
M10.5220.4280.25019.5210.02
M20.2000.9320.11926.115.77
Refinement
Resolution
(Å)ReflectionRRfree
F > 2(25-3.776140.29900.3219
All data25-3.778510.30100.317

Rsym = Σh Σi|Ih,i û (Ih(|/ΣIh for the intensity (I) of i observations of reflection h.

Correlation coefficient = Σh Eo2 Ec2 − Eo2 Ec2/[Σh (Eo2 − Eo2)2 Σh (Ec2 − Ec2)2

Translation function (ta, tb, . . . ) = Σh (|Eo(h)|2 − Σh<|Eo(h)2>)(Ec(h,ta,tb,...)|2 − <|Ec(h)2)

where Eo represents the normalized observed structure factor amplitudes, and Ec represents the normalized structure factors for the search model in a triclinic unit cell with dimensions identical to that of the crystal. The reported peak height represents the value of the function for the translation (ta, tb) of the NCS monomers, divided by the rms value of the translation function density.

R factor = Σ|Fobs − Fcalc|/Σ|Fobs|

Rfree is calculated the same as R factor, except only for 10% of the reflections that were set aside for cross validation and not used in refinement.

B. Crystallization of hERα LBD with DES and GRIP1 NR-Box 2 Peptide

Crystals of a DES-hERα LBD-GRIP1 NR-box 2 peptide complex were obtained by hanging drop vapor diffusion. Prior to crystallization, the DES-hERα LBD (residues 297-554) complex was incubated with a 2-4 fold molar excess of the GRIP1 NR-box 2 peptide 686-KHKILHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6) for 7-16 hr. Two μL samples of this solution were mixed with equal volume samples of reservoir buffer consisting of 25-27% (w/v) PEG 4000, 90 mM Tris (pH 8.75-9.0) and 180 mM Na Acetate and suspended over wells containing 800 μL of the reservoir buffer. After 4-7 days at 19-21° C., rod-like crystals were obtained. The coactivator complex crystals lie in the spacegroup P21 with cell dimensions a=54.09, b=82.22, c=58.04 and β=111.34. Two molecules each of the DES-LBD and the coactivator peptide form the asymmetric unit. A 200 μm×40 μm×40 μm crystal was transferred to a cryosolvent solution containing 25% (w/v) PEG 4000, 10% (w/v) ethylene glycol, 100 mM Tris (pH 8.5), 200 mM Na Acetate and 10 μM peptide and frozen in an N2 stream at −170° C. in a rayon loop. Diffraction data from this crystal were measured at −170° C. using a 300 mm MAR image plate at the Stanford Synchrotron Radiation Laboratory (SSRL) at beamline 7-1 at a wavelength of 1.08 Å. The diffraction images were processed with DENZO and scaled with SCALEPACK (Otwinowski, et al., Methods Enzymol. (1997) 276:307-326) using the default −3σ cutoff

C. Crystallization of hERα LBD with OHT

Crystals of the hERα LBD (residues 297-554) complexed to OHT were obtained by the hanging drop vapor diffusion method. Equal volume aliquots (2 μL) of a solution containing 3.9 mg/mL protein-ligand complex and the reservoir solution containing 9% (w/v) PEG 8000, 6% (w/v) ethylene glycol, 50 mM HEPES (pH 6.7) and 200 mM NaCl were mixed and suspended over 800 μL of the reservoir solution. Hexagonal plate-like crystals formed after 4-7 days at 21-23° C. Both crystal size and quality were improved through microseeding techniques. These crystals belong to the space group P6522 with cell parameters a=b=58.24 Å and c=277.47 Å. The asymmetric unit consists of a single hERα LBD monomer; the dimer axis lies along a crystallographic two-fold. A single crystal (400 μm×250 μm×40 μm) was briefly incubated in a cryoprotectant solution consisting of 10% (w/v) PEG 8000, 25% (w/v) ethylene glycol, 50 mM HEPES (pH 7.0) and 200 mM NaCl and then flash frozen in liquid N2 suspended in a rayon loop. Diffraction data were measured at −170° C. using a 345 mm MAR image plate at SSRL at beamline 9-1 and at a wavelength of 0.98 Å. The diffraction images were processed with DENZO and scaled with SCALEPACK (Otwinowski, et al., supra) using the default −3σ cutoff

Example 16

Structure Determination and Refinement of NR LBD Complexes

A. Structure of hTRβ LBD with T3 and GRIP1 NR-Box 2 Peptide

Data were measured using Cu Ka radiation from an R-axis generator at 50 kV and 300 mA with a 0.3 mM collimator and a Ni filter. Reflections were measured using an R-Axis II detector and integrated with Denzo, and equivalent reflections scaled using Scalepack (Otwinowski and Minor, “Processing of x-ray diffraction data collected in oscillation mode.” In Macromolecular Crystallography, Part A (ed. C. W. Carter, Jr. and R. M. Sweet), pp. 307-326. Academic Press, New York, N.Y.). Possible rotation function solutions were calculated using normalized amplitudes in AMORE from a model of hTRβ LBD with the ligand, T3, omitted; translation function solutions were subsequently determined using TFFC for the two rotation solutions with the highest correlation coefficients. For two hTRβ LBD molecules in the asymmetric unit, the calculated solvent content is 52%. After rigid body refinement of the two hTRβ LBD molecules, electron density maps were calculated. Strong positive density present in both the anomalous and conventional difference Fourier maps for the iodine atoms of the T3 ligand confirmed the correctness of the solution. The iodine atoms for both T3 ligands were modeled as a rigid body, and the structure refined with strict NCS symmetry using CNS. Both 2FoFc and FoFc electron density maps showed interpretable density, related by the NCS operator, near H12 of both molecules of the hTRβ LBD. The electron density could be modeled as a short a-helix, and the observed side chain density was used to tentatively assign the sequence and direction to the chain. The refined model consists of residues of the hTRβ LBD, and peptide residues of the GRIP1 NR-box 2 peptide 686-KHKJLHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6).

Atomic coordinates of the hTRβ LBD:GRP1 site 2 peptide complex are attached as Appendix 1.

B. Structure of hERα LBD with DES and GRIP1 NR-Box 2 Peptide

Initial efforts to determine the structure of the DES-hERα LBD-NR box 2 peptide 686-KHKILHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6) complex utilized a low resolution (3.1 Å) data set (data not shown). A self-rotation search implemented with POLARRFN (“The CCP4 suite: programs for protein crystallography”, Acta Crystallogr. (1994) D50:760-763) indicated the presence of a noncrystallographic dyad. The two LBDs in the asymmetric were located by molecular replacement in AMoRe (CCP4, 1994) using a partial polyalanine model of the human RARγ LBD (Renaud, et al., supra) as the search probe (R=58.2%, CC 35.6% after placement of both monomers). Given that the model at this point was both inaccurate (r.m.s.d. 1.7 Å between this model and the final model based on Cα positions) and incomplete (accounting for only 45% of the total scattering matter in the asymmetric unit), an aggressive density modification protocol was undertaken. Iterative cycles of two-fold NCS averaging in DM (CCP4, 1994) interspersed with model building in MOLOC (Muller, et al., Bull. Soc. Chim. Belg. (1988) 97:655-667) and model refinement in REFMAC (Murshudov, et al., Acta Crystallogr. (1997) D53:240-255) (using tight NCS restraints) were used to quickly build a model of the LBD alone. For this procedure, MAMA (Kleywegt, et al., “Halloween . . . masks and bones. In From First Map to Final Model”, Bailey, et al, eds., Warrington, England, SERC Daresbury Laboratory, 1994) was used for all mask manipulations and PHASES (Furey, et al., PA33 Am. Cryst. Assoc. Mtg. Abstr. (1990) 18:73) and the CCP4 suite (CCP4, 1994) were used for the generation of structure factors and the calculation of weights.

However, although the DES-hERα LBD-NR complex model accounted for ˜90% of the scattering matter in the asymmetric unit, refinement was being hampered by severe model bias. The high-resolution data set of the DES-hERα LBD-NR-box 2 peptide complex became available when the Rfree of the OHT-hERα LBD model was ˜31%. Both monomers in the asymmetric unit of the DES complex crystal were relocated using AMoRe and the incompletely refined OHT-hERα LBD model (with helix 12 and the loop between helices 11 and 12 removed) as the search model. The missing parts of the model were built and the rest of the model was corrected using MOLOC and two-fold averaged maps generated in DM. Initially, refinement was carried out with REFMAC using tight NCS restraints. At later stages, the model was refined without NCS restraints using the simulated annealing, minimization and B-factor refinement protocols in X-PLOR and a maximum-likelihood target. All B-factors were refined isotropically and anisotropic scaling and a bulk solvent correction were used. The Rfree set contained a random sample of 6.5% of all data. In refinement, all data between 27 and 2.03 Å (with no σ cutoff) were used. The final model was composed of residues 305-549 of monomer A, residues 305-461 and 470-554 of monomer B, residues 687-697 of peptide A, residues 686-696 of peptide B, 164 waters, two carboxymethyl groups and a chloride ion. According to PROCHECK, 93.7% of all residues in the model were in the core regions of the Ramachandran plot and none were in the disallowed regions. Thus, the structure of the DES-hERα LBD-NR-box 2 peptide complex has been refined to a crystallographic R-factor of 19.9% (Rfree=25.0%) using data to 2.03 Å resolution.

Ile 689 from the peptide interacts with three receptor residues (Asp 538, Glu 542 and Leu 539). The γ-carboxylate of Glu 542 forms hydrogen bonds to the amides of residues 689 and 690 of the peptide. A water-mediated hydrogen bond network is formed between the imidazole ring of His 377, the γ-carboxylate of Glu 380, and the amide of Tyr 537. Three residues (Glu 380, Leu 536 and Tyr 537) interact with each other through van der Waals contacts and/or hydrogen bonds. Intriguingly, mutations in each these three residues dramatically increase the transcription activity of unliganded ERα LBD (Eng, et al., Mol. Cell. Biol. (1997) 17:4644-4653); Lazennec, et al., Mol Endocrinol. (1997) 11:1375-86; White, et al., EMBO J. (1997) 16:1427-35). Atomic coordinates of DES-LBD-peptide complex are attached as Appendix 2. The structure in Appendix 2 comprises: human ERα residues 305-549 of chain A (SEQ ID NO: 56), human ERα residues 305-549 of chain B (SEQ ID NO: 57); peptide chain C (SEQ ID NO: 58); and peptide chain D (SEQ ID NO: 60).

TABLE 2
Summary of Crystallographic Statistics
Ligand
DESOHT
Data Collection
Space groupP21P6522
Resolution2.031.90
Observations104189269253
Unique3026523064
Completeness (%)98.499.1
Rsym(% i)a7.87.0
Average I/σI9.816.1
Refinement
Number of non-hydrogen atoms41802070
Rcryst (%)b/Rfree (%)19.9/25.023.0/26.1
Bond r.m.s. deviation (Å)0.0060.006
Angle r.m.s. deviation (°)1.051.05
Average B factor (Å2)34.040.4

aRsym = Σi|Ii-, <Ii> n|/ΣiIi where <Ii> is the average intensity over symmetry equivalents

bRcryst = Σ|Fo = Fc|/Σ|Fo|

C. Structure of hERα LBD-OHT Complex

The OHT complex data set was then collected. Starting with one of the monomers of the preliminary low-resolution DES-hERα LBD-NR-box 2 peptide model as the search probe, molecular replacement in AMoRe was used to search for the location of LBD in this crystal form in both P6122 and P6522. A translation search in P6522 yielded the correct solution (R=53.8%, CC=38.2%). In order to reduce model bias, DMMULTI (CCP4, 1994) was then used to project averaged density from the DES complex cell into the OHT complex cell. Using MOLOC, a model of the hERα LBD was built into the resulting density. The model was refined initially in REFMAC and later with the simulated annealing, positional and R-factor refinement protocols in X-PLOR (Brunger, X-PLOR. Version 3.843, New Haven, Conn.: Yale University, 1996) using a maximum-likelihood target (Adams, et al., Proc. Natl. Acad. Sci. USA (1997) 94:5018-23). Anisotropic scaling and a bulk solvent correction were used and all B-factors were refined isotropically. Except for the Rfree set (a random sampling consisting of 8% of the data set), all data between 41 and 1.9 Å (with no σ cutoff) were included. The final model consisted of residues 306-551, the ligand and 78 waters. According to PROCHECK (CCP4, 1994), 91.6% of all residues in the model were in the core regions of the Ramachandran plot and none were in the disallowed regions. Thus, the structure of the OHT-hERα LBD complex has been refined against data of comparable resolution (1.90 Å) to a crystallographic B-factor of 23.0% (Rfree=26.2%). Atomic coordinates of OHT-hERα LBD complex are attached as Appendix 3. The structure in Appendix 3 consists of: atomic coordinates for a portion of human ERα, (SEQ ID NO: 59) complexed with OHT.

Example 17

Structural Analysis of hTRβ LBD:GRIP1 NR-Box 2 Peptide Complex

A. Structure of Cocrystal Complex (Contents of asu)

The asymetric unit (asu) of the crystal contains two monomers of the hTRβ LBD and two molecules of the GRIP1 NR-box 2 peptide 686-KHKILHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6), which observes the NCS relation of the two TR monomers (FIG. 12). The structure of the hTRβ LBD, which closely resembles that of the rTRα LBD (Wagner et al., supra), consists of twelve alpha-helices and two β-strands organized in three layers, resembling an alpha-helical sandwich. The only significant difference between the hTRβ LBD and the rTRα LBD is disorder in the loop between helices H1 and H3. The GRIP1 NR-box 2 peptide forms an amphipathic α-helix of about 3 turns, preceded by 2 residues and followed by 3 residues in extended coil conformation.

The relation of the two monomers of the hTRβ LBD is primarily translational, and does not resemble the homodimer structures reported for the hRXR, or the hER. (Bourguet et al., supra; Brzozowski et al., supra). Furthermore, the interface between the two monomers does not involve residues necessary for formation of the physiological TR dimer. Instead, one of the cocrystal peptides appears to bridge the interaction between the two monomers. The hydrophobic face of the alpha-helix of the cocrystal peptide contacts monomer 1 of the hTRβ LBD at H3, H5, and H12, while the hydrophilic face contacts monomer 2 at the hairpin turn preceding strand S3. The second cocrystal peptide also contacts monomer 2 at H3, H5, and H12, and the two cocrystal peptides observe the same NCS relation as TR LBD monomers.

The common interface between both cocrystal peptides and the hTRβ LBD buries the hydrophobic residues that define the cocrystal peptide (SEQ ID NO: 1) LxxLL sequence motif, residues Ile689, Leu690, Leu693, and Leu694; against the surface of the receptor LBD (FIGS. 16 and 17). The presence of the second peptide in the crystal, duplicating the interactions of the hydrophobic residues, suggests those interactions are specific and drive the interaction of the peptide with the hTRβ LBD, while the hydrophilic interactions provide a fortuitous crystal contact and account for the dependence of crystallization on the presence and concentration of the peptide.

B. Structure of the GRIP1 NR-Box 2 Peptide

The GRIP1 NR-box 2 peptide used in the crystallization is 13 amino acids long (residues 12-24 of SEQ ID NO: 6; 686-KHKILHRLLQDSS-698). For the NR-box 2 peptide in monomer 1 (peptide 1), 12 amino acids are ordered in the crystal. Residues K688-Q694 form an amphipathic helix, with residues K686-H687 and D695-S698 on either end in extended coil conformations. For the NR-box 2 peptide in monomer 2 (peptide 2), residues K688-Q694 again form an amphipathic helix, but the ends of the peptide are disordered. While the resolution of the current data prevents absolute assignment of hydrogen bonds, it is evident from the periodicity of the side chain density that the central residues form an alpha-helix. In the absence of TR the far UV-CD spectrum of the GRIP1 NR-box 2 peptide 686-KHKILHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6) appears to be random coil (data not shown). Stable helix formation may thus be induced by the interaction of the hydrophobic amino acids with the receptor LBD as it has been proposed in other protein:protein interactions, such as p53:MDM2 (Kussie et al., Science (1996) 274:948-953), VP16:TAF31 (Uesugi et al., Science (1996) 277:1310-1313), and CREB:KIX-CBP (Radhakrishnan et al., Cell (1997) 91:741-752).

C. Structure of the hTRβ LBD:GRIP1 NR-Box 2 Peptide Interface

The hTRβ LBD of the cocrystal contributes residues from three helices, H3, H5, and H12 to the interface, which pack against one another to create a hydrophobic cleft. The residues lining the cleft are I280, T281, V283, V284, A287, and K288 from H3; Q301, I302, L305, and K306 from H5; and L454, E457, V458, and F459 from H12. A cysteine residue (C309) from H6 appears to provide a partial surface that is buried deep within the bottom of the cleft.

The GRIP1 NR-box 2 peptide 686-KHKILHRLLQDSS-698 (residues 12-24 of SEQ ID NO:6) binds at the junction of H3 and H12. Leu690 of the bound peptide inserts into a shallow but defined depression at the base of the cleft, making van der Waals contact with L454 and V458 of H12, while peptide residue Ile689 packs against L454 of H12 outside the edge of the cleft; L454, then, interdigitates between the two residues. One further turn C-terminal along the alpha-helix, L693 and L694 of the bound peptide pack into complementary pockets within the hydrophobic cleft. Peptide residue L693 forms van der Waals contact with V284 of H3, while peptide residue L694, bound more deeply in the cleft, makes contact with F298 and L305 of H4 and H5. The hydrophobic interactions of the GRIP1 NR-box 2 peptide with the hTRβ LBD are observed for both cocrystal peptides 1 and 2 in their respective monomers of the crystal dimer complex, suggesting that the interactions are specific to the peptide, and not induced by crystallization.

Example 18

Overall Structure of the DES-hERα-LBD-NR-Box 2 Peptide Complex

The asymmetric unit of the DES-hERα LBD-NR-box 2 peptide 686-KHKILHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6) complex crystals contains the same noncrystallographic dimer of LBDs that has been observed in the previously determined structures of the LBD bound to both E2 and RAL (Brzozowski, et al., supra and Tanenbaum, et al., supra). Beyond the flexible loops between helices 2 and 3 and helices 9 and 10, the two LBDs of the dimer adopt similar structures (r.m.s.d. 0.47 Å based on Ca positions). The conformation of each LBD complexed with DES closely resembles that of the LBD bound to E2 (Brzozowski, et al., supra); each monomer is a wedge shaped molecule consisting of three layers of eleven to twelve helices and a single beta hairpin. In each LBD, the hydrophobic face of helix 12 is packed against helices 3, 5/6 and 11 covering the ligand binding pocket. One NR-box 2 peptide is bound to each LBD in a hydrophobic cleft composed of residues from helices 3, 4, 5 and 12 and the turn between 3 and 4. The density for both peptides in the asymmetric unit is continuous and unambiguous. Residues 687 to 697 from peptide A and residues 686 to 696 from peptide B have been modeled; the remaining residues are disordered. Given that each peptide lies within a different environment within the crystal, it is striking that from residues Ile 689 to Gln 695 each peptide forms a two turn, amphipathic a helix. Flanking this region of common secondary structure, the peptides adopt dissimilar random coil conformations.

Example 19

Structure of the OHT-hERα LBD Complex

The binding of OHT induces a conformation of the hERα LBD that differs in both secondary and tertiary structural organization from that driven by DES binding. In the DES complex, the main chain from residues 339 to 341, 421 to 423, and 527 to 530 form parts of helices 3, 8 and 11 respectively. In contrast, these regions adopt an extended conformation in the OHT complex. In addition, the composition and orientation of helix 12 are different in the two structures. Helix 12 in the DES complex consists of residues 538 to 546 whereas helix 12 in the OHT complex consists of residues 536 to 544. Most dramatically, rather than covering the ligand binding pocket as it does in the DES complex, helix 12 in the OHT complex occupies the part of the coactivator binding groove formed by residues from helices 3, 4, and 5, and the turn connecting helices 3 and 4. This alternative conformation of helix 12 appears to be similar to that observed in the RAL complex (Brzozowski, et al., supra).

Example 20

Coactivator Binding Site Structure and Function

A. TR Coactivator Binding Site

The above examples demonstrate that nuclear receptors, exemplified by TR, GR and ER, are recognized by specific coactivators that bind thereto through a coupling surface comprising a hydrophobic cleft and a charged hydrophobic perimeter. Identification and characterization of this coupling surface and the coactivator binding site of nuclear receptors offers a new target for the design and selection of compounds that modulate binding of coactivator to nuclear receptors.

Residues forming the coactivator binding site were found to cluster within a surprisingly small area with well-defined borders (see, e.g., FIGS. 5, 14, and 15). As is shown in above Examples, mutated residues nearby this area do not affect coactivator binding or transcriptional activation. Additionally, the coactivator binding assays and structural analyses demonstrated that NR-box containing proteins and peptides bind to this site. These results also showed that the GRIP1 coactivator protein binds to the site through a highly (SEQ ID NO: 1) LxxLL.

The structural analyses showed that residues contacting a conserved leucine residue of the (SEQ ID NO: 1) LxxLL motif included V284, F293, I302, L305 and L454. Residues within 4.5 Å of an atom of the bound peptide included T281, V284, K288, F293, Q301, I302, L305, K306, P453, L454 and E457. Structural analyses also revealed two other features of the site: a hydrophobic residue from helix 12 (Phe459) that contributes to local packing, and a cysteine residue contributed by helix 6 (Cys309) that provides a partial surface buried deep within the site. Mutational analyses showed that residues which block GRIP1 and SRC-1 coactivator binding when mutated are residues V284, K288, I302, K306, L454, and V458. Mutated residues likely to undergo a conformational change upon hormone binding included Leu454 and Glu457. Thus, the site identified by mutational, binding assays and crystallography corresponds to a surprisingly small cluster of residues on the surface of the LBD that define a prominent hydrophobic cleft formed by hydrophobic residues corresponding to human TR residues of C-terminal helix 3 (Ile280, Val283, Val284, and Ala287), helix 4 (Phe293), helix 5 (Ile302 and Leu305), helix 6 (Cys309), and helix 12 (Leu454, Val458 and Phe459). Collectively, the Examples indicate that residues forming the site are amino acids corresponding to human TR residues of C-terminal helix 3 (Ile280, Thr281, Val283, Val284, Ala287, and Lys288), helix 4 (Phe293), helix 5 (Gln301, Ile302, Leu3OS, Lys306), helix 6 (Cys309), and helix 12 (Pro453, Leu454, Glu457, Val458 and Phe459). The coactivator binding site is highly conserved among the nuclear receptor super family (FIG. 19).

The coactivator binding site of TR contains charged and hydrophobic residues at its periphery, but only hydrophobic residues at its center (see, e.g., FIGS. 5 and 18). The hydrophobic cleft at the center of the site may play a significant role in driving the coactivator binding reaction. The site is comprised of two parts (FIG. 18), right). Residues contained in helices 3, 5 and 6 (FIG. 18, yellow residues) likely form a constitutive part, since their positions are identical in all nuclear receptor structures reported, including the liganded, activated states of the TR, RAR, and ER, the unliganded RXR, and the inhibitor-liganded ER. By contrast, the residues of helix 12 (FIG. 18, red residues) are differently positioned in the active and inactive states reported. Thus the coactivator binding site for the nuclear receptors is likely to be formed in response to an active hormone by positioning helix 12 against a scaffold formed by helices 3-6. Because the coactivator binding site is so small, it is easy to understand how even slight changes in the position of helix 12, which may, for example, be induced by an antagonist ligand, could impair coactivator binding, and thus receptor activation.

B. ER Coactivator Binding Site

Binding of the NR-box 2 peptide 686-KHKILHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6) to the ERα LED buries 1000 Å2 of predominantly hydrophobic surface area from both molecules. The NR-box 2 peptide binding site is a shallow groove composed of residues Leu 354, Val 355, Ile 358, Ala 361 and Lys 362 from helix 3; Phe 367 and Val 368 from helix 4; Leu 372 from the turn between helices 3 and 4; Gln 375, Val 376, Leu 379 and Glu 380 from helix 5; and Asp 538, Leu 539, Glu 542 and Met 543 from helix 12. The floor and sides of this groove are completely nonpolar, but the ends of this groove are charged. Therefore, structural characterization of the binding site of the NR-box 2 peptide 686-KHKILHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6) to the ERα LBD, which is the same NR-box 2 peptide utilized to crystallize the T3-TR LBD, supports the findings for TR that residues forming the coactivator binding site of nuclear receptors is composed of a well defined hydrophobic cleft and a charged hydrophobic perimeter. These residues are highly conserved among the nuclear receptor super family (FIG. 19). Structural characterization of the coactivator peptide-bound ER LBD also supports the concept of exploiting the slight differences among the coactivator binding sites of nuclear receptors in designing and identifying compounds that target specific nuclear receptors.

The ERα LBD interacts primarily with the hydrophobic face of the NR-box 2 peptide 686-KHKILHRLLQDSS-698 (residues 12-24 of SEQ ID NO: 6) a helix formed by the side chains of Ile 689 and the three (SEQ ID NO: 1) LxxLL motif leucines (Leu 690, Leu 693 and Leu 694). The side chain of Leu 690 is deeply embedded within the groove and forms van der Waals contacts with the side chains of Ile 358, Val 376, Leu 379, Glu 380 and Met 543. The side chain of Leu 694 is similarly isolated within the groove and makes van der Waals contacts with the side chains of Ile 358, Lys 362, Leu 372, Gln 375, Val 376 and Leu 379. In contrast, the side chains of both Ile 689 and the second NR box leucine, Leu 693, rest against the rim of the groove. The side chain of Ile 689 lies in a shallow depression formed by the side chains of Asp 538, Leu 539 and Glu 542. The side chain of Leu 693 makes nonpolar contacts with the side chains of Ile 358 and Leu 539.

The charged and polar side chains which form the hydrophilic face of the peptide helix project away from the ERα receptor and either interact predominantly with solvent or form symmetry contacts. None of the side chains of the polar and charged residues outside the helical region of either peptide in the asymmetric unit, with the exception of Lys 688 of peptide B, is involved in hydrogen bonds or salt bridges with its associated ERα LBD monomer. The ε-amino group of Lys 688 of peptide B hydrogen bonds to the side chain carboxylate of Glu 380 of monomer B. This interaction is presumably a crystal artifact; the main chain atoms of the N-terminal three residues of peptide B are displaced from monomer B and interact extensively with a symmetry-related ERα LBD.

In addition to interacting with the hydrophobic face of the peptide helix, the ERα LBD stabilizes the main chain conformation of the NR box peptide by forming capping interactions with both ends of the peptide helix. Glu 542 and Lys 362 are positioned at opposite ends of the peptide binding site. The side chains of Glu 542 and Lys 362 form van der Waals contacts with main chain and side chain atoms at the N- and C-terminal turns of the peptide helix respectively. These interactions position the stabilizing charges of the γ-carboxylate of Glu 542 and ε-amino group of Lys 362 near the ends of the NR box peptide helix. The side chain carboxylate of Glu 542 hydrogen bonds to the amides of the residues of N-terminal turn of the peptide helix (residues 688 and 689 of peptide A; residues 689 and 690 of peptide B). Similarly, the ε-amino group of Lys 362 hydrogen bonds to the carbonyls of the residues of the C-terminal turn of the peptide helix (residue 693 of peptide A; residues 693 and 694 of peptide B).

Except for the orientation of helix 12, the structure of the peptide binding groove of the ERα LBD is almost identical in the DES and OHT complexes. The region of this groove outside of helix 12 is referred to herein as the “static region” of the NR box binding site. Helix 12 in the OHT complex and the NR box peptide helix in the DES complex interact with the static region of the coactivator recognition groove in strikingly similar ways.

Helix 12 mimics the hydrophobic interactions of the NR box peptide with the static region of the groove with a stretch of residues (residues 540 to 544) that resembles an NR box ((residues 6-10 of SEQ ID NO: 43) LLEML instead of (SEQ ID NO: 1) LxxLL). The side chains of Leu 540 and Met 543 lie in approximately the same locations as those of the first and second motif leucines (Leu 690 and Leu 693) in the peptide complex. Leu 540 is inserted into the groove and makes van der Waals contacts with Leu 354, Val 376 and Glu 380. Met 543 lies along the edge of the groove and forms van der Waals contacts with the side chains of Leu 354, Val 355 and Ile 358. The side chain position of Leu 544 almost exactly overlaps that of the third NR box leucine, Leu 694. Deep within the groove, the Leu 544 side chain makes van der Waals contacts with the side chains of Ile 358, Lys 362, Leu 372, Gln 375, Val 376 and Leu 379.

Helix 12 in the OHT complex is also stabilized by N- and C-terminal capping interactions. Lys 362 interacts with the C-terminal turn of helix 12 much as it does with the equivalent turn of the peptide helix. The Lys 362 side chain packs against the C-terminal turn of the helix 12 with its ε-amino group hydrogen bonding to the carbonyls of residues 543 and 544. Given that the capping interaction at the N-terminal turn coactivator helix is formed by a helix 12 residue (Glu 542), the N-terminal turn of helix 12 in the antagonist complex is forced to interact with another residue, Glu 380. The Glu 380 γ-carboxylate forms van der Waals contacts with Tyr 537 and interacts with the amide of Tyr 537 through a series of water-mediated hydrogen bonds.

In addition to forming these “NR box-like” interactions, helix 12 also forms van der Waals contacts with areas of the ERα LBD outside of the coactivator recognition groove. The side chain of Leu 536 forms van der Waals contacts with Glu 380 and Trp 383 and that of Tyr 537 forms van der Waals contacts with His 373, Val 376 and Glu 380. As a result of these contacts, helix 12 in the OHT complex buries more solvent accessible surface area (˜1200 Å2) than the NR box peptide in the DES-ERA LBD-peptide complex.

Identification and characterization of the coactivator binding site for TR, and extension of this information to other nuclear receptors shows that this site is common for all nuclear receptors identified to date. Additionally, sequence and structural comparison, coupled with the Examples showing differential specificity for coactivator binding to TR, GR and ER, reveal that minor differences between the receptors, such as found in helix 12, are likely to influence specificity of a coactivator for different types of nuclear receptors. Thus, the Examples presented herein demonstrate that information derived from the structure and function of the TR coactivator binding site can be applied in design and selection of compounds that modulate binding of coactivator proteins to nuclear receptors for all members of the nuclear receptor super family.

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All publications and patent applications mentioned in this specification are herein incorporated by reference to the same extent as if each individual publication or patent application was specifically and individually indicated to be incorporated by reference.

The invention now being fully described, it will be apparent to one of ordinary skill in the art that many changes and modifications can be made thereto without departing from the spirit or scope of the appended claims.

ATOM197OSERA23726.60521.41821.7971.0075.478
ATOM198NHISA23824.64822.41022.3531.0075.567
ATOM199CAHISA23823.84221.98121.2361.0075.466
ATOM200CBHISA23822.99020.73221.6611.0075.856
ATOM201CGHISA23822.40819.93320.5421.0040.006
ATOM202CD2HISA23822.79018.75719.9571.0040.006
ATOM203ND1HISA23821.22320.30319.8751.0040.007
ATOM204CE1HISA23820.95119.36518.9531.0040.006
ATOM205NE2HISA23821.87418.44418.9941.0040.007
ATOM206CHISA23822.97123.28420.9641.0074.106
ATOM207OHISA23821.86323.13720.4411.0075.348
ATOM208NTRPA23923.48724.51021.3681.0073.397
ATOM209CATRPA23922.87225.89421.1951.0074.026
ATOM210CBTRPA23923.56327.02622.0051.0081.776
ATOM211CGTRPA23925.02227.36621.6881.0089.676
ATOM212CD2TRPA23925.53228.66221.2401.0093.196
ATOM213CE2TRPA23926.96128.52221.1361.0095.466
ATOM214CE3TRPA23924.93629.91120.9691.0095.356
ATOM215CD1TRPA23926.10226.54821.7811.0094.166
ATOM216NE1TRPA23927.26827.24121.4751.0097.487
ATOM217CZ2TRPA23927.79829.59820.7641.0096.236
ATOM218CZ3TRPA23925.76330.96720.5691.0096.756
ATOM219CH2TRPA23927.17130.82520.4821.0097.326
ATOM220CTRPA23922.79926.40719.7741.0070.776
ATOM221OTRPA23921.70626.56219.2631.0071.708
ATOM222NLYSA24023.94626.70119.1571.0067.107
ATOM223CALYSA24023.97827.18017.7831.0065.636
ATOM224CBLYSA24025.31426.78017.1531.0066.656
ATOM225CGLYSA24026.52927.34217.8721.0069.836
ATOM226CDLYSA24027.80527.03717.1081.0071.496
ATOM227CELYSA24028.98027.72017.7761.0071.316
ATOM228NZLYSA24030.23827.43817.0341.0072.237
ATOM229CLYSA24022.80826.69916.8951.0066.196
ATOM230OLYSA24022.55027.29815.8511.0065.208
ATOM231NASNA24122.11325.64017.3251.0066.697
ATOM232CAASNA24120.97625.07816.5991.0067.536
ATOM233CBASNA24121.12223.56216.5501.0067.986
ATOM234CGASNA24122.30423.12115.6931.0070.196
ATOM235OD1ASNA24122.40423.50614.5031.0071.378
ATOM236ND2ASNA24123.17622.31016.2711.0071.487
ATOM237CASNA24119.57025.42117.1521.0066.626
ATOM238OASNA24118.58124.82216.7311.0064.768
ATOM239NLYSA24219.47526.38018.0691.0066.867
ATOM240CALYSA24218.19126.78618.6421.0067.466
ATOM241CBLYSA24218.16426.39620.1191.0067.936
ATOM242CGLYSA24218.25024.89620.3371.0071.526
ATOM243CDLYSA24217.00424.14919.8211.0074.326
ATOM244CELYSA24215.75524.49120.6431.0074.416
ATOM245NZLYSA24215.92724.16122.1091.0074.447
ATOM246CLYSA24218.14328.29118.4831.0066.286
ATOM247OLYSA24217.10228.92318.5921.0067.618
ATOM248NARGA24319.33428.81318.2041.0064.197
ATOM249CAARGA24319.61730.21917.9751.0062.436
ATOM250CBARGA24321.07030.27417.4631.0060.126

APPENDIX 2
Atomic Coordinates for Human ERα Complexed with DES,
and a GRIP1 NR-box 2 Peptide
CRYST154.09482.21758.04190.00111.3390.00P212
ORIGX11.0000000.0000000.0000000.00000
ORIGX20.0000001.0000000.0000000.00000
ORIGX30.0000000.0000001.0000000.00000
SCALE10.0184860.0000000.0072210.00000
SCALE20.0000000.0121630.0000000.00000
SCALE30.0000000.0000000.0184970.00000
ATOM1CBSERA30535.230−14.787−1.1631.0073.26
ATOM2CSERA30535.331−14.3031.2891.0072.95
ATOM3OSERA30534.146−13.9841.1861.0072.46
ATOM4NSERA30536.797−16.0330.2851.0074.06
ATOM5CASERA30536.138−14.7130.0611.0073.59
ATOM6NLEUA30635.982−14.3132.4491.0072.21
ATOM7CALEUA30635.329−13.9503.7021.0071.05
ATOM8CBLEUA30636.251−14.2564.8781.0070.19
ATOM9CLEUA30634.929−12.4783.7191.0069.57
ATOM10OLEUA30635.580−11.6383.1001.0069.96
ATOM11NALAA30733.851−12.1764.4341.0068.06
ATOM12CAALAA30733.358−10.8104.5411.0064.88
ATOM13CBALAA30731.841−10.7954.4361.0065.83
ATOM14CALAA30733.792−10.2045.8661.0063.36
ATOM15OALAA30733.878−8.9846.0051.0062.73
ATOM16NLEUA30834.064−11.0626.8421.0062.52
ATOM17CALEUA30834.487−10.5988.1561.0062.57
ATOM18CBLEUA30834.423−11.7459.1711.0062.81
ATOM19CGLEUA30833.214−12.6889.1301.0064.21
ATOM20CD1LEUA30833.188−13.51310.4061.0066.28
ATOM21CD2LEUA30831.919−11.8988.9891.0063.80
ATOM22CLEUA30835.903−10.0378.1001.0061.61
ATOM23OLEUA30836.385−9.4459.0661.0062.92
ATOM24NSERA30936.561−10.2196.9591.0060.50
ATOM25CASERA30937.928−9.7436.7711.0058.73
ATOM26CBSERA30938.720−10.7505.9341.0059.53
ATOM27OGSERA30938.889−10.2834.6061.0059.47
ATOM28CSERA30937.986−8.3736.0991.0057.05
ATOM29OSERA30938.965−7.6376.2491.0056.70
ATOM30NLEUA31036.940−8.0385.3521.0052.69
ATOM31CALEUA31036.877−6.7594.6581.0048.20
ATOM32CBLEUA31035.516−6.5963.9741.0048.32
ATOM33CGLEUA31035.301−7.1882.5831.0044.94
ATOM34CD1LEUA31033.951−6.7282.0551.0046.45
ATOM35CD2LEUA31036.417−6.7551.6501.0043.19
ATOM36CLEUA31037.086−5.5895.6091.0046.44
ATOM37OLEUA31036.605−5.6076.7411.0046.78
ATOM38NTHRA31137.812−4.5765.1481.0044.36
ATOM39CATHRA31138.034−3.3805.9491.0042.88
ATOM40CBTHRA31139.313−2.6335.5321.0042.31
ATOM41OG1THRA31139.079−1.9364.3031.0042.50
ATOM42CG2THRA31140.464−3.6065.3501.0046.02
ATOM43CTHRA31136.834−2.4755.6741.0043.21
ATOM44OTHRA31136.021−2.7764.8001.0042.12
ATOM45NALAA31236.726−1.3726.4091.0042.16
ATOM46CAALAA31235.616−0.4446.2281.0040.10
ATOM47CBALAA31235.7410.7097.2051.0040.07
ATOM48CALAA31235.5610.0904.7991.0041.80
ATOM49OALAA31234.5100.0744.1541.0037.81
ATOM50NASPA31336.6980.5644.3041.0042.35
ATOM51CAASPA31336.7521.1042.9531.0042.27
ATOM52CBASPA31338.1331.7032.6801.0043.74
ATOM53CGASPA31338.3233.0543.3481.0046.62
ATOM54OD1ASPA31339.4143.6453.2051.0051.01
ATOM55OD2ASPA31337.3803.5294.0151.0048.89
ATOM56CASPA31336.4220.0271.9261.0038.68
ATOM57OASPA31335.7040.2810.9591.0038.75
ATOM58NGLNA31436.931−1.1792.1451.0034.76
ATOM59CAGLNA31436.666−2.2771.2291.0033.55
ATOM60CBGLNA31437.462−3.5121.6431.0036.90
ATOM61CGGLNA31438.963−3.3841.4361.0040.45
ATOM62CDGLNA31439.700−4.6101.9051.0043.13
ATOM63OE1GLNA31439.394−5.1962.9351.0043.60
ATOM64NE2GLNA31440.701−5.0321.1171.0044.03
ATOM65CGLNA31435.176−2.5951.2011.0034.95
ATOM66OGLNA31434.605−2.8600.1401.0032.89
ATOM67NMETA31534.542−2.5642.3741.0032.54
ATOM68CAMETA31533.115−2.8482.4701.0035.46
ATOM69CBMETA31532.650−2.7943.9261.0037.09
ATOM70CGMETA31531.137−2.7774.0971.0039.42
ATOM71SDMETA31530.443−4.4264.0531.0046.55
ATOM72CEMETA31531.351−5.2055.3971.0045.29
ATOM73CMETA31532.311−1.8591.6401.0031.83
ATOM74OMETA31531.453−2.2470.8521.0032.10
ATOM75NVALA31632.587−0.5601.8301.0032.62
ATOM76CAVALA31631.8820.4701.0791.0031.09
ATOM77CBVALA31632.3951.8881.4251.0034.77
ATOM78CG1VALA31631.7862.8990.4611.0034.10
ATOM79CG2VALA31632.0212.2462.8621.0034.40
ATOM80CVALA31632.0920.232−0.4141.0033.48
ATOM81OVALA31631.1450.266−1.2001.0032.49
ATOM82NSERA31733.337−0.027−0.7951.0033.49
ATOM83CASERA31733.682−0.280−2.1871.0032.88
ATOM84CBSERA31735.165−0.635−2.2971.0035.77
ATOM85OGSERA31735.8250.277−3.1541.0042.70
ATOM86CSERA31732.849−1.396−2.8011.0030.71
ATOM87OSERA31732.279−1.238−3.8801.0031.14
ATOM88NALAA31832.792−2.529−2.1111.0029.51
ATOM89CAALAA31832.035−3.676−2.5801.0029.93
ATOM90CBALAA31832.156−4.811−1.5791.0028.56
ATOM91CALAA31830.565−3.305−2.7711.0031.55
ATOM92OALAA31829.961−3.642−3.7841.0030.64
ATOM93NLEUA31929.997−2.614−1.7911.0034.13
ATOM94CALEUA31928.597−2.212−1.8611.0032.93
ATOM95CBLEUA31928.170−1.576−0.5401.0031.15
ATOM96CGLEUA31928.076−2.5550.6321.0032.27
ATOM97CD1LEUA31927.523−1.8401.8521.0032.14
ATOM98CD2LEUA31927.194−3.7330.2431.0031.82
ATOM99CLEUA31928.340−1.257−3.0201.0034.41
ATOM100OLEUA31927.430−1.475−3.8181.0035.23
ATOM101NLEUA32029.140−0.195−3.1201.0032.53
ATOM102CALEUA32028.9720.756−4.2121.0035.33
ATOM103CBLEUA32030.0521.839−4.1551.0033.52
ATOM104CGLEUA32029.9742.899−3.0541.0034.60
ATOM105CD1LEUA32031.0603.940−3.2921.0033.69
ATOM106CD2LEUA32028.6113.562−3.0441.0031.05
ATOM107CLEUA32029.0520.040−5.5611.0035.41
ATOM108OLEUA32028.2300.271−6.4461.0039.16
ATOM109NAASPA32130.042−0.833−5.7200.5036.33
ATOM110NBASPA32130.041−0.839−5.6950.5035.76
ATOM111CAAASPA32130.214−1.559−6.9770.5037.71
ATOM112CABASPA32130.258−1.595−6.9250.5037.11
ATOM113CBAASPA32131.537−2.334−6.9730.5040.01
ATOM114CBBASPA32131.573−2.374−6.8260.5039.41
ATOM115CGAASPA32131.694−3.230−8.1950.5041.93
ATOM116CGBASPA32132.770−1.562−7.2840.5039.96
ATOM117OD1AASPA32131.523−2.733−9.3290.5042.11
ATOM118OD1BASPA32133.312−1.868−8.3660.5043.41
ATOM119OD2AASPA32131.988−4.432−8.0220.5042.69
ATOM120OD2BASPA32133.170−0.622−6.5640.5041.33
ATOM121CAASPA32129.069−2.524−7.2750.5037.19
ATOM122CBASPA32129.123−2.565−7.2530.5036.68
ATOM123OAASPA32128.820−2.861−8.4340.5036.87
ATOM124OBASPA32128.934−2.942−8.4110.5036.08
ATOM125NALAA32228.374−2.968−6.2351.0035.35
ATOM126CAALAA32227.268−3.902−6.4171.0031.59
ATOM127CBALAA32227.124−4.781−5.1751.0030.73
ATOM128CALAA32225.946−3.204−6.7091.0030.07
ATOM129OALAA32224.955−3.857−7.0361.0026.53
ATOM130NGLUA32325.932−1.880−6.5961.0027.98
ATOM131CAGLUA32324.713−1.117−6.8271.0029.88
ATOM132CBGLUA32325.0270.380−6.8551.0030.98
ATOM133CGGLUA32324.8701.068−5.5091.0031.62
ATOM134CDGLUA32323.4630.940−4.9601.0031.98
ATOM135OE1GLUA32323.183−0.056−4.2571.0033.10
ATOM136OE2GLUA32322.6401.836−5.2331.0030.01
ATOM137CGLUA32324.010−1.515−8.1231.0030.86
ATOM138OGLUA32324.655−1.705−9.1511.0028.86
ATOM139NPROA32422.674−1.659−8.0831.0030.66
ATOM140CDPROA32421.774−1.466−6.9351.0031.01
ATOM141CAPROA32421.935−2.032−9.2901.0030.29
ATOM142CBPROA32420.613−2.598−8.7601.0031.42
ATOM143CGPROA32420.626−2.363−7.2581.0033.66
ATOM144CPROA32421.717−0.785−10.1381.0027.46
ATOM145OPROA32421.8930.332−9.6681.0026.19
ATOM146NPROA32521.335−0.959−11.4031.0027.80
ATOM147CDPROA32521.082−2.198−12.1611.0027.35
ATOM148CAPROA32521.1250.242−12.2111.0025.59
ATOM149CBPROA32521.258−0.266−13.6371.0024.02
ATOM150CGPROA32520.773−1.695−13.5591.0026.00
ATOM151CPROA32519.7490.830−11.9541.0023.73
ATOM152OPROA32518.8730.165−11.4021.0024.83
ATOM153NILEA32619.5712.081−12.3521.0022.11
ATOM154CAILEA32618.2962.762−12.2121.0024.01
ATOM155CBILEA32618.5024.282−12.1331.0025.97
ATOM156CG2ILEA32617.1684.992−12.2861.0020.75
ATOM157CG1ILEA32619.1894.632−10.8051.0029.31
ATOM158CD1ILEA32619.3016.120−10.5251.0032.91
ATOM159CILEA32617.5062.408−13.4711.0025.72
ATOM160OILEA32617.9062.758−14.5811.0025.55
ATOM161NLEUA32716.3921.703−13.3011.0025.57
ATOM162CALEUA32715.5951.279−14.4391.0023.80
ATOM163CBLEUA32714.872−0.029−14.1041.0023.96
ATOM164CGLEUA32715.778−1.210−13.7281.0019.89
ATOM165CD1LEUA32714.944−2.462−13.5831.0021.19
ATOM166CD2LEUA32716.850−1.415−14.8051.0017.53
ATOM167CLEUA32714.5982.317−14.9351.0027.16
ATOM168OLEUA32714.1613.202−14.1941.0025.98
ATOM169NTYRA32814.2512.207−16.2101.0026.56
ATOM170CATYRA32813.3033.123−16.8141.0024.45
ATOM171CBTYRA32813.7243.465−18.2451.0026.72
ATOM172CGTYRA32814.5874.693−18.3141.0027.73
ATOM173CD1TYRA32814.0215.949−18.5181.0028.56
ATOM174CE1TYRA32814.7987.092−18.5091.0029.10
ATOM175CD2TYRA32815.9624.612−18.1101.0026.01
ATOM176CE2TYRA32816.7505.753−18.0981.0030.63
ATOM177CZTYRA32816.1576.988−18.2971.0030.07
ATOM178OHTYRA32816.9178.130−18.2651.0037.94
ATOM179CTYRA32811.9232.501−16.8271.0024.95
ATOM180OTYRA32811.7741.274−16.8461.0027.02
ATOM181NSERA32910.9123.358−16.8001.0025.60
ATOM182CASERA3299.5332.908−16.8371.0029.45
ATOM183CBSERA3298.6613.858−16.0201.0030.80
ATOM184OGSERA3297.2973.721−16.3641.0033.74
ATOM185CSERA3299.1292.947−18.3131.0031.30
ATOM186OSERA3299.9083.397−19.1541.0027.35
ATOM187NGLUA3307.9302.469−18.6291.0032.98
ATOM188CAGLUA3307.4592.482−20.0071.0035.10
ATOM189CBGLUA3306.0311.968−20.0741.0034.67
ATOM190CGLUA3307.5323.924−20.5051.0040.06
ATOM191OGLUA3307.0684.841−19.8261.0042.65
ATOM192NTYRA3318.1244.126−21.6811.0041.16
ATOM193CATYRA3318.2635.470−22.2341.0042.66
ATOM194CBTYRA3319.3235.482−23.3501.0042.54
ATOM195CGTYRA3319.2024.347−24.3451.0038.67
ATOM196CD1TYRA33110.1053.284−24.3341.0034.66
ATOM197CE1TYRA3319.9852.228−25.2331.0034.89
ATOM198CD2TYRA3318.1744.327−25.2871.0037.88
ATOM199CE2TYRA3318.0453.276−26.1931.0034.65
ATOM200CZTYRA3318.9502.232−26.1591.0030.73
ATOM201OHTYRA3318.8141.191−27.0421.0030.97
ATOM202CTYRA3316.9436.043−22.7541.0046.24
ATOM203OTYRA3316.0185.301−23.0961.0045.38
ATOM204NASPA3326.8687.372−22.7921.0049.11
ATOM205CAASPA3325.6848.092−23.2621.0052.40
ATOM206CBASPA3325.7818.321−24.7721.0052.86
ATOM207CASPA3324.3567.410−22.9261.0052.90
ATOM208OASPA3323.5617.116−23.8181.0053.94
ATOM209NPROA3334.1037.144−21.6321.0053.63
ATOM210CDPROA3334.9627.418−20.4651.0053.63
ATOM211CAPROA3332.8406.497−21.2531.0053.55
ATOM212CBPROA3333.0706.076−19.8021.0053.78
ATOM213CGPROA3334.1017.028−19.2901.0053.42
ATOM214CPROA3331.6737.478−21.3981.0052.17
ATOM215OPROA3331.8798.690−21.3951.0051.19
ATOM216NTHRA3340.4576.956−21.5321.0052.26
ATOM217CATHRA334−0.7247.802−21.6871.0054.21
ATOM218CBTHRA334−1.9976.949−21.8131.0053.90
ATOM219OG1THRA334−1.9716.256−23.0651.0053.92
ATOM220CG2THRA334−3.2377.821−21.7611.0054.15
ATOM221CTHRA334−0.8648.782−20.5251.0056.34
ATOM222OTHRA334−1.3898.443−19.4611.0056.44
ATOM223NARGA335−0.38610.002−20.7661.0058.24
ATOM224CAARGA335−0.37711.099−19.8011.0057.96
ATOM225CBARGA335−0.56912.427−20.5311.0060.22
ATOM226CARGA335−1.34910.996−18.6271.0056.61
ATOM227OARGA335−0.91910.908−17.4751.0060.70
ATOM228NPROA336−2.66711.015−18.8891.0052.43
ATOM229CDPROA336−3.38911.117−20.1651.0049.06
ATOM230CAPROA336−3.58710.915−17.7521.0049.58
ATOM231CBPROA336−4.91111.456−18.3021.0048.66
ATOM232CGPROA336−4.64511.809−19.7601.0051.33
ATOM233CPROA336−3.6989.468−17.2791.0049.25
ATOM234OPROA336−4.3408.644−17.9291.0048.06
ATOM235NPHEA337−3.0639.170−16.1471.0047.90
ATOM236CAPHEA337−3.0557.821−15.5821.0046.61
ATOM237CBPHEA337−2.0637.732−14.4211.0047.73
ATOM238CGPHEA337−0.6498.011−14.8051.0046.27
ATOM239CD1PHEA337−0.0179.168−14.3681.0046.55
ATOM240CD2PHEA3370.0617.113−15.5911.0048.12
ATOM241CE1PHEA3371.3059.429−14.7071.0048.09
ATOM242CE2PHEA3371.3867.364−15.9381.0047.57
ATOM243CZPHEA3372.0098.525−15.4951.0048.40
ATOM244CPHEA337−4.4017.338−15.0711.0046.15
ATOM245OPHEA337−5.2508.127−14.6711.0048.34
ATOM246NSERA338−4.5736.022−15.0801.0045.06
ATOM247CASERA338−5.7815.385−14.5781.0045.12
ATOM248CBSERA338−6.4774.594−15.6841.0044.49
ATOM249OGSERA338−6.2273.206−15.5541.0045.78
ATOM250CSERA338−5.2924.439−13.4881.0047.04
ATOM251OSERA338−4.0904.186−13.3871.0044.08
ATOM252NGLUA339−6.2063.916−12.6761.0045.63
ATOM253CAGLUA339−5.8023.012−11.6081.0045.40
ATOM254CBGLUA339−7.0152.521−10.8141.0045.66
ATOM255CGGLUA339−6.6371.680−9.6001.0046.81
ATOM256CDGLUA339−7.7171.652−8.5351.0047.56
ATOM257OE1GLUA339−8.4710.656−8.4771.0047.37
ATOM258OE2GLUA339−7.8102.625−7.7541.0049.29
ATOM259CGLUA339−5.0401.821−12.1701.0045.23
ATOM260OGLUA339−3.8621.641−11.8721.0046.51
ATOM261NALAA340−5.7121.010−12.9821.0042.87
ATOM262CAALAA340−5.078−0.158−13.5741.0040.24
ATOM263CBALAA340−6.055−0.871−14.4961.0041.40
ATOM264CALAA340−3.8370.273−14.3501.0038.83
ATOM265OALAA340−2.909−0.515−14.5431.0035.58
ATOM266NSERA341−3.8361.535−14.7731.0035.79
ATOM267CASERA341−2.7422.133−15.5371.0036.58
ATOM268CBSERA341−3.2313.454−16.1541.0039.01
ATOM269OGSERA341−2.2114.130−16.8641.0036.09
ATOM270CSERA341−1.4802.376−14.6911.0035.63
ATOM271OSERA341−0.3891.913−15.0381.0033.20
ATOM272NMETA342−1.6263.115−13.5951.0035.92
ATOM273CAMETA342−0.4983.396−12.7081.0035.88
ATOM274CBMETA342−0.9124.396−11.6231.0035.96
ATOM275CGMETA3420.2415.218−11.0591.0038.02
ATOM276SDMETA342−0.3086.374−9.7801.0044.73
ATOM277CEMETA3420.6267.815−10.2051.0042.49
ATOM278CMETA342−0.0112.100−12.0591.0034.17
ATOM279OMETA3421.1951.880−11.9091.0033.40
ATOM280NMETA343−0.9571.243−11.6871.0029.95
ATOM281CAMETA343−0.640−0.034−11.0621.0031.96
ATOM282CBMETA343−1.921−0.810−10.7511.0031.70
ATOM283CGMETA343−2.667−0.337−9.5021.0037.13
ATOM284SDMETA343−1.749−0.507−7.9401.0036.00
ATOM285CEMETA343−1.468−2.299−7.8861.0032.14
ATOM286CMETA3430.234−0.875−11.9791.0031.72
ATOM287OMETA3431.159−1.558−11.5271.0030.26
ATOM288NGLYA344−0.069−0.823−13.2721.0029.04
ATOM289CAGLYA3440.688−1.591−14.2421.0024.94
ATOM290CGLYA3442.104−1.085−14.3961.0026.01
ATOM291OGLYA3443.046−1.873−14.4631.0028.72
ATOM292NLEUA3452.2570.232−14.4711.0026.97
ATOM293CALEUA3453.5760.839−14.6081.0031.15
ATOM294CBLEUA3453.4592.361−14.7531.0030.06
ATOM295CGLEUA3452.7652.924−15.9951.0033.50
ATOM296CD1LEUA3452.9014.439−15.9991.0033.52
ATOM297CD2LEUA3453.3792.324−17.2571.0033.22
ATOM298CLEUA3454.4330.534−13.3831.0030.31
ATOM299OLEUA3455.5640.061−13.5051.0032.80
ATOM300NLEUA3463.8840.813−12.2051.0027.83
ATOM301CALEUA3464.5950.596−10.9471.0026.19
ATOM302CBLEUA3463.7291.063−9.7831.0024.51
ATOM303CGLEUA3463.4832.569−9.6821.0026.33
ATOM304CD1LEUA3462.6232.844−8.4631.0027.33
ATOM305CD2LEUA3464.8093.317−9.5871.0024.89
ATOM306CLEUA3465.032−0.848−10.7071.0025.72
ATOM307OLEUA3466.181−1.102−10.3451.0029.86
ATOM308NTHRA3474.117−1.793−10.8911.0023.80
ATOM309CATHRA3474.436−3.196−10.6741.0023.91
ATOM310CBTHRA3473.164−4.058−10.6411.0026.39
ATOM311OG1THRA3472.421−3.860−11.8491.0024.57
ATOM312CG2THRA3472.301−3.682−9.4441.0023.98
ATOM313CTHRA3475.366−3.734−11.7561.0026.17
ATOM314OTHRA3476.176−4.622−11.4961.0027.44
ATOM315NASNA3485.242−3.197−12.9701.0025.48
ATOM316CAASNA3486.092−3.617−14.0821.0023.77
ATOM317CBASNA3485.657−2.926−15.3851.0024.59
ATOM318CGASNA3486.522−3.302−16.5711.0029.93
ATOM319OD1ASNA3487.616−2.799−16.7711.0024.81
ATOM320ND2ASNA3486.010−4.236−17.3911.0032.61
ATOM321CASNA3487.532−3.229−13.7411.0022.82
ATOM322OASNA3488.453−4.027−13.8701.0018.83
ATOM323NLEUA3497.711−1.993−13.2881.0022.58
ATOM324CALEUA3499.030−1.507−12.9141.0021.85
ATOM325CBLEUA3498.929−0.028−12.5361.0022.00
ATOM326CGLEUA34910.1550.673−11.9531.0023.64
ATOM327CD1LEUA34911.2240.826−13.0171.0019.35
ATOM328CD2LEUA3499.7262.040−11.4151.0021.97
ATOM329CLEUA3499.564−2.335−11.7341.0022.94
ATOM330OLEUA34910.724−2.749−11.7171.0023.97
ATOM331NALAA3508.705−2.591−10.7561.0021.67
ATOM332CAALAA3509.113−3.356−9.5861.0021.83
ATOM333CBALAA3507.963−3.441−8.5931.0018.95
ATOM334CALAA3509.568−4.757−9.9851.0021.90
ATOM335OALAA35010.625−5.221−9.5541.0024.15
ATOM336NASPA3518.767−5.423−10.8101.0023.24
ATOM337CAASPA3519.093−6.772−11.2591.0025.87
ATOM338CBASPA3518.028−7.274−12.2391.0027.03
ATOM339CGASPA3518.103−8.772−12.4581.0031.64
ATOM340OD1ASPA3518.217−9.196−13.6281.0035.06
ATOM341OD2ASPA3518.049−9.525−11.4641.0036.86
ATOM342CASPA35110.469−6.825−11.9121.0022.36
ATOM343OASPA35111.219−7.773−11.7021.0025.15
ATOM344NARGA35210.810−5.808−12.6971.0023.58
ATOM345CAARGA35212.115−5.787−13.3471.0021.07
ATOM346CBARGA35212.120−4.785−14.5071.0021.02
ATOM347CGARGA35211.539−5.352−15.7971.0020.44
ATOM348CDARGA35211.554−4.319−16.9151.0020.43
ATOM349NEARGA35210.592−3.245−16.6871.0019.85
ATOM350CZARGA35210.910−1.954−16.6411.0019.69
ATOM351NH1ARGA35212.172−1.564−16.8131.0017.36
ATOM352NH2ARGA3529.962−1.049−16.4411.0021.88
ATOM353CARGA35213.223−5.442−12.3501.0022.11
ATOM354OARGA35214.346−5.945−12.4541.0024.13
ATOM355NGLUA35312.909−4.587−11.3831.0018.66
ATOM356CAGLUA35313.888−4.206−10.3761.0019.08
ATOM357CBGLUA35313.317−3.102−9.4831.0021.62
ATOM358CGGLUA35313.295−1.718−10.1141.0020.97
ATOM359CDGLUA35312.832−0.648−9.1291.0023.84
ATOM360OE1GLUA35311.611−0.531−8.9261.0024.76
ATOM361OE2GLUA35313.686−0.066−8.5571.0024.95
ATOM362CGLUA35314.246−5.423−9.5121.0020.14
ATOM363OGLUA35315.398−5.600−9.1041.0019.40
ATOM364NLEUA35413.246−6.257−9.2351.0019.54
ATOM365CALEUA35413.434−7.452−8.4151.0021.77
ATOM366CBLEUA35412.107−8.209−8.2701.0023.09
ATOM367CGLEUA35411.160−7.606−7.2231.0025.00
ATOM368CD1LEUA3549.720−8.013−7.5101.0023.49
ATOM369CD2LEUA35411.584−8.069−5.8391.0023.31
ATOM370CLEUA35414.500−8.386−8.9811.0023.21
ATOM371OLEUA35415.255−9.007−8.2341.0022.44
ATOM372NVALA35514.560−8.490−10.3021.0022.52
ATOM373CAVALA35515.551−9.343−10.9351.0021.66
ATOM374CBVALA35515.353−9.365−12.4661.0024.35
ATOM375CG1VALA35516.435−10.214−13.1191.0028.16
ATOM376CG2VALA35513.957−9.886−12.7981.0021.59
ATOM377CVALA35516.944−8.811−10.6061.0023.74
ATOM378OVALA35517.857−9.581−10.2911.0023.51
ATOM379NHISA35617.105−7.489−10.6691.0021.27
ATOM380CAHISA35618.392−6.861−10.3691.0021.31
ATOM381CBHISA35618.384−5.390−10.8111.0019.87
ATOM382CGHISA35618.494−5.205−12.2951.0021.77
ATOM383CD2HISA35617.543−5.048−13.2481.0021.66
ATOM384ND1HISA35619.704−5.177−12.9551.0021.11
ATOM385CE1HISA35619.496−5.011−14.2491.0024.96
ATOM386NE2HISA35618.192−4.931−14.4551.0018.37
ATOM387CHISA35618.702−6.947−8.8751.0021.41
ATOM388OHISA35619.864−7.111−8.4651.0021.88
ATOM389NMETA35717.660−6.843−8.0581.0021.84
ATOM390CAMETA35717.837−6.906−6.6101.0021.51
ATOM391CBMETA35716.503−6.668−5.8981.0017.60
ATOM392CGMETA35716.629−6.579−4.3691.0019.36
ATOM393SDMETA35715.051−6.755−3.5311.0023.64
ATOM394CEMETA35714.189−5.332−4.1631.0023.13
ATOM395CMETA35718.411−8.259−6.1921.0023.69
ATOM396OMETA35719.337−8.328−5.3891.0024.41
ATOM397NILEA35817.856−9.331−6.7461.0027.14
ATOM398CAILEA35818.314−10.672−6.4251.0028.79
ATOM399CBILEA35817.529−11.725−7.2321.0032.42
ATOM400CG2ILEA35818.267−13.064−7.2201.0032.77
ATOM401CG1ILEA35816.125−11.880−6.6441.0031.94
ATOM402CD1ILEA35815.062−12.196−7.6801.0034.85
ATOM403CILEA35819.801−10.802−6.7281.0028.75
ATOM404OILEA35820.569−11.305−5.9121.0031.60
ATOM405NASNA35920.207−10.325−7.8971.0027.91
ATOM406CAASNA35921.601−10.401−8.2931.0029.16
ATOM407CBASNA35921.721−10.172−9.8011.0031.88
ATOM408CGASNA35921.253−11.381−10.5991.0039.34
ATOM409OD1ASNA35921.916−12.422−10.6121.0041.27
ATOM410ND2ASNA35920.102−11.255−11.2531.0038.58
ATOM411CASNA35922.476−9.436−7.5101.0030.75
ATOM412OASNA35923.686−9.629−7.4121.0033.35
ATOM413NTRPA36021.872−8.400−6.9401.0030.07
ATOM414CATRPA36022.634−7.451−6.1321.0027.87
ATOM415CBTRPA36021.849−6.150−5.9481.0024.80
ATOM416CGTRPA36022.196−5.392−4.6911.0023.04
ATOM417CD2TRPA36021.501−5.443−3.4381.0019.83
ATOM418CE2TRPA36022.147−4.543−2.5641.0022.31
ATOM419CE3TRPA36020.392−6.165−2.9721.0020.09
ATOM420CD1TRPA36023.212−4.488−4.5291.0018.99
ATOM421NE1TRPA36023.187−3.974−3.2551.0021.17
ATOM422CZ2TRPA36021.721−4.340−1.2431.0020.43
ATOM423CZ3TRPA36019.968−5.965−1.6611.0020.12
ATOM424CH2TRPA36020.635−5.057−0.8121.0018.54
ATOM425CTRPA36022.892−8.099−4.7661.0024.88
ATOM426OTRPA36023.978−7.980−4.1981.0025.00
ATOM427NALAA36121.879−8.789−4.2521.0024.08
ATOM428CAALAA36121.972−9.462−2.9581.0026.06
ATOM429CBALAA36120.676−10.203−2.6721.0020.27
ATOM430CALAA36123.161−10.433−2.8971.0028.44
ATOM431OALAA36123.843−10.531−1.8761.0028.95
ATOM432NLYSA36223.414−11.144−3.9921.0031.41
ATOM433CALYSA36224.530−12.097−4.0471.0033.33
ATOM434CBLYSA36224.564−12.824−5.3901.0034.81
ATOM435CGLYSA36223.319−13.608−5.7561.0036.27
ATOM436CDLYSA36223.458−14.178−7.1671.0038.30
ATOM437CELYSA36222.369−15.193−7.4721.0040.94
ATOM438NZLYSA36222.111−15.322−8.9371.0042.49
ATOM439CLYSA36225.854−11.351−3.8931.0034.17
ATOM440OLYSA36226.880−11.977−3.5951.0035.40
ATOM441NAARGA36325.826−10.059−4.0950.5034.23
ATOM442NBARGA36325.826−10.059−4.0950.5034.03
ATOM443CAAARGA36327.035−9.254−3.9870.5033.25
ATOM444CABARGA36327.035−9.254−3.9870.5032.83
ATOM445CBAARGA36327.031−8.153−5.0440.5034.67
ATOM446CBBARGA36327.031−8.153−5.0450.5034.20
ATOM447CGAARGA36326.933−8.654−6.4780.5036.32
ATOM448CGBARGA36326.930−8.654−6.4800.5035.56
ATOM449CDAARGA36327.745−7.775−7.4150.5038.39
ATOM450CDBARGA36327.752−7.781−7.4140.5037.18
ATOM451NEAARGA36329.171−7.793−7.0910.5039.98
ATOM452NEBARGA36327.195−7.725−8.7620.5037.39
ATOM453CZAARGA36330.086−7.038−7.6920.5040.54
ATOM454CZBARGA36327.905−7.457−9.8550.5040.02
ATOM455NH1AARGA36329.735−6.218−8.6750.5038.13
ATOM456NH1BARGA36329.205−7.191−9.7610.5040.42
ATOM457NH2AARGA36331.358−7.123−7.3260.5043.19
ATOM458NH2BARGA36327.311−7.436−11.0410.5038.91
ATOM459CAARGA36327.207−8.630−2.6100.5033.28
ATOM460CBARGA36327.207−8.630−2.6100.5032.81
ATOM461OAARGA36328.223−7.992−2.3440.5034.18
ATOM462OBARGA36328.223−7.992−2.3450.5033.43
ATOM463NVALA36426.215−8.798−1.7401.0033.12
ATOM464CAVALA36426.288−8.240−0.3891.0033.63
ATOM465CBVALA36424.898−8.1780.2921.0034.97
ATOM466CG1VALA36425.036−7.6081.7001.0035.44
ATOM467CG2VALA36423.946−7.328−0.5321.0036.69
ATOM468CVALA36427.184−9.1570.4281.0034.27
ATOM469OVALA36426.878−10.3410.6031.0034.95
ATOM470NPROA36528.306−8.6260.9351.0036.08
ATOM471CDPROA36528.775−7.2350.7931.0034.84
ATOM472CAPROA36529.231−9.4421.7331.0037.82
ATOM473CBPROA36530.110−8.4082.4301.0034.31
ATOM474CGPROA36530.127−7.2471.4751.0037.77
ATOM475CPROA36528.538−10.3732.7201.0037.61
ATOM476OPROA36527.692−9.9453.5071.0037.74
ATOM477NGLYA36628.890−11.6542.6541.0039.04
ATOM478CAGLYA36628.307−12.6353.5541.0038.27
ATOM479CGLYA36626.991−13.2643.1381.0039.32
ATOM480OGLYA36626.638−14.3363.6351.0039.53
ATOM481NPHEA36726.246−12.6152.2361.0038.60
ATOM482CAPHEA36724.960−13.1481.7831.0036.36
ATOM483CBPHEA36724.281−12.1780.8081.0032.10
ATOM484CGPHEA36722.827−12.4730.5811.0030.12
ATOM485CD1PHEA36722.401−13.083−0.5961.0028.95
ATOM486CD2PHEA36721.882−12.1761.5631.0026.18
ATOM487CE1PHEA36721.050−13.400−0.7921.0029.42
ATOM488CE2PHEA36720.535−12.4911.3731.0027.60
ATOM489CZPHEA36720.118−13.1030.1961.0026.81
ATOM490CPHEA36725.072−14.5191.1171.0036.82
ATOM491OPHEA36724.244−15.3981.3591.0036.55
ATOM492NVALA36826.088−14.6940.2761.0038.28
ATOM493CAVALA36826.289−15.965−0.4201.0042.34
ATOM494CBVALA36827.386−15.850−1.5041.0041.78
ATOM495CG1VALA36826.972−14.831−2.5501.0044.60
ATOM496CG2VALA36828.707−15.457−0.8731.0042.23
ATOM497CVALA36826.664−17.1000.5331.0043.85
ATOM498OVALA36826.469−18.2740.2161.0044.85
ATOM499NASPA36927.199−16.7501.6991.0044.93
ATOM500CAASPA36927.579−17.7552.6881.0044.96
ATOM501CBASPA36928.336−17.1063.8491.0043.76
ATOM502CGASPA36929.608−16.4133.4041.0043.04
ATOM503OD1ASPA36930.121−15.5704.1671.0044.32
ATOM504OD2ASPA36930.097−16.7092.2931.0046.76
ATOM505CASPA36926.340−18.4653.2281.0045.89
ATOM506OASPA36926.360−19.6713.4751.0048.61
ATOM507NLEUA37025.261−17.7143.4071.0043.59
ATOM508CALEUA37024.020−18.2793.9241.0044.24
ATOM509CBLEUA37022.980−17.1734.1101.0041.42
ATOM510CGLEUA37023.404−16.0155.0141.0041.45
ATOM511CD1LEUA37022.219−15.0955.2451.0042.25
ATOM512CD2LEUA37023.931−16.5526.3321.0038.35
ATOM513CLEUA37023.449−19.3603.0131.0044.03
ATOM514OLEUA37023.773−19.4231.8291.0043.63
ATOM515NTHRA37122.593−20.2063.5751.0044.29
ATOM516CATHRA37121.968−21.2722.8061.0044.84
ATOM517CBTHRA37121.293−22.3023.7301.0045.65
ATOM518OG1THRA37120.262−21.6634.4951.0046.43
ATOM519CG2THRA37122.314−22.9034.6771.0046.48
ATOM520CTHRA37120.923−20.6841.8641.0044.93
ATOM521OTHRA37120.418−19.5852.0921.0044.36
ATOM522NLEUA37220.607−21.4180.8041.0043.83
ATOM523CALEUA37219.624−20.971−0.1661.0044.62
ATOM524CBLEUA37219.407−22.043−1.2371.0047.17
ATOM525CGLEUA37218.512−21.690−2.4291.0046.91
ATOM526CD1LEUA37219.005−20.417−3.0981.0048.73
ATOM527CD2LEUA37218.521−22.844−3.4201.0051.12
ATOM528CLEUA37218.307−20.6440.5121.0044.84
ATOM529OLEUA37217.705−19.6020.2611.0043.25
ATOM530NHISA37317.849−21.5581.3821.0043.14
ATOM531CAHISA37316.599−21.3532.1001.0042.23
ATOM532CBHISA37316.318−22.5253.0621.0045.38
ATOM533CGHISA37315.114−22.3153.9341.0051.43
ATOM534CD2HISA37313.808−22.6213.7431.0054.99
ATOM535ND1HISA37315.187−21.7165.1741.0054.26
ATOM536CE1HISA37313.979−21.6635.7091.0053.77
ATOM537NE2HISA37313.124−22.2064.8611.0055.27
ATOM538CHISA37316.665−20.0472.8851.0039.78
ATOM539OHISA37315.677−19.3242.9711.0037.71
ATOM540NASPA37417.839−19.7383.4401.0036.38
ATOM541CAASPA37418.020−18.5164.2191.0037.21
ATOM542CBASPA37419.287−18.6205.0731.0038.17
ATOM543CGASPA37419.064−19.4256.3441.0041.47
ATOM544OD1ASPA37417.896−19.5436.7721.0037.09
ATOM545OD2ASPA37420.052−19.9406.9121.0044.40
ATOM546CASPA37418.083−17.2773.3261.0037.19
ATOM547OASPA37417.598−16.2083.6961.0038.13
ATOM548NGLNA37518.688−17.4312.1521.0033.13
ATOM549CAGLNA37518.788−16.3391.1981.0031.94
ATOM550CBGLNA37519.634−16.756−0.0011.0028.81
ATOM551CGGLNA37521.125−16.5700.1891.0031.71
ATOM552CDGLNA37521.920−17.222−0.9221.0034.49
ATOM553OE1GLNA37521.478−17.267−2.0671.0036.09
ATOM554NE2GLNA37523.097−17.736−0.5881.0040.32
ATOM555CGLNA37517.379−16.0090.7301.0031.50
ATOM556OGLNA37516.990−14.8400.6531.0027.42
ATOM557NVALA37616.617−17.0560.4291.0030.38
ATOM558CAVALA37615.242−16.907−0.0271.0033.50
ATOM559CBVALA37614.588−18.286−0.2861.0030.57
ATOM560CG1VALA37613.093−18.122−0.5161.0033.14
ATOM561CG2VALA37615.232−18.952−1.4851.0030.79
ATOM562CVALA37614.393−16.1591.0021.0033.80
ATOM563OVALA37613.653−15.2370.6611.0034.89
ATOM564NHISA37714.500−16.5682.2611.0033.35
ATOM565CAHISA37713.730−15.9413.3291.0032.81
ATOM566CBHISA37713.966−16.6944.6441.0035.24
ATOM567CGHISA37713.429−15.9895.8511.0040.15
ATOM568CD2HISA37714.054−15.4956.9461.0040.86
ATOM569ND1HISA37712.090−15.7036.0121.0043.08
ATOM570CE1HISA37711.913−15.0627.1541.0042.44
ATOM571NE2HISA37713.089−14.9227.7401.0044.85
ATOM572CHISA37714.058−14.4543.5071.0028.63
ATOM573OHISA37713.158−13.6193.6131.0029.20
ATOM574NLEUA37815.343−14.1253.5441.0024.41
ATOM575CALEUA37815.759−12.7383.7211.0023.21
ATOM576CBLEUA37817.289−12.6503.7431.0020.98
ATOM577CGLEUA37817.960−13.1905.0161.0024.22
ATOM578CD1LEUA37819.471−13.0414.9241.0021.07
ATOM579CD2LEUA37817.431−12.4466.2211.0020.24
ATOM580CLEUA37815.190−11.8272.6301.0024.78
ATOM581OLEUA37814.638−10.7662.9221.0022.09
ATOM582NLEUA37915.321−12.2421.3741.0024.13
ATOM583CALEUA37914.812−11.4470.2621.0025.02
ATOM584CBLEUA37915.307−12.025−1.0621.0027.12
ATOM585CGLEUA37916.724−11.600−1.4371.0024.39
ATOM586CD1LEUA37917.299−12.557−2.4701.0027.58
ATOM587CD2LEUA37916.679−10.178−1.9831.0029.05
ATOM588CLEUA37913.287−11.3550.2461.0027.61
ATOM589OLEUA37912.726−10.301−0.0621.0026.16
ATOM590NGLUA38012.616−12.4540.5761.0025.65
ATOM591CAGLUA38011.154−12.4710.5921.0026.85
ATOM592CBGLUA38010.640−13.8820.8711.0029.38
ATOM593CGGLUA38010.718−14.796−0.3311.0035.58
ATOM594CDGLUA38010.228−16.194−0.0251.0039.31
ATOM595OE1GLUA38010.142−17.008−0.9671.0042.89
ATOM596OE2GLUA3809.927−16.4781.1531.0039.45
ATOM597CGLUA38010.604−11.5261.6491.0025.43
ATOM598OGLUA3809.551−10.9251.4691.0027.75
ATOM599NCYSA38111.324−11.4002.7531.0025.57
ATOM600CACYSA38110.907−10.5303.8431.0026.46
ATOM601CBCYSA38111.570−11.0005.1491.0031.46
ATOM602SGCYSA38111.305−9.9466.6231.0045.32
ATOM603CCYSA38111.262−9.0593.5891.0024.77
ATOM604OCYSA38110.516−8.1663.9751.0025.01
ATOM605NALAA38212.377−8.8152.9031.0022.23
ATOM606CAALAA38212.855−7.4492.6811.0021.83
ATOM607CBALAA38214.319−7.3833.0951.0021.56
ATOM608CALAA38212.705−6.7781.3111.0019.78
ATOM609OALAA38212.996−5.5871.1821.0017.01
ATOM610NTRPA38312.261−7.5070.2941.0017.61
ATOM611CATRPA38312.164−6.915−1.0361.0018.06
ATOM612CBTRPA38311.580−7.928−2.0351.0020.28
ATOM613CGTRPA38310.105−8.201−1.9191.0020.50
ATOM614CD2TRPA3839.049−7.509−2.5991.0022.48
ATOM615CE2TRPA3837.836−8.138−2.2381.0020.41
ATOM616CE3TRPA3839.012−6.420−3.4821.0022.06
ATOM617CD1TRPA3839.506−9.189−1.1901.0023.38
ATOM618NE1TRPA3838.142−9.159−1.3771.0022.59
ATOM619CZ2TRPA3836.598−7.713−2.7241.0021.98
ATOM620CZ3TRPA3837.780−5.998−3.9681.0025.50
ATOM621CH2TRPA3836.589−6.647−3.5871.0023.11
ATOM622CTRPA38311.448−5.564−1.1701.0019.18
ATOM623OTRPA38311.972−4.663−1.8241.0019.27
ATOM624NLEUA38410.273−5.396−0.5671.0018.32
ATOM625CALEUA3849.586−4.118−0.7191.0016.38
ATOM626CBLEUA3848.125−4.218−0.2581.0016.79
ATOM627CGLEUA3847.211−3.013−0.5771.0018.39
ATOM628CD1LEUA3847.464−2.485−1.9951.0013.91
ATOM629CD2LEUA3845.750−3.432−0.4101.0018.38
ATOM630CLEUA38410.324−3.0270.0511.0018.80
ATOM631OLEUA38410.334−1.870−0.3571.0020.90
ATOM632NGLUA38510.949−3.4041.1631.0018.61
ATOM633CAGLUA38511.718−2.4621.9701.0019.58
ATOM634CBGLUA38512.274−3.1543.2131.0017.43
ATOM635CGGLUA38511.292−3.2374.3571.0022.92
ATOM636CDGLUA38511.963−3.6765.6401.0025.83
ATOM637OE1GLUA38512.431−2.7996.3911.0023.69
ATOM638OE2GLUA38512.027−4.8975.8891.0027.64
ATOM639CGLUA38512.890−1.9341.1561.0019.46
ATOM640OGLUA38513.206−0.7431.1961.0015.04
ATOM641NILEA38613.539−2.8420.4311.0013.32
ATOM642CAILEA38614.685−2.484−0.3881.0015.01
ATOM643CBILEA38615.475−3.763−0.8071.0017.43
ATOM644CG2ILEA38616.544−3.424−1.8491.0017.99
ATOM645CG1ILEA38616.185−4.3380.4321.0020.31
ATOM646CD1ILEA38616.682−5.7660.2841.0023.97
ATOM647CILEA38614.273−1.645−1.5981.0016.10
ATOM648OILEA38614.993−0.724−2.0041.0017.42
ATOM649NLEUA38713.112−1.944−2.1671.0017.61
ATOM650CALEUA38712.620−1.173−3.3041.0018.20
ATOM651CBLEUA38711.359−1.814−3.8821.0017.51
ATOM652CGLEUA38711.519−3.064−4.7471.0026.37
ATOM653CD1LEUA38710.173−3.406−5.3951.0024.63
ATOM654CD2LEUA38712.589−2.824−5.8081.0021.58
ATOM655CLEUA38712.2830.249−2.8381.0017.60
ATOM656OLEUA38712.5711.224−3.5301.0017.15
ATOM657NMETA38811.6770.357−1.6601.0017.65
ATOM658CAMETA38811.2861.656−1.1211.0018.49
ATOM659CBMETA38810.3021.4600.0341.0019.65
ATOM660CGMETA3888.8931.105−0.4351.0015.12
ATOM661SDMETA3887.7440.7690.9101.0018.73
ATOM662CEMETA3886.1630.9080.0481.0018.34
ATOM663CMETA38812.4512.553−0.6911.0022.62
ATOM664OMETA38812.4173.767−0.9281.0022.49
ATOM665NILEA38913.4821.988−0.0641.0021.45
ATOM666CAILEA38914.6042.8310.3311.0018.54
ATOM667CBILEA38915.5902.1081.2991.0019.35
ATOM668CG2ILEA38916.3620.9980.5781.0015.50
ATOM669CG1ILEA38916.5563.1421.8891.0021.95
ATOM670CD1ILEA38917.3732.6583.0801.0015.86
ATOM671CILEA38915.3333.322−0.9221.0018.67
ATOM672OILEA38915.8134.453−0.9701.0019.75
ATOM673NGLYA39015.4102.477−1.9431.0020.58
ATOM674CAGLYA39016.0492.895−3.1831.0019.33
ATOM675CGLYA39015.2434.021−3.8191.0017.48
ATOM676OGLYA39015.8014.994−4.3181.0021.87
ATOM677NLEUA39113.9203.888−3.7871.0019.17
ATOM678CALEUA39113.0184.887−4.3431.0021.50
ATOM679CBLEUA39111.5614.420−4.1941.0018.25
ATOM680CGLEUA39110.4805.497−4.3421.0021.98
ATOM681CD1LEUA39110.5796.156−5.7251.0021.39
ATOM682CD2LEUA3919.1154.868−4.1481.0017.15
ATOM683CLEUA39113.2086.216−3.6201.0023.27
ATOM684OLEUA39113.4407.255−4.2431.0023.60
ATOM685NVALA39213.1226.170−2.2951.0023.04
ATOM686CAVALA39213.2827.357−1.4691.0024.42
ATOM687CBVALA39213.1866.9930.0421.0027.38
ATOM688CG1VALA39213.7338.1290.8971.0030.37
ATOM689CG2VALA39211.7396.7120.4141.0023.48
ATOM690CVALA39214.6268.014−1.7541.0027.55
ATOM691OVALA39214.7289.242−1.8321.0027.50
ATOM692NTRPA39315.6527.186−1.9241.0023.65
ATOM693CATRPA39316.9997.670−2.2041.0024.76
ATOM694CBTRPA39317.9776.491−2.1991.0022.86
ATOM695CGTRPA39319.2876.784−2.8571.0025.90
ATOM696CD2TRPA39320.3417.605−2.3391.0028.09
ATOM697CE2TRPA39321.3757.612−3.3021.0029.94
ATOM698CE3TRPA39320.5128.335−1.1541.0030.20
ATOM699CD1TRPA39319.7106.339−4.0771.0026.55
ATOM700NE1TRPA39320.9636.833−4.3511.0030.64
ATOM701CZ2TRPA39322.5668.323−3.1201.0032.43
ATOM702CZ3TRPA39321.6989.044−0.9711.0034.58
ATOM703CH2TRPA39322.7099.030−1.9501.0036.54
ATOM704CTRPA39317.0828.414−3.5471.0025.02
ATOM705OTRPA39317.7679.435−3.6501.0020.97
ATOM706NARGA39416.3997.897−4.5681.0023.06
ATOM707CAARGA39416.4128.531−5.8901.0025.97
ATOM708CBARGA39415.7767.633−6.9651.0024.05
ATOM709CGARGA39416.2436.195−7.0241.0026.05
ATOM710CDARGA39415.8305.551−8.3521.0022.70
ATOM711NEARGA39414.4435.071−8.3631.0020.71
ATOM712CZARGA39414.0533.912−7.8411.0021.26
ATOM713NH1ARGA39414.9443.108−7.2671.0020.09
ATOM714NH2ARGA39412.7833.544−7.9071.0021.26
ATOM715CARGA39415.6229.833−5.8791.0023.40
ATOM716OARGA39415.88910.729−6.6771.0028.61
ATOM717NSERA39514.6389.924−4.9881.0026.65
ATOM718CASERA39513.77611.104−4.9021.0027.46
ATOM719CBSERA39512.39510.696−4.3821.0026.70
ATOM720OGSERA39511.9169.530−5.0291.0022.95
ATOM721CSERA39514.31612.240−4.0331.0031.45
ATOM722OSERA39513.72613.324−3.9771.0028.11
ATOM723NMETA39615.43711.986−3.3681.0033.83
ATOM724CAMETA39616.06112.954−2.4751.0038.83
ATOM725CBMETA39617.46612.483−2.1121.0039.47
ATOM726CGMETA39617.58511.919−0.7151.0041.37
ATOM727SDMETA39619.19212.2620.0041.0042.20
ATOM728CEMETA39620.26311.996−1.4041.0042.84
ATOM729CMETA39616.14314.376−3.0181.0040.69
ATOM730OMETA39615.63715.316−2.4031.0038.85
ATOM731NGLUA39716.79414.526−4.1661.0042.19
ATOM732CAGLUA39716.97115.831−4.7901.0044.80
ATOM733CBGLUA39718.18415.785−5.7291.0046.02
ATOM734CGGLUA39717.88315.189−7.0961.0054.42
ATOM735CDGLUA39719.11714.665−7.8101.0059.40
ATOM736OE1GLUA39719.21913.430−7.9901.0060.63
ATOM737OE2GLUA39719.98015.485−8.1961.0062.71
ATOM738CGLUA39715.73516.322−5.5541.0042.94
ATOM739OGLUA39715.83017.229−6.3761.0044.68
ATOM740NHISA39814.57915.728−5.2801.0040.82
ATOM741CAHISA39813.34216.118−5.9501.0039.21
ATOM742CBHISA39812.92415.043−6.9561.0039.05
ATOM743CGHISA39813.87014.886−8.1041.0041.57
ATOM744CD2HISA39813.90415.484−9.3181.0039.28
ATOM745ND1HISA39814.94014.017−8.0741.0041.85
ATOM746CE1HISA39815.59214.086−9.2201.0040.88
ATOM747NE2HISA39814.98514.969−9.9931.0042.30
ATOM748CHISA39812.21616.332−4.9441.0037.04
ATOM749OHISA39811.28215.535−4.8641.0036.51
ATOM750NPROA39912.28317.427−4.1711.0039.19
ATOM751CDPROA39913.32818.467−4.1981.0035.36
ATOM752CAPROA39911.24317.709−3.1731.0037.10
ATOM753CBPROA39911.60319.101−2.6541.0037.86
ATOM754CGPROA39913.05019.267−2.9631.0035.83
ATOM755CPROA3999.82817.663−3.7441.0037.02
ATOM756OPROA3999.55418.249−4.7891.0038.52
ATOM757NGLYA4008.93816.954−3.0571.0033.58
ATOM758CAGLYA4007.55916.865−3.5031.0032.12
ATOM759CGLYA4007.23015.706−4.4281.0032.43
ATOM760OGLYA4006.06315.344−4.5741.0033.21
ATOM761NLYSA4018.23715.112−5.0551.0031.35
ATOM762CALYSA4017.97214.007−5.9661.0030.75
ATOM763CBLYSA4018.23514.430−7.4151.0035.43
ATOM764CGLYSA4018.13015.927−7.6751.0035.15
ATOM765CDLYSA4019.09616.353−8.7741.0036.88
ATOM766CELYSA4018.73317.721−9.3311.0036.71
ATOM767NZLYSA4017.29518.027−9.1161.0034.22
ATOM768CLYSA4018.76812.746−5.6771.0030.97
ATOM769OLYSA4019.80912.776−5.0061.0027.60
ATOM770NLEUA4028.25611.635−6.1971.0027.28
ATOM771CALEUA4028.88910.334−6.0501.0029.07
ATOM772CBLEUA4027.8669.294−5.5901.0022.55
ATOM773CGLEUA4027.2659.555−4.2071.0024.94
ATOM774CD1LEUA4026.1268.583−3.9371.0019.32
ATOM775CD2LEUA4028.3559.416−3.1571.0021.54
ATOM776CLEUA4029.4489.948−7.4141.0028.78
ATOM777OLEUA4028.7049.836−8.3891.0029.98
ATOM778NLEUA40310.7619.770−7.4871.0027.57
ATOM779CALEUA40311.3939.400−8.7441.0027.17
ATOM780CBLEUA40312.8259.937−8.8161.0026.95
ATOM781CGLEUA40313.40110.027−10.2381.0030.42
ATOM782CD1LEUA40314.51911.046−10.2881.0030.76
ATOM783CD2LEUA40313.9158.665−10.6761.0033.11
ATOM784CLEUA40311.4197.891−8.9011.0024.78
ATOM785OLEUA40312.4287.257−8.6191.0024.68
ATOM786NPHEA40410.3067.319−9.3441.0023.11
ATOM787CAPHEA40410.2395.881−9.5461.0026.93
ATOM788CBPHEA4048.8265.470−9.9461.0027.04
ATOM789CGPHEA4047.8505.513−8.8161.0027.89
ATOM790CD1PHEA4047.0286.623−8.6311.0026.20
ATOM791CD2PHEA4047.7504.444−7.9251.0023.10
ATOM792CE1PHEA4046.1166.668−7.5731.0025.29
ATOM793CE2PHEA4046.8454.481−6.8701.0021.01
ATOM794CZPHEA4046.0265.595−6.6931.0022.91
ATOM795CPHEA40411.2325.507−10.6371.0026.04
ATOM796OPHEA40411.8824.464−10.5781.0027.27
ATOM797NALAA40511.3486.383−11.6261.0028.80
ATOM798CAALAA40512.2716.195−12.7401.0029.21
ATOM799CBALAA40511.6505.287−13.8061.0026.89
ATOM800CALAA40512.5497.578−13.3171.0030.23
ATOM801OALAA40511.7708.508−13.1091.0027.38
ATOM802NPROA40613.6727.737−14.0321.0030.05
ATOM803CDPROA40614.7126.745−14.3521.0026.31
ATOM804CAPROA40613.9779.053−14.6041.0032.10
ATOM805CBPROA40615.2328.800−15.4381.0031.28
ATOM806CGPROA40615.8657.602−14.7761.0031.44
ATOM807CPROA40612.8209.589−15.4361.0032.58
ATOM808OPROA40612.60510.796−15.5071.0032.58
ATOM809NASNA40712.0638.690−16.0531.0032.86
ATOM810CAASNA40710.9359.119−16.8651.0032.78
ATOM811CBASNA40710.9508.418−18.2281.0034.73
ATOM812CGASNA40710.8846.907−18.1211.0035.37
ATOM813OD1ASNA40711.1896.317−17.0771.0030.24
ATOM814ND2ASNA40710.4866.268−19.2151.0034.08
ATOM815CASNA4079.6058.901−16.1661.0034.90
ATOM816OASNA4078.5498.897−16.7981.0036.09
ATOM817NLEUA4089.6608.724−14.8511.0033.56
ATOM818CALEUA4088.4528.544−14.0611.0035.59
ATOM819CBLEUA4088.1417.062−13.8511.0033.81
ATOM820CGLEUA4086.6966.823−13.3971.0036.44
ATOM821CD1LEUA4085.7467.479−14.3901.0034.14
ATOM822CD2LEUA4086.4065.334−13.2871.0032.96
ATOM823CLEUA4088.6079.245−12.7171.0038.03
ATOM824OLEUA4088.8808.614−11.6951.0036.38
ATOM825NLEUA4098.44110.563−12.7411.0037.87
ATOM826CALEUA4098.54811.395−11.5531.0037.95
ATOM827CBLEUA4099.37312.636−11.8771.0039.52
ATOM828CGLEUA40910.02313.399−10.7281.0042.46
ATOM829CD1LEUA40911.10012.547−10.0821.0043.24
ATOM830CD2LEUA40910.61414.691−11.2661.0046.05
ATOM831CLEUA4097.13211.792−11.1631.0037.13
ATOM832OLEUA4096.48212.546−11.8821.0035.70
ATOM833NLEUA4106.65411.284−10.0301.0035.29
ATOM834CALEUA4105.29711.576−9.5831.0033.33
ATOM835CBLEUA4104.50310.277−9.4491.0029.37
ATOM836CGLEUA4104.6459.238−10.5601.0032.75
ATOM837CD1LEUA4104.0267.925−10.1041.0029.16
ATOM838CD2LEUA4103.9589.744−11.8191.0030.70
ATOM839CLEUA4105.20712.332−8.2611.0035.14
ATOM840OLEUA4106.07812.214−7.4001.0036.94
ATOM841NASPA4114.14113.108−8.1051.0034.76
ATOM842CAASPA4113.93313.843−6.8731.0035.40
ATOM843CBASPA4113.73315.341−7.1441.0040.02
ATOM844CGASPA4112.47115.645−7.9281.0041.32
ATOM845OD1ASPA4111.57014.785−8.0011.0045.03
ATOM846OD2ASPA4112.38316.764−8.4741.0045.01
ATOM847CASPA4112.72713.234−6.1791.0036.10
ATOM848OASPA4112.03312.395−6.7621.0034.08
ATOM849NARGA4122.48013.647−4.9401.0035.99
ATOM850CAARGA4121.37513.099−4.1691.0039.37
ATOM851CBARGA4121.26013.824−2.8251.0039.75
ATOM852CGARGA4120.56215.168−2.8701.0040.49
ATOM853CDARGA4120.45415.736−1.4651.0040.65
ATOM854NEARGA412−0.26114.826−0.5771.0037.48
ATOM855CZARGA412−1.57414.855−0.3841.0042.84
ATOM856NH1ARGA412−2.31615.754−1.0241.0040.82
ATOM857NH2ARGA412−2.15013.9860.4381.0038.32
ATOM858CARGA4120.03413.108−4.8891.0039.80
ATOM859OARGA412−0.77512.201−4.7061.0039.92
ATOM860NASNA413−0.19814.119−5.7171.0041.64
ATOM861CAASNA413−1.45814.215−6.4401.0043.19
ATOM862CBASNA413−1.51815.533−7.2101.0046.44
ATOM863CGASNA413−1.73916.718−6.2991.0047.86
ATOM864OD1ASNA413−2.37616.594−5.2491.0048.05
ATOM865ND2ASNA413−1.21317.876−6.6871.0049.43
ATOM866CASNA413−1.67313.044−7.3851.0041.48
ATOM867OASNA413−2.79212.567−7.5461.0040.50
ATOM868NGLNA414−0.60012.577−8.0101.0042.82
ATOM869CAGLNA414−0.70311.448−8.9251.0044.73
ATOM870CBGLNA4140.58511.307−9.7411.0047.52
ATOM871CGGLNA4140.57212.088−11.0491.0050.47
ATOM872CDGLNA4141.91412.713−11.3751.0053.91
ATOM873OE1GLNA4142.59113.257−10.5011.0053.68
ATOM874NE2GLNA4142.30912.637−12.6411.0056.91
ATOM875CGLNA414−0.97010.163−8.1411.0043.21
ATOM876OGLNA414−1.4919.193−8.6821.0042.33
ATOM877NGLYA415−0.61810.168−6.8601.0041.97
ATOM878CAGLYA415−0.8368.992−6.0401.0040.43
ATOM879CGLYA415−2.3068.720−5.8041.0040.80
ATOM880OGLYA415−2.6967.601−5.4721.0037.83
ATOM881NLYSA416−3.1299.748−5.9781.0042.16
ATOM882CALYSA416−4.5669.613−5.7791.0044.34
ATOM883CBLYSA416−5.21210.996−5.7041.0045.65
ATOM884CGLYSA416−4.76111.819−4.5101.0047.42
ATOM885CDLYSA416−4.91013.309−4.7771.0050.97
ATOM886CELYSA416−5.99213.924−3.8981.0053.25
ATOM887NZLYSA416−5.41614.764−2.8091.0056.95
ATOM888CLYSA416−5.2278.793−6.8861.0045.33
ATOM889OLYSA416−6.3398.299−6.7141.0046.50
ATOM890NCYSA417−4.5408.648−8.0151.0045.18
ATOM891CACYSA417−5.0667.890−9.1481.0046.25
ATOM892CBCYSA417−4.0627.902−10.3051.0049.29
ATOM893SGCYSA417−3.9169.493−11.1681.0049.59
ATOM894CCYSA417−5.3736.452−8.7521.0047.18
ATOM895OCYSA417−6.2205.794−9.3591.0046.50
ATOM896NVALA418−4.6715.968−7.7311.0045.07
ATOM897CAVALA418−4.8664.612−7.2321.0042.75
ATOM898CBVALA418−3.5253.841−7.2061.0042.45
ATOM899CG1VALA418−3.6702.563−6.4101.0040.22
ATOM900CG2VALA418−3.0713.538−8.6341.0038.03
ATOM901CVALA418−5.4414.714−5.8181.0041.46
ATOM902OVALA418−4.8835.400−4.9631.0042.08
ATOM903NGLUA419−6.5594.036−5.5791.0040.95
ATOM904CAGLUA419−7.2234.073−4.2751.0042.51
ATOM905CBGLUA419−8.5363.282−4.3331.0044.52
ATOM906CGGLUA419−9.0102.751−2.9841.0050.42
ATOM907CDGLUA419−10.4132.168−3.0351.0054.38
ATOM908OE1GLUA419−10.5821.059−3.5901.0054.09
ATOM909OE2GLUA419−11.3472.820−2.5161.0057.90
ATOM910CGLUA419−6.3703.552−3.1211.0041.11
ATOM911OGLUA419−5.9552.393−3.1161.0039.42
ATOM912NGLYA420−6.1294.419−2.1401.0040.53
ATOM913CAGLYA420−5.3464.049−0.9731.0037.61
ATOM914CGLYA420−3.8544.258−1.1401.0037.01
ATOM915OGLYA420−3.0884.105−0.1901.0032.59
ATOM916NMETA421−3.4444.623−2.3501.0036.21
ATOM917CAMETA421−2.0354.825−2.6561.0036.02
ATOM918CBMETA421−1.7994.607−4.1601.0032.84
ATOM919CGMETA421−0.3514.754−4.6171.0035.82
ATOM920SDMETA4210.8063.611−3.8121.0035.57
ATOM921CEMETA4210.8812.294−5.0051.0032.51
ATOM922CMETA421−1.4746.180−2.2261.0034.93
ATOM923OMETA421−0.2756.294−1.9851.0035.17
ATOM924NVALA422−2.3197.205−2.1181.0033.97
ATOM925CAVALA422−1.8238.520−1.7081.0031.29
ATOM926CBVALA422−2.9279.607−1.7661.0033.14
ATOM927CG1VALA422−3.8239.535−0.5331.0030.10
ATOM928CG2VALA422−2.27910.982−1.8541.0030.08
ATOM929CVALA422−1.2318.498−0.2961.0032.64
ATOM930OVALA422−0.2749.2200.0021.0028.41
ATOM931NGLUA423−1.8037.6700.5711.0031.53
ATOM932CAGLUA423−1.3117.5581.9351.0035.99
ATOM933CBGLUA423−2.1906.5942.7371.0040.37
ATOM934CGGLUA423−3.5887.1293.0431.0049.41
ATOM935CDGLUA423−4.4387.3361.7951.0052.38
ATOM936OE1GLUA423−5.3498.1881.8351.0056.91
ATOM937OE2GLUA423−4.2006.6520.7761.0054.53
ATOM938CGLUA4230.1277.0431.8861.0034.83
ATOM939OGLUA4231.0077.5522.5811.0031.85
ATOM940NILEA4240.3696.0381.0501.0030.17
ATOM941CAILEA4241.7115.4880.9291.0028.99
ATOM942CBILEA4241.6964.1950.1091.0030.96
ATOM943CG2ILEA4243.1083.5880.0681.0027.20
ATOM944CG1ILEA4240.6713.2300.7251.0030.77
ATOM945CD1ILEA4240.8101.7870.2911.0034.69
ATOM946CILEA4242.7006.4830.3121.0028.21
ATOM947OILEA4243.8566.5510.7351.0028.48
ATOM948NPHEA4252.2537.260−0.6751.0027.68
ATOM949CAPHEA4253.1198.253−1.3151.0027.30
ATOM950CBPHEA4252.3818.958−2.4581.0026.36
ATOM951CGPHEA4252.5388.289−3.7981.0027.22
ATOM952CD1PHEA4252.6199.050−4.9581.0027.36
ATOM953CD2PHEA4252.5666.900−3.9051.0027.89
ATOM954CE1PHEA4252.7218.443−6.2071.0029.63
ATOM955CE2PHEA4252.6686.282−5.1491.0027.28
ATOM956CZPHEA4252.7457.056−6.3031.0027.63
ATOM957CPHEA4253.5919.306−0.3121.0025.66
ATOM958OPHEA4254.7579.713−0.3281.0026.33
ATOM959NASPA4262.6809.7460.5521.0027.92
ATOM960CAASPA4262.98410.7591.5701.0028.88
ATOM961CBASPA4261.72111.1022.3691.0032.58
ATOM962CGASPA4260.78112.0341.6131.0037.47
ATOM963OD1ASPA426−0.43212.0391.9251.0037.72
ATOM964OD2ASPA4261.25312.7580.7101.0036.35
ATOM965CASPA4264.07110.2782.5321.0026.96
ATOM966OASPA4264.97411.0302.9001.0027.20
ATOM967NMETA4273.9789.0222.9471.0025.76
ATOM968CAMETA4274.9818.4683.8561.0025.89
ATOM969CBMETA4274.5677.0704.3091.0021.17
ATOM970CGMETA4273.3857.0725.2571.0024.38
ATOM971SDMETA4273.1535.4896.0801.0034.32
ATOM972CEMETA4272.1734.6374.9101.0021.03
ATOM973CMETA4276.3218.4103.1281.0022.29
ATOM974OMETA4277.3638.7603.6891.0022.19
ATOM975NLEUA4286.2857.9851.8681.0021.75
ATOM976CALEUA4287.5067.8921.0751.0022.91
ATOM977CBLEUA4287.2027.252−0.2871.0018.47
ATOM978CGLEUA4286.9105.747−0.1761.0019.24
ATOM979CD1LEUA4286.2785.222−1.4681.0016.82
ATOM980CD2LEUA4288.2045.0100.1311.0016.23
ATOM981CLEUA4288.1489.2690.9021.0023.98
ATOM982OLEUA4289.3669.4161.0341.0023.06
ATOM983NLEUA4297.32810.2810.6281.0023.91
ATOM984CALEUA4297.83711.6420.4621.0026.29
ATOM985CBLEUA4296.71412.571−0.0031.0027.47
ATOM986CGLEUA4296.33112.411−1.4761.0030.78
ATOM987CD1LEUA4295.02213.139−1.7511.0034.75
ATOM988CD2LEUA4297.44912.952−2.3501.0031.96
ATOM989CLEUA4298.42512.1661.7761.0025.83
ATOM990OLEUA4299.48212.8081.7931.0026.42
ATOM991NALAA4307.73411.8902.8771.0026.45
ATOM992CAALAA4308.20112.3334.1851.0026.11
ATOM993CBALAA4307.21411.9095.2651.0023.13
ATOM994CALAA4309.57711.7424.4621.0025.01
ATOM995OALAA43010.45512.4095.0051.0024.31
ATOM996NTHRA4319.76710.4864.0741.0025.25
ATOM997CATHRA43111.0469.8254.2941.0022.78
ATOM998CBTHRA43110.9738.3233.9621.0021.36
ATOM999OG1THRA4319.9247.7274.7271.0020.27
ATOM1000CG2THRA43112.2917.6334.2991.0019.99
ATOM1001CTHRA43112.10310.4773.4291.0023.73
ATOM1002OTHRA43113.23410.6673.8681.0019.60
ATOM1003NSERA43211.73610.8192.1971.0024.32
ATOM1004CASERA43212.67611.4791.3011.0026.96
ATOM1005CBSERA43212.06711.650−0.0931.0028.70
ATOM1006OGSERA43213.08411.930−1.0391.0033.42
ATOM1007CSERA43213.03312.8501.8761.0027.92
ATOM1008OSERA43214.17613.2941.7791.0030.78
ATOM1009NSERA43312.04513.5212.4591.0028.96
ATOM1010CASERA43312.26914.8243.0761.0034.21
ATOM1011CBSERA43310.95715.3873.6231.0035.07
ATOM1012OGSERA43310.17515.9612.5911.0042.38
ATOM1013CSERA43313.26314.6444.2231.0033.43
ATOM1014OSERA43314.15215.4734.4291.0031.94
ATOM1015NARGA43413.10513.5454.9591.0031.32
ATOM1016CAARGA43413.98013.2366.0861.0029.78
ATOM1017CBARGA43413.46811.9946.8191.0029.84
ATOM1018CGARGA43414.33111.5417.9831.0032.17
ATOM1019CDARGA43414.62612.6728.9581.0037.00
ATOM1020NEARGA43415.32112.16910.1401.0039.44
ATOM1021CZARGA43415.93512.93511.0341.0044.06
ATOM1022NH1ARGA43415.94914.25510.8851.0045.52
ATOM1023NH2ARGA43416.52812.38112.0841.0045.01
ATOM1024CARGA43415.41313.0145.6051.0029.24
ATOM1025OARGA43416.35213.5636.1731.0029.72
ATOM1026NPHEA43515.57712.2064.5611.0028.95
ATOM1027CAPHEA43516.90111.9354.0001.0030.59
ATOM1028CBPHEA43516.77711.0452.7581.0032.03
ATOM1029CGPHEA43516.7959.5633.0511.0031.88
ATOM1030CD1PHEA43516.7589.0844.3591.0035.60
ATOM1031CD2PHEA43516.8478.6432.0091.0035.89
ATOM1032CE1PHEA43516.7717.7094.6221.0035.36
ATOM1033CE2PHEA43516.8607.2712.2621.0032.71
ATOM1034CZPHEA43516.8216.8073.5701.0033.24
ATOM1035CPHEA43517.57613.2533.6071.0032.73
ATOM1036OPHEA43518.76313.4643.8711.0031.16
ATOM1037NARGA43616.81214.1372.9751.0033.37
ATOM1038CAARGA43617.34115.4292.5491.0039.13
ATOM1039CBARGA43616.28216.2061.7561.0040.42
ATOM1040CGARGA43616.84617.3170.8771.0043.09
ATOM1041CDARGA43615.75017.9600.0401.0044.53
ATOM1042NEARGA43614.82616.955−0.4721.0048.34
ATOM1043CZARGA43613.53016.913−0.1841.0048.81
ATOM1044NH1ARGA43612.99717.8230.6191.0047.80
ATOM1045NH2ARGA43612.76915.950−0.6871.0049.53
ATOM1046CARGA43617.79216.2503.7531.0038.10
ATOM1047OARGA43618.89616.7893.7641.0041.00
ATOM1048NMETA43716.93616.3344.7661.0039.47
ATOM1049CAMETA43717.25717.0875.9751.0038.20
ATOM1050CBMETA43716.10216.9986.9651.0039.79
ATOM1051CMETA43718.55016.5946.6261.0041.15
ATOM1052OMETA43719.30317.3787.2011.0040.20
ATOM1053NMETA43818.80415.2856.5381.0039.65
ATOM1054CAMETA43820.01114.6937.1171.0039.70
ATOM1055CBMETA43819.78713.2217.4631.0039.90
ATOM1056CGMETA43818.69412.9388.4601.0041.94
ATOM1057SDMETA43818.74711.1888.8801.0043.12
ATOM1058CEMETA43820.37411.0649.6191.0043.73
ATOM1059CMETA43821.17614.7566.1421.0038.03
ATOM1060OMETA43822.32114.5036.5221.0038.39
ATOM1061NASNA43920.88615.0704.8951.0037.64
ATOM1062CAASNA43921.92415.1183.8951.0035.68
ATOM1063CBASNA43923.01916.1254.2431.0040.98
ATOM1064CGASNA43923.93316.4073.0901.0045.09
ATOM1065OD1ASNA43923.52816.2951.9341.0047.16
ATOM1066ND2ASNA43925.19716.7333.3721.0046.87
ATOM1067CASNA43922.55213.7323.7391.0031.06
ATOM1068OASNA43923.76413.5813.6491.0029.54
ATOM1069NLEUA44021.69212.6983.7041.0031.47
ATOM1070CALEUA44022.16111.3263.5791.0031.63
ATOM1071CBLEUA44020.99110.3443.3801.0033.05
ATOM1072CGLEUA44021.4518.8863.2091.0037.07
ATOM1073CD1LEUA44021.9578.3534.5461.0036.18
ATOM1074CD2LEUA44020.3188.0322.6821.0032.33
ATOM1075CLEUA44023.14611.1612.4351.0032.10
ATOM1076OLEUA44022.92511.6711.3331.0032.76
ATOM1077NGLNA44124.22510.4502.7021.0032.54
ATOM1078CAGLNA44125.25510.2201.6991.0031.97
ATOM1079CBGLNA44126.63210.3202.3451.0031.75
ATOM1080CGGLNA44126.89611.6692.9791.0035.56
ATOM1081CDGLNA44127.04012.7481.9391.0034.97
ATOM1082OE1GLNA44127.98512.7821.1671.0035.51
ATOM1083NE2GLNA44126.05313.6591.8991.0035.41
ATOM1084CGLNA44125.1008.8601.0381.0034.08
ATOM1085OGLNA44124.5407.9311.6251.0030.73
ATOM1086NGLYA44225.6088.752−0.1871.0032.78
ATOM1087CAGLYA44225.5287.503−0.9211.0032.91
ATOM1088CGLYA44226.1816.350−0.1841.0031.87
ATOM1089OGLYA44225.6425.245−0.1541.0033.18
ATOM1090NGLUA44327.3406.6030.4161.0030.60
ATOM1091CAGLUA44328.0575.5671.1501.0030.85
ATOM1092CBGLUA44329.3766.1111.7041.0032.74
ATOM1093CGGLUA44330.4256.3780.6461.0036.30
ATOM1094CDGLUA44330.3107.7700.0661.0040.92
ATOM1095OE1GLUA44329.6778.6300.7161.0042.27
ATOM1096OE2GLUA44330.8538.003−1.0381.0046.82
ATOM1097CGLUA44327.2065.0482.2991.0030.43
ATOM1098OGLUA44327.2113.8542.5951.0028.11
ATOM1099NGLUA44426.4825.9552.9481.0030.26
ATOM1100CAGLUA44425.6195.5894.0671.0028.18
ATOM1101CBGLUA44425.1476.8434.7971.0026.32
ATOM1102CGGLUA44426.2507.6335.4631.0029.27
ATOM1103CDGLUA44425.7488.9446.0231.0029.62
ATOM1104OE1GLUA44425.0069.6525.3041.0032.00
ATOM1105OE2GLUA44426.0889.2687.1821.0029.02
ATOM1106CGLUA44424.4034.8133.5721.0026.93
ATOM1107OGLUA44423.9703.8414.1911.0024.78
ATOM1108NPHEA44523.8615.2562.4431.0027.79
ATOM1109CAPHEA44522.6884.6331.8531.0024.50
ATOM1110CBPHEA44522.2545.4160.6101.0025.40
ATOM1111CGPHEA44521.3724.634−0.3161.0023.74
ATOM1112CD1PHEA44520.0344.419−0.0041.0023.00
ATOM1113CD2PHEA44521.8854.094−1.4891.0022.37
ATOM1114CE1PHEA44519.2153.670−0.8551.0022.57
ATOM1115CE2PHEA44521.0793.349−2.3421.0021.69
ATOM1116CZPHEA44519.7413.138−2.0231.0022.25
ATOM1117CPHEA44522.9133.1691.4891.0022.81
ATOM1118OPHEA44522.0832.3161.7961.0022.92
ATOM1119NVALA44624.0192.8680.8221.0022.46
ATOM1120CAVALA44624.2781.4810.4471.0022.26
ATOM1121CBVALA44625.5221.360−0.4651.0022.87
ATOM1122CG1VALA44625.2512.046−1.7991.0022.57
ATOM1123CG2VALA44626.7351.9680.2171.0022.38
ATOM1124CVALA44624.4670.6141.6941.0023.68
ATOM1125OVALA44624.177−0.5861.6801.0022.91
ATOM1126NCYSA44724.9621.2232.7701.0022.02
ATOM1127CACYSA44725.1550.5034.0251.0024.17
ATOM1128CBCYSA44725.9531.3595.0111.0023.95
ATOM1129SGCYSA44727.7381.3244.7311.0028.57
ATOM1130CCYSA44723.7810.1784.6181.0021.14
ATOM1131OCYSA44723.512−0.9605.0021.0019.37
ATOM1132NLEUA44822.9151.1864.6801.0019.28
ATOM1133CALEUA44821.5681.0025.2191.0021.31
ATOM1134CBLEUA44820.8032.3245.2071.0021.90
ATOM1135CGLEUA44821.1423.3376.3031.0026.61
ATOM1136CD1LEUA44820.3284.5946.0721.0027.74
ATOM1137CD2LEUA44820.8272.7607.6721.0024.03
ATOM1138CLEUA44820.766−0.0384.4421.0021.72
ATOM1139OLEUA44820.006−0.8035.0301.0020.87
ATOM1140NLYSA44920.929−0.0553.1191.0021.42
ATOM1141CALYSA44920.205−0.9972.2691.0020.98
ATOM1142CBLYSA44920.440−0.6590.7881.0021.55
ATOM1143CGLYSA44919.438−1.297−0.1731.0024.82
ATOM1144CDLYSA44919.456−0.613−1.5421.0023.33
ATOM1145CELYSA44920.816−0.754−2.2291.0023.58
ATOM1146NZLYSA44920.741−0.482−3.6981.0028.77
ATOM1147CLYSA44920.629−2.4362.5481.0020.33
ATOM1148OLYSA44919.800−3.3452.5521.0020.57
ATOM1149NSERA45021.924−2.6372.7771.0019.25
ATOM1150CASERA45022.451−3.9653.0741.0021.84
ATOM1151CBSERA45023.982−3.9533.0411.0020.59
ATOM1152OGSERA45024.460−3.9751.7021.0029.78
ATOM1153CSERA45021.975−4.4084.4541.0021.58
ATOM1154OSERA45021.728−5.5904.6821.0020.06
ATOM1155NILEA45121.853−3.4495.3691.0022.20
ATOM1156CAILEA45121.385−3.7416.7261.0022.82
ATOM1157CBILEA45121.452−2.4767.6161.0019.62
ATOM1158CG2ILEA45120.593−2.6588.8861.0021.11
ATOM1159CG1ILEA45122.909−2.2107.9991.0022.20
ATOM1160CD1ILEA45123.115−0.9608.8501.0024.48
ATOM1161CILEA45119.952−4.2506.6621.0021.82
ATOM1162OILEA45119.575−5.1847.3691.0021.72
ATOM1163NILEA45219.152−3.6425.7951.0020.18
ATOM1164CAILEA45217.763−4.0585.6491.0018.13
ATOM1165CBILEA45217.024−3.1454.6271.0019.72
ATOM1166CG2ILEA45215.720−3.7924.1691.0018.99
ATOM1167CG1ILEA45216.725−1.7885.2821.0018.33
ATOM1168CD1ILEA45216.284−0.7074.3061.0023.25
ATOM1169CILEA45217.725−5.5175.1911.0019.50
ATOM1170OILEA45216.980−6.3405.7371.0017.60
ATOM1171NLEUA45318.555−5.8444.2091.0019.23
ATOM1172CALEUA45318.589−7.2053.6791.0021.60
ATOM1173CBLEUA45319.624−7.3162.5541.0021.50
ATOM1174CGLEUA45319.835−8.7291.9891.0025.06
ATOM1175CD1LEUA45318.550−9.2501.3641.0025.27
ATOM1176CD2LEUA45320.948−8.6940.9531.0024.73
ATOM1177CLEUA45318.906−8.2454.7461.0019.41
ATOM1178OLEUA45318.198−9.2414.8911.0020.75
ATOM1179NLEUA45419.966−7.9975.4991.0021.35
ATOM1180CALEUA45420.410−8.9256.5301.0023.67
ATOM1181CBLEUA45421.870−8.6256.8781.0020.69
ATOM1182CGLEUA45422.816−8.5845.6731.0024.92
ATOM1183CD1LEUA45424.222−8.2686.1321.0024.27
ATOM1184CD2LEUA45422.785−9.9134.9521.0022.84
ATOM1185CLEUA45419.572−8.9457.8071.0026.06
ATOM1186OLEUA45419.413−9.9978.4381.0027.44
ATOM1187NASNA45519.011−7.7958.1671.0025.01
ATOM1188CAASNA45518.240−7.6819.4001.0026.10
ATOM1189CBASNA45518.439−6.29510.0021.0022.67
ATOM1190CGASNA45517.627−6.10911.2641.0026.67
ATOM1191OD1ASNA45517.899−6.75112.2701.0025.16
ATOM1192ND2ASNA45516.615−5.24611.2121.0020.73
ATOM1193CASNA45516.739−7.9579.4181.0025.78
ATOM1194OASNA45516.230−8.51610.3801.0029.22
ATOM1195NSERA45616.027−7.5498.3811.0028.51
ATOM1196CASERA45614.578−7.7048.3711.0032.52
ATOM1197CBSERA45614.019−7.2137.0331.0035.98
ATOM1198OGSERA45614.266−5.8186.8971.0030.88
ATOM1199CSERA45614.033−9.0868.7111.0033.00
ATOM1200OSERA45613.112−9.2029.5231.0033.07
ATOM1201NGLYA45714.597−10.1308.1171.0028.40
ATOM1202CAGLYA45714.115−11.4648.4131.0036.28
ATOM1203CGLYA45715.055−12.2899.2771.0040.41
ATOM1204OGLYA45714.831−13.4869.4561.0038.20
ATOM1205NVALA45816.095−11.6579.8201.0044.13
ATOM1206CAVALA45817.079−12.35610.6471.0051.09
ATOM1207CBVALA45818.214−11.39911.0951.0051.06
ATOM1208CG1VALA45817.688−10.39012.1041.0051.75
ATOM1209CG2VALA45819.365−12.19911.6921.0050.65
ATOM1210CVALA45816.513−13.06011.8851.0057.26
ATOM1211OVALA45817.085−14.04512.3561.0058.77
ATOM1212NTYRA45915.401−12.56012.4161.0062.31
ATOM1213CATYRA45914.793−13.17713.5921.0068.49
ATOM1214CBTYRA45914.293−12.10014.5601.0070.46
ATOM1215CGTYRA45915.396−11.19615.0691.0071.73
ATOM1216CD1TYRA45915.127−9.88815.4621.0071.93
ATOM1217CE1TYRA45916.147−9.04515.8981.0072.60
ATOM1218CD2TYRA45916.716−11.64415.1281.0072.77
ATOM1219CE2TYRA45917.741−10.81215.5601.0073.55
ATOM1220CZTYRA45917.450−9.51415.9411.0072.93
ATOM1221OHTYRA45918.467−8.68716.3511.0074.56
ATOM1222CTYRA45913.649−14.09713.1871.0071.86
ATOM1223OTYRA45913.380−15.09913.8521.0073.11
ATOM1224NTHRA46012.981−13.75612.0901.0074.84
ATOM1225CATHRA46011.881−14.56711.5891.0077.66
ATOM1226CBTHRA46011.246−13.90010.3731.0076.69
ATOM1227CTHRA46012.436−15.93811.2121.0080.26
ATOM1228OTHRA46011.684−16.86610.9121.0080.82
ATOM1229NPHEA46113.762−16.05111.2311.0082.69
ATOM1230CAPHEA46114.440−17.29910.9051.0085.63
ATOM1231CBPHEA46115.920−17.03410.6301.0085.47
ATOM1232CPHEA46114.284−18.28812.0591.0087.52
ATOM1233OPHEA46114.493−17.94013.2241.0086.53
ATOM1234NLEUA46213.914−19.52011.7241.0089.49
ATOM1235CALEUA46213.711−20.56812.7181.0091.34
ATOM1236CBLEUA46212.961−21.74112.0871.0091.23
ATOM1237CLEUA46215.016−21.06013.3401.0092.05
ATOM1238OLEUA46216.042−21.16512.6641.0091.91
ATOM1239NSERA46314.966−21.35714.6351.0092.53
ATOM1240CASERA46316.131−21.85515.3581.0092.96
ATOM1241CBSERA46316.033−21.48316.8331.0091.67
ATOM1242CSERA46316.189−23.37115.2001.0093.39
ATOM1243OSERA46315.156−24.03415.1021.0093.44
ATOM1244NSERA46417.399−23.91715.1671.0093.82
ATOM1245CASERA46417.577−25.35515.0151.0093.85
ATOM1246CBSERA46417.284−25.76913.5771.0093.74
ATOM1247CSERA46418.997−25.74315.3961.0093.96
ATOM1248OSERA46419.815−26.07414.5351.0093.65
ATOM1249NTHRA46519.279−25.69916.6941.0093.91
ATOM1250CATHRA46520.600−26.03617.2121.0093.79
ATOM1251CBTHRA46520.952−27.48316.8631.0093.38
ATOM1252CTHRA46521.640−25.08516.6341.0093.27
ATOM1253OTHRA46521.302−24.01716.1211.0093.03
ATOM1254NLEUA46622.907−25.47916.7231.0093.26
ATOM1255CALEUA46623.999−24.66516.2071.0092.34
ATOM1256CBLEUA46625.335−25.33816.4981.0091.59
ATOM1257CLEUA46623.829−24.46114.7061.0092.18
ATOM1258OLEUA46624.411−23.54514.1251.0092.67
ATOM1259NLYSA46723.028−25.32314.0861.0091.28
ATOM1260CALYSA46722.772−25.23812.6531.0090.02
ATOM1261CBLYSA46721.740−26.28712.2401.0089.93
ATOM1262CLYSA46722.269−23.84112.3081.0088.35
ATOM1263OLYSA46723.032−22.99011.8491.0088.50
ATOM1264NSERA46820.981−23.61012.5361.0086.02
ATOM1265CASERA46820.384−22.31512.2521.0084.10
ATOM1266CBSERA46818.901−22.33312.6201.0084.08
ATOM1267OGSERA46818.229−23.37811.9371.0083.03
ATOM1268CSERA46821.109−21.23013.0401.0083.39
ATOM1269OSERA46821.264−20.10512.5651.0083.48
ATOM1270NLEUA46921.558−21.57914.2421.0082.04
ATOM1271CALEUA46922.276−20.64015.0981.0080.28
ATOM1272CBLEUA46922.595−21.29416.4361.0079.81
ATOM1273CLEUA46923.564−20.17414.4191.0079.18
ATOM1274OLEUA46924.111−19.12214.7561.0078.61
ATOM1275NGLUA47024.044−20.96913.4661.0076.69
ATOM1276CAGLUA47025.256−20.63812.7261.0074.84
ATOM1277CBGLUA47025.803−21.88012.0321.0074.12
ATOM1278CGLUA47024.920−19.56511.6971.0073.77
ATOM1279OGLUA47025.617−18.55611.5811.0072.94
ATOM1280NGLUA47123.842−19.79210.9531.0072.08
ATOM1281CAGLUA47123.396−18.8429.9451.0070.05
ATOM1282CBGLUA47122.461−19.5268.9441.0071.52
ATOM1283CGGLUA47123.150−19.9767.6681.0072.90
ATOM1284CDGLUA47124.512−20.5867.9321.0074.01
ATOM1285OE1GLUA47125.469−20.2587.1981.0074.22
ATOM1286OE2GLUA47124.626−21.3958.8781.0075.18
ATOM1287CGLUA47122.667−17.69210.6301.0067.33
ATOM1288OGLUA47121.685−17.16510.1071.0067.77
ATOM1289NLYSA47223.152−17.31911.8111.0062.63
ATOM1290CALYSA47222.564−16.22912.5781.0057.41
ATOM1291CBLYSA47221.697−16.77713.7131.0058.74
ATOM1292CGLYSA47220.683−15.77614.2431.0060.32
ATOM1293CDLYSA47219.271−16.34214.2191.0060.73
ATOM1294CELYSA47218.485−15.90915.4491.0061.78
ATOM1295NZLYSA47219.352−15.78816.6581.0060.09
ATOM1296CLYSA47223.662−15.33913.1501.0053.42
ATOM1297OLYSA47223.631−14.12012.9781.0050.87
ATOM1298NASPA47324.628−15.94913.8301.0047.52
ATOM1299CAASPA47325.732−15.19414.4051.0045.55
ATOM1300CBASPA47326.613−16.09415.2691.0050.48
ATOM1301CGASPA47326.380−15.88516.7491.0055.50
ATOM1302OD1ASPA47325.272−15.43617.1181.0058.06
ATOM1303OD2ASPA47327.304−16.17017.5411.0059.81
ATOM1304CASPA47326.557−14.61113.2691.0042.62
ATOM1305OASPA47327.087−13.50613.3731.0042.10
ATOM1306NHISA47426.663−15.36412.1801.0038.05
ATOM1307CAHISA47427.416−14.90411.0261.0037.25
ATOM1308CBHISA47427.429−15.9789.9411.0035.07
ATOM1309CGHISA47428.036−15.5238.6531.0037.36
ATOM1310CD2HISA47429.292−15.1138.3551.0038.86
ATOM1311ND1HISA47427.322−15.4527.4761.0041.31
ATOM1312CE1HISA47428.110−15.0206.5091.0040.86
ATOM1313NE2HISA47429.311−14.8077.0161.0044.49
ATOM1314CHISA47426.749−13.64010.4931.0036.68
ATOM1315OHISA47427.417−12.67610.1321.0036.48
ATOM1316NILEA47525.422−13.65210.4471.0035.93
ATOM1317CAILEA47524.683−12.4999.9631.0036.21
ATOM1318CBILEA47523.174−12.7979.8681.0036.31
ATOM1319CG2ILEA47522.411−11.5279.5131.0038.19
ATOM1320CG1ILEA47522.922−13.8748.8131.0036.97
ATOM1321CD1ILEA47521.528−14.4548.8691.0035.59
ATOM1322CILEA47524.893−11.32210.9071.0035.34
ATOM1323OILEA47525.092−10.18910.4711.0033.20
ATOM1324NHISA47624.857−11.59612.2061.0035.95
ATOM1325CAHISA47625.031−10.54013.1931.0035.06
ATOM1326CBHISA47624.681−11.06214.5851.0037.30
ATOM1327CGHISA47623.210−11.06814.8601.0043.06
ATOM1328CD2HISA47622.329−10.05115.0171.0043.93
ATOM1329ND1HISA47622.476−12.23014.9681.0045.60
ATOM1330CE1HISA47621.207−11.92815.1771.0047.56
ATOM1331NE2HISA47621.091−10.61315.2111.0046.21
ATOM1332CHISA47626.438−9.96613.1701.0035.40
ATOM1333OHISA47626.634−8.77413.4151.0035.45
ATOM1334NARGA47727.420−10.80512.8621.0034.07
ATOM1335CAARGA47728.796−10.33112.7951.0034.18
ATOM1336CBARGA47729.757−11.50612.6051.0041.04
ATOM1337CGARGA47729.800−12.45913.7881.0047.61
ATOM1338CDARGA47730.782−13.59913.5571.0055.67
ATOM1339NEARGA47731.780−13.67514.6221.0060.17
ATOM1340CZARGA47732.780−12.81114.7701.0061.98
ATOM1341NH1ARGA47732.918−11.80313.9181.0064.29
ATOM1342NH2ARGA47733.643−12.95515.7661.0062.79
ATOM1343CARGA47728.906−9.36111.6211.0030.77
ATOM1344OARGA47729.462−8.26811.7531.0033.59
ATOM1345NVALA47828.369−9.76610.4751.0027.65
ATOM1346CAVALA47828.389−8.9309.2801.0027.07
ATOM1347CBVALA47827.658−9.6058.1001.0028.00
ATOM1348CG1VALA47827.672−8.6786.8901.0025.83
ATOM1349CG2VALA47828.319−10.9337.7611.0031.66
ATOM1350CVALA47827.689−7.6109.5841.0026.92
ATOM1351OVALA47828.216−6.5369.2941.0026.97
ATOM1352NLEUA47926.499−7.70210.1711.0025.74
ATOM1353CALEUA47925.727−6.51610.5301.0027.97
ATOM1354CBLEUA47924.474−6.91211.3241.0025.55
ATOM1355CGLEUA47923.211−7.22910.5171.0029.01
ATOM1356CD1LEUA47922.056−7.50311.4811.0027.05
ATOM1357CD2LEUA47922.864−6.0639.5841.0024.92
ATOM1358CLEUA47926.592−5.58211.3691.0025.39
ATOM1359OLEUA47926.595−4.37011.1581.0027.39
ATOM1360NASPA48027.324−6.15812.3201.0026.04
ATOM1361CAASPA48028.206−5.38813.1931.0027.32
ATOM1362CBASPA48028.878−6.30514.2221.0026.67
ATOM1363CGASPA48027.990−6.60215.4171.0031.02
ATOM1364OD1ASPA48028.355−7.50516.1981.0031.50
ATOM1365OD2ASPA48026.935−5.94415.5801.0032.21
ATOM1366CASPA48029.283−4.69912.3611.0025.59
ATOM1367OASPA48029.672−3.56212.6361.0027.15
ATOM1368NLYSA48129.767−5.39411.3401.0025.17
ATOM1369CALYSA48130.794−4.83010.4771.0024.93
ATOM1370CBLYSA48131.306−5.8909.5121.0028.42
ATOM1371CGLYSA48132.158−6.95310.1881.0035.59
ATOM1372CDLYSA48132.894−7.7999.1571.0041.21
ATOM1373CELYSA48133.883−6.9638.3501.0041.48
ATOM1374NZLYSA48134.954−6.3889.2151.0043.22
ATOM1375CLYSA48130.260−3.6359.6961.0026.12
ATOM1376OLYSA48130.979−2.6579.4631.0023.73
ATOM1377NILEA48228.996−3.7059.2911.0025.44
ATOM1378CAILEA48228.421−2.5988.5451.0027.69
ATOM1379CBILEA48227.066−2.9837.9151.0027.59
ATOM1380CG2ILEA48226.470−1.7887.1831.0025.97
ATOM1381CG1ILEA48227.274−4.1316.9221.0023.80
ATOM1382CD1ILEA48226.000−4.8386.5331.0021.30
ATOM1383CILEA48228.253−1.4089.4811.0027.33
ATOM1384OILEA48228.312−0.2569.0451.0028.55
ATOM1385NTHRA48328.046−1.69010.7681.0025.03
ATOM1386CATHRA48327.905−0.63211.7601.0023.62
ATOM1387CBTHRA48327.535−1.19213.1541.0022.18
ATOM1388OG1THRA48326.181−1.65813.1331.0025.39
ATOM1389CG2THRA48327.673−0.11114.2261.0025.84
ATOM.1390CTHRA48329.2570.07411.8581.0023.04
ATOM1391OTHRA48329.3311.30611.8461.0023.55
ATOM1392NASPA48430.324−0.71411.9601.0022.24
ATOM1393CAASPA48431.674−0.15212.0391.0025.48
ATOM1394CBASPA48432.718−1.27312.1071.0026.88
ATOM1395CGASPA48432.629−2.08313.3941.0032.52
ATOM1396OD1ASPA48432.002−1.60814.3661.0033.68
ATOM1397OD2ASPA48433.185−3.19813.4341.0034.63
ATOM1398CASPA48431.9300.71510.8071.0025.16
ATOM1399OASPA48432.4811.81210.9051.0026.05
ATOM1400NTHRA48531.5050.2269.6451.0028.96
ATOM1401CATHRA48531.6890.9608.3941.0026.63
ATOM1402CBTHRA48531.1240.1667.1971.0026.12
ATOM1403OG1THRA48531.753−1.1237.1321.0024.30
ATOM1404CG2THRA48531.3810.9075.8981.0023.31
ATOM1405CTHRA48530.9942.3188.4681.0028.90
ATOM1406OTHRA48531.5833.3548.1371.0027.26
ATOM1407NLEUA48629.7432.3108.9151.0024.76
ATOM1408CALEUA48628.9733.5379.0271.0026.19
ATOM1409CBLEUA48627.5673.2339.5471.0027.27
ATOM1410CGLEUA48626.5082.9218.4861.0023.50
ATOM1411CD1LEUA48625.2102.5509.1831.0022.03
ATOM1412CD2LEUA48626.3094.1287.5771.0021.35
ATOM1413CLEUA48629.6624.5199.9601.0027.36
ATOM1414OLEUA48629.7455.7109.6691.0025.87
ATOM1415NILEA48730.1514.01511.0881.0027.88
ATOM1416CAILEA48730.8434.85712.0551.0028.40
ATOM1417CBILEA48731.2034.05413.3321.0026.74
ATOM1418CG2ILEA48732.2554.80314.1541.0027.54
ATOM1419CG1ILEA48729.9373.81314.1631.0025.93
ATOM1420CD1ILEA48729.2375.08814.6241.0023.42
ATOM1421CILEA48732.1255.39311.4121.0028.89
ATOM1422OILEA48732.4976.55411.6021.0029.85
ATOM1423NHISA48832.7914.53310.6491.0029.71
ATOM1424CAHISA48834.0314.8989.9671.0034.12
ATOM1425CBHISA48834.5853.6919.2071.0036.61
ATOM1426CGHISA48835.7993.9978.3851.0042.74
ATOM1427CD2HISA48835.9704.0897.0451.0043.12
ATOM1428ND1HISA48837.0344.2398.9461.0043.13
ATOM1429CE1HISA48837.9134.4667.9871.0043.40
ATOM1430NE2HISA48837.2934.3816.8251.0045.63
ATOM1431CHISA48833.7996.0518.9981.0032.74
ATOM1432OHISA48834.5777.0048.9551.0031.06
ATOM1433NLEUA48932.7215.9588.2231.0033.56
ATOM1434CALEUA48932.3846.9927.2581.0030.78
ATOM1435CBLEUA48931.1456.5876.4641.0034.67
ATOM1436CGLEUA48931.3105.3535.5741.0034.73
ATOM1437CD1LEUA48929.9454.8565.1251.0033.21
ATOM1438CD2LEUA48932.1835.7014.3781.0035.92
ATOM1439CLEUA48932.1248.3207.9541.0033.97
ATOM1440OLEUA48932.5879.3657.5071.0033.22
ATOM1441NMETA49031.3878.2749.0581.0031.33
ATOM1442CAMETA49031.0569.4829.8011.0030.61
ATOM1443CBMETA49030.0009.16110.8621.0032.34
ATOM1444CGMETA49028.6078.94010.2891.0030.71
ATOM1445SDMETA49027.4578.24711.4961.0031.14
ATOM1446CEMETA49026.3217.40810.4181.0030.36
ATOM1447CMETA49032.28710.10810.4551.0032.22
ATOM1448OMETA49032.41211.33010.5171.0028.25
ATOM1449NALAA49133.1849.26210.9491.0033.81
ATOM1450CAALAA49134.4079.73011.5851.0039.92
ATOM1451CBALAA49135.1688.55412.1851.0037.22
ATOM1452CALAA49135.27510.44510.5501.0042.68
ATOM1453OALAA49135.86511.48710.8381.0045.32
ATOM1454NLYSA49235.3399.8769.3471.0044.39
ATOM1455CALYSA49236.12210.4408.2481.0044.80
ATOM1456CBLYSA49236.1369.4777.0521.0046.96
ATOM1457CGLYSA49237.4908.8406.7441.0047.20
ATOM1458CDLYSA49237.3907.8305.5951.0045.71
ATOM1459CELYSA49238.6316.9375.5181.0045.55
ATOM1460NZLYSA49238.3575.5774.9481.0036.28
ATOM1461CLYSA49235.53411.7807.8091.0045.61
ATOM1462OLYSA49236.22712.6047.2151.0046.18
ATOM1463NALAA49334.25411.9928.1001.0043.75
ATOM1464CAALAA49333.59013.2387.7281.0042.42
ATOM1465CBALAA49332.09713.0017.5281.0040.92
ATOM1466CALAA49333.81614.3058.7961.0041.78
ATOM1467OALAA49333.27715.4108.7071.0040.76
ATOM1468NGLYA49434.60413.9609.8111.0041.01
ATOM1469CAGLYA49434.90314.90410.8731.0041.63
ATOM1470CGLYA49433.85715.06011.9651.0041.18
ATOM1471OGLYA49433.91616.01112.7471.0038.22
ATOM1472NLEUA49532.90514.13812.0431.0039.53
ATOM1473CALEUA49531.87614.24813.0681.0038.91
ATOM1474CBLEUA49530.71313.30412.7691.0039.20
ATOM1475CGLEUA49529.54013.90111.9881.0040.73
ATOM1476CD1LEUA49529.97614.17010.5531.0037.80
ATOM1477CD2LEUA49528.34912.94312.0261.0040.94
ATOM1478CLEUA49532.46113.92314.4311.0036.01
ATOM1479OLEUA49533.34713.07414.5441.0034.85
ATOM1480NTHRA49631.97914.60415.4591.0037.52
ATOM1481CATHRA49632.46214.35016.8121.0035.45
ATOM1482CBTHRA49631.92515.37517.8291.0037.55
ATOM1483OG1THRA49630.49815.26317.9081.0032.93
ATOM1484CG2THRA49632.31516.79717.4341.0036.16
ATOM1485CTHRA49631.93312.98717.2101.0035.67
ATOM1486OTHRA49631.08112.42716.5211.0034.34
ATOM1487NLEUA49732.42912.45218.3191.0034.88
ATOM1488CALEUA49731.96511.15118.7861.0035.67
ATOM1489CBLEUA49732.68910.76020.0741.0041.10
ATOM1490CGLEUA49733.7149.64019.8961.0045.27
ATOM1491CD1LEUA49734.7559.69221.0081.0045.09
ATOM1492CD2LEUA49732.9888.30519.8841.0047.77
ATOM1493CLEUA49730.45511.19819.0261.0033.72
ATOM1494OLEUA49729.71210.35018.5341.0033.20
ATOM1495NGLNA49830.00612.20219.7731.0030.82
ATOM1496CAGLNA49828.58612.34820.0621.0031.47
ATOM1497CBGLNA49828.34413.56620.9511.0030.51
ATOM1498CGGLNA49826.89413.79621.3411.0034.38
ATOM1499CDGLNA49826.71215.13022.0151.0038.60
ATOM1500OE1GLNA49827.36316.11221.6861.0042.92
ATOM1501NE2GLNA49825.80915.17623.0081.0040.02
ATOM1502CGLNA49827.77612.47618.7731.0030.47
ATOM1503OGLNA49826.68211.92718.6651.0030.85
ATOM1504NGLNA49928.31113.19617.7931.0029.52
ATOM1505CAGLNA49927.60313.36216.5241.0030.24
ATOM1506CBGLNA49928.29214.42015.6611.0030.20
ATOM1507CGGLNA49928.13515.84016.1911.0031.60
ATOM1508CDGLNA49928.93016.84915.3891.0031.61
ATOM1509OE1GLNA49929.95616.51814.7951.0030.66
ATOM1510NE2GLNA49928.45718.08915.3641.0034.17
ATOM1511CGLNA49927.52912.04715.7531.0029.40
ATOM1512OGLNA49926.56711.79315.0321.0030.04
ATOM1513NGLNA50028.55011.21415.9031.0025.67
ATOM1514CAGLNA50028.5779.93715.2161.0029.30
ATOM1515CBGLNA50029.9339.27615.4061.0031.52
ATOM1516CGGLNA50031.0129.83914.5081.0033.05
ATOM1517CDGLNA50032.3719.37014.9301.0034.84
ATOM1518OE1GLNA50032.6128.19415.1411.0036.47
ATOM1519NE2GLNA50033.30110.32415.0821.0038.25
ATOM1520CGLNA50027.4599.01715.7111.0027.98
ATOM1521OGLNA50026.7008.46914.9081.0024.84
ATOM1522NHISA50127.3578.86417.0291.0026.20
ATOM1523CAHISA50126.3278.02117.6311.0027.63
ATOM1524CBHISA50126.5357.91919.1451.0027.97
ATOM1525CGHISA50127.8927.42019.5351.0034.27
ATOM1526CD2HISA50128.7266.54018.9311.0036.10
ATOM1527ND1HISA50128.5417.84420.6761.0031.81
ATOM1528CE1HISA50129.7167.24420.7581.0034.89
ATOM1529NE2HISA50129.8546.44819.7121.0037.46
ATOM1530CHISA50124.9358.57217.3481.0024.93
ATOM1531OHISA50123.9987.81517.1071.0026.73
ATOM1532NGLNA50224.7969.89217.3791.0022.79
ATOM1533CAGLNA50223.50410.49817.1191.0026.14
ATOM1534CBGLNA50223.55412.00617.3711.0022.36
ATOM1535CGGLNA50223.46012.37818.8481.0026.19
ATOM1536CDGLNA50223.58913.87519.0891.0028.67
ATOM1537OE1GLNA50223.63214.66318.1491.0028.40
ATOM1538NE2GLNA50223.65114.26820.3551.0024.72
ATOM1539CGLNA50223.05610.22115.6851.0026.19
ATOM1540OGLNA50221.9139.82215.4531.0024.09
ATOM1541NARGA50323.95510.42914.7271.0024.88
ATOM1542CAARGA50323.63010.19613.3261.0025.25
ATOM1543CBARGA50324.77210.66812.4181.0027.63
ATOM1544CGARGA50324.43210.56310.9321.0028.75
ATOM1545CDARGA50325.47911.22210.0561.0027.72
ATOM1546NEARGA50325.07211.2148.6541.0029.35
ATOM1547CZARGA50324.27912.1268.1051.0025.84
ATOM1548NH1ARGA50323.80413.1208.8401.0027.35
ATOM1549NH2ARGA50323.96212.0446.8201.0030.63
ATOM1550CARGA50323.3478.71613.0651.0024.53
ATOM1551OARGA50322.4258.37512.3211.0025.90
ATOM1552NLEUA50424.1437.84113.6721.0023.00
ATOM1553CALEUA50423.9536.40613.4961.0022.60
ATOM1554CBLEUA50424.9715.62114.3231.0025.43
ATOM1555CGLEUA50424.7814.10014.3441.0025.23
ATOM1556CD1LEUA50425.1663.50512.9911.0028.52
ATOM1557CD2LEUA50425.6273.49515.4441.0022.14
ATOM1558CLEUA50422.5416.03013.9341.0022.84
ATOM1559OLEUA50421.8465.28813.2451.0021.51
ATOM1560NALAA50522.1206.54715.0831.0020.16
ATOM1561CAALAA50520.7846.26215.5851.0021.08
ATOM1562CBALAA50520.6056.86816.9801.0023.57
ATOM1563CALAA50519.7386.83214.6281.0020.20
ATOM1564OALAA50518.7546.16414.2931.0017.31
ATOM1565NGLNA50619.9548.06614.1841.0022.11
ATOM1566CAGLNA50619.0138.71113.2771.0021.70
ATOM1567CBGLNA50619.50210.11112.9031.0022.26
ATOM1568CGGLNA50619.24011.15813.9751.0025.84
ATOM1569CDGLNA50620.18712.33313.8571.0032.88
ATOM1570OE1GLNA50620.70412.61412.7771.0031.23
ATOM1571NE2GLNA50620.42313.02514.9681.0032.97
ATOM1572CGLNA50618.8137.88112.0161.0023.57
ATOM1573OGLNA50617.6847.71511.5501.0021.83
ATOM1574NLEUA50719.9057.35411.4741.0019.98
ATOM1575CALEUA50719.8276.53710.2631.0022.03
ATOM1576CBLEUA50721.2316.2449.7251.0023.02
ATOM1577CGLEUA50722.0267.4579.2251.0025.80
ATOM1578CD1LEUA50723.3716.9948.7131.0027.67
ATOM1579CD2LEUA50721.2648.1768.1301.0025.62
ATOM1580CLEUA50719.0905.21910.4961.0022.35
ATOM1581OLEUA50718.2424.8259.6951.0019.33
ATOM1582NLEUA50819.4024.53911.5921.0021.29
ATOM1583CALEUA50818.7553.26011.8811.0020.72
ATOM1584CBLEUA50819.5012.53513.0011.0022.29
ATOM1585CGLEUA50820.9772.31112.6781.0024.70
ATOM1586CD1LEUA50821.6421.55113.8141.0021.37
ATOM1587CD2LEUA50821.0951.54211.3671.0027.88
ATOM1588CLEUA50817.2793.39612.2391.0019.14
ATOM1589OLEUA50816.4982.47812.0031.0017.80
ATOM1590NLEUA50916.8954.53012.8151.0019.23
ATOM1591CALEUA50915.4954.74713.1731.0020.14
ATOM1592CBLEUA50915.3476.03013.9991.0020.28
ATOM1593CGLEUA50915.7105.85815.4791.0021.35
ATOM1594CD1LEUA50915.3547.10616.2631.0019.29
ATOM1595CD2LEUA50914.9894.65616.0381.0020.84
ATOM1596CLEUA50914.6814.84111.8851.0021.69
ATOM1597OLEUA50913.4934.51411.8541.0022.40
ATOM1598NILEA51015.3435.27010.8151.0020.22
ATOM1599CAILEA51014.7105.3979.5081.0020.40
ATOM1600CBILEA51015.7205.9468.4641.0028.34
ATOM1601CG2ILEA51015.2085.7107.0561.0032.54
ATOM1602CG1ILEA51015.9657.4388.6961.0028.23
ATOM1603CD1ILEA51014.7898.1899.2881.0033.16
ATOM1604CILEA51014.2104.0259.0491.0023.21
ATOM1605OILEA51013.1203.9068.4741.0021.16
ATOM1606NLEUA51114.9982.9899.3231.0018.38
ATOM1607CALEUA51114.6331.6348.9171.0020.10
ATOM1608CBLEUA51115.7540.6569.2671.0021.69
ATOM1609CGLEUA51117.1281.0228.6921.0026.03
ATOM1610CD1LEUA51118.024−0.2068.7241.0022.68
ATOM1611CD2LEUA51116.9961.5447.2671.0026.00
ATOM1612CLEUA51113.3261.1819.5431.0018.51
ATOM1613OLEUA51112.6630.2839.0251.0017.40
ATOM1614NSERA51212.9631.79910.6641.0018.68
ATOM1615CASERA51211.7181.47111.3311.0018.67
ATOM1616CBSERA51211.6612.11712.7201.0018.58
ATOM1617OGSERA51210.3152.22913.1651.0027.92
ATOM1618CSERA51210.5721.99410.4641.0018.43
ATOM1619OSERA5129.5841.29610.2361.0013.91
ATOM1620NHISA51310.7133.2289.9821.0018.95
ATOM1621CAHISA5139.6983.8319.1241.0020.82
ATOM1622CBHISA51310.0135.3158.8941.0024.36
ATOM1623CGHISA5139.9236.14610.1361.0032.13
ATOM1624CD2HISA5138.8636.74410.7341.0035.29
ATOM1625ND1HISA51311.0106.39110.9491.0035.00
ATOM1626CE1HISA51310.6247.10111.9951.0034.67
ATOM1627NE2HISA5139.3267.32811.8891.0035.82
ATOM1628CHISA5139.6503.0797.7901.0019.08
ATOM1629OHISA5138.5752.8637.2201.0021.20
ATOM1630NILEA51410.8092.6627.2971.0015.58
ATOM1631CAILEA51410.8491.9216.0381.0016.48
ATOM1632CBILEA51412.3121.6785.5761.0020.09
ATOM1633CG2ILEA51412.3490.6024.4991.0019.55
ATOM1634CG1ILEA51412.8912.9865.0191.0022.62
ATOM1635CD1ILEA51414.3932.9924.8741.0027.34
ATOM1636CILEA51410.1120.5906.2101.0016.40
ATOM1637OILEA5149.3640.1645.3281.0017.91
ATOM1638NARGA51510.301−0.0717.3471.0018.20
ATOM1639CAARGA5159.585−1.3277.5641.0018.05
ATOM1640CBARGA5159.984−1.9808.8891.0018.36
ATOM1641CGARGA5159.173−3.2379.2131.0017.84
ATOM1642CDARGA5159.823−4.4708.6061.0017.94
ATOM1643NEARGA51511.038−4.8139.3341.0026.96
ATOM1644CZARGA51511.406−6.0519.6411.0025.13
ATOM1645NH1ARGA51510.654−7.0809.2811.0023.49
ATOM1646NH2ARGA51512.511−6.25410.3401.0032.16
ATOM1647CARGA5158.089−1.0207.5941.0018.29
ATOM1648OARGA5157.275−1.7597.0381.0016.22
ATOM1649NHISA5167.7260.0858.2371.0019.33
ATOM1650CAHISA5166.3170.4418.3301.0017.78
ATOM1651CBHISA5166.1261.7029.1661.0016.84
ATOM1652CGHISA5164.6922.1019.3121.0018.16
ATOM1653CD2HISA5163.9673.0618.6911.0021.17
ATOM1654ND1HISA5163.8301.46910.1801.0020.70
ATOM1655CE1HISA5162.6332.02210.0891.0021.52
ATOM1656NE2HISA5162.6892.9929.1911.0020.16
ATOM1657CHISA5165.7080.6596.9541.0016.63
ATOM1658OHISA5164.5980.2166.6891.0018.58
ATOM1659NMETA5176.4381.3346.0731.0015.29
ATOM1660CAMETA5175.9251.5894.7301.0016.58
ATOM1661CBMETA5176.8372.5764.0021.0018.66
ATOM1662CGMETA5176.8053.9784.6311.0016.88
ATOM1663SDMETA5177.6705.2433.7011.0024.08
ATOM1664CEMETA5179.3904.7773.9621.0014.30
ATOM1665CMETA5175.7730.2893.9401.0017.86
ATOM1666OMETA5174.7910.1013.2241.0018.25
ATOM1667NSERA5186.741−0.6104.0861.0017.43
ATOM1668CASERA5186.697−1.8963.4031.0018.40
ATOM1669CBSERA5187.974−2.6953.6801.0016.77
ATOM1670OGSERA5187.834−4.0303.2271.0024.23
ATOM1671CSERA5185.476−2.6953.8541.0017.91
ATOM1672OSERA5184.788−3.2953.0301.0018.97
ATOM1673NASNA5195.204−2.6975.1591.0021.82
ATOM1674CAASNA5194.047−3.4185.6961.0021.99
ATOM1675CBASNA5193.957−3.2577.2161.0023.24
ATOM1676CGASNA5195.046−4.0117.9571.0031.14
ATOM1677OD1ASNA5195.585−4.9997.4611.0032.50
ATOM1678ND2ASNA5195.368−3.5459.1631.0029.10
ATOM1679CASNA5192.761−2.8715.0791.0023.76
ATOM1680OASNA5191.902−3.6324.6311.0024.48
ATOM1681NLYSA5202.627−1.5485.0781.0020.58
ATOM1682CALYSA5201.449−0.9004.5121.0025.49
ATOM1683CBLYSA5201.4840.6074.7861.0024.73
ATOM1684CGLYSA5201.5120.9966.2641.0032.31
ATOM1685CDLYSA5200.6560.0807.1331.0037.11
ATOM1686CELYSA520−0.7870.5477.1811.0041.56
ATOM1687NZLYSA520−1.560−0.1348.2611.0042.66
ATOM1688CLYSA5201.380−1.1443.0051.0025.40
ATOM1689OLYSA5200.316−1.4362.4671.0026.44
ATOM1690NGLYA5212.520−1.0212.3321.0022.88
ATOM1691CAGLYA5212.561−1.2360.8971.0021.53
ATOM1692CGLYA5212.177−2.6550.5361.0024.79
ATOM1693OGLYA5211.426−2.878−0.4131.0025.71
ATOM1694NMETA5222.696−3.6191.2901.0022.75
ATOM1695CAMETA5222.393−5.0271.0581.0023.40
ATOM1696CBMETA5223.170−5.8982.0421.0025.74
ATOM1697CGMETA5223.396−7.3081.5591.0031.06
ATOM1698SDMETA5224.572−7.3520.2021.0034.06
ATOM1699CEMETA5226.125−7.2291.1131.0029.28
ATOM1700CMETA5220.893−5.2811.2181.0026.49
ATOM1701OMETA5220.268−5.9200.3611.0025.47
ATOM1702NGLUA5230.321−4.7902.3181.0024.95
ATOM1703CAGLUA523−1.110−4.9542.5661.0027.15
ATOM1704CBGLUA523−1.555−4.2063.8351.0031.08
ATOM1705CGGLUA523−0.830−4.5645.1241.0038.93
ATOM1706CDGLUA523−1.153−3.5856.2581.0046.90
ATOM1707OE1GLUA523−2.225−2.9386.2001.0047.40
ATOM1708OE2GLUA523−0.337−3.4607.2021.0047.39
ATOM1709CGLUA523−1.872−4.3681.3811.0026.10
ATOM1710OGLUA523−2.817−4.9640.8821.0024.25
ATOM1711NHISA524−1.449−3.1820.9401.0024.74
ATOM1712CAHISA524−2.093−2.505−0.1731.0026.17
ATOM1713CBHISA524−1.481−1.125−0.3791.0024.64
ATOM1714CGHISA524−2.233−0.278−1.3551.0030.59
ATOM1715CD2HISA524−3.2270.624−1.1721.0032.15
ATOM1716ND1HISA524−2.008−0.332−2.7131.0027.46
ATOM1717CE1HISA524−2.8290.502−3.3261.0034.58
ATOM1718NE2HISA524−3.5801.094−2.4131.0030.50
ATOM1719CHISA524−1.996−3.294−1.4741.0028.06
ATOM1720OHISA524−2.976−3.419−2.2171.0029.81
ATOM1721NLEUA525−0.811−3.824−1.7461.0027.07
ATOM1722CALEUA525−0.594−4.601−2.9551.0029.30
ATOM1723CBLEUA5250.865−5.039−3.0511.0026.39
ATOM1724CGLEUA5251.307−5.765−4.3211.0029.34
ATOM1725CD1LEUA5250.734−5.076−5.5621.0029.61
ATOM1726CD2LEUA5252.829−5.769−4.3701.0029.22
ATOM1727CLEUA525−1.497−5.822−2.9501.0031.67
ATOM1728OLEUA525−2.128−6.133−3.9571.0032.45
ATOM1729NTYRA526−1.559−6.512−1.8141.0036.14
ATOM1730CATYRA526−2.397−7.698−1.6961.0040.36
ATOM1731CBTYRA526−2.221−8.350−0.3241.0045.27
ATOM1732CGTYRA526−2.849−9.722−0.2291.0050.62
ATOM1733CD1TYRA526−2.114−10.867−0.5371.0054.55
ATOM1734CE1TYRA526−2.698−12.136−0.4821.0057.27
ATOM1735CD2TYRA526−4.188−9.8760.1421.0053.48
ATOM1736CE2TYRA526−4.781−11.1410.2011.0055.93
ATOM1737CZTYRA526−4.029−12.264−0.1131.0056.60
ATOM1738OHTYRA526−4.603−13.515−0.0631.0060.70
ATOM1739CTYRA526−3.852−7.298−1.8931.0042.83
ATOM1740OTYRA526−4.673−8.094−2.3491.0043.49
ATOM1741NSERA527−4.158−6.055−1.5431.0041.55
ATOM1742CASERA527−5.503−5.523−1.6861.0044.04
ATOM1743CBSERA527−5.606−4.169−0.9791.0043.47
ATOM1744OGSERA527−6.954−3.789−0.7861.0047.51
ATOM1745CSERA527−5.817−5.356−3.1721.0044.18
ATOM1746OSERA527−6.883−5.757−3.6421.0044.88
ATOM1747NMETA528−4.883−4.755−3.9011.0041.79
ATOM1748CAMETA528−5.047−4.536−5.3311.0044.04
ATOM1749CBMETA528−3.898−3.679−5.8701.0044.78
ATOM1750CGMETA528−3.965−2.206−5.4681.0045.37
ATOM1751SDMETA528−5.652−1.598−5.2731.0051.83
ATOM1752CEMETA528−5.553−0.004−6.0441.0046.61
ATOM1753CMETA528−5.087−5.871−6.0711.0044.29
ATOM1754OMETA528−5.689−5.979−7.1371.0044.02
ATOM1755NLYSA529−4.443−6.883−5.4991.0046.78
ATOM1756CALYSA529−4.413−8.213−6.0991.0051.28
ATOM1757CBLYSA529−3.550−9.158−5.2611.0050.87
ATOM1758CGLYSA529−2.798−10.204−6.0711.0050.55
ATOM1759CDLYSA529−3.548−11.520−6.1041.0051.25
ATOM1760CELYSA529−2.616−12.694−5.8561.0053.22
ATOM1761NZLYSA529−2.420−12.954−4.4021.0053.22
ATOM1762CLYSA529−5.829−8.768−6.1821.0054.27
ATOM1763OLYSA529−6.325−9.069−7.2661.0055.50
ATOM1764NCYSA530−6.472−8.901−5.0271.0056.71
ATOM1765CACYSA530−7.833−9.416−4.9611.0058.35
ATOM1766CBCYSA530−8.333−9.380−3.5171.0059.78
ATOM1767SGCYSA530−7.289−10.304−2.3581.0063.19
ATOM1768CCYSA530−8.766−8.609−5.8581.0059.36
ATOM1769OCYSA530−9.644−9.169−6.5141.0059.52
ATOM1770NLYSA531−8.569−7.293−5.8881.0059.24
ATOM1771CALYSA531−9.390−6.411−6.7131.0060.14
ATOM1772CBLYSA531−9.158−4.952−6.3171.0058.92
ATOM1773CLYSA531−9.073−6.615−8.1951.0061.48
ATOM1774OLYSA531−9.618−5.928−9.0611.0061.74
ATOM1775NASNA532−8.179−7.561−8.4741.0061.65
ATOM1776CAASNA532−7.783−7.890−9.8401.0061.60
ATOM1777CBASNA532−8.966−8.518−10.5811.0062.28
ATOM1778CGASNA532−8.750−9.985−10.8781.0064.66
ATOM1779OD1ASNA532−8.344−10.352−11.9831.0067.08
ATOM1780ND2ASNA532−9.016−10.836−9.8911.0062.68
ATOM1781CASNA532−7.247−6.710−10.6481.0059.75
ATOM1782OASNA532−7.487−6.615−11.8501.0057.50
ATOM1783NVALA533−6.507−5.822−9.9921.0059.39
ATOM1784CAVALA533−5.954−4.656−10.6691.0058.22
ATOM1785CBVALA533−6.223−3.371−9.8651.0059.20
ATOM1786CG1VALA533−6.181−2.163−10.7851.0059.21
ATOM1787CG2VALA533−7.574−3.467−9.1721.0059.57
ATOM1788CVALA533−4.452−4.767−10.9071.0057.86
ATOM1789OVALA533−3.846−3.874−11.4991.0060.56
ATOM1790NVALA534−3.852−5.863−10.4511.0056.03
ATOM1791CAVALA534−2.417−6.063−10.6211.0054.11
ATOM1792CBVALA534−1.767−6.632−9.3411.0054.02
ATOM1793CG1VALA534−0.300−6.950−9.6011.0052.37
ATOM1794CG2VALA534−1.900−5.635−8.2001.0055.70
ATOM1795CVALA534−2.089−7.008−11.7701.0054.31
ATOM1796OVALA534−2.519−8.164−11.7801.0051.66
ATOM1797NPROA535−1.315−6.527−12.7551.0053.54
ATOM1798CDPROA535−0.749−5.172−12.8741.0054.28
ATOM1799CAPROA535−0.949−7.373−13.8931.0053.24
ATOM1800CBPROA5350.011−6.500−14.6971.0052.71
ATOM1801CGPROA535−0.353−5.102−14.3191.0053.19
ATOM1802CPROA535−0.296−8.664−13.4111.0054.25
ATOM1803OPROA5350.121−8.768−12.2541.0054.56
ATOM1804NLEUA536−0.203−9.645−14.2991.0053.63
ATOM1805CALEUA5360.382−10.926−13.9371.0053.11
ATOM1806CBLEUA536−0.250−12.046−14.7631.0051.88
ATOM1807CGLEUA536−0.686−13.256−13.9381.0051.83
ATOM1808CD1LEUA536−1.953−12.917−13.1731.0049.51
ATOM1809CD2LEUA536−0.905−14.449−14.8541.0053.43
ATOM1810CLEUA5361.895−10.990−14.0811.0052.58
ATOM1811OLEUA5362.414−11.501−15.0751.0055.33
ATOM1812NTYRA5372.601−10.462−13.0871.0048.72
ATOM1813CATYRA5374.057−10.501−13.0931.0044.22
ATOM1814CBTYRA5374.627−9.134−12.7091.0044.52
ATOM1815CGTYRA5374.331−8.053−13.7311.0045.18
ATOM1816CD1TYRA5373.623−6.905−13.3761.0043.77
ATOM1817CE1TYRA5373.334−5.915−14.3171.0045.23
ATOM1818CD2TYRA5374.747−8.187−15.0581.0046.91
ATOM1819CE2TYRA5374.462−7.202−16.0081.0043.93
ATOM1820CZTYRA5373.757−6.071−15.6311.0046.70
ATOM1821OHTYRA5373.472−5.097−16.5651.0048.35
ATOM1822CTYRA5374.401−11.562−12.0561.0041.29
ATOM1823OTYRA5374.330−11.319−10.8561.0041.82
ATOM1824NASPA5384.748−12.748−12.5401.0040.34
ATOM1825CAASPA5385.055−13.896−11.6911.0038.84
ATOM1826CBASPA5385.594−15.037−12.5541.0043.47
ATOM1827CGASPA5384.571−15.531−13.5661.0047.67
ATOM1828OD1ASPA5384.931−16.373−14.4161.0049.33
ATOM1829OD2ASPA5383.405−15.073−13.5111.0048.07
ATOM1830CASPA5385.991−13.676−10.5081.0037.28
ATOM1831OASPA5385.620−13.964−9.3711.0038.55
ATOM1832NLEUA5397.196−13.200−10.7661.0033.83
ATOM1833CALEUA5398.155−12.959−9.6921.0032.80
ATOM1834CBLEUA5399.419−12.323−10.2631.0032.78
ATOM1835CGLEUA53910.561−12.031−9.2921.0030.93
ATOM1836CD1LEUA53910.913−13.280−8.4921.0033.81
ATOM1837CD2LEUA53911.758−11.538−10.0771.0025.92
ATOM1838CLEUA5397.558−12.050−8.6141.0031.85
ATOM1839OLEUA5397.590−12.367−7.4231.0025.63
ATOM1840NLEUA5407.011−10.917−9.0421.0032.07
ATOM1841CALEUA5406.411−9.976−8.1111.0031.03
ATOM1842CBLEUA5405.792−8.800−8.8611.0030.56
ATOM1843CGLEUA5405.124−7.774−7.9451.0031.12
ATOM1844CD1LEUA5406.092−7.357−6.8381.0029.76
ATOM1845CD2LEUA5404.693−6.572−8.7621.0030.85
ATOM1846CLEUA5405.337−10.660−7.2821.0034.55
ATOM1847OLEUA5405.316−10.522−6.0631.0031.60
ATOM1848NLEUA5414.446−11.388−7.9411.0035.64
ATOM1849CALEUA5413.378−12.101−7.2451.0037.84
ATOM1850CBLEUA5412.452−12.771−8.2551.0038.49
ATOM1851CGLEUA5411.244−11.932−8.6781.0039.80
ATOM1852CD1LEUA5410.476−11.476−7.4481.0040.02
ATOM1853CD2LEUA5411.713−10.733−9.4851.0040.48
ATOM1854CLEUA5413.937−13.147−6.2751.0040.10
ATOM1855OLEUA5413.472−13.254−5.1371.0042.72
ATOM1856NGLUA5424.929−13.915−6.7231.0038.45
ATOM1857CAGLUA5425.535−14.932−5.8681.0039.59
ATOM1858CBGLUA5426.738−15.566−6.5641.0041.73
ATOM1859CGGLUA5426.396−16.327−7.8311.0048.34
ATOM1860CDGLUA5426.931−17.747−7.8191.0052.57
ATOM1861OE1GLUA5428.049−17.961−7.2981.0052.70
ATOM1862OE2GLUA5426.230−18.647−8.3311.0053.69
ATOM1863CGLUA5425.989−14.299−4.5531.0039.94
ATOM1864OGLUA5425.567−14.710−3.4721.0040.99
ATOM1865NMETA5436.844−13.287−4.6631.0038.29
ATOM1866CAMETA5437.380−12.580−3.5031.0038.11
ATOM1867CBMETA5438.242−11.408−3.9631.0037.34
ATOM1868CGMETA5439.311−11.797−4.9531.0040.59
ATOM1869SDMETA54310.829−12.223−4.1141.0045.64
ATOM1870CEMETA54312.014−11.399−5.1511.0042.61
ATOM1871CMETA5436.287−12.064−2.5811.0037.94
ATOM1872OMETA5436.413−12.127−1.3581.0039.20
ATOM1873NLEUA5445.218−11.544−3.1751.0039.44
ATOM1874CALEUA5444.100−11.013−2.4081.0040.91
ATOM1875CBLEUA5443.087−10.344−3.3411.0039.88
ATOM1876CGLEUA5441.775−9.905−2.6881.0042.70
ATOM1877CD1LEUA5442.060−8.886−1.5861.0037.35
ATOM1878CD2LEUA5440.854−9.317−3.7411.0038.47
ATOM1879CLEUA5443.420−12.120−1.6141.0042.83
ATOM1880OLEUA5442.957−11.899−0.4961.0042.73
ATOM1881NASPA5453.367−13.313−2.1971.0046.32
ATOM1882CAASPA5452.746−14.456−1.5391.0050.65
ATOM1883CBASPA5452.606−15.617−2.5241.0053.67
ATOM1884CGASPA5451.703−15.278−3.6911.0057.35
ATOM1885OD1ASPA5450.697−14.568−3.4751.0059.99
ATOM1886OD2ASPA5451.999−15.718−4.8241.0059.68
ATOM1887CASPA5453.559−14.898−0.3271.0050.74
ATOM1888OASPA5453.004−15.3880.6571.0049.39
ATOM1889NALAA5464.874−14.723−0.4011.0051.82
ATOM1890CAALAA5465.750−15.0950.7021.0053.12
ATOM1891CBALAA5467.180−14.6780.3951.0053.19
ATOM1892CALAA5465.269−14.4241.9871.0054.67
ATOM1893OALAA5465.476−14.9403.0851.0052.32
ATOM1894NHISA5474.622−13.2701.8381.0056.66
ATOM1895CAHISA5474.102−12.5202.9781.0059.19
ATOM1896CBHISA5474.144−11.0172.6841.0056.70
ATOM1897CGHISA5475.489−10.3942.8961.0054.64
ATOM1898CD2HISA5476.644−10.5062.1991.0053.92
ATOM1899ND1HISA5475.748−9.5143.9251.0052.17
ATOM1900CE1HISA5477.004−9.1113.8531.0052.16
ATOM1901NE2HISA5477.570−9.6982.8141.0051.90
ATOM1902CHISA5472.668−12.9403.3061.0062.77
ATOM1903OHISA5471.842−12.1203.7071.0063.24
ATOM1904NARGA5482.381−14.2243.1331.0068.37
ATOM1905CAARGA5481.053−14.7583.4111.0072.75
ATOM1906CBARGA5480.243−14.8642.1131.0073.73
ATOM1907CGARGA548−1.149−14.2432.1861.0074.04
ATOM1908CDARGA548−1.081−12.7282.2971.0074.50
ATOM1909NEARGA548−2.305−12.1672.8631.0075.04
ATOM1910CZARGA548−2.478−10.8803.1491.0075.59
ATOM1911NH1ARGA548−1.506−10.0062.9191.0075.79
ATOM1912NH2ARGA548−3.627−10.4643.6621.0076.00
ATOM1913CARGA5481.179−16.1334.0611.0074.94
ATOM1914OARGA5480.197−16.6974.5491.0075.15
ATOM1915NLEUA5492.398−16.6654.0631.0076.49
ATOM1916CALEUA5492.669−17.9694.6531.0078.14
ATOM1917CBLEUA5492.971−18.9863.5571.0077.55
ATOM1918CLEUA5493.846−17.8705.6191.0079.13
ATOM1919OLEUA5494.892−17.3175.2151.0080.40
ATOM1920OXTLEUA5493.708−18.3416.7691.0079.46
HETATM1921CP9DESA6005.390−3.061−6.1391.0021.38
HETATM1922CP8DESA6005.834−1.989−5.1341.0022.41
HETATM1923CP7DESA6005.038−0.714−5.2361.0021.32
HETATM1924CP6DESA6003.587−0.864−5.0621.0025.87
HETATM1925CP1DESA6002.987−0.978−3.7841.0023.92
HETATM1926CP2DESA6001.597−1.150−3.6841.0029.77
HETATM1927CP3DESA6000.842−1.214−4.8711.0031.40
HETATM1928OP3DESA600−0.506−1.419−4.8241.0033.36
HETATM1929CP4DESA6001.421−1.099−6.1431.0027.01
HETATM1930CP5DESA6002.793−0.929−6.2301.0027.40
HETATM1931C7DESA6005.6710.461−5.4821.0022.39
HETATM1932C6DESA6007.1130.561−5.8091.0021.75
HETATM1933C5DESA6007.5410.306−7.1311.0019.97
HETATM1934C4DESA6008.8890.429−7.4771.0023.81
HETATM1935C3DESA6009.8140.804−6.4881.0021.88
HETATM1936O3DESA60011.1250.901−6.8391.0022.32
HETATM1937C2DESA6009.4231.066−5.1611.0019.74
HETATM1938C1DESA6008.0660.937−4.8381.0021.25
HETATM1939C8DESA6004.8941.765−5.4431.0021.47
HETATM1940C9DESA6004.9592.468−4.0701.0021.38
HETATM1941CLCLA60114.781−3.035−17.7391.0024.10
ATOM1942CBSERB30512.32121.08625.2951.0064.27
ATOM1943CSERB30512.67222.10227.5481.0064.37
ATOM1944OSERB30513.70122.76027.7021.0066.90
ATOM1945NSERB30512.04523.52125.6061.0063.72
ATOM1946CASERB30511.87522.18726.2511.0064.21
ATOM1947NLEUB30612.19321.29328.4841.0063.09
ATOM1948CALEUB30612.88421.13329.7571.0060.98
ATOM1949CBLEUB30611.88421.20030.9131.0061.23
ATOM1950CGLEUB30612.22120.41732.1831.0062.23
ATOM1951CD1LEUB30613.30421.14432.9661.0062.56
ATOM1952CD2LEUB30610.96520.25833.0271.0064.31
ATOM1953CLEUB30613.66019.81929.8031.0058.39
ATOM1954OLEUB30614.57019.65430.6141.0058.56
ATOM1955NALAB30713.29318.88128.9331.0054.82
ATOM1956CAALAB30713.97117.58928.8611.0050.62
ATOM1957CBALAB30713.09216.58428.1431.0051.30
ATOM1958CALAB30715.30317.71928.1221.0046.84
ATOM1959OALAB30716.19616.88528.2741.0045.62
ATOM1960NLEUB30815.43118.76927.3201.0043.46
ATOM1961CALEUB30816.64318.98326.5421.0043.01
ATOM1962CBLEUB30816.41320.10025.5261.0041.32
ATOM1963CGLEUB30816.31519.70824.0511.0043.10
ATOM1964CD1LEUB30815.94218.23923.9031.0040.51
ATOM1965CD2LEUB30815.28720.60223.3751.0039.80
ATOM1966CLEUB30817.87419.29727.3851.0042.11
ATOM1967OLEUB30819.00019.10226.9321.0044.34
ATOM1968NSERB30917.66919.77528.6081.0040.88
ATOM1969CASERB30918.79620.10029.4751.0042.79
ATOM1970CBSERB30918.56221.44730.1631.0041.25
ATOM1971OGSERB30917.45921.37931.0461.0046.67
ATOM1972CSERB30919.07219.02830.5291.0042.60
ATOM1973OSERB30920.05319.11931.2691.0044.18
ATOM1974NLEUB31018.21718.01230.5961.0039.44
ATOM1975CALEUB31018.39416.93631.5691.0037.62
ATOM1976CBLEUB31017.20515.96931.4991.0038.84
ATOM1977CGLEUB31016.21615.87332.6681.0042.43
ATOM1978CD1LEUB31016.04017.21933.3551.0042.55
ATOM1979CD2LEUB31014.88115.38032.1381.0039.69
ATOM1980CLEUB31019.69116.17431.2851.0034.11
ATOM1981OLEUB31020.11116.07030.1391.0034.41
ATOM1982NTHRB31120.33915.66232.3261.0034.04
ATOM1983CATHRB31121.56414.88832.1271.0032.34
ATOM1984CBTHRB31122.43414.82433.3991.0031.75
ATOM1985OG1THRB31121.72414.11634.4201.0036.20
ATOM1986CG2THRB31122.78216.21233.8931.0031.05
ATOM1987CTHRB31121.14513.46031.7901.0032.37
ATOM1988OTHRB31119.96713.11731.8991.0028.16
ATOM1989NALAB31222.10612.62831.3961.0033.23
ATOM1990CAALAB31221.81111.23731.0531.0035.63
ATOM1991CBALAB31223.07710.52730.5771.0034.00
ATOM1992CALAB31221.21010.48932.2401.0034.29
ATOM1993OALAB31220.2269.76632.0891.0033.10
ATOM1994NASPB31321.80010.66533.4191.0033.90
ATOM1995CAASPB31321.3049.99434.6151.0034.19
ATOM1996CBASPB31322.25810.21935.7881.0042.09
ATOM1997CGASPB31323.4949.35835.7001.0044.87
ATOM1998OD1ASPB31324.5869.85836.0401.0051.57
ATOM1999OD2ASPB31323.3778.18435.2901.0046.79
ATOM2000CASPB31319.92510.52034.9711.0031.99
ATOM2001OASPB31319.0569.76835.4261.0032.03
ATOM2002NGLNB31419.73311.81934.7631.0029.38
ATOM2003CAGLNB31418.45812.45735.0461.0029.73
ATOM2004CBGLNB31418.56213.96634.8321.0032.88
ATOM2005CGGLNB31418.97014.73236.0851.0036.47
ATOM2006CDGLNB31419.21316.20835.8151.0036.76
ATOM2007OE1GLNB31419.30016.63434.6641.0038.79
ATOM2008NE2GLNB31419.32716.99536.8801.0039.72
ATOM2009CGLNB31417.40911.87334.1161.0029.11
ATOM2010OGLNB31416.27411.62034.5221.0028.82
ATOM2011NMETB31517.80111.65732.8641.0027.27
ATOM2012CAMETB31516.90011.07931.8721.0030.41
ATOM2013CBMETB31517.59511.02930.5091.0030.10
ATOM2014CGMETB31516.78710.34529.4211.0038.02
ATOM2015SDMETB31515.25211.22029.0651.0041.12
ATOM2016CEMETB31515.89012.83528.6111.0039.32
ATOM2017CMETB31516.4909.66532.3111.0027.99
ATOM2018OMETB31515.3029.35132.3961.0026.60
ATOM2019NVALB31617.4818.82332.5981.0027.26
ATOM2020CAVALB31617.2297.44733.0271.0024.54
ATOM2021CBVALB31618.5546.70833.3511.0026.22
ATOM2022CG1VALB31618.2725.40434.0961.0029.81
ATOM2023CG2VALB31619.3026.41032.0741.0029.75
ATOM2024CVALB31616.3267.38934.2581.0027.22
ATOM2025OVALB31615.3976.57934.3181.0025.55
ATOM2026NSERB31716.6018.24335.2421.0024.40
ATOM2027CASERB31715.7998.26836.4601.0027.63
ATOM2028CBSERB31716.3589.29437.4511.0031.68
ATOM2029OGSERB31717.4928.77138.1121.0039.97
ATOM2030CSERB31714.3468.60036.1541.0026.73
ATOM2031OSERB31713.4347.93236.6481.0025.65
ATOM2032NALAB31814.1359.63435.3421.0024.19
ATOM2033CAALAB31812.78610.04934.9691.0024.17
ATOM2034CBALAB31812.85011.25034.0221.0021.44
ATOM2035CALAB31812.0388.89034.3061.0021.63
ATOM2036OALAB31810.9028.59834.6481.0020.25
ATOM2037NLEUB31912.6958.22533.3641.0023.37
ATOM2038CALEUB31912.0987.10232.6521.0025.42
ATOM2039CBLEUB31913.0506.63531.5481.0022.03
ATOM2040CGLEUB31913.2647.62230.3941.0020.71
ATOM2041CD1LEUB31914.1466.99529.3311.0023.60
ATOM2042CD2LEUB31911.9188.02029.8031.0023.82
ATOM2043CLEUB31911.7295.92633.5641.0027.26
ATOM2044OLEUB31910.6155.39633.4881.0028.91
ATOM2045NLEUB32012.6565.51634.4261.0026.58
ATOM2046CALEUB32012.3994.40535.3341.0026.73
ATOM2047CBLEUB32013.6574.07536.1451.0026.87
ATOM2048CGLEUB32014.8463.46035.3981.0026.15
ATOM2049CD1LEUB32016.0533.37536.3301.0028.04
ATOM2050CD2LEUB32014.4842.07634.8951.0026.96
ATOM2051CLEUB32011.2494.72236.2901.0029.19
ATOM2052OLEUB32010.4493.84936.6311.0026.66
ATOM2053NASPB32111.1605.97636.7191.0029.72
ATOM2054CAASPB32110.1126.37137.6471.0031.36
ATOM2055CBASPB32110.4947.68338.3361.0036.60
ATOM2056CGASPB32111.4077.46139.5351.0046.11
ATOM2057OD1ASPB32110.8977.05840.6051.0046.64
ATOM2058OD2ASPB32112.6357.67639.4021.0045.98
ATOM2059CASPB3218.7426.49436.9891.0028.29
ATOM2060OASPB3217.7156.43237.6611.0027.19
ATOM2061NALAB3228.7266.65035.6721.0028.34
ATOM2062CAALAB3227.4696.77934.9501.0025.55
ATOM2063CBALAB3227.6687.66833.7281.0024.11
ATOM2064CALAB3226.9115.42034.5231.0022.80
ATOM2065OALAB3225.8105.33833.9791.0024.54
ATOM2066NGLUB3237.6624.35534.7811.0020.16
ATOM2067CAGLUB3237.2293.02134.3861.0021.44
ATOM2068CBGLUB3238.1961.98234.9381.0023.72
ATOM2069CGGLUB3239.3931.74634.0241.0023.58
ATOM2070CDGLUB3238.9881.13432.6851.0025.23
ATOM2071OE1GLUB3238.8521.88131.6921.0021.74
ATOM2072OE2GLUB3238.809−0.09532.6241.0025.49
ATOM2073CGLUB3235.7962.69634.8101.0022.35
ATOM2074OGLUB3235.4092.92635.9511.0022.34
ATOM2075NPROB3244.9862.16533.8801.0019.10
ATOM2076CDPROB3245.2861.80632.4831.0019.11
ATOM2077CAPROB3243.6071.83934.2421.0022.04
ATOM2078CBPROB3242.9191.65832.8931.0021.96
ATOM2079CGPROB3244.0151.13732.0151.0024.13
ATOM2080CPROB3243.6190.55635.0601.0023.44
ATOM2081OPROB3244.590−0.20035.0281.0022.20
ATOM2082NPROB3252.5400.28735.8011.0024.88
ATOM2083CDPROB3251.2991.06835.9451.0026.67
ATOM2084CAPROB3252.520−0.94036.6031.0025.10
ATOM2085CBPROB3251.394−0.69137.5951.0027.09
ATOM2086CGPROB3250.4480.20536.8541.0026.87
ATOM2087CPROB3252.270−2.19235.7761.0025.77
ATOM2088OPROB3251.853−2.11834.6171.0021.69
ATOM2089NILEB3262.538−3.34436.3791.0024.05
ATOM2090CAILEB3262.301−4.62035.7221.0022.51
ATOM2091CBILEB3263.303−5.68836.1851.0025.81
ATOM2092CG2ILEB3263.011−7.01835.4811.0023.78
ATOM2093CG1ILEB3264.729−5.20935.9001.0025.75
ATOM2094CD1ILEB3265.241−5.58534.5331.0027.78
ATOM2095CILEB3260.893−5.02036.1491.0023.63
ATOM2096OILEB3260.632−5.23137.3321.0024.81
ATOM2097NLEUB327−0.018−5.10435.1881.0019.44
ATOM2098CALEUB327−1.399−5.43735.4931.0017.03
ATOM2099CBLEUB327−2.336−4.74734.4931.0018.39
ATOM2100CGLEUB327−2.201−3.21634.3731.0020.69
ATOM2101CD1LEUB327−3.245−2.67933.4061.0014.87
ATOM2102CD2LEUB327−2.384−2.57035.7421.0014.39
ATOM2103CLEUB327−1.662−6.92835.4991.0019.87
ATOM2104OLEUB327−0.854−7.72235.0141.0020.90
ATOM2105NTYRB328−2.803−7.30036.0661.0020.92
ATOM2106CATYRB328−3.202−8.69236.1351.0021.79
ATOM2107CBTYRB328−3.658−9.05037.5501.0022.91
ATOM2108CGTYRB328−2.515−9.37638.4681.0024.60
ATOM2109CD1TYRB328−2.118−10.69638.6771.0025.93
ATOM2110CE1TYRB328−1.034−11.00039.4981.0028.10
ATOM2111CD2TYRB328−1.802−8.36239.1031.0029.46
ATOM2112CE2TYRB328−0.716−8.65439.9261.0035.30
ATOM2113CZTYRB328−0.338−9.97340.1171.0032.59
ATOM2114OHTYRB3280.739−10.25740.9231.0037.24
ATOM2115CTYRB328−4.336−8.94435.1681.0022.25
ATOM2116OTYRB328−5.115−8.03934.8491.0019.77
ATOM2117NSERB329−4.420−10.18034.6981.0025.81
ATOM2118CASERB329−5.480−10.57133.7871.0029.39
ATOM2119CBSERB329−5.002−11.71032.8871.0027.65
ATOM2120OGSERB329−6.091−12.32932.2331.0028.98
ATOM2121CSERB329−6.625−11.04234.6731.0033.17
ATOM2122OSERB329−6.453−11.15735.8881.0032.52
ATOM2123NGLUB330−7.792−11.28934.0841.0038.75
ATOM2124CAGLUB330−8.930−11.77634.8591.0044.91
ATOM2125CBGLUB330−10.134−11.99933.9511.0045.63
ATOM2126CGLUB330−8.493−13.09335.4911.0048.62
ATOM2127OGLUB330−7.739−13.85134.8821.0052.37
ATOM2128NTYRB331−8.952−13.36636.7071.0051.75
ATOM2129CATYRB331−8.575−14.59637.3961.0055.25
ATOM2130CBTYRB331−8.538−14.36538.9111.0053.04
ATOM2131CGTYRB331−9.769−13.66839.4401.0050.70
ATOM2132CD1TYRB331−10.880−14.40039.8561.0047.09
ATOM2133CE1TYRB331−12.035−13.76240.2921.0046.43
ATOM2134CD2TYRB331−9.842−12.27339.4781.0047.52
ATOM2135CE2TYRB331−10.993−11.62539.9131.0043.98
ATOM2136CZTYRB331−12.086−12.37640.3141.0044.33
ATOM2137OHTYRB331−13.239−11.74740.7151.0045.31
ATOM2138CTYRB331−9.528−15.74337.0751.0060.11
ATOM2139OTYRB331−10.748−15.56937.0661.0063.13
ATOM2140NASPB332−8.952−16.91336.8091.0061.60
ATOM2141CAASPB332−9.704−18.12436.4901.0063.58
ATOM2142CBASPB332−10.637−17.89535.2981.0065.11
ATOM2143CGASPB332−11.723−18.95335.2001.0065.32
ATOM2144OD1ASPB332−11.420−20.13635.4631.0063.69
ATOM2145OD2ASPB332−12.876−18.60234.8661.0063.61
ATOM2146CASPB332−8.707−19.22736.1531.0062.86
ATOM2147OASPB332−7.853−19.05635.2871.0062.26
ATOM2148NPROB333−8.811−20.37936.8331.0063.96
ATOM2149CDPROB333−9.808−20.69037.8751.0064.24
ATOM2150CAPROB333−7.901−21.50336.5961.0064.24
ATOM2151CBPROB333−8.015−22.32537.8741.0064.70
ATOM2152CGPROB333−9.410−22.07138.3471.0065.00
ATOM2153CPROB333−8.180−22.34035.3511.0063.90
ATOM2154OPROB333−7.384−23.21435.0071.0063.70
ATOM2155NTHRB334−9.303−22.08434.6831.0063.83
ATOM2156CATHRB334−9.649−22.83233.4751.0063.77
ATOM2157CBTHRB334−11.065−22.47732.9751.0064.63
ATOM2158OG1THRB334−11.132−21.07832.6751.0065.95
ATOM2159CG2THRB334−12.102−22.81734.0361.0065.09
ATOM2160CTHRB334−8.634−22.49932.3881.0062.62
ATOM2161OTHRB334−8.931−21.77431.4371.0060.15
ATOM2162NARGB335−7.432−23.04332.5531.0063.14
ATOM2163CAARGB335−6.324−22.82031.6331.0060.70
ATOM2164CBARGB335−5.130−23.66732.0501.0058.73
ATOM2165CARGB335−6.667−23.08630.1741.0059.71
ATOM2166OARGB335−6.302−22.29829.2981.0062.33
ATOM2167NPROB336−7.377−24.19429.8841.0055.25
ATOM2168CDPROB336−7.938−25.22730.7691.0053.53
ATOM2169CAPROB336−7.698−24.43728.4711.0050.10
ATOM2170CBPROB336−8.399−25.79928.4761.0049.70
ATOM2171CGPROB336−8.164−26.37229.8441.0050.71
ATOM2172CPROB336−8.602−23.32427.9541.0044.54
ATOM2173OPROB336−9.809−23.34228.1791.0044.14
ATOM2174NPHEB337−8.007−22.35027.2741.0039.18
ATOM2175CAPHEB337−8.764−21.22326.7421.0038.25
ATOM2176CBPHEB337−7.850−20.00326.5671.0036.98
ATOM2177CGPHEB337−7.229−19.51727.8461.0036.81
ATOM2178CD1PHEB337−5.846−19.51128.0021.0038.89
ATOM2179CD2PHEB337−8.023−19.06228.8931.0035.97
ATOM2180CE1PHEB337−5.262−19.05929.1851.0036.85
ATOM2181CE2PHEB337−7.449−18.60830.0791.0037.15
ATOM2182CZPHEB337−6.064−18.60730.2241.0038.40
ATOM2183CPHEB337−9.420−21.53525.4021.0036.81
ATOM2184OPHEB337−8.962−22.39924.6581.0036.26
ATOM2185NSERB338−10.504−20.82825.1071.0035.85
ATOM2186CASERB338−11.198−20.98123.8361.0034.76
ATOM2187CBSERB338−12.713−20.94824.0351.0034.85
ATOM2188OGSERB338−13.164−19.62124.2351.0033.53
ATOM2189CSERB338−10.761−19.76123.0371.0034.99
ATOM2190OSERB338−10.143−18.85523.5911.0034.32
ATOM2191NGLUB339−11.075−19.72221.7501.0033.01
ATOM2192CAGLUB339−10.682−18.57920.9501.0033.94
ATOM2193CBGLUB339−11.146−18.73719.5011.0033.79
ATOM2194CGGLUB339−10.758−17.55318.6231.0039.11
ATOM2195CDGLUB339−10.865−17.85217.1371.0043.17
ATOM2196OE1GLUB339−11.990−17.78516.6001.0945.28
ATOM2197OE2GLUB339−9.824−18.15216.5101.0039.19
ATOM2198CGLUB339−11.265−17.29521.5311.0034.28
ATOM2199OGLUB339−10.575−16.28321.6311.0033.65
ATOM2200NALAB340−12.535−17.33921.9201.0031.12
ATOM2201CAALAB340−13.194−16.16422.4691.0029.10
ATOM2202CBALAB340−14.696−16.41222.5731.0033.84
ATOM2203CALAB340−12.639−15.73123.8261.0028.98
ATOM2204OALAB340−12.431−14.54124.0601.0030.48
ATOM2205NSERB341−12.407−16.69124.7191.0026.66
ATOM2206CASERB341−11.882−16.38626.0441.0024.26
ATOM2207CBSERB341−11.867−17.64326.9231.0027.04
ATOM2208OGSERB341−10.851−18.54126.5151.0033.84
ATOM2209CSERB341−10.479−15.79325.9601.0023.97
ATOM2210OSERB341−10.171−14.82426.6511.0021.56
ATOM2211NMETB342−9.631−16.36825.1141.0026.83
ATOM2212CAMETB342−8.271−15.86524.9541.0027.24
ATOM2213CBMETB342−7.477−16.75824.0011.0030.45
ATOM2214CGMETB342−6.038−16.30023.8021.0035.35
ATOM2215SDMETB342−4.866−17.66723.7771.0044.57
ATOM2216CEMETB342−4.034−17.34122.2441.0041.37
ATOM2217CMETB342−8.322−14.44824.3851.0025.31
ATOM2218OMETB342−7.653−13.54124.8741.0026.67
ATOM2219NMETB343−9.114−14.27823.3451.0025.75
ATOM2220CAMETB343−9.262−12.97922.7121.0025.47
ATOM2221CBMETB343−10.210−13.08821.5281.0023.51
ATOM2222CGMETB343−9.540−13.61820.2731.0028.86
ATOM2223SDMETB343−8.325−12.45619.6091.0029.25
ATOM2224CEMETB343−9.344−11.01519.3711.0028.74
ATOM2225CMETB343−9.798−11.96623.7121.0025.37
ATOM2226OMETB343−9.360−10.81023.7281.0024.98
ATOM2227NGLYB344−10.739−12.40324.5361.0023.91
ATOM2228CAGLYB344−11.320−11.52625.5361.0022.43
ATOM2229CGLYB344−10.313−11.10326.5921.0022.06
ATOM2230OGLYB344−10.262−9.93426.9821.0020.87
ATOM2231NLEUB345−9.511−12.04827.0631.0019.36
ATOM2232CALEUB345−8.520−11.74828.0831.0025.74
ATOM2233CBLEUB345−7.886−13.04028.6001.0026.78
ATOM2234CGLEUB345−8.794−14.01029.3621.0030.04
ATOM2235CD1LEUB345−8.099−15.35729.4881.0028.39
ATOM2236CD2LEUB345−9.122−13.44330.7361.0029.93
ATOM2237CLEUB345−7.425−10.82227.5501.0023.24
ATOM2238OLEUB345−7.037−9.86528.2121.0023.43
ATOM2239NLEUB346−6.937−11.10826.3501.0021.92
ATOM2240CALEUB346−5.874−10.30325.7631.0022.71
ATOM2241CBLEUB346−5.343−10.96224.4861.0023.17
ATOM2242CGLEUB346−4.684−12.33124.6681.0020.66
ATOM2243CD1LEUB346−4.303−12.91623.3091.0018.75
ATOM2244CD2LEUB346−3.464−12.18825.5531.0020.84
ATOM2245CLEUB346−6.304−8.87325.4581.0022.99
ATOM2246OLEUB346−5.540−7.93525.6951.0022.07
ATOM2247NTHRB347−7.516−8.69924.9371.0020.53
ATOM2248CATHRB347−7.987−7.35724.6081.0021.89
ATOM2249CBTHRB347−9.152−7.38823.6011.0021.65
ATOM2250OG1THRB347−10.218−8.19024.1231.0019.65
ATOM2251CG2THRB347−8.676−7.95522.2621.0022.01
ATOM2252CTHRB347−8.426−6.59025.8531.0023.60
ATOM2253OTHRB347−8.358−5.35725.8831.0020.31
ATOM2254NASNB348−8.884−7.31426.8741.0022.27
ATOM2255CAASNB348−9.293−6.66728.1141.0023.99
ATOM2256CBASNB348−10.008−7.64229.0561.0022.32
ATOM2257CGASNB348−10.342−7.02230.3981.0028.26
ATOM2258OD1ASNB348−9.478−6.74631.2161.0027.14
ATOM2259ND2ASNB348−11.647−6.76430.6251.0027.02
ATOM2260CASNB348−8.035−6.12028.7981.0019.48
ATOM2261OASNB348−8.014−4.99129.2711.0018.26
ATOM2262NLEUB349−6.984−6.93128.8321.0019.07
ATOM2263CALEUB349−5.724−6.51629.4461.0020.37
ATOM2264CBLEUB349−4.716−7.67429.4341.0018.21
ATOM2265CGLEUB349−3.297−7.31629.8891.0018.24
ATOM2266CD1LEUB349−3.323−6.90431.3561.0012.44
ATOM2267CD2LEUB349−2.370−8.50429.6721.0021.28
ATOM2268CLEUB349−5.131−5.30728.7181.0019.92
ATOM2269OLEUB349−4.738−4.32229.3491.0016.56
ATOM2270NALAB350−5.067−5.39127.3911.0016.67
ATOM2271CAALAB350−4.529−4.30826.5781.0017.11
ATOM2272CBALAB350−4.587−4.69025.0951.0014.15
ATOM2273CALAB350−5.272−2.98826.8051.0017.92
ATOM2274OALAB350−4.650−1.92626.9041.0018.71
ATOM2275NASPB351−6.600−3.05326.8571.0017.51
ATOM2276CAASPB351−7.409−1.85627.0741.0016.57
ATOM2277CBASPB351−8.902−2.20227.0411.0018.97
ATOM2278CGASPB351−9.785−0.97426.8581.0021.80
ATOM2279OD1ASPB351−9.660−0.29225.8241.0024.62
ATOM2280OD2ASPB351−10.604−0.68227.7541.0022.78
ATOM2281CASPB351−7.064−1.22828.4151.0016.81
ATOM2282OASPB351−6.963−0.00928.5341.0015.75
ATOM2283NARGB352−6.894−2.05629.4381.0013.97
ATOM2284CAARGB352−6.552−1.50930.7421.0016.09
ATOM2285CBARGB352−6.728−2.57131.8331.0015.78
ATOM2286CGARGB352−8.189−2.81932.1891.0017.93
ATOM2287CDARGB352−8.323−3.88233.2791.0019.84
ATOM2288NEARGB352−8.010−5.22232.7851.0021.36
ATOM2289CZARGB352−7.187−6.07533.3871.0021.18
ATOM2290NH1ARGB352−6.579−5.74134.5161.0020.51
ATOM2291NH2ARGB352−6.980−7.27532.8641.0028.51
ATOM2292CARGB352−5.123−0.97530.7281.0015.81
ATOM2293OARGB352−4.8350.05731.3391.0015.61
ATOM2294NGLUB353−4.231−1.66530.0191.0015.45
ATOM2295CAGLUB353−2.838−1.22829.9351.0016.59
ATOM2296CBGLUB353−1.990−2.24329.1681.0014.64
ATOM2297CGGLUB353−1.554−3.45629.9731.0018.23
ATOM2298CDGLUB353−0.620−4.35529.1761.0022.72
ATOM2299OE1GLUB353−1.099−5.07828.2751.0021.94
ATOM2300OE2GLUB3530.599−4.32429.4421.0024.41
ATOM2301CGLUB353−2.7290.11929.2191.0015.85
ATOM2302OGLUB353−1.8720.93929.5401.0013.76
ATOM2303NLEUB354−3.5940.33528.2351.0012.93
ATOM2304CALEUB354−3.5561.57527.4721.0015.33
ATOM2305CBLEUB354−4.6161.53426.3601.0016.44
ATOM2306CGLEUB354−4.1740.75025.1121.0017.03
ATOM2307CD1LEUB354−5.3730.50924.1891.0016.70
ATOM2308CD2LEUB354−3.0691.53124.3841.0014.52
ATOM2309CLEUB354−3.7472.80528.3611.0012.78
ATOM2310OLEUB354−3.1233.85028.1411.0014.28
ATOM2311NVALB355−4.6002.68229.3691.0012.60
ATOM2312CAVALB355−4.8443.79130.2791.0016.78
ATOM2313CBVALB355−5.9253.42931.3271.0016.84
ATOM2314CG1VALB355−6.0704.56132.3441.0019.88
ATOM2315CG2VALB355−7.2543.18730.6391.0019.33
ATOM2316CVALB355−3.5334.16130.9861.0019.17
ATOM2317OVALB355−3.1585.32831.0491.0017.30
ATOM2318NHISB356−2.8263.16031.4991.0019.68
ATOM2319CAHISB356−1.5593.41832.1771.0020.64
ATOM2320CBHISB356−1.1102.17432.9451.0021.03
ATOM2321CGHISB356−2.0181.81834.0851.0022.88
ATOM2322CD2HISB356−3.1281.04534.1351.0021.70
ATOM2323ND1HISB356−1.8382.31235.3581.0019.24
ATOM2324CE1HISB356−2.8021.86036.1451.0018.84
ATOM2325NE2HISB356−3.5981.08835.4261.0017.92
ATOM2326CHISB356−0.4793.86131.1841.0019.67
ATOM2327OHISB3560.4244.61431.5471.0019.61
ATOM2328NMETB357−0.5663.41329.9311.0014.92
ATOM2329CAMETB3570.4283.83028.9391.0015.13
ATOM2330CBMETB3570.2393.09927.6041.0013.94
ATOM2331CGMETB3571.1493.63126.4761.0014.71
ATOM2332SDMETB3570.7473.01424.8261.0017.75
ATOM2333CEMETB3570.7461.22225.1221.0015.21
ATOM2334CMETB3570.3165.33428.6991.0014.94
ATOM2335OMETB3571.3196.03128.5601.0017.02
ATOM2336NILEB358−0.9095.83928.6591.0018.01
ATOM2337CAILEB358−1.1227.26328.4231.0019.77
ATOM2338CBILEB358−2.6347.57728.2871.0023.11
ATOM2339CG2ILEB358−2.8799.08028.4501.0025.00
ATOM2340CG1ILEB358−3.1377.10526.9131.0024.19
ATOM2341CD1ILEB358−4.6006.65326.8901.0020.17
ATOM2342CILEB358−0.5018.10029.5501.0022.93
ATOM2343OILEB3580.0809.15329.2991.0023.33
ATOM2344NASNB359−0.6197.63130.7901.0022.34
ATOM2345CAASNB359−0.0298.34131.9241.0023.24
ATOM2346CBASNB359−0.4807.72633.2241.0025.10
ATOM2347CGASNB359−1.8318.17133.6491.0032.65
ATOM2348OD1ASNB359−2.4219.06933.0421.0032.98
ATOM2349ND2ASNB359−2.3647.54934.6911.0033.87
ATOM2350CASNB3591.4738.30631.8371.0024.77
ATOM2351OASNB3592.1529.28532.1491.0024.19
ATOM2352NTRPB3601.9957.14931.4381.0020.82
ATOM2353CATRPB3603.4396.96531.3101.0019.29
ATOM2354CBTRPB3603.7545.52430.8781.0018.59
ATOM2355CGTRPB3605.0855.36330.1761.0018.21
ATOM2356CD2TRPB3605.3105.30828.7561.0014.38
ATOM2357CE2TRPB3606.6985.12928.5611.0013.42
ATOM2358CE3TRPB3604.4755.39227.6331.0015.52
ATOM2359CD1TRPB3606.3065.22130.7621.0013.34
ATOM2360NE1TRPB3607.2835.07829.8001.0016.05
ATOM2361CZ2TRPB3607.2725.03227.2881.0016.84
ATOM2362CZ3TRPB3605.0455.29626.3631.0015.11
ATOM2363CH2TRPB3606.4315.11526.2021.0016.12
ATOM2364CTRPB3603.9797.93930.2731.0020.13
ATOM2365OTRPB3604.9918.60630.4971.0017.26
ATOM2366NALAB3613.2958.01229.1351.0019.34
ATOM2367CAALAB3613.7088.90028.0511.0022.01
ATOM2368CBALAB3612.6828.85526.9211.0019.53
ATOM2369CALAB3613.88310.33628.5521.0022.39
ATOM2370OALAB3614.85811.00528.2101.0019.57
ATOM2371NLYSB3622.93210.79429.3611.0021.96
ATOM2372CALYSB3622.96612.13929.9231.0026.45
ATOM2373CBLYSB3621.74112.36330.8111.0029.79
ATOM2374CGLYSB3620.42612.41730.0641.0033.57
ATOM2375CDLYSB362−0.56313.30430.8051.0036.83
ATOM2376CELYSB362−1.62012.49031.5121.0036.89
ATOM2377NZLYSB362−2.87313.27631.6641.0039.07
ATOM2378CLYSB3624.22312.37930.7571.0027.77
ATOM2379OLYSB3624.66113.51730.9221.0026.93
ATOM2380NARGB3634.80511.30231.2781.0026.61
ATOM2381CAARGB3635.99611.41432.1091.0027.74
ATOM2382CBARGB3635.88710.45733.2981.0028.93
ATOM2383CGARGB3634.65010.70434.1581.0036.07
ATOM2384CDARGB3634.5699.74535.3441.0042.83
ATOM2385NEARGB3634.4778.34434.9281.0049.79
ATOM2386CZARGB3633.3957.58235.0801.0051.48
ATOM2387NH1ARGB3632.3008.08135.6481.0052.17
ATOM2388NH2ARGB3633.4056.31634.6681.0040.24
ATOM2389CARGB3637.30811.19031.3671.0025.80
ATOM2390OARGB3638.37411.18331.9751.0029.36
ATOM2391NVALB3647.23111.00930.0531.0024.28
ATOM2392CAVALB3648.43110.82329.2481.0021.87
ATOM2393CBVALB3648.11610.04827.9471.0021.84
ATOM2394CG1VALB3649.26710.18426.9681.0015.85
ATOM2395CG2VALB3647.8608.56028.2681.0016.24
ATOM2396CVALB3648.92512.24128.9231.0028.14
ATOM2397OVALB3648.21913.02328.2851.0024.24
ATOM2398NPROB36510.14112.59129.3751.0028.57
ATOM2399CDPROB36511.06111.72630.1371.0030.58
ATOM2400CAPROB36510.71913.91929.1381.0032.16
ATOM2401CBPROB36512.18913.73929.5071.0032.70
ATOM2402CGPROB36512.17012.67130.5451.0033.35
ATOM2403CPROB36510.54614.46427.7261.0032.22
ATOM2404OPROB36511.05613.89726.7661.0037.04
ATOM2405NGLYB3669.82115.57027.6091.0034.09
ATOM2406CAGLYB3669.61216.18226.3101.0032.54
ATOM2407CGLYB3668.24115.96925.7001.0033.46
ATOM2408OGLYB3667.79116.77924.8861.0033.73
ATOM2409NPHEB3677.56414.89526.0961.0031.08
ATOM2410CAPHEB3676.25014.59325.5421.0028.60
ATOM2411CBPHEB3675.74513.24426.0581.0025.96
ATOM2412CGPHEB3674.62912.67125.2391.0022.75
ATOM2413CD1PHEB3673.31312.77125.6691.0022.62
ATOM2414CD2PHEB3674.89712.02524.0331.0022.29
ATOM2415CE1PHEB3672.27212.23324.9141.0025.63
ATOM2416CE2PHEB3673.86711.48623.2721.0020.82
ATOM2417CZPHEB3672.55311.58823.7111.0025.50
ATOM2418CPHEB3675.17815.64625.7811.0026.79
ATOM2419OPHEB3674.45816.00124.8541.0023.37
ATOM2420NVALB3685.04916.14327.0091.0031.26
ATOM2421CAVALB3684.02017.15127.2771.0035.71
ATOM2422CBVALB3683.81717.41228.7951.0035.98
ATOM2423CG1VALB3682.94416.32029.3921.0037.64
ATOM2424CG2VALB3685.15717.49529.5081.0035.81
ATOM2425CVALB3684.32818.48226.5981.0035.87
ATOM2426OVALB3683.45019.33026.4571.0037.71
ATOM2427NASPB3695.57218.66526.1751.0035.49
ATOM2428CAASPB3695.95019.90425.5031.0036.54
ATOM2429CBASPB3697.46619.96325.3091.0039.79
ATOM2430CGASPB3698.21320.16926.6151.0044.33
ATOM2431OD1ASPB3699.40919.80726.6841.0048.45
ATOM2432OD2ASPB3697.60420.69327.5721.0043.27
ATOM2433CASPB3695.24819.99724.1491.0034.49
ATOM2434OASPB3695.13121.07423.5711.0034.51
ATOM2435NLEUB3704.77618.85923.6531.0030.97
ATOM2436CALEUB3704.08618.80922.3701.0029.80
ATOM2437CBLEUB3704.14517.38921.7991.0027.27
ATOM2438CGLEUB3705.52216.73321.6881.0028.07
ATOM2439CD1LEUB3705.35315.24221.4001.0030.38
ATOM2440CD2LEUB3706.31617.39620.5741.0022.82
ATOM2441CLEUB3702.62819.21822.5211.0028.04
ATOM2442OLEUB3702.06619.15123.6111.0029.71
ATOM2443NTHRB3712.01119.64521.4251.0028.70
ATOM2444CATHRB3710.60220.01421.4741.0030.31
ATOM2445CBTHRB3710.15020.69020.1631.0031.96
ATOM2446OG1THRB3710.28419.76319.0801.0029.49
ATOM2447CG2THRB3710.99121.93019.8781.0029.98
ATOM2448CTHRB371−0.20818.72621.6661.0030.59
ATOM2449OTHRB3710.30017.62421.4311.0027.10
ATOM2450NLEUB372−1.46118.86322.0871.0027.65
ATOM2451CALEUB372−2.32317.70222.3031.0030.86
ATOM2452CBLEUB372−3.72218.14722.7371.0030.11
ATOM2453CGLEUB372−4.71517.00622.9601.0032.80
ATOM2454CD1LEUB372−4.23116.14724.1261.0034.10
ATOM2455CD2LEUB372−6.10517.56223.2461.0031.16
ATOM2456CLEUB372−2.43716.86321.0341.0031.77
ATOM2457OLEUB372−2.41715.62921.0781.0027.06
ATOM2458NHISB373−2.56417.54819.9051.0031.30
ATOM2459CAHISB373−2.68516.88818.6141.0031.35
ATOM2460CBHISB373−2.84417.93517.5031.0034.30
ATOM2461CGHISB373−2.50317.43016.1321.0041.27
ATOM2462CD2HISB373−3.29317.10515.0791.0042.50
ATOM2463ND1HISB373−1.20517.22015.7151.0043.69
ATOM2464CE1HISB373−1.21016.78714.4651.0048.87
ATOM2465NE2HISB373−2.46516.70814.0561.0043.72
ATOM2466CHISB373−1.46816.01218.3371.0028.29
ATOM2467OHISB373−1.61014.87817.8971.0030.21
ATOM2468NASPB374−0.27516.54118.5891.0028.85
ATOM2469CAASPB3740.95015.78318.3501.0028.28
ATOM2470CBASPB3742.17816.67818.5351.0031.33
ATOM2471CGASPB3742.43317.57717.3331.0039.07
ATOM2472OD1ASPB3743.19518.55717.4781.0040.60
ATOM2473OD2ASPB3741.87417.30516.2461.0038.64
ATOM2474CASPB3741.02914.59219.3031.0029.05
ATOM2475OASPB3741.43213.49418.9081.0024.26
ATOM2476NGLNB3750.64214.81420.5561.0024.52
ATOM2477CAGLNB3750.66713.74921.5471.0027.37
ATOM2478CBGLNB3750.21314.27022.9011.0026.66
ATOM2479CGGLNB3751.16415.23623.5631.0029.74
ATOM2480CDGLNB3750.62315.69124.8901.0033.13
ATOM2481OE1GLNB375−0.04414.95325.6021.0032.82
ATOM2482NE2GLNB3750.89516.95325.2361.0033.98
ATOM2483CGLNB375−0.25912.63021.1041.0024.52
ATOM2484OGLNB3750.07411.45121.2211.0023.56
ATOM2485NVALB376−1.42613.01320.5991.0021.87
ATOM2486CAVALB376−2.40912.05520.1401.0023.44
ATOM2487CBVALB376−3.71812.76019.7171.0022.09
ATOM2488CG1VALB376−4.57211.82318.8771.0024.14
ATOM2489CG2VALB376−4.48613.19220.9541.0016.96
ATOM2490CVALB376−1.85211.25718.9651.0024.15
ATOM2491OVALB376−1.94910.03218.9381.0022.26
ATOM2492NHISB377−1.25111.95318.0071.0025.85
ATOM2493CAHISB377−0.68911.28416.8431.0025.68
ATOM2494CBHISB377−0.07812.30615.8861.0025.27
ATOM2495CGHISB3770.53511.69014.6671.0030.63
ATOM2496CD2HISB3771.82811.55914.2871.0031.03
ATOM2497ND1HISB377−0.21711.08613.6831.0035.05
ATOM2498CE1HISB3770.58810.60712.7501.0033.12
ATOM2499NE2HISB3771.83310.88213.0931.0031.06
ATOM2500CHISB3770.36510.23717.2101.0024.37
ATOM2501OHISB3770.3219.10916.7191.0021.47
ATOM2502NLEUB3781.30710.60918.0721.0019.24
ATOM2503CALEUB3782.3659.69118.4741.0020.09
ATOM2504CBLEUB3783.36310.40219.3881.0018.64
ATOM2505CGLEUB3784.23011.48918.7361.0022.15
ATOM2506CD1LEUB3785.10412.14819.7961.0022.51
ATOM2507CD2LEUB3785.09410.88517.6381.0020.68
ATOM2508CLEUB3781.8328.43319.1611.0018.91
ATOM2509OLEUB3782.2627.32018.8591.0017.52
ATOM2510NLEUB3790.8888.61020.0771.0018.25
ATOM2511CALEUB3790.3177.48620.7951.0018.60
ATOM2512CBLEUB379−0.5267.98921.9681.0016.77
ATOM2513CGLEUB3790.2928.35323.2141.0017.90
ATOM2514CD1LEUB379−0.5789.09224.2111.0015.84
ATOM2515CD2LEUB3790.8517.07523.8421.0022.09
ATOM2516CLEUB379−0.5186.60519.8721.0020.17
ATOM2517OLEUB379−0.4765.37719.9681.0018.11
ATOM2518NGLUB380−1.2737.22218.9711.0019.40
ATOM2519CAGLUB380−2.0866.43518.0491.0020.19
ATOM2520CBGLUB380−2.9947.35017.2221.0022.43
ATOM2521CGGLUB380−4.1827.87418.0071.0025.30
ATOM2522CDGLUB380−5.0708.78917.1881.0029.44
ATOM2523OE1GLUB380−6.2069.06617.6251.0031.70
ATOM2524OE2GLUB380−4.6319.23016.1101.0031.75
ATOM2525CGLUB380−1.2105.59417.1171.0018.92
ATOM2526OGLUB380−1.5864.49116.7221.0019.83
ATOM2527NACYSB381−0.0396.11316.7720.7517.41
ATOM2528NBCYSB381−0.0356.11316.7790.2517.76
ATOM2529CAACYSB3810.8605.38415.8870.7520.19
ATOM2530CABCYSB3810.8755.40715.8840.2517.50
ATOM2531CBACYSB3811.8706.34215.2480.7524.20
ATOM2532CBBCYSB3811.8306.40615.2260.2516.63
ATOM2533SGACYSB3811.1677.51814.0600.7533.54
ATOM2534SGBCYSB3813.0485.65614.1280.2510.36
ATOM2535CACYSB3811.6264.26916.5920.7520.59
ATOM2536CBCYSB3811.6894.30516.5610.2519.19
ATOM2537OACYSB3811.7373.16116.0690.7519.16
ATOM2538OBCYSB3811.9043.24115.9820.2519.25
ATOM2539NALAB3822.1344.56017.7851.0019.04
ATOM2540CAALAB3822.9553.60218.5301.0020.27
ATOM2541CBALAB3824.1354.36419.1431.0018.68
ATOM2542CALAB3822.3562.70219.6071.0016.82
ATOM2543OALAB3823.0701.85220.1421.0013.37
ATOM2544NTRPB3831.0742.85519.9161.0015.30
ATOM2545CATRPB3830.4872.08921.0131.0015.80
ATOM2546CBTRPB383−1.0092.41021.1601.0016.63
ATOM2547CGTRPB383−1.8711.77520.1291.0019.93
ATOM2548CD2TRPB383−2.4930.48320.1981.0020.80
ATOM2549CE2TRPB383−3.2260.30919.0031.0019.27
ATOM2550CE3TRPB383−2.506−0.54221.1551.0021.32
ATOM2551CD1TRPB383−2.2362.31218.9331.0018.59
ATOM2552NE1TRPB383−3.0511.43918.2501.0023.67
ATOM2553CZ2TRPB383−3.963−0.85318.7331.0021.55
ATOM2554CZ3TRPB383−3.243−1.70220.8881.0020.29
ATOM2555CH2TRPB383−3.960−1.84419.6861.0019.03
ATOM2556CTRPB3830.7010.57921.0201.0017.35
ATOM2557OTRPB3830.9820.01022.0771.0013.92
ATOM2558NLEUB3840.568−0.08719.8791.0014.07
ATOM2559CALEUB3840.773−1.53219.9031.0015.98
ATOM2560CBLEUB3840.181−2.20018.6561.0012.19
ATOM2561CGLEUB3840.173−3.73518.7201.0012.97
ATOM2562CD1LEUB384−0.352−4.24020.0891.0010.65
ATOM2563CD2LEUB384−0.707−4.25917.5861.0017.84
ATOM2564CLEUB3842.262−1.86120.0341.0014.64
ATOM2565OLEUB3842.627−2.83320.6901.0013.78
ATOM2566NGLUB3853.116−1.04619.4141.0014.96
ATOM2567CAGLUB3854.565−1.26019.5091.0013.79
ATOM2568CBGLUB3855.336−0.17918.7391.0015.34
ATOM2569CGGLUB3855.297−0.31217.2071.0015.38
ATOM2570CDGLUB3856.1620.73816.5201.0023.97
ATOM2571OE1GLUB3857.3810.50016.3581.0021.03
ATOM2572OE2GLUB3855.6221.80816.1491.0022.19
ATOM2573CGLUB3854.963−1.16120.9871.0015.79
ATOM2574OGLUB3855.788−1.94221.4631.0015.04
ATOM2575NILEB3864.389−0.21321.6901.0013.32
ATOM2576CAILEB3864.723−0.01923.1081.0014.06
ATOM2577CBILEB3864.1731.32623.6141.0015.36
ATOM2578CG2ILEB3864.3741.45125.1301.0015.97
ATOM2579CG1ILEB3864.9102.47622.9071.0017.95
ATOM2580CD1ILEB3864.1183.76822.8741.0021.12
ATOM2581CILEB3864.227−1.16423.9931.0014.97
ATOM2582OILEB3864.905−1.56024.9411.0019.60
ATOM2583NLEUB3873.038−1.67523.7091.0015.18
ATOM2584CALEUB3872.516−2.79124.4781.0015.98
ATOM2585CBLEUB3871.070−3.09724.0801.0017.15
ATOM2586CGLEUB387−0.031−2.11324.4861.0019.65
ATOM2587CD1LEUB387−1.371−2.62823.9721.0017.77
ATOM2588CD2LEUB387−0.075−1.96626.0021.0015.38
ATOM2589CLEUB3873.391−4.01324.1801.0014.69
ATOM2590OLEUB3873.712−4.79225.0761.0014.03
ATOM2591NMETB3883.785−4.17822.9211.0016.43
ATOM2592CAMETB3884.602−5.32922.5471.0016.67
ATOM2593CBMETB3884.673−5.46021.0261.0014.83
ATOM2594CGMETB3883.403−6.06620.4531.0013.91
ATOM2595SDMETB3883.364−6.19318.6751.0017.23
ATOM2596CEMETB3881.906−7.22518.5111.0014.97
ATOM2597CMETB3886.004−5.33223.1331.0020.19
ATOM2598OMETB3886.460−6.36623.6361.0021.50
ATOM2599NILEB3896.707−4.20323.0741.0015.34
ATOM2600CAILEB3898.044−4.20923.6341.0015.59
ATOM2601CBILEB3898.836−2.91123.3221.0014.95
ATOM2602CG2ILEB3898.330−1.74624.1581.0012.81
ATOM2603CG1ILEB38910.325−3.16423.6021.0017.24
ATOM2604CD1ILEB38911.228−1.97223.3571.0015.65
ATOM2605CILEB3897.950−4.44625.1471.0014.30
ATOM2606OILEB3898.844−5.04425.7391.0018.72
ATOM2607NGLYB3906.855−4.00725.7611.0013.99
ATOM2608CAGLYB3906.681−4.21927.1891.0014.87
ATOM2609CGLYB3906.444−5.70227.4631.0018.54
ATOM2610OGLYB3906.989−6.28228.4031.0016.54
ATOM2611NLEUB3915.623−6.32526.6281.0016.15
ATOM2612CALEUB3915.334−7.74326.7751.0018.91
ATOM2613CBLEUB3914.332−8.17925.6991.0019.55
ATOM2614CGLEUB3914.157−9.68925.4571.0020.91
ATOM2615CD1LEUB3913.580−10.35126.6991.0019.41
ATOM2616CD2LEUB3913.232−9.91324.2681.0020.70
ATOM2617CLEUB3916.649−8.51826.6251.0020.31
ATOM2618OLEUB3917.002−9.35227.4651.0018.66
ATOM2619NVALB3927.378−8.21525.5571.0018.71
ATOM2620CAVALB3928.649−8.86825.2781.0019.51
ATOM2621CBVALB3929.288−8.28124.0051.0023.77
ATOM2622CG1VALB39210.751−8.68723.9201.0024.63
ATOM2623CG2VALB3928.520−8.77322.7671.0019.94
ATOM2624CVALB3929.615−8.70726.4501.0022.80
ATOM2625OVALB39210.336−9.63726.8111.0019.36
ATOM2626NTRPB3939.617−7.52227.0461.0022.10
ATOM2627CATRPB39310.492−7.24128.1711.0023.20
ATOM2628CBTRPB39310.388−5.77328.5781.0019.22
ATOM2629CGTRPB39311.056−5.47929.8951.0022.53
ATOM2630CD2TRPB39312.453−5.59130.1931.0020.36
ATOM2631CE2TRPB39312.624−5.20831.5451.0025.65
ATOM2632CE3TRPB39313.578−5.97629.4491.0022.12
ATOM2633CD1TRPB39310.452−5.04631.0441.0023.02
ATOM2634NE1TRPB39311.387−4.88132.0371.0024.91
ATOM2635CZ2TRPB39313.876−5.20032.1711.0023.00
ATOM2636CZ3TRPB39314.829−5.96830.0721.0023.98
ATOM2637CH2TRPB39314.964−5.58231.4231.0023.20
ATOM2638CTRPB39310.208−8.11429.3881.0024.36
ATOM2639OTRPB39311.128−8.71729.9441.0023.04
ATOM2640NARGB3948.952−8.18929.8191.0021.29
ATOM2641CAARGB3948.680−9.00330.9901.0022.43
ATOM2642CBARGB3947.365−8.60131.6671.0023.97
ATOM2643CGARGB3946.259−8.14930.7591.0026.16
ATOM2644CDARGB3945.026−7.72731.5741.0020.86
ATOM2645NEARGB3943.817−7.93730.7861.0019.54
ATOM2646CZARGB3943.327−7.05929.9151.0020.58
ATOM2647NH1ARGB3943.944−5.90229.7221.0017.41
ATOM2648NH2ARGB3942.229−7.34729.2201.0016.82
ATOM2649CARGB3948.695−10.50230.7131.0021.78
ATOM2650OARGB3948.657−11.29431.6481.0023.44
ATOM2651NSERB3958.767−10.88029.4381.0017.10
ATOM2652CASERB3958.805−12.28929.0411.0025.08
ATOM2653CBSERB3958.206−12.47327.6381.0019.47
ATOM2654OGSERB3956.832−12.13627.6191.0021.73
ATOM2655CSERB39510.239−12.83129.0311.0026.29
ATOM2656OSERB39510.458−14.03028.8541.0023.75
ATOM2657NMETB39611.206−11.93829.2101.0030.79
ATOM2658CAMETB39612.620−12.30729.2051.0035.07
ATOM2659CBMETB39613.479−11.06329.4231.0033.84
ATOM2660CGMETB39614.155−10.56928.1711.0036.88
ATOM2661SDMETB39615.149−9.12728.4911.0040.96
ATOM2662CEMETB39616.675−9.84928.9981.0039.67
ATOM2663CMETB39612.983−13.35330.2501.0035.88
ATOM2664OMETB39613.828−14.21530.0111.0034.52
ATOM2665NGLUB39712.348−13.26631.4101.0036.19
ATOM2666CAGLUB39712.604−14.20632.4921.0039.24
ATOM2667CBGLUB39712.153−13.60533.8211.0044.38
ATOM2668CGGLUB39712.983−12.42234.2711.0054.05
ATOM2669CDGLUB39713.483−12.58735.6861.0056.78
ATOM2670OE1GLUB39713.380−11.62136.4701.0060.90
ATOM2671OE2GLUB39713.975−13.68836.0131.0060.82
ATOM2672CGLUB39711.878−15.52832.2731.0036.65
ATOM2673OGLUB39712.021−16.45933.0611.0035.84
ATOM2674NHISB39811.100−15.60931.2021.0032.14
ATOM2675CAHISB39810.347−16.82330.9141.0029.48
ATOM2676CBHISB3988.863−16.56731.1781.0029.87
ATOM2677CGHISB3988.582−16.11132.5741.0031.80
ATOM2678CD2HISB3988.215−16.80133.6781.0029.12
ATOM2679ND1HISB3988.727−14.79932.9721.0033.27
ATOM2680CE1HISB3988.462−14.70134.2621.0032.19
ATOM2681NE2HISB3988.148−15.90234.7141.0033.48
ATOM2682CHISB39810.556−17.31729.4921.0025.95
ATOM2683OHISB3989.637−17.29128.6721.0027.47
ATOM2684NPROB39911.771−17.80129.1861.0029.09
ATOM2685CDPROB39912.926−17.92230.0961.0029.93
ATOM2686CAPROB39912.079−18.30027.8451.0027.40
ATOM2687CBPROB39913.434−18.98828.0161.0032.09
ATOM2688CGPROB39914.062−18.28429.1701.0030.81
ATOM2689CPROB39911.009−19.24627.3191.0029.76
ATOM2690OPROB39910.552−20.13728.0351.0029.18
ATOM2691NGLYB40010.601−19.03526.0711.0027.45
ATOM2692CAGLYB4009.588−19.88425.4661.0026.93
ATOM2693CGLYB4008.161−19.53725.8491.0026.73
ATOM2694OGLYB4007.220−20.15325.3561.0028.36
ATOM2695NLYSB4017.996−18.55426.7271.0025.50
ATOM2696CALYSB4016.668−18.13927.1651.0023.45
ATOM2697CBLYSB4016.435−18.56328.6191.0028.50
ATOM2698CGLYSB4016.476−20.06928.8791.0028.58
ATOM2699CDLYSB4016.181−20.35330.3491.0035.47
ATOM2700CELYSB4016.073−21.84730.6351.0038.59
ATOM2701NZLYSB4017.177−22.61129.9891.0042.39
ATOM2702CLYSB4016.493−16.62227.0601.0021.78
ATOM2703OLYSB4017.465−15.87227.0351.0021.45
ATOM2704NLEUB4025.241−16.18126.9951.0023.45
ATOM2705CALEUB4024.929−14.75926.9251.0021.37
ATOM2706CBLEUB4024.088−14.44925.6891.0018.47
ATOM2707CGLEUB4024.798−14.67324.3601.0016.89
ATOM2708CD1LEUB4023.821−14.39523.2111.0021.23
ATOM2709CD2LEUB4026.011−13.76024.2771.0023.15
ATOM2710CLEUB4024.147−14.39928.1791.0019.66
ATOM2711OLEUB4023.024−14.88028.3811.0018.05
ATOM2712NLEUB4034.743−13.55929.0191.0019.54
ATOM2713CALEUB4034.099−13.14830.2591.0020.21
ATOM2714CBLEUB4035.155−12.85631.3321.0023.16
ATOM2715CGLEUB4034.639−12.68232.7661.0029.54
ATOM2716CD1LEUB4035.519−13.45033.7281.0032.67
ATOM2717CD2LEUB4034.626−11.21333.1381.0032.38
ATOM2718CLEUB4033.219−11.91830.0431.0020.42
ATOM2719OLEUB4033.638−10.78730.2911.0019.18
ATOM2720NPHEB4042.003−12.14529.5651.0021.44
ATOM2721CAPHEB4041.066−11.05329.3401.0021.69
ATOM2722CBPHEB404−0.199−11.59828.6871.0017.26
ATOM2723CGPHEB404−0.026−11.89727.2271.0019.75
ATOM2724CD1PHEB4040.364−13.16726.8011.0017.90
ATOM2725CD2PHEB404−0.210−10.89726.2801.0017.04
ATOM2726CE1PHEB4040.572−13.43425.4471.0019.88
ATOM2727CE2PHEB404−0.007−11.14824.9241.0018.47
ATOM2728CZPHEB4040.386−12.41824.5031.0016.45
ATOM2729CPHEB4040.768−10.40330.6851.0021.95
ATOM2730OPHEB4040.656−9.17730.8041.0022.99
ATOM2731NALAB4050.670−11.24731.7021.0021.12
ATOM2732CAALAB4050.424−10.81433.0661.0022.43
ATOM2733CBALAB405−1.074−10.60333.3041.0024.69
ATOM2734CALAB4050.959−11.92633.9621.0022.40
ATOM2735OALAB4051.133−13.06133.5171.0021.67
ATOM2736NPROB4061.246−11.61235.2301.0025.60
ATOM2737CDPROB4061.129−10.29435.8781.0023.65
ATOM2738CAPROB4061.765−12.63236.1481.0025.91
ATOM2739CBPROB4061.899−11.88237.4751.0027.04
ATOM2740CGPROB4062.017−10.43137.0681.0026.56
ATOM2741CPROB4060.876−13.87336.2591.0025.12
ATOM2742OPROB4061.368−14.96736.5381.0028.92
ATOM2743NASNB407−0.426−13.71336.0391.0023.53
ATOM2744CAASNB407−1.345−14.85236.1091.0024.09
ATOM2745CBASNB407−2.553−14.52636.9861.0024.08
ATOM2746CGASNB407−3.327−13.32836.4861.0026.72
ATOM2747OD1ASNB407−2.851−12.57435.6351.0022.65
ATOM2748ND2ASNB407−4.528−13.14037.0191.0026.46
ATOM2749CASNB407−1.820−15.23134.7141.0026.91
ATOM2750OASNB407−2.859−15.87034.5481.0028.68
ATOM2751NLEUB408−1.059−14.81633.7081.0027.28
ATOM2752CALEUB408−1.387−15.12432.3271.0027.23
ATOM2753CBLEUB408−2.247−14.03031.6991.0026.61
ATOM2754CGLEUB408−2.815−14.46430.3411.0027.51
ATOM2755CD1LEUB408−3.702−15.69230.5461.0028.75
ATOM2756CD2LEUB408−3.598−13.33029.6941.0025.48
ATOM2757CLEUB408−0.113−15.31631.5141.0027.56
ATOM2758OLEUB4080.247−14.46530.6951.0026.86
ATOM2759NLEUB4090.553−16.42631.7591.0027.54
ATOM2760CALEUB4091.786−16.77431.0651.0031.96
ATOM2761CBLEUB4092.786−17.35532.0581.0031.88
ATOM2762CGLEUB4094.186−17.70331.5621.0037.72
ATOM2763CD1LEUB4094.773−16.55130.7701.0039.57
ATOM2764CD2LEUB4095.066−18.01832.7581.0041.72
ATOM2765CLEUB4091.401−17.80530.0091.0031.53
ATOM2766OLEUB4090.921−18.89230.3401.0032.67
ATOM2767NLEUB4101.604−17.46528.7461.0029.58
ATOM2768CALEUB4101.228−18.36127.6601.0031.55
ATOM2769CBLEUB4100.192−17.67226.7621.0029.83
ATOM2770CGLEUB410−1.047−17.08027.4521.0028.55
ATOM2771CD1LEUB410−1.770−16.13526.5011.0026.92
ATOM2772CD2LEUB410−1.979−18.20027.8911.0030.49
ATOM2773CLEUB4102.397−18.83926.8141.0033.88
ATOM2774OLEUB4103.427−18.17026.7261.0036.49
ATOM2775NASPB4112.238−20.01326.2061.0038.80
ATOM2776CAASPB4113.275−20.56225.3361.0038.39
ATOM2777CBASPB4113.657−21.99025.7521.0044.53
ATOM2778CGASPB4112.476−22.94325.7491.0044.90
ATOM2779OD1ASPB4111.773−23.03524.7191.0045.70
ATOM2780OD2ASPB4112.254−23.60326.7861.0050.54
ATOM2781CASPB4112.745−20.55123.9091.0038.57
ATOM2782OASPB4111.549−20.34123.6861.0036.48
ATOM2783NARGB4123.635−20.77722.9491.0036.85
ATOM2784CAARGB4123.259−20.76321.5411.0038.32
ATOM2785CBARGB4124.488−21.08320.6751.0038.69
ATOM2786CGARGB4124.361−22.31419.7991.0040.05
ATOM2787CDARGB4125.644−22.55219.0121.0042.98
ATOM2788NEARGB4125.540−22.09917.6261.0040.95
ATOM2789CZARGB4124.649−22.55916.7531.0041.11
ATOM2790NH1ARGB4123.777−23.49017.1151.0044.01
ATOM2791NH2ARGB4124.632−22.09115.5151.0041.28
ATOM2792CARGB4122.107−21.71221.2171.0037.64
ATOM2793OARGB4121.287−21.42720.3431.0036.51
ATOM2794NASNB4132.041−22.83421.9231.0035.32
ATOM2795CAASNB4130.974−23.79821.6881.0036.68
ATOM2796CBASNB4131.170−25.03522.5701.0037.54
ATOM2797CGASNB4132.017−26.10021.9011.0043.56
ATOM2798OD1ASNB4132.309−26.02220.7041.0046.11
ATOM2799ND2ASNB4132.418−27.10422.6711.0047.04
ATOM2800CASNB413−0.383−23.16821.9821.0034.01
ATOM2801OASNB413−1.349−23.37221.2471.0032.43
ATOM2802NGLNB414−0.447−22.39723.0631.0032.85
ATOM2803CAGLNB414−1.685−21.74123.4491.0031.91
ATOM2804CBGLNB414−1.558−21.17224.8631.0033.17
ATOM2805CGGLNB414−1.528−22.24225.9481.0032.31
ATOM2806CDGLNB414−1.293−21.66727.3271.0034.63
ATOM2807OE1GLNB414−0.176−21.27727.6661.0033.23
ATOM2808NE2GLNB414−2.349−21.60628.1311.0034.56
ATOM2809CGLNB414−2.052−20.63822.4631.0029.57
ATOM2810OGLNB414−3.195−20.20422.4091.0031.32
ATOM2811NGLYB415−1.077−20.19021.6821.0030.96
ATOM2812CAGLYB415−1.350−19.16020.6971.0034.27
ATOM2813CGLYB415−2.184−19.72519.5621.0035.27
ATOM2814OGLYB415−2.918−19.00018.8871.0033.20
ATOM2815NLYSB416−2.070−21.03119.3541.0035.28
ATOM2816CALYSB416−2.819−21.70718.2991.0038.26
ATOM2817CBLYSB416−2.398−23.17718.2011.0038.00
ATOM2818CGLYSB416−0.973−23.40717.7361.0040.05
ATOM2819CDLYSB416−0.405−24.66818.3691.0044.10
ATOM2820CELYSB4160.306−25.54117.3461.0041.85
ATOM2821NZLYSB4161.286−24.76016.5421.0045.63
ATOM2822CLYSB416−4.321−21.64518.5591.0036.93
ATOM2823OLYSB416−5.121−21.79017.6381.0038.36
ATOM2824NCYSB417−4.698−21.43019.8171.0037.10
ATOM2825CACYSB417−6.106−21.37120.1961.0036.46
ATOM2826CBCYSB417−6.218−21.22621.7171.0039.01
ATOM2827SGCYSB417−5.674−22.71022.6121.0043.81
ATOM2828CCYSB417−6.899−20.27719.4911.0035.19
ATOM2829OCYSB417−8.127−20.29619.4851.0033.92
ATOM2830NVALB418−6.195−19.31618.9061.0036.04
ATOM2831CAVALB418−6.838−18.23618.1631.0034.59
ATOM2832CBVALB418−6.525−16.85018.7751.0034.87
ATOM2833CG1VALB418−6.831−15.76317.7651.0035.32
ATOM2834CG2VALB418−7.350−16.63020.0361.0033.65
ATOM2835CVALB418−6.241−18.31716.7641.0034.17
ATOM2836OVALB418−5.020−18.32316.6111.0032.73
ATOM2837NGLUB419−7.084−18.38815.7401.0033.44
ATOM2838CAGLUB419−6.554−18.50014.3901.0034.52
ATOM2839CBGLUB419−7.681−18.72213.3801.0036.21
ATOM2840CGGLUB419−8.597−17.53813.1661.0044.19
ATOM2841CDGLUB419−9.477−17.72311.9461.0048.47
ATOM2842OE1GLUB419−9.157−18.60511.1191.0051.04
ATOM2843OE2GLUB419−10.484−16.99311.8131.0048.91
ATOM2844CGLUB419−5.717−17.28913.9971.0032.89
ATOM2845OGLUB419−6.156−16.14414.1231.0031.09
ATOM2846NGLYB420−4.501−17.56213.5351.0032.84
ATOM2847CAGLYB420−3.594−16.50613.1221.0034.37
ATOM2848CGLYB420−2.722−15.95514.2401.0035.30
ATOM2849OGLYB420−1.745−15.24613.9751.0035.94
ATOM2850NMETB421−3.052−16.28515.4861.0030.08
ATOM2851CAMETB421−2.289−15.78016.6251.0029.22
ATOM2852CBMETB421−3.108−15.92217.9141.0022.54
ATOM2853CGMETB421−2.469−15.27019.1241.0023.82
ATOM2854SDMETB421−2.124−13.49418.8721.0028.40
ATOM2855CEMETB421−3.697−12.80019.2331.0024.67
ATOM2856CMETB421−0.912−16.41616.8211.0029.67
ATOM2857OMETB4210.022−15.75117.2691.0029.76
ATOM2858NVALB422−0.766−17.69416.4841.0030.63
ATOM2859CAVALB4220.524−18.33816.6751.0029.90
ATOM2860CBVALB4220.482−19.83516.2731.0035.74
ATOM2861CG1VALB4220.514−19.99214.7531.0037.64
ATOM2862CG2VALB4221.659−20.55516.8971.0031.68
ATOM2863CVALB4221.669−17.64015.9351.0028.64
ATOM2864OVALB4222.788−17.57116.4411.0026.15
ATOM2865NGLUB4231.402−17.11314.7471.0028.70
ATOM2866CAGLUB4232.454−16.43513.9971.0031.34
ATOM2867CBGLUB4231.963−16.05012.5961.0036.21
ATOM2868CGGLUB4230.502−16.37612.3251.0045.83
ATOM2869CDGLUB4230.250−17.86512.1441.0046.71
ATOM2870OE1GLUB423−0.746−18.36812.7061.0045.97
ATOM2871OE2GLUB4231.045−18.53011.4421.0050.05
ATOM2872CGLUB4232.928−15.18614.7441.0030.57
ATOM2873OGLUB4234.119−14.87014.7591.0026.59
ATOM2874NILEB4242.001−14.47815.3781.0026.19
ATOM2875CAILEB4242.381−13.27916.1111.0026.23
ATOM2876CBILEB4241.134−12.43516.4521.0029.33
ATOM2877CG2ILEB4241.492−11.31517.4251.0030.91
ATOM2878CG1ILEB4240.584−11.81715.1601.0029.09
ATOM2879CD1ILEB424−0.895−11.51415.1871.0030.51
ATOM2880CILEB4243.153−13.67317.3701.0024.22
ATOM2881OILEB4244.152−13.03717.7251.0021.05
ATOM2882NPHEB4252.708−14.74618.0231.0021.71
ATOM2883CAPHEB4253.370−15.23619.2231.0018.85
ATOM2884CBPHEB4252.650−16.47919.7681.0022.98
ATOM2885CGPHEB4251.580−16.18320.7951.0022.17
ATOM2886CD1PHEB4251.287−17.11221.7921.0025.47
ATOM2887CD2PHEB4250.843−15.00120.7471.0026.30
ATOM2888CE1PHEB4250.273−16.87122.7241.0024.33
ATOM2889CE2PHEB425−0.174−14.74921.6761.0025.03
ATOM2890CZPHEB425−0.459−15.68422.6631.0026.44
ATOM2891CPHEB4254.817−15.61018.8851.0020.00
ATOM2892OPHEB4255.741−15.29219.6361.0021.15
ATOM2893NASPB4265.023−16.28117.7541.0019.87
ATOM2894CAASPB4266.378−16.68517.3771.0023.20
ATOM2895CBASPB4266.364−17.51016.0901.0026.53
ATOM2896CGASPB4265.992−18.96516.3351.0034.28
ATOM2897OD1ASPB4266.242−19.46717.4551.0035.24
ATOM2898OD2ASPB4265.448−19.60015.4091.0031.49
ATOM2899CASPB4267.302−15.48917.1981.0021.84
ATOM2900OASPB4268.465−15.52617.5931.0021.55
ATOM2901NMETB4276.788−14.42916.5911.0020.12
ATOM2902CAMETB4277.597−13.23416.3821.0021.02
ATOM2903CBMETB4276.836−12.22815.5201.0018.53
ATOM2904CGMETB4276.864−12.55914.0381.0027.92
ATOM2905SDMETB4276.011−11.34113.0241.0032.84
ATOM2906CEMETB4274.363−11.53213.5811.0033.63
ATOM2907CMETB4277.945−12.61617.7321.0017.42
ATOM2908OMETB4279.073−12.18017.9501.0022.09
ATOM2909NLEUB4286.968−12.59718.6341.0020.47
ATOM2910CALEUB4287.157−12.03319.9681.0020.13
ATOM2911CBLEUB4285.812−11.96420.7061.0017.58
ATOM2912CGLEUB4284.852−10.88720.1791.0018.41
ATOM2913CD1LEUB4283.443−11.15520.6871.0011.95
ATOM2914CD2LEUB4285.324−9.50520.6311.0017.80
ATOM2915CLEUB4288.159−12.85620.7671.0020.68
ATOM2916OLEUB4289.028−12.30521.4451.0020.45
ATOM2917NLEUB4298.037−14.17820.6791.0020.35
ATOM2918CALEUB4298.938−15.08221.3821.0019.82
ATOM2919CBLEUB4298.470−16.53221.2111.0023.13
ATOM2920CGLEUB4297.189−16.83921.9971.0021.85
ATOM2921CD1LEUB4296.551−18.12321.4941.0025.39
ATOM2922CD2LEUB4297.537−16.94423.4751.0024.91
ATOM2923CLEUB42910.361−14.93620.8651.0020.74
ATOM2924OLEUB42911.318−14.96821.6381.0021.02
ATOM2925NALAB43010.495−14.77019.5541.0021.40
ATOM2926CAALAB43011.808−14.60918.9471.0022.77
ATOM2927CBALAB43011.677−14.59617.4321.0021.11
ATOM2928CALAB43012.467−13.31519.4401.0022.40
ATOM2929OALAB43013.670−13.27719.7131.0020.62
ATOM2930NTHRB43111.670−12.25819.5671.0021.09
ATOM2931CATHRB43112.183−10.97420.0211.0022.67
ATOM2932CBTHRB43111.128−9.86619.8631.0023.77
ATOM2933OG1THRB43110.572−9.93618.5471.0023.84
ATOM2934CG2THRB43111.762−8.48920.0731.0021.78
ATOM2935CTHRB43112.603−11.03721.4801.0021.98
ATOM2936OTHRB43113.595−10.42921.8791.0019.85
ATOM2937NSERB43211.844−11.77322.2801.0024.24
ATOM2938CASERB43212.169−11.90623.6931.0026.96
ATOM2939CBSERB43211.055−12.66124.4231.0028.00
ATOM2940OGSERB43211.404−12.88825.7761.0030.31
ATOM2941CSERB43213.491−12.66023.8201.0027.67
ATOM2942OSERB43214.305−12.37724.7011.0023.78
ATOM2943NSERB43313.691−13.62822.9321.0029.27
ATOM2944CASERB43314.914−14.42122.9281.0031.96
ATOM2945CBSERB43314.790−15.57521.9381.0030.84
ATOM2946OGSERB43314.761−16.80822.6251.0038.26
ATOM2947CSERB43316.104−13.55022.5481.0031.47
ATOM2948OSERB43317.204−13.70123.0871.0028.43
ATOM2949NARGB43415.878−12.64121.6071.0029.55
ATOM2950CAARGB43416.926−11.73921.1651.0029.40
ATOM2951CBARGB43416.437−10.91219.9771.0031.56
ATOM2952CGARGB43417.428−9.86819.4931.0036.76
ATOM2953CDARGB43418.694−10.50218.9191.0037.76
ATOM2954NEARGB43419.654−9.47918.5161.0039.50
ATOM2955CZARGB43420.965−9.67318.4181.0044.17
ATOM2956NH1ARGB43421.492−10.86118.6961.0043.17
ATOM2957NH2ARGB43421.750−8.67118.0481.0043.05
ATOM2958CARGB43417.328−10.82722.3261.0029.15
ATOM2959OARGB43418.515−10.61222.5691.0028.82
ATOM2960NPHEB43516.337−10.29723.0391.0024.88
ATOM2961CAPHEB43516.600−9.42224.1861.0025.74
ATOM2962CBPHEB43515.278−8.97224.8251.0026.53
ATOM2963CGPHEB43514.656−7.75824.1831.0030.94
ATOM2964CD1PHEB43515.118−7.27122.9661.0032.65
ATOM2965CD2PHEB43513.592−7.10824.7971.0033.60
ATOM2966CE1PHEB43514.529−6.15522.3721.0036.84
ATOM2967CE2PHEB43512.997−5.98924.2081.0034.96
ATOM2968CZPHEB43513.468−5.51622.9951.0031.64
ATOM2969CPHEB43517.426−10.18425.2331.0025.39
ATOM2970OPHEB43518.414−9.67525.7641.0022.59
ATOM2971NARGB43616.999−11.40525.5281.0024.58
ATOM2972CAARGB43617.675−12.25326.5031.0030.25
ATOM2973CBARGB43616.898−13.56926.6621.0033.32
ATOM2974CGARGB43617.232−14.35827.9151.0038.17
ATOM2975CDARGB43616.135−15.36728.2601.0037.27
ATOM2976NEARGB43615.646−16.08527.0861.0043.92
ATOM2977CZARGB43614.433−15.92326.5571.0046.68
ATOM2978NH1ARGB43613.578−15.06127.0971.0045.59
ATOM2979NH2ARGB43614.074−16.62025.4861.0046.25
ATOM2980CARGB43619.110−12.53126.0481.0029.82
ATOM2981OARGB43620.057−12.39726.8231.0028.76
ATOM2982NAMETB43719.269−12.92124.7890.5030.27
ATOM2983NBMETB43719.252−12.90624.7810.5031.41
ATOM2984CAAMETB43720.591−13.21224.2530.5031.98
ATOM2985CABMETB43720.547−13.20624.1830.5033.77
ATOM2986CBAMETB43720.489−13.64622.7880.5031.34
ATOM2987CBBMETB43720.348−13.59522.7140.5035.88
ATOM2988CGAMETB43720.179−15.12722.5920.5033.62
ATOM2989CGBMETB43721.605−13.59421.8610.5040.47
ATOM2990SDAMETB43720.354−16.09924.1090.5035.21
ATOM2991SDBMETB43721.247−13.93720.1150.5046.79
ATOM2992CEAMETB43722.155−16.19424.2590.5033.20
ATOM2993CEBMETB43721.837−15.63219.9760.5043.22
ATOM2994CAMETB43721.498−11.99324.3660.5033.33
ATOM2995CBMETB43721.487−12.00524.2890.5034.45
ATOM2996OAMETB43722.702−12.12324.5940.5033.54
ATOM2997OBMETB43722.699−12.16224.4380.5034.43
ATOM2998NMETB43820.913−10.80924.2151.0032.07
ATOM2999CAMETB43821.674−9.56024.2981.0032.48
ATOM3000CBMETB43820.930−8.43723.5781.0029.74
ATOM3001CGMETB43821.161−8.36422.0931.0036.73
ATOM3002SDMETB43820.425−6.84921.4621.0038.21
ATOM3003CEMETB43821.693−5.65721.9431.0035.91
ATOM3004CMETB43821.877−9.12225.7381.0028.81
ATOM3005OMETB43822.686−8.24026.0131.0030.13
ATOM3006NASNB43921.120−9.72126.6461.0027.14
ATOM3007CAASNB43921.199−9.35928.0381.0027.34
ATOM3008CBASNB43922.592−9.52428.5981.0034.85
ATOM3009CGASNB43922.624−9.48030.0801.0038.58
ATOM3010OD1ASNB43921.584−9.62030.7241.0042.99
ATOM3011ND2ASNB43923.801−9.26030.6661.0041.14
ATOM3012CASNB43920.745−7.90328.2121.0026.24
ATOM3013OASNB43921.396−7.10628.8911.0019.76
ATOM3014NLEUB44019.625−7.56427.5731.0024.90
ATOM3015CALEUB44019.061−6.21427.6331.0025.04
ATOM3016CBLEUB44017.761−6.15726.8181.0022.36
ATOM3017CGLEUB44017.087−4.78626.7401.0026.33
ATOM3018CD1LEUB44017.958−3.84325.9231.0028.33
ATOM3019CD2LEUB44015.704−4.91426.1111.0024.81
ATOM3020CLEUB44018.782−5.78529.0741.0024.71
ATOM3021OLEUB44018.131−6.50429.8301.0026.96
ATOM3022NGLNB44119.268−4.60929.4521.0025.54
ATOM3023CAGLNB44119.060−4.09930.8071.0025.82
ATOM3024CBGLNB44120.250−3.23131.2341.0030.41
ATOM3025CGGLNB44121.572−3.95631.2281.0030.50
ATOM3026CDGLNB44121.610−5.02832.2791.0032.75
ATOM3027OE1GLNB44121.539−4.77233.4731.0036.52
ATOM3028NE2GLNB44121.703−6.28831.8231.0031.09
ATOM3029CGLNB44117.789−3.26530.8831.0026.93
ATOM3030OGLNB44117.303−2.76829.8661.0025.40
ATOM3031NGLYB44217.266−3.10532.0961.0024.56
ATOM3032CAGLYB44216.058−2.32732.2931.0022.82
ATOM3033CGLYB44216.217−0.87331.8851.0024.19
ATOM3034OGLYB44215.290−0.27931.3411.0020.21
ATOM3035NGLUB44317.387−0.29332.1411.0022.92
ATOM3036CAGLUB44317.6351.10231.7781.0023.33
ATOM3037CBGLUB44318.9601.59032.3781.0024.26
ATOM3038CGGLUB44319.0051.52533.8951.0032.31
ATOM3039CDGLUB44319.7010.27034.4021.0037.68
ATOM3040OE1GLUB44319.343−0.84133.9481.0935.23
ATOM3041OE2GLUB44320.6070.39435.2521.0042.47
ATOM3042CGLUB44317.6621.27830.2621.0023.08
ATOM3043OGLUB44317.2652.32829.7471.0021.80
ATOM3044NGLUB44418.1280.25329.5521.0021.16
ATOM3045CAGLUB44418.1820.30228.0931.0022.60
ATOM3046CBGLUB44419.046−0.83427.5451.0020.89
ATOM3047CGGLUB44420.545−0.61727.7051.0023.24
ATOM3048CDGLUB44421.340−1.86927.3931.0022.11
ATOM3049OE1GLUB44420.817−2.97827.6291.0020.89
ATOM3050OE2GLUB44422.488−1.74626.9141.0025.49
ATOM3051CGLUB44416.7580.15527.5521.0021.06
ATOM3052OGLUB44416.3770.82226.5971.0023.73
ATOM3053NPHEB44515.987−0.73028.1761.0019.01
ATOM3054CAPHEB44514.600−0.96927.7921.0019.44
ATOM3055CBPHEB44513.989−2.06728.6751.0018.12
ATOM3056CGPHEB44512.483−2.05528.7091.0018.13
ATOM3057CD1PHEB44511.746−2.38627.5751.0018.34
ATOM3058CD2PHEB44511.802−1.69429.8721.0016.59
ATOM3059CE1PHEB44510.346−2.35927.5921.0017.15
ATOM3060CE2PHEB44510.406−1.66229.9031.0021.99
ATOM3061CZPHEB4459.674−1.99728.7551.0016.01
ATOM3062CPHEB44513.7580.30427.8881.0015.87
ATOM3063OPHEB44513.0080.61726.9661.0020.27
ATOM3064NVALB44613.8721.04428.9861.0015.90
ATOM3065CAVALB44613.0742.26929.1121.0016.78
ATOM3066CBVALB44613.1652.89530.5311.0018.32
ATOM3067CG1VALB44612.5741.92331.5511.0021.14
ATOM3068CG2VALB44614.5983.25130.8791.0021.04
ATOM3069CVALB44613.4503.29528.0511.0017.91
ATOM3070OVALB44612.5964.02827.5611.0019.37
ATOM3071NCYSB44714.7233.33527.6741.0018.81
ATOM3072CACYSB44715.1614.25526.6351.0017.34
ATOM3073CBCYSB44716.6824.22426.5121.0019.33
ATOM3074SGCYSB44717.5385.13427.7981.0023.60
ATOM3075CCYSB44714.5373.82625.3011.0018.09
ATOM3076OCYSB44713.9884.64324.5631.0017.52
ATOM3077NLEUB44814.6232.53325.0061.0015.60
ATOM3078CALEUB44814.0721.99423.7671.0016.67
ATOM3079CBLEUB44814.3280.49023.6841.0014.82
ATOM3080CGLEUB44815.7300.00923.3011.0023.57
ATOM3081CD1LEUB44815.722−1.52223.1691.0021.61
ATOM3082CD2LEUB44816.1670.65821.9861.0018.92
ATOM3083CLEUB44812.5732.24923.6521.0015.98
ATOM3084OLEUB44812.0782.63322.5901.0018.91
ATOM3085NLYSB44911.8492.03724.7451.0017.94
ATOM3086CALYSB44910.4052.23224.7331.0016.66
ATOM3087CBLYSB4499.7961.74526.0471.0016.45
ATOM3088CGLYSB4498.2851.86126.1151.0016.12
ATOM3089CDLYSB4497.7300.95227.1931.0019.09
ATOM3090CELYSB4498.2011.38028.5801.0017.04
ATOM3091NZLYSB4497.1591.08829.5931.0017.25
ATOM3092CLYSB44910.0583.69624.4861.0018.78
ATOM3093OLYSB4499.1033.99623.7691.0014.84
ATOM3094NSERB45010.8374.61025.0591.0014.50
ATOM3095CASERB45010.5916.03224.8491.0017.11
ATOM3096CBSERB45011.4406.86625.8151.0021.20
ATOM3097OGSERB45010.8596.86827.1081.0030.66
ATOM3098CSERB45010.9216.41823.4051.0017.84
ATOM3099OSERB45010.2797.29222.8211.0018.82
ATOM3100NILEB45111.9265.76822.8281.0016.88
ATOM3101CAILEB45112.3056.06321.4501.0017.11
ATOM3102CBILEB45113.5645.26821.0251.0016.69
ATOM3103CG2ILEB45113.7245.29819.5051.0019.31
ATOM3104CG1ILEB45114.8045.89721.6761.0018.96
ATOM3105CD1ILEB45116.0835.13021.4311.0018.98
ATOM3106CILEB45111.1425.71120.5271.0018.09
ATOM3107OILEB45110.8206.46419.6081.0017.07
ATOM3108NILEB45210.5054.57120.7861.0018.13
ATOM3109CAILEB4529.3734.13719.9761.0016.77
ATOM3110CBILEB4528.8042.77520.4771.0017.40
ATOM3111CG2ILEB4527.4642.49619.8311.0014.33
ATOM3112CG1ILEB4529.7631.63520.1071.0015.36
ATOM3113CD1ILEB4529.4490.32320.8051.0017.76
ATOM3114CILEB4528.2715.19520.0241.0017.47
ATOM3115OILEB4527.7335.58618.9921.0016.50
ATOM3116NLEUB4537.9435.66521.2221.0016.06
ATOM3117CALEUB4536.9036.68021.3741.0017.17
ATOM3118CBLEUB4536.7367.06122.8501.0016.23
ATOM3119CGLEUB4535.7928.22823.1631.0017.60
ATOM3120CD1LEUB4534.3887.88122.7041.0016.94
ATOM3121CD2LEUB4535.8168.53824.6671.0017.17
ATOM3122CLEUB4537.1987.94120.5661.0019.33
ATOM3123OLEUB4536.3208.45819.8791.0021.37
ATOM3124NLEUB4548.4348.42820.6361.0017.68
ATOM3125CALEUB4548.7899.65319.9331.0020.93
ATOM3126CBLEUB4549.95910.34720.6531.0024.33
ATOM3127CGLEUB4549.73510.69922.1301.0026.16
ATOM3128CD1LEUB45411.04611.17022.7491.0024.82
ATOM3129CD2LEUB4548.65811.77722.2591.0023.79
ATOM3130CLEUB4549.1209.49418.4491.0020.75
ATOM3131OLEUB4548.94110.43117.6731.0021.33
ATOM3132NASNB4559.5668.31118.0421.0020.54
ATOM3133CAASNB4559.9518.09316.6511.0019.46
ATOM3134CBASNB45511.1477.14916.5841.0018.58
ATOM3135CGASNB45511.5766.87115.1611.0017.64
ATOM3136OD1ASNB45512.1067.74914.4961.0018.40
ATOM3137ND2ASNB45511.3435.64814.6861.0015.06
ATOM3138CASNB4558.9257.58015.6551.0022.77
ATOM3139OASNB4558.7908.12714.5641.0021.94
ATOM3140NSERB4568.2246.51416.0231.0025.90
ATOM3141CASERB4567.2605.87315.1351.0024.76
ATOM3142CBSERB4566.4024.89415.9391.0026.91
ATOM3143OGSERB4567.2123.81816.3901.0026.24
ATOM3144CSERB4566.3856.77414.2721.0026.52
ATOM3145OSERB4566.3236.58813.0551.0029.22
ATOM3146NGLYB4575.7167.75014.8721.0022.07
ATOM3147CAGLYB4574.8798.62714.0761.0025.19
ATOM3148CGLYB4575.5109.97313.7651.0028.59
ATOM3149OGLYB4574.85110.85013.2141.0028.31
ATOM3150NVALB4586.78910.13014.0921.0031.65
ATOM3151CAVALB4587.48611.39613.8791.0038.50
ATOM3152CBVALB4588.95011.31014.3731.0036.24
ATOM3153CG1VALB4589.82710.65013.3241.0038.50
ATOM3154CG2VALB4589.46312.69914.7011.0039.84
ATOM3155CVALB4587.48311.98212.4641.0046.30
ATOM3156OVALB4587.56713.20112.3021.0047.67
ATOM3157NTYRB4597.39311.13811.4421.0050.45
ATOM3158CATYRB4597.38511.64010.0691.0057.07
ATOM3159CBTYRB4598.23310.7409.1701.0057.05
ATOM3160CGTYRB4599.67310.6809.6111.0059.29
ATOM3161CD1TYRB45910.28411.78610.2031.0060.93
ATOM3162CE1TYRB45911.59111.72510.6621.0061.86
ATOM3163CD2TYRB45910.4149.5109.4861.0059.46
ATOM3164CE2TYRB45911.7269.4399.9431.0059.67
ATOM3165CZTYRB45912.30510.54810.5321.0060.84
ATOM3166OHTYRB45913.59310.47711.0091.0061.39
ATOM3167CTYRB4595.97611.7539.5141.0061.22
ATOM3168OTYRB4595.62912.7508.8741.0062.89
ATOM3169NTHRB4605.16610.7309.7681.0065.15
ATOM3170CATHRB4603.78310.7029.3091.0067.76
ATOM3171CBTHRB4603.1789.2839.4641.0068.02
ATOM3172OG1THRB4601.8909.2358.8361.0067.03
ATOM3173CG2THRB4603.0408.91610.9381.0067.31
ATOM3174CTHRB4602.94511.70010.1071.0070.14
ATOM3175OTHRB4601.71511.64110.0991.0072.35
ATOM3176NPHEB4613.62512.62010.7881.0072.64
ATOM3177CAPHEB4612.96913.63711.6071.0075.05
ATOM3178CBPHEB4613.97714.72012.0121.0075.47
ATOM3179CGPHEB4614.23514.78913.4921.0074.32
ATOM3180CD1PHEB4613.20014.60914.4041.0073.98
ATOM3181CD2PHEB4615.51715.02513.9751.0075.22
ATOM3182CE1PHEB4613.43814.66215.7751.0074.02
ATOM3183CE2PHEB4615.76515.08015.3441.0074.50
ATOM3184CZPHEB4614.72214.89716.2451.0074.10
ATOM3185CPHEB4611.78714.28610.8961.0076.78
ATOM3186OPHEB4611.77514.2799.6451.0077.08
ATOM3187CBGLUB4707.87323.78914.7181.0080.19
ATOM3188CGLUB4708.95821.73115.6501.0079.30
ATOM3189OGLUB4709.88721.51816.4321.0078.21
ATOM3190NGLUB4709.09622.23513.2271.0080.22
ATOM3191CAGLUB4709.06022.83014.5951.0080.03
ATOM3192NGLUB4717.82321.03715.6651.0078.31
ATOM3193CAGLUB4717.59619.95616.6171.0075.83
ATOM3194CBGLUB4716.11819.54316.6041.0076.70
ATOM3195CGGLUB4715.74218.54415.5161.0078.42
ATOM3196CDGLUB4715.06219.19814.3271.0079.69
ATOM3197OE1GLUB4713.82919.39814.3781.0080.26
ATOM3198OE2GLUB4715.76319.51113.3401.0080.72
ATOM3199CGLUB4718.48718.75616.2921.0073.13
ATOM3200OGLUB4718.89718.02117.1891.0073.86
ATOM3201NLYSB4728.78518.56515.0091.0069.65
ATOM3202CALYSB4729.63917.46114.5811.0064.40
ATOM3203CBLYSB4729.57817.29313.0601.0063.78
ATOM3204CGLYSB4728.34316.55212.5661.0064.49
ATOM3205CDLYSB4728.54416.00211.1611.0063.81
ATOM3206CELYSB4727.37916.36810.2491.0064.90
ATOM3207NZLYSB4726.47515.2129.9901.0063.97
ATOM3208CLYSB47211.07117.74915.0141.0061.03
ATOM3209OLYSB47211.84816.83315.2871.0060.28
ATOM3210NASPB47311.41319.03315.0761.0056.84
ATOM3211CAASPB47312.74519.45115.4881.0051.69
ATOM3212CBASPB47312.92320.94015.2421.0050.36
ATOM3213CASPB47312.92319.13816.9701.0049.18
ATOM3214OASPB47313.95918.61917.3851.0046.85
ATOM3215NHISB47411.89819.44917.7581.0045.35
ATOM3216CAHISB47411.92319.20319.1961.0043.65
ATOM3217CBHISB47410.65219.76119.8471.0043.70
ATOM3218CGHISB47410.45819.32621.2671.0043.86
ATOM3219CD2HISB47411.09519.68822.4061.0044.12
ATOM3220ND1HISB4749.51018.39521.6381.0046.60
ATOM3221CE1HISB4749.57218.20222.9431.0045.29
ATOM3222NE2HISB47410.52618.97523.4341.0047.96
ATOM3223CHISB47412.03017.70719.4711.0042.38
ATOM3224OHISB47412.83417.27320.2981.0042.83
ATOM3225NILEB47511.21416.92318.7731.0038.86
ATOM3226CAILEB47511.22215.47518.9431.0036.53
ATOM3227CBILEB47510.10514.82218.1101.0036.56
ATOM3228CG2ILEB47510.39013.33517.9111.0036.17
ATOM3229CG1ILEB4758.77014.99818.8321.0035.81
ATOM3230CD1ILEB4757.59814.41018.0941.0041.77
ATOM3231CILEB47512.57514.89818.5321.0033.72
ATOM3232OILEB47513.11214.02319.2071.0031.50
ATOM3233NHISB47613.12115.37517.4291.0033.65
ATOM3234CAHISB47614.42114.88616.9921.0033.31
ATOM3235CBHISB47614.78215.48115.6371.0037.30
ATOM3236CGHISB47614.13214.78114.4861.0043.64
ATOM3237CD2HISB47613.72313.49814.3421.0045.25
ATOM3238ND1HISB47613.81615.41913.3061.0048.37
ATOM3239CE1HISB47613.23814.56012.4841.0048.87
ATOM3240NE2HISB47613.17013.38713.0891.0048.11
ATOM3241CHISB47615.50615.21318.0221.0031.20
ATOM3242OHISB47616.44214.43618.2081.0027.25
ATOM3243NARGB47715.38716.36518.6841.0030.64
ATOM3244CAARGB47716.36116.75419.7031.0030.09
ATOM3245CBARGB47716.14418.21420.1211.0033.46
ATOM3246CGARGB47716.32219.21218.9821.0040.74
ATOM3247CDARGB47716.27420.64919.4791.0045.91
ATOM3248NEARGB47717.51421.02020.1551.0051.37
ATOM3249CZARGB47718.37521.92719.7021.0053.68
ATOM3250NH1ARGB47718.14022.56718.5601.0053.04
ATOM3251NH2ARGB47719.48022.18520.3891.0051.79
ATOM3252CARGB47716.23215.83520.9251.0026.97
ATOM3253OARGB47717.23315.38721.4861.0027.34
ATOM3254NVALB47814.99915.55821.3381.0023.70
ATOM3255CAVALB47814.78014.68522.4821.0024.79
ATOM3256CBVALB47813.28614.61322.8611.0024.83
ATOM3257CG1VALB47813.08813.64624.0221.0026.23
ATOM3258CG2VALB47812.78115.99623.2431.0028.26
ATOM3259CVALB47815.28413.29422.1121.0026.10
ATOM3260OVALB47815.91912.61322.9271.0024.28
ATOM3261NLEUB47915.02112.88920.8701.0022.92
ATOM3262CALEUB47915.45611.58420.3791.0021.96
ATOM3263CBLEUB47914.99211.37218.9301.0022.63
ATOM3264CGLEUB47913.57510.79818.7561.0020.82
ATOM3265CD1LEUB47913.23110.68917.2741.0022.53
ATOM3266CD2LEUB47913.4959.44019.4201.0023.08
ATOM3267CLEUB47916.97511.47120.4531.0021.90
ATOM3268OLEUB47917.50610.41620.7781.0023.11
ATOM3269NASPB48017.67512.56020.1431.0023.65
ATOM3270CAASPB48019.14112.56620.1981.0024.29
ATOM3271CBASPB48019.69213.88919.6491.0026.88
ATOM3272CGASPB48019.77313.91418.1291.0033.32
ATOM3273OD1ASPB48019.85712.83617.4991.0035.44
ATOM3274OD2ASPB48019.75715.02217.5631.0032.44
ATOM3275CASPB48019.59012.40621.6561.0024.13
ATOM3276OASPB48020.55111.69721.9561.0024.88
ATOM3277NLYSB48118.88713.07722.5601.0025.18
ATOM3278CALYSB48119.21313.01023.9801.0026.78
ATOM3279CBLYSB48118.26213.89824.7851.0031.37
ATOM3280CGLYSB48118.96214.78825.8041.0043.84
ATOM3281CDLYSB48118.78014.26027.2191.0046.08
ATOM3282CELYSB48120.12013.92827.8651.0050.99
ATOM3283NZLYSB48121.17714.92227.5111.0054.35
ATOM3284CLYSB48119.12411.57524.4951.0026.87
ATOM3285OLYSB48119.95111.14525.3051.0020.37
ATOM3286NILEB48218.12410.83024.0271.0023.26
ATOM3287CAILEB48217.9819.45224.4721.0021.07
ATOM3288CBILEB48216.6558.82824.0151.0019.80
ATOM3289CG2ILEB48216.5807.37024.4911.0017.40
ATOM3290CG1ILEB48215.4799.60624.6021.0017.16
ATOM3291CD1ILEB48214.1369.20923.9911.0019.43
ATOM3292CILEB48219.1358.61623.9471.0020.21
ATOM3293OILEB48219.6217.72224.6401.0025.55
ATOM3294NTHRB48319.5698.89622.7221.0021.89
ATOM3295CATHRB48320.7018.17622.1411.0022.67
ATOM3296CBTHRB48321.0308.66220.6951.0023.34
ATOM3297OG1THRB48319.8908.47519.8511.0027.33
ATOM3298CG2THRB48322.2037.88220.1161.0024.46
ATOM3299CTHRB48321.9138.44123.0351.0023.51
ATOM3300OTHRB48322.6507.52023.3811.0027.01
ATOM3301NASPB48422.1199.70323.4041.0022.88
ATOM3302CAASPB48423.23710.05824.2761.0024.93
ATOM3303CBASPB48423.20111.54624.6521.0028.69
ATOM3304CGASPB48423.50412.46423.4851.0029.19
ATOM3305OD1ASPB48423.98211.98422.4371.0029.63
ATOM3306OD2ASPB48423.25613.68123.6271.0032.02
ATOM3307CASPB48423.1259.24925.5671.0024.40
ATOM3308OASPB48424.1258.78026.1031.0025.60
ATOM3309NTHRB48521.8999.09626.0661.0020.16
ATOM3310CATHRB48521.6708.36527.3071.0022.28
ATOM3311CBTHRB48520.2038.52127.7631.0024.64
ATOM3312OG1THRB48519.8789.91427.8301.0024.28
ATOM3313CG2THRB48519.9937.89629.1331.0023.32
ATOM3314CTHRB48522.0176.88127.1881.0022.13
ATOM3315OTHRB48522.5746.28428.1151.0023.30
ATOM3316NLEUB48621.6866.29026.0451.0023.08
ATOM3317CALEUB48621.9694.88125.7921.0022.26
ATOM3318CBLEUB48621.3464.45224.4641.0020.93
ATOM3319CGLEUB48619.8784.03124.5331.0024.92
ATOM3320CD1LEUB48619.2954.00323.1231.0021.96
ATOM3321CD2LEUB48619.7632.65825.1961.0023.90
ATOM3322CLEUB48623.4774.63425.7421.0024.12
ATOM3323OLEUB48623.9843.68126.3341.0024.02
ATOM3324NILEB48724.1915.49025.0221.0024.53
ATOM3325CAILEB48725.6405.34524.9131.0025.16
ATOM3326CBILEB48726.2076.37923.8991.0025.57
ATOM3327CG2ILEB48727.7256.52224.0511.0024.54
ATOM3328CG1ILEB48725.8575.93622.4701.0025.63
ATOM3329CD1ILEB48726.5384.64622.0211.0025.68
ATOM3330CILEB48726.2755.51826.3071.0023.60
ATOM3331OILEB48727.2004.79426.6711.0023.65
ATOM3332NHISB48825.7556.45627.0811.0021.75
ATOM3333CAHISB48826.2516.72028.4311.0026.07
ATOM3334CBHISB48825.4507.87129.0411.0026.99
ATOM3335CGHISB48825.8188.19630.4551.0033.06
ATOM3336CD2HISB48825.2457.83831.6291.0032.79
ATOM3337ND1HISB48826.8699.02530.7791.0036.45
ATOM3338CE1HISB48826.9279.16432.0911.0035.93
ATOM3339NE2HISB48825.9538.45332.6301.0033.88
ATOM3340CHISB48826.1235.46329.2921.0026.85
ATOM3341OHISB48827.0715.05429.9671.0028.52
ATOM3342NLEUB48924.9494.85029.2661.0028.00
ATOM3343CALEUB48924.7153.64230.0401.0025.94
ATOM3344CBLEUB48923.2983.12729.7881.0027.07
ATOM3345CGLEUB48922.1583.90930.4451.0031.71
ATOM3346CD1LEUB48920.8273.51629.7991.0028.08
ATOM3347CD2LEUB48922.1433.61631.9491.0029.30
ATOM3348CLEUB48925.7182.56129.6421.0026.84
ATOM3349OLEUB48926.2411.83230.4861.0020.86
ATOM3350NMETB49025.9782.45328.3451.0023.82
ATOM3351CAMETB49026.9001.43827.8571.0026.38
ATOM3352CBMETB49026.7751.30626.3361.0027.29
ATOM3353CGMETB49025.4180.77625.8951.0021.68
ATOM3354SDMETB49025.2080.73924.1061.0026.30
ATOM3355CEMETB49023.4610.41224.0221.0019.66
ATOM3356CMETB49028.3411.74328.2471.0026.42
ATOM3357OMETB49029.1090.83328.5741.0024.76
ATOM3358NALAB49128.7133.01828.2071.0026.67
ATOM3359CAALAB49130.0743.39428.5771.0030.73
ATOM3360CBALAB49130.2994.88228.3351.0026.66
ATOM3361CALAB49130.2503.05330.0561.0032.08
ATOM3362OALAB49131.1942.36130.4381.0034.66
ATOM3363NLYSB49229.3163.52330.8781.0033.17
ATOM3364CALYSB49229.3543.26732.3091.0032.82
ATOM3365CBLYSB49228.1103.84932.9761.0036.38
ATOM3366CGLYSB49228.4124.79734.1231.0038.68
ATOM3367CDLYSB49227.2424.88735.0841.0041.41
ATOM3368CELYSB49226.2996.01334.6981.0047.57
ATOM3369NZLYSB49226.3957.18435.6181.0050.76
ATOM3370CLYSB49229.4531.77132.6191.0034.08
ATOM3371OLYSB49230.0901.38233.5931.0034.31
ATOM3372NALAB49328.8350.93531.7881.0032.03
ATOM3373CAALAB49328.867−0.51031.9981.0030.70
ATOM3374CBALAB49327.719−1.18131.2451.0028.80
ATOM3375CALAB49330.201−1.15631.6061.0033.75
ATOM3376OALAB49330.402−2.35631.8191.0030.53
ATOM3377NGLYB49431.102−0.37231.0201.0033.50
ATOM3378CAGLYB49432.405−0.90330.6561.0033.71
ATOM3379CGLYB49432.639−1.36029.2301.0034.40
ATOM3380OGLYB49433.663−1.98928.9501.0033.13
ATOM3381NLEUB49531.712−1.05628.3261.0031.76
ATOM3382CALEUB49531.859−1.45226.9251.0030.57
ATOM3383CBLEUB49530.494−1.41526.2161.0030.67
ATOM3384CGLEUB49529.610−2.67526.2561.0029.59
ATOM3385CD1LEUB49529.315−3.05827.7001.0026.60
ATOM3386CD2LEUB49528.307−2.41625.5011.0027.52
ATOM3387CLEUB49532.829−0.51526.2021.0030.53
ATOM3388OLEUB49532.8550.68826.4681.0028.14
ATOM3389NTHRB49633.628−1.06425.2911.0028.03
ATOM3390CATHRB49634.567−0.24324.5291.0029.06
ATOM3391CBTHRB49635.511−1.09523.6651.0029.40
ATOM3392OG1THRB49634.753−1.75822.6411.0030.29
ATOM3393CG2THRB49636.228−2.12224.5151.0028.12
ATOM3394CTHRB49633.7700.65223.5901.0030.12
ATOM3395OTHRB49632.5800.43323.3801.0029.74
ATOM3396NLEUB49734.4301.65423.0181.0030.44
ATOM3397CALEUB49733.7622.56722.1041.0028.54
ATOM3398CBLEUB49734.7683.56421.5291.0031.14
ATOM3399CGLEUB49735.2094.71922.4341.0033.58
ATOM3400CD1LEUB49736.1205.65921.6521.0031.42
ATOM3401CD2LEUB49733.9925.46922.9421.0035.08
ATOM3402CLEUB49733.0951.80020.9671.0027.35
ATOM3403OLEUB49731.9672.10520.5741.0024.03
ATOM3404NGLNB49833.7980.79720.4471.0026.17
ATOM3405CAGLNB49833.289−0.00919.3481.0026.32
ATOM3406CBGLNB49834.411−0.87618.7711.0027.25
ATOM3407CGGLNB49833.967−1.79617.6451.0032.67
ATOM3408CDGLNB49834.965−2.91217.3741.0038.39
ATOM3409OE1GLNB49835.737−3.29818.2541.0036.78
ATOM3410NE2GLNB49834.953−3.43716.1531.0033.18
ATOM3411CGLNB49832.112−0.88819.7741.0025.70
ATOM3412OGLNB49831.167−1.07619.0091.0025.35
ATOM3413NGLNB49932.173−1.43420.9861.0024.01
ATOM3414CAGLNB49931.093−2.28121.4871.0025.34
ATOM3415CBGLNB49931.501−2.93522.8151.0028.38
ATOM3416CGGLNB49932.537−4.05622.6691.0029.13
ATOM3417CDGLNB49932.913−4.68723.9951.0030.80
ATOM3418OE1GLNB49933.306−3.99724.9371.0033.62
ATOM3419NE2GLNB49932.797−6.00424.0741.0030.64
ATOM3420CGLNB49929.842−1.43021.6931.0025.70
ATOM3421OGLNB49928.715−1.91021.5541.0026.22
ATOM3422NGLNB50030.062−0.16022.0201.0023.09
ATOM3423CAGLNB50028.9890.79322.2561.0023.53
ATOM3424CBGLNB50029.5642.10722.7821.0026.17
ATOM3425CGGLNB50029.9582.07324.2521.0027.71
ATOM3426CDGLNB50030.8123.26224.6411.0029.32
ATOM3427OE1GLNB50030.5594.38624.2071.0028.48
ATOM3428NE2GLNB50031.8313.02125.4631.0025.07
ATOM3429CGLNB50028.1511.07421.0151.0024.24
ATOM3430OGLNB50026.9230.94921.0531.0024.40
ATOM3431NHISB50128.7901.46519.9151.0023.08
ATOM3432CAHISB50128.0041.73918.7241.0026.92
ATOM3433CBHISB50128.7912.57717.6971.0032.00
ATOM3434CGHISB50129.9881.89617.1051.0036.97
ATOM3435CD2HISB50130.1220.71016.4651.0040.32
ATOM3436ND1HISB50131.2242.50517.0421.0037.88
ATOM3437CE1HISB50132.0661.72416.3891.0038.81
ATOM3438NE2HISB50131.4220.62816.0281.0041.21
ATOM3439CHISB50127.4510.45718.1231.0025.91
ATOM3440OHISB50126.3690.45717.5311.0020.13
ATOM3441NGLNB50228.165−0.64818.3171.0024.94
ATOM3442CAGLNB50227.698−1.92617.8041.0021.88
ATOM3443CBGLNB50228.785−2.99617.9531.0024.62
ATOM3444CGGLNB50229.796−3.00116.7971.0026.55
ATOM3445CDGLNB50230.843−4.10916.9021.0027.06
ATOM3446OE1GLNB50230.716−5.03317.7051.0028.49
ATOM3447NE2GLNB50231.882−4.01816.0781.0021.90
ATOM3448CGLNB50226.428−2.34118.5541.0022.39
ATOM3449OGLNB50225.464−2.80717.9441.0022.24
ATOM3450NARGB50326.421−2.15919.8741.0020.54
ATOM3451CAARGB50325.259−2.52320.6781.0022.04
ATOM3452CBARGB50325.602−2.51922.1801.0022.51
ATOM3453CGARGB50324.451−3.02223.0771.0023.34
ATOM3454CDARGB50324.853−3.11024.5501.0022.18
ATOM3455NEARGB50323.743−3.54625.3951.0019.62
ATOM3456CZARGB50323.329−4.80725.4971.0019.88
ATOM3457NH1ARGB50323.933−5.76524.8091.0016.40
ATOM3458NH2ARGB50322.303−5.11026.2801.0019.71
ATOM3459CARGB50324.102−1.55820.4091.0019.05
ATOM3460OARGB50322.945−1.96820.3511.0018.87
ATOM3461NLEUB50424.414−0.27620.2391.0020.19
ATOM3462CALEUB50423.3750.71419.9691.0019.33
ATOM3463CBLEUB50423.9722.11719.8551.0016.25
ATOM3464CGLEUB50422.9833.17319.3441.0020.35
ATOM3465CD1LEUB50421.9303.44920.4271.0017.97
ATOM3466CD2LEUB50423.7294.44818.9551.0020.86
ATOM3467CLEUB50422.6590.35718.6671.0021.22
ATOM3468OLEUB50421.4330.47818.5661.0019.28
ATOM3469NALAB50523.428−0.08517.6761.0018.55
ATOM3470CAALAB50522.859−0.47316.3961.0018.20
ATOM3471CBALAB50523.973−0.74515.3821.0018.45
ATOM3472CALAB50521.986−1.71616.5621.0019.54
ATOM3473OALAB50520.871−1.77416.0411.0017.63
ATOM3474NGLNB50622.497−2.70617.2931.0020.30
ATOM3475CAGLNB50621.772−3.95517.5131.0019.48
ATOM3476CBGLNB50622.590−4.89318.4091.0021.75
ATOM3477CGGLNB50623.798−5.55117.7271.0020.85
ATOM3478CDGLNB50624.819−6.07018.7361.0026.18
ATOM3479OE1GLNB50624.564−6.08419.9431.0021.83
ATOM3480NE2GLNB50625.977−6.49918.2451.0025.39
ATOM3481CGLNB50620.421−3.67218.1661.0021.39
ATOM3482OGLNB50619.396−4.23317.7661.0020.87
ATOM3483NLEUB50720.433−2.80019.1711.0019.52
ATOM3484CALEUB50719.219−2.41819.8841.0023.04
ATOM3485CBLEUB50719.548−1.45521.0301.0022.82
ATOM3486CGLEUB50720.182−2.01122.3131.0026.12
ATOM3487CD1LEUB50720.203−0.91623.3601.0029.33
ATOM3488CD2LEUB50719.415−3.21322.8161.0027.80
ATOM3489CLEUB50718.212−1.73018.9711.0022.19
ATOM3490OLEUB50717.036−2.07018.9641.0023.00
ATOM3491NLEUB50818.678−0.74518.2141.0021.53
ATOM3492CALEUB50817.7970.00617.3321.0020.60
ATOM3493CBLEUB50818.5351.23616.8051.0017.57
ATOM3494CGLEUB50818.9342.21817.9131.0017.67
ATOM3495CD1LEUB50819.5663.44617.3011.0020.04
ATOM3496CD2LEUB50817.7242.61118.7251.0018.49
ATOM3497CLEUB50817.235−0.83116.1831.0021.17
ATOM3498OLEUB50816.118−0.59715.7281.0021.88
ATOM3499NLEUB50918.000−1.81315.7131.0021.89
ATOM3500CALEUB50917.511−2.65714.6311.0022.81
ATOM3501CBLEUB50918.603−3.59714.1451.0022.65
ATOM3502CGLEUB50919.645−2.89113.2781.0029.11
ATOM3503CD1LEUB50920.697−3.88812.8291.0025.69
ATOM3504CD2LEUB50918.965−2.24812.0821.0027.92
ATOM3505CLEUB50916.302−3.46215.0951.0023.32
ATOM3506OLEUB50915.409−3.75914.3031.0023.36
ATOM3507NILEB51016.264−3.79616.3801.0023.36
ATOM3508CAILEB51015.148−4.56216.9121.0020.99
ATOM3509CBILEB51015.448−5.04118.3611.0028.60
ATOM3510CG2ILEB51014.162−5.43519.0751.0028.10
ATOM3511CG1ILEB51016.383−6.26018.3081.0026.57
ATOM3512CD1ILEB51017.429−6.30119.4191.0030.14
ATOM3513CILEB51013.852−3.74616.8461.0017.65
ATOM3514OILEB51012.767−4.30816.7591.0016.11
ATOM3515NLEUB51113.961−2.42116.8671.0018.12
ATOM3516CALEUB51112.772−1.57416.7741.0016.95
ATOM3517CBLEUB51113.147−0.10016.9811.0022.66
ATOM3518CGLEUB51113.6070.26218.4061.0022.13
ATOM3519CD1LEUB51113.4041.75118.6521.0025.29
ATOM3520CD2LEUB51112.830−0.54919.4251.0025.08
ATOM3521CLEUB51112.112−1.77115.3971.0016.65
ATOM3522OLEUB51110.915−1.57815.2421.0017.09
ATOM3523NSERB51212.901−2.16114.4011.0015.83
ATOM3524CASERB51212.355−2.40813.0721.0018.66
ATOM3525CBSERB51213.484−2.64412.0741.0017.62
ATOM3526OGSERB51213.079−3.55011.0621.0032.77
ATOM3527CSERB51211.454−3.63813.1541.0018.54
ATOM3528OSERB51210.373−3.68312.5451.0017.01
ATOM3529NHISB51311.899−4.62513.9291.0015.54
ATOM3530CAHISB51311.141−5.86014.1151.0017.67
ATOM3531CBHISB51312.013−6.91614.7901.0019.03
ATOM3532CGHISB51313.063−7.47513.8861.0027.06
ATOM3533CD2HISB51312.980−8.36412.8681.0028.40
ATOM3534ND1HISB51314.378−7.06613.9321.0028.92
ATOM3535CE1HISB51315.061−7.67812.9811.0030.75
ATOM3536NE2HISB51314.235−8.47212.3211.0030.08
ATOM3537CHISB5139.895−5.60214.9581.0015.35
ATOM3538OHISB5138.846−6.19214.7041.0014.83
ATOM3539NILEB51410.012−4.74415.9421.0013.35
ATOM3540CAILEB5148.865−4.41716.7761.0015.48
ATOM3541CBILEB5149.295−3.53417.9671.0020.02
ATOM3542CG2ILEB5148.067−2.91818.6501.0012.84
ATOM3543CG1ILEB51410.093−4.39718.9621.0022.87
ATOM3544CD1ILEB51410.691−3.64120.1151.0029.62
ATOM3545CILEB5147.797−3.71715.9231.0015.16
ATOM3546OILEB5146.606−3.97216.0781.0016.61
ATOM3547NARGB5158.224−2.82315.0301.0016.33
ATOM3548CAARGB5157.280−2.13814.1501.0017.54
ATOM3549CBARGB5158.010−1.17313.2141.0020.15
ATOM3550CGARGB5157.080−0.45412.2341.0021.47
ATOM3551CDARGB5156.4070.74912.8911.0026.05
ATOM3552NEARGB5157.2201.94812.7161.0024.91
ATOM3553CZARGB5156.7343.17512.5471.0024.61
ATOM3554NH1ARGB5155.4243.39312.5221.0022.46
ATOM3555NH2ARGB5157.5694.18212.3741.0023.15
ATOM3556CARGB5156.545−3.18213.3041.0016.60
ATOM3557OARGB5155.332−3.09313.0871.0014.51
ATOM3558NHISB5167.298−4.17112.8271.0018.50
ATOM3559CAHISB5166.743−5.23711.9971.0017.26
ATOM3560CBHISB5167.861−6.17611.5331.0018.14
ATOM3561CGHISB5167.405−7.22310.5681.0024.87
ATOM3562CD2HISB5167.060−8.52110.7541.0026.64
ATOM3563ND1HISB5167.258−6.9789.2201.0021.82
ATOM3564CE1HISB5166.839−8.0788.6191.0028.42
ATOM3565NE2HISB5166.711−9.0289.5261.0024.47
ATOM3566CHISB5165.685−6.02812.7591.0016.87
ATOM3567OHISB5164.596−6.30312.2401.0014.81
ATOM3568NMETB5175.999−6.39613.9971.0016.48
ATOM3569CAMETB5175.049−7.16214.8011.0015.39
ATOM3570CBMETB5175.701−7.58716.1141.0021.05
ATOM3571CGMETB5176.790−8.63815.9171.0020.76
ATOM3572SDMETB5177.380−9.32017.4701.0023.96
ATOM3573CEMETB5178.104−7.87918.2261.0020.45
ATOM3574CMETB5173.789−6.36815.0801.0016.23
ATOM3575OMETB5172.688−6.92415.1481.0016.02
ATOM3576NSERB5183.954−5.06015.2471.0013.32
ATOM3577CASERB5182.827−4.18615.5051.0016.34
ATOM3578CBSERB5183.316−2.76515.8351.0017.48
ATOM3579OGSERB5182.234−1.84015.8431.0017.46
ATOM3580CSERB5181.906−4.14714.2841.0014.73
ATOM3581OSERB5180.688−4.24714.4171.0019.16
ATOM3582NASNB5192.474−4.00613.0911.0014.52
ATOM3583CAASNB5191.622−3.95311.9071.0015.35
ATOM3584CBASNB5192.432−3.50910.6981.0019.21
ATOM3585CGASNB5192.700−2.02910.7291.0020.58
ATOM3586OD1ASNB5191.839−1.25811.1501.0026.36
ATOM3587ND2ASNB5193.891−1.61810.3071.0019.62
ATOM3588CASNB5190.911−5.28011.6581.0016.74
ATOM3589OASNB519−0.265−5.29911.2971.0020.58
ATOM3590NLYSB5201.608−6.38711.8851.0018.60
ATOM3591CALYSB5200.992−7.69911.7171.0020.04
ATOM3592CBLYSB5202.038−8.80111.8721.0025.44
ATOM3593CGLYSB5203.037−8.84910.7281.0031.68
ATOM3594CDLYSB5202.507−9.6639.5581.0042.56
ATOM3595CELYSB5202.186−8.7788.3641.0045.61
ATOM3596NZLYSB5201.435−9.5267.3121.0046.00
ATOM3597CLYSB520−0.099−7.86812.7691.0018.88
ATOM3598OLYSB520−1.183−8.35812.4781.0021.75
ATOM3599NGLYB5210.191−7.45513.9981.0017.83
ATOM3600CAGLYB521−0.792−7.56915.0581.0016.19
ATOM3601CGLYB521−2.000−6.67414.8331.0016.59
ATOM3602OGLYB521−3.128−7.06015.1251.0016.57
ATOM3603NMETB522−1.766−5.46714.3261.0017.48
ATOM3604CAMETB522−2.852−4.52714.0421.0018.25
ATOM3605CBMETB522−2.276−3.21213.5161.0021.27
ATOM3606CGMETB522−3.190−2.01813.7071.0026.97
ATOM3607SDMETB522−3.199−1.47715.4171.0030.35
ATOM3608CEMETB522−1.659−0.60515.4751.0029.86
ATOM3609CMETB522−3.794−5.11912.9891.0018.68
ATOM3610OMETB522−5.022−5.00813.0971.0018.80
ATOM3611NGLUB523−3.205−5.73111.9661.0018.22
ATOM3612CAGLUB523−3.968−6.35710.8891.0023.41
ATOM3613CBGLUB523−3.031−6.9469.8301.0028.74
ATOM3614CGGLUB523−2.224−5.9359.0301.0034.42
ATOM3615CDGLUB523−1.095−6.5978.2391.0045.58
ATOM3616OE1GLUB523−0.131−5.8947.8571.0049.48
ATOM3617OE2GLUB523−1.169−7.8257.9991.0045.97
ATOM3618CGLUB523−4.812−7.48211.4651.0023.98
ATOM3619OGLUB523−5.993−7.61611.1471.0022.08
ATOM3620NHISB524−4.187−8.28712.3261.0023.46
ATOM3621CAHISB524−4.846−9.42812.9521.0026.20
ATOM3622CBHISB524−3.824−10.24513.7431.0027.26
ATOM3623CGHISB524−4.378−11.50914.3211.0030.91
ATOM3624CD2HISB524−4.308−12.79213.8921.0030.90
ATOM3625ND1HISB524−5.107−11.53715.4901.0028.87
ATOM3626CE1HISB524−5.461−12.78015.7571.0030.45
ATOM3627NE2HISB524−4.989−13.56114.8031.0029.19
ATOM3628CHISB524−5.996−9.02513.8701.0027.69
ATOM3629OHISB524−7.061−9.65613.8601.0025.00
ATOM3630NLEUB525−5.777−7.97714.6551.0023.84
ATOM3631CALEUB525−6.786−7.49215.5881.0025.77
ATOM3632CBLEUB525−6.217−6.35816.4441.0022.22
ATOM3633CGLEUB525−7.164−5.77817.4981.0026.81
ATOM3634CD1LEUB525−7.763−6.92218.3211.0023.32
ATOM3635CD2LEUB525−6.414−4.79318.3991.0018.95
ATOM3636CLEUB525−8.013−6.99514.8421.0026.84
ATOM3637OLEUB525−9.154−7.24715.2491.0026.73
ATOM3638NTYRB526−7.764−6.27113.7571.0026.86
ATOM3639CATYRB526−8.819−5.72612.9181.0030.89
ATOM3640CBTYRB526−8.201−4.81811.8541.0034.31
ATOM3641CGTYRB526−9.183−4.22310.8781.0043.50
ATOM3642CD1TYRB526−10.058−3.21111.2671.0047.66
ATOM3643CE1TYRB526−10.943−2.63610.3571.0048.85
ATOM3644CD2TYRB526−9.218−4.6519.5521.0048.52
ATOM3645CE2TYRB526−10.098−4.0838.6341.0052.43
ATOM3646CZTYRB526−10.955−3.0779.0431.0051.67
ATOM3647OHTYRB526−11.810−2.5048.1291.0057.01
ATOM3648CTYRB526−9.577−6.88012.2651.0030.90
ATOM3649OTYRB526−10.793−6.82912.1131.0031.48
ATOM3650NSERB527−8.849−7.92611.8891.0031.39
ATOM3651CASERB527−9.460−9.09511.2661.0033.73
ATOM3652CBSERB527−8.377−10.04810.7491.0034.13
ATOM3653OGSERB527−8.945−11.22210.1961.0043.67
ATOM3654CSERB527−10.339−9.81312.2881.0034.34
ATOM3655OSERB527−11.446−10.26111.9731.0033.42
ATOM3656NMETB528−9.840−9.91613.5171.0031.66
ATOM3657CAMETB528−10.574−10.57214.5891.0029.77
ATOM3658CBMETB528−9.682−10.74315.8201.0032.96
ATOM3659CGMETB528−8.651−11.85915.6991.0033.47
ATOM3660SDMETB528−9.359−13.42715.1341.0038.28
ATOM3661CEMETB528−10.265−13.91516.5791.0036.01
ATOM3662CMETB528−11.800−9.74714.9531.0029.42
ATOM3663OMETB528−12.835−10.29315.3311.0028.65
ATOM3664NLYSB529−11.673−8.42914.8501.0030.64
ATOM3665CALYSB529−12.781−7.53315.1491.0031.80
ATOM3666CBLYSB529−12.323−6.07915.0271.0032.86
ATOM3667CGLYSB529−13.436−5.04315.1141.0036.42
ATOM3668CDLYSB529−13.114−3.85214.2241.0041.74
ATOM3669CELYSB529−13.734−2.56414.7411.0043.45
ATOM3670NZLYSB529−15.221−2.56914.6341.0046.51
ATOM3671CLYSB529−13.857−7.84014.1161.0036.60
ATOM3672OLYSB529−15.049−7.87714.4241.0034.04
ATOM3673NCYSB530−13.407−8.08312.8891.0040.04
ATOM3674CACYSB530−14.286−8.40911.7731.0044.58
ATOM3675CBCYSB530−13.460−8.53510.4911.0050.64
ATOM3676SGCYSB530−13.369−7.0349.5041.0067.65
ATOM3677CCYSB530−15.065−9.69212.0161.0042.88
ATOM3678OCYSB530−16.274−9.74111.8071.0040.15
ATOM3679NLYSB531−14.360−10.73312.4471.0041.92
ATOM3680CALYSB531−14.980−12.02312.7281.0042.60
ATOM3681CBLYSB531−13.907−13.09112.9271.0044.77
ATOM3682CLYSB531−15.844−11.90713.9771.0044.43
ATOM3683OLYSB531−16.623−12.80414.2961.0044.09
ATOM3684NASNB532−15.678−10.79314.6851.0044.98
ATOM3685CAASNB532−16.437−10.49615.8931.0044.10
ATOM3686CBASNB532−17.833−10.00315.5061.0045.14
ATOM3687CGASNB532−18.526−9.27116.6331.0046.54
ATOM3688OD1ASNB532−19.729−9.42416.8371.0050.62
ATOM3689ND2ASNB532−17.771−8.47117.3751.0046.07
ATOM3690CASNB532−16.557−11.65716.8821.0043.34
ATOM3691OASNB532−17.655−11.99417.3211.0041.42
ATOM3692NVALB533−15.434−12.26417.2431.0043.45
ATOM3693CAVALB533−15.471−13.37118.1901.0044.06
ATOM3694CBVALB533−14.170−14.21918.1201.0045.56
ATOM3695CG1VALB533−13.661−14.26316.6831.0045.67
ATOM3696CG2VALB533−13.107−13.64419.0451.0044.16
ATOM3697CVALB533−15.670−12.83519.6111.0043.24
ATOM3698OVALB533−15.894−13.60220.5481.0044.21
ATOM3699NVALB534−15.596−11.51119.7551.0040.44
ATOM3700CAVALB534−15.765−10.84921.0491.0037.80
ATOM3701CBVALB534−14.630−11.25922.0381.0036.38
ATOM3702CG1VALB534−13.324−10.57521.6581.0034.35
ATOM3703CG2VALB534−15.021−10.91023.4631.0039.34
ATOM3704CVALB534−15.752−9.32920.8571.0037.97
ATOM3705OVALB534−15.026−8.80820.0081.0039.45
ATOM3706NPROB535−16.575−8.59721.6251.0037.81
ATOM3707CDPROB535−17.529−9.07822.6401.0038.74
ATOM3708CAPROB535−16.608−7.13521.4921.0036.79
ATOM3709CBPROB535−17.846−6.72922.2881.0036.98
ATOM3710CGPROB535−18.004−7.80923.2981.0039.77
ATOM3711CPROB535−15.338−6.49422.0491.0033.95
ATOM3712OPROB535−14.786−6.96323.0401.0034.93
ATOM3713NLEUB536−14.881−5.42621.4091.0033.42
ATOM3714CALEUB536−13.675−4.73221.8511.0033.40
ATOM3715CBLEUB536−12.829−4.31420.6471.0029.31
ATOM3716CGLEUB536−12.219−5.43319.7981.0030.06
ATOM3717CD1LEUB536−11.344−4.82218.7141.0030.85
ATOM3718CD2LEUB536−11.398−6.37020.6761.0028.96
ATOM3719CLEUB536−14.036−3.49822.6661.0030.50
ATOM3720OLEUB536−15.024−2.82922.3831.0029.91
ATOM3721NTYRB537−13.231−3.19423.6761.0028.69
ATOM3722CATYRB537−13.494−2.03224.5051.0029.89
ATOM3723CBTYRB537−12.618−2.07125.7501.0032.50
ATOM3724CGTYRB537−12.849−3.32726.5431.0039.46
ATOM3725CD1TYRB537−13.923−3.43127.4211.0041.90
ATOM3726CE1TYRB537−14.174−4.60928.1181.0045.72
ATOM3727CD2TYRB537−12.022−4.43526.3791.0047.39
ATOM3728CE2TYRB537−12.262−5.62027.0721.0049.93
ATOM3729CZTYRB537−13.340−5.69927.9401.0048.80
ATOM3730OHTYRB537−13.582−6.87228.6241.0053.90
ATOM3731CTYRB537−13.262−0.76123.7091.0027.09
ATOM3732OTYRB537−12.518−0.75722.7291.0026.15
ATOM3733NASPB538−13.9090.31524.1411.0026.12
ATOM3734CAASPB538−13.8301.59823.4611.0025.27
ATOM3735CBASPB538−14.7482.59824.1641.0028.85
ATOM3736CGASPB538−16.2272.28523.9401.0033.90
ATOM3737OD1ASPB538−17.0522.61324.8191.0032.68
ATOM3738OD2ASPB538−16.5621.70722.8821.0038.26
ATOM3739CASPB538−12.4472.21723.2611.0025.18
ATOM3740OASPB538−12.1202.62622.1471.0026.41
ATOM3741NLEUB539−11.6372.30924.3131.0020.76
ATOM3742CALEUB539−10.3122.91124.1501.0019.65
ATOM3743CBLEUB539−9.5672.99125.4961.0017.48
ATOM3744CGLEUB539−8.1163.51125.4691.0016.46
ATOM3745CD1LEUB539−8.0514.89224.8381.0016.43
ATOM3746CD2LEUB539−7.5643.56926.8951.0015.57
ATOM3747CLEUB539−9.4842.12723.1271.0016.75
ATOM3748OLEUB539−8.8622.71622.2491.0020.36
ATOM3749NLEUB540−9.4870.80323.2391.0018.23
ATOM3750CALEUB540−8.743−0.04822.3191.0018.05
ATOM3751CBLEUB540−8.909−1.52822.7011.0016.38
ATOM3752CGLEUB540−8.188−2.55421.8211.0019.81
ATOM3753CD1LEUB540−6.679−2.30321.8281.0019.27
ATOM3754CD2LEUB540−8.473−3.95222.3271.0018.00
ATOM3755CLEUB540−9.2410.16920.8911.0021.50
ATOM3756OLEUB540−8.4490.29319.9641.0020.41
ATOM3757NLEUB541−10.5590.20620.7261.0022.40
ATOM3758CALEUB541−11.1640.41919.4131.0023.27
ATOM3759CBLEUB541−12.6860.42919.5271.0025.12
ATOM3760CGLEUB541−13.410−0.80818.9991.0036.53
ATOM3761CD1LEUB541−14.910−0.67119.2731.0030.98
ATOM3762CD2LEUB541−13.136−0.97117.5081.0031.93
ATOM3763CLEUB541−10.6971.75118.8421.0022.46
ATOM3764OLEUB541−10.3591.84517.6661.0026.29
ATOM3765NGLUB542−10.6942.78119.6801.0023.96
ATOM3766CAGLUB542−10.2484.10619.2701.0026.91
ATOM3767CBGLUB542−10.2505.05020.4681.0030.84
ATOM3768CGGLUB542−11.1666.24520.3471.0037.20
ATOM3769CDGLUB542−11.1387.10521.5971.0039.98
ATOM3770OE1GLUB542−12.2237.38522.1441.0039.92
ATOM3771OE2GLUB542−10.0287.49422.0341.0038.96
ATOM3772CGLUB542−8.8264.01018.7241.0027.90
ATOM3773OGLUB542−8.5304.49217.6341.0029.32
ATOM3774NMETB543−7.9453.38819.4991.0026.41
ATOM3775CAMETB543−6.5523.23719.1071.0023.53
ATOM3776CBMETB543−5.7492.59120.2471.0024.60
ATOM3777CGMETB543−5.8123.33821.5791.0026.46
ATOM3778SDMETB543−5.3735.08421.4671.0029.45
ATOM3779CEMETB543−3.5854.97121.3491.0025.43
ATOM3780CMETB543−6.4032.40717.8321.0025.80
ATOM3781OMETB543−5.5352.68617.0041.0023.59
ATOM3782NLEUB544−7.2541.39417.6731.0027.74
ATOM3783CALEUB544−7.2020.52216.4991.0026.32
ATOM3784CBLEUB544−8.069−0.72116.7191.0026.75
ATOM3785CGLEUB544−8.274−1.63215.5021.0028.12
ATOM3786CD1LEUB544−6.956−2.29415.1361.0026.36
ATOM3787CD2LEUB544−9.330−2.68015.8031.0027.00
ATOM3788CLEUB544−7.6721.25215.2501.0026.97
ATOM3789OLEUB544−7.0361.18114.1951.0024.25
ATOM3790NASPB545−8.7871.96115.3721.0030.37
ATOM3791CAASPB545−9.3382.70214.2441.0032.34
ATOM3792CBASPB545−10.6683.34614.6371.0036.61
ATOM3793CGASPB545−11.8182.37014.5651.0042.73
ATOM3794OD1ASPB545−12.8582.62415.2111.0047.39
ATOM3795OD2ASPB545−11.6761.34213.8631.0046.96
ATOM3796CASPB545−8.3823.76213.7111.0031.27
ATOM3797OASPB545−8.4434.12012.5321.0030.53
ATOM3798NALAB546−7.5064.27214.5721.0029.02
ATOM3799CAALAB546−6.5435.28014.1411.0031.21
ATOM3800CBALAB546−5.6465.69315.3061.0030.98
ATOM3801CALAB546−5.6974.73112.9961.0032.14
ATOM3802OALAB546−5.1895.49012.1701.0033.78
ATOM3803NHISB547−5.5553.41012.9431.0032.27
ATOM3804CAHISB547−4.7732.76711.8921.0037.73
ATOM3805CBHISB547−3.9911.57612.4571.0035.83
ATOM3806CGHISB547−2.7961.96813.2691.0034.54
ATOM3807CD2HISB547−2.6982.55314.4861.0030.23
ATOM3808ND1HISB547−1.5021.75512.8401.0034.23
ATOM3809CE1HISB547−0.6592.19313.7601.0036.72
ATOM3810NE2HISB547−1.3602.68114.7681.0031.48
ATOM3811CHISB547−5.6492.28610.7351.0043.69
ATOM3812OHISB547−5.1782.1529.6061.0046.04
ATOM3813NARGB548−6.9192.02011.0191.0048.35
ATOM3814CAARGB548−7.8431.5519.9931.0054.74
ATOM3815CBARGB548−8.5220.26710.4521.0054.66
ATOM3816CARGB548−8.8862.6199.6811.0059.94
ATOM3817OARGB548−8.5803.8129.6721.0062.81
ATOM3818NLEUB549−10.1162.1869.4221.0064.81
ATOM3819CALEUB549−11.2043.1099.1121.0067.59
ATOM3820CBLEUB549−12.4782.3278.7991.0068.06
ATOM3821CLEUB549−11.4494.06910.2751.0069.12
ATOM3822OLEUB549−11.4515.29710.0361.0068.96
ATOM3823OXTLEUB549−11.6343.57911.4121.0070.70
HETATM3824CP9DESB600−4.547−6.07722.0001.0018.55
HETATM3825CP8DESB600−3.163−6.36521.4671.0017.72
HETATM3826CP7DESB600−2.897−7.85321.3811.0021.17
HETATM3827CP6DESB600−3.719−8.55120.3741.0022.05
HETATM3828CP1DESB600−3.405−8.48118.9981.0021.32
HETATM3829CP2DESB600−4.239−9.09518.0631.0021.61
HETATM3830CP3DESB600−5.388−9.77118.5091.0024.89
HETATM3831OP3DESB600−6.244−10.33917.6001.0024.94
HETATM3832CP4DESB600−5.718−9.85819.8601.0024.08
HETATM3833CP5DESB600−4.877−9.24020.7911.0024.67
HETATM3834C7DESB600−1.998−8.46022.1901.0016.67
HETATM3835C6DESB600−1.330−7.83423.3251.0015.39
HETATM3836C5DESB600−2.054−7.64224.5221.0017.62
HETATM3837C4DESB600−1.433−7.07225.6341.0016.16
HETATM3838C3DESB600−0.077−6.68525.5421.0020.04
HETATM3839O3DESB6000.509−6.11326.6551.0015.55
HETATM3840C2DESB6000.669−6.86624.3531.0018.94
HETATM3841C1DESB6000.035−7.44023.2411.0015.20
HETATM3842C8DESB600−1.642−9.90321.9421.0017.61
HETATM3843C9DESB600−0.440−10.00920.9981.0011.63
HETATM3844C1CBMB417−4.997−22.99425.2731.0055.80
HETATM3845O4CBMB417−4.789−24.18725.0031.0055.56
HETATM3846O3CBMB417−4.798−22.55926.5521.0056.04
HETATM3847C2CBMB417−5.468−21.96024.2641.0057.04
HETATM3848C1CBMB530−15.278−5.12410.2431.0087.39
HETATM3849O4CBMB530−15.852−5.0869.0641.0087.68
HETATM3850O3CBMB530−15.832−4.29111.2011.0086.22
HETATM3851C2CBMB530−14.207−5.88610.6281.0087.65
ATOM3852CBHISC6879.818−20.030−2.2111.0063.34
ATOM3853CHISC68710.133−20.267−4.6891.0063.49
ATOM3854OHISC68711.204−20.840−4.4721.0063.87
ATOM3855NHISC6877.944−19.563−3.7581.0065.42
ATOM3856CAHISC6879.424−19.484−3.5861.0064.86
ATOM3857NLYSC6889.533−20.281−5.8751.0062.00
ATOM3858CALYSC68810.101−20.999−7.0091.0060.81
ATOM3859CBLYSC6888.980−21.540−7.9011.0061.76
ATOM3860CLYSC68811.050−20.127−7.8271.0057.47
ATOM3861OLYSC68812.253−20.379−7.8581.0057.64
ATOM3862NILEC68910.511−19.103−8.4821.0055.74
ATOM3863CAILEC68911.326−18.212−9.3061.0053.09
ATOM3864CBILEC68910.496−17.057−9.8891.0053.83
ATOM3865CG2ILEC68911.334−16.286−10.9021.0054.55
ATOM3866CG1ILEC6899.229−17.603−10.5511.0052.90
ATOM3867CD1ILEC6898.406−16.550−11.2581.0050.45
ATOM3868CILEC68912.513−17.611−8.5601.0050.82
ATOM3869OILEC68913.616−17.550−9.0971.0051.28
ATOM3870NLEUC69012.288−17.162−7.3291.0048.01
ATOM3871CALEUC69013.362−16.570−6.5341.0047.33
ATOM3872CBLEUC69012.812−16.058−5.1991.0042.51
ATOM3873CGLEUC69013.835−15.501−4.2061.0040.67
ATOM3874CD1LEUC69014.575−14.324−4.8311.0039.95
ATOM3875CD2LEUC69013.128−15.078−2.9261.0038.77
ATOM3876CLEUC69014.445−17.615−6.2821.0048.87
ATOM3877OLEUC69015.643−17.340−6.3931.0046.71
ATOM3878NHISC69114.001−18.818−5.9391.0051.36
ATOM3879CAHISC69114.886−19.946−5.6751.0053.35
ATOM3880CBHISC69114.042−21.203−5.4601.0058.64
ATOM3881CGHISC69114.655−22.195−4.5261.0062.94
ATOM3882CD2HISC69115.503−23.227−4.7511.0064.95
ATOM3883ND1HISC69114.392−22.202−3.1731.0065.49
ATOM3884CE1HISC69115.053−23.195−2.6051.0068.18
ATOM3885NE2HISC69115.733−23.833−3.5401.0068.77
ATOM3886CHISC69115.824−20.162−6.8611.0052.19
ATOM3887OHISC69117.048−20.153−6.7171.0047.53
ATOM3888NARGC69215.222−20.350−8.0321.0052.37
ATOM3889CAARGC69215.949−20.586−9.2711.0052.90
ATOM3890CBARGC69214.955−20.832−10.4101.0054.04
ATOM3891CGARGC69215.575−20.826−11.7971.0057.52
ATOM3892CDARGC69214.528−21.048−12.8741.0058.25
ATOM3893NEARGC69214.375−19.878−13.7321.0061.43
ATOM3894CZARGC69213.218−19.260−13.9511.0064.32
ATOM3895NH1ARGC69212.108−19.706−13.3781.0063.22
ATOM3896NH2ARGC69213.171−18.197−14.7461.0065.93
ATOM3897CARGC69216.873−19.434−9.6391.0053.09
ATOM3898OARGC69218.047−19.644−9.9561.0053.06
ATOM3899NLEUC69316.338−18.217−9.6071.0050.73
ATOM3900CALEUC69317.125−17.039−9.9451.0049.53
ATOM3901CBLEUC69316.249−15.784−9.8811.0049.56
ATOM3902CGLEUC69315.781−15.245−11.2391.0049.78
ATOM3903CD1LEUC69315.219−16.389−12.0791.0050.30
ATOM3904CD2LEUC69314.728−14.170−11.0371.0048.79
ATOM3905CLEUC69318.318−16.904−9.0061.0048.38
ATOM3906OLEUC69319.382−16.426−9.4021.0046.35
ATOM3907NLEUC69418.135−17.329−7.7611.0046.74
ATOM3908CALEUC69419.204−17.272−6.7751.0049.41
ATOM3909CBLEUC69418.634−17.415−5.3621.0045.20
ATOM3910CGLEUC69418.222−16.128−4.6431.0040.19
ATOM3911CD1LEUC69417.456−16.474−3.3711.0041.65
ATOM3912CD2LEUC69419.453−15.307−4.3171.0035.91
ATOM3913CLEUC69420.172−18.417−7.0581.0054.15
ATOM3914OLEUC69421.370−18.320−6.7761.0053.55
ATOM3915NGLNC69519.634−19.498−7.6191.0057.44
ATOM3916CAGLNC69520.416−20.685−7.9591.0062.46
ATOM3917CBGLNC69519.477−21.853−8.3041.0061.95
ATOM3918CGGLNC69519.548−23.010−7.3111.0061.49
ATOM3919CDGLNC69518.454−24.053−7.4901.0062.78
ATOM3920OE1GLNC69518.262−24.928−6.6531.0063.33
ATOM3921NE2GLNC69517.720−23.969−8.6081.0060.37
ATOM3922CGLNC69521.330−20.414−9.1491.0065.13
ATOM3923OGLNC69522.517−20.740−9.1161.0065.87
ATOM3924NASPC69620.761−19.824−10.1971.0067.67
ATOM3925CAASPC69621.492−19.500−11.4201.0070.66
ATOM3926CBASPC69620.801−18.348−12.1511.0071.06
ATOM3927CGASPC69620.127−18.792−13.4301.0071.70
ATOM3928OD1ASPC69620.637−18.455−14.5211.0072.47
ATOM3929OD2ASPC69619.086−19.478−13.3421.0071.41
ATOM3930CASPC69622.951−19.132−11.1691.0072.41
ATOM3931OASPC69623.245−18.115−10.5411.0072.56
ATOM3932NSERC69723.859−19.967−11.6681.0074.67
ATOM3933CASERC69725.291−19.741−11.5071.0076.45
ATOM3934CBSERC69726.019−21.076−11.3771.0076.00
ATOM3935CSERC69725.841−18.960−12.6961.0078.44
ATOM3936OSERC69726.286−17.809−12.4891.0079.20
ATOM3937OXTSERC69725.818−19.510−13.8201.0080.07
ATOM3938CBLYSD686−14.07013.66116.8431.0050.28
ATOM3939CLYSD686−13.68214.41819.1991.0051.59
ATOM3940OLYSD686−12.62914.73819.7591.0050.42
ATOM3941NLYSD686−12.91015.79617.2831.0050.43
ATOM3942CALYSD686−13.97614.87217.7691.0050.62
ATOM3943NHISD687−14.61713.67619.7871.0049.91
ATOM3944CAHISD687−14.44713.17621.1441.0051.28
ATOM3945CBHISD687−15.80612.98421.8281.0054.12
ATOM3946CGHISD687−15.71312.33623.1771.0060.06
ATOM3947CD2HISD687−15.41811.06423.5391.0061.05
ATOM3948ND1HISD687−15.91113.03024.3521.0062.39
ATOM3949CE1HISD687−15.74112.21525.3781.0062.76
ATOM3950NE2HISD687−15.44111.01624.9121.0063.46
ATOM3951CHISD687−13.69111.84921.1631.0049.55
ATOM3952OHISD687−14.09910.87820.5241.0050.84
ATOM3953NLYSD688−12.59311.81621.9091.0044.00
ATOM3954CALYSD688−11.78410.61122.0381.0040.31
ATOM3955CBLYSD688−10.44610.77321.2991.0041.42
ATOM3956CGLYSD688−10.51310.59519.7801.0042.76
ATOM3957CDLYSD688−9.12310.71619.1521.0038.66
ATOM3958CELYSD688−9.16210.52917.6401.0038.28
ATOM3959NZLYSD688−7.89410.97016.9861.0031.58
ATOM3960CLYSD688−11.50610.37823.5171.0036.70
ATOM3961OLYSD688−11.27111.32624.2661.0033.38
ATOM3962NILED689−11.5499.12223.9421.0033.06
ATOM3963CAILED689−11.2558.80625.3281.0028.70
ATOM3964CBILED689−11.4387.30125.6071.0030.88
ATOM3965CG2ILED689−10.7256.91226.8991.0031.45
ATOM3966CG1ILED689−12.9276.97125.7211.0032.57
ATOM3967CD1ILED689−13.3085.67925.0311.0029.79
ATOM3968CILED689−9.7909.19325.5411.0027.64
ATOM3969OILED689−9.4059.64926.6111.0025.54
ATOM3970NLEUD690−8.9859.02124.4961.0024.25
ATOM3971CALEUD690−7.5639.34824.5491.0026.63
ATOM3972CBLEUD690−6.9039.02123.2001.0022.83
ATOM3973CGLEUD690−5.4339.38722.9921.0025.47
ATOM3974CD1LEUD690−4.5958.77224.1081.0024.03
ATOM3975CD2LEUD690−4.9568.89821.6161.0020.87
ATOM3976CLEUD690−7.34410.82324.9021.0026.64
ATOM3977OLEUD690−6.40811.16525.6251.0028.34
ATOM3978NHISD691−8.20611.69424.3831.0027.77
ATOM3979CAHISD691−8.10713.12524.6651.0029.16
ATOM3980CBHISD691−9.15613.90723.8611.0030.89
ATOM3981CGHISD691−8.90313.93522.3861.0037.09
ATOM3982CD2HISD691−7.75014.00021.6791.0041.39
ATOM3983ND1HISD691−9.92013.90621.4581.0041.65
ATOM3984CE1HISD691−9.40713.95320.2421.0044.64
ATOM3985NE2HISD691−8.09114.01020.3471.0041.94
ATOM3986CHISD691−8.33813.37326.1591.0026.65
ATOM3987OHISD691−7.60214.12026.8021.0024.50
ATOM3988NARGD692−9.37112.74226.7031.0025.70
ATOM3989CAARGD692−9.69112.91228.1141.0029.11
ATOM3990CBARGD692−10.95912.13428.4721.0030.84
ATOM3991CGARGD692−11.25512.12929.9631.0041.63
ATOM3992CDARGD692−12.50211.32730.2901.0048.83
ATOM3993NEARGD692−13.61812.19830.6471.0054.50
ATOM3994CZARGD692−14.49812.67729.7741.0059.37
ATOM3995NH1ARGD692−14.39212.37128.4861.0060.97
ATOM3996NH2ARGD692−15.48313.46430.1881.0059.07
ATOM3997CARGD692−8.54812.45129.0111.0028.30
ATOM3998OARGD692−8.13913.16729.9291.0026.50
ATOM3999NLEUD693−8.03011.25928.7371.0024.87
ATOM4000CALEUD693−6.94310.70529.5361.0027.17
ATOM4001CBLEUD693−6.6749.25429.1161.0028.45
ATOM4002CGLEUD693−7.8448.30029.3911.0030.40
ATOM4003CD1LEUD693−7.5756.93228.7781.0034.79
ATOM4004CD2LEUD693−8.0438.17130.8941.0032.02
ATOM4005CLEUD693−5.67011.53929.4401.0025.96
ATOM4006OLEUD693−4.94811.70030.4281.0027.01
ATOM4007NLEUD694−5.39512.08028.2571.0025.33
ATOM4008CALEUD694−4.20712.90628.0621.0027.22
ATOM4009CBLEUD694−3.94813.12626.5721.0024.61
ATOM4010CGLEUD694−3.11812.08025.8251.0022.20
ATOM4011CD1LEUD694−3.23012.33224.3241.0021.13
ATOM4012CD2LEUD694−1.66612.14826.2751.0021.34
ATOM4013CLEUD694−4.33614.27028.7421.0032.40
ATOM4014OLEUD694−3.33914.88929.1021.0031.55
ATOM4015NGLND695−5.57014.73328.9151.0036.93
ATOM4016CAGLND695−5.82016.03229.5281.0043.18
ATOM4017CBGLND695−7.02216.69428.8621.0040.48
ATOM4018CGGLND695−6.77217.07127.4221.0037.99
ATOM4019CDGLND695−7.94317.76426.7951.0035.86
ATOM4020OE1GLND695−7.86318.89526.3421.0038.84
ATOM4021NE2GLND695−9.08217.06026.7571.0031.62
ATOM4022CGLND695−6.04916.00931.0341.0048.74
ATOM4023OGLND695−6.11917.06531.6601.0051.25
ATOM4024NASPD696−6.17514.81831.6111.0054.01
ATOM4025CAASPD696−6.39814.70233.0471.0062.23
ATOM4026CBASPD696−6.21713.23833.4851.0063.97
ATOM4027CGASPD696−7.52712.46733.4751.0067.72
ATOM4028OD1ASPD696−8.52812.99632.9411.0068.11
ATOM4029OD2ASPD696−7.55211.33334.0031.0068.95
ATOM4030CASPD696−5.45615.62233.8401.0065.60
ATOM4031OASPD696−4.31215.18934.1341.0068.33
ATOM4032OXTASPD696−5.87416.75534.1401.0069.20
HETATM4033OHOH116.153−0.605−4.4251.0017.11
HETATM4034OHOH216.570−5.304−16.5601.0021.44
HETATM4035OHOH318.5260.742−4.4951.0023.43
HETATM4036OHOH413.647−2.1878.5881.0025.82
HETATM4037OHOH59.778−5.8252.5091.0020.58
HETATM4038OHOH617.072−3.605−8.0151.0018.38
HETATM4039OHOH724.920−1.689−2.7801.0025.74
HETATM4040OHOH87.321−5.6495.0611.0024.11
HETATM4041OHOH925.976−3.53515.1581.0026.78
HETATM4042OHOH1015.088−7.006−15.1921.0019.64
HETATM4043OHOH1114.0700.925−5.9531.0020.55
HETATM4044OHOH1218.0083.407−6.6541.0032.30
HETATM4045OHOH1331.949−8.39313.4871.0030.64
HETATM4046OHOH1419.625−2.804−4.2791.0024.45
HETATM4047OHOH1511.7411.079−21.1401.0025.87
HETATM4048OHOH1625.06713.95114.1531.0031.07
HETATM4049OHOH1715.5011.323−10.3931.0021.01
HETATM4050OHOH1813.8803.349−11.4821.0024.28
HETATM4051OHOH1917.5910.979−8.8281.0035.26
HETATM4052OHOH2023.682−2.041−0.3141.0037.90
HETATM4053OHOH2115.7549.49611.8411.0039.44
HETATM4054OHOH22−4.9437.574−3.0661.0037.67
HETATM4055OHOH236.8770.354−15.9821.0036.92
HETATM4056OHOH2415.806−4.0028.6711.0030.38
HETATM4057OHOH2517.185−3.158−5.3211.0028.89
HETATM4058OHOH2617.5729.24917.0091.0030.15
HETATM4059OHOH2724.096−2.92911.6041.0031.37
HETATM4060OHOH2822.324−5.871−11.9801.0032.74
HETATM4061OHOH2927.547−12.361−0.8011.0036.61
HETATM4062OHOH3011.17313.442−2.7191.0035.41
HETATM4063OHOH3115.438−9.5275.4831.0029.88
HETATM4064OHOH329.946−6.5645.9831.0035.05
HETATM4065OHOH337.59911.680−15.2611.0038.68
HETATM4066OHOH3420.11210.503−5.1091.0042.66
HETATM4067OHOH3515.97210.34314.8971.0041.73
HETATM4068OHOH3622.401−5.914−9.5271.0028.08
HETATM4069OHOH3716.128−0.899−8.1091.0033.13
HETATM4070OHOH383.58115.655−3.7061.0041.37
HETATM4071OHOH3931.90013.54521.3391.0037.79
HETATM4072OHOH4020.058−7.53014.1191.0047.51
HETATM4073OHOH4134.6346.66815.6321.0029.24
HETATM4074OHOH4217.96810.511−9.0851.0044.60
HETATM4075OHOH4323.258−17.325−4.0881.0044.10
HETATM4076OHOH444.034−1.47227.5211.0015.22
HETATM4077OHOH45−5.943−0.01836.0881.0021.11
HETATM4078OHOH466.084−1.50929.4781.0019.51
HETATM4079OHOH479.7621.06115.6211.0027.74
HETATM4080OHOH481.8040.71717.2601.0020.97
HETATM4081OHOH490.9290.42130.2811.0019.64
HETATM4082OHOH509.6274.27131.2311.0019.02
HETATM4083OHOH512.121−0.26113.6541.0026.09
HETATM4084OHOH5220.06010.27517.7111.0025.49
HETATM4085OHOH53−6.7860.73633.4831.0022.34
HETATM4086OHOH542.751−4.13627.7601.0019.93
HETATM4087OHOH555.994−4.07931.2921.0032.27
HETATM4088OHOH5619.41616.92121.6451.0025.54
HETATM4089OHOH574.8332.32529.0061.0019.00
HETATM4090OHOH58−7.638−8.93137.8091.0024.79
HETATM4091OHOH5928.442−4.67321.8751.0024.32
HETATM4092OHOH601.094−4.89332.1001.0024.27
HETATM4093OHOH610.905−7.30632.7831.0021.33
HETATM4094OHOH623.396−2.97132.3061.0026.13
HETATM4095OHOH6310.3634.57628.3911.0033.43
HETATM4096OHOH6419.551−6.47316.5971.0035.38
HETATM4097OHOH65−2.888−19.62715.6651.0027.99
HETATM4098OHOH66−7.275−9.74531.0771.0027.00
HETATM4099OHOH6710.1893.58016.5101.0024.19
HETATM4100OHOH682.7410.71628.3821.0016.48
HETATM4101OHOH6923.522−4.32313.9431.0027.48
HETATM4102OHOH7017.1338.13319.6861.0032.24
HETATM4103OHOH71−0.2954.53535.8841.0033.42
HETATM4104OHOH729.51910.82834.8421.0029.38
HETATM4105OHOH736.29114.87829.0701.0028.21
HETATM4106OHOH74−1.7216.48013.3811.0049.91
HETATM4107OHOH7510.091−15.42726.1941.0024.17
HETATM4108OHOH765.0297.46117.7181.0018.91
HETATM4109OHOH773.7582.08614.3061.0028.28
HETATM4110OHOH78−1.390−18.73933.1831.0041.11
HETATM4111OHOH7912.703−8.68732.1191.0036.21
HETATM4112OHOH8022.270−6.45114.8441.0033.21
HETATM4113OHOH811.4584.60534.0261.0023.59
HETATM4114OHOH821.759−2.15830.3741.0028.78
HETATM4115OHOH836.153−21.37223.1881.0031.14
HETATM4116OHOH8436.5250.46320.7921.0045.26
HETATM4117OHOH8513.8329.69613.7921.0033.12
HETATM4118OHOH8631.1666.63524.9241.0035.19
HETATM4119OHOH878.844−10.38934.1801.0048.80
HETATM4120OHOH889.581−6.95634.1361.0042.95
HETATM4121OHOH89−1.56315.88727.5961.0039.35
HETATM4122OHOH90−5.28610.34532.7571.0035.20
HETATM4123OHOH9115.0350.60713.3391.0029.53
HETATM4124OHOH92−10.984−1.50030.2721.0029.84
HETATM4125OHOH93−7.239−0.271−1.2071.0048.98
HETATM4126OHOH9418.022−4.90234.2861.0035.28
HETATM4127OHOH9529.347−6.31919.9201.0037.20
HETATM4128OHOH96−14.309−19.36920.9451.0030.23
HETATM4129OHOH9731.4964.61418.7161.0038.79
HETATM4130OHOH9826.5679.75925.6291.0029.72
HETATM4131OHOH992.84814.5311.1341.0038.08
HETATM4132OHOH100−9.3735.699−7.9531.0053.23
HETATM4133OHOH101−10.137−0.553−6.7421.0047.72
HETATM4134OHOH10210.558−10.36315.4031.0040.97
HETATM4135OHOH10321.07917.16618.9291.0032.40
HETATM4136OHOH10425.810−5.92122.5061.0037.69
HETATM4137OHOH10522.493−1.31134.4651.0049.94
HETATM4138OHOH10619.31710.97738.7031.0040.60
HETATM4139OHOH1074.47913.9513.0451.0045.33
HETATM4140OHOH10820.41819.35334.0441.0042.18
HETATM4141OHOH109−3.0658.93614.0621.0038.41
HETATM4142OHOH11026.856−4.674−10.9401.0055.67
HETATM4143OHOH1112.032−6.3875.6141.0042.23
HETATM4144OHOH1120.6010.228−17.2681.0040.57
HETATM4145OHOH1134.90313.488−14.0501.0047.72
HETATM4146OHOH1143.98616.140−0.9601.0040.66
HETATM4147OHOH11512.968−19.5612.7411.0040.76
HETATM4148OHOH1167.17015.5832.5991.0043.69
HETATM4149OHOH117−1.96610.6063.5721.0052.63
HETATM4150OHOH11829.03010.6446.7071.0042.54
HETATM4151OHOH1190.4684.3548.3741.0038.69
HETATM4152OHOH12029.08617.11919.2721.0045.51
HETATM4153OHOH12124.61417.60920.1741.0053.55
HETATM4154OHOH122−15.3180.36226.6861.0036.77
HETATM4155OHOH123−3.857−24.78628.3251.0039.64
HETATM4156OHOH12421.72822.17831.9831.0043.73
HETATM4157OHOH12531.650−7.37021.6421.0040.53
HETATM4158OHOH12625.42110.43621.1611.0032.31
HETATM4159OHOH12710.317−9.45712.9981.0037.77
HETATM4160OHOH12822.72314.88715.4271.0047.90
HETATM4161OHOH1296.7029.55637.5961.0047.81
HETATM4162OHOH13027.98713.5577.1671.0041.15
HETATM4163OHOH13130.79816.4997.5881.0058.47
HETATM4164OHOH13210.071−0.571−20.3931.0038.79
HETATM4165OHOH1339.5628.334−21.3921.0036.80
HETATM4166OHOH1346.7126.0588.8221.0037.43
HETATM4167OHOH1355.9278.45410.5941.0042.34
HETATM4168OHOH1364.4726.30610.9731.0037.35
HETATM4169OHOH1376.7927.7217.0511.0047.23
HETATM4170OHOH13824.51311.58233.7241.0045.55
HETATM4171OHOH139−2.528−20.36112.3541.0052.13
HETATM4172OHOH140−7.8647.70619.2481.0047.82
HETATM4173OHOH14111.577−16.96224.3981.0039.43
HETATM4174OHOH14218.08712.263−5.5071.0033.36
HETATM4175OHOH143−6.816−14.19010.6741.0051.32
HETATM4176OHOH144−7.377−16.70133.5281.0057.11
HETATM4177OHOH145−5.379−20.10732.6891.0043.01
HETATM4178OHOH1468.766−7.947−16.2741.0049.96
HETATM4179OHOH14710.946−7.937−18.1421.0055.67
END

<
APPENDIX 3
Atomic Coordinates for Human ERα Complexed With OHT
CRYST1 58.242 58.242 277.467 90.00 90.00 120.00 P 65 2 2 12
ORIGX1  1.000000  0.000000  0.000000  0.00000
ORIGX2  0.000000  1.000000  0.000000  0.00000
ORIGX3  0.000000  0.000000  1.000000  0.00000
SCALE1  0.017170  0.009913  0.000000  0.00000
SCALE2  0.000000  0.019826  0.000000  0.00000
SCALE3  0.000000  0.000000  0.003604  0.00000
ATOM1CBLEU3066.63811.5023.9891.0061.20
ATOM2CLEU3067.38110.6846.2311.0061.47
ATOM3OLEU3066.40711.0206.9051.0062.09
ATOM4NLEU3066.3699.1284.5881.0062.32
ATOM5CALEU3067.23210.3304.7541.0061.30
ATOM6NALA3078.60910.6056.7301.0060.52
ATOM7CAALA3078.89110.9128.1251.0058.77
ATOM8CBALA30710.31810.5018.4651.0059.70
ATOM9CALA3078.69212.3938.4291.0057.51
ATOM10OALA3078.45112.7709.5741.0057.64
ATOM11NLEU3088.78913.2287.4001.0055.82
ATOM12CALEU3088.63814.6687.5731.0056.62
ATOM13CBLEU3089.29815.4026.4061.0057.48
ATOM14CGLEU30810.63714.8225.9481.0059.17
ATOM15CD1LEU30810.47414.1894.5691.0060.38
ATOM16CD2LEU30811.69415.9205.9331.0058.46
ATOM17CLEU3087.19015.1307.7101.0056.51
ATOM18OLEU3086.93516.3077.9611.0055.58
ATOM19NSER3096.24614.2087.5461.0057.04
ATOM20CASER3094.82814.5447.6571.0056.46
ATOM21CBSER3094.03413.8966.5141.0056.79
ATOM22OGSER3094.07112.4796.5881.0057.23
ATOM23CSER3094.26114.0959.0031.0056.13
ATOM24OSER3093.16614.5079.3981.0055.17
ATOM25NLEU3105.01613.2579.7061.0054.31
ATOM26CALEU3104.59112.74911.0041.0053.55
ATOM27CBLEU3105.65111.81111.5821.0054.40
ATOM28CGLEU3105.58610.33311.1891.0056.49
ATOM29CD1LEU3105.53010.2009.6761.0057.06
ATOM30CD2LEU3106.8099.61011.7391.0057.28
ATOM31CLEU3104.33013.86512.0031.0053.18
ATOM32OLEU3104.99314.90511.9841.0053.17
ATOM33NTHR3113.35213.64112.8741.0051.71
ATOM34CATHR3113.01714.60413.9121.0049.93
ATOM35CBTHR3111.52714.55414.2751.0048.96
ATOM36OG1THR3111.24213.31114.9301.0047.20
ATOM37CG2THR3110.66614.68813.0271.0050.99
ATOM38CTHR3113.81514.20115.1451.0048.84
ATOM39OTHR3114.37113.10315.1971.0046.66
ATOM40NALA3123.85715.07816.1411.0048.76
ATOM41CAALA3124.59014.79817.3691.0047.75
ATOM42CBALA3124.35915.91018.3781.0047.06
ATOM43CALA3124.17113.46017.9641.0047.41
ATOM44OALA3125.00912.60918.2621.0045.52
ATOM45NASP3132.86813.27518.1431.0047.58
ATOM46CAASP3132.36712.03218.7141.0047.63
ATOM47CBASP3130.84812.10018.8791.0051.96
ATOM48CGASP3130.43012.87220.1181.0056.21
ATOM49OD1ASP3131.31413.23420.9291.0056.38
ATOM50OD2ASP313−0.78513.11720.2821.0059.15
ATOM51CASP3132.74510.84617.8351.0043.93
ATOM52OASP3132.9599.74118.3301.0044.77
ATOM53NGLN3142.82611.08116.5311.0044.52
ATOM54CAGLN3143.18210.02815.5881.0044.73
ATOM55CBGLN3142.84910.46414.1561.0045.05
ATOM56CGGLN3141.5349.88613.6261.0048.47
ATOM57CDGLN3140.98210.64612.4281.0050.37
ATOM58OE1GLN3141.64911.51511.8561.0049.38
ATOM59NE2GLN314−0.24810.31812.0431.0051.74
ATOM60CGLN3144.6739.72215.7071.0043.26
ATOM61OGLN3145.1008.58015.5551.0043.93
ATOM62NMET3155.45910.75715.9801.0042.29
ATOM63CAMET3156.90110.60616.1301.0041.26
ATOM64CBMET3157.56511.98516.2241.0042.43
ATOM65CGMET3159.08211.93916.3561.0042.34
ATOM66SDMET3159.90611.19014.9251.0046.22
ATOM67CEMET3159.54712.40813.6801.0037.32
ATOM68CMET3157.2189.79117.3791.0038.89
ATOM69OMET3158.0028.84117.3351.0040.02
ATOM70NVAL3166.59910.16518.4911.0037.65
ATOM71CAVAL3166.8199.47619.7561.0039.56
ATOM72CBVAL3166.02310.13620.8971.0039.22
ATOM73CG1VAL3166.2459.37322.1921.0044.43
ATOM74CG2VAL3166.44611.58321.0591.0041.04
ATOM75CVAL3166.4048.01219.6641.0040.04
ATOM76OVAL3167.1417.11720.0771.0037.86
ATOM77NSER3175.2157.76719.1271.0041.90
ATOM78CASER3174.7336.40018.9971.0041.68
ATOM79CBSER3173.3116.40218.4151.0043.85
ATOM80OGSER3173.2255.63117.2301.0049.38
ATOM81CSER3175.6965.60118.1141.0039.72
ATOM82OSER3176.0114.44618.4071.0040.21
ATOM83NALA3186.1826.22017.0431.0038.35
ATOM84CAALA3187.1145.54016.1531.0036.96
ATOM85CBALA3187.4856.44814.9861.0037.92
ATOM86CALA3188.3755.13716.9201.0038.31
ATOM87OALA3188.8203.99216.8441.0033.94
ATOM88NLEU3198.9386.08917.6641.0036.92
ATOM89CALEU31910.1615.85418.4381.0038.56
ATOM90CBLEU31910.6607.17419.0401.0040.86
ATOM91CGLEU31911.1368.26418.0711.0041.25
ATOM92CD1LEU31911.7149.44018.8571.0044.30
ATOM93CD2LEU31912.1827.69317.1401.0042.61
ATOM94CLEU3199.9654.82619.5491.0038.33
ATOM95OLEU31910.7793.91619.7291.0033.91
ATOM96NLEU3208.8794.98220.2971.0037.39
ATOM97CALEU3208.5674.06721.3871.0041.55
ATOM98CBLEU3207.2394.46722.0491.0038.47
ATOM99CGLEU3207.2365.58223.0991.0044.81
ATOM100CD1LEU3205.8765.63423.8021.0044.96
ATOM101CD2LEU3208.3345.33224.1121.0043.36
ATOM102CLEU3208.4662.64220.8431.0041.11
ATOM103OLEU3208.9711.69721.4431.0041.87
ATOM104NASP3217.8122.50419.6961.0043.94
ATOM105CAASP3217.6131.21019.0531.0044.77
ATOM106CBASP3216.6691.37217.8601.0048.39
ATOM107CGASP3215.2061.31818.2551.0052.39
ATOM108OD1ASP3214.9011.42219.4641.0053.56
ATOM109OD2ASP3214.3571.17217.3461.0055.81
ATOM110CASP3218.9110.56518.5681.0044.37
ATOM111OASP3219.030−0.66118.5331.0044.67
ATOM112NALA3229.8781.39518.1931.0040.75
ATOM113CAALA32211.1530.90517.6861.0037.81
ATOM114CBALA32211.7721.95416.7761.0038.07
ATOM115CALA32212.1480.51318.7691.0035.52
ATOM116OALA32213.219−0.02018.4731.0036.11
ATOM117NGLU32311.7990.76820.0221.0035.61
ATOM118CAGLU32312.7040.46021.1171.0036.39
ATOM119CBGLU32312.0420.76822.4591.0035.09
ATOM120CGGLU32312.2092.21022.8991.0037.93
ATOM121CDGLU32313.6572.56923.2001.0037.29
ATOM122OE1GLU32314.3133.17322.3261.0034.21
ATOM123OE2GLU32314.1342.24524.3091.0038.02
ATOM124CGLU32313.205−0.97821.1101.0038.01
ATOM125OGLU32312.425−1.93120.9991.0038.37
ATOM126NPRO32414.527−1.15121.2251.0036.03
ATOM127CDPRO32415.522−0.06921.3451.0036.69
ATOM128CAPRO32415.158−2.47421.2401.0036.42
ATOM129CBPRO32416.633−2.16621.0031.0035.75
ATOM130CGPRO32416.811−0.80721.6101.0035.46
ATOM131CPRO32414.940−3.16222.5831.0035.75
ATOM132OPRO32414.616−2.51723.5801.0034.97
ATOM133NPRO32515.134−4.48522.6311.0035.24
ATOM134CDPRO32515.530−5.38621.5341.0037.02
ATOM135CAPRO32514.942−5.20823.8891.0034.65
ATOM136CBPRO32514.753−6.65223.4391.0035.83
ATOM137CGPRO32515.589−6.74322.2001.0034.88
ATOM138CPRO32516.132−5.07024.8241.0034.51
ATOM139OPRO32517.237−4.72324.3991.0029.92
ATOM140NILE32615.899−5.32226.1061.0033.62
ATOM141CAILE32616.975−5.26527.0751.0035.02
ATOM142CBILE32616.458−4.89128.4731.0038.11
ATOM143CG2ILE32617.557−5.11029.5041.0038.70
ATOM144CG1ILE32615.987−3.43128.4661.0040.48
ATOM145CD1ILE32616.035−2.74729.8151.0042.96
ATOM146CILE32617.567−6.66827.1031.0034.14
ATOM147OILE32616.875−7.63427.4271.0034.88
ATOM148NLEU32718.840−6.78426.7451.0029.64
ATOM149CALEU32719.493−8.08326.7161.0029.54
ATOM150CBLEU32720.528−8.13525.5871.0027.76
ATOM151CGLEU32719.978−7.80024.1961.0029.02
ATOM152CD1LEU32721.068−7.99323.1391.0028.76
ATOM153CD2LEU32718.775−8.68823.8911.0031.26
ATOM154CLEU32720.156−8.43828.0301.0031.21
ATOM155OLEU32720.393−7.57828.8911.0030.12
ATOM156NTYR32820.445−9.72528.1811.0030.99
ATOM157CATYR32821.087−10.22929.3811.0030.95
ATOM158CBTYR32820.409−11.52029.8421.0033.38
ATOM159CGTYR32819.194−11.27230.6861.0033.05
ATOM160CD1TYR32819.253−11.39832.0711.0031.92
ATOM161CE1TYR32818.152−11.11432.8641.0036.01
ATOM162CD2TYR32817.996−10.86230.1101.0036.05
ATOM163CE2TYR32816.880−10.57430.8991.0037.27
ATOM164CZTYR32816.973−10.70232.2741.0037.66
ATOM165OHTYR32815.896−10.39733.0711.0044.66
ATOM166CTYR32822.529−10.52029.0671.0033.66
ATOM167OTYR32822.884−10.74427.9101.0034.78
ATOM168NSER32923.359−10.49630.1031.0033.97
ATOM169CASER32924.767−10.80029.9621.0037.29
ATOM170CBSER32925.526−10.34231.2041.0036.51
ATOM171OGSER32926.787−10.96531.2821.0037.13
ATOM172CSER32924.835−12.31729.8321.0040.43
ATOM173OSER32923.980−13.02830.3631.0040.11
ATOM174NGLU33025.845−12.81129.1281.0041.40
ATOM175CAGLU33025.992−14.24228.9281.0047.43
ATOM176CBGLU33026.423−14.52427.4841.0048.64
ATOM177CGGLU33025.278−14.87026.5421.0050.20
ATOM178CDGLU33025.765−15.40525.1981.0053.25
ATOM179OE1GLU33025.909−16.64025.0621.0053.27
ATOM180OE2GLU33026.004−14.59024.2801.0051.80
ATOM181CGLU33026.999−14.85229.8931.0049.67
ATOM182OGLU33028.207−14.74129.6961.0050.11
ATOM183NTYR33126.498−15.49330.9421.0053.62
ATOM184CATYR33127.373−16.13031.9211.0058.16
ATOM185CBTYR33128.092−15.07832.7741.0059.55
ATOM186CGTYR33127.239−14.46033.8601.0063.08
ATOM187CD1TYR33126.656−13.20533.6821.0064.50
ATOM188CE1TYR33125.864−12.63034.6761.0065.99
ATOM189CD2TYR33127.010−15.12835.0651.0063.52
ATOM190CE2TYR33126.219−14.56336.0661.0065.60
ATOM191CZTYR33125.648−13.31435.8641.0067.20
ATOM192OHTYR33124.855−12.75336.8391.0067.40
ATOM193CTYR33126.603−17.08032.8231.0059.05
ATOM194OTYR33125.393−16.94233.0021.0059.22
ATOM195NASP33227.320−18.04533.3871.0061.62
ATOM196CAASP33226.719−19.02634.2811.0064.20
ATOM197CBASP33227.681−20.19434.5001.0065.99
ATOM198CGASP33226.961−21.51634.6481.0068.11
ATOM199OD1ASP33227.575−22.56434.3511.0069.54
ATOM200OD2ASP33225.781−21.50535.0601.0067.40
ATOM201CASP33226.393−18.37135.6191.0063.33
ATOM202OASP33227.292−18.07336.4061.0063.90
ATOM203NPRO33325.096−18.14835.8961.0063.64
ATOM204CDPRO33323.945−18.50935.0531.0064.35
ATOM205CAPRO33324.677−17.52137.1541.0063.52
ATOM206CBPRO33323.165−17.33336.9931.0063.53
ATOM207CGPRO33322.866−17.61135.5561.0064.15
ATOM208CPRO33325.010−18.41938.3321.0063.29
ATOM209OPRO33325.129−17.96439.4681.0063.28
ATOM210NTHR33425.160−19.70438.0371.0064.26
ATOM211CATHR33425.475−20.69739.0501.0066.09
ATOM212CBTHR33424.929−22.08038.6451.0066.90
ATOM213OG1THR33425.571−22.51337.4391.0068.06
ATOM214CG2THR33423.423−22.01238.4111.0067.57
ATOM215CTHR33426.982−20.80439.2691.0065.67
ATOM216OTHR33427.432−21.32340.2891.0064.77
ATOM217NARG33527.759−20.30838.3131.0065.65
ATOM218CAARG33529.214−20.36038.4211.0066.60
ATOM219CBARG33529.835−20.50037.0301.0066.74
ATOM220CARG33529.757−19.11339.1231.0067.09
ATOM221OARG33529.100−18.07139.1481.0067.31
ATOM222NPRO33630.968−19.20739.7021.0067.62
ATOM223CDPRO33631.820−20.40839.7131.0067.30
ATOM224CAPRO33631.601−18.08640.4101.0067.42
ATOM225CBPRO33632.982−18.62140.7831.0066.43
ATOM226CGPRO33632.829−20.09740.7791.0067.52
ATOM227CPRO33631.701−16.82839.5611.0068.26
ATOM228OPRO33631.996−16.89538.3711.0069.04
ATOM229NPHE33731.460−15.68140.1831.0069.49
ATOM230CAPHE33731.529−14.40839.4801.0071.39
ATOM231CBPHE33730.818−13.32340.2941.0072.31
ATOM232CGPHE33731.219−11.92439.9211.0073.21
ATOM233CD1PHE33730.632−11.28738.8331.0072.82
ATOM234CD2PHE33732.191−11.24540.6531.0073.43
ATOM235CE1PHE33731.006−9.99338.4791.0073.28
ATOM236CE2PHE33732.573−9.95040.3061.0073.00
ATOM237CZPHE33731.980−9.32339.2171.0072.90
ATOM238CPHE33732.985−14.01339.2451.0071.38
ATOM239OPHE33733.336−13.48738.1891.0071.56
ATOM240NSER33833.825−14.27340.2411.0071.53
ATOM241CASER33835.248−13.94740.1721.0070.98
ATOM242CBSER33835.957−14.48741.4141.0070.43
ATOM243OGSER33835.547−15.81841.6791.0069.59
ATOM244CSER33835.931−14.50438.9241.0071.20
ATOM245OSER33836.951−13.97238.4751.0071.35
ATOM246NGLU33935.368−15.57338.3691.0070.20
ATOM247CAGLU33935.930−16.21537.1831.0069.48
ATOM248CBGLU33935.279−17.58536.9711.0071.07
ATOM249CGGLU33935.996−18.74037.6561.0072.60
ATOM250CDGLU33935.382−20.08937.3181.0074.26
ATOM251OE1GLU33934.786−20.22036.2271.0073.51
ATOM252OE2GLU33935.496−21.02038.1441.0076.44
ATOM253CGLU33935.770−15.38535.9101.0068.15
ATOM254OGLU33936.722−15.21635.1441.0068.99
ATOM255NALA34034.562−14.87435.6941.0064.41
ATOM256CAALA34034.246−14.08334.5071.0060.69
ATOM257CBALA34032.767−13.70934.5231.0061.17
ATOM258CALA34035.096−12.82434.3261.0057.00
ATOM259OALA34035.634−12.27035.2871.0057.46
ATOM260NSER34135.215−12.38833.0761.0052.15
ATOM261CASER34135.972−11.18832.7361.0046.53
ATOM262CBSER34136.839−11.43931.4971.0048.64
ATOM263OGSER34137.184−10.22630.8461.0046.48
ATOM264CSER34134.957−10.08732.4441.0043.52
ATOM265OSER34134.090−10.24831.5891.0039.92
ATOM266NMET34235.052−8.97833.1661.0041.24
ATOM267CAMET34234.121−7.87532.9601.0042.46
ATOM268CBMET34234.449−6.72333.9121.0045.61
ATOM269CGMET34233.228−6.08934.5601.0052.39
ATOM270SDMET34231.791−7.20134.6311.0057.92
ATOM271CEMET34231.999−7.88136.2391.0056.18
ATOM272CMET34234.124−7.36531.5161.0040.22
ATOM273OMET34233.063−7.12130.9381.0039.23
ATOM274NMET34335.307−7.20430.9301.0038.72
ATOM275CAMET34335.395−6.70829.5581.0038.50
ATOM276CBMET34336.838−6.31829.2161.0041.15
ATOM277CGMET34337.022−5.74927.8041.0040.31
ATOM278SDMET34336.032−4.26027.4271.0045.23
ATOM279CEMET34336.113−3.35828.9871.0040.45
ATOM280CMET34334.880−7.74128.5611.0035.36
ATOM281OMET34334.368−7.38427.5011.0035.51
ATOM282NGLY34435.017−9.02028.9021.0035.53
ATOM283CAGLY34434.533−10.07228.0241.0033.41
ATOM284CGLY34433.015−10.06328.0471.0031.74
ATOM285OGLY34432.359−10.23327.0191.0029.58
ATOM286NLEU34532.459−9.86029.2381.0032.89
ATOM287CALEU34531.011−9.80429.4151.0034.95
ATOM288CBLEU34530.665−9.63130.9021.0037.56
ATOM289CGLEU34530.942−10.77431.8831.0043.03
ATOM290CD1LEU34530.537−10.35733.2971.0041.57
ATOM291CD2LEU34530.164−11.99831.4491.0042.80
ATOM292CLEU34530.430−8.61428.6331.0033.71
ATOM293OLEU34529.479−8.75727.8681.0030.29
ATOM294NLEU34631.021−7.44328.8431.0030.20
ATOM295CALEU34630.569−6.21728.1931.0032.00
ATOM296CBLEU34631.317−5.01628.7711.0028.16
ATOM297CGLEU34631.091−4.76730.2691.0029.84
ATOM298CD1LEU34631.815−3.49830.6681.0029.98
ATOM299CD2LEU34629.614−4.64430.5811.0033.97
ATOM300CLEU34630.732−6.25026.6821.0030.70
ATOM301OLEU34629.869−5.76525.9551.0029.13
ATOM302NTHR34731.839−6.81626.2121.0030.47
ATOM303CATHR34732.086−6.91124.7811.0030.93
ATOM304CBTHR34733.472−7.50124.4971.0029.97
ATOM305OG1THR34734.481−6.60424.9821.0035.40
ATOM306CG2THR34733.666−7.70723.0041.0033.58
ATOM307CTHR34731.036−7.80424.1221.0031.97
ATOM308OTHR34730.516−7.48623.0491.0030.75
ATOM309NASN34830.737−8.92624.7681.0029.31
ATOM310CAASN34829.757−9.86824.2421.0032.63
ATOM311CBASN34829.767−11.16125.0651.0031.64
ATOM312CGASN34828.646−12.11724.6621.0039.14
ATOM313OD1ASN34827.549−12.07825.2201.0041.91
ATOM314ND2ASN34828.920−12.97023.6831.0042.05
ATOM315CASN34828.361−9.25124.2621.0029.02
ATOM316OASN34827.558−9.47723.3531.0032.76
ATOM317NLEU34928.078−8.46725.2981.0028.74
ATOM318CALEU34926.782−7.81125.4211.0028.58
ATOM319CBLEU34926.650−7.14826.7951.0026.56
ATOM320CGLEU34925.376−6.32827.0501.0033.67
ATOM321CD1LEU34924.140−7.19926.8401.0028.82
ATOM322CD2LEU34925.392−5.77928.4711.0033.11
ATOM323CLEU34926.638−6.76224.3191.0028.07
ATOM324OLEU34925.616−6.70323.6291.0025.22
ATOM325NALA35027.675−5.94124.1571.0028.50
ATOM326CAALA35027.668−4.88623.1481.0028.46
ATOM327CBALA35028.972−4.09423.2091.0028.12
ATOM328CALA35027.468−5.46121.7501.0028.75
ATOM329OALA35026.649−4.95820.9831.0030.90
ATOM330NASP35128.213−6.50921.4201.0027.20
ATOM331CAASP35128.093−7.14320.1121.0029.75
ATOM332CBASP35129.036−8.34520.0101.0034.16
ATOM333CGASP35130.498−7.94019.9781.0037.50
ATOM334OD1ASP35131.354−8.83120.1481.0037.55
ATOM335OD2ASP35130.789−6.73819.7841.0035.50
ATOM336CASP35126.661−7.60019.8131.0030.52
ATOM337OASP35126.193−7.45818.6871.0027.77
ATOM338NARG35225.968−8.15020.8111.0027.18
ATOM339CAARG35224.593−8.60220.6051.0026.21
ATOM340CBARG35224.148−9.53421.7521.0026.52
ATOM341CGARG35224.567−10.99121.5321.0031.03
ATOM342CDARG35224.128−11.91122.6661.0029.80
ATOM343NEARG35224.898−11.67523.8791.0030.44
ATOM344CZARG35224.364−11.36325.0541.0031.68
ATOM345NH1ARG35223.050−11.25125.1771.0031.18
ATOM346NH2ARG35225.144−11.14826.1041.0032.03
ATOM347CARG35223.642−7.41120.5021.0027.16
ATOM348OARG35222.702−7.42619.7081.0026.65
ATOM349NGLU35323.896−6.37021.2911.0024.30
ATOM350CAGLU35323.045−5.17821.2611.0026.39
ATOM351CBGLU35323.461−4.20422.3651.0024.91
ATOM352CGGLU35323.147−4.66923.7711.0027.93
ATOM353CDGLU35323.425−3.58724.7951.0030.71
ATOM354OE1GLU35324.564−3.53425.3041.0030.09
ATOM355OE2GLU35322.506−2.78925.0851.0030.53
ATOM356CGLU35323.131−4.45619.9201.0024.27
ATOM357OGLU35322.169−3.82619.4671.0028.71
ATOM358NLEU35424.296−4.54019.2931.0026.61
ATOM359CALEU35424.522−3.87218.0171.0026.62
ATOM360CBLEU35425.952−4.12117.5431.0026.36
ATOM361CGLEU35426.372−3.25716.3511.0029.24
ATOM362CD1LEU35426.243−1.77416.7221.0026.59
ATOM363CD2LEU35427.794−3.60715.9621.0028.88
ATOM364CLEU35423.559−4.30016.9261.0027.72
ATOM365OLEU35423.074−3.47516.1521.0024.00
ATOM366NVAL35523.291−5.59816.8541.0028.82
ATOM367CAVAL35522.386−6.12515.8441.0029.45
ATOM368CBVAL35522.259−7.65515.9751.0031.76
ATOM369CG1VAL35521.423−8.20514.8341.0033.55
ATOM370CG2VAL35523.649−8.28215.9981.0031.36
ATOM371CVAL35521.020−5.49916.0351.0027.71
ATOM372OVAL35520.382−5.03915.0801.0029.61
ATOM373NHIS35620.580−5.47317.2881.0027.76
ATOM374CAHIS35619.291−4.90617.6271.0028.35
ATOM375CBHIS35618.936−5.23119.0791.0031.12
ATOM376CGHIS35618.602−6.67519.3071.0035.93
ATOM377CD2HIS35619.352−7.70019.7791.0033.95
ATOM378ND1HIS35617.363−7.20819.0181.0036.62
ATOM379CE1HIS35617.364−8.49919.3041.0033.33
ATOM380NE2HIS35618.559−8.82319.7671.0032.16
ATOM381CHIS35619.300−3.39817.4121.0028.25
ATOM382OHIS35618.272−2.81217.1001.0028.99
ATOM383NMET35720.457−2.76517.5741.0025.31
ATOM384CAMET35720.526−1.32217.3691.0024.63
ATOM385CBMET35721.902−0.78917.7661.0023.61
ATOM386CGMET35722.0110.73617.6991.0024.66
ATOM387SDMET35723.7321.29017.8591.0027.30
ATOM388CEMET35724.1400.67219.5141.0023.62
ATOM389CMET35720.256−1.01115.8981.0024.83
ATOM390OMET35719.619−0.00315.5691.0026.78
ATOM391NILE35820.757−1.87415.0201.0026.25
ATOM392CAILE35820.553−1.72113.5761.0030.33
ATOM393CBILE35821.204−2.88812.7891.0033.86
ATOM394CG2ILE35820.759−2.86011.3341.0033.68
ATOM395CG1ILE35822.728−2.79912.8741.0036.89
ATOM396CD1ILE35823.299−1.46912.4511.0039.10
ATOM397CILE35819.055−1.72113.3101.0032.20
ATOM398OILE35818.519−0.81712.6621.0032.02
ATOM399NASN35918.379−2.74813.8141.0033.12
ATOM400CAASN35916.945−2.86113.6381.0033.35
ATOM401CBASN35916.434−4.10114.3631.0037.59
ATOM402CGASN35916.739−5.37413.6271.0044.38
ATOM403OD1ASN35917.045−5.32912.4371.0047.35
ATOM404ND2ASN35916.673−6.50814.3201.0042.48
ATOM405CASN35916.224−1.63414.1491.0032.74
ATOM406OASN35915.261−1.16313.5301.0031.39
ATOM407NTRP36016.706−1.10415.2641.0027.92
ATOM408CATRP36016.1020.08715.8421.0029.47
ATOM409CBTRP36016.7030.34717.2281.0027.66
ATOM410CGTRP36016.5221.74717.7071.0030.40
ATOM411CD2TRP36017.4932.80117.6571.0027.54
ATOM412CE2TRP36016.8883.95418.2041.0029.42
ATOM413CE3TRP36018.8192.88317.2051.0028.37
ATOM414CD1TRP36015.3992.28418.2641.0027.75
ATOM415NE1TRP36015.6093.61118.5661.0030.84
ATOM416CZ2TRP36017.5585.18018.3101.0027.74
ATOM417CZ3TRP36019.4884.10617.3091.0024.49
ATOM418CH2TRP36018.8535.23217.8581.0025.09
ATOM419CTRP36016.3121.29614.9261.0027.90
ATOM420OTRP36015.3602.00214.5811.0028.83
ATOM421NALA36117.5591.52014.5231.0028.25
ATOM422CAALA36117.8942.63713.6451.0029.20
ATOM423CBALA36119.3462.53913.2201.0028.89
ATOM424CALA36117.0062.68512.4031.0031.08
ATOM425OALA36116.5313.74612.0111.0031.30
ATOM426NLYS36216.7951.52611.7831.0030.93
ATOM427CALYS36215.9811.44310.5811.0034.15
ATOM428CBLYS36216.0120.01610.0231.0033.67
ATOM429CGLYS36217.252−0.2819.1981.0039.40
ATOM430CDLYS36217.547−1.7749.1361.0043.60
ATOM431CELYS36218.852−2.0468.3891.0047.06
ATOM432NZLYS36219.178−3.5078.2881.0050.34
ATOM433CLYS36214.5451.87210.8151.0035.81
ATOM434OLYS36213.8212.1689.8591.0037.95
ATOM435NARG36314.1341.92112.0791.0034.23
ATOM436CAARG36312.7702.31312.4091.0036.04
ATOM437CBARG36312.1781.30713.3911.0036.71
ATOM438CGARG36312.169−0.11012.8271.0040.36
ATOM439CDARG36311.468−1.08613.7461.0042.17
ATOM440NEARG36310.161−0.58614.1581.0045.19
ATOM441CZARG3639.314−1.26214.9291.0049.41
ATOM442NH1ARG3639.642−2.46715.3741.0048.02
ATOM443NH2ARG3638.143−0.72915.2611.0051.54
ATOM444CARG36312.6543.74312.9431.0037.40
ATOM445OARG36311.5674.19913.3031.0038.22
ATOM446NVAL36413.7854.44213.0021.0035.66
ATOM447CAVAL36413.8045.83613.4311.0034.06
ATOM448CBVAL36415.2316.27113.8271.0033.87
ATOM449CG1VAL36415.2937.77913.9951.0031.08
ATOM450CG2VAL36415.6415.57115.1131.0031.30
ATOM451CVAL36413.3606.59112.1711.0033.19
ATOM452OVAL36414.0286.53111.1461.0033.04
ATOM453NPRO36512.2257.31012.2341.0034.69
ATOM454CDPRO36511.3597.49213.4131.0034.19
ATOM455CAPRO36511.7248.05011.0691.0035.96
ATOM456CBPRO36510.6088.91811.6451.0036.59
ATOM457CGPRO36510.1358.15712.8421.0039.59
ATOM458CPRO36512.7568.87810.3211.0037.19
ATOM459OPRO36513.4309.72610.9071.0040.29
ATOM460NGLY36612.8788.6249.0231.0034.78
ATOM461CAGLY36613.8169.3718.2121.0033.54
ATOM462CGLY36615.1688.7228.0071.0034.26
ATOM463OGLY36615.8589.0357.0341.0037.15
ATOM464NPHE36715.5547.8148.9011.0033.13
ATOM465CAPHE36716.8607.1648.7871.0032.04
ATOM466CBPHE36717.1386.29110.0161.0030.22
ATOM467CGPHE36718.5445.77310.0801.0030.60
ATOM468CD1PHE36718.8274.4469.7511.0031.94
ATOM469CD2PHE36719.5896.60110.4851.0029.20
ATOM470CE1PHE36720.1333.9509.8281.0028.30
ATOM471CE2PHE36720.8966.12210.5681.0028.12
ATOM472CZPHE36721.1714.79110.2401.0025.41
ATOM473CPHE36717.0336.3337.5241.0031.46
ATOM474OPHE36718.0736.4056.8831.0032.30
ATOM475NVAL36816.0275.5417.1651.0035.20
ATOM476CAVAL36816.1234.7185.9591.0038.98
ATOM477CBVAL36815.0763.5845.9451.0040.61
ATOM478CG1VAL36815.5432.4476.8431.0041.48
ATOM479CG2VAL36813.7174.1136.3901.0041.60
ATOM480CVAL36815.9655.5234.6731.0040.06
ATOM481OVAL36816.1564.9923.5791.0041.66
ATOM482NASP36915.6086.7984.7981.0038.65
ATOM483CAASP36915.4657.6463.6211.0037.15
ATOM484CBASP36914.7008.9293.9541.0039.89
ATOM485CGASP36913.2548.6714.3021.0045.59
ATOM486OD1ASP36912.6867.6723.8061.0046.34
ATOM487OD2ASP36912.6819.4725.0741.0049.13
ATOM488CASP36916.8558.0103.1361.0034.91
ATOM489OASP36917.0388.4311.9951.0034.25
ATOM490NLEU37017.8387.8414.0161.0031.76
ATOM491CALEU37019.2298.1533.7051.0028.08
ATOM492CBLEU37020.0208.3395.0031.0028.81
ATOM493CGLEU37019.5239.3956.0001.0028.74
ATOM494CD1LEU37020.3159.2757.2991.0030.81
ATOM495CD2LEU37019.69310.7925.4041.0029.77
ATOM496CLEU37019.8847.0432.8931.0031.25
ATOM497OLEU37019.3415.9432.7841.0031.78
ATOM498NTHR37121.0527.3332.3311.0028.86
ATOM499CATHR37121.7936.3361.5691.0032.90
ATOM500CBTHR37122.9796.9440.8181.0033.44
ATOM501OG1THR37123.8807.5231.7661.0034.59
ATOM502CG2THR37122.5148.002−0.1781.0032.63
ATOM503CTHR37122.3735.3152.5391.0035.31
ATOM504OTHR37122.5365.5913.7331.0031.27
ATOM505NLEU37222.7024.1412.0151.0034.34
ATOM506CALEU37223.2733.0732.8221.0035.46
ATOM507CBLEU37223.5181.8411.9441.0037.73
ATOM508CGLEU37224.3620.7042.5151.0042.43
ATOM509CD1LEU37223.6900.1453.7571.0045.60
ATOM510CD2LEU37224.534−0.3831.4551.0044.29
ATOM511CLEU37224.5873.5483.4441.0036.95
ATOM512OLEU37224.8133.3744.6431.0035.57
ATOM513NHIS37325.4424.1592.6271.0035.68
ATOM514CAHIS37326.7294.6563.0991.0036.60
ATOM515CBHIS37327.5065.2821.9351.0044.01
ATOM516CGHIS37328.5386.2802.3601.0050.69
ATOM517CD2HIS37329.8576.1382.6361.0054.69
ATOM518ND1HIS37328.2467.6132.5611.0053.77
ATOM519CE1HIS37329.3398.2482.9451.0057.09
ATOM520NE2HIS37330.3317.3762.9991.0057.23
ATOM521CHIS37326.5755.6694.2441.0036.22
ATOM522OHIS37327.3505.6505.2011.0033.05
ATOM523NASP37425.5806.5494.1481.0032.03
ATOM524CAASP37425.3427.5415.1961.0030.76
ATOM525CBASP37424.3548.6034.7131.0030.12
ATOM526CGASP37425.0189.6723.8601.0035.83
ATOM527OD1ASP37426.2649.7443.8421.0034.39
ATOM528OD2ASP37424.29110.4403.1991.0035.39
ATOM529CASP37424.8056.8766.4721.0030.33
ATOM530OASP37425.1527.2757.5871.0027.04
ATOM531NGLN37523.9445.8776.3091.0025.71
ATOM532CAGLN37523.4035.1577.4541.0026.68
ATOM533CBGLN37522.4244.0776.9931.0029.70
ATOM534CGGLN37521.1014.6166.4841.0029.16
ATOM535CDGLN37520.2193.5145.9401.0035.87
ATOM536OE1GLN37520.1552.4266.5101.0030.97
ATOM537NE2GLN37519.5413.7854.8271.0034.51
ATOM538CGLN37524.5564.5028.2141.0025.51
ATOM539OGLN37524.5854.5139.4421.0028.14
ATOM540NVAL37625.5043.9387.4751.0026.62
ATOM541CAVAL37626.6593.2818.0711.0029.24
ATOM542CBVAL37627.5312.5977.0031.0029.66
ATOM543CG1VAL37628.8122.0717.6351.0028.29
ATOM544CG2VAL37626.7451.4696.3411.0029.90
ATOM545CVAL37627.5264.2858.8211.0030.87
ATOM546OVAL37627.9534.0299.9481.0030.09
ATOM547NHIS37727.7855.4288.1911.0028.05
ATOM548CAHIS37728.6026.4578.8141.0028.68
ATOM549CBHIS37728.7927.6397.8641.0030.26
ATOM550CGHIS37729.5088.7918.4881.0033.89
ATOM551CD2HIS37729.07310.0178.8631.0034.99
ATOM552ND1HIS37730.8468.7408.8231.0037.01
ATOM553CE1HIS37731.2019.8849.3771.0034.79
ATOM554NE2HIS37730.14410.6779.4131.0034.95
ATOM555CHIS37727.9836.95410.1141.0025.13
ATOM556OHIS37728.6777.10211.1151.0025.93
ATOM557NLEU37826.6787.20610.1071.0024.58
ATOM558CALEU37826.0157.69511.3151.0026.40
ATOM559CBLEU37824.5428.00111.0271.0026.29
ATOM560CGLEU37824.2919.18010.0731.0028.06
ATOM561CD1LEU37822.7789.3539.8691.0027.66
ATOM562CD2LEU37824.91110.45810.6421.0030.08
ATOM563CLEU37826.1206.69512.4591.0028.55
ATOM564OLEU37826.3797.07513.6051.0024.76
ATOM565NLEU37925.9195.41412.1531.0024.29
ATOM566CALEU37926.0004.38813.1821.0027.03
ATOM567CBLEU37925.4013.07312.6671.0028.53
ATOM568CGLEU37923.8753.02312.8451.0030.29
ATOM569CD1LEU37923.2481.94311.9631.0033.04
ATOM570CD2LEU37923.5632.75914.3121.0029.45
ATOM571CLEU37927.4304.17613.6701.0027.18
ATOM572OLEU37927.6533.97914.8661.0025.95
ATOM573NGLU38028.4024.23612.7621.0025.86
ATOM574CAGLU38029.7864.05413.1731.0027.58
ATOM575CBGLU38030.7304.03611.9681.0030.36
ATOM576CGGLU38032.1723.78512.3801.0037.98
ATOM577CDGLU38033.0803.47111.2101.0045.23
ATOM578OE1GLU38032.8694.04810.1201.0042.99
ATOM579OE2GLU38034.0042.64611.3861.0045.79
ATOM580CGLU38030.2185.15914.1331.0027.50
ATOM581OGLU38031.0564.93715.0101.0026.67
ATOM582NACYS38129.6376.33913.9650.7524.89
ATOM583NBCYS38129.6456.35213.9800.2525.79
ATOM584CAACYS38129.9697.46614.8260.7524.12
ATOM585CABCYS38129.9937.48114.8470.2524.86
ATOM586CBACYS38129.6218.78114.1220.7525.96
ATOM587CBBCYS38129.7668.81414.1150.2525.62
ATOM588SGACYS38130.6989.19212.7320.7531.63
ATOM589SGBCYS38130.22710.31215.0590.2525.40
ATOM590CACYS38129.2377.42216.1620.7522.07
ATOM591CBCYS38129.2117.49816.1590.2523.97
ATOM592OACYS38129.8127.73017.2060.7521.97
ATOM593OBCYS38129.7247.94017.1870.2523.99
ATOM594NALA38227.9747.01216.1281.0023.41
ATOM595CAALA38227.1407.01517.3181.0022.83
ATOM596CBALA38225.7857.58716.9481.0025.50
ATOM597CALA38226.9135.75518.1311.0025.39
ATOM598OALA38226.3745.83719.2341.0023.09
ATOM599NTRP38327.3114.60217.6151.0025.98
ATOM600CATRP38327.0263.35418.3181.0023.80
ATOM601CBTRP38327.6692.17217.5801.0022.52
ATOM602CGTRP38329.1302.05417.7621.0024.42
ATOM603CD2TRP38329.7971.34718.8031.0027.31
ATOM604CE2TRP38331.1821.48418.5791.0028.24
ATOM605CE3TRP38329.3600.60919.9121.0027.37
ATOM606CD1TRP38330.1022.57816.9651.0024.58
ATOM607NE1TRP38331.3422.23917.4461.0027.35
ATOM608CZ2TRP38332.1330.90919.4201.0028.76
ATOM609CZ3TRP38330.3050.03920.7451.0028.09
ATOM610CH2TRP38331.6740.19120.4961.0029.77
ATOM611CTRP38327.3563.30919.8021.0023.54
ATOM612OTRP38326.5262.86620.5841.0022.90
ATOM613NLEU38428.5423.76520.2111.0020.37
ATOM614CALEU38428.8643.71321.6401.0022.41
ATOM615CBLEU38430.3693.89021.8831.0024.98
ATOM616CGLEU38430.8243.64523.3361.0027.33
ATOM617CD1LEU38430.2732.30523.8531.0029.71
ATOM618CD2LEU38432.3363.64823.3981.0026.07
ATOM619CLEU38428.0754.73222.4531.0019.44
ATOM620OLEU38427.7064.45823.5951.0023.24
ATOM621NGLU38527.8075.90921.8851.0020.80
ATOM622CAGLU38527.0116.89522.6121.0021.32
ATOM623CBGLU38526.8618.17721.7971.0021.91
ATOM624CGGLU38528.1159.02021.7051.0021.61
ATOM625CDGLU38527.88210.25620.8601.0029.53
ATOM626OE1GLU38527.37411.25621.4011.0030.54
ATOM627OE2GLU38528.18810.21919.6581.0029.97
ATOM628CGLU38525.6166.29222.8361.0022.26
ATOM629OGLU38525.0226.43823.9021.0022.26
ATOM630NILE38625.1015.61721.8121.0022.03
ATOM631CAILE38623.7794.99521.8961.0022.74
ATOM632CBILE38623.3284.45520.4981.0022.88
ATOM633CG2ILE38622.0093.64720.6181.0023.85
ATOM634CG1ILE38623.0855.65119.5611.0025.05
ATOM635CD1ILE38622.9945.29718.0781.0026.42
ATOM636CILE38623.7663.89722.9611.0022.50
ATOM637OILE38622.8233.81823.7461.0024.75
ATOM638NLEU38724.8103.07123.0201.0022.25
ATOM639CALEU38724.8682.03024.0511.0022.95
ATOM640CBLEU38726.0961.13223.8641.0024.61
ATOM641CGLEU38726.0700.19422.6541.0023.21
ATOM642CD1LEU38727.297−0.70922.7051.0025.36
ATOM643CD2LEU38724.791−0.63122.6521.0026.29
ATOM644CLEU38724.9442.66025.4381.0026.22
ATOM645OLEU38724.2872.20426.3861.0023.55
ATOM646NMET38825.7513.71325.5541.0023.92
ATOM647CAMET38825.9244.38526.8351.0024.26
ATOM648CBMET38827.0885.37826.7611.0023.87
ATOM649CGMET38828.4404.72226.7431.0024.08
ATOM650SDMET38829.7265.99226.7361.0027.70
ATOM651CEMET38831.1395.04127.0781.0021.74
ATOM652CMET38824.6605.09427.3211.0023.33
ATOM653OMET38824.3415.02628.5051.0025.58
ATOM654NILE38923.9355.77526.4361.0024.62
ATOM655CAILE38922.7296.44026.9051.0024.03
ATOM656CBILE38922.1327.43925.8521.0027.01
ATOM657CG2ILE38921.4136.70524.7061.0023.98
ATOM658CG1ILE38921.1858.40226.5841.0025.49
ATOM659CD1ILE38920.4319.38325.6831.0025.45
ATOM660CILE38921.6945.40127.3491.0026.54
ATOM661OILE38920.9385.63128.2941.0022.58
ATOM662NGLY39021.6794.24726.6871.0027.14
ATOM663CAGLY39020.7533.20127.0901.0028.42
ATOM664CGLY39021.1332.71928.4821.0029.67
ATOM665OGLY39020.2752.52129.3481.0029.21
ATOM666NLEU39122.4332.54728.6991.0026.06
ATOM667CALEU39122.9552.09129.9831.0029.23
ATOM668CBLEU39124.4761.93729.8991.0028.37
ATOM669CGLEU39125.2061.65631.2101.0030.81
ATOM670CD1LEU39124.7170.33231.7931.0025.73
ATOM671CD2LEU39126.7091.61930.9581.0025.25
ATOM672CLEU39122.6033.07031.1041.0030.84
ATOM673OLEU39122.1562.66932.1861.0029.19
ATOM674NVAL39222.8174.35530.8501.0028.91
ATOM675CAVAL39222.5065.36931.8511.0028.86
ATOM676CBVAL39222.9236.77031.3531.0030.08
ATOM677CG1VAL39222.3297.85432.2371.0032.32
ATOM678CG2VAL39224.4426.87031.3721.0028.52
ATOM679CVAL39221.0135.32732.1651.0028.42
ATOM680OVAL39220.6215.34533.3271.0030.38
ATOM681NTRP39320.1915.24131.1251.0028.23
ATOM682CATRP39318.7325.18631.2801.0029.70
ATOM683CBTRP39318.0665.04629.9061.0030.09
ATOM684CGTRP39316.6054.67029.9531.0033.50
ATOM685CD2TRP39315.5165.49930.3691.0031.76
ATOM686CE2TRP39314.3364.72530.2641.0038.11
ATOM687CE3TRP39315.4196.82130.8241.0032.56
ATOM688CD1TRP39316.0573.45929.6181.0034.31
ATOM689NE1TRP39314.6963.48629.8011.0034.36
ATOM690CZ2TRP39313.0735.23330.5971.0037.93
ATOM691CZ3TRP39314.1627.32631.1551.0035.24
ATOM692CH2TRP39313.0076.53131.0391.0037.77
ATOM693CTRP39318.2564.05132.1911.0032.07
ATOM694OTRP39317.4604.27533.1091.0032.12
ATOM695NARG39418.7382.83731.9571.0031.90
ATOM696CAARG39418.2881.72932.7871.0036.63
ATOM697CBARG39418.4920.38932.0651.0036.41
ATOM698CGARG39419.9140.00931.7641.0036.50
ATOM699CDARG39419.929−1.13230.7481.0036.34
ATOM700NEARG39421.282−1.56130.4171.0033.97
ATOM701CZARG39421.864−1.35029.2391.0031.61
ATOM702NH1ARG39421.208−0.71528.2811.0032.42
ATOM703NH2ARG39423.098−1.78429.0221.0029.81
ATOM704CARG39418.9111.69734.1801.0036.69
ATOM705OARG39418.4450.96635.0481.0037.07
ATOM706NSER39519.9542.49234.3951.0033.63
ATOM707CASER39520.6032.56435.7011.0035.69
ATOM708CBSER39522.1122.78435.5401.0032.94
ATOM709OGSER39522.6961.81134.6881.0032.37
ATOM710CSER39520.0103.71336.5311.0036.44
ATOM711OSER39520.3893.91637.6871.0038.68
ATOM712NMET39619.0764.44935.9371.0036.46
ATOM713CAMET39618.4315.58836.5891.0043.08
ATOM714CBMET39617.2756.10435.7251.0043.87
ATOM715CGMET39617.4817.50735.1761.0046.18
ATOM716SDMET39615.9628.27834.5811.0049.58
ATOM717CEMET39614.9888.29836.0651.0053.58
ATOM718CMET39617.9065.30337.9921.0046.18
ATOM719OMET39618.1256.08938.9131.0046.34
ATOM720NGLU39717.2154.18038.1521.0049.39
ATOM721CAGLU39716.6453.82139.4441.0052.12
ATOM722CBGLU39715.2963.13039.2461.0055.34
ATOM723CGGLU39714.1664.07338.8731.0058.86
ATOM724CDGLU39713.1953.44837.8911.0063.28
ATOM725OE1GLU39713.6602.92536.8541.0064.68
ATOM726OE2GLU39711.9723.47538.1551.0065.39
ATOM727CGLU39717.5482.93340.2831.0052.75
ATOM728OGLU39717.0712.18741.1391.0053.96
ATOM729NHIS39818.8513.01440.0401.0050.25
ATOM730CAHIS39819.8132.22040.7921.0049.34
ATOM731CBHIS39820.2711.01839.9631.0052.04
ATOM732CGHIS39819.1870.01739.7211.0053.95
ATOM733CD2HIS39818.750−1.02240.4721.0053.92
ATOM734ND1HIS39818.3740.05438.6081.0055.91
ATOM735CE1HIS39817.482−0.91738.6851.0055.53
ATOM736NE2HIS39817.688−1.58539.8061.0055.81
ATOM737CHIS39820.9993.08441.1961.0047.44
ATOM738OHIS39822.1212.88740.7301.0044.91
ATOM739NPRO39920.7554.04942.0961.0046.45
ATOM740CDPRO39919.4434.30042.7211.0047.27
ATOM741CAPRO39921.7854.96842.5861.0045.35
ATOM742CBPRO39921.1275.63143.7931.0047.40
ATOM743CGPRO39919.6605.56143.5041.0047.72
ATOM744CPRO39923.0864.27042.9581.0044.70
ATOM745OPRO39923.0783.23343.6271.0046.46
ATOM746NGLY40024.2024.84042.5091.0041.57
ATOM747CAGLY40025.5064.28142.8131.0039.84
ATOM748CGLY40025.9073.04742.0221.0037.85
ATOM749OGLY40027.0272.56042.1761.0040.48
ATOM750NLYS40125.0122.53741.1801.0036.39
ATOM751CALYS40125.3151.34440.3901.0034.47
ATOM752CBLYS40124.5620.13040.9471.0036.12
ATOM753CGLYS40124.633−0.00742.4661.0039.30
ATOM754CDLYS40124.288−1.42942.9031.0044.38
ATOM755CELYS40124.459−1.60544.4081.0046.68
ATOM756NZLYS40124.968−2.96944.7471.0053.37
ATOM757CLYS40124.9691.48538.9111.0032.34
ATOM758OLYS40124.1412.30838.5311.0031.16
ATOM759NLEU40225.6120.66338.0861.0028.52
ATOM760CALEU40225.3580.65836.6481.0029.06
ATOM761CBLEU40226.6610.84735.8671.0029.26
ATOM762CGLEU40227.2782.24236.0291.0024.67
ATOM763CD1LEU40228.6232.31035.3101.0027.47
ATOM764CD2LEU40226.3123.27735.4821.0024.93
ATOM765CLEU40224.755−0.68636.2921.0030.43
ATOM766OLEU40225.367−1.72736.5351.0031.36
ATOM767NLEU40323.552−0.65835.7351.0031.07
ATOM768CALEU40322.873−1.88035.3351.0032.96
ATOM769CBLEU40321.361−1.69335.4341.0033.86
ATOM770CGLEU40320.551−2.99135.4151.0039.29
ATOM771CD1LEU40320.584−3.63736.8061.0043.62
ATOM772CD2LEU40319.128−2.68934.9981.0041.32
ATOM773CLEU40323.255−2.21833.8991.0030.06
ATOM774OLEU40322.543−1.87032.9561.0031.63
ATOM775NPHE40424.383−2.89333.7331.0029.19
ATOM776CAPHE40424.834−3.25632.4031.0028.93
ATOM777CBPHE40426.201−3.92932.4931.0030.05
ATOM778CGPHE40427.305−2.99832.9261.0030.78
ATOM779CD1PHE40427.794−3.03334.2281.0032.91
ATOM780CD2PHE40427.848−2.07832.0301.0032.75
ATOM781CE1PHE40428.816−2.16034.6381.0034.73
ATOM782CE2PHE40428.864−1.20532.4231.0030.68
ATOM783CZPHE40429.350−1.24233.7271.0031.43
ATOM784CPHE40423.809−4.18131.7561.0030.80
ATOM785OPHE40423.625−4.17530.5381.0028.09
ATOM786NALA40523.138−4.96732.5941.0030.25
ATOM787CAALA40522.104−5.91032.1631.0029.78
ATOM788CBALA40522.745−7.17231.5981.0029.97
ATOM789CALA40521.309−6.23733.4291.0031.95
ATOM790OALA40521.785−5.99534.5351.0032.36
ATOM791NPRO40620.088−6.77933.2881.0034.40
ATOM792CDPRO40619.356−7.10232.0531.0035.81
ATOM793CAPRO40619.303−7.10134.4901.0036.41
ATOM794CBPRO40617.985−7.65433.9351.0035.38
ATOM795CGPRO40617.922−7.15332.5191.0036.49
ATOM796CPRO40619.997−8.08435.4331.0037.32
ATOM797OPRO40619.698−8.11236.6261.0038.34
ATOM798NASN40720.924−8.87734.9021.0036.69
ATOM799CAASN40721.652−9.84735.7121.0038.85
ATOM800CBASN40721.582−11.24335.0831.0039.69
ATOM801CGASN40722.232−11.30633.7111.0044.10
ATOM802OD1ASN40722.345−10.29633.0091.0037.78
ATOM803ND2ASN40722.660−12.50333.3191.0045.74
ATOM804CASN40723.100−9.43535.8741.0038.12
ATOM805OASN40723.965−10.25636.1781.0039.81
ATOM806NLEU40823.364−8.14935.6711.0037.80
ATOM807CALEU40824.713−7.63135.7991.0036.89
ATOM808CBLEU40825.449−7.72034.4591.0036.09
ATOM809CGLEU40826.972−7.60934.5501.0035.08
ATOM810CD1LEU40827.525−8.77535.3541.0039.15
ATOM811CD2LEU40827.578−7.58733.1581.0036.85
ATOM812CLEU40824.670−6.18736.2861.0040.55
ATOM813OLEU40824.646−5.24835.4911.0038.29
ATOM814NLEU40924.644−6.03437.6071.0039.50
ATOM815CALEU40924.606−4.73338.2571.0041.00
ATOM816CBLEU40923.392−4.65839.1841.0043.69
ATOM817CGLEU40923.164−3.38239.9931.0047.35
ATOM818CD1LEU40922.848−2.23339.0581.0047.09
ATOM819CD2LEU40922.014−3.60340.9761.0049.38
ATOM820CLEU40925.894−4.56639.0601.0041.80
ATOM821OLEU40926.178−5.35839.9601.0041.00
ATOM822NLEU41026.676−3.54438.7271.0039.23
ATOM823CALEU41027.931−3.29639.4231.0040.45
ATOM824CBLEU41029.106−3.35438.4421.0041.59
ATOM825CGLEU41029.457−4.66037.7161.0044.87
ATOM826CD1LEU41030.972−4.72837.5541.0045.41
ATOM827CD2LEU41028.949−5.87238.4841.0047.02
ATOM828CLEU41027.946−1.94440.1321.0040.67
ATOM829OLEU41027.361−0.97039.6521.0040.22
ATOM830NASP41128.610−1.89041.2811.0041.57
ATOM831CAASP41128.717−0.64042.0251.0042.69
ATOM832CBASP41128.490−0.87443.5281.0044.44
ATOM833CGASP41129.655−1.57844.2101.0046.70
ATOM834OD1ASP41129.537−1.84945.4261.0051.44
ATOM835OD2ASP41130.680−1.86143.5531.0048.79
ATOM836CASP41130.088−0.01641.7791.0043.70
ATOM837OASP41130.933−0.61041.1071.0038.48
ATOM838NARG41230.2951.18142.3211.0046.78
ATOM839CAARG41231.5541.90542.1711.0049.97
ATOM840CBARG41231.6013.09043.1381.0051.28
ATOM841CGARG41230.9714.36442.6141.0054.77
ATOM842CDARG41231.6445.58043.2191.0054.61
ATOM843NEARG41233.0715.61542.9121.0056.53
ATOM844CZARG41233.8276.70842.9851.0061.90
ATOM845NH1ARG41233.2917.86643.3561.0063.48
ATOM846NH2ARG41235.1206.64542.6821.0061.21
ATOM847CARG41232.7711.02642.4291.0050.29
ATOM848OARG41233.6280.86641.5611.0051.02
ATOM849NASN41332.8440.46943.6331.0051.94
ATOM850CAASN41333.969−0.37544.0211.0053.15
ATOM851CBASN41333.719−0.98045.4031.0055.88
ATOM852CGASN41333.6540.07346.4961.0057.99
ATOM853OD1ASN41333.6971.27646.2231.0058.27
ATOM854ND2ASN41333.551−0.37547.7421.0057.90
ATOM855CASN41334.235−1.48043.0131.0053.95
ATOM856OASN41335.386−1.74342.6591.0053.67
ATOM857NGLN41433.173−2.12942.5471.0055.33
ATOM858CAGLN41433.326−3.19841.5731.0055.42
ATOM859CBGLN41431.991−3.90441.3431.0055.44
ATOM860CGGLN41431.645−4.93342.3911.0056.07
ATOM861CDGLN41430.203−5.37642.3361.0057.40
ATOM862OE1GLN41429.296−4.53642.4021.0060.22
ATOM863NE2GLN41429.973−6.66442.1991.0057.27
ATOM864CGLN41433.850−2.63040.2591.0055.51
ATOM865OGLN41434.654−3.26539.5781.0056.16
ATOM866NGLY41533.398−1.43039.9101.0057.07
ATOM867CAGLY41533.849−0.80638.6801.0058.51
ATOM868CGLY41535.350−0.58238.6891.0061.10
ATOM869OGLY41536.023−0.74837.6711.0059.47
ATOM870NLYS41635.877−0.21139.8511.0062.77
ATOM871CALYS41637.3050.04140.0111.0065.49
ATOM872CBLYS41637.6340.26241.4911.0066.04
ATOM873CGLYS41638.1211.66341.8231.0068.71
ATOM874CDLYS41637.0782.43942.6131.0070.98
ATOM875CELYS41637.4042.44844.1001.0071.84
ATOM876NZLYS41636.2252.07944.9331.0071.95
ATOM877CLYS41638.159−1.10539.4721.0066.41
ATOM878OLYS41639.361−0.94639.2691.0067.15
ATOM879NCYS41737.538−2.25739.2381.0067.33
ATOM880CACYS41738.270−3.41438.7411.0068.16
ATOM881CBCYS41737.951−4.64239.6021.0070.88
ATOM882SGCYS41738.592−4.54941.3011.0076.09
ATOM883CCYS41738.015−3.73637.2701.0067.54
ATOM884OCYS41738.632−4.65336.7201.0068.48
ATOM885NVAL41837.111−2.99436.6311.0064.67
ATOM886CAVAL41836.817−3.22635.2181.0059.97
ATOM887CBVAL41835.326−2.91734.8791.0059.60
ATOM888CG1VAL41834.971−1.50335.2841.0059.13
ATOM889CG2VAL41835.072−3.12133.3911.0054.85
ATOM890CVAL41837.739−2.36234.3551.0058.37
ATOM891OVAL41837.799−1.14034.5121.0055.44
ATOM892NGLU41938.463−3.01233.4501.0056.02
ATOM893CAGLU41939.403−2.32832.5701.0054.28
ATOM894CBGLU41940.149−3.35131.7101.0057.57
ATOM895CGGLU41939.385−3.77930.4681.0060.87
ATOM896CDGLU41940.179−4.72229.5841.0063.34
ATOM897OE1GLU41940.432−5.87030.0111.0064.90
ATOM898OE2GLU41940.546−4.31328.4621.0063.18
ATOM899CGLU41938.761−1.28131.6621.0052.05
ATOM900OGLU41937.665−1.48131.1311.0049.82
ATOM901NGLY42039.465−0.16531.4911.0049.45
ATOM902CAGLY42038.9830.90830.6421.0046.22
ATOM903CGLY42037.8951.76731.2541.0044.55
ATOM904OGLY42037.4172.70530.6191.0042.08
ATOM905NMET42137.5031.47132.4881.0043.41
ATOM906CAMET42136.4492.24833.1231.0042.48
ATOM907CBMET42135.3061.32733.5541.0042.34
ATOM908CGMET42134.5900.63532.3961.0038.22
ATOM909SDMET42132.9270.10232.8431.0038.56
ATOM910CEMET42132.0031.69932.7661.0035.54
ATOM911CMET42136.9233.05934.3121.0041.64
ATOM912OMET42136.1133.51235.1111.0039.77
ATOM913NVAL42238.2323.25634.4301.0043.42
ATOM914CAVAL42238.7574.01935.5571.0044.79
ATOM915CBVAL42240.2854.24835.4331.0046.54
ATOM916CG1VAL42240.5955.08634.2061.0048.25
ATOM917CG2VAL42240.8134.92036.6961.0046.24
ATOM918CVAL42238.0565.37235.6891.0044.09
ATOM919OVAL42237.6915.78336.7831.0044.12
ATOM920NGLU42337.8466.05534.5701.0042.07
ATOM921CAGLU42337.1927.35634.6161.0040.24
ATOM922CBGLU42337.9098.33833.6841.0044.02
ATOM923CGGLU42339.4118.46733.8931.0050.04
ATOM924CDGLU42340.0969.15832.7191.0055.64
ATOM925OE1GLU42339.53910.15632.2051.0056.66
ATOM926OE2GLU42341.1888.70332.3061.0058.02
ATOM927CGLU42335.7047.33734.2501.0035.77
ATOM928OGLU42334.8817.95534.9191.0033.20
ATOM929NILE42435.3456.61733.1971.0036.16
ATOM930CAILE42433.9496.64332.7711.0031.63
ATOM931CBILE42433.8036.08731.3471.0033.58
ATOM932CG2ILE42434.6396.93630.3951.0033.48
ATOM933CG1ILE42434.2044.61731.2961.0034.46
ATOM934CD1ILE42433.8573.95529.9781.0034.67
ATOM935CILE42432.8906.03533.6851.0028.89
ATOM936OILE42431.7296.44333.6321.0026.49
ATOM937NPHE42533.2615.09134.5421.0029.26
ATOM938CAPHE42532.2574.52035.4471.0029.87
ATOM939CBPHE42532.9033.52936.4231.0031.26
ATOM940CGPHE42531.9482.49636.9591.0032.17
ATOM941CD1PHE42531.1242.78338.0481.0033.70
ATOM942CD2PHE42531.8811.23036.3811.0030.64
ATOM943CE1PHE42530.2441.81438.5631.0032.60
ATOM944CE2PHE42531.0100.25636.8811.0031.55
ATOM945CZPHE42530.1890.54937.9731.0033.34
ATOM946CPHE42531.5945.64936.2401.0030.17
ATOM947OPHE42530.3685.77436.2761.0026.71
ATOM948NASP42632.4156.48336.8701.0029.45
ATOM949CAASP42631.8937.58737.6611.0032.29
ATOM950CBASP42633.0318.29138.4011.0033.49
ATOM951CGASP42633.4557.54639.6551.0039.42
ATOM952OD1ASP42632.7676.57440.0381.0038.35
ATOM953OD2ASP42634.4807.93440.2561.0039.58
ATOM954CASP42631.1338.59236.8061.0029.02
ATOM955OASP42630.1549.17537.2571.0031.34
ATOM956NMET42731.5858.79735.5721.0030.69
ATOM957CAMET42730.9199.73634.6751.0028.63
ATOM958CBMET42731.7449.91233.4071.0026.83
ATOM959CGMET42733.03210.68033.6081.0031.41
ATOM960SDMET42733.96210.78332.0771.0034.87
ATOM961CEMET42735.40911.75332.6431.0044.60
ATOM962CMET42729.5269.20234.3241.0028.70
ATOM963OMET42728.5369.94734.3021.0025.01
ATOM964NLEU42829.4517.90234.0571.0025.13
ATOM965CALEU42828.1737.29233.7301.0027.60
ATOM966CBLEU42828.3795.82433.3321.0028.00
ATOM967CGLEU42829.0395.68231.9571.0026.99
ATOM968CD1LEU42829.6784.30331.7821.0027.80
ATOM969CD2LEU42827.9955.92730.8941.0025.33
ATOM970CLEU42827.2107.41234.9161.0029.59
ATOM971OLEU42826.0417.74334.7431.0027.07
ATOM972NLEU42927.7017.14736.1261.0030.40
ATOM973CALEU42926.8597.25137.3231.0030.59
ATOM974CBLEU42927.6756.88438.5711.0031.76
ATOM975CGLEU42928.0785.41538.7571.0032.43
ATOM976CD1LEU42928.9615.26439.9951.0031.60
ATOM977CD2LEU42926.8254.57338.9031.0034.66
ATOM978CLEU42926.3198.68137.4661.0030.46
ATOM979OLEU42925.1438.90137.7691.0028.40
ATOM980NALA43027.1939.65637.2371.0031.34
ATOM981CAALA43026.80611.05937.3321.0029.83
ATOM982CBALA43028.01711.95137.0781.0031.29
ATOM983CALA43025.69611.38736.3441.0031.04
ATOM984OALA43024.75312.10736.6741.0030.79
ATOM985NTHR43125.80210.85435.1281.0030.30
ATOM986CATHR43124.78611.10534.1121.0028.81
ATOM987CBTHR43125.20710.53332.7371.0030.55
ATOM988OG1THR43126.56910.89332.4651.0031.88
ATOM989CG2THR43124.32111.08731.6341.0025.63
ATOM990CTHR43123.46210.48134.5301.0029.49
ATOM991OTHR43122.40211.09934.3971.0026.18
ATOM992NSER43223.5209.25335.0371.0028.11
ATOM993CASER43222.3088.57335.4801.0029.78
ATOM994CBSER43222.6397.17736.0081.0033.11
ATOM995OGSER43221.4546.41236.1361.0036.92
ATOM996CSER43221.6519.39936.5891.0031.49
ATOM997OSER43220.4339.57636.6131.0030.09
ATOM998NASER43322.4769.90137.4960.7532.09
ATOM999NBSER43322.4749.90637.5000.2531.10
ATOM1000CAASER43322.00210.71538.6050.7535.68
ATOM1001CABSER43321.98510.71738.6080.2532.21
ATOM1002CBASER43323.18511.09739.5020.7537.18
ATOM1003CBBSER43323.14511.10439.5290.2531.45
ATOM1004OGASER43322.82312.09040.4430.7544.09
ATOM1005OGBSER43323.7859.95340.0530.2529.52
ATOM1006CASER43321.29911.97138.0910.7535.01
ATOM1007CBSER43321.29511.97638.0920.2532.88
ATOM1008OASER43320.25712.37338.6120.7535.34
ATOM1009OBSER43320.26412.39138.6220.2533.42
ATOM1010NARG43421.86712.57937.0541.0033.38
ATOM1011CAARG43421.30013.78836.4701.0034.19
ATOM1012CBARG43422.23914.35435.4001.0033.89
ATOM1013CGARG43421.67015.52834.6251.0038.30
ATOM1014CDARG43421.55916.78735.4791.0037.91
ATOM1015NEARG43421.15817.94434.6801.0037.78
ATOM1016CZARG43420.48818.99535.1491.0041.06
ATOM1017NH1ARG43420.13219.04936.4281.0040.70
ATOM1018NH2ARG43420.17519.99834.3371.0038.78
ATOM1019CARG43419.93713.49135.8731.0033.48
ATOM1020OARG43418.99614.26636.0531.0030.54
ATOM1021NPHE43519.83112.37135.1581.0034.68
ATOM1022CAPHE43518.56311.96334.5491.0035.02
ATOM1023CBPHE43518.72710.63433.7961.0034.96
ATOM1024CGPHE43519.24010.77932.3861.0037.63
ATOM1025CD1PHE43519.45912.03531.8241.0042.03
ATOM1026CD2PHE43519.5219.64931.6231.0041.24
ATOM1027CE1PHE43519.95312.16430.5211.0043.11
ATOM1028CE2PHE43520.0169.76830.3221.0040.59
ATOM1029CZPHE43520.23311.02929.7751.0040.63
ATOM1030CPHE43517.52711.78035.6571.0035.49
ATOM1031OPHE43516.36112.13535.4961.0034.78
ATOM1032NARG43617.96811.21636.7771.0038.27
ATOM1033CAARG43617.09410.98237.9241.0040.67
ATOM1034CBARG43617.84410.21539.0121.0040.70
ATOM1035CGARG43616.9429.59040.0681.0044.98
ATOM1036CDARG43617.6488.45940.8101.0048.09
ATOM1037NEARG43618.9828.84141.2751.0050.16
ATOM1038CZARG43620.1198.36140.7771.0052.19
ATOM1039NH1ARG43620.0997.47239.7901.0049.34
ATOM1040NH2ARG43621.2838.77041.2661.0051.85
ATOM1041CARG43616.57612.30238.4931.0040.40
ATOM1042OARG43615.38212.45838.7301.0041.49
ATOM1043NMET43717.47713.25238.7061.0040.02
ATOM1044CAMET43717.09014.54639.2451.0041.02
ATOM1045CBMET43718.32915.42739.4401.0040.29
ATOM1046CMET43716.09915.22138.2991.0040.81
ATOM1047OMET43715.11115.80538.7341.0042.46
ATOM1048NMET43816.36715.12737.0011.0039.02
ATOM1049CAMET43815.51015.73235.9881.0040.11
ATOM1050CBMET43816.23715.79334.6511.0038.16
ATOM1051CGMET43817.35216.79434.6011.0041.52
ATOM1052SDMET43817.99916.86232.9431.0043.94
ATOM1053CEMET43816.69817.74832.0961.0039.96
ATOM1054CMET43814.22114.96435.7831.0037.72
ATOM1055OMET43813.30515.45135.1251.0036.82
ATOM1056NASN43914.15513.75936.3371.0038.81
ATOM1057CAASN43912.98112.91936.1741.0040.77
ATOM1058CBASN43911.76213.55636.8471.0044.52
ATOM1059CGASN43910.56612.62036.8871.0048.29
ATOM1060OD1ASN43910.72111.40036.9641.0048.48
ATOM1061ND2ASN4399.36513.18936.8291.0050.23
ATOM1062CASN43912.72512.74434.6771.0039.36
ATOM1063OASN43911.63713.03734.1721.0037.76
ATOM1064NLEU44013.74912.27433.9721.0037.65
ATOM1065CALEU44013.65512.05232.5321.0035.22
ATOM1066CBLEU44014.99911.57631.9871.0034.70
ATOM1067CGLEU44015.02211.46730.4621.0035.45
ATOM1068CD1LEU44014.89012.86229.8691.0035.24
ATOM1069CD2LEU44016.29710.79529.9991.0035.30
ATOM1070CLEU44012.58711.02432.1961.0036.48
ATOM1071OLEU44012.5189.96732.8261.0037.36
ATOM1072NGLN44111.76311.32831.1971.0036.82
ATOM1073CAGLN44110.69610.42030.7851.0038.51
ATOM1074CBGLN4419.43111.21130.4431.0038.23
ATOM1075CGGLN4418.91212.06331.5921.0042.46
ATOM1076CDGLN4418.36211.22732.7291.0044.91
ATOM1077OE1GLN4417.26810.66832.6291.0047.31
ATOM1078NE2GLN4419.11911.13233.8181.0044.06
ATOM1079CGLN44111.0999.56529.5851.0038.48
ATOM1080OGLN44111.9239.97628.7631.0035.80
ATOM1081NGLY44210.5008.37829.4941.0036.03
ATOM1082CAGLY44210.7927.46828.4011.0037.72
ATOM1083CGLY44210.5998.11227.0431.0036.88
ATOM1084OGLY44211.3817.87726.1231.0033.72
ATOM1085NGLU4439.5568.92526.9181.0036.59
ATOM1086CAGLU4439.2699.60325.6611.0037.13
ATOM1087CBGLU4437.95610.37925.7641.0041.57
ATOM1088CGGLU4436.7239.48825.8791.0047.76
ATOM1089CDGLU4436.4839.00827.3021.0053.96
ATOM1090OE1GLU4435.6198.12327.4981.0057.66
ATOM1091OE2GLU4437.1599.51528.2251.0056.13
ATOM1092CGLU44310.40810.55125.3111.0035.27
ATOM1093OGLU44310.75910.70424.1451.0033.85
ATOM1094NGLU44410.98411.17926.3311.0032.09
ATOM1095CAGLU44412.09712.09526.1261.0033.92
ATOM1096CBGLU44412.33212.92427.3881.0034.97
ATOM1097CGGLU44411.16913.84527.7321.0038.28
ATOM1098CDGLU44411.38314.61029.0231.0038.11
ATOM1099OE1GLU44411.80013.99330.0261.0039.53
ATOM1100OE2GLU44411.13215.83429.0361.0040.77
ATOM1101CGLU44413.35611.30525.7701.0033.59
ATOM1102OGLU44414.08511.67024.8421.0033.35
ATOM1103NPHE44513.59010.21526.5011.0030.68
ATOM1104CAPHE44514.7539.35726.2761.0032.49
ATOM1105CBPHE44514.7038.13927.2031.0029.35
ATOM1106CGPHE44515.6677.04726.8281.0030.78
ATOM1107CD1PHE44517.0367.20127.0301.0028.25
ATOM1108CD2PHE44515.2055.86326.2661.0030.62
ATOM1109CE1PHE44517.9336.19526.6751.0028.67
ATOM1110CE2PHE44516.0954.84825.9081.0031.37
ATOM1111CZPHE44517.4605.01526.1131.0030.37
ATOM1112CPHE44514.8508.88524.8291.0031.11
ATOM1113OPHE44515.9248.94724.2211.0032.20
ATOM1114NVAL44613.7398.41524.2661.0028.63
ATOM1115CAVAL44613.7877.94322.8891.0027.94
ATOM1116CBVAL44612.4787.19322.4781.0028.48
ATOM1117CG1VAL44612.3185.93923.3431.0029.61
ATOM1118CG2VAL44611.2658.09222.6071.0027.23
ATOM1119CVAL44614.0999.06421.9001.0027.28
ATOM1120OVAL44614.7818.83720.9041.0028.07
ATOM1121NCYS44713.61910.27522.1661.0028.97
ATOM1122CACYS44713.91911.39421.2721.0029.14
ATOM1123CBCYS44713.15612.65321.6931.0028.90
ATOM1124SGCYS44711.38912.59121.3091.0035.68
ATOM1125CCYS44715.42011.67721.3281.0028.03
ATOM1126OCYS44716.06311.88520.3021.0029.34
ATOM1127NLEU44815.96911.68622.5381.0027.28
ATOM1128CALEU44817.39211.93822.7291.0025.30
ATOM1129CBLEU44817.73311.93224.2201.0027.72
ATOM1130CGLEU44817.24813.13525.0401.0029.54
ATOM1131CD1LEU44817.80713.04226.4541.0030.85
ATOM1132CD2LEU44817.68814.43424.3761.0030.24
ATOM1133CLEU44818.24510.90222.0081.0027.62
ATOM1134OLEU44819.20711.25221.3271.0025.10
ATOM1135NLYS44917.9059.62122.1621.0025.16
ATOM1136CALYS44918.6738.57021.5061.0027.55
ATOM1137CBLYS44918.1357.18521.9001.0028.99
ATOM1138CGLYS44919.1346.05221.6941.0034.70
ATOM1139CDLYS44918.7374.78922.4591.0032.67
ATOM1140CELYS44917.2674.41922.2201.0031.87
ATOM1141NZLYS44917.0222.96722.4721.0029.14
ATOM1142CLYS44918.6268.74919.9901.0025.88
ATOM1143OLYS44919.6108.48919.2961.0025.93
ATOM1144NSER45017.4829.19719.4801.0026.07
ATOM1145CASER45017.3239.42118.0521.0027.24
ATOM1146CBSER45015.8579.70517.7211.0032.24
ATOM1147OGSER45015.0988.51917.7791.0034.94
ATOM1148CSER45018.17610.60717.6181.0026.78
ATOM1149OSER45018.76310.59816.5351.0025.85
ATOM1150NILE45118.23111.63218.4631.0026.94
ATOM1151CAILE45119.03212.81018.1551.0026.13
ATOM1152CBILE45118.95013.85019.2911.0027.72
ATOM1153CG2ILE45120.01914.92919.1011.0020.53
ATOM1154CG1ILE45117.55314.47519.3221.0029.49
ATOM1155CD1ILE45117.37715.47320.4471.0036.24
ATOM1156CILE45120.48912.38117.9891.0024.88
ATOM1157OILE45121.16112.77117.0341.0026.96
ATOM1158NILE45220.97711.58218.9311.0022.72
ATOM1159CAILE45222.35911.12018.8801.0021.95
ATOM1160CBILE45222.66010.15520.0501.0023.57
ATOM1161CG2ILE45223.9829.43519.8041.0022.10
ATOM1162CG1ILE45222.71810.94921.3711.0021.70
ATOM1163CD1ILE45222.76810.06022.6241.0025.30
ATOM1164CILE45222.65610.41917.5571.0023.02
ATOM1165OILE45223.65010.70816.8851.0021.25
ATOM1166NLEU45321.7799.49717.1731.0022.83
ATOM1167CALEU45321.9848.76815.9351.0022.05
ATOM1168CBLEU45320.8437.76415.7331.0022.06
ATOM1169CGLEU45320.7127.18914.3241.0022.03
ATOM1170CD1LEU45321.8156.16514.1071.0024.81
ATOM1171CD2LEU45319.3286.53514.1561.0024.73
ATOM1172CLEU45322.0929.68714.7171.0023.95
ATOM1173OLEU45322.9629.50113.8601.0024.60
ATOM1174NLEU45421.22010.68714.6381.0026.72
ATOM1175CALEU45421.23411.59913.4941.0026.45
ATOM1176CBLEU45419.85212.24213.3301.0025.51
ATOM1177CGLEU45418.73711.22213.0521.0030.16
ATOM1178CD1LEU45417.40511.92612.9551.0028.76
ATOM1179CD2LEU45419.03710.47811.7591.0032.59
ATOM1180CLEU45422.29212.70313.5521.0028.24
ATOM1181OLEU45422.77813.14812.5131.0029.06
ATOM1182NASN45522.63813.14614.7571.0026.56
ATOM1183CAASN45523.60414.23614.9341.0026.79
ATOM1184CBASN45523.28414.99816.2241.0026.20
ATOM1185CGASN45524.17416.21716.4191.0027.26
ATOM1186OD1ASN45524.17117.13415.6021.0030.83
ATOM1187ND2ASN45524.93116.23017.5061.0027.16
ATOM1188CASN45525.06213.78214.9541.0030.63
ATOM1189OASN45525.96514.51714.5251.0027.69
ATOM1190NSER45625.26812.56915.4611.0030.48
ATOM1191CASER45626.57211.92815.5791.0035.26
ATOM1192CBSER45626.39310.39315.5051.0039.69
ATOM1193OGSER45625.8719.95314.2431.0030.73
ATOM1194CSER45627.62712.34414.5621.0035.56
ATOM1195OSER45628.59913.04114.8841.0033.00
ATOM1196NGLY45727.43711.88613.3341.0033.88
ATOM1197CAGLY45728.39312.18912.2921.0036.77
ATOM1198CGLY45727.87613.01711.1361.0037.02
ATOM1199OGLY45728.31012.80510.0131.0038.66
ATOM1200NVAL45826.96713.95611.3921.0039.12
ATOM1201CAVAL45826.43814.80210.3171.0043.81
ATOM1202CBVAL45825.23115.64810.7551.0044.25
ATOM1203CG1VAL45824.20915.7139.6311.0044.51
ATOM1204CG2VAL45824.63815.09812.0131.0050.53
ATOM1205CVAL45827.47215.8019.8171.0046.72
ATOM1206OVAL45827.39116.2658.6811.0047.08
ATOM1207NTYR45928.43216.14410.6701.0050.74
ATOM1208CATYR45929.45617.11410.3011.0055.43
ATOM1209CBTYR45929.64718.12911.4331.0056.62
ATOM1210CGTYR45928.37518.87011.7811.0059.34
ATOM1211CD1TYR45928.09419.22913.0951.0060.73
ATOM1212CE1TYR45926.90019.86713.4291.0062.14
ATOM1213CD2TYR45927.43019.17510.7951.0062.16
ATOM1214CE2TYR45926.23419.81211.1181.0063.83
ATOM1215CZTYR45925.97620.15412.4371.0062.88
ATOM1216OHTYR45924.79020.76412.7671.0062.56
ATOM1217CTYR45930.79116.4899.9281.0057.21
ATOM1218OTYR45931.79317.1899.7981.0056.86
ATOM1219NTHR46030.80015.1739.7501.0059.22
ATOM1220CATHR46032.01814.4749.3661.0062.25
ATOM1221CBTHR46032.50213.53110.4991.0063.07
ATOM1222OG1THR46033.47412.6139.9831.0067.80
ATOM1223CG2THR46031.34412.75911.0841.0060.23
ATOM1224CTHR46031.75913.6788.0861.0063.54
ATOM1225OTHR46032.45712.7087.7821.0063.91
ATOM1226NPHE46130.75814.1137.3261.0065.06
ATOM1227CAPHE46130.39513.4466.0801.0067.00
ATOM1228CBPHE46129.05213.9755.5631.0066.48
ATOM1229CGPHE46127.86713.1475.9911.0066.30
ATOM1230CD1PHE46126.65713.7546.3121.0065.58
ATOM1231CD2PHE46127.96311.7606.0851.0066.41
ATOM1232CE1PHE46125.56212.9966.7231.0065.45
ATOM1233CE2PHE46126.87210.9946.4941.0066.83
ATOM1234CZPHE46125.67011.6166.8141.0065.12
ATOM1235CPHE46131.46313.6045.0041.0068.38
ATOM1236OPHE46132.18114.6064.9621.0068.98
ATOM1237NLEU46231.54212.6014.1321.0069.57
ATOM1238CALEU46232.51112.5453.0391.0071.68
ATOM1239CBLEU46232.08011.4752.0301.0071.00
ATOM1240CLEU46232.81013.8562.3041.0072.40
ATOM1241OLEU46233.72514.5902.6801.0073.45
ATOM1242NSER46332.04314.1411.2531.0073.22
ATOM1243CASER46332.26215.3430.4491.0072.61
ATOM1244CBSER46332.54414.942−1.0051.0073.38
ATOM1245CSER46331.12616.3620.4911.0071.17
ATOM1246OSER46330.45516.5281.5111.0072.05
ATOM1247NSER46430.93217.049−0.6331.0068.86
ATOM1248CASER46429.89218.063−0.7591.0066.06
ATOM1249CBSER46430.51419.457−0.7041.0066.26
ATOM1250CSER46429.10817.887−2.0601.0063.72
ATOM1251OSER46428.65718.862−2.6621.0062.88
ATOM1252NTHR46528.95416.638−2.4931.0060.93
ATOM1253CATHR46528.20516.343−3.7091.0057.47
ATOM1254CBTHR46528.18514.824−4.0041.0057.80
ATOM1255OG1THR46527.52514.135−2.9341.0054.75
ATOM1256CG2THR46529.60614.287−4.1491.0057.49
ATOM1257CTHR46526.76716.824−3.5231.0054.93
ATOM1258OTHR46526.34917.129−2.4071.0054.26
ATOM1259NLEU46626.01316.892−4.6141.0051.85
ATOM1260CALEU46624.62517.330−4.5501.0049.25
ATOM1261CBLEU46624.01317.349−5.9561.0048.74
ATOM1262CGLEU46622.95318.415−6.2531.0048.72
ATOM1263CD1LEU46622.15618.002−7.4821.0048.32
ATOM1264CD2LEU46622.03318.594−5.0571.0048.14
ATOM1265CLEU46623.81716.397−3.6501.0048.16
ATOM1266OLEU46622.96116.845−2.8831.0045.90
ATOM1267NLYS46724.09315.099−3.7501.0046.47
ATOM1268CALYS46723.39914.100−2.9471.0047.45
ATOM1269CBLYS46723.80212.693−3.3951.0049.38
ATOM1270CGLYS46722.82911.602−2.9741.0052.70
ATOM1271CDLYS46723.56110.301−2.6821.0056.48
ATOM1272CELYS46723.1059.180−3.6041.0059.54
ATOM1273NZLYS46724.1508.117−3.7321.0061.22
ATOM1274CLYS46723.73814.284−1.4721.0046.89
ATOM1275OLYS46722.88414.108−0.6041.0046.06
ATOM1276NSER46824.98914.644−1.2021.0045.82
ATOM1277CASER46825.45714.8540.1601.0046.82
ATOM1278CBSER46826.97615.0500.1731.0047.85
ATOM1279OGSER46827.40715.5371.4351.0055.73
ATOM1280CSER46824.77816.0630.7901.0044.24
ATOM1281OSER46824.47316.0621.9831.0042.98
ATOM1282NLEU46924.54717.100−0.0111.0042.33
ATOM1283CALEU46923.89018.3010.4861.0040.42
ATOM1284CBLEU46924.00219.427−0.5451.0044.47
ATOM1285CGLEU46925.43819.874−0.8491.0046.70
ATOM1286CD1LEU46925.51420.477−2.2461.0046.70
ATOM1287CD2LEU46925.89020.8830.1991.0047.32
ATOM1288CLEU46922.42317.9960.7861.0039.06
ATOM1289OLEU46921.85618.5051.7601.0034.97
ATOM1290NGLU47021.81417.151−0.0461.0035.46
ATOM1291CAGLU47020.41816.7680.1451.0034.38
ATOM1292CBGLU47019.91415.963−1.0521.0038.02
ATOM1293CGGLU47019.77216.773−2.3291.0042.67
ATOM1294CDGLU47019.33915.923−3.5091.0048.30
ATOM1295OE1GLU47019.67114.716−3.5381.0050.53
ATOM1296OE2GLU47018.66616.463−4.4121.0051.06
ATOM1297CGLU47020.29015.9161.4031.0034.37
ATOM1298OGLU47019.32116.0352.1571.0032.60
ATOM1299NGLU47121.27415.0461.6061.0034.66
ATOM1300CAGLU47121.30914.1622.7661.0035.68
ATOM1301CBGLU47122.51513.2222.6711.0034.57
ATOM1302CGGLU47122.37612.1221.6141.0037.98
ATOM1303CDGLU47121.47610.9892.0631.0039.79
ATOM1304OE1GLU47120.26811.0271.7431.0041.12
ATOM1305OE2GLU47121.97410.0612.7371.0032.11
ATOM1306CGLU47121.39314.9834.0521.0034.79
ATOM1307OGLU47120.59614.7934.9691.0032.80
ATOM1308NLYS47222.35815.8984.1121.0033.93
ATOM1309CALYS47222.51816.7395.2911.0035.58
ATOM1310CBLYS47223.68317.7105.0971.0039.11
ATOM1311CGLYS47225.05017.0505.1381.0041.47
ATOM1312CDLYS47226.08017.9575.7941.0046.97
ATOM1313CELYS47227.44517.2865.8621.0048.40
ATOM1314NZLYS47227.85016.7024.5471.0051.55
ATOM1315CLYS47221.23717.5235.5821.0034.78
ATOM1316OLYS47220.79517.6076.7241.0033.95
ATOM1317NASP47320.64318.0974.5451.0033.47
ATOM1318CAASP47319.42018.8654.7201.0034.63
ATOM1319CBASP47318.92319.4043.3801.0037.21
ATOM1320CGASP47317.65420.2213.5221.0043.24
ATOM1321OD1ASP47316.55919.6873.2301.0045.20
ATOM1322OD2ASP47317.75021.3963.9321.0045.59
ATOM1323CASP47318.33917.9985.3381.0032.93
ATOM1324OASP47317.64218.4166.2641.0032.87
ATOM1325NHIS47418.19916.7844.8271.0032.74
ATOM1326CAHIS47417.18515.8825.3431.0032.21
ATOM1327CBHIS47417.18514.5754.5681.0032.79
ATOM1328CGHIS47416.04713.6754.9241.0036.22
ATOM1329CD2HIS47414.71113.8134.7501.0038.33
ATOM1330ND1HIS47416.22712.4565.5421.0038.97
ATOM1331CE1HIS47415.05311.8835.7321.0037.99
ATOM1332NE2HIS47414.11612.6865.2611.0037.43
ATOM1333CHIS47417.40315.5736.8151.0029.74
ATOM1334OHIS47416.46015.5437.5961.0029.90
ATOM1335NILE47518.65315.3267.1851.0027.80
ATOM1336CAILE47518.97115.0148.5711.0025.61
ATOM1337CBILE47520.47814.7088.7201.0025.59
ATOM1338CG2ILE47520.87714.71310.1931.0027.17
ATOM1339CG1ILE47520.78713.3418.0921.0026.17
ATOM1340CD1ILE47522.25813.0717.8491.0027.07
ATOM1341CILE47518.57616.2019.4601.0027.91
ATOM1342OILE47517.92816.03810.4851.0029.16
ATOM1343NHIS47618.95617.4049.0541.0029.41
ATOM1344CAHIS47618.62118.5759.8461.0029.73
ATOM1345CBHIS47619.34219.7969.2811.0032.27
ATOM1346CGHIS47620.77719.8679.6991.0039.44
ATOM1347CD2HIS47621.35519.70710.9151.0039.81
ATOM1348ND1HIS47621.80920.0678.8081.0039.79
ATOM1349CE1HIS47622.95920.0279.4561.0039.98
ATOM1350NE2HIS47622.71219.80910.7351.0040.26
ATOM1351CHIS47617.12018.8109.9481.0031.40
ATOM1352OHIS47616.63619.33610.9511.0029.79
ATOM1353NARG47716.37418.3968.9291.0031.82
ATOM1354CAARG47714.92918.5708.9561.0031.53
ATOM1355CBARG47714.34318.3767.5571.0034.95
ATOM1356CGARG47714.42519.6276.7001.0040.46
ATOM1357CDARG47713.69819.4455.3701.0045.22
ATOM1358NEARG47714.10720.4564.3991.0053.05
ATOM1359CZARG47713.64721.7054.3761.0055.89
ATOM1360NH1ARG47712.75622.1065.2741.0056.17
ATOM1361NH2ARG47714.08422.5583.4571.0059.49
ATOM1362CARG47714.31017.5829.9311.0030.70
ATOM1363OARG47713.36017.90310.6491.0030.24
ATOM1364NVAL47814.86316.3759.9721.0029.67
ATOM1365CAVAL47814.35115.36910.8871.0029.68
ATOM1366CBVAL47814.93713.97510.5751.0032.01
ATOM1367CG1VAL47814.46112.97311.6091.0032.93
ATOM1368CG2VAL47814.50613.5289.1691.0031.00
ATOM1369CVAL47814.69615.77412.3161.0029.81
ATOM1370OVAL47813.86015.67713.2201.0030.25
ATOM1371NLEU47915.92916.23212.5161.0028.81
ATOM1372CALEU47916.36016.67413.8361.0028.74
ATOM1373CBLEU47917.79917.21013.7791.0026.65
ATOM1374CGLEU47918.91016.15213.8531.0026.05
ATOM1375CD1LEU47920.23116.77213.3951.0025.81
ATOM1376CD2LEU47919.02815.60315.2771.0025.34
ATOM1377CLEU47915.41117.77714.3131.0029.54
ATOM1378OLEU47914.99717.78615.4721.0029.00
ATOM1379NASP48015.07618.70313.4151.0031.52
ATOM1380CAASP48014.16219.80013.7411.0033.84
ATOM1381CBASP48013.94320.71212.5281.0034.37
ATOM1382CGASP48015.05521.74312.3451.0036.26
ATOM1383OD1ASP48015.11922.35411.2571.0036.56
ATOM1384OD2ASP48015.86021.95113.2741.0034.19
ATOM1385CASP48012.81819.22214.1741.0033.48
ATOM1386OASP48012.18619.72415.1051.0033.89
ATOM1387NLYS48112.37918.16113.4981.0033.90
ATOM1388CALYS48111.10617.53613.8391.0032.97
ATOM1389CBLYS48110.71916.48912.7841.0034.66
ATOM1390CLYS48111.16416.89515.2251.0033.57
ATOM1391OLYS48110.16716.86915.9431.0035.37
ATOM1392NILE48212.32816.37715.6071.0032.71
ATOM1393CAILE48212.45715.76416.9221.0031.60
ATOM1394CBILE48213.74314.91317.0281.0032.65
ATOM1395CG2ILE48213.87714.33818.4301.0032.50
ATOM1396CG1ILE48213.69713.78515.9951.0032.72
ATOM1397CD1ILE48214.97812.96915.9081.0033.37
ATOM1398CILE48212.45616.85317.9941.0031.69
ATOM1399OILE48211.94616.64919.0971.0029.98
ATOM1400NTHR48313.02718.01217.6791.0031.33
ATOM1401CATHR48313.02219.10918.6441.0031.71
ATOM1402CBTHR48313.75620.35118.1091.0032.92
ATOM1403OG1THR48315.11120.01217.7881.0029.99
ATOM1404CG2THR48313.75621.45219.1601.0030.47
ATOM1405CTHR48311.55919.48318.9201.0032.85
ATOM1406OTHR48311.14619.59820.0701.0031.83
ATOM1407NASP48410.78519.65617.8511.0031.91
ATOM1408CAASP4849.36920.00317.9651.0034.15
ATOM1409CBASP4848.70820.01316.5911.0037.41
ATOM1410CGASP4849.27021.08015.6801.0042.02
ATOM1411OD1ASP4849.87122.04516.1981.0043.26
ATOM1412OD2ASP4849.10620.95214.4451.0042.49
ATOM1413CASP4848.65718.98518.8401.0033.16
ATOM1414OASP4847.83019.33919.6761.0034.86
ATOM1415NTHR4858.99617.71518.6461.0033.91
ATOM1416CATHR4858.39616.63519.4141.0034.41
ATOM1417CBTHR4858.87515.26818.8851.0033.58
ATOM1418OG1THR4858.40015.09417.5421.0037.04
ATOM1419CG2THR4858.34714.13819.7511.0030.89
ATOM1420CTHR4858.70816.75720.9031.0035.15
ATOM1421OTHR4857.81816.60021.7441.0031.99
ATOM1422NLEU4869.96617.04621.2291.0033.77
ATOM1423CALEU48610.36817.19222.6211.0034.31
ATOM1424CBLEU48611.87917.44822.7211.0032.00
ATOM1425CGLEU48612.77616.20122.7541.0034.99
ATOM1426CD1LEU48614.23316.61322.5211.0032.65
ATOM1427CD2LEU48612.63515.48124.1051.0029.90
ATOM1428CLEU4869.59718.34823.2561.0034.87
ATOM1429OLEU4869.07818.22524.3621.0035.85
ATOM1430NILE4879.51319.46922.5481.0035.59
ATOM1431CAILE4878.78720.62523.0641.0036.79
ATOM1432CBILE4878.89021.82622.0951.0037.32
ATOM1433CG2ILE4877.83322.88422.4431.0040.19
ATOM1434CG1ILE48710.29222.44322.1811.0036.00
ATOM1435CD1ILE48710.63523.04123.5441.0033.58
ATOM1436CILE4877.31520.25723.2761.0038.56
ATOM1437OILE4876.70820.62824.2821.0038.52
ATOM1438NHIS4886.74919.52122.3261.0040.33
ATOM1439CAHIS4885.35719.09622.4271.0042.29
ATOM1440CBHIS4884.96218.28221.1971.0044.26
ATOM1441CGHIS4883.61217.64721.3051.0047.75
ATOM1442CD2HIS4882.36918.17521.2141.0047.46
ATOM1443ND1HIS4883.44016.29821.5341.0051.09
ATOM1444CE1HIS4882.14816.02321.5771.0051.15
ATOM1445NE2HIS4881.47717.14421.3851.0050.22
ATOM1446CHIS4885.15418.25423.6851.0042.55
ATOM1447OHIS4884.23318.49824.4671.0043.02
ATOM1448NLEU4896.02217.26623.8791.0039.91
ATOM1449CALEU4895.93616.39925.0481.0039.93
ATOM1450CBLEU4897.08715.39625.0481.0038.83
ATOM1451CGLEU4896.96114.24224.0561.0039.31
ATOM1452CD1LEU4898.25913.45624.0271.0039.01
ATOM1453CD2LEU4895.79913.34524.4591.0041.98
ATOM1454CLEU4895.97317.20326.3391.0040.24
ATOM1455OLEU4895.26716.88827.2981.0038.72
ATOM1456NMET4906.79818.24626.3531.0039.94
ATOM1457CAMET4906.93919.10227.5221.0041.50
ATOM1458CBMET4908.20819.95327.3941.0039.15
ATOM1459CGMET4909.49519.16927.6081.0041.69
ATOM1460SDMET49010.97820.10627.1611.0035.76
ATOM1461CEMET49012.17818.77527.0561.0039.22
ATOM1462CMET4905.71820.00427.7171.0042.33
ATOM1463OMET4905.29620.25828.8481.0041.09
ATOM1464NALA4915.16220.49826.6161.0043.15
ATOM1465CAALA4913.98321.35126.6931.0043.79
ATOM1466CBALA4913.62221.87925.3111.0043.93
ATOM1467CALA4912.84120.51027.2511.0046.16
ATOM1468OALA4912.07320.96728.0951.0044.69
ATOM1469NLYS4922.75219.26826.7831.0046.29
ATOM1470CALYS4921.71118.35127.2221.0049.90
ATOM1471CBLYS4921.77217.05326.4111.0050.03
ATOM1472CGLYS4921.08717.13525.0621.0053.81
ATOM1473CDLYS492−0.00216.08424.9301.0059.00
ATOM1474CELYS492−0.98816.45323.8271.0061.85
ATOM1475NZLYS492−1.35115.28122.9761.0062.89
ATOM1476CLYS4921.84118.02528.7011.0051.15
ATOM1477OLYS4920.84517.78429.3791.0053.37
ATOM1478NALA4933.07218.01229.1991.0050.15
ATOM1479CAALA4933.32117.70630.6001.0049.17
ATOM1480CBALA4934.77717.31430.7941.0050.39
ATOM1481CALA4932.97118.88531.5011.0049.36
ATOM1482OALA4933.08918.79932.7231.0051.57
ATOM1483NGLY4942.55419.98930.8931.0048.61
ATOM1484CAGLY4942.18521.15931.6711.0046.92
ATOM1485CGLY4943.32222.10732.0061.0045.46
ATOM1486OGLY4943.20622.92132.9191.0043.58
ATOM1487NLEU4954.43122.00931.2841.0044.81
ATOM1488CALEU4955.55522.89931.5401.0042.34
ATOM1489CBLEU4956.84722.29330.9881.0043.79
ATOM1490CGLEU4957.71221.45931.9361.0040.99
ATOM1491CD1LEU4957.02220.15632.2601.0044.70
ATOM1492CD2LEU4959.07221.18931.2701.0042.12
ATOM1493CLEU4955.27824.22730.8471.0042.13
ATOM1494OLEU4954.66424.25829.7781.0042.49
ATOM1495NTHR4965.71825.32431.4521.0042.73
ATOM1496CATHR4965.52126.63630.8451.0043.56
ATOM1497CBTHR4965.84127.76731.8291.0046.09
ATOM1498OG1THR4967.22227.68832.2081.0043.92
ATOM1499CG2THR4964.96527.66233.0641.0045.63
ATOM1500CTHR4966.47126.76429.6601.0045.54
ATOM1501OTHR4967.37025.93929.4881.0043.39
ATOM1502NLEU4976.28027.80028.8491.0045.02
ATOM1503CALEU4977.13528.02027.6881.0045.12
ATOM1504CBLEU4976.71029.28626.9441.0046.62
ATOM1505CGLEU4975.93329.08025.6401.0050.20
ATOM1506CD1LEU4975.88630.39724.8751.0050.95
ATOM1507CD2LEU4976.58927.99024.7981.0050.91
ATOM1508CLEU4978.59928.13528.1011.0044.94
ATOM1509OLEU4979.47427.51627.4931.0045.03
ATOM1510NGLN4988.86228.92729.1371.0041.14
ATOM1511CAGLN49810.22129.10129.6271.0040.54
ATOM1512CBGLN49810.24630.14030.7431.0043.82
ATOM1513CGGLN49811.58530.27031.4371.0043.37
ATOM1514CDGLN49811.53931.26032.5841.0047.03
ATOM1515OE1GLN49810.56531.30833.3321.0049.18
ATOM1516NE2GLN49812.59132.05432.7271.0045.30
ATOM1517CGLN49810.77727.77330.1451.0039.39
ATOM1518OGLN49811.92327.42229.8661.0035.05
ATOM1519NGLN4999.96527.04030.9021.0036.49
ATOM1520CAGLN49910.39125.74831.4341.0036.91
ATOM1521CBGLN4999.31425.15532.3441.0038.84
ATOM1522CGGLN4999.15525.82533.7031.0041.33
ATOM1523CDGLN4998.03925.18734.5121.0042.74
ATOM1524OE1GLN4997.02724.76033.9551.0045.44
ATOM1525NE2GLN4998.22225.10735.8291.0043.48
ATOM1526CGLN49910.65524.77330.2851.0035.03
ATOM1527OGLN49911.44623.83230.4221.0036.59
ATOM1528NGLN5009.98024.99429.1621.0034.14
ATOM1529CAGLN50010.13624.13827.9901.0034.65
ATOM1530CBGLN5009.04224.43626.9581.0033.90
ATOM1531CGGLN5007.67223.87227.3151.0036.62
ATOM1532CDGLN5006.55824.41926.4351.0040.17
ATOM1533OE1GLN5006.66024.41725.2071.0040.22
ATOM1534NE2GLN5005.48224.88627.0641.0041.82
ATOM1535CGLN50011.51124.35027.3581.0034.96
ATOM1536OGLN50012.25623.38727.1241.0030.79
ATOM1537N