WO2006117592A1

WO2006117592A1 - Methods of modulating nuclear receptors

Info

Publication number: WO2006117592A1
Application number: PCT/IB2005/001493
Authority: WO
Inventors: Jérôme FAGART; Marie-Edith Oblin; Jessica Huyet; Gregory Pinon
Original assignee: Inserm
Priority date: 2005-04-29
Filing date: 2005-04-29
Publication date: 2006-11-09

Abstract

The present invention relates to novel compositions, methods and tools for modulating nuclear receptor function. More particularly, the invention discloses the identification of the crystal structure of nuclear receptors and the atomic interface with ligands thereof. The invention allows the design, identification or selection of novel candidate modulators of nuclear receptors, which may be used in the pharmaceutical industry. The invention also discloses novel nuclear receptor constructs, recombinant vectors, cells and methods for producing the same in high amounts, as well as their use to produce antibodies, ligands or crystals thereof. The invention is particularly suited for developing modulators of mineralocorticoid receptors, which may be used for treating various disorders, including hypertension.

Description

METHODS OF MODULATING NUCLEAR RECEPTORS

The present invention relates to novel compositions, methods and tools for modulating nuclear receptor function. More particularly, the invention discloses the identification of the crystal structure of nuclear receptors and the atomic interface with ligands thereof. The invention allows the design, identification or selection of novel candidate modulators of nuclear receptors, which maybe used in the pharmaceutical industry. The invention also discloses novel nuclear receptor constructs, recombinant vectors, cells and methods for producing the same in high amounts, as well as their use to produce antibodies, ligands or crystals thereof. The invention is particularly suited for developing modulators of mineralocorticoid receptors, which may be used for treating various disorders, including hypertension.

Background

The human mineralocorticoid receptor (MR) belongs to a family of ligand-activated transcription factors that includes other steroid, retinoid and Vitamin D receptors, as well as orphan receptors. These receptors have a common modular structure, with three major functional domains : the N-terminal region contains a constitutive transactivation function, the central DNA-binding domain, composed of zinc-finger domains, is involved in DNA binding and receptor dimerization, and the C-terminal region, which contains the Ligand-Binding Domain (LBD) is involved in several important functions, including nuclear localization, interaction with heat-shock protein hsp90, and ligand- dependent activation (Pinon et al., MoI. Cell. Endocrinol., 2004, 217, 181-188). The MR receptor is involved in several important metabolic pathways, including the reabsorption of sodium and the control of blood pressure. As a result, a number of agonists or antagonists of the MR have been disclosed and studied in the art for their therapeutic activity, including aldosterone (the natural ligand), progesterone, spironolactone and cortisone. MR antagonists are mainly used as antihypertensive agents in the treatment of essential hypertension. They improve survival in heart failure, and have beneficial effects in preventing the development of cardiac fibrosis and renal damage in patients with essential hypertension. These compounds are also used to treat primary aldosteronism. However, although existing MR antagonists such as spironolactone are effective MR blockers, they also have some undesirable side effects since they bind other receptors, such as the progesterone receptor. Furthermore, considering the nature and low stability of the MR, the precise activation mechanism of this receptor has not been fully described or explained in the art. Moreover, while various homology models have been proposed in the art, no clear description of the ligand-receptor interactions have been disclosed, and there is no method available in the art to design specific ligands of the MR.

Summary of the Present Invention

The present invention discloses, for the first time, the crystal structures of the LBD of MR associated with various ligands thereof. These structures, the first to be reported for MR, identify the specific contacts between the LBD and MR ligands, clarify the mechanism of activation of this receptor and allow, for the first time, the design or screening or identification of specific ligands of the MR. The invention also provides constructs and compounds suitable for screening a candidate MR modulator. The invention also provides improved methods of producing MR LBD polypeptides, which may be used to generate antibodies, to screen ligands, or for further crystallization.

An object of the present invention thus resides in isolated or purified complexes comprising a MR LBD polypeptide and a ligand thereof.

Another object of this invention resides in a crystalline complex comprising a MR LBD polypeptide and a ligand thereof.

A further object of this invention relates to any polypeptide comprising a MR LBD polypeptide sequence fused to a tag. As will be further disclosed below, the MR LBD polypeptide sequence and the tag may be fused directly or through a linker sequence, which preferably comprises a cleavage domain. Furthermore, the MR LBD polypeptide is preferably a human wild-type or mutant MR LBD polypeptide. An other object of this invention lies in a polypeptide comprising a mutated human MR LBD sequence, wherein the mutated MR LBD comprises a mutation selected from N770A, Q776A, S810L, S810M, R817A, M852A C910A, T945A and any combinations thereof.

An other object of this invention is an isolated polypeptide comprising a MR LBD polypeptide sequence comprising amino acid residues 737-984 of SEQ ID NO: 1 or a mutant thereof, more preferably amino acid residues 731-984 of SEQ ID NO: 1 or a mutant thereof, wherein said polypeptide does not contain amino acid residues 1-730 of a MR polypeptide sequence.

The invention also relates to any nucleic acid encoding a polypeptide as defined above, as well as any vector comprising such a nucleic acid and any recombinant cell comprising such a nucleic acid or vector.

A further aspect of this invention relates to methods of producing a MR LBD polypeptide, comprising:

(a) culturing a recombinant cell as disclosed above under conditions allowing expression to occur, and (b) collecting the polypeptide from the cell.

Li a particular aspect, this invention relates to methods of producing a MR LBD polypeptide, comprising:

(a) culturing a cell comprising a recombinant nucleic acid encoding a MR LBD polypeptide fused to a tag, under conditions allowing expression to occur,

(b) collecting the polypeptide from the cell, and

(c) optionally, separating the MR LBD polypeptide from the tag.

hi a particular embodiment of the above method, the cell is cultured in the presence of a MR ligand, and a complex of the MR LBD polypeptide and the ligand is collected. Preferably, the cell is a prokaryotic cell, more preferably an E. coli strain. A further object of this invention is a method for preparing a crystalline complex comprising a MR LBD polypeptide and a ligand thereof, the method comprising:

(a) providing a solution comprising a MR LBD polypeptide and a ligand thereof, the MR LBD polypeptide preferably being recombinant, more preferably produced by a method as disclosed above,

(b) crystallizing the polypeptide, and

(c) providing a crystalline complex diffracting X-ray to a resolution of about 3 A or better.

The invention also relates to the use of a polypeptide or of a complex as defined above for drug design or screening.

An other object of this invention resides in the use of a polypeptide or of a complex as defined above for the production of an anti MR antibody.

The invention also relates to any antibody that binds an epitope comprised in a polypeptide or in a complex as defined above. The antibody may be a polyclonal antibody, a monoclonal antibody, or a fragment or derivative thereof. Such antibodies may be used for instance for detecting or dosing the MR in any sample, in vitro, ex vivo or in vivo, for purification purposes, or as binding reagents in binding experiments.

A further object of this invention resides in methods for identifying, characterizing, screening or optimizing MR ligands, the method comprising contacting a candidate compound in vitro with a polypeptide or a complex as defined above, and determining the ability of said candidate compound to bind the MR LBD domain of said polypeptide or complex.

In a particular aspect, the invention relates to methods for identifying, characterizing, screening or optimizing MR ligands, the method comprising contacting a candidate compound in vitro with a recombinant cell as defined above, more preferably a comprising a recombinant nucleic acid encoding a MR LBD polypeptide fused to a tag, under conditions allowing expression of the MR LBD polypeptide in said cell, and assessing the production of a complex between the MR LBD polypeptide and the candidate compound. The formation of said complex can be assessed by determining the presence of soluble MR LBD polypeptides in said culture.

The invention also relates to methods for identifying a MR modulator, comprising: (a) providing a computerized modeling system comprising atomic coordinates of a MR LBD polypeptide complex,

(b) designing a compound that fits spatially into the binding pocket of the MR LBD, and

(c) optionally testing the capacity of the compound to bind to a MR polypeptide and/or modulate the activity thereof.

The invention also resides in methods for producing a candidate MR modulator, comprising:

(a) providing a computerized modeling system comprising atomic coordinates of a MR LBD polypeptide complex,

(b) synthesizing a compound that fits spatially into the binding pocket of the MR LBD, and

The method may be used for identifying or producing specific MR modulators, including agonists or antagonists thereof. The atomic coordinates preferably comprise the atomic coordinates of Table 1 or Table 2.

The invention also encompasses the use of a compound produced by a method as defined above, for the manufacture of a medicament for use in the treatment of a human subject, in particular for regulating blood pressure. The invention also encompasses corresponding methods of treatment, comprising administering to a subject in need thereof an effective amount of a compound produced by a method as defined above. More preferably, MR antagonists compounds produced by the present invention can be used as anti-hypertensive agents, e.g., to treat, prevent or alleviate essential hypertension, heart failure (in particular to improve survival in heart failure), cardiac fibrosis, primary aldosteronism or renal damages in patients with hypertension. MR agonists compounds produced by the present invention can be used to treat or prevent or alleviate for instance adrenal gland diseases (Addison's disease).

A further object of this invention resides in the use of a compound selected from 5α- pregnan-20-one and a derivative thereof for the manufacture of an anti-progestin medicament. The invention also encompasses corresponding methods of inducing anti- progestin activity in a subject, comprising administering to a subject in need thereof an effective amount of a compound selected from 5α-pregnan-20-one or a derivative thereof. More preferably, the medicament or method may be used to treat, prevent or alleviate emergency contraception, long term estrogen-free contraception, and proliferative endometrium diseases such as myomas and endometriosis. The derivatives include 5α-pregnan-20-one compounds comprising a side chain at one or several different positions of the steroid skeleton, namely at the position C7, CIl, Cl 5, Cl 8 or Cl 9. Such side chains may be hydrophobic or polar, unsaturated or saturated, aromatic or aliphatic, linear or not, or a combination thereof.

Detailed Description of the Present Invention

MR LBD polypeptides or sequences

The present invention now discloses and provides MR polypeptides, in purified or isolated form, either alone or in complexes with ligands, which may be used in many applications, such as to produce antibodies, to screen or validate MR ligands, and/or to produce MR crystals.

More particularly, the invention relates to any polypeptide comprising a MR LBD polypeptide sequence fused to a tag. The invention also relates to polypeptides comprising a mutated human MR LBD sequence, wherein the mutated MR LBD comprises a mutation selected from N770A, Q776A, S810L, S810M, R817A, M852A C910A, T945A and any combinations thereof.

Within the context of this invention, a "MR LBD" polypeptide designates any amino acid molecule or sequence comprising a functional ligand-binding domain of a mineralocorticoid receptor, i.e., a LBD domain that retains the ability to bind MR ligands. In a preferred embodiment, the MR LBD polypeptide is a human wild-type or mutant MR LBD polypeptide, i.e., comprises the amino acid sequence of a functional LBD of a human mineralocorticoid receptor. The amino acid sequence of an exemplary wild type human MR is depicted in SEQ ID NO: 1 (Access number in the Swiss-Prot bank: P08235), in which residues 1-602 represent the N-terminal domain ; residues 603- 669 represent the DNA-binding domain ; residues 670-736 represent the Hinge region and residues 737-984 represent the Ligand-binding domain (on the basis of the crystal structure). In a specific embodiment, a MR LBD polypeptide sequence of the present invention comprises amino acid residues 737-984 of SEQ ID NO: 1 or a variant and/or mutant thereof, more preferably amino acid residues 731-984 of SEQ ID NO: 1 or a variant and/or mutant thereof.

The term "variant" designates any naturally-occurring variants of a MR polypeptide, including SNPs, splicing variants, truncated forms, etc.

The term "mutant" designates any polypeptide comprising one or several amino acid modifications, including one or several amino acid substitution(s), deletion(s) or insertion(s). In a preferred embodiment, the term "mutant" designates MR LBD sequences comprising between 1 and 5 amino acid modifications, more preferably between 1 and 4, even more preferably, 1, 2 or 3 amino acid modifications. Specific examples of such mutants include MR LBD polypeptides comprising a mutation selected from N770A, Q776A, S810L, S810M, R817A, M852A C910A, T945A and any combinations thereof.

In this respect, the invention now discloses that the C910A mutation enables the crystallization of the MR LBD polypeptide, by increasing the stability and productivity of the polypeptide. Furthermore, the C910A mutation does not affect the ability of the mutated MR LBD polypeptide to bind MR ligands. Accordingly, the invention relates to any MR polypeptide or MR LBD comprising the mutation C91 OA or any other mutation resulting in the replacement of cysteine residue 910 by an other amino acid residue devoid of free SH group. The invention more specifically relates to a functional human MR polypeptide or MR LBD comprising a mutation resulting in the replacement of cysteine residue 910 by an other amino acid residue devoid of free SH group. As discussed above, the polypeptides of this invention may include a combination of mutations, such as S810L and C910X, X being any amino acid residue devoid of free SH group, preferably an alanine residue.

In a specific embodiment, the invention relates to an isolated polypeptide comprising a MR LBD polypeptide sequence comprising amino acid residues 737-984 of SEQ ID NO: 1 or a variant or mutant thereof, more preferably amino acid residues 731-984 of SEQ ID NO: 1 or a variant or mutant thereof, wherein said polypeptide does not contain amino acid residues 1-730 of a MR polypeptide sequence. In a specific embodiment, the MR LBD polypeptide sequence comprises a mutation selected from N770A, Q776A, S810L, S810M, R817A, M852A C910A, T945A and any combinations thereof.

As indicated above, the polypeptides of this invention may comprise additional amino acid residues, which may be heterologous to a MR polypeptide sequence (i.e., not found in a naturally-occurring MR polypeptide, or arranged in a different manner). In particular, the invention provides polypeptides comprising a MR LBD polypeptide sequence fused to a tag. The tag may be located at any end of the polypeptide, i.e., N- or

C-terminal end, or inserted within the LBD domain. Preferably, the tag is located at one (or both) terminal ends of the MR LBD polypeptide sequence. Furthermore, the MR

LBD polypeptide sequence and the tag may be fused directly to each other, or, more preferably, through a linker sequence, which preferably comprises a cleavage domain.

The tag may be any amino acid domain conferring on the polypeptide additional property(ies), such as stability, solubility, conformation, ease of purification, etc. Examples of such tags include, for instance, GST, Thioredoxin, Maltose binding protein (MBP) and a polyHis (comprising e.g., from 3 to 8 consecutive histidine residues), which may be used in combination(s).

In a specific embodiment, the invention relates to a polypeptide comprising a MR LBD polypeptide sequence and a GST sequence, the GST sequence being fused directly or through a linker to the N-terminus of the MR LBD polypeptide sequence. In an other specific embodiment, the invention relates to a polypeptide comprising a MR LBD polypeptide sequence and a polyHis sequence, the polyHis sequence being fused directly or through a linker to the N- or C-terminus of the MR LBD polypeptide sequence.

In an other specific embodiment, the invention relates to a polypeptide comprising a MR LBD polypeptide sequence and a MBP sequence, the MBP sequence being fused directly or through a linker to the N- or C-terminus of the MR LBD polypeptide sequence.

In a specific embodiment, the invention relates to a polypeptide comprising a MR LBD polypeptide sequence and a thioredoxin sequence, the thioredoxin sequence being fused directly or through a linker to the N- or C-terminus of the MR LBD polypeptide sequence. In a specific embodiment, the polypeptide further comprises a polyHis tag.

The above polypeptides may be produced by various techniques known per se in the art, such as by recombinant techniques, artificial synthesis or combinations thereof. Improved production methods using recombinant techniques will be disclosed below.

In this regard, the invention also relates to any nucleic acid encoding a polypeptide as defined above. The nucleic acid may be DNA (e.g., cDNA) or RNA (e.g., mRNA), and may be single- or double-stranded. The nucleic acid may be in isolated form, or included in a cloning and/or expression vector. In this respect, the invention also relates to a recombinant vector comprising a nucleic acid molecule as defined above. The vector may be a plasmid, cosmid, phage, viral vector, artificial chromosome, etc. The vector may be either replicating or integrative. Examples of preferred vectors include phages and plasmids, which are available in the art. The vector may comprise any regulatory elements, such as a promoter, origin of replication, selection gene, etc. Specific examples of such vectors are disclosed in the experimental section, and represent particular objects of this invention. Production of MR LBD Polypeptides

A further aspect of this invention relates to methods of producing a MR LBD polypeptide as disclosed above. A typical production method comprises: (a) culturing a recombinant cell as disclosed above under conditions allowing expression to occur, and

(b) collecting the polypeptide from the cell.

The MR LBD polypeptides are typically produced within the cell, and their collection preferably involves a prior step of releasing the polypeptides from the cell, e.g., by altering the cell membranes (e.g., cell lysis).

In a particular aspect, this invention relates to methods of producing a MR LBD polypeptide, comprising: (a) culturing a cell comprising a recombinant nucleic acid encoding a MR LBD polypeptide fused to a tag, under conditions allowing expression to occur,

(b) collecting the polypeptide from the cell, and

(c) optionally, separating the MR LBD polypeptide from the tag.

The cell may be any eukaryotic or prokaryotic cell, such as a yeast cell, plant cell, insect cell, mammalian cell or a bacterial cell. Preferably, the cell is a prokaryotic cell, more preferably an E. coli strain. The polypeptide may be collected by any suitable means or process, including centrifugation, filtration, affinity separation, chromatography, gel migration, etc. In a particular embodiment, the polypeptide is purified or collected based on the presence of the tag moiety, e.g., by affinity using a tag-specific ligand. Upon collection (or prior to collecting the polypeptides), the MR LBD polypeptide may be separated from the tag by any convenient means, i.e., by chemical, enzymatic or physical cleavage. Where the polypeptide comprises a linker sequence containing a cleavage site, the MR LBD polypeptide is conveniently separated from the tag by use of a specific reagent that cleaves said site.

A specific example of a linker sequence to be used in the present invention is SerAspLeuValProArgGlySer, that contains the thrombin cleavage site (LeuValProArgGlySer). Upon contacting the polypeptide with thrombin, two fragments are generated, tag-SerAspLeuValProArg on the one hand and GlySer-MR LBD on the other hand. Other linker sequences may be found in the literature, such as for instance Factor Xa (IleGluGlyAsp); prescission protease (LeuGluValLeuPheGlnGlyPro) and Enterokinase (AspAspAspAspLys).

In a particular embodiment of the above method, the cell is cultured in the presence of a MR ligand. In such embodiment, a complex of the MR LBD polypeptide and the ligand is formed and collected. Such an embodiment is particularly advantageous since applicants have now discovered that the presence of the ligand greatly stabilized the MR LBD polypeptide, and facilitates the production and collection thereof. In a particular embodiment, the process is conducted by adding the ligand early in the culture, e.g., at the beginning of the production phase. The ligand may be any MR agonist or antagonist.

As used herein, the term "agonist" has its general meaning in the art. In particular an agonist means an agent that supplements or potentiates the bioactivity of a functional protein or polypeptide. By way of specific example, an "agonist" is a compound that interacts with MR, mutated or not, to promote a transcriptional response. An agonist can induce changes in a receptor that place the receptor in an active conformation, allowing the receptor to influence transcription, either positively or negatively. There can be several different ligand-induced changes in the receptor's conformation. The term "agonist" specifically encompasses partial agonists. As used herein, the term "partial agonist" means an entity that can bind to a receptor and induce only part of the changes in the receptor or other target that are induced by agonists. The differences can be qualitative or quantitative. Thus, a partial agonist can induce some of the conformation changes induced by agonists, but not others, or it can only induce certain changes to a limited extent.

As used herein, the term "antagonist" has its general meaning in the art. In particular an "antagonist" means an agent that decreases or inhibits the bioactivity of a functional protein or polypeptide. By way of specific example, an "antagonist" is a compound that interacts with MR, mutated or not, to inhibit a transcriptional response. An antagonist can bind to a receptor but fails to induce conformational changes that alter the receptor's transcriptional regulatory properties or physiologically relevant conformations. Binding of an antagonist can also block the binding, and therefore the actions, of an agonist. The term "antagonist" specifically encompasses partial antagonists. As used herein, the term "partial antagonist" means an entity that can bind to a receptor or other target and inhibit only part of the changes in the receptor or other target that are induced by antagonists. The differences can be qualitative or quantitative. Thus, a partial antagonist can inhibit some of the conformation changes induced by an antagonist, but not others, or it can inhibit certain changes to a limited extent.

Examples of MR agonists include, for instance aldosterone, Cortisol and deoxycorticosterone. Examples of MR antagonist include for instance progesterone, spironolactone and cortisone. The ligand may by any known or selected MR ligand, for which a complex with the MR LBD is sought. Alternatively, the ligand may be a candidate ligand, whose ability to form a complex with the MR LBD is to be assessed. Such embodiment will be disclosed later.

The polypeptides or complexes of the present invention may be efficiently used to produce MR crystals, anti-MR antibodies or MR ligands.

Production of MR crystals

As discussed above, a further object of this invention is a method for preparing a crystalline complex comprising a MR LBD polypeptide and a ligand thereof, the method comprising:

(a) providing a solution comprising a MR LBD polypeptide and a ligand thereof,

(b) crystallizing the polypeptide, and

The MR LBD polypeptide of step (a) is preferably a recombinant polypeptide, even more preferably produced by a method as disclosed above. Most preferably, step (a) uses a complex of a MR LBD polypeptide and a ligand as produced by a method as disclosed above.

The complex is preferably crystallized using the vapor diffusion method. In this regard, it is preferred to use a reservoir solution comprising HEPES or PIPES, pH 6.5 to 7.5, 200-300 mM NaCl and 15 to 30% PEG4000. The complex preferably crystallizes in the space group of P3₁ or P3₂ and diffracts X-ray to a resolution of about 2.5 A or better, most preferably about 2 Å or better.

An other object of this invention resides in a crystalline complex comprising a MR LBD polypeptide and a ligand thereof. The crystalline complex preferably has a space group of P3₁ or P3₂ and/or a resolution of about 2.5 A or better. The ligand may be any MR ligand as discussed above.

In a specific embodiment, the invention provides a crystalline MR LBD-S810L-C910A complexed with DOC, progesterone or with spironolactone and a crystalline MR LBD- C910A complexed with DOC, which are characterized by any one of the features of Table 3 and 4, or a combination thereof.

In a further specific embodiment, the invention provides a crystalline MR LBD-S810L- C910A complexed with DOC or with progesterone, which is characterized by the atomic structural coordinates of Table 1 or Table 2, respectively.

Aldosterone, the main mineralocorticoid hormone, plays a key role in the reabsorption of sodium, and is involved in controlling blood pressure (Bonvalet et al., Kidney Int. Suppl., 1998, 65, S49-56). Its effects are mediated by the mineralocorticoid receptor (MR), a ligand-activated transcription factor belonging to the nuclear receptor superfamily (Evans et al., Science, 1988, 240, 889-895). Crystallographic and in-vitro studies of numerous nuclear receptors have suggested that, in the absence of ligand, the lower portion of the LBD that surrounds the ligand-binding cavity is rather dynamic, and may exhibit some of the properties of a molten globule. Binding an agonist ligand compacts the LBD by establishing numerous stabilizing polar and hydrophobic contacts, thus stabilizing the C-terminal H12 helix in its active conformation, which in turn promotes coactivator binding (Nagy et al., Trends Biochem. Sci., 2004, 29, 317- 324). Mutagenesis analyses based on three-dimensional models of the LBD of MR have highlighted the contact between Asn770 and the 21-hydroxyl group of aldosterone as being crucial for stabilizing the receptor in its active form (Fagart et al., EMBO J., 1998, 17, 3317-3325). Conversely it has been proposed that the antagonist character of progesterone is attributable to its inability to establish contact with Asn770 (Fagart et al., EMBO J., 1998, 17, 3317-3325). Recently, a missense mutation (S810L) in the LBD of MR has been detected in a severe form of hypertension (Geller et al., Science, 2000, 289, 119-123). In-vitro experiments have revealed that the S810L mutation within the human MR completely changes the response of the receptor to antagonist ligands. Progesterone, which acts as an antagonist when bound to the wild type (WT) MR, fully activates MR-S810L (Geller et al., Science, 2000, 289, 119-123).

To identify the steroid-receptor contacts involved in the activation of MR-S810L, the MR LBD-S810L-C910A was crystallized in complexes with progesterone and with DOC, an agonist of both WT and mutant receptors, that differs from progesterone by having a hydroxyl group at the 21 position (Table 1-3, Fig. 1-3). The structures of both MR-S 81OL complexes, the first MR structures to be reported, contain 11 α-helices and 4 small β-strands assembled into the canonical 3 layers α-helical structure of nuclear receptors (Nagy et al., Trends Biochem. Sci., 2004, 29, 317-324) (Fig. 4). In particular, the C-terminal Hl 2 helix that harbors the AF2 activation function is folded back towards the core of the domain in the active conformation. When these MR LBD- S810L-C910A crystal structures were superimposed over those of other steroid receptors in their agonist conformation (Brzozowski et al., Nature, 1997, 389, 753-758; Williams et al., Nature, 1998, 393, 392-396; Matias et al., J. Biol. Chem., 2000, 275, 26164-26171; Sack et al., Proc. Natl. Acad. Sci. U. S. A., 2001, 98, 4904-4909; Bledsoe et al., Cell, 2002, 110, 93-105; Kauppi et al., J. Biol. Chem., 2003, 278, 22748-22754), the secondary structure elements matched closely (Fig. 4).

The crystal structures reported here clearly identify the contacts involved in the interaction between MR LBD-S810L-C910A and progesterone. The C3 -ketone function at the A-ring of progesterone is hydrogen bonded to the highly conserved residues Gln776 and Arg817 (Fig. 2). The C20-ketone group at the D-ring is C- H-O hydrogen- bonded to the Ca atom of Cys942. The structure unambiguously shows that the Cδ- methyl groups of Leu810 form short contacts with the C19-methyl group of progesterone (3.6 A) and with Gln776 (3.0 A) (Fig. 2). The structure also reveals a distance of 4.3 A between Ala773 and Leu810, ruling out the hypothesis based on homology modeling that the stabilizing contact between H3 and H5 helices occurs via these two amino acids (Geller et al., Science, 2000, 289, 119-123). The structure also revealed that progesterone does not establish the hydrogen bond with Asn770, proposed by Pinon et al. (Pinon et al., MoI. Cell. Endocrinol., 2004, 217, 181-188). The network of contacts created by Leu810 at the A-ring is sufficient to stabilize the progesterone/MR LBD-S810L-C910A complex in its active state. Indeed, replacing Gln776 or Arg817 by an alanine within MR-S810L (MR-S810L-Q776A; MR-S810L- R817A) ten fold lowers the affinity of the receptor for progesterone (Fig. 5 a) and completely abolishes the ability of progesterone to activate MR-S810L (Fig. 6a). The antagonist property of progesterone was restored as it is able to inhibit the aldosterone induced-activity of MR-S810L-Q776A and MR-S810L-R817A (Fig. 6b). The hypothesis that the network of contacts at the A-ring, created by Leu810, is responsible for the progesterone-induced MR-S810L activation is strengthened by the observation that 5α-pregnane-20-one, a progesterone derivative lacking the C3 -ketone moiety, displays antagonist properties when bound to MR S810L (Pinon et al., MoI. Cell. Endocrinol., 2004, 217, 181-188).

Within the MR LBD-S810L-C910A, DOC adopts a position very similar to that of progesterone, as revealed when the structures are superimposed (Fig. 2). AU the contacts observed in the progesterone/MR LBD-S810L-C910A complex are present in the DOC/MR LBD-S810L-C910A complex. The network of contacts at the A-ring created by Leu810 is present, as well as the hydrogen bond between the C20-ketone function and Cys942. Interestingly, an additional network of hydrogen bonds has been identified in the DOC/MR LBD-S810L-C910A complex. The C21-hydroxyl group of DOC establishes two strong hydrogen bonds with Asn770 and Thr945 (Fig. 1 and 2). The contact between the C21-hydroxyl group and Asn770 has been shown to be determinant for MR activation (Fagart et al., EMBO J., 1998, 17, 3317-3325). This contact must also be of crucial importance in stabilizing the aldosterone/MR-S810L complex in its active state. Indeed, despite a slight lower affinity (Fig. 5b), aldosterone retains its agonist character when Gln776 or Arg817 are replaced by an alanine within MR-S810L (Fig. 6a). It is likely that the network of contacts at the A-ring strengthens the stability of the aldosterone/MR-S810L complex, since this complex is more stable than the one formed with the WT receptor (Pinon et al., MoI. Cell. Endocrinol., 2004, 217, 181-188).

Thus, the crystal structures reported here and the mutagenesis analyses allowed us to conclude that two distinct networks of contacts are involved in stabilizing MR-S810L in its active state. How far each is implicated depends on the structure of the steroids. The activation of MR-S 81OL by 21-hydroxylated steroids requires contact with Asn770, as described for the WT receptor, whereas activation by steroids lacking the 21-hydroxyl group requires the contacts created by Leu810 at the steroid A-ring.

Antibodies

The invention also relates to any antibody that binds an epitope comprised in a polypeptide or in a complex as defined above. Such antibodies may be used for instance for detecting or dosing the MR in any sample, in vitro, ex vivo or in vivo, for purification purposes, or as binding reagents in binding experiments.

The antibody may be a polyclonal or a monoclonal antibody. Furthermore, the term antibody also includes fragments and derivatives thereof, in particular fragments and derivatives of said monoclonal or polyclonal antibodies having substantially the same antigenic specificity. These include antibody fragments (e.g., Fab, Fab'2, CDRs, etc), humanized antibodies, poly-functional antibodies, Single Chain antibodies (ScFv), etc. These may be produced according to conventional methods, including immunization of an animal and collection of serum (polyclonal) or spleen cells (to produce hybridomas by fusion with appropriate cell lines).

To produce polyclonal antibodies from various species, the antigen is generally combined with an adjuvant (e.g., Freund's adjuvant) and administered to an animal, typically by sub-cutaneous injection. Repeated injections may be performed. Blood samples are collected and immunoglobulins or serum are separated. Monoclonal antibodies may be produced from various species as described for instance in Harlow et al (Antibodies: A laboratory Manual, CSH Press, 1988). Briefly, these methods comprise immunizing an animal with the antigen, followed by a recovery of spleen cells, which are then fused with immortalized cells, such as myeloma cells. The resulting hybridomas produce the monoclonal antibodies and can be selected by limit dilutions to isolate individual clones. Antibodies may also be produced by selection of combinatorial libraries of immunoglobulins, as disclosed for instance in Ward et al (Nature 341 (1989) 544). Fab or F(ab')2 fragments may be produced by protease digestion, according to conventional techniques. Humanized antibodies can be prepared as previously described (Jones 1986; Riechmann 1988).

Preferred antibodies of this invention are prepared by immunization with a MR LBD polypeptide or complex of this invention.

The antibodies may be coupled to heterologous moieties, such as toxins, labels, drugs or other therapeutic agents, covalently or not, either directly or through the use of coupling agents or linkers.

Drug Design and selection

A further object of this invention resides in methods for identifying, characterizing, screening or optimizing MR ligands, using the constructs and methods as disclosed above. More particularly, these screening or validating methods use the polypeptides, complexes or recombinant cells as disclosed above to evaluate the ability of a candidate molecule to bind a MR polypeptide, or use the atomic coordinates obtained from MR crystals to design and produce ligands.

In a first embodiment, the method comprises contacting a candidate compound in vitro with a polypeptide as defined above, and determining the ability of said candidate compound to bind the MR LBD domain of said polypeptide. The polypeptide may be in solution, or immobilized on a support. The binding of a candidate molecule to such polypeptide may be assessed by any technique known per se in the art, such as immunoenzymatic or fluorescent or isotopic techniques, the use of a labeled reference ligand, competition assays, gel migration, etc.

In another embodiment, the method comprises contacting a candidate compound in vitro with a complex as defined above and determining the ability of said candidate compound to displace the binding of the ligand in the MR LBD domain of said complex. Well known techniques in the art can be used for measuring the displacement of said ligand. For example, the dosage of the ligand can be carried out by High

Pressure Liquid Chromatography (HPLC), Fast Protein Liquid Chromatography

(FPLC), filtration, Dextran-Charcoal separation, Hydroxyhapatite chromatography, etc. The complex may be in solution, or immobilized on a support.

In a particular aspect, the invention relates to methods for identifying, characterizing, screening or optimizing MR ligands, the method comprising contacting a candidate compound in vitro with a recombinant cell as defined above, more preferably comprising a recombinant nucleic acid encoding a MR LBD polypeptide fused to a tag, under conditions allowing expression of the MR LBD polypeptide in said cell, and assessing the production of a complex between the MR LBD polypeptide and the candidate compound. The formation of said complex can be assessed by determining the presence of soluble MR LBD polypeptides in said culture.

The invention also relates to methods for identifying a candidate MR modulator, comprising:

(a) providing a computerized modeling system comprising atomic coordinates of a MR LBD polypeptide complex, (b) designing a compound that fits spatially into the binding pocket of the MR

LBD, and

A used herein a "MR modulator" designates any compound, natural or not (e.g., synthetic), that is able to interact with a MR (mutated or not) to modulate a transcriptional response. In a preferred embodiment, said MR modulator is an MR agonist or an MR antagonist. In a particular embodiment the compound is a steroid compound.

As used herein, the term "binding pocket of MR LBD" refers to the cavity within the MR LBD where a ligand of a MR can bind. This cavity can be empty, or can contain water molecules or other molecules from the solvent. The binding pocket generally comprises the region of space encompassed by residues shown in Figure 1. Depending on the structure of the ligand, the "binding pocket of MR LBD" can also include other residues that are unmasked by ligand binding to the MR LBD.

Compounds that fit spatially into the binding pocket may interact, directly or not, with all or a number of amino acid residue(s) involved in said binding pocket, as disclosed above. Alternatively, compounds that fit spatially into the binding pocket may not interact with any such residues but simply fit into said space.

LBD and is able to interact with amino acids in the binding pocket of MR LBD,

(c) synthesizing said compound and,

(d) optionally testing the capacity of the compound to bind to a MR polypeptide and/or modulate the activity thereof.

The invention also relates to any data carrier (e.g., hardware, software, floppy disc, etc.) comprising atomic coordinates of a MR LBD polypeptide complex. The invention also relates to the use of a crystallized complex as defined above to obtain atomic coordinates of a MR LBD polypeptide complex. Therapeutic Utility

The invention allows the design, screening, identification, synthesis or optimisation of MR modulators. More particularly, the invention provides improved methods of producing MR ligands having increased selectivity.

Furthermore, the present invention has discovered and established a level of structural and functional homology between the crystal structures of the LBD of the Progesterone Receptor (PR) and of the MR LBD-S810L-C910A, and can therefore allow the design of novel anti-progestin compounds. PR is characterized by having a methionine residue at the position corresponding to LeuδlO in MR-S810L (Met759 in hPR), and MR Asn770 is conserved in PRs (Asn719 in hPR). The Met759 in PR creates a network of contacts at the progesterone A-ring similar to that of Leu810 in MR-S810L and Asn719 does not form any hydrogen bond with the ligand as it occurs in MR-S 81OL complexed with progesterone (Fig. 7). Superimposition of the structures of the LBDs of PR and MR-S810L-C910A, both complexed with progesterone, reveals a close fit of both ligands and amino acid side chains of the ligand-binding cavity (Fig. 7).

Thus, the invention now allows to propose the use of 5α-pregnan-20-one (compound Pl) as a PR antagonist. 5α-pregnan-20-one is commercially-available from Steraloids (Newport, RI USA) under reference P4230-000 and has the following formula:

Such a compound, as well as derivatives thereof, shall be superior to existing PR antagonists due to the absence of the ketone function at the C3 position, which should increase the selectivity towards the PR. Furthermore, the affinity of this compound for

PR could easily be increased, if necessary, by introducing one or several side chain(s) at different positions of the steroid skeleton, namely at the position C7, C11, C15, C18 or C 19. These side chains are preferably hydrophobic or polar, unsaturated or saturated, aromatic or aliphatic, linear or not, or a combination thereof. As illustrated by e.g., RU486 (mifepristone), the potential clinical applications of progesterone receptor antagonists cover a broad field and are very promising in major public health areas, including emergency contraception, long term estrogen-free contraception, myomas and endometriosis (progesterone receptor antagonists displaying direct antiproliferative effects in the endometrium).

An object of this invention thus resides in the use of a MR modulating compound produced by a method as defined above, for the manufacture of a medicament for use in the treatment of a human subject, in particular for regulating blood pressure. The invention also encompasses corresponding methods of treatment, comprising administering to a subject in need thereof an effective amount of a MR modulating compound produced by a method as defined above. More preferably, MR antagonists compounds produced by the present invention can be used as anti-hypertensive agents, e.g., to treat, prevent or alleviate essential hypertension, heart failure (in particular to improve survival in heart failure), cardiac fibrosis, primary aldosteronism or renal damages in patients with hypertension. MR agonists compounds produced by the present invention can be used to treat or prevent or alleviate for instance adrenal gland diseases (Addison's disease).

A further object of this invention resides in the use of a compound selected from 5α- pregnan-20-one having the following formula:

and a derivative thereof, for the manufacture of an anti-progestin medicament. The invention also encompasses corresponding methods of inducing anti-progestin activity in a subject, comprising administering to a subject in need thereof an effective amount of a compound selected from 5α-pregnan-20-one and a derivative thereof. More preferably, the medicament or method may be used for emergency contraception and long term estrogen-free contraception, and to treat, prevent or alleviate proliferative endometrium diseases such as myomas and endometriosis. The derivatives include 5α- pregnan-20-one compounds comprising a side chain at one or several different positions of the steroid skeleton, namely at the position C7, CIl, C15, C18 or C19. These side chains could be hydrophobic or polar, unsaturated or saturated, aromatic or aliphatic, linear or not, or a combination of them.

The above compounds may be administered according to conventional routes, such as systemic or oral administrations. They may be used at dosages similar to those reported for commercial MR or PR antagonists.

In both therapeutic and prophylactic treatments, the above compounds can be administered in several dosages or as a single dose until a desired response has been achieved. The treatment is typically monitored and repeated dosages can be administered as necessary. Compounds of the invention may be administered according to dosage regimens established whenever activation or inactivation of MR or PR is required.

The daily dosage of the products may be varied over a wide range from 0.01 to 1,000 mg per adult per day. Preferably, the compositions contain 0.01, 0.05, 0.1, 0.5, 1.0, 2.5, 5.0, 10.0, 15.0, 25.0, 50.0, 100, 250 and 500 mg of the active ingredient for the symptomatic adjustment of the dosage to the patient to be treated. A medicament typically contains from about 0.01 mg to about 500 mg of the active ingredient, preferably from 1 mg to about 100 mg of the active ingredient. An effective amount of the drug is ordinarily supplied at a dosage level from 0.0002 mg/kg to about 20 mg/kg of body weight per day, especially from about 0.001 mg/kg to 7 mg/kg of body weight per day. It will be understood, however, that the specific dose level and frequency of dosage for any particular patient may be varied and will depend upon a variety of factors including the activity of the specific compound employed, the metabolic stability, and length of action of that compound, the age, the body weight, general health, sex, diet, mode and time of administration, rate of excretion, drug combination, the severity of the particular condition, and the host undergoing therapy

The above mentioned compounds can be administered in a variety of different ways. Examples include administering a composition containing a pharmaceutically acceptable carrier via oral, intranasal, rectal, topical, intraperitoneal, intravenous, intramuscular, subcutaneous, subdermal, transdermal, and intrathecal methods.

For oral administration, the active ingredient can be administered in solid dosage forms, such as capsules, tablets, and powders, or in liquid dosage forms, such as elixirs, syrups, and suspensions. The active component(s) can be encapsulated in gelatin capsules together with inactive ingredients and powdered carriers, such as glucose, lactose, sucrose, mannitol, starch, cellulose or cellulose derivatives, magnesium stearate, stearic acid, sodium saccharin, talcum, magnesium carbonate. Examples of additional inactive ingredients that may be added to provide desirable color, taste, stability, buffering capacity, dispersion or other known desirable features are red iron oxide, silica gel, sodium lauryl sulfate, titanium dioxide, and edible white ink. Similar diluents can be used to make compressed tablets. Both tablets and capsules can be manufactured as sustained release products to provide for continuous release of medication over a period of hours. Compressed tablets can be sugar coated or film coated to mask any unpleasant taste and protect the tablet from the atmosphere, or enteric-coated for selective disintegration in the gastrointestinal tract. Liquid dosage forms for oral administration can contain coloring and flavoring to increase patient acceptance.

If desired, it is possible to formulate solid or liquid formulations in an enteric-coated or otherwise protected form. In the case of liquid formulations, the formulation can be mixed or simply coadministered with a protectant, such as a liquid mixture of medium chain triglycerides, or the formulation can be filled into enteric capsules (e.g., of soft or hard gelatin, which are themselves optionally additionally enteric coated). Alternatively, solid formulations comprising above mentioned compounds can be coated with enteric materials to form tablets. The thickness of enteric coating on tablets or capsules can vary. Typical thickness range from 0.5 to 4 microns in thickness. The enteric coating may comprise any of the enteric materials conventionally utilized in orally administrable pharmaceutical formulations. Suitable enteric coating materials are known, for example, from Remington's Pharmaceutical Sciences, Mace Publishing Company, Philadelphia, 17th ed. (1985); and Hagars Handbuch der Pharmazeutischen Praxie, Springer Verlag, 4th ed., Vol. 7a (1971).

Compositions prepared for intravenous administration typically contain 100 to 500 ml of sterile 0.9% NaCl or 5% glucose optionally supplemented with a 20% albumin solution and 100 to 500 mg of a polypeptide of the invention. Methods for preparing parenterally administrable compositions are well-known in the art and described in more detail in various sources, including, for example, Remington's Pharmaceutical Science, Mack Publishing, Philadelphia, PA, 17th ed., (1985).

Particularly when the compositions are to be used in vivo, the components used to formulate the pharmaceutical compositions of the present invention are preferably of high purity and are substantially free of potentially harmful contaminants (e.g., at least National Food (NF) grade, generally at least analytical grade, and more typically at least pharmaceutical grade). Moreover, compositions intended for in vivo use are usually sterile. To the extent that a given compound must be synthesized prior to use, the resulting product is typically substantially free of any potentially toxic agents, particularly any endotoxins, which may be present during the synthesis or purification process. Compositions for parental administration are also sterile, substantially isotonic and made under GMP conditions.

Further aspects and advantages of the present invention will be disclosed in the following examples, which should be regarded as illustrative and not limiting the scope of the present application.

Legend to the Figures

Figure 1 Crystal structures of the MR LBD-S810L-C910A. Diagram showing LBD/DOC interactions. Hydrogen bonds and van der Waals interactions are indicated as solid arrows and dashed lines, respectively. The colors of the residue names are based on the LBD structural elements from which they originate. W indicates a water molecule.

Figure 2 Superimposition of the DOC/ and progesterone/MR LBD-S810L-C910A crystal structures. Stereo view showing the superimposition of the ligand-binding pockets of MR LBD-S810L-C910A associated with DOC and with progesterone. The carbon atoms are depicted in light blue and white in the DOC- and progesterone-MR LBD-S810L-C910A complexes, respectively. Only polar and charged residues, and two critical hydrophobic residues are shown. The panel b of the figure was produced using Dino (DINO : Visualizing Structural Biology ( 2002 ) http : //www . dino3d. org) .

Figure 3 Stereo view of the 2Fo-Fc electron density map showing DOC and the surrounding residues in the MR LBD-S810L-C910A binding pocket. The map was calculated at 1.96 A and contoured at Is .

Figure 4 Conservation of the overall fold of the LBD of the steroid receptors. The MR LBD-S810L-C910A (blue) is shown superimposed on those of the androgen (orange), glucocorticoid (pink) and progesterone (yellow) receptors (AR, GR and PR) using the LSQ function in the O package (Jones et al. (1991) Acta Crystallogr. A. 47, 110-119). PDB accession numbers are 1137, 1M2Z and 1A28 for AR, GR and PR, respectively. The secondary structural elements are depicted as ribbons and arrows. The figure was generated using Open PyMoI version 0.93.

Figure 5 Scatchard plot of [³H]progesterone (a) and [³H] aldosterone (b) binding. Mutant MRs were synthesized in-vitro in rabbit reticulocyte lysate. After a three-fold dilution, the lysate was incubated for 4 h at 4°C with increasing concentration of labeled steroid. Bound and Unbound steroids were separated by the dextran-charcoal method.

Figure 6 Transcriptional activation of luciferase activity by mutant MRs in response to aldosterone and progesterone. Transfected HEK-293T cells were exposed for 24 h to increasing concentrations of aldosterone (a, full lines), progesterone alone (a, dashed dotted) or 10^"7 M aldosterone plus increasing concentrations of progesterone (b). Transactivations were determined by luciferase activity, normalized to the internal β- galactosidase control, and expressed as a percentage of the MR-S810L activity at 10^-6 M aldosterone. Each point is the mean ± SEM of three separate experiments.

Figure 7 Superimposition of the ligand-binding pocket of MR LBD-S810L-C910A and PR complexed with progesterone. Only polar and charged residues, and a critical hydrophobic residue are showed. The carbon atoms are depicted in light blue and white for the progesterone/PR LBD and progesterone/MR LBD-S810L-C910A complexes, respectively. The figure was produced using DINO (DINO: Visualizing Structural Biology (2002) http://www.dino3d.org)

Examples

Vectors

The expression plasmid pchMR contains the entire coding sequence of the human MR (Fagart et al., EMBO J., 1998, 17, 3317-3325). The plasmid pchMR-C910A encoding for MR-C910A was constructed from pchMR using the quick-change, site-directed mutagenesis procedure from Stratagene (Amsterdam, The Netherlands) and the primers 5'-ATGGTAACTAAGGCTCCCAACAATTCT-3' (SEQ ID NO: 2) and 5'-CCCAGAATTGTTGGGAGCCTTAGTACCAT-3' (SEQ ID NO: 3) (MWG BIOTECH, Ebersberg, Germany). After sequencing, the Bpu1102I-Afl lI fragment of the resulting MR construct was subcloned into pchMR. The S810L mutation was introduced in the plasmid pchMR-Q776A, pchMR-R817A (Fagart et al., EMBO J., 1998, 17, 3317-3325) and pchMR-C910A using the primers 5'- TCTTGGATGTGTCTATTATCATTTGCC TTGAGCTGG-3' (SEQ ID NO: 4) and 5'- CCAGCTCAAGGCAAATGATAATAGACACATCCAAGA-3' (SEQ ID NO: 5) using the same procedure as above.

Sequence 731-984 from pchMR-S810L-C910A or pchMR-C910A was amplified by PCR using the primers 5'-GCGTGGATCCTCACGAGCGCTCACACCTTCCCCCG-3' (SEQ ID NO: 6) and 5'-

CGCCGAAGCTTTCACTTCCGGTGGAAGTAGAGCGGCTT-3' (SEQ ID NO: 7) and subcloned into the pGEX-KG vector

(http://seq.yeastgenome.org/vectordb/vector_descrip/COMPLETE/PGEXKG.SEQ.html ) at the BamΗl and HindIIl restriction sites and the resulting vectors (pMRLBDL810 and pMRLBD) were sequenced.

The pMRLBDA852 vector containing the M852A and C910A mutations was constructed from the pMRLBD vector using the quick-change, site-directed mutagenesis procedure from Stratagene (Amsterdam, The Netherlands) and the primers 5'-GAACTATGCCAGGGGGCGCACCAAATCAGCCTTC-3' (SEQ ID NO: 8) and 5'-GAAGGCTGATTTGGTGCGCCCCCTGGCATAGTTC-3' (SEQ ID NO: 9) (MWG BIOTECH, Ebersberg, Germany). After sequencing, the BamΗl- HindIIl fragment of the resulting construct was subcloned into pMRLBD.

The pMRLBD, pMRLBDL810 and pMRLBD A852 vectors code for the fusion proteins in which the LBD harboring the C910A mutation (pMRLBD), the S810L and C910A mutations (pMRLBDL810) or the M852A and C910A mutations (pMRLBD A852) was fused at the C-terminus of the Glutathione S-transferase (GST) from Schistosoma Japonicum through the 8 amino acids linker (SerAspLeuValProArgGlySer) that contains the thrombin cleavage site (LeuValProArgGlySer). Action of thrombin generates two fragments (GST-SerAspLeuValProArg and GlySer-MR LBD731-984). The plasmid pFC31Luc contains the mouse mammary tumor virus (MMTV) promoter that drives the luciferase gene (Gouilleux et al., Nucleic Acids Res., 1991, 19, 1563- 1669). The plasmid pcβgal codes for β-galactosidase (Pinon et al., MoI. Cell. Endocrinol., 2004, 217, 181-188).

Steroid-binding characteristics at equilibrium. Mutant MRs were expressed in vitro using the T7-coupled rabbit reticulocyte lysate system (Promega). The reticulocyte lysates were diluted 4-fold with TEGWM buffer (20 mM Tris HCl, 1 mM EDTA, 20 niM sodium tungstate, 1 mM β-mercaptoethanol, 10% glycerol, pH 7.4) and incubated with 3x10^-10 - 3x10^-7M [³H]aldosterone or [³H]progesterone (Amersham) for 3 h at 4°C. Bound and free steroids were separated by the dextran-charcoal method (Fagart et al., EMBO J., 1998, 17, 3317-3325). The change in Bound as a function of Unbound steroid was analyzed as previously described (Claire et al., FEBS Lett., 1978, 88, 295-299), and the dissociation constant at equilibrium, Kd, was calculated. Cultured cells and transfection procedures.

HEK-293T cells were cultured and transfected in high glucose containing Dulbecco's modified essential medium supplemented with 10% (v/v) charcoal stripped and heat- inactivated fetal calf serum (FCS), 25 mM HEPES, 2x non-essential amino acids, 2 mM glutamine, 100 IU/ml penicillin and 100 μg/ml streptomycin at 37°C in a humidified atmosphere with 5% CO₂. Transfection was carried out using the phosphate calcium precipitation method. The phosphate solution, prepared for one T75 flask, contained 2 μg of one of the MR expression vectors, 7 μg pFC31Luc and 1 μg pcβgal in HBS supplemented with 160 mM CaCl₂. Twelve hours after transfection, the cells were replated in twelve-well plates. The steroids (Sigma) were added 24 h after seeding, and the plates then incubated for 24 h. The β-galactosidase (Herbomel et al., Cell, 1984, 39, 653-662) and luciferase (de Wet et al., MoI. Cell. Biol., 1987, 7, 725-737) activities of cell extracts were assayed. To standardize transfection efficiency, the relative light units obtained in the luciferase assay, were divided by the optical density obtained in the β- galactosidase assay. Each point is the mean ± SEM of three separate experiments.

Effect of the C910A and S810L mutations on the MR transactivation activity

The effect of the two mutations (S810L and C910A) on the transactivation of the MR in response to aldosterone has been measured in cotransfection assays. The experimental protocol used was the one described above. In these experiments it was shown that aldosterone or deoxycorticosterone (1 nM) activates MR, MR-S810L, MR-C910A and

MR-S810L-C910A to the same level. Furthermore the experiments show that MR, MR-

S810L, MR-C910A and MR-S810L-C910A are activated by aldosterone in a dose dependent manner and that the aldosterone concentration required to induce 50% of the maximal receptor response was nearly the same (0.1 nM).

Expression and purification.

Expression and purification of the MR LBD-S810L-C910A in complex with DOC. BL21 codon-plus (DE3) RIL stains (Stratagene) transformed using the expression vector pMRLBDL810 were grown at 37°C in 2x LB supplemented with ampicillin (100 μg/ml), choramphenicol (50 μg/ml) and 100 μM DOC, and the expression was induced for 14-16 hours at 15°C by adding 100 μM IPTG. After centrifuging, the cells were disrupted by sonication in a TENGDO buffer (50 mM Tris-HCl, pH 7.5, 5 niM EDTA, 150 mM NaCl, 10% (v/v) glycerol, 100 μM DOC and 0.1% (w/v) n-octyl-β-glucoside). The lysate was centrifuged at 105,000 g for 1 h at 4°C, and the supernatant was loaded onto a 5 ml GSTrap column (Amersham) equilibrated in TENGDO buffer. After washing, the fusion protein was eluted using the loading buffer supplemented with 15 mM reduced glutathione. TENGDO buffer was added to the eluate to give a protein concentration of 1 mg/ml, and thrombin cleavage (20 units/mg fusion protein) was performed overnight at 4° C. The protein mixture was then diluted 5-fold in HGDO buffer (HEPES 10 mM, pH 6.8, 10% (v/v) glycerol, 100 μM DOC and 0.1% (w/v) n- octyl-β-glucoside) loaded onto a UnoSl column (Biorad) and eluted with a NaCl gradient (0 - 500 mM) in HGDO buffer. The fractions containing the LBD were pooled, and concentrated onto a vivaspin concentrator (Vivascience, 6 ml, 10,000 Da of molecular weight cut-off) to a protein content of 8.5 mg/ml.

Expression and purification of the MR LBD-S810L-C910A in complex with progesterone.

BL21 codon-plus (DE3) RIL stains (Stratagene) transformed using the expression vector pMRLBDL810 were grown at 37⁰C in 2x LB supplemented with ampicillin (100 μg/ml), choramphenicol (50 μg/ml) and 100 μM progesterone, and the expression was induced for 14-16 hours at 15°C by adding 100 μM IPTG. After centrifuging, the cells were disrupted by sonication in a TENGPO buffer (50 mM Tris-HCl, pH 7.5, 5 mM EDTA, 150 mM NaCl, 10% (v/v) glycerol, 100 μM progesterone and 0.1% (w/v) n- octyl-β-glucoside). The lysate was centrifuged at 105,000 g for 1 h at 4°C, and the supernatant was loaded onto a 5 ml GSTrap column (Amersham) equilibrated in TENGPO buffer. After washing, the fusion protein was eluted using the loading buffer supplemented with 15 mM reduced glutathione. TENGPO buffer was added to the eluate to give a protein concentration of 1 mg/ml, and thrombin cleavage (20 units/mg fusion protein) was performed overnight at 4° C. The protein mixture was then diluted 5-fold in HGPO buffer (HEPES 10 mM, pH 6.8, 10% (v/v) glycerol, 100 μM progesterone and 0.1% (w/v) n-octyl-β-glucoside) loaded onto a UnoSl column (Biorad) and eluted with a NaCl gradient (0 - 500 mM) in HGPO buffer. The fractions containing the LBD were pooled. After adding NaCl (4 M) to obtain a 230 mM final concentration, the eluate was concentrated onto a vivaspin concentrator (Vivascience, 6 ml, 10,000 Da of molecular weight cut-off) to a protein content of 8.5 mg/ml.

Expression and purification of the MR LBD-S810L-C910A in complex with spironolactone.

BL21 codon-plus (DE3) RIL stains (Stratagene) transformed using the expression vector pMRLBDL810 were grown at 37⁰C in 2x LB supplemented with ampicillin (100 μg/ml), choramphenicol (50 μg/ml) and 100 μM spironolactone, and the expression was induced for 14-16 hours at 15°C by adding 100 μM IPTG. After centrifuging, the cells were disrupted by sonication in a TENGSO buffer (50 mM Tris-HCl, pH 7.5, 5 niM EDTA, 150 mM NaCl, 10% (v/v) glycerol, 100 μM spironolactone and 0.1% (w/v) n- octyl-β-glucoside). The lysate was centrifuged at 105,000 g for 1 h at 4°C, and the supernatant was loaded onto a 5 ml GSTrap column (Amersham) equilibrated in TENGSO buffer. After washing, the fusion protein was eluted using the loading buffer supplemented with 15 mM reduced glutathione. TENGSO buffer was added to the eluate to give a protein concentration of 1 mg/ml, and thrombin cleavage (20 units/mg fusion protein) was performed overnight at 4° C. The protein mixture was then diluted 5-fold in HGSO buffer (HEPES 10 mM, pH 6.8, 10% (v/v) glycerol, 100 μM spironolactone and 0.1% (w/v) n-octyl-β-glucoside) loaded onto a UnoSl column (Biorad) and eluted with a NaCl gradient (0 - 500 mM) in HGSO buffer. The fractions containing the LBD were pooled. After adding NaCl (4 M) to obtain a 230 mM final concentration, the eluate was concentrated onto a vivaspin concentrator (Vivascience, 6 ml, 10,000 Da of molecular weight cut-off) to a protein content of 8.5 mg/ml.

Expression and purification of the MR LBD-C910A in complex with deoxycorticosterone.

BL21 codon-plus (DE3) RIL stains (Stratagene) transformed using the expression vector pMRLBD were grown at 37⁰C in 2x LB supplemented with ampicillin (100 μg/ml), choramphenicol (50 μg/ml) and 100 μM DOC, and the expression was induced for 14-16 hours at 15°C by adding 100 μM IPTG. After centrifuging, the cells were disrupted by sonication in a TENGDO buffer (50 mM Tris-HCl, pH 7.5, 5 mM EDTA, 150 mM NaCl, 10% (v/v) glycerol, 100 μM DOC and 0.1% (w/v) n-octyl-β-glucoside). The lysate was centrifuged at 105,000 g for 1 h at 4°C, and the supernatant was loaded onto a 5 ml GSTrap column (Amersham) equilibrated in TENGDO buffer. After washing, the fusion protein was eluted using the loading buffer supplemented with 15 mM reduced glutathione. TENGDO buffer was added to the eluate to give a protein concentration of 1 mg/ml, and thrombin cleavage (20 units/mg fusion protein) was performed overnight at 4° C. The protein mixture was then diluted 5-fold in HGDO buffer (HEPES 10 mM, pH 6.8, 10% (v/v) glycerol, 100 μM DOC and 0.1% (w/v) n- octyl-β-glucoside) loaded onto a UnoSl column (Biorad) and eluted with a NaCl gradient (0 - 500 mM) in HGDO buffer. The fractions containing the LBD were pooled. After adding NaCl (4 M) to obtain a 230 mM final concentration, the eluate was concentrated onto a vivaspin concentrator (Vivascience, 6 ml, 10,000 Da of molecular weight cut-off) to a protein content of 8.5 mg/ml.

Crystallizations and data collection.

The crystals of the MR LBD-S810L-C910A associated with DOC or progesterone were grown at room temperature using the vapor diffusion method in 2 μl hanging drops containing 1 μl protein solution and 1 μl reservoir solution. The reservoir solution for the DOC/MR LBD-S810L-C910A complex contained 100 mM HEPES, pH 7.0, 230 mM NaCl, 17.5% PEG 4000 and that for the progesterone/MR LBD-S810L-C910A complex contained 100 mM PIPES, pH 6.8, 230 mM NaCl, 27.5% PEG 4000. Crystals grew within a few days to 200 x 200 x 20 μm³. Before data collection, the DOC/MR LBD-S810L-C910A crystal was flash frozen in the mother liquor supplemented with 30% PEG300, whereas the progesterone/MR LBD-S810L-C910A crystal was flash frozen without adding cryoprotecting agent. The crystals of the MR LBD-S810L-C910A associated with spironolactone was grown at room temperature using the vapor diffusion method in 2 μl hanging drops containing 1 μl protein solution and 1 μl reservoir solution. The reservoir solution contained 100 mM HEPES, pH 6.8, 230 mM NaCl, 25% PEG 4000. Crystals grew within a few days to 200 x 200 x 20 μm . Before data collection, the crystal was flash frozen without adding cryoprotecting agent. The crystals of the MR LBD-C910A associated with DOC was grown at room temperature using the vapor diffusion method in 2 μl hanging drops containing 1 μl protein solution and 1 μl reservoir solution. The reservoir solution contained 100 mM HEPES, pH 7.1, 460 mM NaCl, 20% PEG 4000. Crystals grew within a few days to 200 x 200 x 20 μm³. Before data collection, the crystal was flash frozen in 100 mM HEPES, pH 7.1, 230 mM NaCl, 20% PEG 4000 and 30% PEG300.

Diffraction data were collected at 69°K on FIP-BM30A beamline at the European Synchrotron Radiation Facility (Grenoble, France) using a MAR CCD detector. The wavelengths used during data collection were 0.9796 and 0.9798 A for the DOC/MR LBD-S810L-C910A and progesterone/MR LBD-S810L-C910A crystals, respectively. These crystals diffracted up to 1.96 and 2.34 A, respectively. The data were processed using MOSFLM (Powell et al., Acta Crystallogr. D Biol. Crystallogr., 1999, 55, 1690- 1695) and SCALA from the CCP4 program suite (Collaborative Computational Project, N. The CCP4 suite: programs for protein crystallography., Acta Crystallogr. D Biol. Crystallogr., 1994, 50, 760-763). Data collection statistics are summarized in Table 3. The wavelengths used during data collection were 0.9799 and 0.9797 A for the DOC/MR LBD-C910A and spironolactone/MR LBD-S810L-C910A crystals, respectively. These crystals diffracted up to 2.46 and 2.31 A, respectively. The data were processed using XDS (Kabsch, J., Appl. Cryst., 1993, 26, 795-800). Data collection statistics are summarized in Table 4.

Structure determinations and refinements.

The structures of the MR LBD-S810L-C910A complexed with DOC and with progesterone were solved by molecular replacement with the Beast likelihood based program of the CCP4 suite using the homology model of the hMR LBD we had generated previously as the search model (Auzou et al., MoI. Pharmacol., 2000, 58, 684-91). For the progesterone/MR LBD-S810L-C910A crystal, a clear and unique rotation solution was obtained in the P3₁ space group. With this orientation, three translated positions where found within the asymmetric unit. Cycles of manual model building using the SigmaA weighted 2Fo-Fc maps followed by simulated annealing and individual isotropic B factor refinements were performed using CNS (Brunger et al., Acta Crystallogr. D Biol. Crystallogr., 1998, 54, 905-21). Solvent molecules were located in a Fo-Fc map contoured at 3σ. hi the case of the diffraction data of the DOC/MR LBD-S810L-C910A crystal, the twinning-detect program of the CNS package revealed the presence of a nearly perfect twinning. Molecular replacement gave two rotation solutions related by a two fold axis perpendicular to the three-fold axis leading to an apparent P321 space group (Yeates, Methods in enzymology, 1997, 276, 344-358). Taking into account the perfect twinning of the data, only one rotation solution was considered. This rotation solution gave two translated positions. In the case of perfectly twinned data, detwinning can only be achieved by using the amplitudes of the model. To exclude any bias, the refinement of the model and the location of the water molecules were performed using the complete data set (i.e. without detwinning). After each cycle of refinement, the maps were generated after detwinning the data using the perfect-detwin program in the CNS package and the refined model. The final models were validated with PROCHECK (Laskowski et al., J. Appl. Crystallogr., 1993, 26, 283-291), 99.3 and 100% of the residues lie within the allowed regions of the Ramachandran Plot for the DOC/MR LBD-S810L-C91 OA and progesterone/MR LBD- S810L-C910A structures, respectively. The structure refinement statistics are summarized in the Table 3.

The structures of the MR LBD-S810L-C910A complexed with spironolactone and MR LBD-C910A complexed with DOC were solved by molecular replacement with Phaser (Storoni et al., Acta Crystallogr., 2004, D60, 432-438; McCoy et al., Acta Crystallogr., 2005, D61, 458-464) and the Beast likelihood based program of the CCP4 suite, respectively and using the homology model of the hMR LBD we had generated previously as the search model (Auzou et al.₅ MoI. Pharmacol., 2000, 58, 684-91). The MR LBD-S810L-C910A complexed with spironolactone crystallized in the P3₂ space group with 6 molecules within the asymmetric unit. The MR LBD-C910A complexed with DOC crystallized in the P3i space group with 3 molecules within the asymmetric unit. Refinement of these two structures is in process. R factors are 31.2 and 24.1%, respectively.

Coordinates

The coordinates of the MR LBD-S810L-C910A associated with deoxycorticosterone and with progesterone have been deposited in the Protein Data Bank with accession numbers 1Y9R and 1YA3, respectively (see Tables 1 and 2, respectively).

5α-pregnan-20-one modulates PR

The ability of compound 5α-pregnan-20-one and derivatives thereof to inactivate PR is tested in co-tranfection assays. Briefly, HEK-293T cells are cultured and transfected in high glucose containing Dulbecco's modified essential medium supplemented with 10% (v/v) charcoal stripped and heat-inactivated fetal calf serum (FCS), 25 mM HEPES, 2x non-essential amino acids, 2 mM glutamine, 100 IU/ml penicillin and 100 mg/ml streptomycin at 37°C in a humidified atmosphere with 5% CO₂. Transfections are carried out using the phosphate calcium precipitation method. The phosphate solution, prepared for one T75 flask (20ml), contains 4 μg of the PR expression vectors (pSG5PR), 14 μg pFC31Luc and 2 mg pSVβgal (Promega) in HBS supplemented with 125 mM CaC12. Twelve hours after transfection, the transfected cells are replated in twelve-well plates (lml/well). 5α-pregnan-20-one (Pl) is added 24 h after seeding, and the plates then incubated for 24 h. The β-galactosidase and luciferase activities of cell extracts are assayed. To standardize transfection efficiency, the relative light units obtained in the luciferase assay are divided by the optical density obtained in the β- galactosidase assay.

Production and characterization of polyclonal antibodies against MR LBD The fusion protein GST-MR LBD-S810L-C910A in complex with DOC was purified as described above and four times injected to two rabbits (15 days between each injection).

Two weeks after the fourth injection, rabbits were bled. The serums were prepared and frozen.

The ability of the serums to recognize the MR LBD-S810L-C910A was tested by Western Blot. At a 1/500 dilution, the antibodies from rabbit 2 recognized 0.1 ng of purified MR LBD-S810L-C910A.

Table 1 Atomic structure coordinate data obtained from X-ray diffraction from the ligand-binding domain of the mineralocorticoid receptor in complex with deoxycorticosterone and harboring the S810L and C910A mutations

ATOM 499 C ILE A 802 57.277 51.036 -13.113 1.00 18.86 C

ATOM 500 O ILE A 802 57.560 51.606 -12.059 1.00 19.22 O

ATOM 501 CB ILE A 802 57.719 48.606 -13.191 1.00 16.21 C

ATOM 502 CGl ILE A 802 57.129 47.222 -13.469 1.00 17.36 C

ATOM 503 CG2 ILE A 802 58.468 48.570 -11.884 1.00 16.07 C

ATOM 504 CDl ILE A 802 56.342 46.623 -12.319 1.00 14.36 C

ATOM 505 N GLN A 803 57.534 51.567 -14.300 1.00 18.47 N

ATOM 506 CA GLN A 803 58.189 52.859 -14.399 1.00 19.19 C

ATOM 507 C GLN A 803 57.281 54.019 -13.993 1.00 18.42 C

ATOM 508 O GLN A 803 57.654 54.862 -13.170 1.00 17.21 O

ATOM 509 CB GLN A 803 58.725 53.069 -15.819 1.00 18.96 C

ATOM 510 CG GLN A 803 60.095 52.454 -16.057 1.00 21.18 C

ATOM 511 CD GLN A 803 60.647 52.760 -17.441 1.00 23.26 C

ATOM 512 OEl GLN A 803 61.858 52.690 -17.673 1.00 22.17 O

ATOM 513 NE2 GLN A 803 59.759 53.091 -18.369 1.00 23.06 N

ATOM 514 N TYR A 804 56.089 54.060 -14.571 1.00 18.60 N

ATOM 515 CA TYR A 804 55.134 55.118 -14.269 1.00 18.69 C

ATOM 516 C TYR A 804 54.634 55.082 -12.829 1.00 18.60 C

ATOM 517 O TYR A 804 54.067 56.059 -12.354 1.00 20.29 O

ATOM 518 CB TYR A 804 53.940 55.021 -15.215 1.00 18.81 C

ATOM 519 CG TYR A 804 54.140 55.704 -16.541 1.00 20.72 C

ATOM 520 CDl TYR A 804 54.298 57.089 -16.616 1.00 22.39 C

ATOM 521 CD2 TYR A 804 54.151 54.975 -17.729 1.00 22.91 C

ATOM 522 CEl TYR A 804 54.459 57.729 -17.840 1.00 22.84 C

ATOM 523 CE2 TYR A 804 54.313 55.607 -18.957 1.00 21.73 C

ATOM 524 CZ TYR A 804 54.464 56.983 -19.007 1.00 22.91 C

ATOM 525 OH TYR A 804 54.606 57.618 -20.223 1.00 25.32 O

ATOM 526 N SER A 805 54.859 53.966 -12.133 1.00 18.87 N

ATOM 527 CA SER A 805 54.390 53.809 -10.758 1.00 19.04 C

ATOM 528 C SER A 805 55.470 53.477 -9.726 1.00 19.82 C

ATOM 529 O SER A 805 55.150 53.270 -8.556 1.00 19.69 O

ATOM 530 CB SER A 805 53.337 52.700 -10.691 1.00 18.66 C

ATOM 531 OG SER A 805 53.951 51.421 -10.799 1.00 13.78 O

ATOM 532 N TRP A 806 56.735 53.429 -10.129 1.00 19.30 N

ATOM 533 CA TRP A 806 57.775 53.087 -9.158 1.00 20.50 C

ATOM 534 C TRP A 806 57.715 53.887 -7.855 1.00 20.70 C

ATOM 535 O TRP A 806 57.750 53.294 -6.777 1.00 21.07 O

ATOM 536 CB TRP A 806 59.174 53.212 -9.767 1.00 21.34 C

ATOM 537 CG TRP A 806 59.691 54.604 -9.846 1.00 23.62 C

ATOM 538 CDl TRP A 806 59.260 55.595 -10.675 1.00 23.35 C

ATOM 539 CD2 TRP A 806 60.743 55.168 -9.057 1.00 24.11 C

ATOM 540 NEl TRP A 806 59.981 56.741 -10.453 1.00 24.11 N

ATOM 541 CE2 TRP A 806 60.898 56.507 -9.465 1.00 23.18 C

ATOM 542 CE3 TRP A 806 61.572 54.669 -8.043 1.00 24.91 C

ATOM 543 CZ2 TRP A 806 61.849 57.357 -8.895 1.00 25.24 C

ATOM 544 CZ3 TRP A 806 62.517 55.516 -7.477 1.00 24.39 C

ATOM 545 CH2 TRP A 806 62.648 56.843 -7.905 1.00 23.96 C

ATOM 546 N MET A 807 57.615 55.217 -7.939 1.00 20.60 N

ATOM 547 CA MET A 807 57.572 56.051 -6.729 1.00 19.30 C

ATOM 548 C MET A 807 56.428 55.681 -5.774 1.00 18.29 C

ATOM 549 O MET A 807 56.620 55.663 -4.560 1.00 17.94 O

ATOM 550 CB MET A 807 57.483 57.540 -7.085 1.00 18.24 C

ATOM 551 CG MET A 807 58.713 58.374 -6.684 1.00 17.36 C

ATOM 552 SD MET A 807 59.242 58.208 -4.945 1.00 14.94 S

ATOM 553 CE MET A 807 60.547 56.973 -5.136 1.00 16.77 C

ATOM 554 N CYS A 808 55.247 55.400 -6.321 1.00 19.20 N

ATOM 555 CA CYS A 808 54.095 55.001 -5.507 1.00 18.91 C

ATOM 556 C CYS A 808 54.515 53.766 -4.703 1.00 17.54 C

ATOM 557 O CYS A 808 54.420 53.738 -3.475 1.00 15.96 O

ATOM 558 CB CYS A 808 52.896 54.624 -6.398 1.00 23.33 C

ATOM 559 SG CYS A 808 52.075 55.968 -7.339 1.00 27.97 S

ATOM 560 N LEU A 809 54.994 52.759 -5.429 1.00 14.97 N

ATOM 561 CA LEU A 809 55.443 51.488 -4.871 1.00 15.49 C

ATOM 562 C LEU A 809 56.312 51.653 -3.627 1.00 15.64 C

ATOM 563 O LEU A 809 55.884 51.378 -2.504 1.00 17.26 O

ATOM 564 CB LEU A 809 56.228 50.710 -5.937 1.00 15.30 C

ATOM 565 CG LEU A 809 55.547 50.555 -7.304 1.00 14.37 C

ATOM 566 CDl LEU A 809 56.559 50.155 -8.366 1.00 15.59 C

ATOM 567 CD2 LEU A 809 54.435 49.539 -7.197 1.00 13.30 C

ATOM 568 N LEU A 810 57.536 52.116 -3.836 1.00 15.55 N

ATOM 569 CA LEU A 810 58.475 52.304 -2.743 1.00 14.75 C

ATOM 570 C LEU A 810 57.895 53.121 -1.598 1.00 14.50 C

ATOM 571 O LEU A 810 58.023 52.736 -0.436 1.00 13.52 O

ATOM 572 CB LEU A 810 59.762 52.948 -3.270 1.00 15.59 C

ATOM 721 CDl LEU A 827 59.367 59.607 7.149 1.00 13.24 C

ATOM 722 CD2 LEU A 827 57.818 57.614 7.051 1.00 13.46 C

ATOM 723 N TYR A 828 60.572 53.840 8.609 1.00 16.53 N

ATOM 724 CA TYR A 828 61.520 52.730 8.471 1.00 17.02 C

ATOM 725 C TYR A 828 61.972 52.456 7.022 1.00 17.80 C

ATOM 726 O TYR A 828 61.541 51.474 6.400 1.00 16.35 O

ATOM 727 CB TYR A 828 60.880 51.475 9.069 1.00 15.75 C

ATOM 728 CG TYR A 828 61.823 50.347 9.425 1.00 17.34 C

ATOM 729 CDl TYR A 828 62.360 49.518 8.442 1.00 15.45 C

ATOM 730 CD2 TYR A 828 62.142 50.079 10.761 1.00 18.13 C

ATOM 731 CEl TYR A 828 63.183 48.454 8.771 1.00 18.03 C

ATOM 732 CE2 TYR A 828 62.968 49.010 11.103 1.00 20.09 C

ATOM 733 CZ TYR A 828 63.483 48.204 10.102 1.00 20.25 C

ATOM 734 OH TYR A 828 64.304 47.154 10.428 1.00 24.43 O

ATOM 735 N PHE A 829 62.844 53.318 6.492 1.00 17.30 N

ATOM 736 CA PHE A 829 63.355 53.148 5.127 1.00 18.16 C

ATOM 737 C PHE A 829 64.027 51.793 4.939 1.00 18.77 C

ATOM 738 O PHE A 829 63.743 51.070 3.985 1.00 18.72 O

ATOM 739 CB PHE A 829 64.379 54.226 4.781 1.00 18.25 C

ATOM 740 CG PHE A 829 63.812 55.608 4.699 1.00 20.23 C

ATOM 741 CDl PHE A 829 63.663 56.384 5.840 1.00 19.71 C

ATOM 742 CD2 PHE A 829 63.451 56.150 3.469 1.00 20.82 C

ATOM 743 CEl PHE A 829 63.169 57.691 5.753 1.00 19.39 C

ATOM 744 CE2 PHE A 829 62.957 57.451 3.377 1.00 19.67 C

ATOM 745 CZ PHE A 829 62.818 58.220 4.521 1.00 18.57 C

ATOM 746 N ALA A 830 64.942 51.472 5.847 1.00 17.84 N

ATOM 747 CA ALA A 830 65.667 50.220 5.801 1.00 19.89 C

ATOM 748 C ALA A 830 66.132 49.865 7.203 1.00 21.05 C

ATOM 749 O ALA A 830 66.266 50.741 8.054 1.00 21.42 O

ATOM 750 CB ALA A 830 66.868 50.343 4.859 1.00 22.51 C

ATOM 751 N PRO A 831 66.379 48.569 7.459 1.00 21.79 N

ATOM 752 CA PRO A 831 66.835 48.094 8.766 1.00 22.06 C

ATOM 753 C PRO A 831 68.034 48.910 9.250 1.00 22.36 C

ATOM 754 O PRO A 831 68.206 49.132 10.443 1.00 21.79 O

ATOM 755 CB PRO A 831 67.190 46.634 8.493 1.00 22.45 C

ATOM 756 CG PRO A 831 66.200 46.247 7.446 1.00 21.58 C

ATOM 757 CD PRO A 831 66.225 47.443 6.519 1.00 22.47 C

ATOM 758 N ASP A 832 68.854 49.363 8.309 1.00 23.82 N

ATOM 759 CA ASP A 832 70.029 50.157 8.647 1.00 24.79 C

ATOM 760 C ASP A 832 69.795 51.643 8.380 1.00 25.48 C

ATOM 761 O ASP A 832 70.749 52.406 8.225 1.00 26.09 O

ATOM 762 CB ASP A 832 71.236 49.673 7.843 1.00 23.59 C

ATOM 763 CG ASP A 832 71.043 49.836 6.343 1.00 22.49 C

ATOM 764 ODl ASP A 832 71.988 49.529 5.592 1.00 20.33 O

ATOM 765 OD2 ASP A 832 69.951 50.270 5.918 1.00 22.45 O

ATOM 766 N LEU A 833 68.529 52.059 8.339 1.00 25.39 N

ATOM 767 CA LEU A 833 68.217 53.460 8.077 1.00 26.30 C

ATOM 768 C LEU A 833 66.823 53.855 8.584 1.00 26.51 C

ATOM 769 O LEU A 833 65.816 53.651 7.897 1.00 26.28 O

ATOM 770 CB LEU A 833 68.329 53.728 6.572 1.00 25.60 C

ATOM 111 CG LEU A 833 68.601 55.154 6.092 1.00 26.70 C

ATOM 772 CDl LEU A 833 69.845 55.704 6.776 1.00 26.02 C

ATOM 773 CD2 LEU A 833 68.784 55.147 4.582 1.00 26.28 C

ATOM 774 N VAL A 834 66.775 54.417 9.792 1.00 27.46 N

ATOM 775 CA VAL A 834 65.516 54.852 10.399 1.00 27.47 C

ATOM 776 C VAL A 834 65.491 56.361 10.626 1.00 28.07 C

ATOM 111 O VAL A 834 66.488 56.960 11.043 1.00 29.73 O

ATOM 778 CB VAL A 834 65.263 54.136 11.746 1.00 26.95 C

ATOM 779 CGl VAL A 834 64.004 54.683 12.399 1.00 28.80 C

ATOM 780 CG2 VAL A 834 65.122 52.647 11.518 1.00 25.67 C

ATOM 781 N PHE A 835 64.339 56.970 10.362 1.00 27.78 N

ATOM 782 CA PHE A 835 64.186 58.414 10.501 1.00 28.54 C

ATOM 783 C PHE A 835 63.321 58.917 11.658 1.00 30.06 C

ATOM 784 O PHE A 835 62.189 58.469 11.861 1.00 30.95 O

ATOM 785 CB PHE A 835 63.644 58.995 9.193 1.00 26.20 C

ATOM 786 CG PHE A 835 64.687 59.192 8.131 1.00 25.29 C

ATOM 787 CDl PHE A 835 65.526 58.149 7.749 1.00 25.36 C

ATOM 788 CD2 PHE A 835 64.805 60.415 7.480 1.00 24.97 C

ATOM 789 CEl PHE A 835 66.464 58.322 6.728 1.00 25.14 C

ATOM 790 CE2 PHE A 835 65.746 60.598 6.457 1.00 25.37 C

ATOM 791 CZ PHE A 835 66.572 59.551 6.081 1.00 24.02 C

ATOM 792 N ASN A 836 63.885 59.862 12.404 1.00 30.20 N

ATOM 793 CA ASN A 836 63.230 60.513 13.533 1.00 32.79 C

ATOM 794 C ASN A 836 63.101 61.976 13.102 1.00 34.05 C

ATOM 2201 CB ASN B 770 128.217 23.016 19.804 1.00 19.18 C

ATOM 2202 CG ASN B 770 127.416 24.312 19.711 1.00 19.44 C

ATOM 2203 ODl ASN B 770 126.198 24.289 19.546 1.00 19.85 O

ATOM 2204 ND2 ASN B 770 128.102 25.446 19.800 1.00 19.40 N

ATOM 2205 N ARG B 771 129.469 20.569 21.179 1.00 19.95 N

ATOM 2206 CA ARG B 771 130.270 19.348 21.190 1.00 22.06 C

ATOM 2207 C ARG B 771 129.398 18.194 21.690 1.00 23.11 C

ATOM 2208 O ARG B 771 129.407 17.101 21.120 1.00 23.10 O

ATOM 2209 CB ARG B 771 131.482 19.536 22.105 1.00 20.92 C

ATOM 2210 CG ARG B 771 132.428 18.352 22.169 1.00 21.41 C

ATOM 2211 CD ARG B 771 133.471 18.584 23.243 1.00 25.37 C

ATOM 2212 NE ARG B 771 134.187 19.833 23.020 1.00 28.28 N

ATOM 2213 CZ ARG B 771 134.958 20.431 23.923 1.00 30.14 C

ATOM 2214 NHl ARG B 771 135.114 19.890 25.127 1.00 28.66 N

ATOM 2215 NH2 ARG B 771 135.571 21.573 23.620 1.00 28.69 N

ATOM 2216 N LEU B 772 128.635 18.462 22.750 1.00 23.46 N

ATOM 2217 CA LEU B 772 127.723 17.483 23.340 1.00 22.09 C

ATOM 2218 C LEU B 772 126.658 17.110 22.315 1.00 21.32 C

ATOM 2219 O LEU B 772 126.296 15.945 22.173 1.00 19.88 O

ATOM 2220 CB LEU B 772 127.041 18.077 24.578 1.00 22.12 C

ATOM 2221 CG LEU B 772 126.231 17.174 25.521 1.00 22.11 C

ATOM 2222 CDl LEU B 772 125.610 18.026 26.621 1.00 20.66 C

ATOM 2223 CD2 LEU B 772 125.150 16.443 24.769 1.00 21.82 C

ATOM 2224 N ALA B 773 126.148 18.115 21.616 1.00 20.09 N

ATOM 2225 CA ALA B 773 125.125 17.909 20.601 1.00 17.69 C

ATOM 2226 C ALA B 773 125.634 16.980 19.508 1.00 17.24 C

ATOM 2227 O ALA B 773 124.931 16.056 19.082 1.00 16.49 O

ATOM 2228 CB ALA B 773 124.728 19.236 19.998 1.00 16.69 C

ATOM 2229 N GLY B 774 126.851 17.247 19.044 1.00 16.83 N

ATOM 2230 CA GLY B 774 127.442 16.431 18.003 1.00 15.52 C

ATOM 2231 C GLY B 774 127.431 14.984 18.428 1.00 17.62 C

ATOM 2232 O GLY B 774 127.151 14.101 17.631 1.00 18.42 O

ATOM 2233 N LYS B 775 127.701 14.741 19.705 1.00 20.09 N

ATOM 2234 CA LYS B 775 127.717 13.381 20.226 1.00 22.07 C

ATOM 2235 C LYS B 775 126.303 12.811 20.355 1.00 22.81 C

ATOM 2236 O LYS B 775 126.058 11.662 19.993 1.00 23.78 O

ATOM 2237 CB LYS B lib 128.445 13.359 21.570 1.00 23.78 C

ATOM 2238 CG LYS B 775 129.885 13.832 21.463 1.00 24.10 C

ATOM 2239 CD LYS B lib 130.509 14.074 22.826 1.00 27.45 C

ATOM 2240 CE LYS B lib 131.956 14.512 22.682 1.00 25.23 C

ATOM 2241 NZ LYS B lib 132.754 13.441 22.038 1.00 26.58 N

ATOM 2242 N GLN B 776 125.374 13.619 20.851 1.00 24.08 N

ATOM 2243 CA GLN B 776 123.987 13.182 20.998 1.00 24.36 C

ATOM 2244 C GLN B 776 123.376 12.889 19.629 1.00 24.39 C

ATOM 2245 O GLN B 776 122.438 12.100 19.501 1.00 24.38 O

ATOM 2246 CB GLN B 776 123.163 14.260 21.719 1.00 23.88 C

ATOM 2247 CG GLN B 776 122.831 13.938 23.173 1.00 25.09 C

ATOM 2248 CD GLN B 776 122.199 15.117 23.924 1.00 25.97 C

ATOM 2249 OEl GLN B 776 121.277 15.764 23.436 1.00 28.39 O

ATOM 2250 NE2 GLN B 776 122.694 15.383 25.122 1.00 24.28 N

ATOM 2251 N MET B 111 123.910 13.521 18.594 1.00 25.37 N

ATOM 2252 CA MET B 111 123.373 13.293 17.266 1.00 26.98 C

ATOM 2253 C MET B 111 123.664 11.891 16.762 1.00 26.85 C

ATOM 2254 O MET B 111 122.934 11.366 15.925 1.00 26.38 O

ATOM 2255 CB MET B 111 123.925 14.307 16.272 1.00 27.49 C

ATOM 2256 CG MET B 111 122.837 14.830 15.375 1.00 27.40 C

ATOM 2257 SD MET B 111 121.585 15.531 16.446 1.00 25.16 S

ATOM 2258 CE MET B 111 122.616 17.046 16.425 1.00 23.62 C

ATOM 2259 N ILE B 778 124.735 11.288 17.264 1.00 27.19 N

ATOM 2260 CA ILE B 778 125.086 9.943 16.836 1.00 28.34 C

ATOM 2261 C ILE B 778 123.950 9.024 17.259 1.00 27.92 C

ATOM 2262 O ILE B 778 123.443 8.237 16.465 1.00 27.32 O

ATOM 2263 CB ILE B 778 126.375 9.442 17.504 1.00 29.33 C

ATOM 2264 CGl ILE B 778 127.345 10.600 17.738 1.00 30.31 C

ATOM 2265 CG2 ILE B 778 127.029 8.419 16.605 1.00 28.47 C

ATOM 2266 CDl ILE B 778 128.448 10.284 18.724 1.00 30.31 C

ATOM 2267 N GLN B 779 123.565 9.142 18.525 1.00 28.79 N

ATOM 2268 CA GLN B 779 122.493 8.342 19.091 1.00 28.76 C

ATOM 2269 C GLN B 779 121.163 8.677 18.438 1.00 28.00 C

ATOM 2270 O GLN B 779 120.293 7.822 18.337 1.00 30.37 O

ATOM 2271 CB GLN B 779 122.377 8.585 20.594 1.00 29.48 C

ATOM 2272 CG GLN B 779 123.601 8.242 21.403 1.00 28.93 C

ATOM 2273 CD GLN B 779 123.329 8.330 22.893 1.00 31.25 C

ATOM 2274 OEl GLN B 779 122.839 9.349 23.388 1.00 32.65 O

SUBSTITUTE SHEET (RULE 26) ATOM 2275 NE2 GLN B 779 123.642 7.260 23.618 1.00 31.51 N

ATOM 2276 N VAL B 780 121.006 9.921 18.004 1.00 26.11 N

ATOM 2277 CA VAL B 780 119.769 10.345 17.362 1.00 25.40 C

ATOM 2278 C VAL B 780 119.473 9.476 16.148 1.00 24.63 C

ATOM 2279 O VAL B 780 118.382 8.916 16.031 1.00 24.56 O

ATOM 2280 CB VAL B 780 119.837 11.823 16.915 1.00 25.24 C

ATOM 2281 CGl VAL B 780 118.647 12.155 16.030 1.00 24.54 C

ATOM 2282 CG2 VAL B 780 119.859 12.740 18.134 1.00 25.12 C

ATOM 2283 N VAL B 781 120.442 9.373 15.240 1.00 24.41 N

ATOM 2284 CA VAL B 781 120.269 8.556 14.045 1.00 23.35 C

ATOM 2285 C VAL B 781 120.138 7.085 14.414 1.00 22.41 C

ATOM 2286 O VAL B 781 119.252 6.406 13.913 1.00 22.06 O

ATOM 2287 CB VAL B 781 121.438 8.735 13.042 1.00 25.16 C

ATOM 2288 CGl VAL B 781 121.027 9.703 11.948 1.00 25.47 C

ATOM 2289 CG2 VAL B 781 122.676 9.255 13.757 1.00 24.60 C

ATOM 2290 N LYS B 782 121.013 6.594 15.293 1.00 23.39 N

ATOM 2291 CA LYS B 782 120.943 5.197 15.727 1.00 23.48 C

ATOM 2292 C LYS B 782 119.522 4.957 16.207 1.00 23.40 C

ATOM 2293 O LYS B 782 119.008 3.833 16.162 1.00 23.78 O

ATOM 2294 CB LYS B 782 121.912 4.926 16.883 1.00 24.30 C

ATOM 2295 CG LYS B 782 121.632 3.617 17.625 1.00 23.35 C

ATOM 2296 CD LYS B 782 122.428 3.524 18.927 1.00 25.13 C

ATOM 2297 CE LYS B 782 121.927 2.388 19.804 1.00 24.71 C

ATOM 2298 NZ LYS B 782 122.577 2.350 21.147 1.00 23.65 N

ATOM 2299 N TRP B 783 118.892 6.030 16.673 1.00 21.63 N

ATOM 2300 CA TRP B 783 117.525 5.957 17.150 1.00 21.67 C

ATOM 2301 C TRP B 783 116.545 5.960 15.975 1.00 20.39 C

ATOM 2302 O TRP B 783 115.730 5.058 15.843 1.00 21.37 O

ATOM 2303 CB TRP B 783 117.227 7.138 18.087 1.00 21.77 C

ATOM 2304 CG TRP B 783 115.803 7.187 18.569 1.00 17.52 C

ATOM 2305 CDl TRP B 783 115.182 6.290 19.380 1.00 18.79 C

ATOM 2306 CD2 TRP B 783 114.841 8.201 18.281 1.00 17.42 C

ATOM 2307 NEl TRP B 783 113.884 6.682 19.623 1.00 18.56 N

ATOM 2308 CE2 TRP B 783 113.651 7.855 18.959 1.00 17.67 C

ATOM 2309 CE3 TRP B 783 114.866 9.371 17.516 1.00 16.11 C

ATOM 2310 CZ2 TRP B 783 112.500 8.639 18.896 1.00 18.03 C

ATOM 2311 CZ3 TRP B 783 113.718 10.150 17.456 1.00 18.37 C

ATOM 2312 CH2 TRP B 783 112.554 9.780 18.142 1.00 16.04 C

ATOM 2313 N ALA B 784 116.644 6.963 15.112 1.00 19.65 N

ATOM 2314 CA ALA B 784 115.739 7.079 13.970 1.00 20.93 C

ATOM 2315 C ALA B 784 116.135 6.255 12.743 1.00 21.60 C

ATOM 2316 O ALA B 784 115.964 6.702 11.606 1.00 22.44 O

ATOM 2317 CB ALA B 784 115.585 8.549 13.585 1.00 17.84 C

ATOM 2318 N LYS B 785 116.668 5.059 12.971 1.00 22.50 N

ATOM 2319 CA LYS B 785 117.064 4.177 11.870 1.00 22.29 C

ATOM 2320 C LYS B 785 116.372 2.830 12.047 1.00 20.96 C

ATOM 2321 O LYS B 785 116.150 2.097 11.081 1.00 20.14 O

ATOM 2322 CB LYS B 785 118.583 3.964 11.850 1.00 23.66 C

ATOM 2323 CG LYS B 785 119.100 2.947 12.863 1.00 24.85 C

ATOM 2324 CD LYS B 785 120.576 2.618 12.616 1.00 27.28 C

ATOM 2325 CE LYS B 785 121.151 1.720 13.707 1.00 24.46 C

ATOM 2326 NZ LYS B 785 120.379 0.445 13.851 1.00 28.33 N

ATOM 2327 N VAL B 786 116.044 2.517 13.299 1.00 19.86 N

ATOM 2328 CA VAL B 786 115.377 1.265 13.652 1.00 19.98 C

ATOM 2329 C VAL B 786 113.970 1.611 14.163 1.00 20.05 C

ATOM 2330 O VAL B 786 113.330 0.837 14.875 1.00 19.48 O

ATOM 2331 CB VAL B 786 116.195 0.512 14.741 1.00 18.59 C

ATOM 2332 CGl VAL B 786 115.459 -0.727 15.222 1.00 22.22 C

ATOM 2333 CG2 VAL B 786 117.525 0.097 14.176 1.00 17.05 C

ATOM 2334 N LEU B 787 113.501 2.787 13.756 1.00 20.54 N

ATOM 2335 CA LEU B 787 112.198 3.307 14.154 1.00 19.64 C

ATOM 2336 C LEU B 787 111.040 2.740 13.334 1.00 19.44 C

ATOM 2337 O LEU B 787 111.124 2.614 12.106 1.00 17.52 O

ATOM 2338 CB LEU B 787 112.209 4.832 14.028 1.00 19.31 C

ATOM 2339 CG LEU B 787 111.375 5.672 14.998 1.00 19.82 C

ATOM 2340 CDl LEU B 787 111.782 5.335 16.429 1.00 18.68 C

ATOM 2341 CD2 LEU B 787 111.594 7.168 14.709 1.00 15.87 C

ATOM 2342 N PRO B 788 109.935 2.388 14.007 1.00 19.65 N

ATOM 2343 CA PRO B 788 108.760 1.839 13.329 1.00 19.84 C

ATOM 2344 C PRO B 788 108.303 2.807 12.243 1.00 19.71 C

ATOM 2345 O PRO B 788 108.309 4.019 12.450 1.00 19.83 O

ATOM 2346 CB PRO B 788 107.744 1.723 14.457 1.00 20.63 C

ATOM 2347 CG PRO B 788 108.600 1.419 15.634 1.00 20.95 C

ATOM 2348 CD PRO B 788 109.735 2.397 15.466 1.00 21.59 C ATOM 2349 N GLY B 789 107.931 2.266 11.087 1.00 19.41 N

ATOM 2350 CA GLY B 789 107.468 3.085 9.981 1.00 18.68 C

ATOM 2351 C GLY B 789 108.461 4.058 9.372 1.00 17.40 C

ATOM 2352 O GLY B 789 108.604 4.110 8.153 1.00 17.40 O

ATOM 2353 N PHE B 790 109.134 4.833 10.221 1.00 17.82 N

ATOM 2354 CA PHE B 790 110.118 5.837 9.802 1.00 17.44 C

ATOM 2355 C PHE B 790 111.359 5.270 9.111 1.00 18.06 C

ATOM 2356 O PHE B 790 111.892 5.895 8.193 1.00 17.63 O

ATOM 2357 CB PHE B 790 110.572 6.661 11.015 1.00 15.31 C

ATOM 2358 CG PHE B 790 111.524 7.784 10.677 1.00 11.69 C

ATOM 2359 CDl PHE B 790 111.046 8.984 10.147 1.00 9.09 C

ATOM 2360 CD2 PHE B 790 112.893 7.644 10.900 1.00 11.09 C

ATOM 2361 CEl PHE B 790 111.917 10.031 9.849 1.00 10.00 C

ATOM 2362 CE2 PHE B 790 113.777 8.681 10.603 1.00 11.67 C

ATOM 2363 CZ PHE B 790 113.283 9.884 10.075 1.00 11.15 C

ATOM 2364 N LYS B 791 111.823 4.104 9.557 1.00 18.19 N

ATOM 2365 CA LYS B 791 113.019 3.491 8.971 1.00 20.37 C

ATOM 2366 C LYS B 791 112.712 2.890 7.608 1.00 22.26 C

ATOM 2367 O LYS B 791 113.605 2.421 6.908 1.00 21.58 O

ATOM 2368 CB LYS B 791 113.561 2.393 9.883 1.00 17.93 C

ATOM 2369 CG LYS B 791 112.678 1.162 9.971 1.00 18.89 C

ATOM 2370 CD LYS B 791 113.293 0.112 10.869 1.00 19.10 C

ATOM 2371 CE LYS B 791 112.343 -1.060 '11.083 1.00 20.83 C

ATOM 2372 NZ LYS B 791 111.624 -1.437 9.846 1.00 21.64 N

ATOM 2373 N ASN B 792 111.441 2.916 7.229 1.00 24.04 N

ATOM 2374 CA ASN B 792 111.027 2.340 5.956 1.00 24.65 C

ATOM 2375 C ASN B 792 110.941 3.351 4.821 1.00 25.32 C

ATOM 2376 O ASN B 792 110.850 2.978 3.647 1.00 25.54 O

ATOM 2377 CB ASN B 792 109.701 1.604 6.157 1.00 25.01 C

ATOM 2378 CG ASN B 792 109.841 0.425 7.123 1.00 24.64 C

ATOM 2379 ODl ASN B 792 109.103 0.305 8.109 1.00 26.90 O

ATOM 2380 ND2 ASN B 792 110.799 -0.443 6.841 1.00 19.59 N

ATOM 2381 N LEU B 793 110.979 4.633 5.174 1.00 24.15 N

ATOM 2382 CA LEU B 793 110.938 5.695 4.183 1.00 23.14 C

ATOM 2383 C LEU B 793 112.327 5.838 3.584 1.00 23.04 C

ATOM 2384 O LEU B 793 113.318 5.442 4.202 1.00 23.38 O

ATOM 2385 CB LEU B 793 110.547 7.020 4.833 1.00 24.42 C

ATOM 2386 CG LEU B 793 109.096 7.221 5.254 1.00 24.49 C

ATOM 2387 CDl LEU B 793 109.021 8.420 6.172 1.00 26.85 C

ATOM 2388 CD2 LEU B 793 108.215 7.420 4.023 1.00 26.25 C

ATOM 2389 N PRO B 794 112.418 6.427 2.379 1.00 22.15 N

ATOM 2390 CA PRO B 794 113.693 6.633 1.686 1.00 21.76 C

ATOM 2391 C PRO B 794 114.725 7.297 2.582 1.00 21.67 C

ATOM 2392 O PRO B 794 114.401 8.217 3.330 1.00 21.59 O

ATOM 2393 CB PRO B 794 113.305 7.516 0.505 1.00 21.48 C

ATOM 2394 CG PRO B 794 112.095 8.246 1.009 1.00 22.26 C

ATOM 2395 CD PRO B 794 111.336 7.152 1.695 1.00 22.86 C

ATOM 2396 N LEU B 795 115.973 6.838 2.495 1.00 22.23 N

ATOM 2397 CA LEU B 795 117.034 7.394 3.322 1.00 21.97 C

ATOM 2398 C LEU B 795 117.154 8.901 3.212 1.00 22.20 C

ATOM 2399 O LEU B 795 117.624 9.557 4.137 1.00 23.33 O

ATOM 2400 CB LEU B 795 118.388 6.753 2.996 1.00 20.31 C

ATOM 2401 CG LEU B 795 119.581 7.335 3.774 1.00 20.32 C

ATOM 2402 CDl LEU B 795 119.180 7.649 5.221 1.00 20.49 C

ATOM 2403 CD2 LEU B 795 120.744 6.353 3.756 1.00 17.35 C

ATOM 2404 N GLU B 796 116.723 9.455 2.088 1.00 22.99 N

ATOM 2405 CA GLU B 796 116.810 10.891 1.898 1.00 21.40 C

ATOM 2406 C GLU B 796 115.868 11.585 2.862 1.00 20.24 C

ATOM 2407 O GLU B 796 116.260 12.525 3.552 1.00 19.80 O

ATOM 2408 CB GLU B 796 116.441 11.269 0.460 1.00 23.26 C

ATOM 2409 CG GLU B 796 117.238 10.529 -0.610 1.00 27.47 C

ATOM 2410 CD GLU B 796 118.731 10.688 -0.433 1.00 30.51 C

ATOM 2411 OEl GLU B 796 119.199 11.848 -0.337 1.00 30.30 O

ATOM 2412 OE2 GLU B 796 119.439 9.654 -0.390 1.00 33.10 O

ATOM 2413 N ASP B 797 114.628 11.107 2.909 1.00 20.04 N

ATOM 2414 CA ASP B 797 113.607 11.697 3.764 1.00 18.84 C

ATOM 2415 C ASP B 797 113.982 11.580 5.233 1.00 19.58 C

ATOM 2416 O ASP B 797 113.797 12.528 5.993 1.00 20.16 O

ATOM 2417 CB ASP B 797 112.241 11.039 3.503 1.00 19.98 C

ATOM 2418 CG ASP B 797 111.751 11.262 2.077 1.00 21.37 C

ATOM 2419 ODl ASP B 797 112.517 10.950 1.148 1.00 23.86 O

ATOM 2420 OD2 ASP B 797 110.615 11.746 1.876 1.00 21.22 O

ATOM 2421 N GLN B 798 114.533 10.432 5.621 1.00 19.15 N

ATOM 2422 CA GLN B 798 114.930 10.212 7.010 1.00 20.81 C ATOM 2423 C GLN B 798 115.888 11.294 7.496 1.00 20.13 C

ATOM 2424 O GLN B 798 115.627 11.953 8.500 1.00 18.79 O

ATOM 2425 CB GLN B 798 115.604 8.845 7.189 1.00 19.12 C

ATOM 2426 CG GLN B 798 114.695 7.650 7.008 1.00 19.93 C

ATOM 2427 CD GLN B 798 115.435 6.342 7.198 1.00 19.30 C

ATOM 2428 OEl GLN B 798 116.312 6.231 8.053 1.00 20.68 O

ATOM 2429 NE2 GLN B 798 115.084 5.343 6.398 1.00 19.75 N

ATOM 2430 N ILE B 799 116.997 11.464 6.780 1.00 20.53 N

ATOM 2431 CA ILE B 799 118.004 12.455 7.139 1.00 20.09 C

ATOM 2432 C ILE B 799 117.445 13.876 7.108 1.00 20.87 C

ATOM 2433 O ILE B 799 117.861 14.735 7.886 1.00 20.84 O

ATOM 2434 CB ILE B 799 119.216 12.381 6.191 1.00 19.41 C

ATOM 2435 CGl ILE B 799 119.688 10.930 6.070 1.00 19.04 C

ATOM 2436 CG2 ILE B 799 120.354 13.224 6.745 1.00 17.77 C

ATOM 2437 CDl ILE B 799 120.753 10.706 5.025 1.00 17.61 C

ATOM 2438 N THR B 800 116.506 14.119 6.203 1.00 20.57 N

ATOM 2439 CA THR B 800 115.892 15.432 6.087 1.00 21.56 C

ATOM 2440 C THR B 800 115.052 15.733 7.332 1.00 19.08 C

ATOM 2441 O THR B 800 115.282 16.729 8.015 1.00 18.05 O

ATOM 2442 CB THR B 800 114.989 15.528 4.827 1.00 21.24 C

ATOM 2443 OGl THR B 800 115.800 15.451 3.642 1.00 23.62 O

ATOM 2444 CG2 THR B 800 114.222 16.848 4.820 1.00 22.88 C

ATOM 2445 N LEU B 801 114.087 14.860 7.619 1.00 19.02 N

ATOM 2446 CA LEU B 801 113.226 15.047 8.771 1.00 17.33 C

ATOM 2447 C LEU B 801 114.064 15.100 10.031 1.00 17.00 C

ATOM 2448 O LEU B 801 113.639 15.653 11.033 1.00 17.75 O

ATOM 2449 CB LEU B 801 112.177 13.933 8.867 1.00 14.93 C

ATOM 2450 CG LEU B 801 111.036 13.998 7.851 1.00 11.40 C

ATOM 2451 CDl LEU B 801 110.008 12.925 8.172 1.00 14.07 C

ATOM 2452 CD2 LEU B 801 110.390 15.354 7.871 1.00 8.00 C

ATOM 2453 N ILE B 802 115.255 14.516 9.987 1.00 17.39 N

ATOM 2454 CA ILE B 802 116.131 14.578 11.146 1.00 17.50 C

ATOM 2455 C ILE B 802 116.755 15.989 11.231 1.00 19.05 C

ATOM 2456 O ILE B 802 116.749 16.606 12.289 1.00 18.55 O

ATOM 2457 CB ILE B 802 117.247 13.496 11.083 1.00 15.05 C

ATOM 2458 CGl ILE B 802 116.646 12.110 11.350 1.00 13.76 C

ATOM 2459 CG2 ILE B 802 118.326 13.793 12.120 1.00 16.26 C

ATOM 2460 CDl ILE B 802 117.602 10.963 11.155 1.00 7.06 C

ATOM 2461 N GLN B 803 117.271 16.513 10.120 1.00 19.23 N

ATOM 2462 CA GLN B 803 117.878 17.850 10.142 1.00 19.21 C

ATOM 2463 C GLN B 803 116.868 18.946 10.516 1.00 20.69 C

ATOM 2464 O GLN B 803 117.183 19.853 11.285 1.00 20.48 O

ATOM 2465 CB GLN B 803 118.521 18.171 8.785 1.00 17.72 C

ATOM 2466 CG GLN B 803 119.735 17.309 8.469 1.00 16.34 C

ATOM 2467 CD GLN B 803 120.126 17.327 6.996 1.00 16.71 C

ATOM 2468 OEl GLN B 803 119.340 17.710 6.133 1.00 15.94 O

ATOM 2469 NE2 GLN B 803 121.343 16.882 6.704 1.00 18.00 N

ATOM 2470 N TYR B 804 115.655 18.861 9.982 1.00 19.61 N

ATOM 2471 CA TYR B 804 114.630 19.852 10.289 1.00 20.20 C

ATOM 2472 C TYR B 804 114.167 19.813 11.752 1.00 19.45 C

ATOM 2473 O TYR B 804 113.794 20.837 12.317 1.00 19.24 O

ATOM 2474 CB TYR B 804 113.425 19.660 9.362 1.00 21.04 C

ATOM 2475 CG TYR B 804 113.550 20.370 8.030 1.00 23.27 C

ATOM 2476 CDl TYR B 804 113.268 21.728 7.915 1.00 22.08 C

ATOM 2477 CD2 TYR B 804 113.937 19.676 6.880 1.00 24.62 C

ATOM 2478 CEl TYR B 804 113.360 22.384 6.686 1.00 24.42 C

ATOM 2479 CE2 TYR B 804 114.036 20.322 5.646 1.00 24.68 C

ATOM 2480 CZ TYR B 804 113.742 21.672 5.555 1.00 23.58 C

ATOM 2481 OH TYR B 804 113.795 22.298 4.331 1.00 23.08 O

ATOM 2482 N SER B 805 114.216 18.641 12.378 1.00 19.73 N

ATOM 2483 CA SER B 805 113.750 18.530 13.754 1.00 17.44 C

ATOM 2484 C SER B 805 114.799 18.302 14.844 1.00 17.24 C

ATOM 2485 O SER B 805 114.442 18.254 16.019 1.00 17.07 O

ATOM 2486 CB SER B 805 112.699 17.420 13.842 1.00 18.08 C

ATOM 2487 OG SER B 805 113.257 16.153 13.517 1.00 14.36 O

ATOM 2488 N TRP B 806 116.076 18.195 14.485 1.00 15.75 N

ATOM 2489 CA TRP B 806 117.107 17.918 15.491 1.00 17.42 C

ATOM 2490 C TRP B 806 117.033 18.703 16.804 1.00 17.33 C

ATOM 2491 O TRP B 806 117.098 18.109 17.873 1.00 16.68 O

ATOM 2492 CB TRP B 806 118.518 18.050 14.903 1.00 17.24 C

ATOM 2493 CG TRP B 806 119.014 19.447 14.706 1.00 19.59 C

ATOM 2494 CDl TRP B 806 118.759 20.268 13.647 1.00 19.18 C

ATOM 2495 CD2 TRP B 806 119.876 20.178 15.581 1.00 20.36 C

ATOM 2496 NEl TRP B 806 119.413 21.464 13.804 1.00 19.67 N ATOM 2497 CE2 TRP B 806 120.106 21.437 14.985 1.00 20.62 C

ATOM 2498 CE3 TRP B 806 120.481 19.892 16.814 1.00 20.98 C

ATOM 2499 CZ2 TRP B 806 120.911 22.407 15.576 1.00 20.68 C

ATOM 2500 CZ3 TRP B 806 121.284 20.858 17.401 1.00 21.19 C

ATOM 2501 CH2 TRP B 806 121.491 22.100 16.780 1.00 22.27 C

ATOM 2502 N MET B 807 116.893 20.022 16.724 1.00 17.92 N

ATOM 2503 CA MET B 807 116.819 20.858 17.921 1.00 17.88 C

ATOM 2504 C MET B 807 115.635 20.433 18.799 1.00 17.63 C

ATOM 2505 O MET B 807 115.772 20.311 20.022 1.00 16.41 O

ATOM 2506 CB MET B 807 116.697 22.335 17.525 1.00 17.35 C

ATOM 2507 CG MET B 807 116.876 23.308 18.684 1.00 17.21 C

ATOM 2508 SD MET B 807 118.484 23.144 19.551 1.00 19.97 S

ATOM 2509 CE MET B 807 119.767 24.161 18.692 1.00 19.02 C

ATOM 2510 N CYS B 808 114.478 20.208 18.174 1.00 17.37 N

ATOM 2511 CA CYS B 808 113.289 19.754 18.897 1.00 17.38 C

ATOM 2512 C CYS B 808 113.647 18.488 19.685 1.00 16.47 C

ATOM 2513 O CYS B 808 113.399 18.394 20.887 1.00 13.35 O

ATOM 2514 CB CYS B 808 112.145 19.411 17.925 1.00 19.14 C

ATOM 2515 SG CYS B 808 111.333 20.806 17.109 1.00 21.61 S

ATOM 2516 N LEU B 809 114.248 17.522 18.995 1.00 13.73 N

ATOM 2517 CA LEU B 809 114.618 16.263 19.629 1.00 14.58 C

ATOM 2518 C LEU B 809 115.509 16.427 20.860 1.00 15.05 C

ATOM 2519 O LEU B 809 115.128 16.050 21.965 1.00 14.55 O

ATOM 2520 CB LEU B 809 115.322 15.354 18.623 1.00 15.25 C

ATOM 2521 CG LEU B 809 114.560 14.965 17.355 1.00 12.10 C

ATOM 2522 CDl LEU B 809 115.479 14.123 16.482 1.00 15.95 C

ATOM 2523 CD2 LEU B 809 113.299 14.193 17.710 1.00 12.55 C

ATOM 2524 N LEU B 810 116.695 16.991 20.664 1.00 15.66 N

ATOM 2525 CA LEU B 810 117.639 17.171 21.757 1.00 14.94 C

ATOM 2526 C LEU B 810 117.130 18.009 22.938 1.00 14.69 C

ATOM 2527 O LEU B 810 117.445 17.701 24.087 1.00 12.19 O

ATOM 2528 CB LEU B 810 118.944 17.754 21.215 1.00 12.94 C

ATOM 2529 CG LEU B 810 119.619 16.904 20.133 1.00 15.68 C

ATOM 2530 CDl LEU B 810 120.849 17.617 19.578 1.00 16.24 C

ATOM 2531 CD2 LEU B 810 120.004 15.559 20.714 1.00 13.89 C

ATOM 2532 N SER B 811 116.357 19.061 22.667 1.00 15.05 N

ATOM 2533 CA SER B 811 115.843 19.905 23.739 1.00 14.65 C

ATOM 2534 C SER B 811 114.801 19.140 24.543 1.00 15.90 C

ATOM 2535 O SER B 811 114.862 19.088 25.772 1.00 12.66 O

ATOM 2536 CB SER B 811 115.224 21.186 23.174 1.00 13.79 C

ATOM 2537 OG SER B 811 114.117 20.915 22.333 1.00 16.33 O

ATOM 2538 N PHE B 812 113.853 18.541 23.828 1.00 17.18 N

ATOM 2539 CA PHE B 812 112.786 17.756 24.435 1.00 17.60 C

ATOM 2540 C PHE B 812 113.390 16.647 25.311 1.00 17.31 C

ATOM 2541 O PHE B 812 112.814 16.244 26.325 1.00 15.46 O

ATOM 2542 CB PHE B 812 111.931 17.145 23.321 1.00 15.81 C

ATOM 2543 CG PHE B 812 110.708 16.429 23.807 1.00 15.06 C

ATOM 2544 CDl PHE B 812 109.733 17.102 24.538 1.00 17.53 C

ATOM 2545 CD2 PHE B 812 110.513 15.083 23.510 1.00 14.87 C

ATOM 2546 CEl PHE B 812 108.576 16.445 24.969 1.00 13.14 C

ATOM 2547 CE2 PHE B 812 109.363 14.424 23.935 1.00 15.32 C

ATOM 2548 CZ PHE B 812 108.395 15.114 24.668 1.00 15.17 C

ATOM 2549 N ALA B 813 114.559 16.165 24.903 1.00 19.08 N

ATOM 2550 CA ALA B 813 115.249 15.100 25.619 1.00 18.74 C

ATOM 2551 C ALA B 813 115.927 15.685 26.839 1.00 19.66 C

ATOM 2552 O ALA B 813 116.160 14.993 27.829 1.00 16.94 O

ATOM 2553 CB ALA B 813 116.282 14.442 24.708 1.00 20.35 C

ATOM 2554 N LEU B 814 116.261 16.968 26.746 1.00 20.05 N

ATOM 2555 CA LEU B 814 116.903 17.665 27.842 1.00 19.68 C

ATOM 2556 C LEU B 814 115.873 17.861 28.960 1.00 21.34 C

ATOM 2557 O LEU B 814 116.186 17.716 30.144 1.00 20.41 O

ATOM 2558 CB LEU B 814 117.455 19.003 27.344 1.00 17.16 C

ATOM 2559 CG LEU B 814 117.777 20.070 28.392 1.00 18.57 C

ATOM 2560 CDl LEU B 814 118.630 19.489 29.501 1.00 14.89 C

ATOM 2561 CD2 LEU B 814 118.471 21.232 27.708 1.00 18.54 C

ATOM 2562 N SER B 815 114.638 18.180 28.588 1.00 21.48 N

ATOM 2563 CA SER B 815 113.601 18.353 29.597 1.00 22.36 C

ATOM 2564 C SER B 815 113.406 17.010 30.314 1.00 21.38 C

ATOM 2565 O SER B 815 113.189 16.974 31.530 1.00 18.93 O

ATOM 2566 CB SER B 815 112.285 18.808 28.953 1.00 22.92 C

ATOM 2567 OG SER B 815 111.773 17.819 28.082 1.00 24.32 O

ATOM 2568 N TRP B 816 113.503 15.913 29.562 1.00 18.65 N

ATOM 2569 CA TRP B 816 113.344 14.583 30.148 1.00 18.77 C

ATOM 2570 C TRP B 816 114.370 14.272 31.234 1.00 18.76 C ATOM 2571 O TRP B 816 113.997 14.102 32.392 1.00 19.30 O

ATOM 2572 CB TRP B 816 113.406 13.485 29.084 1.00 15.69 C

ATOM 2573 CG TRP B 816 113.232 12.115 29.686 1.00 13.79 C

ATOM 2574 CDl TRP B 816 114.184 11.143 29.810 1.00 12.93 C

ATOM 2575 CD2 TRP B 816 112.039 11.582 30.276 1.00 12.20 C

ATOM 2576 NEl TRP B 816 113.658 10.041 30.440 1.00 10.34 N

ATOM 2577 CE2 TRP B 816 112.342 10.287 30.733 1.00 11.57 C

ATOM 2578 CE3 TRP B 816 110.741 12.076 30.458 1.00 11.28 C

ATOM 2579 CZ2 TRP B 816 111.396 9.481 31.357 1.00 11.04 C

ATOM 2580 CZ3 TRP B 816 109.807 11.277 31.073 1.00 11.30 C

ATOM 2581 CH2 TRP B 816 110.137 9.990 31.517 1.00 11.39 C

ATOM 2582 N ARG B 817 115.644 14.173 30.856 1.00 17.69 N

ATOM 2583 CA ARG B 817 116.710 13.885 31.809 1.00 17.88 C

ATOM 2584 C ARG B 817 116.672 14.882 32.975 1.00 18.03 C

ATOM 2585 O ARG B 817 116.923 14.516 34.121 1.00 17.30 O

ATOM 2586 CB ARG B 817 118.084 13.962 31.126 1.00 17.15 C

ATOM 2587 CG ARG B 817 118.330 12.967 30.003 1.00 18.05 C

ATOM 2588 CD ARG B 817 119.756 13.111 29.467 1.00 18.88 C

ATOM 2589 NE ARG B 817 120.025 14.440 28.915 1.00 15.29 N

ATOM 2590 CZ ARG B 817 119.625 14.849 27.712 1.00 18.15 C

ATOM 2591 NHl ARG B 817 118.938 14.033 26.927 1.00 16.76 N

ATOM 2592 NH2 ARG B 817 119.916 16.074 27.286 1.00 14.97 N

ATOM 2593 N SER B 818 116.371 16.142 32.678 1.00 18.90 N

ATOM 2594 CA SER B 818 116.289 17.177 33.715 1.00 20.18 C

ATOM 2595 C SER B 818 115.143 16.818 34.643 1.00 20.55 C

ATOM 2596 O SER B 818 115.279 16.835 35.871 1.00 22.66 O

ATOM 2597 CB SER B 818 116.031 18.553 33.087 1.00 20.20 C

ATOM 2598 OG SER B 818 117.134 18.976 32.297 1.00 19.93 O

ATOM 2599 N TYR B 819 114.013 16.488 34.028 1.00 18.45 N

ATOM 2600 CA TYR B 819 112.809 16.090 34.732 1.00 17.91 C

ATOM 2601 C TYR B 819 113.084 14.767 35.445 1.00 18.54 C

ATOM 2602 O TYR B 819 112.703 14.570 36.599 1.00 15.19 O

ATOM 2603 CB TYR B 819 111.679 15.950 33.704 1.00 15.91 C

ATOM 2604 CG TYR B 819 110.462 15.158 34.131 1.00 17.10 C

ATOM 2605 CDl TYR B 819 109.828 15.400 35.357 1.00 17.40 C

ATOM 2606 CD2 TYR B 819 109.885 14.233 33.265 1.00 16.23 C

ATOM 2607 CEl TYR B 819 108.649 14.745 35.698 1.00 18.46 C

ATOM 2608 CE2 TYR B 819 108.701 13.572 33.595 1.00 18.98 C

ATOM 2609 CZ TYR B 819 108.088 13.836 34.812 1.00 16.96 C

ATOM 2610 OH TYR B 819 106.911 13.210 35.127 1.00 18.36 O

ATOM 2611 N LYS B 820 113.790 13.882 34.749 1.00 21.84 N

ATOM 2612 CA LYS B 820 114.129 12.564 35.265 1.00 24.87 C

ATOM 2613 C LYS B 820 115.082 12.620 36.459 1.00 26.17 C

ATOM 2614 O LYS B 820 114.673 12.830 37.597 1.00 27.97 O

ATOM 2615 CB LYS B 820 114.758 11.721 34.149 1.00 27.00 C

ATOM 2616 CG LYS B 820 114.488 10.215 34.232 1.00 29.98 C

ATOM 2617 CD LYS B 820 115.000 9.591 35.525 1.00 32.25 C

ATOM 2618 CE LYS B 820 114.548 8.141 35.645 1.00 34.19 C

ATOM 2619 NZ LYS B 820 115.155 7.444 36.814 1.00 34.80 N

ATOM 2620 N HIS B 821 116.361 12.427 36.173 1.00 28.05 N

ATOM 2621 CA HIS B 821 117.411 12.404 37.180 1.00 27.26 C

ATOM 2622 C HIS B 821 117.374 13.452 38.288 1.00 26.79 C

ATOM 2623 O HIS B 821 117.696 13.145 39.433 1.00 29.46 O

ATOM 2624 CB HIS B 821 118.771 12.460 36.480 1.00 28.56 C

ATOM 2625 CG HIS B 821 118.886 11.524 35.317 1.00 29.31 C

ATOM 2626 NDl HIS B 821 118.560 10.188 35.404 1.00 29.23 N

ATOM 2627 CD2 HIS B 821 119.278 11.733 34.038 1.00 29.18 C

ATOM 2628 CEl HIS B 821 118.746 9.614 34.229 1.00 30.56 C

ATOM 2629 NE2 HIS B 821 119.180 10.529 33.383 1.00 29.73 N

ATOM 2630 N THR B 822 116.983 14.681 37.976 1.00 26.20 N

ATOM 2631 CA THR B 822 116.975 15.727 39.001 1.00 24.35 C

ATOM 2632 C THR B 822 115.616 16.342 39.329 1.00 24.88 C

ATOM 2633 O THR B 822 115.530 17.311 40.080 1.00 23.31 O

ATOM 2634 CB THR B 822 117.984 16.853 38.626 1.00 21.95 C

ATOM 2635 OGl THR B 822 117.384 18.143 38.817 1.00 18.62 O

ATOM 2636 CG2 THR B 822 118.421 16.707 37.179 1.00 21.75 C

ATOM 2637 N ASN B 823 114.553 15.772 38.777 1.00 26.66 N

ATOM 2638 CA ASN B 823 113.206 16.276 39.027 1.00 29.13 C

ATOM 2639 C ASN B 823 112.991 17.691 38.502 1.00 29.99 C

ATOM 2640 O ASN B 823 112.247 18.487 39.084 1.00 30.69 O

ATOM 2641 CB ASN B 823 112.887 16.185 40.524 1.00 28.71 C

ATOM 2642 CG ASN B 823 112.756 14.743 40.995 1.00 29.09 C

ATOM 2643 ODl ASN B 823 113.286 13.831 40.368 1.00 29.15 O

ATOM 2644 ND2 ASN B 823 112.057 14.534 42.102 1.00 29.60 N ATOM 2645 N SER B 824 113.674 17.995 37.402 1.00 30.72 N

ATOM 2646 CA SER B 824 113.552 19.272 36.700 1.00 32.55 C

ATOM 2647 C SER B 824 114.247 20.537 37.202 1.00 32.02 C

ATOM 2648 O SER B 824 114.663 21.361 36.384 1.00 33.37 O

ATOM 2649 CB SER B 824 112.068 19.586 36.482 1.00 32.05 C

ATOM 2650 OG SER B 824 111.439 18.549 35.748 1.00 32.96 O

ATOM 2651 N GLN B 825 114.380 20.707 38.516 1.00 31.37 N

ATOM 2652 CA GLN B 825 115.006 21.920 39.051 1.00 28.75 C

ATOM 2653 C GLN B 825 116.332 22.249 38.373 1.00 27.16 C

ATOM 2654 O GLN B 825 116.742 23.406 38.335 1.00 26.48 O

ATOM 2655 CB GLN B 825 115.246 21.794 40.556 1.00 29.65 C

ATOM 2656 CG GLN B 825 115.385 23.141 41.268 1.00 30.16 C

ATOM 2657 CD GLN B 825 116.531 23.177 42.260 1.00 29.59 C

ATOM 2658 OEl GLN B 825 117.636 23.610 41.932 1.00 30.60 O

ATOM 2659 NE2 GLN B 825 116.277 22.714 43.479 1.00 28.77 N

ATOM 2660 N PHE B 826 116.997 21.223 37.851 1.00 26.25 N

ATOM 2661 CA PHE B 826 118.279 21.381 37.169 1.00 23.48 C

ATOM 2662 C PHE B 826 118.167 20.940 35.712 1.00 22.65 C

ATOM 2663 O PHE B 826 117.339 20.087 35.379 1.00 21.68 O

ATOM 2664 CB PHE B 826 119.357 20.511 37.815 1.00 23.38 C

ATOM 2665 CG PHE B 826 119.611 20.805 39.257 1.00 24.24 C

ATOM 2666 CDl PHE B 826 118.653 20.517 40.222 1.00 25.31 C

ATOM 2667 CD2 PHE B 826 120.832 21.334 39.662 1.00 25.35 C

ATOM 2668 CEl PHE B 826 118.909 20.747 41.571 1.00 24.98 C

ATOM 2669 CE2 PHE B 826 121.097 21.569 41.009 1.00 26.83 C

ATOM 2670 CZ PHE B 826 120.133 21.273 41.964 1.00 26.38 C

ATOM 2671 N LEU B 827 119.013 21.515 34.858 1.00 20.43 N

ATOM 2672 CA LEU B 827 119.052 21.165 33.441 1.00 19.12 C

ATOM 2673 C LEU B 827 120.126 20.092 33.246 1.00 19.48 C

ATOM 2674 O LEU B 827 121.316 20.395 33.212 1.00 17.36 O

ATOM 2675 CB LEU B 827 119.385 22.393 32.583 1.00 20.01 C

ATOM 2676 CG LEU B 827 118.263 23.342 32.129 1.00 16.86 C

ATOM 2677 CDl LEU B 827 118.849 24.433 31.249 1.00 18.78 C

ATOM 2678 CD2 LEU B 827 117.216 22.570 31.344 1.00 18.22 C

ATOM 2679 N TYR B 828 119.696 18.841 33.107 1.00 20.59 N

ATOM 2680 CA TYR B 828 120.626 17.728 32.942 1.00 21.69 C

ATOM 2681 C TYR B 828 121.053 17.542 31.489 1.00 20.63 C

ATOM 2682 O TYR B 828 120.561 16.651 30.796 1.00 19.55 O

ATOM 2683 CB TYR B 828 119.991 16.438 33.480 1.00 22.20 C

ATOM 2684 CG TYR B 828 120.965 15.303 33.745 1.00 21.57 C

ATOM 2685 CDl TYR B 828 121.506 14.556 32.697 1.00 23.90 C

ATOM 2686 CD2 TYR B 828 121.331 14.963 35.049 1.00 23.05 C

ATOM 2687 CEl TYR B 828 122.388 13.490 32.942 1.00 23.59 C

ATOM 2688 CE2 TYR B 828 122.214 13.900 35.307 1.00 23.68 C

ATOM 2689 CZ TYR B 828 122.734 13.170 34.246 1.00 25.07 C

ATOM 2690 OH TYR B 828 123.592 12.117 34.487 1.00 28.70 O

ATOM 2691 N PHE B 829 121.967 18.395 31.035 1.00 20.27 N

ATOM 2692 CA PHE B 829 122.470 18.318 29.672 1.00 19.43 C

ATOM 2693 C PHE B 829 123.209 16.995 29.463 1.00 19.26 C

ATOM 2694 O PHE B 829 123.072 16.355 28.421 1.00 17.03 O

ATOM 2695 CB PHE B 829 123.421 19.487 29.375 1.00 18.37 C

ATOM 2696 CG PHE B 829 122.721^' 20.791 29.085 1.00 19.63 C

ATOM 2697 CDl PHE B 829 122.385 21.663 30.109 1.00 21.39 C

ATOM 2698 CD2 PHE B 829 122.383 21.138 27.779 1.00 19.21 C

ATOM 2699 CEl PHE B 829 121.722 22.868 29.837 1.00 22.39 C

ATOM 2700 CE2 PHE B 829 121.724 22.327 27.500 1.00 20.64 C

ATOM 2701 CZ PHE B 829 121.392 23.196 28.530 1.00 20.15 C

ATOM 2702 N ALA B 830 123.989 16.605 30.466 1.00 20.33 N

ATOM 2703 CA ALA B 830 124.770 15.375 30.440 1.00 22.37 C

ATOM 2704 C ALA B 830 125.341 15.126 31.839 1.00 24.59 C

ATOM 2705 O ALA B 830 125.481 16.055 32.636 1.00 26.01 O

ATOM 2706 CB ALA B 830 125.899 15.501 29.425 1.00 24.51 C

ATOM 2707 N PRO B 831 125.673 13.865 32.156 1.00 25.78 N

ATOM 2708 CA PRO B 831 126.229 13.483 33.458 1.00 26.60 C

ATOM 2709 C PRO B 831 127.240 14.468 34.040 1.00 27.12 C

ATOM 2710 O PRO B 831 127.191 14.782 35.227 1.00 27.11 O

ATOM 2711 CB PRO B 831 126.849 12.127 33.169 1.00 25.87 C

ATOM 2712 CG PRO B 831 125.874 11.545 32.216 1.00 25.53 C

ATOM 2713 CD PRO B 831 125.602 12.694 31.266 1.00 25.45 C

ATOM 2714 N ASP B 832 128.149 14.955 33.200 1.00 27.90 N

ATOM 2715 CA ASP B 832 129.177 15.893 33.644 1.00 27.70 C

ATOM 2716 C ASP B 832 128.878 17.313 33.185 1.00 28.27 C

ATOM 2717 O ASP B 832 129.785 18.146 33.103 1.00 28.72 O

ATOM 2718 CB ASP B 832 130.531 15.488 33.080 1.00 27.31 C

ATOM 2793 C HIS B 841 125.500 32.852 32.515 1.00 36.94 C

ATOM 2794 O HIS B 841 125.390 33.361 31.400 1.00 37.15 O

ATOM 2795 CB HIS B 841 124.616 33.609 34.717 1.00 38.13 C

ATOM 2796 N GLN B 842 126.632 32.322 32.969 1.00 36.98 N

ATOM 2797 CA GLN B 842 127.862 32.312 32.182 1.00 36.42 C

ATOM 2798 C GLN B 842 127.729 31.503 30.895 1.00 35.79 C

ATOM 2799 O GLN B 842 128.723 31.240 30.218 1.00 37.75 O

ATOM 2800 CB GLN B 842 129.019 31.758 33.025 1.00 36.65 C

ATOM 2801 CG GLN B 842 129.285 32.539 34.311 1.00 35.39 C

ATOM 2802 CD GLN B 842 130.002 33.856 34.074 1.00 36.40 C

ATOM 2803 OEl GLN B 842 131.208 33.880 33.813 1.00 36.59 O

ATOM 2804 NE2 GLN B 842 129.263 34.959 34.156 1.00 35.07 N

ATOM 2805 N SER B 843 126.506 31.093 30.564 1.00 34.33 N

ATOM 2806 CA SER B 843 126.265 30.344 29.334 1.00 32.10 C

ATOM 2807 C SER B 843 125.745 31.351 28.316 1.00 31.30 C

ATOM 2808 O SER B 843 125.549 31.026 27.137 1.00 30.17 O

ATOM 2809 CB SER B 843 125.218 29.236 29.545 1.00 31.75 C

ATOM 2810 OG SER B 843 123.892 29.733 29.463 1.00 29.25 O

ATOM 2811 N ALA B 844 125.538 32.582 28.786 1.00 29.17 N

ATOM 2812 CA ALA B 844 125.031 33.670 27.952 1.00 28.58 C

ATOM 2813 C ALA B 844 123.824 33.151 27.185 1.00 27.58 C

ATOM 2814 O ALA B 844 123.492 33.633 26.100 1.00 27.06 O

ATOM 2815 CB ALA B 844 126.113 34.146 26.987 1.00 26.74 C

ATOM 2816 N MET B 845 123.165 32.165 27.782 1.00 27.44 N

ATOM 2817 CA MET B 845 122.003 31.533 27.183 1.00 28.14 C

ATOM 2818 C MET B 845 120.904 31.385 28.233 1.00 27.41 C

ATOM 2819 O MET B 845 119.951 30.629 28.052 1.00 26.21 O

ATOM 2820 CB MET B 845 122.420 30.166 26.647 1.00 29.50 C

ATOM 2821 CG MET B 845 121.421 29.492 25.752 1.00 31.14 C

ATOM 2822 SD MET B 845 122.000 27.848 25.380 1.00 33.39 S

ATOM 2823 CE MET B 845 121.393 26.977 26.820 1.00 32.58 C

ATOM 2824 N TYR B 846 121.062 32.119 29.331 1.00 28.07 N

ATOM 2825 CA TYR B 846 120.117 32.103 30.444 1.00 27.46 C

ATOM 2826 C TYR B 846 118.691 32.262 29.957 1.00 27.62 C

ATOM 2827 O TYR B 846 117.765 31.634 30.480 1.00 28.13 O

ATOM 2828 CB TYR B 846 120.444 33.233 31.414 1.00 29.07 C

ATOM 2829 CG TYR B 846 119.486 33.361 32.573 1.00 30.54 C

ATOM 2830 CDl TYR B 846 119.354 32.338 33.515 1.00 29.13 C

ATOM 2831 CD2 TYR B 846 118.720 34.512 32.738 1.00 30.53 C

ATOM 2832 CEl TYR B 846 118.483 32.462 34.590 1.00 30.99 C

ATOM 2833 CE2 TYR B 846 117.847 34.648 33.812 1.00 31.16 C

ATOM 2834 CZ TYR B 846 117.734 33.622 34.733 1.00 30.44 C

ATOM 2835 OH TYR B 846 116.884 33.766 35.801 1.00 30.67 O

ATOM 2836 N GLU B 847 118.523 33.110 28.952 1.00 25.79 N

ATOM 2837 CA GLU B 847 117.217 33.373 28.375 1.00 25.63 C

ATOM 2838 C GLU B 847 116.626 32.147 27.705 1.00 23.91 C

ATOM 2839 O GLU B 847 115.410 31.918 27.757 1.00 22.97 O

ATOM 2840 CB GLU B 847 117.321 34.518 27.366 1.00 28.26 C

ATOM 2841 CG GLU B 847 117.750 35.829 27.990 1.00 30.44 C

ATOM 2842 CD GLU B 847 116.948 36.152 29.235 1.00 32.97 C

ATOM 2843 OEl GLU B 847 117.121 35.443 30.251 1.00 33.08 O

ATOM 2844 OE2 GLU B 847 116.139 37.104 29.193 1.00 32.62 O

ATOM 2845 N LEU B 848 117.482 31.360 27.067 1.00 21.80 N

ATOM 2846 CA LEU B 848 117.025 30.153 26.391 1.00 21.00 C

ATOM 2847 C LEU B 848 116.858 29.039 27.411 1.00 19.37 C

ATOM 2848 O LEU B 848 115.861 28.310 27.396 1.00 19.40 O

ATOM 2849 CB LEU B 848 118.017 29.730 25.300 1.00 20.30 C

ATOM 2850 CG LEU B 848 118.250 30.682 24.121 1.00 22.46 C

ATOM 2851 CDl LEU B 848 119.401 31.639 24.433 1.00 22.79 C

ATOM 2852 CD2 LEU B 848 118.574 29.869 22.869 1.00 24.25 C

ATOM 2853 N CYS B 849 117.840 28.910 28.297 1.00 19.79 N

ATOM 2854 CA CYS B 849 117.787 27.894 29.334 1.00 20.05 C

ATOM 2855 C CYS B 849 116.449 28.007 30.036 1.00 20.16 C

ATOM 2856 O CYS B 849 115.800 27.003 30.305 1.00 20.01 O

ATOM 2857 CB CYS B 849 118.918 28.085 30.349 1.00 19.75 C

ATOM 2858 SG CYS B 849 120.565 27.544 29.792 1.00 21.77 S

ATOM 2859 N GLN B 850 116.032 29.242 30.301 1.00 20.34 N

ATOM 2860 CA GLN B 850 114.767 29.500 30.981 1.00 20.59 C

ATOM 2861 C GLN B 850 113.588 28.847 30.284 1.00 19.09 C

ATOM 2862 O GLN B 850 112.728 28.262 30.940 1.00 18.20 O

ATOM 2863 CB GLN B 850 114.531 31.009 31.101 1.00 22.32 C

ATOM 2864 CG GLN B 850 115.190 31.626 32.309 1.00 23.21 C

ATOM 2865 CD GLN B 850 114.425 31.355 33.591 1.00 25.85 C

ATOM 2866 OEl GLN B 850 114.199 30.198 33.970 1.00 25.31 O ATOM 2867 NE2 GLN B 850 114.017 32.427 34.269 1.00 24.13 N

ATOM 2868 N GLY B 851 113.544 28.959 28.956 1.00 18.49 N

ATOM 2869 CA GLY B 851 112.463 28.349 28.201 1.00 14.61 C

ATOM 2870 C GLY B 851 112.554 26.832 28.177 1.00 14.05 C

ATOM 2871 O GLY B 851 111.541 26.139 28.132 1.00 11.08 O

ATOM 2872 N MET B 852 113.765 26.296 28.203 1.00 14.96 N

ATOM 2873 CA MET B 852 113.907 24.844 28.182 1.00 17.74 C

ATOM 2874 C MET B 852 113.497 24.289 29.541 1.00 20.65 C

ATOM 2875 O MET B 852 112.693 23.360 29.627 1.00 20.06 O

ATOM 2876 CB MET B 852 115.344 24.439 27.856 1.00 18.08 C

ATOM 2877 CG MET B 852 115.717 24.637 26.392 1.00 18.19 C

ATOM 2878 SD MET B 852 117.345 23.948 26.017 1.00 19.85 S

ATOM 2879 CE MET B 852 118.397 25.273 26.454 1.00 17.76 C

ATOM 2880 N HIS B 853 114.048 24.866 30.604 1.00 21.66 N

ATOM 2881 CA HIS B 853 113.699 24.419 31.947 1.00 23.74 C

ATOM 2882 C HIS B 853 112.189 24.553 32.137 1.00 24.05 C

ATOM 2883 O HIS B 853 111.577 23.785 32.878 1.00 26.30 O

ATOM 2884 CB HIS B 853 114.458 25.238 32.990 1.00 21.43 C

ATOM 2885 CG HIS B 853 113.982 25.024 34.394 1.00 22.41 C

ATOM 2886 NDl HIS B 853 112.896 25.690 34.920 1.00 21.42 N

ATOM 2887 CD2 HIS B 853 114.445 24.220 35.380 1.00 22.67 C

ATOM 2888 CEl HIS B 853 112.712 25.308 36.171 1.00 20.88 C

ATOM 2889 NE2 HIS B 853 113.638 24.416 36.476 1.00 21.81 N

ATOM 2890 N GLN B 854 111.595 25.527 31.449 1.00 25.29 N

ATOM 2891 CA GLN B 854 110.150 25.767 31.506 1.00 24.34 C

ATOM 2892 C GLN B 854 109.428 24.491 31.102 1.00 23.97 C

ATOM 2893 O GLN B 854 108.491 24.046 31.768 1.00 25.11 O

ATOM 2894 CB GLN B 854 109.762 26.881 30.532 1.00 26.50 C

ATOM 2895 CG GLN B 854 108.271 26.932 30.202 1.00 26.68 C

ATOM 2896 CD GLN B 854 107.456 27.585 31.294 1.00 26.74 C

ATOM 2897 OEl GLN B 854 107.532 27.201 32.461 1.00 26.78 O

ATOM 2898 NE2 GLN B 854 106.668 28.582 30.920 1.00 28.23 N

ATOM 2899 N ILE B 855 109.864 23.922 29.986 1.00 22.88 N

ATOM 2900 CA ILE B 855 109.289 22.689 29.473 1.00 21.05 C

ATOM 2901 C ILE B 855 109.417 21.625 30.549 1.00 19.54 C

ATOM 2902 O ILE B 855 108.460 20.919 30.850 1.00 20.71 O

ATOM 2903 CB ILE B 855 110.031 22.218 28.199 1.00 19.11 C

ATOM 2904 CGl ILE B 855 109.873 23.261 27.094 1.00 18.87 C

ATOM 2905 CG2 ILE B 855 109.520 20.859 27.761 1.00 19.69 C

ATOM ■ 2906 CDl ILE B 855 108.444 23.617 26.780 1.00 14.77 C

ATOM 2907 N SER B 856 110.606 21.533 31.133 1.00 18.75 N

ATOM 2908 CA SER B 856 110.896 20.564 32.188 1.00 18.87 C

ATOM 2909 C SER B 856 109.862 20.581 33.313 1.00 18.49 C

ATOM 2910 O SER B 856 109.479 19.529 33.825 1.00 17.77 O

ATOM 2911 CB SER B 856 112.281 20.841 32.780 1.00 17.23 C

ATOM 2912 OG SER B 856 113.134 21.426 31.809 1.00 20.89 O

ATOM 2913 N LEU B 857 109.429 21.775 33.710 1.00 19.07 N

ATOM 2914 CA LEU B 857 108.442 21.904 34.777 1.00 19.01 C

ATOM 2915 C LEU B 857 107.063 21.472 34.292 1.00 20.72 C

ATOM 2916 O LEU B 857 106.314 20.824 35.026 1.00 20.43 O

ATOM 2917 CB LEU B 857 108.375 23.348 35.289 1.00 18.24 C

ATOM 2918 CG LEU B 857 109.670 24.045 35.720 1.00 16.97 C

ATOM 2919 CDl LEU B 857 109.331 25.438 36.260 1.00 15.91 C

ATOM 2920 CD2 LEU B 857 110.393 23.224 36.781 1.00 14.59 C

ATOM 2921 N GLN B 858 106.720 21.824 33.055 1.00 20.32 N

ATOM 2922 CA GLN B 858 105.425 21.434 32.533 1.00 20.04 C

ATOM 2923 C GLN B 858 105.378 19.910 32.580 1.00 20.08 C

ATOM 2924 O GLN B 858 104.306 19.312 32.715 1.00 19.10 O

ATOM 2925 CB GLN B 858 105.242 21.929 31.096 1.00 20.88 C

ATOM 2926 CG GLN B 858 105.507 23.416 30.875 1.00 22.65 C

ATOM 2927 CD GLN B 858 104.618 24.331 31.702 1.00 22.72 C

ATOM 2928 OEl GLN B 858 103.510 23.960 32.090 1.00 24.51 O

ATOM 2929 NE2 GLN B 858 105.093 25.549 31.949 1.00 21.76 N

ATOM 2930 N PHE B 859 106.556 19.296 32.474 1.00 19.14 N

ATOM 2931 CA PHE B 859 106.703 17.843 32.529 1.00 20.23 C

ATOM 2932 C PHE B 859 106.277 17.395 33.927 1.00 21.23 C

ATOM 2933 O PHE B 859 105.614 16.368 34.090 1.00 20.82 O

ATOM 2934 CB PHE B 859 108.172 17.449 32.315 1.00 20.13 C

ATOM 2935 CG PHE B 859 108.540 17.137 30.882 1.00 18.90 C

ATOM 2936 CDl PHE B 859 108.121 17.951 29.833 1.00 20.46 C

ATOM 2937 CD2 PHE B 859 109.341 16.037 30.595 1.00 19.09 C

ATOM 2938 CEl PHE B 859 108.496 17.668 28.506 1.00 20.49 C

ATOM 2939 CE2 PHE B 859 109.725 15.744 29.277 1.00 20.26 C

ATOM 2940 CZ PHE B 859 109.299 16.563 28.231 1.00 18.00 C

ATOM 3015 CB GLU B 868 103.118 9.776 27.636 1.00 19.67 C

ATOM 3016 CG GLU B 868 103.363 11.234 27.975 1.00 20.60 C

ATOM 3017 CD GLU B 868 102.557 11.669 29.199 1.00 22.58 C

ATOM 3018 OEl GLU B 868 102.629 12.857 29.583 1.00 20.99 O

ATOM 3019 OE2 GLU B 868 101.854 10.811 29.777 1.00 20.27 O

ATOM 3020 N TYR B 869 106.179 10.086 26.548 1.00 17.88 N

ATOM 3021 CA TYR B 869 107.318 10.910 26.152 1.00 16.45 C

ATOM 3022 C TYR B 869 107.919 10.346 24.872 1.00 15.83 C

ATOM 3023 O TYR B 869 108.074 11.046 23.872 1.00 13.82 O

ATOM 3024 CB TYR B 869 108.372 10.873 27.264 1.00 16.27 C

ATOM 3025 CG TYR B 869 109.812 10.997 26.799 1.00 17.29 C

ATOM 3026 CDl TYR B 869 110.305 12.200 26.294 1.00 13.27 C

ATOM 3027 CD2 TYR B 869 110.695 9.925 26.928 1.00 16.08 C

ATOM 3028 CEl TYR B 869 111.635 12.343 25.942 1.00 14.16 C

ATOM 3029 CE2 TYR B 869 112.044 10.057 26.570 1.00 18.02 C

ATOM 3030 CZ TYR B 869 112.501 11.273 26.080 1.00 16.02 C

ATOM 3031 OH TYR B 869 113.816 11.419 25.731 1.00 15.24 O

ATOM 3032 N THR B 870 108.251 9.061 24.926 1.00 15.11 N

ATOM 3033 CA THR B 870 108.845 8.379 23.800 1.00 15.29 C

ATOM 3034 C THR B 870 108.037 8.572 22.511 1.00 14.44 C

ATOM 3035 O THR B 870 108.615 8.663 21.443 1.00 14.75 O

ATOM 3036 CB THR B 870 109.001 6.870 24.086 1.00 13.64 C

ATOM 3037 OGl THR B 870 109.715 6.255 23.004 1.00 16.11 O

ATOM 3038 CG2 THR B 870 107.645 6.211 24.216 1.00 11.56 C

ATOM 3039 N ILE B 871 106.711 8.633 22.609 1.00 14.43 N

ATOM 3040 CA ILE B 871 105.888 8.823 21.415 1.00 15.25 C

ATOM 3041 C ILE B 871 105.868 10.291 20.989 1.00 15.44 C

ATOM 3042 O ILE B 871 105.783 10.600 19.803 1.00 12.69 O

ATOM 3043 CB ILE B 871 104.431 8.329 21.626 1.00 14.55 C

ATOM 3044 CGl ILE B 871 103.616 8.584 20.365 1.00 15.06 C

ATOM 3045 CG2 ILE B 871 103.797 9.032 22.808 1.00 16.81 C

ATOM 3046 CDl ILE B 871 102.233 8.053 20.415 1.00 16.40 C

ATOM 3047 N MET B 872 105.954 11.188 21.966 1.00 17.26 N

ATOM 3048 CA MET B 872 105.959 12.617 21.691 1.00 17.97 C

ATOM 3049 C MET B 872 107.270 12.983 21.022 1.00 18.66 C

ATOM 3050 O MET B 872 107.346 13.932 20.235 1.00 21.54 O

ATOM 3051 CB MET B 872 105.797 13.409 22.988 1.00 17.80 C

ATOM 3052 CG MET B 872 104.357 13.553 23.446 1.00 19.84 C

ATOM 3053 SD MET B 872 104.234 13.989 25.202 1.00 23.27 S

ATOM 3054 CE MET B 872 104.896 15.618 25.214 1.00 20.71 C

ATOM 3055 N LYS B 873 108.312 12.227 21.337 1.00 17.12 N

ATOM 3056 CA LYS B 873 109.607 12.486 20.741 1.00 14.19 C

ATOM 3057 C LYS B 873 109.504 12.129 19.255 1.00 14.10 C

ATOM 3058 O LYS B 873 110.018 12.858 18.398 1.00 13.75 O

ATOM 3059 CB LYS B 873 110.690 11.657 21.456 1.00 12.09 C

ATOM 3060 CG LYS B 873 112.107 12.171 21.236 1.00 11.43 C

ATOM 3061 CD LYS B 873 113.035 11.817 22.395 1.00 14.16 C

ATOM 3062 CE LYS B 873 113.753 10.478 22.201 1.00 13.99 C

ATOM 3063 NZ LYS B 873 112.864 9.318 21.937 1.00 10.58 N

ATOM 3064 N VAL B 874 108.823 11.026 18.934 1.00 12.94 N

ATOM 3065 CA VAL B 874 108.688 10.653 17.523 1.00 12.72 C

ATOM 3066 C VAL B 874 107.814 11.664 16.795 1.00 12.12 C

ATOM 3067 O VAL B 874 107.995 11.926 15.601 1.00 12.49 O

ATOM 3068 CB VAL B 874 108.090 9.232 17.333 1.00 13.72 C

ATOM 3069 CGl VAL B 874 107.762 9.000 15.846 1.00 10.66 C

ATOM 3070 CG2 VAL B 874 109.092 8.181 17.804 1.00 12.65 C

ATOM 3071 N LEU B 875 106.875 12.241 17.527 1.00 12.71 N

ATOM 3072 CA LEU B 875 105.970 13.245 16.976 1.00 13.02 C

ATOM 3073 C LEU B 875 106.783 14.496 16.611 1.00 13.62 C

ATOM 3074 O LEU B 875 106.441 15.209 15.668 1.00 12.67 O

ATOM 3075 CB LEU B 875 104.899 13.597 18.014 1.00 10.40 C

ATOM 3076 CG LEU B 875 104.091 12.420 18.573 1.00 9.62 C

ATOM 3077 CDl LEU B 875 103.377 12.829 19.855 1.00 10.22 C

ATOM 3078 CD2 LEU B 875 103.107 11.946 17.535 1.00 8.55 C

ATOM 3079 N LEU B 876 107.861 14.747 17.358 1.00 14.73 N

ATOM 3080 CA LEU B 876 108.723 15.908 17.102 1.00 16.54 C

ATOM 3081 C LEU B 876 109.595 15.715 15.855 1.00 16.66 C

ATOM 3082 O LEU B 876 109.979 16.688 15.206 1.00 17.15 O

ATOM 3083 CB LEU B 876 109.634 16.203 18.304 1.00 14.92 C

ATOM 3084 CG LEU B 876 109.051 16.856 19.555 1.00 17.14 C

ATOM 3085 CDl LEU B 876 110.191 17.433 20.385 1.00 19.09 C

ATOM 3086 CD2 LEU B 876 108.090 17.954 19.172 1.00 16.37 C

ATOM 3087 N LEU B 877 109.903 14.458 15.538 1.00 15.04 N

ATOM 3088 CA LEU B 877 110.720 14.121 14.377 1.00 14.81 C ATOM 3089 C LEU B 877 109.913 14.287 13.099 1.00 15.21 C

ATOM 3090 O LEU B 877 110.463 14.547 12.027 1.00 15.78 O

ATOM 3091 CB LEU B 877 111.221 12.675 14.490 1.00 13.25 C

ATOM 3092 CG LEU B 877 111.785 11.939 13.273 1.00 11.80 C

ATOM 3093 CDl LEU B 877 113.024 12.641 12.758 1.00 11.17 C

ATOM 3094 CD2 LEU B 877 112.100 10.476 13.676 1.00 10.13 C

ATOM 3095 N LEU B 878 108.602 14.141 13.232 1.00 15.27 N

ATOM 3096 CA LEU B 878 107.670 14.256 12.121 1.00 15.50 C

ATOM 3097 C LEU B 878 106.874 15.548 12.255 1.00 15.31 C

ATOM 3098 O LEU B 878 105.737 15.619 11.795 1.00 18.62 O

ATOM 3099 CB LEU B 878 106.690 13.082 12.151 1.00 13.42 C

ATOM 3100 CG LEU B 878 107.236 11.658 12.238 1.00 9.76 C

ATOM 3101 CDl LEU B 878 106.112 10.744 12.646 1.00 8.61 C

ATOM 3102 CD2 LEU B 878 107.839 11.236 10.917 1.00 7.12 C

ATOM 3103 N SER B 879 107.474 16.566 12.865 1.00 14.93 N

ATOM 3104 CA SER B 879 106.800 17.847 13.088 1.00 15.31 C

ATOM 3105 C SER B 879 107.075 18.966 12.084 1.00 15.55 C

ATOM 3106 O SER B 879 106.208 19.806 11.825 1.00 14.47 O

ATOM 3107 CB SER B 879 107.146 18.381 14.482 1.00 15.29 C

ATOM 3108 OG SER B 879 108.416 19.018 14.475 1.00 15.55 O

ATOM 3109 N THR B 880 108.277 19.006 11.529 1.00 16.03 N

ATOM 3110 CA THR B 880 108.591 20.076 10.595 1.00 14.82 C

ATOM 3111 C THR B 880 109.004 19.537 9.224 1.00 16.19 C

ATOM 3112 O THR B 880 109.915 18.730 9.103 1.00 14.85 O

ATOM 3113 CB THR B 880 109.689 20.990 11.180 1.00 15.81 C

ATOM 3114 OGl THR B 880 109.357 21.344 12.539 1.00 16.17 O

ATOM 3115 CG2 THR B 880 109.796 22.261 10.364 1.00 16.90 C

ATOM 3116 N ILE B 881 108.309 19.977 8.185 1.00 17.30 N

ATOM 3117 CA ILE B 881 108.613 19.508 6.842 1.00 18.21 C

ATOM 3118 C ILE B 881 108.853 20.665 5.892 1.00 19.13 C

ATOM 3119 O ILE B 881 108.538 21.821 6.206 1.00 14.98 O

ATOM 3120 CB ILE B 881 107.451 18.678 6.249 1.00 17.09 C

ATOM 3121 CGl ILE B 881 106.239 19.583 6.016 1.00 17.47 C

ATOM 3122 CG2 ILE B 881 107.119 17.524 7.169 1.00 19.47 C

ATOM 3123 CDl ILE B 881 105.102 18.952 5.229 1.00 10.53 C

ATOM 3124 N PRO B 882 109.422 20.366 4.710 1.00 19.59 N

ATOM 3125 CA PRO B 882 109.677 21.420 3.731 1.00 21.75 C

ATOM 3126 C PRO B 882 108.312 22.020 3.414 1.00 23.10 C

ATOM 3127 O PRO B 882 107.313 21.300 3.363 1.00 24.13 O

ATOM 3128 CB PRO B 882 110.262 20.655 2.543 1.00 21.09 C

ATOM 3129 CG PRO B 882 110.973 19.506 3.202 1.00 21.56 C

ATOM 3130 CD PRO B 882 109.972 19.076 4.257 1.00 21.13 C

ATOM 3131 N LYS B 883 108.279 23.333 3.223 1.00 23.86 N

ATOM 3132 CA LYS B 883 107.062 24.071 2.920 1.00 24.81 C

ATOM 3133 C LYS B 883 106.122 23.437 1.901 1.00 25.90 C

ATOM 3134 O LYS B 883 104.922 23.698 1.927 1.00 27.33 O

ATOM 3135 CB LYS B 883 107.425 25.475 2.434 1.00 26.03 C

ATOM 3136 CG LYS B 883 106.276 26.205 1.769 1.00 27.14 C

ATOM 3137 CD LYS B 883 106.761 27.382 0.945 1.00 25.04 C

ATOM 3138 CE LYS B 883 105.660 27.899 0.029 1.00 24.96 C

ATOM 3139 NZ LYS B 883 104.424 28.291 0.761 1.00 23.40 N

ATOM 3140 N ASP B 884 106.646 22.618 0.997 1.00 26.82 N

ATOM 3141 CA ASP B 884 105.784 22.023 -0.012 1.00 27.87 C

ATOM 3142 C ASP B 884 105.498 20.541 0.185 1.00 27.80 C

ATOM 3143 O ASP B 884 104.448 20.050 -0.226 1.00 27.02 O

ATOM 3144 CB ASP B 884 106.367 22.280 -1.396 1.00 27.54 C

ATOM 3145 CG ASP B 884 106.699 23.736 -1.611 1.00 29.27 C

ATOM 3146 ODl ASP B 884 107.613 24.249 -0.928 1.00 30.16 O

ATOM 3147 OD2 ASP B 884 106.041 24.374 -2.453 1.00 28.90 O

ATOM 3148 N GLY B 885 106.427 19.832 0.814 1.00 28.29 N

ATOM 3149 CA GLY B 885 106.207 18.423 1.063 1.00 26.89 C

ATOM 3150 C GLY B 885 107.396 17.527 0.833 1.00 25.25 C

ATOM 3151 O GLY B 885 108.525 17.994 0.672 1.00 26.70 O

ATOM 3152 N LEU B 886 107.118 16.228 0.831 1.00 22.60 N

ATOM 3153 CA LEU B 886 108.110 15.173 0.621 1.00 21.28 C

ATOM 3154 C LEU B 886 107.560 14.271 -0.468 1.00 19.86 C

ATOM 3155 O LEU B 886 106.356 14.273 -0.705 1.00 21.51 O

ATOM 3156 CB LEU B 886 108.271 14.337 1.893 1.00 19.53 C

ATOM 3157 CG LEU B 886 108.787 15.032 3.152 1.00 19.23 C

ATOM 3158 CDl LEU B 886 108.453 14.201 4.380 1.00 20.17 C

ATOM 3159 CD2 LEU B 886 110.297 15.254 3.021 1.00 18.97 C

ATOM 3160 N LYS B 887 108.421 13.499 -1.122 1.00 21.13 N

ATOM 3161 CA LYS B 887 107.952 12.580 -2.156 1.00 23.37 C

ATOM 3162 C LYS B 887 106.845 11.733 -1.541 1.00 25.17 C

ATOM 3311 CZ ARG B 904 93.087 9.640 17.125 1.00 27.27 C

ATOM 3312 NHl ARG B 904 93.531 10.420 16.143 1.00 26.00 N

ATOM 3313 NH2 ARG B 904 92.830 8.362 16.885 1.00 27.22 N

ATOM 3314 N LYS B 905 95.759 6.404 22.057 1.00 23.77 N

ATOM 3315 CA LYS B 905 95.520 5.088 22.656 1.00 24.63 C

ATOM 3316 C LYS B 905 96.175 5.005 24.032 1.00 26.85 C

ATOM 3317 O LYS B 905 95.736 4.248 24.895 1.00 27.29 O

ATOM 3318 CB LYS B 905 96.135 3.967 21.817 1.00 23.48 C

ATOM 3319 CG LYS B 905 95.502 3.670 20.475 1.00 21.62 C

ATOM 3320 CD LYS B 905 96.164 2.424 19.914 1.00 20.88 C

ATOM 3321 CE LYS B 905 95.721 2.084 18.507 1.00 17.96 C

ATOM 3322 NZ LYS B 905 96.311 0.773 18.105 1.00 16.21 N

ATOM 3323 N MET B 906 97.242 5.774 24.223 1.00 28.18 N

ATOM 3324 CA MET B 906 97.973 5.742 25.477 1.00 30.63 C

ATOM 3325 C MET B 906 97.308 6.521 26.596 1.00 31.94 C

ATOM 3326 O MET B 906 97.355 6.103 27.755 1.00 32.52 O

ATOM 3327 CB MET B 906 99.393 6.259 25.278 1.00 31.76 C

ATOM 3328 CG MET B 906 100.379 5.650 26.250 1.00 33.14 C

ATOM 3329 SD MET B 906 101.890 6.592 26.383 1.00 36.55 S

ATOM 3330 CE MET B 906 102.033 6.716 28.152 1.00 37.44 C

ATOM 3331 N VAL B 907 96.694 7.652 26.262 1.00 32.18 N

ATOM 3332 CA VAL B 907 96.025 8.440 27.281 1.00 33.03 C

ATOM 3333 C VAL B 907 94.737 7.721 27.682 1.00 34.22 C

ATOM 3334 O VAL B 907 93.647 8.299 27.657 1.00 32.78 O

ATOM 3335 CB VAL B 907 95.680 9.852 26.779 1.00 32.96 C

ATOM 3336 CGl VAL B 907 95.301 10.730 27.961 1.00 30.91 C

ATOM 3337 CG2 VAL B 907 96.851 10.442 26.015 1.00 32.25 C

ATOM 3338 N THR B 908 94.883 6.446 28.036 1.00 35.27 N

ATOM 3339 CA THR B 908 93.764 5.611 28.460 1.00 36.48 C

ATOM 3340 C THR B 908 94.255 4.335 29.135 1.00 36.96 C

ATOM 3341 O THR B 908 93.648 3.858 30.094 1.00 38.03 O

ATOM 3342 CB THR B 908 92.859 5.225 27.272 1.00 35.90 C

ATOM 3343 OGl THR B 908 93.601 5.325 26.047 1.00 36.61 O

ATOM 3344 CG2 THR B 908 91.633 6.131 27.217 1.00 35.77 C

ATOM 3345 N GLN B 919 91.427 14.204 28.001 1.00 39.16 N

ATOM 3346 CA GLN B 919 91.907 15.569 28.197 1.00 38.41 C

ATOM 3347 C GLN B 919 93.424 15.689 28.162 1.00 37.51 C

ATOM 3348 O GLN B 919 93.965 16.648 27.611 1.00 37.83 O

ATOM 3349 CB GLN B 919 91.392 16.124 29.528 1.00 39.92 C

ATOM 3350 CG GLN B 919 91.688 15.247 30.744 1.00 39.57 C

ATOM 3351 CD GLN B 919 90.824 14.003 30.788 1.00 39.94 C

ATOM 3352 OEl GLN B 919 89.598 14.089 30.742 1.00 41.03 O

ATOM 3353 NE2 GLN B 919 91.458 12.840 30.879 1.00 39.04 N

ATOM 3354 N ARG B 920 94.106 14.717 28.757 1.00 36.21 N

ATOM 3355 CA ARG B 920 95.561 14.721 28.796 1.00 34.19 C

ATOM 3356 C ARG B 920 96.135 14.753 27.380 1.00 33.08 C

ATOM 3357 O ARG B 920 97.219 15.296 27.153 1.00 32.69 O

ATOM 3358 CB ARG B 920 96.059 13.487 29.547 1.00 34.15 C

ATOM 3359 CG ARG B 920 97.545 13.487 29.839 1.00 33.80 C

ATOM 3360 CD ARG B 920 97.890 12.365 30.789 1.00 34.38 C

ATOM 3361 NE ARG B 920 99.287 12.397 31.205 1.00 35.05 N

ATOM 3362 CZ ARG B 920 99.762 11.738 32.257 1.00 35.48 C

ATOM 3363 NHl ARG B 920 98.948 10.998 33.000 1.00 33.72 N

ATOM 3364 NH2 ARG B 920 101.047 11.822 32.572 1.00 35.29 N

ATOM 3365 N PHE B 921 95.395 14.176 26.437 1.00 31.49 N

ATOM 3366 CA PHE B 921 95.799 14.142 25.032 1.00 30.62 C

ATOM 3367 C PHE B 921 96.168 15.554 24.590 1.00 29.57 C

ATOM 3368 O PHE B 921 97.277 15.802 24.120 1.00 21.11 O

ATOM 3369 CB PHE B 921 94.643 13.634 24.161 1.00 28.32 C

ATOM 3370 CG PHE B 921 94.980 13.528 22.701 1.00 26.93 C

ATOM 3371 CDl PHE B 921 95.464 12.341 22.172 1.00 28.17 C

ATOM 3372 CD2 PHE B 921 94.820 14.624 21.852 1.00 28.47 C

ATOM 3373 CEl PHE B 921 95.786 12.239 20.819 1.00 27.39 C

ATOM 3374 CE2 PHE B 921 95.140 14.537 20.499 1.00 26.53 C

ATOM 3375 CZ PHE B 921 95.625 13.341 19.980 1.00 27.47 C

ATOM 3376 N TYR B 922 95.214 16.468 24.744 1.00 29.54 N

ATOM 3377 CA TYR B 922 95.392 17.869 24.376 1.00 30.15 C

ATOM 3378 C TYR B 922 96.511 18.515 25.181 1.00 28.89 C

ATOM 3379 O TYR B 922 97.292 19.309 24.655 1.00 29.32 O

ATOM 3380 CB TYR B 922 94.084 18.639 24.592 1.00 31.58 C

ATOM 3381 CG TYR B 922 94.252 20.144 24.626 1.00 34.87 C

ATOM 3382 CDl TYR B 922 94.803 20.830 23.545 1.00 35.84 C

ATOM 3383 CD2 TYR B 922 93.884 20.881 25.751 1.00 35.53 C

ATOM 3384 CEl TYR B 922 94.987 22.211 23.581 1.00 36.95 C ATOM 3385 CE2 TYR B 922 94.065 22.264 25.797 1.00 37.72 C

ATOM 3386 CZ TYR B 922 94.618 22.922 24.708 1.00 37.24 C

ATOM 3387 OH TYR B 922 94.805 24.289 24.745 1.00 39.22 O

ATOM 3388 N GLN B 923 96.581 18.181 26.464 1.00 27.39 N

ATOM 3389 CA GLN B 923 97.617 18.728 27.319 1.00 26.49 C

ATOM 3390 C GLN B 923 98.991 18.387 26.734 1.00 25.47 C

ATOM 3391 O GLN B 923 99.942 19.169 26.840 1.00 27.46 O

ATOM 3392 CB GLN B 923 97.489 18.152 28.731 1.00 26.22 C

ATOM 3393 CG GLN B 923 96.287 18.670 29.520 1.00 25.65 C

ATOM 3394 CD GLN B 923 95.989 17.833 30.753 1.00 25.06 C

ATOM 3395 OEl GLN B 923 95.139 16.943 30.723 1.00 25.30 O

ATOM 3396 NE2 GLN B 923 96.696 18.109 31.843 1.00 25.30 N

ATOM 3397 N LEU B 924 99.093 17.222 26.104 1.00 22.04 N

ATOM 3398 CA LEU B 924 100.361 16.805 25.530 1.00 19.28 C

ATOM 3399 C LEU B 924 100.588 17.429 24.154 1.00 17.66 C

ATOM 3400 O LEU B 924 101.679 17.914 23.877 1.00 15.14 O

ATOM 3401 CB LEU B 924 100.436 15.268 25.473 1.00 18.80 C

ATOM 3402 CG LEU B 924 100.133 14.587 26.820 1.00 19.00 C

ATOM 3403 CDl LEU B 924 100.271 13.072 26.711 1.00 19.63 C

ATOM 3404 CD2 LEU B 924 101.078 15.118 27.882 1.00 16.68 C

ATOM 3405 N THR B 925 99.569 17.447 23.296 1.00 16.93 N

ATOM 3406 CA THR B 925 99.762 18.045 21.976 1.00 18.34 C

ATOM 3407 C THR B 925 99.976 19.557 22.082 1.00 20.27 C

ATOM 3408 O THR B 925 100.587 20.161 21.203 1.00 21.01 O

ATOM 3409 CB THR B 925 98.579 17.746 21.011 1.00 17.46 C

ATOM 3410 OGl THR B 925 97.340 18.119 21.623 1.00 20.71 O

ATOM 3411 CG2 THR B 925 98.533 16.262 20.659 1.00 14.78 C

ATOM 3412 N LYS B 926 99.492 20.164 23.166 1.00 21.36 N

ATOM 3413 CA LYS B 926 99.657 21.601 23.358 1.00 21.93 C

ATOM 3414 C LYS B 926 101.135 21.891 23.613 1.00 21.41 C

ATOM 3415 O LYS B 926 101.709 22.823 23.051 1.00 19.92 O

ATOM 3416 CB LYS B 926 98.808 22.094 24.544 1.00 23.67 C

ATOM 3417 CG LYS B 926 99.490 22.022 25.911 1.00 24.90 C

ATOM 3418 CD LYS B 926 99.503 23.392 26.602 1.00 22.12 C

ATOM 3419 CE LYS B 926 100.334 23.378 27.884 1.00 22.58 C

ATOM 3420 NZ LYS B 926 101.795 23.212 27.621 1.00 18.51 N

ATOM 3421 N LEU B 927 101.746 21.066 24.456 1.00 21.61 N

ATOM 3422 CA LEU B 927 103.154 21.199 24.794 1.00 22.01 C

ATOM 3423 C LEU B 927 104.016 21.096 23.526 1.00 21.91 C

ATOM 3424 O LEU B 927 104.776 22.015 23.210 1.00 22.09 O

ATOM 3425 CB LEU B 927 103.544 20.104 25.788 1.00 21.62 C

ATOM 3426 CG LEU B 927 104.739 20.361 26.703 1.00 23.50 C

ATOM 3427 CDl LEU B 927 104.868 19.198 27.669 1.00 24.71 C

ATOM 3428 CD2 LEU B 927 106.015 20.536 25.889 1.00 24.83 C

ATOM 3429 N LEU B 928 103.891 19.982 22.806 1.00 22.05 N

ATOM 3430 CA LEU B 928 104.656 19.784 21.576 1.00 21.17 C

ATOM 3431 C LEU B 928 104.544 21.041 20.717 1.00 20.65 C

ATOM 3432 O LEU B 928 105.521 21.480 20.127 1.00 20.61 O

ATOM 3433 CB LEU B 928 104.141 18.563 20.797 1.00 21.52 C

ATOM 3434 CG LEU B 928 104.431 17.170 21.379 1.00 21.60 C

ATOM 3435 CDl LEU B 928 103.944 16.099 20.416 1.00 24.48 C

ATOM 3436 CD2 LEU B 928 105.926 16.999 21.607 1.00 23.27 C

ATOM 3437 N ASP B 929 103.351 21.627 20.669 1.00 22.16 N

ATOM 3438 CA ASP B 929 103.134 22.850 19.897 1.00 23.34 C

ATOM 3439 C ASP B 929 104.019 23.959 20.456 1.00 23.47 C

ATOM 3440 O ASP B 929 104.645 24.705 19.705 1.00 24.75 O

ATOM 3441 CB ASP B 929 101.666 23.290 19.983 1.00 25.21 C

ATOM 3442 CG ASP B 929 101.010 23.410 18.619 1.00 25.22 C

ATOM 3443 ODl ASP B 929 100.885 22.378 17.930 1.00 27.88 O

ATOM 3444 OD2 ASP B 929 100.623 24.537 18.238 1.00 26.54 O

ATOM 3445 N SER B 930 104.064 24.048 21.781 1.00 23.83 N

ATOM 3446 CA SER B 930 104.856 25.048 22.483 1.00 24.14 C

ATOM 3447 C SER B 930 106.342 24.828 22.229 1.00 25.45 C

ATOM 3448 O SER B 930 107.170 25.716 22.452 1.00 24.98 O

ATOM 3449 CB SER B 930 104.590 24.963 23.993 1.00 26.00 C

ATOM 3450 OG SER B 930 103.199 24.871 24.274 1.00 25.12 O

ATOM 3451 N MET B 931 106.681 23.627 21.782 1.00 24.63 N

ATOM 3452 CA MET B 931 108.067 23.296 21.515 1.00 24.34 C

ATOM 3453 C MET B 931 108.535 24.079 20.285 1.00 24.86 C

ATOM 3454 O MET B 931 109.654 24.587 20.254 1.00 23.88 O

ATOM 3455 CB MET B 931 108.194 21.790 21.281 1.00 23.51 C

ATOM 3456 CG MET B 931 109.469 21.179 21.811 1.00 24.70 C

ATOM 3457 SD MET B 931 109.676 21.465 23.575 1.00 23.26 S

ATOM 3458 CE MET B 931 111.380 20.958 23.807 1.00 22.82 C

ATOM 3607 OEl GLU B 948 131.537 36.981 13.725 1.00 40.48 O

ATOM 3608 OE2 GLU B 948 130.582 38.636 14.806 1.00 42.01 O

ATOM 3609 N SER B 949 130.852 32.209 14.442 1.00 33.07 N

ATOM 3610 CA SER B 949 131.685 31.295 15.201 1.00 32.16 C

ATOM 3611 C SER B 949 133.079 31.893 15.331 1.00 32.58 C

ATOM 3612 O SER B 949 133.541 32.172 16.439 1.00 31.85 O

ATOM 3613 CB SER B 949 131.758 29.942 14.496 1.00 32.15 C

ATOM 3614 OG SER B 949 132.612 29.052 15.188 1.00 32.97 O

ATOM 3615 N HIS B 950 133.741 32.098 14.194 1.00 32.98 N

ATOM 3616 CA HIS B 950 135.084 32.665 14.182 1.00 32-.76 C

ATOM 3617 C HIS B 950 135.096 34.165 14.440 1.00 33.39 C

ATOM 3618 O HIS B 950 135.272 34.973 13.527 1.00 33.72 O

ATOM 3619 CB HIS B 950 135.781 32.344 12.860 1.00 32.12 C

ATOM 3620 CG HIS B 950 136.605 31.094 12.908 1.00 32.82 C

ATOM 3621 NDl HIS B 950 137.811 31.024 13.572 1.00 33.17 N

ATOM 3622 CD2 HIS B 950 136.380 29.857 12.408 1.00 32.40 C

ATOM 3623 CEl HIS B 950 138.293 29.798 13.479 1.00 33.83 C

ATOM 3624 NE2 HIS B 950 137.444 29.069 12.111 1.00 34.00 N

ATOM 3625 N ALA B 951 134.912 34.513 15.709 1.00 33.11 N

ATOM 3626 CA ALA B 951 134.890 35.896 16.176 1.00 31.22 C

ATOM 3627 C ALA B 951 134.386 35.875 17.613 1.00 30.64 C

ATOM 3628 O ALA B 951 134.848 36.643 18.461 1.00 31.01 O

ATOM 3629 CB ALA B 951 133.971 36.739 15.307 1.00 30.49 C

ATOM 3630 N LEU B 952 133.432 34.984 17.876 1.00 28.88 N

ATOM 3631 CA LEU B 952 132.859 34.827 19.206 1.00 29.01 C

ATOM 3632 C LEU B 952 133.585 33.704 19.937 1.00 28.64 C

ATOM 3633 O LEU B 952 133.477 33.570 21.156 1.00 29.64 O

ATOM 3634 CB LEU B 952 131.371 34.481 19.111 1.00 29.37 C

ATOM 3635 CG LEU B 952 130.435 35.497 18.453 1.00 30.56 C

ATOM 3636 CDl LEU B 952 129.013 34.970 18.510 1.00 31.45 C

ATOM 3637 CD2 LEU B 952 130.533 36.842 19.162 1.00 30.79 C

ATOM 3638 N LYS B 953 134.328 32.905 19.179 1.00 28.78 N

ATOM 3639 CA LYS B 953 135.067 31.772 19.725 1.00 29.06 C

ATOM 3640 C LYS B 953 134.106 30.679 20.175 1.00 29.74 C

ATOM 3641 O LYS B 953 134.335 29.998 21.170 1.00 30.77 O

ATOM 3642 CB LYS B 953 135.959 32.207 20.896 1.00 29.53 C

ATOM 3643 CG LYS B 953 137.076 33.157 20.486 1.00 26.23 C

ATOM 3644 CD LYS B 953 138.015 33.453 21.644 1.00 26.29 C

ATOM 3645 CE LYS B 953 139.131 34.399 21.223 1.00 26.21 C

ATOM 3646 NZ LYS B 953 138.629 35.658 20.618 1.00 24.73 N

ATOM 3647 N VAL B 954 133.012 30.541 19.441 1.00 29.67 N

ATOM 3648 CA VAL B 954 132.029 29.511 19.724 1.00 30.01 C

ATOM 3649 C VAL B 954 132.474 28.375 18.823 1.00 29.43 C

ATOM 3650 O VAL B 954 132.816 28.605 17.665 1.00 29.30 O

ATOM 3651 CB VAL B 954 130.605 29.962 19.329 1.00 30.95 C

ATOM 3652 CGl VAL B 954 129.641 28.789 19.410 1.00 31.94 C

ATOM 3653 CG2 VAL B 954 130.145 31.083 20.248 1.00 32.30 C

ATOM 3654 N GLU B 955 132.486 27.157 19.347 1.00 28.95 N

ATOM 3655 CA GLU B 955 132.922 26.024 18.549 1.00 27.69 C

ATOM 3656 C GLU B 955 131.849 24.965 18.298 1.00 26.55 C

ATOM 3657 O GLU B 955 131.137 24.546 19.213 1.00 24.30 O

ATOM 3658 CB GLU B 955 134.127 25.366 19.217 1.00 27.47 C

ATOM 3659 CG GLU B 955 134.945 24.481 18.303 1.00 26.06 C

ATOM 3660 CD GLU B 955 135.994 23.691 19.061 1.00 26.43 C

ATOM 3661 OEl GLU B 955 136.706 24.292 19.901 1.00 26.15 O

ATOM 3662 OE2 GLU B 955 136.104 22.472 18.816 1.00 25.49 O

ATOM 3663 N PHE B 956 131.750 24.550 17.039 1.00 27.13 N

ATOM 3664 CA PHE B 956 130.826 23.507 16.609 1.00 26.37 C

ATOM 3665 C PHE B 956 131.716 22.390 16.069 1.00 27.81 C

ATOM 3666 O PHE B 956 132.642 22.645 15.291 1.00 29.07 O

ATOM 3667 CB PHE B 956 129.900 23.998 15.493 1.00 24.04 C

ATOM 3668 CG PHE B 956 128.936 25.079 15.921 1.00 23.11 C

ATOM 3669 CDl PHE B 956 129.362 26.395 16.077 1.00 20.85 C

ATOM 3670 CD2 PHE B 956 127.598 24.778 16.158 1.00 21.31 C

ATOM 3671 CEl PHE B 956 128.470 27.395 16.461 1.00 19.75 C

ATOM 3672 CE2 PHE B 956 126.698 25.770 16.541 1.00 19.90 C

ATOM 3673 CZ PHE B 956 127.137 27.082 16.692 1.00 20.35 C

ATOM 3674 N PRO B 957 131.458 21.143 16.486 1.00 28.36 N

ATOM 3675 CA PRO B 957 132.226 19.965 16.059 1.00 29.21 C

ATOM 3676 C PRO B 957 132.451 19.887 14.547 1.00 30.29 C

ATOM 3677 O PRO B 957 133.277 20.605 13.986 1.00 30.16 O

ATOM 3678 CB PRO B 957 131.378 18.808 16.570 1.00 28.25 C

ATOM 3679 CG PRO B 957 130.802 19.370 17.843 1.00 30.70 C

ATOM 3680 CD PRO B 957 130.379 20.761 17.415 1.00 28.41 C ATOM 3681 N ALA B 958 131.710 18.993 13.901 1.00 30.78 N

ATOM 3682 CA ALA B 958 131.788 18.794 12.460 1.00 30.86 C

ATOM 3683 C ALA B 958 130.444 18.205 12.066 1.00 31.64 C

ATOM 3684 O ALA B 958 130.028 18.256 10.909 1.00 32.36 O

ATOM 3685 CB ALA B 958 132.912 17.817 12.120 1.00 31.00 C

ATOM 3686 N MET B 959 129.773 17.654 13.070 1.00 31.77 N

ATOM 3687 CA MET B 959 128.473 17.023 12.920 1.00 31.68 C

ATOM 3688 C MET B 959 127.386 18.083 12.774 1.00 31.01 C

ATOM 3689 O MET B 959 126.564 18.026 11.859 1.00 30.64 O

ATOM 3690 CB MET B 959 128.209 16.160 14.152 1.00 33.27 C

ATOM 3691 N LEU B 960 127.397 19.051 13.683 1.00 30.46 N

ATOM 3692 CA LEU B 960 126.429 20.140 13.670 1.00 29.55 C

ATOM 3693 C LEU B 960 126.675 21.053 12.472 1.00 29.10 C

ATOM 3694 O LEU B 960 125.755 21.359 11.714 1.00 27.92 O

ATOM 3695 CB LEU B 960 126.535 20.945 14.964 1.00 28.14 C

ATOM 3696 CG LEU B 960 126.265 20.143 16.237 1.00 28.24 C

ATOM 3697 CDl LEU B 960 126.551 20.999 17.466 1.00 27.96 C

ATOM 3698 CD2 LEU B 960 124.829 19.662 16.229 1.00 26.64 C

ATOM 3699 N VAL B 961 127.922 21.486 12.312 1.00 28.40 N

ATOM 3700 CA VAL B 961 128.292 22.358 11.202 1.00 27.06 C

ATOM 3701 C VAL B 961 127.637 21.854 9.924 1.00 26.99 C

ATOM 3702 O VAL B 961 127.221 22.638 9.075 1.00 28.06 O

ATOM 3703 CB VAL B 961 129.819 22.370 10.970 1.00 25.30 C

ATOM 3704 CGl VAL B 961 130.181 23.493 10.024 1.00 26.08 C

ATOM 3705 CG2 VAL B 961 130.562 22.506 12.297 1.00 26.30 C

ATOM 3706 N GLU B 962 127.543 20.536 9.790 1.00 27.24 N

ATOM 3707 CA GLU B 962 126.948 19.949 8.601 1.00 27.45 C

ATOM 3708 C GLU B 962 125.431 20.152 8.553 1.00 27.25 C

ATOM 3709 O GLU B 962 124.856 20.325 7.476 1.00 25.70 O

ATOM 3710 CB GLU B 962 127.277 18.456 8.533 1.00 29.06 C

ATOM 3711 CG GLU B 962 127.529 17.949 7.120 1.00 30.34 C

ATOM 3712 CD GLU B 962 128.884 18.378 6.566 1.00 31.18 C

ATOM 3713 OEl GLU B 962 129.136 19.598 6.448 1.00 31.64 O

ATOM 3714 OE2 GLU B 962 129.700 17.486 6.245 1.00 31.98 O

ATOM 3715 N ILE B 963 124.784 20.117 9.716 1.00 26.63 N

ATOM 3716 CA ILE B 963 123.341 20.315 9.776 1.00 26.49 C

ATOM 3717 C ILE B 963 123.073 21.803 9.624 1.00 26.63 C

ATOM 3718 O ILE B 963 122.188 22.217 8.876 1.00 26.52 O

ATOM 3719 CB ILE B 963 122.743 19.850 11.126 1.00 26.54 C

ATOM 3720 CGl ILE B 963 123.035 18.363 11.355 1.00 26.71 C

ATOM 3721 CG2 ILE B 963 121.241 20.086 11.131 1.00 24.89 C

ATOM 3722 CDl ILE B 963 122.676 17.892 12.735 1.00 26.43 C

ATOM 3723 N ILE B 964 123.853 22.605 10.341 1.00 27.15 N

ATOM 3724 CA ILE B 964 123.706 24.052 10.296 1.00 27.58 C

ATOM 3725 C ILE B 964 123.729 24.590 8.871 1.00 27.73 C

ATOM 3726 O ILE B 964 122.731 25.107 8.370 1.00 27.88 O

ATOM 3727 CB ILE B 964 124.830 24.763 11.087 1.00 28.14 C

ATOM 3728 CGl ILE B 964 124.444 24.906 12.566 1.00 27.65 C

ATOM 3729 CG2 ILE B 964 125.095 26.131 10.480 1.00 30.21 C

ATOM 3730 CDl ILE B 964 124.452 23.613 13.354 1.00 24.65 C

ATOM 3731 N SER B 965 124.884 24.470 8.231 1.00 27.87 N

ATOM 3732 CA SER B 965 125.068 24.963 6.877 1.00 28.12 C

ATOM 3733 C SER B 965 123.945 24.546 5.937 1.00 28.51 C

ATOM 3734 O SER B 965 123.681 25.228 4.952 1.00 29.28 O

ATOM 3735 CB SER B 965 126.411 24.470 6.324 1.00 28.76 C

ATOM 3736 OG SER B 965 127.478 24.806 7.198 1.00 27.41 O

ATOM 3737 N ASP B 966 123.283 23.436 6.257 1.00 30.13 N

ATOM 3738 CA ASP B 966 122.213 22.891 5.425 1.00 30.96 C

ATOM 3739 C ASP B 966 120.810 23.340 5.830 1.00 30.86 C

ATOM 3740 O ASP B 966 120.011 23.750 4.989 1.00 31.03 O

ATOM 3741 CB ASP B 966 122.288 21.359 5.451 1.00 31.66 C

ATOM 3742 CG ASP B 966 121.574 20.710 4.274 1.00 31.55 C

ATOM 3743 ODl ASP B 966 121.654 19.470 4.147 1.00 32.65 O

ATOM 3744 OD2 ASP B 966 120.941 21.430 3.476 1.00 32.06 O

ATOM 3745 N GLN B 967 120.517 23.249 7.122 1.00 30.31 N

ATOM 3746 CA GLN B 967 119.215 23.629 7.660 1.00 30.24 C

ATOM 3747 C GLN B 967 118.980 25.135 7.610 1.00 31.33 C

ATOM 3748 O GLN B 967 118.010 25.602 7.011 1.00 32.75 O

ATOM 3749 CB GLN B 967 119.102 23.126 9.109 1.00 27.16 C

ATOM 3750 CG GLN B 967 118.099 23.851 9.997 1.00 26.30 C

ATOM 3751 CD GLN B 967 118.338 23.588 11.484 1.00 24.72 C

ATOM 3752 OEl GLN B 967 119.456 23.733 11.978 1.00 25.75 O

ATOM 3753 NE2 GLN B 967 117.289 23.207 12.198 1.00 23.94 N

ATOM 3754 N LEU B 968 119.890 25.881 8.227 1.00 32.15 N

HETATM 3903 C16 ICA 2001 62.783 62.371 -2.767 1.00 22.91 C

HETATM 3904 C17 ICA 2001 64.191 61.781 -2.827 1.00 23.10 C

HETATM 3905 C18 ICA 2001 63.777 59.840 -4.641 1.00 21.79 C

HETATM 3906 C19 ICA 2001 62.491 55.483 -2.844 1.00 21.33 C

HETATM 3907 C20 ICA 2001 65.186 62.539 -3.782 1.00 24.99 C

HETATM 3908 C21 ICA 2001 66.647 62.221 -3.763 1.00 24.61 C

HETATM 3909 03 ICA 2001 60.965 53.288 1.456 1.00 22.73 O

HETATM 3910 O20 ICA 2001 64.753 63.409 -4.575 1.00 26.54 O

HETATM 3911 021 ICA 2001 67.653 63.121 -4.383 1.00 27.30 O

HETATM 3912 Cl ICA 3001 123.114 20.114 23.578 1.00 19.17 C

HETATM 3913 C2 ICA 3001 122.534 18.719 24.248 1.00 18.08 C

HETATM 3914 C3 ICA 3001 121.203 18.926 25.073 1.00 16.56 C

HETATM 3915 C4 ICA 3001 120.324 20.088 24.904 1.00 17.27 C

HETATM 3916 C5 ICA 3001 120.586 21.091 23.876 1.00 17.50 C

HETATM 3917 C6 ICA 3001 119.539 22.272 23.703 1.00 17.74 C

HETATM 3918 C7 ICA 3001 120.170 23.677 23.556 1.00 21.17 C

HETATM 3919 C8 ICA 3001 121.383 23.816 22.526 1.00 19.03 C

HETATM 3920 C9 ICA 3001 122.581 22.721 22.917 1.00 18.76 C

HETATM 3921 ClO ICA 3001 121.997 21.126 22.978 1.00 17.83 C

HETATM 3922 CIl ICA 3001 123.936 22.921 22.097 1.00 19.21 C

HETATM 3923 C12 ICA 3001 124.415 24.422 22.067 1.00 19.18 C

HETATM 3924 C13 ICA 3001 123.265 25.449 21.404 1.00 19.55 C

HETATM 3925 C14 ICA 3001 121.991 25.339 22.407 1.00 19.94 C

HETATM 3926 C15 ICA 3001 121.067 26.573 22.046 1.00 20.87 C

HETATM 3927 C16 ICA 3001 122.035 27.652 21.608 1.00 19.05 C

HETATM 3928 C17 ICA 3001 123.467 27.015 21.607 1.00 19.66 C

HETATM 3929 C18 ICA 3001 123.017 25.048 19.832 1.00 18.29 C

HETATM 3930 C19 ICA 3001 121.595 20.531 21.590 1.00 15.88 C

HETATM 3931 C20 ICA 3001 124.391 27.617 20.613 1.00 23.10 C

HETATM 3932 C21 ICA 3001 125.865 27.517 20.833 1.00 19.96 C

HETATM 3933 03 ICA 3001 120.940 18.118 25.887 1.00 17.19 O

HETATM 3934 020 ICA 3001 123.925 28.113 19.542 1.00 23.72 O

HETATM 3935 021 ICA 3001 126.744 27.924 19.787 1.00 23.42 O

HETATM 3936 O HOH 1001 49.507 65.137 11.968 1.00 30.45 O

HETATM 3937 O HOH 1002 60.147 50.684 -0.038 1.00 20.45 O

HETATM 3938 O HOH 1003 81.373 71.079 -9.758 1.00 33.72 O

HETATM 3939 O HOH 1004 38.408 45.301 -21.024 1.00 25.46 O

HETATM 3940 O HOH 1005 116.858 36.020 15.468 1.00 9.70 O

HETATM 3941 O HOH 1006 117.020 5.008 35.616 1.00 22.02 O

HETATM 3942 O HOH 1007 53.629 41.838 -27.847 1.00 25.63 O

HETATM 3943 O HOH 1008 31.293 68.100 -11.515 1.00 16.95 O

HETATM 3944 O HOH 1009 133.486 25.782 30.270 1.00 19.64 O

HETATM 3945 O HOH 1010 43.678 63.413 1.186 1.00 33.91 O

HETATM 3946 O HOH 1011 31.283 58.167 0.565 1.00 20.65 O

HETATM 3947 O HOH 1012 28.016 51.173 9.790 1.00 34.49 O

HETATM 3948 O HOH 1013 26.284 49.773 -1.366 1.00 24.73 O

HETATM 3949 O HOH 1014 121.380 12.162 27.383 1.00 16.47 O

HETATM 3950 O HOH 1015 99.844 24.778 2.480 1.00 21.96 O

HETATM 3951 O HOH 1016 100.632 24.385 36.207 1.00 15.70 O

HETATM 3952 O HOH 1017 99.325 1.738 7.889 1.00 14.55 O

HETATM 3953 O HOH 1018 113.206 34.261 30.650 1.00 25.46 O

HETATM 3954 O HOH 1019 28.639 43.549 -4.250 1.00 27.68 O

HETATM 3955 O HOH 1020 131.802 34.870 29.385 1.00 24.60 O

HETATM 3956 O HOH 1021 39.957 62.315 12.293 1.00 20.19 O

HETATM 3957 O HOH 1022 122.520 19.218 0.940 1.00 30.67 O

HETATM 3958 O HOH 1023 102.143 28.274 37.726 1.00 38.10 O

HETATM 3959 O HOH 1024 109.121 31.190 32.005 1.00 16.87 O

HETATM 3960 O HOH 1025 58.394 70.008 16.204 1.00 26.18 O

HETATM 3961 O HOH 1026 66.043 57.882 -22.891 1.00 21.55 O

HETATM 3962 O HOH 1027 48.520 43.708 10.945 1.00 26.90 O

HETATM 3963 O HOH 1028 40.697 59.609 7.882 1.00 24.81 O

HETATM 3964 O HOH 1029 108.981 5.434 -0.939 1.00 29.25 O

HETATM 3965 O HOH 1030 60.835 50.587 -11.102 1.00 26.02 O

HETATM 3966 O HOH 1031 76.016 57.150 -2.719 1.00 23.40 O

HETATM 3967 O HOH 1032 35.341 48.164 -17.698 1.00 23.33 O

HETATM 3968 O HOH 1033 131.072 16.346 17.992 1.00 24.73 O

HETATM 3969 O HOH 1034 32.983 66.759 -6.996 1.00 28.12 O

HETATM 3970 O HOH 1035 100.274 9.683 38.487 1.00 22.30 O

HETATM 3971 O HOH 1036 83.624 59.682 8.283 1.00 34.14 O

HETATM 3972 O HOH 1037 38.000 64.454 -2.943 1.00 18.57 O

HETATM 3973 O HOH 1038 80.162 49.563 -5.268 1.00 25.34 O

HETATM 3974 O HOH 1039 104.758 31.000 30.650 1.00 28.40 O

HETATM 3975 O HOH 1040 105.320 28.411 4.934 1.00 25.68 O

HETATM 3976 O HOH 1041 52.983 57.014 -0.092 1.00 23.84 O

HETATM 4199 O HOH 1264 78.165 66.441 19.181 1.00 24.40 O

HETATM 4200 O HOH 1265 96.984 22.516 27.431 1.00 28.02 O

HETATM 4201 O HOH 1266 117.030 37.111 23.567 1.00 25.41 O

HETATM 4202 O HOH 1267 125.198 42.036 18.126 1.00 20.77 O

HETATM 4203 O HOH 1268 43.079 66.822 16.053 1.00 35.81 O

HETATM 4204 O HOH 1269 41.391 31.216 -7.792 1.00 37.38 O

HETATM 4205 O HOH 1270 57.841 56.559 20.746 1.00 25.84 O

HETATM 4206 O HOH 1271 31.072 66.580 -15.301 1.00 17.70 O

HETATM 4207 O HOH 1272 132.459 13.097 32.518 1.00 17.19 O

HETATM 4208 O HOH 1273 104.347 28.393 30.818 1.00 37.68 O

HETATM 4209 O HOH 1274 114.698 4.675 27.897 1.00 17.03 O

HETATM 4210 O HOH 1275 28.301 56.084 -4.623 1.00 27.15 O

HETATM 4211 O HOH 1276 113.913 40.955 31.344 1.00 36.01 O

HETATM 4212 O HOH 1277 89.352 22.014 27.031 1.00 34.78 O

HETATM 4213 O HOH 1278 111.920 35.517 17.354 1.00 19.03 O

HETATM 4214 O HOH 1279 103.914 3.643 32.152 1.00 38.88 O

HETATM 4215 O HOH 1280 121.689 37.383 8.677 1.00 25.64 O

HETATM 4216 O HOH 1281 95.602 16.863 15.101 1.00 30.85 O

HETATM 4217 O HOH 1282 62.429 38.502 -1.030 1.00 32.40 O

HETATM 4218 O HOH 1283 101.346 18.339 39.308 1.00 19.67 O

HETATM 4219 O HOH 1284 133.399 30.110 38.806 1.00 45.31 O

HETATM 4220 O HOH 1285 73.964 66.868 20.493 1.00 21.77 O

HETATM 4221 O HOH 1286 53.857 62.698 -26.142 1.00 33.17 O

HETATM 4222 O HOH 1287 118.194 41.498 22.255 1.00 16.60 O

HETATM 4223 O HOH 1288 52.071 41.988 -1.466 1.00 13.26 O

HETATM 4224 O HOH 1289 30.155 60.977 -4.417 1.00 26.39 O

HETATM 4225 O HOH 1290 137.723 19.834 27.654 1.00 21.44 O

HETATM 4226 O HOH 1291 79.241 63.122 -10.150 1.00 43.99 O

HETATM 4227 O HOH 1292 25.180 58.412 -2.115 1.00 12.42 O

HETATM 4228 O HOH 1293 130.109 38.682 29.918 1.00 27.35 O

HETATM 4229 O HOH 1294 24.320 53.679 -2.892 1.00 15.07 O

HETATM 4230 O HOH 1295 139.061 28.556 38.189 1.00 19.45 O

HETATM 4231 O HOH 1296 129.627 32.222 44.269 1.00 22.26 O

HETATM 4232 O HOH 1297 109.201 30.424 -3.886 1.00 57.25 O

HETATM 4233 O HOH 1298 73.972 75.623 -8.176 1.00 30.06 O

HETATM 4234 O HOH 1299 86.586 62.740 7.426 1.00 34.38 O

HETATM 4235 O HOH 1300 27.604 66.396 -12.928 1.00 17.51 O

HETATM 4236 O HOH 1301 92.706 26.712 16.408 1.00 35.15 O

HETATM 4237 O HOH 1302 104.826 37.984 35.929 1.00 25.97 O

HETATM 4238 O HOH 1303 131.379 23.703 41.956 1.00 39.55 O

HETATM 4239 O HOH 1304 112.919 42.744 32.107 1.00 32.04 O

HETATM 4240 O HOH 1305 24.373 49.282 11.537 1.00 28.55 O

HETATM 4241 O HOH 1306 126.945 44.829 13.186 1.00 35.83 O

HETATM 4242 O HOH 1307 57.349 34.173 -4.762 1.00 23.18 O

HETATM 4243 O HOH 1308 29.397 38.680 -1.365 1.00 29.85 O

HETATM 4244 O HOH 1309 131.236 38.491 10.432 1.00 15.12 O

HETATM 4245 O HOH 1310 60.833 60.008 -22.104 1.00 32.00 O

HETATM 4246 O HOH 1311 60.525 39.962 -3.954 1.00 20.00 O

HETATM 4247 O HOH 1312 134.567 33.515 10.013 1.00 24.99 O

HETATM 4248 O HOH 1313 27.754 34.904 -3.859 1.00 26.44 O

HETATM 4249 O HOH 1314 47.257 41.496 8.949 1.00 14.71 O

HETATM 4250 O HOH 1315 56.095 34.007 -20.532 1.00 32.43 O

HETATM 4251 O HOH 1316 80.653 59.899 17.167 1.00 24.10 O

HETATM 4252 O HOH 1317 112.408 33.317 26.992 1.00 43.47 O

HETATM 4253 O HOH 1318 40.204 62.034 19.099 1.00 27.98 O

HETATM 4254 O HOH 1319 135.220 19.756 38.926 1.00 17.91 O

HETATM 4255 O HOH 1320 29.322 48.425 6.947 1.00 20.28 O

HETATM 4256 O HOH 1321 31.602 46.749 -10.874 1.00 22.63 O

HETATM 4257 O HOH 1322 36.728 66.716 -10.608 1.00 32.63 O

HETATM 4258 O HOH 1323 120.646 39.787 22.450 1.00 25.17 O

HETATM 4259 O HOH 1324 25.999 57.429 1.442 1.00 26.33 O

HETATM 4260 O HOH 1325 25.703 68.054 -13.791 1.00 31.82 O

HETATM 4261 O HOH 1326 74.628 44.161 -2.339 1.00 37.91 O

HETATM 4262 O HOH 1327 101.891 27.541 5.259 1.00 21.52 O

HETATM 4263 O HOH 1328 130.237 25.444 44.934 1.00 27.33 O

HETATM 4264 O HOH 1329 93.321 2.840 16.477 1.00 33.30 O

HETATM 4265 O HOH 1330 96.454 16.917 37.155 1.00 26.93 O

HETATM 4266 O HOH 1331 25.064 46.939 7.531 1.00 17.66 O

HETATM 4267 O HOH 1332 32.716 64.764 -12.546 1.00 23.73 O

HETATM 4268 O HOH 1333 60.135 70.301 11.783 1.00 23.55 O

HETATM 4269 O HOH 1334 126.915 38.367 24.210 1.00 30.70 O

HETATM 4270 O HOH 1335 122.424 38.872 5.923 1.00 27.91 O

HETATM 4271 O HOH 1336 123.691 13.869 27.540 1.00 22.47 O

HETATM 4272 O HOH 1337 52.445 64.955 -13.477 1.00 30.23 O HETATM 4273 O HOH 1338 114.700 42.258 20.956 1.00 21.08 O

HETATM 4274 O HOH 1339 95.892 29.997 15.630 1.00 29.64 O

HETATM 4275 O HOH 1340 27.871 47.487 -7.242 1.00 22.18 O

HETATM 4276 O HOH 1341 23.919 51.259 13.622 1.00 25.70 O

HETATM 4277 O HOH 1342 30.146 42.155 2.701 1.00 33.41 O

HETATM 4278 O HOH 1343 134.120 33.384 36.841 1.00 35.45 O

HETATM 4279 O HOH 1344 29.308 62.840 -12.157 1.00 18.20 O

HETATM 4280 O HOH 1345 116.412 18.104 42.550 1.00 45.17 O

HETATM 4281 O HOH 1346 58.435 49.585 -21.248 1.00 19.35 O

HETATM 4282 O HOH 1347 26.053 66.420 -9.515 1.00 28.46 O

HETATM 4283 O HOH 1348 35.990 49.109 -14.066 1.00 26.47 O

HETATM 4284 O HOH 1349 121.032 35.638 33.948 1.00 29.38 O

HETATM 4285 O HOH 1350 24.222 52.758 -6.714 1.00 18.92 O

HETATM 4286 O HOH 1351 73.487 46.175 -4.870 1.00 29.20 O

HETATM 4287 O HOH 1352 103.656 32.215 25.302 1.00 41.62 O

HETATM 4288 O HOH 1353 25.942 60.324 2.279 1.00 15.99 O

HETATM 4289 O HOH 1354 127.732 37.630 30.777 1.00 35.61 O

HETATM 4290 O HOH 1355 27.411 61.345 -15.457 1.00 23.90 O

HETATM 4291 O HOH 1356 27.778 46.624 -11.950 1.00 17.94 O

HETATM 4292 O HOH 1357 35.833 68.687 -12.863 1.00 37.96 O

HETATM 4293 O HOH 1358 103.458 28.182 18.126 1.00 22.39 O

HETATM 4294 O HOH 1359 137.453 19.353 21.897 1.00 24.53 O

HETATM 4295 O HOH 1360 106.238 3.138 24.617 1.00 36.15 O

HETATM 4296 O HOH 1361 131.417 16.035 14.512 1.00 24.04 O

HETATM 4297 O HOH 1362 50.618 67.877 9.139 1.00 28.11 O

HETATM 4298 O HOH 1363 123.111 42.044 22.698 1.00 27.41 O

HETATM 4299 O HOH 1364 47.751 52.143 -14.368 1.00 31.76 O

HETATM 4300 O HOH 1365 30.418 58.080 -13.906 1.00 22.32 O

HETATM 4301 O HOH 1366 123.430 34.022 12.389 1.00 30.40 O

HETATM 4302 O HOH 1367 54.882 64.511 10.260 1.00 38.01 O

HETATM 4303 O HOH 1368 27.292 60.052 -12.961 1.00 17.66 O

HETATM 4304 O HOH 1369 104.428 1.694 13.040 1.00 28.81 O

HETATM 4305 O HOH 1370 120.573 26.783 41.748 1.00 42.35 O

HETATM 4306 O HOH 1371 123.040 13.009 42.343 1.00 30.42 O

HETATM 4307 O HOH 1372 67.241 71.726 6.618 1.00 25.86 O

HETATM 4308 O HOH 1373 131.055 22.238 30.143 1.00 41.31 O

HETATM 4309 O HOH 1374 134.020 25.369 43.902 1.00 43.79 O

HETATM 4310 O HOH 1375 54.545 64.600 -28.059 1.00 43.30 O

HETATM 4311 O HOH 1376 101.544 28.426 8.396 1.00 35.69 O

HETATM 4312 O HOH 1377 114.610 20.863 43.805 1.00 31.15 O

HETATM 4313 O HOH 1378 114.192 30.005 13.321 1.00 48.48 O

HETATM 4314 O HOH 1379 106.782 21.117 28.704 1.00 32.27 O

HETATM 4315 O HOH 1380 107.593 36.659 12.182 1.00 32.78 O

HETATM 4316 O HOH 1381 59.583 34.111 -9.690 1.00 43.79 O

HETATM 4317 O HOH 1382 70.672 44.969 -1.433 1.00 28.59 O

HETATM 4318 O HOH 1383 38.989 61.422 -4.746 1.00 26.01 O

HETATM 4319 O HOH 1384 132.380 22.190 32.927 1.00 44.83 O

HETATM 4320 O HOH 1385 141.501 22.179 24.801 1.00 54.03 O

HETATM 4321 O HOH 1386 132.111 34.532 45.380 1.00 38.99 O

HETATM 4322 O HOH 1387 76.890 50.299 5.839 1.00 42.86 O

HETATM 4323 O HOH 1388 86.160 7.783 26.960 1.00 19.96 O

HETATM 4324 O HOH 1389 109.388 31.890 29.341 1.00 32.18 O

HETATM 4325 O HOH 1390 41.992 67.807 3.187 1.00 35.58 O

HETATM 4326 O HOH 1391 126.882 36.555 5.213 1.00 29.01 O

HETATM 4327 O HOH 1392 120.208 40.979 8.368 1.00 30.22 O

HETATM 4328 O HOH 1393 72.935 59.092 13.814 1.00 37.15 O

HETATM 4329 O HOH 1394 32.928 68.741 -17.844 1.00 21.79 O

HETATM 4330 O HOH 1395 134.579 33.777 6.198 1.00 41.24 O

HETATM 4331 O HOH 1396 38.775 64.512 8.936 1.00 35.27 O

HETATM 4332 O HOH 1397 79.901 70.704 -12.971 1.00 39.89 O

HETATM 4333 O HOH 1398 99.261 25.836 20.292 1.00 43.86 O

HETATM 4334 O HOH 1399 51.698 58.115 -24.597 1.00 30.68 O

HETATM 4335 O HOH 1400 121.820 37.161 20.904 1.00 39.91 O

HETATM 4336 O HOH 1401 29.706 53.441 1.353 1.00 32.77 O

HETATM 4337 O HOH 1402 73.699 63.968 19.667 1.00 35.07 O

HETATM 4338 O HOH 1403 101.283 31.940 10.059 1.00 43.74 O

HETATM 4339 O HOH 1404 86.218 61.097 13.295 1.00 32.18 O

HETATM 4340 O HOH 1405 42.854 66.914 11.077 1.00 34.22 O

HETATM 4341 O HOH 1406 104.548 28.339 8.981 1.00 23.79 O

HETATM 4342 O HOH 1407 27.322 56.073 10.332 1.00 36.90 O

HETATM 4343 O HOH 1408 65.480 51.846 15.352 1.00 54.16 O

HETATM 4344 O HOH 1409 45.868 67.475 10.364 1.00 31.00 O

HETATM 4345 O HOH 1410 108.929 30.086 27.261 1.00 30.24 O

HETATM 4346 O HOH 1411 28.554 59.200 -16.352 1.00 33.04 O HETATM 4347 O HOH 1412 106.550 37.974 10.274 1.00 29.40 O

HETATM 4348 O HOH 1413 109.370 38.810 13.919 1.00 41.19 O

HETATM 4349 O HOH 1414 124.586 42.265 25.423 1.00 36.93 O

HETATM 4350 O HOH 1415 136.881 17.852 19.046 1.00 33.20 O

HETATM 4351 O HOH 1416 132.638 37.318 48.178 1.00 35.18 O

HETATM 4352 O HOH 1417 105.034 29.405 35.773 1.00 42.01 O

HETATM 4353 O HOH 1418 127.749 39.419 35.000 1.00 23.92 O

HETATM 4354 O HOH 1419 128.108 34.312 7.426 1.00 38.05 O

HETATM 4355 O HOH 1420 120.665 35.120 18.931 1.00 34.85 O

HETATM 4356 O HOH 1421 131.338 30.233 44.533 1.00 33.21 O

HETATM 4357 O HOH 1422 57.368 43.249 7.327 1.00 31.35 O

HETATM 4358 O HOH 1423 24.822 52.922 7.364 1.00 21.19 O

HETATM 4359 O HOH 1424 72.794 50.262 -6.462 1.00 32.71 O

HETATM 4360 O HOH 1425 46.464 62.874 8.519 1.00 37.32 O

HETATM 4361 O HOH 1426 119.257 0.984 18.584 1.00 25.64 O

HETATM 4362 O HOH 1427 135.243 37.676 32.274 1.00 38.25 O

HETATM 4363 O HOH 1428 34.165 51.102 -16.800 1.00 40.75 O

HETATM 4364 O HOH 1429 56.235 66.751 -27.695 1.00 31.30 O

HETATM 4365 O HOH 1430 117.568 32.458 11.885 1.00 21.71 O

HETATM 4366 O HOH 1431 69.626 73.604 -15.898 1.00 19.30 O

HETATM 4367 O HOH 1432 111.982 40.462 27.810 1.00 29.86 O

HETATM 4368 O HOH 1433 48.580 43.492 13.455 1.00 29.92 O

HETATM 4369 O HOH 1434 111.848 33.005 17.054 1.00 25.44 O

HETATM 4370 O HOH 1435 43.955 61.171 6.647 1.00 25.02 O

HETATM 4371 O HOH 1436 91.516 13.768 34.795 1.00 52.98 O

HETATM 4372 O HOH 1437 133.282 39.323 45.555 1.00 24.14 O

HETATM 4373 O HOH 1438 125.664 45.848 15.636 1.00 34.94 O

HETATM 4374 O HOH 1439 41.078 68.803 17.955 1.00 29.87 O

HETATM 4375 O HOH 1440 42.588 38.734 -15.698 1.00 41.46 O

HETATM 4376 O HOH 1441 128.197 36.907 21.425 1.00 37.74 O

HETATM 4377 O HOH 1442 27.257 56.142 -16.462 1.00 23.46 O

HETATM 4378 O HOH 1443 72.820 64.595 12.308 1.00 38.91 O

HETATM 4379 O HOH 1444 135.654 38.638 28.796 1.00 35.88 O

HETATM 4380 O HOH 1445 115.552 44.311 21.916 1.00 30.25 O

HETATM 4381 O HOH 1446 29.780 41.106 15.236 1.00 41.33 O

HETATM 4382 O HOH 1447 33.334 69.040 -20.183 1.00 27.24 O

HETATM 4383 O HOH 1448 122.260 43.985 27.510 1.00 26.63 O

HETATM 4384 O HOH 1449 72.060 50.830 -10.430 1.00 33.58 O

HETATM 4385 O HOH 1450 55.674 39.357 5.560 1.00 46.92 O

HETATM 4386 O HOH 1451 69.968 62.920 -17.124 1.00 20.76 O

HETATM 4387 O HOH 1452 29.975 37.026 -3.886 1.00 25.41 O

HETATM 4388 O HOH 1453 103.327 36.361 9.976 1.00 39.61 O

HETATM 4389 O HOH 1454 22.226 55.379 6.321 1.00 26.26 O

HETATM 4390 O HOH 1455 132.387 33.280 40.981 1.00 30.35 O

HETATM 4391 O HOH 1456 108.550 39.896 9.148 1.00 29.18 O

HETATM 4392 O HOH 1457 139.150 26.961 41.114 1.00 33.06 O

HETATM 4393 O HOH 1458 122.953 24.738 2.000 1.00 30.31 O

HETATM 4394 O HOH 1459 84.842 57.678 9.676 1.00 24.67 O

HETATM 4395 O HOH 1460 130.432 40.268 18.811 1.00 29.38 O

HETATM 4396 O HOH 1461 118.696 13.195 23.645 1.00 33.34 O

END

Table 2 Atomic structure coordinate data obtained from X-ray diffraction from the ligand-binding domain of the mineralocorticoid receptor in complex with progesterone and harboring the S810L and C91 OA mutations

Head Col 2: ATOM

Head Col 3: ATOM TYPE

Head Col 4: RESIDUE TYPE

Head Col 5: CHAIN

Head Col 6: RESIDUE

Head Col 5: X

Head Col 6: Y

Head Col 7: Z

Head Col 8: OCC

Head Col 9: B

Head Col 10: ATOM

ATOM 1 N SER A 737 104.845 3.975 17.446 1.00 63.54 N

ATOM 2 CA SER A 737 104.554 3.256 16.173 1.00 64.03 C

ATOM 3 C SER A 737 105.433 2.016 15.996 1.00 63.32 C

ATOM 4 O SER A 737 106.561 2.096 15.494 1.00 63.72 O

ATOM 5 CB SER A 737 104.748 4.189 14.975 1.00 64.72 C

ATOM 6 OG SER A 737 104.512 3.491 13.762 1.00 66.41 O

ATOM 7 N PRO A 738 104.920 0.848 16.411 1.00 61.96 N

ATOM 8 CA PRO A 738 105.633 -0.423 16.310 1.00 60.23 C

ATOM 9 C PRO A 738 106.223 -0.735 14.932 1.00 59.56 C

ATOM 10 O PRO A 738 107.446 -0.817 14.784 1.00 60.00 O

ATOM 11 CB PRO A 738 104.572 -1.438 16.729 1.00 60.33 C

ATOM 12 CG PRO A 738 103.821 -0.707 17.769 1.00 61.73 C

ATOM 13 CD PRO A 738 103.649 0.671 17.139 1.00 62.48 C

ATOM 14 N VAL A 739 105.358 -0.907 13.930 1.00 58.00 N

ATOM 15 CA VAL A 739 105.794 -1.253 12.574 1.00 56.35 C

ATOM 16 C VAL A 739 106.948 -0.423 12.043 1.00 55.78 C

ATOM 17 O VAL A 739 107.922 -0.963 11.509 1.00 55.35 O

ATOM 18 CB VAL A 739 104.644 -1.150 11.557 1.00 55.83 C

ATOM 19 CGl VAL A 739 105.157 -1.447 10.151 1.00 55.72 C

ATOM 20 CG2 VAL A 739 103.546 -2.119 11.925 1.00 57.28 C

ATOM 21 N MET A 740 106.853 0.893 12.175 1.00 54.89 N

ATOM 22 CA MET A 740 107.931 1.713 11.667 1.00 53.54 C

ATOM 23 C MET A 740 109.229 1.446 12.418 1.00 51.59 C

ATOM 24 O MET A 740 110.293 1.372 11.804 1.00 50.24 O

ATOM 25 CB MET A 740 107.571 3.195 11.724 1.00 53.73 C

ATOM 26 CG MET A 740 108.649 4.043 11.092 1.00 55.02 C

ATOM 27 SD MET A 740 108.062 5.541 10.349 1.00 56.06 S

ATOM 28 CE MET A 740 107.434 6.374 11.763 1.00 57.46 C

ATOM 29 N VAL A 741 109.156 1.287 13.738 1.00 49.84 N

ATOM 30 CA VAL A 741 110.374 1.007 14.503 1.00 48.92 C

ATOM 31 C VAL A 741 110.989 -0.350 14.133 1.00 47.66 C

ATOM 32 O VAL A 741 112.214 -0.471 13.994 1.00 46.42 O

ATOM 33 CB VAL A 741 110.116 1.016 16.014 1.00 48.09 C

ATOM 34 CGl VAL A 741 111.401 0.653 16.748 1.00 47.98 C

ATOM 35 CG2 VAL A 741 109.624 2.380 16.448 1.00 46.52 C

ATOM 36 N LEU A 742 110.133 -1.391 13.974 1.00 46.74 N

ATOM 37 CA LEU A 742 110.587 -2.761 13.625 1.00 46.82 C

ATOM 38 C LEU A 742 111.446 -2.819 12.369 1.00 47.04 C

ATOM 39 O LEU A 742 112.506 -3.442 12.372 1.00 46.03 O

ATOM 40 CB LEU A 742 109.402 -3.684 13.412 1.00 46.58 C

ATOM 41 CG LEU A 742 108.409 -3.871 14.558 1.00 47.49 C

ATOM 42 CDl LEU A 742 107.435 -4.989 14.256 1.00 46.70 C

ATOM 43 CD2 LEU A 742 109.137 -4.133 15.856 1.00 49.01 C

ATOM 44 N GLU A 743 111.082 -2.029 11.282 1.00 47.85 N

ATOM 45 CA GLU A 743 111.860 -2.210 9.956 1.00 50.11 C

ATOM 46 C GLU A 743 113.298 -1.605 9.824 1.00 51.16 C

ATOM 47 O GLU A 743 114.213 -2.198 9.244 1.00 53.18 O

ATOM 48 CB GLU A 743 111.135 -1.674 8.706 1.00 51.11 C

ATOM 49 CG GLU A 743 109.775 -1.042 8.778 1.00 55.12 C

ATOM 50 CD GLU A 743 108.968 -1.366 7.522 1.00 55.32 C

ATOM 125 CB ALA A 752 129.249 -16.870 6.638 1.00 67.29 C

ATOM 126 N GLY A 753 132.148 -15.155 6.125 1.00 67.65 N

ATOM 127 CA GLY A 753 133.578 -15.334 5.937 1.00 68.22 C

ATOM 128 C GLY A 753 133.856 -16.762 5.485 1.00 68.00 C

ATOM 129 O GLY A 753 134.504 -17.543 6.182 1.00 66.99 O

ATOM 130 N TYR A 754 133.342 -17.109 4.314 1.00 68.66 N

ATOM 131 CA TYR A 754 133.523 -18.441 3.772 1.00 69.08 C

ATOM 132 C TYR A 754 134.973 -18.630 3.327 1.00 69.86 C

ATOM 133 O TYR A 754 135.720 -17.659 3.170 1.00 70.00 O

ATOM 134 CB TYR A 754 132.583 -18.640 2.586 1.00 69.99 C

ATOM 135 CG TYR A 754 132.592 -20.037 2.026 1.00 71.26 C

ATOM 136 CDl TYR A 754 132.231 -20.275 0.702 1.00 72.03 C

ATOM 137 CD2 TYR A 754 132.949 -21.127 2.821 1.00 71.85 C

ATOM 138 CEl TYR A 754 132.225 -21.566 0.176 1.00 73.20 C

ATOM 139 CE2 TYR A 754 132.947 -22.422 2.310 1.00 72.69 C

ATOM 140 CZ TYR A 754 132.583 -22.634 0.986 1.00 73.08 C

ATOM 141 OH TYR A 754 132.566 -23.907 0.469 1.00 74.11 O

ATOM 142 N ASP A 760 136.165 -28.702 1.003 1.00 60.71 N

ATOM 143 CA ASP A 760 135.082 -28.327 1.899 1.00 60.86 C

ATOM 144 C ASP A 760 134.324 -29.545 2.422 1.00 60.08 C

ATOM 145 O ASP A 760 133.394 -30.052 1.788 1.00 59.52 O

ATOM 146 CB ASP A 760 134.110 -27.375 1.196 1.00 63.13 C

ATOM 147 CG ASP A 760 133.581 -27.934 -0.118 1.00 65.70 C

ATOM 148 ODl ASP A 760 132.484 -27.493 -0.538 1.00 65.65 O

ATOM 149 OD2 ASP A 760 134.257 -28.800 -0.731 1.00 65.83 O

ATOM 150 N THR A 761 134.736 -30.011 3.594 1.00 59.30 N

ATOM 151 CA THR A 761 134.112 -31.159 4.223 1.00 57.51 C

ATOM 152 C THR A 761 132.804 -30.748 4.880 1.00 56.80 C

ATOM 153 O THR A 761 132.252 -29.688 4.576 1.00 56.36 O

ATOM 154 CB THR A 761 135.030 -31.768 5.292 1.00 56.43 C

ATOM 155 OGl THR A 761 135.353 -30.776 6.272 1.00 55.53 O

ATOM 156 CG2 THR A 761 136.304 -32.275 4.660 1.00 57.15 C

ATOM 157 N ALA A 762 132.312 -31.601 5.774 1.00 55.73 N

ATOM 158 CA ALA A 762 131.073 -31.341 6.487 1.00 55.37 C

ATOM 159 C ALA A 762 131.415 -30.535 7.728 1.00 54.82 C

ATOM 160 O ALA A 762 130.669 -29.646 8.131 1.00 53.97 O

ATOM 161 CB ALA A 762 130.404 -32.658 6.879 1.00 54.13 C

ATOM 162 N GLU A 763 132.561 -30.856 8.317 1.00 54.70 N

ATOM 163 CA GLU A 763 133.043 -30.191 9.518 1.00 55.19 C

ATOM 164 C GLU A 763 133.387 -28.714 9.280 1.00 53.90 C

ATOM 165 O GLU A 763 133.101 -27.861 10.124 1.00 52.04 O

ATOM 166 CB GLU A 763 134.265 -30.944 10.066 1.00 57.04 C

ATOM 167 CG GLU A 763 134.988 -31.798 9.019 1.00 60.23 C

ATOM 168 CD GLU A 763 134.267 -33.112 8.719 1.00 62.29 C

ATOM 169 OEl GLU A 763 134.295 -33.559 7.547 1.00 62.47 O

ATOM 170 OE2 GLU A 763 133.680 -33.707 9.657 1.00 63.08 O

ATOM 171 N ASN A 764 133.997 -28.415 8.134 1.00 53.05 N

ATOM 172 CA ASN A 764 134.358 -27.040 7.814 1.00 52.60 C

ATOM 173 C ASN A 764 133.122 -26.229 7.487 1.00 51.93 C

ATOM 174 O ASN A 764 133.034 -25.044 7.825 1.00 52.62 O

ATOM 175 CB ASN A 764 135.327 -26.989 6.633 1.00 52.41 C

ATOM 176 CG ASN A 764 136.736 -27.311 7.037 1.00 53.73 C

ATOM 177 ODl ASN A 764 137.648 -27.314 6.211 1.00 54.61 O

ATOM 178 ND2 ASN A 764 136.931 -27.581 8.321 1.00 54.04 N

ATOM 179 N LEU A 765 132.169 -26.876 6.826 1.00 50.18 N

ATOM 180 CA LEU A 765 130.932 -26.216 6.455 1.00 49.18 C

ATOM 181 C LEU A 765 130.133 -25.838 7.693 1.00 48.50 C

ATOM 182 O LEU A 765 129.616 -24.724 7.795 1.00 48.42 O

ATOM 183 CB LEU A 765 130.089 -27.121 5.563 1.00 48.53 C

ATOM 184 CG LEU A 765 128.775 -26.485 5.111 1.00 49.47 C

ATOM 185 CDl LEU A 765 129.005 -25.024 4.668 1.00 49.53 C

ATOM 186 CD2 LEU A 765 128.189 -27.313 3.983 1.00 50.07 C

ATOM 187 N LEU A 766 130.030 -26.778 8.626 1.00 46.74 N

ATOM 188 CA LEU A 766 129.299 -26.544 9.858 1.00 44.39 C

ATOM 189 C LEU A 766 130.032 -25.541 10.734 1.00 42.11 C

ATOM 190 O LEU A 766 129.410 -24.750 11.434 1.00 42.05 O

ATOM 191 CB LEU A 766 129.118 -27.852 10.634 1.00 43.35 C

ATOM 192 CG LEU A 766 128.264 -28.946 10.002 1.00 44.97 C

ATOM 193 CDl LEU A 766 128.050 -30.053 11.036 1.00 46.43 C

ATOM 194 CD2 LEU A 766 126.922 -28.376 9.545 1.00 45.30 C

ATOM 195 N SER A 767 131.357 -25.576 10.706 1.00 39.62 N

ATOM 196 CA SER A 767 132.124 -24.651 11.531 1.00 37.65 C

ATOM 197 C SER A 767 131.875 -23.237 11.050 1.00 36.57 C

ATOM 198 O SER A 767 131.757 -22.313 11.838 1.00 35.10 O ATOM 199 CB SER A 767 133.612 -24.993 11.471 1.00 36.07 C

ATOM 200 OG SER A 767 133.882 -26.164 12.227 1.00 35.85 O

ATOM 201 N THR A 768 131.765 -23.098 9.738 1.00 36.62 N

ATOM 202 CA THR A 768 131.523 -21.816 9.114 1.00 35.66 C

ATOM 203 C THR A 768 130.158 -21.257 9.519 1.00 33.48 C

ATOM 204 O THR A 768 130.057 -20.097 9.926 1.00 33.69 O

ATOM 205 CB THR A 768 131.606 -21.945 7.566 1.00 36.68 C

ATOM 206 OGl THR A 768 132.910 -22.422 7.192 1.00 37.65 O

ATOM 207 CG2 THR A 768 131.366 -20.604 6.905 1.00 35.47 C

ATOM 208 N LEU A 769 129.114 -22.075 9.408 1.00 32.94 N

ATOM 209 CA LEU A 769 127.765 -21.633 9.764 1.00 33.99 C

ATOM 210 C LEU A 769 127.707 -21.279 11.259 1.00 34.46 C

ATOM 211 O LEU A 769 127.040 -20.328 11.652 1.00 33.73 O

ATOM 212 CB LEU A 769 126.732 -22.709 9.401 1.00 32.23 C

ATOM 213 CG LEU A 769 126.567 -23.135 7.916 1.00 33.51 C

ATOM 214 CDl LEU A 769 125.569 -24.284 7.831 1.00 28.96 C

ATOM 215 CD2 LEU A 769 126.079 -21.984 7.041 1.00 29.65 C

ATOM 216 N ASN A 770 128.423 -22.024 12.097 1.00 35.04 N

ATOM 217 CA ASN A 770 128.450 -21.685 13.518 1.00 35.50 C

ATOM 218 C ASN A 770 129.086 -20.286 13.711 1.00 35.38 C

ATOM 219 O ASN A 770 128.566 -19.476 14.493 1.00 35.05 O

ATOM 220 CB ASN A 770 129.214 -22.749 14.331 1.00 36.80 C

ATOM 221 CG ASN A 770 128.417 -24.042 14.503 1.00 37.58 C

ATOM 222 ODl ASN A 770 127.190 -24.030 14.475 1.00 38.88 O

ATOM 223 ND2 ASN A 770 129.115 -25.158 14.699 1.00 39.85 N

ATOM 224 N ARG A 771 130.202 -20.003 13.029 1.00 34.30 N

ATOM 225 CA ARG A 771 130.835 -18.685 13.148 1.00 35.86 C

ATOM 226 C ARG A 771 129.885 -17.601 12.631 1.00 36.18 C

ATOM 227 O ARG A 111 129.812 -16.507 13.197 1.00 35.99 O

ATOM 228 CB ARG A 111 132.149 -18.607 12.355 1.00 38.15 C

ATOM 229 CG ARG A 111 133.289 -19.417 12.937 1.00 41.60 C

ATOM 230 CD ARG A 111 134.651 -19.036 12.336 1.00 42.89 C

ATOM 231 NE ARG A 111 135.590 -20.158 12.427 1.00 45.12 N

ATOM 232 CZ ARG A 111 136.919 -20.048 12.451 1.00 46.45 C

ATOM 233 NHl ARG ^•A 111 137.510 -18.860 12.388 1.00 46.17 N

ATOM 234 NH2 ARG A 111 137.663 -21.140 12.554 1.00 48.85 N

ATOM 235 N LEU A 772 129.174 -17.905 11.545 1.00 34.79 N

ATOM 236 CA LEU A 772 128.207 -16.970 10.966 1.00 34.88 C

ATOM 237 C LEU A 772 127.090 -16.769 11.977 1.00 33.53 C

ATOM 238 O LEU A 772 126.531 -15.674 12.093 1.00 32.47 O

ATOM 239 CB LEU A 772 127.611 -17.530 9.654 1.00 34.05 C

ATOM 240 CG LEU A 772 126.412 -16.792 9.032 1.00 33.63 C

ATOM 241 CDl LEU A 772 126.850 -15.463 8.413 1.00 30.42 C

ATOM 242 CD2 LEU A 772 125.766 -17.680 7.985 1.00 30.67 C

ATOM 243 N ALA A 773 126.763 -17.833 12.701 1.00 33.59 N

ATOM 244 CA ALA A 773 125.701 -17.766 13.696 1.00 35.72 C

ATOM 245 C ALA A 773 126.143 -16.817 14.796 1.00 35.94 C

ATOM 246 O ALA A 773 125.390 -15.934 15.203 1.00 36.79 O

ATOM 247 CB ALA A 773 125.416 -19.159 14.280 1.00 35.70 C

ATOM 248 N GLY A 774 127.372 -17.003 15.265 1.00 36.75 N

ATOM 249 CA GLY A 774 127.893 -16.146 16.311 1.00 38.11 C

ATOM 250 C GLY A 774 127.885 -14.680 15.908 1.00 39.96 C

ATOM 251 O GLY A 774 127.654 -13.800 16.740 1.00 40.02 O

ATOM 252 N LYS A lib 128.129 -14.421 14.624 1.00 41.10 N

ATOM 253 CA LYS A lib 128.167 -13.062 14.094 1.00 41.29 C

ATOM 254 C LYS A lib 126.750 -12.519 13.941 1.00 40.37 C

ATOM 255 O LYS A lib 126.517 -11.319 14.090 1.00 41.94 O

ATOM 256 CB LYS A lib 128.896 -13.042 12.743 1.00 44.74 C

ATOM 257 CG LYS A lib 129.540 -11.702 12.387 1.00 47.94 C

ATOM 258 CD LYS A lib 131.053 -11.704 12.608 1.00 50.36 C

ATOM 259 CE LYS A lib 131.673 -10.333 12.259 1.00 52.61 C

ATOM 260 NZ LYS A lib 133.177 -10.275 12.412 1.00 53.35 N

ATOM 261 N GLN A 116 125.796 -13.399 13.648 1.00 39.36 N

ATOM 262 CA GLN A 776 124.407 -12.966 13.513 1.00 37.25 C

ATOM 263 C GLN A 776 123.787 -12.693 14.879 1.00 36.03 C

ATOM 264 O GLN A 776 122.902 -11.858 15.011 1.00 35.95 O

ATOM 265 CB GLN A 776 123.573 -14.022 12.779 1.00 36.38 C

ATOM 266 CG GLN A 776 123.892 -14.141 11.309 1.00 35.35 C

ATOM 267 CD GLN A 776 123.052 -15.184 10.626 1.00 32.33 C

ATOM 268 OEl GLN A 776 122.271 -15.879 11.270 1.00 35.08 O

ATOM 269 NE2 GLN A 776 123.202 -15.302 9.316 1.00 31.36 N

ATOM 270 N MET A 111 124.234 -13.417 15.895 1.00 35.63 N

ATOM 271 CA MET A 111 123.708 -13.217 17.235 1.00 35.77 C

ATOM 272 C MET A 111 124.137 -11.865 17.777 1.00 35.90 C

ATOM 347 CA VAL A 786 115.855 -1.398 20.997 1.00 38.30 C

ATOM 348 C VAL A 786 114.438 -1.794 20.587 1.00 38.56 C

ATOM 349 O VAL A 786 113.741 -1.060 19.884 1.00 38.20 O

ATOM 350 CB VAL A 786 116.519 -0.668 19.798 1.00 37.13 C

ATOM 351 CGl VAL A 786 117.683 0.160 20.281 1.00 38.06 C

ATOM 352 CG2 VAL A 786 116.982 -1.659 18.769 1.00 35.73 C

ATOM 353 N LEU A 787 114.027 -2.967 21.053 1.00 38.28 N

ATOM 354 CA LEU A 787 112.722 -3.526 20.766 1.00 39.04 C

ATOM 355 C LEU A 787 111.682 -3.023 21.764 1.00 39.05 C

ATOM 356 O LEU A 787 111.834 -3.211 22.971 1.00 40.85 O

ATOM 357 CB LEU A 787 112.835 -5.042 20.849 1.00 40.41 C

ATOM 358 CG LEU A 787 111.729 -5.967 20.370 1.00 40.85 C

ATOM 359 CDl LEU A 787 111.730 -6.005 18.845 1.00 41.18 C

ATOM 360 CD2 LEU A 787 111.988 -7.363 20.945 1.00 39.69 C

ATOM 361 N PRO A 788 110.609 -2.386 21.273 1.00 38.02 N

ATOM 362 CA PRO A 788 109.537 -1.855 22.125 1.00 38.27 C

ATOM 363 C PRO A 788 108.943 -2.906 23.068 1.00 37.80 C

ATOM 364 O PRO A 788 108.548 -3.999 22.647 1.00 36.06 O

ATOM 365 CB PRO A 788 108.512 -1.322 21.114 1.00 38.65 C

ATOM 366 CG PRO A 788 109.365 -0.911 19.969 1.00 39.63 C

ATOM 367 CD PRO A 788 110.349 -2.072 19.859 1.00 38.93 C

ATOM 368 N GLY A 789 108.869 -2.543 24.344 1.00 37.55 N

ATOM 369 CA GLY A 789 108.362 -3.448 25.353 1.00 39.06 C

ATOM 370 C GLY A 789 109.539 -4.259 25.862 1.00 40.22 C

ATOM 371 O GLY A 789 110.125 -3.951 26.899 1.00 40.99 O

ATOM 372 N PHE A 790 109.892 -5.286 25.094 1.00 39.84 N

ATOM 373 CA PHE A 790 110.997 -6.187 25.394 1.00 38.80 C

ATOM 374 C PHE A 790 112.178 -5.531 26.082 1.00 38.35 C

ATOM 375 O PHE A 790 112.764 -6.115 26.994 1.00 38.86 O

ATOM 376 CB PHE A 790 111.492 -6.838 24.106 1.00 35.95 C

ATOM 377 CG PHE A 790 112.490 -7.937 24.322 1.00 34.87 C

ATOM 378 CDl PHE A 790 112.074 -9.217 24.653 1.00 33.06 C

ATOM 379 CD2 PHE A 790 113.850 -7.698 24.165 1.00 33.01 C

ATOM 380 CEl PHE A 790 112.992 -10.241 24.823 1.00 31.74 C

ATOM 381 CE2 PHE A 790 114.768 -8.706 24.332 1.00 30.32 C

ATOM 382 CZ PHE A 790 114.339 -9.987 24.662 1.00 31.63 C

ATOM 383 N LYS A 791 112.540 -4.332 25.650 1.00 39.67 N

ATOM 384 CA LYS A 791 113.683 -3.648 26.255 1.00 41.67 C

ATOM 385 C LYS A 791 113.429 -3.110 27.668 1.00 42.24 C

ATOM 386 O LYS A 791 114.359 -2.673 28.339 1.00 42.05 O

ATOM 387 CB LYS A 791 114.166 -2.510 25.350 1.00 42.52 C

ATOM 388 CG LYS A 791 113.161 -1.378 25.118 1.00 44.02 C

ATOM 389 CD LYS A 791 113.839 -0.239 24.359 1.00 45.88 C

ATOM 390 CE LYS A 791 112.932 0.958 24.153 1.00 46.93 C

ATOM 391 NZ LYS A 791 111.812 0.645 23.233 1.00 47.54 N

ATOM 392 N ASN A 792 112.181 -3.153 28.129 1.00 42.90 N

ATOM 393 CA ASN A 792 111.850 -2.655 29.464 1.00 43.59 C

ATOM 394 C ASN A 792 111.638 -3.740 30.524 1.00 44.33 C

ATOM 395 O ASN A 792 111.414 -3.431 31.700 1.00 44.74 O

ATOM 396 CB ASN A 792 110.623 -1.748 29.394 1.00 44.05 C

ATOM 397 CG ASN A 792 110.943 -0.377 28.808 1.00 46.47 C

ATOM 398 ODl ASN A 792 112.015 0.184 29.065 1.00 47.32 O

ATOM 399 ND2 ASN A 792 110.012 0.175 28.019 1.00 46.99 N

ATOM 400 N LEU A 793 111.703 -5.005 30.104 1.00 42.67 N

ATOM 401 CA LEU A 793 111.564 -6.131 31.019 1.00 41.83 C

ATOM 402 C LEU A 793 112.892 -6.288 31.755 1.00 42.31 C

ATOM 403 O LEU A 793 113.941 -5.920 31.230 1.00 42.81 O

ATOM 404 CB LEU A 793 111.327 -7.438 30.247 1.00 40.35 C

ATOM 405 CG LEU A 793 110.089 -7.786 29.423 1.00 39.06 C

ATOM 406 CDl LEU A 793 110.430 -9.009 28.605 1.00 36.88 C

ATOM 407 CD2 LEU A 793 108.872 -8.053 30.311 1.00 35.90 C

ATOM 408 N PRO A 794 112.872 -6.834 32.981 1.00 42.66 N

ATOM 409 CA PRO A 794 114.162 -6.991 33.656 1.00 42.23 C

ATOM 410 C PRO A 794 115.153 -7.685 32.710 1.00 43.33 C

ATOM 411 O PRO A 794 114.786 -8.628 32.002 1.00 43.32 O

ATOM 412 CB PRO A 794 113.813 -7.841 34.886 1.00 41.91 C

ATOM 413 CG PRO A 794 112.400 -8.374 34.597 1.00 40.33 C

ATOM 414 CD PRO A 794 111.766 -7.262 33.851 1.00 41.72 C

ATOM 415 N LEU A 795 116.400 -7'.2IO 32.692 1.00 44.42 N

ATOM 416 CA LEU A 795 117.438 -7.759 31.823 1.00 45.24 C

ATOM 417 C LEU A 795 117.489 -9.287 31.866 1.00 46.50 C

ATOM 418 O LEU A 795 117.892 -9.941 30.898 1.00 46.20 O

ATOM 419 CB LEU A 795 118.795 -7.173 32.214 1.00 44.95 C

ATOM 420 CG LEU A 795 120.001 -7.505 31.330 1.00 46.07 C

ATOM 643 CB HIS A 821 118.495 -13.226 -1.994 1.00 56.59 C

ATOM 644 CG HIS A 821 118.731 -12.007 -1.153 1.00 59.84 C

ATOM 645 NDl HIS A 821 119.171 -10.809 -1.678 1.00 60.68 N

ATOM 646 CD2 HIS A 821 118.588 -11.801 0.178 1.00 60.17 C

ATOM 647 CEl HIS A 821 119.288 -9.920 -0.708 1.00 60.48 C

ATOM 648 NE2 HIS A 821 118.940 -10.497 0.428 1.00 59.47 N

ATOM 649 N THR A 822 116.454 -15.451 -3.432 1.00 55.06 N

ATOM 650 CA THR A 822 116.422 -16.584 -4.349 1.00 55.83 C

ATOM 651 C THR A 822 115.040 -17.166 -4.619 1.00 56.74 C

ATOM 652 O THR A 822 114.928 -18.317 -5.048 1.00 57.03 O

ATOM 653 CB THR A 822 117.311 -17.729 -3.837 1.00 55.54 C

ATOM 654 OGl THR A 822 116.582 -18.503 -2.874 1.00 56.33 O

ATOM 655 CG2 THR A 822 118.576 -17.175 -3.198 1.00 54.68 C

ATOM 656 N ASN A 823 113.990 -16.391 -4.378 1.00 56.11 N

ATOM 657 CA ASN A 823 112.648 -16.902 -4.613 1.00 56.60 C

ATOM 658 C ASN A 823 112.493 -18.252 -3.901 1.00 56.54 C

ATOM 659 O ASN A 823 111.778 -19.136 -4.377 1.00 57.20 O

ATOM 660 CB ASN A 823 112.396 -17.090 -6.118 1.00 56.72 C

ATOM 661 CG ASN A 823 112.584 -15.808 -6.917 1.00 57.02 C

ATOM 662 ODl ASN A 823 112.036 -14.757 -6.580 1.00 57.74 O

ATOM 663 ND2 ASN A 823 113.360 -15.894 -7.992 1.00 57.01 N

ATOM 664 N SER A 824 113.185 -18.410 -2.773 1.00 56.31 N

ATOM 665 CA SER A 824 113.126 -19.636 -1.967 1.00 55.14 C

ATOM 666 C SER A 824 113.780 -20.857 -2.594 1.00 53.61 C

ATOM 667 O SER A 824 113.750 -21.937 -2.017 1.00 53.73 O

ATOM 668 CB SER A 824 111.672 -19.986 -1.619 1.00 54.99 C

ATOM 669 OG SER A 824 111.067 -18.971 -0.829 1.00 54.28 O

ATOM 670 N GLN A 825 114.390 -20.690 -3.759 1.00 53.08 N

ATOM 671 CA GLN A 825 115.007 -21.820 -4.431 1.00 52.32 C

ATOM 672 C GLN A 825 116.280 -22.363 -3.765 1.00 51.88 C

ATOM 673 O GLN A 825 116.634 -23.526 -3.957 1.00 51.69 O

ATOM 674 CB GLN A 825 115.261 -21.465 -5.902 1.00 53.19 C

ATOM 675 CG GLN A 825 113.989 -21.024 -6.648 1.00 52.28 C

ATOM 676 CD GLN A 825 114.139 -21.033 -8.167 1.00 52.78 C

ATOM 677 OEl GLN A 825 114.079 -22.090 -8.795 1.00 52.28 O

ATOM 678 NE2 GLN A 825 114.330 -19.852 -8.759 1.00 53.03 N

ATOM 679 N PHE A 826 116.964 -21.541 -2.978 1.00 51.07 N

ATOM 680 CA PHE A 826 118.172 -22.003 -2.294 1.00 50.52 C

ATOM 681 C PHE A 826 118.173 -21.468 -0.872 1.00 48.58 C

ATOM 682 O PHE A 826 117.291 -20.705 -0.501 1.00 49.00 O

ATOM 683 CB PHE A 826 119.427 -21.504 -3.022 1.00 51.76 C

ATOM 684 CG PHE A 826 119.304 -21.524 -4.512 1.00 54.34 C

ATOM 685 CDl PHE A 826 119.198 -22.724 -5.197 1.00 56.01 C

ATOM 686 CD2 PHE A 826 119.248 -20.334 -5.230 1.00 55.83 C

ATOM 687 CEl PHE A 826 119.030 -22.740 -6.586 1.00 57.48 C

ATOM 688 CE2 PHE A 826 119.083 -20.336 -6.606 1.00 56.04 C

ATOM 689 CZ PHE A 826 118.972 -21.542 -7.290 1.00 57.11 C

ATOM 690 N LEU A 827 119.153 -21.880 -0.077 1.00 47.61 N

ATOM 691 CA LEU A 827 119.283 -21.400 1.297 1.00 46.46 C

ATOM 692 C LEU A 827 120.313 -20.265 1.283 1.00 45.11 C

ATOM 693 O LEU A 827 121.476 -20.459 0.931 1.00 43.32 O

ATOM 694 CB LEU A 827 119.741 -22.529 2.238 1.00 48.63 C

ATOM 695 CG LEU A 827 118.720 -23.617 2.613 1.00 49.39 C

ATOM 696 CDl LEU A 827 119.258 -24.479 3.738 1.00 49.21 C

ATOM 697 CD2 LEU A 827 117.403 -22.964 3.019 1.00 50.01 C

ATOM 698 N TYR A 828 119.861 -19.075 1.659 1.00 44.94 N

ATOM 699 CA TYR A 828 120.701 -17.885 1.674 1.00 44.26 C

ATOM 700 C TYR A 828 121.220 -17.544 3.093 1.00 43.93 C

ATOM 701 O TYR A 828 120.775 -16.578 3.715 1.00 44.21 O

ATOM 702 CB TYR A 828 119.876 -16.739 1.083 1.00 45.55 C

ATOM 703 CG TYR A 828 120.667 -15.576 0.546 1.00 47.57 C

ATOM 704 CDl TYR A 828 121.249 -14.655 1.410 1.00 47.73 C

ATOM 705 CD2 TYR A 828 120.798 -15.368 -0.831 1.00 48.34 C

ATOM 706 CEl TYR A 828 121.933 -13.555 0.932 1.00 49.39 C

ATOM 707 CE2 TYR A 828 121.492 -14.261 -1.325 1.00 49.13 C

ATOM 708 CZ TYR A 828 122.052 -13.358 -0.431 1.00 50.66 C

ATOM 709 OH TYR A 828 122.719 -12.234 -0.876 1.00 53.13 O

ATOM 710 N PHE A 829 122.161 -18.345 3.601 1.00 42.89 N

ATOM 711 CA PHE A 829 122.719 -18.112 4.935 1.00 42.29 C

ATOM 712 C PHE A 829 123.442 -16.763 4.977 1.00 42.52 C

ATOM 713 O PHE A 829 123.301 -15.992 5.936 1.00 40.49 O

ATOM 714 CB PHE A 829 123.709 -19.222 5.323 1.00 40.86 C

ATOM 715 CG PHE A 829 123.078 -20.576 5.515 1.00 41.74 C

ATOM 716 CDl PHE A 829 123.041 -21.505 4.479 1.00 40.69 C

ATOM 865 N LEU A 848 117.420 -31.338 7.741 1.00 47.81 N

ATOM 866 CA LEU A 848 117.288 -30.118 8.467 1.00 44.30 C

ATOM 867 C LEU A 848 117.189 -28.981 7.481 1.00 42.52 C

ATOM 868 O LEU A 848 116.370 -28.092 7.644 1.00 41.23 O

ATOM 869 CB LEU A 848 118.446 -29.951 9.447 1.00 41.66 C

ATOM 870 CG LEU A 848 118.273 -30.752 10.742 1.00 39.13 C

ATOM 871 CDl LEU A 848 119.462 -30.569 11.674 1.00 39.25 C

ATOM 872 CD2 LEU A 848 116.975 -30.373 11.445 1.00 38.71 C

ATOM 873 N CYS A 849 118.024 -29.006 6.444 1.00 42.32 N

ATOM 874 CA CYS A 849 118.004 -27.986 5.402 1.00 41.79 C

ATOM 875 C CYS A 849 116.648 -27.995 4.707 1.00 42.23 C

ATOM 876 O CYS A 849 116.053 -26.941 4.461 1.00 43.29 O

ATOM 877 CB CYS A 849 119.085 -28.265 4.361 1.00 41.38 C

ATOM 878 SG CYS A 849 120.734 -27.733 4.829 1.00 46.64 S

ATOM 879 N GLN A 850 116.175 -29.199 4.391 1.00 42.66 N

ATOM 880 CA GLN A 850 114.899 -29.407 3.724 1.00 42.41 C

ATOM 881 C GLN A 850 113.778 -28.718 4.485 1.00 41.36 C

ATOM 882 O GLN A 850 112.941 -28.044 3.884 1.00 39.59 O

ATOM 883 CB GLN A 850 114.615 -30.908 3.597 1.00 45.38 C

ATOM 884 CG GLN A 850 114.737 -31.457 2.168 1.00 51.88 C

ATOM 885 CD GLN A 850 114.027 -32.801 1.975 1.00 55.96 C

ATOM 886 OEl GLN A 850 113.542 -33.107 0.881 1.00 57.10 O

ATOM 887 NE2 GLN A 850 113.960 -33.604 3.041 1.00 57.25 N

ATOM 888 N GLY A 851 113.769 -28.885 5.806 1.00 40.53 N

ATOM 889 CA GLY A 851 112.754 -28.252 6.634 1.00 38.41 C

ATOM 890 C GLY A 851 112.783 -26.735 6.528 1.00 38.77 C

ATOM 891 O GLY A 851 111.737 -26.091 6.391 1.00 37.50 O

ATOM 892 N MET A 852 113.978 -26.149 6.585 1.00 38.50 N

ATOM 893 CA MET A 852 114.097 -24.700 6.479 1.00 39.27 C

ATOM 894 C MET A 852 113.662 -24.231 5.089 1.00 41.19 C

ATOM 895 O MET A 852 112.886 -23.278 4.953 1.00 42.38 O

ATOM 896 CB MET A 852 115.534 -24.266 6.771 1.00 39.15 C

ATOM 897 CG MET A 852 115.960 -24.556 8.203 1.00 38.14 C

ATOM 898 SD MET A 852 117.674 -24.160 8.581 1.00 39.29 S

ATOM 899 CE MET A 852 118.545 -25.364 7.622 1.00 34.81 C

ATOM 900 N HIS A 853 114.153 -24.908 4.056 1.00 42.73 N

ATOM 901 CA HIS A 853 113.794 -24.570 2.683 1.00 44.83 C

ATOM 902 C HIS A 853 112.274 -24.644 2.543 1.00 45.17 C

ATOM 903 O HIS A 853 111.677 -23.921 1.747 1.00 45.80 O

ATOM 904 CB HIS A 853 114.489 -25.546 1.720 1.00 46.28 C

ATOM 905 CG HIS A 853 114.015 -25.451 0.301 1.00 48.00 C

ATOM 906 NDl HIS A 853 113.147 -26.366 -0.256 1.00 47.40 N

ATOM 907 CD2 HIS A 853 114.278 -24.544 -0.670 1.00 48.26 C

ATOM 908 CEl HIS A 853 112.895 -26.025 -1.507 1.00 48.88 C

ATOM 909 NE2 HIS A 853 113.569 -24.923 -1.783 1.00 47.96 N

ATOM 910 N GLN A 854 111.654 -25.503 3.349 1.00 46.12 N

ATOM 911 CA GLN A 854 110.204 -25.682 3.336 1.00 46.23 C

ATOM 912 C GLN A 854 109.476 -24.460 3.901 1.00 44.45 C

ATOM 913 O GLN A 854 108.335 -24.171 3.523 1.00 44.97 O

ATOM 914 CB GLN A 854 109.822 -26.922 4.148 1.00 49.08 C

ATOM 915 CG GLN A 854 108.479 -27.518 3.762 1.00 53.29 C

ATOM 916 CD GLN A 854 108.597 -28.497 2.597 1.00 56.18 C

ATOM 917 OEl GLN A 854 109.694 -28.737 2.078 1.00 56.16 O

ATOM 918 NE2 GLN A 854 107.465 -29.064 2.178 1.00 56.99 N

ATOM 919 N ILE A 855 110.122 -23.757 4.828 1.00 42.60 N

ATOM 920 CA ILE A 855 109.525 -22.560 5.408 1.00 40.26 C

ATOM 921 C ILE A 855 109.571 -21.467 4.347 1.00 38.83 C

ATOM 922 O ILE A 855 108.615 -20.717 4.168 1.00 37.21 O

ATOM 923 CB ILE A 855 110.306 -22.077 6.660 1.00 39.14 C

ATOM 924 CGl ILE A 855 110.217 -23.120 7.772 1.00 37.80 C

ATOM 925 CG2 ILE A 855 109.756 -20.754 7.142 1.00 37.29 C

ATOM 926 CDl ILE A 855 108.820 -23.429 8.242 1.00 35.56 C

ATOM 927 N SER A 856 110.695 -21.394 3.642 1.00 38.48 N

ATOM 928 CA SER A 856 110.876 -20.397 2.594 1.00 40.09 C

ATOM ^■ 929 C SER A 856 109.764 -20.566 1.568 1.00 39.58 C

ATOM 930 O SER A 856 109.126 -19.593 1.159 1.00 39.29 O

ATOM 931 CB SER A 856 112.231 -20.578 1.898 1.00 40.96 C

ATOM 932 OG SER A 856 113.299 -20.586 2.830 1.00 44.36 O

ATOM 933 N LEU A 857 109.544 -21.809 1.153 1.00 39.03 N

ATOM 934 CA LEU A 857 108.514 -22.106 0.176 1.00 38.90 C

ATOM 935 C LEU A 857 107.193 -21.592 0.672 1.00 39.32 C

ATOM 936 O LEU A 857 106.390 -21.102 -0.113 1.00 40.05 O

ATOM 937 CB LEU A 857 108.422 -23.607 -0.095 1.00 38.70 C

ATOM 938 CG LEU A 857 109.528 -24.228 -0.946 1.00 38.18 C

ATOM 1013 C PHE A 866 107.527 -7.051 6.453 1.00 42.41 C

ATOM 1014 O PHE A 866 108.116 -7.313 7.501 1.00 41.02 O

ATOM 1015 CB PHE A 866 108.873 -6.347 4.464 1.00 42.58 C

ATOM 1016 CG PHE A 866 110.090 -5.913 5.257 1.00 39.16 C

ATOM 1017 CDl PHE A 866 111.081 -6.836 5.600 1.00 37.95 C

ATOM 1018 CD2 PHE A 866 110.231 -4.592 5.672 1.00 37.87 C

ATOM 1019 CEl PHE A 866 112.191 -6.457 6.345 1.00 38.28 C

ATOM 1020 CE2 PHE A 866 111.334 -4.195 6.414 1.00 39.01 C

ATOM 1021 CZ PHE A 866 112.322 -5.130 6.757 1.00 40.95 C

ATOM 1022 N GLU A 867 106.387 -6.368 6.416 1.00 42.58 N

ATOM 1023 CA GLU A 867 105.752 -5.901 7.641 1.00 43.29 C

ATOM 1024 C GLU A 867 105.296 -7.084 8.501 1.00 42.00 C

ATOM 1025 O GLU A 867 105.406 -7.044 9.730 1.00 41.03 O

ATOM 1026 CB GLU A 867 104.557 -5.006 7.318 1.00 46.17 C

ATOM 1027 CG GLU A 867 104.923 -3.646 6.764 1.00 51.71 C

ATOM 1028 CD GLU A 867 104.362 -3.417 5.372 1.00 55.12 C

ATOM 1029 OEl GLU A 867 104.639 -2.349 4.779 1.00 58.48 O

ATOM 1030 OE2 GLU A 867 103.644 -4.303 4.868 1.00 56.06 O

ATOM 1031 N GLU A 868 104.781 -8.133 7.853 1.00 40.47 N

ATOM 1032 CA GLU A 868 104.333 -9.328 8.564 1.00 38.04 C

ATOM 1033 C GLU A 868 105.528 -10.050 9.169 1.00 35.33 C

ATOM 1034 O GLU A 868 105.533 -10.386 10.346 1.00 35.20 O

ATOM 1035 CB GLU A 868 103.611 -10.268 7.610 1.00 40.16 C

ATOM 1036 CG GLU A 868 102.282 -9.738 7.115 1.00 40.11 C

ATOM 1037 CD GLU A 868 101.825 -10.483 5.887 1.00 41.51 C

ATOM 1038 OEl GLU A 868 100.666 -10.300 5.462 1.00 42.23 O

ATOM 1039 OE2 GLU A 868 102.645 -11.253 5.338 1.00 42.86 O

ATOM 1040 N TYR A 869 106.541 -10.271 8.340 1.00 33.72 N

ATOM 1041 CA TYR A 869 107.773 -10.935 8.742 1.00 31.64 C

ATOM 1042 C TYR A 869 108.339 -10.342 10.026 1.00 33.55 C

ATOM 1043 O TYR A 869 108.691 -11.053 10.984 1.00 33.25 O

ATOM 1044 CB TYR A 869 108.804 -10.783 7.626 1.00 27.09 C

ATOM 1045 CG TYR A 869 110.221 -11.104 8.035 1.00 25.41 C

ATOM 1046 CDl TYR A 869 110.597 -12.407 8.321 1.00 25.41 C

ATOM 1047 CD2 TYR A 869 111.190 -10.092 8.154 1.00 25.85 C

ATOM 1048 CEl TYR A 869 111.883 -12.709 8.713 1.00 23.31 C

ATOM 1049 CE2 TYR A 869 112.487 -10.389 8.550 1.00 24.93 C

ATOM 1050 CZ TYR A 869 112.820 -11.707 8.826 1.00 23.45 C

ATOM 1051 OH TYR A 869 114.092 -12.045 9.202 1.00 24.89 O

ATOM 1052 N THR A 870 108.429 -9.022 10.021 1.00 34.44 N

ATOM 1053 CA THR A 870 108.980 -8.288 11.139 1.00 36.49 C

ATOM 1054 C THR A 870 108.263 -8.525 12.476 1.00 36.81 C

ATOM 1055 O THR A 870 108.907 -8.842 13.473 1.00 36.54 O

ATOM 1056 CB THR A 870 109.017 -6.780 10.789 1.00 37.70 C

ATOM 1057 OGl THR A 870 110.375 -6.358 10.652 1.00 38.88 O

ATOM 1058 CG2 THR A 870 108.321 -5.950 11.852 1.00 39.90 C

ATOM 1059 N ILE A 871 106.939 -8.389 12.494 1.00 35.35 N

ATOM 1060 CA ILE A 871 106.174 -8.594 13.717 1.00 34.20 C

ATOM 1061 C ILE A 871 106.268 -10.056 14.125 1.00 34.91 C

ATOM 1062 O ILE A 871 106.343 -10.376 15.314 1.00 35.40 O

ATOM 1063 CB ILE A 871 104.676 -8.212 13.513 1.00 34.97 C

ATOM 1064 CGl ILE A 871 104.568 -6.879 12.746 1.00 33.19 C

ATOM 1065 CG2 ILE A 871 103.966 -8.104 14.864 1.00 32.31 C

ATOM 1066 CDl ILE A 871 103.145 -6.485 12.404 1.00 33.22 C

ATOM 1067 N MET A 872 106.277 -10.941 13.128 1.00 35.04 N

ATOM 1068 CA MET A 872 106.350 -12.379 13.361 1.00 33.75 C

ATOM 1069 C MET A 872 107.665 -12.800 13.989 1.00 33.84 C

ATOM 1070 O MET A 872 107.718 -13.781 14.721 1.00 34.86 O

ATOM 1071 CB MET A 872 106.147 -13.141 12.052 1.00 34.55 C

ATOM 1072 CG MET A 872 104.708 -13.163 11.552 1.00 32.87 C

ATOM 1073 SD MET A 872 104.582 -13.810 9.853 1.00 35.89 S

ATOM 1074 CE MET A 872 104.415 -15.582 10.143 1.00 31.47 C

ATOM 1075 N LYS A 873 108.732 -12.067 13.701 1.00 33.24 N

ATOM 1076 CA LYS A 873 110.025 -12.406 14.266 1.00 32.07 C

ATOM 1077 C LYS A 873 110.047 -12.008 15.750 1.00 31.48 C

ATOM 1078 O LYS A 873 110.739 -12.614 16.564 1.00 31.07 O

ATOM 1079 CB LYS A 873 111.135 -11.710 13.473 1.00 32.58 C

ATOM 1080 CG LYS A 873 112.544 -12.001 13.959 1.00 36.08 C

ATOM 1081 CD LYS A 873 113.556 -12.213 12.807 1.00 36.47 C

ATOM 1082 CE LYS A 873 113.621 -11.035 11.850 1.00 35.20 C

ATOM 1083 NZ LYS A 873 113.968 -9.774 12.547 1.00 40.74 N

ATOM 1084 N VAL A 874 109.271 -10.994 16.105 1.00 30.58 N

ATOM 1085 CA VAL A 874 109.205 -10.575 17.497 1.00 30.88 C

ATOM 1086 C VAL A 874 108.391 -11.631 18.248 1.00 31.11 C ATOM 1087 O VAL A 874 108.724 -12.006 19.364 1.00 33.06 O

ATOM 1088 CB VAL A 874 108.521 -9.184 17.647 1.00 29.42 C

ATOM 1089 CGl VAL A 874 108.282 -8.881 19.106 1.00 30.93 C

ATOM 1090 CG2 VAL A 874 109.399 -8.103 17.060 1.00 27.53 C

ATOM 1091 N LEU A 875 107.328 -12.124 17.628 1.00 30.59 N

ATOM 1092 CA LEU A 875 106.503 -13.133 18.274 1.00 30.64 C

ATOM 1093 C LEU A 875 107.287 -14.434 18.482 1.00 30.68 C

ATOM 1094 O LEU A 875 107.037 -15.183 19.430 1.00 28.65 O

ATOM 1095 CB LEU A 875 105.219 -13.362 17.463 1.00 30.53 C

ATOM 1096 CG LEU A 875 104.232 -12.175 17.431 1.00 31.80 C

ATOM 1097 CDl LEU A 875 103.125 -12.413 16.397 1.00 29.96 C

ATOM 1098 CD2 LEU A 875 103.624 -11.986 18.811 1.00 29.54 C

ATOM 1099 N LEU A 876 108.241 -14.707 17.602 1.00 30.82 N

ATOM 1100 CA LEU A 876 109.046 -15.895 17.771 1.00 31.78 C

ATOM 1101 C LEU A 876 109.929 -15.663 19.003 1.00 33.31 C

ATOM 1102 O LEU A 876 110.163 -16.584 19.777 1.00 35.99 O

ATOM 1103 CB LEU A 876 109.892 -16.173 16.518 1.00 32.17 C

ATOM 1104 CG LEU A 876 109.123 -16.628 15.261 1.00 34.13 C

ATOM 1105 CDl LEU A 876 110.070 -16.845 14.116 1.00 31.98 C

ATOM 1106 CD2 LEU A 876 108.367 -17.907 15.554 1.00 32.15 C

ATOM 1107 N LEU A 877 110.405 -14.434 19.197 1.00 33.48 N

ATOM 1108 CA LEU A 877 111.231 -14.108 20.362 1.00 33.94 C

ATOM 1109 C LEU A 877 110.452 -14.344 21.669 1.00 35.65 C

ATOM 1110 O LEU A 877 111.046 -14.655 22.706 1.00 34.62 O

ATOM 1111 CB LEU A 877 111.707 -12.643 20.297 1.00 32.65 C

ATOM 1112 CG LEU A 877 112.466 -12.084 21.508 1.00 33.85 C

ATOM 1113 CDl LEU A 877 113.651 -13.004 21.876 1.00 32.25 C

ATOM 1114 CD2 LEU A 877 112.955 -10.670 21.201 1.00 31.47 C

ATOM 1115 N LEU A 878 109.125 -14.195 21.611 1.00 36.90 N

ATOM 1116 CA LEU A 878 108.266 -14.398 22.772 1.00 36.46 C

ATOM 1117 C LEU A 878 107.492 -15.688 22.598 1.00 36.47 C

ATOM 1118 O LEU A 878 106.377 -15.804 23.094 1.00 37.51 O

ATOM 1119 CB LEU A 878 107.253 -13.272 22.892 1.00 37.33 C

ATOM 1120 CG LEU A 878 107.669 -11.807 22.966 1.00 39.99 C

ATOM 1121 CDl LEU A 878 109.052 -11.589 22.412 1.00 39.86 C

ATOM 1122 CD2 LEU A 878 106.622 -10.998 22.205 1.00 38.67 C

ATOM 1123 N SER A 879 108.069 -16.666 21.910 1.00 35.88 N

ATOM 1124 CA SER A 879 107.343 -17.911 21.670 1.00 35.00 C

ATOM 1125 C SER A 879 107.543 -19.026 22.685 1.00 36.01 C

ATOM 1126 O SER A 879 106.766 -19.977 22.701 1.00 36.77 O

ATOM 1127 CB SER A 879 107.641 -18.435 20.260 1.00 33.63 C

ATOM 1128 OG SER A 879 108.997 -18.830 20.098 1.00 31.57 O

ATOM 1129 N THR A 880 108.568 -18.899 23.530 1.00 37.57 N

ATOM 1130 CA THR A 880 108.873 -19.887 24.562 1.00 38.56 C

ATOM 1131 C THR A 880 109.241 -19.273 25.909 1.00 39.24 C

ATOM 1132 O THR A 880 110.129 -18.427 25.989 1.00 41.76 O

ATOM 1133 CB THR A 880 110.042 -20.764 24.136 1.00 38.70 C

ATOM 1134 OGl THR A 880 109.629 -21.606 23.059 1.00 39.88 O

ATOM 1135 CG2 THR A 880 110.529 -21.627 25.305 1.00 37.89 C

ATOM 1136 N ILE A 881 108.548 -19.694 26.959 1.00 39.84 N

ATOM 1137 CA ILE A 881 108.833 -19.214 28.306 1.00 40.63 C

ATOM 1138 C ILE A 881 109.167 -20.349 29.277 1.00 40.62 C

ATOM 1139 O ILE A 881 108.969 -21.527 28.984 1.00 39.45 O

ATOM 1140 CB ILE A 881 107.635 -18.442 28.918 1.00 41.62 C

ATOM 1141 CGl ILE A 881 106.369 -19.287 28.754 1.00 41.28 C

ATOM 1142 CG2 ILE A 881 107.518 -17.009 28.306 1.00 42.36 C

ATOM 1143 CDl ILE A 881 105.161 -18.704 29.408 1.00 39.19 C

ATOM 1144 N PRO A 882 109.695 -19.995 30.458 1.00 40.72 N

ATOM 1145 CA PRO A 882 110.040 -20.994 31.472 1.00 40.17 C

ATOM 1146 C PRO A 882 108.755 -21.685 31.943 1.00 40.48 C

ATOM 1147 O PRO A 882 107.709 -21.049 32.032 1.00 39.33 O

ATOM 1148 CB PRO A 882 110.685 -20.151 32.570 1.00 40.00 C

ATOM 1149 CG PRO A 882 111.352 -19.051 31.783 1.00 39.20 C

ATOM 1150 CD PRO A 882 110.265 -18.680 30.810 1.00 40.20 C

ATOM 1151 N LYS A 883 108.846 -22.980 32.242 1.00 41.58 N

ATOM 1152 CA LYS A 883 107.702 -23.796 32.675 1.00 42.02 C

ATOM 1153 C LYS A 883 106.730 -23.160 33.683 1.00 41.94 C

ATOM 1154 O LYS A 883 105.518 -23.379 33.617 1.00 39.79 O

ATOM 1155 CB LYS A 883 108.213 -25.122 33.230 1.00 41.96 C

ATOM 1156 N ASP A 884 107.256 -22.390 34.628 1.00 43.84 N

ATOM 1157 CA ASP A 884 106.399 -21.771 35.630 1.00 44.63 C

ATOM 1158 C ASP A 884 106.284 -20.268 35.498 1.00 45.18 C

ATOM 1159 O ASP A 884 105.971 -19.595 36.470 1.00 46.44 O

ATOM 1160 CB ASP A 884 106.885 -22.115 37.042 1.00 44.90 C ATOM 1161 CG ASP A 884 106.568 -23.552 37.441 1.00 46.45 C

ATOM 1162 ODl ASP A 884 107.518 -24.345 37.609 1.00 46.46 O

ATOM 1163 OD2 ASP A 884 105.369 -23.885 37.594 1.00 45.40 O

ATOM 1164 N GLY A 885 106.556 -19.733 34.313 1.00 45.66 N

ATOM 1165 CA GLY A 885 106.424 -18.298 34.121 1.00 47.08 C

ATOM 1166 C GLY A 885 107.677 -17.462 34.297 1.00 46.90 C

ATOM 1167 O GLY A 885 108.686 -17.953 34.794 1.00 48.11 O

ATOM 1168 N LEU A 886 107.596 -16.194 33.894 1.00 45.60 N

ATOM 1169 CA LEU A 886 108.715 -15.256 33.979 1.00 44.98 C

ATOM 1170 C LEU A 886 108.630 -14.342 35.184 1.00 44.44 C

ATOM 1171 O LEU A 886 107.618 -14.295 35.878 1.00 43.02 O

ATOM 1172 CB LEU A 886 108.773 -14.376 32.726 1.00 44.29 C

ATOM 1173 CG LEU A 886 109.442 -14.918 31.464 1.00 45.52 C

ATOM 1174 CDl LEU A 886 108.956 -14.152 30.245 1.00 45.58 C

ATOM 1175 CD2 LEU A 886 110.946 -14.823 31.607 1.00 42.55 C

ATOM 1176 N LYS A 887 109.706 -13.601 35.413 1.00 46.59 N

ATOM 1177 CA LYS A 887 109.753 -12.652 36.516 1.00 47.63 C

ATOM 1178 C LYS A 887 108.613 -11.642 36.348 1.00 47.32 C

ATOM 1179 O LYS A 887 107.709 -11.568 37.179 1.00 47.70 O

ATOM 1180 CB LYS A 887 111.099 -11.931 36.527 1.00 46.30 C

ATOM 1181 N SER A 888 108.651 -10.878 35.260 1.00 48.03 N

ATOM 1182 CA SER A 888 107.624 -9.874 34.999 1.00 49.40 C

ATOM 1183 C SER A 888 106.527 -10.392 34.041 1.00 48.81 C

ATOM 1184 O SER A 888 106.098 -9.697 33.119 1.00 50.28 O

ATOM 1185 CB SER A 888 108.296 -8.616 34.435 1.00 49.35 C

ATOM 1186 OG SER A 888 108.069 -7.492 35.272 1.00 51.31 O

ATOM 1187 N GLN A 889 106.075 -11.617 34.288 1.00 48.42 N

ATOM 1188 CA GLN A 889 105.047 -12.285 33.483 1.00 47.32 C

ATOM 1189 C GLN A 889 103.862 -11.401 33.109 1.00 46.83 C

ATOM 1190 O GLN A 889 103.412 -11.410 31.955 1.00 Al .11 O

ATOM 1191 CB GLN A 889 104.536 -13.522 34.225 1.00 47.10 C

ATOM 1192 CG GLN A 889 103.425 -14.292 33.509 1.00 47.26 C

ATOM 1193 CD GLN A 889 103.917 -15.163 32.360 1.00 46.38 C

ATOM 1194 OEl GLN A 889 103.117 -15.689 31.590 1.00 45.72 O

ATOM 1195 NE2 GLN A 889 105.227 -15.326 32.246 1.00 46.58 N

ATOM 1196 N ALA A 890 103.342 -10.653 34.079 1.00 45.32 N

ATOM 1197 CA ALA A 890 102.208 -9.772 33.810 1.00 43.96 C

ATOM 1198 C ALA A 890 102.567 -8.851 32.651 1.00 42.88 C

ATOM 1199 O ALA A 890 101.782 -8.673 31.718 1.00 42.56 O

ATOM 1200 CB ALA A 890 101.878 -8.953 35.043 1.00 43.98 C

ATOM 1201 N ALA A 891 103.771 -8.290 32.714 1.00 39.75 N

ATOM 1202 CA ALA A 891 104.260 -7.380 31.688 1.00 38.32 C

ATOM 1203 C ALA A 891 104.524 -8.113 30.386 1.00 36.85 C

ATOM 1204 O ALA A 891 104.248 -7.594 29.299 1.00 36.30 O

ATOM 1205 CB ALA A 891 105.531 -6.694 32.164 1.00 37.30 C

ATOM 1206 N PHE A 892 105.074 -9.315 30.500 1.00 35.35 N

ATOM 1207 CA PHE A 892 105.368 -10.127 29.332 1.00 34.77 C

ATOM 1208 C PHE A 892 104.121 -10.343 28.476 1.00 36.37 C

ATOM 1209 O PHE A 892 104.120 -10.066 27.272 1.00 35.82 O

ATOM 1210 CB PHE A 892 105.906 -11.480 29.764 1.00 33.14 C

ATOM 1211 CG PHE A 892 106.130 -12.426 28.625 1.00 33.01 C

ATOM 1212 CDl PHE A 892 107.241 -12.290 27.801 1.00 34.23 C

ATOM 1213 CD2 PHE A 892 105.231 -13.456 28.372 1.00 32.26 C

ATOM 1214 CEl PHE A 892 107.452 -13.175 26.744 1.00 34.03 C

ATOM 1215 CE2 PHE A 892 105.440 -14.337 27.319 1.00 33.16 C

ATOM 1216 CZ PHE A 892 106.558 -14.194 26.505 1.00 32.02 C

ATOM 1217 N GLU A 893 103.056 -10.839 29.102 1.00 37.58 N

ATOM 1218 CA GLU A 893 101.815 -11.099 28.380 1.00 38.67 C

ATOM 1219 C GLU A 893 101.189 -9.855 27.777 1.00 38.75 C

ATOM 1220 O GLU A 893 100.621 -9.918 26.695 1.00 38.93 O

ATOM 1221 CB GLU A 893 100.808 -11.803 29.283 1.00 40.62 C

ATOM 1222 CG GLU A 893 101.229 -13.228 29.631 1.00 44.96 C

ATOM 1223 CD GLU A 893 100.291 -13.890 30.617 1.00 48.11 C

ATOM 1224 OEl GLU A 893 99.290 -13.251 31.013 1.00 49.36 O

ATOM 1225 OE2 GLU A 893 100.564 -15.047 31.005 1.00 49.40 O

ATOM 1226 N GLU A 894 101.286 -8.723 28.460 1.00 39.44 N

ATOM 1227 CA GLU A 894 100.721 -7.493 27.924 1.00 40.07 C

ATOM 1228 C GLU A 894 101.403 -7.210 26.587 1.00 39.97 C

ATOM 1229 O GLU A 894 100.753 -7.001 25.562 1.00 37.04 O

ATOM 1230 CB GLU A 894 100.979 -6.346 28.897 1.00 42.06 C

ATOM 1231 CG GLU A 894 100.512 -4.973 28.433 1.00 45.67 C

ATOM 1232 CD GLU A 894 101.096 -3.854 29.299 1.00 49.82 C

ATOM 1233 OEl GLU A 894 101.095 -2.674 28.864 1.00 50.94 O

ATOM 1234 OE2 GLU A 894 101.563 -4.161 30.419 1.00 49.05 O

ATOM 1383 CD GLN A 919 91.267 -18.774 7.961 1.00 44.76 C

ATOM 1384 OEl GLN A 919 92.100 -19.621 7.641 1.00 43.14 O

ATOM 1385 NE2 GLN A 919 90.892 -18.579 9.221 1.00 45.40 N

ATOM 1386 N ARG A 920 94.143 -14.833 6.545 1.00 45.79 N

ATOM 1387 CA ARG A 920 95.594 -14.729 6.497 1.00 44.66 C

ATOM 1388 C ARG A 920 96.195 -14.718 7.909 1.00 43.57 C

ATOM 1389 O ARG A 920 97.276 -15.259 8.132 1.00 42.77 O

ATOM 1390 CB ARG A 920 96.009 -13.468 5.737 1.00 45.49 C

ATOM 1391 CG ARG A 920 97.396 -13.539 5.103 1.00 46.79 C

ATOM 1392 CD ARG A 920 97.774 -12.208 4.493 1.00 46.33 C

ATOM 1393 NE ARG A 920 98.891 -12.298 3.558 1.00 47.11 N

ATOM 1394 CZ ARG A 920 100.120 -12.675 3.881 1.00 47.48 C

ATOM 1395 NHl ARG A 920 100.402 -13.013 5.128 1.00 51.53 N

ATOM 1396 NH2 ARG A 920 101.079 -12.679 2.966 1.00 46.73 N

ATOM 1397 N PHE A 921 95.492 -14.107 8.859 1.00 42.56 N

ATOM 1398 CA PHE A 921 95.973 -14.075 10.235 1.00 41.14 C

ATOM 1399 C PHE A 921 96.246 -15.497 10.714 1.00 41.15 C

ATOM 1400 O PHE A 921 97.366 -15.847 11.060 1.00 40.38 O

ATOM 1401 CB PHE A 921 94.938 -13.462 11.167 1.00 39.00 C

ATOM 1402 CG PHE A 921 95.360 -13.461 12.610 1.00 36.95 C

ATOM 1403 CDl PHE A 921 96.273 -12.516 13.084 1.00 35.77 C

ATOM 1404 CD2 PHE A 921 94.851 -14.404 13.501 1.00 36.46 C

ATOM 1405 CEl PHE A 921 96.672 -12.509 14.429 1.00 33.64 C

ATOM 1406 CE2 PHE A 921 95.241 -14.407 14.845 1.00 33.65 C

ATOM 1407 CZ PHE A 921 96.152 -13.456 15.310 1.00 34.71 C

ATOM 1408 N TYR A 922 95.212 -16.321 10.732 1.00 41.83 N

ATOM 1409 CA TYR A 922 95.377 -17.684 11.194 1.00 43.27 C

ATOM 1410 C TYR A 922 96.384 -18.500 10.402 1.00 42.82 C

ATOM 1411 O TYR A 922 96.938 -19.474 10.905 1.00 42.10 O

ATOM 1412 CB TYR A 922 94.016 -18.366 11.252 1.00 46.58 C

ATOM 1413 CG TYR A 922 93.150 -17.699 12.289 1.00 50.44 C

ATOM 1414 CDl TYR A 922 92.204 -16.731 11.928 i.oo 52.33 C

ATOM 1415 CD2 TYR A 922 93.357 -17.949 13.652 1.00 51.87 C

ATOM 1416 CEl TYR A 922 91.492 -16.024 12.900 1.00 53.85 C

ATOM 1417 CE2 TYR A 922 92.659 -17.250 14.627 1.00 53.81 C

ATOM 1418 CZ TYR A 922 91.732 -16.290 14.246 1.00 55.05 C

ATOM 1419 OH TYR A 922 91.068 -15.579 15.215 1.00 58.51 O

ATOM 1420 N GLN A 923 96.640 -18.085 9.169 1.00 43.12 N

ATOM 1421 CA GLN A 923 97.611 -18.767 8.316 1.00 41.77 C

ATOM 1422 C GLN A 923 99.030 -18.451 8.778 1.00 41.14 C

ATOM 1423 O GLN A 923 99.897 -19.319 8.812 1.00 40.90 O

ATOM 1424 CB GLN A 923 97.439 -18.301 6.876 1.00 43.04 C

ATOM 1425 CG GLN A 923 96.047 -18.543 6.326 1.00 44.14 C

ATOM 1426 CD GLN A 923 95.992 -18.346 4.836 1.00 45.14 C

ATOM 1427 OEl GLN A 923 96.011 -17.216 4.348 1.00 45.27 O

ATOM 1428 NE2 GLN A 923 95.945 -19.451 4.095 1.00 44.26 N

ATOM 1429 N LEU A 924 99.255 -17.192 9.133 1.00 40.22 N

ATOM 1430 CA LEU A 924 100.556 -16.750 9.591 1.00 38.45 C

ATOM 1431 C LEU A 924 100.853 -17.303 10.989 1.00 37.63 C

ATOM 1432 O LEU A 924 101.991 -17.667 11.280 1.00 37.02 O

ATOM 1433 CB LEU A 924 100.613 -15.213 9.587 1.00 39.28 C

ATOM 1434 CG LEU A 924 100.373 -14.482 8.253 1.00 37.49 C

ATOM 1435 CDl LEU A 924 100.554 -13.007 8.462 1.00 36.77 C

ATOM 1436 CD2 LEU A 924 101.340 -14.964 7.188 1.00 38.39 C

ATOM 1437 N THR A 925 99.835 -17.379 11.848 1.00 36.49 N

ATOM 1438 CA THR A 925 100.032 -17.899 13.198 1.00 37.16 C

ATOM 1439 C THR A 925 100.128 -19.427 13.227 1.00 37.95 C

ATOM 1440 O THR A 925 100.621 -20.009 14.196 1.00 37.49 O

ATOM 1441 CB THR A 925 98.924 -17.444 14.139 1.00 37.40 C

ATOM 1442 OGl THR A 925 97.651 -17.728 13.553 1.00 39.76 O

ATOM 1443 CG2 THR A 925 99.044 -15.963 14.404 1.00 36.73 C

ATOM 1444 N LYS A 926 99.657 -20.071 12.162 1.00 37.93 N

ATOM 1445 CA LYS A 926 99.752 -21.513 12.046 1.00 39.86 C

ATOM 1446 C LYS A 926 101.229 -21.732 11.677 1.00 40.89 C

ATOM 1447 O LYS A 926 101.916 -22.596 12.243 1.00 41.79 O

ATOM 1448 CB LYS A 926 98.834 -22.013 10.928 1.00 42.44 C

ATOM 1449 CG LYS A 926 98.519 -23.499 10.983 1.00 45.62 C

ATOM 1450 CD LYS A 926 97.492 -23.820 12.073 1.00 50.96 C

ATOM 1451 CE LYS A 926 97.397 -25.338 12.347 1.00 51.58 ■ C

ATOM 1452 NZ LYS A 926 96.327 -25.696 13.341 1.00 49.74 N

ATOM 1453 N LEO A 927 101.711 -20.923 10.734 1.00 39.36 N

ATOM 1454 CA LEU A 927 103.098 -20.966 10.289 1.00 37.37 C

ATOM 1455 C LEU A 927 104.023 -20.764 11.489 1.00 37.49 C

ATOM 1456 O LEU A 927 105.087 -21.373 11.575 1.00 37.79 O ATOM 1457 CB LEU A 927 103.366 -19.854 9.276 1.00 37.09 C

ATOM 1458 CG LEU A 927 104.751 -19.881 8.637 1.00 37.23 C

ATOM 1459 CDl LEU A 927 104.889 -21.156 7.842 1.00 36.21 C

ATOM 1460 CD2 LEU A 927 104.951 -18.677 7.741 1.00 38.17 C

ATOM 1461 N LEU A 928 103.628 -19.896 12.414 1.00 35.64 N

ATOM 1462 CA LEU A 928 104.451 -19.664 13.586 1.00 33.78 C

ATOM 1463 C LEU A 928 104.522 -20.907 14.475 1.00 34.01 C

ATOM 1464 O LEU A 928 105.591 -21.222 15.004 1.00 33.10 O

ATOM 1465 CB LEU A 928 103.928 -18.464 14.375 1.00 31.64 C

ATOM 1466 CG LEU A 928 104.336 -17.114 13.776 1.00 31.46 C

ATOM 1467 CDl LEU A 928 103.241 -16.071 13.999 1.00 31.62 C

ATOM 1468 CD2 LEU A 928 105.650 -16.684 14.387 1.00 30.48 C

ATOM 1469 N ASP A 929 103.409 -21.625 14.636 1.00 33.62 N

ATOM 1470 CA ASP A 929 103.434 -22.831 15.464 1.00 34.55 C

ATOM 1471 C ASP A 929 104.304 -23.906 14.817 1.00 33.86 C

ATOM 1472 O ASP A 929 105.053 -24.612 15.497 1.00 33.64 O

ATOM 1473 CB ASP A 929 102.034 -23.416 15.671 1.00 36.76 C

ATOM 1474 CG ASP A 929 101.097 -22.487 16.414 1.00 37.10 C

ATOM 1475 ODl ASP A 929 101.553 -21.531 17.078 1.00 39.54 O

ATOM 1476 OD2 ASP A 929 99.880 -22.738 16.343 1.00 38.98 O

ATOM 1477 N SER A 930 104.272 -23.976 13.491 1.00 34.41 N

ATOM 1478 CA SER A 930 105.066 -24.974 12.785 1.00 35.37 C

ATOM 1479 C SER A 930 106.560 -24.728 12.960 1.00 34.87 C

ATOM 1480 O SER A 930 107.346 -25.673 12.940 1.00 36.58 O

ATOM 1481 CB SER A 930 104.702 -25.009 11.291 1.00 37.00 C

ATOM 1482 OG SER A 930 104.966 -23.776 10.651 1.00 39.86 O

ATOM 1483 N MET A 931 106.949 -23.468 13.126 1.00 33.11 N

ATOM 1484 CA MET A 931 108.343 -23.137 13.336 1.00 35.01 C

ATOM 1485 C MET A 931 108.860 -23.891 14.555 1.00 36.28 C

ATOM 1486 O MET A 931 109.988 -24.384 14.549 1.00 38.08 O

ATOM 1487 CB MET A 931 108.507 -21.632 13.543 1.00 37.14 C

ATOM 1488 CG MET A 931 108.563 -20.831 12.258 1.00 37.35 C

ATOM 1489 SD MET A 931 109.926 -21.374 11.239 1.00 36.47 S

ATOM 1490 CE MET A 931 111.274 -20.491 11.955 1.00 37.02 C

ATOM 1491 N HIS A 932 108.030 -23.984 15.596 1.00 37.00 N

ATOM 1492 CA HIS A 932 108.382 -24.704 16.833 1.00 37.48 C

ATOM 1493 C HIS A 932 108.892 -26.115 16.536 1.00 36.26 C

ATOM 1494 O HIS A 932 109.873 -26.587 17.104 1.00 34.50 O

ATOM 1495 CB HIS A 932 107.149 -24.848 17.731 1.00 39.56 C

ATOM 1496 CG HIS A 932 106.964 -23.739 18.719 1.00 42.17 C

ATOM 1497 NDl HIS A 932 107.764 -23.592 19.833 1.00 41.89 N

ATOM 1498 CD2 HIS A 932 106.052 -22.739 18.776 1.00 43.03 C

ATOM 1499 CEl HIS A 932 107.353 -22.548 20.533 1.00 42.38 C

ATOM 1500 NE2 HIS A 932 106.315 -22.014 19.914 1.00 42.95 N

ATOM 1501 N ASP A 933 108.178 -26.792 15.652 1.00 36.45 N

ATOM 1502 CA ASP A 933 108.500 -28.154 15.280 1.00 36.84 C

ATOM 1503 C ASP A 933 109.819 -28.221 14.559 1.00 35.42 C

ATOM 1504 O ASP A 933 110.628 -29.111 14.824 1.00 34.47 O

ATOM 1505 CB ASP A 933 107.368 -28.711 14.421 1.00 40.87 C

ATOM 1506 CG ASP A 933 106.010 -28.478 15.058 1.00 44.38 C

ATOM 1507 ODl ASP A 933 105.939 -28.471 16.305 1.00 48.14 O

ATOM 1508 OD2 ASP A 933 105.018 -28.285 14.326 1.00 46.47 O

ATOM 1509 N LEU A 934 110.046 -27.267 13.662 1.00 34.81 N

ATOM 1510 CA LEU A 934 111.295 -27.217 12.914 1.00 32.89 C

ATOM 1511 C LEU A 934 112.473 -26.903 13.828 1.00 31.65 C

ATOM 1512 O LEU A 934 113.531 -27.500 13.696 1.00 32.37 O

ATOM 1513 CB LEU A 934 111.205 -26.158 11.826 1.00 32.18 C

ATOM 1514 CG LEU A 934 112.432 -25.939 10.936 1.00 31.70 C

ATOM 1515 CDl LEU A 934 112.762 -27.198 10.143 1.00 32.78 C

ATOM 1516 CD2 LEU A 934 112.128 -24.801 9.992 1.00 31.17 C

ATOM 1517 N VAL A 935 112.285 -25.972 14.761 1.00 31.48 N

ATOM 1518 CA VAL A 935 113.355 -25.581 15.673 1.00 32.26 C

ATOM 1519 C VAL A 935 113.668 -26.637 16.734 1.00 31.69 C

ATOM 1520 O VAL A 935 114.799 -26.748 17.200 1.00 30.79 O

ATOM 1521 CB VAL A 935 113.043 -24.229 16.360 1.00 31.93 C

ATOM 1522 CGl VAL A 935 113.947 -24.041 17.574 1.00 32.47 C

ATOM 1523 CG2 VAL A 935 113.249 -23.087 15.366 1.00 32.38 C

ATOM 1524 N SER A 936 112.678 -27.425 17.111 1.00 33.31 N

ATOM 1525 CA SER A 936 112.945 -28.460 18.084 1.00 35.59 C

ATOM 1526 C SER A 936 113.917 -29.510 17.502 1.00 35.92 C

ATOM 1527 O SER A 936 114.694 -30.103 18.242 1.00 36.83 O

ATOM 1528 CB SER A 936 111.636 -29.125 18.512 1.00 35.72 C

ATOM 1529 OG SER A 936 111.903 -30.276 19.295 1.00 39.84 O

ATOM 1530 N ASP A 937 113.877 -29.728 16.183 1.00 36.89 N ATOM 1531 CA ASP A 937 114.761 -30.696 15.524 1.00 37.70 C

ATOM 1532 C ASP A 937 116.133 -30.075 15.308 1.00 36.43 C

ATOM 1533 O ASP A 937 117.165 -30.740 15.410 1.00 38.12 O

ATOM 1534 CB ASP A 937 114.193 -31.124 14.170 1.00 42.27 C

ATOM 1535 CG ASP A 937 113.033 -32.085 14.297 1.00 45.39 C

ATOM 1536 ODl ASP A 937 112.443 -32.427 13.248 1.00 47.44 O

ATOM 1537 OD2 ASP A 937 112.716 -32.505 15.436 1.00 48.73 O

ATOM 1538 N LEU A 938 116.126 -28.792 14.992 1.00 34.16 N

ATOM 1539 CA LEU A 938 117.342 -28.031 14.788 1.00 32.34 C

ATOM 1540 C LEU A 938 118.212 -28.061 16.054 1.00 31.79 C

ATOM 1541 O LEU A 938 119.439 -28.246 15.985 1.00 31.39 O

ATOM 1542 CB LEU A 938 116.956 -26.592 14.447 1.00 30.74 C

ATOM 1543 CG LEU A 938 117.053 -25.919 13.062 1.00 32.27 C

ATOM 1544 CDl LEU A 938 117.241 -26.895 11.902 1.00 29.48 C

ATOM 1545 CD2 LEU A 938 115.786 -25.070 12.898 1.00 31.19 C

ATOM 1546 N LEU A 939 117.570 -27.892 17.210 1.00 31.54 N

ATOM 1547 CA LEU A 939 118.275 -27.863 18.492 1.00 32.10 C

ATOM 1548 C LEU A 939 118.800 -29.225 18.957 1.00 33.79 C

ATOM 1549 O LEU A 939 119.886 -29.335 19.546 1.00 33.46 O

ATOM 1550 CB LEU A 939 117.362 -27.240 19.550 1.00 32.37 C

ATOM 1551 CG LEU A 939 117.232 -25.711 19.494 1.00 30.29 C

ATOM 1552 CDl LEU A 939 116.188 -25.239 20.497 1.00 31.40 C

ATOM 1553 CD2 LEU A 939 118.584 -25.060 19.762 1.00 30.13 C

ATOM 1554 N GLU A 940 118.033 -30.268 18.675 1.00 34.20 N

ATOM 1555 CA GLU A 940 118.436 -31.605 19.047 1.00 33.98 C

ATOM 1556 C GLU A 940 119.707 -31.934 18.314 1.00 33.45 C

ATOM 1557 O GLU A 940 120.648 -32.474 18.897 1.00 36.18 O

ATOM 1558 CB GLU A 940 117.351 -32.603 18.680 1.00 35.94 C

ATOM 1559 CG GLU A 940 116.173 -32.559 19.610 1.00 38.06 C

ATOM 1560 CD GLU A 940 115.132 -33.576 19.236 1.00 40.45 C

ATOM 1561 OEl GLU A 940 115.450 -34.451 18.397 1.00 42.57 O

ATOM 1562 OE2 GLU A 940 114.010 -33.505 19.779 1.00 40.75 O

ATOM 1563 N PHE A 941 119.737 -31.619 17.025 1.00 31.95 N

ATOM 1564 CA PHE A 941 120.934 -31.871 16.245 1.00 30.77 C

ATOM 1565 C PHE A 941 122.050 -30.937 16.733 1.00 31.50 C

ATOM 1566 O PHE A 941 123.211 -31.331 16.810 1.00 31.46 O

ATOM 1567 CB PHE A 941 120.684 -31.615 14.758 1.00 29.04 C

ATOM 1568 CG PHE A 941 121.861 -31.967 13.894 1.00 27.20 C

ATOM 1569 CDl PHE A 941 122.323 -33.279 13.848 1.00 24.87 C

ATOM 1570 CD2 PHE A 941 122.536 -30.987 13.163 1.00 28.70 C

ATOM 1571 CEl PHE A 941 123.431 -33.622 13.098 1.00 25.80 C

ATOM 1572 CE2 PHE A 941 123.660 -31.309 12.402 1.00 27.92 C

ATOM 1573 CZ PHE A 941 124.112 -32.635 12.368 1.00 30.93 C

ATOM 1574 N CYS A 942 121.691 -29.691 17.050 1.00 32.43 N

ATOM 1575 CA CYS A 942 122.676 -28.726 17.528 1.00 33.05 C

ATOM 1576 C CYS A 942 123.234 -29.138 18.892 1.00 33.87 C

ATOM 1577 O CYS A 942 124.429 -28.992 19.154 1.00 33.79 O

ATOM 1578 CB CYS A 942 122.049 -27.341 17.619 1.00 31.15 C

ATOM 1579 SG CYS A 942 123.194 -26.062 18.097 1.00 33.00 S

ATOM 1580 N PHE A 943 122.370 -29.642 19.765 1.00 34.58 N

ATOM 1581 CA PHE A 943 122.808 -30.084 21.082 1.00 35.79 C

ATOM 1582 C PHE A 943 123.739 -31.290 20.957 1.00 36.75 C

ATOM 1583 O PHE A 943 124.650 -31.458 21.765 1.00 37.52 O

ATOM 1584 CB PHE A 943 121.609 -30.462 21.962 1.00 35.33 C

ATOM 1585 CG PHE A 943 120.728 -29.295 22.345 1.00 32.62 C

ATOM 1586 CDl PHE A 943 121.178 -27.984 22.212 1.00 32.21 C

ATOM 1587 CD2 PHE A 943 119.455 -29.516 22.869 1.00 31.64 C

ATOM 1588 CEl PHE A 943 120.392 -26.919 22.591 1.00 30.24 C

ATOM 1589 CE2 PHE A 943 118.653 -28.455 23.254 1.00 32.54 C

ATOM 1590 CZ PHE A 943 119.120 -27.148 23.116 1.00 33.35 C

ATOM 1591 N TYR A 944 123.507 -32.136 19.958 1.00 37.73 N

ATOM 1592 CA TYR A 944 124.355 -33.303 19.772 1.00 38.57 C

ATOM 1593 C TYR A 944 125.747 -32.916 19.267 1.00 40.25 C

ATOM 1594 O TYR A 944 126.764 -33.330 19.834 1.00 38.46 O

ATOM 1595 CB TYR A 944 123.733 -34.297 18.783 1.00 39.61 C

ATOM 1596 CG TYR A 944 124.702 -35.405 18.412 1.00 40.57 C

ATOM 1597 CDl TYR A 944 125.159 -36.299 19.383 1.00 40.45 C

ATOM 1598 CD2 TYR A 944 125.241 -35.503 17.122 1.00 39.55 C

ATOM 1599 CEl TYR A 944 126.130 -37.259 19.095 1.00 39.94 C

ATOM 1600 CE2 TYR A 944 126.228 -36.474 16.819 1.00 40.86 C

ATOM 1601 CZ TYR A 944 126.664 -37.343 17.822 1.00 41.58 C

ATOM 1602 OH TYR A 944 127.641 -38.295 17.589 1.00 43.74 O

ATOM 1603 N THR A 945 125.789 -32.132 18.193 1.00 41.77 N

ATOM 1604 CA THR A 945 127.059 -31.711 17.618 1.00 44.10 C ATOM 1605 C THR A 945 127.877 -30.946 18.654 1.00 45.94 C

ATOM 1606 O THR A 945 129.107 -31.015 18.665 1.00 43.72 O

ATOM 1607 CB THR A 945 126.843 -30.827 16.383 1.00 44.71 C

ATOM 1608 OGl THR A 945 126.069 -31.542 15.411 1.00 46.74 O

ATOM 1609 CG2 THR A 945 128.167 -30.470 15.762 1.00 45.86 C

ATOM 1610 N PHE A 946 127.182 -30.220 19.528 1.00 48.03 N

ATOM 1611 CA PHE A 946 127.841 -29.458 20.576 1.00 50.33 C

ATOM 1612 C PHE A 946 128.551 -30.408 21.533 1.00 52.17 C

ATOM 1613 O PHE A 946 129.732 -30.228 21.832 1.00 52.93 O

ATOM 1614 CB PHE A 946 126.824 -28.612 21.350 1.00 50.71 C

ATOM 1615 CG PHE A 946 127.431 -27.821 22.483 1.00 51.03 C

ATOM 1616 CDl PHE A 946 128.452 -26.910 22.245 1.00 52.36 C

ATOM 1617 CD2 PHE A 946 126.984 -27.993 23.791 1.00 51.89 C

ATOM 1618 CEl PHE A 946 129.021 -26.179 23.295 1.00 53.26 C

ATOM 1619 CE2 PHE A 946 127.544 -27.269 24.846 1.00 51.48 C

ATOM 1620 CZ PHE A 946 128.562 -26.363 24.597 1.00 52.88 C

ATOM 1621 N ARG A 947 127.827 -31.422 22.002 1.00 53.63 N

ATOM 1622 CA ARG A 947 128.372 -32.411 22.935 1.00 55.87 C

ATOM 1623 C ARG A 947 129.536 -33.235 22.368 1.00 55.10 C

ATOM 1624 O ARG A 947 130.331 -33.793 23.123 1.00 55.41 O

ATOM 1625 CB ARG A 947 127.265 -33.370 23.385 1.00 57.02 C

ATOM 1626 CG ARG A 947 126.084 -32.682 24.035 1.00 61.75 C

ATOM 1627 CD ARG A 947 124.825 -33.545 23.947 1.00 63.49 C

ATOM 1628 NE ARG A 947 123.624 -32.798 24.321 1.00 65.98 N

ATOM 1629 CZ ARG A 947 122.408 -33.335 24.412 1.00 66.63 C

ATOM 1630 NHl ARG A 947 122.228 -34.624 24.151 1.00 67.64 N

ATOM 1631 NH2 ARG A 947 121.372 -32.585 24.772 1.00 66.45 N

ATOM 1632 N GLU A 948 129.636 -33.309 21.045 1.00 54.31 N

ATOM 1633 CA GLU A 948 130.683 -34.096 20.401 1.00 52.83 C

ATOM 1634 C GLU A 948 131.642 -33.221 19.624 1.00 53.22 C

ATOM 1635 O GLU A 948 132.516 -33.728 18.919 1.00 53.13 O

ATOM 1636 CB GLU A 948 130.049 -35.095 19.442 1.00 51.20 C

ATOM 1637 CG GLU A 948 128.987 -35.931 20.079 1.00 49.62 C

ATOM 1638 CD GLU A 948 129.551 -37.169 20.706 1.00 50.65 C

ATOM 1639 OEl GLU A 948 128.835 -37.795 21.523 1.00 50.37 O

ATOM 1640 OE2 GLU A 948 130.704 -37.523 20.366 1.00 48.51 O

ATOM 1641 N SER A 949 131.470 -31.908 19.749 1.00 53.62 N

ATOM 1642 CA SER A 949 132.302 -30.950 19.033 1.00 53.97 C

ATOM 1643 C SER A 949 133.796 -31.255 19.097 1.00 54.56 C

ATOM 1644 O SER A 949 134.493 -31.182 18.078 1.00 54.49 O

ATOM 1645 CB SER A 949 132.018 -29.521 19.534 1.00 53.28 C

ATOM 1646 OG SER A 949 131.816 -29.483 20.935 1.00 50.23 O

ATOM 1647 N HIS A 950 134.283 -31.599 20.286 1.00 54.50 N

ATOM 1648 CA HIS A 950 135.689 -31.918 20.465 1.00 54.56 C

ATOM 1649 C HIS A 950 136.086 -33.099 19.576 1.00 54.84 C

ATOM 1650 O HIS A 950 137.174 -33.113 19.006 1.00 55.32 O

ATOM 1651 CB HIS A 950 135.966 -32.236 21.925 1.00 53.94 C

ATOM 1652 N ALA A 951 135.202 -34.082 19.441 1.00 55.00 N

ATOM 1653 CA ALA A 951 135.498 -35.256 18.613 1.00 55.95 C

ATOM 1654 C ALA A 951 135.167 -35.083 17.122 1.00 56.62 C

ATOM 1655 O ALA A 951 135.863 -35.636 16.268 1.00 56.68 O

ATOM 1656 CB ALA A 951 134.768 -36.492 19.167 1.00 54.67 C

ATOM 1657 N LEU A 952 134.115 -34.325 16.809 1.00 56.04 N

ATOM 1658 CA LEU A 952 133.714 -34.123 15.420 1.00 55.22 C

ATOM 1659 C LEU A 952 134.548 -33.060 14.702 1.00 55.95 C

ATOM 1660 O LEU A 952 134.529 -32.963 13.470 1.00 56.05 O

ATOM 1661 CB LEU A 952 132.229 -33.748 15.357 1.00 54.00 C

ATOM 1662 CG LEU A 952 131.296 -34.639 16.179 1.00 54.47 C

ATOM 1663 CDl LEU A 952 129.855 -34.342 15.817 1.00 54.51 C

ATOM 1664 CD2 LEU A 952 131.603 -36.096 15.909 1.00 54.38 C

ATOM 1665 N LYS A 953 135.278 -32.260 15.471 1.00 56.08 N

ATOM 1666 CA LYS A 953 136.105 -31.215 14.897 1.00 56.40 C

ATOM 1667 C LYS A 953 135.234 -30.094 14.327 1.00 56.67 C

ATOM 1668 O LYS A 953 135.611 -29.413 13.363 1.00 57.27 O

ATOM 1669 CB LYS A 953 137.004 -31.800 13.813 1.00 57.29 C

ATOM 1670 N VAL A 954 134.064 -29.911 14.934 1.00 55.18 N

ATOM 1671 CA VAL A 954 133.127 -28.869 14.531 1.00 53.50 C

ATOM 1672 C VAL A 954 133.252 -27.679 15.487 1.00 51.93 C

ATOM 1673 O VAL A 954 132.895 -27.771 16.660 1.00 51.33 O

ATOM 1674 CB VAL A 954 131.682 -29.398 14.567 1.00 54.17 C

ATOM 1675 CGl VAL A 954 131.364 -29.942 15.950 1.00 54.54 C

ATOM 1676 CG2 VAL A 954 130.710 -28.291 14.193 1.00 54.86 C

ATOM 1677 N GLU A 955 133.749 -26.560 14.978 1.00 50.86 N

ATOM 1678 CA GLU A 955 133.943 -25.368 15.795 1.00 50.07 C ATOM 1679 C GLU A 955 132.676 -24.587 16.178 1.00 49.33 C

ATOM 1680 O GLU A 955 131.812 -24.331 15.339 1.00 50.12 O

ATOM 1681 CB GLU A 955 134.923 -24.437 15.091 1.00 49.76 C

ATOM 1682 N PHE A 956 132.581 -24.217 17.456 1.00 47.79 N

ATOM 1683 CA PHE A 956 131.470 -23.422 17.981 1.00 46.68 C

ATOM 1684 C PHE A 956 132.059 -22.153 18.609 1.00 Al .11 C

ATOM 1685 O PHE A 956 133.004 -22.230 19.393 1.00 46.85 O

ATOM 1686 CB PHE A 956 130.696 -24.177 19.075 1.00 46.72 C

ATOM 1687 CG PHE A 956 129.539 -25.008 18.564 1.00 46.86 C

ATOM 1688 CDl PHE A 956 129.669 -26.380 18.375 1.00 45.84 C

ATOM 1689 CD2 PHE A 956 128.315 -24.410 18.269 1.00 45.54 C

ATOM 1690 CEl PHE A 956 128.588 -27.144 17.897 1.00 46.60 C

ATOM 1691 CE2 PHE A 956 127.246 -25.160 17.795 1.00 44.83 C

ATOM 1692 CZ PHE A 956 127.380 -26.530 17.607 1.00 45.04 C

ATOM 1693 N PRO A 957 131.502 -20.970 18.282 1.00 49.37 N

ATOM 1694 CA PRO A 957 131.984 -19.694 18.828 1.00 50.86 C

ATOM 1695 C PRO A 957 131.672 -19.553 20.320 1.00 52.38 C

ATOM 1696 O PRO A 957 130.666 -20.080 20.808 1.00 53.22 O

ATOM 1697 CB PRO A 957 131.219 -18.650 18.013 1.00 50.61 C

ATOM 1698 CG PRO A 957 130.805 -19.378 16.779 1.00 50.47 C

ATOM 1699 CD PRO A 957 130.437 -20.733 17.294 1.00 49.76 C

ATOM 1700 N ALA A 958 132.521 -18.816 21.031 1.00 52.88 N

ATOM 1701 CA ALA A 958 132.350 -18.588 22.466 1.00 54.01 C

ATOM 1702 C ALA A 958 130.915 -18.208 22.814 1.00 54.22 C

ATOM 1703 O ALA A 958 130.367 -18.665 23.819 1.00 54.33 O

ATOM 1704 CB ALA A 958 133.307 -17.484 22.947 1.00 52.63 C

ATOM 1705 N MET A 959 130.315 -17.371 21.976 1.00 55.16 N

ATOM 1706 CA MET A 959 128.955 -16.911 22.197 1.00 54.89 C

ATOM 1707 C MET A 959 127.953 -18.050 22.155 1.00 53.59 C

ATOM 1708 O MET A 959 127.188 -18.237 23.104 1.00 52.18 O

ATOM 1709 CB MET A 959 128.596 -15.868 21.152 1.00 59.12 C

ATOM 1710 CG MET A 959 127.141 -15.465 21.127 1.00 63.53 C

ATOM 1711 SD MET A 959 127.089 -13.675 21.258 1.00 71.97 S

ATOM 1712 CE MET A 959 128.874 -13.312 21.500 1.00 68.63 C

ATOM 1713 N LEU A 960 127.941 -18.807 21.058 1'.00 52.51 N

ATOM 1714 CA LEU A 960 127.014 -19.928 20.951 1.00 50.20 C

ATOM 1715 C LEU A 960 127.252 -20.890 22.103 1.00 49.57 C

ATOM 1716 O LEU A 960 126.303 -21.361 22.721 1.00 49.09 O

ATOM 1717 CB LEU A 960 127.177 -20.665 19.622 1.00 50.04 C

ATOM 1718 CG LEU A 960 126.218 -20.200 18.525 1.00 50.26 C

ATOM 1719 CDl LEU A 960 126.527 -18.760 18.170 1.00 50.68 C

ATOM 1720 CD2 LEU A 960 126.348 -21.091 17.304 1.00 51.79 C

ATOM 1721 N VAL A 961 128.515 -21.174 22.405 1.00 49.23 N

ATOM 1722 CA VAL A 961 128.819 -22.078 23.511 1.00 49.70 C

ATOM 1723 C VAL A 961 128.195 -21.515 24.774 1.00 49.75 C

ATOM 1724 O VAL A 961 127.630 -22.244 25.583 1.00 49.98 O

ATOM 1725 CB VAL A 961 130.337 -22.218 23.760 1.00 49.92 C

ATOM 1726 CGl VAL A 961 130.578 -22.570 25.209 1.00 49.89 C

ATOM 1727 CG2 VAL A 961 130.941 -23.284 22.840 1.00 49.81 C

ATOM 1728 N GLU A 962 128.298 -20.203 24.928 1.00 49.70 N

ATOM 1729 CA GLU A 962 127.756 -19.523 26.089 1.00 50.37 C

ATOM 1730 C GLU A 962 126.248 -19.751 26.223 1.00 49.36 C

ATOM 1731 O GLU A 962 125.753 -20.100 27.292 1.00 51.07 O

ATOM 1732 CB GLU A 962 128.041 -18.028 25.975 1.00 52.09 C

ATOM 1733 CG GLU A 962 128.259 -17.344 27.301 1.00 57.22 C

ATOM 1734 CD GLU A 962 129.639 -17.613 27.865 1.00 59.70 C

ATOM 1735 OEl GLU A 962 129.843 -18.697 28.460 1.00 63.49 O

ATOM 1736 OE2 GLU A 962 130.521 -16.740 27.716 1.00 59.63 O

ATOM 1737 N ILE A 963 125.531 -19.568 25.121 1.00 47.55 N

ATOM 1738 CA ILE A 963 124.078 -19.714 25.073 1.00 46.72 C

ATOM 1739 C ILE A 963 123.530 -21.135 25.213 1.00 46.74 C

ATOM 1740 O ILE A 963 122.639 -21.403 26.031 1.00 44.41 O

ATOM 1741 CB ILE A 963 123.543 -19.115 23.751 1.00 47.54 C

ATOM 1742 CGl ILE A 963 123.697 -17.586 23.792 1.00 47.56 C

ATOM 1743 CG2 ILE A 963 122.098 -19.564 23.506 1.00 46.67 C

ATOM 1744 CDl ILE A 963 123.423 -16.881 22.485 1.00 47.96 C

ATOM 1745 N ILE A 964 124.053 -22.024 24.377 1.00 46.58 N

ATOM 1746 CA ILE A 964 123.643 -23.416 24.352 1.00 47.54 C

ATOM 1747 C ILE A 964 123.905 -24.078 25.691 1.00 48.89 C

ATOM 1748 O ILE A 964 123.109 -24.899 26.158 1.00 48.90 O

ATOM 1749 CB ILE A 964 124.401 -24.179 23.239 1.00 46.31 C

ATOM 1750 CGl ILE A 964 123.857 -23.757 21.871 1.00 44.38 C

ATOM 1751 CG2 ILE A 964 124.297 -25.683 23.461 1.00 43.40 C

ATOM 1752 CDl ILE A 964 124.790 -24.077 20.723 1.00 43.09 C ATOM 1753 N SER A 965 125.026 -23.712 26.301 1.00 49.48 N

ATOM 1754 CA SER A 965 125.411 -24.264 27.588 1.00 50.59 C

ATOM 1755 C SER A 965 124.329 -24.011 28.638 1.00 52.20 C

ATOM 1756 O SER A 965 123.730 -24.956 29.138 1.00 53.12 O

ATOM 1757 CB SER A 965 126.741 -23.657 28.055 1.00 50.83 C

ATOM 1758 OG SER A 965 127.561 -24.620 28.705 1.00 48.44 O

ATOM 1759 N ASP A 966 124.057 -22.753 28.968 1.00 53.56 N

ATOM 1760 CA ASP A 966 123.052 -22.489 29.991 1.00 56.57 C

ATOM 1761 C ASP A 966 121.610 -22.470 29.494 1.00 57.61 C

ATOM 1762 O ASP A 966 120.710 -21.987 30.189 1.00 58.34 O

ATOM 1763 CB ASP A 966 123.378 -21.203 30.767 1.00 58.86 C

ATOM 1764 CG ASP A 966 123.504 -19.986 29.878 1.00 60.96 C

ATOM 1765 ODl ASP A 966 122.599 -19.123 29.926 1.00 61.18 O

ATOM 1766 OD2 ASP A 966 124.510 -19.893 29.140 1.00 61.75 O

ATOM 1767 N GLN A 967 121.398 -23.017 28.296 1.00 57.84 N

ATOM 1768 CA GLN A 967 120.068 -23.118 27.710 1.00 56.17 C

ATOM 1769 C GLN A 967 119.594 -24.531 28.003 1.00 57.35 C

ATOM 1770 O GLN A 967 118.446 -24.737 28.388 1.00 57.27 O

ATOM 1771 CB GLN A 967 120.102 -22.904 26.196 1.00 54.12 C

ATOM 1772 CG GLN A 967 118.743 -23.101 25.540 1.00 51.80 C

ATOM 1773 CD GLN A 967 118.812 -23.203 24.020 1.00 51.92 C

ATOM 1774 OEl GLN A 967 117.792 -23.427 23.355 1.00 50.53 O

ATOM 1775 NE2 GLN A 967 120.012 -23.041 23.462 1.00 48.75 N

ATOM 1776 N LEU A 968 120.486 -25.504 27.824 1.00 58.57 N

ATOM 1777 CA LEU A 968 120.150 -26.902 28.086 1.00 60.31 C

ATOM HlS C LEU A 968 119.461 -27.077 29.446 1.00 61.45 C

ATOM 1779 O LEU A 968 118.413 -27.721 29.546 1.00 61.82 O

ATOM 1780 CB LEU A 968 121.407 -27.775 28.028 1.00 60.25 C

ATOM 1781 CG LEU A 968 122.002 -28.033 26.643 1.00 60.75 C

ATOM 1782 CDl LEU A 968 123.273 -28.869 26.768 1.00 60.09 C

ATOM 1783 CD2 LEU A 968 120.974 -28.759 25.787 1.00 61.01 C

ATOM 1784 N PRO A 969 120.026 -26.488 30.553 1.00 62.23 N

ATOM 1785 CA PRO A 969 119.449 -26.598 31.896 1.00 63.46 C

ATOM 1786 C PRO A 969 118.066 -25.955 32.005 1.00 65.06 C

ATOM 1787 O PRO A 969 117.241 -26.378 32.819 1.00 66.04 O

ATOM 1788 CB PRO A 969 120.477 -25.881 32.767 1.00 62.69 C

ATOM 1789 CG PRO A 969 121.743 -26.160 32.062 1.00 61.81 C

ATOM 1790 CD PRO A 969 121.367 -25.888 30.632 1.00 61.27 C

ATOM 1791 N LYS A 970 117.825 -24.926 31.192 1.00 65.83 N

ATOM 1792 CA LYS A 970 116.548 -24.226 31.200 1.00 66.48 C

ATOM 1793 C LYS A 970 115.510 -24.932 30.334 1.00 67.87 C

ATOM 1794 O LYS A 970 114.333 -24.535 30.293 1.00 68.00 O

ATOM 1795 CB LYS A 970 116.743 -22.776 30.743 1.00 66.23 C

ATOM 1796 CG LYS A 970 117.288 -21.878 31.854 1.00 66.65 C

ATOM 1797 CD LYS A 970 118.117 -20.714 31.339 1.00 65.32 C

ATOM 1798 CE LYS A 970 117.291 -19.653 30.641 1.00 64.99 C

ATOM 1799 NZ LYS A 970 118.185 -18.499 30.290 1.00 64.86 N

ATOM 1800 N VAL A 971 115.939 -25.997 29.665 1.00 68.89 N

ATOM 1801 CA VAL A 971 115.051 -26.761 28.799 1.00 69.85 C

ATOM 1802 C VAL A 971 114.759 -28.132 29.365 1.00 71.19 C

ATOM 1803 O VAL A 971 113.595 -28.532 29.458 1.00 72.44 O

ATOM 1804 CB VAL A 971 115.654 -26.947 27.389 1.00 69.28 C

ATOM 1805 CGl VAL A 971 114.852 -27.984 26.605 1.00 68.95 C

ATOM 1806 CG2 VAL A 971 115.657 -25.616 26.650 1.00 68.84 C

ATOM 1807 N GLU A 972 115.815 -28.850 29.736 1.00 72.38 N

ATOM 1808 CA GLU A 972 115.676 -30.200 30.274 1.00 73.99 C

ATOM 1809 C GLU A 972 114.576 -30.359 31.313 1.00 74.25 C

ATOM 1810 O GLU A 972 114.138 -29.384 31.927 1.00 75.21 O

ATOM 1811 CB GLU A 972 117.014 -30.680 30.845 1.00 75.06 C

ATOM 1812 N SER A 973 114.133 -31.597 31.505 1.00 73.95 N

ATOM 1813 CA SER A 973 113.064 -31.893 32.455 1.00 73.57 C

ATOM 1814 C SER A 973 111.890 -30.950 32.213 1.00 72.68 C

ATOM 1815 O SER A 973 111.267 -30.440 33.154 1.00 73.17 O

ATOM 1816 CB SER A 973 113.553 -31.750 33.899 1.00 74.65 C

ATOM 1817 N GLY A 974 111.563 -30.728 31.249 1.00 71.01 N

ATOM 1818 CA GLY A 974 110.462 -29.937 30.764 1.00 68.04 C

ATOM 1819 C GLY A 974 110.433 -28.567 31.420 1.00 65.75 C

ATOM 1820 O GLY A 974 109.346 -28.060 31.715 1.00 65.42 O

ATOM 1821 N ASN A 975 111.602 -27.949 31.637 1.00 63.53 N

ATOM 1822 CA ASN A 975 111.601 -26.632 32.254 1.00 62.04 C

ATOM 1823 C ASN A 975 111.276 -25.493 31.286 1.00 60.21 C

ATOM 1824 O ASN A 975 111.403 -24.315 31.633 1.00 59.94 O

ATOM 1825 CB ASN A 975 112.938 -26.375 32.942 1.00 62.80 C

ATOM 1826 CG ASN A 975 113.349 -27.526 33.835 1.00 64.78 C ATOM 1827 ODl ASN A 975 112.578 -27.962 34.691 1.00 66.39 O

ATOM 1828 ND2 ASN A 975 114.564 -28.030 33.641 1.00 65.67 N

ATOM 1829 N ALA A 976 110.872 -25.851 30.081 1.00 57.76 N

ATOM 1830 CA ALA A 976 110.499 -24.869 29.064 1.00 54.51 C

ATOM 1831 C ALA A 976 109.065 -25.080 28.622 1.00 53.18 C

ATOM 1832 O ALA A 976 108.546 -26.190 28.704 1.00 53.15 O

ATOM 1833 CB ALA A 976 111.440 -24.935 27.869 1.00 54.41 C

ATOM 1834 N LYS A 977 108.424 -24.010 28.162 1.00 50.87 N

ATOM 1835 CA LYS A 977 107.050 -24.095 27.700 1.00 48.80 C

ATOM 1836 C LYS A 977 106.824 -23.297 26.413 1.00 49.15 C

ATOM 1837 O LYS A 977 106.893 -22.067 26.397 1.00 48.78 O

ATOM 1838 CB LYS A 977 106.084 -23.598 28.781 1.00 47.50 C

ATOM 1839 CG LYS A 977 104.657 -23.457 28.271 1.00 46.24 C

ATOM 1840 CD LYS A 977 103.710 -22.834 29.282 1.00 47.02 C

ATOM 1841 CE LYS A 977 102.357 -22.547 28.622 1.00 46.60 C

ATOM 1842 NZ LYS A 977 101.319 -22.012 29.557 1.00 47.18 N

ATOM 1843 N PRO A 978 106.554 -23.998 25.311 1.00 48.45 N

ATOM 1844 CA PRO A 978 . 106.310 -23.363 24.017 1.00 47.46 C

ATOM 1845 C PRO A 978 104.889 -22.809 23.991 1.00 46.44 C

ATOM 1846 O PRO A 978 103.969 -23.457 24.476 1.00 46.82 O

ATOM 1847 CB PRO A 978 106.475 -24.520 23.032 1.00 49.67 C

ATOM 1848 CG PRO A 978 107.350 -25.498 23.776 1.00 49.72 C

ATOM 1849 CD PRO A 978 106.741 -25.445 25.143 1.00 49.03 C

ATOM 1850 N LEU A 979 104.705 -21.620 23.431 1.00 45.60 N

ATOM 1851 CA LEU A 979 103.374 -21.034 23.362 1.00 45.52 C

ATOM 1852 C LEU A 979 102.846 -21.149 21.944 1.00 45.73 C

ATOM 1853 O LEU A 979 103.486 -20.688 20.995 1.00 47.45 O

ATOM 1854 CB LEU A 979 103.421 -19.563 23.761 1.00 45.66 C

ATOM 1855 CG LEU A 979 104.096 -19.252 25.094 1.00 45.20 C

ATOM 1856 CDl LEU A 979 104.107 -17.740 25.297 1.00 44.97 C

ATOM 1857 CD2 LEU A 979 103.355 -19.970 26.231 1.00 44.37 C

ATOM 1858 N TYR A 980 101.675 -21.755 21.797 1.00 44.91 N

ATOM 1859 CA TYR A 980 101.081 -21.926 20.479 1.00 43.16 C

ATOM 1860 C TYR A 980 99.833 -21.094 20.319 1.00 43.35 C

ATOM 1861 O TYR A 980 99.218 -20.686 21.300 1.00 42.13 O

ATOM 1862 CB TYR A 980 100.705 -23.383 20.254 1.00 42.60 C

ATOM 1863 CG TYR A 980 101.876 -24.320 20.200 1.00 41.26 C

ATOM 1864 CDl TYR A 980 102.491 -24.630 18.988 1.00 40.53 C

ATOM 1865 CD2 TYR A 980 102.370 -24.902 21.363 1.00 41.58 C

ATOM 1866 CEl TYR A 980 103.571 -25.506 18.940 1.00 42.06 C

ATOM 1867 CE2 TYR A 980 103.450 -25.774 21.331 1.00 41.53 C

ATOM 1868 CZ TYR A 980 104.045 -26.074 20.121 1.00 42.24 C

ATOM 1869 OH TYR A 980 105.108 -26.944 20.102 1.00 44.70 O

ATOM 1870 N PHE A 981 99.462 -20.857 19.067 1.00 44.79 N

ATOM 1871 CA PHE A 981 98.260 -20.105 18.750 1.00 46.14 C

ATOM 1872 C PHE A 981 97.107 -21.070 18.452 1.00 48.39 C

ATOM 1873 O PHE A 981 95.932 -20.696 18.548 1.00 49.61 O

ATOM 1874 CB PHE A 981 98.508 -19.209 17.545 1.00 44.27 C

ATOM 1875 CG PHE A 981 99.477 -18.119 17.812 1.00 43.08 C

ATOM 1876 CDl PHE A 981 99.100 -17.010 18.567 1.00 43.14 C

ATOM 1877 CD2 PHE A 981 100.787 -18.219 17.366 1.00 39.86 C

ATOM 1878 CEl PHE A 981 100.029 -16.012 18.878 1.00 43.95 C

ATOM 1879 CE2 PHE A 981 101.710 -17.242 17.669 1.00 39.64 C

ATOM 1880 CZ PHE A 981 101.335 -16.131 18.430 1.00 41.27 C

ATOM 1881 N HIS A 982 97.451 -22.304 18.088 1.00 49.43 N

ATOM 1882 CA HIS A 982 96.457 -23.327 11.111 1.00 51.92 C

ATOM 1883 C HIS A 982 96.869 -24.662 18.399 1.00 52.76 C

ATOM 1884 O HIS A 982 97.713 -25.057 18.955 1.00 54.21 O

ATOM 1885 CB HIS A 982 96.325 -23.488 16.261 1.00 53.51 C

ATOM 1886 CG HIS A 982 96.340 -22.192 15.507 1.00 57.17 C

ATOM 1887 NDl HIS A 982 95.452 -21.166 15.762 1.00 57.25 N

ATOM 1888 CD2 HIS A 982 97.134 -21.759 14.498 1.00 57.32 C

ATOM 1889 CEl HIS A 982 95.700 -20.160 14.942 1.00 58.56 C

ATOM 1890 NE2 HIS A 982 96.715 -20.495 14.164 1.00 57.51 N

TER 1891 HIS A 982

ATOM 1892 N PRO B 738 104.645 69.790 -1.388 1.00 63.01 N

ATOM 1893 CA PRO B 738 105.707 68.799 -1.119 1.00 63.32 C

ATOM 1894 C PRO B 738 106.317 68.214 -2.393 1.00 63.16 C

ATOM 1895 O PRO B 738 107.424 67.674 -2.364 1.00 62.53 O

ATOM 1896 CB PRO B 738 105.075 67.706 -0.269 1.00 62.79 C

ATOM 1897 CG PRO B 738 104.029 68.494 0.484 1.00 62.76 C

ATOM 1898 CD PRO B 738 103.467 69.489 -0.553 1.00 63.17 C

ATOM 1899 N VAL B 739 105.601 68.336 -3.509 1.00 62.79 N

ATOM 1900 CA VAL B 739 106.067 67.793 -4.785 1.00 62.62 C ATOM 1901 C VAL B 739 107.163 68.608 -5.456 1.00 61.34 C

ATOM 1902 O VAL B 739 108.062 68.060 -6.088 1.00 60.34 O

ATOM 1903 CB VAL B 739 104.913 67.666 -5.781 1.00 63.60 C

ATOM 1904 CGl VAL B 739 105.392 66.954 -7.030 1.00 63.73 C

ATOM 1905 CG2 VAL B 739 103.757 66.928 -5.135 1.00 63.57 C

ATOM 1906 N MET B 740 107.081 69.922 -5.326 1.00 61.61 N

ATOM 1907 CA MET B 740 108.070 70.789 -5.940 1.00 61.04 C

ATOM 1908 C MET B 740 109.435 70.616 -5.276 1.00 60.25 C

ATOM 1909 O MET B 740 110.443 70.430 -5.967 1.00 59.13 O

ATOM 1910 CB MET B 740 107.597 72.245 -5.865 1.00 62.12 C

ATOM 1911 CG MET B 740 108.462 73.214 -6.645 1.00 63.55 C

ATOM 1912 SD MET B 740 107.715 74.845 -6.839 1.00 65.33 S

ATOM 1913 CE MET B 740 107.387 74.824 -8.613 1.00 64.28 C

ATOM 1914 N VAL B 741 109.474 70.660 -3.943 1.00 60.25 N

ATOM 1915 CA VAL B 741 110.740 70.490 -3.217 1.00 59.58 C

ATOM 1916 C VAL B 741 111.388 69.168 -3.588 1.00 59.56 C

ATOM 1917 O VAL B 741 112.591 69.093 -3.853 1.00 59.24 O

ATOM 1918 CB VAL B 741 110.539 70.493 -1.694 1.00 58.86 C

ATOM 1919 CGl VAL B 741 109.529 69.429 -1.301 1.00 58.96 C

ATOM 1920 CG2 VAL B 741 111.877 70.235 -1.000 1.00 57.58 C

ATOM 1921 N LEU B 742 110.565 68.127 -3.592 1.00 60.10 N

ATOM 1922 CA LEU B 742 110.994 66.781 -3.933 1.00 60.71 C

ATOM 1923 C LEU B 742 111.753 66.768 -5.253 1.00 61.02 C

ATOM 1924 O LEU B 742 112.842 66.209 -5.340 1.00 61.88 O

ATOM 1925 CB LEU B 742 109.772 65.872 -4.051 1.00 60.44 C

ATOM 1926 CG LEU B 742 109.617 64.774 -3.013 1.00 58.85 C

ATOM 1927 CDl LEU B 742 108.291 64.059 -3.225 1.00 59.70 C

ATOM 1928 CD2 LEU B 742 110.791 63.817 -3.138 1.00 59.89 C

ATOM 1929 N GLU B 743 111.166 67.378 -6.279 1.00 61.87 N

ATOM 1930 CA GLU B 743 111.788 67.416 -7.591 1.00 63.80 C

ATOM 1931 C GLU B 743 113.061 68.248 -7.564 1.00 64.25 C

ATOM 1932 O GLU B 743 113.855 68.226 -8.499 1.00 63.09 O

ATOM 1933 CB GLU B 743 110.806 67.975 -8.626 1.00 64.28 C

ATOM 1934 CG GLU B 743 109.603 67.073 -8.887 1.00 67.53 C

ATOM 1935 CD GLU B 743 108.767 67.509 -10.090 1.00 69.39 C

ATOM 1936 OEl GLU B 743 109.227 67.323 -11.237 1.00 71.44 O

ATOM 1937 OE2 GLU B 743 107.648 68.027 -9.893 1.00 70.18 O

ATOM 1938 N ASN B 744 113.254 68.974 -6.472 1.00 65.76 N

ATOM 1939 CA ASN B 744 114.422 69.824 -6.318 1.00 66.31 C

ATOM 1940 C ASN B 744 115.538 69.050 -5.631 1.00 66.26 C

ATOM 1941 O ASN B 744 116.699 69.124 -6.032 1.00 67.41 O

ATOM 1942 CB ASN B 744 114.055 71.051 -5.483 1.00 68.42 C

ATOM 1943 CG ASN B 744 115.051 72.191 -5.639 1.00 71.53 C

ATOM 1944 ODl ASN B 744 114.674 73.368 -5.678 1.00 72.49 O

ATOM 1945 ND2 ASN B 744 116.333 71.844 -5.732 1.00 71.84 N

ATOM 1946 N ILE B 745 115.175 68.292 -4.604 1.00 65.05 N

ATOM 1947 CA ILE B 745 116.141 67.515 -3.845 1.00 63.50 C

ATOM 1948 C ILE B 745 116.834 66.393 -4.626 1.00 63.04 C

ATOM 1949 O ILE B 745 117.961 66.024 -4.307 1.00 63.07 O

ATOM 1950 CB ILE B 745 115.480 66.871 -2.617 1.00 63.54 C

ATOM 1951 CGl ILE B 745 114.492 67.832 -1.967 1.00 63.73 C

ATOM 1952 CG2 ILE B 745 116.539 66.523 -1.601 1.00 64.66 C

ATOM 1953 CDl ILE B 745 113.916 67.304 -0.666 1.00 62.05 C

ATOM 1954 N GLU B 746 116.163 65.849 -5.639 1.00 62.87 N

ATOM 1955 CA GLU B 746 116.700 64.737 -6.439 1.00 62.41 C

ATOM 1956 C GLU B 746 118.134 64.899 -6.978 1.00 62.17 C

ATOM 1957 O GLU B 746 118.394 65.718 -7.860 1.00 63.39 O

ATOM 1958 CB GLU B 746 115.754 64.434 -7.606 1.00 61.08 C

ATOM 1959 CG GLU B 746 116.158 63.214 -8.417 1.00 62.07 C

ATOM 1960 CD GLU B 746 115.793 61.895 -7.741 1.00 61.58 C

ATOM 1961 OEl GLU B 746 116.474 60.883 -8.011 1.00 61.57 O

ATOM 1962 OE2 GLU B 746 114.820 61.864 -6.954 1.00 62.50 O

ATOM 1963 N PRO B 747 119.080 64.100 -6.458 1.00 63.44 N

ATOM 1964 CA PRO B 747 120.492 64.128 -6.862 1.00 63.68 C

ATOM 1965 C PRO B 747 120.700 63.847 -8.350 1.00 64.42 C

ATOM 1966 O PRO B 747 119.747 63.602 -9.084 1.00 64.63 O

ATOM 1967 CB PRO B 747 121.120 63.042 -5.993 1.00 63.65 C

ATOM 1968 CG PRO B 747 120.266 63.047 -4.773 1.00 63.89 C

ATOM 1969 CD PRO B 747 118.879 63.155 -5.346 1.00 63.91 C

ATOM 1970 N GLU B 748 121.955 63.882 -8.785 1.00 64.78 N

ATOM 1971 CA GLU B 748 122.292 63.617 -10.178 1.00 65.97 C

ATOM 1972 C GLU B 748 123.249 62.428 -10.254 1.00 65.99 C

ATOM 1973 O GLU B 748 123.967 62.141 -9.293 1.00 65.54 O

ATOM 1974 CB GLU B 748 122.940 64.846 -10.821 1.00 67.87 C ATOM 1975 CG GLU B 748 124.346 65.146 -10.332 1.00 71.30 C

ATOM 1976 CD GLU B 748 124.392 65.542 -8.869 1.00 73.26 C

ATOM 1977 OEl GLU B 748 124.100 64.687 -8.003 1.00 74.81 O

ATOM 1978 OE2 GLU B 748 124.720 66.715 -8.587 1.00 74.43 O

ATOM 1979 N ILE B 749 123.248 61.747 -11.402 1.00 65.98 N

ATOM 1980 CA ILE B 749 124.085 60.563 -11.645 1.00 64.56 C

ATOM 1981 C ILE B 749 125.457 60.547 -10.952 1.00 63.33 C

ATOM 1982 O ILE B 749 125.987 61.593 -10.577 1.00 62.35 O

ATOM 1983 CB ILE B 749 124.265 60.320 -13.181 1.00 64.24 C

ATOM 1984 CGl ILE B 749 124.939 61.529 -13.851 1.00 63.31 C

ATOM 1985 CG2 ILE B 749 122.899 60.059 -13.823 1.00 63.77 C

ATOM 1986 CDl ILE B 749 125.845 62.338 -12.952 1.00 62.54 C

ATOM 1987 N VAL B 750 126.011 59.346 -10.784 1.00 62.73 N

ATOM 1988 CA VAL B 750 127.308 59.146 -10.131 1.00 61.99 C

ATOM 1989 C VAL B 750 128.098 58.026 -10.811 1.00 62.17 C

ATOM 1990 O VAL B 750 127.520 57.137 -11.435 1.00 62.01 O

ATOM 1991 CB VAL B 750 127.117 58.797 -8.626 1.00 61.57 C

ATOM 1992 CGl VAL B 750 128.405 58.241 -8.029 1.00 61.58 C

ATOM 1993 CG2 VAL B 750 126.693 60.042 -7.865 1.00 61.78 C

ATOM 1994 N TYR B 751 129.423 58.080 -10.693 1.00 62.69 N

ATOM 1995 CA TYR B 751 130.291 57.069 -11.288 1.00 63.03 C

ATOM 1996 C TYR B 751 130.653 55.970 -10.294 1.00 63.54 C

ATOM 1997 O TYR B 751 130.910 56.239 -9.117 1.00 63.14 O

ATOM 1998 CB TYR B 751 131.574 57.711 -11.828 1.00 62.87 C

ATOM 1999 CG TYR B 751 131.404 58.365 -13.178 1.00 62.55 C

ATOM 2000 CDl TYR B 751 130.784 59.603 -13.307 1.00 61.98 C

ATOM 2001 CD2 TYR B 751 131.825 57.714 -14.338 1.00 63.45 C

ATOM 2002 CEl TYR B 751 130.584 60.176 -14.560 1.00 62.19 C

ATOM 2003 CE2 TYR B 751 131.628 58.276 -15.595 1.00 62.38 C

ATOM 2004 CZ TYR B 751 131.008 59.502 -15.699 1.00 62.12 C

ATOM 2005 OH TYR B 751 130.804 60.038 -16.948 1.00 62.03 O

ATOM 2006 N ALA B 752 130.677 54.733 -10.780 1.00 64.18 N

ATOM 2007 CA ALA B 752 131.000 53.578 -9.946 1.00 65.09 C

ATOM 2008 C ALA B 752 132.501 53.469 -9.666 1.00 66.17 C

ATOM 2009 O ALA B 752 132.980 52.451 -9.147 1.00 67.46 O

ATOM 2010 CB ALA B 752 130.494 52.298 -10.616 1.00 64.46 C

ATOM 2011 N ASP B 760 136.248 40.654 -16.332 1.00 70.18 N

ATOM 2012 CA ASP B 760 134.977 40.796 -15.625 1.00 70.51 C

ATOM 2013 C ASP B 760 134.644 39.516 -14.865 1.00 70.65 C

ATOM 2014 O ASP B 760 134.183 38.534 -15.452 1.00 70.83 O

ATOM 2015 CB ASP B 760 133.841 41.094 -16.609 1.00 70.28 C

ATOM 2016 CG ASP B 760 134.154 42.251 -17.537 1.00 69.96 C

ATOM 2017 ODl ASP B 760 134.386 43.372 -17.039 1.00 69.01 O

ATOM 2018 OD2 ASP B 760 134.162 42.035 -18.769 1.00 69.95 O

ATOM 2019 N THR B 761 134.869 39.526 -13.558 1.00 70.32 N

ATOM 2020 CA THR B 761 134.587 38.345 -12.761 1.00 69.72 C

ATOM 2021 C THR B 761 133.587 38.630 -11.666 1.00 68.88 C

ATOM 2022 O THR B 761 133.448 39.762 -11.214 1.00 68.96 O

ATOM 2023 CB THR B 761 135.857 37.800 -12.094 1.00 69.42 C

ATOM 2024 OGl THR B 761 136.327 38.742 -11.125 1.00 70.31 O

ATOM 2025 CG2 THR B 761 136.935 37.565 -13.131 1.00 70.19 C

ATOM 2026 N ALA B 762 132.901 37.579 -11.237 1.00 68.26 N

ATOM 2027 CA ALA B 762 131.920 37.692 -10.175 1.00 67.48 C

ATOM 2028 C ALA B 762 132.553 38.445 -9.023 1.00 66.99 C

ATOM 2029 O ALA B 762 131.886 39.215 -8.339 1.00 67.48 O

ATOM 2030 CB ALA B 762 131.489 36.310 -9.712 1.00 66.46 C

ATOM 2031 N GLU B 763 133.849 38.234 -8.824 1.00 66.25 N

ATOM 2032 CA GLU B 763 134.554 38.884 -7.734 1.00 65.79 C

ATOM 2033 C GLU B 763 134.822 40.367 -7.954 1.00 64.16 C

ATOM 2034 O GLU B 763 134.722 41.158 -7.019 1.00 63.45 O

ATOM 2035 CB GLU B 763 135.873 38.158 -7.434 1.00 67.56 C

ATOM 2036 CG GLU B 763 136.443 37.303 -8.573 1.00 69.35 C

ATOM 2037 CD GLU B 763 135.824 35.914 -8.653 1.00 70.11 C

ATOM 2038 OEl GLU B 763 136.578 34.931 -8.806 1.00 71.15 O

ATOM 2039 OE2 GLU B 763 134.588 35.799 -8.572 1.00 68.73 O

ATOM 2040 N ASN B 764 135.156 40.750 -9.180 1.00 63.44 N

ATOM 2041 CA ASN B 764 135.441 42.154 -9.468 1.00 62.64 C

ATOM 2042 C ASN B 764 134.181 42.978 -9.721 1.00 60.75 C

ATOM 2043 O ASN B 764 134.125 44.175 -9.414 1.00 59.81 O

ATOM 2044 CB ASN B 764 136.386 42.263 -10.668 1.00 64.45 C

ATOM 2045 CG ASN B 764 137.843 42.101 -10.280 1.00 66.17 C

ATOM 2046 ODl ASN B 764 138.739 42.381 -11.075 1.00 68.31 O

ATOM 2047 ND2 ASN B 764 138.090 41.654 -9.050 1.00 66.63 N

ATOM 2048 N LEU B 765 133.170 42.333 -10.285 1.00 58.37 N

ATOM 2197 N ALA B 784 117.672 62.990 1.825 1.00 35.79 N

ATOM 2198 CA ALA B 784 116.709 62.750 2.878 1.00 37.01 C

ATOM 2199 C ALA B 784 116.755 63.860 3.942 1.00 37.14 C

ATOM 2200 O ALA B 784 115.735 64.211 4.535 1.00 36.50 O

ATOM 2201 CB ALA B 784 116.981 61.382 3.502 1.00 35.88 C

ATOM 2202 N LYS B 785 117.936 64.420 4.161 1.00 37.36 N

ATOM 2203 CA LYS B 785 118.131 65.465 5.157 1.00 39.38 C

ATOM 2204 C LYS B 785 117.269 66.708 4.938 1.00 40.51 C

ATOM 2205 O LYS B 785 116.953 67.416 5.891 1.00 41.46 O

ATOM 2206 CB LYS B 785 119.624 65.855 5.211 1.00 40.68 C

ATOM 2207 N VAL B 786 116.904 66.972 3.683 1.00 42.45 N

ATOM 2208 CA VAL B 786 116.074 68.125 3.323 1.00 43.31 C

ATOM 2209 C VAL B 786 114.700 67.635 2.890 1.00 45.26 C

ATOM 2210 O VAL B 786 113.929 68.353 2.249 1.00 46.94 O

ATOM 2211 CB VAL B 786 116.696 68.912 2.154 1.00 43.86 C

ATOM 2212 CGl VAL B 786 117.737 69.902 2.668 1.00 44.54 C

ATOM 2213 CG2 VAL B 786 117.363 67.947 1.201 1.00 44.81 C

ATOM 2214 N LEU B 787 114.396 66.395 3.237 1.00 45.79 N

ATOM 2215 CA LEU B 787 113.121 65.814 2.869 1.00 46.10 C

ATOM 2216 C LEU B 787 112.053 66.290 3.839 1.00 46.27 C

ATOM 2217 O LEU B 787 112.235 66.258 5.061 1.00 46.38 O

ATOM 2218 CB LEU B 787 113.239 64.291 2.881 1.00 45.66 C

ATOM 2219 CG LEU B 787 112.122 63.435 2.297 1.00 45.71 C

ATOM 2220 CDl LEU B 787 111.718 63.920 0.906 1.00 44.39 C

ATOM 2221 CD2 LEU B 787 112.632 61.992 2.256 1.00 45.44 C

ATOM 2222 N PRO B 788 110.922 66.760 3.298 1.00 46.47 N

ATOM 2223 CA PRO B 788 109.775 67.268 4.057 1.00 45.40 C

ATOM 2224 C PRO B 788 109.169 66.274 5.048 1.00 45.19 C

ATOM 2225 O PRO B 788 108.726 65.193 4.662 1.00 45.23 O

ATOM 2226 CB PRO B 788 108.776 67.652 2.965 1.00 44.30 C

ATOM 2227 CG PRO B 788 109.647 68.013 1.814 1.00 44.47 C

ATOM 2228 CD PRO B 788 110.721 66.951 1.850 1.00 46.30 C

ATOM 2229 N GLY B 789 109.138 66.669 6.321 1.00 44.80 N

ATOM 2230 CA GLY B 789 108.562 65.840 7.365 1.00 43.69 C

ATOM 2231 C GLY B 789 109.575 64.884 7.939 1.00 44.15 C

ATOM 2232 O GLY B 789 109.769 64.814 9.148 1.00 45.26 O

ATOM 2233 N PHE B 790 110.223 64.138 7.057 1.00 44.10 N

ATOM 2234 CA PHE B 790 111.233 63.172 7.461 1.00 44.37 C

ATOM 2235 C PHE B 790 112.301 63.878 8.299 1.00 45.42 C

ATOM 2236 O PHE B 790 112.737 63.366 9.331 1.00 44.99 O

ATOM 2237 CB PHE B 790 111.868 62.548 6.208 1.00 41.69 C

ATOM 2238 CG PHE B 790 112.872 61.464 6.497 1.00 39.29 C

ATOM 2239 CDl PHE B 790 112.465 60.231 6.975 1.00 39.50 C

ATOM 2240 CD2 PHE B 790 114.228 61.674 6.267 1.00 38.09 C

ATOM 2241 CEl PHE B 790 113.393 59.218 7.218 1.00 39.03 C

ATOM 2242 CE2 PHE B 790 115.159 60.676 6.505 1.00 36.51 C

ATOM 2243 CZ PHE B 790 114.742 59.444 6.981 1.00 38.00 C

ATOM 2244 N LYS B 791 112.704 65.064 7.850 1.00 45.86 N

ATOM 2245 CA LYS B 791 113.738 65.830 8.533 1.00 47.84 C

ATOM 2246 C LYS B 791 113.344 66.346 9.917 1.00 48.14 C

ATOM 2247 O LYS B 791 114.190 66.851 10.652 1.00 48.20 O

ATOM 2248 CB LYS B 791 114.177 67.009 7.660 1.00 47.22 C

ATOM 2249 CG LYS B 791 113.072 68.001 7.343 1.00 47.70 C

ATOM 2250 CD LYS B 791 113.659 69.233 6.691 1.00 46.67 C

ATOM 2251 CE LYS B 791 112.620 70.296 6.474 1.00 47.55 C

ATOM 2252 NZ LYS B 791 113.242 71.505 5.883 1.00 49.50 N

ATOM 2253 N ASN B 792 112.067 66.216 10.269 1.00 49.44 N

ATOM 2254 CA ASN B 792 111.571 66.685 11.563 1.00 49.19 C

ATOM 2255 C ASN B 792 111.611 65.596 12.614 1.00 49.61 C

ATOM 2256 O ASN B 792 111.658 65.881 13.810 1.00 50.59 O

ATOM 2257 CB ASN B 792 110.143 67.209 11.426 1.00 49.48 C

ATOM 2258 CG ASN B 792 110.087 68.599 10.808 1.00 50.04 C

ATOM 2259 ODl ASN B 792 110.984 69.413 11.017 1.00 49.66 O

ATOM 2260 ND2 ASN B 792 109.039 68.869 10.034 1.00 48.80 N

ATOM 2261 N LEU B 793 111.578 64.349 12.163 1.00 49.21 N

ATOM 2262 CA LEU B 793 111.635 63.220 13.075 1.00 49.33 C

ATOM 2263 C LEU B 793 112.985 63.261 13.776 1.00 49.95 C

ATOM 2264 O LEU B 793 113.941 63.840 13.261 1.00 49.55 O

ATOM 2265 CB LEU B 793 111.526 61.905 12.302 1.00 48.85 C

ATOM 2266 CG LEU B 793 110.281 61.675 11.448 1.00 49.84 C

ATOM 2267 CDl LEU B 793 110.412 60.355 10.714 1.00 49.77 C

ATOM 2268 CD2 LEU B 793 109.036 61.678 12.329 1.00 48.78 C

ATOM 2269 N PRO B 794 113.078 62.670 14.974 1.00 50.94 N

ATOM 2270 CA PRO B 794 114.373 62.687 15.657 1.00 51.70 C ATOM 2271 C PRO B 794 115.418 62.083 14.734 1.00 52.94 C

ATOM 2272 O PRO B 794 115.076 61.341 13.809 1.00 53.82 O

ATOM 2273 CB PRO B 794 114.124 61.838 16.906 1.00 51.64 C

ATOM 2274 CG PRO B 794 112.884 61.038 16.574 1.00 52.47 C

ATOM 2275 CD PRO B 794 112.054 62.019 15.802 1.00 51.32 C

ATOM 2276 N LEO B 795 116.687 62.400 14.975 1.00 54.23 N

ATOM 2277 CA LEU B 795 117.773 61.896 14.136 1.00 54.67 C

ATOM 2278 C LEU B 795 117.924 60.391 14.263 1.00 55.08 C

ATOM 2279 O LEU B 795 118.370 59.730 13.326 1.00 55.74 O

ATOM 2280 CB LEU B 795 119.094 62.592 14.488 1.00 53.71 C

ATOM 2281 CG LEU B 795 120.116 62.839 13.367 1.00 53.07 C

ATOM 2282 CDl LEU B 795 120.697 64.239 13.471 1.00 54.97 C

ATOM 2283 CD2 LEU B 795 121.225 61.813 13.462 1.00 52.57 C

ATOM 2284 N GLU B 796 117.554 59.849 15.420 1.00 55.80 N

ATOM 2285 CA GLU B 796 117.643 58.410 15.635 1.00 56.83 C

ATOM 2286 C GLU B 796 116.736 57.724 14.625 1.00 55.55 C

ATOM 2287 O GLU B 796 117.154 56.799 13.929 1.00 56.03 O

ATOM 2288 CB GLU B 796 117.210 58.053 17.064 1.00 59.30 C

ATOM 2289 CG GLU B 796 116.751 56.599 17.273 1.00 61.59 C

ATOM 2290 CD GLU B 796 117.885 55.570 17.282 1.00 62.82 C

ATOM 2291 OEl GLU B 796 117.607 54.387 16.978 1.00 63.54 O

ATOM 2292 OE2 GLU B 796 119.041 55.928 17.598 1.00 63.32 O

ATOM 2293 N ASP B 797 115.496 58.194 14.545 1.00 54.48 N

ATOM 2294 CA ASP B 797 114.510 57.632 13.620 1.00 54.60 C

ATOM 2295 C ASP B 797 114.900 57.851 12.166 1.00 53.05 C

ATOM 2296 O ASP B 797 114.732 56.967 11.329 1.00 53.95 O

ATOM 2297 CB ASP B 797 113.125 58.240 13.873 1.00 54.67 C

ATOM 2298 CG ASP B 797 112.452 57.680 15.123 1.00 55.59 C

ATOM 2299 ODl ASP B 797 113.125 57.012 15.936 1.00 54.35 O

ATOM 2300 OD2 ASP B 797 111.235 57.912 15.290 1.00 56.35 O

ATOM 2301 N GLN B 798 115.421 59.029 11.863 1.00 51.43 N

ATOM 2302 CA GLN B 798 115.825 59.316 10.504 1.00 50.40 C

ATOM 2303 C GLN B 798 116.834 58.281 10.010 1.00 49.90 C

ATOM 2304 O GLN B 798 116.721 57.773 8.894 1.00 50.30 O

ATOM 2305 CB GLN B 798 116.436 60.709 10.428 1.00 50.93 C

ATOM 2306 CG GLN B 798 115.429 61.828 10.582 1.00 50.80 C

ATOM 2307 CD GLN B 798 116.082 63.191 10.540 1.00 49.78 C

ATOM 2308 OEl GLN B 798 116.824 63.491 9.614 1.00 49.66 O

ATOM 2309 NE2 GLN B 798 115.799 64.028 11.531 1.00 48.46 N

ATOM 2310 N ILE B 799 117.809 57.951 10.850 1.00 48.33 N

ATOM 2311 CA ILE B 799 118.835 56.998 10.463 1.00 48.37 C

ATOM 2312 C ILE B 799 118.348 55.564 10.458 1.00 48.14 C

ATOM 2313 O ILE B 799 118.744 54.769 9.601 1.00 48.31 O

ATOM 2314 CB ILE B 799 120.075 57.127 11.372 1.00 49.81 C

ATOM 2315 CGl ILE B 799 120.696 58.509 11.169 1.00 49.23 C

ATOM 2316 CG2 ILE B 799 121.091 56.039 11.049 1.00 49.07 C

ATOM 2317 CDl ILE B 799 121.850 58.801 12.067 1.00 51.51 C

ATOM 2318 N THR B 800 117.485 55.227 11.407 1.00 47.44 N

ATOM 2319 CA THR B 800 116.960 53.877 11.471 1.00 45.90 C

ATOM 2320 C THR B 800 116.192 53.584 10.188 1.00 46.10 C

ATOM 2321 O THR B 800 116.241 52.471 9.677 1.00 46.23 O

ATOM 2322 CB THR B 800 116.000 53.690 12.665 1.00 47.15 C

ATOM 2323 OGl THR B 800 116.639 54.111 13.879 1.00 46.42 O

ATOM 2324 CG2 THR B 800 115.589 52.229 12.784 1.00 43.46 C

ATOM 2325 N LEU B 801 115.475 54.581 9.674 1.00 46.21 N

ATOM 2326 CA LEU B 801 114.701 54.395 8.450 1.00 45.43 C

ATOM 2327 C LEU B 801 115.608 54.164 7.246 1.00 44.93 C

ATOM 2328 O LEU B 801 115.361 53.285 6.418 1.00 44.75 O

ATOM 2329 CB LEU B 801 113.802 55.611 8.173 1.00 45.47 C

ATOM 2330 CG LEU B 801 112.384 55.723 8.758 1.00 44.68 C

ATOM 2331 CDl LEU B 801 111.665 54.391 8.611 1.00 42.94 C

ATOM 2332 CD2 LEU B 801 112.433 56.118 10.212 1.00 44.86 C

ATOM 2333 N ILE B 802 116.668 54.952 7.154 1.00 45.08 N

ATOM 2334 CA ILE B 802 117.597 54.841 6.037 1.00 45.09 C

ATOM 2335 C ILE B 802 118.321 53.495 5.988 1.00 45.89 C

ATOM 2336 O ILE B 802 118.598 52.973 4.910 1.00 46.05 O

ATOM 2337 CB ILE B 802 118.617 55.985 6.094 1.00 43.95 C

ATOM 2338 CGl ILE B 802 117.895 57.284 6.476 1.00 43.41 C

ATOM 2339 CG2 ILE B 802 119.299 56.147 4.748 1.00 44.32 C

ATOM 2340 CDl ILE B 802 118.781 58.516 6.504 1.00 42.43 C

ATOM 2341 N GLN B 803 118.611 52.920 7.151 1.00 46.31 N

ATOM 2342 CA GLN B 803 119.315 51.647 7.183 1.00 48.33 C

ATOM 2343 C GLN B 803 118.394 50.495 6.859 1.00 48.44 C

ATOM 2344 O GLN B 803 118.820 49.485 6.304 1.00 48.61 O

ATOM 2493 C LYS B 820 116.664 57.058 -19.431 1.00 55.94 C

ATOM 2494 O LYS B 820 116.880 58.094 -20.060 1.00 56.13 O

ATOM 2495 CB LYS B 820 115.478 58.003 -17.431 1.00 53.37 C

ATOM 2496 N HIS B 821 117.494 56.020 -19.493 1.00 57.19 N

ATOM 2497 CA HIS B 821 118.704 56.117 -20.304 1.00 58.41 C

ATOM 2498 C HIS B 821 118.850 55.059 -21.396 1.00 59.23 C

ATOM 2499 O HIS B 821 119.693 55.205 -22.285 1.00 58.87 O

ATOM 2500 CB HIS B 821 119.945 56.098 -19.399 1.00 59.74 C

ATOM 2501 CG HIS B 821 120.027 57.264 -18.461 1.00 61.93 C

ATOM 2502 NDl HIS B 821 119.346 58.443 -18.674 1.00 64.65 N

ATOM 2503 CD2 HIS B 821 120.701 57.431 -17.296 1.00 62.97 C

ATOM 2504 CEl HIS B 821 119.595 59.283 -17.685 1.00 63.46 C

ATOM 2505 NE2 HIS B 821 120.416 58.693 -16.835 1.00 63.35 N

ATOM 2506 N THR B 822 118.033 54.007 -21.340 1.00 59.30 N

ATOM 2507 CA THR B 822 118.106 52.935 -22.334 1.00 59.44 C

ATOM 2508 C THR B 822 116.741 52.322 -22.630 1.00 59.70 C

ATOM 2509 O THR B 822 116.656 51.215 -23.175 1.00 58.76 O

ATOM 2510 CB THR B 822 119.028 51.782 -21.858 1.00 59.73 C

ATOM 2511 OGl THR B 822 118.301 50.930 -20.963 1.00 59.95 O

ATOM 2512 CG2 THR B 822 120.257 52.325 -21.138 1.00 59.77 C

ATOM 2513 N ASN B 823 115.677 53.036 -22.273 1.00 60.04 N

ATOM 2514 CA ASN B 823 114.328 52.525 -22.482 1.00 60.40 C

ATOM 2515 C ASN B 823 114.197 51.151 -21.822 1.00 60.21 C

ATOM 2516 O ASN B 823 113.570 50.242 -22.362 1.00 59.26 O

ATOM 2517 CB ASN B 823 114.013 52.418 -23.976 1.00 61.52 C

ATOM 2518 CG ASN B 823 113.721 53.767 -24.611 1.00 62.17 C

ATOM 2519 ODl ASN B 823 112.667 54.359 -24.382 1.00 64.47 O

ATOM 2520 ND2 ASN B 823 114.657 54.259 -25.413 1.00 62.43 N

ATOM 2521 N SER B 824 114.814 51.016 -20.651 1.00 60.17 N

ATOM 2522 CA SER B 824 114.773 49.784 -19.871 1.00 59.75 C

ATOM 2523 C SER B 824 115.264 48.567 -20.643 1.00 59.45 C

ATOM 2524 O SER B 824 114.737 47.466 -20.490 1.00 59.31 O

ATOM 2525 CB SER B 824 113.346 49.546 -19.372 1.00 59.84 C

ATOM 2526 OG SER B 824 112.953 50.580 -18.490 1.00 58.26 O

ATOM 2527 N GLN B 825 116.282 48.771 -21.470 1.00 59.72 N

ATOM 2528 CA GLN B 825 116.844 47.687 -22.262 1.00 59.17 C

ATOM 2529 C GLN B 825 118.186 47.229 -21.701 1.00 57.60 C

ATOM 2530 O GLN B 825 118.766 46.246 -22.166 1.00 57.50 O

ATOM 2531 CB GLN B 825 116.991 48.127 -23.725 1.00 61.75 C

ATOM 2532 CG GLN B 825 115.749 48.830 -24.289 1.00 64.10 C

ATOM 2533 CD GLN B 825 115.570 48.629 -25.794 1.00 65.65 C

ATOM 2534 OEl GLN B 825 114.476 48.289 -26.264 1.00 65.05 O

ATOM 2535 NE2 GLN B 825 116.646 48.841 -26.556 1.00 66.34 N

ATOM 2536 N PHE B 826 118.661 47.947 -20.690 1.00 56.18 N

ATOM 2537 CA PHE B 826 119.924 47.640 -20.023 1.00 55.11 C

ATOM 2538 C PHE B 826 119.826 48.123 -18.581 1.00 53.99 C

ATOM 2539 O PHE B 826 118.978 48.946 -18.263 1.00 53.86 O

ATOM 2540 CB PHE B 826 121.095 48.378 -20.688 1.00 55.14 C

ATOM 2541 CG PHE B 826 121.369 47.960 -22.103 1.00 55.61 C

ATOM 2542 CDl PHE B 826 121.856 46.687 -22.388 1.00 57.11 C

ATOM 2543 CD2 PHE B 826 121.170 48.850 -23.151 1.00 55.17 C

ATOM 2544 CEl PHE B 826 122.145 46.310 -23.705 1.00 57.39 C

ATOM 2545 CE2 PHE B 826 121.454 48.485 -24.467 1.00 55.94 C

ATOM 2546 CZ PHE B 826 121.944 47.215 -24.745 1.00 56.91 C

ATOM 2547 N LEU B 827 120.691 47.608 -17.715 1.00 53.42 N

ATOM 2548 CA LEU B 827 120.715 48.034 -16.324 1.00 53.25 C

ATOM 2549 C LEU B 827 121.761 49.129 -16.251 1.00 53.41 C

ATOM 2550 O LEU B 827 122.944 48.870 -16.444 1.00 53.01 O

ATOM 2551 CB LEU B 827 121.100 46.878 -15.401 1.00 54.36 C

ATOM 2552 CG LEU B 827 119.996 45.840 -15.181 1.00 55.15 C

ATOM 2553 CDl LEU B 827 120.481 44.741 -14.250 1.00 54.90 C

ATOM 2554 CD2 LEU B 827 118.755 46.538 -14.610 1.00 55.42 C

ATOM 2555 N TYR B 828 121.311 50.348 -15.969 1.00 53.76 N

ATOM 2556 CA TYR B 828 122.175 51.520 -15.900 1.00 54.30 C

ATOM 2557 C TYR B 828 122.633 51.857 -14.474 1.00 53.02 C

ATOM 2558 O TYR B 828 122.166 52.833 -13.881 1.00 53.56 O

ATOM 2559 CB TYR B 828 121.414 52.708 -16.513 1.00 57.67 C

ATOM 2560 CG TYR B 828 122.283 53.869 -16.953 1.00 59.96 C

ATOM 2561 CDl TYR B 828 122.748 54.810 -16.033 1.00 60.69 C

ATOM 2562 CD2 TYR B 828 122.676 53.999 -18.288 1.00 61.68 C

ATOM 2563 CEl TYR B 828 123.588 55.849 -16.430 1.00 62.53 C

ATOM 2564 CE2 TYR B 828 123.518 55.034 -18.694 1.00 62.41 C

ATOM 2565 CZ TYR B 828 123.970 55.953 -17.758 1.00 62.61 C

ATOM 2566 OH TYR B 828 124.810 56.969 -18.147 1.00 64.20 O ATOM 2567 N PHE B 829 123.550 51.064 -13.924 1.00 52.06 N

ATOM 2568 CA PHE B 829 124.041 51.306 -12.562 1.00 51.84 C

ATOM 2569 C PHE B 829 124.742 52.659 -12.435 1.00 52.17 C

ATOM 2570 O PHE B 829 124.673 53.324 -11.395 1.00 50.44 O

ATOM 2571 CB PHE B 829 125.013 50.205 -12.132 1.00 51.30 C

ATOM 2572 CG PHE B 829 124.368 48.861 -11.943 1.00 52.41 C

ATOM 2573 CDl PHE B 829 124.172 48.004 -13.020 1.00 52.23 C

ATOM 2574 CD2 PHE B 829 123.958 48.449 -10.684 1.00 51.64 C

ATOM 2575 CEl PHE B 829 123.580 46.758 -12.844 1.00 51.29 C

ATOM 2576 CE2 PHE B 829 123.364 47.205 -10.501 1.00 51.86 C

ATOM 2577 CZ PHE B 829 123.176 46.360 -11.583 1.00 50.71 C

ATOM 2578 N ALA B 830 125.420 53.053 -13.506 1.00 52.02 N

ATOM 2579 CA ALA B 830 126.158 54.300 -13.534 1.00 53.41 C

ATOM 2580 C ALA B 830 126.579 54.552 -14.967 1.00 54.64 C

ATOM 2581 O ALA B 830 126.621 53.624 -15.780 1.00 55.85 O

ATOM 2582 CB ALA B 830 127.379 54.197 -12.642 1.00 52.58 C

ATOM 2583 N PRO B 831 126.882 55.814 -15.304 1.00 55.29 N

ATOM 2584 CA PRO B 831 127.301 56.159 -16.666 1.00 55.78 C

ATOM 2585 C PRO B 831 128.467 55.291 -17.158 1.00 56.34 C

ATOM 2586 O PRO B 831 128.548 54.954 -18.339 1.00 56.12 O

ATOM 2587 CB PRO B 831 127.680 57.633 -16.538 1.00 55.78 C

ATOM 2588 CG PRO B 831 126.719 58.128 -15.515 1.00 54.73 C

ATOM 2589 CD PRO B 831 126.752 57.025 -14.474 1.00 55.36 C

ATOM 2590 N ASP B 832 129.358 54.923 -16.243 1.00 56.72 N

ATOM 2591 CA ASP B 832 130.511 54.107 -16.592 1.00 57.27 C

ATOM 2592 C ASP B 832 130.252 52.619 -16.446 1.00 57.55 C

ATOM 2593 O ASP B 832 131.058 51.808 -16.901 1.00 57.78 O

ATOM 2594 CB ASP B 832 131.725 54.487 -15.732 1.00 58.24 C

ATOM 2595 CG ASP B 832 131.491 54.263 -14.236 1.00 59.03 C

ATOM 2596 ODl ASP B 832 132.475 54.340 -13.458 1.00 58.45 O

ATOM 2597 OD2 ASP B 832 130.328 54.019 -13.836 1.00 58.51 O

ATOM 2598 N LED B 833 129.136 52.249 -15.820 1.00 58.25 N

ATOM 2599 CA LEU B 833 128.830 50.831 -15.630 1.00 58.38 C

ATOM 2600 C LEU B 833 127.396 50.428 -15.978 1.00 59.01 C

ATOM 2601 O LEU B 833 126.499 50.460 -15.127 1.00 59.38 O

ATOM 2602 CB LEU B 833 129.142 50.427 -14.187 1.00 57.96 C

ATOM 2603 CG LEU B 833 128.978 48.953 -13.811 1.00 58.01 C

ATOM 2604 CDl LEU B 833 129.918 48.093 -14.645 1.00 57.91 C

ATOM 2605 CD2 LEU B 833 129.262 48.786 -12.322 1.00 58.17 C

ATOM 2606 N VAL B 834 127.194 50.028 -17.231 1.00 59.01 N

ATOM 2607 CA VAL B 834 125.882 49.614 -17.715 1.00 58.35 C

ATOM 2608 C VAL B 834 125.887 48.130 -18.093 1.00 59.79 C

ATOM 2609 O VAL B 834 126.558 47.725 -19.040 1.00 60.50 O

ATOM 2610 CB VAL B 834 125.476 50.460 -18.932 1.00 57.17 C

ATOM 2611 CGl VAL B 834 124.072 50.119 -19.370 1.00 56.36 C

ATOM 2612 CG2 VAL B 834 125.578 51.922 -18.577 1.00 57.75 C

ATOM 2613 N PHE B 835 125.132 47.323 -17.348 1.00 60.76 N

ATOM 2614 CA PHE B 835 125.059 45.879 -17.581 1.00 60.41 C

ATOM 2615 C PHE B 835 124.342 45.398 -18.841 1.00 61.37 C

ATOM 2616 O PHE B 835 123.241 45.841 -19.179 1.00 61.36 O

ATOM 2617 CB PHE B 835 124.437 45.192 -16.366 1.00 59.15 C

ATOM 2618 CG PHE B 835 125.397 44.979 -15.227 1.00 58.08 C

ATOM 2619 CDl PHE B 835 126.572 45.720 -15.134 1.00 55.94 C

ATOM 2620 CD2 PHE B 835 125.103 44.061 -14.221 1.00 56.64 C

ATOM 2621 CEl PHE B 835 127.431 45.551 -14.057 1.00 55.37 C

ATOM 2622 CE2 PHE B 835 125.959 43.890 -13.142 1.00 54.47 C

ATOM 2623 CZ PHE B 835 127.123 44.634 -13.059 1.00 54.14 C

ATOM 2624 N ASN B 836 124.996 44.453 -19.509 1.00 63.08 N

ATOM 2625 CA ASN B 836 124.520 43.820 -20.737 1.00 64.30 C

ATOM 2626 C ASN B 836 123.844 42.522 -20.303 1.00 65.09 C

ATOM 2627 O ASN B 836 123.776 42.223 -19.108 1.00 64.84 O

ATOM 2628 CB ASN B 836 125.730 43.491 -21.626 1.00 65.39 C

ATOM 2629 CG ASN B 836 125.596 44.028 -23.038 1.00 66.59 C

ATOM 2630 ODl ASN B 836 125.192 43.311 -23.951 1.00 67.62 O

ATOM 2631 ND2 ASN B 836 125.936 45.301 -23.224 1.00 67.57 N

ATOM 2632 N GLU B 837 123.349 41.750 -21.263 1.00 65.39 N

ATOM 2633 CA GLU B 837 122.727 40.480 -20.932 1.00 66.16 C

ATOM 2634 C GLU B 837 123.819 39.558 -20.363 1.00 66.48 C

ATOM 2635 O GLU B 837 123.559 38.741 -19.476 1.00 66.17 O

ATOM 2636 CB GLU B 837 122.113 39.839 -22.182 1.00 67.42 C

ATOM 2637 CG GLU B 837 120.990 40.643 -22.859 1.00 69.51 C

ATOM 2638 CD GLU B 837 121.477 41.545 -23.995 1.00 70.80 C

ATOM 2639 OEl GLU B 837 122.408 41.137 -24.728 1.00 71.10 O

ATOM 2640 OE2 GLU B 837 120.912 42.650 -24.165 1.00 69.30 O ATOM 2641 N GLU B 838 125.042 39.709 -20.875 1.00 66.77 N

ATOM 2642 CA GLU B 838 126.189 38.902 -20.451 1.00 66.55 C

ATOM 2643 C GLU B 838 126.755 39.256 -19.072 1.00 66.34 C

ATOM 2644 O GLU B 838 127.090 38.366 -18.289 1.00 66.58 O

ATOM 2645 CB GLU B 838 127.328 39.010 -21.473 1.00 68.14 C

ATOM 2646 CG GLU B 838 127.006 38.597 -22.917 1.00 70.70 C

ATOM 2647 CD GLU B 838 126.462 39.744 -23.770 1.00 71.63 C

ATOM 2648 OEl GLU B 838 125.239 40.018 -23.697 1.00 71.16 O

ATOM 2649 OE2 GLU B 838 127.262 40.372 -24.509 1.00 70.97 O

ATOM 2650 N LYS B 839 126.894 40.551 -18.785 1.00 65.81 N

ATOM 2651 CA LYS B 839 127.431 40.992 -17.496 1.00 64.34 C

ATOM 2652 C LYS B 839 126.575 40.540 -16.322 1.00 62.95 C

ATOM 2653 O LYS B 839 127.099 40.211 -15.255 1.00 62.01 O

ATOM 2654 CB LYS B 839 127.575 42.513 -17.458 1.00 65.91 C

ATOM 2655 CG LYS B 839 128.864 43.038 -18.067 1.00 67.58 C

ATOM 2656 CD LYS B 839 128.919 44.551 -17.942 1.00 69.28 C

ATOM 2657 CE LYS B 839 130.081 45.144 -18.717 1.00 69.58 C

ATOM 2658 NZ LYS B 839 129.951 46.635 -18.809 1.00 70.80 N

ATOM 2659 N MET B 840 125.259 40.530 -16.516 1.00 60.61 N

ATOM 2660 CA MET B 840 124.358 40.098 -15.462 1.00 58.55 C

ATOM 2661 C MET B 840 124.757 38.671 -15.124 1.00 58.43 C

ATOM 2662 O MET B 840 124.778 38.283 -13.955 1.00 57.56 O

ATOM 2663 CB MET B 840 122.914 40.161 -15.947 1.00 57.40 C

ATOM 2664 CG MET B 840 122.558 41.500 -16.576 1.00 55.93 C

ATOM 2665 SD MET B 840 120.825 41.603 -16.996 1.00 55.27 S

ATOM 2666 CE MET B 840 120.590 43.381 -17.154 1.00 55.68 C

ATOM 2667 N HIS B 841 125.081 37.897 -16.158 1.00 58.42 N

ATOM 2668 CA HIS B 841 125.521 36.512 -15.976 1.00 58.39 C

ATOM 2669 C HIS B 841 126.845 36.508 -15.221 1.00 58.16 C

ATOM 2670 O HIS B 841 126.996 35.832 -14.201 1.00 58.79 O

ATOM 2671 CB HIS B 841 125.718 35.808 -17.328 1.00 57.78 C

ATOM 2672 CG HIS B 841 124.457 35.261 -17.924 1.00 56.86 C

ATOM 2673 NDl HIS B 841 123.681 34.317 -17.287 1.00 56.78 N

ATOM 2674 CD2 HIS B 841 123.848 35.512 -19.108 1.00 56.01 C

ATOM 2675 CEl HIS B 841 122.648 34.010 -18.051 1.00 55.70 C

ATOM 2676 NE2 HIS B 841 122.726 34.721 -19.161 1.00 55.33 N

ATOM 2677 N GLN B 842 127.806 37.271 -15.729 1.00 58.34 N

ATOM 2678 CA GLN B 842 129.119 37.356 -15.101 1.00 58.60 C

ATOM 2679 C GLN B 842 129.090 37.972 -13.706 1.00 57.05 C

ATOM 2680 O GLN B 842 130.068 37.880 -12.972 1.00 56.69 O

ATOM 2681 CB GLN B 842 130.084 38.156 -15.981 1.00 60.99 C

ATOM 2682 CG GLN B 842 130.461 37.476 -17.285 1.00 63.56 C

ATOM 2683 CD GLN B 842 130.866 36.028 -17.086 1.00 64.81 C

ATOM 2684 OEl GLN B 842 131.983 35.738 -16.644 1.00 65.69 O

ATOM 2685 NE2 GLN B 842 129.964 35.106 -17.426 1.00 64.55 N

ATOM 2686 N SER B 843 127.982 38.612 -13.343 1.00 55.72 N

ATOM 2687 CA SER B 843 127.875 39.214 -12.017 1.00 54.56 C

ATOM 2688 C SER B 843 127.650 38.112 -10.998 1.00 54.81 C

ATOM 2689 O SER B 843 127.881 38.306 -9.797 1.00 54.29 O

ATOM 2690 CB SER B 843 126.704 40.189 -11.952 1.00 52.79 C

ATOM 2691 OG SER B 843 125.479 39.488 -11.894 1.00 51.61 O

ATOM 2692 N ALA B 844 ■ 127.212 36.953 -11.499 1.00 54.85 N

ATOM 2693 CA ALA B 844 126.904 35.788 -10.676 1.00 54.15 C

ATOM 2694 C ALA B 844 125.667 36.153 -9.861 1.00 54.25 C

ATOM 2695 O ALA B 844 125.253 35.426 -8.956 1.00 53.87 O

ATOM 2696 CB ALA B 844 128.082 35.455 -9.749 1.00 54.51 C

ATOM 2697 N MET B 845 125.072 37.283 -10.230 1.00 54.03 N

ATOM 2698 CA MET B 845 123.905 37.833 -9.556 1.00 53.62 C

ATOM 2699 C MET B 845 122.679 37.814 -10.477 1.00 53.25 C

ATOM 2700 O MET B 845 121.639 38.393 -10.164 1.00 53.29 O

ATOM 2701 CB MET B 845 124.233 39.262 -9.137 1.00 53.69 C

ATOM 2702 CG MET B 845 123.366 39.851 -8.062 1.00 53.48 C

ATOM 2703 SD MET B 845 123.280 41.639 -8.299 1.00 56.93 S

ATOM 2704 CE MET B 845 125.004 42.066 -8.238 1.00 52.45 C

ATOM 2705 N TYR B 846 122.785 37.149 -11.619 1.00 52.35 N

ATOM 2706 CA TYR B 846 121.790 37.187 -12.747 1.00 50.32 C

ATOM 2707 C TYR B 846 120.229 37.305 -12.572 1.00 49.62 C

ATOM 2708 O TYR B 846 119.629 38.155 -13.255 1.00 52.39 O

ATOM 2709 CB TYR B 846 122.131 36.055 -13.688 1.00 49.86 C

ATOM 2710 CG TYR B 846 121.183 35.946 -14.857 1.00 48.22 C

ATOM 2711 CDl TYR B 846 120.014 35.209 -14.710 1.00 48.84 C

ATOM 2712 CD2 TYR B 846 121.431 36.548 -16.089 1.00 48.26 C

ATOM 2713 CEl TYR B 846 119.114 35.069 -15.758 1.00 49.11 C

ATOM 2714 CE2 TYR B 846 120.531 36.417 -17.147 1.00 48.91 C ATOM 2715 CZ TYR B 846 119.377 35.676 -16.971 1.00 49.56 C

ATOM 2716 OH TYR B 846 118.481 35.543 -18.004 1.00 51.65 O

ATOM 2717 N GLU B 847 119.536 36.528 -11.715 1.00 47.62 N

ATOM 2718 CA GLU B 847 118.070 36.655 -11.601 1.00 45.32 C

ATOM 2719 C GLU B 847 117.649 37.811 -10.706 1.00 43.58 C

ATOM 2720 O GLU B 847 116.489 38.238 -10.686 1.00 44.33 O

ATOM 2721 CB GLU B 847 117.470 35.341 -11.099 1.00 45.44 C

ATOM 2722 N LEU B 848 118.624 38.309 -9.952 1.00 40.26 N

ATOM 2723 CA LEU B 848 118.413 39.466 -9.107 1.00 38.10 C

ATOM 2724 C LEU B 848 118.440 40.636 -10.069 1.00 37.71 C

ATOM 2725 O LEU B 848 117.702 41.611 -9.905 1.00 38.58 O

ATOM 2726 CB LEU B 848 119.498 39.609 -8.036 1.00 32.89 C

ATOM 2727 CG LEU B 848 119.431 38.620 -6.869 1.00 30.16 C

ATOM 2728 CDl LEU B 848 120.511 38.945 -5.857 1.00 28.29 C

ATOM 2729 CD2 LEU B 848 118.062 38.650 -6.218 1.00 24.32 C

ATOM 2730 N CYS B 849 119.303 40.509 -11.078 1.00 39.85 N

ATOM 2731 CA CYS B 849 119.491 41.511 -12.126 1.00 40.37 C

ATOM 2732 C CYS B 849 118.287 41.442 -13.058 1.00 39.52 C

ATOM 2733 O CYS B 849 117.803 42.469 -13.538 1.00 39.70 O

ATOM 2734 CB CYS B 849 120.783 41.232 -12.909 1.00 42.35 C

ATOM 2735 SG CYS B 849 122.312 41.763 -12.099 1.00 47.17 S

ATOM 2736 N GLN B 850 117.813 40.224 -13.307 1.00 40.05 N

ATOM 2737 CA GLN B 850 116.637 40.002 -14.140 1.00 41.96 C

ATOM 2738 C GLN B 850 115.429 40.610 -13.419 1.00 40.83 C

ATOM 2739 O GLN B 850 114.571 41.240 -14.042 1.00 40.58 O

ATOM 2740 CB GLN B 850 116.407 38.503 -14.356 1.00 44.49 C

ATOM 2741 CG GLN B 850 116.669 38.023 -15.781 1.00 49.87 C

ATOM 2742 CD GLN B 850 115.818 38.760 -16.818 1.00 51.96 C

ATOM 2743 OEl GLN B 850 114.600 38.553 -16.904 1.00 52.57 O

ATOM 2744 NE2 GLN B 850 116.460 39.617 -17.616 1.00 51.29 N

ATOM 2745 N GLY B 851 115.371 40.411 -12.103 1.00 39.27 N

ATOM 2746 CA GLY B 851 114.290 40.965 -11.307 1.00 38.40 C

ATOM 2747 C GLY B 851 114.262 42.489 -11.302 1.00 39.88 C

ATOM 2748 O GLY B 851 113.187 43.096 -11.302 1.00 39.97 O

ATOM 2749 N MET B 852 115.431 43.125 -11.282 1.00 40.41 N

ATOM 2750 CA MET B 852 115.480 44.584 -11.295 1.00 42.54 C

ATOM 2751 C MET B 852 115.151 45.081 -12.706 1.00 43.59 C

ATOM 2752 O MET B 852 114.519 46.122 -12.878 1.00 43.30 O

ATOM 2753 CB MET B 852 116.864 45.074 -10.848 1.00 42.86 C

ATOM 2754 CG MET B 852 117.242 44.601 -9.453 1.00 44.28 C

ATOM 2755 SD MET B 852 118.902 45.074 -8.905 1.00 46.67 S

ATOM 2756 CE MET B 852 119.885 43.805 -9.650 1.00 43.93 C

ATOM 2757 N HIS B 853 115.573 44.324 -13.716 1.00 45.03 N

ATOM 2758 CA HIS B 853 115.287 44.683 -15.101 1.00 46.25 C

ATOM 2759 C HIS B 853 113.777 44.683 -15.299 1.00 45.74 C

ATOM 2760 O HIS B 853 113.243 45.517 -16.030 1.00 46.41 O

ATOM 2761 CB HIS B 853 115.940 43.682 -16.060 1.00 48.65 C

ATOM 2762 CG HIS B 853 115.596 43.905 -17.502 1.00 50.48 C

ATOM 2763 NDl HIS B 853 114.920 42.972 -18.260 1.00 52.48 N

ATOM 2764 CD2 HIS B 853 115.845 44.950 -18.328 1.00 51.10 C

ATOM 2765 CEl HIS B 853 114.768 43.433 -19.490 1.00 52.52 C

ATOM 2766 NE2 HIS B 853 115.320 44.631 -19.558 1.00 51.38 N

ATOM 2767 N GLN B 854 113.094 43.751 -14.637 1.00 45.72 N

ATOM 2768 CA GLN B 854 111.632 43.656 -14.731 1.00 46.12 C

ATOM 2769 C GLN B 854 110.936 44.888 -14.166 1.00 45.27 C

ATOM 2770 O GLN B 854 109.964 45.376 -14.746 1.00 46.34 O

ATOM 2771 CB GLN B 854 111.113 42.409 -14.010 1.00 46.65 C

ATOM 2772 CG GLN B 854 111.553 41.100 -14.653 1.00 49.87 C

ATOM 2773 CD GLN B 854 110.921 40.882 -16.021 1.00 51.98 C

ATOM 2774 OEl GLN B 854 111.505 40.221 -16.883 1.00 53.62 O

ATOM 2775 NE2 GLN B 854 109.719 41.427 -16.224 1.00 51.44 N

ATOM 2776 N ILE B 855 111.413 45.376 -13.026 1.00 43.50 N

ATOM 2777 CA ILE B 855 110.831 46.570 -12.433 1.00 42.69 C

ATOM 2778 C ILE B 855 110.988 47.667 -13.483 1.00 43.12 C

ATOM 2779 O ILE B 855 110.085 48.465 -13.717 1.00 42.28 O

ATOM 2780 CB ILE B 855 111.587 46.989 -11.153 1.00 41.39 C

ATOM 2781 CGl ILE B 855 111.321 45.979 -10.039 1.00 40.90 C

ATOM 2782 CG2 ILE B 855 111.175 48.387 -10.733 1.00 40.72 C

ATOM 2783 CDl ILE B 855 109.872 45.911 -9.615 1.00 40.49 C

ATOM 2784 N SER B 856 112.150 47.667 -14.125 1.00 44.05 N

ATOM 2785 CA SER B 856 112.484 48.638 -15.148 1.00 44.54 C

ATOM 2786 C SER B 856 111.472 48.577 -16.286 1.00 45.20 C

ATOM 2787 O SER B 856 111.060 49.611 -16.820 1.00 43.50 O

ATOM 2788 CB SER B 856 113.896 48.346 -15.676 1.00 45.80 C ATOM 2789 OG SER B 856 114.475 49.479 -16.303 1.00 48.47 O

ATOM 2790 N LEU B 857 111.072 47.362 -16.656 1.00 46.52 N

ATOM 2791 CA LEU B 857 110.117 47.186 -17.744 1.00 46.99 C

ATOM 2792 C LEU B 857 108.740 47.699 -17.368 1.00 47.60 C

ATOM 2793 O LEU B 857 107.977 48.127 -18.233 1.00 48.14 O

ATOM 2794 CB LEU B 857 110.023 45.720 -18.170 1.00 47.52 C

ATOM 2795 CG LEU B 857 111.266 45.067 -18.778 1.00 49.13 C

ATOM 2796 CDl LEU B 857 110.863 43.722 -19.387 1.00 48.39 C

ATOM 2797 CD2 LEU B 857 111.874 45.991 -19.848 1.00 49.26 C

ATOM 2798 N GLN B 858 108.423 47.657 -16.077 1.00 47.81 N

ATOM 2799 CA GLN B 858 107.140 48.139 -15.595 1.00 47.41 C

ATOM 2800 C GLN B 858 107.128 49.666 -15.640 1.00 47.70 C

ATOM 2801 O GLN B 858 106.070 50.296 -15.559 1.00 46.08 O

ATOM 2802 CB GLN B 858 106.905 47.655 -14.170 1.00 48.48 C

ATOM 2803 CG GLN B 858 106.010 46.439 -14.087 1.00 52.62 C

ATOM 2804 CD GLN B 858 105.943 45.873 -12.691 1.00 55.37 C

ATOM 2805 OEl GLN B 858 106.940 45.376 -12.156 1.00 57.49 O

ATOM 2806 NE2 GLN B 858 104.766 45.952 -12.081 1.00 57.45 N

ATOM 2807 N PHE B 859 108.316 50.251 -15.762 1.00 47.22 N

ATOM 2808 CA PHE B 859 108.446 51.694 -15.831 1.00 48.81 C

ATOM 2809 C PHE B 859 108.152 52.161 -17.251 1.00 49.81 C

ATOM 2810 O PHE B 859 107.532 53.206 -17.458 1.00 50.53 O

ATOM 2811 CB PHE B 859 109.855 52.118 -15.410 1.00 47.87 C

ATOM 2812 CG PHE B 859 110.034 52.254 -13.919 1.00 45.89 C

ATOM 2813 CDl PHE B 859 109.097 51.724 -13.029 1.00 44.77 C

ATOM 2814 CD2 PHE B 859 111.158 52.893 -13.406 1.00 44.36 C

ATOM 2815 CEl PHE B 859 109.280 51.828 -11.653 1.00 43.45 C

ATOM 2816 CE2 PHE B 859 111.352 53.002 -12.032 1.00 44.85 C

ATOM 2817 CZ PHE B 859 110.411 52.466 -11.151 1.00 44.59 C

ATOM 2818 N VAL B 860 108.596 51.384 -18.233 1.00 50.32 N

ATOM 2819 CA VAL B 860 108.346 51.736 -19.625 1.00 50.98 C

ATOM 2820 C VAL B 860 106.894 51.475 -19.956 1.00 50.78 C

ATOM 2821 O VAL B 860 106.246 52.276 -20.618 1.00 52.68 O

ATOM 2822 CB VAL B 860 109.196 50.904 -20.601 1.00 51.63 C

ATOM 2823 CGl VAL B 860 108.648 51.050 -22.015 1.00 51.67 C

ATOM 2824 CG2 VAL B 860 110.633 51.366 -20.558 1.00 53.65 C

ATOM 2825 N ARG B 861 106.386 50.343 -19.498 1.00 50.40 N

ATOM 2826 CA ARG B 861 105.011 49.982 -19.768 1.00 50.38 C

ATOM 2827 C ARG B 861 103.987 50.848 -19.043 1.00 49.62 C

ATOM 2828 O ARG B 861 102.869 51.002 -19.513 1.00 49.50 O

ATOM 2829 CB ARG B 861 104.803 48.497 -19.453 1.00 51.96 C

ATOM 2830 CG ARG B 861 105.257 47.574 -20.597 1.00 53.96 C

ATOM 2831 CD ARG B 861 105.131 46.090 -20.268 1.00 56.86 C

ATOM 2832 NE ARG B 861 105.945 45.697 -19.119 1.00 60.80 N

ATOM 2833 CZ ARG B 861 106.355 44.453 -18.888 1.00 62.38 C

ATOM 2834 NHl ARG B 861 106.022 43.486 -19.730 1.00 63.67 N

ATOM 2835 NH2 ARG B 861 107.103 44.169 -17.825 1.00 64.05 N

ATOM 2836 N LEU B 862 104.365 51.429 -17.911 1.00 49.97 N

ATOM 2837 CA LEU B 862 103.449 52.293 -17.157 1.00 49.61 C

ATOM 2838 C LEU B 862 103.609 53.767 -17.519 1.00 49.46 C

ATOM 2839 O LEU B 862 102.713 54.579 -17.282 1.00 49.00 O

ATOM 2840 CB LEU B 862 103.683 52.147 -15.658 1.00 48.23 C

ATOM 2841 CG LEU B 862 102.780 51.173 -14.926 1.00 47.00 C

ATOM 2842 CDl LEU B 862 103.567 50.509 -13.820 1.00 47.17 C

ATOM 2843 CD2 LEU B 862 101.584 51.921 -14.378 1.00 48.65 C

ATOM 2844 N GLN B 863 104.754 54.108 -18.096 1.00 49.46 N

ATOM 2845 CA GLN B 863 105.029 55.492 -18.453 .1.00 49.96 C

ATOM 2846 C GLN B 863 105.074 56.254 -17.131 1.00 48.89 C

ATOM 2847 O GLN B 863 104.471 57.311 -16.982 1.00 49.84 O

ATOM 2848 CB GLN B 863 103.933 56.037 -19.388 1.00 50.91 C

ATOM 2849 CG GLN B 863 103.888 55.358 -20.765 1.00 52.91 C

ATOM 2850 CD GLN B 863 104.955 55.886 -21.734 1.00 55.95 C

ATOM 2851 OEl GLN B 863 105.630 55.113 -22.428 1.00 56.29 O

ATOM 2852 NE2 GLN B 863 105.098 57.209 -21.795 1.00 57.06 N

ATOM 2853 N LEU B 864 105.792 55.678 -16.172 1.00 47.88 N

ATOM 2854 CA LEU B 864 105.967 56.249 -14.846 1.00 47.45 C

ATOM 2855 C LEU B 864 106.612 57.609 -15.056 1.00 48.18 C

ATOM 2856 O LEU B 864 107.509 57.752 -15.889 1.00 49.55 O

ATOM 2857 CB LEU B 864 106.872 55.327 -14.025 1.00 46.98 C

ATOM 2858 CG LEU B 864 106.962 55.369 -12.498 1.00 45.37 C

ATOM 2859 CDl LEU B 864 107.930 56.420 -12.075 1.00 47.14 C

ATOM 2860 CD2 LEU B 864 105.598 55.589 -11.893 1.00 46.29 C

ATOM 2861 N THR B 865 106.152 58.608 -14.314 1.00 47.49 N

ATOM 2862 CA THR B 865 106.680 59.955 -14.459 1.00 47.36 C

ATOM 2937 CG LYS B 873 112.854 57.283 -5.299 1.00 37.48 C

ATOM 2938 CD LYS B 873 114.291 57.802 -5.324 1.00 37.89 C

ATOM 2939 CE LYS B 873 114.345 59.316 -5.119 1.00 40.46 C

ATOM 2940 NZ LYS B 873 115.706 59.818 -4.808 1.00 38.82 N

ATOM 2941 N VAL B 874 110.161 58.258 -1.747 1.00 34.39 N

ATOM 2942 CA VAL B 874 109.942 58.643 -0.368 1.00 35.99 C

ATOM 2943 C VAL B 874 109.171 57.514 0.305 1.00 36.68 C

ATOM 2944 O VAL B 874 109.531 57.061 1.403 1.00 36.21 O

ATOM 2945 CB VAL B 874 109.157 59.960 -0.269 1.00 35.10 C

ATOM 2946 CGl VAL B 874 108.765 60.228 1.179 1.00 36.53 C

ATOM 2947 CG2 VAL B 874 110.013 61.091 -0.777 1.00 35.41 C

ATOM 2948 N LEU B 875 108.131 57.040 -0.377 1.00 36.81 N

ATOM 2949 CA LEU B 875 107.294 55.960 0.140 1.00 35.51 C

ATOM 2950 C LEU B 875 108.079 54.700 0.532 1.00 35.75 C

ATOM 2951 O LEU B 875 107.681 53.966 1.431 1.00 35.80 O

ATOM 2952 CB LEU B 875 106.214 55.635 -0.885 1.00 34.55 C

ATOM 2953 CG LEU B 875 104.766 55.758 -0.405 1.00 34.33 C

ATOM 2954 CDl LEU B 875 104.653 56.723 0.758 1.00 33.40 C

ATOM 2955 CD2 LEU B 875 103.910 56.188 -1.571 1.00 32.77 C

ATOM 2956 N LEU B 876 109.202 54.456 -0.133 1.00 35.67 N

ATOM 2957 CA LEU B 876 110.031 53.296 0.179 1.00 36.04 C

ATOM 2958 C LEU B 876 110.870 53.554 1.440 1.00 36.51 C

ATOM 2959 O LEU B 876 111.162 52.635 2.200 1.00 34.68 O

ATOM 2960 CB LEU B 876 110.929 52.963 -1.017 1.00 34.73 C

ATOM 2961 CG LEU B 876 110.175 52.263 -2.156 1.00 37.07 C

ATOM 2962 CDl LEU B 876 111.027 52.183 -3.422 1.00 32.84 C

ATOM 2963 CD2 LEU B 876 109.792 50.856 -1.684 1.00 34.65 C

ATOM 2964 N LEU B 877 111.247 54.815 1.643 1.00 38.25 N

ATOM 2965 CA LEU B 877 112.030 55.240 2.798 1.00 37.96 C

ATOM 2966 C LEU B 877 111.238 55.026 4.081 1.00 39.24 C

ATOM 2967 O LEU B 877 111.809 54.885 5.164 1.00 38.80 O

ATOM 2968 CB LEU B 877 112.371 56.724 2.663 1.00 38.07 C

ATOM 2969 CG LEU B 877 113.089 57.426 3.822 1.00 37.03 C

ATOM 2970 CDl LEU B 877 114.415 56.732 4.114 1.00 36.77 C

ATOM 2971 CD2 LEU B 877 113.316 58.885 3.459 1.00 36.61 C

ATOM 2972 N LEU B 878 109.913 55.011 3.940 1.00 41.14 N

ATOM 2973 CA LEU B 878 108.994 54.831 5.056 1.00 40.76 C

ATOM 2974 C LEU B 878 108.302 53.479 4.960 1.00 40.92 C

ATOM 2975 O LEU B 878 107.235 53.294 5.529 1.00 39.30 O

ATOM 2976 CB LEU B 878 107.933 55.932 5.017 1.00 40.46 C

ATOM 2977 CG LEU B 878 108.453 57.355 4.798 1.00 39.87 C

ATOM 2978 CDl LEU B 878 107.281 58.294 4.515 1.00 39.02 C

ATOM 2979 CD2 LEU B 878 109.237 57.812 6.013 1.00 38.84 C

ATOM 2980 N SER B 879 108.915 52.537 4.247 1.00 42.71 N

ATOM 2981 CA SER B 879 108.331 51.205 4.040 1.00 44.21 C

ATOM 2982 C SER B 879 108.715 50.104 5.028 1.00 45.46 C

ATOM 2983 O SER B 879 108.064 49.065 5.064 1.00 45.07 O

ATOM 2984 CB SER B 879 108.682 50.693 2.640 1.00 44.88 C

ATOM 2985 OG SER B 879 110.046 50.267 2.577 1.00 43.27 O

ATOM 2986 N THR B 880 109.771 50.319 5.807 1.00 47.14 N

ATOM 2987 CA THR B 880 110.238 49.314 6.761 1.00 48.77 C

ATOM 2988 C THR B 880 110.557 49.924 8.127 1.00 49.09 C

ATOM 2989 O THR B 880 111.376 50.835 8.230 1.00 49.63 O

ATOM 2990 CB THR B 880 111.513 48.645 6.246 1.00 50.00 C

ATOM 2991 OGl THR B 880 111.406 48.438 4.832 1.00 51.54 O

ATOM 2992 CG2 THR B 880 111.728 47.310 6.942 1.00 50.03 C

ATOM 2993 N ILE B 881 109.925 49.417 9.178 1.00 49.20 N

ATOM 2994 CA ILE B 881 110.168 49.953 10.513 1.00 49.11 C

ATOM 2995 C ILE B 881 110.583 48.892 11.518 1.00 49.35 C

ATOM 2996 O ILE B 881 110.610 47.698 11.231 1.00 48.30 O

ATOM 2997 CB ILE B 881 108.910 50.639 11.104 1.00 47.22 C

ATOM 2998 CGl ILE B 881 107.775 49.612 11.198 1.00 47.16 C

ATOM 2999 CG2 ILE B 881 108.541 51.866 10.290 1.00 46.50 C

ATOM 3000 CDl ILE B 881 106.446 50.165 11.705 1.00 47.11 C

ATOM 3001 N PRO B 882 110.946 49.334 12.717 1.00 50.28 N

ATOM 3002 CA PRO B 882 111.334 48.356 13.722 1.00 52.01 C

ATOM 3003 C PRO B 882 110.040 47.639 _ 14.088 1.00 53.94 C

ATOM 3004 O PRO B 882 108.979 48.263 14.127 1.00 54.55 O

ATOM 3005 CB PRO B 882 111.872 49.237 14.843 1.00 52.53 C

ATOM 3006 CG PRO B 882 112.488 50.386 14.076 1.00 49.14 C

ATOM 3007 CD PRO B 882 111.401 50.685 13.091 1.00 50.04 C

ATOM 3008 N LYS B 883 110.112 46.337 14.333 1.00 55.06 N

ATOM 3009 CA LYS B 883 108.915 45.578 14.665 1.00 55.94 C

ATOM 3010 C LYS B 883 108.068 46.261 15.739 1.00 56.44 C ATOM 3011 O LYS B 883 106.843 46.357 15.608 1.00 56.28 O

ATOM 3012 CB LYS B 883 109.296 44.168 15.127 1.00 56.99 C

ATOM 3013 CG LYS B 883 108.107 43.242 15.352 1.00 57.57 C

ATOM 3014 CD LYS B 883 108.564 41.838 15.732 1.00 59.61 C

ATOM 3015 CE LYS B 883 109.204 41.812 17.116 1.00 60.47 C

ATOM 3016 NZ LYS B 883 108.195 41.582 18.198 1.00 60.10 N

ATOM 3017 N ASP B 884 108.718 46.754 16.789 1.00 56.80 N

ATOM 3018 CA ASP B 884 107.998 47.393 17.880 1.00 56.35 C

ATOM 3019 C ASP B 884 107.620 48.848 17.665 1.00 55.22 C

ATOM 3020 O ASP B 884 106.704 49.348 18.317 1.00 54.83 O

ATOM 3021 CB ASP B 884 108.780 47.217 19.179 1.00 57.59 C

ATOM 3022 CG ASP B 884 108.636 45.809 19.744 1.00 60.45 C

ATOM 3023 ODl ASP B 884 107.547 45.499 20.267 1.00 60.85 O

ATOM 3024 OD2 ASP B 884 109.591 45.004 19.649 1.00 62.58 O

ATOM 3025 N GLY B 885 108.303 49.531 16.753 1.00 53.87 N

ATOM 3026 CA GLY B 885 107.955 50.916 16.503 1.00 53.51 C

ATOM 3027 C GLY B 885 109.101 51.899 16.572 1.00 53.40 C

ATOM 3028 O GLY B 885 110.156 51.600 17.126 1.00 54.08 O

ATOM 3029 N LEU B 886 108.878 53.085 16.008 1.00 52.89 N

ATOM 3030 CA LEU B 886 109.882 54.141 15.973 1.00 52.08 C

ATOM 3031 C LEU B 886 109.786 55.078 17.174 1.00 51.99 C

ATOM 3032 O LEU B 886 108.795 55.078 17.899 1.00 50.47 O

ATOM 3033 CB LEU B 886 109.743 54.949 14.676 1.00 51.02 C

ATOM 3034 CG LEU B 886 110.331 54.353 13.390 1.00 51.55 C

ATOM 3035 CDl LEU B 886 109.644 54.945 12.164 1.00 50.22 C

ATOM 3036 CD2 LEU B 886 111.823 54.627 13.348 1.00 50.47 C

ATOM 3037 N LYS B 887 110.829 55.878 17.371 1.00 52.65 N

ATOM 3038 CA LYS B 887 110.875 56.831 18.474 1.00 53.02 C

ATOM 3039 C LYS B 887 109.604 57.672 18.519 1.00 51.76 C

ATOM 3040 O LYS B 887 108.951 57.762 19.554 1.00 51.72 O

ATOM 3041 CB LYS B 887 112.107 57.733 18.336 1.00 52.75 C

ATOM 3042 N SER B 888 109.258 58.287 17.395 1.00 51.60 N

ATOM 3043 CA SER B 888 108.052 59.105 17.311 1.00 52.10 C

ATOM 3044 C SER B 888 107.088 58.416 16.366 1.00 51.73 C

ATOM 3045 O SER B 888 106.815 58.904 15.269 1.00 51.36 O

ATOM 3046 CB SER B 888 108.380 60.500 16.778 1.00 52.45 C

ATOM 3047 OG SER B 888 109.184 61.226 17.696 1.00 55.30 O

ATOM 3048 N GLN B 889 106.586 57.268 16.804 1.00 51.65 N

ATOM 3049 CA GLN B 889 105.659 56.475 16.008 1.00 51.30 C

ATOM 3050 C GLN B 889 104.461 57.324 15.605 1.00 50.92 C

ATOM 3051 O GLN B 889 103.964 57.228 14.482 1.00 50.05 O

ATOM 3052 CB GLN B 889 105.211 55.249 16.812 1.00 50.60 C

ATOM 3053 CG GLN B 889 104.590 54.125 15.984 1.00 50.03 C

ATOM 3054 CD GLN B 889 105.452 53.723 14.800 1.00 48.73 C

ATOM 3055 OEl GLN B 889 106.625 53.390 14.955 1.00 47.38 O

ATOM 3056 NE2 GLN B 889 104.865 53.744 13.610 1.00 49.05 N

ATOM 3057 N ALA B 890 104.012 58.166 16.529 1.00 51.08 N

ATOM 3058 CA ALA B 890 102.882 59.043 16.272 1.00 50.66 C

ATOM 3059 C ALA B 890 103.166 59.946 15.065 1.00 50.01 C

ATOM 3060 O ALA B 890 102.337 60.059 14.158 1.00 49.97 O

ATOM 3061 CB ALA B 890 102.592 59.892 17.512 1.00 50.18 C

ATOM 3062 N ALA B 891 104.346 60.566 15.048 1.00 47.91 N

ATOM 3063 CA ALA B 891 104.729 61.477 13.962 1.00 46.92 C

ATOM 3064 C ALA B 891 104.960 60.779 12.621 1.00 45.67 C

ATOM 3065 O ALA B 891 104.445 61.199 11.585 1.00 45.29 O

ATOM 3066 CB ALA B 891 105.974 62.264 14.365 1.00 44.92 C

ATOM 3067 N PHE B 892 105.749 59.717 12.653 1.00 45.13 N

ATOM 3068 CA PHE B 892 106.061 58.935 11.463 1.00 43.70 C

ATOM 3069 C PHE B 892 104.790 58.525 10.709 1.00 42.61 C

ATOM 3070 O PHE B 892 104.684 58.699 9.494 1.00 41.26 O

ATOM 3071 CB PHE B 892 106.860 57.693 11.886 1.00 43.06 C

ATOM 3072 CG PHE B 892 106.943 56.629 10.828 1.00 43.20 C

ATOM 3073 CDl PHE B 892 107.919 56.691 9.827 1.00 42.73 C

ATOM 3074 CD2 PHE B 892 106.017 55.577 10.811 1.00 40.90 C

ATOM 3075 CEl PHE B 892 107.970 55.721 8.820 1.00 42.09 C

ATOM 3076 CE2 PHE B 892 106.053 54.610 9.819 1.00 42.05 C

ATOM 3077 CZ PHE B 892 107.030 54.676 8.816 1.00 43.04 C

ATOM 3078 N GLU B 893 103.823 57.996 11.447 1.00 41.96 N

ATOM 3079 CA GLU B 893 102.568 57.530 10.874 1.00 42.52 C

ATOM 3080 C GLU B 893 101.793 58.646 10.158 1.00 42.65 C

ATOM 3081 O GLU B 893 101.022 58.389 9.231 1.00 41.66 O

ATOM 3082 CB GLU B 893 101.711 56.926 11.990 1.00 44.83 C

ATOM 3083 CG GLU B 893 100.827 55.754 11.594 1.00 49.56 C

ATOM 3084 CD GLU B 893 101.147 54.492 12.396 1.00 53.81 C ATOM 3085 OEl GLU B 893 100.979 54.508 13.637 1.00 56.16 O

ATOM 3086 OE2 GLU B 893 101.558 53.476 11.791 1.00 55.11 O

ATOM 3087 N GLU B 894 101.995 59.886 10.584 1.00 42.08 N

ATOM 3088 CA GLU B 894 101.281 61.000 9.977 1.00 42.63 C

ATOM 3089 C GLU B 894 101.942 61.469 8.689 1.00 43.56 C

ATOM 3090 O GLU B 894 101.272 61.862 7.732 1.00 42.14 O

ATOM 3091 CB GLU B 894 101.183 62.152 10.967 1.00 43.71 C

ATOM 3092 N MET B 895 103.267 61.431 8.678 1.00 45.47 N

ATOM 3093 CA MET B 895 104.026 61.840 7.514 1.00 46.21 C

ATOM 3094 C MET B 895 103.872 60.818 6.381 1.00 45.64 C

ATOM 3095 O MET B 895 103.693 61.190 5.217 1.00 44.76 O

ATOM 3096 CB MET B 895 105.488 62.001 7.914 1.00 49.32 C

ATOM 3097 CG MET B 895 106.440 62.231 6.777 1.00 53.53 C

ATOM 3098 SD MET B 895 108.111 62.314 7.424 1.00 61.68 S

ATOM 3099 CE MET B 895 108.483 60.580 7.699 1.00 57.14 C

ATOM 3100 N ARG B 896 103.931 59.532 6.717 1.00 44.24 N

ATOM 3101 CA ARG B 896 103.794 58.496 5.698 1.00 43.49 C

ATOM 3102 C ARG B 896 102.440 58.650 5.019 1.00 42.58 C

ATOM 3103 O ARG B 896 102.367 58.739 3.798 1.00 42.50 O

ATOM 3104 CB ARG B 896 103.933 57.090 6.313 1.00 42.57 C

ATOM 3105 CG ARG B 896 103.657 55.927 5.339 1.00 44.09 C

ATOM 3106 CD ARG B 896 103.907 54.568 6.014 1.00 46.57 C

ATOM 3107 NE ARG B 896 103.003 53.499 5.573 1.00 49.13 N

ATOM 3108 CZ ARG B 896 103.127 52.816 4.439 1.00 49.63 C

ATOM 3109 NHl ARG B 896 104.124 53.081 3.604 1.00 50.34 N

ATOM 3110 NH2 ARG B 896 102.262 51.851 4.143 1.00 52.44 N

ATOM 3111 N THR B 897 101.379 58.698 5.822 1.00 42.70 N

ATOM 3112 CA THR B 897 100.008 58.850 5.324 1.00 42.60 C

ATOM 3113 C THR B 897 99.821 60.006 4.348 1.00 42.53 C

ATOM 3114 O THR B 897 99.240 59.846 3.267 1.00 40.95 O

ATOM 3115 CB THR B 897 99.007 59.081 6.488 1.00 43.57 C

ATOM 3116 OGl THR B 897 98.758 57.842 7.160 1.00 46.63 O

ATOM 3117 CG2 THR B 897 97.679 59.646 5.965 1.00 43.55 C

ATOM 3118 N ASN B 898 100.283 61.179 4.756 1.00 42.36 N

ATOM 3119 CA ASN B 898 100.145 62.360 3.926 1.00 43.82 C

ATOM 3120 C ASN B 898 100.914 62.203 2.626 1.00 43.61 C

ATOM 3121 O ASN B 898 100.570 62.821 1.613 1.00 42.69 O

ATOM 3122 CB ASN B 898 ^■ 100.627 63.601 4.687 1.00 44.76 C

ATOM 3123 CG ASN B 898 99.908 63.778 6.020 1.00 45.34 C

ATOM 3124 ODl ASN B 898 98.737 63.393 6.172 1.00 42.95 O

ATOM 3125 ND2 ASN B 898 100.600 64.375 6.987 1.00 44.49 N

ATOM 3126 N TYR B 899 101.949 61.369 2.659 1.00 42.38 N

ATOM 3127 CA TYR B 899 102.768 61.140 1.480 1.00 42.65 C

ATOM 3128 C TYR B 899 102.046 60.196 0.536 1.00 43.32 C

ATOM 3129 O TYR B 899 102.268 60.215 -0.675 1.00 43.14 O

ATOM 3130 CB TYR B 899 104.140 60.584 1.883 1.00 41.69 C

ATOM 3131 CG TYR B 899 105.237 61.637 1.956 1.00 40.53 C

ATOM 3132 CDl TYR B 899 105.762 62.208 0.798 1.00 39.58 C

ATOM 3133 CD2 TYR B 899 105.756 62.049 3.182 1.00 40.31 C

ATOM 3134 CEl TYR B 899 106.782 63.166 0.860 1.00 41.96 C

ATOM 3135 CE2 TYR B 899 106.773 63.003 3.261 1.00 40.13 C

ATOM 3136 CZ TYR B 899 107.284 63.559 2.101 1.00 41.98 C

ATOM 3137 OH TYR B 899 108.292 64.501 2.175 1.00 41.66 O

ATOM 3138 N ILE B 900 101.166 59.378 1.098 1.00 44.33 N

ATOM 3139 CA ILE B 900 100.385 58.441 0.299 1.00 46.40 C

ATOM 3140 C ILE B 900 99.280 59.249 -0.367 1.00 46.26 C

ATOM 3141 O ILE B 900 98.954 59.040 -1.538 1.00 46.08 O

ATOM 3142 CB ILE B 900 99.731 57.324 1.182 1.00 47.11 C

ATOM 3143 CGl ILE B 900 100.824 56.446 1.808 1.00 48.42 C

ATOM 3144 CG2 ILE B 900 98.767 56.469 0.335 1.00 45.97 C

ATOM 3145 CDl ILE B 900 100.312 55.298 2.667 1.00 46.40 C

ATOM 3146 N LYS B 901 98.710 60.179 0.393 1.00 47.22 N

ATOM 3147 CA LYS B 901 97.639 61.013 -0.122 1.00 47.56 C

ATOM 3148 C LYS B 901 98.167 61.885 -1.238 1.00 47.31 C

ATOM 3149 O LYS B 901 97.441 62.209 -2.170 1.00 47.65 O

ATOM 3150 CB LYS B 901 97.042 61.861 1.003 1.00 48.68 C

ATOM 3151 CG LYS B 901 95.994 61.102 1.815 1.00 50.49 C

ATOM 3152 CD LYS B 901 95.623 61.793 3.122 1.00 52.29 C

ATOM 3153 CE LYS B 901 94.453 61.053 3.787 1.00 55.16 C

ATOM 3154 NZ LYS B 901 94.062 61.605 5.119 1.00 56.57 N

ATOM 3155 N GLU B 902 99.439 62.250 -1.144 1.00 46.77 N

ATOM 3156 CA GLU B 902 100.071 63.065 -2.168 1.00 47.95 C

ATOM 3157 C GLU B 902 100.095 62.268 -3.468 1.00 47.69 C

ATOM 3158 O GLU B 902 99.570 62.714 -4.487 1.00 47.53 O

ATOM 3381 N ASP B 937 115.184 39.564 -1.552 1.00 38.12 N

ATOM 3382 CA ASP B 937 116.076 38.601 -2.177 1.00 38.54 C

ATOM 3383 C ASP B 937 117.446 39.234 -2.443 1.00 36.88 C

ATOM 3384 O ASP B 937 118.451 38.548 -2.602 1.00 37.62 O

ATOM 3385 CB ASP B 937 115.447 38.062 -3.471 1.00 39.60 C

ATOM 3386 CG ASP B 937 114.249 37.167 -3.201 1.00 41.97 C

ATOM 3387 ODl ASP B 937 114.190 36.564 -2.105 1.00 42.36 O

ATOM 3388 OD2 ASP B 937 113.367 37.058 -4.082 1.00 43.73 O

ATOM 3389 N LEU B 938 117.483 40.555 -2.487 1.00 36.66 N

ATOM 3390 CA LEU B 938 118.743 41.261 -2.689 1.00 34.33 C

ATOM 3391 C LEU B 938 119.512 41.262 -1.362 1.00 33.23 C

ATOM 3392 O LEU B 938 120.719 41.011 -1.327 1.00 33.12 O

ATOM 3393 CB LEU B 938 118.477 42.703 -3.150 1.00 32.46 C

ATOM 3394 CG LEU B 938 117.888 42.872 -4.559 1.00 34.41 C

ATOM 3395 CDl LEU B 938 117.514 44.330 -4.820 1.00 31.83 C

ATOM 3396 CD2 LEU B 938 118.895 42.396 -5.592 1.00 31.99 C

ATOM 3397 N LEU B 939 118.807 41.539 -0.269 1.00 32.60 N

ATOM 3398 CA LEU B 939 119.436 41.574 1.045 1.00 33.76 C

ATOM 3399 C LEU B 939 120.007 40.207 1.415 1.00 34.71 C

ATOM 3400 O LEU B 939 121.076 40.126 2.016 1.00 34.69 O

ATOM 3401 CB LEU B 939 118.431 42.050 2.094 1.00 32.25 C

ATOM 3402 CG LEU B 939 117.974 43.500 1.897 1.00 31.20 C

ATOM 3403 CDl LEU B 939 116.683 43.726 2.651 1.00 28.65 C

ATOM 3404 CD2 LEU B 939 119.058 44.486 2.363 1.00 29.61 C

ATOM 3405 N GLU B 940 119.306 39.135 1.045 1.00 36.58 N

ATOM 3406 CA GLU B 940 119.772 37.767 1.318 1.00 37.84 C

ATOM 3407 C GLU B 940 121.084 37.527 0.585 1.00 38.43 C

ATOM 3408 O GLU B 940 122.093 37.117 1.178 1.00 38.87 O

ATOM 3409 CB GLU B 940 118.753 36.735 0.835 1.00 40.11 C

ATOM 3410 CG GLU B 940 117.643 36.383 1.824 1.00 43.87 C

ATOM 3411 CD GLU B 940 116.532 35.535 1.182 1.00 47.89 C

ATOM 3412 OEl GLU B 940 116.780 34.913 0.121 1.00 47.32 O

ATOM 3413 OE2 GLU B 940 115.408 35.482 1.742 1.00 48.80 O

ATOM 3414 N PHE B 941 121.070 37.775 -0.718 1.00 37.83 N

ATOM 3415 CA PHE B 941 122.274 37.588 -1.501 1.00 38.51 C

ATOM 3416 C PHE B 941 123.393 38.507 -0.996 1.00 38.95 C

ATOM 3417 O PHE B 941 124.572 38.172 -1.104 1.00 39.61 O

ATOM 3418 CB PHE B 941 122.005 37.876 -2.981 1.00 38.92 C

ATOM 3419 CG PHE B 941 123.178 37.573 -3.877 1.00 39.30 C

ATOM 3420 CDl PHE B 941 123.287 36.342 -4.515 1.00 39.84 C

ATOM 3421 CD2 PHE B 941 124.195 38.501 -4.048 1.00 37.14 C

ATOM 3422 CEl PHE B 941 124.395 36.048 -5.307 1.00 40.39 C

ATOM 3423 CE2 PHE B 941 125.303 38.216 -4.834 1.00 39.85 C

ATOM 3424 CZ PHE B 941 125.405 36.989 -5.465 1.00 39.71 C

ATOM 3425 N CYS B 942 123.022 39.665 -0.452 1.00 39.61 N

ATOM 3426 CA CYS B 942 123.996 40.628 0.056 1.00 40.66 C

ATOM 3427 C CYS B 942 124.570 40.180 1.412 1.00 40.79 C

ATOM 3428 O CYS B 942 125.779 40.237 1.627 1.00 40.52 O

ATOM 3429 CB CYS B 942 123.335 42.017 0.159 1.00 40.67 C

ATOM 3430 SG CYS B 942 124.407 43.420 0.709 1.00 44.59 S

ATOM 3431 N PHE B 943 123.697 39.731 2.313 1.00 41.95 N

ATOM 3432 CA PHE B 943 124.099 39.256 3.638 1.00 43.22 C

ATOM 3433 C PHE B 943 125.077 38.082 3.532 1.00 43.85 C

ATOM 3434 O PHE B 943 125.999 37.959 4.341 1.00 44.00 O

ATOM 3435 CB PHE B 943 122.861 38.810 4.433 1.00 43.39 C

ATOM 3436 CG PHE B 943 121.938 39.937 4.820 1.00 43.16 C

ATOM 3437 CDl PHE B 943 120.610 39.684 5.132 1.00 43.32 C

ATOM 3438 CD2 PHE B 943 122.399 41.247 4.879 1.00 42.99 C

ATOM 3439 CEl PHE B 943 119.752 40.713 5.495 1.00 44.66 C

ATOM 3440 CE2 PHE B 943 121.550 42.285 5.243 1.00 43.41 C

ATOM 3441 CZ PHE B 943 120.219 42.019 5.551 1.00 44.13 C

ATOM 3442 N TYR B 944 124.869 37.217 2.541 1.00 44.16 N

ATOM 3443 CA TYR B 944 125.727 36.050 2.340 1.00 45.23 C

ATOM 3444 C TYR B 944 127.070 36.490 1.816 1.00 46.61 C

ATOM 3445 O TYR B 944 128.123 36.112 2.340 1.00 46.27 O

ATOM 3446 CB TYR B 944 125.103 35.079 1.334 1.00 45.26 C

ATOM 3447 CG TYR B 944 126.073 34.028 0.824 1.00 45.64 C

ATOM 3448 CDl TYR B 944 126.498 34.029 -0.504 1.00 44.11 C

ATOM 3449 CD2 TYR B 944 126.587 33.048 1.679 1.00 45.21 C

ATOM 3450 CEl TYR B 944 127.408 33.087 -0.962 1.00 44.52 C

ATOM 3451 CE2 TYR B 944 127.491 32.106 1.224 1.00 44.69 C

ATOM 3452 CZ TYR B 944 127.897 32.131 -0.089 1.00 43.96 C

ATOM 3453 OH TYR B 944 128.801 31.192 -0.514 1.00 44.54 O

ATOM 3454 N THR B 945 127.009 37.278 0.752 1.00 47.29 N ATOM 3455 CA THR B 945 128.190 37.813 0.127 1.00 49.25 C

ATOM 3456 C THR B 945 128.980 38.615 1.168 1.00 50.71 C

ATOM 3457 O THR B 945 130.205 38.723 1.082 1.00 50.67 O

ATOM 3458 CB THR B 945 127.780 38.689 -1.075 1.00 50.26 C

ATOM 3459 OGl THR B 945 128.006 37.955 -2.289 1.00 51.45 O

ATOM 3460 CG2 THR B 945 128.552 39.980 -1.098 1.00 48.66 C

ATOM 3461 N PHE B 946 128.271 39.164 2.153 1.00 51.66 N

ATOM 3462 CA PHE B 946 128.887 39.940 3.225 1.00 52.38 C

ATOM 3463 C PHE B 946 129.596 39.013 4.208 1.00 53.03 C

ATOM 3464 O PHE B 946 130.770 39.200 4.500 1.00 53.13 O

ATOM 3465 CB PHE B 946 127.818 40.740 3.969 1.00 52.45 C

ATOM 3466 CG PHE B 946 128.345 41.539 5.125 1.00 51.19 C

ATOM 3467 CDl PHE B 946 129.109 42.672 4.900 1.00 51.12 C

ATOM 3468 CD2 PHE B 946 128.036 41.184 6.439 1.00 51.78 C

ATOM 3469 CEl PHE B 946 129.554 43.457 5.963 1.00 51.97 C

ATOM 3470 CE2 PHE B 946 128.474 41.958 7.513 1.00 51.74 C

ATOM 3471 CZ PHE B 946 129.235 43.099 7.275 1.00 51.82 C

ATOM 3472 N ARG B 947 128.876 38.025 4.730 1.00 54.43 N

ATOM 3473 CA ARG B 947 129.460 37.069 5.675 1.00 56.48 C

ATOM 3474 C ARG B 947 130.676 36.393 5.072 1.00 56.66 C

ATOM 3475 O ARG B 947 131.728 36.325 5.685 1.00 56.54 O

ATOM 3476 CB ARG B 947 128.453 35.977 6.045 1.00 57.75 C

ATOM 3477 CG ARG B 947 127.386 36.390 7.040 1.00 60.93 C

ATOM 3478 CD ARG B 947 128.020 37.049 8.252 1.00 63.59 C

ATOM 3479 NE ARG B 947 127.071 37.260 9.341 1.00 65.55 N

ATOM 3480 CZ ARG B 947 127.365 37.911 10.463 1.00 65.80 C

ATOM 3481 NHl ARG B 947 128.583 38.421 10.640 1.00 64.17 N

ATOM 3482 NH2 ARG B 947 126.443 38.051 11.409 1.00 66.32 N

ATOM 3483 N GLU B 948 130.505 35.895 3.854 1.00 58.42 N

ATOM 3484 CA GLU B 948 131.537 35.179 3.113 1.00 59.31 C

ATOM 3485 C GLU B 948 132.447 36.061 2.256 1.00 60.93 C

ATOM 3486 O GLU B 948 133.056 35.583 1.300 1.00 60.40 O

ATOM 3487 CB GLU B 948 130.856 34.130 2.229 1.00 58.42 C

ATOM 3488 CG GLU B 948 130.759 32.751 2.853 1.00 56.76 C

ATOM 3489 CD GLU B 948 132.092 32.022 2.818 1.00 56.74 C

ATOM 3490 OEl GLU B 948 132.993 32.360 3.624 1.00 57.33 O

ATOM 3491 OE2 GLU B 948 132.244 31.122 1.963 1.00 55.39 O

ATOM 3492 N SER B 949 132.546 37.340 2.613 1.00 63.13 N

ATOM 3493 CA SER B 949 133.365 38.307 1.873 1.00 64.79 C

ATOM 3494 C SER B 949 134.826 37.889 1.695 1.00 66.53 C

ATOM 3495 O SER B 949 135.398 38.005 0.604 1.00 67.08 O

ATOM 3496 CB SER B 949 133.316 39.667 2.567 1.00 63.19 C

ATOM 3497 OG SER B 949 134.068 40.622 1.845 1.00 63.26 O

ATOM 3498 N HIS B 950 135.434 37.426 2.779 1.00 67.51 N

ATOM 3499 CA HIS B 950 136.818 36.983 2.746 1.00 67.97 C

ATOM 3500 C HIS B 950 137.038 35.908 1.673 1.00 66.70 C

ATOM 3501 O HIS B 950 137.889 36.063 0.786 1.00 66.52 O

ATOM 3502 CB HIS B 950 137.213 36.457 4.133 1.00 70.56 C

ATOM 3503 CG HIS B 950 136.115 35.711 4.837 1.00 73.76 C

ATOM 3504 NDl HIS B 950 135.694 34.454 4.450 1.00 74.81 N

ATOM 3505 CD2 HIS B 950 135.356 36.046 5.910 1.00 74.75 C

ATOM 3506 CEl HIS B 950 134.727 34.048 5.254 1.00 74.40 C

ATOM 3507 NE2 HIS B 950 134.503 34.994 6.149 1.00 74.83 N

ATOM 3508 N ALA B 951 136.254 34.833 1.754 1.00 64.84 N

ATOM 3509 CA ALA B 951 136.350 33.715 0.819 1.00 62.96 C

ATOM 3510 C ALA B 951 135.946 34.063 -0.618 1.00 62.05 C

ATOM 3511 O ALA B 951 136.672 33.751 -1.558 1.00 62.12 O

ATOM 3512 CB ALA B 951 135.510 32.552 1.328 1.00 61.86 C

ATOM 3513 N LEU B 952 134.788 34.701 -0.779 1.00 60.95 N

ATOM 3514 CA LEU B 952 134.279 35.088 -2.096 1.00 59.73 C

ATOM 3515 C LEU B 952 135.124 36.178 -2.742 1.00 59.57 C

ATOM 3516 O LEU B 952 135.096 36.369 -3.962 1.00 59.49 O

ATOM 3517 CB LEU B 952 132.825 35.571 -1.980 1.00 58.60 C

ATOM 3518 CG LEU B 952 131.685 34.539 -1.982 1.00 58.00 C

ATOM 3519 CDl LEU B 952 131.923 33.453 -0.947 1.00 56.44 C

ATOM 3520 CD2 LEU B 952 130.373 35.263 -1.723 1.00 56.97 C

ATOM 3521 N LYS B 953 135.877 36.891 -1.912 1.00 59.80 N

ATOM 3522 CA LYS B 953 136.730 37.969 -2.387 1.00 59.96 C

ATOM 3523 C LYS B 953 135.865 39.076 -2.975 1.00 60.58 C

ATOM 3524 O LYS B 953 135.917 39.357 -4.176 1.00 60.59 O

ATOM 3525 CB LYS B 953 137.711 37.439 -3.433 1.00 59.53 C

ATOM 3526 N VAL B 954 135.064 39.692 -2.105 1.00 61.21 N

ATOM 3527 CA VAL B 954 134.161 40.777 -2.483 1.00 61.13 C

ATOM 3528 C VAL B 954 134.334 41.953 -1.515 1.00 61.22 C ATOM 3529 O VAL B 954 134.014 41.847 -0.326 1.00 61.78 O

ATOM 3530 CB VAL B 954 132.680 40.317 -2.434 1.00 60.87 C

ATOM 3531 CGl VAL B 954 131.758 41.487 -2.751 1.00 60.29 C

ATOM 3532 CG2 VAL B 954 132.451 39.176 -3.414 1.00 60.37 C

ATOM 3533 N GLU B 955 134.830 43.074 -2.031 1.00 60.45 N

ATOM 3534 CA GLU B 955 135.051 44.259 -1.213 1.00 60.17 C

ATOM 3535 C GLU B 955 133.770 45.022 -0.876 1.00 59.59 C

ATOM 3536 O GLU B 955 132.883 45.171 -1.718 1.00 60.22 O

ATOM 3537 CB GLU B 955 136.034 45.181 -1.914 1.00 60.42 C

ATOM 3538 N PHE B 956 133.690 45.505 0.362 1.00 58.42 N

ATOM 3539 CA PHE B 956 132.540 46.274 0.843 1.00 58.09 C

ATOM 3540 C PHE B 956 133.011 47.613 1.409 1.00 57.85 C

ATOM 3541 O PHE B 956 133.874 47.643 2.282 1.00 57.20 O

ATOM 3542 CB PHE B 956 131.812 45.534 1.965 1.00 57.33 C

ATOM 3543 CG PHE B 956 130.840 44.496 1.494 1.00 56.28 C

ATOM 3544 CDl PHE B 956 131.285 43.305 0.936 1.00 56.21 C

ATOM 3545 CD2 PHE B 956 129.472 44.694 1.655 1.00 56.84 C

ATOM 3546 CEl PHE B 956 130.385 42.320 0.542 1.00 56.61 C

ATOM 3547 CE2 PHE B 956 128.559 43.717 1.265 1.00 57.75 C

ATOM 3548 CZ PHE B 956 129.017 42.523 0.711 1.00 57.25 C

ATOM 3549 N PRO B 957 132.438 48.738 0.938 1.00 57.83 N

ATOM 3550 CA PRO B 957 132.844 50.058 1.444 1.00 58.06 C

ATOM 3551 C PRO B 957 132.566 50.169 2.947 1.00 58.29 C

ATOM 3552 O PRO B 957 131.598 49.591 3.450 1.00 59.02 O

ATOM 3553 CB PRO B 957 131.968 51.032 0.644 1.00 57.84 C

ATOM 3554 CG PRO B 957 131.581 50.258 -0.580 1.00 57.96 C

ATOM 3555 CD PRO B 957 131.348 48.874 -0.047 1.00 58.40 C

ATOM 3556 N ALA B 958 133.404 50.918 3.655 1.00 57.64 N

ATOM 3557 CA ALA B 958 133.238 51.101 5.092 1.00 58.29 C

ATOM 3558 C ALA B 958 131.808 51.517 5.453 1.00 58.86 C

ATOM 3559 O ALA B 958 131.256 51.067 6.466 1.00 58.19 O

ATOM 3560 CB ALA B 958 134.234 52.147 5.607 1.00 57.92 C

ATOM 3561 N MET B 959 131.211 52.382 4.633 1.00 59.34 N

ATOM 3562 CA MET B 959 129.846 52.839 4.882 1.00 59.58 C

ATOM 3563 C MET B 959 128.890 51.659 4.879 1.00 58.17 C

ATOM 3564 O MET B 959 128.139 51.458 5.826 1.00 57.24 O

ATOM 3565 CB MET B 959 129.420 53.860 3.819 1.00 62.24 C

ATOM 3566 CG MET B 959 127.903 53.967 3.595 1.00 65.57 C

ATOM 3567 SD MET B 959 126.928 54.733 4.928 1.00 70.94 S

ATOM 3568 CE MET B 959 126.204 56.151 4.066 1.00 66.98 C

ATOM 3569 N LEU B 960 128.930 50.875 3.811 1.00 57.14 N

ATOM 3570 CA LEU B 960 128.056 49.723 3.704 1.00 55.97 C

ATOM 3571 C LEU B 960 128.377 48.654 4.736 1.00 55.86 C

ATOM 3572 O LEU B 960 127.544 47.796 5.021 1.00 55.25 O

ATOM 3573 CB LEU B 960 128.126 49.148 2.294 1.00 55.65 C

ATOM 3574 CG LEU B 960 127.123 49.726 1.287 1.00 55.18 C

ATOM 3575 CDl LEU B 960 126.996 51.230 1.432 1.00 53.85 C

ATOM 3576 CD2 LEU B 960 127.582 49.363 -0.112 1.00 55.93 C

ATOM 3577 N VAL B 961 129.579 48.702 5.302 1.00 55.57 N

ATOM 3578 CA VAL B 961 129.954 47.728 6.316 1.00 55.25 C

ATOM 3579 C VAL B 961 129.169 48.028 7.588 1.00 55.21 C

ATOM 3580 O VAL B 961 128.602 47.128 8.208 1.00 54.85 O

ATOM 3581 CB VAL B 961 131.475 47.778 6.640 1.00 55.80 C

ATOM 3582 CGl VAL B 961 131.769 46.966 7.905 1.00 55.68 C

ATOM 3583 CG2 VAL B 961 132.285 47.212 5.479 1.00 54.86 C

ATOM 3584 N GLU B 962 129.127 49.301 7.965 1.00 54.93 N

ATOM 3585 CA GLU B 962 128.419 49.713 9.168 1.00 55.82 C

ATOM 3586 C GLU B 962 126.896 49.649 9.046 1.00 55.83 C

ATOM 3587 O GLU B 962 126.177 49.676 10.047 1.00 56.87 O

ATOM 3588 CB GLU B 962 128.859 51.120 9.571 1.00 55.31 C

ATOM 3589 CG GLU B 962 130.325 51.192 9.932 1.00 55.66 C

ATOM 3590 CD GLU B 962 130.732 52.539 10.499 1.00 55.78 C

ATOM 3591 OEl GLU B 962 131.894 52.659 10.942 1.00 55.08 O

ATOM 3592 OE2 GLU B 962 129.899 53.471 10.505 1.00 55.74 O

ATOM 3593 N ILE B 963 126.391 49.559 7.827 1.00 55.62 N

ATOM 3594 CA ILE B 963 124.947 49.481 7.650 1.00 55.65 C

ATOM 3595 C ILE B 963 124.460 48.045 7.704 1.00 53.89 C

ATOM 3596 O ILE B 963 123.465 47.747 8.356 1.00 53.91 O

ATOM 3597 CB ILE B 963 124.501 50.077 6.301 1.00 55.88 C

ATOM 3598 CGl ILE B 963 124.611 51.600 6.349 1.00 55.43 C

ATOM 3599 CG2 ILE B 963 123.086 49.609 5.975 1.00 54.92 C

ATOM 3600 CDl ILE B 963 124.122 52.290 5.093 1.00 57.28 C

ATOM 3601 N ILE B 964 125.182 47.173 7.010 1.00 53.64 N

ATOM 3602 CA ILE B 964 124.854 45.756 6.903 1.00 53.84 C ATOM 3603 C ILE B 964 125.136 44.936 8.164 1.00 54.30 C

ATOM 3604 O ILE B 964 124.423 43.981 8.449 1.00 53.90 O

ATOM 3605 CB ILE B 964 125.605 45.131 5.701 1.00 53.60 C

ATOM 3606 CGl ILE B 964 125.337 45.964 4.442 1.00 53.00 C

ATOM 3607 CG2 ILE B 964 125.145 43.700 5.470 1.00 53.43 C

ATOM 3608 CDl ILE B 964 126.077 45.493 3.213 1.00 52.76 C

ATOM 3609 N SER B 965 126.165 45.309 8.916 1.00 54.29 N

ATOM 3610 CA SER B 965 126.509 44.595 10.140 1.00 54.67 C

ATOM 3611 C SER B 965 125.465 44.921 11.192 1.00 55.69 C

ATOM 3612 O SER B 965 125.361 44.260 12.227 1.00 55.74 O

ATOM 3613 CB SER B 965 127.868 45.043 10.654 1.00 54.36 C

ATOM 3614 OG SER B 965 127.686 45.970 11.699 1.00 54.52 O

ATOM 3615 N ASP B 966 124.690 45.956 10.915 1.00 57.30 N

ATOM 3616 CA ASP B 966 123.653 46.393 11.830 1.00 58.89 C

ATOM 3617 C ASP B 966 122.294 45.821 11.404 1.00 59.41 C

ATOM 3618 O ASP B 966 121.520 45.325 12.228 1.00 59.40 O

ATOM 3619 CB ASP B 966 123.606 47.917 11.827 1.00 59.66 C

ATOM 3620 CG ASP B 966 123.274 48.491 13.177 1.00 61.24 C

ATOM 3621 ODl ASP B 966 122.251 48.078 13.761 1.00 62.53 O

ATOM 3622 OD2 ASP B 966 124.032 49.365 13.649 1.00 62.10 O

ATOM 3623 N GLN B 967 122.034 45.877 10.101 1.00 59.79 N

ATOM 3624 CA GLN B 967 120.781 45.415 9.505 1.00 59.67 C

ATOM 3625 C GLN B 967 120.587 43.883 9.396 1.00 59.13 C

ATOM 3626 O GLN B 967 119.453 43.401 9.431 1.00 57.87 O

ATOM 3627 CB GLN B 967 120.643 46.081 8.120 1.00 60.37 C

ATOM 3628 CG GLN B 967 119.591 45.484 7.184 1.00 60.44 C

ATOM 3629 CD GLN B 967 119.720 46.002 5.760 1.00 59.98 C

ATOM 3630 OEl GLN B 967 118.720 46.205 5.066 1.00 60.47 O

ATOM 3631 NE2 GLN B 967 120.951 46.228 5.322 1.00 58.76 N

ATOM 3632 N LEU B 968 121.686 43.134 9.290 1.00 58.98 N

ATOM 3633 CA LEU B 968 121.648 41.674 9.135 1.00 59.08 C

ATOM 3634 C LEU B 968 120.970 40.860 10.247 1.00 59.74 C

ATOM 3635 O LEU B 968 120.162 39.973 9.956 1.00 59.79 O

ATOM 3636 CB LEU B 968 123.075 41.147 8.883 1.00 58.69 C

ATOM 3637 CG LEU B 968 123.392 39.655 8.669 1.00 58.05 C

ATOM 3638 CDl LEU B 968 122.456 39.038 7.641 1.00 59.23 C

ATOM 3639 CD2 LEU B 968 124.846 39.518 8.226 1.00 58.49 C

ATOM 3640 N PRO B 969 121.305 41.122 11.525 1.00 60.22 N

ATOM 3641 CA PRO B 969 120.690 40.383 12.639 1.00 60.76 C

ATOM 3642 C PRO B 969 119.317 40.967 12.972 1.00 61.17 C

ATOM 3643 O PRO B 969 118.483 40.325 13.608 1.00 61.79 O

ATOM 3644 CB PRO B 969 121.691 40.576 13.769 1.00 60.47 C

ATOM 3645 CG PRO B 969 122.168 41.967 13.525 1.00 61.12 C

ATOM 3646 CD PRO B 969 122.388 41.992 12.017 1.00 60.62 C

ATOM 3647 N LYS B 970 119.100 42.197 12.527 1.00 62.06 N

ATOM 3648 CA LYS B 970 117.843 42.897 12.734 1.00 63.45 C

ATOM 3649 C LYS B 970 116.788 42.262 11.829 1.00 64.71 C

ATOM 3650 O LYS B 970 115.657 42.006 12.245 1.00 65.60 O

ATOM 3651 CB LYS B 970 118.026 44.361 12.362 1.00 63.97 C

ATOM 3652 CG LYS B 970 117.290 45.347 13.241 1.00 65.27 C

ATOM 3653 CD LYS B 970 117.857 45.394 14.664 1.00 65.68 C

ATOM 3654 CE LYS B 970 117.394 44.208 15.517 1.00 65.16 C

ATOM 3655 NZ LYS B 970 117.612 44.459 16.968 1.00 63.29 N

ATOM 3656 N VAL B 971 117.183 42.004 10.585 1.00 65.83 N

ATOM 3657 CA VAL B 971 116.311 41.396 9.578 1.00 66.57 C

ATOM 3658 C VAL B 971 116.142 39.898 9.829 1.00 66.87 C

ATOM 3659 O VAL B 971 115.027 39.393 9.971 1.00 67.22 O

ATOM 3660 CB VAL B 971 116.900 41.574 8.144 1.00 66.82 C

ATOM 3661 CGl VAL B 971 115.963 40.964 7.114 1.00 66.91 C

ATOM 3662 CG2 VAL B 971 117.134 43.053 7.841 1.00 66.76 C

ATOM 3663 N GLU B 972 117.268 39.196 9.874 1.00 67.19 N

ATOM 3664 CA GLU B 972 117.289 37.757 10.085 1.00 67.84 C

ATOM 3665 C GLU B 972 116.503 37.300 11.324 1.00 67.70 C

ATOM 3666 O GLU B 972 116.046 36.156 11.380 1.00 67.40 O

ATOM 3667 CB GLU B 972 118.746 37.283 10.179 1.00 68.70 C

ATOM 3668 CG GLU B 972 119.186 36.297 9.085 1.00 69.71 C

ATOM 3669 CD GLU B 972 118.962 36.814 7.666 1.00 70.77 C

ATOM 3670 OEl GLU B 972 117.809 37.181 7.335 1.00 70.54 O

ATOM 3671 OE2 GLU B 972 119.941 36.845 6.885 1.00 69.09 O

ATOM 3672 N SER B 973 116.345 38.192 12.303 1.00 67.24 N

ATOM 3673 CA SER B 973 115.625 37.868 13.538 1.00 66.63 C

ATOM 3674 C SER B 973 114.118 38.028 13.379 1.00 66.56 C

ATOM 3675 O SER B 973 113.338 37.521 14.187 1.00 67.15 O

ATOM 3676 CB SER B 973 116.104 38.761 14.687 1.00 66.19 C ATOM 3677 OG SER B 973 115.248 39.874 14.868 1.00 65.38 O

ATOM 3678 N GLY B 974 113.722 38.896 12.456 1.00 66.07 N

ATOM 3679 CA GLY B 974 112.314 39.135 12.212 1.00 65.16 C

ATOM 3680 C GLY B 974 111.854 40.473 12.758 1.00 64.76 C

ATOM 3681 O GLY B 974 110.663 40.779 12.741 1.00 64.78 O

ATOM 3682 N ASN B 975 112.791 41.283 13.235 1.00 64.47 N

ATOM 3683 CA ASN B 975 112.436 42.577 13.794 1.00 64.10 C

ATOM 3684 C ASN B 975 112.128 43.636 12.745 1.00 63.27 C

ATOM 3685 O ASN B 975 111.801 44.775 13.076 1.00 64.12 O

ATOM 3686 CB ASN B 975 113.535 43.054 14.739 1.00 65.41 C

ATOM 3687 CG ASN B 975 113.351 42.515 16.143 1.00 66.35 C

ATOM 3688 ODl ASN B 975 112.283 42.670 16.734 1.00 66.89 O

ATOM 3689 ND2 ASN B 975 114.391 41.880 16.685 1.00 66.14 N

ATOM 3690 N ALA B 976 112.213 43.255 11.479 1.00 61.72 N

ATOM 3691 CA ALA B 976 111.911 44.179 10.400 1.00 60.14 C

ATOM 3692 C ALA B 976 110.431 44.042 10.089 1.00 59.47 C

ATOM 3693 O ALA B 976 109.928 42.933 9.962 1.00 59.15 O

ATOM 3694 CB ALA B 976 112.732 43.836 9.173 1.00 61.32 C

ATOM 3695 N LYS B 977 109.730 45.164 9.982 1.00 58.82 N

ATOM 3696 CA LYS B 977 108.310 45.128 9.673 1.00 58.52 C

ATOM 3697 C LYS B 977 108.016 45.907 8.394 1.00 58.51 C

ATOM 3698 O LYS B 977 107.972 47.141 8.396 1.00 58.89 O

ATOM 3699 CB LYS B 977 107.497 45.699 10.836 1.00 58.45 C

ATOM 3700 CG LYS B 977 105.998 45.623 10.627 1.00 55.98 C

ATOM 3701 CD LYS B 977 105.275 45.690 11.958 1.00 56.78 C

ATOM 3702 CE LYS B 977 103.773 45.532 11.794 1.00 55.79 C

ATOM 3703 NZ LYS B 977 103.189 46.682 11.053 1.00 55.95 N

ATOM 3704 N PRO B 978 107.816 45.193 7.277 1.00 57.61 N

ATOM 3705 CA PRO B 978 107.530 45.876 6.015 1.00 56.65 C

ATOM 3706 C PRO B 978 106.065 46.266 5.957 1.00 55.56 C

ATOM 3707 O PRO B 978 105.193 45.437 6.195 1.00 55.60 O

ATOM 3708 CB PRO B 978 107.865 44.824 4.956 1.00 57.81 C

ATOM 3709 CG PRO B 978 108.674 43.776 5.704 1.00 58.14 C

ATOM 3710 CD PRO B 978 108.023 43.756 7.050 1.00 57.45 C

ATOM 3711 N LEU B 979 105.794 47.528 5.652 1.00 54.74 N

ATOM 3712 CA LEU B 979 104.421 47.992 5.545 1.00 54.03 C

ATOM 3713 C LEU B 979 103.958 47.716 4.111 1.00 53.53 C

ATOM 3714 O LEU B 979 104.634 48.084 3.147 1.00 53.68 O

ATOM 3715 CB LEU B 979 104.356 49.480 5.875 1.00 54.41 C

ATOM 3716 CG LEU B 979 105.016 49.835 7.212 1.00 54.98 C

ATOM 3717 CDl LEU B 979 104.931 51.341 7.452 1.00 55.24 C

ATOM 3718 CD2 LEU B 979 104.336 49.072 8.338 1.00 55.40 C

ATOM 3719 N TYR B 980 102.814 47.048 3.981 1.00 52.92 N

ATOM 3720 CA TYR B 980 102.258 46.678 2.675 1.00 52.49 C

ATOM 3721 C TYR B 980 100.969 47.409 2.322 1.00 51.45 C

ATOM 3722 O TYR B 980 100.129 47.651 3.191 1.00 51.49 O

ATOM 3723 CB TYR B 980 101.995 45.171 2.633 1.00 52.41 C

ATOM 3724 CG TYR B 980 103.225 44.346 2.359 1.00 53.92 C

ATOM 3725 CDl TYR B 980 103.699 44.191 1.057 1.00 53.70 C

ATOM 3726 CD2 TYR B 980 103.938 43.747 3.398 1.00 54.22 C

ATOM 3727 CEl TYR B 980 104.851 43.464 0.791 1.00 53.70 C

ATOM 3728 CE2 TYR B 980 105.100 43.019 3.141 1.00 55.06 C

ATOM 3729 CZ TYR B 980 105.551 42.887 1.831 1.00 54.50 C

ATOM 3730 OH TYR B 980 106.718 42.208 1.556 1.00 55.72 O

ATOM 3731 N PHE B 981 100.816 47.746 1.042 1.00 50.11 N

ATOM 3732 CA PHE B 981 99.623 48.447 0.564 1.00 49.08 C

ATOM 3733 C PHE B 981 98.518 47.468 0.171 1.00 49.36 C

ATOM 3734 O PHE B 981 97.335 47.805 0.187 1.00 48.66 O

ATOM 3735 CB PHE B 981 99.986 49.333 -0.630 1.00 48.46 C

ATOM 3736 CG PHE B 981 100.662 50.616 -0.243 1.00 47.43 C

ATOM 3737 CDl PHE B 981 99.929 51.779 -0.101 1.00 46.73 C

ATOM 3738 CD2 PHE B 981 102.017 50.642 0.057 1.00 47.63 C

ATOM 3739 CEl PHE B 981 100.530 52.945 0.334 1.00 46.82 C

ATOM 3740 CE2 PHE B 981 102.623 51.807 0.493 1.00 46.28 C

ATOM 3741 CZ PHE B 981 101.875 52.958 0.634 1.00 46.47 C

ATOM 3742 N HIS B 982 98.921 46.248 -0.165 1.00 48.57 N

ATOM 3743 CA HIS B 982 97.987 45.210 -0.582 1.00 49.03 C

ATOM 3744 C HIS B 982 98.469 43.839 -0.109 1.00 50.51 C

ATOM 3745 O HIS B 982 99.344 43.551 0.483 1.00 52.00 O

ATOM 3746 CB HIS B 982 97.868 45.207 -2.107 1.00 46.74 C

ATOM 3747 CG HIS B 982 97.522 46.541 -2.693 1.00 44.11 C

ATOM 3748 NDl HIS B 982 96.291 47.137 -2.516 1.00 44.39 N

ATOM 3749 CD2 HIS B 982 98.234 47.378 -3.484 1.00 42.51 C

ATOM 3750 CEl HIS B 982 96.258 48.280 -3.178 1.00 43.02 C ATOM 3751 NE2 HIS B 982 97.424 48.448 -3.775 1.00 42.86 N

TER 3752 HIS B 982

ATOM 3753 N SER C 737 44.481 40.777 -10.876 1.00 63.01 N

ATOM 3754 CA SER C 737 45.486 40.886 -9.778 1.00 63.64 C

ATOM 3755 C SER C 737 45.908 39.517 -9.254 1.00 63.18 C

ATOM 3756 O SER C 737 47.026 39.075 -9.537 1.00 63.81 O

ATOM 3757 CB SER C 737 44.943 41.747 -8.627 1.00 64.86 C

ATOM 3758 OG SER C 737 45.609 41.446 -7.410 1.00 64.36 O

ATOM 3759 N PRO C 738 45.033 38.823 -8.484 1.00 62.74 N

ATOM 3760 CA PRO C 738 45.423 37.500 -7.972 1.00 61.38 C

ATOM 3761 C PRO C 738 45.994 36.615 -9.074 1.00 59.76 C

ATOM 3762 O PRO C 738 47.053 36.009 -8.927 1.00 59.07 O

ATOM 3763 CB PRO C 738 44.115 36.954 -7.409 1.00 60.91 C

ATOM 3764 CG PRO C 738 43.461 38.188 -6.890 1.00 61.54 C

ATOM 3765 CD PRO C 738 43.672 39.162 -8.029 1.00 61.38 C

ATOM 3766 N VAL C 739 45.285 36.558 -10.189 1.00 58.51 N

ATOM 3767 CA VAL C 739 45.728 35.756 -11.307 1.00 57.36 C

ATOM 3768 C VAL C 739 46.986 36.359 -11.929 1.00 56.53 C

ATOM 3769 O VAL C 739 47.868 35.638 -12.392 1.00 56.74 O

ATOM 3770 CB VAL C 739 44.610 35.640 -12.360 1.00 57.92 C

ATOM 3771 CGl VAL C 739 44.020 37.016 -12.645 1.00 58.98 C

ATOM 3772 CG2 VAL C 739 45.152 35.002 -13.628 1.00 59.29 C

ATOM 3773 N MET C 740 47.084 37.682 -11.903 1.00 56.31 N

ATOM 3774 CA MET C 740 48.230 38.376 -12.484 1.00 54.49 C

ATOM 3775 C MET C 740 49.543 38.058 -11.767 1.00 53.54 C

ATOM 3776 O MET C 740 50.573 37.828 -12.415 1.00 53.33 O

ATOM 3777 CB MET C 740 47.968 39.880 -12.475 1.00 55.12 C

ATOM 3778 CG MET C 740 49.104 40.728 -13.015 1.00 56.55 C

ATOM 3779 SD MET C 740 48.573 42.436 -13.360 1.00 58.05 S

ATOM 3780 CE MET C 740 48.047 42.270 -15.054 1.00 58.28 C

ATOM 3781 N VAL C 741 49.515 38.052 -10.436 1.00 52.26 N

ATOM 3782 CA VAL C 741 50.713 37.745 -9.662 1.00 51.84 C

ATOM 3783 C VAL C 741 51.117 36.303 -9.897 1.00 51.69 C

ATOM 3784 O VAL C 741 52.297 35.993 -10.063 1.00 50.01 O

ATOM 3785 CB VAL C 741 50.503 37.982 -8.142 1.00 52.53 C

ATOM 3786 CGl VAL C 741 49.188 38.696 -7.899 1.00 51.96 C

ATOM 3787 CG2 VAL C 741 50.545 36.645 -7.386 1.00 52.17 C

ATOM 3788 N LEU C 742 50.126 35.421 -9.918 1.00 52.13 N

ATOM 3789 CA LEU C 742 50.392 34.018 -10.155 1.00 53.31 C

ATOM 3790 C LEU C 742 51.169 33.809 -11.452 1.00 54.05 C

ATOM 3791 O LEU C 742 52.061 32.967 -11.515 1.00 55.16 O

ATOM 3792 CB LEU C 742 49.079 33.237 -10.215 1.00 52.82 C

ATOM 3793 CG LEU C 742 48.357 33.034 -8.884 1.00 52.30 C

ATOM 3794 CDl LEU C 742 47.111 32.181 -9.103 1.00 52.50 C

ATOM 3795 CD2 LEU C 742 49.304 32.360 -7.892 1.00 51.44 C

ATOM 3796 N GLU C 743 50.831 34.577 -12.482 1.00 54.77 N

ATOM 3797 CA GLU C 743 51.493 34.450 -13.775 1.00 55.99 C

ATOM 3798 C GLU C 743 52.917 34.990 -13.722 1.00 55.54 C

ATOM 3799 O GLU C 743 53.770 34.607 -14.526 1.00 55.45 O

ATOM 3800 CB GLU C 743 50.689 35.197 -14.839 1.00 58.02 C

ATOM 3801 CG GLU C 743 49.221 34.799 -14.883 1.00 62.01 C

ATOM 3802 CD GLU C 743 48.398 35.681 -15.820 1.00 65.24 C

ATOM 3803 OEl GLU C 743 47.149 35.538 -15.845 1.00 65.70 O

ATOM 3804 OE2 GLU C 743 49.003 36.514 -16.534 1.00 65.63 O

ATOM 3805 N ASN C 744 53.168 35.873 -12.760 1.00 55.17 N

ATOM 3806 CA ASN C 744 54.480 36.479 -12.593 1.00 54.39 C

ATOM 3807 C ASN C 744 55.462 35.559 -11.882 1.00 53.96 C

ATOM 3808 O ASN C 744 56.593 35.380 -12.341 1.00 54.20 O

ATOM 3809 CB ASN C 744 54.358 37.789 -11.802 1.00 56.24 C

ATOM 3810 CG ASN C 744 55.672 38.571 -11.741 1.00 57.23 C

ATOM 3811 ODl ASN C 744 56.760 37.994 -11.680 1.00 57.12 O

ATOM 3812 ND2 ASN C 744 55.569 39.892 -11.749 1.00 57.64 N

ATOM 3813 N ILE C 745 55.031 34.983 -10.762 1.00 52.69 N

ATOM 3814 CA ILE C 745 55.888 34.107 -9.971 1.00 51.91 C

ATOM 3815 C ILE C 745 56.020 32.710 -10.545 1.00 52.55 C

ATOM 3816 O ILE C 745 56.661 31.847 -9.950 1.00 52.37 O

ATOM 3817 CB ILE C 745 55.387 33.991 -8.524 1.00 51.07 C

ATOM 3818 CGl ILE C 745 54.190 33.030 -8.452 1.00 51.27 C

ATOM 3819 CG2 ILE C 745 55.016 35.371 -8.008 1.00 51.01 C

ATOM 3820 CDl ILE C 745 53.547 32.921 -7.065 1.00 50.54 C

ATOM 3821 N GLU C 746 55.420 32.485 -11.705 1.00 52.85 N

ATOM 3822 CA GLU C 746 55.506 31.178 -12.334 1.00 53.91 C

ATOM 3823 C GLU C 746 56.959 30.878 -12.672 1.00 54.38 C

ATOM 3824 O GLU C 746 57.680 31.755 -13.148 1.00 54.20 O

ATOM 4047 CG2 VAL C 781 60.448 26.166 -0.781 1.00 46.96 C

ATOM 4048 N LYS C 782 60.274 27.934 -4.367 1.00 46.64 N

ATOM 4049 CA LYS C 782 60.505 29.355 -4.620 1.00 47.30 C

ATOM 4050 C LYS C 782 59.191 29.984 -5.081 1.00 46.60 C

ATOM 4051 O LYS C 782 58.886 31.137 -4.757 1.00 45.59 O

ATOM 4052 CB LYS C 782 61.591 29.554 -5.691 1.00 48.81 C

ATOM 4053 CG LYS C 782 62.940 30.081 -5.151 1.00 52.33 C

ATOM 4054 CD LYS C 782 64.096 29.105 -5.453 1.00 52.97 C

ATOM 4055 CE LYS C 782 65.476 29.791 -5.521 1.00 54.24 C

ATOM 4056 NZ LYS C 782 66.652 28.890 -5.317 1.00 54.83 N

ATOM 4057 N TRP C 783 58.416 29.202 -5.837 1.00 45.58 N

ATOM 4058 CA TRP C 783 57.117 29.617 -6.368 1.00 43.19 C

ATOM 4059 C TRP C 783 56.086 29.791 -5.268 1.00 42.27 C

ATOM 4060 O TRP C 783 55.298 30.730 -5.287 1.00 40.95 O

ATOM 4061 CB TRP C 783 56.604 28.564 -7.355 1.00 42.75 C

ATOM 4062 CG TRP C 783 55.131 28.655 -7.690 1.00 42.85 C

ATOM 4063 CDl TRP C 783 54.529 29.581 -8.487 1.00 41.75 C

ATOM 4064 CD2 TRP C 783 54.089 27.754 -7.264 1.00 41.58 C

ATOM 4065 NEl TRP C 783 53.182 29.312 -8.591 1.00 40.94 N

ATOM 4066 CE2 TRP C 783 52.887 28.200 -7.852 1.00 39.96 C

ATOM 4067 CE3 TRP C 783 54.062 26.610 -6.451 1.00 41.86 C

ATOM 4068 CZ2 TRP C 783 51.663 27.546 -7.652 1.00 42.08 C

ATOM 4069 CZ3 TRP C 783 52.845 25.952 -6.253 1.00 42.84 C

ATOM 4070 CH2 TRP C 783 51.660 26.425 -6.853 1.00 43.33 C

ATOM 4071 N ALA C 784 56.100 28.872 -4.313 1.00 42.66 N

ATOM 4072 CA ALA C 784 55.147 28.887 -3.214 1.00 43.15 C

ATOM 4073 C ALA C 784 55.406 29.923 -2.126 1.00 43.01 C

ATOM 4074 O ALA C 784 54.485 30.275 -1.384 1.00 43.30 O

ATOM 4075 CB ALA C 784 55.061 27.497 -2.595 1.00 42.39 C

ATOM 4076 N LYS C 785 56.639 30.410 -2.028 1.00 42.83 N

ATOM ^' 4077 CA LYS C 785 56.985 31.396 -1.002 1.00 44.25 C

ATOM 4078 C LYS C 785 56.426 32.765 -1.335 1.00 44.66 C

ATOM 4079 O LYS C 785 56.299 33.613 -0.462 1.00 46.99 O

ATOM 4080 CB LYS C 785 58.501 31.501 -0.841 1.00 45.46 C

ATOM 4081 CG LYS C 785 59.267 31.513 -2.149 1.00 49.32 C

ATOM 4082 CD LYS C 785 60.740 31.843 -1.917 1.00 51.81 C

ATOM 4083 CE LYS C 785 60.915 32.864 -0.804 1.00 53.39 C

ATOM 4084 NZ LYS C 785 62.360 33.114 -0.559 1.00 55.10 N

ATOM 4085 N VAL C 786 56.100 32.978 -2.604 1.00 43.88 N

ATOM 4086 CA VAL C 786 55.536 34.243 -3.049 1.00 43.65 C

ATOM 4087 C VAL C 786 54.053 34.057 -3.362 1.00 44.05 C

ATOM 4088 O VAL C 786 53.391 34.972 -3.843 1.00 42.87 O

ATOM 4089 CB VAL C 786 56.262 34.758 -4.300 1.00 42.97 C

ATOM 4090 CGl VAL C 786 57.666 35.237 -3.923 1.00 41.07 C

ATOM 4091 CG2 VAL C 786 56.352 33.653 -5.330 1.00 39.48 C

ATOM 4092 N LEU C 787 53.550 32.858 -3.072 1.00 44.10 N

ATOM 4093 CA LEU C 787 52.159 32.497 -3.310 1.00 44.47 C

ATOM 4094 C LEU C 787 51.211 33.292 -2.427 1.00 44.38 C

ATOM 4095 O LEU C 787 51.260 33.190 -1.202 1.00 45.51 O

ATOM 4096 CB LEU C 787 51.949 31.007 -3.025 1.00 44.54 C

ATOM 4097 CG LEU C 787 50.945 30.233 -3.880 1.00 44.76 C

ATOM 4098 CDl LEU C 787 50.652 31.009 -5.160 1.00 45.38 C

ATOM 4099 CD2 LEU C 787 51.496 28.858 -4.183 1.00 43.54 C

ATOM 4100 N PRO C 788 50.326 34.088 -3.034 1.00 42.92 N

ATOM 4101 CA PRO C 788 49.380 34.873 -2.241 1.00 42.46 C

ATOM 4102 C PRO C 788 48.560 33.958 -1.323 1.00 42.00 C

ATOM 4103 O PRO C 788 48.026 32.931 -1.768 1.00 40.36 O

ATOM 4104 CB PRO C 788 48.511 35.545 -3.305 1.00 42.67 C

ATOM 4105 CG PRO C 788 49.440 35.683 -4.470 1.00 43.23 C

ATOM 4106 CD PRO C 788 50.167 34.357 -4.472 1.00 43.64 C

ATOM 4107 N GLY C 789 48.464 34.342 -0.051 1.00 42.31 N

ATOM 4108 CA GLY C 789 47.722 33.560 0.923 1.00 43.71 C

ATOM 4109 C GLY C 789 48.600 32.498 1.561 1.00 46.00 C

ATOM 4110 O GLY C 789 48.904 32.547 2.758 1.00 46.64 O

ATOM 4111 N PHE C 790 49.007 31.532 0.748 1.00 45.93 N

ATOM 4112 CA PHE C 790 49.857 30.447 1.201 1.00 47.47 C

ATOM 4113 C PHE C 790 51.154 31.019 1.759 1.00 48.02 C

ATOM 4114 O PHE C 790 51.783 30.432 2.639 1.00 47.35 O

ATOM 4115 CB PHE C 790 50.158 29.531 0.027 1.00 46.76 C

ATOM 4116 CG PHE C 790 50.995 28.358 0.383 1.00 45.79 C

ATOM 4117 CDl PHE C 790 50.425 27.239 0.972 1.00 45.63 C

ATOM 4118 CD2 PHE C 790 52.361 28.369 0.133 1.00 46.41 C

ATOM 4119 CEl PHE C 790 51.206 26.148 1.307 1.00 45.47 C

ATOM 4120 CE2 PHE C 790 53.154 27.278 0.466 1.00 45.42 C

ATOM 4195 CDl ILE C 799 58.537 24.589 4.336 1.00 40.75 C

ATOM 4196 N THR C 800 54.379 21.188 5.032 1.00 42.75 N

ATOM 4197 CA THR C 800 53.542 19.986 5.105 1.00 42.82 C

ATOM 4198 C THR C 800 52.737 19.876 3.811 1.00 41.12 C

ATOM 4199 O THR C 800 52.555 18.797 3.267 1.00 41.10 O

ATOM 4200 CB THR C 800 52.556 20.049 6.311 1.00 44.11 C

ATOM 4201 OGl THR C 800 53.238 19.693 7.521 1.00 45.18 O

ATOM 4202 CG2 THR C 800 51.412 19.086 6.108 1.00 44.43 C

ATOM 4203 N LEU C 801 52.262 21.014 3.320 1.00 41.10 N

ATOM 4204 CA LEU C 801 51.488 21.057 2.091 1.00 40.00 C

ATOM 4205 C LEU C 801 52.339 20.719 0.864 1.00 39.54 C

ATOM 4206 O LEU C 801 51.918 19.952 -0.001 1.00 37.61 O

ATOM 4207 CB LEU C 801 50.828 22.443 1.952 1.00 40.89 C

ATOM 4208 CG LEU C 801 49.522 22.645 2.751 1.00 39.93 C

ATOM 4209 CDl LEU C 801 48.846 23.950 2.349 1.00 40.29 C

ATOM 4210 CD2 LEU C 801 48.582 21.472 2.542 1.00 40.57 C

ATOM 4211 N ILE C 802 53.543 21.282 0.791 1.00 40.22 N

ATOM 4212 CA ILE C 802 54.435 21.008 -0.333 1.00 41.29 C

ATOM 4213 C ILE C 802 54.831 19.520 -0.364 1.00 42.05 C

ATOM 4214 O ILE C 802 54.851 18.905 -1.425 1.00 42.29 O

ATOM 4215 CB ILE C 802 55.719 21.872 -0.253 1.00 40.95 C

ATOM 4216 CGl ILE C 802 55.356 23.358 -0.260 1.00 40.97 C

ATOM 4217 CG2 ILE C 802 56.624 21.591 -1.448 1.00 40.27 C

ATOM 4218 CDl ILE C 802 56.543 24.271 -0.062 1.00 39.36 C

ATOM 4219 N GLN C 803 55.137 18.948 0.800 1.00 43.04 N

ATOM 4220 CA GLN C 803 55.543 17.542 0.893 1.00 44.19 C

ATOM 4221 C GLN C 803 54.413 16.599 0.490 1.00 44.96 C

ATOM 4222 O GLN C 803 54.620 15.663 -0.284 1.00 43.88 O

ATOM 4223 CB GLN C 803 55.994 17.206 2.319 1.00 44.33 C

ATOM 4224 CG GLN C 803 57.391 17.699 2.678 1.00 46.96 C

ATOM 4225 CD GLN C 803 57.732 17.495 4.158 1.00 48.59 C

ATOM 4226 OEl GLN C 803 56.882 17.093 4.951 1.00 50.26 O

ATOM 4227 NE2 GLN C 803 58.983 17.764 4.526 1.00 48.58 N

ATOM 4228 N TYR C 804 53.221 16.856 1.027 1.00 45.02 N

ATOM 4229 CA TYR C 804 52.055 16.046 0.732 1.00 45.12 C

ATOM 4230 C TYR C 804 51.654 16.089 -0.735 1.00 43.87 C

ATOM 4231 O TYR C 804 51.115 15.118 -1.253 1.00 44.69 O

ATOM 4232 CB TYR C 804 50.868 16.509 1.577 1.00 48.67 C

ATOM 4233 CG TYR C 804 50.867 16.017 3.010 1.00 53.09 C

ATOM 4234 CDl TYR C 804 52.013 16.099 3.805 1.00 54.50 C

ATOM 4235 CD2 TYR C 804 49.703 15.507 3.584 1.00 53.86 C

ATOM 4236 CEl TYR C 804 51.995 15.688 5.137 1.00 55.65 C

ATOM 4237 CE2 TYR C 804 49.672 15.093 4.911 1.00 55.63 C

ATOM 4238 CZ TYR C 804 50.817 15.185 5.685 1.00 56.23 C

ATOM 4239 OH TYR C 804 50.786 14.783 7.008 1.00 57.37 O

ATOM 4240 N SER C 805 51.931 17.201 -1.412 1.00 42.86 N

ATOM 4241 CA SER C 805 51.535 17.349 -2.808 1.00 40.46 C

ATOM 4242 C SER C 805 52.616 17.387 -3.876 1.00 39.86 C

ATOM 4243 O SER C 805 52.287 17.480 -5.059 1.00 39.46 O

ATOM 4244 CB SER C 805 50.706 18.612 -2.961 1.00 39.44 C

ATOM 4245 OG SER C 805 51.530 19.752 -2.785 1.00 38.69 O

ATOM 4246 N TRP C 806 53.885 17.320 -3.485 1.00 38.84 N

ATOM 4247 CA TRP C 806 54.983 17.410 -4.456 1.00 39.08 C

ATOM 4248 C TRP C 806 54.720 16.646 -5.758 1.00 39.80 C

ATOM 4249 O TRP C 806 54.931 17.179 -6.849 1.00 38.11 O

ATOM 4250 CB TRP C 806 56.315 16.941 -3.829 1.00 39.06 C

ATOM 4251 CG TRP C 806 56.496 15.452 -3.772 1.00 39.48 C

ATOM 4252 CDl TRP C 806 55.919 14.591 -2.891 1.00 39.43 C

ATOM 4253 CD2 TRP C 806 57.281 14.644 -4.666 1.00 40.43 C

ATOM 4254 NEl TRP C 806 56.294 13.299 -3.176 1.00 40.35 N

ATOM 4255 CE2 TRP C 806 57.129 13.304 -4.261 1.00 39.90 C

ATOM 4256 CE3 TRP C 806 58.095 14.926 -5.773 1.00 40.49 C

ATOM 4257 CZ2 TRP C 806 57.763 12.242 -4.921 1.00 42.77 C

ATOM 4258 CZ3 TRP C 806 58.724 13.871 -6.431 1.00 39.91 C

ATOM 4259 CH2 TRP C 806 58.555 12.546 -6.002 1.00 40.77 C

ATOM 4260 N MET C 807 54.245 15.405 -5.635 1.00 42.32 N

ATOM 4261 CA MET C 807 53.951 14.564 -6.793 1.00 43.82 C

ATOM 4262 C MET C 807 52.851 15.151 -7.705 1.00 43.96 C

ATOM 4263 O MET C 807 52.954 15.078 -8.940 1.00 43.20 O

ATOM 4264 CB MET C 807 53.557 13.159 -6.332 1.00 46.86 C

ATOM 4265 CG MET C 807 53.530 12.144 -7.463 1.00 49.80 C

ATOM 4266 SD MET C 807 55.177 11.454 -7.778 1.00 58.35 S

ATOM 4267 CE MET C 807 55.456 12.020 -9.505 1.00 53.36 C

ATOM 4268 N CYS C 808 51.807 15.724 -7.106 1.00 41.93 N

ATOM 4343 O ARG C 817 54.914 21.311 -23.031 1.00 41.67 O

ATOM 4344 CB ARG C 817 56.072 21.269 -19.980 1.00 37.33 C

ATOM 4345 CG ARG C 817 56.557 22.266 -18.919 1.00 37.21 C

ATOM 4346 CD ARG C 817 58.032 22.051 -18.591 1.00 38.50 C

ATOM 4347 NE ARG C 817 58.331 20.683 -18.165 1.00 38.11 N

ATOM 4348 CZ ARG C 817 57.965 20.159 -16.998 1.00 35.69 C

ATOM 4349 NHl ARG C 817 57.284 20.880 -16.112 1.00 38.06 N

ATOM 4350 NH2 ARG C 817 58.267 18.906 -16.726 1.00 35.68 N

ATOM 4351 N SER C 818 54.111 19.585 -21.830 1.00 41.61 N

ATOM 4352 CA SER C 818 53.941 18.710 -22.998 1.00 42.77 C

ATOM 4353 C SER C 818 52.899 19.264 -23.949 1.00 43.85 C

ATOM 4354 O SER C 818 53.055 19.231 -25.166 1.00 44.28 O

ATOM 4355 CB SER C 818 53.509 17.316 -22.564 1.00 41.75 C

ATOM 4356 OG SER C 818 54.238 16.894 -21.431 1.00 41.52 O

ATOM 4357 N TYR C 819 51.822 19.758 -23.361 1.00 45.54 N

ATOM 4358 CA TYR C 819 50.707 20.348 -24.084 1.00 46.74 C

ATOM 4359 C TYR C 819 51.160 21.548 -24.933 1.00 47.33 C

ATOM 4360 O TYR C 819 51.062 21.531 -26.162 1.00 46.47 O

ATOM 4361 CB TYR C 819 49.655 20.752 -23.044 1.00 46.05 C

ATOM 4362 CG TYR C 819 48.637 21.786 -23.460 1.00 47.81 C

ATOM 4363 CDl TYR C 819 48.024 21.738 -24.720 1.00 47.97 C

ATOM 4364 CD2 TYR C 819 48.234 22.777 -22.565 1.00 46.63 C

ATOM 4365 CEl TYR C 819 47.033 22.649 -25.070 1.00 47.09 C

ATOM 4366 CE2 TYR C 819 47.251 23.688 -22.904 1.00 47.44 C

ATOM 4367 CZ TYR C 819 46.650 23.618 -24.158 1.00 48.69 C

ATOM 4368 OH TYR C 819 45.648 24.510 -24.476 1.00 49.27 O

ATOM 4369 N LYS C 820 51.693 22.566 -24.271 1.00 48.73 N

ATOM 4370 CA LYS C 820 52.139 23.782 -24.943 1.00 49.94 C

ATOM 4371 C LYS C 820 53.393 23.687 -25.816 1.00 50.69 C

ATOM 4372 O LYS C 820 53.586 24.510 -26.708 1.00 50.73 O

ATOM 4373 CB LYS C 820 52.323 24.894 -23.905 1.00 50.34 C

ATOM 4374 N HIS C 821 54.241 22.696 -25.579 1.00 50.77 N

ATOM 4375 CA HIS C 821 55.465 22.586 -26.360 1.00 52.17 C

ATOM 4376 C HIS C 821 55.468 21.529 -27.450 1.00 51.78 C

ATOM 4377 O HIS C 821 56.269 21.607 -28.378 1.00 51.20 O

ATOM 4378 CB HIS C 821 56.658 22.339 -25.426 1.00 54.18 C

ATOM 4379 CG HIS C 821 56.951 23.486 -24.509 1.00 54.61 C

ATOM 4380 NDl HIS C 821 57.596 23.327 -23.301 1.00 55.52 N

ATOM 4381 CD2 HIS C 821 56.678 24.808 -24.618 1.00 56.19 C

ATOM 4382 CEl HIS C 821 57.703 24.500 -22.702 1.00 54.84 C

ATOM 4383 NE2 HIS C 821 57.153 25.415 -23.481 1.00 56.40 N

ATOM 4384 N THR C 822 54.585 20.543 -27.351 1.00 52.61 N

ATOM 4385 CA THR C 822 54.561 19.479 -28.349 1.00 52.56 C

ATOM 4386 C THR C 822 53.176 19.086 -28.819 1.00 53.35 C

ATOM 4387 O THR C 822 53.014 18.030 -29.431 1.00 55.11 O

ATOM 4388 CB THR C 822 55.214 18.207 -27.818 1.00 51.59 C

ATOM 4389 OGl THR C 822 54.379 17.655 -26.795 1.00 49.14 O

ATOM 4390 CG2 THR C 822 56.605 18.508 -27.251 1.00 51.47 C

ATOM 4391 N ASN C 823 52.186 19.929 -28.542 1.00 54.16 N

ATOM 4392 CA ASN C 823 50.805 19.649 -28.932 1.00 55.07 C

ATOM 4393 C ASN C 823 50.259 18.440 -28.160 1.00 54.78 C

ATOM 4394 O ASN C 823 49.199 17.903 -28.497 1.00 55.16 O

ATOM 4395 CB ASN C 823 50.710 19.378 -30.442 1.00 55.77 C

ATOM 4396 CG ASN C 823 51.131 20.573 -31.285 1.00 57.01 C

ATOM 4397 ODl ASN C 823 50.725 21.708 -31.027 1.00 55.85 O

ATOM 4398 ND2 ASN C 823 51.938 20.315 -32.316 1.00 58.85 N

ATOM 4399 N SER C 824 50.990 18.032 -27.123 1.00 54.05 N

ATOM 4400 CA SER C 824 50.630 16.892 -26.287 1.00 54.01 C

ATOM 4401 C SER C 824 50.908 15.581 -26.996 1.00 55.16 C

ATOM 4402 O SER C 824 50.246 14.577 -26.739 1.00 55.92 O

ATOM 4403 CB SER C 824 49.157 16.943 -25.865 1.00 53.83 C

ATOM 4404 OG SER C 824 49.017 17.505 -24.575 1.00 50.73 O

ATOM 4405 N GLN C 825 51.885 15.594 -27.895 1.00 56.42 N

ATOM 4406 CA GLN C 825 52.268 14.392 -28.622 1.00 57.09 C

ATOM 4407 C GLN C 825 53.410 13.675 -27.887 1.00 56.85 C

ATOM 4408 O GLN C 825 53.611 12.480 -28.075 1.00 58.45 O

ATOM 4409 CB GLN C 825 52.701 14.743 -30.053 1.00 58.69 C

ATOM 4410 CG GLN C 825 51.606 14.565 -31.115 1.00 63.32 C

ATOM 4411 CD GLN C 825 52.124 14.700 -32.558 1.00 65.40 C

ATOM 4412 OEl GLN C 825 51.362 14.991 -33.485 1.00 66.48 O

ATOM 4413 NE2 GLN C 825 53.428 14.497 -32.742 1.00 66.73 N

ATOM 4414 N PHE C 826 54.145 14.410 -27.049 1.00 55.09 N

ATOM 4415 CA PHE C 826 55.269 13.865 -26.280 1.00 53.22 C

ATOM 4416 C PHE C 826 55.182 14.333 -24.815 1.00 51.20 C

ATOM 4935 N ALA C 890 41.297 26.623 9.985 1.00 49.53 N

ATOM 4936 CA ALA C 890 40.350 27.630 9.568 1.00 49.18 C

ATOM 4937 C ALA C 890 40.993 28.552 8.550 1.00 48.75 C

ATOM 4938 O ALA C 890 40.405 28.861 7.514 1.00 50.11 O

ATOM 4939 CB ALA C 890 39.833 28.419 10.755 1.00 49.13 C

ATOM 4940 N ALA C 891 42.211 28.987 8.855 1.00 46.25 N

ATOM 4941 CA ALA C 891 42.952 29.849 7.956 1.00 44.65 C

ATOM 4942 C ALA C 891 43.072 29.144 6.608 1.00 43.76 C

ATOM 4943 O ALA C 891 42.765 29.718 5.561 1.00 42.96 O

ATOM 4944 CB ALA C 891 44.328 30.123 8.530 1.00 44.29 C

ATOM 4945 N PHE C 892 43.503 27.885 6.652 1.00 42.19 N

ATOM 4946 CA PHE C 892 43.683 27.072 5.455 1.00 40.33 C

ATOM 4947 C PHE C 892 42.447 26.958 4.575 1.00 41.13 C

ATOM 4948 O PHE C 892 42.528 27.068 3.348 1.00 41.16 O

ATOM 4949 CB PHE C 892 44.114 25.660 5.843 1.00 39.94 C

ATOM 4950 CG PHE C 892 44.008 24.660 4.719 1.00 39.68 C

ATOM 4951 CDl PHE C 892 45.028 24.530 3.779 1.00 39.99 C

ATOM 4952 CD2 PHE C 892 42.876 23.853 4.593 1.00 40.52 C

ATOM 4953 CEl PHE C 892 44.918 23.606 2.730 1.00 40.26 C

ATOM 4954 CE2 PHE C 892 42.760 22.933 3.548 1.00 39.71 C

ATOM 4955 CZ PHE C 892 43.783 22.811 2.617 1.00 39.03 C

ATOM 4956 N GLU C 893 41.303 26.715 5.199 1.00 40.94 N

ATOM 4957 CA GLU C 893 40.079 26.531 4.447 1.00 41.31 C

ATOM 4958 C GLU C 893 39.560 27.794 3.779 1.00 40.78 C

ATOM 4959 O GLU C 893 38.996 27.721 2.693 1.00 41.30 O

ATOM 4960 CB GLU C 893 39.019 25.884 5.350 1.00 42.61 C

ATOM 4961 CG GLU C 893 39.343 24.409 5.631 1.00 45.50 C

ATOM 4962 CD GLU C 893 38.230 23.645 6.327 1.00 46.99 C

ATOM 4963 OEl GLU C 893 38.512 22.557 6.871 1.00 47.52 O

ATOM 4964 OE2 GLU C 893 37.079 24.121 6.342 1.00 49.83 O

ATOM 4965 N GLU C 894 39.775 28.949 4.404 1.00 40.47 N

ATOM 4966 CA GLU C 894 39.319 30.216 3.844 1.00 42.18 C

ATOM 4967 C GLU C 894 40.082 30.558 2.572 1.00 42.54 C

ATOM 4968 O GLU C 894 39.534 31.135 1.626 1.00 42.06 O

ATOM 4969 CB GLU C 894 39.489 31.342 4.866 1.00 43.23 C

ATOM 4970 CG GLU C 894 39.560 32.745 4.257 1.00 Al .21 C

ATOM 4971 CD GLU C 894 38.205 33.276 3.778 1.00 49.92 C

ATOM 4972 OEl GLU C 894 38.196 34.281 3.030 1.00 53.24 O

ATOM 4973 OE2 GLU C 894 37.154 32.706 4.150 1.00 47.68 O

ATOM 4974 N MET C 895 41.354 30.195 2.555 1.00 43.11 N

ATOM 4975 CA MET C 895 42.202 30.466 1.411 1.00 43.51 C

ATOM 4976 C MET C 895 41.932 29.518 0.249 1.00 41.56 C

ATOM 4977 O MET C 895 42.039 29.905 -0.917 1.00 40.16 O

ATOM 4978 CB MET C 895 43.658 30.365 1.835 1.00 48.09 C

ATOM 4979 CG MET C 895 44.643 30.495 0.713 1.00 50.51 C

ATOM 4980 SD MET C 895 46.188 29.881 1.328 1.00 57.83 S

ATOM 4981 CE MET C 895 46.059 28.171 0.856 1.00 53.49 C

ATOM 4982 N ARG C 896 41.593 28.276 0.565 1.00 40.19 N

ATOM 4983 CA ARG C 896 41.313 27.300 -0.475 1.00 40.50 C

ATOM 4984 C ARG C 896 40.013 27.709 -1.152 1.00 41.19 C

ATOM 4985 O ARG C 896 39.905 27.722 -2.384 1.00 41.10 O

ATOM 4986 CB ARG C 896 41.185 25.903 0.129 1.00 40.51 C

ATOM 4987 CG ARG C 896 41.163 24.801 -0.900 1.00 42.00 C

ATOM 4988 CD ARG C 896 41.322 23.443 -0.235 1.00 43.28 C

ATOM 4989 NE ARG C 896 40.063 22.705 -0.253 1.00 45.84 N

ATOM 4990 CZ ARG C 896 39.625 22.006 -1.290 1.00 45.25 C

ATOM 4991 NHl ARG C 896 40.348 21.937 -2.401 1.00 43.34 N

ATOM 4992 NH2 ARG C 896 38.448 21.403 -1.225 1.00 46.27 N

ATOM 4993 N THR C 897 39.030 28.058 -0.330 1.00 40.81 N

ATOM 4994 CA THR C 897 37.738 28.499 -0.826 1.00 41.74 C

ATOM 4995 C THR C 897 37.934 29.623 -1.842 1.00 41.21 C

ATOM 4996 O THR C 897 37.508 29.515 -3.002 1.00 39.92 O

ATOM 4997 CB THR C 897 36.843 29.014 0.334 1.00 42.99 C

ATOM 4998 OGl THR C 897 36.380 27.903 1.116 1.00 45.13 O

ATOM 4999 CG2 THR C 897 35.646 29.766 -0.210 1.00 43.20 C

ATOM 5000 N ASN C 898 38.585 30.697 -1.396 1.00 40.32 N

ATOM 5001 CA ASN C 898 38.851 31.848 -2.251 1.00 39.40 C

ATOM 5002 C ASN C 898 39.525 31.460 -3.568 1.00 37.33 C

ATOM 5003 O ASN C 898 39.251 32.044 -4.622 1.00 36.58 O

ATOM 5004 CB ASN C 898 39.727 32.869 -1.521 1.00 41.05 C

ATOM 5005 CG ASN C 898 39.019 33.526 -0.346 1.00 42.23 C

ATOM 5006 ODl ASN C 898 39.629 34.276 0.404 1.00 43.48 O

ATOM 5007 ND2 ASN C 898 37.726 33.255 -0.188 1.00 44.83 N

ATOM 5008 N TYR C 899 40.412 30.484 -3.519 1.00 35.05 N

ATOM 5379 OE2 GLU C 948 63.616 -3.945 -2.242 1.00 65.87 O

ATOM 5380 N SER C 949 65.967 1.026 -4.170 1.00 68.67 N

ATOM 5381 CA SER C 949 66.864 1.754 -5.062 1.00 69.96 C

ATOM 5382 C SER C 949 68.206 1.030 -5.165 1.00 70.33 C

ATOM 5383 O SER C 949 68.867 1.072 -6.205 1.00 69.62 O

ATOM 5384 CB SER C 949 67.077 3.195 -4.564 1.00 71.28 C

ATOM 5385 OG SER C 949 67.888 3.253 -3.399 1.00 73.26 O

ATOM 5386 N HIS C 950 68.597 0.364 -4.079 1.00 71.06 N

ATOM 5387 CA HIS C 950 69.853 -0.385 -4.039 1.00 71.13 C

ATOM 5388 C HIS C 950 69.762 -1.542 -5.029 1.00 70.19 C

ATOM 5389 O HIS C 950 70.656 -1.757 -5.847 1.00 69.75 O

ATOM 5390 CB HIS C 950 70.110 -0.929 -2.622 1.00 73.07 C

ATOM 5391 CG HIS C 950 70.415 0.133 -1.605 1.00 74.79 C

ATOM 5392 NDl HIS C 950 70.063 0.019 -0.276 1.00 74.93 N

ATOM 5393 CD2 HIS C 950 71.038 1.331 -1.726 1.00 75.00 C

ATOM 5394 CEl HIS C 950 70.454 1.100 0.376 1.00 74.75 C

ATOM 5395 NE2 HIS C 950 71.048 1.911 -0.480 1.00 75.39 N

ATOM 5396 N ALA C 951 68.666 -2.284 -4.953 1.00 69.41 N

ATOM 5397 CA ALA C 951 68.457 -3.405 -5.852 1.00 68.38 C

ATOM 5398 C ALA C 951 68.483 -2.915 -7.293 1.00 67.99 C

ATOM 5399 O ALA C 951 69.431 -3.181 -8.033 1.00 66.84 O

ATOM 5400 CB ALA C 951 67.118 -4.071 -5.554 1.00 68.30 C

ATOM 5401 N LEU C 952 67.437 -2.173 -7.660 1.00 67.83 N

ATOM 5402 CA LEU C 952 67.244 -1.633 -9.009 1.00 66.52 C

ATOM 5403 C LEU C 952 68.348 -0.748 -9.574 1.00 65.69 C

ATOM 5404 O LEU C 952 68.478 -0.624 -10.792 1.00 65.91 O

ATOM 5405 CB LEU C 952 65.914 -0.876 -9.076 1.00 65.60 C

ATOM 5406 CG LEU C 952 64.629 -1.702 -8.909 1.00 67.05 C

ATOM 5407 CDl LEU C 952 64.471 -2.656 -10.093 1.00 65.82 C

ATOM 5408 CD2 LEU C 952 64.664 -2.479 -7.596 1.00 66.99 C

ATOM 5409 N LYS C 953 69.141 -0.141 -8.699 1.00 64.86 N

ATOM 5410 CA LYS C 953 70.220 0.745 -9.129 1.00 64.08 C

ATOM 5411 C LYS C 953 69.629 2.056 -9.624 1.00 63.69 C

ATOM 5412 O LYS C 953 69.966 2.532 -10.707 1.00 64.22 O

ATOM 5413 CB LYS C 953 71.049 0.095 -10.232 1.00 62.90 C

ATOM 5414 N VAL C 954 68.740 2.631 -8.823 1.00 63.04 N

ATOM 5415 CA VAL C 954 68.109 3.893 -9.172 1.00 63.05 C

ATOM 5416 C VAL C 954 68.424 4.956 -8.128 1.00 61.98 C

ATOM 5417 O VAL C 954 67.966 4.875 -6.991 1.00 61.40 O

ATOM 5418 CB VAL C 954 66.582 3.743 -9.276 1.00 63.46 C

ATOM 5419 CGl VAL C 954 66.037 4.727 -10.302 1.00 63.53 C

ATOM 5420 CG2 VAL C 954 66.226 2.311 -9.657 1.00 63.64 C

ATOM 5421 N GLU C 955 69.199 5.955 -8.531 1.00 61.28 N

ATOM 5422 CA GLU C 955 69.593 7.046 -7.648 1.00 61.50 C

ATOM 5423 C GLU C 955 68.480 8.078 -7.408 1.00 61.25 C

ATOM 5424 O GLU C 955 67.795 8.500 -8.338 1.00 60.75 O

ATOM 5425 CB GLU C 955 70.820 7.756 -8.235 1.00 62.25 C

ATOM 5426 CG GLU C 955 72.100 6.927 -8.202 1.00 65.15 C

ATOM 5427 CD GLU C 955 73.090 7.328 -9.289 1.00 67.16 C

ATOM 5428 OEl GLU C 955 74.243 6.835 -9.266 1.00 66.65 O

ATOM 5429 OE2 GLU C 955 72.709 8.134 -10.167 1.00 67.80 O

ATOM 5430 N PHE C 956 68.311 8.482 -6.152 1.00 60.94 N

ATOM 5431 CA PHE C 956 67.314 9.488 -5.778 1.00 61.08 C

ATOM 5432 C PHE C 956 68.002 10.787 -5.325 1.00 60.65 C

ATOM 5433 O PHE C 956 68.931 10.752 -4.522 1.00 60.47 O

ATOM 5434 CB PHE C 956 66.440 8.996 -4.615 1.00 61.26 C

ATOM 5435 CG PHE C 956 65.185 8.288 -5.035 1.00 61.53 C

ATOM 5436 CDl PHE C 956 65.146 6.900 -5.140 1.00 61.73 C

ATOM 5437 CD2 PHE C 956 64.019 9.013 -5.280 1.00 61.90 C

ATOM 5438 CEl PHE C 956 63.958 6.247 -5.481 1.00 62.04 C

ATOM 5439 CE2 PHE C 956 62.834 8.375 -5.619 1.00 60.45 C

ATOM 5440 CZ PHE C 956 62.800 6.988 -5.719 1.00 60.97 C

ATOM 5441 N PRO C 957 67.639 11.928 -5.537 1.00 60.24 N

ATOM 5442 CA PRO C 957 68.247 13.121 -4.931 1.00 59.26 C

ATOM 5443 C PRO C 957 67.954 13.145 -3.431 1.00 57.86 C

ATOM 5444 O PRO C 957 66.907 12.675 -2.995 1.00 58.06 O

ATOM 5445 CB PRO C 957 67.549 14.274 -5.656 1.00 59.97 C

ATOM 5446 CG PRO C 957 67.252 13.695 -6.990 1.00 59.98 C

ATOM 5447 CD PRO C 957 66.762 12.300 -6.660 1.00 59.99 C

ATOM 5448 N ALA C 958 68.867 13.704 -2.647 1.00 57.24 N

ATOM 5449 CA ALA C 958 68.687 13.773 -1.199 1.00 56.11 C

ATOM 5450 C ALA C 958 67.408 14.512 -0.822 1.00 54.84 C

ATOM 5451 O ALA C 958 66.715 14.117 0.120 1.00 54.71 O

ATOM 5452 CB ALA C 958 69.883 14.442 -0.557 1.00 56.12 C

ATOM 5601 CA LEU C 979 40.306 16.697 -0.864 1.00 49.17 C

ATOM 5602 C LEU C 979 39.731 16.636 -2.260 1.00 49.11 C

ATOM 5603 O LEU C 979 40.434 16.908 -3.239 1.00 50.25 O

ATOM 5604 CB LEU C 979 40.575 18.151 -0.482 1.00 48.26 C

ATOM 5605 CG LEU C 979 41.075 18.392 0.946 1.00 47.16 C

ATOM 5606 CDl LEU C 979 41.035 19.881 1.246 1.00 47.50 C

ATOM 5607 CD2 LEU C 979 40.207 17.633 1.943 1.00 46.69 C

ATOM 5608 N TYR C 980 38.458 16.270 -2.351 1.00 48.70 N

ATOM 5609 CA TYR C 980 37.788 16.168 -3.641 1.00 47.97 C

ATOM 5610 C TYR C 980 36.741 17.244 -3.844 1.00 46.82 C

ATOM 5611 O TYR C 980 36.097 17.694 -2.899 1.00 47.13 O

ATOM 5612 CB TYR C 980 37.131 14.792 -3.787 1.00 47.99 C

ATOM 5613 CG TYR C 980 38.118 13.647 -3.699 1.00 48.18 C

ATOM 5614 CDl TYR C 980 38.797 13.189 -4.835 1.00 47.69 C

ATOM 5615 CD2 TYR C 980 38.391 13.034 -2.474 1.00 47.71 C

ATOM 5616 CEl TYR C 980 39.720 12.145 -4.742 1.00 47.02 C

ATOM 5617 CE2 TYR C 980 39.304 12.001 -2.377 1.00 46.28 C

ATOM 5618 CZ TYR C 980 39.964 11.560 -3.507 1.00 47.19 C

ATOM 5619 OH TYR C 980 40.859 10.519 -3.388 1.00 49.61 O

ATOM 5620 N PHE C 981 36.580 17.663 -5.091 1.00 46.59 N

ATOM 5621 CA PHE C 981 35.580 18.664 -5.407 1.00 45.42 C

ATOM 5622 C PHE C 981 34.234 17.955 -5.522 1.00 46.48 C

ATOM 5623 O PHE C 981 33.182 18.580 -5.383 1.00 46.64 O

ATOM 5624 CB PHE C 981 35.941 19.371 -6.717 1.00 42.72 C

ATOM 5625 CG PHE C 981 37.030 20.408 -6.566 1.00 39.60 C

ATOM 5626 CDl PHE C 981 36.730 21.691 -6.099 1.00 37.76 C

ATOM 5627 CD2 PHE C 981 38.352 20.097 -6.873 1.00 37.57 C

ATOM 5628 CEl PHE C 981 37.726 22.642 -5.942 1.00 37.96 C

ATOM 5629 CE2 PHE C 981 39.360 21.036 -6.721 1.00 39.00 C

ATOM 5630 CZ PHE C 981 39.050 22.314 -6.255 1.00 39.55 C

ATOM 5631 N HIS C 982 34.275 16.641 -5.747 1.00 46.76 N

ATOM 5632 CA HIS C 982 33.060 15.847 -5.895 1.00 47.35 C

ATOM 5633 C HIS C 982 33.280 14.436 -5.348 1.00 50.21 C

ATOM 5634 O HIS C 982 32.932 14.151 -4.062 1.00 51.43 O

ATOM 5635 CB HIS C 982 32.685 15.759 -7.378 1.00 44.69 C

ATOM 5636 CG HIS C 982 32.864 17.047 -8.126 1.00 40.67 C

ATOM 5637 NDl HIS C 982 31.975 18.093 -8.031 1.00 38.26 N

ATOM 5638 CD2 HIS C 982 33.851 17.466 -8.952 1.00 39.85 C

ATOM 5639 CEl HIS C 982 32.405 19.103 -8.765 1.00 38.33 C

ATOM 5640 NE2 HIS C 982 33.541 18.749 -9.335 1.00 40.10 N

TER 5641 HIS C 982

HETATM 5642 Cl STR 1001 123.500 -20.174 10.969 1.00 30.54 C

HETATM 5643 C2 STR 1001 123.023 -18.813 10.360 1.00 31.76 C

HETATM 5644 C3 STR 1001 121.674 -18.904 9.636 1.00 31.69 C

HETATM 5645 03 STR 1001 121.452 -18.083 8.724 1.00 36.27 O

HETATM 5646 C4 STR 1001 120.671 -19.919 9.953 1.00 33.17 C

HETATM 5647 C5 STR 1001 120.891 -20.913 11.024 1.00 31.59 C

HETATM 5648 C6 STR 1001 119.724 -21.967 11.388 1.00 33.43 C

HETATM 5649 C7 STR 1001 120.237 -23.401 11.331 1.00 32.01 C

HETATM 5650 C8 STR 1001 121.554 -23.623 12.207 1.00 31.29 C

HETATM 5651 C9 STR 1001 122.780 -22.613 11.696 1.00 32.46 C

HETATM 5652 ClO STR 1001 122.337 -21.078 11.747 1.00 32.10 C

HETATM 5653 CIl STR 1001 124.222 -22.865 12.386 1.00 32.71 C

HETATM 5654 C12 STR 1001 124.602 -24.321 12.388 1.00 33.80 C

HETATM 5655 C13 STR 1001 123.457 -25.286 13.074 1.00 32.32 C

HETATM 5656 C14 STR 1001 122.099 -25.080 12.179 1.00 32.37 C

HETATM 5657 C15 STR 1001 121.144 -26.262 12.472 1.00 32.18 C

HETATM 5658 C16 STR 1001 122.174 -27.376 12.794 1.00 33.31 C

HETATM 5659 C17 STR 1001 123.636 -26.746 12.769 1.00 32.86 C

HETATM 5660 C18 STR 1001 123.307 -24.954 14.689 1.00 31.71 C

HETATM 5661 C19 STR 1001 122.134 -20.577 13.267 1.00 30.94 C

HETATM 5662 C20 STR 1001 124.685 -27.511 13.527 1.00 33.96 C

HETATM 5663 020 STR 1001 124.323 -28.137 14.571 1.00 36.61 O

HETATM 5664 C21 STR 1001 126.133 -27.558 13.038 1.00 34.41 C

HETATM 5665 Cl STR 2001 124.574 49.229 -6.492 1.00 37.68 C

HETATM 5666 C2 STR 2001 123.992 50.586 -6.868 1.00 36.08 C

HETATM 5667 C3 STR 2001 122.748 50.469 -7.774 1.00 36.62 C

HETATM 5668 03 STR 2001 122.629 51.343 -8.623 1.00 38.39 O

HETATM 5669 C4 STR 2001 121.783 49.353 -7.683 1.00 37.49 C

HETATM 5670 C5 STR 2001 122.070 48.271 -6.659 1.00 37.99 C

HETATM 5671 C6 STR 2001 121.061 47.106 -6.440 1.00 37.86 C

HETATM 5672 C7 STR 2001 121.770 45.772 -6.287 1.00 37.93 C

HETATM 5673 C8 STR 2001 122.895 45.679 -5.308 1.00 36.55 C

HETATM 5674 C9 STR 2001 124.084 46.783 -5.761 1.00 37.81 C

Table 3 Data collection and refinement statistics for the DOC/MR LBD-S810L-C910A and progesterone/MR LBD-S810L-C910A complexes

Table 4 Data collection for the DOC/MR LBD- C910A and spironolactone/MR LBD-S810L-C910A complexes

Claims

I. A polypeptide comprising a MR LBD polypeptide sequence fused to a tag.

2. The polypeptide of claim I, wherein the MR LBD polypeptide sequence and the tag are fused through a linker sequence, which preferably comprises a cleavage domain.

3. The polypeptide of claim 1 or 2, wherein the MR LBD polypeptide is a human wild- type or mutant MR LBD polypeptide.

4. The polypeptide of claim 3, wherein the MR LBD polypeptide sequence comprises amino acid residues 737-984 of SEQ DD NO: 1 or a mutant thereof, more preferably amino acid residues 731 -984 of SEQ ID NO: 1 or a mutant thereof.

5. The polypeptide of claim 3 or 4, wherein the MR LBD polypeptide sequence comprises a mutation selected from N770A, Q776A, S810L, S810M, R817A, M852A C910A, T945A and any combinations thereof.

6. The polypeptide of any one of claims 1 to 5, wherein the tag is selected from GST, Thioredoxin and.polyHis.

7. A polypeptide comprising a mutated human MR LBD sequence, wherein the mutated MR LBD comprises a mutation selected from N770A, Q776A, S810L, S810M, R817A, M852A C910A, T945A and any combinations thereof.

8. A nucleic acid encoding a polypeptide of any one of the preceding claims.

9. A recombinant vector comprising a nucleic acid molecule of claim 8.

10. An isolated or purified complex comprising a MR LBD polypeptide and a ligand thereof.

11. A crystalline complex comprising a MR LBD polypeptide and a ligand thereof.

12. The complex of claim 10 or 11, wherein the MR LBD polypeptide is a human wild- type or mutant MR LBD polypeptide.

13. The complex of claim 10, 11 or 12, wherein the MR LBD polypeptide is as defined in any one of claims 1-7.

14. The complex of any one of claims 10 to 13, wherein the ligand is an MR agonist, selected preferably from aldosterone, Cortisol and deoxycorticosterone.

15. The complex of any one of claims 10 to 13, wherein the ligand is an MR antagonist, selected preferably from progesterone, spironolactone and cortisone.

16. A crystalline DOC/MR LBD-S810L-C910A or progesterone/MR LBD-S810L- C910 A complex of claim 11 , characterized by the atomic structural coordinates of Table

1 or Table 2, respectively.

17. A method of producing a MR LBD polypeptide, comprising

(b) collecting the polypeptide from the cell, and

(c) optionally, separating the MR LBD polypeptide from the tag.

18. The method of claim 17, wherein the cell is a prokaryotic cell, preferably E. coli.

19. The method of claim 17 or 18, wherein the MR LBD polypeptide is as defined in any one of claims 1 to 7.

20. The method of any one of claims 17 to 19, wherein the tag is GST.

21. The method of any one of claims 17-20, wherein the cell is cultured in the presence of a MR ligand, and a complex of the MR LBD polypeptide and the ligand is collected.

22. The method of claim 21, wherein the ligand is an MR agonist or antagonist, selected preferably from aldosterone, Cortisol, deoxycorticosterone, progesterone, spironolactone and cortisone.

23. A method for preparing a crystalline complex comprising a MR LBD polypeptide and a ligand thereof, the method comprising:

(a) providing a solution comprising a MR LBD polypeptide and a ligand thereof,

(b) crystallizing the polypeptide, and

24. The method of claim 23, wherein the MR LBD polypeptide is recombinant, preferably produced by a method of any one of claims 17-22.

25. The method of claim 23 or 24, wherein the complex is crystallized using the vapor diffusion method.

26. The method of claim 25, wherein the reservoir solution comprises HEPES or PIPES, pH 6.5 to 7.5, 200-300 mM NaCl and 15 to 30% PEG4000.

27. The use of a polypeptide according to any one of claims 1 to 7 or of a complex according to any one of claims 10 to 16 for drug design or screening.

28. The use of a polypeptide according to any one of claims 1 to 7 or of a complex according to any one of claims 10 to 16 for the production of an anti MR antibody.

29. An antibody that binds an epitope comprised in a polypeptide according to any one of claims 1 to 7 or in a complex according to any one of claims 10 to 16.

30. The antibody of claim 29, which is a monoclonal antibody, or a fragment or derivative thereof.

31. A method for identifying, characterizing, screening or optimizing MR ligands, the method comprising contacting a candidate compound in vitro with a polypeptide according to any one of claims 1 to 7 or a complex according to any one of claims 10 to 16, and determining the ability of said candidate compound to bind the MR LBD domain of said polypeptide or complex.

32. A method for identifying, characterizing, screening or optimizing MR ligands, the method comprising contacting a candidate compound in vitro with a recombinant cell comprising a recombinant nucleic acid encoding a MR LBD polypeptide fused to a tag, under conditions allowing expression of the MR LBD polypeptide in said cell, and assessing the production of a complex between the MR LBD polypeptide and the candidate compound.

33. The method of claim 32, wherein assessing the formation of said complex comprises determining the presence of soluble MR LBD polypeptides in said culture.

34. A method for identifying a candidate MR modulator, comprising:

LBD, and

35. A method for producing a candidate MR modulator, comprising:

(b) designing a compound that fits spatially into the binding pocket of the MR LBD, (c) synthesizing said compound

36. The method of claim 34 or 35, wherein the atomic coordinates comprise the atomic coordinates of Table 1 or Table 2.

37. The method of any one of claims 34 to 36, for identifying or producing specific MR modulators.

38. A recombinant cell comprising a recombinant nucleic acid encoding a MR LBD polypeptide fused to a tag.

39. The cell of claim 38, which is a prokaryotic cell, preferably a E. CoIi strain.

40. The use of a compound produced by a method of any one of claims 29 to 32, for the manufacture of a medicament for treating hypertension with hyperaldosteronism, essential hypertension and cardiac failure.

41. The use of compound 5α-pregnan-20-one (Pl) having the formula

or a derivative thereof for the manufacture of a medicament for emergency contraception, long term estrogen-free contraception, or for treating, preventing or alleviating proliferative endometrium diseases such as myomas and endometriosis.

42. An isolated polypeptide comprising a MR LBD polypeptide sequence comprising amino acid residues 737-984 of SEQ ID NO: 1 or a mutant thereof, more preferably amino acid residues 731-984 of SEQ ID NO: 1 or a mutant thereof, wherein said polypeptide does not contain amino acid residues 1-730 of a MR polypeptide sequence.

43. The polypeptide of claim 42, wherein the MR LBD polypeptide sequence comprises a mutation selected from N770A, Q776A, S810L, S810M, R817A, M852A C910A, T945A and any combinations thereof.