AX132 PCSK9 antagonists

[0001] This application is a 371 of PCT/US2010/054714, filed Oct. 29, 2010, which claims benefit of U.S. provisional application, U.S. Ser. No. 61/256,732, filed Oct. 30, 2009, and claims benefit of U.S. provisional application, U.S. Ser. No. 61/323,148, filed Apr. 12, 2010.

[0002] Not Applicable.

[0003] Not Applicable.

[0004] Proprotein convertase subtilisin-kexin type 9 (hereinafter called “PCSK9”), also known as neural apoptosis-regulated convertase 1 (“NARC-1”), is a proteinase K-like subtilase identified as the 9^th member of the secretory subtilase family; see Seidah et al., 2003 PNAS 100:928-933. The gene for PCSK9 localizes to human chromosome 1p33-p34.3; Seidah et al., supra. PCSK9 is expressed in cells capable of proliferation and differentiation including, for example, hepatocytes, kidney mesenchymal cells, intestinal ileum, and colon epithelia as well as embryonic brain telencephalon neurons; Seidah et al., supra.

[0005] Original synthesis of PCSK9 is in the form of an inactive enzyme precursor, or zymogen, of ˜72-kDa which undergoes autocatalytic, intramolecular processing in the endoplasmic reticulum (“ER”) to activate its functionality. This internal processing event has been reported to occur at the SSVFAQ↓SIPWNL¹⁵⁸ motif (SEQ ID NOs: 19 and 20, respectively); Benjannet et al., 2004 J. Biol. Chem. 279:48865-48875. Such internal processing has been reported as a requirement of exit from the ER; Benjannet et al., supra; Seidah et al., supra. The cleaved and, thereby, activated protein is secreted in association with the cleaved peptide; supra.

[0006] The sequence for human PCSK9 (˜22-kb long with 12 exons encoding a 692 amino acid protein) can be found in one instance at Deposit No. NP_—777596.2. Human, mouse and rat PCSK9 nucleic acid sequences have been deposited; see, e.g., GenBank Accession Nos.: AX21327530 (also AX207686), NP_—705793 (also Q80W65), and P59996, respectively. PCSK9 possesses several domains found in other proprotein convertases, including an N-terminal signal sequence, a pro domain, a catalytic domain and a cysteine-rich C terminal domain. The PCSK9 catalytic domain shares high sequence similarity with the proteinase K family of subtilases and, notably, a catalytic triad of D186, H226 and S386.

[0007] PCSK9 is disclosed and/or claimed in several patent publications including, but not limited to the following: PCT Publication Nos. WO 01/31007, WO 01/57081, WO 02/14358, WO 01/98468, WO 02/102993, WO 02/102994, WO 02/46383, WO 02/90526, WO 01/77137, and WO 01/34768; US Publication Nos. US 2004/0009553 and US 2003/0119038, and European Publication Nos. EP 1 440 981, EP 1 067 182, and EP 1 471 152.

[0008] PCSK9 has been ascribed a role in the differentiation of hepatic and neuronal cells (Seidah et al., supra.), is highly expressed in embryonic liver, and has been strongly implicated in cholesterol homeostasis. Studies have suggested a specific role for PCSK9 in cholesterol biosynthesis or uptake. In a study of cholesterol-fed rats, Maxwell et al. found that PCSK9 was downregulated in a similar manner to three other genes involved in cholesterol biosynthesis, Maxwell et al., 2003 J. Lipid Res. 44:2109-2119. The expression of PCSK9 has, in fact, been shown to be regulated by sterol regulatory element-binding proteins (“SREBP”), as seen with other genes involved in cholesterol metabolism; supra. Later support for these findings came about through a study of PCSK9 transcriptional regulation which demonstrated that such regulation was quite typical of other genes implicated in lipoprotein metabolism; Dubuc et al., 2004 Arterioscler. Thromb. Vasc. Biol. 24:1454-1459. Statins have been shown to upregulate PCSK9 expression in a manner attributed to the cholesterol-lowering effects of the drugs; supra. Moreover, it has been shown that PCSK9 promoters possess two conserved sites involved in cholesterol regulation, a sterol regulatory element and an Sp1 site; supra.

[0009] Several lines of evidence demonstrate that PCSK9, in particular, lowers the amount of hepatic LDLR protein and thus compromises the liver's ability to remove LDL cholesterol from the circulation. Adenovirus-mediated overexpression of PCSK9 in the livers of mice results in the accumulation of circulating LDL-C due to a dramatic loss of hepatic LDLR protein, with no effect on LDLR mRNA levels; Benjannet et al., 2004 J. Biol. Chem. 279:48865-48875; Maxwell & Breslow, 2004 PNAS 101:7100-7105; Park et al., 2004 J. Biol. Chem. 279:50630-50638; and Lalanne et al., 2005 J. Lipid Res. 46:1312-1319. The effect of PCSK9 over-expression on raising circulating LDL-C levels in mice is completely dependent on the expression of LDLR, again, indicating that the regulation of LDL-C by PCSK9 is mediated through downregulation of LDLR protein. In agreement with these findings, mice lacking PCSK9 or in which PCSK9 mRNA has been lowered by antisense oligonucleotide inhibitors have higher levels of hepatic LDLR protein and a greater ability to clear circulating LDL-C; Rashid et al., 2005 PNAS 102:5374-5379; and Graham et al., 2007 J. Lipid Res. 48(4):763-767. In addition, lowering PCSK9 levels in cultured human hepatocytes by siRNA also results in higher LDLR protein levels and an increased ability to take up LDL-C; Benjannet et al., 2004 J. Biol. Chem. 279:48865-48875; and Lalanne et al., 2005 J. Lipid Res. 46:1312-1319. Together, these data indicate that PCSK9 action leads to increased LDL-C by lowering LDLR protein levels.

[0010] A number of mutations in the gene PCSK9 have also been conclusively associated with autosomal dominant hypercholesterolemia (“ADH”), an inherited metabolism disorder characterized by marked elevations of low density lipoprotein (“LDL”) particles in the plasma which can lead to premature cardiovascular failure; see Abifadel et al., 2003 Nature Genetics 34:154-156; Timms et al., 2004 Hum. Genet. 114:349-353; Leren, 2004 Clin. Genet. 65:419-422. A later-published study on the S127R mutation of Abifadel et al., supra, reported that patients carrying such a mutation exhibited higher total cholesterol and apoB 100 in the plasma attributed to (1) an overproduction of apoB 100-containing lipoproteins, such as low density lipoprotein (“LDL”), very low density lipoprotein (“VLDL”) and intermediate density lipoprotein (“IDL”), and (2) an associated reduction in clearance or conversion of said lipoproteins; Ouguerram et al., 2004 Arterioscler. Thromb. Vasc. Biol. 24:1448-1453.

[0011] Accordingly, there can be no doubt that PCSK9 plays a role in the regulation of LDL. The expression or upregulation of PCSK9 is associated with increased plasma levels of LDL cholesterol, and the corresponding inhibition or lack of expression of PCSK9 is associated with reduced LDL cholesterol plasma levels. Decreased levels of LDL cholesterol associated with sequence variations in PCSK9 have been found to confer protection against coronary heart disease; Cohen, 2006 N. Engl. J. Med. 354:1264-1272.

[0012] The identification of compounds and/or agents effective in the treatment of cardiovascular affliction is highly desirable. In clinical trials, reductions in LDL cholesterol levels have been directly related to the rate of coronary events; Law et al., 2003 BMJ 326:1423-1427. More recently, the moderate lifelong reduction in plasma LDL cholesterol levels was found to correlate with a substantial reduction in the incidence of coronary events; Cohen et al., supra. This was the case even in populations with a high prevalence of non-lipid-related cardiovascular risk factors; supra. Accordingly, there is great benefit to be reaped from the managed control of LDL cholesterol levels.

[0013] The present invention advances these interests by providing antagonists of PCSK9 of use for inhibiting the activities of PCSK9 and the corresponding role PCSK9 plays in various therapeutic conditions.

[0014] The present invention relates to protein-specific antagonists of PCSK9 and, in particular embodiments, those antagonists that inhibit human PCSK9. Broadly, protein-specific antagonists of PCSK9 (or “PCSK9-specific antagonists” as referred to herein) are PCSK9 protein binding molecules or molecules effective in the selective binding of PCSK9 and inhibition of PCSK9 function. In particular embodiments, the present invention relates to monoclonal antibody variants having high affinity and desired properties from a therapeutic perspective. These molecules are of import in the treatment of conditions associated with or impacted by PCSK9 function, including, but not limited to hypercholesterolemia, coronary heart disease, metabolic syndrome, acute coronary syndrome and related conditions. PCSK9-specific antagonists are characterized by selective recognition and binding to PCSK9. PCSK9-specific antagonists do not show significant binding to proteins other than PCSK9, other than in those specific instances where the antagonist is supplemented or designed to confer an additional, distinct specificity to the PCSK9-specific binding component.

[0015] PCSK9-specific antagonists forming particular embodiments hereof comprise (a) a heavy chain variable region comprising a CDR3 domain comprising (in select embodiments, consisting of) a sequence selected from the group consisting of: SEQ ID NOs: 1-5, SEQ ID NO: 7, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NOs: 13-63, residues 4-12 of the foregoing sequences that are 15 amino acids in length, and equivalents thereof characterized as having one or more (in specific embodiments, 1-5 or 1-3) amino acid substitutions that do not reduce specificity for PCSK9 by more than 50% (in specific embodiments, by more than 60%, 70%, 80%, and 90%); and/or (b) a light chain variable region comprising a CDR3 domain comprising (in select embodiments, consisting of) a sequence selected from the group consisting of: SEQ ID NOs: 295-301, SEQ ID NO: 303, SEQ ID NOs: 305-334, residues 4-13 of the foregoing sequences that are 16 amino acids in length, and equivalents thereof characterized as having one or more (in specific embodiments, 1-5 or 1-3) amino acid substitutions that do not reduce specificity for PCSK9 by more than 50% (in specific embodiments, by more than 60%, 70%, 80%, and 90%).

[0016] PCSK9-specific antagonists forming additional embodiments hereof comprise (a) a heavy chain variable region comprising a CDR2 domain comprising (in select embodiments, consisting of) a sequence selected from the group consisting of: SEQ ID NOs: 64-68, SEQ ID NO: 70, SEQ ID NO: 72, SEQ ID NO: 74, SEQ ID NOs: 76-182, residues 4-20 of the foregoing sequences that are 23 amino acids in length, and equivalents thereof characterized as having one or more (in specific embodiments, 1-5 or 1-3) amino acid substitutions that do not reduce specificity for PCSK9 by more than 50% (in specific embodiments, by more than 60%, 70%, 80%, and 90%); and/or (b) a light chain variable region comprising a CDR2 domain comprising (in select embodiments, consisting of) a sequence selected from the group consisting of: SEQ ID NOs: 335-339, SEQ ID NO: 341, SEQ ID NOs: 343-346, residues 4-10 of the foregoing sequences that are 13 amino acids in length, and equivalents thereof characterized as having one or more (in specific embodiments, 1-5 or 1-3) amino acid substitutions that do not reduce specificity for PCSK9 by more than 50% (in specific embodiments, by more than 60%, 70%, 80%, and 90%).

[0017] In specific embodiments, PCSK9-specific antagonists bind to human PCSK9 with a K_D of 1.2×10⁻⁶ M or less. In more specific embodiments, PCSK9-specific antagonists bind to human PCSK9 with a K_D of 1×10⁻⁷ M or less. In additional embodiments, PCSK9-specific antagonists bind to human PCSK9 with a K_D of 1×10⁻⁸ M or less. In further embodiments, PCSK9-specific antagonists bind to human PCSK9 with a K_D of 5×10⁻⁹ M or less, or of 1×10⁻⁹ M or less. In select embodiments, PCSK9-specific antagonists bind to human PCSK9 with a K_D of 1×10⁻¹⁰ M or less, a K_D of 1×10⁻¹¹ M or less, or a K_D of 1×10⁻¹² M or less. In specific embodiments, PCSK9-specific antagonists do not bind proteins other than PCSK9 at the above levels indicated for binding to PCSK9.

[0018] Particular embodiments of the present invention include PCSK9-specific antagonists which exhibit binding to PCSK9 at one of the above prescribed levels and compete for binding to PCSK9 with AX132 and its variants as described herein. AX132 and its disclosed variants, described as any antibody molecules fitting within the descriptions, sequence and/or functional limitations provided throughout the present disclosure, form important PCSK9-specific antagonists hereof.

[0019] AX132 antibody molecules are characterized as comprising a (i) heavy chain variable region (“VH”) comprising SEQ ID NO: 360 or SEQ ID NO: 361; and (ii) a light chain variable region (“VL”) comprising SEQ ID NO: 511. Said VH and VL regions comprise the full complement of disclosed CDRs 1, 2 and 3 for the VH [SEQ ID NOs: 189 (or SEQ ID NO: 191) as CDR1; SEQ ID NO: 68 (or SEQ ID NO: 70) as CDR2; and SEQ ID NO: 5 (or SEQ ID NO: 7) as CDR3] and VL regions [SEQ ID NOs: 349 (or SEQ ID NO: 351) as CDR1; SEQ ID NO: 339 (or SEQ ID NO: 341) as CDR2; and SEQ ID NO: 301 (or SEQ ID NO: 303) as CDR3], respectively. Examples of AX132 antibody molecules include without limitation: (i) a Fab which comprises a light chain comprising SEQ ID NO: 554 and an Fd chain comprising amino acids comprising amino acids 1-221 of SEQ ID NO: 552 (or SEQ ID NO: 552); (ii) a full length antibody molecule which comprises a light chain comprising SEQ ID NO: 558 and a heavy chain comprising SEQ ID NO: 556; and (iii) an antibody produced by the expression of SEQ ID NO: 560.

[0020] AX213 antibody molecules, an example of specific variants described herein, are characterized as comprising a (i) heavy chain variable region (“VH”) comprising SEQ ID NO: 362 or SEQ ID NO: 363; and (ii) a light chain variable region (“VL”) comprising SEQ ID NO: 511. Said VH and VL regions comprise the full complement of disclosed CDRs 1, 2 and 3 for the VH [SEQ ID NO: 193 (or SEQ ID NO: 195) as CDR1; SEQ ID NO: 72 (or SEQ ID NO: 74) as CDR2; and SEQ ID NO: 9 (or SEQ ID NO: 11) as CDR3)] and VL regions [SEQ ID NO: 349 (or SEQ ID NO: 351) as CDR1; SEQ ID NO: 339 (or SEQ ID NO: 341) as CDR2; and SEQ ID NO: 301 (or SEQ ID NO: 303) as CDR3], respectively. Examples of AX213 antibody molecules include without limitation: (i) a Fab which comprises a light chain comprising SEQ ID NO: 554 and an Fd chain comprising amino acids comprising amino acids 1-221 of SEQ ID NO: 562 (or SEQ ID NO: 562); (ii) a full length antibody molecule which comprises a light chain comprising SEQ ID NO: 566 and a heavy chain comprising SEQ ID NO: 564; and (iii) an antibody produced by the expression of SEQ ID NO: 569.

[0021] PCSK9-specific antagonists are effective in counteracting PCSK9-dependent inhibition of cellular LDL-uptake, and particularly human PCSK9-dependent inhibition of cellular LDL uptake. Repeatedly, PCSK9-specific antagonists as described herein have demonstrated dose-dependent inhibition of the effects of PCSK9 on LDL uptake. Accordingly, the disclosed PCSK9-specific antagonists are of import for lowering plasma LDL cholesterol levels. The disclosed antagonists also have utility for various diagnostic purposes, including the detection and quantification of PCSK9.

[0022] In particular embodiments, the present invention encompasses antibody molecules comprising the disclosed heavy and/or light chain variable regions, equivalents of said regions having one or more amino acid substitutions that do not substantially impact function, and homologs thereof. Select embodiments comprise isolated PCSK9-specific antagonists that comprise disclosed CDR domains or sets of the heavy and/or light chain CDR domains, and equivalents of such domains characterized as having one or more amino acid substitutions. As will be appreciated by those skilled in the art, fragments of PCSK9-specific antagonists that retain the ability to antagonize PCSK9 may be inserted into various frameworks; see, e.g., U.S. Pat. No. 6,818,418 and references contained therein, the collective disclosures of which are incorporated herein by reference, which discuss various scaffolds which may be used to display antibody loops previously selected on the basis of antigen binding. In the alternative, genes encoding for VL and VH may be joined, using recombinant methods, for example using a synthetic linker that enables them to be made as a single protein chain in which the VL and VH regions pair to form monovalent molecules, otherwise known as single chain Fvs (“ScFVs”); see, e.g., Bird et al., 1988 Science 242: 423-426, and Huston et al., 1988 Proc. Natl. Acad. Sci. USA 85:5879-5883, the disclosures of which are incorporated herein by reference. In another alternative, the VH and VL may be fused with two interactive domains, and form a Fab-like molecule, see, e.g., ccFv, Wang et al., U.S. Pat. No. 6,833,441 and U.S. Pat. No. 7,429,652.

[0023] PCSK-9 specific antagonists and fragments may be in the form of various non-antibody-based scaffolds, including but not limited to avimers (Avidia); DARPins (Molecular Partners); Adnectins (Adnexus), Anticalins (Pieris) and Affibodies (Affibody). The use of alternative scaffolds for protein binding is well appreciated in the scientific literature, see, e.g., Binz & Plückthun, 2005 Curr. Opin. Biotech. 16:1-11; the disclosure of which is incorporated herein by reference.

[0024] Accordingly, any PCSK9-specific antagonist, including antibody molecules and non-antibody-based scaffolds comprising (i) the disclosed heavy and/or light chain variable region CDR3 sequences (heavy chain variable region CDR3 sequence selected from SEQ ID NOs: 1-5, 7, 9, 11, 13-63, and residues 4-12 of the foregoing sequences that are 15 amino acids in length; light chain variable region CDR3 sequence selected from SEQ ID NOs: 295-301, 303, 305-334, and residues 4-13 of the foregoing sequences that are 16 amino acids in length), (ii) the disclosed heavy and/or light chain variable region CDR2 sequences (heavy chain variable region CDR2 sequence selected from SEQ ID NOs: 64-68, 70, 72, 74, 76-182, and residues 4-20 of the foregoing sequences that are 23 amino acids in length; light chain variable region CDR2 sequence selected from SEQ ID NOs: 335-339, 341, 343-346 and residues 4-10 of the foregoing sequences that are 13 amino acids in length), (iii) the disclosed heavy and/or light chain variable region CDR1 sequences (heavy chain variable region CDR1 sequence selected from SEQ ID NOs: 183-189, 191, 193, 195, 197-294, and residues 4-13 of the foregoing sequences that are 16 amino acids in length; light chain variable region CDR1 sequence selected from SEQ ID NOs: 347-349, 351, 353-359 and residues 4-14 of the foregoing sequences that are 17 amino acids in length), (iv) the disclosed heavy chain variable CDR1, CDR2 and CDR3 sequences or the disclosed light chain variable CDR1, CDR2 and CDR3 sequences, (v) a full complement (CDRs 1, 2 and 3) of the disclosed heavy and light chain CDRs within a variable region framework of a human heavy and/or light chain sequence, respectively, or (vi) the disclosed heavy and/or light chain variable regions (heavy chain variable sequence selected from SEQ ID NOs: 360-510; light chain variable sequence selected from SEQ ID NOs: 511-549) form important embodiments of the present invention; where antagonists, antibody molecules or scaffolds exhibit selectivity for PCSK9 and counteract PCSK9-dependent inhibition of cellular LDL-uptake.

[0025] In another aspect, the present invention provides nucleic acid encoding the disclosed PCSK9-specific antagonists and, in particular embodiments, PCSK9-specific antagonists which comprise the disclosed heavy and light chains, the disclosed variable heavy and light regions and select components thereof (including CDRs 1, 2 and/or 3), particularly the disclosed respective CDR3 or CDR2 regions. In another aspect, the present invention provides vectors comprising said nucleic acid. The present invention, additionally, provides isolated cell(s) comprising nucleic acid encoding disclosed PCSK9-specific antagonists. In another aspect, the present invention provides isolated cell(s) comprising a polypeptide or vector of the present invention.

[0026] The present invention provides methods for making PCSK9-specific antagonists disclosed herein including but not limited to antibodies, antigen binding fragments, derivatives, chimeric molecules, fusions of any of the foregoing with another polypeptide, or alternative structures/compositions capable of specifically binding PCSK9 which comprise the disclosed sequences. The methods comprise: (i) incubating a cell comprising nucleic acid encoding the PCSK9-specific antagonist(s), or which comprises individual nucleic acids encoding one or more components thereof, said nucleic acids which, when expressed, collectively produce the antagonist(s), under conditions that allow for the expression and/or assembly of the PCSK9-specific antagonist(s), and (ii) isolating said antagonist(s) from the cell. One of skill in the art can obtain PCSK9-specific antagonists disclosed herein using standard recombinant DNA techniques as well.

[0027] The present invention provides a method for antagonizing the activity or function of PCSK9 or a noted effect of PCSK9 which comprises contacting a cell, population of cells, or tissue sample of interest expressing PCSK9 (or treated with or having therein human PCSK9) with a PCSK9-specific antagonist disclosed herein under conditions that allow said antagonist to bind to PCSK9. Specific embodiments of the present invention include such methods wherein the cell is a human cell. Additional embodiments are wherein the cell expresses human-derived PCSK9.

[0028] In another aspect, the present invention provides a method for antagonizing the activity or function of PCSK9 or a noted effect of PCSK9 in a subject exhibiting a condition associated with PCSK9 activity, or a condition where the functioning of PCSK9 is contraindicated for a particular subject, which comprises administering to the subject a therapeutically effective amount of a PCSK9-specific antagonist of the present invention in a pharmaceutical or other composition.

[0029] The present invention, thus, encompasses a method of treating a condition associated with PCSK9 activity, or a condition wherein the functioning of PCSK9 is contraindicated for a particular subject, which comprises administering to the subject a therapeutically effective amount of a PCSK9-specific antagonist of the present invention in a pharmaceutical or other composition. In select embodiments, the condition is hypercholesterolemia, coronary heart disease, metabolic syndrome, acute coronary syndrome or related conditions.

[0030] In specific embodiments, the present invention encompasses a method of administering a disclosed PCSK9-specific antagonist to a subject which comprises delivering a therapeutically effective amount of a pharmaceutical or other composition comprising a PCSK9-specific antagonist as disclosed herein.

[0031] In another aspect, the present invention provides a pharmaceutical composition or other composition comprising a PCSK9-specific antagonist of the invention characterized as comprising a pharmaceutically acceptable carrier including but not limited to an excipient, diluent, stabilizer, buffer, or alternative designed to facilitate administration of the antagonist in the desired amount to the treated individual.

[0032] The following table offers a generalized outline of the sequences discussed in the present application. The Sequence Listing including all notations, sequences and features forms an express part of the disclosure hereof:

[0033]

TABLE 1
SEQ ID NO:	DESCRIPTION
SEQ ID NOs: 1-5, 7, 9,	HEAVY CHAIN CDR3
11, 13-63
SEQ ID NOs: 6, 8, 10,	HEAVY CHAIN CDR3; NUCLEIC ACID
12
SEQ ID NOs: 64-68, 70,	HEAVY CHAIN CDR2
72, 74, 76-182
SEQ ID NOs: 69, 71, 73,	HEAVY CHAIN CDR2; NUCLEIC ACID
75
SEQ ID NOs: 183-189,	HEAVY CHAIN CDR1
191, 193, 195, 197-294
SEQ ID NOs: 190, 192,	HEAVY CHAIN CDR1; NUCLEIC ACID
194, 196
SEQ ID NOs: 295-301,	LIGHT CHAIN CDR3
303, 305-334
SEQ ID NOs: 302, 304	LIGHT CHAIN CDR3; NUCLEIC ACID
SEQ ID NOs: 335-339,	LIGHT CHAIN CDR2
341, 343-346
SEQ ID NOs: 340, 342	LIGHT CHAIN CDR2; NUCLEIC ACID
SEQ ID NOs: 347-349,	LIGHT CHAIN CDR1
351, 353-359
SEQ ID NOs: 350, 352	LIGHT CHAIN CDR1; NUCLEIC ACID
SEQ ID NOs: 360-510	VARIABLE HEAVY REGIONS
SEQ ID NOs: 550, 561	VARIABLE HEAVY REGIONS;
	NUCLEIC ACID
SEQ ID NOs: 511-549	VARIABLE LIGHT REGIONS
SEQ ID NO: 551	VARIABLE LIGHT REGION;
	NUCLEIC ACID
SEQ ID NOs: 552, 562	FAB HEAVY CHAIN
SEQ ID NOs: 553, 563	FAB HEAVY CHAIN; NUCLEIC ACID
SEQ ID NO: 554	FAB LIGHT CHAIN
SEQ ID NO: 555	FAB LIGHT CHAIN; NUCLEIC ACID
SEQ ID NOs: 556, 564	IGG2 HEAVY CHAIN
SEQ ID NOs: 557, 565	IGG2 HEAVY CHAIN; NUCLEIC ACID
SEQ ID NOs: 558, 566	IGG2 LIGHT CHAIN
SEQ ID NOs: 559, 567,	IGG2 LIGHT CHAIN; NUCLEIC ACID
568
SEQ ID NOs: 560, 569	ANTIBODY EXPRESSION
	VECTOR SEQUENCE
SEQ ID NO: 570	FRAGMENT OF PROCESSING SITE
SEQ ID NO: 571	FRAGMENT OF PROCESSING SITE
SEQ ID NO: 572	Constant domain of IgG1
SEQ ID NO: 573	Constant domain of IgG2
SEQ ID NO: 574	Constant domain of IgG4
SEQ ID NO: 575	Constant domain of IgG2m4
SEQ ID NOs: 576-582	AX132 EPITOPES
SEQ ID NOs: 583-590	AX132 AND VARIANT FRAMEWORK
	REGIONS
SEQ ID NO: 591-592	CONSENSUS VARIABLE HEAVY
	AND VARIABLE LIGHT REGIONS,
	RESPECTIVELY
SEQ ID NO: 593-641	FIGURE SEQUENCES
SEQ ID NO: 642	PCSK9
SEQ ID NOs: 643-644	AX132 CONTACT RESIDUES
SEQ ID NO: 645	EGF_AB PEPTIDE
SEQ ID NOs: 646-647	pMAB9-AX132; and complementary
	sequence; respectively

[0054] The present invention relates to protein-specific antagonists of PCSK9 and, in particular embodiments, those antagonists that inhibit human PCSK9. Protein-specific antagonists of PCSK9 (or “PCSK9-specific antagonists”) in accordance herewith are effective in the selective binding to and inhibition of PCSK9 function and, thus, are of import in the treatment of conditions associated with or impacted by PCSK9 function, including, but not limited to, hypercholesterolemia, coronary heart disease, metabolic syndrome, acute coronary syndrome and related conditions. Use of the term “antagonist” refers to the fact that the subject molecule can antagonize the functioning of PCSK9. Use of the term “antagonizing” or derivatives thereof refers to the act of opposing, counteracting, inhibiting, neutralizing or curtailing one or more functions of PCSK9. Reference herein to PCSK9 function or PCSK9 activity refers to any function or activity that is driven by, requires, or is exacerbated or enhanced by PCSK9. PCSK9-specific antagonists as described herein have proven to be effective for counteracting human PCSK9-dependent inhibition of cellular LDL-uptake.

[0055] One important embodiment hereof relates to AX132 antibody molecules and variants thereof. Specific embodiments of the present invention include AX132 antibody molecules characterized as comprising a (i) heavy chain variable region (“VH”) comprising or consisting of SEQ ID NO: 360 or SEQ ID NO: 361; and (ii) a light chain variable region (“VL”) comprising SEQ ID NO: 511. Said VH and VL regions comprise the full complement of disclosed CDRs 1, 2 and 3 for the VH [SEQ ID NOs: 189 (or SEQ ID NO: 191) as CDR1; SEQ ID NO: 68 (or SEQ ID NO: 70) as CDR2; and SEQ ID NO: 5 (or SEQ ID NO: 7) as CDR3] and VL regions [SEQ ID NOs: 349 (or SEQ ID NO: 351) as CDR1; SEQ ID NO: 339 (or SEQ ID NO: 341) as CDR2; and SEQ ID NO: 301 (or SEQ ID NO: 303) as CDR3], respectively. Examples of AX132 antibody molecules include without limitation: (i) a Fab which comprises a light chain comprising SEQ ID NO: 554 and an Fd chain comprising amino acids comprising amino acids 1-221 of SEQ ID NO: 552 (or SEQ ID NO: 552); (ii) a full length antibody molecule which comprises a light chain comprising SEQ ID NO: 558 and a heavy chain comprising SEQ ID NO: 556; and (iii) an antibody produced by the expression of SEQ ID NO: 560.

[0056] In specific embodiments, AX132 variants comprise in contiguous order for one or both heavy or light chains: (a) framework 1 (FR1) sequence; (b) CDR1 sequence; (c) framework 2 (FR2) sequence; (d) CDR2 sequence; (e) framework 3 (FR3) sequence, (f) CDR3 sequence; and (g) framework 4 (FR4) sequence. In specific embodiments, the heavy chain comprises in contiguous order: (a) FR1 sequence SEQ ID NO: 583; (b) CDR1 sequence selected from the group consisting of: SEQ ID NOs: 183, 185, 187, 189, 193, and 197-294; (c) FR2 sequence SEQ ID NO: 584; (d) CDR2 sequence selected from the group consisting of: SEQ ID NOs: 64, 66, 68, 72, and 76-182; (e) FR3 sequence SEQ ID NO: 585; (f) CDR3 sequence selected from the group consisting of: SEQ ID NOs: 1, 3, 5, 9, and 13-63; and (g) FR4 sequence SEQ ID NO: 586. In specific embodiments, the light chain comprises in contiguous order: (a) FR1 sequence SEQ ID NO: 587; (b) CDR1 sequence selected from the group consisting of: SEQ ID NOs: 347, 349 and 353-359; (c) FR2 sequence SEQ ID NO: 588; (d) CDR2 sequence selected from the group consisting of: SEQ ID NOs: 335, 337, 339, and 3430-346; (e) FR3 sequence SEQ ID NO: 589; (f) CDR3 sequence selected from the group consisting of: SEQ ID NOs: 295, 297, 299, 301, and 305-334; and (g) FR4 sequence SEQ ID NO: 590. The present invention includes antibody molecules have both heavy and light chains as described above and equivalents thereof characterized as having one or more (in specific embodiments, 1-5 or 1-3) amino acid substitutions that do not reduce specificity for PCSK9 by more than 50% (in specific embodiments, by more than 60%, 70%, 80%, and 90%). The select group of AX132 antibodies exemplified demonstrate without limitation that PCSK9-specific antagonists as disclosed herein effectively inhibit human PCSK9.

[0057] One particular AX132 variant is AX213. AX213 antibody molecules are characterized as comprising a (i) heavy chain variable region (“VH”) comprising SEQ ID NO: 362 or SEQ ID NO: 363; and (ii) a light chain variable region (“VL”) comprising SEQ ID NO: 511. Said VH and VL regions comprise the full complement of disclosed CDRs 1, 2 and 3 for the VH [SEQ ID NO: 193 (or SEQ ID NO: 195) as CDR1; SEQ ID NO: 72 (or SEQ ID NO: 74) as CDR2; and SEQ ID NO: 9 (or SEQ ID NO: 11) as CDR3)] and VL regions [SEQ ID NO: 349 (or SEQ ID NO: 351) as CDR1; SEQ ID NO: 339 (or SEQ ID NO: 341) as CDR2; and SEQ ID NO: 301 (or SEQ ID NO: 303) as CDR3], respectively. Examples of AX213 antibody molecules include without limitation: (i) a Fab which comprises a light chain comprising SEQ ID NO: 554 and an Fd chain comprising amino acids comprising amino acids 1-221 of SEQ ID NO: 562 (or SEQ ID NO: 562); (ii) a full length antibody molecule which comprises a light chain comprising SEQ ID NO: 566 and a heavy chain comprising SEQ ID NO: 564; and (iii) an antibody produced by the expression of SEQ ID NO: 569.

[0058] The CDR definitions arrived at and disclosed herein were defined using the Abmaxis in-silico program, Luo et al., U.S. Pat. No. 7,117,096 and U.S. Patent Publication No. US2004/0010376 or WO03/099999. Applicants wish to note, however, that various other methods are also available to delineate and define the start and end points of the CDR sequences, including but not limited to Kabat, 1991 Sequences of Proteins of Immunological Interest, 5^th edit., NIH Publication no. 91-3242 U.S. Department of Health and Human Services; Clothia et al., 1987 J. Mol. Biol. 196:901-917; Clothia et al., 1989 Nature 342:877-883; Lefranc, 1997 Immunol. Today, 18:509; and Chen et al., 1999 J. Mol. Biol. 293:865-881. These and other methods have been reviewed and are well within the realm of skills possessed by those in the art; see, e.g., Honegger & Plückthun, 2001 J. Mol. Biol. 309:657-670. While the current inventors have employed the Abmaxis program to define the CDRs, the present invention fully encompasses the different definitions around the sequences and the varying CDR delineations arrived at through use of any different analysis software or methods. For example, CDRs may also be defined as the component of the antibody molecules that binds an epitope or which is involved in binding the antigen. The CDR may comprise from 5-20 amino acids. In particular embodiments, the CDRs may further comprise from 2-6 flanking amino acids on each side of the CDR into the framework region. The above methods and resulting CDR definitions based on the presently disclosed sequences are fully within the scope of the present disclosure and anticipated herein.

[0059] PCSK9-specific molecules also have utility for various diagnostic purposes in the detection and quantification of PCSK9.

[0060] Disclosed PCSK9-specific antagonists are, furthermore, unique in that select embodiments have demonstrated a preferential recognition of processed PCSK9, the active form of PCSK9.

[0061] PCSK9-specific antagonists as disclosed herein are desirable molecules for lowering plasma LDL cholesterol levels and are of utility for any primate, mammal or vertebrate of commercial or domestic veterinary importance. PCSK9-specific antagonists are of utility as well to inhibit the activity of PCSK9 in any population of cells or tissues possessing the LDL receptor. The utility of the disclosed antagonists is directly measurable by assays readily available to the skilled artisan. Means for measuring LDL uptake are described in the literature; see, e.g., Barak & Webb, 1981 J. Cell Biol. 90:595-604, and Stephan & Yurachek, 1993 J. Lipid Res. 34:325330. In addition, means for measuring LDL cholesterol in plasma is well described in the literature; see, e.g., McNamara et al., 2006 Clinica Chimica Acta 369:158-167. The particular impact of the disclosed antagonists on cellular LDL uptake may also be measured through a method which comprises providing purified PCSK9 and labeled LDL particles to a cell sample; providing a PCSK9 antagonist to the cell sample; incubating said cell sample for a period of time sufficient to allow LDL particle uptake by the cells; quantifying the amount of label incorporated into the cell; and identifying those antagonists that result in an increase in the amount of quantified label taken up by the cells as compared with that observed when PCSK9 is administered alone. An additional method for measuring the impact of the disclosed antagonists comprises providing purified PCSK9 and labeled LDL particles to a cell sample; providing a PCSK9 antagonist to the cell sample; incubating said cell sample for a period of time sufficient to allow LDL particle uptake by the cells; isolating cells of the cell sample by removing the supernate; reducing non-specific association of labeled LDL particles (whether to the plate, the cells, or anything other than the LDL receptor); lysing the cells; quantifying the amount of label retained within the cell lysate; and identifying those antagonists that result in an increase in the amount of quantified label taken up by the cells as compared with that observed when PCSK9 is administered alone. Antagonists that result in an increase in the amount of quantified label are PCSK9 antagonists.

[0062] Any type of cell bearing the LDL receptor can be employed in the above methods including, but not limited to HEK cells, HepG2 cells, and CHO cells. LDL particles derived from any source are of use in the above-described assays. In particular assays, the LDL particles are fresh particles derived from blood. This can be accomplished by any method available to the skilled artisan including, but not limited to, the method of Havel et al., 1955 J. Clin. Invest. 34: 1345-1353. The LDL particles may be labeled with fluorescence. The labeled LDL particles may have incorporated therein visible wavelength excited fluorophore 3,3′-dioctadecylindocarbocyanine iodide (dil(3)) to form the highly fluorescent LDL derivative dil(3)-LDL. Any label which enables the skilled artisan to detect LDL in the cellular lysate may be used. An LDL analog may be used that would only become detectable (e.g., become fluorescent or fluoresce at a different wavelength, etc.) when metabolized intracellularly or, for instance, if it were to become associated with (or dissociated from) other molecules in the process of becoming internalized (e.g. a FRET assay, in which an LDL analog would become associated with a secondary fluor, or else be dissociated from a quencher). Any means available in the art for detecting internalization of labeled LDL particles can be employed. The incubation time for the LDL particles and PCSK9 with the cells is an amount of time sufficient to allow LDL particle uptake by the cells. This time may be within the range of 5 minutes to 360 minutes. The concentration of PCSK9 added to the cells may be in the range of 1 nM to 5 μM and, in specific methods, be in the range of 0.1 nM to 3 μM. One specific means by which the skilled artisan can determine a range of concentrations for a particular PCSK9 protein is to develop a dose response curve in the LDL-uptake assay. A concentration of PCSK9 can be selected that promotes close to maximal loss of LDL-uptake and is still in the linear range of the dose response curve. Typically, this concentration is ˜5 times the EC-50 of the protein extracted from the dose response curve. The concentrations can vary by protein.

[0063] Broadly, PCSK9-specific antagonists as defined herein selectively recognize and specifically bind to PCSK9. An antibody is typically said to specifically bind an antigen when the dissociation constant is ≦1 μM, preferably ≦100 nM and most preferably ≦10 nM. Use of the terms “selective” or “specific” herein, further, refers to the fact that the disclosed antagonists do not show significant binding to proteins other than PCSK9, except in those specific instances where the antagonist is supplemented or designed to confer an additional, distinct specificity to the PCSK9-specific binding portion (as, for example, in bispecific or bifunctional molecules where the molecule is designed to bind two molecules or effect two functions, at least one of which is to specifically bind PCSK9). In specific embodiments, PCSK9-specific antagonists bind to human PCSK9 with a K_D of 1.2×10⁻⁶ M or less. In more specific embodiments, PCSK9-specific antagonists bind to human PCSK9 with a K_D of 5×10⁻⁷ M or less, of 2×10⁻⁷ M or less, or of 1×10⁻⁷ M or less. In additional embodiments, PCSK9-specific antagonists bind to human PCSK9 with a K_D of 1×10⁻⁸ M or less. In further embodiments, PCSK9-specific antagonists bind to human PCSK9 with a K_D of 5×10⁻⁹ M or less, or of 1×10⁻⁹ M or less. In select embodiments, PCSK9-specific antagonists bind to human PCSK9 with a K_D of 1×10⁻¹⁰ M or less, a K_D of 1×10⁻¹¹ M or less, or a K_D of 1×10⁻¹² M or less. In specific embodiments, PCSK9-specific antagonists do not bind proteins other than PCSK9 at the above K_Ds. K_D refers to the dissociation constant obtained from the ratio of K_d (the dissociation rate of a particular binding molecule-target protein interaction) to K_a (the association rate of the particular binding molecule-target protein interaction), or K_d/K_a which is expressed as a molar concentration (M). K_D values can be determined using methods well established in the art. A preferred method for determining the K_D of a binding molecule is by using surface plasmon resonance, for example employing a biosensor system such as a Biacore™ (GE Healthcare Life Sciences) system.

[0064] PCSK9-specific antagonists disclosed herein have been shown to dose-dependently inhibit human PCSK9 dependent effects on LDL uptake. Accordingly, PCSK9-specific antagonists as disclosed herein are characterized by their ability to counteract PCSK9-dependent inhibition of LDL uptake into cells. This uptake of LDL into cells by the LDL receptor is referred to herein as “cellular LDL uptake”. In specific embodiments, PCSK9-specific antagonists counteract or antagonize human PCSK9-dependent inhibition of LDL uptake into cells, exhibiting an IC₅₀ of less than 1.0×10⁻⁶ M, or, in order of preference, less than 1×10⁻⁷ M, 1×10⁻⁸ M, 1×10⁻⁹ M, 1×10⁻¹⁰ M, 1×10⁻¹¹ M and 1×10⁻¹² M. The extent of inhibition by any PCSK9-specific antagonist may be measured quantitatively in statistical comparison to a control, or via any alternative method available in the art for assessing a negative effect on, or inhibition of, PCSK9 function (i.e., any method capable of assessing antagonism of PCSK9 function). In specific embodiments, the inhibition is at least about 10% inhibition. In other embodiments, the inhibition is at least 20%, 30%, 40%, 50%, 60%, 70,%, 80%, 90%, or 95%. Accordingly, PCSK9-specific antagonists capable of effecting these levels of inhibition of PCSK9 function form particular embodiments hereof. Specific embodiments provide PCSK9 antagonists as described that, upon administration to a subject, lower LDL by at least 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65% and above. In specific embodiments, the PCSK9 antagonists lower LDL by those levels for a period of at least 7 days, 10 days, 15 days, 20 days, 25 days, 30 days, 35 days, 40 days and longer. In particular embodiments, the percent lowering is greater than or equal to 10, 15, 20 and 25 for over 20, 30 or 40 days. Particular embodiments, provide lowering greater than or equal to 25% for over 40 days (see, e.g., Example 19 and FIG. 17). Specific embodiments also provide for PCSK9-specific antagonists that bind to human FcRn at approximately pH 6.0 and dissociate at approximately pH 7.3 (see, e.g., Example 17 and FIGS. 14-15). Particular embodiments are wherein the disclosed PCSK9-specific antagonists exhibit a dissociation of <5% (in specific embodiments, less than 3% or 1%) at neutral pH. Dissociation (or % bound) can be calculated as described in Example 17. Specific embodiments, also provide PCSK-9 specific antagonists as described herein that have a ½ life in mice of greater than 50, 60, 70, 80, 90 or 95 hours (see, e.g., Example 18 and FIG. 16). In particular embodiments, PCSK9-specific antagonists are provided that have a ½ life in primates of greater than 50, 60, 70, 80, 90, 100, 110, 120, 130, 140 and 145 hours (see, e.g., Example 18). The present invention also provides, in specific embodiments, PCSK9-specific antagonists that, after 1 week of stress at 45° C. (under conditions similar to that described in Example 20), in pH 5, 6, 7 or 8 buffers have essentially no increase in oligomers, higher order aggregates and exhibit no clipping (see, e.g., Example 20 and Table 13). In specific embodiments, the above effects are as seen in humans and non-human primates (or where particularly specified, mice). In specific embodiments, the above effects are seen following intravenous or subcutaneous administration.

[0065] A PCSK9-specific antagonist in accordance herewith can be any binding molecule that specifically binds human PCSK9 protein including, but not limited to, antibody molecules as defined below, any PCSK9-specific binding structure, any polypeptide or nucleic acid structure that specifically binds PCSK9, and any of the foregoing incorporated into various protein scaffolds; including but not limited to, various non-antibody-based scaffolds, and various structures capable of affording or allowing for selective binding to PCSK9 including but not limited to small modular immunopharmaceuticals (or “SMIPs”; see, Haan & Maggos, 2004 Biocentury January 26); Immunity proteins (see, e.g., Chak et al., 1996 Proc. Natl. Acad. Sci. USA 93:6437-6442); cytochrome b562 (see Ku and Schultz, 1995 Proc. Natl. Acad. Sci. USA 92:6552-6556); the peptide α2p8 (see Barthe et al., 2000 Protein Sci. 9:942-955); avimers (Avidia; see Silverman et al., 2005 Nat. Biotechnol. 23:1556-1561); DARPins (Molecular Partners; see Binz et al., 2003 J. Mol. Biol. 332:489-503; and Forrer et al., 2003 FEBS Lett. 539:2-6); Tetranectins (see, Kastrup et al., 1998 Acta. Crystallogr. D. Biol. Crystallogr. 54:757-766); Adnectins (Adnexus; see, Xu et al., 2002 Chem. Biol. 9:933-942), Anticalins (Pieris; see Vogt & Skerra, 2004 Chemobiochem. 5:191-199; Beste et al., 1999 Proc. Natl. Acad. Sci. USA 96:1898-1903; Lamla & Erdmann, 2003 J. Mol. Biol. 329:381-388; and Lamla & Erdmann, 2004 Protein Expr. Purif. 33:39-47); A-domain proteins (see North & Blacklow, 1999 Biochemistry 38:3926-3935), Lipocalins (see Schlehuber & Skerra, 2005 Drug Discov. Today 10:23-33); Repeat-motif proteins such as Ankyrin repeat proteins (see Sedgwick & Smerdon, 1999 Trends Biochem. Sci. 24:311-316; Mosavi et al., 2002 Proc. Natl. Acad. Sci. USA 99:16029-16034; and Binz et al., 2004 Nat. Biotechnol. 22:575-582); Insect Defensin A (see Zhao et al., 2004 Peptides 25:629-635); Kunitz domains (see Roberts et al., 1992 Proc. Natl. Acad. Sci. USA 89:2429-2433; Roberts et al., 1992 Gene 121:9-15; Dennis & Lazarus, 1994 J. Biol. Chem. 269:22129-22136; and Dennis & Lazarus, 1994 J. Biol. Chem. 269:22137-22144); PDZ-Domains (see Schneider et al., 1999 Nat. Biotechnol. 17:170-175); Scorpion toxins such as Charybdotoxin (see Vita et al., 1998 Biopolymers 47:93-100); 10^th fibronectin type III domain (or 10Fn3; see Koide et al., 1998 J. Mol. Biol. 284:1141-1151, and Xu et al., 2002 Chem. Biol. 9:933-942); CTLA-4 (extracellular domain; see Nuttall et al., 1999 Proteins 36:217-227; and Irving et al., 2001 J. Immunol. Methods 248:31-45); Knottins (see Souriau et al., 2005 Biochemistry 44:7143-7155 and Lehtio et al., 2000 Proteins 41:316-322); Neocarzinostatin (see Heyd et al. 2003 Biochemistry 42:5674-5683); carbohydrate binding module 4-2 (CBM4-2; see Cicortas et al., 2004 Protein Eng. Des. Sel. 17:213-221); Tendamistat (see McConnell & Hoess, 1995 J. Mol. Biol. 250:460-470, and Li et al., 2003 Protein Eng. 16:65-72); T cell receptor (see Holler et al., 2000 Proc. Natl. Acad. Sci. USA 97:5387-5392; Shusta et al., 2000 Nat. Biotechnol. 18:754-759; and Li et al., 2005 Nat. Biotechnol. 23:349-354); Affibodies (Affibody; see Nord et al., 1995 Protein Eng. 8:601-608; Nord et al., 1997 Nat. Biotechnol. 15:772-777; Gunneriusson et al., 1999 Protein Eng. 12:873-878); and other selective binding proteins or scaffolds recognized in the literature; see, e.g., Binz & Plückthun, 2005 Curr. Opin. Biotech. 16:1-11; Gill & Damle, 2006 Curr. Opin. Biotechnol. 17:1-6; Hosse et al., 2006 Protein Science 15:14-27; Binz et al., 2005 Nat. Biotechnol. 23:1257-1268; Hey et al., 2005 Trends in Biotechnol. 23:514-522; Binz & Plückthun, 2005 Curr. Opin. Biotech. 16:459-469; Nygren & Skerra, 2004 J. Immunolog. Methods 290:3-28; Nygren & Uhlen, 1997 Curr. Opin. Struct. Biol. 7:463-469; the disclosures of which are incorporated herein by reference. Antibodies and the use of antigen-binding fragments is well defined and understood in the literature. The use of alternative scaffolds for protein binding is well appreciated in the scientific literature as well, see, e.g., Binz & Plückthun, 2005 Curr. Opin. Biotech. 16:1-11; Gill & Damle, 2006 Curr. Opin. Biotechnol. 17:1-6; Hosse et al., 2006 Protein Science 15:14-27; Binz et al., 2005 Nat. Biotechnol. 23:1257-1268; Hey et al., 2005 Trends in Biotechnol. 23:514-522; Binz & Plückthun, 2005 Curr. Opin. Biotech. 16:459-469; Nygren & Skerra, 2004 J. Immunolog. Methods 290:3-28; Nygren & Uhlen, 1997 Curr. Opin. Struct. Biol. 7:463-469; the disclosures of which are incorporated herein by reference. Accordingly, non-antibody-based scaffolds or antagonist molecules in accordance herewith exhibiting selectivity for PCSK9 that counteract PCSK9-dependent inhibition of cellular LDL-uptake form important embodiments of the present invention. Aptamers (nucleic acid or peptide molecules capable of selectively binding a target molecule) are one specific example. They can be selected from random sequence pools or identified from natural sources such as riboswitches. Peptide aptamers, nucleic acid aptamers (e.g., structured nucleic acid, including both DNA and RNA-based structures) and nucleic acid decoys can be effective for selectively binding and inhibiting proteins of interest; see, e.g., Hoppe-Seyler & Butz, 2000 J. Mol. Med. 78:426-430; Bock et al., 1992 Nature 355:564-566; Bunka & Stockley, 2006 Nat. Rev. Microbiol. 4:588-596; Martell et al., 2002 Molec. Ther. 6:30-34; Jayasena, 1999 Clin. Chem. 45:1628-1650; the disclosures of which are incorporated herein by reference.

[0066] The three-dimensional structure of PCSK9 in complex with the AX132 FAb, determined using x-ray crystallography, revealed that a linear sequence of the light chain of this FAb encompassing residues 26-34 with a sequence of SQYVGSYLN (SEQ ID NO: 643) makes a specific interaction with the surface of PCSK9 used to bind the EGF-A domain of LDLR. This observation suggests that peptides, heterologous proteins, or other entities that include this sequence of amino acids could be designed and used to specifically disrupt the interaction between PCSK9 and LDLR. Smaller subsets of this sequence may also be useful, and the structural studies suggest that residues 28-32 (YVGSY) (SEQ ID NO: 644) appears to be the shortest such sequence that might confer specific recognition of the PCSK9 surface. Furthermore, the crystal structure of the PCSK9:AX132 Fab complex can be used to rationally design new chemical entities that embody similar interactions as that observed in the crystal structure. Accordingly, polypeptides or peptides comprising (or consisting essentially of: SEQ ID NO: 643 or SEQ ID NO: 644 are contemplated herein.

[0067] Given AX132's significant neutralizing activity and the activity of its variants, it is clearly of interest to identify other PCSK9-specific antagonists that bind to PCSK9 in the same manner as AX132 or one of its variants. One means of identifying antagonists and particularly antibodies that bind to the same region or epitope as AX132 or its variants, or an overlapping epitope is through a competition or similar assay where the candidate antibody or binding molecule would have to out-compete AX132 (or variant) for the epitope. Competitive antagonists encompassed herein are molecules that inhibit (i.e., prevent, or interfere with, AX132 (or variant) binding in comparison to a control) or reduce AX132 (or variant) binding by at least 50%, 60%, 70%, and 80% in order of increasing preference (even more preferably, at least 90% and, most preferably, at least 95%) at 1 μM or less with AX132 (or variant) at or below its K_D, and in particular those molecules that antagonize (i) PCSK9 binding to the LDL receptor, (ii) PCSK9 internalization into cells, or (iii) both PCSK9 binding to the LDL receptor and PCSK9 internalization into cells. Competition between binding members may be readily assayed in vitro for example using ELISA and/or by monitoring the interaction of the antibodies with PCSK9 in solution. The exact means for conducting the analysis is not critical. PCSK9 may be immobilized to a 96-well plate or may be placed in a homogenous solution. In specific embodiments, the ability of unlabeled candidate antibody(ies) to block the binding of labeled AX132 (or variant) can be measured using radioactive, enzyme or other labels. In the reverse assay, the ability of unlabeled antibodies to interfere with the interaction of labeled AX132 (or variant) with PCSK9 wherein said AX132 (or variant) and PCSK9 are already bound is determined. In specific embodiments, (i) PCSK9 is contacted with labeled AX132 (or variant); (ii) PCSK9 is contacted with the candidate antibody or pool of antibodies; and (iii) antibodies capable of interrupting or preventing complexes between PCSK9 and AX132 (or variant) are identified. The readout in such an example is through measurement of bound label. AX132 (or variant) and the candidate antibody(ies) may be added in any order or at the same time.

[0068] Antibodies identified as AX132 (or variant) competitors in the above or other suitable assays may be tested for the ability to antagonize or neutralize (i) PCSK9 binding to the LDL receptor; and/or (ii) PCSK9 internalization into cells. These parameters may be measured through the use of assays similar to that employed or described in the current specification. In specific embodiments, the inhibition demonstrated by the competing antibody is at least about 10% inhibition. In other embodiments, the inhibition is at least 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% or 95%.

[0069] The present invention specifically encompasses PCSK9-specific antagonists and particularly monoclonal antibody molecules (and their corresponding amino acid and nucleic acid sequences) that selectively bind to the same epitope as AX132 (or variant) or an overlapping epitope interfering with AX132 (or variant)'s binding to PCSK9. Monoclonal antibodies that specifically bind to the epitope of AX132 (or variant), or an overlapping epitope antagonize or neutralize (i) PCSK9 binding to the LDL receptor; (ii) PCSK9 internalization into cells, or (iii) both. A monoclonal antibody molecule in accordance herewith may be an intact (complete or full length) antibody, a substantially intact antibody, or a portion or fragment of an antibody comprising an antigen-binding portion, e.g., a Fab fragment, Fab′ fragment or F(ab′)₂ fragment of a murine antibody or of a chimeric antibody or of a humanized antibody or of a human antibody. Monoclonal, as used herein, refers to a homogeneous or substantially homogeneous (or pure) antibody population (i.e., at least about 90%, 91%, 92%, 93%, 94%, 95%, 96%, more preferably at least about 97% or 98%, or most preferably at least 99% of the antibodies in the population are identical and would compete in an ELISA assay for the same antigen or epitope). In specific embodiments of the present invention, the present invention provides monoclonal antibodies that (i) compete for binding to PCSK9 with a AX132 (or variant) antibody molecule, reducing AX132 (or variant) binding by at least 50% at 1 μM or less with AX132 (or variant) at or below its K_D, (ii) block PCSK9 binding to the LDL receptor, (iii) inhibit PCSK9 internalization into the cell, and (iv) comprise a specific antigen-binding region, VH, VL, set of CDRs or heavy CDR3, heavy and/or light chain or any variant of these components as described herein.

[0070] In any of the above assays for identifying antibodies binding the same or overlapping epitope region as AX132 (or variant), binding of the known binder (i.e., AX132 (or variant) antibody molecule) as compared to the binding of the candidate binder should be distinguishable. This can (but need not) be accomplished through the use of labels on either or both molecules as will be readily appreciated by the skilled artisan. Labels, as used herein, refer to another molecule or agent incorporated into/affixed to the antibody molecule. In one embodiment, the label is a detectable marker, e.g., a radiolabeled amino acid or attachment to a polypeptide of biotinyl moieties that can be detected by marked avidin (e.g., streptavidin containing a fluorescent marker or enzymatic activity that can be detected by optical or colorimetric methods). Various methods of labeling polypeptides and glycoproteins are known in the art and may be used. Examples of labels for polypeptides include, but are not limited to, the following: radioisotopes or radionuclides (e.g., ³H, ¹⁴C, ¹⁵N, ³⁵S, ⁹⁰Y, ⁹⁹Tc, ¹¹¹In, ¹²⁵I, ¹³¹I), fluorescent labels (e.g., FITC, rhodamine, lanthanide phosphors), enzymatic labels (e.g., horseradish peroxidase, β-galactosidase, luciferase, alkaline phosphatase), chemiluminescent markers, biotinyl groups, predetermined polypeptide epitopes recognized by a secondary reporter (e.g., leucine zipper pair sequences, binding sites for secondary antibodies, metal binding domains, epitope tags), magnetic agents, such as gadolinium chelates, toxins such as pertussis toxin, taxol, cytochalasin B, gramicidin D, ethidium bromide, emetine, mitomycin, etoposide, tenoposide, vincristine, vinblastine, colchicin, doxorubicin, daunorubicin, dihydroxy anthracin dione, mitoxantrone, mithramycin, actinomycin D, 1-dehydrotestosterone, glucocorticoids, procaine, tetracaine, lidocaine, propranolol, and puromycin and analogs or homologs thereof. In some embodiments, labels are attached by spacer arms of various lengths to reduce potential steric hindrance.

[0071] In particular embodiments, the present invention encompasses antagonists as described herein characterized as binding specifically to any epitope sequence selected from the group consisting of: SEQ ID NOs: 576, 577, 579-582 and 237-RDA, or regions therein such as 157-NL-158 or SEQ ID NO: 578. In particular embodiments, the epitope sequence is within SEQ ID NOs: 576 and/or 577, or sub-regions therein such as 157-NL-158 or SEQ ID NO: 578. In particular embodiments, the antagonists described herein bind to SEQ ID NOs: 579, 580, 581 and 582, as well as 237-RDA. These epitopes are described further in Example 8 and in FIG. 4. The numerical numbers provide the starting and/or ending position on human PCSK9.

[0072] In specific embodiments, binding of a PCSK9-specific antagonist is significantly reduced or a mutant PCSK9 protein having one or more (e.g., 1, 2, 3, 4, 5 or more) mutations at the following residue positions: 192 and 379, as compared to a wild-type PCSK9 protein (SEQ ID NO: 642). In certain embodiments, binding of a PCSK9-specific antagonist is significantly reduced for a mutant PCSK9 protein having one or more (e.g., 1, 2, 3, 4, 5 or more) of the following mutations: D192G and F379Y.

[0073] An AX132 (or variant) antibody used as the standard for the competition assays may be any antibody molecule described herein. Molecules (peptides, antagonists, antibody molecules, etc.) tested may be from any source or library. In particular embodiments, the molecules are selected from a phage display library. In specific embodiments the molecules are selected using an EGF_AB peptide (293-DKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQ RRCEDIDECQDPDTCSQLCVNLE-372; SEQ ID NO: 645) that competes with AX132 in a manner similar to that described in Example 11.

[0074] Expression and selection of any of the PCSK9-specific antagonists described in the present application may be achieved using suitable technologies including, but not limited to phage display (see, e.g., International Application Number WO 92/01047, Kay et al., 1996 Phage Display of Peptides and Proteins: A Laboratory Manual, San Diego: Academic Press), Wang et al., 2010 J. Mol. Biol. 1088-1101; Wang et al., U.S. Pat. No. 7,175,983, yeast display, bacterial display, T7 display, and ribosome display (see, e.g., Lowe & Jermutus, 2004 Curr. Pharm. Biotech. 517-527).

[0075] Particular PCSK9-specific antagonists forming part of the present invention are antibody molecules or antibodies. “Antibody molecule” or “Antibody” as described herein refers to an immunoglobulin-derived structure with selective binding to human PCSK9 including, but not limited to, a full length or whole antibody, an antigen binding fragment (a fragment derived, physically or conceptually, from an antibody structure), a derivative of any of the foregoing, a fusion of any of the foregoing with another polypeptide, or any alternative structure/composition which incorporates any of the foregoing for purposes of selectively binding to/inhibiting the function of PCSK9. Antibody molecules can exist, for example, as intact immunoglobulins or as a number of well characterized fragments produced by, for example, digestion with various peptidases. The recognized immunoglobulin genes include the kappa, lambda, alpha, gamma, delta, epsilon and mu constant region genes, as well as a myriad of immunoglobulin variable region genes. Light chains are classified as gamma, mu, alpha, delta, or epsilon, which in turn define the immunoglobulin classes, IgG, IgM, IgA, IgD and IgE, respectively. “Whole” antibodies or “full length” antibodies often refers to proteins that comprise two heavy (H) and two light (L) chains inter-connected by disulfide bonds which comprise: (1) in terms of the heavy chains, a variable region (abbreviated herein as “V_H”) and a heavy chain constant region which comprises three domains, C_H1, C_H2, and C_H3; and (2) in terms of the light chains, a light chain variable region (abbreviated herein as “V_L”) and a light chain constant region which comprises one domain, C_L. Pepsin digests an antibody below the disulfide linkages in the hinge region to produce F(ab)′₂, a dimer of Fab which itself is a light chain joined to V_H-C_H1 by a disulfide bond. The F(ab)′₂ may be reduced under mild conditions to break the disulfide linkage in the hinge region thereby converting the F(ab)′₂ dimer into an Fab′ monomer. The Fab′ monomer is essentially a Fab with part of the hinge region broken. While various antibody fragments are defined in terms of the digestion of an intact antibody, one of skill will appreciate that such Fab′ fragments may be synthesized de novo either chemically or by utilizing recombinant DNA methodology. Thus, the term antibody, as used herein, also includes antibody fragments either produced by the modification of whole antibodies or those synthesized de novo using recombinant DNA methodologies.

[0076] Antibody fragments and, more specifically, antigen binding fragments are molecules possessing an antibody variable region or segment thereof (which comprises one or more of the disclosed CDR 3 or CDR2 domains, heavy and/or light, within framework regions of heavy and/or light chains, as appropriate), which confers selective binding to PCSK9, and particularly human PCSK9. Antibody fragments containing such an antibody variable region include, but are not limited to the following antibody molecules: a Fab, a F(ab′)₂, a Fd, a Fv, a scFv, ccFv, bispecific antibody molecules (antibody molecules comprising a PCSK9-specific antibody or antigen binding fragment as disclosed herein linked to a second functional moiety having a different binding specificity than the antibody, including, without limitation, another peptide or protein such as an antibody, or receptor ligand), a bispecific single chain Fv dimer, an isolated CDR3, a minibody, a ‘scAb’, a dAb fragment, a diabody, a triabody, a tetrabody, a minibody, and artificial antibodies based upon protein scaffolds, including but not limited to fibronectin type III polypeptide antibodies (see, e.g., U.S. Pat. No. 6,703,199 and International Application Numbers WO 02/32925 and WO 00/34784) or cytochrome B; see, e.g., Nygren et al., 1997 Curr. Opinion Struct. Biol. 7:463-469; the disclosures of which are incorporated herein by reference. The antibody portions or binding fragments may be natural, or partly or wholly synthetically produced. Such antibody portions can be prepared by various means known by one of skill in the art, including, but not limited to, conventional techniques, such as papain or pepsin digestion. One of skill in the art will, furthermore, appreciate that any of the above antibody molecules, including full length as well as the various antibody fragments, may be synthesized de novo either chemically or by utilizing recombinant DNA methodology. Thus, the term antibody, as used herein, also includes full length antibodies and antibody fragments either produced by the generation or modification of whole antibodies or those synthesized de novo using recombinant DNA methodologies.

[0077] The term “isolated” as used herein in reference to antibody molecules, PCSK9-specific antagonists in general, encoding nucleic acid or other describes a property as it pertains to the disclosed PCSK9-specific antagonists, nucleic acid or other that makes them different from that found in nature. The difference can be, for example, that they are of a different purity than that found in nature, or that they are of a different structure or form part of a different structure than that found in nature. A structure not found in nature, for example, includes recombinant human immunoglobulin structures including, but not limited to, recombinant human immunoglobulin structures with optimized CDRs. Other examples of structures not found in nature are PCSK9-specific antagonists or nucleic acid substantially free of other cellular material. Isolated PCSK9-specific antagonists are generally free of other protein-specific antagonists having different protein specificities (i.e., possess an affinity for other than PCSK9).

[0078] In one particular aspect, the present invention provides isolated PCSK9-specific antagonists which antagonize PCSK9 function. In particular embodiments, said PCSK9-specific antagonists inhibit human PCSK9's antagonism of cellular LDL uptake by interfering with PCSK9 binding to the LDL receptor and resultant PCSK9 cell internalization. Disclosed PCSK9-specific antagonists, thus, form desirable molecules for lowering plasma LDL-cholesterol levels; see, e.g., Cohen et al., 2005 Nat. Genet. 37:161-165 (wherein significantly lower plasma LDL cholesterol levels were noted in individuals heterozygous for a nonsense mutation in allele PCSK9); Rashid et al., 2005 Proc. Natl. Acad. Sci. USA 102:5374-5379 (wherein PCSK9-knockout mice evidenced increased numbers of LDLRs in hepatocytes, accelerated plasma LDL clearance, and significantly lower plasma cholesterol levels); and Cohen et al., 2006 N Engl. J. Med. 354:1264-1272 (wherein humans heterozygous for mutated, loss of function, PCSK9 exhibited a significant reduction in the long-term risk of developing atherosclerotic heart disease).

[0079] Through repeat experiments, antibody molecules tested herein herein dose-dependently inhibited the effects of both human PCSK9 on LDL uptake. In specific embodiments, the present invention, thus, encompasses isolated PCSK9-specific antagonists as described herein, as well as equivalents (characterized as having one or more (in specific embodiments, 1-5 or 1-3) amino acid substitutions that do not degrade the PCSK9-selective property of the disclosed AX132 or variant antibody molecules) or homologs thereof. Particular embodiments comprise isolated PCSK9-specific antagonists that comprise the CDR domains disclosed herein or sets of heavy and/or light chain CDR domains disclosed herein, or equivalents thereof, characterized as having one or more amino acid substitutions.

[0080] Use of the terms “domain” or “region” herein simply refers to the respective portion of the antibody molecule wherein the sequence or segment at issue will reside or, in the alternative, currently resides.

[0081] In specific embodiments, the present invention provides isolated PCSK9-specific antagonists and, in more specific embodiments, antibody molecules that comprise (i) a heavy chain variable region selected from the group consisting of: SEQ ID NOs: 360-510 and/or (ii) a light chain variable region selected from the group consisting of: SEQ ID NOs: 511-549; equivalents thereof characterized as having one or more (in particular embodiments, 1-5 or 1-3) amino acid substitutions, and homologs thereof. This group also encompasses, for SEQ ID NOs: 360, 362, and 364-510, PCSK9 antibody molecules that do not have the last 3 amino acid residues in the sequence (see, e.g., SEQ ID NOs: 361 and 363); due to varying interpretations on variable region boundaries. The disclosed antagonists should counteract or inhibit human PCSK9-dependent inhibition of cellular LDL uptake. In specific embodiments, the present invention provides homologs of the disclosed antagonists characterized as comprising a heavy chain variable and/or a light chain variable region being at least 90% (or in specific embodiments, at least 95%, 97% or 99%) identical in sequence to either or both, respectively, of (i) a heavy chain variable region selected from the group consisting of: SEQ ID NOs: 360-510 and/or (ii) a light chain variable region selected from the group consisting of: SEQ ID NOs: 511-549; said antagonists which inhibit human PCSK9-dependent inhibition of cellular LDL uptake by at least 10%.

[0082] In particular embodiments, the present invention provides isolated PCSK9-specific antagonists and, in more specific embodiments, PCSK9 antibody molecules that comprise (i) variable heavy CDR3 sequence selected from the group consisting of: SEQ ID NOs: 1-5, 7, 9, 11, 13-63 and residues 4-12 of SEQ ID NOs: 1, 3, 5, 9 and 13-63 and/or (ii) variable light CDR3 sequence selected from the group consisting of: SEQ ID NOs: 295-301, 303, 305-334 and residues 4-13 of SEQ ID NOs: 295, 297, 299, 301 and 305-334; and equivalents thereof characterized as having one or more (in particular embodiments, 1-5 or 1-3) amino acid substitutions; specific embodiments of which inhibit human PCSK9-dependent inhibition of cellular LDL uptake by at least 10%. Specific embodiments provide isolated antagonists which additionally comprise in the heavy and/or light chain variable regions CDR1 and/or CDR2 sequences as described herein; or equivalents thereof characterized as having one or more (in specific embodiments, 1-5 or 1-3) amino acid substitutions in any one or more of the CDR sequences. In specific embodiments, the present invention provides homologs of the disclosed antagonists characterized as being at least 90% (in specific embodiments, 95%, 97%, or 99%) identical to the CDR3 sequences or within each of the CDR1, CDR2 and CDR3 sequences; said antagonists which inhibit human PCSK9-dependent inhibition of cellular LDL uptake by at least 10%.

[0083] In particular embodiments, the present invention provides isolated PCSK9-specific antagonists and, in more specific embodiments, PCSK9 antibody molecules that comprise (i) variable heavy CDR2 sequence selected from the group consisting of: SEQ ID NOs: 64-68, 70, 72, 74, 76-182 and residues 4-20 of SEQ ID NOs: 64, 66, 68, 72 and 76-182 and/or (ii) variable light CDR2 sequence selected from the group consisting of: SEQ ID NOs: 335-339, 341, 343-346, and residues 4-10 of SEQ ID NOs: 335, 337, 339 and 343-346; and equivalents thereof characterized as having one or more (in particular embodiments, 1-5 or 1-3) amino acid substitutions; specific embodiments of which inhibit human PCSK9-dependent inhibition of cellular LDL uptake by at least 10%. Specific embodiments provide isolated antagonists which additionally comprise heavy and/or light chain variable regions CDR1 and/or CDR3 sequences as described herein; or equivalents thereof characterized as having one or more (in specific embodiments, 1-5 or 1-3) amino acid substitutions in any one or more of the CDR sequences. In specific embodiments, the present invention provides homologs of the disclosed antagonists characterized as being at least 90% (in specific embodiments, 95%, 97%, or 99%) identical to the CDR2 sequences or within each of the CDR1, CDR2 and CDR3 sequences; said antagonists which inhibit human PCSK9-dependent inhibition of cellular LDL uptake by at least 10%.

[0084] Select variable heavy CDR1 regions comprise sequence selected from the group consisting of: SEQ ID NOs: 183-189, 191, 193, 195 197-294, and residues 4-13 of SEQ ID NOs: 183, 185, 187, 189, 193 and 197-294; and equivalents thereof characterized as having one or more (in particular embodiments, 1-5 or 1-3) amino acid substitutions.

[0085] Select variable light CDR1 regions comprise sequence selected from the group consisting of: SEQ ID NOs: 347-349, 351, 353-359, and residues 4-14 of SEQ ID NOs: 347, 349 and 353-359; and equivalents thereof characterized as having one or more (in particular embodiments, 1-5 or 1-3) amino acid substitutions.

[0086] Specific embodiments provide isolated PCSK9-specific antagonists and, in more specific embodiments, antibody molecules which comprise one or more (in particular embodiments, one of each CDR1, 2, and 3 regions) heavy chain variable region CDR1, CDR2, and CDR3 sequences and light chain variable region CDR1, CDR2, and CDR3 sequences as disclosed herein; and equivalents thereof characterized as having one or more (in particular embodiments, 1-5 or 1-3) amino acid substitutions in any one or more of the CDR sequences; specific embodiments of which inhibit human PCSK9-dependent inhibition of cellular LDL uptake by at least 10%. In specific embodiments, the present invention provides homologs of the disclosed antagonists characterized as being at least 90% (in specific embodiments, 95%, 97%, or 99%) identical over the disclosed heavy and light chain variable region CDR1, CDR2 and CDR3 sequences, respectively; said antagonists which inhibit human PCSK9-dependent inhibition of cellular LDL uptake by at least 10%.

[0087] One particular aspect of the present invention encompasses isolated PCSK9-specific antagonists and, in more specific embodiments, antibody molecules which are variants of that disclosed above which inhibit human PCSK9-dependent inhibition of cellular LDL uptake by at least 10%.

[0088] Additional distinct embodiments encompass isolated PCSK9-specific antagonists which comprise: (a) a heavy chain variable region comprising CDR1, CDR2 and CDR3 sequence, wherein (i) the CDR1 sequence is selected from the group consisting of: SEQ ID NOs: 183-189, 191, 193, 195, 197-294, and residues 4-13 of SEQ ID NOs: 183, 185, 187, 189, 193, and 197-294; (ii) the CDR2 sequence is selected from the group consisting of: SEQ ID NOs: 64-68, 70, 72, 74, 76-182 and residues 4-20 of SEQ ID NOs: 64, 66, 68, 72 and 76-182; and (iii) the CDR3 sequence is selected from the group consisting of: SEQ ID NOs: 1-5, 7, 9, 11, 13-63, and residues 4-12 of SEQ ID NOs: 1, 3, 5, 9 and 13-63 and/or (b) a light chain variable region comprising CDR1, CDR2 and CDR3 sequence, wherein (i) the CDR1 sequence is selected from the group consisting of: SEQ ID NOs: 347-349, 351, 353-359, and residues 4-14 of SEQ ID NOs: 347, 349 and 353-359; (ii) the CDR2 sequence is selected from the group consisting of: SEQ ID NOs: 335-339, 341, 343-346 and residues 4-10 of SEQ ID NOs: 335, 337, 339, and 343-346; and (iii) the CDR3 sequence is selected from the group consisting of: SEQ ID NOs: 295-301, 303, 305-334, and residues 4-13 of SEQ ID NOs: 295, 297, 299, 301 and 305-334; and equivalents thereof characterized as having one or more (in particular embodiments, 1-5 or 1-3) amino acid substitutions; specific embodiments of which inhibit human PCSK9-dependent inhibition of cellular LDL uptake by at least 10%.

[0089] In specific embodiments herein the CDRs are in place of the corresponding regions of AX132 (or disclosed variants) or alternative antagonist, antibody molecule or scaffold structure with or without amino acid substitutions (in specific embodiments, 1-5 or 1-3); specific embodiments of which inhibit human PCSK9-dependent inhibition of cellular LDL uptake by at least 10%.

[0090] Particular embodiments are isolated PCSK9-specific antagonists which comprise the above-described VH and VL regions in a full length antibody. Specific embodiments herein further comprise a series of amino acids selected from the group consisting of: SEQ ID NO: 572 (IgG1), SEQ ID NO: 573 (IgG2), SEQ ID NO: 574 (IgG4) and SEQ ID NO: 575 (IgG2 m4).

[0091] Amino acid substitutions encompassed herein may be conservative or non-conservative amino acid substitutions. Amino acid substitutions, as one of ordinary skill in the art will appreciate, are substitutions that replace an amino acid residue with one imparting similar or better (for the intended purpose) functional and/or chemical characteristics. Antagonists bearing amino acid substitutions can be tested for retained or better activity using functional assays available in the art or described herein. PCSK9-specific antagonists possessing one or more amino acid substitutions which retain the ability to selectively bind to human PCSK9 and antagonize PCSK9 functioning at a level the same or better than AX132 (or variant) antibody molecules as described herein are referred to herein as “functional equivalents” of the disclosed antagonists and form specific embodiments of the present invention. Conservative amino acid substitutions are often ones in which the amino acid residue is replaced with an amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been defined in the art. These families include amino acids with basic side chains (e.g., lysine, arginine, histidine), acidic side chains (e.g., aspartic acid, glutamic acid), uncharged polar side chains (e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine, tryptophan), nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine), beta-branched side chains (e.g., threonine, valine, isoleucine) and aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine). Modifications as described above may or may not be designed to significantly alter the binding or functional inhibition characteristics of the PCSK9-specific antagonist, and may improve such properties. The purpose for making a substitution is not significant and can include, but is by no means limited to, replacing a residue with one better able to maintain or enhance the structure of the molecule, the charge or hydrophobicity of the molecule, or the size of the molecule. For instance, one may desire simply to substitute a less desired residue with one of the same polarity or charge. Such modifications can be introduced by standard techniques known in the art, such as site-directed mutagenesis and PCR-mediated mutagenesis. One specific means by which those of skill in the art accomplish conservative amino acid substitutions is alanine scanning mutagenesis as discussed in, for example, MacLennan et al., 1998 Acta Physiol. Scand. Suppl. 643:55-67, and Sasaki et al., 1998 Adv. Biophys. 35:1-24.

[0092] In one specific embodiment of the present invention, a CDR disclosed herein is altered so as to generate a more stable variant or a variant that is recombinantly expressed at higher levels. For example, if Asn-Gly or Asp-Gly is in a CDR, the invention encompasses variants wherein the Asp or Asn is changed to Glu or Ala or wherein the Gly is changed to Ala. A benefit of such a change is removal of the potential for isoaspartate formation. Also, if a Met is in a CDR in an exposed position, the scope of the present invention includes variants wherein the Met is changed to Lys, Leu, Ala, or Phe. A benefit of such a change is removal of the potential for methionine oxidation. If an Asn is in a CDR of the invention, the scope of the present invention includes variants wherein Asn is changed to Gln or Ala. A benefit of such a change is removal of the potential for deamidation. Furthermore, if an Asn-Pro is in a CDR of the present invention, the present invention includes variants wherein Asn is changed to Gln or Ala or wherein Pro is changed to Ala. A benefit of such a change is removal of a possible scissile Asn-Pro peptide bond. The scope of the invention includes embodiments wherein the heavy or light chain CDRs of any of the disclosed antibody molecules are independently changed in one or more places as described above.

[0093] In another aspect, the present invention provides isolated PCSK9-specific antagonists and, in more specific embodiments, antibody molecules which comprise heavy and/or light chain variable regions comprising amino acid sequences that are homologous to the corresponding amino acid sequences of the disclosed antibodies, wherein the antibody molecules inhibit PCSK9-dependent inhibition of cellular LDL uptake. Specific embodiments are antagonists which comprise heavy and/or light chain variable regions which are at least 90% identical to disclosed heavy and/or light chain variable regions (or heavy and/or light chains), respectively. Reference to “at least 90% identical” includes at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 and 100% identical sequences along the full length of the molecule disclosed herein.

[0094] PCSK9-specific antagonists with amino acid sequences homologous to the amino acid sequences of antagonists described herein are typically produced to improve one or more of the properties of the antagonist without negatively impacting its specificity for PCSK9. One method of obtaining such sequences, which is not the only method available to the skilled artisan, is to mutate sequence encoding the PCSK9-specific antagonist or specificity-determining region(s) thereof, express an antagonist comprising the mutated sequence(s), and test the encoded antagonist for retained function using available functional assays including those described herein. Mutation may be by site-directed or random mutagenesis. As one of skill in the art will appreciate, however, other methods of mutagenesis can readily bring about the same effect. For example, in certain methods, the spectrum of mutants are constrained by non-randomly targeting amino acid substitutions based on either amino acid chemical or structural characteristics, or else by protein structural considerations. In affinity maturation experiments, several such mutations may be found in a single selected molecule, whether they are randomly or non-randomly selected. There are also various structure-based approaches toward affinity maturation as demonstrated in, e.g., U.S. Pat. No. 7,117,096, PCT Pub. Nos.: WO 02/084277 and WO 03/099999; the disclosures of which are incorporated herein by reference.

[0095] As used herein, the percent homology between two amino acid or nucleic acid sequences is equivalent to the percent identity between the two sequences, and these two terms will be used interchangeably throughout. As used herein, % identity of two nucleic acid or amino acid sequences is determined using the algorithm of Karlin and Altschul (Proc. Natl. Acad. Sci. USA 90:5873-5877, 1993). Such an algorithm is incorporated into the NBLAST and XBLAST programs of Altschul et al., 1990 J. Mol. Biol. 215:403-410. BLAST nucleotide searches are performed with the NBLAST program, score=100, wordlength=12, to obtain nucleic acid sequences homologous to a nucleic acid molecule of the invention. BLAST protein searches are performed with the XBLAST program, score=50, wordlength=3, to obtain amino acid sequences homologous to an amino acid sequence disclosed herein. To obtain gapped alignments for comparison purposes, Gapped BLAST is utilized as described in Altschul et al., 1997 Nucleic Acids Res. 25:3389-3402. When utilizing BLAST and Gapped BLAST programs, the default parameters of the respective programs (e.g., XBLAST and NBLAST) are used.

[0096] Utilization of components of one or more disclosed PCSK9-specific molecules to produce other binding molecules with similar or better specificity is well within the realm of one skilled in the art. This can be accomplished, for example, using techniques of recombinant DNA technology. One specific example of this involves the introduction of DNA encoding the immunoglobulin variable region, or one or more of the CDRs, of an antibody to the variable region, constant region, or constant region plus framework regions, as appropriate, of a different immunoglobulin. Such molecules form important aspects of the present invention. Specific immunoglobulins or the corresponding sequences, into which particular disclosed sequences may be inserted or, in the alternative, form the essential part of, include but are not limited to the following antibody molecules which form particular embodiments of the present invention: a Fab (monovalent fragment with variable light (VL), variable heavy (VH), constant light (CL) and constant heavy 1 (CH1) domains), a F(ab′)₂ (bivalent fragment comprising two Fab fragments linked by a disulfide bridge or alternative at the hinge region), a Fd (VH and CH1 domains), a Fv (VL and VH domains), a scFv (a single chain Fv where VL and VH are joined by a linker, e.g., a peptide linker, see, e.g., Bird et al., 1988 Science 242:423-426, Huston et al., 1988 PNAS USA 85:5879-5883), a bispecific antibody molecule (an antibody molecule comprising a PCSK9-specific antibody or antigen binding fragment as disclosed herein linked to a second functional moiety having a different binding specificity than the antibody, including, without limitation, another peptide or protein such as an antibody, or receptor ligand), a bispecific single chain Fv dimer (see, e.g., PCT/US92/09965), an isolated CDR3, a minibody (single chain-CH₃ fusion that self assembles into a bivalent dimer of about 80 kDa), a ‘scAb’ (an antibody fragment containing VH and VL as well as either CL or CH₁), a dAb fragment (VH domain, see, e.g., Ward et al., 1989 Nature 341:544-546, and McCafferty et al., 1990 Nature 348:552-554; or VL domain; Holt et al., 2003 Trends in Biotechnology 21:484-489), a diabody (see, e.g., Holliger et al., 1993 PNAS USA 90:6444-6448 and International Application Number WO 94/13804), a triabody, a tetrabody, a minibody (a scFv joined to a CH3; see, e.g., Hu et al., 1996 Cancer Res. 56:3055-3061), IgG, IgG1, IgG2, IgG3, IgG4, IgM, IgD, IgA, IgE or any derivatives thereof, and artificial antibodies based upon protein scaffolds, including but not limited to fibronectin type III polypeptide antibodies (see, e.g., U.S. Pat. No. 6,703,199 and International Application Number WO 02/32925) or cytochrome B; see, e.g., Koide et al., 1998 J. Molec. Biol. 284:1141-1151, and Nygren et al., 1997 Current Opinion in Structural Biology 7:463-469; the disclosures of which are incorporated herein by reference. Certain antibody molecules including, but not limited to, Fv, scFv, diabody molecules or domain antibodies (Domantis) may be stabilized by incorporating disulfide bridges to line the VH and VL domains, see, e.g., Reiter et al., 1996 Nature Biotech. 14:1239-1245; the disclosure of which is incorporated herein by reference. Bispecific antibodies may be produced using conventional technologies (see, e.g., Holliger & Winter, 1993 Current Opinion Biotechnol. 4:446-449, specific methods of which include production chemically, or from hybrid hybridomas) and other technologies including, but not limited to, the BiTE™ technology (molecules possessing antigen binding regions of different specificity with a peptide linker) and knobs-into-holes engineering (see, e.g., Ridgeway et al., 1996 Protein Eng. 9:616-621; the disclosure of which is incorporated herein by reference). Bispecific diabodies may be produced in E. coli, and these molecules as other PCSK9-specific antagonists, as one of skill in the art will appreciate, may be selected using phage display in the appropriate libraries (see, e.g., International Application Number WO 94/13804; the disclosure of which is incorporated herein by reference).

[0097] Variable domains, into which CDRs of interest are inserted, may be obtained from any germ-line or rearranged human variable domain. Variable domains may also be synthetically produced. The CDR regions can be introduced into the respective variable domains using recombinant DNA technology. One means by which this can be achieved is described in Marks et al., 1992 Bio/Technology 10:779-783; the disclosure of which is incorporated herein by reference. A variable heavy domain may be paired with a variable light domain to provide an antigen binding site. In addition, independent regions (e.g., a variable heavy domain alone) may be used to bind antigen. The artisan is well aware, as well, that two domains of an Fv fragment, VL and VH, while perhaps coded by separate genes, may be joined, using recombinant methods, by a synthetic linker that enables them to be made as a single protein chain in which the VL and VH regions pair to form monovalent molecules (scFvs).

[0098] Specific embodiments provide the CDR(s) in germline framework regions. Framework regions, including but not limited to human framework regions, are known to those of skill in the art (e.g., a human or non-human framework). The framework regions may be naturally occurring or consensus framework regions. In one aspect, the framework region of an antibody of the invention is human (see, e.g., Clothia et al., 1998 J. Mol. Biol. 278:457-479 for a listing of human framework regions; said disclosure of which is incorporated herein by reference in its entirety). Specific embodiments herein provide the disclosed heavy and/or light chain variable CDR3 sequences into VH3 or VK3, respectively, in place of the relevant CDR. Specific embodiments herein provide the disclosed heavy and/or light chain variable CDR1, CDR2 and/or CDR3 sequences into VH3 or VK3, respectively, in place of the relevant CDRs.

[0099] The present invention encompasses antibody molecules that are human, humanized, deimmunized, chimeric and primatized. The invention also encompasses antibody molecules produced by the process of veneering; see, e.g., Mark et al., 1994 Handbook of Experimental Pharmacology, vol. 113: The pharmacology of monoclonal Antibodies, Springer-Verlag, pp. 105-134; the disclosure of which is incorporated herein by reference. “Human” in reference to the disclosed antibody molecules specifically refers to antibody molecules having variable and/or constant regions derived from human germline immunoglobulin sequences, wherein said sequences may, but need not, be modified/altered to have certain amino acid substitutions or residues that are not encoded by human germline immunoglobulin sequence. Such mutations can be introduced by methods including, but not limited to, random or site-specific mutagenesis in vitro, or by somatic mutation in vivo. Specific examples of mutation techniques discussed in the literature are that disclosed in Gram et al., 1992 PNAS USA 89:3576-3580; Barbas et al., 1994 PNAS USA 91:3809-3813, and Schier et al., 1996 J. Mol. Biol. 263:551-567; the disclosures of which are incorporated herein by reference. These are only specific examples and do not represent the only available techniques. There are a plethora of mutation techniques in the scientific literature which are available to, and widely appreciated by, the skilled artisan. “Humanized” in reference to the disclosed antibody molecules refers specifically to antibody molecules wherein CDR sequences derived from another mammalian species, such as a mouse, are grafted onto human framework sequences. “Primatized” in reference to the disclosed antibody molecules refers to antibody molecules wherein CDR sequences of a non-primate are inserted into primate framework sequences, see, e.g., WO 93/02108 and WO 99/55369; the disclosures of which are incorporated herein by reference.

[0100] Specific antibodies of the present invention are monoclonal antibodies and, in particular embodiments, are in one of the following antibody formats: IgD, IgA, IgE, IgM, IgG1, IgG2, IgG3, IgG4 or any derivative of any of the foregoing. The language “derivatives thereof” or “derivatives” in this respect includes, inter alia, (i) antibodies and antibody molecules with amino acid modifications in one or both variable regions (i.e., VH and/or VL), (ii) antibodies and antibody molecules with manipulations in the constant regions of the heavy and/or light chains, and/or (iii) antibodies and antibody molecules that contain additional chemical moieties which are not normally a part of the immunoglobulin molecule (e.g., pegylation).

[0101] Manipulations of the variable regions can be within one or more of the VH and/or VL CDR regions. Site-directed mutagenesis, random mutagenesis or other method for generating sequence or molecule diversity can be utilized to create mutants which can subsequently be tested for a particular functional property of interest in available in vitro or in vivo assays including those described herein.

[0102] Antibodies of the present invention also include those in which modifications have been made to the framework residues within VH and/or VL to improve one or more properties of the antibody of interest. Typically, such framework modifications are made to decrease the immunogenicity of the antibody. For example, one approach is to “backmutate” one or more framework residues to the corresponding germline sequence. More specifically, an antibody that has undergone somatic mutation may contain framework residues that differ from the germline sequence from which the antibody is derived. Such residues can be identified by comparing the antibody framework sequences to the germline sequences from which the antibody is derived. Such “backmutated” antibodies are also intended to be encompassed by the invention. Another type of framework modification involves mutating one or more residues within the framework region, or even within one or more CDR regions, to remove T cell epitopes to thereby reduce the potential immunogenicity of the antibody. This approach is also referred to as “deimmunization” and is described in further detail in U.S. Patent Publication No. 20030153043 by Carr et al; the disclosure of which is incorporated herein by reference.

[0103] In addition or alternative to modifications made within the framework or CDR regions, antibodies of the invention may be engineered to include modifications within the Fc or constant regions, where present, typically to alter one or more functional properties of the antibody, such as serum half-life, complement fixation, Fc receptor binding, and/or antigen-dependent cellular cytotoxicity.

[0104] The concept of generating “hybrids” or “combinatorial” IgG forms comprising various antibody isotypes to hone in on desired effector functionality has generally been described; see, e.g., Tao et al., 1991 J. Exp. Med. 173:1025-1028. A specific embodiment of the present invention encompasses antibody molecules that possess specific manipulations in the Fc region which have been found to result in reduced or altered binding to FcγR receptors, C1q or FcRn on the part of the antibody. The present invention, therefore, encompasses antibodies in accordance with the present description that do not provoke (or provoke to a lesser extent) antibody-dependent cellular cytotoxicity (“ADCC”), complement-mediated cytotoxicity (“CMC”), or form immune complexes, while retaining normal pharmacokinetic (“PK”) properties. Specific embodiments of the present invention provide an antibody molecule as defined in accordance with the present invention which comprises, as part of its immunoglobulin structure, SEQ ID NO: 575 and, in particular embodiments, residues 107-326 of SEQ ID NO: 575 as part of the immunoglobulin structure. The present invention encompasses antibody molecules which comprise: (i) a light chain variable region selected from the group consisting of: SEQ ID NOs: 511-549 (and in specific embodiments, selected from the group consisting of: SEQ ID NOs: 511-518, 520-524 and 526-549), and (ii) a heavy chain variable region selected from the group consisting of: SEQ ID NOs: 360-510 in sequence with (adjacent to) or followed by a series of amino acids selected from the group consisting of: SEQ ID NO: 572 (IgG1), SEQ ID NO: 573 (IgG2), SEQ ID NO: 574 (IgG4) and SEQ ID NO: 575 (IgG2 m4). In particular embodiments, the light chain and heavy chain pairings of (i) and (ii) above are (a) SEQ ID NOs: 360 and 511, and (b) SEQ ID NOs: 362 and 511.

[0105] The present invention also encompasses crystals The present invention includes crystals comprising any PCSK9-specific antagonist of the invention complexed with PCSK9 or a peptide epitope thereof.

[0106] Several crystallization methods are known in the art (Giegé, et al., (1994) Acta Crystallogr. D50: 339-350; McPherson, (1990) Eur. J. Biochem. 189: 1-23). Such methods include microbatch, hanging drop, seeding and dialysis. Preferably, hanging-drop vapor diffusion (McPherson, (1976) J. Biol. Chem. 251: 6300-6303) or microbatch methods (Chayen (1997) Structure 5: 1269-1274) are used. In each of these methods, it is important to promote continued crystal growth after nucleation by maintaining a supersaturated solution. In the microbatch method, polypeptide is mixed with precipitants to achieve supersaturation, the vessel is sealed and set aside until crystals appear. In the dialysis method, polypeptide is retained in a sealed dialysis membrane which is placed into a solution containing precipitant. Equilibration across the membrane increases the precipitant concentration thereby causing the polypeptide to reach supersaturation levels.

[0107] Once a crystal of the present invention is grown, X-ray diffraction data can be collected. One method for determining structure with X-ray diffraction data includes use of synchrotron radiation, under standard cryogenic condition; however, alternative methods may also be used. For example, crystals can be characterized by using X-rays produced by a conventional source, such as a sealed tube or a rotating anode. Methods of characterization include, but are not limited to, precession photography, oscillation photography and diffractometer data collection.

[0108] The crystallizable compositions provided by this invention are amenable to X-ray crystallography for providing the three-dimensional structure of the PCSK9/PCSK9-specific antagonist complex. The present invention includes crystals which effectively diffract X-rays for the determination of the atomic coordinates of the PCSK9/PCSK9-specific antagonist complex to a resolution of greater than about 5.0 Ångströms (e.g., about 4.5 Å, about 4.0 Å, about 3 Å, about 2.5 Å, about 2 Å, about 1.95 Å, about 1 Å), preferably greater than about 4.0 Ångströms (e.g., about 3 Å, about 2.5 Å, about 2 Å, about 1.95 Å, about 1 Å), more preferably greater than about 2.8 Ångströms (e.g., about 2.5 Å, about 2 Å, about 1.95 Å, about 1 Å) and most preferably greater than about 2.0 Ångströms (e.g., about 1.95 Å, about 1.5 Å, about 1.0 Å).

[0109] The scope of the present invention also encompasses a crystalline complex between a PCSK9-specific antagonist of the present invention (e.g., a Fab comprising the heavy chain amino acid sequence set forth in SEQ ID NO: 552 and the light chain amino acid sequence set forth in SEQ ID NO: 554) and PCSK9 in space group The complex of PCSK9 and the AX132 Fab fragment crystallized in space group P6₅ and comprising the unit cell dimensions a=155.946 Å, b=155.946 Å, c=160.037 Å and α=90°, β=90°, γ=120°, wherein the Fab is derived from the antibody AX132 as described herein.

[0110] The present invention includes PCSK9/PCSK9-specific antagonist complex crystals whose three-dimensional structure is described by the structure coordinates set forth in Table 14. The scope of the present invention also includes crystals that possess structural coordinates which are similar to those set forth in Table 14. Structural similarity between crystals is discussed in detail below.

[0111] The term “structure coordinates” refers to Cartesian coordinates derived from mathematical equations related to the patterns obtained on diffraction of a beam of X-rays by the atoms (scattering centers) of a molecule. The diffraction data are used to calculate electron density maps and to establish the positions of the individual atoms of the molecule.

[0112] Those of skill in the art will understand that a set of structure coordinates for an enzyme or an enzyme-complex or a portion thereof, is a relative set of points that define a shape in three dimensions. Thus, it is possible that an entirely different set of coordinates could define a similar or identical shape. Moreover, slight variations in the individual coordinates will have little effect on overall shape.

[0113] The present invention includes crystals exhibiting structural coordinates which are similar to those set forth in Table 14 but for crystallographic permutations of the structure coordinates, fractionalization of the structure coordinates, additions, subtractions, rotations or translations to sets of the structure coordinates or any combinations of the above.

[0114] Alternatively, modifications in the crystal structure due to mutations, additions, substitutions, and/or deletions of amino acids, or other changes in any of the components that make up the crystal may also account for variations in structure coordinates. If such variations are within an acceptable standard error as compared to the coordinates of Table 14, the resulting three-dimensional shape is considered to be the same and, accordingly, the modified crystal is considered to be within the scope of the present invention.

[0115] Various computational analyses may be used to determine whether a crystal is sufficiently similar to the crystals whose structural coordinates are set forth in Table 14 as to be considered the same. Such analyses may be carried out in current software applications, such as the Molecular Similarity application of QUANTA (Molecular Simulations Inc., San Diego, Calif.) version 4.1, and as described in the accompanying User's Guide.

[0116] The Molecular Similarity application permits comparisons between different structures, different conformations of the same structure, and different parts of the same structure. In general, the procedure used in Molecular Similarity to compare structures is divided into four steps: 1) input the structures to be compared; 2) define the atom equivalences in these structures; 3) perform a fitting operation; and 4) analyze the results. Each structure is identified by a name. One structure is identified as the target (i.e., the fixed structure); all remaining structures are working structures (i.e., moving structures). Since atom equivalency within QUANTA is defined by user input, for the purpose of this invention we will define equivalent atoms as alpha carbon atoms (Cα) or all protein backbone atoms (N, Cα, C and O) for all conserved residues between the two structures being compared. When a rigid fitting method is used, the working structure is translated and rotated to obtain an optimum fit with the target structure. The fitting operation uses a least squares fitting algorithm that computes the optimum translation and rotation to be applied to the moving structure, such that the root mean square difference of the fit over the specified pairs of equivalent atom is an absolute minimum. This number, given in Ångströms, is reported by QUANTA.

[0117] The term “root mean square deviation” (RMSD) is a commonly known term in the art which, in general, means the square root of the arithmetic mean of the squares of the deviations from the mean distance of corresponding atoms. It is a way to express the deviation or variation from a trend or object.

[0118] The term “least squares” relates to a method based on the principle that the best estimate of a value is that in which the sum of the squares of the deviations of observed values is a minimum.

[0119] For the purpose of this invention, any crystalline molecule characterized by a set of structure coordinates that has a RMSD of conserved residue backbone atoms (N, Cα, C, O) or of alpha carbon atoms (Cα) only of less than about 1.5 Å when superimposed—using backbone atoms or alpha carbon atoms—on the relevant structure coordinates of Table 14 are considered identical and are within the scope of the present invention. In an embodiment, the root mean square deviation is about 1.5 Å or about 1.0 Å or about 0.75 Å or about 0.5 Å or about 0.25 Å or about 0.10 Å.

[0120] The present invention also encompasses any non-crystalline PCSK9-specific antagonist that, when converted to Fab format, binds to human PCSK9 in a manner characterized by a three dimensional structure which is characterized by a set of structure coordinates that has a RMSD of conserved residue backbone atoms (N, Cα, C, O) or of alpha carbon atoms (Cα) only of less than about 1.5 Å when superimposed—using backbone atoms or alpha carbon atoms—on the relevant structure coordinates of Table 14 are considered identical and are within the scope of the present invention. In an embodiment, the root mean square deviation is about 1.5 Å or about 1.0 Å or about 0.75 Å or about 0.5 Å or about 0.25 Å or about 0.10 Å.

[0121] In particular embodiments, the present invention encompasses PCSK9-specific antagonists that bind to PCSK9 within 10 Å or less from at least one (in specific embodiments, at least 2, 4, 10, 15, 20, 25, 30 or 35; or all) of the following residues on PCSK9: S153, I154, P155, W156, N157, L158, D192, H193, R194, E195, I196, E197, G198, R199, 5221, H229, G232, S235, G236, 8237, D238, A239, G240, K243, G244, D367, I368, I369, G370, A371, S372, S373, D374, C375, 5376, T377, C378, F379, V380, S381. In specific embodiments, the present invention encompasses PCSK9-specific antagonists that bind to PCSK9 within 5 Å or less from at least one (in specific embodiments, at least 2, 4 or 10; or all) of the following residues on PCSK9: S153, P155, R194, E195, R237, D238, A239, I369, D374, C375, S376, T377, C378, F379.

[0122] Specific PCSK9-specific antagonists may carry a detectable label, or may be conjugated to a toxin (e.g., a cytotoxin), a radioactive isotope, a radionuclide, a liposome, a targeting moiety, a biosensor, a cationic tail, or an enzyme (e.g., via a peptidyl bond or linker). Such PCSK9-specific antagonist compositions form an additional aspect of the present invention.

[0123] In another aspect, the present invention provides isolated nucleic acid encoding disclosed PCSK9-specific antagonists. “Isolated” as mentioned prior refers to the property of the thing referred to that makes them different from that found in nature. The difference can be, for example, that they are of a different purity than that found in nature, or that they are of a different structure or form part of a different structure than that found in nature. An example of nucleic acid not found in nature is, for example, nucleic acid substantially free of other cellular material. The nucleic acid may be present in whole cells, in a cell lysate, or in a partially purified or substantially pure form. In specific instances, a nucleic acid may be isolated when purified away from other cellular components or other contaminants, e.g., other cellular nucleic acids or proteins, for example, using standard techniques, including without limitation, alkaline/SDS treatment, CsCl banding, column chromatography, agarose gel electrophoresis and other suitable methods known in the art. The nucleic acid may include DNA (inclusive of cDNA) and/or RNA. Nucleic acids of the present invention can be obtained using standard molecular biology techniques. For antibodies expressed by hybridomas (e.g., hybridomas prepared from transgenic mice carrying human immunoglobulin genes), cDNAs encoding the light and heavy chains of the antibody made by the hybridoma can be obtained by standard PCR amplification or cDNA cloning techniques. For antibodies obtained from an immunoglobulin gene library (e.g., using phage display techniques), nucleic acid encoding the antibody can be recovered from the library.

[0124] The present invention encompasses isolated nucleic acid encoding disclosed variable heavy and/or light chains and select components thereof, particularly the disclosed variable or respective CDR regions. In specific embodiments hereof, the CDR(s) are provided within antibody framework regions and, in particular embodiments, human framework regions. Specific embodiments provide isolated nucleic acid encoding the CDR(s) into germline framework regions including, but not limited to, human germline framework regions. Specific embodiments herein provide isolated nucleic acid encoding heavy chain CDR3 sequence selected from the group consisting of: SEQ ID NOs: 1-5, 7, 9, 11, 13-63, and residues 4-12 of SEQ ID NOs: 1, 3, 5, 9, and 13-63 (in specific embodiments, said nucleic acid of which comprises a sequence selected from the group consisting of: SEQ ID NOs: 6, 8, 10 and 12). Specific embodiments herein provide isolated nucleic acid encoding heavy chain CDR2 sequence selected from the group consisting of: SEQ ID NOs: 64-68, 70, 72, 74, 76-182, and residues 4-20 of SEQ ID NOs: 64, 66, 68, 72 and 76-182 (in specific embodiments, said nucleic acid of which comprises a sequence selected from the group consisting of: SEQ ID NOs: 69, 71, 73 and 75). Specific embodiments herein provide isolated nucleic acid encoding heavy chain CDR1 sequence selected from the group consisting of: SEQ ID NOs: 183-189, 191, 193, 195, 197-294 and residues 4-13 of SEQ ID NOs: 183, 185, 187, 189, 193 and 197-294 (in specific embodiments, said nucleic acid of which comprises a sequence selected from the group consisting of: SEQ ID NOs: 190, 192, 194 and 196). Specific embodiments herein provide nucleic acid encoding the disclosed heavy chain variable CDR1, CDR2 and/or CDR3 sequences into VH3 in place of the relevant CDRs. Specific embodiments herein provide isolated nucleic acid encoding light chain CDR3 sequence selected from the group consisting of: SEQ ID NOs: 295-301, 303, 305-334, and residues 4-13 of SEQ ID NOs: 295, 297, 299, 301 and 305-334 (in specific embodiments, said nucleic acid of which comprises a sequence selected from the group consisting of: SEQ ID NOs: 302 and 304). Specific embodiments herein provide isolated nucleic acid encoding light chain CDR2 sequence selected from the group consisting of: SEQ ID NOs: 335-339, 341, 343-346, and residues 4-10 of SEQ ID NOs: 335, 337, 339 and 343-346 (in specific embodiments, said nucleic acid of which comprises a sequence selected from the group consisting of: SEQ ID NOs: 340 and 342). Specific embodiments herein provide isolated nucleic acid encoding light chain CDR1 sequence selected from the group consisting of: SEQ ID NOs: 347-349, 351, 353-359 and residues 4-14 of SEQ ID NOs: 347, 349 and 353-359 (in specific embodiments, said nucleic acid of which comprises a sequence selected from the group consisting of: SEQ ID NOs: 350 and 352). Specific embodiments herein provide nucleic acid encoding the disclosed light chain variable CDR1, CDR2 and/or CDR3 sequences into VK3 (or VK1) in place of the relevant CDRs. Specific embodiments provide both the heavy and light chain CDRs (1, 2 and 3) or some combination of one or more thereof.

[0125] The isolated nucleic acid encoding the variable regions can be provided within any desired antibody molecule format including, but not limited to, the following: F(ab′)₂, a Fab, a Fv, a scFv, bispecific antibody molecules (antibody molecules comprising a PCSK9-specific antibody or antigen binding fragment as disclosed herein linked to a second functional moiety having a different binding specificity than the antibody, including, without limitation, another peptide or protein such as an antibody, or receptor ligand), a bispecific single chain Fv dimer, a minibody, a dAb fragment, diabody, triabody or tetrabody, a minibody, IgG, IgG1, IgG2, IgG3, IgG4, IgM, IgD, IgA, IgE or any derivatives thereof.

[0126] Specific embodiments provide isolated nucleic acid which encodes PCSK9-specific antagonists and, in more specific embodiments, antibody molecules comprising (i) a heavy chain variable domain selected from the group consisting of: SEQ ID NOs: 360-510; specific embodiments of which comprise nucleic acid sequence SEQ ID NO: 550 or SEQ ID NO: 561; and/or (ii) a light chain variable domain selected from the group consisting of: SEQ ID NOs: 511-549; specific embodiments of which comprise nucleic acid sequence SEQ ID NO: 551. The present invention further provides in specific embodiments, homologs of the antagonists disclosed above, characterized as being at least 90% (in specific embodiments, 95%, 97% or 99%) identical through the heavy and/or light chain variable regions.

[0127] Additional embodiments provide isolated nucleic acid encoding PCSK9-specific antagonists and, in more specific embodiments, antibody molecules which comprise (i) a light chain selected from the group consisting of: SEQ ID NOs: 558, 566, and 554 (specific embodiments of which comprise nucleic acid selected from the group consisting of: SEQ ID NOs: 559, 567, 568 and 555); and/or (ii) a heavy chain or Fd chain selected from the group consisting of: SEQ ID NOs: 552, 562, 556, 564 and amino acids 1-221 of SEQ ID NOs: 562 and 552 (specific embodiments of which comprise nucleic acid selected from the group consisting of: SEQ ID NOs: 553, 563, 557, 565 and nucleotides 1-663 of SEQ ID NOs: 553 and 563. The present invention further provides in specific embodiments, homologs of the antagonists disclosed above, characterized as being at least 90% identical over the heavy and/or light chains.

[0128] Specific embodiments of the present invention encompass nucleic acid encoding antibody molecules that possess manipulations in the Fc region which result in reduced or altered binding to FcγR receptors, C1q or FcRn on the part of the antibody. One specific embodiment of the present invention is isolated nucleic acid which encodes for antibody molecules comprising as part of their immunoglobulin structure SEQ ID NO: 575 and, in particular embodiments, residues 107-326 of SEQ ID NO: 575. In specific embodiments, synthetic PCSK9-specific antagonists can be produced by expression from nucleic acid generated from oligonucleotides synthesized and assembled within suitable expression vectors; see, e.g., Knappick et al., 2000 J. Mol. Biol. 296:57-86, and Krebs et al., 2001 J. Immunol. Methods 254:67-84.

[0129] The present invention encompasses nucleic acid encoding antibody molecules which comprise: (i) the disclosed nucleic acid encoding the light chain variable region, and (ii) the disclosed nucleic acid encoding the heavy chain variable region, followed in sequence by (adjacent to) a set of nucleotides encoding for a set of amino acids selected from the group consisting of: SEQ ID NO: 572 (IgG1), SEQ ID NO: 573 (IgG2), SEQ ID NO: 574 (IgG4) and SEQ ID NO: 575 (IgG2 m4). Plasmid sequence comprising heavy and light chain AX132 anti-PCSK9 antibody molecule sequence can be found as SEQ ID NO: 560. Plasmid sequence comprising heavy and light chain AX213 anti-PCSK9 antibody molecule sequence can be found as SEQ ID NO: 569. Nucleic acid encoding such antibody molecules form important embodiments hereof. Additional plasmid sequences can be obtained by substituting the altered region for that present in the disclosed plasmid sequences.

[0130] Also included within the present invention are isolated nucleic acids comprising nucleotide sequences which are at least about 90% identical and more preferably at least about 95% identical to the full length of the nucleotide sequences described herein, and which nucleotide sequences encode PCSK9-specific antagonists which inhibit PCSK9-dependent inhibition of cellular LDL uptake by at least 10%.

[0131] Reference to “at least about 90% identical” throughout the application includes at least about 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% identical.

[0132] The invention further provides isolated nucleic acid at least a portion of which hybridizes to the complement of nucleic acid encoding any one of the variable heavy, variable light, heavy chain, and light chain regions disclosed herein under stringent hybridization conditions, said nucleic acid of which confers upon antibody molecules the ability to specifically bind PCSK9 and antagonize PCSK9 function, and PCSK9-specific antagonists expressed employing said nucleic acid. Methods for hybridizing nucleic acids are well-known in the art; see, e.g., Ausubel, Current Protocols in Molecular Biology, John Wiley & Sons, N.Y., 6.3.1-6.3.6, 1989. Stringent hybridization conditions involve hybridizing at 68° C. in 5×SSC/5×Denhardt's solution (or equivalent)/1.0% SDS, and washing in 0.2×SSC/0.1% SDS at room temperature. Moderately stringent conditions include washing in 3×SSC at 42° C. The parameters of salt concentration and temperature can be varied to achieve the optimal level of identity between the probe and the target nucleic acid. The skilled artisan can manipulate various hybridization and/or washing conditions to specifically target nucleic acid in the hybridizing portion that is at least 80, 85, 90, 95, 98, or 99% identical to the variable heavy, variable light, heavy chain and/or light chain regions disclosed herein. Basic parameters affecting the choice of hybridization conditions and guidance for devising suitable conditions are set forth by Sambrook et al., Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., chapters 9 and 11, 1989 and Ausubel et al. (eds), Current Protocols in Molecular Biology, John Wiley & Sons, Inc., sections 2.10 and 6.3-6.4, 1995 (the disclosures of which are incorporated herein by reference), and can be readily determined by those having ordinary skill in the art. PCSK9 antagonists having one or more regions comprising nucleic acid which hybridizes to the disclosed heavy chain, light chain, variable heavy or variable light regions under stringent hybridization conditions should be effective in antagonizing one or more functions of PCSK9. Said antagonists and encoding nucleic acid, thus, form important embodiments of the present invention.

[0133] In another aspect, the present invention provides vectors comprising the nucleic acid disclosed herein. Vectors in accordance with the present invention include, but are not limited to, plasmids and other expression constructs (e.g., phage or phagemid, as appropriate) suitable for the expression of the desired antibody molecule at the appropriate level for the intended purpose; see, e.g., Sambrook & Russell, Molecular Cloning: A Laboratory Manual: 3^rd Edition, Cold Spring Harbor Laboratory Press; the disclosure of which is incorporated herein by reference. For most cloning purposes, DNA vectors may be used. Typical vectors include plasmids, modified viruses, bacteriophage, cosmids, yeast artificial chromosomes, bacterial artificial chromosomes, and other forms of episomal or integrated DNA. It is well within the purview of the skilled artisan to determine an appropriate vector for a particular gene transfer, generation of a recombinant PCSK9-specific antagonist, or other use. In specific embodiments, in addition to a recombinant gene, the vector may also contain an origin of replication for autonomous replication in a host cell, appropriate regulatory sequences, such as a promoter, a termination sequence, a polyadenylation sequence, an enhancer sequence, a selectable marker, a limited number of useful restriction enzyme sites, and/or other sequences as appropriate and the potential for high copy number. Examples of expression vectors for the production of protein-specific antagonists are well known in the art; see, e.g., Persic et al., 1997 Gene 187:9-18; Boel et al., 2000 J. Immunol. Methods 239:153-166, and Liang et al., 2001 J. Immunol. Methods 247:119-130; the disclosures of which are incorporated herein by reference. If desired, nucleic acid encoding the antagonist may be integrated into the host chromosome using techniques well known in the art; see, e.g., Ausubel, Current Protocols in Molecular Biology, John Wiley & Sons, 1999, and Marks et al., International Application Number WO 95/17516. Nucleic acid may also be expressed on plasmids maintained episomally or incorporated into an artificial chromosome; see, e.g., Csonka et al., 2000 J. Cell Science 113:3207-3216; Vanderbyl et al., 2002 Molecular Therapy 5:10. Specifically with regards to antibody molecules, the antibody light chain gene and the antibody heavy chain gene can be inserted into separate vectors or, more typically, both genes may be inserted into the same expression vector. Nucleic acid encoding any PCSK9-specific antagonist or component thereof can be inserted into an expression vector using standard methods (e.g., ligation of complementary restriction sites on the nucleic acid fragment and vector, or blunt end ligation if no restriction sites are present). Another specific example of how this may be carried out is through use of recombinational methods, e.g. the Clontech “InFusion” system, or Invitrogen “TOPO” system (both in vitro), or intracellularly (e.g. the Cre-Lox system). Specifically with regards to antibody molecules, the light and heavy chain variable regions can be used to create full-length antibody genes of any antibody isotype by inserting them into expression vectors already encoding heavy chain constant and light chain constant regions of the desired isotype such that the VH segment is operatively linked to the CH segment(s) within the vector and the VL segment is operatively linked to the CL segment within the vector. Additionally or alternatively, the recombinant expression vector comprising nucleic acid encoding a PCSK9-specific antagonist can encode a signal peptide that facilitates secretion of the antagonist from a host cell. The nucleic acid can be cloned into the vector such that the nucleic acid encoding a signal peptide is linked in-frame adjacent to the PCSK9-specific antagonist-encoding nucleic acid. The signal peptide may be an immunoglobulin or a non-immunoglobulin signal peptide. Any technique available to the skilled artisan may be employed to introduce the nucleic acid into the host cell; see, e.g., Morrison, 1985 Science, 229:1202. Methods of subcloning nucleic acid molecules of interest into expression vectors, transforming or transfecting host cells containing the vectors, and methods of making substantially pure protein comprising the steps of introducing the respective expression vector into a host cell, and cultivating the host cell under appropriate conditions are well known. The PCSK9-specific antagonist so produced may be harvested from the host cells in conventional ways. Techniques suitable for the introduction of nucleic acid into cells of interest will depend on the type of cell being used. General techniques include, but are not limited to, calcium phosphate transfection, DEAE-Dextran, electroporation, liposome-mediated transfection and transduction using viruses appropriate to the cell line of interest (e.g., retrovirus, vaccinia, baculovirus, or bacteriophage).

[0134] In another aspect, the present invention provides isolated cell(s) comprising nucleic acid encoding disclosed PCSK9-specific antagonists. A variety of different cell lines are contemplated herein and can be used for the recombinant production of PCSK9-specific antagonists, including but not limited to those from prokaryotic organisms (e.g., E. coli, Bacillus, and Streptomyces) and from eukaryotic (e.g., yeast, Baculovirus, and mammalian); see, e.g., Breitling et al., Recombinant antibodies, John Wiley & Sons, Inc. and Spektrum Akademischer Verlag, 1999; the disclosure of which is incorporated herein by reference. Plant cells, including transgenic plants, and animal cells, including transgenic animals (other than humans), comprising the nucleic acid or antagonists disclosed herein are also contemplated as part of the present invention. Suitable mammalian cells or cell lines including, but not limited to, those derived from Chinese Hamster Ovary (CHO cells, including but not limited to DHFR-CHO cells (described in Urlaub and Chasin, 1980 Proc. Natl. Acad. Sci. USA 77:4216-4220) used, for example, with a DHFR selectable marker (e.g., as described in Kaufman and Sharp, 1982 Mol. Biol. 159:601-621), NS0 myeloma cells (where a GS expression system as described in WO 87/04462, WO 89/01036, and EP 338,841 may be used), COS cells, SP2 cells, HeLa cells, baby hamster kidney cells, YB2/0 rat myeloma cells, human embryonic kidney cells, human embryonic retina cells, and others comprising the nucleic acid or antagonists disclosed herein form additional embodiments of the present invention; the preceding cited disclosures of which are incorporated herein by reference. Specific embodiments of the present invention comprising nucleic acid encoding disclosed PCSK9-specific antagonists include, but are not limited to, E. coli; see, e.g., Plückthun, 1991 Bio/Technology 9:545-551, or yeast, such as Pichia, and recombinant derivatives thereof (see, e.g., Li et al., 2006 Nat. Biotechnol. 24:210-215); the preceding disclosures of which are incorporated herein by reference. Specific embodiments of the present invention relate to eukaryotic cells comprising nucleic acid encoding the disclosed PCSK9-specific antagonists, see, Chadd & Chamow, 2001 Current Opinion in Biotechnology 12:188-194, Andersen & Krummen, 2002 Current Opinion in Biotechnology 13:117, Larrick & Thomas, 2001 Current Opinion in Biotechnology 12:411-418; the disclosures of which are incorporated herein by reference. Specific embodiments of the present invention relate to mammalian cells comprising nucleic acid encoding the disclosed PCSK9-specific antagonists which are able to produce PCSK9-specific antagonists with proper post translational modifications. Post translational modifications include, but are by no means limited to, disulfide bond formation and glycosylation. Another type of post translational modification is signal peptide cleavage. Preferred embodiments herein have the appropriate glycosylation; see, e.g., Yoo et al., 2002 J. Immunol. Methods 261:1-20; the disclosure of which is incorporated herein by reference. Naturally occurring antibodies contain at least one N-linked carbohydrate attached to a heavy chain. Id. Different types of mammalian host cells can be used to provide for efficient post-translational modifications. Examples of such host cells include Chinese Hamster Ovary (CHO), HeLa, C6, PC12, and myeloma cells; see, Yoo et al., 2002 J. Immunol. Methods 261:1-20, and Persic et al., 1997 Gene 187:9-18; the disclosures of which are incorporated herein by reference.

[0135] In another aspect, the present invention provides isolated cell(s) comprising a polypeptide of the present invention.

[0136] In another aspect, the present invention provides a method of making a PCSK9-specific antagonist of the present invention, which comprises incubating a cell comprising nucleic acid encoding the PCSK9-specific antagonist, or a heavy and/or light chain or a fragment thereof (e.g., VH and/or VL, or one or more of the disclosed heavy and/or light chain variable region CDRs) of a desired PCSK9-specific antagonist (dictated by the desired antagonist) with specificity for human PCSK9 under conditions that allow the expression of the PCSK9-specific antagonist, or the expression and assembly of said heavy and/or light chains or fragment into a PCSK9-specific antagonist, and isolating said PCSK9-specific antagonist from the cell. One example by which to generate particular desired heavy and/or light chain sequence or fragment is to first amplify (and modify) the germline heavy and/or light chain variable sequences or fragment using PCR. Germline sequence for human heavy and/or light variable regions are readily available to the skilled artisan, see, e.g., the “Vbase” human germline sequence database, and Kabat, E. A. et al., 1991 Sequences of Proteins of Immunological Interest, Fifth Edition, U.S. Department of Health and Human Services, NIH Publication No. 91-3242; Tomlinson, I. M. et al., 1992 “The Repertoire of Human Germline VH Sequences Reveals about Fifty Groups of VH Segments with Different Hypervariable Loops” J. Mol. Biol. 227:776-798; and Cox, J. P. L. et al., 1994 “A Directory of Human Germ-line VK Segments Reveals a Strong Bias in their Usage” Eur. J. Immunol. 24:827-836; the disclosures of which are incorporated herein by reference. Mutagenesis of germline sequences may be carried out using standard methods, e.g., PCR-mediated mutagenesis where the mutations are incorporated into PCR primers, or site-directed mutagenesis. If full-length antibodies are desired, sequence is available for the human heavy chain constant region genes; see, e.g., Kabat. E. A. et al., 1991 Sequences of Proteins of Immunological Interest, Fifth Edition, U.S. Department of Health and Human Services, NIH Publication No. 91-3242. Fragments containing these regions may be obtained, for example, by standard PCR amplification. Alternatively, the skilled artisan can avail him/herself of vectors already encoding heavy and/or light chain constant regions.

[0137] Fab expression and purification may be achieved in a number of ways. One common way is to perform papain digestion of whole IgG1s to release two equivalents of Fab and one equivalent of Fc region. However, for phage displayed libraries, which also needs to be expressed in E. coli, Fab is typically displayed via covalent linkage to a protein and also to a hexahistidine tag (His-tag). In a typical fashion, induction by IPTG is followed by intracellular expression of the Fab. Subsequently, whole cells are lysed and the desired Fab is purified using a nickel affinity column. Depending on the specific case, this can yield high background in analytical SE-HPLC, presumably from misfolded, partially folded, disulfide scrambled or proteolyzed Fabs containing the His-tag since His-tag does not discriminate between these and the correctly folded Fab. Thus, in specific embodiments, expression of Fabs is carried out as follows: the periplasmic transport signal from phage, such as pIII and pVIII coat protein leader sequences, are utilized in the expression vector to localize the Fab polypeptides into the oxidizing environment of the periplasmic space. There, chaperone-like enzymes can facilitate correct Fab folding and thus allow formation of correct disulfide bonds. The initial overnight growth phase may be set at 30° C. Subsequently, the bacterial culture can be induced into Fab production, using lower concentration of IPTG (1 mM, 0.5 mM, or 0.1 mM) to induce the lac operon and start translation of the Fab genes. The temperature can be lowered to 22-23° C. Both the low IPTG and low temperature slow the E. coli protein synthesis in order to avoid overloading the periplasmic folding machinery. Cells may then be harvested by low speed centrifugation (˜4000 g) and undergo periplasmic extraction. Periplasmic extraction is a gentle osmotic release process that primarily aims to make the outer bacterial cell wall leaky via mild osmotic shock, allowing Fabs to escape the periplasm into the surrounding media. After extraction, the cells can then be centrifuged at high speed (>15000 g) and the supernatant, containing released soluble Fab is saved for affinity chromatography.

[0138] In the specific embodiment above, affinity chromatography can be as follows: Affinity purification using protein G resin selectively binds folded constant region of the Fab at neutral pH (typically, using PBS or HBS at ˜7.0-7.4). The bound Fab can be released under acidic pH (typically with glycine-HCl, pH 2.7-4.0) and eluted into a tube containing 1M Tris base at pH 9 to minimize exposure of the Fab to acidic pH. Alternatively, because the extract from the periplasmic extraction is relatively clean compared to a whole cell lysate, a nickel affinity column may be used to purify a Fab with a His-tag. In both cases, the eluted Fabs are buffer exchanged (e.g., by dialysis or centrifugal filtration using 30 kD MW cutoff filters) into the storage buffer, typically PBS or any preferred formulation buffer. The sample can be analyzed using analytical size exclusion (SE) HPLC generally show single peak consisting of >95% desired product. Additional polishing may be performed, if desired, using orthogonal methods, such as cation (CEX) or anion exchange (AEX) or hydrophobic interaction (HIC) chromatography.

[0139] Accordingly, in specific embodiments, the expression vector used for expression of the disclosed PCSK9-specific antagonists comprises sequence for phage coat protein pIII or pVIII leaders sequence or other export leader sequence to export the expressed antagonist into the bacterial periplasm. In specific embodiments, this is for the expression of Fab. In specific embodiments, the invention comprises a method for producing a PCSK9-specific antagonist which comprises: (a) inserting a vector as described herein into a cell (in particular embodiments, the vector encodes a Fab); wherein the vector comprises a phage coat protein PIII or pVIII leader sequence; (b) culturing the cell under conditions appropriate for production of the PCSK9-specific antagonist; and (c) isolating the PCSK9-specific antagonist produced by periplasmic extraction using gentle lysis conditions to disrupt primarily the outer cell wall to release periplasmic contents and minimize contamination by intracellular contents. In specific embodiments, this may further comprise purifying the PCSK9-specific antagonist by: (i) affinity of the constant domain to protein G to purify correctly folded PCSK9-specific antagonists (such as Fabs); (ii) affinity of the His-tag to a nickel affinity column; or (iii) other suitable purification technique. This may then be followed by analyzing the buffer-exchanged Fab or isolated PCSK9-specific antagonist using SDS-PAGE, analytical SE-HPLC, or mass spectrometry to QC the final product.

[0140] Available techniques exist to recombinantly produce other antibody molecules which retain the specificity of an original antibody. A specific example of this is where DNA encoding the immunoglobulin variable region or the CDRs is introduced into the constant regions, or constant regions and framework regions, or simply the framework regions, of another antibody molecule; see, e.g., EP-184,187, GB 2188638, and EP-239400; the disclosures of which are incorporated herein by reference. Cloning and expression of antibody molecules, including chimeric antibodies, are described in the literature; see, e.g., EP 0120694 and EP 0125023; the disclosures of which are incorporated herein by reference.

[0141] Antibody molecules in accordance with the present invention may, in one instance, be raised and then screened for characteristics identified herein using known techniques. Basic techniques for the preparation of monoclonal antibodies are described in the literature, see, e.g., Kohler and Milstein (1975, Nature 256:495-497); the disclosure of which is incorporated herein by reference. Fully human monoclonal antibodies can be produced by available methods. These methods include, but are by no means limited to, the use of genetically engineered mouse strains which possess an immune system whereby the mouse antibody genes have been inactivated and in turn replaced with a repertoire of functional human antibody genes, while leaving other components of the mouse immune system unchanged. Such genetically engineered mice allow for the natural in vivo immune response and affinity maturation process which results in high affinity, full human monoclonal antibodies. This technology is well known in the art and is fully detailed in various publications, including but not limited to U.S. Pat. Nos. 5,545,806; 5,569,825; 5,625,126; 5,633,425; 5,789,650; 5,877,397; 5,661,016; 5,814,318; 5,874,299; 5,770,249 (assigned to GenPharm International and available through Medarex, under the umbrella of the “UltraMab Human Antibody Development System”); as well as U.S. Pat. Nos. 5,939,598; 6,075,181; 6,114,598; 6,150,584 and related family members (assigned to Abgenix, disclosing their XenoMouse® technology); the disclosures of which are incorporated herein by reference. See also reviews from Kellerman and Green, 2002 Curr. Opinion in Biotechnology 13:593-597, and Kontermann & Stefan, 2001 Antibody Engineering, Springer Laboratory Manuals; the disclosures of which are incorporated herein by reference.

[0142] Alternatively, a library having potential PCSK9-specific antagonists or any library of antibody molecules may be brought into contact with PCSK9, and ones able to demonstrate specific binding selected. Functional studies can then be carried out to ensure proper functionality, e.g., inhibition of PCSK9-dependent inhibition of cellular LDL uptake. There are various techniques available to the skilled artisan for the selection of protein-specific molecules from libraries using enrichment technologies including, but not limited to, phage display (e.g., see technology from Abmaxis disclosed in U.S. Pat. Nos. 7,175,983 and 7,117,096, WO 03/099999, and Wang et al., 2010 J. Mol. Biol. 395:1088-1101 and Cambridge Antibody Technology (“CAT”) disclosed in U.S. Pat. Nos. 5,565,332; 5,733,743; 5,871,907; 5,872,215; 5,885,793; 5,962,255; 6,140,471; 6,225,447; 6,291,650; 6,492,160; 6,521,404; 6,544,731; 6,555,313; 6,582,915; 6,593,081, as well as other U.S. family members and/or applications which rely on priority filing GB 9206318, filed May 24, 1992; see also Vaughn et al., 1996, Nature Biotechnology 14:309-314), ribosome display (see, e.g., Hanes and Pluckthün, 1997 Proc. Natl. Acad. Sci. 94:4937-4942), bacterial display (see, e.g., Georgiou, et al., 1997 Nature Biotechnology 15:29-34) and/or yeast display (see, e.g., Kieke, et al., 1997 Protein Engineering 10:1303-1310, and Wang et al., 2010 J. Immunol. Methods 354:11-19); the preceding disclosures of which are incorporated herein by reference. A library, for example, can be displayed on the surface of bacteriophage particles, with nucleic acid encoding the PCSK9-specific antagonist or fragment thereof expressed and displayed on its surface. Nucleic acid may then be isolated from bacteriophage particles exhibiting the desired level of activity and the nucleic acid used in the development of desired antagonist. Phage display has been thoroughly described in the literature; see, e.g., Wang et al., 2010 J. Mol. Biol. 395:1088-1101, Kontermann & Stefan, supra, and International Application Number WO 92/01047; the disclosures of which are incorporated herein by reference. Specifically with regard to antibody molecules, individual heavy or light chain clones in accordance with the present invention may also be used to screen for complementary heavy or light chains, respectively, capable of interaction therewith to form a molecule of the combined heavy and light chains; see, e.g., International Application Number WO 92/01047. Any method of panning which is available to the skilled artisan may be used to identify PCSK9-specific antagonists. Another specific method for accomplishing this is to pan against the target antigen in solution, e.g. biotinylated, soluble PCSK9, and then capture the PCSK9-specific antagonist-phage complexes on streptavidin-coated magnetic beads, which are then washed to remove nonspecifically-bound phage. The captured phage can then be recovered from the beads in the same way they would be recovered from the surface of a plate, as described herein.

[0143] PCSK9-specific antagonists may be purified by techniques available to one of skill in the art. Titers of the relevant antagonist preparation, ascites, hybridoma culture fluids, or relevant sample may be determined by various serological or immunological assays which include, but are not limited to, precipitation, passive agglutination, enzyme-linked immunosorbent antibody (“ELISA”) techniques and radioimmunoassay (“RIA”) techniques.

[0144] The present invention relates in part to methods employing PCSK9-specific antagonists described herein for antagonizing PCSK9 function; said methods of which are further described below. Use of the term “antagonizing” throughout the present application refers to the act of opposing, inhibiting, counteracting, neutralizing or curtailing one or more functions of PCSK9. Inhibition or antagonism of one or more of PCSK9-associated functional properties can be readily determined according to methodologies known to the art (see, e.g., Barak & Webb, 1981 J. Cell Biol. 90:595-604; Stephan & Yurachek, 1993 J. Lipid Res. 34:325330; and McNamara et al., 2006 Clinica Chimica Acta 369:158-167) as well as those described herein. Inhibition or antagonism will effectuate a decrease in PCSK9 activity relative to that seen in the absence of the antagonist or, for example, that seen when a control antagonist of irrelevant specificity is present. Preferably, a PCSK9-specific antagonist in accordance with the present invention antagonizes PCSK9 functioning to the point that there is a decrease of at least 10%, of the measured parameter including but not limited to the activities disclosed herein, and more preferably, a decrease of at least 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90% and 95% of the measured parameter. Such inhibition/antagonism of PCSK9 functioning is particularly effective in those instances where PCSK9 functioning is contributing at least in part to a particular phenotype, disease, disorder or condition which is negatively impacting the subject.

[0145] In one aspect, the present invention provides a method for antagonizing the activity of PCSK9, which comprises contacting a cell, population of cells or tissue sample capable of being affected by PCSK9 (i.e., which expresses and/or comprises LDL receptors) with a PCSK9-specific antagonist disclosed herein under conditions that allow said antagonist to bind to PCSK9 when present and inhibit PCSK9's inhibition of cellular LDL uptake. Specific embodiments of the present invention include such methods wherein the cell is a human cell.

[0146] In another aspect, the present invention provides a method for antagonizing the activity of PCSK9 in a subject, which comprises administering to the subject a therapeutically effective amount of a PCSK9-specific antagonist of the present invention. In specific embodiments, the methods for antagonizing PCSK9 function are for the treatment of a PCSK9-associated disease, disorder or condition or, alternatively, a disease, disorder or condition that could benefit from the effects of a PCSK9 antagonist. The medicament would be useful in a subject(s) exhibiting a condition associated with PCSK9 activity, or a condition where the functioning of PCSK9 is contraindicated for a particular subject. In select embodiments, the condition may be hypercholesterolemia, coronary heart disease, metabolic syndrome, acute coronary syndrome or related conditions.

[0147] The present invention, thus, contemplates the use of PCSK9-specific antagonists described herein in various methods of treatment where antagonizing PCSK9 function is desirable. The method of treatment can be prophylactic or therapeutic in nature. In specific embodiments, the present invention relates to a method of treatment for a condition associated with/attributed to PCSK9 activity, or a condition where the functioning of PCSK9 is contraindicated for a particular subject, which comprises administering to the subject a therapeutically effective amount of a PCSK9-specific antagonist of the present invention. In select embodiments, the condition may be hypercholesterolemia, coronary heart disease, metabolic syndrome, acute coronary syndrome or related conditions.

[0148] Methods of treatment in accordance with the present invention comprise administering to an individual a therapeutically (or prophylactically) effective amount of a PCSK9-specific antagonist of the present invention. Use of the terms “therapeutically effective” or “prophylactically effective” in reference to an amount refers to the amount necessary at the intended dosage to achieve the desired therapeutic/prophylactic effect for the period of time desired. The desired effect may be, for example, amelioration of at least one symptom associated with the treated condition. These amounts will vary, as the skilled artisan will appreciate, according to various factors, including but not limited to the disease state, age, sex and weight of the individual, and the ability of the PCSK9-specific antagonist to elicit the desired effect in the individual. The response may be documented by in vitro assay, in vivo non-human animal studies, and/or further supported from clinical trials.

[0149] The present invention provides methods for treating or preventing disorders of cholesterol or lipid homeostasis and disorders and complications associated therewith, e.g., hypercholesterolemia, hyperlipidemia, hypertriglyceridaemia, sitosterolemia, atherosclerosis, arteriosclerosis, coronary heart disease, metabolic syndrome, acute coronary syndrome, vascular inflammation, xanthoma and related conditions.

[0150] The present invention also provides methods for improving blood cholesterol markers associated with increased risk of heart disease. These markers include, but are not limited to, high total cholesterol, high LDL, high total cholesterol to HDL ratio and high LDL to HDL ratio.

[0151] In general, a total cholesterol of less than 200 mg/dL is considered desirable, 200-239 mg/dL is considered borderline high and 240 mg/dL and above is considered high. For example, the present invention comprises methods for reducing total cholesterol, e.g., to less than or equal to about 200 mg/dL by administering a therapeutically effective amount of a PCSK9-specific antagonist of the present invention.

[0152] In general, a blood LDL level of less than 100 mg/dL is considered optimal; 100-129 mg/dL is considered near optimal/above optimal, 130-159 mg/dL is considered borderline high, 160-189 mg/dL is considered high and 190 mg/dL and above is considered very high. For example, the present invention comprises methods for reducing LDL, e.g., to less than about 100 mg/dL by administering a therapeutically effective amount of a PCSK9-specific antagonist of the present invention.

[0153] In general, HDL levels considered normal are at least 35-40 mg/dL. For example, the present invention comprises methods for increasing HDL, e.g., to greater than or equal to about 35-40 mg/dL by administering a therapeutically effective amount of anti-PCSK9 antibody or antigen binding fragment thereof of the present invention.

[0154] Another indicator of heart disease risk is the ratio of total cholesterol to HDL. In general, a very low risk of heart disease correlates with a ratio of <3.4 (men) or <3.3 (women); a low risk is associated with a ratio of 4.0 (men) or 3.8 (women), an average risk is associated with a ratio of 5.0 (men) or 4.5 (women), a moderate risk is associated with a ratio of 9.5 (men) or 7.0 (women) and a high risk is associated with a ratio of >23 (men) or >11 (women). For example, the present invention comprises methods for reducing the ratio of total cholesterol to HDL, e.g., to less than about 4.5 or 5.0 by administering a therapeutically effective amount of a PCSK9-specific antagonist of the present invention.

[0155] A further indicator of heart disease risk is the ratio of LDL to HDL. In general, a very low risk is associated with a ratio of 1 (men) or 1.5 (women), an average risk is associated with a ratio of 3.6 (men) or 3.2 (women), a moderate risk is associated with a ratio of 6.3 (men) or 5.0 (women) and a high risk is associated with a ratio of 8 (men) or 6.1 (women). For example, the present invention comprises methods for the ratio of LDL to HDL, e.g., to less than or equal to about 3.2 or 3.6 by administering a therapeutically effective amount of a PCSK9-specific antagonist of the present invention.

[0156] The PCSK9-specific antagonist may be administered as a pharmaceutical composition. The present invention, thus, provides a pharmaceutically acceptable composition comprising a PCSK9-specific antagonist of the invention and a pharmaceutically acceptable carrier including but not limited to an excipient, diluent, stabilizer, buffer, or alternative designed to facilitate administration of the antagonist in the desired format and amount to the treated individual.

[0157] The pharmaceutical composition may be formulated by any number of strategies known in the art, see, e.g., McGoff and Scher, 2000 Solution Formulation of Proteins/Peptides: In—McNally, E. J., ed. Protein Formulation and Delivery. New York, N.Y.: Marcel Dekker; pp. 139-158; Akers & Defilippis, 2000, Peptides and Proteins as Parenteral Solutions. In—Pharmaceutical Formulation Development of Peptides and Proteins. Philadelphia, Pa.: Taylor and Francis; pp. 145-177; Akers et al., 2002, Pharm. Biotechnol. 14:47-127. A pharmaceutically acceptable composition suitable for patient administration will contain an effective amount of the PCSK9-specific antagonist in a formulation which both retains biological activity while also promoting maximal stability during storage within an acceptable temperature range.

[0158] The antagonist-based pharmaceutically acceptable composition may, in particular embodiments, be in liquid or solid form, or in the form of gas particles or aerosolized particles. Any technique for production of liquid or solid formulations may be utilized. Such techniques are well within the realm of the abilities of the skilled artisan. Solid formulations may be produced by any available method including, but not limited to, lyophilization, spray drying, or drying by supercritical fluid technology. Solid formulations for oral administration may be in any form rendering the antagonist accessible to the patient in the prescribed amount and within the prescribed period of time. The oral formulation can take the form of a number of solid formulations including, but not limited to, a tablet, capsule, or powder. Solid formulations may alternatively be lyophilized and brought into solution prior to administration for either single or multiple dosing according to methods well known to the skilled artisan. Antagonist compositions should generally be formulated within a biologically relevant pH range and may be buffered to maintain a proper pH range during storage. Both liquid and solid formulations generally require storage at lower temperatures (e.g., 2-8° C.) in order to retain stability for longer periods. Formulated antagonist compositions, especially liquid formulations, may contain a bacteriostat to prevent or minimize proteolysis during storage, including but not limited to effective concentrations (e.g., ≦1% w/v) of benzyl alcohol, phenol, m-cresol, chlorobutanol, methylparaben, and/or propylparaben. A bacteriostat may be contraindicated for some patients. Therefore, a lyophilized formulation may be reconstituted in a solution either containing or not containing such a component. Additional components may be added to either a buffered liquid or solid antagonist formulation, including but not limited to sugars as a cryoprotectant (including but not limited to polyhydroxy hydrocarbons such as sorbitol, mannitol, glycerol, and dulcitol and/or disaccharides such as sucrose, lactose, maltose, or trehalose) and, in some instances, a relevant salt (including but not limited to NaCl, KCl, or LiCl). Such antagonist formulations, especially liquid formulations slated for long term storage, will rely on a useful range of total osmolarity to both promote long term stability at temperatures of, for example, 2-8° C. or higher, while also making the formulation useful for parenteral injection. As appropriate, preservatives, stabilizers, buffers, antioxidants and/or other additives may be included. The formulations may contain a divalent cation (including but not limited to MgCl2, CaCl2, and MnCl2); and/or a non-ionic surfactant (including but not limited to Polysorbate-80 (Tween 80™), Polysorbate-60 (Tween 60™), Polysorbate-40 (Tween 40™), and Polysorbate-20 (Tween 20™), polyoxyethylene alkyl ethers, including but not limited to Brij 58™, Brij35™, as well as others such as Triton X-100™, Triton X-114™, NP40™, Span 85 and the Pluronic series of non-ionic surfactants (e.g., Pluronic 121)). Any combination of such components form specific embodiments of the present invention.

[0159] Pharmaceutical compositions in liquid format may include a liquid carrier, e.g., water, petroleum, animal oil, vegetable oil, mineral oil, or synthetic oil. The liquid format may also include physiological saline solution, dextrose or other saccharide solution or glycols, such as ethylene glycol, propylene glycol or polyethylene glycol.

[0160] Preferably, the pharmaceutical composition may be in the form of a parenterally acceptable aqueous solution that is pyrogen-free with suitable pH, tonicity, and stability. Pharmaceutical compositions may be formulated for administration after dilution in isotonic vehicles, for example, Sodium Chloride Injection, Ringer's Injection, or Lactated Ringer's Injection.

[0161] One aspect of the present invention is a pharmaceutical composition which comprises: (i) about 50 to about 200 mg/mL of the PCSK9-specific antagonists described herein; (ii) a polyhydroxy hydrocarbon (including but not limited to sorbitol, mannitol, glycerol and dulcitol) and/or a disaccharide (including but not limited to sucrose, lactose, maltose and trehalose); the total of said polyhydroxy hydrocarbon and/or disaccharide being about 1% to about 6% weight per volume (“w/v”) of the formulation; (iii) about 5 mM to about 200 mM of histidine, imidazole, phosphate or acetic acid which serves as a buffering agent to prevent pH drift over the shelf life of the pharmaceutical composition and as a tonicity modifier; (iv) about 5 mM to about 200 mM of arginine, proline, phenylalanine, alanine, glycine, lysine, glutamic acid, aspartic acid or methionine to counteract aggregation; (v) about 0.01M to about 0.1M of hydrochloric acid (“HCl”) in an amount sufficient to achieve a pH in the range of about 5.5 to about 7.5; and (vi) a liquid carrier including but not limited to sterile water, petroleum, animal oil, vegetable oil, mineral oil, synthetic oil, physiological saline solution, dextrose or other saccharide solution or glycols, such as ethylene glycol, propylene glycol or polyethylene glycol; wherein said pharmaceutical composition has a pH in the range of about 5.5 to about 7.5; and wherein said pharmaceutical composition optionally comprises about 0.01% to about 1% w/v of the formulation of a non-ionic surfactant (including but not limited to Polysorbate-80 (Tween 80™), Polysorbate-60 (Tween 60™), Polysorbate-40 (Tween 40™), and Polysorbate-20 (Tween 20™), polyoxyethylene alkyl ethers, including but not limited to Brij 58™, Brij35™, as well as others such as Triton X-100™, Triton X-114™, NP40™, Span 85 and the Pluronic series of non-ionic surfactants (e.g., Pluronic 121)).

[0162] HCl may be added as free acid, Histidine-HCl or Arginine-HCl. Where supplied as Histidine-HCl or Arginine-HCl, the total amounts of Histidine or Arginine in the HCl form should be that specified above. Accordingly, some or all of the HCl depending on the amounts of Histidine and/or Arginine may be supplied as Histidine-HCl and/or Arginine-HCl; as appropriate. Use of the term “about” with respect to amounts disclosed in the specification means within 10% of the specified numbers provided. A range provided as, for example” in “about 50 to about 200” expressly includes as distinct embodiments each number within said range. As such in the above example, embodiments including but not limited to those having 50, 100, 125, 150 and 200 form specific embodiments herein. Pharmaceutical compositions as disclosed herein have general applicability despite the mode of administration. In specific embodiments, the disclosed pharmaceutical compositions are useful for subcutaneous administration as a liquid or upon reconstitution of a lyophilized form. Proteins that can be employed in the disclosed formulations include any polymeric protein or polypeptide characterized as comprising covalently linked amino acid residues delivered for purposes of effecting a therapeutic benefit. Proteins of use in the present compositions include but are not limited to any antibody molecules as defined herein or any non-antibody or non-immunoglobulin proteins, peptides, pegylated proteins and fusion proteins.

[0163] Specific aspects of the present invention relate to the above disclosed pharmaceutical compositions which comprise: (i) about 50 to about 200 mg/mL of the PCSK9-specific antagonists described herein; (ii) about 1% to about 6% (in particular embodiments from about 2% to about 6%) w/v mannitol, trehalose or sucrose; (iii) about 10 mM to about 100 mM of histidine; (iv) about 25 mM to about 100 mM of arginine or proline; (v) about 0.02 M to about 0.05M of hydrochloric acid (“HCl”) in an amount sufficient to achieve a pH in the range of about 5.8 to about 7; and (vi) a liquid carrier including but not limited to sterile water, petroleum, animal oil, vegetable oil, mineral oil, synthetic oil, physiological saline solution, dextrose or other saccharide solution or glycols, such as ethylene glycol, propylene glycol or polyethylene glycol; wherein said pharmaceutical composition has a pH in the range of about 5.8 to about 7; and wherein said pharmaceutical composition optionally comprising about 0.01% to about 1% w/v of the formulation of a non-ionic surfactant (including but not limited to Polysorbate-80 (Tween 80™), Polysorbate-60 (Tween 60™), Polysorbate-40 (Tween 40™), and Polysorbate-20 (Tween 20™), polyoxyethylene alkyl ethers, including but not limited to Brij 58™, Brij35™, as well as others such as Triton X-100™, Triton X-114™, NP40™, Span 85 and the Pluronic series of non-ionic surfactants (e.g., Pluronic 121)).

[0164] Specific embodiments provide pharmaceutical compositions which comprise: (i) 50 to 200 mg/mL of the PCSK9-specific antagonists described herein; (ii) about 1% to about 6% (in particular embodiments from about 2% to about 6%) w/v mannitol, trehalose or sucrose; (iii) about 10 mM to about 150 mM of histidine; (iv) about 10 mM to about 150 mM of arginine or proline; (v) about 0.03 M to about 0.05 M of hydrochloric acid (“HCl”) in an amount sufficient to achieve a pH in the range of about 5.8 to about 6.5; and (vi) a liquid carrier including but not limited to sterile water, petroleum, animal oil, vegetable oil, mineral oil, synthetic oil, physiological saline solution, dextrose or other saccharide solution or glycols, such as ethylene glycol, propylene glycol or polyethylene glycol; wherein said pharmaceutical composition has a pH in the range of about 5.8 to about 6.5; and wherein said pharmaceutical composition optionally comprising about 0.01% to about 1% w/v of Polysorbate-80 (Tween 80™) or Polysorbate-20 (Tween 20™).

[0165] Specific embodiments herein provide pharmaceutical compositions which comprise: (i) 50 to 200 mg/mL of the PCSK9-specific antagonists described herein; (ii) about 1% to about 6% (in particular embodiments from about 2% to about 6%) w/v sucrose; (iii) about 25 mM to about 100 mM of histidine; (iv) about 25 mM to about 100 mM of arginine; (v) about 0.040 M to about 0.045 M of hydrochloric acid (“HCl”) in an amount sufficient to achieve a pH of about 6; and (vi) sterile water; wherein said pharmaceutical composition has a pH of about 6; and wherein said pharmaceutical composition optionally comprising about 0.01% to about 1% w/v of Polysorbate-80 (Tween 80™) or Polysorbate-20 (Tween 20™). In specific embodiments thereof, the levels of histidine and arginine are within 25 mM of each other and, in other embodiments are the same.

[0166] Specific embodiments herein provide pharmaceutical compositions which comprise (i) 50 to 200 mg/mL of the PCSK9-specific antagonists described herein; (ii) sucrose, histidine and arginine in one of the following amounts: (a) about 1% w/v sucrose, about 10 mM histidine and about 25 mM arginine; (b) about 2% w/v sucrose, about 25 mM histidine and about 25 mM arginine; (c) about 3% w/v sucrose, about 50 mM histidine and about 50 mM arginine; or (d) about 6% w/v sucrose, about 100 mM histidine and about 100 mM arginine; (iii) about 0.04 mol or, alternatively, about 1.46 g of HCl; and (iv) sterile water; wherein said pharmaceutical composition has a pH of about 6; and wherein said pharmaceutical composition optionally comprising about 0.01% to about 1% w/v of Polysorbate-80 (Tween 80™) or Polysorbate-20 (Tween 20™). Specific embodiments herein are wherein the amounts of sucrose, histidine and arginine in (ii) above are that described in (c) or (d). Specific embodiments employing pharmaceutical formulations as described above wherein the amounts of sucrose, histidine and arginine are that specified in (ii) (c) were found to provide an osmolality similar to the physiological value of 300 mOsm and provided stability in both the liquid and lyophilized form.

[0167] Specific embodiments herein provide pharmaceutical compositions as described which comprise 50 to 200 mg/ml of any one of the various PCSK9-specific antagonists described herein. For purposes of exemplification of one distinct embodiment thereof, and not to be construed as a limitation, is the following: a pharmaceutical formulation as described above which comprises: a PCSK9-specific antagonist which comprises: (a) a light chain comprising SEQ ID NO: 558; and (b) a heavy chain comprising SEQ ID NO: 556; wherein said PCSK9-specific antagonist is an antibody molecule that antagonizes PCSK9's inhibition of cellular LDL uptake. An additional embodiment is a pharmaceutical formulation as described above which comprises: a PCSK9-specific antagonist which comprises: (a) a light chain comprising SEQ ID NO: 566; and (b) a heavy chain comprising SEQ ID NO: 564; wherein said PCSK9-specific antagonist is an antibody molecule that antagonizes PCSK9's inhibition of cellular LDL uptake.

[0168] Particular embodiments herein are pharmaceutical compositions according to the above description which are lyophilized and reconstituted. In specific embodiments, said protein concentration in said lyophilized and reconstituted solution is up to 2-fold higher than in the pre-lyophilized composition. In specific embodiments, the protein or PCSK9-specific antagonist concentration in the lyophilized and/or reconstituted pharmaceutical composition is in the range of about 50 mg/mL to about 300 mg/mL. Diluents useful for reconstituting the lyophilized pharmaceutical compositions include but are not limited to sterile water, bacteriostatic water for injection (“BWFI”), phosphate-buffered saline, a sterile saline solution, physiological saline solution, Ringer's solution or dextrose solution and may in specific embodiments contain 0.01-1% (w/v) of Polysorbate-80 (Tween 80™) or Polysorbate-20 (Tween 20™). In specific embodiments, lyophilized powder can be reconstituted with 1/60.2× original volume (or 0.167 mL) up to 1× (1 mL).

[0169] Exemplary embodiments of the present invention are pharmaceutical compositions as described herein which are stable. Other embodiments of the present invention are pharmaceutical compositions as described herein which are stable to lyophilization and reconstitution. Various methods are available to the skilled artisan to prepare lyophilized compositions; see, e.g., Martin & Mo, 2007 “Stability Considerations for Lyophilized Biologics” Amer. Pharm. Rev. “Stable” as used herein refers to the property of the protein or PCSK9-specific antagonist to retain its physical or chemical stability, conformational integrity, or its ability to exhibit less denaturation, protein clipping, aggregation, fragmentation, acidic variant formation or loss of biological activity compared with a control sample at a temperature in the range of 4-37° C. for at least about 30 days. Other embodiments remain stable for up to 3 months, 6 months, 12 months, 2 years or longer periods at the above temperatures. In specific embodiments the formulation exhibits no significant changes at 2-8° C. for at least 6 months, and preferably 12 months, 2 years or longer, in order of preference. Specific embodiments experience less than 10% or, in particular embodiments, less than 5% of denaturation, protein clipping, aggregation, fragmentation, acidic variant formation or loss of biological activity compared with a control sample at a temperature in the range of 25-45° C. (or alternatively 2-8° C.) for at least about 30 days, 3 months, 6 months, 12 months, 2 years or longer. Stability of the formulations can be tested via several means known to the skilled artisan including, but not limited to Size Exclusion Chromatography (SEC-HPLC) to measure aggregation and fragmentation, Dynamic Light Scattering (DLS) to measure particle size of concentrated samples, capillary SDS-PAGE to measure fragmentation and capillary iso-electric focusing (cIEF) or cation exchange chromatography (“CEX”) to measure acidic variants formation. Techniques suitable for the analysis of protein stability are well understood by those of skill in the art: see review in Peptide and Protein Drug Delivery, 247-301, Vincent Lee Ed., Marcel Dekker, Inc., New York, N.Y., Pubs. (1991) and Jones, 1993 Adv. Drug Delivery Rev. 10:29-90.

[0170] Pharmaceutical compositions as described herein should be sterile. There are various techniques available to the skilled artisan to accomplish this including, but not limited to, filtration through sterile filtration membranes. In specific embodiments, employing lyophilized and reconstituted compositions, this may be done prior to or following lyophilization and reconstitution.

[0171] Dosing of antagonist therapeutics is well within the realm of the skilled artisan, see, e.g., Lederman et al., 1991 Int. J. Cancer 47:659-664; Bagshawe et al., 1991 Antibody, Immunoconjugates and Radiopharmaceuticals 4:915-922, and will vary based on a number of factors including but not limited to the particular PCSK9-specific antagonist utilized, the patient being treated, the condition of the patient, the area being treated, the route of administration, and the treatment desired. A physician or veterinarian of ordinary skill can readily determine and prescribe the effective therapeutic amount of the antagonist. Dosage ranges may be from about 0.01 to 100 mg/kg, and more usually 0.05 to 25 mg/kg, of the host body weight. For example, dosages can be 0.3 mg/kg body weight, 1 mg/kg body weight, 3 mg/kg body weight, 5 mg/kg body weight or 10 mg/kg body weight or within the range of 1-10 mg/kg. For purposes of illustration, and not limitation, in specific embodiments, a dose of 5 mg to 2.0 g may be utilized to deliver the antagonist systemically. In specific embodiments, the concentration of the dose provided will be in the range of about 8 mg/mL to about 200 mg/mL. In other embodiments, a dose contemplated for use in the present invention is from about 50 mg/mL to about 150 mg/mL. In specific embodiments, the dose will be from about 0.1 mL to about 1.5 mL and in specific embodiments is 1 mL. Optimal precision in achieving concentrations of antagonist within a range that yields efficacy without toxicity requires a regimen based on the kinetics of the drug's availability to the target site(s). This involves a consideration of the distribution, equilibrium, and elimination of the PCSK9-specific antagonist. Antagonists described herein may be used alone at appropriate dosages. Alternatively, co-administration or sequential administration of other agents may be desirable. It will be possible to present a therapeutic dosing regime for the PCSK9-specific antagonists of the present invention in conjunction with alternative treatment regimes. For example, PCSK9-specific antagonists may be used in combination or in conjunction with other drugs (therapeutic and/or prophylactic). In specific embodiments, the PCSK9-specific antagonists are used in combination or in conjunction with cholesterol-lowering drugs, for example, cholesterol absorption inhibitors (e.g., Zetia®) and cholesterol synthesis inhibitors (e.g., Zocor® and Vytorin®). The present invention contemplates such combinations and they form an important embodiment hereof. Accordingly, the present invention relates to methods of treatment as described above where the PCSK9-specific antagonist is administered/delivered simultaneously with, following or prior to another drug or drugs (therapeutic and/or prophylactic), including but not limited to cholesterol-lowering drugs, including cholesterol absorption inhibitors.

[0172] Individuals (subjects) capable of treatment as described herein include primates, human and non-human, and include any non-human mammal or vertebrate of commercial or domestic veterinary importance.

[0173] The PCSK9-specific antagonist may be administered to an individual by any route of administration appreciated in the art, including but not limited to oral administration, administration by injection (specific embodiments of which include intravenous, subcutaneous, intraperitoneal or intramuscular injection), or administration by inhalation, intranasal, or topical administration, either alone or in combination with other agents designed to assist in the treatment of the individual. The PCSK9-specific antagonist may also be administered by injection devices, injector pens, needleless devices; and subcutaneous patch delivery systems. The route of administration should be determined based on a number of considerations appreciated by the skilled artisan including, but not limited to, the desired physiochemical characteristics of the treatment. Treatment may be provided on a daily, weekly, biweekly, or monthly basis, or any other regimen that delivers the appropriate amount of PCSK9-specific antagonist to the individual at the prescribed times such that the desired treatment is effected and maintained. The formulations may be administered in a single dose or in more than one dose at separate times.

[0174] Also contemplated are methods of using the disclosed antagonists in the manufacture of a medicament for treatment of a PCSK9-associated disease, disorder or condition or, alternatively, a disease, disorder or condition that could benefit from the effects of a PCSK9 antagonist. The medicament would be useful in a subject(s) exhibiting a condition associated with PCSK9 activity, or a condition where the functioning of PCSK9 is contraindicated for a particular subject. In select embodiments, the condition may be hypercholesterolemia, coronary heart disease, metabolic syndrome, acute coronary syndrome or related conditions.

[0175] PCSK9-specific antagonists disclosed herein may also be used as a method of diagnosis of PCSK9. In select embodiments, the present invention encompasses methods of identifying or quantifying the level of PCSK9 present in a sample (including but not limited to a biological sample, e.g., serum or blood) which comprises contacting the sample with a PCSK9-specific antagonist described herein and detecting or quantifying, respectively, binding to PCSK9. The PCSK9-specific antagonist may be used in various assay formats known to the skilled artisan and may form part of a kit (the general features of a kit of which are further described below).

[0176] The present invention further provides for the administration of disclosed anti-PCSK9 antagonists for purposes of gene therapy. Through such methods, cells of a subject are transformed with nucleic acid encoding a PCSK9-specific antagonist of the invention. Subjects comprising the nucleic acids then produce the PCSK9-specific antagonists endogenously. Previously, Alvarez, et al, Clinical Cancer Research 6:3081-3087, 2000, introduced single-chain anti-ErbB2 antibodies to subjects using a gene therapy approach. The methods disclosed by Alvarez, et al, supra, may be easily adapted for the introduction of nucleic acids encoding an anti-PCSK9 antibody of the invention to a subject.

[0177] Nucleic acids encoding any PCSK9-specific antagonist may be introduced to a subject.

[0178] The nucleic acids may be introduced to the cells of a subject by any means known in the art. In preferred embodiments, the nucleic acids are introduced as part of a viral vector. Examples of preferred viruses from which the vectors may be derived include lentiviruses, herpes viruses, adenoviruses, adeno-associated viruses, vaccinia virus, baculovirus, alphavirus, influenza virus, and other recombinant viruses with desirable cellular tropism.

[0179] Various companies produce viral vectors commercially, including, but by no means limited to, Avigen, Inc. (Alameda, Calif.; AAV vectors), Cell Genesys (Foster City, Calif.; retroviral, adenoviral, AAV vectors, and lentiviral vectors), Clontech (retroviral and baculoviral vectors), Genovo, Inc. (Sharon Hill, Pa.; adenoviral and AAV vectors), Genvec (adenoviral vectors), IntroGene (Leiden, Netherlands; adenoviral vectors), Molecular Medicine (retroviral, adenoviral, AAV, and herpes viral vectors), Norgen (adenoviral vectors), Oxford BioMedica (Oxford, United Kingdom; lentiviral vectors), and Transgene (Strasbourg, France; adenoviral, vaccinia, retroviral, and lentiviral vectors).

[0180] Methods for constructing and using viral vectors are known in the art (see, e.g., Miller, et al, BioTechniques 7:980-990, 1992). Preferably, the viral vectors are replication defective, that is, they are unable to replicate autonomously, and thus are not infectious, in the target cell. Preferably, the replication defective virus is a minimal virus, i.e., it retains only the sequences of its genome which are necessary for encapsidating the genome to produce viral particles. Defective viruses, which entirely or almost entirely lack viral genes, are preferred. Use of defective viral vectors allows for administration to cells in a specific, localized area, without concern that the vector can infect other cells. Thus, a specific tissue can be specifically targeted.

[0181] Examples of vectors comprising attenuated or defective DNA virus sequences include, but are not limited to, a defective herpes virus vector (Kanno et al, Cancer Gen. Ther. 6:147-154, 1999; Kaplitt et al, J. Neurosci. Meth. 71:125-132, 1997 and Kaplitt et al, J. Neuro One. 19:137-147, 1994).

[0182] Adenoviruses are eukaryotic DNA viruses that can be modified to efficiently deliver a nucleic acid of the invention to a variety of cell types. Attenuated adenovirus vectors, such as the vector described by Strafford-Perricaudet et al, J. Clin. Invest. 90:626-630, 1992 are desirable in some instances. Various replication defective adenovirus and minimum adenovirus vectors have been described (PCT Publication Nos. WO94/26914, WO94/28938, WO94/28152, WO94/12649, WO95/02697 and WO96/22378). The replication defective recombinant adenoviruses according to the invention can be prepared by any technique known to a person skilled in the art (Levrero et al, Gene 101:195, 1991; EP 185573; Graham, EMBO J. 3:2917, 1984; Graham et al, J. Gen. Virol. 36:59, 1977).

[0183] The adeno-associated viruses (AAV) are DNA viruses of relatively small size which can integrate, in a stable and site-specific manner, into the genome of the cells which they infect. They are able to infect a wide spectrum of cells without inducing any effects on cellular growth, morphology or differentiation, and they do not appear to be involved in human pathologies. The use of vectors derived from the AAVs for transferring genes in vitro and in vivo has been described (see Daly, et al, Gene Ther. 8:1343-1346, 2001, Larson et al, Adv. Exp. Med. Bio. 489:45-57, 2001; PCT Publication Nos. WO 91/18088 and WO 93/09239; U.S. Pat. Nos. 4,797,368 and 5,139,941 and EP 488528B1).

[0184] In another embodiment, the gene can be introduced in a retroviral vector, e.g., as described in U.S. Pat. Nos. 5,399,346, 4,650,764, 4,980,289, and 5,124,263; Mann et al, Cell 33:153, 1983; Markowitz et al, J. Virol., 62:1120, 1988; EP 453242 and EP178220. The retroviruses are integrating viruses which infect dividing cells.

[0185] Lentiviral vectors can be used as agents for the direct delivery and sustained expression of nucleic acids encoding a PCSK9-specific antagonist of the invention in several tissue types, including brain, retina, muscle, liver and blood. The vectors can efficiently transduce dividing and nondividing cells in these tissues, and maintain long-term expression of the PCSK9-specific antagonist. For a review, see Zufferey et al, J. Virol. 72:9873-80, 1998 and Kafri et al, Curr. Opin. Mol. Ther. 3:316-326, 2001. Lentiviral packaging cell lines are available and known generally in the art. They facilitate the production of high-titer lentivirus vectors for gene therapy. An example is a tetracycline-inducible VSV-G pseudotyped lentivirus packaging cell line which can generate virus particles at titers greater than 10⁶ IU/ml for at least 3 to 4 days; see Kafri et al, J. Virol. 73:576-584, 1999. The vector produced by the inducible cell line can be concentrated as needed for efficiently transducing nondividing cells in vitro and in vivo.

[0186] Sindbis virus is a member of the alphavirus genus and has been studied extensively since its discovery in various parts of the world beginning in 1953. Gene transduction based on alphavirus, particularly Sindbis virus, has been well-studied in vitro (see Straus et al, Microbiol. Rev., 58:491-562, 1994; Bredenbeek et al, J. Virol., 67:6439-6446, 1993; Ijima et al, Int. J. Cancer 80:110-118, 1999 and Sawai et al, Biochim. Biophyr. Res. Comm. 248:315-323, 1998. Many properties of alphavirus vectors make them a desirable alternative to other virus-derived vector systems being developed, including rapid engineering of expression constructs, production of high-titered stocks of infectious particles, infection of nondividing cells, and high levels of expression (Strauss et al, 1994 supra). Use of Sindbis virus for gene therapy has been described. (Wahlfors et al, Gene. Ther. 7:472-480, 2000 and Lundstrom, J. Recep. Sig. Transduct. Res. 19(1-4):673-686, 1999.

[0187] In another embodiment, a vector can be introduced to cells by lipofection or with other transfection facilitating agents (peptides, polymers, etc.). Synthetic cationic lipids can be used to prepare liposomes for in vivo and in vitro transfection of a gene encoding a marker (Feigner et al, Proc. Natl. Acad. Sci. USA 84:7413-7417, 1987 and Wang et al, Proc. Natl. Acad. Sci. USA 84:7851-7855, 1987). Useful lipid compounds and compositions for transfer of nucleic acids are described in PCT Publication Nos. WO 95/18863 and WO 96/17823, and in U.S. Pat. No. 5,459,127.

[0188] It is also possible to introduce the vector in vivo as a naked DNA plasmid. Naked DNA vectors for gene therapy can be introduced into desired host cells by methods known in the art, e.g., electroporation, microinjection, cell fusion, DEAE dextran, calcium phosphate precipitation, use of a gene gun, or use of a DNA vector transporter (see, e.g., Wilson, et al, J. Biol. Chem. 267:963-967, 1992; Williams et al, Proc. Natl. Acad. Sci. USA 88:2726-2730, 1991). Other reagents commonly used for transfection of plasmids include, but are by no means limited to, FuGene, Lipofectin, and Lipofectamine Receptor-mediated DNA delivery approaches can also be used (Wu et al, J. Biol. Chem. 263:14621-14624, 1988). U.S. Pat. Nos. 5,580,859 and 5,589,466 disclose delivery of exogenous DNA sequences, free of transfection facilitating agents, in a mammal Recently, a relatively low voltage, high efficiency in vivo DNA transfer technique, termed electrotransfer, has been described (Vilquin et al, Gene Ther. 8:1097, 2001; Payen et al, Exp. Hematol. 29:295-300, 2001; Mir, Bioelectrochemistry 53:1-10, 2001; PCT Publication Nos. WO 99/01157, WO 99/01158 and WO 99/01175).

[0189] Pharmaceutical compositions suitable for such gene therapy approaches and comprising nucleic acids encoding an anti-PCSK9 antagonist of the present invention are included within the scope of the present invention.

[0190] In another aspect, the present invention provides a method for identifying, isolating, quantifying or antagonizing PCSK9 in a sample of interest using a PCSK9-specific antagonist of the present invention. The PCSK9-specific antagonists may be utilized as research tools in immunochemical assays, such as Western blots, ELISAs, radioimmunoassay, immunohistochemical assays, immunoprecipitations, or other immunochemical assays known in the art (see, e.g., Immunological Techniques Laboratory Manual, ed. Goers, J. 1993, Academic Press) or various purification protocols. The antagonists may have a label incorporated therein or affixed thereto to facilitate ready identification or measurement of the activities associated therewith. One skilled in the art is readily familiar with the various types of detectable labels (e.g., enzymes, dyes, or other suitable molecules which are either readily detectable or cause some activity/result that is readily detectable) which are or may be useful in the above protocols.

[0191] An additional aspect of the present invention are kits comprising PCSK9-specific antagonists or pharmaceutical compositions disclosed herein and instructions for use. Kits typically but need not include a label indicating the intended use of the contents of the kit. The term label includes any writing, or recorded material supplied on or with the kit, or which otherwise accompanies the kit. In specific embodiments wherein the pharmaceutical composition is provided lyophilized, the kit may include sterile water or saline for reconstitution of the formulation into liquid form. In specific embodiments, the amount of water or saline is from about 0.1 ml to 1.0 ml.

[0192] The following examples are provided to illustrate the present invention without limiting the same hereto:

[0193] A synthetic human Fab library was panned against human PCSK9. Antigen protein PCSK9 was coated on Maxisorp well stripe (Nunc-Immuno Modules) at a concentration of 1-10 μg/ml for overnight at 4° C. Multiple wells of antigen were prepared for each library. 5% milk in PBS was used to block the coated wells at room temperature for 1-2 hours. After a wash with PBS, 100 μl of phage library solution/well (usually 1-5×10¹² in 2% milk-PBS) was added into 4 parallel wells, and incubated for designed length of time (usually 1-2 hours). After several washings with PBST and PBS, the bound phages were eluted from the wells with fresh-prepared 1.4% triethylamine in ddH2O (10 minutes incubation at room temperature), followed immediately with neutralization by adding 50 μl of 1M Tris-HCl (pH 6.8).

[0194] The eluted, enriched phage pool was further amplified through the following steps: First, TG1 cells were infected with eluted phages at 37° C. for 1 hour, then plated out on 2YT agar plates with 2% glucose and 100 μg/ml carbenicillin for overnight culture. Thus TG1 cells harboring enriched phagemid library were harvested from the plates, and infected with helper phage GMCT for 1 hour. The Fab-display phages were then generated from those TG1 cells harboring both library phagemids and GMCT helper phage genome by overnight growth in 2xYT/carbenicillin/Kanamycin at 22° C. The phagemid particles were purified from overnight culture supernatants by precipitation with PEG/NaCl, and re-suspended in PBS. The PEG-precipitation was repeated once. The phage concentration was determined by OD₂₆₈ measurement.

[0195] With amplified first round phages, the panning process as described above was repeated twice for further enrichment of PCSK9-binding phages. The eluted phages from the third round panning were used to infect TG1 cells. The TG1 cells harboring phagemids from third round panning were picked from 2YT agar plates for Fab ELISA screening assay.

[0196] Over 10,000 clones from third round panning were picked by MegaPix Picking Robot (Genetix), and inoculated into 384-well plates with 60 μl of 2YT/2% Glucose/carbenicillin for overnight culture at 30° C. with 450 rpm shaking. The duplicated plates were made by transferring ˜1-3 μl overnight culture from each well into new plates with 50 μl/well of 2YT/0.1% Glucose/carbenicillin. The duplicated plates were incubated in a shaker at 30° C. for 6 hours, then 10 μl/well of IPTG was added for a final concentration of 1 mM. After overnight culture at 22° C., the soluble Fab in IPTG-induction plates were released by adding lysozyme into each well.

[0197] To detect the antigen binding activity of soluble Fabs generated from the above experiment, the antigen plates were generated by overnight coating of 5 μg/ml human PCSK9 antigen. After blocking with 5% milk-PBS and a wash with PBST, 15-20 μl of Fab samples from IPTG-induction plates was transferred into antigen plates for 1-2 hours incubation at room temperature. The plates were washed 5 times with PBS-T, and added with 1:2000 diluted goat anti-human Kappa-HRP (SouthernBiotech Cat. No. 2060-05) or 1:10,000 diluted goat anti-human Fab-HRP in 5% MPBS for 1 hour incubation. After washing away unbound HRP-conjugates with PBST, the substrate solution QuantaBlu WS (Pierce 15169) was then added to each well and incubated for 5-15 minutes. The relative fluorescence units (RFU) of each well was measured to determine the Fab binding activity by using excitation wavelength 330 nm and emission detection wavelength 410 nm.

[0198] The ELISA results showed 30 to 80% clones from third round panning of individual PDL1 sub-libraries bound to antigen PCSK9. The positive clones were then sent out for DNA sequencing. A total of 128 unique Fab sequences were identified from the PDL1 library.

[0199] One particular PCSK9 antagonist of interest, AX114, comprising the following variable heavy and variable light regions was identified from the PDL1-VH3/VK3 sub-library.

[0200]

(AX114 VH)

SEQ 360

EVQLLESGGGLVQPGGSLRLSCKASGYTFSSYGMYWVRQAPGKGLEWIGW

IDPGSGGTKYNEKFKGKATISRDNSKNTLYLQMNSLRAEDTAVYYCARER

YGYYFDYWGQGTLVTVSSAS

(AX114 VK)

SEQ 512

EIVLTQSPATLSLSPGERATITCRASQYVGTYLNWYQQKPGQAPRLLIYD

ASNRATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQVWDSSPPVAFG

GGTKVEIK

[0201] 50 ml of overnight cultures for individual clones in 2YT/2% glucose/Carbenicillin 100 μg/ml were grown in 37° C. shaker incubator. In the second day, 750 mL to 1 L of 2YT/0.1% glucose/100 μg/mL Carbenicillin was inoculated for each clone by transferring 5-10 ml of the overnight culture. The cultures were grown at 30° C. with shaking for approximately 3-4 hours until OD600˜1. IPTG was added to the culture to reach the final concentration of 0.1-0.5 mM. After overnight IPTG induction at 22° C., the cells pellets were collected by centrifugation at 10,000 rpm for 10-15 minutes, to proceed for periplasmic preparation.

[0202] Soluble Fabs were extracted from cell periplasm. The periplasmic preparation was performed as follows. The TG1 pellet was re-suspended in 20 mL pre-chilled PPB buffer (20% Sucrose+2 mM EDTA+30 mM Tris, pH=8), and incubated on ice for 1 hour. The supernatant with soluble Fab was collected by centrifugation. Subsequently, the cell pellet was further re-suspended in 20 mL pre-chilled 5 mM magnesium sulfate with 1 hour incubation on ice. Two supernatants were combined for further Fab purification.

[0203] The soluble Fab from the periplasmic extraction was purified using a HiTrap Protein G HP column (GE Healthcare). The column was initially equilibrated with equilibration buffer (PBS or Tris, pH 7.3). The supernatant from periplasmic preparation was loaded onto a 1-ml or 5-mL protein-G column (HiTrap, GE healthcare). After wash with 10 column volumes (CVs) of equilibration buffer, Fab protein was eluted with 8 CVs of elution buffer (0.3 M acetic acid, pH3). The eluted fractions were collected, and neutralized with 0.5 volume of 1M Tris, pH 9 buffer. The Fab samples were buffer-exchanged into PBS using Amicon centrifugal filters with 10 kD molecular weight cutoff. The quality of purified Fab was analyzed using size exclusion HPLC (SE-HPLC). Purified Fab was also used for ELISA assay and Biacore assay (below). Overall, the summary of Fab yields is ˜1-2 mg/L with high degree of variability, from less than 1 mg/L to well over 10 mg/L. All Fabs show single main peak by SE-HPLC. The ELISA assay results confirmed all Fabs isolated from PDL1 library bound to human PCSK9 antigen.

[0204] The LDL-Receptor (LDLR) and EGF_AB domain of LDLR (this domain involves the interaction with PCSK9) were immobilized on two different flow cells in the same CM5 chips by coupling of amine groups of LDLR or EGF_AB domain onto carboxylated surfaces of sensor chips according to the instruction of Amine Coupling Kit (GE/Biacore). Briefly, LDLR and EGF_AB were diluted to 20 μg/ml in pH 4.5 10 mM Acetate buffer and injected to two flow cells on the same CM5 chip to achieve an immobilization level of ˜1500 RU. 100 nM human PCSK9 alone in running buffer (1×HBSP with 0.1 mM CaCl₂) was injected into the flow cells (at 20 μl/minute for 2.5 minutes) to measure the interaction of PSK9 with LDLR and EGF_AB domain. After injection, the flow cells were regenerated by 10 mM HCl.

[0205] To determine the impact of the binding of Fab antibody to PCSK9, each purified Fab sample (1 μM in the running buffer) was incubated with human PCSK9 at the concentration of 100 nM for 30 minutes at room temperature. The prepared PCSK9/Fab samples were injected into the CM5 chip, and binding of PCSK9/Fab complex was measured. As shown in FIG. 1, human PCSK9 alone bound to both LDLR and EGF_AB domain. When the binding of Fab antibody did not inhibit the PCSK9-LDLR interaction, the binding of PCSK9/Fab complex to LDLR or EGF_AB resulted in higher binding RU then PCSK9 alone. Among the Fab antibodies tested, AX114 Fab showed significant inhibition on PCSK9 binding to LDLR or EGF_AB domain.

[0206] Human PCSK9 protein was immobilized on CM5 chip by coupling primary amine groups of PCSK9 onto carboxylated surfaces of sensor chips according to the instruction of Amine Coupling Kit (GE/Biacore). Briefly, hPCSK9 protein was diluted to 50 μg/ml in pH 5.5/10 mM Acetate solution, and was injected onto the NHS/EDC activated surface to achieve an immobilization level of 1000-2000 RU, followed with surface inactivation by injection of Ethanolamine The Fab or IgG protein (1 μM in HBS-P buffer) was then injected for 3 minutes binding, followed by 5 minutes dissociation. In the binding epitope binning assay, two flow cells were immobilized with same amount of hPCSK9 protein to detect the binding competition between antibody 1 and antibody 2. On the flow cell 1, antibody 1 was injected twice to occupy its binding epitope, antibody 2 was then injected for binding. The flow cell 2 was setup as a reference, only antibody 2 was injected onto it for binding. To determine whether there was competition between antibody 1 and antibody 2, the sensorgrams of antibody 2 from both flow cells were overplayed. When two antibodies competed, pre-occupation of antibody 1 could significantly or totally inhibit the antibody 1 binding. Cross competition for 19 antibodies from PDL1 library was completed, and 3 independent epitope bins on human PCSK9 were identified, see table 2.

[0207]

	TABLE 2
	Bin 1 binder	Bin 2 binder	Bin 3 binder
	AX114	AX1	AX116
	AX132	AX9
	AX139	AX40
	AX212	AX56
	AX213	AX115
	AX210	AX118
	AX211	AX119
		AX188
		AX189
		AX191
	Bin 1 Binder	VH SEQ ID NO	VL SEQ ID NO
	AX114	360	512
	AX132	360	511
	AX137	360	517
	AX139	360	523
	AX210	364	511
	AX211	365	511
	AX212	366	511
	AX213	362	511

[0208] Optimization libraries for AX114 were designed and constructed. All AX114 libraries were panned against PCSK9 antigen for 3-6 rounds as described in Example 1. The clones were picked for Fab ELISA screening as described in Example 2. The PCSK9 binding clones were expressed in TG1 cells for Fab secretion. Purified Fab proteins (Example 3) were run on Biacore for affinity measurements (see Example 14). From these libraries, a total of 135 AX114 variants (listed in table 3) that bind to human PCSK9 were identified, including AX132 (comprising VH and VL regions SEQ ID No: 360 and 511, respectively).

[0209]

TABLE 3
sequence ID for AX114 and its variants
	Sequences	SEQ ID NO:
	VH	360-510
	VK	511-549
	VH_CDR1	189, 191 193, 195, 197-294
	VH_CDR2	68, 70, 72, 74, 76-182
	VH_CDR3	5, 7, 9, 11, 13-63
	VK_CDR1	349, 351, 353-359
	VK_CDR2	339, 341, 343-346
	VK_CDR3	301, 303, 305-334
>SEQ ID NO: 360 (AX132 VH)
EVQLLESGGGLVQPGGSLRLSCKASGYTFSSYGMYWVRQAPGKGLEWI
GWIDPGSGGTKYNEKFKGKATISRDNSKNTLYLQMNSLRAEDTAVYYCA
RERYGYYFDYWGQGTLVTVSSAS [in specific embodiments,
SEQ ID NO: 361]
>SEQ ID NO: 511 (AX132 VK)
EIVLTQSPATLSLSPGERATITCRASQYVGSYLNWYQQKPGQAPRLLIY
DASNRATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQVWDSSPP
VVFGGGTKVEIK
>SEQ ID NO: 362 (AX213 VH)
EVQLLESGGGLVQPGGSLRLSCKASGYTFSRYGINWVRQAPGKGLEWI
GRIDPGNGGTRYNEKFKGKATISRDNSKNTLYLQMNSLRAEDTAVYYCA
RANDGYSFDYWGQGTLVTVSSAS [in specific embodiments,
SEQ ID NO: 363]
>SEQ ID NO: 511 (AX213 VK)
EIVLTQSPATLSLSPGERATITCRASQYVGSYLNWYQQKPGQAPRLLIY
DASNRATGIPARFSGSGSGTDFTLTISSLEPEDFAVYYCQVWDSSPP
VVFGGGTKVEIK

[0210] The sequence changes in the CDR regions for AX114 variants are illustrated in FIGS. 2 and 3.

[0211] Definitions: Given residue on the PCSK9 is counted as in contact with a given antibody, if Cα (see, e.g., “Introduction to Protein Structure” by Carl Branden & John Tooze, 2^nd edition, 1999 Garland publishing) atom of PCSK9 residue is within 10 Angstroms from CA of that antibody. For X-ray structure, the residues in contact define the epitope. For docking poses within a given epitope bin, the residues in the contacts with frequency higher than threshold (>50-75%) define the epitope. Two proteins (e.g. AX114 with a control Fab that competes with AX114 to bind to EGF_AB domain of LDL receptor) are defined as compete based on their structural model if the distance between any Cα atoms of these proteins is shorter than 5 Å.

[0212] Docking procedure: To determine the epitope for AX132, docking was performed with a program involving rigid-body translation/rotation of one partner with respect to the other with optimization of side-chains; see, Gray, J J et al., 2003 J. Mol. Biol. 331:281-299. Since AX114 and AX132 compete with the control Fab, the initial configuration was started from the X-ray structure of control Fab with antibody pulled away approximately 15 Angstroms. The low scoring poses have been clustered and analyzed for contacts to determine the epitope. The epitope for AX213 is assumed similar to AX114/AX132 based on sequence similarity and competition data.

[0213] Based on computational docking studies, three bins have been determined, as shown in FIG. 4. Based on the AX132 binding differentiation between human and rat PCSK9 (table 4), human PCSK9 chimeric mutations to rat PCSK9 residues have been selected to differentiate and test epitope bins. Total 6 chimeric mutants have been designed. Each mutant represents a patch on PCSK9, see table 5. Mutant #1 is in bin 1 and is expected to abrogate binding of AX114/AX132/AX213 based on cross-species binding data. Mutant #2 (from bin 2) or mutant 3 (from bin 3) are expected to abrogate binding of other antibodies.

[0214]

TABLE 4
binding affinities of AX132 variants to human, rhesus, mouse
and rat PCSK9
		Human	Rhesus
		PCSK9	PCSK9	Mouse 9	rat PCSK9
Molecule	Format	KD (M)	KD (M)	KD (M)	KD (M)
AX114	IgG2	2.40E−08	1.16E−08	1.12E−08	N/A
AX132	IgG2	6.16E−09	2.59E−09	2.76E−09	E−7
AX137	IgG2	9.98E−09	1.00E−08	no binding	N/A
AX210	IgG2	2.64E−09	9.44E−10	3.60E−09	N/A
AX211	IgG2	1.63E−09	4.93E−10	1.66E−09	N/A
AX212	IgG2	2.12E−09	7.74E−10	2.74E−09	N/A
AX213	IgG2	2.07E−09	1.89E−09	3.25E−09	N/A

[0215]

TABLE 5
human PCSK9 mutants with residues of rat PCSK9
	Mutants	Residues of rat PCSK9
	Mutant #1	192, 379
	Mutant #2	366, 426
	Mutant #3	201, 202, 206, 207, 247, 248
	Mutant #4	245, 396, 405, 420, 440, 443
	Mutant #5	177, 179, 277, 280
	Mutant #6	162, 173

[0216] The human PCSK9 mutant proteins were produced from HEK293 cells. Briefly, the gene of a full-length human PCSK9 inside a mammalian expression vector with His-tag was modified by site-directed mutagenesis to induce the corresponding mutations based on table 5. Then the vectors of PCSK9 mutants were transiently transfected into human HEK293 cells for 7 to 10 days culture at 37° C. The His-tagged PCSK9 mutant proteins were purified from the culture supernatants by NTA column (GE Healthcare, Pittsburgh, Pa.). The quality of PCSK9 proteins were analyzed using 10% SDS-PAGE.

[0217] ELISA assays were performed to study the bindings of PCSK9 mutants to anti-PCSK9 antibody AX132. Briefly, the PCSK9 mutant proteins were diluted with PBS to the concentration of 5 μg/ml, and coated to a 96-well ELISA plate with 100 μl/each well for overnight at 4° C. After blocking with 5% milk-PBS, AX132 samples (in 5% milk-PBS with 1:2 serial dilution at start concentration of 4 nM) were added to the wells coated with individual PCSK9 mutants, and incubated for 1 hour at room temperature. After PBS wash, the anti-human K antibody conjugated with HRP was added and incubated for another hour. The TMB substrate solution (Thermo Scientific) was then added into PBS-washed plate for 10-20 minutes of development. After adding stop solution, the plates were measured for the absorbance at 450 nM.

[0218] The ELISA results shown in FIG. 5A indicated a significant loss of binding of PCSK9 mutant #1 to antibody AX132. This result suggested that AX132 binds to predicted Bin I. PCSK9 mutant #1 has the amino acid substitutions of D192G and F379Y (FIG. 5B). This region is involved in the binding to EGF_AB domain of LDL receptor.

[0219] In order to identify the various epitope regions of PCSK9 recognized by anti-PCSK9 antibodies, hydrogen deuterium exchange was applied to PCSK9, followed by peptide digestion and mass spectrometry based on protocol of Wood and Hamuro (2001) and further developed and automated; see Hamuro et al., 2003 J. Biomolec. Tech. 14:171-182; and Coales et al., 2009 Rapid Comm. Mass Spectrom. 23:639-647. The multi-step procedure is described in the following.

[0220] Antibody affinity column preparation: Antibody was immobilized by overnight incubation with cyanogen bromide activated Poros AL resin followed by washing with PBS using a filter funnel. The reaction was capped by resuspending the dried resin in ethanolamine solution for 2 hours and followed with washing with PBS using a filter funnel. The resin was resuspended in PBS then packed into a column. Column was equilibrated with PBS with 2 mM NaCl pH 7 in exchange buffer H at 3° C. All column injections and incubations were done using a syringe pump.

[0221] On-solution and off-column deuterium exchange: Exchange H buffer was prepared as PBS in water. Exchange D buffer was prepared as PBS in D2O. Exchange HD buffer was prepared as PBS in 50% D2O. All exchange steps were conducted at 3° C. The mAb column was cleaned with 0.8% formic acid and washed and equilibrated with exchange HD buffer. On-solution exchange of deuterons was initiated by mixing PCSK9 sample 1:1 with exchange D buffer and incubated for predetermined times. The mixture was then injected into mAb column and washed with exchange HD buffer. Off-column exchange was initiated by washing with exchange H buffer and incubating for predetermined times. Off-column exchange was quenched and PCSK9 was eluted using 0.8% formic acid. Fractions were collected and analyzed.

[0222] On- and off-column deuterium exchange: All exchange steps were conducted at 3° C. The mAb column was cleaned with 0.8% formic acid and washed and equilibrated with exchange HD buffer. PCSK9 in exchange H buffer was loaded onto the mAb column and washed with exchange H buffer. On-column exchange of deuterons was initiated by the injection of exchange HD buffer and incubating for predetermined times. Off-column exchange was performed and quenched as above. Fractions were collected and analyzed.

[0223] Full deuteration of PCSK9: PCSK9 was equilibrated in PBS prepared in D2O and incubated at 60° C. for 3 hours. This was cooled to room temperature and stored on ice. Fully deuterated PCSK9 was loaded onto an antibody affinity column in HD exchange buffer and washed in same buffer. Elution and analysis were carried out the same as above.

[0224] Peptide Analysis by Mass Spectrometry: Eluted PCSK9 was injected into an immobilized pepsin column and then onto a C18 reversed-phase LC-MS to identify fragments. PCSK9 from eluted fractions was denatured and reduced in 2M urea, 1M TCEP, pH3, 0° C. for 2 minutes. The sample was then passed over immobilized pepsin column in buffer A (0.05% TFA in water). The peptic fragments were loaded onto a reversed phase trap column and desalted in buffer A. Peptic fragments were separated by a C18 column with a linear gradient of 13-40% Buffer B (95% acetonitrile, 5% water, 0.0025% TFA) in 23 minutes. Peptides were detected by mass spectrometry.

[0225] The shift in the masses of known peptic fragments detected by MS is used to determine the HD exchange level. The percent exchange is determined from ratio HD exchange of bound vs. unbound PCSK9 and indicates degree of epitope protection by the antibody. Percent deuteration change is cutoff at 5% as threshold to remove noise.

[0226] The HD exchange profiles for AX132 and AX213 antibodies are shown in FIG. 6. The PCSK9 peptic fragments that exhibit the greatest deuteration difference upon AX213 or AX132 binding are 155-PWNL-158 (SEQ ID NO: 576) and 364-PGEDIIGASSDCSTC-378 (SEQ ID NO: 577) where subfragments 157-NL-158 and 370-GASSDCSTC-378 (SEQ ID NO: 578) appear to contain the epitope. There may be other weakly interacting sites but these are below the cutoff threshold (5%) and are likely due to indirect or local structural perturbations.

[0227] FIG. 7 shows PCSK9 (PDB: 2PMW) with the two peptic fragments containing the AX132 and AX213 epitope highlighted. Grey corresponds to 155-PWNL-158 (SEQ ID NO: 576) and dark grey corresponds to 364-PGEDIIGASSDCSTC-378 (SEQ ID NO: 577). The auto cleaved prodomain is largely hidden from this view.

[0228] The HD exchange data is consistent with the PCSK9 mutagenesis data in Example 7. Both 155- and 364-peptides are located in the epitope bin #1 as shown in FIG. 4,

[0229] Thermostabilities of Fabs and Fab domains were determined from DSC experiments by analysis and deconvolution of excess heat capacity function in Origin 5.0. The melting transition temperatures (Tm) for Fabs or Fab domains are indicated in Table 6. The Tm of various Fabs and Fab domains range from 72 to 78° C. for PDL1 derived antibodies, which is consistent with well folded antibody Fab region.

[0230]

TABLE 6
Thermostabilities of AX114 variants
	IgG	Fab domain (Tm, ° C.)
	Ax114-IgG1	76.7
	AX114-IgG2	76.5
	AX132-IgG2	77.4

Expression

[0231] Nucleic acid expressing AX132 Fab was incorporated into a phage library display vector, and extraneous N- and C-terminal residues were removed from the vector prior to expression and purification of the Fab for crystallization, as follows:

• • [0232] 1) Codons expressing 3 extra amino acids (AGS) between the p3 leader and the H chain FR1 in the vector were removed, generating an authentic heavy chain N-terminus following cleavage of the p3 signal peptide in E. coli.
  • [0233] 2) In order to facilitate Fab crystallization, the GR1 adaptor domain coding region at the heavy chain C-terminus in the vector was removed prior to Fab expression and purification, and a termination codon was introduced immediately following the coding sequences of the HA and His tags. This was accomplished by subcloning the light and heavy chain Fab expression cassette (HindIII-XhoI) into plasmid pMAB9, which carries those modifications.
    The final expression plasmid for purification is illustrated in FIGS. 20A-E, and the vector map is illustrated in FIG. 19. The plasmid expresses both the light and heavy chains in a bicistronic message off the lac promoter. The light chain open reading frame is expressed at the 5′ end of the message following the p8 leader, and then the heavy chain follows after the p3 leader.
    Purification of AX132

[0234] AX 132 was purified from E. coli over a nickel affinity column followed by SP Sepharose column chromatography,

Purification of PCSK9:

[0235] Secreted PCSK9 was captured from HEK 293 cell over a capto Q column. The bound protein was pooled and further purified over a nickel affinity column followed by size exclusion column (S200) chromatography

Complex-Generation:

[0236] Purified AX 132 was mixed with purified PCSK9 at a molar ratio of 1.5:1 and incubated for 12 hours at 4° C. The mixture was further fractionated on a 2× Superdex 200 (16-60) column to get rid of uncomplexed AX 132. The purified complex was concentrated to 10 mg/ml and crystallized without any freeze-thaws.

Crystallization

[0237] The PCSK9:AX132 complex yielded crystals in different crystallization conditions. Generally, the complex was frozen in the presence of cryoprotectant. The crystal diffracted up to 3.09 Å at synchrotron. The structure of PCSK9 bound to the AX132 Fab fragment was determined by a molecular replacement method. AX132 binds at the EGF-A binding site. The light chain of the antibody AX132 is mainly responsible for the interactions with PCSK9. Multiple hydrogen bonding and hydrophobic interactions are observed at the interface.

[0238] FIG. 8 depicts the crystal structure of PCSK9 bound to the AX132 antibody. FIG. 9 shows the surface area representation of PCSK9 with the AX132 epitope. The coordinates for the crystal structure discussed are presented in Table 14, Example 21.

[0239] The residues involved in the binding are identified by calculating the difference in accessible surface area between the AX132:PCSK9 crystal structure and PCSK9 structure alone. PCSK9 residues that show buried surface area upon complex formation with AX132 antibody are included as a part of the epitope. The solvent accessible surface of a protein is defined as the locus of the center of a probe sphere (representing a solvent molecule) as it rolls over the Van der Waals surface of the protein. The solvent accessible surface area was calculated by using the program AREAIMOL (see, Lee et al., 1997 J. Mol. Biol. 55:5-11 and Saff et al., 1997 The Mathematical Intelligencer 19:5-11), which generates surface points on an extended sphere about each atom (at a distance from the atom center equal to the sum of the atom and probe radii) and eliminates those that lie within equivalent spheres associated with neighboring atoms (Briggs, P. J. 2000, CCP4 Newsletter No. 38, CCLRC, Darebury).

[0240] The antibodies with AX132 binding epitope can also be selected out from a phage display antibody library using EGF_AB peptide that competes with AX132. After binding of phage library to human PCSK9 coated on plate, the EGF_AB protein can be added to elute the binding phages. The individual clones from the EGF_AB eluted phage pool can then be screened against human PCSK9 and PCSK9 mutant #1. As shown in FIG. 5A, AX132 bind to human PCSK9 with high affinity, but very low affinity to human PCSK9 mutant #1 (see, Example 7). The Fabs that bind to human PCSK9 can be subjected to a binding screening assay against PCSK9 mutant #1 protein, and the Fab with strong binding to human PCSK9 but weak binding to PCSK9 mutant #1 will share the AX132 binding epitope.

[0241] The DNA sequence encoding the Vk1 or VK3 light chain variable region was amplified by polymerase chain reaction from plasmid template. The product of this amplification was cloned into plasmid pVUNSAGS-FB-LCK that had been previously digested with Fspl and Bmtl, using the InFusion cloning system (Clontech). The resulting plasmid was verified by DNA sequencing across the variable region. Endotoxin-free plasmid preparations were made using the Qiagen Endo-Free plasmid maxiprep kit. The DNA sequence encoding the heavy chain variable region of VH3 was amplified by polymerase chain reaction, and the amplified product was cloned into plasmid pVl JNSA-BF-HCG2M4 that had been previously digested with Fspl and Bmtl. The resulting plasmid was verified by DNA sequencing across the variable region. Endotoxin-free plasmid preparations were made using the Qiagen Endo-Free plasmid maxiprep kit.

[0242] The plasmid DNA for heavy and light chain was mixed at 1:3, and co-tranfected into HEK293 cells. After 5-7 days culture, the supernatant was harvested and proceeded for Protein-A column purification. Briefly, the cell free supernatant was loaded on to protein-A column pre-equilibrated with three column volume of 20 mM Tris-HCl pH7.0 at a flow rate of 5.0 mL/min. The column was washed with three column volumes of the 20 mM Tris-HCl pH7.0 followed by a five column volume wash with 20 mM Tris-HCl pH7.0 containing 1M NaCl to remove the host cell proteins. The anti-PCSK9 antibody was eluted with five column volume of 100 mM Glycine, 100 mM Arginine pH 3.0 and immediately neutralized with 1M Tris-HCl pH8.0.

[0243] Anti-PCSK9 IgG2 monoclonal antibodies were expressed in glyco-engineered Pichia pastoris GFI 5.0 host YGLY8316, which is capable of transferring terminal galactose at its complex N-linked glycan. Anti-PCSK9 heavy and light chains were codon optimized and expressed under methanol tightly inducible promoter AOX1 using Saccharomyces cerevisiae alpha mating factor presequence as secretion signal sequence. Anti-PCSK9 antibody from Pichia pastoris GFI 5.0 host YGLY8316 was captured from cell free supernatant media by affinity chromatography using MabSelect™ medium from GE Healthcare (Cat. #17-5199-01). The cell free supernatant was loaded on to Mabselect column (XK 16/20, 1.6 cm×10.0 cm) pre-equilibrated with three column volume of 20 mM Tris-HCl pH7.0 at a flow rate of 5.0 mL/min. The column was washed with three column volumes of the 20 mM Tris-HCl pH7.0 followed by a five column volume wash with 20 mM Tris-HCl pH7.0 containing 1M NaCl to remove the host cell proteins. The anti-PCSK9 antibody was eluted with five column volume of 100 mM Glycine, 100 mM Arginine pH 3.0 and immediately neutralized with 1M Tris-HCl pH8.0. AX213 antibody was well expressed in Pichia, yielding ca. 300-700 mg/L of protein in a small scale fermentation process. The yield for AX114 was 5 mg/L in small scale.

[0244] Strong Cation Exchange Chromatography employing Source 30S resin from GE Healthcare (Cat #17-1273-02) was used as the second step purification to remove the clipped species and aggregates. A MabSelect™ (GE Healthcare, Pittsburgh, Pa.) pool of the anti-PCSK9 antibody was 5× diluted with 25 mM Sodium acetate pH5.0 and loaded on to the Source 30S column pre-equilibrated with three column volume of 25 mM Sodium acetate pH5.0. After loading, the column was washed with three column volume of the 25 mM Sodium acetate pH5.0 and elution was performed by developing a linear gradient over ten column volume ranging from 100 mM to 150 mM Sodium chloride in 25 mM Sodium acetate pH5.0. The fractions containing good assembled anti-PCSK9 antibody was pooled together. The Source 30S pooled fractions that contained the anti-PCSK9 antibody was buffer exchanged into the formulation buffer containing 6% Sucrose, 100 mM Arginine, 100 mM Histidine pH6.0 (HyClone® Cat #RR10804.02) and sterile filtered using 0.2 μm PES (PolyEtherSulfone) membrane filter and stored @4° C. until release.

[0245] To determine the binding affinity of Fab to PCSK9, Fab capture-based Biacore assay was developed. First, goat anti-Fab IgGs were immobilized onto CM5 chip by amine coupling as described above. The anti-Fab IgGs were diluted to 200 μg/ml in pH 5/10 mM Acetate solution, and injected onto the NHS/EDC activated surface to achieve an immobilization level of ˜10,000 RU, followed with surface inactivation by injection of Ethanolamine. Then Fab samples at concentration of 2 μg/ml in HBS-P running buffer were injected for 3 minutes at flow speed of 20 ul/min, followed with K-injection (3 minutes injection for association and 6 minutes for dissociation) of PCSK9 at concentration of 10 to 100 nM. The sensor chip surface was regenerated by 30 second injection of 100 mM phosphoric acid. The binding sensorgrams were fitted with 1:1 Langmuir binding model to determine the binding affinity. The Fab affinities of AX114, AX132 and other variants are shown in table 7.

[0246]

TABLE 7
Fab binding affinity
	Fabs	Binding affinity to human PCSK9
	Name	ka (1/Ms)	kd (1/s)	KD (M)
	AX114	7.17E+04	3.48E−03	4.85E−08
	AX132	9.11E+04	1.08E−03	1.18E−08
	AX137	1.07E+05	2.08E−03	1.95E−08
	AX139	8.97E+04	1.18E−03	1.32E−08
	AX201	1.31E+05	1.02E−03	7.82E−09
	AX202	1.09E+05	1.02E−03	9.43E−09
	AX204	2.34E+05	9.87E−04	8.39E−09
	AX205	1.04E+05	9.72E−04	9.45E−09
	AX206	1.22E+05	1.03E−03	8.42E−09
	AX207	1.11E+05	1.00E−03	9.23E−09
	AX208	9.84E+04	2.59E−03	2.64E−08
	AX209	1.12E+05	1.07E−03	9.60E−09
	AX210	1.72E+05	2.87E−04	1.67E−09
	Ax211	1.97E+05	3.29E−04	1.67E−09
	AX212	1.59E+05	2.33E−04	1.47E−09
	AX213	2.43E+05	3.29E−04	1.37E−09
	AX214	1.92E+05	3.19E−04	1.60E−09
	AX215	1.16E+05	3.76E−04	3.47E−09
	AX216	1.15E+05	2.88E−04	2.51E−09
	AX217	1.38E+05	3.40E−04	2.52E−09
	AX239	3.03E+04	9.60E−04	3.16E−08
	AX240	1.60E+05	1.66E−04	1.04E−09
	AX241	1.97E+05	1.60E−04	8.13E−10
	AX242	1.62E+05	1.93E−04	1.19E−09
	AX243	1.31E+05	1.91E−04	1.46E−09
	AX244	1.89E+05	2.03E−04	1.07E−09
	AX245	1.12E+05	3.19E−04	2.84E−09
	AX246	2.49E+05	2.01E−04	8.06E−10
	AX247	1.86E+05	2.44E−04	1.31E−09
	AX248	1.89E+05	2.07E−04	1.09E−09
	AX249	1.90E+05	2.06E−04	1.08E−09
	AX250	3.07E+05	2.40E−04	7.81E−10
	AX251	2.54E+05	2.52E−04	9.93E−10
	AX252	1.37E+05	4.67E−04	3.42E−09
	AX253	1.61E+05	6.81E−04	4.23E−09
	AX254	9.24E+04	2.95E−04	3.19E−09
	AX255	9.61E+04	3.91E−04	4.07E−09
	AX256	1.26E+05	3.65E−04	2.90E−09
	AX257	2.53E+05	1.68E−04	6.64E−10
	AX258	1.12E+05	6.30E−04	5.63E−09
	AX259	6.92E+04	6.04E−04	8.73E−09
	AX260	4.19E+04	5.20E−04	1.24E−08
	AX260	2.64E+04	5.70E−04	2.16E−08
	AX263	2.78E+04	1.70E−04	6.11E−09
	AX267	1.29E+05	4.75E−04	3.70E−09
	AX268	2.77E+04	4.17E−04	1.50E−08
	AX269	1.13E+05	3.14E−04	2.77E−09
	AX269	9.49E+04	3.20E−04	3.37E−09
	AX299	1.03E+05	2.57E−04	2.51E−09
	AX300	1.15E+05	3.12E−04	2.72E−09
	AX301	1.28E+05	6.00E−04	4.67E−09
	AX302	1.14E+05	6.68E−04	5.89E−09
	AX303	7.37E+04	8.61E−04	1.17E−08
	AX306	9.04E+04	4.47E−04	4.94E−09
	AX307	8.88E+04	2.70E−03	3.03E−08
	AX308	5.23E+04	2.59E−03	4.96E−08
	AX310	1.09E+05	7.43E−04	6.79E−09
	AX311	1.47E+05	4.98E−04	3.39E−09
	AX312	1.58E+05	1.41E−03	8.94E−09
	AX313	2.13E+05	7.35E−04	3.46E−09
	AX314	1.09E+05	1.72E−03	1.58E−08
	AX315	4.65E+04	2.31E−04	4.97E−09
	AX316	1.57E+05	5.63E−04	3.59E−09
	AX318	1.67E+05	2.71E−05	1.62E−10
	AX319	2.59E+05	4.25E−05	1.64E−10
	AX320	1.51E+05	2.62E−05	1.74E−10
	AX322	1.19E+05	1.83E−04	1.54E−09
	AX323	1.79E+05	8.36E−05	4.66E−10
	AX325	1.39E+05	1.19E−04	8.53E−10
	AX326	1.68E+05	6.52E−05	3.87E−10
	AX329	1.33E+05	2.09E−04	1.57E−09

[0247] The Fabs which showed functional efficacy in the cell-base assays were converted into IgG molecules. The affinities of those IgG molecules were also measured by Biacore assay. Briefly, anti-human IgG monoclonal antibody form Human Antibody Capture Kit provided by Biacore was immobilized on CM5 chips at level of 8000 to 10000 RU. The IgG samples at concentration of ˜0.4 μg/ml was injected onto a sensor chip for 2 minutes at a flow rate of 20 μl/min, then PCSK9 proteins at 5 concentrations (3.75 to 60 nM) were injected onto an IgG captured flow cell for binding kinetic analysis. After each round injection, the sensor chip surface was regenerated by 30 second injection of 3M Magnesium Chloride. The affinities of AX114, AX1213 and other variants are shown in table 8 and table 9.

[0248]

TABLE 8
Purified IgGs against human PCSK9
	Name	ka (1/Ms)	kd (1/s)	KD (M)
	AX114	1.51E+05	3.61E−03	2.40E−08
	AX132	2.48E+05	1.52E−03	6.16E−09
	AX137	3.33E+05	3.32E−03	9.98E−09
	AX210	2.35E+05	6.21E−04	2.64E−09
	AX211	3.61E+05	5.89E−04	1.63E−09
	AX212	1.53E+05	3.24E−04	2.12E−09
	AX213	3.53E+05	7.30E−04	2.07E−09

[0249]

TABLE 9
Purified IgGs against rhesus PCSK9
	Name	ka (1/Ms)	kd (1/s)	KD (M)
	AX240	1.41E+06	3.09E−04	2.20E−10
	AX241	1.56E+06	3.46E−04	2.22E−10
	AX242	1.76E+06	3.25E−04	1.85E−10
	AX243	7.71E+05	8.70E−04	1.13E−09
	AX245	8.90E+05	1.05E−03	1.18E−09
	AX246	1.48E+06	6.14E−04	4.16E−10
	AX248	1.16E+06	4.58E−04	3.96E−10
	AX249	1.22E+06	6.53E−04	5.35E−10
	AX250	2.09E+06	6.23E−04	2.98E−10
	AX253	1.62E+06	1.76E−03	1.09E−09
	AX267	1.38E+06	1.26E−03	9.13E−10
	AX277	9.99E+05	1.67E−03	1.67E−09
	AX369	9.71E+05	2.30E−03	2.37E−09
	AX370	1.01E+06	2.31E−03	2.28E−09
	AX402	1.09E+06	2.32E−03	2.12E−09
	AX406	8.86E+05	2.01E−03	2.27E−09
	AX408	7.65E+05	1.50E−03	1.96E−09
	AX415	7.50E+05	3.12E−03	4.15E−09
	AX417	1.10E+06	9.04E−04	8.22E−10
	AX419	1.25E+06	9.41E−04	7.51E−10
	AX426	6.92E+05	6.28E−04	9.08E−10
	AX427	7.45E+05	5.60E−04	7.51E−10
	AX428	6.55E+05	4.43E−04	6.76E−10
	AX429	7.25E+05	5.88E−04	8.11E−10
	AX430	9.15E+05	8.52E−04	9.31E−10
	AX432	7.39E+05	1.25E−03	1.69E−09
	AX436	4.81E+05	7.93E−04	1.65E−09
	AX439	7.40E+05	7.36E−04	9.94E−10
	AX441	7.92E+05	8.22E−04	1.04E−09
	AX444	7.08E+05	4.99E−04	7.06E−10

[0250] This assay is a variant of the one described in Fisher et al., 2007 J. Biol. Chem. 282:20502-20512. AlexaFluor647-labeled PCSK9 (final concentration 10 nM) was combined with varying amounts of AX132 and variants and to this was added Eu(8044)-labeled LDLR ectodomain to a final concentration of ˜4 nM (sufficient to give ˜20,000 counts at F1620 nM on the Rubystar) in 10 mM HEPES (pH 7.4), 150 mM NaCl, 0.1 mM CaCl₂, 0.05% (w/v) BSA in a total volume of 50 μL using 96 well black Dynatech U bottom plates. After at least 90 minutes of equilibration, samples were read in a Rubystar reader (BMG Corp.) using 20 flashes per well, a 50 μsec integration delay, and a 200 μsec total integration time. Data were expressed as the ratio of (Fl₆₆₅/Fl₆₂₀×10000), and IC₅₀s for AX132 and variants were determined from the inflection point of a sigmoidal dose-response curve using a standard four parameter fit.

[0251] FIG. 10 illustrates the activity of AX132 and its variants in the PCSK9-LDLR interaction TR-FRET assay. The IgG of AX132 and its variants are potent [with an IC₅₀ of 2.4 to 5.9 nM] and inhibit the PCSK9-LDLR interaction fully.

[0252] On day 1, 30,000 HepG2 or HEK cells/well were plated in a 96 well polyD-lysine coated plate. On day 2, the media was switched to no-serum containing DMEM media. On day 3, the media was removed and the cells were washed with OptiMEM. Purified PCSK9 was added in 100 μl of DMEM media containing LPDS and dI-LDL. The plates were incubated at 37° C. for 6.5 hours. The cells were washed quickly in TBS containing 2 mg/ml BSA; then washed in TBS-BSA for 2 minutes; and then washed twice (but quickly) with TBS. The cells were lysed in 100 μl RIPA buffer. Fluorescence was then measured in the plate using an Ex 520, Em 580 nm. The total cellular protein in each well was measured using a BCA Protein Assay and the fluorescence units were then normalized to total protein.

[0253] The Exopolar Assay is effective for characterizing variant effects on LDL uptake; see Table 10 below illustrating how the potencies of PCSK9 mutants correlate with plasma LDL-cholesterol in the Exopolar Assay.

[0254]

	TABLE 10
				EC-50 (nM)
	Mutation	Gain/Loss	LDL-C (mg/dI)	Exopolar
	S127R	Gain	277	14
	D374Y	Gain	388	1.3
	Wild-type		140	51
	R46L	Loss	116	78

[0255] Results: 54 Fabs listed in table 11 inhibited the effect of human (“h”), rhesus (“rh”) and murine (“m”) PCSK9 on LDL uptake in a dose-dependent way, with IC50 (human PCSK9) ranging from 4˜178.7 nM.

[0256]

TABLE 11
Inhibition of PCSK9 on LDL uptake by Fabs
	Fab IC50 (nM)
	Antibody	hPCSK9	rhPCSK9	mPCSK9
	AX114	178.7	194.0	326.0
	AX132	62.2	N/A	26.9
	AX137	74.4	N/A	27.4
	AX139	37.7	N/A	22.9
	AX201	36.0	N/A	N/A
	AX202	31.2	N/A	N/A
	AX204	26.7	N/A	N/A
	AX205	26.1	N/A	N/A
	AX206	30.3	N/A	N/A
	AX207	25.6	N/A	N/A
	AX209	35.4	N/A	N/A
	AX210	26.8	N/A	N/A
	AX211	12.6	N/A	N/A
	AX212	13.8	N/A	N/A
	AX213	14.7	N/A	N/A
	AX214	15.1	N/A	N/A
	AX215	19.3	N/A	N/A
	AX216	17.1	N/A	N/A
	AX217	21.4	N/A	N/A
	AX240	65	N/A	N/A
	AX241	5	N/A	N/A
	AX242	9	N/A	N/A
	AX243	17	N/A	N/A
	AX244	13	N/A	N/A
	AX245	28	N/A	N/A
	AX246	17	N/A	N/A
	AX248	29	N/A	N/A
	AX249	25	N/A	N/A
	AX250	11	N/A	N/A
	AX254	11	N/A	N/A
	AX255	4	N/A	N/A
	AX256	18	N/A	N/A
	AX257	13	N/A	N/A
	AX258	11	N/A	N/A
	AX259	9	N/A	N/A
	AX267	11	N/A	N/A
	AX268	12	N/A	N/A
	AX269	22	N/A	N/A
	AX272	19	N/A	N/A
	AX273	10	N/A	N/A
	AX277	20	N/A	N/A
	AX302	20	N/A	N/A
	AX303	19	N/A	N/A
	AX304	23	N/A	N/A
	AX305	42.0	N/A	N/A
	AX318	7	N/A	N/A
	AX319	7	N/A	N/A
	AX320	9	N/A	N/A
	AX322	26	N/A	N/A
	AX323	13	N/A	N/A
	AX325	4	N/A	N/A
	AX326	11	N/A	N/A
	AX329	9	N/A	N/A
	AX330	20	N/A	N/A

[0257] For IgGs, 7 antibodies listed in table 12 dose-dependently inhibited the effects of both human and rhesus PCSK9 on LDL uptake (FIG. 11-13); an effect which was reproducibly observed. The amount of PCSK9 added to the cells was ˜5-320 nM.

[0258]

TABLE 12
inhibition of PCSK9 by IgGs
	IgG2 IC50 (nM)
	Antibody	hPCSK9	rhPCSK9	mPCSK9
	AX114	36.6	14.4	27.4
	AX132	8.9	11.5	9.4
	AX137	9.8	10.0	5.3
	AX210	6.5	9.7	15.9
	AX211	7.5	4.4	11.1
	AX212	9.5	4.7	7.3
	AX213	11.1	10.2	7.0

[0259] FIGS. 11A-F illustrate (i) AX114 or AX132 (IgG)'s dose-dependent inhibition of human PCSK9-dependent loss of cellular LDL-uptake (A, D); (ii) AX114 or Ax132 (IgG)'s dose-dependent inhibition of murine PCSK9-dependent loss of cellular LDL-uptake (B, E); and (iii) AX114 or AX132 (IgG)'s dose-dependent inhibition of rhesus PCSK9-dependent loss of cellular LDL-uptake (C, F).

[0260] FIGS. 12A-F illustrate (i) AX210 or AX211 (IgG)'s dose-dependent inhibition of human PCSK9-dependent loss of cellular LDL-uptake (A, D); (ii) AX210 or AX211 (IgG)'s dose-dependent inhibition of murine PCSK9-dependent loss of cellular LDL-uptake (B, E); and (iii) AX210 or AX211 (IgG)'s dose-dependent inhibition of rhesus PCSK9-dependent loss of cellular LDL-uptake (C, F).

[0261] FIGS. 13A-F illustrate (i) AX212 or AX213 (IgG)'s dose-dependent inhibition of human PCSK9-dependent loss of cellular LDL-uptake (A, D); (ii) AX212 or AX213 (IgG)'s dose-dependent inhibition of murine PCSK9-dependent loss of cellular LDL-uptake (B, E); and (iii) AX212 or AX213 (IgG)'s dose-dependent inhibition of rhesus PCSK9-dependent loss of cellular LDL-uptake (C, F).

[0262] Our internal data showed that monoclonal antibodies with identical Fc sequences but different Fab domains can bind FcRn with considerable differences. Moreover, an apparent correlation between dissociation at neutral pH and in vivo pharmacokinetics was observed: mAbs with slow dissociation (i.e. >5% “% bound” tend to show shorter terminal half life (t½) in vivo). This feature was used as an in vitro screening tool for antibody pharmacokinetics.

[0263] The neutral pH dissociation of mAbs from human FcRn was measured by SPR using a Biacore T-100 instrument. Briefly, purified FcRn protein was immobilized onto a Biacore CM5 biosensor chip and PBSP (50 mM NaPO4, 150 mM NaCl and 0.05% (v/v) Surfactant 20) pH 7.3 was used as running buffer. The mAbs were diluted with PBSP pH 6.0 to 100 nM, allowed to bind FcRn for 3 minutes to reach equilibrium and followed by 1 minute of dissociation in pH 7.3 running buffer. A report point (Stability) was inserted at 5 seconds after the end of mAb binding and the “% bound” was calculated as RUStability/RUBinding (%).

[0264] FIGS. 14-15 illustrate binding of AX114, AX132, AX210-213 to immobilized human FcRn with Biacore. The sensorgrams show both binding at pH 6.0 and dissociation at pH 7.3. A report point (Stability) was inserted at 5 seconds after then end of pH 6.0 binding and the “% bound” was calculated as RU_Stability/RU_Binding(%).

[0265] The interaction between IgG and FcRn is species-specific. Human FcRn mice have recently been suggested as a valuable surrogate system for evaluating mAb pharmacokinetics; Petkova et al., 2006 Int. Immunol. 12:1759-69. The human FcRn mice (heterozygous Tg276) used in this study were obtained from Jackson Laboratory (Bar Harbor, Me.). They are deficient in mouse FcRn-α chain and carry a human FcRn-α chain gene. Id. Our internal data showed that unlike mouse or rat FcRn, this “hybrid” FcRn had comparable human IgG binding characteristics as that of human and monkey FcRn. In addition, good terminal half life correlation between this human FcRn mice and non-human primate was observed.

[0266] For pharmacokinetics studies, each animal (2-3/group) received a single intravenous injection of mAb at 10 mg/kg via tail vein. Series of 10 μL of blood was collected at specified time points. A validated anti-human IgG immunoassay was used to determine all mAb levels.

[0267] The pharmacokinetic profile of AX114, AX132 and AX213 were determined in human FcRn mice following a single 10 mg/kg IV administration. FIG. 16 illustrates the half-life of AX114 and AX132 determined to be 79.6 and 65.5 hours, respectively. The half-life of AX213 was determined to be 97 hours.

[0268] The pharmacokinetic profile of AX132 was also determined in rhesus monkey following a single 10 mg/kg IV administration. The half-life of AX132 was determined to be 147 hours.

[0269] To characterize pharmacokinetics, pharmacodynamics and target engagement of AX132, a single dose study was conducted in 6 Rhesus monkeys at 1 mg/kg with subcutaneous route of administration. All Rhesus monkeys used in the study were naive to biologies. Blood samples were collected from the saphenous/femoral vessel at designated time points post dosing and the resulting plasma/serum was stored at −70° C. until analysis.

[0270] To generate lipoprotein profiles, plasma or serum was fractionated by chromatography over Superose-6 size exclusion column (GE LifeSciences, Inc.). Total cholesterol levels in the column effluent were continuously measured via in-line mixture with a commercially available enzymatic colorimetric cholesterol detection reagent (Total Cholesterol E, Wako USA) followed by downstream spectrophotometric detection of the reaction products at 600 nm absorbance. The first peak of cholesterol eluted from the column was attributed to VLDL, the second peak to LDL and the third to HDL; the area under each peak was calculated using software provided with the HPLC. To calculate the cholesterol concentration for each lipoprotein fraction, the ratio of the corresponding peak area to total peak area was multiplied by the total cholesterol concentration measured in the sample.

[0271] The lipoprotein analysis of the serum samples were carried out as described above. An anti-human IgG ELISA using commercially available reagents was used to quantify Ax132 levels.

[0272] As shown in FIG. 17, AX132 significantly lowered LDL cholesterol following a single dose, with a maximum mean reduction of 60%, and >25% LDL-C lowering for 42 days.

[0273] High Performance-Size Exclusion Chromatography (HP-SEC) is an analytical method used to separate proteins based on order of decreasing size. This method was used to quantitate the level of aggregation and/or fragmentation of proteins after process and purification (time zero) and after accelerated stability studies. Size Exclusion Chromatography was performed with a Waters 2690 Separations Module/996 Photodiode Array Detector. Material was separated using a TSKgel G3000SW_XL (4.6×300 mm) column with a Phenomenex pre-filter GFC 4000 (4×3 mm) The column was loaded with 10 μg of material and eluted with a 25 mM sodium phosphate 300 mM sodium chloride pH 7.0 mobile phase at a flow rate of 0.5 ml/min for 30 min. Data was acquired from 200-500 nm and 220 nm profiles were reported.

[0274] Monoclonal antibodies were formulated at 0.5 mg/ml in pH 5, 6, 7, and 8 buffers. The buffers contained 150 mM sodium chloride and 10 mM acetate, histidine, phosphate, and TRIS for pH 5, 6, 7, and 8 respectively. HP-SEC was used to characterize material purity at time zero and after one weak at 45° C. Stability results are summarized in Table 13 below. FIG. 18 shows time zero SEC profiles. The boxed labels in the figure define the approximate elution times of higher order aggregates (HOAs), oligomer, monomer, and clipped protein.

[0275]

TABLE 13
Physical Stability data at time zero and after thermal stress (1 week 45 C.)
	1 week stress at 45 C. in
	pH 5, 6, 7, and 8 buffers
	T0	Inc in
			Elution	Pre				Pre
	Cell	Theoretical	time	Mon2				Mon2	Inc in	Inc in	Inc in
mAb1	line	pl	(min)	Peak	Olig3	HOA4	Clip5	Peak	Olig3	HOA4	Clip5
AX114	HEK293	7.6815	16.1	no	<5%	No	no	na	no	no	no
AX132	HEK293	7.6815	16.0	no	<5%	No	no	na	no	no	1%
											pH 8
AX210	HEK293	7.8225	16.1	no	<5%	No	no	na	≈2%	no	no
AX211	HEK293	7.9447	16.1	no	<5%	No	no	na	no	no	no
AX212	HEK293	7.8223	16.2	no	≈25%	No	no	na	no	no	no
AX213	HEK293	7.8231	16.1	no	<5%	No	no	na	no	no	no
1mAb: monoclonal antibody
2Mon: monomer
3Olig: Oligomer
4HOA: higher order aggregate
5Clip: Clipped protein

[0276] The coordinates for the crystal structures discussed in Example 10 are presented in Table 14 (full length PCSK9 and AX132 Fab).

[0277]

TABLE 14
PCSK9 and AX132 Fab complex x-ray structure
ATOM	17	CB	PRO	B	155	−82.132	20.346	−24.263	1.00	87.08	C
ATOM	1	N	SER	B	153	−87.150	14.839	−25.924	1.00	107.36	N
ATOM	2	CA	SER	B	153	−87.121	15.824	−27.023	1.00	107.09	C
ATOM	3	CB	SER	B	153	−88.455	16.570	−27.109	1.00	107.02	C
ATOM	4	OG	SER	B	153	−88.594	17.255	−28.345	1.00	107.56	O
ATOM	5	C	SER	B	153	−85.944	16.829	−26.896	1.00	106.67	C
ATOM	6	O	SER	B	153	−85.196	16.763	−25.908	1.00	107.20	O
ATOM	7	N	ILE	B	154	−85.791	17.752	−27.900	1.00	98.66	N
ATOM	8	CA	ILE	B	154	−84.757	18.804	−27.957	1.00	97.20	C
ATOM	9	CB	ILE	B	154	−84.874	19.708	−29.237	1.00	97.44	C
ATOM	10	CG1	ILE	B	154	−84.778	18.907	−30.560	1.00	97.90	C
ATOM	11	CD1	ILE	B	154	−83.348	18.623	−31.113	1.00	99.30	C
ATOM	12	CG2	ILE	B	154	−83.924	20.925	−29.210	1.00	97.05	C
ATOM	13	C	ILE	B	154	−84.794	19.659	−26.673	1.00	96.02	C
ATOM	14	O	ILE	B	154	−85.832	20.274	−26.366	1.00	96.01	O
ATOM	15	N	PRO	B	155	−83.657	19.697	−25.928	1.00	87.96	N
ATOM	16	CA	PRO	B	155	−83.593	20.523	−24.706	1.00	86.99	C
ATOM	18	CG	PRO	B	155	−81.704	19.043	−24.862	1.00	86.72	C
ATOM	19	CD	PRO	B	155	−82.363	19.027	−26.185	1.00	87.68	C
ATOM	20	C	PRO	B	155	−83.939	22.001	−24.985	1.00	85.91	C
ATOM	21	O	PRO	B	155	−83.438	22.547	−25.973	1.00	85.74	O
ATOM	22	N	TRP	B	156	−84.796	22.642	−24.145	1.00	79.85	N
ATOM	23	CA	TRP	B	156	−85.226	24.051	−24.327	1.00	79.03	C
ATOM	24	CB	TRP	B	156	−85.929	24.634	−23.078	1.00	78.53	C
ATOM	25	CG	TRP	B	156	−85.005	25.173	−22.022	1.00	77.29	C
ATOM	26	CD1	TRP	B	156	−84.573	24.522	−20.904	1.00	77.25	C
ATOM	27	NE1	TRP	B	156	−83.715	25.325	−20.186	1.00	76.73	N
ATOM	28	CE2	TRP	B	156	−83.578	26.525	−20.835	1.00	76.79	C
ATOM	29	CD2	TRP	B	156	−84.383	26.469	−21.995	1.00	77.04	C
ATOM	30	CE3	TRP	B	156	−84.414	27.588	−22.849	1.00	77.32	C
ATOM	31	CZ3	TRP	B	156	−83.643	28.695	−22.529	1.00	76.08	C
ATOM	32	CH2	TRP	B	156	−82.875	28.729	−21.359	1.00	76.36	C
ATOM	33	CZ2	TRP	B	156	−82.833	27.660	−20.494	1.00	76.64	C
ATOM	34	C	TRP	B	156	−84.141	25.004	−24.852	1.00	78.84	C
ATOM	35	O	TRP	B	156	−84.399	25.797	−25.755	1.00	78.45	O
ATOM	36	N	ASN	B	157	−82.937	24.912	−24.262	1.00	76.67	N
ATOM	37	CA	ASN	B	157	−81.762	25.708	−24.553	1.00	76.65	C
ATOM	38	CB	ASN	B	157	−80.649	25.360	−23.568	1.00	76.70	C
ATOM	39	CG	ASN	B	157	−80.500	23.895	−23.179	1.00	77.44	C
ATOM	40	OD1	ASN	B	157	−81.398	23.247	−22.587	1.00	78.09	O
ATOM	41	ND2	ASN	B	157	−79.332	23.336	−23.494	1.00	78.70	N
ATOM	42	C	ASN	B	157	−81.302	25.627	−26.021	1.00	76.86	C
ATOM	43	O	ASN	B	157	−80.858	26.632	−26.591	1.00	76.92	O
ATOM	44	N	LEU	B	158	−81.451	24.440	−26.641	1.00	78.20	N
ATOM	45	CA	LEU	B	158	−81.061	24.168	−28.028	1.00	78.40	C
ATOM	46	CB	LEU	B	158	−80.758	22.675	−28.179	1.00	78.20	C
ATOM	47	CG	LEU	B	158	−79.638	22.072	−27.335	1.00	77.54	C
ATOM	48	CD1	LEU	B	158	−79.387	20.643	−27.746	1.00	77.52	C
ATOM	49	CD2	LEU	B	158	−78.357	22.824	−27.511	1.00	77.42	C
ATOM	50	C	LEU	B	158	−82.081	24.636	−29.115	1.00	78.95	C
ATOM	51	O	LEU	B	158	−81.763	24.593	−30.320	1.00	78.73	O
ATOM	52	N	GLU	B	159	−83.291	25.099	−28.677	1.00	80.20	N
ATOM	53	CA	GLU	B	159	−84.392	25.571	−29.528	1.00	80.74	C
ATOM	54	CB	GLU	B	159	−85.654	25.870	−28.689	1.00	80.85	C
ATOM	55	CG	GLU	B	159	−86.337	24.617	−28.128	1.00	83.98	C
ATOM	56	CD	GLU	B	159	−87.623	24.729	−27.301	1.00	87.83	C
ATOM	57	OE1	GLU	B	159	−88.207	25.840	−27.214	1.00	89.05	O
ATOM	58	OE2	GLU	B	159	−88.049	23.686	−26.740	1.00	88.45	O
ATOM	59	C	GLU	B	159	−84.070	26.715	−30.528	1.00	80.76	C
ATOM	60	O	GLU	B	159	−84.777	26.852	−31.529	1.00	80.51	O
ATOM	61	N	ARG	B	160	−83.009	27.513	−30.275	1.00	79.37	N
ATOM	62	CA	ARG	B	160	−82.620	28.641	−31.131	1.00	79.76	C
ATOM	63	CB	ARG	B	160	−82.410	29.887	−30.277	1.00	79.64	C
ATOM	64	CG	ARG	B	160	−83.685	30.582	−29.832	1.00	79.80	C
ATOM	65	CD	ARG	B	160	−83.400	32.060	−29.603	1.00	80.11	C
ATOM	66	NE	ARG	B	160	−83.932	32.569	−28.335	1.00	79.71	N
ATOM	67	CZ	ARG	B	160	−85.105	33.176	−28.210	1.00	79.38	C
ATOM	68	NH1	ARG	B	160	−85.894	33.338	−29.269	1.00	80.19	N
ATOM	69	NH2	ARG	B	160	−85.506	33.617	−27.031	1.00	78.06	N
ATOM	70	C	ARG	B	160	−81.386	28.416	−32.041	1.00	80.50	C
ATOM	71	O	ARG	B	160	−80.926	29.378	−32.691	1.00	80.44	O
ATOM	72	N	ILE	B	161	−80.841	27.159	−32.081	1.00	82.33	N
ATOM	73	CA	ILE	B	161	−79.657	26.815	−32.892	1.00	83.00	C
ATOM	74	CB	ILE	B	161	−78.418	26.346	−32.057	1.00	82.95	C
ATOM	75	CG1	ILE	B	161	−78.717	25.103	−31.232	1.00	83.40	C
ATOM	76	CD1	ILE	B	161	−78.270	23.767	−31.910	1.00	85.12	C
ATOM	77	CG2	ILE	B	161	−77.847	27.458	−31.182	1.00	82.40	C
ATOM	78	C	ILE	B	161	−79.984	25.903	−34.106	1.00	83.49	C
ATOM	79	O	ILE	B	161	−80.884	25.057	−34.006	1.00	83.63	O
ATOM	80	N	THR	B	162	−79.224	26.091	−35.244	1.00	83.22	N
ATOM	81	CA	THR	B	162	−79.316	25.413	−36.559	1.00	83.35	C
ATOM	82	CB	THR	B	162	−78.521	24.057	−36.634	1.00	83.59	C
ATOM	83	OG1	THR	B	162	−77.332	24.237	−37.432	1.00	83.88	O
ATOM	84	CG2	THR	B	162	−79.360	22.854	−37.155	1.00	83.18	C
ATOM	85	C	THR	B	162	−80.735	25.516	−37.147	1.00	83.30	C
ATOM	86	O	THR	B	162	−81.293	26.622	−37.185	1.00	83.19	O
ATOM	87	N	GLY	B	176	−70.723	20.546	−35.205	1.00	140.14	N
ATOM	88	CA	GLY	B	176	−69.466	20.083	−35.782	1.00	140.14	C
ATOM	89	C	GLY	B	176	−68.282	21.003	−35.539	1.00	140.03	C
ATOM	90	O	GLY	B	176	−68.462	22.201	−35.295	1.00	140.10	O
ATOM	91	N	GLY	B	177	−67.073	20.432	−35.614	1.00	136.95	N
ATOM	92	CA	GLY	B	177	−65.807	21.142	−35.416	1.00	136.21	C
ATOM	93	C	GLY	B	177	−64.711	20.729	−36.389	1.00	135.59	C
ATOM	94	O	GLY	B	177	−64.029	19.720	−36.147	1.00	135.76	O
ATOM	95	N	SER	B	178	−64.539	21.534	−37.507	1.00	128.99	N
ATOM	96	CA	SER	B	178	−63.569	21.359	−38.622	1.00	127.64	C
ATOM	97	CB	SER	B	178	−64.250	21.579	−39.977	1.00	128.00	C
ATOM	98	OG	SER	B	178	−64.514	22.945	−40.265	1.00	128.21	O
ATOM	99	C	SER	B	178	−62.324	22.258	−38.493	1.00	126.31	C
ATOM	100	O	SER	B	178	−62.346	23.420	−38.931	1.00	126.19	O
ATOM	101	N	LEU	B	179	−61.235	21.706	−37.884	1.00	118.00	N
ATOM	102	CA	LEU	B	179	−59.969	22.406	−37.598	1.00	115.97	C
ATOM	103	CB	LEU	B	179	−59.268	22.923	−38.892	1.00	116.34	C
ATOM	104	CG	LEU	B	179	−57.735	22.921	−38.922	1.00	116.65	C
ATOM	105	CD1	LEU	B	179	−57.196	21.592	−39.416	1.00	116.41	C
ATOM	106	CD2	LEU	B	179	−57.216	24.022	−39.817	1.00	116.41	C
ATOM	107	C	LEU	B	179	−60.259	23.551	−36.573	1.00	114.12	C
ATOM	108	O	LEU	B	179	−59.376	24.361	−36.285	1.00	114.17	O
ATOM	109	N	VAL	B	180	−61.512	23.591	−36.026	1.00	105.44	N
ATOM	110	CA	VAL	B	180	−61.996	24.548	−35.027	1.00	102.74	C
ATOM	111	CB	VAL	B	180	−63.488	24.952	−35.144	1.00	102.92	C
ATOM	112	CG1	VAL	B	180	−63.808	26.126	−34.229	1.00	102.10	C
ATOM	113	CG2	VAL	B	180	−63.860	25.286	−36.568	1.00	103.04	C
ATOM	114	C	VAL	B	180	−61.737	23.899	−33.705	1.00	100.85	C
ATOM	115	O	VAL	B	180	−62.422	22.940	−33.302	1.00	100.51	O
ATOM	116	N	GLU	B	181	−60.725	24.429	−33.040	1.00	95.52	N
ATOM	117	CA	GLU	B	181	−60.286	23.968	−31.750	1.00	93.31	C
ATOM	118	CB	GLU	B	181	−58.754	23.963	−31.695	1.00	93.78	C
ATOM	119	CG	GLU	B	181	−58.163	22.856	−30.839	1.00	95.42	C
ATOM	120	CD	GLU	B	181	−58.611	21.438	−31.161	1.00	97.54	C
ATOM	121	OE1	GLU	B	181	−59.571	20.963	−30.510	1.00	98.37	O
ATOM	122	OE2	GLU	B	181	−58.003	20.801	−32.054	1.00	98.34	O
ATOM	123	C	GLU	B	181	−60.882	24.838	−30.661	1.00	91.24	C
ATOM	124	O	GLU	B	181	−60.742	26.058	−30.691	1.00	90.90	O
ATOM	125	N	VAL	B	182	−61.574	24.198	−29.720	1.00	83.34	N
ATOM	126	CA	VAL	B	182	−62.203	24.834	−28.581	1.00	80.42	C
ATOM	127	CB	VAL	B	182	−63.678	24.408	−28.435	1.00	80.28	C
ATOM	128	CG1	VAL	B	182	−64.275	24.918	−27.133	1.00	79.85	C
ATOM	129	CG2	VAL	B	182	−64.503	24.882	−29.616	1.00	79.66	C
ATOM	130	C	VAL	B	182	−61.385	24.448	−27.363	1.00	78.88	C
ATOM	131	O	VAL	B	182	−61.327	23.273	−27.006	1.00	78.56	O
ATOM	132	N	TYR	B	183	−60.732	25.424	−26.744	1.00	75.90	N
ATOM	133	CA	TYR	B	183	−59.945	25.203	−25.541	1.00	74.25	C
ATOM	134	CB	TYR	B	183	−58.703	26.075	−25.548	1.00	74.20	C
ATOM	135	CG	TYR	B	183	−57.561	25.512	−26.366	1.00	75.11	C
ATOM	136	CD1	TYR	B	183	−56.510	24.831	−25.756	1.00	75.82	C
ATOM	137	CE1	TYR	B	183	−55.436	24.342	−26.501	1.00	76.26	C
ATOM	138	CZ	TYR	B	183	−55.406	24.533	−27.875	1.00	76.26	C
ATOM	139	OH	TYR	B	183	−54.348	24.061	−28.624	1.00	77.47	O
ATOM	140	CE2	TYR	B	183	−56.453	25.187	−28.502	1.00	75.43	C
ATOM	141	CD2	TYR	B	183	−57.512	25.685	−27.746	1.00	75.11	C
ATOM	142	C	TYR	B	183	−60.805	25.516	−24.330	1.00	72.94	C
ATOM	143	O	TYR	B	183	−61.482	26.538	−24.300	1.00	73.00	O
ATOM	144	N	LEU	B	184	−60.802	24.650	−23.341	1.00	68.66	N
ATOM	145	CA	LEU	B	184	−61.598	24.882	−22.156	1.00	67.26	C
ATOM	146	CB	LEU	B	184	−62.680	23.801	−22.077	1.00	67.15	C
ATOM	147	CG	LEU	B	184	−63.354	23.530	−20.744	1.00	67.01	C
ATOM	148	CD1	LEU	B	184	−64.242	24.673	−20.322	1.00	67.88	C
ATOM	149	CD2	LEU	B	184	−64.171	22.290	−20.831	1.00	66.74	C
ATOM	150	C	LEU	B	184	−60.725	24.918	−20.906	1.00	66.66	C
ATOM	151	O	LEU	B	184	−60.114	23.913	−20.563	1.00	66.73	O
ATOM	152	N	LEU	B	185	−60.651	26.071	−20.240	1.00	65.50	N
ATOM	153	CA	LEU	B	185	−59.894	26.218	−19.007	1.00	65.04	C
ATOM	154	CB	LEU	B	185	−59.206	27.584	−18.911	1.00	64.85	C
ATOM	155	CG	LEU	B	185	−57.923	27.771	−19.677	1.00	63.72	C
ATOM	156	CD1	LEU	B	185	−58.192	28.459	−20.951	1.00	62.36	C
ATOM	157	CD2	LEU	B	185	−56.975	28.647	−18.914	1.00	62.83	C
ATOM	158	C	LEU	B	185	−60.943	26.118	−17.933	1.00	65.33	C
ATOM	159	O	LEU	B	185	−61.788	27.002	−17.826	1.00	65.52	O
ATOM	160	N	ASP	B	186	−60.923	25.033	−17.162	1.00	69.66	N
ATOM	161	CA	ASP	B	186	−61.877	24.787	−16.096	1.00	69.85	C
ATOM	162	CB	ASP	B	186	−63.224	24.309	−16.694	1.00	70.50	C
ATOM	163	CG	ASP	B	186	−64.456	24.744	−15.888	1.00	73.29	C
ATOM	164	OD1	ASP	B	186	−65.209	23.853	−15.411	1.00	74.50	O
ATOM	165	OD2	ASP	B	186	−64.666	25.982	−15.722	1.00	77.37	O
ATOM	166	C	ASP	B	186	−61.306	23.784	−15.098	1.00	69.28	C
ATOM	167	O	ASP	B	186	−60.110	23.791	−14.810	1.00	68.99	O
ATOM	168	N	THR	B	187	−62.175	22.937	−14.559	1.00	69.19	N
ATOM	169	CA	THR	B	187	−61.860	21.885	−13.606	1.00	68.93	C
ATOM	170	CB	THR	B	187	−63.157	21.450	−12.844	1.00	68.58	C
ATOM	171	OG1	THR	B	187	−64.084	20.833	−13.739	1.00	67.31	O
ATOM	172	CG2	THR	B	187	−63.827	22.585	−12.090	1.00	68.14	C
ATOM	173	C	THR	B	187	−61.353	20.698	−14.426	1.00	69.35	C
ATOM	174	O	THR	B	187	−61.200	20.799	−15.658	1.00	69.24	O
ATOM	175	N	SER	B	188	−61.133	19.564	−13.747	1.00	72.98	N
ATOM	176	CA	SER	B	188	−60.778	18.312	−14.397	1.00	73.83	C
ATOM	177	CB	SER	B	188	−60.395	17.274	−13.348	1.00	73.82	C
ATOM	178	OG	SER	B	188	−61.266	17.343	−12.228	1.00	75.61	O
ATOM	179	C	SER	B	188	−62.075	17.877	−15.146	1.00	73.93	C
ATOM	180	O	SER	B	188	−63.155	18.377	−14.828	1.00	74.16	O
ATOM	181	N	ILE	B	189	−61.974	17.023	−16.166	1.00	75.20	N
ATOM	182	CA	ILE	B	189	−63.160	16.595	−16.918	1.00	75.33	C
ATOM	183	CB	ILE	B	189	−63.315	17.325	−18.303	1.00	75.17	C
ATOM	184	CG1	ILE	B	189	−62.291	16.857	−19.328	1.00	74.91	C
ATOM	185	CD1	ILE	B	189	−62.849	16.079	−20.326	1.00	74.99	C
ATOM	186	CG2	ILE	B	189	−63.244	18.842	−18.208	1.00	74.89	C
ATOM	187	C	ILE	B	189	−63.173	15.060	−17.055	1.00	75.92	C
ATOM	188	O	ILE	B	189	−62.105	14.431	−17.112	1.00	76.37	O
ATOM	189	N	GLN	B	190	−64.377	14.464	−17.115	1.00	78.71	N
ATOM	190	CA	GLN	B	190	−64.573	13.031	−17.324	1.00	78.81	C
ATOM	191	CB	GLN	B	190	−65.935	12.599	−16.719	1.00	79.20	C
ATOM	192	CG	GLN	B	190	−66.291	11.106	−16.838	1.00	80.98	C
ATOM	193	CD	GLN	B	190	−65.218	10.268	−16.184	1.00	84.40	C
ATOM	194	OE1	GLN	B	190	−64.398	9.600	−16.863	1.00	85.93	O
ATOM	195	NE2	GLN	B	190	−65.178	10.319	−14.838	1.00	84.61	N
ATOM	196	C	GLN	B	190	−64.528	12.852	−18.868	1.00	78.44	C
ATOM	197	O	GLN	B	190	−65.557	12.986	−19.530	1.00	78.67	O
ATOM	198	N	SER	B	191	−63.335	12.619	−19.437	1.00	76.26	N
ATOM	199	CA	SER	B	191	−63.125	12.472	−20.886	1.00	76.40	C
ATOM	200	CB	SER	B	191	−61.641	12.584	−21.242	1.00	76.30	C
ATOM	201	OG	SER	B	191	−60.774	11.931	−20.321	1.00	76.89	O
ATOM	202	C	SER	B	191	−63.742	11.221	−21.507	1.00	76.56	C
ATOM	203	O	SER	B	191	−63.870	11.147	−22.735	1.00	76.51	O
ATOM	204	N	ASP	B	192	−64.123	10.249	−20.657	1.00	76.51	N
ATOM	205	CA	ASP	B	192	−64.731	8.972	−21.021	1.00	77.11	C
ATOM	206	CB	ASP	B	192	−64.437	7.919	−19.946	1.00	77.96	C
ATOM	207	CG	ASP	B	192	−62.956	7.651	−19.710	1.00	81.51	C
ATOM	208	OD1	ASP	B	192	−62.098	8.236	−20.470	1.00	85.26	O
ATOM	209	OD2	ASP	B	192	−62.633	6.861	−18.764	1.00	84.42	O
ATOM	210	C	ASP	B	192	−66.228	9.066	−21.249	1.00	76.46	C
ATOM	211	O	ASP	B	192	−66.799	8.171	−21.881	1.00	76.47	O
ATOM	212	N	HIS	B	193	−66.868	10.135	−20.742	1.00	71.48	N
ATOM	213	CA	HIS	B	193	−68.302	10.347	−20.896	1.00	70.66	C
ATOM	214	CB	HIS	B	193	−68.760	11.679	−20.308	1.00	69.92	C
ATOM	215	CG	HIS	B	193	−70.227	11.703	−20.063	1.00	67.58	C
ATOM	216	ND1	HIS	B	193	−70.738	11.592	−18.798	1.00	65.49	N
ATOM	217	CE1	HIS	B	193	−72.055	11.611	−18.938	1.00	65.26	C
ATOM	218	NE2	HIS	B	193	−72.408	11.730	−20.211	1.00	65.88	N
ATOM	219	CD2	HIS	B	193	−71.250	11.777	−20.942	1.00	66.29	C
ATOM	220	C	HIS	B	193	−68.702	10.216	−22.354	1.00	71.00	C
ATOM	221	O	HIS	B	193	−68.100	10.843	−23.217	1.00	70.97	O
ATOM	222	N	ARG	B	194	−69.698	9.364	−22.618	1.00	72.56	N
ATOM	223	CA	ARG	B	194	−70.195	9.035	−23.949	1.00	72.97	C
ATOM	224	CB	ARG	B	194	−71.371	8.065	−23.872	1.00	73.07	C
ATOM	225	CG	ARG	B	194	−71.020	6.680	−23.334	1.00	71.88	C
ATOM	226	CD	ARG	B	194	−70.534	5.692	−24.386	1.00	70.41	C
ATOM	227	NE	ARG	B	194	−71.239	5.796	−25.672	1.00	69.15	N
ATOM	228	CZ	ARG	B	194	−72.366	5.156	−25.988	1.00	67.53	C
ATOM	229	NH1	ARG	B	194	−72.916	5.324	−27.182	1.00	66.06	N
ATOM	230	NH2	ARG	B	194	−72.952	4.350	−25.110	1.00	66.67	N
ATOM	231	C	ARG	B	194	−70.530	10.244	−24.783	1.00	73.51	C
ATOM	232	O	ARG	B	194	−70.356	10.201	−25.999	1.00	73.71	O
ATOM	233	N	GLU	B	195	−70.984	11.321	−24.140	1.00	74.05	N
ATOM	234	CA	GLU	B	195	−71.321	12.577	−24.796	1.00	74.65	C
ATOM	235	CB	GLU	B	195	−71.857	13.566	−23.770	1.00	74.69	C
ATOM	236	CG	GLU	B	195	−73.312	13.345	−23.447	1.00	75.96	C
ATOM	237	CD	GLU	B	195	−74.199	14.009	−24.471	1.00	78.05	C
ATOM	238	OE1	GLU	B	195	−74.682	13.293	−25.377	1.00	78.92	O
ATOM	239	OE2	GLU	B	195	−74.397	15.244	−24.381	1.00	79.60	O
ATOM	240	C	GLU	B	195	−70.102	13.201	−25.436	1.00	74.65	C
ATOM	241	O	GLU	B	195	−70.190	13.725	−26.548	1.00	74.72	O
ATOM	242	N	ILE	B	196	−68.967	13.149	−24.730	1.00	73.62	N
ATOM	243	CA	ILE	B	196	−67.730	13.773	−25.156	1.00	73.67	C
ATOM	244	CB	ILE	B	196	−67.386	14.919	−24.181	1.00	73.39	C
ATOM	245	CG1	ILE	B	196	−67.087	14.413	−22.746	1.00	72.89	C
ATOM	246	CD1	ILE	B	196	−66.340	15.398	−21.869	1.00	71.68	C
ATOM	247	CG2	ILE	B	196	−68.451	16.011	−24.223	1.00	73.36	C
ATOM	248	C	ILE	B	196	−66.528	12.877	−25.455	1.00	74.30	C
ATOM	249	O	ILE	B	196	−65.459	13.403	−25.759	1.00	74.46	O
ATOM	250	N	GLU	B	197	−66.671	11.556	−25.367	1.00	77.64	N
ATOM	251	CA	GLU	B	197	−65.571	10.634	−25.623	1.00	78.11	C
ATOM	252	CB	GLU	B	197	−66.039	9.218	−25.284	1.00	78.29	C
ATOM	253	CG	GLU	B	197	−65.094	8.094	−25.675	1.00	80.67	C
ATOM	254	CD	GLU	B	197	−65.213	7.595	−27.109	1.00	84.14	C
ATOM	255	OE1	GLU	B	197	−64.154	7.241	−27.691	1.00	85.48	O
ATOM	256	OE2	GLU	B	197	−66.352	7.566	−27.652	1.00	84.38	O
ATOM	257	C	GLU	B	197	−65.078	10.775	−27.088	1.00	78.33	C
ATOM	258	O	GLU	B	197	−65.889	10.888	−28.006	1.00	77.70	O
ATOM	259	N	GLY	B	198	−63.760	10.805	−27.279	1.00	79.97	N
ATOM	260	CA	GLY	B	198	−63.155	10.931	−28.601	1.00	80.78	C
ATOM	261	C	GLY	B	198	−63.125	12.335	−29.184	1.00	81.70	C
ATOM	262	O	GLY	B	198	−62.354	12.594	−30.119	1.00	81.82	O
ATOM	263	N	ARG	B	199	−63.974	13.254	−28.657	1.00	82.07	N
ATOM	264	CA	ARG	B	199	−64.025	14.643	−29.107	1.00	82.71	C
ATOM	265	CB	ARG	B	199	−65.478	15.135	−29.363	1.00	83.22	C
ATOM	266	CG	ARG	B	199	−66.383	14.288	−30.315	1.00	85.09	C
ATOM	267	CD	ARG	B	199	−65.757	13.859	−31.646	1.00	88.67	C
ATOM	268	NE	ARG	B	199	−65.336	15.001	−32.478	1.00	93.40	N
ATOM	269	CZ	ARG	B	199	−64.332	14.985	−33.365	1.00	95.58	C
ATOM	270	NH1	ARG	B	199	−63.613	13.880	−33.552	1.00	96.91	N
ATOM	271	NH2	ARG	B	199	−64.033	16.080	−34.059	1.00	96.23	N
ATOM	272	C	ARG	B	199	−63.255	15.546	−28.128	1.00	82.57	C
ATOM	273	O	ARG	B	199	−62.553	16.450	−28.562	1.00	82.54	O
ATOM	274	N	VAL	B	200	−63.346	15.278	−26.823	1.00	81.88	N
ATOM	275	CA	VAL	B	200	−62.645	16.074	−25.811	1.00	82.39	C
ATOM	276	CB	VAL	B	200	−63.532	16.470	−24.599	1.00	82.30	C
ATOM	277	CG1	VAL	B	200	−62.754	17.342	−23.624	1.00	82.32	C
ATOM	278	CG2	VAL	B	200	−64.785	17.208	−25.063	1.00	82.80	C
ATOM	279	C	VAL	B	200	−61.318	15.438	−25.401	1.00	82.80	C
ATOM	280	O	VAL	B	200	−61.308	14.351	−24.833	1.00	83.26	O
ATOM	281	N	MET	B	201	−60.210	16.138	−25.687	1.00	81.97	N
ATOM	282	CA	MET	B	201	−58.824	15.754	−25.428	1.00	82.08	C
ATOM	283	CB	MET	B	201	−57.973	16.215	−26.633	1.00	82.67	C
ATOM	284	CG	MET	B	201	−56.563	15.650	−26.664	1.00	86.68	C
ATOM	285	SD	MET	B	201	−55.285	16.848	−26.166	1.00	94.50	S
ATOM	286	CE	MET	B	201	−53.765	15.772	−26.202	1.00	93.41	C
ATOM	287	C	MET	B	201	−58.299	16.402	−24.139	1.00	81.18	C
ATOM	288	O	MET	B	201	−58.375	17.613	−24.004	1.00	81.66	O
ATOM	289	N	VAL	B	202	−57.742	15.619	−23.207	1.00	76.40	N
ATOM	290	CA	VAL	B	202	−57.201	16.193	−21.968	1.00	75.21	C
ATOM	291	CB	VAL	B	202	−57.488	15.305	−20.727	1.00	74.80	C
ATOM	292	CG1	VAL	B	202	−56.634	15.704	−19.538	1.00	74.05	C
ATOM	293	CG2	VAL	B	202	−58.961	15.338	−20.355	1.00	74.22	C
ATOM	294	C	VAL	B	202	−55.714	16.527	−22.138	1.00	74.85	C
ATOM	295	O	VAL	B	202	−54.922	15.636	−22.431	1.00	74.77	O
ATOM	296	N	THR	B	203	−55.341	17.804	−21.957	1.00	76.16	N
ATOM	297	CA	THR	B	203	−53.939	18.230	−22.074	1.00	75.76	C
ATOM	298	CB	THR	B	203	−53.791	19.707	−22.484	1.00	75.68	C
ATOM	299	OG1	THR	B	203	−54.117	20.556	−21.381	1.00	75.47	O
ATOM	300	CG2	THR	B	203	−54.603	20.071	−23.730	1.00	75.36	C
ATOM	301	C	THR	B	203	−53.191	17.904	−20.784	1.00	75.63	C
ATOM	302	O	THR	B	203	−53.823	17.586	−19.767	1.00	75.46	O
ATOM	303	N	ASP	B	204	−51.847	17.984	−20.823	1.00	77.72	N
ATOM	304	CA	ASP	B	204	−51.004	17.699	−19.657	1.00	77.96	C
ATOM	305	CB	ASP	B	204	−49.553	17.422	−20.106	1.00	77.97	C
ATOM	306	C	ASP	B	204	−51.035	18.862	−18.648	1.00	78.07	C
ATOM	307	O	ASP	B	204	−50.476	18.734	−17.551	1.00	78.14	O
ATOM	308	N	PHE	B	205	−51.681	20.000	−19.026	1.00	77.35	N
ATOM	309	CA	PHE	B	205	−51.773	21.198	−18.201	1.00	77.05	C
ATOM	310	CB	PHE	B	205	−52.185	22.435	−19.014	1.00	76.92	C
ATOM	311	CG	PHE	B	205	−52.052	23.686	−18.184	1.00	76.42	C
ATOM	312	CD1	PHE	B	205	−50.846	24.370	−18.120	1.00	76.04	C
ATOM	313	CE1	PHE	B	205	−50.711	25.509	−17.322	1.00	76.41	C
ATOM	314	CZ	PHE	B	205	−51.770	25.942	−16.555	1.00	76.80	C
ATOM	315	CE2	PHE	B	205	−52.975	25.265	−16.595	1.00	76.24	C
ATOM	316	CD2	PHE	B	205	−53.117	24.147	−17.414	1.00	76.25	C
ATOM	317	C	PHE	B	205	−52.658	21.061	−16.999	1.00	77.20	C
ATOM	318	O	PHE	B	205	−53.790	20.576	−17.103	1.00	77.05	O
ATOM	319	N	GLU	B	206	−52.138	21.560	−15.861	1.00	78.14	N
ATOM	320	CA	GLU	B	206	−52.770	21.615	−14.550	1.00	78.71	C
ATOM	321	CB	GLU	B	206	−52.774	20.246	−13.895	1.00	78.73	C
ATOM	322	CG	GLU	B	206	−53.559	20.204	−12.606	1.00	80.94	C
ATOM	323	CD	GLU	B	206	−53.553	18.848	−11.930	1.00	83.15	C
ATOM	324	OE1	GLU	B	206	−54.647	18.256	−11.754	1.00	83.16	O
ATOM	325	OE2	GLU	B	206	−52.446	18.379	−11.573	1.00	85.09	O
ATOM	326	C	GLU	B	206	−52.023	22.608	−13.673	1.00	78.91	C
ATOM	327	O	GLU	B	206	−50.796	22.571	−13.591	1.00	78.97	O
ATOM	328	N	ASN	B	207	−52.771	23.509	−13.038	1.00	79.45	N
ATOM	329	CA	ASN	B	207	−52.290	24.546	−12.123	1.00	79.62	C
ATOM	330	CB	ASN	B	207	−51.621	25.721	−12.860	1.00	79.53	C
ATOM	331	CG	ASN	B	207	−50.999	26.739	−11.913	1.00	79.76	C
ATOM	332	OD1	ASN	B	207	−51.654	27.303	−11.010	1.00	81.14	O
ATOM	333	ND2	ASN	B	207	−49.712	27.006	−12.090	1.00	79.96	N
ATOM	334	C	ASN	B	207	−53.491	25.008	−11.308	1.00	79.67	C
ATOM	335	O	ASN	B	207	−54.229	25.903	−11.720	1.00	79.86	O
ATOM	336	N	VAL	B	208	−53.708	24.368	−10.169	1.00	77.92	N
ATOM	337	CA	VAL	B	208	−54.844	24.685	−9.309	1.00	78.49	C
ATOM	338	CB	VAL	B	208	−55.932	23.555	−9.333	1.00	78.44	C
ATOM	339	CG1	VAL	B	208	−56.307	23.167	−10.757	1.00	78.06	C
ATOM	340	CG2	VAL	B	208	−55.512	22.320	−8.537	1.00	78.22	C
ATOM	341	C	VAL	B	208	−54.378	25.014	−7.893	1.00	79.11	C
ATOM	342	O	VAL	B	208	−53.314	24.559	−7.507	1.00	79.41	O
ATOM	343	N	PRO	B	209	−55.135	25.755	−7.070	1.00	81.83	N
ATOM	344	CA	PRO	B	209	−54.683	25.979	−5.690	1.00	82.62	C
ATOM	345	CB	PRO	B	209	−55.588	27.115	−5.195	1.00	82.43	C
ATOM	346	CG	PRO	B	209	−56.400	27.543	−6.378	1.00	82.07	C
ATOM	347	CD	PRO	B	209	−56.440	26.399	−7.306	1.00	81.97	C
ATOM	348	C	PRO	B	209	−54.901	24.721	−4.848	1.00	83.65	C
ATOM	349	O	PRO	B	209	−55.779	23.915	−5.171	1.00	83.64	O
ATOM	350	N	GLU	B	210	−54.111	24.546	−3.768	1.00	88.20	N
ATOM	351	CA	GLU	B	210	−54.277	23.383	−2.889	1.00	89.74	C
ATOM	352	CB	GLU	B	210	−53.256	23.381	−1.729	1.00	89.55	C
ATOM	353	C	GLU	B	210	−55.719	23.435	−2.380	1.00	90.57	C
ATOM	354	O	GLU	B	210	−56.228	24.532	−2.087	1.00	90.41	O
ATOM	355	N	GLU	B	211	−56.397	22.265	−2.362	1.00	94.51	N
ATOM	356	CA	GLU	B	211	−57.792	22.170	−1.924	1.00	95.89	C
ATOM	357	CB	GLU	B	211	−58.384	20.760	−2.085	1.00	95.83	C
ATOM	358	CG	GLU	B	211	−59.166	20.582	−3.374	1.00	96.71	C
ATOM	359	CD	GLU	B	211	−58.341	20.326	−4.626	1.00	98.31	C
ATOM	360	OE1	GLU	B	211	−57.101	20.520	−4.597	1.00	99.53	O
ATOM	361	OE2	GLU	B	211	−58.943	19.930	−5.651	1.00	98.49	O
ATOM	362	C	GLU	B	211	−57.994	22.716	−0.527	1.00	96.75	C
ATOM	363	O	GLU	B	211	−57.235	22.401	0.402	1.00	96.76	O
ATOM	364	N	ASP	B	212	−59.002	23.594	−0.403	1.00	100.07	N
ATOM	365	CA	ASP	B	212	−59.353	24.245	0.855	1.00	100.92	C
ATOM	366	CB	ASP	B	212	−59.966	25.636	0.574	1.00	100.87	C
ATOM	367	C	ASP	B	212	−60.273	23.321	1.699	1.00	101.36	C
ATOM	368	O	ASP	B	212	−59.990	22.121	1.877	1.00	101.83	O
ATOM	369	N	ALA	B	220	−64.416	12.642	−5.714	1.00	107.90	N
ATOM	370	CA	ALA	B	220	−63.510	12.432	−6.856	1.00	108.17	C
ATOM	371	CB	ALA	B	220	−62.875	11.044	−6.803	1.00	108.18	C
ATOM	372	C	ALA	B	220	−64.175	12.680	−8.228	1.00	107.99	C
ATOM	373	O	ALA	B	220	−63.526	13.212	−9.133	1.00	108.10	O
ATOM	374	N	SER	B	221	−65.463	12.279	−8.380	1.00	105.36	N
ATOM	375	CA	SER	B	221	−66.286	12.492	−9.588	1.00	104.82	C
ATOM	376	CB	SER	B	221	−66.943	11.200	−10.083	1.00	104.98	C
ATOM	377	OG	SER	B	221	−66.303	10.735	−11.264	1.00	106.07	O
ATOM	378	C	SER	B	221	−67.299	13.640	−9.308	1.00	103.94	C
ATOM	379	O	SER	B	221	−68.445	13.644	−9.772	1.00	104.03	O
ATOM	380	N	LYS	B	222	−66.813	14.603	−8.502	1.00	97.73	N
ATOM	381	CA	LYS	B	222	−67.413	15.840	−8.056	1.00	96.15	C
ATOM	382	CB	LYS	B	222	−67.589	15.848	−6.533	1.00	96.42	C
ATOM	383	CG	LYS	B	222	−68.380	17.045	−5.993	1.00	97.85	C
ATOM	384	CD	LYS	B	222	−69.836	17.113	−6.522	1.00	100.51	C
ATOM	385	CE	LYS	B	222	−70.544	18.401	−6.165	1.00	101.09	C
ATOM	386	NZ	LYS	B	222	−71.729	18.637	−7.034	1.00	101.72	N
ATOM	387	C	LYS	B	222	−66.420	16.908	−8.498	1.00	94.80	C
ATOM	388	O	LYS	B	222	−66.796	18.070	−8.600	1.00	94.92	O
ATOM	389	N	CYS	B	223	−65.149	16.516	−8.779	1.00	89.06	N
ATOM	390	CA	CYS	B	223	−64.125	17.431	−9.279	1.00	87.39	C
ATOM	391	CB	CYS	B	223	−62.733	16.818	−9.218	1.00	87.43	C
ATOM	392	SG	CYS	B	223	−62.208	16.366	−7.551	1.00	90.01	S
ATOM	393	C	CYS	B	223	−64.506	17.717	−10.681	1.00	85.86	C
ATOM	394	O	CYS	B	223	−64.776	18.872	−11.006	1.00	86.32	O
ATOM	395	N	ASP	B	224	−64.594	16.660	−11.508	1.00	80.28	N
ATOM	396	CA	ASP	B	224	−64.974	16.782	−12.908	1.00	78.53	C
ATOM	397	CB	ASP	B	224	−64.517	15.581	−13.764	1.00	79.51	C
ATOM	398	CG	ASP	B	224	−64.381	14.211	−13.116	1.00	81.45	C
ATOM	399	OD1	ASP	B	224	−65.095	13.951	−12.105	1.00	83.11	O
ATOM	400	OD2	ASP	B	224	−63.569	13.382	−13.636	1.00	83.60	O
ATOM	401	C	ASP	B	224	−66.417	17.221	−13.200	1.00	76.34	C
ATOM	402	O	ASP	B	224	−66.799	17.373	−14.348	1.00	75.54	O
ATOM	403	N	SER	B	225	−67.176	17.481	−12.146	1.00	72.60	N
ATOM	404	CA	SER	B	225	−68.564	17.906	−12.142	1.00	70.75	C
ATOM	405	CB	SER	B	225	−68.948	18.338	−10.732	1.00	70.68	C
ATOM	406	OG	SER	B	225	−70.346	18.509	−10.593	1.00	71.29	O
ATOM	407	C	SER	B	225	−68.881	19.022	−13.134	1.00	69.45	C
ATOM	408	O	SER	B	225	−69.705	18.849	−14.037	1.00	69.51	O
ATOM	409	N	HIS	B	226	−68.213	20.152	−12.959	1.00	67.18	N
ATOM	410	CA	HIS	B	226	−68.384	21.368	−13.731	1.00	65.54	C
ATOM	411	CB	HIS	B	226	−67.775	22.527	−12.943	1.00	66.03	C
ATOM	412	CG	HIS	B	226	−68.050	23.885	−13.494	1.00	67.26	C
ATOM	413	ND1	HIS	B	226	−67.015	24.731	−13.866	1.00	68.03	N
ATOM	414	CE1	HIS	B	226	−67.596	25.843	−14.284	1.00	69.18	C
ATOM	415	NE2	HIS	B	226	−68.929	25.764	−14.196	1.00	68.94	N
ATOM	416	CD2	HIS	B	226	−69.229	24.521	−13.682	1.00	68.58	C
ATOM	417	C	HIS	B	226	−67.837	21.304	−15.152	1.00	64.16	C
ATOM	418	O	HIS	B	226	−68.570	21.600	−16.087	1.00	64.08	O
ATOM	419	N	GLY	B	227	−66.569	20.938	−15.308	1.00	59.89	N
ATOM	420	CA	GLY	B	227	−65.918	20.862	−16.606	1.00	57.91	C
ATOM	421	C	GLY	B	227	−66.559	19.870	−17.542	1.00	57.07	C
ATOM	422	O	GLY	B	227	−66.580	20.101	−18.749	1.00	56.80	O
ATOM	423	N	THR	B	228	−67.066	18.749	−16.997	1.00	56.49	N
ATOM	424	CA	THR	B	228	−67.718	17.703	−17.779	1.00	55.25	C
ATOM	425	CB	THR	B	228	−67.908	16.416	−16.945	1.00	55.36	C
ATOM	426	OG1	THR	B	228	−66.617	15.986	−16.499	1.00	55.00	O
ATOM	427	CG2	THR	B	228	−68.598	15.284	−17.718	1.00	54.69	C
ATOM	428	C	THR	B	228	−68.980	18.294	−18.344	1.00	54.71	C
ATOM	429	O	THR	B	228	−69.159	18.226	−19.558	1.00	54.21	O
ATOM	430	N	HIS	B	229	−69.822	18.921	−17.478	1.00	54.98	N
ATOM	431	CA	HIS	B	229	−71.068	19.581	−17.869	1.00	54.94	C
ATOM	432	CB	HIS	B	229	−71.761	20.249	−16.676	1.00	54.87	C
ATOM	433	CG	HIS	B	229	−73.182	20.612	−16.969	1.00	56.60	C
ATOM	434	ND1	HIS	B	229	−73.533	21.889	−17.344	1.00	58.44	N
ATOM	435	CE1	HIS	B	229	−74.838	21.861	−17.560	1.00	58.78	C
ATOM	436	NE2	HIS	B	229	−75.347	20.652	−17.328	1.00	59.04	N
ATOM	437	CD2	HIS	B	229	−74.295	19.839	−16.964	1.00	58.70	C
ATOM	438	C	HIS	B	229	−70.830	20.596	−18.986	1.00	54.67	C
ATOM	439	O	HIS	B	229	−71.518	20.524	−20.001	1.00	54.62	O
ATOM	440	N	LEU	B	230	−69.850	21.508	−18.831	1.00	54.53	N
ATOM	441	CA	LEU	B	230	−69.571	22.503	−19.852	1.00	54.58	C
ATOM	442	CB	LEU	B	230	−68.631	23.570	−19.340	1.00	54.42	C
ATOM	443	CG	LEU	B	230	−69.134	24.331	−18.137	1.00	54.76	C
ATOM	444	CD1	LEU	B	230	−68.075	25.189	−17.588	1.00	53.99	C
ATOM	445	CD2	LEU	B	230	−70.327	25.160	−18.468	1.00	54.36	C
ATOM	446	C	LEU	B	230	−69.079	21.900	−21.169	1.00	55.03	C
ATOM	447	O	LEU	B	230	−69.569	22.309	−22.234	1.00	55.41	O
ATOM	448	N	ALA	B	231	−68.146	20.920	−21.120	1.00	56.16	N
ATOM	449	CA	ALA	B	231	−67.674	20.261	−22.329	1.00	56.30	C
ATOM	450	CB	ALA	B	231	−66.598	19.260	−21.978	1.00	56.06	C
ATOM	451	C	ALA	B	231	−68.909	19.545	−22.980	1.00	56.96	C
ATOM	452	O	ALA	B	231	−69.020	19.449	−24.220	1.00	56.80	O
ATOM	453	N	GLY	B	232	−69.836	19.095	−22.121	1.00	59.26	N
ATOM	454	CA	GLY	B	232	−71.076	18.461	−22.529	1.00	59.55	C
ATOM	455	C	GLY	B	232	−71.926	19.502	−23.210	1.00	60.10	C
ATOM	456	O	GLY	B	232	−72.435	19.243	−24.292	1.00	60.36	O
ATOM	457	N	VAL	B	233	−72.041	20.710	−22.618	1.00	61.09	N
ATOM	458	CA	VAL	B	233	−72.819	21.810	−23.203	1.00	61.50	C
ATOM	459	CB	VAL	B	233	−72.984	23.009	−22.244	1.00	61.31	C
ATOM	460	CG1	VAL	B	233	−73.636	24.194	−22.945	1.00	60.60	C
ATOM	461	CG2	VAL	B	233	−73.789	22.612	−21.018	1.00	61.89	C
ATOM	462	C	VAL	B	233	−72.251	22.248	−24.573	1.00	61.96	C
ATOM	463	O	VAL	B	233	−73.034	22.489	−25.497	1.00	62.26	O
ATOM	464	N	VAL	B	234	−70.922	22.337	−24.714	1.00	60.75	N
ATOM	465	CA	VAL	B	234	−70.352	22.756	−25.989	1.00	61.40	C
ATOM	466	CB	VAL	B	234	−68.872	23.198	−25.877	1.00	61.51	C
ATOM	467	CG1	VAL	B	234	−68.288	23.565	−27.247	1.00	59.64	C
ATOM	468	CG2	VAL	B	234	−68.713	24.336	−24.879	1.00	61.44	C
ATOM	469	C	VAL	B	234	−70.522	21.730	−27.102	1.00	62.31	C
ATOM	470	O	VAL	B	234	−71.164	22.032	−28.107	1.00	62.51	O
ATOM	471	N	SER	B	235	−69.936	20.528	−26.924	1.00	65.08	N
ATOM	472	CA	SER	B	235	−69.889	19.474	−27.934	1.00	65.81	C
ATOM	473	CB	SER	B	235	−68.441	19.226	−28.329	1.00	65.94	C
ATOM	474	OG	SER	B	235	−67.686	18.789	−27.205	1.00	67.86	O
ATOM	475	C	SER	B	235	−70.558	18.146	−27.670	1.00	66.01	C
ATOM	476	O	SER	B	235	−70.314	17.225	−28.436	1.00	65.96	O
ATOM	477	N	GLY	B	236	−71.380	18.036	−26.636	1.00	66.49	N
ATOM	478	CA	GLY	B	236	−72.083	16.792	−26.322	1.00	67.15	C
ATOM	479	C	GLY	B	236	−72.830	16.189	−27.497	1.00	67.77	C
ATOM	480	O	GLY	B	236	−73.471	16.909	−28.263	1.00	67.70	O
ATOM	481	N	ARG	B	237	−72.720	14.860	−27.666	1.00	70.52	N
ATOM	482	CA	ARG	B	237	−73.357	14.101	−28.748	1.00	71.20	C
ATOM	483	CB	ARG	B	237	−72.983	12.613	−28.639	1.00	71.49	C
ATOM	484	CG	ARG	B	237	−71.768	12.239	−29.499	1.00	72.04	C
ATOM	485	CD	ARG	B	237	−71.175	10.847	−29.206	1.00	71.96	C
ATOM	486	NE	ARG	B	237	−69.909	10.643	−29.937	1.00	71.37	N
ATOM	487	CZ	ARG	B	237	−68.687	10.761	−29.415	1.00	71.09	C
ATOM	488	NH1	ARG	B	237	−68.531	11.077	−28.132	1.00	70.70	N
ATOM	489	NH2	ARG	B	237	−67.614	10.563	−30.171	1.00	71.58	N
ATOM	490	C	ARG	B	237	−74.892	14.283	−28.885	1.00	71.39	C
ATOM	491	O	ARG	B	237	−75.409	14.334	−30.007	1.00	71.19	O
ATOM	492	N	ASP	B	238	−75.601	14.382	−27.749	1.00	71.16	N
ATOM	493	CA	ASP	B	238	−77.054	14.516	−27.705	1.00	71.52	C
ATOM	494	CB	ASP	B	238	−77.650	13.479	−26.722	1.00	71.63	C
ATOM	495	CG	ASP	B	238	−77.532	12.031	−27.144	1.00	73.10	C
ATOM	496	OD1	ASP	B	238	−77.848	11.720	−28.334	1.00	75.60	O
ATOM	497	OD2	ASP	B	238	−77.149	11.198	−26.293	1.00	74.54	O
ATOM	498	C	ASP	B	238	−77.556	15.870	−27.282	1.00	71.43	C
ATOM	499	O	ASP	B	238	−78.565	16.337	−27.810	1.00	71.16	O
ATOM	500	N	ALA	B	239	−76.906	16.456	−26.268	1.00	69.73	N
ATOM	501	CA	ALA	B	239	−77.309	17.714	−25.671	1.00	69.78	C
ATOM	502	CB	ALA	B	239	−77.607	17.499	−24.192	1.00	69.61	C
ATOM	503	C	ALA	B	239	−76.339	18.888	−25.878	1.00	69.98	C
ATOM	504	O	ALA	B	239	−76.380	19.860	−25.117	1.00	70.14	O
ATOM	505	N	GLY	B	240	−75.507	18.809	−26.914	1.00	69.35	N
ATOM	506	CA	GLY	B	240	−74.540	19.858	−27.223	1.00	69.93	C
ATOM	507	C	GLY	B	240	−75.059	20.857	−28.230	1.00	70.35	C
ATOM	508	O	GLY	B	240	−75.989	20.552	−28.991	1.00	70.72	O
ATOM	509	N	VAL	B	241	−74.477	22.071	−28.227	1.00	68.65	N
ATOM	510	CA	VAL	B	241	−74.865	23.136	−29.153	1.00	68.57	C
ATOM	511	CB	VAL	B	241	−74.481	24.545	−28.611	1.00	68.64	C
ATOM	512	CG1	VAL	B	241	−74.415	25.596	−29.720	1.00	69.14	C
ATOM	513	CG2	VAL	B	241	−75.455	24.997	−27.535	1.00	68.83	C
ATOM	514	C	VAL	B	241	−74.203	22.769	−30.469	1.00	68.68	C
ATOM	515	O	VAL	B	241	−74.902	22.445	−31.431	1.00	68.58	O
ATOM	516	N	ALA	B	242	−72.849	22.751	−30.471	1.00	67.47	N
ATOM	517	CA	ALA	B	242	−71.997	22.391	−31.603	1.00	67.98	C
ATOM	518	CB	ALA	B	242	−70.755	23.270	−31.637	1.00	67.56	C
ATOM	519	C	ALA	B	242	−71.611	20.928	−31.472	1.00	68.56	C
ATOM	520	O	ALA	B	242	−70.426	20.625	−31.362	1.00	68.61	O
ATOM	521	N	LYS	B	243	−72.625	20.019	−31.484	1.00	70.17	N
ATOM	522	CA	LYS	B	243	−72.479	18.549	−31.373	1.00	70.58	C
ATOM	523	CB	LYS	B	243	−73.758	17.824	−31.839	1.00	70.40	C
ATOM	524	CG	LYS	B	243	−74.950	17.975	−30.932	1.00	70.91	C
ATOM	525	CD	LYS	B	243	−76.200	17.759	−31.720	1.00	72.46	C
ATOM	526	CE	LYS	B	243	−77.325	17.308	−30.848	1.00	73.73	C
ATOM	527	NZ	LYS	B	243	−78.202	18.439	−30.481	1.00	74.94	N
ATOM	528	C	LYS	B	243	−71.289	18.034	−32.199	1.00	70.80	C
ATOM	529	O	LYS	B	243	−71.208	18.312	−33.406	1.00	70.91	O
ATOM	530	N	GLY	B	244	−70.372	17.340	−31.532	1.00	71.40	N
ATOM	531	CA	GLY	B	244	−69.188	16.758	−32.149	1.00	71.80	C
ATOM	532	C	GLY	B	244	−67.989	17.656	−32.409	1.00	72.07	C
ATOM	533	O	GLY	B	244	−67.100	17.249	−33.170	1.00	72.10	O
ATOM	534	N	ALA	B	245	−67.931	18.881	−31.786	1.00	74.12	N
ATOM	535	CA	ALA	B	245	−66.802	19.826	−31.942	1.00	73.82	C
ATOM	536	CB	ALA	B	245	−67.190	21.205	−31.464	1.00	73.58	C
ATOM	537	C	ALA	B	245	−65.612	19.324	−31.149	1.00	73.72	C
ATOM	538	O	ALA	B	245	−65.804	18.821	−30.056	1.00	73.86	O
ATOM	539	N	SER	B	246	−64.390	19.405	−31.684	1.00	76.47	N
ATOM	540	CA	SER	B	246	−63.265	18.895	−30.892	1.00	76.25	C
ATOM	541	CB	SER	B	246	−62.144	18.310	−31.755	1.00	76.56	C
ATOM	542	OG	SER	B	246	−61.518	19.218	−32.647	1.00	77.19	O
ATOM	543	C	SER	B	246	−62.796	19.919	−29.879	1.00	75.82	C
ATOM	544	O	SER	B	246	−62.778	21.113	−30.174	1.00	75.68	O
ATOM	545	N	MET	B	247	−62.484	19.452	−28.664	1.00	75.61	N
ATOM	546	CA	MET	B	247	−62.064	20.290	−27.540	1.00	75.40	C
ATOM	547	CB	MET	B	247	−63.145	20.308	−26.465	1.00	75.44	C
ATOM	548	CG	MET	B	247	−64.413	20.931	−26.899	1.00	76.86	C
ATOM	549	SD	MET	B	247	−65.642	20.855	−25.589	1.00	79.70	S
ATOM	550	CE	MET	B	247	−64.971	22.118	−24.482	1.00	79.04	C
ATOM	551	C	MET	B	247	−60.806	19.822	−26.860	1.00	74.96	C
ATOM	552	O	MET	B	247	−60.548	18.620	−26.791	1.00	75.05	O
ATOM	553	N	ARG	B	248	−60.047	20.777	−26.312	1.00	75.49	N
ATOM	554	CA	ARG	B	248	−58.836	20.513	−25.545	1.00	74.89	C
ATOM	555	CB	ARG	B	248	−57.587	21.112	−26.198	1.00	75.20	C
ATOM	556	CG	ARG	B	248	−57.578	20.887	−27.698	1.00	77.26	C
ATOM	557	CD	ARG	B	248	−56.245	21.122	−28.343	1.00	79.96	C
ATOM	558	NE	ARG	B	248	−55.613	19.847	−28.644	1.00	81.95	N
ATOM	559	CZ	ARG	B	248	−54.391	19.515	−28.244	1.00	83.83	C
ATOM	560	NH1	ARG	B	248	−53.894	18.316	−28.540	1.00	84.54	N
ATOM	561	NH2	ARG	B	248	−53.653	20.376	−27.541	1.00	84.67	N
ATOM	562	C	ARG	B	248	−59.087	21.076	−24.158	1.00	74.04	C
ATOM	563	O	ARG	B	248	−59.463	22.232	−24.032	1.00	73.90	O
ATOM	564	N	SER	B	249	−58.950	20.239	−23.128	1.00	71.20	N
ATOM	565	CA	SER	B	249	−59.164	20.579	−21.729	1.00	70.17	C
ATOM	566	CB	SER	B	249	−59.736	19.366	−20.999	1.00	69.92	C
ATOM	567	OG	SER	B	249	−59.511	19.446	−19.602	1.00	68.99	O
ATOM	568	C	SER	B	249	−57.850	21.031	−21.050	1.00	69.89	C
ATOM	569	O	SER	B	249	−56.810	20.406	−21.278	1.00	70.14	O
ATOM	570	N	LEU	B	250	−57.916	22.099	−20.203	1.00	66.61	N
ATOM	571	CA	LEU	B	250	−56.812	22.648	−19.391	1.00	65.82	C
ATOM	572	CB	LEU	B	250	−56.351	23.994	−19.919	1.00	65.38	C
ATOM	573	CG	LEU	B	250	−55.208	23.974	−20.898	1.00	64.50	C
ATOM	574	CD1	LEU	B	250	−55.702	23.663	−22.312	1.00	64.17	C
ATOM	575	CD2	LEU	B	250	−54.523	25.306	−20.908	1.00	63.05	C
ATOM	576	C	LEU	B	250	−57.325	22.798	−17.956	1.00	65.75	C
ATOM	577	O	LEU	B	250	−58.399	23.350	−17.777	1.00	66.25	O
ATOM	578	N	ARG	B	251	−56.608	22.285	−16.937	1.00	67.20	N
ATOM	579	CA	ARG	B	251	−57.095	22.367	−15.552	1.00	67.06	C
ATOM	580	CB	ARG	B	251	−56.857	21.076	−14.773	1.00	66.51	C
ATOM	581	CG	ARG	B	251	−57.683	21.030	−13.516	1.00	65.46	C
ATOM	582	CD	ARG	B	251	−57.459	19.766	−12.738	1.00	65.04	C
ATOM	583	NE	ARG	B	251	−58.350	19.702	−11.575	1.00	65.85	N
ATOM	584	CZ	ARG	B	251	−57.945	19.431	−10.334	1.00	65.92	C
ATOM	585	NH1	ARG	B	251	−58.822	19.402	−9.332	1.00	66.09	N
ATOM	586	NH2	ARG	B	251	−56.658	19.186	−10.085	1.00	66.35	N
ATOM	587	C	ARG	B	251	−56.608	23.553	−14.764	1.00	67.70	C
ATOM	588	O	ARG	B	251	−55.438	23.587	−14.360	1.00	67.90	O
ATOM	589	N	VAL	B	252	−57.518	24.528	−14.524	1.00	67.49	N
ATOM	590	CA	VAL	B	252	−57.211	25.746	−13.756	1.00	67.57	C
ATOM	591	CB	VAL	B	252	−57.228	27.057	−14.566	1.00	67.13	C
ATOM	592	CG1	VAL	B	252	−56.161	27.053	−15.656	1.00	67.37	C
ATOM	593	CG2	VAL	B	252	−58.607	27.350	−15.131	1.00	66.31	C
ATOM	594	C	VAL	B	252	−58.046	25.845	−12.498	1.00	68.12	C
ATOM	595	O	VAL	B	252	−57.782	26.706	−11.650	1.00	68.43	O
ATOM	596	N	LEU	B	253	−59.048	24.968	−12.365	1.00	65.71	N
ATOM	597	CA	LEU	B	253	−59.889	24.997	−11.189	1.00	66.27	C
ATOM	598	CB	LEU	B	253	−61.365	25.338	−11.518	1.00	65.95	C
ATOM	599	CG	LEU	B	253	−61.632	26.540	−12.451	1.00	64.62	C
ATOM	600	CD1	LEU	B	253	−63.059	26.692	−12.730	1.00	63.03	C
ATOM	601	CD2	LEU	B	253	−61.039	27.832	−11.937	1.00	63.96	C
ATOM	602	C	LEU	B	253	−59.746	23.712	−10.404	1.00	67.24	C
ATOM	603	O	LEU	B	253	−59.663	22.636	−10.990	1.00	67.26	O
ATOM	604	N	ASN	B	254	−59.679	23.826	−9.070	1.00	72.03	N
ATOM	605	CA	ASN	B	254	−59.555	22.675	−8.196	1.00	73.18	C
ATOM	606	CB	ASN	B	254	−58.866	23.055	−6.882	1.00	73.11	C
ATOM	607	CG	ASN	B	254	−59.635	23.933	−5.921	1.00	73.35	C
ATOM	608	OD1	ASN	B	254	−60.873	23.945	−5.851	1.00	73.95	O
ATOM	609	ND2	ASN	B	254	−58.895	24.683	−5.117	1.00	73.40	N
ATOM	610	C	ASN	B	254	−60.929	22.017	−8.018	1.00	74.16	C
ATOM	611	O	ASN	B	254	−61.852	22.372	−8.732	1.00	74.14	O
ATOM	612	N	CYS	B	255	−61.074	21.070	−7.085	1.00	80.58	N
ATOM	613	CA	CYS	B	255	−62.333	20.370	−6.860	1.00	82.09	C
ATOM	614	CB	CYS	B	255	−62.127	19.108	−6.036	1.00	82.62	C
ATOM	615	SG	CYS	B	255	−61.022	17.905	−6.832	1.00	89.25	S
ATOM	616	C	CYS	B	255	−63.427	21.222	−6.329	1.00	81.75	C
ATOM	617	O	CYS	B	255	−64.589	20.917	−6.584	1.00	82.38	O
ATOM	618	N	GLN	B	256	−63.079	22.314	−5.639	1.00	77.66	N
ATOM	619	CA	GLN	B	256	−64.057	23.252	−5.091	1.00	77.30	C
ATOM	620	CB	GLN	B	256	−63.590	23.807	−3.733	1.00	77.93	C
ATOM	621	CG	GLN	B	256	−63.313	22.757	−2.649	1.00	81.07	C
ATOM	622	CD	GLN	B	256	−61.881	22.827	−2.088	1.00	87.25	C
ATOM	623	OE1	GLN	B	256	−61.041	23.719	−2.429	1.00	89.83	O
ATOM	624	NE2	GLN	B	256	−61.568	21.877	−1.194	1.00	88.70	N
ATOM	625	C	GLN	B	256	−64.361	24.387	−6.094	1.00	76.06	C
ATOM	626	O	GLN	B	256	−64.995	25.374	−5.747	1.00	76.16	O
ATOM	627	N	GLY	B	257	−63.912	24.223	−7.330	1.00	70.38	N
ATOM	628	CA	GLY	B	257	−64.100	25.186	−8.411	1.00	68.58	C
ATOM	629	C	GLY	B	257	−63.271	26.444	−8.277	1.00	67.40	C
ATOM	630	O	GLY	B	257	−63.500	27.409	−9.009	1.00	67.30	O
ATOM	631	N	LYS	B	258	−62.297	26.434	−7.349	1.00	63.96	N
ATOM	632	CA	LYS	B	258	−61.401	27.547	−7.062	1.00	62.84	C
ATOM	633	CB	LYS	B	258	−61.073	27.568	−5.566	1.00	62.59	C
ATOM	634	CG	LYS	B	258	−60.889	28.968	−5.004	1.00	63.89	C
ATOM	635	CD	LYS	B	258	−61.172	29.003	−3.504	1.00	66.19	C
ATOM	636	CE	LYS	B	258	−59.925	29.279	−2.696	1.00	68.11	C
ATOM	637	NZ	LYS	B	258	−59.951	28.592	−1.372	1.00	70.08	N
ATOM	638	C	LYS	B	258	−60.123	27.507	−7.911	1.00	62.15	C
ATOM	639	O	LYS	B	258	−59.550	26.452	−8.117	1.00	62.29	O
ATOM	640	N	GLY	B	259	−59.711	28.661	−8.409	1.00	62.62	N
ATOM	641	CA	GLY	B	259	−58.507	28.810	−9.211	1.00	61.64	C
ATOM	642	C	GLY	B	259	−57.771	30.085	−8.845	1.00	61.25	C
ATOM	643	O	GLY	B	259	−58.114	30.754	−7.853	1.00	61.08	O
ATOM	644	N	THR	B	260	−56.742	30.431	−9.633	1.00	60.84	N
ATOM	645	CA	THR	B	260	−55.981	31.658	−9.397	1.00	60.16	C
ATOM	646	CB	THR	B	260	−54.619	31.406	−8.736	1.00	59.90	C
ATOM	647	OG1	THR	B	260	−53.793	30.546	−9.540	1.00	60.29	O
ATOM	648	CG2	THR	B	260	−54.741	30.915	−7.327	1.00	58.45	C
ATOM	649	C	THR	B	260	−55.826	32.420	−10.684	1.00	60.24	C
ATOM	650	O	THR	B	260	−55.965	31.834	−11.759	1.00	60.08	O
ATOM	651	N	VAL	B	261	−55.559	33.736	−10.580	1.00	62.43	N
ATOM	652	CA	VAL	B	261	−55.346	34.609	−11.732	1.00	62.54	C
ATOM	653	CB	VAL	B	261	−55.159	36.076	−11.269	1.00	62.53	C
ATOM	654	CG1	VAL	B	261	−54.689	36.982	−12.411	1.00	62.52	C
ATOM	655	CG2	VAL	B	261	−56.443	36.614	−10.639	1.00	62.50	C
ATOM	656	C	VAL	B	261	−54.105	34.051	−12.435	1.00	62.77	C
ATOM	657	O	VAL	B	261	−54.156	33.687	−13.615	1.00	62.53	O
ATOM	658	N	SER	B	262	−53.013	33.932	−11.655	1.00	64.10	N
ATOM	659	CA	SER	B	262	−51.694	33.417	−12.028	1.00	63.98	C
ATOM	660	CB	SER	B	262	−50.844	33.245	−10.768	1.00	63.93	C
ATOM	661	OG	SER	B	262	−51.594	32.577	−9.765	1.00	63.42	O
ATOM	662	C	SER	B	262	−51.805	32.088	−12.800	1.00	63.70	C
ATOM	663	O	SER	B	262	−51.284	31.978	−13.911	1.00	63.66	O
ATOM	664	N	GLY	B	263	−52.499	31.118	−12.212	1.00	59.41	N
ATOM	665	CA	GLY	B	263	−52.699	29.818	−12.829	1.00	59.00	C
ATOM	666	C	GLY	B	263	−53.432	29.909	−14.148	1.00	58.77	C
ATOM	667	O	GLY	B	263	−53.094	29.199	−15.085	1.00	58.40	O
ATOM	668	N	THR	B	264	−54.435	30.800	−14.230	1.00	59.19	N
ATOM	669	CA	THR	B	264	−55.214	31.016	−15.446	1.00	59.40	C
ATOM	670	CB	THR	B	264	−56.492	31.846	−15.157	1.00	59.23	C
ATOM	671	OG1	THR	B	264	−57.212	31.270	−14.085	1.00	57.85	O
ATOM	672	CG2	THR	B	264	−57.407	31.974	−16.359	1.00	58.64	C
ATOM	673	C	THR	B	264	−54.255	31.654	−16.486	1.00	60.21	C
ATOM	674	O	THR	B	264	−54.314	31.273	−17.654	1.00	60.35	O
ATOM	675	N	LEU	B	265	−53.363	32.592	−16.064	1.00	60.92	N
ATOM	676	CA	LEU	B	265	−52.390	33.217	−16.968	1.00	61.51	C
ATOM	677	CB	LEU	B	265	−51.507	34.228	−16.242	1.00	61.56	C
ATOM	678	CG	LEU	B	265	−52.105	35.499	−15.796	1.00	61.07	C
ATOM	679	CD1	LEU	B	265	−51.031	36.384	−15.256	1.00	61.15	C
ATOM	680	CD2	LEU	B	265	−52.793	36.196	−16.930	1.00	61.14	C
ATOM	681	C	LEU	B	265	−51.475	32.148	−17.562	1.00	62.10	C
ATOM	682	O	LEU	B	265	−51.352	32.085	−18.782	1.00	62.27	O
ATOM	683	N	ILE	B	266	−50.845	31.306	−16.699	1.00	62.02	N
ATOM	684	CA	ILE	B	266	−49.958	30.220	−17.110	1.00	62.61	C
ATOM	685	CB	ILE	B	266	−49.356	29.498	−15.889	1.00	62.34	C
ATOM	686	CG1	ILE	B	266	−48.527	30.489	−15.077	1.00	61.21	C
ATOM	687	CD1	ILE	B	266	−48.121	30.072	−13.744	1.00	59.56	C
ATOM	688	CG2	ILE	B	266	−48.495	28.315	−16.321	1.00	62.82	C
ATOM	689	C	ILE	B	266	−50.668	29.297	−18.126	1.00	63.41	C
ATOM	690	O	ILE	B	266	−50.049	28.912	−19.122	1.00	63.60	O
ATOM	691	N	GLY	B	267	−51.962	29.030	−17.891	1.00	64.02	N
ATOM	692	CA	GLY	B	267	−52.840	28.261	−18.763	1.00	64.93	C
ATOM	693	C	GLY	B	267	−53.057	28.971	−20.086	1.00	66.04	C
ATOM	694	O	GLY	B	267	−53.084	28.326	−21.120	1.00	66.22	O
ATOM	695	N	LEU	B	268	−53.191	30.301	−20.091	1.00	68.50	N
ATOM	696	CA	LEU	B	268	−53.379	31.042	−21.340	1.00	69.85	C
ATOM	697	CB	LEU	B	268	−53.910	32.463	−21.083	1.00	69.65	C
ATOM	698	CG	LEU	B	268	−55.356	32.607	−20.643	1.00	68.47	C
ATOM	699	CD1	LEU	B	268	−55.673	34.048	−20.359	1.00	67.56	C
ATOM	700	CD2	LEU	B	268	−56.322	32.090	−21.679	1.00	67.17	C
ATOM	701	C	LEU	B	268	−52.068	31.097	−22.137	1.00	71.25	C
ATOM	702	O	LEU	B	268	−52.103	31.106	−23.374	1.00	71.19	O
ATOM	703	N	GLU	B	269	−50.918	31.140	−21.413	1.00	76.14	N
ATOM	704	CA	GLU	B	269	−49.556	31.179	−21.963	1.00	77.92	C
ATOM	705	CB	GLU	B	269	−48.522	31.419	−20.838	1.00	78.06	C
ATOM	706	CG	GLU	B	269	−47.137	31.853	−21.311	1.00	80.49	C
ATOM	707	CD	GLU	B	269	−45.980	31.559	−20.357	1.00	84.46	C
ATOM	708	OE1	GLU	B	269	−45.848	30.397	−19.901	1.00	85.61	O
ATOM	709	OE2	GLU	B	269	−45.191	32.492	−20.081	1.00	85.68	O
ATOM	710	C	GLU	B	269	−49.311	29.834	−22.667	1.00	78.53	C
ATOM	711	O	GLU	B	269	−48.644	29.787	−23.705	1.00	78.67	O
ATOM	712	N	PHE	B	270	−49.890	28.756	−22.102	1.00	77.08	N
ATOM	713	CA	PHE	B	270	−49.835	27.406	−22.618	1.00	77.95	C
ATOM	714	CB	PHE	B	270	−50.502	26.457	−21.619	1.00	77.76	C
ATOM	715	CG	PHE	B	270	−50.556	25.010	−22.025	1.00	77.89	C
ATOM	716	CD1	PHE	B	270	−49.751	24.066	−21.401	1.00	78.17	C
ATOM	717	CE1	PHE	B	270	−49.803	22.720	−21.779	1.00	78.00	C
ATOM	718	CZ	PHE	B	270	−50.656	22.319	−22.783	1.00	77.50	C
ATOM	719	CE2	PHE	B	270	−51.467	23.236	−23.408	1.00	77.66	C
ATOM	720	CD2	PHE	B	270	−51.426	24.579	−23.024	1.00	77.70	C
ATOM	721	C	PHE	B	270	−50.555	27.378	−23.977	1.00	78.85	C
ATOM	722	O	PHE	B	270	−49.995	26.856	−24.934	1.00	79.16	O
ATOM	723	N	ILE	B	271	−51.781	27.942	−24.067	1.00	78.91	N
ATOM	724	CA	ILE	B	271	−52.584	28.020	−25.297	1.00	79.98	C
ATOM	725	CB	ILE	B	271	−53.980	28.639	−25.023	1.00	79.66	C
ATOM	726	CG1	ILE	B	271	−54.744	27.834	−23.994	1.00	79.30	C
ATOM	727	CD1	ILE	B	271	−55.932	28.488	−23.539	1.00	79.71	C
ATOM	728	CG2	ILE	B	271	−54.806	28.767	−26.297	1.00	79.37	C
ATOM	729	C	ILE	B	271	−51.834	28.818	−26.364	1.00	81.30	C
ATOM	730	O	ILE	B	271	−51.953	28.499	−27.540	1.00	80.98	O
ATOM	731	N	ARG	B	272	−51.076	29.861	−25.957	1.00	89.76	N
ATOM	732	CA	ARG	B	272	−50.321	30.685	−26.897	1.00	91.79	C
ATOM	733	CB	ARG	B	272	−49.724	31.948	−26.240	1.00	91.99	C
ATOM	734	CG	ARG	B	272	−49.015	32.925	−27.212	1.00	93.58	C
ATOM	735	CD	ARG	B	272	−49.915	33.388	−28.356	1.00	96.32	C
ATOM	736	NE	ARG	B	272	−49.252	34.288	−29.309	1.00	98.43	N
ATOM	737	CZ	ARG	B	272	−49.192	34.072	−30.623	1.00	99.37	C
ATOM	738	NH1	ARG	B	272	−49.730	32.977	−31.149	1.00	99.79	N
ATOM	739	NH2	ARG	B	272	−48.586	34.946	−31.419	1.00	99.85	N
ATOM	740	C	ARG	B	272	−49.266	29.850	−27.565	1.00	92.79	C
ATOM	741	O	ARG	B	272	−49.134	29.938	−28.779	1.00	93.00	O
ATOM	742	N	LYS	B	273	−48.549	29.016	−26.788	1.00	96.33	N
ATOM	743	CA	LYS	B	273	−47.516	28.113	−27.295	1.00	97.71	C
ATOM	744	CB	LYS	B	273	−46.703	27.484	−26.153	1.00	97.59	C
ATOM	745	CG	LYS	B	273	−45.899	28.533	−25.361	1.00	99.09	C
ATOM	746	CD	LYS	B	273	−45.328	27.986	−24.044	1.00	100.65	C
ATOM	747	CE	LYS	B	273	−44.717	29.045	−23.148	1.00	100.83	C
ATOM	748	NZ	LYS	B	273	−44.250	28.449	−21.855	1.00	101.62	N
ATOM	749	C	LYS	B	273	−48.172	27.061	−28.176	1.00	98.53	C
ATOM	750	O	LYS	B	273	−47.726	26.863	−29.302	1.00	98.77	O
ATOM	751	N	SER	B	274	−49.273	26.449	−27.707	1.00	99.80	N
ATOM	752	CA	SER	B	274	−50.037	25.441	−28.450	1.00	101.05	C
ATOM	753	CB	SER	B	274	−51.272	25.015	−27.662	1.00	101.07	C
ATOM	754	OG	SER	B	274	−50.945	24.670	−26.328	1.00	102.23	O
ATOM	755	C	SER	B	274	−50.486	25.957	−29.809	1.00	101.70	C
ATOM	756	O	SER	B	274	−50.572	25.180	−30.755	1.00	101.92	O
ATOM	757	N	GLN	B	275	−50.789	27.259	−29.896	1.00	101.88	N
ATOM	758	CA	GLN	B	275	−51.251	27.923	−31.104	1.00	102.84	C
ATOM	759	CB	GLN	B	275	−51.856	29.289	−30.743	1.00	102.72	C
ATOM	760	CG	GLN	B	275	−52.759	29.880	−31.816	1.00	102.15	C
ATOM	761	CD	GLN	B	275	−52.885	31.385	−31.755	1.00	100.72	C
ATOM	762	OE1	GLN	B	275	−52.233	32.074	−30.964	1.00	100.81	O
ATOM	763	NE2	GLN	B	275	−53.735	31.931	−32.605	1.00	100.53	N
ATOM	764	C	GLN	B	275	−50.100	28.079	−32.082	1.00	103.88	C
ATOM	765	O	GLN	B	275	−50.283	27.824	−33.272	1.00	104.18	O
ATOM	766	N	LEU	B	276	−48.920	28.490	−31.583	1.00	107.99	N
ATOM	767	CA	LEU	B	276	−47.721	28.700	−32.391	1.00	109.33	C
ATOM	768	CB	LEU	B	276	−46.615	29.395	−31.577	1.00	109.22	C
ATOM	769	CG	LEU	B	276	−46.896	30.833	−31.126	1.00	109.42	C
ATOM	770	CD1	LEU	B	276	−46.028	31.208	−29.954	1.00	109.47	C
ATOM	771	CD2	LEU	B	276	−46.742	31.838	−32.268	1.00	109.48	C
ATOM	772	C	LEU	B	276	−47.221	27.386	−32.974	1.00	110.36	C
ATOM	773	O	LEU	B	276	−47.159	27.245	−34.202	1.00	110.44	O
ATOM	774	N	VAL	B	277	−46.894	26.416	−32.080	1.00	116.52	N
ATOM	775	CA	VAL	B	277	−46.396	25.061	−32.383	1.00	117.56	C
ATOM	776	CB	VAL	B	277	−46.286	24.164	−31.102	1.00	117.53	C
ATOM	777	CG1	VAL	B	277	−46.084	22.685	−31.446	1.00	117.63	C
ATOM	778	CG2	VAL	B	277	−45.172	24.662	−30.182	1.00	117.65	C
ATOM	779	C	VAL	B	277	−47.229	24.437	−33.507	1.00	118.10	C
ATOM	780	O	VAL	B	277	−46.736	24.368	−34.636	1.00	118.31	O
ATOM	781	N	GLN	B	278	−48.489	24.045	−33.207	1.00	120.99	N
ATOM	782	CA	GLN	B	278	−49.422	23.455	−34.161	1.00	121.66	C
ATOM	783	CB	GLN	B	278	−50.691	22.919	−33.450	1.00	121.92	C
ATOM	784	CG	GLN	B	278	−50.444	21.903	−32.324	1.00	123.58	C
ATOM	785	CD	GLN	B	278	−51.715	21.462	−31.608	1.00	126.12	C
ATOM	786	OE1	GLN	B	278	−52.738	22.166	−31.571	1.00	127.28	O
ATOM	787	NE2	GLN	B	278	−51.677	20.276	−31.009	1.00	126.75	N
ATOM	788	C	GLN	B	278	−49.803	24.535	−35.196	1.00	121.49	C
ATOM	789	O	GLN	B	278	−50.590	25.429	−34.855	1.00	121.77	O
ATOM	790	N	PRO	B	279	−49.239	24.526	−36.443	1.00	122.36	N
ATOM	791	CA	PRO	B	279	−49.655	25.544	−37.427	1.00	121.69	C
ATOM	792	CB	PRO	B	279	−48.575	25.458	−38.532	1.00	121.88	C
ATOM	793	CG	PRO	B	279	−47.539	24.434	−38.030	1.00	122.28	C
ATOM	794	CD	PRO	B	279	−48.296	23.566	−37.058	1.00	122.41	C
ATOM	795	C	PRO	B	279	−51.051	25.080	−37.864	1.00	120.73	C
ATOM	796	O	PRO	B	279	−51.204	24.135	−38.659	1.00	120.92	O
ATOM	797	N	VAL	B	280	−52.071	25.680	−37.228	1.00	115.26	N
ATOM	798	CA	VAL	B	280	−53.465	25.315	−37.445	1.00	113.52	C
ATOM	799	CB	VAL	B	280	−54.075	24.563	−36.204	1.00	113.87	C
ATOM	800	CG1	VAL	B	280	−53.477	23.156	−36.042	1.00	113.62	C
ATOM	801	CG2	VAL	B	280	−53.941	25.378	−34.907	1.00	113.84	C
ATOM	802	C	VAL	B	280	−54.311	26.493	−37.970	1.00	112.03	C
ATOM	803	O	VAL	B	280	−53.749	27.428	−38.557	1.00	111.92	O
ATOM	804	N	GLY	B	281	−55.637	26.408	−37.767	1.00	105.64	N
ATOM	805	CA	GLY	B	281	−56.626	27.405	−38.168	1.00	102.84	C
ATOM	806	C	GLY	B	281	−57.292	28.151	−37.017	1.00	100.46	C
ATOM	807	O	GLY	B	281	−56.594	28.825	−36.246	1.00	100.89	O
ATOM	808	N	PRO	B	282	−58.652	28.074	−36.883	1.00	91.19	N
ATOM	809	CA	PRO	B	282	−59.336	28.813	−35.810	1.00	89.14	C
ATOM	810	CB	PRO	B	282	−60.793	28.825	−36.263	1.00	89.19	C
ATOM	811	CG	PRO	B	282	−60.943	27.627	−37.050	1.00	89.93	C
ATOM	812	CD	PRO	B	282	−59.628	27.349	−37.717	1.00	91.00	C
ATOM	813	C	PRO	B	282	−59.167	28.240	−34.408	1.00	87.01	C
ATOM	814	O	PRO	B	282	−58.887	27.050	−34.242	1.00	86.82	O
ATOM	815	N	LEU	B	283	−59.339	29.115	−33.401	1.00	80.72	N
ATOM	816	CA	LEU	B	283	−59.198	28.804	−31.981	1.00	78.15	C
ATOM	817	CB	LEU	B	283	−57.789	29.242	−31.551	1.00	78.20	C
ATOM	818	CG	LEU	B	283	−57.040	28.350	−30.582	1.00	78.62	C
ATOM	819	CD1	LEU	B	283	−56.323	27.223	−31.317	1.00	79.96	C
ATOM	820	CD2	LEU	B	283	−56.004	29.145	−29.848	1.00	78.44	C
ATOM	821	C	LEU	B	283	−60.248	29.532	−31.107	1.00	76.26	C
ATOM	822	O	LEU	B	283	−60.404	30.746	−31.215	1.00	76.25	O
ATOM	823	N	VAL	B	284	−60.948	28.794	−30.240	1.00	69.65	N
ATOM	824	CA	VAL	B	284	−61.933	29.344	−29.306	1.00	66.85	C
ATOM	825	CB	VAL	B	284	−63.381	28.841	−29.550	1.00	66.64	C
ATOM	826	CG1	VAL	B	284	−64.343	29.377	−28.497	1.00	65.54	C
ATOM	827	CG2	VAL	B	284	−63.863	29.209	−30.942	1.00	65.81	C
ATOM	828	C	VAL	B	284	−61.444	29.024	−27.895	1.00	65.45	C
ATOM	829	O	VAL	B	284	−61.199	27.872	−27.592	1.00	65.31	O
ATOM	830	N	VAL	B	285	−61.270	30.022	−27.047	1.00	64.37	N
ATOM	831	CA	VAL	B	285	−60.844	29.783	−25.674	1.00	63.25	C
ATOM	832	CB	VAL	B	285	−59.605	30.599	−25.256	1.00	63.09	C
ATOM	833	CG1	VAL	B	285	−59.359	30.481	−23.766	1.00	62.67	C
ATOM	834	CG2	VAL	B	285	−58.371	30.144	−26.020	1.00	63.08	C
ATOM	835	C	VAL	B	285	−62.045	30.077	−24.809	1.00	62.71	C
ATOM	836	O	VAL	B	285	−62.540	31.205	−24.818	1.00	62.92	O
ATOM	837	N	LEU	B	286	−62.545	29.067	−24.097	1.00	63.34	N
ATOM	838	CA	LEU	B	286	−63.694	29.235	−23.217	1.00	62.71	C
ATOM	839	CB	LEU	B	286	−64.766	28.183	−23.501	1.00	62.52	C
ATOM	840	CG	LEU	B	286	−65.735	27.853	−22.392	1.00	62.69	C
ATOM	841	CD1	LEU	B	286	−66.769	28.949	−22.197	1.00	62.31	C
ATOM	842	CD2	LEU	B	286	−66.418	26.550	−22.686	1.00	63.41	C
ATOM	843	C	LEU	B	286	−63.215	29.258	−21.743	1.00	62.46	C
ATOM	844	O	LEU	B	286	−62.615	28.292	−21.246	1.00	62.37	O
ATOM	845	N	LEU	B	287	−63.451	30.412	−21.082	1.00	62.84	N
ATOM	846	CA	LEU	B	287	−63.089	30.686	−19.698	1.00	62.24	C
ATOM	847	CB	LEU	B	287	−62.236	31.948	−19.625	1.00	62.14	C
ATOM	848	CG	LEU	B	287	−60.959	31.917	−20.414	1.00	61.78	C
ATOM	849	CD1	LEU	B	287	−60.962	33.019	−21.408	1.00	61.94	C
ATOM	850	CD2	LEU	B	287	−59.779	32.050	−19.518	1.00	60.79	C
ATOM	851	C	LEU	B	287	−64.385	30.871	−18.905	1.00	62.08	C
ATOM	852	O	LEU	B	287	−64.886	31.998	−18.807	1.00	62.29	O
ATOM	853	N	PRO	B	288	−64.966	29.773	−18.353	1.00	63.14	N
ATOM	854	CA	PRO	B	288	−66.243	29.892	−17.615	1.00	62.63	C
ATOM	855	CB	PRO	B	288	−66.932	28.565	−17.937	1.00	62.45	C
ATOM	856	CG	PRO	B	288	−65.820	27.623	−18.305	1.00	62.93	C
ATOM	857	CD	PRO	B	288	−64.524	28.370	−18.394	1.00	63.06	C
ATOM	858	C	PRO	B	288	−66.010	30.119	−16.112	1.00	62.16	C
ATOM	859	O	PRO	B	288	−66.469	29.365	−15.245	1.00	62.44	O
ATOM	860	N	LEU	B	289	−65.265	31.183	−15.823	1.00	62.09	N
ATOM	861	CA	LEU	B	289	−64.851	31.538	−14.492	1.00	61.42	C
ATOM	862	CB	LEU	B	289	−63.469	30.909	−14.214	1.00	61.52	C
ATOM	863	CG	LEU	B	289	−62.367	31.084	−15.278	1.00	60.95	C
ATOM	864	CD1	LEU	B	289	−61.614	32.401	−15.094	1.00	59.80	C
ATOM	865	CD2	LEU	B	289	−61.395	29.911	−15.247	1.00	60.26	C
ATOM	866	C	LEU	B	289	−64.805	33.038	−14.291	1.00	61.25	C
ATOM	867	O	LEU	B	289	−64.786	33.797	−15.256	1.00	61.35	O
ATOM	868	N	ALA	B	290	−64.756	33.473	−13.038	1.00	61.46	N
ATOM	869	CA	ALA	B	290	−64.732	34.884	−12.737	1.00	61.26	C
ATOM	870	CB	ALA	B	290	−66.158	35.363	−12.513	1.00	61.09	C
ATOM	871	C	ALA	B	290	−63.893	35.186	−11.516	1.00	61.37	C
ATOM	872	O	ALA	B	290	−63.746	34.334	−10.649	1.00	61.38	O
ATOM	873	N	GLY	B	291	−63.370	36.398	−11.459	1.00	60.73	N
ATOM	874	CA	GLY	B	291	−62.595	36.936	−10.351	1.00	61.16	C
ATOM	875	C	GLY	B	291	−62.833	38.433	−10.364	1.00	61.50	C
ATOM	876	O	GLY	B	291	−63.539	38.924	−11.244	1.00	61.91	O
ATOM	877	N	GLY	B	292	−62.253	39.175	−9.432	1.00	61.91	N
ATOM	878	CA	GLY	B	292	−62.401	40.623	−9.436	1.00	62.03	C
ATOM	879	C	GLY	B	292	−61.699	41.185	−10.660	1.00	62.38	C
ATOM	880	O	GLY	B	292	−60.960	40.443	−11.327	1.00	62.27	O
ATOM	881	N	TYR	B	293	−61.909	42.493	−10.987	1.00	64.79	N
ATOM	882	CA	TYR	B	293	−61.232	43.050	−12.157	1.00	64.90	C
ATOM	883	CB	TYR	B	293	−61.637	44.508	−12.443	1.00	64.83	C
ATOM	884	CG	TYR	B	293	−60.623	45.227	−13.312	1.00	65.53	C
ATOM	885	CD1	TYR	B	293	−60.693	45.163	−14.700	1.00	66.24	C
ATOM	886	CE1	TYR	B	293	−59.739	45.790	−15.502	1.00	67.57	C
ATOM	887	CZ	TYR	B	293	−58.686	46.482	−14.913	1.00	68.84	C
ATOM	888	OH	TYR	B	293	−57.712	47.094	−15.680	1.00	71.12	O
ATOM	889	CE2	TYR	B	293	−58.592	46.543	−13.534	1.00	67.77	C
ATOM	890	CD2	TYR	B	293	−59.563	45.929	−12.746	1.00	66.45	C
ATOM	891	C	TYR	B	293	−59.714	42.903	−11.993	1.00	64.84	C
ATOM	892	O	TYR	B	293	−59.172	43.323	−10.968	1.00	64.89	O
ATOM	893	N	SER	B	294	−59.048	42.287	−12.987	1.00	64.99	N
ATOM	894	CA	SER	B	294	−57.600	42.074	−13.014	1.00	65.59	C
ATOM	895	CB	SER	B	294	−57.289	40.586	−13.096	1.00	65.66	C
ATOM	896	OG	SER	B	294	−55.979	40.351	−13.585	1.00	65.02	O
ATOM	897	C	SER	B	294	−56.990	42.734	−14.231	1.00	66.16	C
ATOM	898	O	SER	B	294	−57.414	42.428	−15.345	1.00	66.20	O
ATOM	899	N	ARG	B	295	−55.970	43.597	−14.041	1.00	68.26	N
ATOM	900	CA	ARG	B	295	−55.282	44.255	−15.158	1.00	68.63	C
ATOM	901	CB	ARG	B	295	−54.300	45.317	−14.636	1.00	68.95	C
ATOM	902	CG	ARG	B	295	−53.713	46.206	−15.724	1.00	69.57	C
ATOM	903	CD	ARG	B	295	−52.767	47.221	−15.138	1.00	70.03	C
ATOM	904	NE	ARG	B	295	−52.075	47.948	−16.200	1.00	72.60	N
ATOM	905	CZ	ARG	B	295	−51.133	48.873	−16.008	1.00	73.70	C
ATOM	906	NH1	ARG	B	295	−50.745	49.194	−14.778	1.00	74.10	N
ATOM	907	NH2	ARG	B	295	−50.562	49.472	−17.047	1.00	74.62	N
ATOM	908	C	ARG	B	295	−54.538	43.203	−15.999	1.00	68.50	C
ATOM	909	O	ARG	B	295	−54.693	43.179	−17.217	1.00	68.72	O
ATOM	910	N	VAL	B	296	−53.761	42.326	−15.333	1.00	66.22	N
ATOM	911	CA	VAL	B	296	−52.969	41.263	−15.956	1.00	65.91	C
ATOM	912	CB	VAL	B	296	−51.887	40.658	−15.025	1.00	65.76	C
ATOM	913	CG1	VAL	B	296	−52.460	39.654	−14.039	1.00	64.52	C
ATOM	914	CG2	VAL	B	296	−50.778	40.031	−15.833	1.00	65.21	C
ATOM	915	C	VAL	B	296	−53.767	40.230	−16.733	1.00	66.07	C
ATOM	916	O	VAL	B	296	−53.389	39.925	−17.846	1.00	66.43	O
ATOM	917	N	LEU	B	297	−54.848	39.698	−16.172	1.00	64.68	N
ATOM	918	CA	LEU	B	297	−55.660	38.716	−16.865	1.00	64.85	C
ATOM	919	CB	LEU	B	297	−56.741	38.146	−15.935	1.00	64.83	C
ATOM	920	CG	LEU	B	297	−57.642	37.028	−16.456	1.00	64.77	C
ATOM	921	CD1	LEU	B	297	−56.857	35.817	−16.880	1.00	64.90	C
ATOM	922	CD2	LEU	B	297	−58.574	36.588	−15.382	1.00	65.00	C
ATOM	923	C	LEU	B	297	−56.255	39.385	−18.090	1.00	65.24	C
ATOM	924	O	LEU	B	297	−56.053	38.885	−19.184	1.00	65.29	O
ATOM	925	N	ASN	B	298	−56.909	40.548	−17.928	1.00	65.33	N
ATOM	926	CA	ASN	B	298	−57.491	41.310	−19.030	1.00	65.69	C
ATOM	927	CB	ASN	B	298	−58.071	42.609	−18.523	1.00	65.52	C
ATOM	928	CG	ASN	B	298	−59.430	42.467	−17.930	1.00	65.42	C
ATOM	929	OD1	ASN	B	298	−59.889	41.361	−17.614	1.00	64.87	O
ATOM	930	ND2	ASN	B	298	−60.108	43.588	−17.769	1.00	64.99	N
ATOM	931	C	ASN	B	298	−56.485	41.616	−20.137	1.00	66.28	C
ATOM	932	O	ASN	B	298	−56.849	41.546	−21.314	1.00	66.62	O
ATOM	933	N	ALA	B	299	−55.237	41.965	−19.760	1.00	64.24	N
ATOM	934	CA	ALA	B	299	−54.166	42.287	−20.679	1.00	64.70	C
ATOM	935	CB	ALA	B	299	−52.941	42.711	−19.895	1.00	64.65	C
ATOM	936	C	ALA	B	299	−53.842	41.079	−21.527	1.00	65.39	C
ATOM	937	O	ALA	B	299	−53.663	41.214	−22.735	1.00	65.12	O
ATOM	938	N	ALA	B	300	−53.773	39.898	−20.882	1.00	66.94	N
ATOM	939	CA	ALA	B	300	−53.476	38.603	−21.477	1.00	68.02	C
ATOM	940	CB	ALA	B	300	−53.287	37.563	−20.386	1.00	67.68	C
ATOM	941	C	ALA	B	300	−54.589	38.172	−22.428	1.00	68.95	C
ATOM	942	O	ALA	B	300	−54.325	37.566	−23.455	1.00	69.09	O
ATOM	943	N	CYS	B	301	−55.824	38.491	−22.105	1.00	74.05	N
ATOM	944	CA	CYS	B	301	−56.923	38.122	−22.970	1.00	75.78	C
ATOM	945	CB	CYS	B	301	−58.244	38.228	−22.222	1.00	75.64	C
ATOM	946	SG	CYS	B	301	−58.381	37.099	−20.810	1.00	78.21	S
ATOM	947	C	CYS	B	301	−56.895	39.004	−24.200	1.00	76.78	C
ATOM	948	O	CYS	B	301	−57.223	38.542	−25.298	1.00	77.13	O
ATOM	949	N	GLN	B	302	−56.467	40.269	−24.019	1.00	81.35	N
ATOM	950	CA	GLN	B	302	−56.351	41.259	−25.081	1.00	82.53	C
ATOM	951	CB	GLN	B	302	−56.133	42.670	−24.496	1.00	82.87	C
ATOM	952	CG	GLN	B	302	−55.970	43.814	−25.507	1.00	84.29	C
ATOM	953	CD	GLN	B	302	−54.565	44.367	−25.477	1.00	87.06	C
ATOM	954	OE1	GLN	B	302	−53.874	44.430	−26.512	1.00	89.24	O
ATOM	955	NE2	GLN	B	302	−54.092	44.774	−24.290	1.00	87.85	N
ATOM	956	C	GLN	B	302	−55.236	40.840	−26.022	1.00	82.94	C
ATOM	957	O	GLN	B	302	−55.491	40.793	−27.216	1.00	83.12	O
ATOM	958	N	ARG	B	303	−54.033	40.495	−25.499	1.00	83.14	N
ATOM	959	CA	ARG	B	303	−52.901	40.065	−26.319	1.00	83.88	C
ATOM	960	CB	ARG	B	303	−51.648	39.825	−25.459	1.00	84.35	C
ATOM	961	CG	ARG	B	303	−50.440	39.294	−26.239	1.00	87.43	C
ATOM	962	CD	ARG	B	303	−49.226	40.219	−26.312	1.00	92.85	C
ATOM	963	NE	ARG	B	303	−48.042	39.479	−26.791	1.00	96.60	N
ATOM	964	CZ	ARG	B	303	−46.772	39.876	−26.661	1.00	98.59	C
ATOM	965	NH1	ARG	B	303	−46.484	41.029	−26.055	1.00	99.18	N
ATOM	966	NH2	ARG	B	303	−45.783	39.123	−27.133	1.00	99.96	N
ATOM	967	C	ARG	B	303	−53.262	38.840	−27.190	1.00	83.75	C
ATOM	968	O	ARG	B	303	−52.950	38.815	−28.387	1.00	84.03	O
ATOM	969	N	LEU	B	304	−53.945	37.853	−26.592	1.00	79.66	N
ATOM	970	CA	LEU	B	304	−54.403	36.617	−27.227	1.00	79.27	C
ATOM	971	CB	LEU	B	304	−55.014	35.732	−26.133	1.00	79.28	C
ATOM	972	CG	LEU	B	304	−54.840	34.216	−26.188	1.00	79.49	C
ATOM	973	CD1	LEU	B	304	−53.393	33.793	−26.419	1.00	79.48	C
ATOM	974	CD2	LEU	B	304	−55.271	33.617	−24.883	1.00	80.20	C
ATOM	975	C	LEU	B	304	−55.433	36.891	−28.332	1.00	79.16	C
ATOM	976	O	LEU	B	304	−55.456	36.190	−29.332	1.00	78.82	O
ATOM	977	N	ALA	B	305	−56.274	37.915	−28.150	1.00	78.62	N
ATOM	978	CA	ALA	B	305	−57.295	38.302	−29.116	1.00	78.76	C
ATOM	979	CB	ALA	B	305	−58.250	39.295	−28.483	1.00	78.61	C
ATOM	980	C	ALA	B	305	−56.650	38.889	−30.371	1.00	78.89	C
ATOM	981	O	ALA	B	305	−57.161	38.683	−31.473	1.00	78.50	O
ATOM	982	N	ARG	B	306	−55.513	39.607	−30.182	1.00	82.77	N
ATOM	983	CA	ARG	B	306	−54.686	40.219	−31.233	1.00	83.19	C
ATOM	984	CB	ARG	B	306	−53.537	41.096	−30.666	1.00	83.62	C
ATOM	985	CG	ARG	B	306	−53.958	42.091	−29.584	1.00	86.19	C
ATOM	986	CD	ARG	B	306	−53.874	43.551	−29.983	1.00	90.92	C
ATOM	987	NE	ARG	B	306	−55.167	44.216	−29.792	1.00	93.38	N
ATOM	988	CZ	ARG	B	306	−55.325	45.431	−29.268	1.00	94.24	C
ATOM	989	NH1	ARG	B	306	−54.266	46.135	−28.868	1.00	94.00	N
ATOM	990	NH2	ARG	B	306	−56.545	45.950	−29.137	1.00	94.74	N
ATOM	991	C	ARG	B	306	−54.096	39.059	−32.014	1.00	82.50	C
ATOM	992	O	ARG	B	306	−54.136	39.084	−33.241	1.00	82.73	O
ATOM	993	N	ALA	B	307	−53.612	38.009	−31.307	1.00	79.21	N
ATOM	994	CA	ALA	B	307	−53.081	36.802	−31.941	1.00	78.26	C
ATOM	995	CB	ALA	B	307	−52.368	35.919	−30.916	1.00	78.38	C
ATOM	996	C	ALA	B	307	−54.190	36.012	−32.675	1.00	77.40	C
ATOM	997	O	ALA	B	307	−53.981	34.858	−33.022	1.00	77.54	O
ATOM	998	N	GLY	B	308	−55.342	36.649	−32.902	1.00	76.27	N
ATOM	999	CA	GLY	B	308	−56.490	36.098	−33.620	1.00	75.00	C
ATOM	1000	C	GLY	B	308	−57.519	35.267	−32.875	1.00	74.15	C
ATOM	1001	O	GLY	B	308	−58.621	35.044	−33.392	1.00	74.25	O
ATOM	1002	N	VAL	B	309	−57.170	34.798	−31.665	1.00	74.16	N
ATOM	1003	CA	VAL	B	309	−58.005	33.952	−30.798	1.00	72.79	C
ATOM	1004	CB	VAL	B	309	−57.222	33.470	−29.545	1.00	72.94	C
ATOM	1005	CG1	VAL	B	309	−57.930	32.303	−28.879	1.00	73.15	C
ATOM	1006	CG2	VAL	B	309	−55.775	33.092	−29.876	1.00	72.80	C
ATOM	1007	C	VAL	B	309	−59.361	34.588	−30.403	1.00	71.77	C
ATOM	1008	O	VAL	B	309	−59.451	35.794	−30.139	1.00	71.89	O
ATOM	1009	N	VAL	B	310	−60.404	33.751	−30.354	1.00	67.70	N
ATOM	1010	CA	VAL	B	310	−61.773	34.115	−29.964	1.00	65.94	C
ATOM	1011	CB	VAL	B	310	−62.806	33.548	−30.985	1.00	66.01	C
ATOM	1012	CG1	VAL	B	310	−64.228	33.545	−30.432	1.00	65.64	C
ATOM	1013	CG2	VAL	B	310	−62.732	34.304	−32.304	1.00	64.95	C
ATOM	1014	C	VAL	B	310	−61.973	33.586	−28.526	1.00	64.79	C
ATOM	1015	O	VAL	B	310	−61.924	32.389	−28.309	1.00	64.43	O
ATOM	1016	N	LEU	B	311	−62.136	34.484	−27.548	1.00	65.24	N
ATOM	1017	CA	LEU	B	311	−62.322	34.107	−26.141	1.00	64.15	C
ATOM	1018	CB	LEU	B	311	−61.370	34.859	−25.202	1.00	63.97	C
ATOM	1019	CG	LEU	B	311	−59.878	34.536	−25.347	1.00	64.52	C
ATOM	1020	CD1	LEU	B	311	−59.187	35.472	−26.313	1.00	65.02	C
ATOM	1021	CD2	LEU	B	311	−59.174	34.704	−24.056	1.00	64.24	C
ATOM	1022	C	LEU	B	311	−63.759	34.342	−25.734	1.00	63.45	C
ATOM	1023	O	LEU	B	311	−64.360	35.368	−26.100	1.00	63.75	O
ATOM	1024	N	VAL	B	312	−64.337	33.365	−25.016	1.00	61.15	N
ATOM	1025	CA	VAL	B	312	−65.720	33.450	−24.529	1.00	59.55	C
ATOM	1026	CB	VAL	B	312	−66.698	32.496	−25.240	1.00	59.24	C
ATOM	1027	CG1	VAL	B	312	−68.120	32.761	−24.793	1.00	58.49	C
ATOM	1028	CG2	VAL	B	312	−66.583	32.632	−26.757	1.00	58.14	C
ATOM	1029	C	VAL	B	312	−65.665	33.287	−23.028	1.00	59.03	C
ATOM	1030	O	VAL	B	312	−64.942	32.420	−22.542	1.00	59.28	O
ATOM	1031	N	THR	B	313	−66.364	34.159	−22.298	1.00	60.50	N
ATOM	1032	CA	THR	B	313	−66.337	34.186	−20.834	1.00	59.73	C
ATOM	1033	CB	THR	B	313	−65.370	35.307	−20.388	1.00	59.82	C
ATOM	1034	OG1	THR	B	313	−65.293	35.342	−18.954	1.00	61.73	O
ATOM	1035	CG2	THR	B	313	−65.781	36.664	−20.889	1.00	59.54	C
ATOM	1036	C	THR	B	313	−67.686	34.306	−20.124	1.00	58.80	C
ATOM	1037	O	THR	B	313	−68.658	34.806	−20.700	1.00	58.72	O
ATOM	1038	N	ALA	B	314	−67.739	33.872	−18.854	1.00	56.48	N
ATOM	1039	CA	ALA	B	314	−68.978	33.997	−18.079	1.00	56.09	C
ATOM	1040	CB	ALA	B	314	−68.988	33.039	−16.893	1.00	55.49	C
ATOM	1041	C	ALA	B	314	−69.050	35.440	−17.593	1.00	55.97	C
ATOM	1042	O	ALA	B	314	−68.021	36.021	−17.215	1.00	56.24	O
ATOM	1043	N	ALA	B	315	−70.247	36.036	−17.626	1.00	54.10	N
ATOM	1044	CA	ALA	B	315	−70.388	37.397	−17.154	1.00	53.49	C
ATOM	1045	CB	ALA	B	315	−71.734	37.952	−17.549	1.00	53.36	C
ATOM	1046	C	ALA	B	315	−70.200	37.440	−15.627	1.00	53.40	C
ATOM	1047	O	ALA	B	315	−69.737	38.460	−15.106	1.00	53.51	O
ATOM	1048	N	GLY	B	316	−70.496	36.326	−14.944	1.00	50.96	N
ATOM	1049	CA	GLY	B	316	−70.407	36.221	−13.500	1.00	51.09	C
ATOM	1050	C	GLY	B	316	−71.795	36.017	−12.933	1.00	51.70	C
ATOM	1051	O	GLY	B	316	−72.798	36.418	−13.540	1.00	51.47	O
ATOM	1052	N	ASN	B	317	−71.873	35.369	−11.775	1.00	53.82	N
ATOM	1053	CA	ASN	B	317	−73.149	35.071	−11.126	1.00	54.21	C
ATOM	1054	CB	ASN	B	317	−73.183	33.588	−10.795	1.00	53.67	C
ATOM	1055	CG	ASN	B	317	−72.945	32.681	−11.969	1.00	53.09	C
ATOM	1056	OD1	ASN	B	317	−73.258	32.996	−13.112	1.00	52.07	O
ATOM	1057	ND2	ASN	B	317	−72.392	31.521	−11.710	1.00	53.94	N
ATOM	1058	C	ASN	B	317	−73.322	35.916	−9.866	1.00	55.00	C
ATOM	1059	O	ASN	B	317	−73.792	35.435	−8.843	1.00	55.03	O
ATOM	1060	N	PHE	B	318	−72.957	37.174	−9.939	1.00	57.87	N
ATOM	1061	CA	PHE	B	318	−73.018	38.000	−8.759	1.00	59.18	C
ATOM	1062	CB	PHE	B	318	−71.639	38.625	−8.558	1.00	59.07	C
ATOM	1063	CG	PHE	B	318	−70.543	37.591	−8.502	1.00	60.43	C
ATOM	1064	CD1	PHE	B	318	−70.408	36.753	−7.397	1.00	60.99	C
ATOM	1065	CE1	PHE	B	318	−69.408	35.784	−7.353	1.00	61.38	C
ATOM	1066	CZ	PHE	B	318	−68.543	35.638	−8.418	1.00	62.04	C
ATOM	1067	CE2	PHE	B	318	−68.652	36.469	−9.513	1.00	61.99	C
ATOM	1068	CD2	PHE	B	318	−69.664	37.433	−9.562	1.00	61.64	C
ATOM	1069	C	PHE	B	318	−74.093	39.053	−8.750	1.00	59.93	C
ATOM	1070	O	PHE	B	318	−74.101	39.886	−7.840	1.00	60.27	O
ATOM	1071	N	ARG	B	319	−75.009	39.028	−9.748	1.00	62.41	N
ATOM	1072	CA	ARG	B	319	−76.081	40.020	−9.913	1.00	63.19	C
ATOM	1073	CB	ARG	B	319	−77.305	39.725	−9.016	1.00	63.23	C
ATOM	1074	CG	ARG	B	319	−78.540	40.496	−9.473	1.00	64.48	C
ATOM	1075	CD	ARG	B	319	−79.855	39.992	−8.921	1.00	67.70	C
ATOM	1076	NE	ARG	B	319	−80.960	40.830	−9.410	1.00	71.37	N
ATOM	1077	CZ	ARG	B	319	−82.248	40.501	−9.322	1.00	72.76	C
ATOM	1078	NH1	ARG	B	319	−82.612	39.345	−8.777	1.00	73.52	N
ATOM	1079	NH2	ARG	B	319	−83.183	41.314	−9.813	1.00	72.41	N
ATOM	1080	C	ARG	B	319	−75.479	41.435	−9.704	1.00	63.42	C
ATOM	1081	O	ARG	B	319	−76.033	42.268	−8.989	1.00	63.73	O
ATOM	1082	N	ASP	B	320	−74.312	41.662	−10.320	1.00	60.42	N
ATOM	1083	CA	ASP	B	320	−73.530	42.873	−10.230	1.00	60.55	C
ATOM	1084	CB	ASP	B	320	−72.304	42.552	−9.364	1.00	60.60	C
ATOM	1085	CG	ASP	B	320	−71.544	43.741	−8.807	1.00	61.89	C
ATOM	1086	OD1	ASP	B	320	−72.018	44.900	−8.997	1.00	63.22	O
ATOM	1087	OD2	ASP	B	320	−70.464	43.523	−8.172	1.00	63.66	O
ATOM	1088	C	ASP	B	320	−73.091	43.307	−11.623	1.00	60.89	C
ATOM	1089	O	ASP	B	320	−73.323	42.608	−12.596	1.00	60.80	O
ATOM	1090	N	ASP	B	321	−72.457	44.456	−11.723	1.00	62.47	N
ATOM	1091	CA	ASP	B	321	−71.955	44.980	−12.973	1.00	63.25	C
ATOM	1092	CB	ASP	B	321	−71.748	46.490	−12.827	1.00	63.52	C
ATOM	1093	CG	ASP	B	321	−70.868	47.151	−13.863	1.00	66.23	C
ATOM	1094	OD1	ASP	B	321	−70.991	46.787	−15.099	1.00	68.25	O
ATOM	1095	OD2	ASP	B	321	−70.047	48.029	−13.466	1.00	69.51	O
ATOM	1096	C	ASP	B	321	−70.664	44.203	−13.367	1.00	63.26	C
ATOM	1097	O	ASP	B	321	−69.640	44.266	−12.668	1.00	63.00	O
ATOM	1098	N	ALA	B	322	−70.742	43.466	−14.505	1.00	63.34	N
ATOM	1099	CA	ALA	B	322	−69.678	42.617	−15.058	1.00	63.47	C
ATOM	1100	CB	ALA	B	322	−70.135	41.973	−16.351	1.00	63.32	C
ATOM	1101	C	ALA	B	322	−68.329	43.277	−15.249	1.00	63.71	C
ATOM	1102	O	ALA	B	322	−67.333	42.599	−15.461	1.00	63.80	O
ATOM	1103	N	CYS	B	323	−68.293	44.587	−15.157	1.00	65.81	N
ATOM	1104	CA	CYS	B	323	−67.083	45.376	−15.328	1.00	66.30	C
ATOM	1105	CB	CYS	B	323	−67.449	46.810	−15.689	1.00	66.41	C
ATOM	1106	SG	CYS	B	323	−68.421	46.951	−17.215	1.00	71.16	S
ATOM	1107	C	CYS	B	323	−66.222	45.326	−14.114	1.00	65.76	C
ATOM	1108	O	CYS	B	323	−65.083	45.788	−14.154	1.00	66.03	O
ATOM	1109	N	LEU	B	324	−66.755	44.785	−13.022	1.00	60.42	N
ATOM	1110	CA	LEU	B	324	−66.002	44.698	−11.774	1.00	60.17	C
ATOM	1111	CB	LEU	B	324	−66.902	44.989	−10.549	1.00	59.89	C
ATOM	1112	CG	LEU	B	324	−67.731	46.250	−10.542	1.00	57.86	C
ATOM	1113	CD1	LEU	B	324	−68.629	46.254	−9.347	1.00	56.82	C
ATOM	1114	CD2	LEU	B	324	−66.874	47.477	−10.635	1.00	54.79	C
ATOM	1115	C	LEU	B	324	−65.353	43.332	−11.636	1.00	60.54	C
ATOM	1116	O	LEU	B	324	−64.750	43.051	−10.593	1.00	60.71	O
ATOM	1117	N	TYR	B	325	−65.481	42.497	−12.694	1.00	60.77	N
ATOM	1118	CA	TYR	B	325	−64.988	41.133	−12.770	1.00	61.44	C
ATOM	1119	CB	TYR	B	325	−66.184	40.173	−12.748	1.00	61.31	C
ATOM	1120	CG	TYR	B	325	−67.056	40.381	−11.534	1.00	61.96	C
ATOM	1121	CD1	TYR	B	325	−66.831	39.667	−10.359	1.00	62.39	C
ATOM	1122	CE1	TYR	B	325	−67.591	39.901	−9.216	1.00	63.69	C
ATOM	1123	CZ	TYR	B	325	−68.614	40.841	−9.250	1.00	64.04	C
ATOM	1124	OH	TYR	B	325	−69.381	41.077	−8.135	1.00	65.21	O
ATOM	1125	CE2	TYR	B	325	−68.855	41.563	−10.408	1.00	63.14	C
ATOM	1126	CD2	TYR	B	325	−68.082	41.324	−11.542	1.00	62.84	C
ATOM	1127	C	TYR	B	325	−64.132	40.863	−13.994	1.00	62.04	C
ATOM	1128	O	TYR	B	325	−64.366	41.428	−15.044	1.00	61.85	O
ATOM	1129	N	SER	B	326	−63.156	39.989	−13.873	1.00	62.89	N
ATOM	1130	CA	SER	B	326	−62.288	39.610	−14.988	1.00	63.61	C
ATOM	1131	CB	SER	B	326	−60.863	40.095	−14.774	1.00	63.85	C
ATOM	1132	OG	SER	B	326	−60.802	41.499	−14.935	1.00	64.07	O
ATOM	1133	C	SER	B	326	−62.317	38.100	−15.085	1.00	63.80	C
ATOM	1134	O	SER	B	326	−62.452	37.444	−14.051	1.00	64.86	O
ATOM	1135	N	PRO	B	327	−62.235	37.505	−16.286	1.00	65.20	N
ATOM	1136	CA	PRO	B	327	−62.054	38.141	−17.592	1.00	64.67	C
ATOM	1137	CB	PRO	B	327	−61.389	37.029	−18.418	1.00	64.01	C
ATOM	1138	CG	PRO	B	327	−61.990	35.765	−17.876	1.00	65.29	C
ATOM	1139	CD	PRO	B	327	−62.281	36.032	−16.410	1.00	64.99	C
ATOM	1140	C	PRO	B	327	−63.287	38.808	−18.223	1.00	64.37	C
ATOM	1141	O	PRO	B	327	−63.144	39.327	−19.323	1.00	64.00	O
ATOM	1142	N	ALA	B	328	−64.462	38.849	−17.542	1.00	62.54	N
ATOM	1143	CA	ALA	B	328	−65.677	39.500	−18.072	1.00	62.61	C
ATOM	1144	CB	ALA	B	328	−66.788	39.500	−17.029	1.00	62.46	C
ATOM	1145	C	ALA	B	328	−65.443	40.936	−18.573	1.00	62.77	C
ATOM	1146	O	ALA	B	328	−65.986	41.317	−19.615	1.00	62.83	O
ATOM	1147	N	SER	B	329	−64.635	41.719	−17.839	1.00	62.16	N
ATOM	1148	CA	SER	B	329	−64.330	43.111	−18.152	1.00	62.02	C
ATOM	1149	CB	SER	B	329	−63.787	43.835	−16.930	1.00	61.96	C
ATOM	1150	OG	SER	B	329	−62.597	43.229	−16.448	1.00	61.98	O
ATOM	1151	C	SER	B	329	−63.422	43.347	−19.347	1.00	62.28	C
ATOM	1152	O	SER	B	329	−63.419	44.473	−19.854	1.00	62.32	O
ATOM	1153	N	ALA	B	330	−62.636	42.327	−19.796	1.00	65.17	N
ATOM	1154	CA	ALA	B	330	−61.765	42.458	−20.969	1.00	65.63	C
ATOM	1155	CB	ALA	B	330	−60.979	41.177	−21.200	1.00	65.46	C
ATOM	1156	C	ALA	B	330	−62.722	42.749	−22.153	1.00	66.41	C
ATOM	1157	O	ALA	B	330	−63.680	41.992	−22.382	1.00	66.58	O
ATOM	1158	N	PRO	B	331	−62.585	43.907	−22.844	1.00	73.00	N
ATOM	1159	CA	PRO	B	331	−63.554	44.219	−23.923	1.00	73.50	C
ATOM	1160	CB	PRO	B	331	−63.334	45.714	−24.166	1.00	73.46	C
ATOM	1161	CG	PRO	B	331	−61.916	45.944	−23.767	1.00	72.99	C
ATOM	1162	CD	PRO	B	331	−61.573	44.978	−22.687	1.00	72.92	C
ATOM	1163	C	PRO	B	331	−63.366	43.369	−25.188	1.00	73.88	C
ATOM	1164	O	PRO	B	331	−64.265	43.259	−26.028	1.00	74.31	O
ATOM	1165	N	GLU	B	332	−62.191	42.757	−25.294	1.00	77.27	N
ATOM	1166	CA	GLU	B	332	−61.781	41.912	−26.398	1.00	77.53	C
ATOM	1167	CB	GLU	B	332	−60.258	41.718	−26.367	1.00	78.10	C
ATOM	1168	CG	GLU	B	332	−59.474	43.022	−26.258	1.00	81.67	C
ATOM	1169	CD	GLU	B	332	−59.396	43.680	−24.879	1.00	86.35	C
ATOM	1170	OE1	GLU	B	332	−59.799	43.043	−23.874	1.00	86.76	O
ATOM	1171	OE2	GLU	B	332	−58.924	44.841	−24.807	1.00	88.63	O
ATOM	1172	C	GLU	B	332	−62.503	40.562	−26.373	1.00	76.52	C
ATOM	1173	O	GLU	B	332	−62.771	39.986	−27.436	1.00	77.06	O
ATOM	1174	N	VAL	B	333	−62.818	40.060	−25.164	1.00	70.74	N
ATOM	1175	CA	VAL	B	333	−63.481	38.769	−24.964	1.00	68.74	C
ATOM	1176	CB	VAL	B	333	−63.067	38.120	−23.622	1.00	68.83	C
ATOM	1177	CG1	VAL	B	333	−61.556	38.105	−23.460	1.00	68.45	C
ATOM	1178	CG2	VAL	B	333	−63.708	38.838	−22.453	1.00	68.60	C
ATOM	1179	C	VAL	B	333	−64.993	38.873	−25.115	1.00	67.53	C
ATOM	1180	O	VAL	B	333	−65.553	39.955	−24.914	1.00	67.70	O
ATOM	1181	N	ILE	B	334	−65.654	37.763	−25.476	1.00	62.01	N
ATOM	1182	CA	ILE	B	334	−67.101	37.785	−25.621	1.00	60.41	C
ATOM	1183	CB	ILE	B	334	−67.598	36.945	−26.826	1.00	60.26	C
ATOM	1184	CG1	ILE	B	334	−67.270	37.654	−28.123	1.00	60.39	C
ATOM	1185	CD1	ILE	B	334	−66.925	36.721	−29.207	1.00	62.55	C
ATOM	1186	CG2	ILE	B	334	−69.098	36.676	−26.764	1.00	59.89	C
ATOM	1187	C	ILE	B	334	−67.676	37.401	−24.267	1.00	59.53	C
ATOM	1188	O	ILE	B	334	−67.498	36.266	−23.833	1.00	59.35	O
ATOM	1189	N	THR	B	335	−68.313	38.373	−23.578	1.00	57.48	N
ATOM	1190	CA	THR	B	335	−68.887	38.225	−22.242	1.00	56.89	C
ATOM	1191	CB	THR	B	335	−68.621	39.466	−21.384	1.00	56.86	C
ATOM	1192	OG1	THR	B	335	−67.231	39.840	−21.464	1.00	57.03	O
ATOM	1193	CG2	THR	B	335	−69.005	39.267	−19.945	1.00	56.65	C
ATOM	1194	C	THR	B	335	−70.320	37.833	−22.344	1.00	56.75	C
ATOM	1195	O	THR	B	335	−71.130	38.558	−22.901	1.00	56.71	O
ATOM	1196	N	VAL	B	336	−70.640	36.665	−21.808	1.00	55.91	N
ATOM	1197	CA	VAL	B	336	−71.988	36.106	−21.868	1.00	55.24	C
ATOM	1198	CB	VAL	B	336	−71.927	34.722	−22.551	1.00	55.29	C
ATOM	1199	CG1	VAL	B	336	−73.309	34.265	−22.994	1.00	55.31	C
ATOM	1200	CG2	VAL	B	336	−70.941	34.717	−23.721	1.00	55.00	C
ATOM	1201	C	VAL	B	336	−72.746	36.041	−20.532	1.00	55.10	C
ATOM	1202	O	VAL	B	336	−72.345	35.348	−19.588	1.00	54.55	O
ATOM	1203	N	GLY	B	337	−73.860	36.744	−20.491	1.00	54.20	N
ATOM	1204	CA	GLY	B	337	−74.765	36.737	−19.350	1.00	54.32	C
ATOM	1205	C	GLY	B	337	−75.665	35.524	−19.514	1.00	54.86	C
ATOM	1206	O	GLY	B	337	−75.630	34.863	−20.568	1.00	54.77	O
ATOM	1207	N	ALA	B	338	−76.478	35.199	−18.499	1.00	55.32	N
ATOM	1208	CA	ALA	B	338	−77.341	34.029	−18.609	1.00	55.65	C
ATOM	1209	CB	ALA	B	338	−76.927	32.989	−17.593	1.00	55.37	C
ATOM	1210	C	ALA	B	338	−78.802	34.362	−18.439	1.00	56.20	C
ATOM	1211	O	ALA	B	338	−79.153	35.135	−17.537	1.00	56.29	O
ATOM	1212	N	THR	B	339	−79.660	33.766	−19.304	1.00	57.13	N
ATOM	1213	CA	THR	B	339	−81.121	33.916	−19.264	1.00	57.44	C
ATOM	1214	CB	THR	B	339	−81.695	34.682	−20.460	1.00	57.24	C
ATOM	1215	OG1	THR	B	339	−81.399	33.995	−21.678	1.00	56.49	O
ATOM	1216	CG2	THR	B	339	−81.275	36.110	−20.491	1.00	57.07	C
ATOM	1217	C	THR	B	339	−81.804	32.556	−19.161	1.00	58.11	C
ATOM	1218	O	THR	B	339	−81.255	31.538	−19.589	1.00	58.12	O
ATOM	1219	N	ASN	B	340	−83.013	32.544	−18.609	1.00	61.87	N
ATOM	1220	CA	ASN	B	340	−83.762	31.311	−18.486	1.00	62.65	C
ATOM	1221	CB	ASN	B	340	−84.601	31.300	−17.235	1.00	62.41	C
ATOM	1222	CG	ASN	B	340	−85.516	32.464	−17.167	1.00	62.27	C
ATOM	1223	OD1	ASN	B	340	−86.269	32.767	−18.103	1.00	60.60	O
ATOM	1224	ND2	ASN	B	340	−85.447	33.145	−16.043	1.00	62.99	N
ATOM	1225	C	ASN	B	340	−84.609	31.019	−19.714	1.00	63.43	C
ATOM	1226	O	ASN	B	340	−84.453	31.674	−20.758	1.00	63.12	O
ATOM	1227	N	ALA	B	341	−85.494	29.995	−19.584	1.00	66.06	N
ATOM	1228	CA	ALA	B	341	−86.365	29.522	−20.647	1.00	67.26	C
ATOM	1229	CB	ALA	B	341	−87.083	28.264	−20.224	1.00	66.99	C
ATOM	1230	C	ALA	B	341	−87.329	30.561	−21.175	1.00	68.26	C
ATOM	1231	O	ALA	B	341	−87.692	30.499	−22.356	1.00	68.61	O
ATOM	1232	N	GLN	B	342	−87.703	31.537	−20.315	1.00	69.30	N
ATOM	1233	CA	GLN	B	342	−88.617	32.635	−20.628	1.00	70.34	C
ATOM	1234	CB	GLN	B	342	−89.531	32.965	−19.440	1.00	70.57	C
ATOM	1235	CG	GLN	B	342	−90.370	31.805	−18.937	1.00	72.94	C
ATOM	1236	CD	GLN	B	342	−89.597	30.971	−17.945	1.00	76.85	C
ATOM	1237	OE1	GLN	B	342	−89.030	31.481	−16.957	1.00	77.98	O
ATOM	1238	NE2	GLN	B	342	−89.547	29.660	−18.195	1.00	77.87	N
ATOM	1239	C	GLN	B	342	−87.824	33.860	−21.006	1.00	70.57	C
ATOM	1240	O	GLN	B	342	−88.361	34.961	−20.998	1.00	70.82	O
ATOM	1241	N	ASP	B	343	−86.543	33.673	−21.330	1.00	71.09	N
ATOM	1242	CA	ASP	B	343	−85.611	34.727	−21.727	1.00	71.24	C
ATOM	1243	CB	ASP	B	343	−85.893	35.218	−23.147	1.00	71.51	C
ATOM	1244	CG	ASP	B	343	−85.819	34.036	−24.078	1.00	74.17	C
ATOM	1245	OD1	ASP	B	343	−84.666	33.581	−24.392	1.00	76.97	O
ATOM	1246	OD2	ASP	B	343	−86.896	33.516	−24.459	1.00	78.55	O
ATOM	1247	C	ASP	B	343	−85.408	35.815	−20.705	1.00	70.72	C
ATOM	1248	O	ASP	B	343	−85.076	36.951	−21.036	1.00	70.59	O
ATOM	1249	N	GLN	B	344	−85.570	35.442	−19.442	1.00	67.52	N
ATOM	1250	CA	GLN	B	344	−85.422	36.350	−18.324	1.00	67.56	C
ATOM	1251	CB	GLN	B	344	−86.637	36.247	−17.404	1.00	67.61	C
ATOM	1252	CG	GLN	B	344	−87.911	36.741	−18.088	1.00	68.31	C
ATOM	1253	CD	GLN	B	344	−87.688	38.051	−18.840	1.00	70.11	C
ATOM	1254	OE1	GLN	B	344	−87.908	38.154	−20.067	1.00	68.92	O
ATOM	1255	NE2	GLN	B	344	−87.223	39.082	−18.113	1.00	71.30	N
ATOM	1256	C	GLN	B	344	−84.085	36.159	−17.625	1.00	67.41	C
ATOM	1257	O	GLN	B	344	−83.588	35.027	−17.597	1.00	67.29	O
ATOM	1258	N	PRO	B	345	−83.429	37.242	−17.131	1.00	66.24	N
ATOM	1259	CA	PRO	B	345	−82.117	37.052	−16.496	1.00	66.31	C
ATOM	1260	CB	PRO	B	345	−81.731	38.445	−16.016	1.00	66.17	C
ATOM	1261	CG	PRO	B	345	−82.587	39.369	−16.736	1.00	66.05	C
ATOM	1262	CD	PRO	B	345	−83.849	38.653	−17.080	1.00	66.08	C
ATOM	1263	C	PRO	B	345	−82.240	36.042	−15.371	1.00	66.57	C
ATOM	1264	O	PRO	B	345	−83.214	36.098	−14.591	1.00	66.73	O
ATOM	1265	N	VAL	B	346	−81.297	35.076	−15.336	1.00	67.36	N
ATOM	1266	CA	VAL	B	346	−81.278	33.987	−14.364	1.00	67.43	C
ATOM	1267	CB	VAL	B	346	−80.250	32.896	−14.756	1.00	67.44	C
ATOM	1268	CG1	VAL	B	346	−80.161	31.789	−13.712	1.00	67.51	C
ATOM	1269	CG2	VAL	B	346	−80.601	32.291	−16.095	1.00	67.50	C
ATOM	1270	C	VAL	B	346	−81.105	34.456	−12.936	1.00	67.73	C
ATOM	1271	O	VAL	B	346	−80.188	35.216	−12.646	1.00	67.53	O
ATOM	1272	N	THR	B	347	−81.994	33.994	−12.041	1.00	73.64	N
ATOM	1273	CA	THR	B	347	−81.890	34.274	−10.610	1.00	74.69	C
ATOM	1274	CB	THR	B	347	−83.182	34.813	−10.024	1.00	74.30	C
ATOM	1275	OG1	THR	B	347	−83.446	36.056	−10.662	1.00	74.34	O
ATOM	1276	CG2	THR	B	347	−83.080	35.038	−8.534	1.00	74.12	C
ATOM	1277	C	THR	B	347	−81.330	32.997	−9.955	1.00	75.60	C
ATOM	1278	O	THR	B	347	−81.999	31.954	−9.960	1.00	76.22	O
ATOM	1279	N	LEU	B	348	−80.064	33.083	−9.471	1.00	80.17	N
ATOM	1280	CA	LEU	B	348	−79.281	32.008	−8.826	1.00	80.74	C
ATOM	1281	CB	LEU	B	348	−77.863	31.912	−9.460	1.00	80.52	C
ATOM	1282	CG	LEU	B	348	−77.772	31.673	−10.954	1.00	80.04	C
ATOM	1283	CD1	LEU	B	348	−76.563	32.385	−11.548	1.00	78.71	C
ATOM	1284	CD2	LEU	B	348	−77.802	30.199	−11.271	1.00	80.04	C
ATOM	1285	C	LEU	B	348	−79.159	32.383	−7.349	1.00	81.10	C
ATOM	1286	O	LEU	B	348	−78.241	33.132	−6.972	1.00	81.74	O
ATOM	1287	N	GLY	B	349	−80.108	31.914	−6.545	1.00	80.68	N
ATOM	1288	CA	GLY	B	349	−80.145	32.243	−5.127	1.00	80.71	C
ATOM	1289	C	GLY	B	349	−80.483	33.700	−4.864	1.00	80.56	C
ATOM	1290	O	GLY	B	349	−81.431	34.254	−5.447	1.00	80.70	O
ATOM	1291	N	THR	B	350	−79.697	34.337	−3.978	1.00	80.62	N
ATOM	1292	CA	THR	B	350	−79.888	35.763	−3.619	1.00	80.69	C
ATOM	1293	CB	THR	B	350	−79.344	36.046	−2.201	1.00	80.96	C
ATOM	1294	OG1	THR	B	350	−77.978	35.604	−2.099	1.00	82.21	O
ATOM	1295	CG2	THR	B	350	−80.205	35.381	−1.117	1.00	81.74	C
ATOM	1296	C	THR	B	350	−79.277	36.677	−4.689	1.00	79.69	C
ATOM	1297	O	THR	B	350	−79.548	37.877	−4.748	1.00	79.91	O
ATOM	1298	N	LEU	B	351	−78.453	36.061	−5.531	1.00	74.98	N
ATOM	1299	CA	LEU	B	351	−77.746	36.657	−6.628	1.00	73.84	C
ATOM	1300	CB	LEU	B	351	−76.284	36.235	−6.512	1.00	74.24	C
ATOM	1301	CG	LEU	B	351	−75.557	36.676	−5.255	1.00	74.58	C
ATOM	1302	CD1	LEU	B	351	−74.238	36.009	−5.168	1.00	75.49	C
ATOM	1303	CD2	LEU	B	351	−75.356	38.179	−5.229	1.00	75.38	C
ATOM	1304	C	LEU	B	351	−78.381	36.247	−7.983	1.00	72.90	C
ATOM	1305	O	LEU	B	351	−79.607	36.113	−8.083	1.00	73.12	O
ATOM	1306	N	GLY	B	352	−77.553	36.090	−9.004	1.00	68.29	N
ATOM	1307	CA	GLY	B	352	−77.976	35.757	−10.354	1.00	66.37	C
ATOM	1308	C	GLY	B	352	−77.007	36.329	−11.365	1.00	65.12	C
ATOM	1309	O	GLY	B	352	−75.901	36.746	−10.992	1.00	64.78	O
ATOM	1310	N	THR	B	353	−77.407	36.367	−12.648	1.00	62.17	N
ATOM	1311	CA	THR	B	353	−76.532	36.867	−13.713	1.00	61.44	C
ATOM	1312	CB	THR	B	353	−77.124	36.662	−15.111	1.00	61.66	C
ATOM	1313	OG1	THR	B	353	−76.054	36.868	−16.040	1.00	61.54	O
ATOM	1314	CG2	THR	B	353	−78.303	37.631	−15.429	1.00	61.65	C
ATOM	1315	C	THR	B	353	−76.077	38.298	−13.587	1.00	61.03	C
ATOM	1316	O	THR	B	353	−76.855	39.160	−13.168	1.00	60.67	O
ATOM	1317	N	ASN	B	354	−74.824	38.558	−14.015	1.00	58.04	N
ATOM	1318	CA	ASN	B	354	−74.276	39.903	−14.038	1.00	57.12	C
ATOM	1319	CB	ASN	B	354	−72.749	39.874	−14.104	1.00	57.05	C
ATOM	1320	CG	ASN	B	354	−72.064	39.672	−12.776	1.00	56.66	C
ATOM	1321	OD1	ASN	B	354	−72.706	39.594	−11.736	1.00	57.85	O
ATOM	1322	ND2	ASN	B	354	−70.743	39.579	−12.765	1.00	55.21	N
ATOM	1323	C	ASN	B	354	−74.893	40.594	−15.265	1.00	57.09	C
ATOM	1324	O	ASN	B	354	−75.561	39.948	−16.068	1.00	56.51	O
ATOM	1325	N	PHE	B	355	−74.684	41.902	−15.396	1.00	58.97	N
ATOM	1326	CA	PHE	B	355	−75.226	42.761	−16.455	1.00	58.97	C
ATOM	1327	CB	PHE	B	355	−76.600	43.333	−15.984	1.00	58.89	C
ATOM	1328	CG	PHE	B	355	−76.642	43.671	−14.500	1.00	58.25	C
ATOM	1329	CD1	PHE	B	355	−77.335	42.862	−13.605	1.00	56.71	C
ATOM	1330	CE1	PHE	B	355	−77.323	43.140	−12.238	1.00	56.45	C
ATOM	1331	CZ	PHE	B	355	−76.618	44.223	−11.758	1.00	56.46	C
ATOM	1332	CE2	PHE	B	355	−75.933	45.039	−12.626	1.00	57.61	C
ATOM	1333	CD2	PHE	B	355	−75.922	44.753	−13.991	1.00	57.66	C
ATOM	1334	C	PHE	B	355	−74.251	43.911	−16.701	1.00	59.20	C
ATOM	1335	O	PHE	B	355	−73.104	43.883	−16.238	1.00	59.27	O
ATOM	1336	N	GLY	B	356	−74.725	44.932	−17.385	1.00	60.17	N
ATOM	1337	CA	GLY	B	356	−73.904	46.095	−17.649	1.00	60.92	C
ATOM	1338	C	GLY	B	356	−73.343	46.069	−19.034	1.00	61.66	C
ATOM	1339	O	GLY	B	356	−73.620	45.134	−19.790	1.00	61.68	O
ATOM	1340	N	ARG	B	357	−72.579	47.127	−19.367	1.00	64.73	N
ATOM	1341	CA	ARG	B	357	−71.935	47.380	−20.662	1.00	65.38	C
ATOM	1342	CB	ARG	B	357	−71.306	48.777	−20.705	1.00	65.63	C
ATOM	1343	CG	ARG	B	357	−70.518	49.113	−19.467	1.00	66.74	C
ATOM	1344	CD	ARG	B	357	−69.864	50.459	−19.552	1.00	68.76	C
ATOM	1345	NE	ARG	B	357	−68.612	50.445	−18.800	1.00	69.87	N
ATOM	1346	CZ	ARG	B	357	−67.437	50.189	−19.354	1.00	70.36	C
ATOM	1347	NH1	ARG	B	357	−67.346	49.960	−20.662	1.00	70.41	N
ATOM	1348	NH2	ARG	B	357	−66.340	50.161	−18.608	1.00	71.53	N
ATOM	1349	C	ARG	B	357	−70.919	46.329	−21.055	1.00	65.47	C
ATOM	1350	O	ARG	B	357	−70.777	46.056	−22.249	1.00	65.45	O
ATOM	1351	N	CYS	B	358	−70.244	45.716	−20.067	1.00	67.67	N
ATOM	1352	CA	CYS	B	358	−69.251	44.680	−20.337	1.00	68.19	C
ATOM	1353	CB	CYS	B	358	−68.303	44.504	−19.162	1.00	68.27	C
ATOM	1354	SG	CYS	B	358	−67.381	46.018	−18.746	1.00	70.93	S
ATOM	1355	C	CYS	B	358	−69.827	43.353	−20.848	1.00	68.00	C
ATOM	1356	O	CYS	B	358	−69.128	42.613	−21.543	1.00	68.04	O
ATOM	1357	N	VAL	B	359	−71.118	43.091	−20.558	1.00	67.04	N
ATOM	1358	CA	VAL	B	359	−71.850	41.916	−21.035	1.00	66.98	C
ATOM	1359	CB	VAL	B	359	−73.146	41.644	−20.231	1.00	66.79	C
ATOM	1360	CG1	VAL	B	359	−73.978	40.544	−20.865	1.00	66.32	C
ATOM	1361	CG2	VAL	B	359	−72.828	41.290	−18.800	1.00	66.58	C
ATOM	1362	C	VAL	B	359	−72.156	42.215	−22.506	1.00	67.34	C
ATOM	1363	O	VAL	B	359	−72.738	43.273	−22.817	1.00	68.24	O
ATOM	1364	N	ASP	B	360	−71.728	41.309	−23.407	1.00	67.45	N
ATOM	1365	CA	ASP	B	360	−71.927	41.451	−24.838	1.00	67.13	C
ATOM	1366	CB	ASP	B	360	−70.766	40.803	−25.610	1.00	67.44	C
ATOM	1367	CG	ASP	B	360	−69.434	41.534	−25.368	1.00	70.71	C
ATOM	1368	OD1	ASP	B	360	−69.374	42.758	−25.618	1.00	74.94	O
ATOM	1369	OD2	ASP	B	360	−68.444	40.878	−24.919	1.00	73.47	O
ATOM	1370	C	ASP	B	360	−73.303	40.935	−25.240	1.00	66.55	C
ATOM	1371	O	ASP	B	360	−73.968	41.539	−26.091	1.00	66.82	O
ATOM	1372	N	LEU	B	361	−73.754	39.849	−24.602	1.00	62.14	N
ATOM	1373	CA	LEU	B	361	−75.047	39.220	−24.876	1.00	61.50	C
ATOM	1374	CB	LEU	B	361	−75.059	38.557	−26.280	1.00	61.27	C
ATOM	1375	CG	LEU	B	361	−74.367	37.179	−26.492	1.00	61.28	C
ATOM	1376	CD1	LEU	B	361	−74.698	36.631	−27.854	1.00	60.90	C
ATOM	1377	CD2	LEU	B	361	−72.831	37.244	−26.309	1.00	60.87	C
ATOM	1378	C	LEU	B	361	−75.373	38.192	−23.815	1.00	61.29	C
ATOM	1379	O	LEU	B	361	−74.502	37.803	−23.045	1.00	61.49	O
ATOM	1380	N	PHE	B	362	−76.611	37.747	−23.789	1.00	61.00	N
ATOM	1381	CA	PHE	B	362	−77.075	36.747	−22.863	1.00	61.06	C
ATOM	1382	CB	PHE	B	362	−78.384	37.205	−22.234	1.00	60.86	C
ATOM	1383	CG	PHE	B	362	−78.173	38.342	−21.274	1.00	60.86	C
ATOM	1384	CD1	PHE	B	362	−78.162	38.120	−19.906	1.00	59.91	C
ATOM	1385	CE1	PHE	B	362	−77.950	39.175	−19.018	1.00	58.68	C
ATOM	1386	CZ	PHE	B	362	−77.733	40.449	−19.495	1.00	58.51	C
ATOM	1387	CE2	PHE	B	362	−77.725	40.689	−20.847	1.00	59.36	C
ATOM	1388	CD2	PHE	B	362	−77.951	39.637	−21.737	1.00	61.08	C
ATOM	1389	C	PHE	B	362	−77.261	35.479	−23.667	1.00	61.49	C
ATOM	1390	O	PHE	B	362	−77.217	35.536	−24.895	1.00	61.81	O
ATOM	1391	N	ALA	B	363	−77.445	34.343	−23.003	1.00	62.20	N
ATOM	1392	CA	ALA	B	363	−77.624	33.047	−23.648	1.00	62.13	C
ATOM	1393	CB	ALA	B	363	−76.264	32.485	−24.055	1.00	62.04	C
ATOM	1394	C	ALA	B	363	−78.261	32.122	−22.617	1.00	62.26	C
ATOM	1395	O	ALA	B	363	−78.217	32.436	−21.416	1.00	62.48	O
ATOM	1396	N	PRO	B	364	−78.824	30.971	−23.028	1.00	60.56	N
ATOM	1397	CA	PRO	B	364	−79.418	30.053	−22.046	1.00	60.70	C
ATOM	1398	CB	PRO	B	364	−79.785	28.853	−22.896	1.00	60.33	C
ATOM	1399	CG	PRO	B	364	−79.975	29.394	−24.223	1.00	59.88	C
ATOM	1400	CD	PRO	B	364	−78.984	30.455	−24.396	1.00	60.34	C
ATOM	1401	C	PRO	B	364	−78.468	29.647	−20.917	1.00	61.27	C
ATOM	1402	O	PRO	B	364	−77.380	29.150	−21.194	1.00	61.78	O
ATOM	1403	N	GLY	B	365	−78.885	29.866	−19.666	1.00	63.45	N
ATOM	1404	CA	GLY	B	365	−78.091	29.540	−18.481	1.00	63.91	C
ATOM	1405	C	GLY	B	365	−78.856	29.033	−17.268	1.00	64.44	C
ATOM	1406	O	GLY	B	365	−78.378	29.171	−16.142	1.00	64.33	O
ATOM	1407	N	GLU	B	366	−80.033	28.444	−17.474	1.00	66.98	N
ATOM	1408	CA	GLU	B	366	−80.819	27.923	−16.367	1.00	68.00	C
ATOM	1409	CB	GLU	B	366	−81.943	28.894	−15.962	1.00	68.37	C
ATOM	1410	CG	GLU	B	366	−82.522	28.588	−14.592	1.00	71.56	C
ATOM	1411	CD	GLU	B	366	−83.672	29.463	−14.135	1.00	76.80	C
ATOM	1412	OE1	GLU	B	366	−83.399	30.568	−13.599	1.00	79.89	O
ATOM	1413	OE2	GLU	B	366	−84.845	29.045	−14.306	1.00	78.54	O
ATOM	1414	C	GLU	B	366	−81.388	26.570	−16.715	1.00	67.88	C
ATOM	1415	O	GLU	B	366	−81.985	26.415	−17.777	1.00	67.93	O
ATOM	1416	N	ASP	B	367	−81.234	25.598	−15.799	1.00	68.26	N
ATOM	1417	CA	ASP	B	367	−81.717	24.241	−15.963	1.00	68.38	C
ATOM	1418	CB	ASP	B	367	−83.232	24.160	−15.669	1.00	69.02	C
ATOM	1419	CG	ASP	B	367	−84.035	23.000	−16.269	1.00	72.86	C
ATOM	1420	OD1	ASP	B	367	−83.614	21.803	−16.083	1.00	77.07	O
ATOM	1421	OD2	ASP	B	367	−85.099	23.275	−16.919	1.00	76.42	O
ATOM	1422	C	ASP	B	367	−81.239	23.723	−17.325	1.00	67.72	C
ATOM	1423	O	ASP	B	367	−82.011	23.400	−18.220	1.00	67.13	O
ATOM	1424	N	ILE	B	368	−79.919	23.728	−17.483	1.00	64.65	N
ATOM	1425	CA	ILE	B	368	−79.262	23.289	−18.692	1.00	64.75	C
ATOM	1426	CB	ILE	B	368	−78.073	24.205	−19.070	1.00	64.52	C
ATOM	1427	CG1	ILE	B	368	−78.462	25.700	−19.157	1.00	64.19	C
ATOM	1428	CD1	ILE	B	368	−79.483	26.137	−20.261	1.00	63.84	C
ATOM	1429	CG2	ILE	B	368	−77.334	23.692	−20.320	1.00	63.95	C
ATOM	1430	C	ILE	B	368	−78.851	21.836	−18.541	1.00	65.40	C
ATOM	1431	O	ILE	B	368	−77.982	21.492	−17.728	1.00	65.45	O
ATOM	1432	N	ILE	B	369	−79.479	20.983	−19.342	1.00	68.85	N
ATOM	1433	CA	ILE	B	369	−79.184	19.564	−19.310	1.00	69.23	C
ATOM	1434	CB	ILE	B	369	−80.406	18.721	−19.759	1.00	69.28	C
ATOM	1435	CG1	ILE	B	369	−80.376	17.337	−19.141	1.00	70.78	C
ATOM	1436	CD1	ILE	B	369	−80.909	17.246	−17.682	1.00	73.48	C
ATOM	1437	CG2	ILE	B	369	−80.594	18.651	−21.256	1.00	69.21	C
ATOM	1438	C	ILE	B	369	−77.888	19.296	−20.049	1.00	69.27	C
ATOM	1439	O	ILE	B	369	−77.704	19.817	−21.152	1.00	69.70	O
ATOM	1440	N	GLY	B	370	−76.991	18.544	−19.414	1.00	67.64	N
ATOM	1441	CA	GLY	B	370	−75.678	18.200	−19.957	1.00	67.43	C
ATOM	1442	C	GLY	B	370	−74.966	17.113	−19.179	1.00	67.40	C
ATOM	1443	O	GLY	B	370	−75.383	16.770	−18.075	1.00	67.49	O
ATOM	1444	N	ALA	B	371	−73.878	16.575	−19.748	1.00	67.13	N
ATOM	1445	CA	ALA	B	371	−73.044	15.510	−19.191	1.00	66.88	C
ATOM	1446	CB	ALA	B	371	−71.784	15.340	−20.020	1.00	66.63	C
ATOM	1447	C	ALA	B	371	−72.685	15.559	−17.699	1.00	67.05	C
ATOM	1448	O	ALA	B	371	−71.899	16.414	−17.248	1.00	67.24	O
ATOM	1449	N	SER	B	372	−73.234	14.587	−16.935	1.00	69.52	N
ATOM	1450	CA	SER	B	372	−72.948	14.425	−15.507	1.00	69.69	C
ATOM	1451	CB	SER	B	372	−74.163	13.888	−14.773	1.00	69.34	C
ATOM	1452	OG	SER	B	372	−73.778	13.661	−13.432	1.00	68.66	O
ATOM	1453	C	SER	B	372	−71.789	13.435	−15.337	1.00	70.18	C
ATOM	1454	O	SER	B	372	−71.873	12.313	−15.834	1.00	70.36	O
ATOM	1455	N	SER	B	373	−70.712	13.842	−14.640	1.00	74.56	N
ATOM	1456	CA	SER	B	373	−69.540	12.991	−14.390	1.00	74.78	C
ATOM	1457	CB	SER	B	373	−68.397	13.804	−13.788	1.00	74.54	C
ATOM	1458	OG	SER	B	373	−68.850	14.486	−12.629	1.00	74.19	O
ATOM	1459	C	SER	B	373	−69.893	11.784	−13.489	1.00	75.14	C
ATOM	1460	O	SER	B	373	−69.060	10.880	−13.352	1.00	75.75	O
ATOM	1461	N	ASP	B	374	−71.121	11.761	−12.898	1.00	76.21	N
ATOM	1462	CA	ASP	B	374	−71.622	10.677	−12.050	1.00	76.51	C
ATOM	1463	CB	ASP	B	374	−73.078	10.926	−11.658	1.00	76.87	C
ATOM	1464	CG	ASP	B	374	−73.278	11.831	−10.456	1.00	77.21	C
ATOM	1465	OD1	ASP	B	374	−72.258	12.144	−9.768	1.00	77.96	O
ATOM	1466	OD2	ASP	B	374	−74.471	12.237	−10.193	1.00	76.93	O
ATOM	1467	C	ASP	B	374	−71.489	9.273	−12.686	1.00	76.86	C
ATOM	1468	O	ASP	B	374	−71.069	8.341	−11.998	1.00	77.61	O
ATOM	1469	N	CYS	B	375	−71.848	9.121	−13.977	1.00	73.83	N
ATOM	1470	CA	CYS	B	375	−71.746	7.884	−14.756	1.00	73.51	C
ATOM	1471	CB	CYS	B	375	−72.947	6.965	−14.529	1.00	73.63	C
ATOM	1472	SG	CYS	B	375	−74.337	7.199	−15.678	1.00	76.02	S
ATOM	1473	C	CYS	B	375	−71.561	8.290	−16.221	1.00	73.03	C
ATOM	1474	O	CYS	B	375	−71.981	9.388	−16.577	1.00	73.09	O
ATOM	1475	N	SER	B	376	−70.912	7.455	−17.064	1.00	68.20	N
ATOM	1476	CA	SER	B	376	−70.627	7.806	−18.467	1.00	67.70	C
ATOM	1477	CB	SER	B	376	−69.542	6.924	−19.071	1.00	67.82	C
ATOM	1478	OG	SER	B	376	−70.072	5.678	−19.480	1.00	68.81	O
ATOM	1479	C	SER	B	376	−71.787	8.094	−19.439	1.00	67.35	C
ATOM	1480	O	SER	B	376	−71.529	8.558	−20.554	1.00	66.71	O
ATOM	1481	N	THR	B	377	−73.055	7.869	−19.012	1.00	66.32	N
ATOM	1482	CA	THR	B	377	−74.239	8.165	−19.829	1.00	66.42	C
ATOM	1483	CB	THR	B	377	−74.876	6.901	−20.383	1.00	66.19	C
ATOM	1484	OG1	THR	B	377	−75.281	6.064	−19.314	1.00	65.85	O
ATOM	1485	CG2	THR	B	377	−73.982	6.162	−21.326	1.00	66.15	C
ATOM	1486	C	THR	B	377	−75.243	9.045	−19.074	1.00	66.82	C
ATOM	1487	O	THR	B	377	−76.346	9.295	−19.570	1.00	67.04	O
ATOM	1488	N	CYS	B	378	−74.857	9.523	−17.882	1.00	69.75	N
ATOM	1489	CA	CYS	B	378	−75.691	10.360	−17.010	1.00	70.60	C
ATOM	1490	CB	CYS	B	378	−75.242	10.253	−15.553	1.00	70.72	C
ATOM	1491	SG	CYS	B	378	−75.535	8.635	−14.779	1.00	76.79	S
ATOM	1492	C	CYS	B	378	−75.737	11.815	−17.436	1.00	69.95	C
ATOM	1493	O	CYS	B	378	−74.714	12.384	−17.826	1.00	69.93	O
ATOM	1494	N	PHE	B	379	−76.914	12.435	−17.273	1.00	68.10	N
ATOM	1495	CA	PHE	B	379	−77.121	13.845	−17.529	1.00	67.31	C
ATOM	1496	CB	PHE	B	379	−78.233	14.050	−18.545	1.00	67.28	C
ATOM	1497	CG	PHE	B	379	−77.766	13.764	−19.933	1.00	67.51	C
ATOM	1498	CD1	PHE	B	379	−77.097	14.732	−20.668	1.00	67.75	C
ATOM	1499	CE1	PHE	B	379	−76.638	14.459	−21.959	1.00	67.92	C
ATOM	1500	CZ	PHE	B	379	−76.858	13.219	−22.517	1.00	68.53	C
ATOM	1501	CE2	PHE	B	379	−77.516	12.243	−21.796	1.00	69.39	C
ATOM	1502	CD2	PHE	B	379	−77.972	12.519	−20.505	1.00	68.25	C
ATOM	1503	C	PHE	B	379	−77.485	14.553	−16.242	1.00	66.84	C
ATOM	1504	O	PHE	B	379	−78.048	13.957	−15.328	1.00	66.88	O
ATOM	1505	N	VAL	B	380	−77.182	15.831	−16.174	1.00	66.05	N
ATOM	1506	CA	VAL	B	380	−77.512	16.661	−15.029	1.00	65.75	C
ATOM	1507	CB	VAL	B	380	−76.405	16.742	−13.944	1.00	65.44	C
ATOM	1508	CG1	VAL	B	380	−75.179	17.514	−14.436	1.00	65.48	C
ATOM	1509	CG2	VAL	B	380	−76.945	17.343	−12.653	1.00	64.28	C
ATOM	1510	C	VAL	B	380	−77.930	18.021	−15.542	1.00	65.90	C
ATOM	1511	O	VAL	B	380	−77.429	18.493	−16.573	1.00	66.20	O
ATOM	1512	N	SER	B	381	−78.840	18.649	−14.816	1.00	65.11	N
ATOM	1513	CA	SER	B	381	−79.308	19.958	−15.153	1.00	64.86	C
ATOM	1514	CB	SER	B	381	−80.818	20.000	−14.994	1.00	64.84	C
ATOM	1515	OG	SER	B	381	−81.278	21.322	−14.804	1.00	65.85	O
ATOM	1516	C	SER	B	381	−78.584	20.962	−14.261	1.00	64.52	C
ATOM	1517	O	SER	B	381	−78.762	20.938	−13.051	1.00	64.12	O
ATOM	1518	N	GLN	B	382	−77.738	21.818	−14.859	1.00	65.97	N
ATOM	1519	CA	GLN	B	382	−76.989	22.857	−14.125	1.00	66.38	C
ATOM	1520	CB	GLN	B	382	−75.483	22.638	−14.200	1.00	66.64	C
ATOM	1521	CG	GLN	B	382	−75.010	21.530	−13.285	1.00	68.46	C
ATOM	1522	CD	GLN	B	382	−73.504	21.374	−13.324	1.00	71.37	C
ATOM	1523	OE1	GLN	B	382	−72.728	22.346	−13.165	1.00	73.24	O
ATOM	1524	NE2	GLN	B	382	−73.052	20.136	−13.508	1.00	71.55	N
ATOM	1525	C	GLN	B	382	−77.347	24.270	−14.559	1.00	65.83	C
ATOM	1526	O	GLN	B	382	−78.046	24.421	−15.560	1.00	66.06	O
ATOM	1527	N	SER	B	383	−76.907	25.303	−13.804	1.00	64.06	N
ATOM	1528	CA	SER	B	383	−77.200	26.709	−14.136	1.00	63.37	C
ATOM	1529	CB	SER	B	383	−78.417	27.208	−13.363	1.00	63.26	C
ATOM	1530	OG	SER	B	383	−79.509	26.312	−13.464	1.00	63.66	O
ATOM	1531	C	SER	B	383	−76.005	27.650	−13.911	1.00	62.65	C
ATOM	1532	O	SER	B	383	−75.120	27.339	−13.109	1.00	63.21	O
ATOM	1533	N	GLY	B	384	−75.972	28.782	−14.610	1.00	61.71	N
ATOM	1534	CA	GLY	B	384	−74.884	29.739	−14.426	1.00	60.72	C
ATOM	1535	C	GLY	B	384	−74.402	30.424	−15.675	1.00	60.19	C
ATOM	1536	O	GLY	B	384	−74.737	30.001	−16.775	1.00	60.26	O
ATOM	1537	N	THR	B	385	−73.606	31.484	−15.527	1.00	60.84	N
ATOM	1538	CA	THR	B	385	−73.095	32.176	−16.696	1.00	60.30	C
ATOM	1539	CB	THR	B	385	−72.612	33.595	−16.392	1.00	60.29	C
ATOM	1540	OG1	THR	B	385	−71.719	33.599	−15.282	1.00	60.49	O
ATOM	1541	CG2	THR	B	385	−73.734	34.539	−16.152	1.00	60.32	C
ATOM	1542	C	THR	B	385	−72.096	31.285	−17.414	1.00	60.14	C
ATOM	1543	O	THR	B	385	−71.858	31.498	−18.600	1.00	60.76	O
ATOM	1544	N	SER	B	386	−71.538	30.259	−16.718	1.00	59.68	N
ATOM	1545	CA	SER	B	386	−70.610	29.290	−17.308	1.00	58.69	C
ATOM	1546	CB	SER	B	386	−70.208	28.255	−16.276	1.00	58.66	C
ATOM	1547	OG	SER	B	386	−69.090	28.756	−15.570	1.00	59.58	O
ATOM	1548	C	SER	B	386	−71.328	28.575	−18.415	1.00	58.08	C
ATOM	1549	O	SER	B	386	−70.886	28.598	−19.560	1.00	57.08	O
ATOM	1550	N	GLN	B	387	−72.474	27.969	−18.068	1.00	57.98	N
ATOM	1551	CA	GLN	B	387	−73.350	27.253	−18.974	1.00	58.10	C
ATOM	1552	CB	GLN	B	387	−74.580	26.756	−18.211	1.00	58.10	C
ATOM	1553	CG	GLN	B	387	−74.321	25.450	−17.479	1.00	59.28	C
ATOM	1554	CD	GLN	B	387	−73.438	25.567	−16.264	1.00	62.12	C
ATOM	1555	OE1	GLN	B	387	−73.404	26.591	−15.573	1.00	64.35	O
ATOM	1556	NE2	GLN	B	387	−72.688	24.512	−15.964	1.00	63.82	N
ATOM	1557	C	GLN	B	387	−73.706	28.133	−20.185	1.00	57.84	C
ATOM	1558	O	GLN	B	387	−73.647	27.665	−21.320	1.00	57.46	O
ATOM	1559	N	ALA	B	388	−73.996	29.413	−19.940	1.00	57.44	N
ATOM	1560	CA	ALA	B	388	−74.321	30.379	−20.971	1.00	57.87	C
ATOM	1561	CB	ALA	B	388	−74.751	31.670	−20.321	1.00	58.03	C
ATOM	1562	C	ALA	B	388	−73.137	30.628	−21.913	1.00	58.24	C
ATOM	1563	O	ALA	B	388	−73.307	30.586	−23.137	1.00	58.05	O
ATOM	1564	N	ALA	B	389	−71.932	30.874	−21.330	1.00	59.19	N
ATOM	1565	CA	ALA	B	389	−70.680	31.119	−22.054	1.00	59.09	C
ATOM	1566	CB	ALA	B	389	−69.537	31.386	−21.083	1.00	58.69	C
ATOM	1567	C	ALA	B	389	−70.379	29.920	−22.949	1.00	59.41	C
ATOM	1568	O	ALA	B	389	−70.090	30.121	−24.127	1.00	59.39	O
ATOM	1569	N	ALA	B	390	−70.536	28.675	−22.417	1.00	59.10	N
ATOM	1570	CA	ALA	B	390	−70.335	27.416	−23.148	1.00	59.27	C
ATOM	1571	CB	ALA	B	390	−70.634	26.231	−22.246	1.00	59.50	C
ATOM	1572	C	ALA	B	390	−71.223	27.368	−24.389	1.00	59.18	C
ATOM	1573	O	ALA	B	390	−70.762	27.016	−25.465	1.00	58.96	O
ATOM	1574	N	HIS	B	391	−72.466	27.771	−24.245	1.00	59.70	N
ATOM	1575	CA	HIS	B	391	−73.437	27.824	−25.327	1.00	60.45	C
ATOM	1576	CB	HIS	B	391	−74.748	28.343	−24.754	1.00	60.64	C
ATOM	1577	CG	HIS	B	391	−75.881	28.349	−25.711	1.00	61.44	C
ATOM	1578	ND1	HIS	B	391	−76.895	27.390	−25.638	1.00	62.58	N
ATOM	1579	CE1	HIS	B	391	−77.758	27.717	−26.591	1.00	62.78	C
ATOM	1580	NE2	HIS	B	391	−77.364	28.815	−27.263	1.00	61.77	N
ATOM	1581	CD2	HIS	B	391	−76.170	29.229	−26.701	1.00	60.82	C
ATOM	1582	C	HIS	B	391	−72.941	28.752	−26.446	1.00	60.78	C
ATOM	1583	O	HIS	B	391	−73.011	28.394	−27.626	1.00	60.82	O
ATOM	1584	N	VAL	B	392	−72.431	29.940	−26.073	1.00	60.26	N
ATOM	1585	CA	VAL	B	392	−71.934	30.895	−27.048	1.00	60.56	C
ATOM	1586	CB	VAL	B	392	−71.837	32.337	−26.501	1.00	60.49	C
ATOM	1587	CG1	VAL	B	392	−70.866	33.192	−27.316	1.00	59.89	C
ATOM	1588	CG2	VAL	B	392	−73.219	32.987	−26.456	1.00	60.00	C
ATOM	1589	C	VAL	B	392	−70.675	30.361	−27.706	1.00	60.89	C
ATOM	1590	O	VAL	B	392	−70.504	30.544	−28.910	1.00	61.08	O
ATOM	1591	N	ALA	B	393	−69.822	29.658	−26.943	1.00	60.20	N
ATOM	1592	CA	ALA	B	393	−68.610	29.042	−27.496	1.00	60.46	C
ATOM	1593	CB	ALA	B	393	−67.728	28.480	−26.381	1.00	60.29	C
ATOM	1594	C	ALA	B	393	−69.051	27.932	−28.506	1.00	60.76	C
ATOM	1595	O	ALA	B	393	−68.423	27.773	−29.542	1.00	60.67	O
ATOM	1596	N	GLY	B	394	−70.158	27.237	−28.218	1.00	60.47	N
ATOM	1597	CA	GLY	B	394	−70.731	26.231	−29.105	1.00	60.83	C
ATOM	1598	C	GLY	B	394	−71.095	26.913	−30.409	1.00	61.49	C
ATOM	1599	O	GLY	B	394	−70.561	26.545	−31.452	1.00	61.48	O
ATOM	1600	N	ILE	B	395	−71.940	27.986	−30.350	1.00	59.97	N
ATOM	1601	CA	ILE	B	395	−72.324	28.798	−31.517	1.00	60.21	C
ATOM	1602	CB	ILE	B	395	−73.238	29.997	−31.149	1.00	59.85	C
ATOM	1603	CG1	ILE	B	395	−74.560	29.509	−30.540	1.00	59.07	C
ATOM	1604	CD1	ILE	B	395	−75.597	30.517	−30.318	1.00	56.08	C
ATOM	1605	CG2	ILE	B	395	−73.496	30.836	−32.396	1.00	58.99	C
ATOM	1606	C	ILE	B	395	−71.075	29.268	−32.270	1.00	60.82	C
ATOM	1607	O	ILE	B	395	−70.963	29.023	−33.459	1.00	60.79	O
ATOM	1608	N	ALA	B	396	−70.132	29.901	−31.572	1.00	62.66	N
ATOM	1609	CA	ALA	B	396	−68.893	30.389	−32.166	1.00	63.99	C
ATOM	1610	CB	ALA	B	396	−67.994	30.993	−31.104	1.00	63.67	C
ATOM	1611	C	ALA	B	396	−68.144	29.297	−32.910	1.00	65.18	C
ATOM	1612	O	ALA	B	396	−67.522	29.590	−33.929	1.00	65.64	O
ATOM	1613	N	ALA	B	397	−68.192	28.046	−32.420	1.00	66.67	N
ATOM	1614	CA	ALA	B	397	−67.481	26.966	−33.077	1.00	67.47	C
ATOM	1615	CB	ALA	B	397	−67.364	25.760	−32.167	1.00	67.14	C
ATOM	1616	C	ALA	B	397	−68.193	26.611	−34.351	1.00	68.29	C
ATOM	1617	O	ALA	B	397	−67.538	26.383	−35.358	1.00	68.46	O
ATOM	1618	N	MET	B	398	−69.518	26.615	−34.346	1.00	70.12	N
ATOM	1619	CA	MET	B	398	−70.253	26.291	−35.562	1.00	71.55	C
ATOM	1620	CB	MET	B	398	−71.707	26.108	−35.259	1.00	71.19	C
ATOM	1621	CG	MET	B	398	−72.011	24.717	−34.979	1.00	71.23	C
ATOM	1622	SD	MET	B	398	−73.527	24.713	−34.090	1.00	72.01	S
ATOM	1623	CE	MET	B	398	−74.705	24.947	−35.431	1.00	72.24	C
ATOM	1624	C	MET	B	398	−70.068	27.307	−36.668	1.00	72.80	C
ATOM	1625	O	MET	B	398	−70.022	26.937	−37.845	1.00	73.11	O
ATOM	1626	N	MET	B	399	−69.950	28.584	−36.276	1.00	75.45	N
ATOM	1627	CA	MET	B	399	−69.737	29.715	−37.153	1.00	76.60	C
ATOM	1628	CB	MET	B	399	−69.784	30.998	−36.335	1.00	76.93	C
ATOM	1629	CG	MET	B	399	−71.138	31.385	−35.885	1.00	78.25	C
ATOM	1630	SD	MET	B	399	−71.060	33.142	−35.460	1.00	81.74	S
ATOM	1631	CE	MET	B	399	−72.769	33.407	−35.066	1.00	81.33	C
ATOM	1632	C	MET	B	399	−68.353	29.584	−37.760	1.00	77.22	C
ATOM	1633	O	MET	B	399	−68.220	29.669	−38.974	1.00	77.23	O
ATOM	1634	N	LEU	B	400	−67.325	29.365	−36.915	1.00	76.33	N
ATOM	1635	CA	LEU	B	400	−65.936	29.226	−37.346	1.00	77.44	C
ATOM	1636	CB	LEU	B	400	−64.965	29.365	−36.170	1.00	77.12	C
ATOM	1637	CG	LEU	B	400	−64.811	30.729	−35.539	1.00	76.49	C
ATOM	1638	CD1	LEU	B	400	−64.013	30.617	−34.295	1.00	76.33	C
ATOM	1639	CD2	LEU	B	400	−64.101	31.702	−36.459	1.00	75.61	C
ATOM	1640	C	LEU	B	400	−65.679	27.928	−38.104	1.00	78.55	C
ATOM	1641	O	LEU	B	400	−64.640	27.811	−38.754	1.00	78.47	O
ATOM	1642	N	SER	B	401	−66.614	26.951	−38.008	1.00	83.21	N
ATOM	1643	CA	SER	B	401	−66.532	25.676	−38.712	1.00	84.86	C
ATOM	1644	CB	SER	B	401	−67.538	24.675	−38.161	1.00	85.02	C
ATOM	1645	OG	SER	B	401	−66.854	23.694	−37.400	1.00	86.31	O
ATOM	1646	C	SER	B	401	−66.806	25.932	−40.171	1.00	85.71	C
ATOM	1647	O	SER	B	401	−66.036	25.489	−41.022	1.00	85.97	O
ATOM	1648	N	ALA	B	402	−67.881	26.692	−40.453	1.00	87.49	N
ATOM	1649	CA	ALA	B	402	−68.301	27.071	−41.792	1.00	88.50	C
ATOM	1650	CB	ALA	B	402	−69.740	27.534	−41.756	1.00	88.32	C
ATOM	1651	C	ALA	B	402	−67.408	28.157	−42.437	1.00	89.39	C
ATOM	1652	O	ALA	B	402	−67.193	28.122	−43.651	1.00	90.05	O
ATOM	1653	N	GLU	B	403	−66.905	29.121	−41.654	1.00	88.89	N
ATOM	1654	CA	GLU	B	403	−66.093	30.194	−42.210	1.00	89.62	C
ATOM	1655	CB	GLU	B	403	−66.934	31.483	−42.301	1.00	89.85	C
ATOM	1656	CG	GLU	B	403	−68.060	31.403	−43.317	1.00	91.79	C
ATOM	1657	CD	GLU	B	403	−69.147	32.466	−43.267	1.00	94.98	C
ATOM	1658	OE1	GLU	B	403	−70.339	32.075	−43.285	1.00	96.52	O
ATOM	1659	OE2	GLU	B	403	−68.822	33.679	−43.231	1.00	95.76	O
ATOM	1660	C	GLU	B	403	−64.809	30.399	−41.401	1.00	89.80	C
ATOM	1661	O	GLU	B	403	−64.673	31.415	−40.722	1.00	89.82	O
ATOM	1662	N	PRO	B	404	−63.837	29.467	−41.471	1.00	88.89	N
ATOM	1663	CA	PRO	B	404	−62.587	29.614	−40.692	1.00	89.06	C
ATOM	1664	CB	PRO	B	404	−61.704	28.485	−41.210	1.00	88.92	C
ATOM	1665	CG	PRO	B	404	−62.379	27.990	−42.431	1.00	89.10	C
ATOM	1666	CD	PRO	B	404	−63.827	28.207	−42.225	1.00	88.89	C
ATOM	1667	C	PRO	B	404	−61.843	30.937	−40.746	1.00	89.38	C
ATOM	1668	O	PRO	B	404	−61.071	31.243	−39.833	1.00	89.29	O
ATOM	1669	N	GLU	B	405	−62.077	31.724	−41.800	1.00	94.03	N
ATOM	1670	CA	GLU	B	405	−61.424	33.021	−41.962	1.00	94.48	C
ATOM	1671	CB	GLU	B	405	−60.953	33.222	−43.414	1.00	94.82	C
ATOM	1672	CG	GLU	B	405	−59.644	32.488	−43.697	1.00	97.73	C
ATOM	1673	CD	GLU	B	405	−59.402	32.015	−45.125	1.00	102.06	C
ATOM	1674	OE1	GLU	B	405	−59.461	32.859	−46.057	1.00	103.17	O
ATOM	1675	OE2	GLU	B	405	−59.138	30.798	−45.309	1.00	103.58	O
ATOM	1676	C	GLU	B	405	−62.212	34.217	−41.358	1.00	93.93	C
ATOM	1677	O	GLU	B	405	−61.967	35.374	−41.720	1.00	94.12	O
ATOM	1678	N	LEU	B	406	−63.146	33.927	−40.414	1.00	90.47	N
ATOM	1679	CA	LEU	B	406	−63.928	34.956	−39.725	1.00	89.50	C
ATOM	1680	CB	LEU	B	406	−65.167	34.369	−39.024	1.00	89.48	C
ATOM	1681	CG	LEU	B	406	−66.506	34.396	−39.753	1.00	88.84	C
ATOM	1682	CD1	LEU	B	406	−67.483	33.473	−39.089	1.00	88.84	C
ATOM	1683	CD2	LEU	B	406	−67.102	35.767	−39.764	1.00	87.85	C
ATOM	1684	C	LEU	B	406	−63.031	35.560	−38.669	1.00	89.00	C
ATOM	1685	O	LEU	B	406	−62.284	34.841	−37.990	1.00	89.04	O
ATOM	1686	N	THR	B	407	−63.094	36.872	−38.523	1.00	88.63	N
ATOM	1687	CA	THR	B	407	−62.281	37.526	−37.512	1.00	87.98	C
ATOM	1688	CB	THR	B	407	−61.776	38.896	−37.998	1.00	88.20	C
ATOM	1689	OG1	THR	B	407	−62.718	39.924	−37.660	1.00	88.82	O
ATOM	1690	CG2	THR	B	407	−61.437	38.917	−39.497	1.00	88.11	C
ATOM	1691	C	THR	B	407	−63.112	37.632	−36.240	1.00	87.20	C
ATOM	1692	O	THR	B	407	−64.333	37.469	−36.293	1.00	87.26	O
ATOM	1693	N	LEU	B	408	−62.461	37.926	−35.104	1.00	83.82	N
ATOM	1694	CA	LEU	B	408	−63.150	38.086	−33.837	1.00	82.78	C
ATOM	1695	CB	LEU	B	408	−62.143	38.376	−32.722	1.00	82.53	C
ATOM	1696	CG	LEU	B	408	−62.696	38.851	−31.380	1.00	82.25	C
ATOM	1697	CD1	LEU	B	408	−63.598	37.798	−30.727	1.00	82.62	C
ATOM	1698	CD2	LEU	B	408	−61.576	39.199	−30.436	1.00	82.94	C
ATOM	1699	C	LEU	B	408	−64.180	39.215	−33.955	1.00	82.54	C
ATOM	1700	O	LEU	B	408	−65.314	39.051	−33.489	1.00	82.55	O
ATOM	1701	N	ALA	B	409	−63.795	40.344	−34.605	1.00	81.97	N
ATOM	1702	CA	ALA	B	409	−64.659	41.516	−34.779	1.00	81.35	C
ATOM	1703	CB	ALA	B	409	−63.871	42.672	−35.361	1.00	81.52	C
ATOM	1704	C	ALA	B	409	−65.874	41.213	−35.633	1.00	80.96	C
ATOM	1705	O	ALA	B	409	−66.945	41.771	−35.386	1.00	80.76	O
ATOM	1706	N	GLU	B	410	−65.699	40.309	−36.617	1.00	80.96	N
ATOM	1707	CA	GLU	B	410	−66.710	39.842	−37.567	1.00	80.62	C
ATOM	1708	CB	GLU	B	410	−66.014	39.093	−38.711	1.00	80.93	C
ATOM	1709	CG	GLU	B	410	−65.963	39.834	−40.033	1.00	83.23	C
ATOM	1710	CD	GLU	B	410	−64.677	39.602	−40.809	1.00	87.13	C
ATOM	1711	OE1	GLU	B	410	−64.421	38.451	−41.248	1.00	88.89	O
ATOM	1712	OE2	GLU	B	410	−63.915	40.584	−40.969	1.00	89.23	O
ATOM	1713	C	GLU	B	410	−67.650	38.891	−36.874	1.00	79.82	C
ATOM	1714	O	GLU	B	410	−68.822	38.779	−37.234	1.00	79.68	O
ATOM	1715	N	LEU	B	411	−67.113	38.187	−35.889	1.00	78.35	N
ATOM	1716	CA	LEU	B	411	−67.839	37.207	−35.119	1.00	77.79	C
ATOM	1717	CB	LEU	B	411	−66.867	36.153	−34.596	1.00	77.78	C
ATOM	1718	CG	LEU	B	411	−67.515	34.903	−34.097	1.00	78.03	C
ATOM	1719	CD1	LEU	B	411	−67.345	33.767	−35.086	1.00	78.21	C
ATOM	1720	CD2	LEU	B	411	−66.983	34.561	−32.737	1.00	79.18	C
ATOM	1721	C	LEU	B	411	−68.681	37.847	−34.001	1.00	77.24	C
ATOM	1722	O	LEU	B	411	−69.831	37.441	−33.802	1.00	77.27	O
ATOM	1723	N	ARG	B	412	−68.130	38.849	−33.291	1.00	76.11	N
ATOM	1724	CA	ARG	B	412	−68.868	39.539	−32.231	1.00	75.55	C
ATOM	1725	CB	ARG	B	412	−68.009	40.629	−31.581	1.00	75.61	C
ATOM	1726	CG	ARG	B	412	−68.578	41.165	−30.270	1.00	75.68	C
ATOM	1727	CD	ARG	B	412	−67.779	42.318	−29.686	1.00	76.09	C
ATOM	1728	NE	ARG	B	412	−66.410	41.948	−29.333	1.00	76.59	N
ATOM	1729	CZ	ARG	B	412	−65.366	42.123	−30.143	1.00	78.24	C
ATOM	1730	NH1	ARG	B	412	−65.535	42.649	−31.357	1.00	78.09	N
ATOM	1731	NH2	ARG	B	412	−64.146	41.775	−29.749	1.00	79.25	N
ATOM	1732	C	ARG	B	412	−70.114	40.149	−32.851	1.00	75.03	C
ATOM	1733	O	ARG	B	412	−71.220	39.914	−32.358	1.00	75.17	O
ATOM	1734	N	GLN	B	413	−69.921	40.886	−33.966	1.00	74.22	N
ATOM	1735	CA	GLN	B	413	−70.953	41.540	−34.766	1.00	73.43	C
ATOM	1736	CB	GLN	B	413	−70.301	42.219	−35.965	1.00	73.44	C
ATOM	1737	CG	GLN	B	413	−69.415	43.393	−35.576	1.00	73.24	C
ATOM	1738	CD	GLN	B	413	−70.167	44.690	−35.561	1.00	72.45	C
ATOM	1739	OE1	GLN	B	413	−71.411	44.719	−35.704	1.00	72.48	O
ATOM	1740	NE2	GLN	B	413	−69.425	45.783	−35.373	1.00	70.30	N
ATOM	1741	C	GLN	B	413	−72.012	40.539	−35.229	1.00	73.02	C
ATOM	1742	O	GLN	B	413	−73.201	40.787	−35.048	1.00	72.86	O
ATOM	1743	N	ARG	B	414	−71.571	39.396	−35.800	1.00	75.91	N
ATOM	1744	CA	ARG	B	414	−72.421	38.300	−36.272	1.00	75.71	C
ATOM	1745	CB	ARG	B	414	−71.555	37.219	−36.942	1.00	76.10	C
ATOM	1746	CG	ARG	B	414	−72.166	36.681	−38.235	1.00	79.15	C
ATOM	1747	CD	ARG	B	414	−71.243	35.718	−38.987	1.00	85.28	C
ATOM	1748	NE	ARG	B	414	−71.509	35.701	−40.431	1.00	88.74	N
ATOM	1749	CZ	ARG	B	414	−71.101	36.643	−41.287	1.00	91.15	C
ATOM	1750	NH1	ARG	B	414	−71.403	36.551	−42.578	1.00	92.85	N
ATOM	1751	NH2	ARG	B	414	−70.399	37.695	−40.851	1.00	91.02	N
ATOM	1752	C	ARG	B	414	−73.325	37.712	−35.133	1.00	74.46	C
ATOM	1753	O	ARG	B	414	−74.515	37.478	−35.356	1.00	74.04	O
ATOM	1754	N	LEU	B	415	−72.759	37.512	−33.921	1.00	68.09	N
ATOM	1755	CA	LEU	B	415	−73.501	37.017	−32.764	1.00	67.32	C
ATOM	1756	CB	LEU	B	415	−72.561	36.841	−31.577	1.00	67.07	C
ATOM	1757	CG	LEU	B	415	−71.715	35.604	−31.538	1.00	66.56	C
ATOM	1758	CD1	LEU	B	415	−70.568	35.777	−30.549	1.00	66.03	C
ATOM	1759	CD2	LEU	B	415	−72.554	34.350	−31.266	1.00	65.00	C
ATOM	1760	C	LEU	B	415	−74.591	38.032	−32.381	1.00	67.36	C
ATOM	1761	O	LEU	B	415	−75.722	37.642	−32.052	1.00	67.10	O
ATOM	1762	N	ILE	B	416	−74.234	39.348	−32.425	1.00	68.45	N
ATOM	1763	CA	ILE	B	416	−75.152	40.442	−32.127	1.00	68.32	C
ATOM	1764	CB	ILE	B	416	−74.435	41.815	−32.035	1.00	67.86	C
ATOM	1765	CG1	ILE	B	416	−73.425	41.848	−30.881	1.00	67.10	C
ATOM	1766	CD1	ILE	B	416	−72.503	43.080	−30.854	1.00	65.57	C
ATOM	1767	CG2	ILE	B	416	−75.453	42.945	−31.889	1.00	66.91	C
ATOM	1768	C	ILE	B	416	−76.298	40.439	−33.154	1.00	68.96	C
ATOM	1769	O	ILE	B	416	−77.454	40.451	−32.752	1.00	68.93	O
ATOM	1770	N	HIS	B	417	−75.975	40.390	−34.462	1.00	74.14	N
ATOM	1771	CA	HIS	B	417	−76.957	40.405	−35.536	1.00	75.34	C
ATOM	1772	CB	HIS	B	417	−76.288	40.576	−36.912	1.00	76.00	C
ATOM	1773	CG	HIS	B	417	−77.281	40.887	−37.995	1.00	79.28	C
ATOM	1774	ND1	HIS	B	417	−77.849	42.162	−38.121	1.00	82.13	N
ATOM	1775	CE1	HIS	B	417	−78.699	42.080	−39.137	1.00	82.76	C
ATOM	1776	NE2	HIS	B	417	−78.727	40.842	−39.657	1.00	83.50	N
ATOM	1777	CD2	HIS	B	417	−77.825	40.071	−38.935	1.00	81.69	C
ATOM	1778	C	HIS	B	417	−77.945	39.241	−35.522	1.00	75.44	C
ATOM	1779	O	HIS	B	417	−79.073	39.401	−35.971	1.00	75.49	O
ATOM	1780	N	PHE	B	418	−77.541	38.085	−35.001	1.00	76.60	N
ATOM	1781	CA	PHE	B	418	−78.407	36.912	−34.952	1.00	76.73	C
ATOM	1782	CB	PHE	B	418	−77.574	35.642	−35.078	1.00	77.20	C
ATOM	1783	CG	PHE	B	418	−76.787	35.408	−36.338	1.00	79.44	C
ATOM	1784	CD1	PHE	B	418	−76.803	36.338	−37.377	1.00	81.12	C
ATOM	1785	CE1	PHE	B	418	−76.056	36.129	−38.533	1.00	82.00	C
ATOM	1786	CZ	PHE	B	418	−75.304	34.976	−38.667	1.00	82.73	C
ATOM	1787	CE2	PHE	B	418	−75.286	34.034	−37.656	1.00	82.54	C
ATOM	1788	CD2	PHE	B	418	−76.022	34.254	−36.491	1.00	81.60	C
ATOM	1789	C	PHE	B	418	−79.206	36.813	−33.663	1.00	76.39	C
ATOM	1790	O	PHE	B	418	−80.242	36.139	−33.646	1.00	76.28	O
ATOM	1791	N	SER	B	419	−78.701	37.427	−32.578	1.00	73.74	N
ATOM	1792	CA	SER	B	419	−79.308	37.404	−31.256	1.00	73.75	C
ATOM	1793	CB	SER	B	419	−78.556	38.338	−30.314	1.00	73.84	C
ATOM	1794	OG	SER	B	419	−77.436	37.727	−29.700	1.00	74.19	O
ATOM	1795	C	SER	B	419	−80.734	37.853	−31.302	1.00	73.84	C
ATOM	1796	O	SER	B	419	−81.040	38.766	−32.061	1.00	73.99	O
ATOM	1797	N	ALA	B	420	−81.605	37.240	−30.484	1.00	71.93	N
ATOM	1798	CA	ALA	B	420	−83.005	37.625	−30.365	1.00	72.07	C
ATOM	1799	CB	ALA	B	420	−83.745	36.590	−29.542	1.00	71.93	C
ATOM	1800	C	ALA	B	420	−83.013	38.999	−29.644	1.00	72.40	C
ATOM	1801	O	ALA	B	420	−82.185	39.205	−28.751	1.00	72.46	O
ATOM	1802	N	LYS	B	421	−83.897	39.937	−30.051	1.00	74.23	N
ATOM	1803	CA	LYS	B	421	−83.988	41.299	−29.487	1.00	74.62	C
ATOM	1804	CB	LYS	B	421	−83.947	42.338	−30.610	1.00	74.66	C
ATOM	1805	CG	LYS	B	421	−82.547	42.783	−30.946	1.00	76.25	C
ATOM	1806	CD	LYS	B	421	−81.924	41.947	−32.054	1.00	78.94	C
ATOM	1807	CE	LYS	B	421	−80.544	42.425	−32.471	1.00	79.71	C
ATOM	1808	NZ	LYS	B	421	−79.899	41.465	−33.406	1.00	80.33	N
ATOM	1809	C	LYS	B	421	−85.189	41.583	−28.572	1.00	74.71	C
ATOM	1810	O	LYS	B	421	−86.234	40.961	−28.717	1.00	74.88	O
ATOM	1811	N	ASP	B	422	−85.035	42.533	−27.638	1.00	75.41	N
ATOM	1812	CA	ASP	B	422	−86.057	42.990	−26.672	1.00	75.73	C
ATOM	1813	CB	ASP	B	422	−87.007	44.040	−27.285	1.00	76.30	C
ATOM	1814	CG	ASP	B	422	−86.437	44.958	−28.360	1.00	78.13	C
ATOM	1815	OD1	ASP	B	422	−85.237	45.372	−28.230	1.00	78.71	O
ATOM	1816	OD2	ASP	B	422	−87.193	45.274	−29.336	1.00	80.16	O
ATOM	1817	C	ASP	B	422	−86.846	41.924	−25.868	1.00	75.29	C
ATOM	1818	O	ASP	B	422	−87.839	42.245	−25.206	1.00	75.54	O
ATOM	1819	N	VAL	B	423	−86.389	40.677	−25.899	1.00	72.35	N
ATOM	1820	CA	VAL	B	423	−87.045	39.568	−25.209	1.00	71.53	C
ATOM	1821	CB	VAL	B	423	−86.847	38.225	−25.933	1.00	71.50	C
ATOM	1822	CG1	VAL	B	423	−87.586	38.219	−27.275	1.00	71.38	C
ATOM	1823	CG2	VAL	B	423	−85.370	37.910	−26.124	1.00	71.72	C
ATOM	1824	C	VAL	B	423	−86.777	39.517	−23.713	1.00	71.24	C
ATOM	1825	O	VAL	B	423	−87.544	38.891	−22.980	1.00	71.04	O
ATOM	1826	N	ILE	B	424	−85.710	40.192	−23.253	1.00	69.40	N
ATOM	1827	CA	ILE	B	424	−85.372	40.256	−21.831	1.00	69.33	C
ATOM	1828	CB	ILE	B	424	−83.852	40.479	−21.624	1.00	69.22	C
ATOM	1829	CG1	ILE	B	424	−82.966	39.459	−22.357	1.00	68.76	C
ATOM	1830	CD1	ILE	B	424	−81.464	39.930	−22.473	1.00	67.42	C
ATOM	1831	CG2	ILE	B	424	−83.513	40.562	−20.155	1.00	69.12	C
ATOM	1832	C	ILE	B	424	−86.142	41.435	−21.246	1.00	69.45	C
ATOM	1833	O	ILE	B	424	−86.150	42.493	−21.869	1.00	69.43	O
ATOM	1834	N	ASN	B	425	−86.764	41.278	−20.062	1.00	72.98	N
ATOM	1835	CA	ASN	B	425	−87.468	42.374	−19.397	1.00	73.43	C
ATOM	1836	CB	ASN	B	425	−88.543	41.841	−18.432	1.00	73.75	C
ATOM	1837	CG	ASN	B	425	−89.486	42.891	−17.818	1.00	75.20	C
ATOM	1838	OD1	ASN	B	425	−89.341	44.124	−18.010	1.00	77.09	O
ATOM	1839	ND2	ASN	B	425	−90.491	42.419	−17.056	1.00	75.14	N
ATOM	1840	C	ASN	B	425	−86.405	43.217	−18.656	1.00	73.62	C
ATOM	1841	O	ASN	B	425	−85.893	42.785	−17.618	1.00	73.33	O
ATOM	1842	N	GLU	B	426	−86.061	44.408	−19.211	1.00	76.51	N
ATOM	1843	CA	GLU	B	426	−85.051	45.338	−18.671	1.00	76.99	C
ATOM	1844	CB	GLU	B	426	−84.946	46.653	−19.505	1.00	77.36	C
ATOM	1845	CG	GLU	B	426	−84.451	46.494	−20.946	1.00	80.58	C
ATOM	1846	CD	GLU	B	426	−82.965	46.603	−21.329	1.00	85.39	C
ATOM	1847	OE1	GLU	B	426	−82.675	47.253	−22.367	1.00	86.18	O
ATOM	1848	OE2	GLU	B	426	−82.097	46.025	−20.625	1.00	86.84	O
ATOM	1849	C	GLU	B	426	−85.252	45.650	−17.181	1.00	76.56	C
ATOM	1850	O	GLU	B	426	−84.302	46.052	−16.515	1.00	76.36	O
ATOM	1851	N	ALA	B	427	−86.480	45.442	−16.667	1.00	75.86	N
ATOM	1852	CA	ALA	B	427	−86.903	45.679	−15.282	1.00	75.92	C
ATOM	1853	CB	ALA	B	427	−88.383	45.409	−15.137	1.00	75.89	C
ATOM	1854	C	ALA	B	427	−86.121	44.920	−14.195	1.00	75.95	C
ATOM	1855	O	ALA	B	427	−85.977	45.442	−13.089	1.00	76.02	O
ATOM	1856	N	TRP	B	428	−85.611	43.715	−14.505	1.00	75.20	N
ATOM	1857	CA	TRP	B	428	−84.837	42.878	−13.588	1.00	75.04	C
ATOM	1858	CB	TRP	B	428	−84.603	41.511	−14.243	1.00	75.43	C
ATOM	1859	CG	TRP	B	428	−83.974	40.446	−13.377	1.00	77.09	C
ATOM	1860	CD1	TRP	B	428	−84.627	39.444	−12.722	1.00	78.40	C
ATOM	1861	NE1	TRP	B	428	−83.720	38.604	−12.105	1.00	78.60	N
ATOM	1862	CE2	TRP	B	428	−82.445	39.035	−12.383	1.00	77.96	C
ATOM	1863	CD2	TRP	B	428	−82.560	40.204	−13.171	1.00	78.20	C
ATOM	1864	CE3	TRP	B	428	−81.382	40.862	−13.572	1.00	77.89	C
ATOM	1865	CZ3	TRP	B	428	−80.160	40.346	−13.171	1.00	77.32	C
ATOM	1866	CH2	TRP	B	428	−80.081	39.181	−12.399	1.00	76.83	C
ATOM	1867	CZ2	TRP	B	428	−81.206	38.518	−11.981	1.00	77.51	C
ATOM	1868	C	TRP	B	428	−83.502	43.533	−13.263	1.00	74.49	C
ATOM	1869	O	TRP	B	428	−82.938	43.281	−12.201	1.00	74.39	O
ATOM	1870	N	PHE	B	429	−82.992	44.352	−14.180	1.00	71.16	N
ATOM	1871	CA	PHE	B	429	−81.722	45.030	−14.002	1.00	71.13	C
ATOM	1872	CB	PHE	B	429	−81.100	45.403	−15.369	1.00	70.85	C
ATOM	1873	CG	PHE	B	429	−80.897	44.253	−16.314	1.00	70.76	C
ATOM	1874	CD1	PHE	B	429	−80.117	43.159	−15.949	1.00	71.06	C
ATOM	1875	CE1	PHE	B	429	−79.955	42.075	−16.812	1.00	70.57	C
ATOM	1876	CZ	PHE	B	429	−80.551	42.090	−18.052	1.00	70.73	C
ATOM	1877	CE2	PHE	B	429	−81.311	43.175	−18.440	1.00	70.60	C
ATOM	1878	CD2	PHE	B	429	−81.482	44.257	−17.571	1.00	70.51	C
ATOM	1879	C	PHE	B	429	−81.861	46.287	−13.170	1.00	71.33	C
ATOM	1880	O	PHE	B	429	−82.913	46.900	−13.188	1.00	71.38	O
ATOM	1881	N	PRO	B	430	−80.807	46.735	−12.470	1.00	73.47	N
ATOM	1882	CA	PRO	B	430	−80.905	48.014	−11.761	1.00	73.85	C
ATOM	1883	CB	PRO	B	430	−79.493	48.199	−11.175	1.00	73.71	C
ATOM	1884	CG	PRO	B	430	−78.873	46.883	−11.199	1.00	73.53	C
ATOM	1885	CD	PRO	B	430	−79.454	46.157	−12.353	1.00	73.62	C
ATOM	1886	C	PRO	B	430	−81.189	49.125	−12.788	1.00	74.59	C
ATOM	1887	O	PRO	B	430	−80.551	49.129	−13.836	1.00	74.54	O
ATOM	1888	N	GLU	B	431	−82.130	50.055	−12.498	1.00	80.83	N
ATOM	1889	CA	GLU	B	431	−82.507	51.176	−13.378	1.00	81.60	C
ATOM	1890	CB	GLU	B	431	−83.287	52.266	−12.613	1.00	82.19	C
ATOM	1891	CG	GLU	B	431	−84.205	51.738	−11.499	1.00	86.77	C
ATOM	1892	CD	GLU	B	431	−85.528	52.458	−11.219	1.00	91.61	C
ATOM	1893	OE1	GLU	B	431	−85.495	53.696	−11.002	1.00	93.91	O
ATOM	1894	OE2	GLU	B	431	−86.592	51.781	−11.204	1.00	92.08	O
ATOM	1895	C	GLU	B	431	−81.322	51.797	−14.118	1.00	81.10	C
ATOM	1896	O	GLU	B	431	−81.396	52.006	−15.332	1.00	81.11	O
ATOM	1897	N	ASP	B	432	−80.212	52.054	−13.405	1.00	79.98	N
ATOM	1898	CA	ASP	B	432	−79.032	52.650	−14.039	1.00	79.83	C
ATOM	1899	CB	ASP	B	432	−78.114	53.367	−13.030	1.00	80.23	C
ATOM	1900	CG	ASP	B	432	−77.464	52.452	−12.013	1.00	82.98	C
ATOM	1901	OD1	ASP	B	432	−76.200	52.487	−11.896	1.00	85.48	O
ATOM	1902	OD2	ASP	B	432	−78.211	51.687	−11.327	1.00	85.86	O
ATOM	1903	C	ASP	B	432	−78.266	51.729	−14.994	1.00	79.05	C
ATOM	1904	O	ASP	B	432	−77.451	52.233	−15.759	1.00	79.13	O
ATOM	1905	N	GLN	B	433	−78.530	50.388	−14.964	1.00	74.87	N
ATOM	1906	CA	GLN	B	433	−77.887	49.397	−15.849	1.00	73.54	C
ATOM	1907	CB	GLN	B	433	−77.585	48.078	−15.128	1.00	73.41	C
ATOM	1908	CG	GLN	B	433	−76.494	48.154	−14.079	1.00	73.19	C
ATOM	1909	CD	GLN	B	433	−75.246	48.854	−14.525	1.00	72.32	C
ATOM	1910	OE1	GLN	B	433	−74.502	48.395	−15.396	1.00	72.62	O
ATOM	1911	NE2	GLN	B	433	−74.996	50.003	−13.925	1.00	72.78	N
ATOM	1912	C	GLN	B	433	−78.673	49.113	−17.124	1.00	72.69	C
ATOM	1913	O	GLN	B	433	−78.066	48.758	−18.122	1.00	72.79	O
ATOM	1914	N	ARG	B	434	−80.001	49.284	−17.096	1.00	70.39	N
ATOM	1915	CA	ARG	B	434	−80.933	49.043	−18.202	1.00	69.41	C
ATOM	1916	CB	ARG	B	434	−82.350	49.503	−17.846	1.00	69.21	C
ATOM	1917	CG	ARG	B	434	−82.790	49.107	−16.459	1.00	69.34	C
ATOM	1918	CD	ARG	B	434	−84.272	48.914	−16.404	1.00	72.35	C
ATOM	1919	NE	ARG	B	434	−84.937	49.688	−15.347	1.00	74.41	N
ATOM	1920	CZ	ARG	B	434	−85.379	49.180	−14.198	1.00	74.96	C
ATOM	1921	NH1	ARG	B	434	−85.209	47.899	−13.924	1.00	75.62	N
ATOM	1922	NH2	ARG	B	434	−85.997	49.954	−13.318	1.00	75.15	N
ATOM	1923	C	ARG	B	434	−80.487	49.584	−19.565	1.00	68.75	C
ATOM	1924	O	ARG	B	434	−80.503	48.863	−20.567	1.00	68.68	O
ATOM	1925	N	VAL	B	435	−80.063	50.824	−19.605	1.00	69.69	N
ATOM	1926	CA	VAL	B	435	−79.630	51.434	−20.859	1.00	69.16	C
ATOM	1927	CB	VAL	B	435	−79.319	52.950	−20.680	1.00	69.68	C
ATOM	1928	CG1	VAL	B	435	−79.223	53.634	−22.034	1.00	69.67	C
ATOM	1929	CG2	VAL	B	435	−80.336	53.662	−19.758	1.00	70.48	C
ATOM	1930	C	VAL	B	435	−78.405	50.727	−21.446	1.00	68.06	C
ATOM	1931	O	VAL	B	435	−78.319	50.560	−22.659	1.00	68.42	O
ATOM	1932	N	LEU	B	436	−77.455	50.355	−20.583	1.00	62.44	N
ATOM	1933	CA	LEU	B	436	−76.184	49.748	−20.936	1.00	61.31	C
ATOM	1934	CB	LEU	B	436	−75.187	50.001	−19.814	1.00	61.19	C
ATOM	1935	CG	LEU	B	436	−75.048	51.449	−19.364	1.00	60.52	C
ATOM	1936	CD1	LEU	B	436	−75.019	51.546	−17.855	1.00	58.88	C
ATOM	1937	CD2	LEU	B	436	−73.804	52.074	−19.923	1.00	59.40	C
ATOM	1938	C	LEU	B	436	−76.227	48.265	−21.243	1.00	60.83	C
ATOM	1939	O	LEU	B	436	−75.425	47.798	−22.044	1.00	60.74	O
ATOM	1940	N	THR	B	437	−77.122	47.523	−20.600	1.00	61.21	N
ATOM	1941	CA	THR	B	437	−77.254	46.086	−20.776	1.00	60.77	C
ATOM	1942	CB	THR	B	437	−77.896	45.475	−19.558	1.00	60.68	C
ATOM	1943	OG1	THR	B	437	−77.178	45.957	−18.448	1.00	60.46	O
ATOM	1944	CG2	THR	B	437	−77.811	43.977	−19.557	1.00	60.66	C
ATOM	1945	C	THR	B	437	−77.946	45.730	−22.094	1.00	60.69	C
ATOM	1946	O	THR	B	437	−79.155	46.032	−22.257	1.00	60.93	O
ATOM	1947	N	PRO	B	438	−77.186	45.075	−23.030	1.00	59.45	N
ATOM	1948	CA	PRO	B	438	−77.763	44.714	−24.323	1.00	59.43	C
ATOM	1949	CB	PRO	B	438	−76.575	44.148	−25.106	1.00	59.07	C
ATOM	1950	CG	PRO	B	438	−75.608	43.738	−24.113	1.00	59.06	C
ATOM	1951	CD	PRO	B	438	−75.772	44.650	−22.948	1.00	59.53	C
ATOM	1952	C	PRO	B	438	−78.874	43.715	−24.166	1.00	59.80	C
ATOM	1953	O	PRO	B	438	−78.681	42.690	−23.504	1.00	59.99	O
ATOM	1954	N	ASN	B	439	−80.048	44.031	−24.734	1.00	61.38	N
ATOM	1955	CA	ASN	B	439	−81.202	43.156	−24.666	1.00	61.71	C
ATOM	1956	CB	ASN	B	439	−82.453	43.972	−24.765	1.00	61.56	C
ATOM	1957	CG	ASN	B	439	−83.616	43.278	−24.141	1.00	62.42	C
ATOM	1958	OD1	ASN	B	439	−83.963	42.129	−24.488	1.00	64.09	O
ATOM	1959	ND2	ASN	B	439	−84.250	43.957	−23.198	1.00	62.21	N
ATOM	1960	C	ASN	B	439	−81.103	42.097	−25.788	1.00	61.96	C
ATOM	1961	O	ASN	B	439	−81.911	42.076	−26.722	1.00	62.22	O
ATOM	1962	N	LEU	B	440	−80.090	41.216	−25.678	1.00	61.01	N
ATOM	1963	CA	LEU	B	440	−79.773	40.158	−26.642	1.00	61.13	C
ATOM	1964	CB	LEU	B	440	−78.401	40.491	−27.264	1.00	61.11	C
ATOM	1965	CG	LEU	B	440	−78.293	41.836	−27.960	1.00	59.46	C
ATOM	1966	CD1	LEU	B	440	−76.926	42.042	−28.476	1.00	58.29	C
ATOM	1967	CD2	LEU	B	440	−79.271	41.930	−29.105	1.00	58.76	C
ATOM	1968	C	LEU	B	440	−79.736	38.721	−26.091	1.00	61.57	C
ATOM	1969	O	LEU	B	440	−79.230	38.491	−24.994	1.00	61.27	O
ATOM	1970	N	VAL	B	441	−80.247	37.758	−26.862	1.00	62.02	N
ATOM	1971	CA	VAL	B	441	−80.214	36.328	−26.483	1.00	62.90	C
ATOM	1972	CB	VAL	B	441	−81.570	35.746	−26.017	1.00	62.40	C
ATOM	1973	CG1	VAL	B	441	−81.444	34.252	−25.761	1.00	62.92	C
ATOM	1974	CG2	VAL	B	441	−82.092	36.460	−24.775	1.00	61.58	C
ATOM	1975	C	VAL	B	441	−79.655	35.552	−27.680	1.00	63.94	C
ATOM	1976	O	VAL	B	441	−80.283	35.579	−28.737	1.00	64.07	O
ATOM	1977	N	ALA	B	442	−78.496	34.882	−27.524	1.00	63.55	N
ATOM	1978	CA	ALA	B	442	−77.838	34.123	−28.593	1.00	65.18	C
ATOM	1979	CB	ALA	B	442	−76.643	33.361	−28.056	1.00	64.97	C
ATOM	1980	C	ALA	B	442	−78.740	33.182	−29.379	1.00	66.71	C
ATOM	1981	O	ALA	B	442	−79.629	32.497	−28.839	1.00	66.50	O
ATOM	1982	N	ALA	B	443	−78.506	33.180	−30.688	1.00	72.51	N
ATOM	1983	CA	ALA	B	443	−79.223	32.337	−31.630	1.00	74.74	C
ATOM	1984	CB	ALA	B	443	−80.508	33.007	−32.070	1.00	74.63	C
ATOM	1985	C	ALA	B	443	−78.323	32.072	−32.820	1.00	76.48	C
ATOM	1986	O	ALA	B	443	−77.381	32.839	−33.082	1.00	76.64	O
ATOM	1987	N	LEU	B	444	−78.576	30.936	−33.489	1.00	83.55	N
ATOM	1988	CA	LEU	B	444	−77.880	30.481	−34.689	1.00	85.83	C
ATOM	1989	CB	LEU	B	444	−76.964	29.278	−34.398	1.00	85.77	C
ATOM	1990	CG	LEU	B	444	−75.812	29.013	−35.370	1.00	85.71	C
ATOM	1991	CD1	LEU	B	444	−76.248	28.122	−36.509	1.00	85.91	C
ATOM	1992	CD2	LEU	B	444	−75.150	30.303	−35.853	1.00	85.83	C
ATOM	1993	C	LEU	B	444	−79.042	30.122	−35.619	1.00	87.65	C
ATOM	1994	O	LEU	B	444	−79.531	28.979	−35.621	1.00	87.86	O
ATOM	1995	N	PRO	B	445	−79.562	31.140	−36.347	1.00	91.99	N
ATOM	1996	CA	PRO	B	445	−80.728	30.905	−37.201	1.00	93.36	C
ATOM	1997	CB	PRO	B	445	−81.401	32.282	−37.238	1.00	93.34	C
ATOM	1998	CG	PRO	B	445	−80.375	33.270	−36.705	1.00	92.71	C
ATOM	1999	CD	PRO	B	445	−79.122	32.545	−36.433	1.00	91.94	C
ATOM	2000	C	PRO	B	445	−80.406	30.379	−38.603	1.00	94.82	C
ATOM	2001	O	PRO	B	445	−79.243	30.442	−39.030	1.00	95.02	O
ATOM	2002	N	PRO	B	446	−81.423	29.864	−39.339	1.00	100.30	N
ATOM	2003	CA	PRO	B	446	−81.172	29.360	−40.707	1.00	101.67	C
ATOM	2004	CB	PRO	B	446	−82.565	28.945	−41.192	1.00	101.62	C
ATOM	2005	CG	PRO	B	446	−83.513	29.671	−40.290	1.00	100.98	C
ATOM	2006	CD	PRO	B	446	−82.841	29.705	−38.971	1.00	100.26	C
ATOM	2007	C	PRO	B	446	−80.494	30.374	−41.646	1.00	103.06	C
ATOM	2008	O	PRO	B	446	−81.112	31.345	−42.102	1.00	103.50	O
ATOM	2009	N	SER	B	447	−79.193	30.120	−41.908	1.00	108.30	N
ATOM	2010	CA	SER	B	447	−78.239	30.894	−42.717	1.00	109.79	C
ATOM	2011	CB	SER	B	447	−77.048	30.038	−43.148	1.00	109.70	C
ATOM	2012	OG	SER	B	447	−77.472	28.871	−43.833	1.00	110.07	O
ATOM	2013	C	SER	B	447	−78.721	31.820	−43.859	1.00	110.65	C
ATOM	2014	O	SER	B	447	−78.629	33.043	−43.691	1.00	110.94	O
ATOM	2015	N	THR	B	448	−79.205	31.263	−45.007	1.00	111.76	N
ATOM	2016	CA	THR	B	448	−79.627	32.021	−46.211	1.00	112.95	C
ATOM	2017	CB	THR	B	448	−81.051	32.675	−46.122	1.00	113.38	C
ATOM	2018	OG1	THR	B	448	−81.534	32.935	−47.451	1.00	114.43	O
ATOM	2019	CG2	THR	B	448	−81.088	33.990	−45.303	1.00	113.43	C
ATOM	2020	C	THR	B	448	−78.504	32.906	−46.819	1.00	113.06	C
ATOM	2021	O	THR	B	448	−77.312	32.666	−46.587	1.00	113.35	O
ATOM	2022	N	GLY	B	452	−75.461	38.623	−50.141	1.00	127.63	N
ATOM	2023	CA	GLY	B	452	−74.322	39.520	−50.305	1.00	127.36	C
ATOM	2024	C	GLY	B	452	−73.994	40.335	−49.067	1.00	127.27	C
ATOM	2025	O	GLY	B	452	−74.774	40.335	−48.104	1.00	127.36	O
ATOM	2026	N	TRP	B	453	−72.829	41.046	−49.090	1.00	122.80	N
ATOM	2027	CA	TRP	B	453	−72.319	41.891	−47.987	1.00	122.17	C
ATOM	2028	CB	TRP	B	453	−70.949	42.535	−48.332	1.00	122.48	C
ATOM	2029	CG	TRP	B	453	−70.383	43.388	−47.225	1.00	124.10	C
ATOM	2030	CD1	TRP	B	453	−69.563	42.980	−46.214	1.00	125.45	C
ATOM	2031	NE1	TRP	B	453	−69.277	44.037	−45.377	1.00	125.89	N
ATOM	2032	CE2	TRP	B	453	−69.926	45.156	−45.830	1.00	126.02	C
ATOM	2033	CD2	TRP	B	453	−70.633	44.786	−46.998	1.00	125.51	C
ATOM	2034	CE3	TRP	B	453	−71.391	45.766	−47.669	1.00	126.21	C
ATOM	2035	CZ3	TRP	B	453	−71.418	47.056	−47.160	1.00	126.79	C
ATOM	2036	CH2	TRP	B	453	−70.706	47.393	−45.998	1.00	127.19	C
ATOM	2037	CZ2	TRP	B	453	−69.963	46.457	−45.312	1.00	126.61	C
ATOM	2038	C	TRP	B	453	−73.304	42.963	−47.472	1.00	121.09	C
ATOM	2039	O	TRP	B	453	−73.843	43.745	−48.267	1.00	121.09	O
ATOM	2040	N	GLN	B	454	−73.493	43.010	−46.132	1.00	112.45	N
ATOM	2041	CA	GLN	B	454	−74.348	43.982	−45.450	1.00	110.83	C
ATOM	2042	CB	GLN	B	454	−75.655	43.349	−44.953	1.00	111.06	C
ATOM	2043	CG	GLN	B	454	−76.547	42.747	−46.064	1.00	112.66	C
ATOM	2044	CD	GLN	B	454	−76.778	43.590	−47.325	1.00	114.86	C
ATOM	2045	OE1	GLN	B	454	−77.171	44.775	−47.288	1.00	116.38	O
ATOM	2046	NE2	GLN	B	454	−76.544	42.975	−48.487	1.00	115.50	N
ATOM	2047	C	GLN	B	454	−73.595	44.729	−44.337	1.00	109.32	C
ATOM	2048	O	GLN	B	454	−72.538	44.271	−43.875	1.00	109.03	O
ATOM	2049	N	LEU	B	455	−74.120	45.907	−43.938	1.00	102.05	N
ATOM	2050	CA	LEU	B	455	−73.486	46.731	−42.907	1.00	100.09	C
ATOM	2051	CB	LEU	B	455	−73.601	48.239	−43.203	1.00	99.99	C
ATOM	2052	CG	LEU	B	455	−72.755	49.173	−42.336	1.00	99.59	C
ATOM	2053	CD1	LEU	B	455	−71.273	48.977	−42.577	1.00	98.61	C
ATOM	2054	CD2	LEU	B	455	−73.148	50.606	−42.538	1.00	99.38	C
ATOM	2055	C	LEU	B	455	−73.909	46.390	−41.474	1.00	98.78	C
ATOM	2056	O	LEU	B	455	−75.098	46.445	−41.116	1.00	98.56	O
ATOM	2057	N	PHE	B	456	−72.909	46.036	−40.657	1.00	93.82	N
ATOM	2058	CA	PHE	B	456	−73.130	45.694	−39.266	1.00	92.42	C
ATOM	2059	CB	PHE	B	456	−72.575	44.301	−38.925	1.00	92.95	C
ATOM	2060	CG	PHE	B	456	−73.280	43.119	−39.552	1.00	94.75	C
ATOM	2061	CD1	PHE	B	456	−74.642	43.167	−39.835	1.00	96.82	C
ATOM	2062	CE1	PHE	B	456	−75.290	42.077	−40.415	1.00	97.51	C
ATOM	2063	CZ	PHE	B	456	−74.586	40.924	−40.684	1.00	98.15	C
ATOM	2064	CE2	PHE	B	456	−73.240	40.850	−40.395	1.00	97.34	C
ATOM	2065	CD2	PHE	B	456	−72.590	41.946	−39.826	1.00	96.09	C
ATOM	2066	C	PHE	B	456	−72.531	46.742	−38.370	1.00	90.96	C
ATOM	2067	O	PHE	B	456	−71.347	47.078	−38.502	1.00	90.49	O
ATOM	2068	N	CYS	B	457	−73.373	47.247	−37.450	1.00	87.32	N
ATOM	2069	CA	CYS	B	457	−73.034	48.272	−36.478	1.00	85.52	C
ATOM	2070	CB	CYS	B	457	−73.687	49.596	−36.852	1.00	85.99	C
ATOM	2071	SG	CYS	B	457	−73.007	50.355	−38.340	1.00	87.56	S
ATOM	2072	C	CYS	B	457	−73.413	47.873	−35.088	1.00	83.67	C
ATOM	2073	O	CYS	B	457	−74.446	47.243	−34.870	1.00	83.32	O
ATOM	2074	N	ARG	B	458	−72.595	48.290	−34.140	1.00	77.84	N
ATOM	2075	CA	ARG	B	458	−72.821	48.044	−32.733	1.00	76.05	C
ATOM	2076	CB	ARG	B	458	−72.061	46.810	−32.248	1.00	75.58	C
ATOM	2077	CG	ARG	B	458	−70.567	46.915	−32.358	1.00	73.81	C
ATOM	2078	CD	ARG	B	458	−69.871	45.766	−31.679	1.00	72.65	C
ATOM	2079	NE	ARG	B	458	−68.418	45.964	−31.645	1.00	71.73	N
ATOM	2080	CZ	ARG	B	458	−67.708	46.168	−30.542	1.00	70.47	C
ATOM	2081	NH1	ARG	B	458	−68.301	46.188	−29.357	1.00	69.87	N
ATOM	2082	NH2	ARG	B	458	−66.402	46.355	−30.615	1.00	71.94	N
ATOM	2083	C	ARG	B	458	−72.488	49.289	−31.914	1.00	75.38	C
ATOM	2084	O	ARG	B	458	−71.528	50.012	−32.201	1.00	75.32	O
ATOM	2085	N	THR	B	459	−73.298	49.526	−30.897	1.00	74.97	N
ATOM	2086	CA	THR	B	459	−73.165	50.632	−29.970	1.00	74.11	C
ATOM	2087	CB	THR	B	459	−74.576	50.978	−29.470	1.00	74.25	C
ATOM	2088	OG1	THR	B	459	−75.305	51.553	−30.549	1.00	75.21	O
ATOM	2089	CG2	THR	B	459	−74.583	51.928	−28.291	1.00	74.38	C
ATOM	2090	C	THR	B	459	−72.233	50.216	−28.829	1.00	73.34	C
ATOM	2091	O	THR	B	459	−72.508	49.232	−28.140	1.00	73.34	O
ATOM	2092	N	VAL	B	460	−71.143	50.946	−28.626	1.00	71.16	N
ATOM	2093	CA	VAL	B	460	−70.229	50.646	−27.524	1.00	70.53	C
ATOM	2094	CB	VAL	B	460	−68.835	50.047	−27.892	1.00	70.38	C
ATOM	2095	CG1	VAL	B	460	−68.605	50.023	−29.385	1.00	70.18	C
ATOM	2096	CG2	VAL	B	460	−67.669	50.708	−27.151	1.00	70.10	C
ATOM	2097	C	VAL	B	460	−70.219	51.769	−26.496	1.00	70.41	C
ATOM	2098	O	VAL	B	460	−69.932	52.922	−26.831	1.00	70.49	O
ATOM	2099	N	TRP	B	461	−70.587	51.449	−25.256	1.00	71.19	N
ATOM	2100	CA	TRP	B	461	−70.600	52.468	−24.220	1.00	71.20	C
ATOM	2101	CB	TRP	B	461	−71.716	52.230	−23.222	1.00	70.38	C
ATOM	2102	CG	TRP	B	461	−73.086	52.530	−23.725	1.00	68.32	C
ATOM	2103	CD1	TRP	B	461	−73.821	51.788	−24.600	1.00	66.23	C
ATOM	2104	NE1	TRP	B	461	−75.082	52.327	−24.739	1.00	65.16	N
ATOM	2105	CE2	TRP	B	461	−75.176	53.441	−23.950	1.00	65.89	C
ATOM	2106	CD2	TRP	B	461	−73.944	53.582	−23.271	1.00	67.24	C
ATOM	2107	CE3	TRP	B	461	−73.789	54.645	−22.363	1.00	66.29	C
ATOM	2108	CZ3	TRP	B	461	−74.852	55.511	−22.164	1.00	65.24	C
ATOM	2109	CH2	TRP	B	461	−76.054	55.355	−22.858	1.00	64.31	C
ATOM	2110	CZ2	TRP	B	461	−76.233	54.336	−23.768	1.00	64.76	C
ATOM	2111	C	TRP	B	461	−69.271	52.531	−23.493	1.00	72.30	C
ATOM	2112	O	TRP	B	461	−68.647	51.506	−23.189	1.00	72.67	O
ATOM	2113	N	SER	B	462	−68.861	53.744	−23.181	1.00	74.24	N
ATOM	2114	CA	SER	B	462	−67.647	53.992	−22.450	1.00	75.66	C
ATOM	2115	CB	SER	B	462	−67.283	55.462	−22.583	1.00	75.63	C
ATOM	2116	OG	SER	B	462	−67.969	56.222	−21.593	1.00	75.96	O
ATOM	2117	C	SER	B	462	−67.941	53.748	−20.995	1.00	76.81	C
ATOM	2118	O	SER	B	462	−69.083	53.488	−20.615	1.00	76.78	O
ATOM	2119	N	ALA	B	463	−66.913	53.899	−20.169	1.00	83.59	N
ATOM	2120	CA	ALA	B	463	−67.059	53.845	−18.733	1.00	85.46	C
ATOM	2121	CB	ALA	B	463	−65.747	53.449	−18.103	1.00	85.21	C
ATOM	2122	C	ALA	B	463	−67.388	55.321	−18.382	1.00	86.93	C
ATOM	2123	O	ALA	B	463	−66.940	56.237	−19.096	1.00	87.12	O
ATOM	2124	N	HIS	B	464	−68.181	55.542	−17.317	1.00	91.57	N
ATOM	2125	CA	HIS	B	464	−68.569	56.865	−16.837	1.00	93.29	C
ATOM	2126	CB	HIS	B	464	−69.353	56.682	−15.550	1.00	93.19	C
ATOM	2127	CG	HIS	B	464	−70.259	57.811	−15.222	1.00	94.40	C
ATOM	2128	ND1	HIS	B	464	−70.153	58.482	−14.026	1.00	95.91	N
ATOM	2129	CE1	HIS	B	464	−71.114	59.398	−14.042	1.00	96.37	C
ATOM	2130	NE2	HIS	B	464	−71.815	59.356	−15.177	1.00	96.33	N
ATOM	2131	CD2	HIS	B	464	−71.279	58.342	−15.938	1.00	95.65	C
ATOM	2132	C	HIS	B	464	−67.316	57.718	−16.583	1.00	94.53	C
ATOM	2133	O	HIS	B	464	−66.354	57.220	−16.007	1.00	94.76	O
ATOM	2134	N	SER	B	465	−67.299	58.973	−17.040	1.00	98.33	N
ATOM	2135	CA	SER	B	465	−66.131	59.856	−16.882	1.00	100.02	C
ATOM	2136	CB	SER	B	465	−66.287	61.104	−17.743	1.00	99.96	C
ATOM	2137	OG	SER	B	465	−67.287	61.959	−17.209	1.00	100.90	O
ATOM	2138	C	SER	B	465	−65.818	60.262	−15.426	1.00	101.11	C
ATOM	2139	O	SER	B	465	−64.683	60.648	−15.123	1.00	101.22	O
ATOM	2140	N	GLY	B	466	−66.819	60.185	−14.555	1.00	105.25	N
ATOM	2141	CA	GLY	B	466	−66.659	60.566	−13.161	1.00	106.92	C
ATOM	2142	C	GLY	B	466	−67.039	62.020	−12.944	1.00	108.18	C
ATOM	2143	O	GLY	B	466	−67.212	62.759	−13.923	1.00	108.28	O
ATOM	2144	N	PRO	B	467	−67.153	62.482	−11.672	1.00	110.29	N
ATOM	2145	CA	PRO	B	467	−67.595	63.862	−11.426	1.00	110.92	C
ATOM	2146	CB	PRO	B	467	−68.260	63.783	−10.037	1.00	110.81	C
ATOM	2147	CG	PRO	B	467	−68.208	62.298	−9.634	1.00	110.68	C
ATOM	2148	CD	PRO	B	467	−67.043	61.752	−10.399	1.00	110.39	C
ATOM	2149	C	PRO	B	467	−66.599	65.015	−11.571	1.00	111.61	C
ATOM	2150	O	PRO	B	467	−66.978	66.145	−11.229	1.00	111.89	O
ATOM	2151	N	THR	B	468	−65.366	64.776	−12.095	1.00	112.93	N
ATOM	2152	CA	THR	B	468	−64.389	65.867	−12.288	1.00	113.63	C
ATOM	2153	CB	THR	B	468	−63.022	65.346	−12.752	1.00	113.72	C
ATOM	2154	OG1	THR	B	468	−62.623	64.204	−11.980	1.00	114.00	O
ATOM	2155	CG2	THR	B	468	−61.943	66.443	−12.763	1.00	113.06	C
ATOM	2156	C	THR	B	468	−64.931	66.818	−13.341	1.00	114.18	C
ATOM	2157	O	THR	B	468	−65.436	66.351	−14.358	1.00	114.47	O
ATOM	2158	N	ARG	B	469	−64.854	68.139	−13.109	1.00	116.36	N
ATOM	2159	CA	ARG	B	469	−65.353	69.118	−14.087	1.00	116.78	C
ATOM	2160	CB	ARG	B	469	−65.519	70.513	−13.460	1.00	116.61	C
ATOM	2161	C	ARG	B	469	−64.473	69.131	−15.377	1.00	117.02	C
ATOM	2162	O	ARG	B	469	−64.922	69.595	−16.431	1.00	117.28	O
ATOM	2163	N	MET	B	470	−63.235	68.594	−15.286	1.00	115.47	N
ATOM	2164	CA	MET	B	470	−62.323	68.485	−16.418	1.00	115.35	C
ATOM	2165	CB	MET	B	470	−61.003	69.219	−16.122	1.00	115.40	C
ATOM	2166	C	MET	B	470	−62.120	66.978	−16.703	1.00	115.23	C
ATOM	2167	O	MET	B	470	−60.997	66.521	−16.945	1.00	115.36	O
ATOM	2168	N	ALA	B	471	−63.240	66.207	−16.656	1.00	112.94	N
ATOM	2169	CA	ALA	B	471	−63.279	64.754	−16.886	1.00	112.30	C
ATOM	2170	CB	ALA	B	471	−64.280	64.082	−15.953	1.00	112.14	C
ATOM	2171	C	ALA	B	471	−63.595	64.378	−18.328	1.00	111.87	C
ATOM	2172	O	ALA	B	471	−64.359	65.075	−19.019	1.00	111.95	O
ATOM	2173	N	THR	B	472	−63.013	63.245	−18.764	1.00	108.06	N
ATOM	2174	CA	THR	B	472	−63.203	62.708	−20.104	1.00	107.28	C
ATOM	2175	CB	THR	B	472	−62.134	63.281	−21.061	1.00	107.44	C
ATOM	2176	OG1	THR	B	472	−62.624	63.256	−22.403	1.00	107.35	O
ATOM	2177	CG2	THR	B	472	−60.753	62.607	−20.918	1.00	107.39	C
ATOM	2178	C	THR	B	472	−63.468	61.169	−20.148	1.00	106.42	C
ATOM	2179	O	THR	B	472	−62.699	60.386	−19.579	1.00	106.26	O
ATOM	2180	N	ALA	B	473	−64.578	60.768	−20.808	1.00	100.03	N
ATOM	2181	CA	ALA	B	473	−64.996	59.380	−21.021	1.00	98.90	C
ATOM	2182	CB	ALA	B	473	−66.484	59.238	−20.767	1.00	98.99	C
ATOM	2183	C	ALA	B	473	−64.674	59.012	−22.481	1.00	98.11	C
ATOM	2184	O	ALA	B	473	−65.074	59.735	−23.392	1.00	97.85	O
ATOM	2185	N	ILE	B	474	−63.934	57.908	−22.701	1.00	94.49	N
ATOM	2186	CA	ILE	B	474	−63.512	57.467	−24.042	1.00	93.51	C
ATOM	2187	CB	ILE	B	474	−61.943	57.470	−24.185	1.00	93.53	C
ATOM	2188	CG1	ILE	B	474	−61.326	58.856	−23.878	1.00	93.64	C
ATOM	2189	CD1	ILE	B	474	−60.862	59.102	−22.394	1.00	94.37	C
ATOM	2190	CG2	ILE	B	474	−61.478	57.016	−25.563	1.00	93.58	C
ATOM	2191	C	ILE	B	474	−64.149	56.122	−24.419	1.00	92.67	C
ATOM	2192	O	ILE	B	474	−64.214	55.218	−23.588	1.00	92.53	O
ATOM	2193	N	ALA	B	475	−64.619	56.010	−25.670	1.00	89.81	N
ATOM	2194	CA	ALA	B	475	−65.227	54.810	−26.233	1.00	89.14	C
ATOM	2195	CB	ALA	B	475	−66.705	55.038	−26.489	1.00	88.89	C
ATOM	2196	C	ALA	B	475	−64.489	54.415	−27.532	1.00	88.97	C
ATOM	2197	O	ALA	B	475	−64.430	55.202	−28.478	1.00	88.77	O
ATOM	2198	N	ARG	B	476	−63.899	53.202	−27.555	1.00	91.20	N
ATOM	2199	CA	ARG	B	476	−63.126	52.687	−28.694	1.00	91.05	C
ATOM	2200	CB	ARG	B	476	−61.694	52.324	−28.252	1.00	91.07	C
ATOM	2201	CG	ARG	B	476	−60.980	53.406	−27.489	1.00	91.51	C
ATOM	2202	CD	ARG	B	476	−59.652	52.942	−26.945	1.00	93.16	C
ATOM	2203	NE	ARG	B	476	−58.894	54.061	−26.366	1.00	95.08	N
ATOM	2204	CZ	ARG	B	476	−58.959	54.441	−25.086	1.00	95.78	C
ATOM	2205	NH1	ARG	B	476	−59.744	53.793	−24.230	1.00	96.38	N
ATOM	2206	NH2	ARG	B	476	−58.241	55.476	−24.657	1.00	95.88	N
ATOM	2207	C	ARG	B	476	−63.785	51.463	−29.343	1.00	90.94	C
ATOM	2208	O	ARG	B	476	−64.694	50.868	−28.758	1.00	90.98	O
ATOM	2209	N	CYS	B	477	−63.304	51.083	−30.552	1.00	88.88	N
ATOM	2210	CA	CYS	B	477	−63.772	49.922	−31.321	1.00	88.83	C
ATOM	2211	CB	CYS	B	477	−64.138	50.326	−32.744	1.00	88.48	C
ATOM	2212	SG	CYS	B	477	−65.297	51.695	−32.860	1.00	87.32	S
ATOM	2213	C	CYS	B	477	−62.704	48.862	−31.359	1.00	89.31	C
ATOM	2214	O	CYS	B	477	−61.568	49.075	−30.903	1.00	89.18	O
ATOM	2215	N	ALA	B	478	−63.054	47.733	−31.983	1.00	94.15	N
ATOM	2216	CA	ALA	B	478	−62.116	46.645	−32.192	1.00	94.86	C
ATOM	2217	CB	ALA	B	478	−62.863	45.389	−32.620	1.00	95.20	C
ATOM	2218	C	ALA	B	478	−61.164	47.106	−33.316	1.00	95.16	C
ATOM	2219	O	ALA	B	478	−61.631	47.763	−34.248	1.00	95.16	O
ATOM	2220	N	PRO	B	479	−59.846	46.811	−33.249	1.00	97.02	N
ATOM	2221	CA	PRO	B	479	−58.929	47.265	−34.309	1.00	97.37	C
ATOM	2222	CB	PRO	B	479	−57.707	46.383	−34.097	1.00	97.36	C
ATOM	2223	CG	PRO	B	479	−57.687	46.161	−32.634	1.00	97.31	C
ATOM	2224	CD	PRO	B	479	−59.118	46.070	−32.201	1.00	97.04	C
ATOM	2225	C	PRO	B	479	−59.451	47.186	−35.747	1.00	97.84	C
ATOM	2226	O	PRO	B	479	−59.298	48.148	−36.511	1.00	98.32	O
ATOM	2227	N	ASP	B	480	−60.100	46.072	−36.106	1.00	98.53	N
ATOM	2228	CA	ASP	B	480	−60.631	45.901	−37.448	1.00	98.64	C
ATOM	2229	CB	ASP	B	480	−60.437	44.456	−37.960	1.00	99.11	C
ATOM	2230	CG	ASP	B	480	−60.712	43.321	−36.971	1.00	101.51	C
ATOM	2231	OD1	ASP	B	480	−60.634	43.567	−35.723	1.00	103.08	O
ATOM	2232	OD2	ASP	B	480	−60.994	42.179	−37.436	1.00	103.88	O
ATOM	2233	C	ASP	B	480	−62.046	46.457	−37.642	1.00	98.13	C
ATOM	2234	O	ASP	B	480	−62.797	45.971	−38.492	1.00	98.13	O
ATOM	2235	N	GLU	B	481	−62.394	47.501	−36.867	1.00	95.63	N
ATOM	2236	CA	GLU	B	481	−63.689	48.187	−36.919	1.00	95.12	C
ATOM	2237	CB	GLU	B	481	−64.466	48.026	−35.600	1.00	94.98	C
ATOM	2238	CG	GLU	B	481	−65.174	46.694	−35.404	1.00	93.55	C
ATOM	2239	CD	GLU	B	481	−66.047	46.588	−34.164	1.00	91.31	C
ATOM	2240	OE1	GLU	B	481	−65.681	47.169	−33.115	1.00	89.30	O
ATOM	2241	OE2	GLU	B	481	−67.097	45.909	−34.240	1.00	90.31	O
ATOM	2242	C	GLU	B	481	−63.471	49.667	−37.174	1.00	95.14	C
ATOM	2243	O	GLU	B	481	−62.396	50.193	−36.855	1.00	95.26	O
ATOM	2244	N	GLU	B	482	−64.501	50.343	−37.733	1.00	96.88	N
ATOM	2245	CA	GLU	B	482	−64.494	51.782	−38.033	1.00	96.69	C
ATOM	2246	CB	GLU	B	482	−64.755	52.040	−39.542	1.00	97.05	C
ATOM	2247	CG	GLU	B	482	−63.538	51.866	−40.458	1.00	98.77	C
ATOM	2248	CD	GLU	B	482	−62.350	52.817	−40.312	1.00	100.97	C
ATOM	2249	OE1	GLU	B	482	−62.551	54.010	−39.973	1.00	101.66	O
ATOM	2250	OE2	GLU	B	482	−61.208	52.359	−40.555	1.00	101.54	O
ATOM	2251	C	GLU	B	482	−65.510	52.552	−37.160	1.00	95.97	C
ATOM	2252	O	GLU	B	482	−66.665	52.138	−37.067	1.00	96.15	O
ATOM	2253	N	LEU	B	483	−65.086	53.661	−36.525	1.00	94.44	N
ATOM	2254	CA	LEU	B	483	−65.987	54.467	−35.695	1.00	93.65	C
ATOM	2255	CB	LEU	B	483	−65.188	55.264	−34.656	1.00	93.65	C
ATOM	2256	CG	LEU	B	483	−65.994	55.805	−33.488	1.00	92.96	C
ATOM	2257	CD1	LEU	B	483	−65.282	55.536	−32.197	1.00	92.61	C
ATOM	2258	CD2	LEU	B	483	−66.223	57.289	−33.628	1.00	92.74	C
ATOM	2259	C	LEU	B	483	−66.763	55.413	−36.611	1.00	93.20	C
ATOM	2260	O	LEU	B	483	−66.282	56.505	−36.919	1.00	92.99	O
ATOM	2261	N	LEU	B	484	−67.948	54.990	−37.057	1.00	91.03	N
ATOM	2262	CA	LEU	B	484	−68.770	55.780	−37.969	1.00	90.35	C
ATOM	2263	CB	LEU	B	484	−69.846	54.914	−38.623	1.00	90.12	C
ATOM	2264	CG	LEU	B	484	−69.384	53.855	−39.611	1.00	90.20	C
ATOM	2265	CD1	LEU	B	484	−70.429	53.636	−40.680	1.00	89.15	C
ATOM	2266	CD2	LEU	B	484	−67.994	54.169	−40.221	1.00	89.63	C
ATOM	2267	C	LEU	B	484	−69.424	56.993	−37.337	1.00	90.26	C
ATOM	2268	O	LEU	B	484	−69.623	58.010	−38.005	1.00	90.42	O
ATOM	2269	N	SER	B	485	−69.800	56.877	−36.073	1.00	90.25	N
ATOM	2270	CA	SER	B	485	−70.469	57.948	−35.371	1.00	89.82	C
ATOM	2271	CB	SER	B	485	−71.974	57.816	−35.544	1.00	89.68	C
ATOM	2272	OG	SER	B	485	−72.718	57.958	−34.345	1.00	89.43	O
ATOM	2273	C	SER	B	485	−70.095	57.962	−33.916	1.00	89.74	C
ATOM	2274	O	SER	B	485	−69.499	57.017	−33.401	1.00	89.92	O
ATOM	2275	N	CYS	B	486	−70.447	59.055	−33.257	1.00	89.97	N
ATOM	2276	CA	CYS	B	486	−70.186	59.279	−31.850	1.00	89.87	C
ATOM	2277	CB	CYS	B	486	−68.778	59.840	−31.644	1.00	90.20	C
ATOM	2278	SG	CYS	B	486	−68.445	60.453	−29.975	1.00	93.44	S
ATOM	2279	C	CYS	B	486	−71.276	60.219	−31.339	1.00	88.92	C
ATOM	2280	O	CYS	B	486	−71.765	61.088	−32.076	1.00	88.97	O
ATOM	2281	N	SER	B	487	−71.697	59.966	−30.095	1.00	83.57	N
ATOM	2282	CA	SER	B	487	−72.712	60.680	−29.337	1.00	82.49	C
ATOM	2283	CB	SER	B	487	−74.099	60.102	−29.605	1.00	82.58	C
ATOM	2284	OG	SER	B	487	−74.369	58.914	−28.880	1.00	82.74	O
ATOM	2285	C	SER	B	487	−72.306	60.585	−27.861	1.00	81.85	C
ATOM	2286	O	SER	B	487	−71.257	60.001	−27.570	1.00	81.86	O
ATOM	2287	N	SER	B	488	−73.086	61.194	−26.942	1.00	79.82	N
ATOM	2288	CA	SER	B	488	−72.791	61.200	−25.502	1.00	79.19	C
ATOM	2289	CB	SER	B	488	−71.826	62.331	−25.148	1.00	79.19	C
ATOM	2290	OG	SER	B	488	−72.426	63.603	−25.331	1.00	79.03	O
ATOM	2291	C	SER	B	488	−74.054	61.326	−24.675	1.00	78.79	C
ATOM	2292	O	SER	B	488	−75.085	61.775	−25.188	1.00	78.90	O
ATOM	2293	N	PHE	B	489	−73.974	60.952	−23.391	1.00	75.75	N
ATOM	2294	CA	PHE	B	489	−75.117	61.012	−22.485	1.00	75.43	C
ATOM	2295	CB	PHE	B	489	−75.921	59.717	−22.597	1.00	75.12	C
ATOM	2296	CG	PHE	B	489	−77.093	59.529	−21.677	1.00	73.56	C
ATOM	2297	CD1	PHE	B	489	−78.318	60.123	−21.958	1.00	71.80	C
ATOM	2298	CE1	PHE	B	489	−79.419	59.928	−21.123	1.00	70.76	C
ATOM	2299	CZ	PHE	B	489	−79.303	59.114	−20.020	1.00	70.83	C
ATOM	2300	CE2	PHE	B	489	−78.095	58.500	−19.732	1.00	70.74	C
ATOM	2301	CD2	PHE	B	489	−76.993	58.704	−20.563	1.00	71.60	C
ATOM	2302	C	PHE	B	489	−74.686	61.267	−21.056	1.00	75.85	C
ATOM	2303	O	PHE	B	489	−73.584	60.884	−20.653	1.00	75.64	O
ATOM	2304	N	SER	B	490	−75.571	61.918	−20.305	1.00	79.05	N
ATOM	2305	CA	SER	B	490	−75.419	62.298	−18.911	1.00	79.93	C
ATOM	2306	CB	SER	B	490	−74.873	63.722	−18.835	1.00	80.03	C
ATOM	2307	OG	SER	B	490	−75.315	64.449	−17.699	1.00	81.51	O
ATOM	2308	C	SER	B	490	−76.810	62.206	−18.296	1.00	80.40	C
ATOM	2309	O	SER	B	490	−77.742	62.767	−18.856	1.00	80.25	O
ATOM	2310	N	ARG	B	491	−76.964	61.477	−17.170	1.00	84.03	N
ATOM	2311	CA	ARG	B	491	−78.258	61.283	−16.500	1.00	85.04	C
ATOM	2312	CB	ARG	B	491	−78.178	60.137	−15.482	1.00	84.72	C
ATOM	2313	C	ARG	B	491	−78.840	62.573	−15.886	1.00	86.05	C
ATOM	2314	O	ARG	B	491	−80.022	62.591	−15.560	1.00	86.32	O
ATOM	2315	N	SER	B	492	−78.013	63.650	−15.761	1.00	91.60	N
ATOM	2316	CA	SER	B	492	−78.324	64.991	−15.218	1.00	92.72	C
ATOM	2317	CB	SER	B	492	−77.248	65.420	−14.212	1.00	92.72	C
ATOM	2318	OG	SER	B	492	−76.036	65.860	−14.812	1.00	92.51	O
ATOM	2319	C	SER	B	492	−78.477	66.092	−16.313	1.00	93.57	C
ATOM	2320	O	SER	B	492	−78.938	67.198	−16.019	1.00	94.01	O
ATOM	2321	N	GLY	B	493	−78.053	65.788	−17.540	1.00	96.27	N
ATOM	2322	CA	GLY	B	493	−78.109	66.709	−18.671	1.00	96.99	C
ATOM	2323	C	GLY	B	493	−76.892	67.606	−18.788	1.00	97.51	C
ATOM	2324	O	GLY	B	493	−76.600	68.118	−19.876	1.00	97.74	O
ATOM	2325	N	LYS	B	494	−76.173	67.795	−17.661	1.00	98.26	N
ATOM	2326	CA	LYS	B	494	−74.973	68.633	−17.543	1.00	98.74	C
ATOM	2327	CB	LYS	B	494	−74.570	68.799	−16.055	1.00	98.94	C
ATOM	2328	CG	LYS	B	494	−75.584	69.547	−15.192	1.00	100.15	C
ATOM	2329	CD	LYS	B	494	−75.531	69.091	−13.731	1.00	102.35	C
ATOM	2330	CE	LYS	B	494	−76.668	69.652	−12.887	1.00	103.47	C
ATOM	2331	NZ	LYS	B	494	−78.005	69.083	−13.257	1.00	103.97	N
ATOM	2332	C	LYS	B	494	−73.784	68.125	−18.385	1.00	98.61	C
ATOM	2333	O	LYS	B	494	−72.873	67.487	−17.851	1.00	98.84	O
ATOM	2334	N	ARG	B	495	−73.792	68.407	−19.695	1.00	96.50	N
ATOM	2335	CA	ARG	B	495	−72.702	67.973	−20.574	1.00	96.64	C
ATOM	2336	CB	ARG	B	495	−73.033	66.666	−21.333	1.00	96.79	C
ATOM	2337	CG	ARG	B	495	−74.345	66.675	−22.085	1.00	96.15	C
ATOM	2338	CD	ARG	B	495	−74.561	65.412	−22.880	1.00	95.77	C
ATOM	2339	NE	ARG	B	495	−75.702	65.601	−23.773	1.00	96.50	N
ATOM	2340	CZ	ARG	B	495	−75.601	65.836	−25.078	1.00	96.55	C
ATOM	2341	NH1	ARG	B	495	−76.692	66.036	−25.808	1.00	96.40	N
ATOM	2342	NH2	ARG	B	495	−74.410	65.868	−25.666	1.00	96.96	N
ATOM	2343	C	ARG	B	495	−72.171	69.040	−21.503	1.00	96.85	C
ATOM	2344	O	ARG	B	495	−72.881	69.988	−21.831	1.00	96.81	O
ATOM	2345	N	ARG	B	496	−70.912	68.882	−21.915	1.00	96.61	N
ATOM	2346	CA	ARG	B	496	−70.236	69.795	−22.829	1.00	97.36	C
ATOM	2347	CB	ARG	B	496	−68.947	70.374	−22.207	1.00	97.76	C
ATOM	2348	CG	ARG	B	496	−69.188	71.646	−21.366	1.00	99.31	C
ATOM	2349	CD	ARG	B	496	−67.969	72.560	−21.228	1.00	101.85	C
ATOM	2350	NE	ARG	B	496	−66.832	71.927	−20.546	1.00	104.10	N
ATOM	2351	CZ	ARG	B	496	−65.770	71.399	−21.157	1.00	104.55	C
ATOM	2352	NH1	ARG	B	496	−65.676	71.420	−22.485	1.00	104.86	N
ATOM	2353	NH2	ARG	B	496	−64.797	70.845	−20.446	1.00	104.83	N
ATOM	2354	C	ARG	B	496	−69.997	69.133	−24.191	1.00	97.42	C
ATOM	2355	O	ARG	B	496	−69.019	69.439	−24.880	1.00	97.20	O
ATOM	2356	N	GLY	B	497	−70.911	68.232	−24.552	1.00	97.26	N
ATOM	2357	CA	GLY	B	497	−70.893	67.497	−25.810	1.00	97.69	C
ATOM	2358	C	GLY	B	497	−69.932	66.331	−25.891	1.00	98.14	C
ATOM	2359	O	GLY	B	497	−69.592	65.716	−24.876	1.00	98.09	O
ATOM	2360	N	GLU	B	498	−69.501	66.026	−27.130	1.00	99.98	N
ATOM	2361	CA	GLU	B	498	−68.601	64.928	−27.490	1.00	100.60	C
ATOM	2362	CB	GLU	B	498	−69.422	63.637	−27.690	1.00	100.54	C
ATOM	2363	CG	GLU	B	498	−70.232	63.578	−28.982	1.00	99.77	C
ATOM	2364	CD	GLU	B	498	−71.598	64.247	−29.036	1.00	99.78	C
ATOM	2365	OE1	GLU	B	498	−72.349	64.209	−28.031	1.00	99.38	O
ATOM	2366	OE2	GLU	B	498	−71.933	64.781	−30.118	1.00	99.93	O
ATOM	2367	C	GLU	B	498	−67.810	65.231	−28.770	1.00	101.27	C
ATOM	2368	O	GLU	B	498	−68.208	66.105	−29.542	1.00	101.37	O
ATOM	2369	N	ARG	B	499	−66.720	64.488	−29.015	1.00	102.02	N
ATOM	2370	CA	ARG	B	499	−65.915	64.670	−30.220	1.00	103.16	C
ATOM	2371	CB	ARG	B	499	−64.914	65.838	−30.075	1.00	103.36	C
ATOM	2372	CG	ARG	B	499	−63.771	65.661	−29.066	1.00	104.82	C
ATOM	2373	CD	ARG	B	499	−63.010	66.968	−28.889	1.00	107.27	C
ATOM	2374	NE	ARG	B	499	−61.560	66.786	−28.803	1.00	108.74	N
ATOM	2375	CZ	ARG	B	499	−60.748	66.743	−29.859	1.00	110.20	C
ATOM	2376	NH1	ARG	B	499	−61.237	66.848	−31.091	1.00	110.76	N
ATOM	2377	NH2	ARG	B	499	−59.440	66.584	−29.690	1.00	110.74	N
ATOM	2378	C	ARG	B	499	−65.212	63.403	−30.683	1.00	103.63	C
ATOM	2379	O	ARG	B	499	−64.716	62.654	−29.843	1.00	103.79	O
ATOM	2380	N	MET	B	500	−65.166	63.166	−32.016	1.00	104.97	N
ATOM	2381	CA	MET	B	500	−64.464	62.024	−32.618	1.00	105.67	C
ATOM	2382	CB	MET	B	500	−65.081	61.555	−33.951	1.00	105.49	C
ATOM	2383	CG	MET	B	500	−66.574	61.518	−33.996	1.00	105.68	C
ATOM	2384	SD	MET	B	500	−67.135	61.048	−35.655	1.00	106.00	S
ATOM	2385	CE	MET	B	500	−68.702	61.924	−35.734	1.00	106.42	C
ATOM	2386	C	MET	B	500	−63.063	62.545	−32.907	1.00	106.25	C
ATOM	2387	O	MET	B	500	−62.922	63.593	−33.548	1.00	106.65	O
ATOM	2388	N	GLU	B	501	−62.032	61.841	−32.436	1.00	108.32	N
ATOM	2389	CA	GLU	B	501	−60.643	62.261	−32.642	1.00	108.99	C
ATOM	2390	CB	GLU	B	501	−60.233	63.351	−31.631	1.00	109.08	C
ATOM	2391	CG	GLU	B	501	−60.598	63.038	−30.191	1.00	109.68	C
ATOM	2392	CD	GLU	B	501	−59.428	63.072	−29.234	1.00	111.33	C
ATOM	2393	OE1	GLU	B	501	−58.397	62.407	−29.499	1.00	112.50	O
ATOM	2394	OE2	GLU	B	501	−59.550	63.768	−28.203	1.00	111.64	O
ATOM	2395	C	GLU	B	501	−59.677	61.091	−32.599	1.00	109.25	C
ATOM	2396	O	GLU	B	501	−59.884	60.161	−31.813	1.00	109.40	O
ATOM	2397	N	ALA	B	502	−58.619	61.134	−33.439	1.00	110.32	N
ATOM	2398	CA	ALA	B	502	−57.623	60.066	−33.487	1.00	110.50	C
ATOM	2399	CB	ALA	B	502	−56.732	60.212	−34.706	1.00	110.43	C
ATOM	2400	C	ALA	B	502	−56.799	60.056	−32.206	1.00	110.60	C
ATOM	2401	O	ALA	B	502	−56.305	61.106	−31.785	1.00	110.53	O
ATOM	2402	N	GLN	B	503	−56.705	58.877	−31.556	1.00	111.55	N
ATOM	2403	CA	GLN	B	503	−55.966	58.704	−30.301	1.00	111.77	C
ATOM	2404	CB	GLN	B	503	−56.926	58.536	−29.112	1.00	111.82	C
ATOM	2405	CG	GLN	B	503	−56.555	59.397	−27.905	1.00	112.75	C
ATOM	2406	CD	GLN	B	503	−56.913	58.792	−26.555	1.00	113.67	C
ATOM	2407	OE1	GLN	B	503	−57.487	59.470	−25.683	1.00	113.67	O
ATOM	2408	NE2	GLN	B	503	−56.572	57.514	−26.337	1.00	113.24	N
ATOM	2409	C	GLN	B	503	−54.970	57.548	−30.402	1.00	111.66	C
ATOM	2410	O	GLN	B	503	−54.878	56.702	−29.506	1.00	111.55	O
ATOM	2411	N	GLY	B	504	−54.226	57.547	−31.504	1.00	110.07	N
ATOM	2412	CA	GLY	B	504	−53.219	56.544	−31.810	1.00	109.96	C
ATOM	2413	C	GLY	B	504	−53.490	55.899	−33.147	1.00	109.86	C
ATOM	2414	O	GLY	B	504	−53.667	54.682	−33.219	1.00	110.09	O
ATOM	2415	N	GLY	B	505	−53.547	56.727	−34.193	1.00	107.76	N
ATOM	2416	CA	GLY	B	505	−53.794	56.312	−35.574	1.00	107.17	C
ATOM	2417	C	GLY	B	505	−55.244	55.983	−35.853	1.00	106.75	C
ATOM	2418	O	GLY	B	505	−55.739	56.207	−36.966	1.00	106.70	O
ATOM	2419	N	LYS	B	506	−55.921	55.438	−34.817	1.00	103.97	N
ATOM	2420	CA	LYS	B	506	−57.319	55.021	−34.795	1.00	103.43	C
ATOM	2421	CB	LYS	B	506	−57.475	53.707	−34.009	1.00	103.22	C
ATOM	2422	C	LYS	B	506	−58.195	56.119	−34.201	1.00	102.98	C
ATOM	2423	O	LYS	B	506	−57.736	56.916	−33.374	1.00	102.94	O
ATOM	2424	N	LEU	B	507	−59.462	56.138	−34.640	1.00	100.19	N
ATOM	2425	CA	LEU	B	507	−60.488	57.086	−34.243	1.00	99.60	C
ATOM	2426	CB	LEU	B	507	−61.489	57.283	−35.389	1.00	99.62	C
ATOM	2427	CG	LEU	B	507	−61.238	58.461	−36.300	1.00	99.92	C
ATOM	2428	CD1	LEU	B	507	−62.162	58.412	−37.512	1.00	99.81	C
ATOM	2429	CD2	LEU	B	507	−61.374	59.779	−35.541	1.00	100.26	C
ATOM	2430	C	LEU	B	507	−61.244	56.677	−33.010	1.00	99.14	C
ATOM	2431	O	LEU	B	507	−62.007	55.710	−33.045	1.00	99.30	O
ATOM	2432	N	VAL	B	508	−61.059	57.418	−31.926	1.00	97.74	N
ATOM	2433	CA	VAL	B	508	−61.807	57.153	−30.702	1.00	97.21	C
ATOM	2434	CB	VAL	B	508	−60.965	57.106	−29.391	1.00	97.40	C
ATOM	2435	CG1	VAL	B	508	−59.822	56.097	−29.491	1.00	97.46	C
ATOM	2436	CG2	VAL	B	508	−60.459	58.492	−28.979	1.00	97.58	C
ATOM	2437	C	VAL	B	508	−62.985	58.151	−30.656	1.00	96.62	C
ATOM	2438	O	VAL	B	508	−63.221	58.856	−31.633	1.00	96.62	O
ATOM	2439	N	CYS	B	509	−63.723	58.190	−29.551	1.00	95.28	N
ATOM	2440	CA	CYS	B	509	−64.854	59.076	−29.355	1.00	94.70	C
ATOM	2441	CB	CYS	B	509	−66.158	58.379	−29.765	1.00	94.39	C
ATOM	2442	SG	CYS	B	509	−67.660	58.918	−28.888	1.00	93.73	S
ATOM	2443	C	CYS	B	509	−64.799	59.439	−27.882	1.00	94.85	C
ATOM	2444	O	CYS	B	509	−64.850	58.556	−27.023	1.00	94.75	O
ATOM	2445	N	ARG	B	510	−64.580	60.734	−27.590	1.00	98.66	N
ATOM	2446	CA	ARG	B	510	−64.523	61.210	−26.214	1.00	98.77	C
ATOM	2447	CB	ARG	B	510	−63.126	61.622	−25.716	1.00	98.96	C
ATOM	2448	CG	ARG	B	510	−62.429	62.761	−26.441	1.00	99.61	C
ATOM	2449	CD	ARG	B	510	−61.444	63.535	−25.547	1.00	101.26	C
ATOM	2450	NE	ARG	B	510	−60.647	62.705	−24.625	1.00	101.83	N
ATOM	2451	CZ	ARG	B	510	−59.442	62.197	−24.891	1.00	102.45	C
ATOM	2452	NH1	ARG	B	510	−58.866	62.412	−26.068	1.00	102.46	N
ATOM	2453	NH2	ARG	B	510	−58.806	61.463	−23.979	1.00	102.87	N
ATOM	2454	C	ARG	B	510	−65.574	62.221	−25.907	1.00	98.65	C
ATOM	2455	O	ARG	B	510	−65.911	63.044	−26.755	1.00	98.46	O
ATOM	2456	N	ALA	B	511	−66.129	62.119	−24.704	1.00	99.45	N
ATOM	2457	CA	ALA	B	511	−67.163	63.007	−24.210	1.00	99.87	C
ATOM	2458	CB	ALA	B	511	−68.338	62.210	−23.677	1.00	99.79	C
ATOM	2459	C	ALA	B	511	−66.569	63.865	−23.118	1.00	100.26	C
ATOM	2460	O	ALA	B	511	−65.663	63.428	−22.394	1.00	100.16	O
ATOM	2461	N	HIS	B	512	−67.062	65.104	−23.017	1.00	103.56	N
ATOM	2462	CA	HIS	B	512	−66.572	66.038	−22.022	1.00	103.97	C
ATOM	2463	CB	HIS	B	512	−66.059	67.328	−22.680	1.00	104.15	C
ATOM	2464	CG	HIS	B	512	−65.158	67.086	−23.851	1.00	104.58	C
ATOM	2465	ND1	HIS	B	512	−63.836	66.696	−23.679	1.00	104.80	N
ATOM	2466	CE1	HIS	B	512	−63.344	66.555	−24.901	1.00	105.05	C
ATOM	2467	NE2	HIS	B	512	−64.263	66.828	−25.833	1.00	104.85	N
ATOM	2468	CD2	HIS	B	512	−65.424	67.166	−25.176	1.00	104.75	C
ATOM	2469	C	HIS	B	512	−67.647	66.339	−21.017	1.00	104.07	C
ATOM	2470	O	HIS	B	512	−68.814	66.544	−21.377	1.00	103.94	O
ATOM	2471	N	ASN	B	513	−67.249	66.344	−19.745	1.00	108.70	N
ATOM	2472	CA	ASN	B	513	−68.135	66.661	−18.637	1.00	109.06	C
ATOM	2473	CB	ASN	B	513	−67.662	65.942	−17.371	1.00	108.93	C
ATOM	2474	CG	ASN	B	513	−68.626	66.037	−16.216	1.00	109.02	C
ATOM	2475	OD1	ASN	B	513	−69.822	65.727	−16.324	1.00	108.87	O
ATOM	2476	ND2	ASN	B	513	−68.118	66.469	−15.077	1.00	109.30	N
ATOM	2477	C	ASN	B	513	−68.090	68.195	−18.458	1.00	109.45	C
ATOM	2478	O	ASN	B	513	−67.032	68.806	−18.668	1.00	109.67	O
ATOM	2479	N	ALA	B	514	−69.225	68.822	−18.102	1.00	112.49	N
ATOM	2480	CA	ALA	B	514	−69.271	70.277	−17.905	1.00	112.56	C
ATOM	2481	CB	ALA	B	514	−70.691	70.785	−18.130	1.00	112.61	C
ATOM	2482	C	ALA	B	514	−68.781	70.659	−16.492	1.00	112.54	C
ATOM	2483	O	ALA	B	514	−68.324	69.783	−15.741	1.00	112.68	O
ATOM	2484	N	PHE	B	515	−68.862	71.962	−16.126	1.00	112.66	N
ATOM	2485	CA	PHE	B	515	−68.475	72.372	−14.779	1.00	112.19	C
ATOM	2486	CB	PHE	B	515	−68.331	73.903	−14.673	1.00	112.23	C
ATOM	2487	C	PHE	B	515	−69.586	71.830	−13.844	1.00	111.78	C
ATOM	2488	O	PHE	B	515	−70.780	72.017	−14.123	1.00	111.67	O
ATOM	2489	N	GLY	B	516	−69.175	71.100	−12.804	1.00	110.55	N
ATOM	2490	CA	GLY	B	516	−70.078	70.509	−11.817	1.00	109.70	C
ATOM	2491	C	GLY	B	516	−71.000	69.405	−12.305	1.00	109.14	C
ATOM	2492	O	GLY	B	516	−71.985	69.068	−11.632	1.00	109.15	O
ATOM	2493	N	GLY	B	517	−70.672	68.842	−13.468	1.00	107.91	N
ATOM	2494	CA	GLY	B	517	−71.421	67.753	−14.079	1.00	106.83	C
ATOM	2495	C	GLY	B	517	−71.141	66.421	−13.414	1.00	106.05	C
ATOM	2496	O	GLY	B	517	−69.981	66.074	−13.178	1.00	105.89	O
ATOM	2497	N	GLU	B	518	−72.218	65.673	−13.112	1.00	104.44	N
ATOM	2498	CA	GLU	B	518	−72.240	64.353	−12.468	1.00	103.79	C
ATOM	2499	CB	GLU	B	518	−73.714	63.883	−12.390	1.00	104.31	C
ATOM	2500	CG	GLU	B	518	−73.988	62.379	−12.342	1.00	107.59	C
ATOM	2501	CD	GLU	B	518	−74.554	61.735	−13.604	1.00	111.39	C
ATOM	2502	OE1	GLU	B	518	−74.894	62.473	−14.563	1.00	112.80	O
ATOM	2503	OE2	GLU	B	518	−74.652	60.483	−13.630	1.00	112.20	O
ATOM	2504	C	GLU	B	518	−71.289	63.314	−13.137	1.00	102.42	C
ATOM	2505	O	GLU	B	518	−70.720	62.456	−12.452	1.00	102.42	O
ATOM	2506	N	GLY	B	519	−71.128	63.434	−14.456	1.00	95.77	N
ATOM	2507	CA	GLY	B	519	−70.298	62.569	−15.288	1.00	93.38	C
ATOM	2508	C	GLY	B	519	−70.952	62.276	−16.624	1.00	91.71	C
ATOM	2509	O	GLY	B	519	−72.173	62.415	−16.775	1.00	91.45	O
ATOM	2510	N	VAL	B	520	−70.136	61.873	−17.604	1.00	85.33	N
ATOM	2511	CA	VAL	B	520	−70.610	61.549	−18.953	1.00	83.96	C
ATOM	2512	CB	VAL	B	520	−70.257	62.615	−20.026	1.00	83.84	C
ATOM	2513	CG1	VAL	B	520	−71.053	63.895	−19.825	1.00	84.23	C
ATOM	2514	CG2	VAL	B	520	−68.762	62.878	−20.107	1.00	82.88	C
ATOM	2515	C	VAL	B	520	−70.246	60.147	−19.455	1.00	83.10	C
ATOM	2516	O	VAL	B	520	−69.364	59.482	−18.903	1.00	82.93	O
ATOM	2517	N	TYR	B	521	−70.927	59.734	−20.542	1.00	77.36	N
ATOM	2518	CA	TYR	B	521	−70.719	58.483	−21.248	1.00	76.11	C
ATOM	2519	CB	TYR	B	521	−72.014	57.659	−21.271	1.00	75.84	C
ATOM	2520	CG	TYR	B	521	−72.279	56.875	−20.014	1.00	74.40	C
ATOM	2521	CD1	TYR	B	521	−71.496	55.778	−19.678	1.00	73.61	C
ATOM	2522	CE1	TYR	B	521	−71.726	55.057	−18.514	1.00	73.69	C
ATOM	2523	CZ	TYR	B	521	−72.783	55.405	−17.690	1.00	73.71	C
ATOM	2524	OH	TYR	B	521	−73.029	54.664	−16.560	1.00	75.02	O
ATOM	2525	CE2	TYR	B	521	−73.591	56.480	−18.016	1.00	73.04	C
ATOM	2526	CD2	TYR	B	521	−73.333	57.208	−19.172	1.00	73.38	C
ATOM	2527	C	TYR	B	521	−70.376	58.817	−22.676	1.00	75.67	C
ATOM	2528	O	TYR	B	521	−71.056	59.644	−23.272	1.00	75.79	O
ATOM	2529	N	ALA	B	522	−69.352	58.187	−23.236	1.00	75.50	N
ATOM	2530	CA	ALA	B	522	−69.011	58.380	−24.644	1.00	75.36	C
ATOM	2531	CB	ALA	B	522	−67.509	58.343	−24.849	1.00	75.31	C
ATOM	2532	C	ALA	B	522	−69.682	57.201	−25.354	1.00	75.24	C
ATOM	2533	O	ALA	B	522	−69.425	56.045	−25.017	1.00	75.54	O
ATOM	2534	N	ILE	B	523	−70.584	57.471	−26.280	1.00	75.34	N
ATOM	2535	CA	ILE	B	523	−71.266	56.367	−26.911	1.00	75.13	C
ATOM	2536	CB	ILE	B	523	−72.780	56.459	−26.667	1.00	74.87	C
ATOM	2537	CG1	ILE	B	523	−73.084	56.834	−25.200	1.00	74.58	C
ATOM	2538	CD1	ILE	B	523	−74.213	57.663	−25.036	1.00	74.23	C
ATOM	2539	CG2	ILE	B	523	−73.447	55.142	−27.051	1.00	74.99	C
ATOM	2540	C	ILE	B	523	−70.871	56.188	−28.372	1.00	75.66	C
ATOM	2541	O	ILE	B	523	−71.472	56.794	−29.261	1.00	75.68	O
ATOM	2542	N	ALA	B	524	−69.855	55.338	−28.624	1.00	77.17	N
ATOM	2543	CA	ALA	B	524	−69.367	55.050	−29.976	1.00	77.63	C
ATOM	2544	CB	ALA	B	524	−67.969	54.457	−29.905	1.00	77.24	C
ATOM	2545	C	ALA	B	524	−70.312	54.102	−30.761	1.00	78.11	C
ATOM	2546	O	ALA	B	524	−70.984	53.267	−30.151	1.00	78.12	O
ATOM	2547	N	ARG	B	525	−70.370	54.249	−32.104	1.00	78.26	N
ATOM	2548	CA	ARG	B	525	−71.152	53.387	−32.983	1.00	79.17	C
ATOM	2549	CB	ARG	B	525	−72.256	54.140	−33.724	1.00	78.49	C
ATOM	2550	CG	ARG	B	525	−73.134	53.238	−34.584	1.00	77.19	C
ATOM	2551	CD	ARG	B	525	−74.204	52.490	−33.806	1.00	74.80	C
ATOM	2552	NE	ARG	B	525	−75.051	51.713	−34.710	1.00	71.66	N
ATOM	2553	CZ	ARG	B	525	−76.000	50.870	−34.324	1.00	69.01	C
ATOM	2554	NH1	ARG	B	525	−76.228	50.663	−33.034	1.00	68.93	N
ATOM	2555	NH2	ARG	B	525	−76.730	50.224	−35.224	1.00	67.79	N
ATOM	2556	C	ARG	B	525	−70.131	52.755	−33.927	1.00	80.77	C
ATOM	2557	O	ARG	B	525	−69.737	53.366	−34.930	1.00	81.03	O
ATOM	2558	N	CYS	B	526	−69.661	51.534	−33.550	1.00	84.10	N
ATOM	2559	CA	CYS	B	526	−68.646	50.752	−34.245	1.00	85.63	C
ATOM	2560	CB	CYS	B	526	−67.808	49.986	−33.240	1.00	85.67	C
ATOM	2561	SG	CYS	B	526	−67.028	51.045	−32.001	1.00	86.73	S
ATOM	2562	C	CYS	B	526	−69.216	49.854	−35.307	1.00	86.72	C
ATOM	2563	O	CYS	B	526	−70.177	49.127	−35.059	1.00	86.85	O
ATOM	2564	N	CYS	B	527	−68.638	49.930	−36.517	1.00	86.58	N
ATOM	2565	CA	CYS	B	527	−69.110	49.182	−37.679	1.00	88.11	C
ATOM	2566	CB	CYS	B	527	−69.933	50.094	−38.590	1.00	87.81	C
ATOM	2567	SG	CYS	B	527	−71.199	51.072	−37.722	1.00	87.72	S
ATOM	2568	C	CYS	B	527	−68.031	48.439	−38.457	1.00	89.37	C
ATOM	2569	O	CYS	B	527	−66.840	48.717	−38.310	1.00	89.09	O
ATOM	2570	N	LEU	B	528	−68.464	47.481	−39.284	1.00	91.74	N
ATOM	2571	CA	LEU	B	528	−67.579	46.684	−40.136	1.00	94.12	C
ATOM	2572	CB	LEU	B	528	−67.845	45.175	−39.990	1.00	93.84	C
ATOM	2573	CG	LEU	B	528	−67.467	44.499	−38.679	1.00	93.16	C
ATOM	2574	CD1	LEU	B	528	−67.902	43.074	−38.710	1.00	92.63	C
ATOM	2575	CD2	LEU	B	528	−65.968	44.576	−38.403	1.00	92.08	C
ATOM	2576	C	LEU	B	528	−67.726	47.142	−41.604	1.00	96.20	C
ATOM	2577	O	LEU	B	528	−68.639	46.703	−42.330	1.00	96.27	O
ATOM	2578	N	LEU	B	529	−66.826	48.060	−42.013	1.00	101.19	N
ATOM	2579	CA	LEU	B	529	−66.801	48.654	−43.341	1.00	103.82	C
ATOM	2580	CB	LEU	B	529	−67.066	50.162	−43.241	1.00	103.71	C
ATOM	2581	CG	LEU	B	529	−67.526	50.876	−44.500	1.00	103.99	C
ATOM	2582	CD1	LEU	B	529	−68.929	50.463	−44.903	1.00	103.65	C
ATOM	2583	CD2	LEU	B	529	−67.502	52.368	−44.292	1.00	104.17	C
ATOM	2584	C	LEU	B	529	−65.463	48.354	−43.998	1.00	105.85	C
ATOM	2585	O	LEU	B	529	−64.440	48.938	−43.629	1.00	105.85	O
ATOM	2586	N	PRO	B	530	−65.462	47.394	−44.950	1.00	113.01	N
ATOM	2587	CA	PRO	B	530	−64.207	47.020	−45.619	1.00	114.85	C
ATOM	2588	CB	PRO	B	530	−64.560	45.707	−46.324	1.00	114.74	C
ATOM	2589	CG	PRO	B	530	−66.027	45.796	−46.581	1.00	114.03	C
ATOM	2590	CD	PRO	B	530	−66.609	46.618	−45.471	1.00	113.18	C
ATOM	2591	C	PRO	B	530	−63.733	48.104	−46.587	1.00	116.79	C
ATOM	2592	O	PRO	B	530	−64.550	48.652	−47.352	1.00	117.04	O
ATOM	2593	N	GLN	B	531	−62.405	48.413	−46.538	1.00	120.37	N
ATOM	2594	CA	GLN	B	531	−61.736	49.449	−47.339	1.00	122.30	C
ATOM	2595	CB	GLN	B	531	−61.674	49.073	−48.844	1.00	122.37	C
ATOM	2596	CG	GLN	B	531	−60.765	47.872	−49.170	1.00	123.50	C
ATOM	2597	CD	GLN	B	531	−61.035	47.202	−50.518	1.00	125.13	C
ATOM	2598	OE1	GLN	B	531	−61.895	47.613	−51.314	1.00	125.49	O
ATOM	2599	NE2	GLN	B	531	−60.297	46.132	−50.803	1.00	125.67	N
ATOM	2600	C	GLN	B	531	−62.456	50.797	−47.061	1.00	123.38	C
ATOM	2601	O	GLN	B	531	−63.323	51.236	−47.832	1.00	123.60	O
ATOM	2602	N	ALA	B	532	−62.136	51.406	−45.908	1.00	124.93	N
ATOM	2603	CA	ALA	B	532	−62.755	52.653	−45.485	1.00	126.34	C
ATOM	2604	CB	ALA	B	532	−63.765	52.379	−44.380	1.00	126.15	C
ATOM	2605	C	ALA	B	532	−61.735	53.690	−45.027	1.00	127.47	C
ATOM	2606	O	ALA	B	532	−60.935	53.423	−44.123	1.00	127.79	O
ATOM	2607	N	ASN	B	533	−61.760	54.874	−45.667	1.00	129.58	N
ATOM	2608	CA	ASN	B	533	−60.896	56.006	−45.335	1.00	130.77	C
ATOM	2609	CB	ASN	B	533	−60.371	56.707	−46.611	1.00	130.82	C
ATOM	2610	CG	ASN	B	533	−59.372	55.919	−47.435	1.00	131.44	C
ATOM	2611	OD1	ASN	B	533	−58.173	55.852	−47.120	1.00	132.13	O
ATOM	2612	ND2	ASN	B	533	−59.841	55.321	−48.530	1.00	131.80	N
ATOM	2613	C	ASN	B	533	−61.818	56.929	−44.539	1.00	131.52	C
ATOM	2614	O	ASN	B	533	−62.575	57.704	−45.132	1.00	131.65	O
ATOM	2615	N	CYS	B	534	−61.818	56.803	−43.207	1.00	132.79	N
ATOM	2616	CA	CYS	B	534	−62.710	57.648	−42.419	1.00	133.86	C
ATOM	2617	CB	CYS	B	534	−63.591	56.830	−41.481	1.00	133.93	C
ATOM	2618	SG	CYS	B	534	−64.768	55.741	−42.336	1.00	135.03	S
ATOM	2619	C	CYS	B	534	−62.004	58.801	−41.720	1.00	134.34	C
ATOM	2620	O	CYS	B	534	−60.982	58.585	−41.062	1.00	134.48	O
ATOM	2621	N	SER	B	535	−62.545	60.034	−41.898	1.00	133.21	N
ATOM	2622	CA	SER	B	535	−61.988	61.287	−41.371	1.00	133.80	C
ATOM	2623	CB	SER	B	535	−61.343	62.075	−42.512	1.00	133.78	C
ATOM	2624	OG	SER	B	535	−62.285	62.439	−43.512	1.00	134.38	O
ATOM	2625	C	SER	B	535	−62.971	62.205	−40.630	1.00	134.13	C
ATOM	2626	O	SER	B	535	−64.168	62.208	−40.920	1.00	133.92	O
ATOM	2627	N	VAL	B	536	−62.436	63.018	−39.704	1.00	133.66	N
ATOM	2628	CA	VAL	B	536	−63.204	63.990	−38.926	1.00	134.48	C
ATOM	2629	CB	VAL	B	536	−62.823	64.004	−37.423	1.00	134.45	C
ATOM	2630	CG1	VAL	B	536	−63.703	64.970	−36.626	1.00	134.41	C
ATOM	2631	CG2	VAL	B	536	−62.907	62.610	−36.834	1.00	134.51	C
ATOM	2632	C	VAL	B	536	−63.047	65.372	−39.554	1.00	135.15	C
ATOM	2633	O	VAL	B	536	−61.924	65.824	−39.800	1.00	135.25	O
ATOM	2634	N	HIS	B	537	−64.176	66.039	−39.809	1.00	136.24	N
ATOM	2635	CA	HIS	B	537	−64.192	67.375	−40.380	1.00	137.05	C
ATOM	2636	CB	HIS	B	537	−65.002	67.415	−41.688	1.00	137.20	C
ATOM	2637	CG	HIS	B	537	−64.287	66.848	−42.883	1.00	138.47	C
ATOM	2638	ND1	HIS	B	537	−64.571	67.293	−44.171	1.00	139.63	N
ATOM	2639	CE1	HIS	B	537	−63.786	66.590	−44.974	1.00	139.83	C
ATOM	2640	NE2	HIS	B	537	−63.020	65.733	−44.288	1.00	139.91	N
ATOM	2641	CD2	HIS	B	537	−63.331	65.887	−42.955	1.00	139.28	C
ATOM	2642	C	HIS	B	537	−64.690	68.370	−39.330	1.00	137.40	C
ATOM	2643	O	HIS	B	537	−65.864	68.736	−39.305	1.00	137.42	O
ATOM	2644	N	THR	B	538	−63.777	68.780	−38.441	1.00	136.73	N
ATOM	2645	CA	THR	B	538	−64.031	69.734	−37.362	1.00	137.31	C
ATOM	2646	CB	THR	B	538	−62.838	69.736	−36.391	1.00	137.31	C
ATOM	2647	OG1	THR	B	538	−62.335	68.410	−36.237	1.00	137.37	O
ATOM	2648	CG2	THR	B	538	−63.182	70.320	−35.032	1.00	137.41	C
ATOM	2649	C	THR	B	538	−64.244	71.142	−37.951	1.00	137.73	C
ATOM	2650	O	THR	B	538	−63.608	71.494	−38.949	1.00	137.83	O
ATOM	2651	N	ALA	B	539	−65.130	71.940	−37.328	1.00	137.80	N
ATOM	2652	CA	ALA	B	539	−65.430	73.316	−37.741	1.00	138.09	C
ATOM	2653	CB	ALA	B	539	−66.688	73.353	−38.607	1.00	137.95	C
ATOM	2654	C	ALA	B	539	−65.597	74.208	−36.488	1.00	138.39	C
ATOM	2655	O	ALA	B	539	−66.600	74.053	−35.789	1.00	138.43	O
ATOM	2656	N	PRO	B	540	−64.639	75.124	−36.163	1.00	137.90	N
ATOM	2657	CA	PRO	B	540	−64.789	75.965	−34.955	1.00	138.18	C
ATOM	2658	CB	PRO	B	540	−63.554	76.868	−35.000	1.00	138.11	C
ATOM	2659	CG	PRO	B	540	−62.563	76.098	−35.784	1.00	138.04	C
ATOM	2660	CD	PRO	B	540	−63.372	75.428	−36.854	1.00	137.89	C
ATOM	2661	C	PRO	B	540	−66.092	76.771	−34.890	1.00	138.52	C
ATOM	2662	O	PRO	B	540	−66.703	77.001	−35.937	1.00	138.52	O
ATOM	2663	N	PRO	B	541	−66.550	77.190	−33.683	1.00	140.26	N
ATOM	2664	CA	PRO	B	541	−67.822	77.938	−33.594	1.00	140.69	C
ATOM	2665	CB	PRO	B	541	−67.994	78.175	−32.090	1.00	140.62	C
ATOM	2666	CG	PRO	B	541	−67.103	77.184	−31.430	1.00	140.29	C
ATOM	2667	CD	PRO	B	541	−65.952	76.993	−32.347	1.00	140.16	C
ATOM	2668	C	PRO	B	541	−67.874	79.243	−34.397	1.00	141.21	C
ATOM	2669	O	PRO	B	541	−66.997	80.103	−34.245	1.00	141.24	O
ATOM	2670	N	ALA	B	542	−68.902	79.372	−35.269	1.00	143.91	N
ATOM	2671	CA	ALA	B	542	−69.118	80.543	−36.131	1.00	144.42	C
ATOM	2672	CB	ALA	B	542	−69.882	80.143	−37.381	1.00	144.31	C
ATOM	2673	C	ALA	B	542	−69.822	81.712	−35.419	1.00	144.79	C
ATOM	2674	O	ALA	B	542	−69.664	82.863	−35.843	1.00	144.89	O
ATOM	2675	N	GLU	B	543	−70.603	81.409	−34.344	1.00	146.53	N
ATOM	2676	CA	GLU	B	543	−71.364	82.347	−33.488	1.00	146.91	C
ATOM	2677	CB	GLU	B	543	−70.434	83.292	−32.689	1.00	146.88	C
ATOM	2678	CG	GLU	B	543	−69.338	82.595	−31.894	1.00	147.35	C
ATOM	2679	CD	GLU	B	543	−67.935	83.145	−32.090	1.00	147.98	C
ATOM	2680	OE1	GLU	B	543	−67.271	83.452	−31.072	1.00	148.23	O
ATOM	2681	OE2	GLU	B	543	−67.497	83.270	−33.258	1.00	148.17	O
ATOM	2682	C	GLU	B	543	−72.480	83.137	−34.206	1.00	147.16	C
ATOM	2683	O	GLU	B	543	−73.279	83.804	−33.539	1.00	147.21	O
ATOM	2684	N	ALA	B	544	−72.538	83.042	−35.553	1.00	149.04	N
ATOM	2685	CA	ALA	B	544	−73.493	83.719	−36.434	1.00	149.34	C
ATOM	2686	CB	ALA	B	544	−72.873	83.882	−37.817	1.00	149.30	C
ATOM	2687	C	ALA	B	544	−74.877	83.025	−36.540	1.00	149.62	C
ATOM	2688	O	ALA	B	544	−75.082	81.958	−35.948	1.00	149.52	O
ATOM	2689	N	SER	B	545	−75.827	83.658	−37.299	1.00	151.45	N
ATOM	2690	CA	SER	B	545	−77.200	83.181	−37.566	1.00	151.69	C
ATOM	2691	CB	SER	B	545	−78.032	84.266	−38.246	1.00	151.68	C
ATOM	2692	OG	SER	B	545	−78.545	85.206	−37.317	1.00	151.78	O
ATOM	2693	C	SER	B	545	−77.176	81.923	−38.437	1.00	151.85	C
ATOM	2694	O	SER	B	545	−78.085	81.092	−38.348	1.00	151.87	O
ATOM	2695	N	MET	B	546	−76.114	81.791	−39.272	1.00	153.34	N
ATOM	2696	CA	MET	B	546	−75.849	80.651	−40.155	1.00	153.39	C
ATOM	2697	CB	MET	B	546	−74.703	80.994	−41.125	1.00	153.18	C
ATOM	2698	C	MET	B	546	−75.479	79.409	−39.301	1.00	153.47	C
ATOM	2699	O	MET	B	546	−75.531	78.278	−39.800	1.00	153.61	O
ATOM	2700	N	GLY	B	547	−75.123	79.654	−38.028	1.00	153.18	N
ATOM	2701	CA	GLY	B	547	−74.730	78.652	−37.042	1.00	152.83	C
ATOM	2702	C	GLY	B	547	−73.400	78.010	−37.378	1.00	152.65	C
ATOM	2703	O	GLY	B	547	−72.613	78.582	−38.144	1.00	152.76	O
ATOM	2704	N	THR	B	548	−73.138	76.812	−36.812	1.00	150.47	N
ATOM	2705	CA	THR	B	548	−71.906	76.068	−37.091	1.00	149.88	C
ATOM	2706	CB	THR	B	548	−71.132	75.686	−35.821	1.00	149.84	C
ATOM	2707	OG1	THR	B	548	−71.382	76.632	−34.786	1.00	149.65	O
ATOM	2708	CG2	THR	B	548	−69.648	75.634	−36.061	1.00	149.67	C
ATOM	2709	C	THR	B	548	−72.256	74.903	−38.018	1.00	149.55	C
ATOM	2710	O	THR	B	548	−73.048	74.028	−37.651	1.00	149.53	O
ATOM	2711	N	ARG	B	549	−71.690	74.925	−39.238	1.00	147.12	N
ATOM	2712	CA	ARG	B	549	−71.929	73.922	−40.278	1.00	146.62	C
ATOM	2713	CB	ARG	B	549	−72.792	74.529	−41.403	1.00	146.51	C
ATOM	2714	CG	ARG	B	549	−74.211	74.886	−40.969	1.00	146.04	C
ATOM	2715	CD	ARG	B	549	−74.934	75.740	−41.987	1.00	145.51	C
ATOM	2716	NE	ARG	B	549	−76.346	75.935	−41.643	1.00	144.95	N
ATOM	2717	CZ	ARG	B	549	−77.362	75.291	−42.217	1.00	144.63	C
ATOM	2718	NH1	ARG	B	549	−77.136	74.398	−43.175	1.00	144.47	N
ATOM	2719	NH2	ARG	B	549	−78.611	75.536	−41.840	1.00	144.53	N
ATOM	2720	C	ARG	B	549	−70.622	73.340	−40.844	1.00	146.42	C
ATOM	2721	O	ARG	B	549	−69.584	74.009	−40.816	1.00	146.41	O
ATOM	2722	N	VAL	B	550	−70.684	72.080	−41.337	1.00	145.57	N
ATOM	2723	CA	VAL	B	550	−69.584	71.312	−41.954	1.00	145.24	C
ATOM	2724	CB	VAL	B	550	−68.425	70.923	−40.987	1.00	145.19	C
ATOM	2725	CG1	VAL	B	550	−68.861	69.903	−39.940	1.00	145.05	C
ATOM	2726	CG2	VAL	B	550	−67.199	70.440	−41.753	1.00	145.00	C
ATOM	2727	C	VAL	B	550	−70.151	70.126	−42.755	1.00	145.09	C
ATOM	2728	O	VAL	B	550	−71.102	69.486	−42.295	1.00	145.05	O
ATOM	2729	N	HIS	B	551	−69.587	69.850	−43.956	1.00	145.41	N
ATOM	2730	CA	HIS	B	551	−70.079	68.758	−44.798	1.00	145.22	C
ATOM	2731	CB	HIS	B	551	−71.275	69.187	−45.673	1.00	145.55	C
ATOM	2732	CG	HIS	B	551	−70.979	70.102	−46.819	1.00	146.57	C
ATOM	2733	ND1	HIS	B	551	−70.529	71.399	−46.618	1.00	147.29	N
ATOM	2734	CE1	HIS	B	551	−70.406	71.925	−47.826	1.00	147.67	C
ATOM	2735	NE2	HIS	B	551	−70.775	71.061	−48.778	1.00	147.78	N
ATOM	2736	CD2	HIS	B	551	−71.158	69.900	−48.147	1.00	147.30	C
ATOM	2737	C	HIS	B	551	−69.075	67.895	−45.558	1.00	144.66	C
ATOM	2738	O	HIS	B	551	−67.962	68.337	−45.874	1.00	144.55	O
ATOM	2739	N	CYS	B	552	−69.501	66.638	−45.833	1.00	142.01	N
ATOM	2740	CA	CYS	B	552	−68.746	65.621	−46.566	1.00	141.40	C
ATOM	2741	CB	CYS	B	552	−69.012	64.216	−46.023	1.00	141.22	C
ATOM	2742	SG	CYS	B	552	−68.536	63.969	−44.292	1.00	139.76	S
ATOM	2743	C	CYS	B	552	−69.128	65.732	−48.037	1.00	141.30	C
ATOM	2744	O	CYS	B	552	−70.177	65.231	−48.462	1.00	141.33	O
ATOM	2745	N	HIS	B	553	−68.278	66.420	−48.799	1.00	140.49	N
ATOM	2746	CA	HIS	B	553	−68.472	66.649	−50.224	1.00	140.01	C
ATOM	2747	CB	HIS	B	553	−68.969	68.077	−50.447	1.00	140.00	C
ATOM	2748	C	HIS	B	553	−67.175	66.373	−50.985	1.00	139.66	C
ATOM	2749	O	HIS	B	553	−66.997	66.840	−52.114	1.00	139.69	O
ATOM	2750	N	GLN	B	554	−66.277	65.584	−50.354	1.00	137.93	N
ATOM	2751	CA	GLN	B	554	−64.980	65.160	−50.881	1.00	137.37	C
ATOM	2752	CB	GLN	B	554	−64.135	64.574	−49.728	1.00	137.42	C
ATOM	2753	CG	GLN	B	554	−62.657	64.982	−49.707	1.00	137.46	C
ATOM	2754	CD	GLN	B	554	−61.878	64.336	−48.570	1.00	137.87	C
ATOM	2755	OE1	GLN	B	554	−62.354	64.218	−47.431	1.00	138.13	O
ATOM	2756	NE2	GLN	B	554	−60.652	63.905	−48.848	1.00	137.66	N
ATOM	2757	C	GLN	B	554	−65.214	64.123	−52.013	1.00	136.96	C
ATOM	2758	O	GLN	B	554	−66.355	63.942	−52.465	1.00	136.89	O
ATOM	2759	N	GLN	B	555	−64.140	63.455	−52.472	1.00	136.84	N
ATOM	2760	CA	GLN	B	555	−64.193	62.457	−53.544	1.00	136.32	C
ATOM	2761	CB	GLN	B	555	−62.766	62.050	−53.968	1.00	136.30	C
ATOM	2762	C	GLN	B	555	−65.084	61.219	−53.223	1.00	135.91	C
ATOM	2763	O	GLN	B	555	−64.559	60.153	−52.872	1.00	136.01	O
ATOM	2764	N	GLY	B	556	−66.413	61.384	−53.354	1.00	133.72	N
ATOM	2765	CA	GLY	B	556	−67.408	60.339	−53.098	1.00	132.66	C
ATOM	2766	C	GLY	B	556	−67.532	59.892	−51.649	1.00	131.92	C
ATOM	2767	O	GLY	B	556	−68.062	58.806	−51.374	1.00	131.89	O
ATOM	2768	N	HIS	B	557	−67.022	60.734	−50.718	1.00	130.00	N
ATOM	2769	CA	HIS	B	557	−67.022	60.539	−49.268	1.00	129.20	C
ATOM	2770	CB	HIS	B	557	−66.075	61.560	−48.601	1.00	129.39	C
ATOM	2771	CG	HIS	B	557	−64.616	61.179	−48.582	1.00	130.76	C
ATOM	2772	ND1	HIS	B	557	−63.909	60.921	−49.757	1.00	131.87	N
ATOM	2773	CE1	HIS	B	557	−62.667	60.645	−49.378	1.00	131.98	C
ATOM	2774	NE2	HIS	B	557	−62.530	60.719	−48.050	1.00	132.18	N
ATOM	2775	CD2	HIS	B	557	−63.762	61.075	−47.531	1.00	131.65	C
ATOM	2776	C	HIS	B	557	−68.452	60.738	−48.744	1.00	128.37	C
ATOM	2777	O	HIS	B	557	−69.127	61.687	−49.166	1.00	128.41	O
ATOM	2778	N	VAL	B	558	−68.922	59.845	−47.833	1.00	123.42	N
ATOM	2779	CA	VAL	B	558	−70.278	59.929	−47.252	1.00	122.31	C
ATOM	2780	CB	VAL	B	558	−71.199	58.691	−47.485	1.00	122.30	C
ATOM	2781	CG1	VAL	B	558	−72.624	59.133	−47.810	1.00	122.05	C
ATOM	2782	CG2	VAL	B	558	−70.663	57.762	−48.573	1.00	122.17	C
ATOM	2783	C	VAL	B	558	−70.256	60.358	−45.777	1.00	121.63	C
ATOM	2784	O	VAL	B	558	−69.283	60.081	−45.068	1.00	121.34	O
ATOM	2785	N	LEU	B	559	−71.327	61.051	−45.332	1.00	117.23	N
ATOM	2786	CA	LEU	B	559	−71.486	61.517	−43.958	1.00	116.45	C
ATOM	2787	CB	LEU	B	559	−72.326	62.806	−43.897	1.00	116.37	C
ATOM	2788	CG	LEU	B	559	−72.570	63.383	−42.503	1.00	115.80	C
ATOM	2789	CD1	LEU	B	559	−71.488	64.347	−42.122	1.00	115.41	C
ATOM	2790	CD2	LEU	B	559	−73.930	64.037	−42.415	1.00	115.21	C
ATOM	2791	C	LEU	B	559	−72.162	60.397	−43.186	1.00	116.11	C
ATOM	2792	O	LEU	B	559	−73.250	59.945	−43.567	1.00	115.98	O
ATOM	2793	N	THR	B	560	−71.501	59.946	−42.109	1.00	114.52	N
ATOM	2794	CA	THR	B	560	−71.975	58.856	−41.261	1.00	114.17	C
ATOM	2795	CB	THR	B	560	−70.936	57.742	−41.193	1.00	114.04	C
ATOM	2796	OG1	THR	B	560	−69.707	58.299	−40.747	1.00	113.63	O
ATOM	2797	CG2	THR	B	560	−70.738	57.039	−42.529	1.00	113.63	C
ATOM	2798	C	THR	B	560	−72.408	59.303	−39.877	1.00	114.27	C
ATOM	2799	O	THR	B	560	−73.401	58.785	−39.366	1.00	114.13	O
ATOM	2800	N	GLY	B	561	−71.673	60.243	−39.282	1.00	117.40	N
ATOM	2801	CA	GLY	B	561	−71.985	60.734	−37.945	1.00	117.64	C
ATOM	2802	C	GLY	B	561	−71.793	62.211	−37.677	1.00	117.75	C
ATOM	2803	O	GLY	B	561	−70.841	62.828	−38.169	1.00	117.59	O
ATOM	2804	N	CYS	B	562	−72.706	62.763	−36.849	1.00	121.48	N
ATOM	2805	CA	CYS	B	562	−72.740	64.161	−36.417	1.00	121.78	C
ATOM	2806	CB	CYS	B	562	−74.093	64.807	−36.735	1.00	122.20	C
ATOM	2807	SG	CYS	B	562	−74.284	65.432	−38.438	1.00	124.74	S
ATOM	2808	C	CYS	B	562	−72.408	64.282	−34.924	1.00	121.24	C
ATOM	2809	O	CYS	B	562	−73.171	63.821	−34.071	1.00	121.19	O
ATOM	2810	N	SER	B	563	−71.279	64.913	−34.617	1.00	117.71	N
ATOM	2811	CA	SER	B	563	−70.834	65.153	−33.246	1.00	117.39	C
ATOM	2812	CB	SER	B	563	−69.533	64.413	−32.958	1.00	117.54	C
ATOM	2813	OG	SER	B	563	−69.786	63.090	−32.517	1.00	117.97	O
ATOM	2814	C	SER	B	563	−70.649	66.651	−33.033	1.00	116.99	C
ATOM	2815	O	SER	B	563	−70.457	67.375	−34.006	1.00	116.83	O
ATOM	2816	N	SER	B	564	−70.711	67.120	−31.773	1.00	114.82	N
ATOM	2817	CA	SER	B	564	−70.551	68.535	−31.436	1.00	114.48	C
ATOM	2818	CB	SER	B	564	−71.828	69.317	−31.734	1.00	114.59	C
ATOM	2819	OG	SER	B	564	−71.646	70.710	−31.531	1.00	114.76	O
ATOM	2820	C	SER	B	564	−70.180	68.741	−29.992	1.00	114.22	C
ATOM	2821	O	SER	B	564	−70.838	68.191	−29.107	1.00	114.08	O
ATOM	2822	N	HIS	B	565	−69.151	69.574	−29.749	1.00	113.98	N
ATOM	2823	CA	HIS	B	565	−68.708	69.894	−28.392	1.00	113.78	C
ATOM	2824	CB	HIS	B	565	−67.494	69.057	−27.985	1.00	113.77	C
ATOM	2825	CG	HIS	B	565	−66.183	69.733	−28.190	1.00	113.56	C
ATOM	2826	ND1	HIS	B	565	−65.582	69.762	−29.427	1.00	113.36	N
ATOM	2827	CE1	HIS	B	565	−64.445	70.415	−29.253	1.00	113.77	C
ATOM	2828	NE2	HIS	B	565	−64.295	70.814	−27.985	1.00	113.71	N
ATOM	2829	CD2	HIS	B	565	−65.397	70.382	−27.297	1.00	113.47	C
ATOM	2830	C	HIS	B	565	−68.514	71.397	−28.124	1.00	113.61	C
ATOM	2831	O	HIS	B	565	−68.098	72.138	−29.014	1.00	113.77	O
ATOM	2832	N	TRP	B	566	−68.811	71.832	−26.887	1.00	111.53	N
ATOM	2833	CA	TRP	B	566	−68.699	73.226	−26.459	1.00	111.30	C
ATOM	2834	CB	TRP	B	566	−70.073	73.892	−26.382	1.00	110.76	C
ATOM	2835	CG	TRP	B	566	−71.099	73.138	−25.594	1.00	108.53	C
ATOM	2836	CD1	TRP	B	566	−71.464	73.367	−24.303	1.00	107.11	C
ATOM	2837	NE1	TRP	B	566	−72.470	72.505	−23.934	1.00	106.14	N
ATOM	2838	CE2	TRP	B	566	−72.776	71.694	−24.996	1.00	105.83	C
ATOM	2839	CD2	TRP	B	566	−71.936	72.070	−26.065	1.00	106.56	C
ATOM	2840	CE3	TRP	B	566	−72.043	71.377	−27.284	1.00	105.74	C
ATOM	2841	CZ3	TRP	B	566	−72.978	70.362	−27.399	1.00	104.64	C
ATOM	2842	CH2	TRP	B	566	−73.805	70.015	−26.323	1.00	104.70	C
ATOM	2843	CZ2	TRP	B	566	−73.721	70.664	−25.111	1.00	105.03	C
ATOM	2844	C	TRP	B	566	−67.886	73.431	−25.176	1.00	111.98	C
ATOM	2845	O	TRP	B	566	−67.531	72.456	−24.509	1.00	111.85	O
ATOM	2846	N	GLU	B	567	−67.561	74.707	−24.858	1.00	114.23	N
ATOM	2847	CA	GLU	B	567	−66.761	75.104	−23.688	1.00	115.12	C
ATOM	2848	CB	GLU	B	567	−65.441	75.762	−24.139	1.00	115.08	C
ATOM	2849	CG	GLU	B	567	−64.472	74.828	−24.866	1.00	115.87	C
ATOM	2850	CD	GLU	B	567	−64.594	74.654	−26.379	1.00	117.42	C
ATOM	2851	OE1	GLU	B	567	−63.621	74.151	−26.991	1.00	118.08	O
ATOM	2852	OE2	GLU	B	567	−65.652	75.009	−26.953	1.00	117.83	O
ATOM	2853	C	GLU	B	567	−67.542	75.993	−22.684	1.00	115.59	C
ATOM	2854	O	GLU	B	567	−67.103	76.191	−21.549	1.00	115.56	O
ATOM	2855	N	VAL	B	568	−68.716	76.482	−23.111	1.00	117.31	N
ATOM	2856	CA	VAL	B	568	−69.635	77.344	−22.368	1.00	118.32	C
ATOM	2857	CB	VAL	B	568	−70.463	78.177	−23.408	1.00	118.29	C
ATOM	2858	CG1	VAL	B	568	−71.539	77.344	−24.110	1.00	118.30	C
ATOM	2859	CG2	VAL	B	568	−71.051	79.447	−22.803	1.00	118.56	C
ATOM	2860	C	VAL	B	568	−70.501	76.567	−21.313	1.00	119.01	C
ATOM	2861	O	VAL	B	568	−70.265	75.385	−21.061	1.00	119.09	O
ATOM	2862	N	GLU	B	569	−71.477	77.251	−20.693	1.00	122.68	N
ATOM	2863	CA	GLU	B	569	−72.409	76.693	−19.717	1.00	123.60	C
ATOM	2864	CB	GLU	B	569	−72.467	77.576	−18.453	1.00	123.70	C
ATOM	2865	CG	GLU	B	569	−73.180	76.948	−17.254	1.00	124.32	C
ATOM	2866	CD	GLU	B	569	−74.701	77.019	−17.209	1.00	125.29	C
ATOM	2867	OE1	GLU	B	569	−75.277	78.004	−17.728	1.00	125.60	O
ATOM	2868	OE2	GLU	B	569	−75.319	76.086	−16.644	1.00	125.58	O
ATOM	2869	C	GLU	B	569	−73.802	76.581	−20.364	1.00	124.11	C
ATOM	2870	O	GLU	B	569	−74.515	75.611	−20.085	1.00	124.23	O
ATOM	2871	N	ASP	B	570	−74.194	77.564	−21.219	1.00	125.99	N
ATOM	2872	CA	ASP	B	570	−75.518	77.548	−21.864	1.00	126.58	C
ATOM	2873	CB	ASP	B	570	−76.498	78.498	−21.136	1.00	126.73	C
ATOM	2874	CG	ASP	B	570	−77.684	77.795	−20.486	1.00	127.25	C
ATOM	2875	OD1	ASP	B	570	−77.472	77.067	−19.479	1.00	127.50	O
ATOM	2876	OD2	ASP	B	570	−78.825	77.974	−20.980	1.00	127.65	O
ATOM	2877	C	ASP	B	570	−75.590	77.646	−23.424	1.00	126.73	C
ATOM	2878	O	ASP	B	570	−74.856	76.924	−24.118	1.00	126.77	O
ATOM	2879	N	LEU	B	571	−76.516	78.506	−23.954	1.00	124.61	N
ATOM	2880	CA	LEU	B	571	−76.769	78.734	−25.387	1.00	124.78	C
ATOM	2881	CB	LEU	B	571	−77.398	77.485	−26.034	1.00	124.75	C
ATOM	2882	C	LEU	B	571	−77.608	80.015	−25.697	1.00	124.83	C
ATOM	2883	O	LEU	B	571	−77.023	81.037	−26.069	1.00	125.00	O
ATOM	2884	N	GLY	B	572	−78.945	79.933	−25.562	1.00	119.93	N
ATOM	2885	CA	GLY	B	572	−79.876	81.033	−25.819	1.00	119.70	C
ATOM	2886	C	GLY	B	572	−80.172	81.292	−27.285	1.00	119.66	C
ATOM	2887	O	GLY	B	572	−81.252	81.776	−27.636	1.00	119.48	O
ATOM	2888	N	GLN	B	584	−78.485	72.651	−48.615	1.00	150.06	N
ATOM	2889	CA	GLN	B	584	−77.758	72.137	−47.448	1.00	150.10	C
ATOM	2890	CB	GLN	B	584	−78.497	72.514	−46.135	1.00	150.24	C
ATOM	2891	CG	GLN	B	584	−79.016	73.963	−46.047	1.00	150.44	C
ATOM	2892	CD	GLN	B	584	−80.441	74.074	−45.527	1.00	150.94	C
ATOM	2893	OE1	GLN	B	584	−80.989	73.160	−44.898	1.00	151.33	O
ATOM	2894	NE2	GLN	B	584	−81.078	75.207	−45.777	1.00	150.78	N
ATOM	2895	C	GLN	B	584	−77.532	70.583	−47.559	1.00	149.91	C
ATOM	2896	O	GLN	B	584	−78.009	69.837	−46.690	1.00	149.95	O
ATOM	2897	N	PRO	B	585	−76.804	70.067	−48.596	1.00	147.52	N
ATOM	2898	CA	PRO	B	585	−76.641	68.600	−48.725	1.00	147.11	C
ATOM	2899	CB	PRO	B	585	−76.683	68.379	−50.247	1.00	147.20	C
ATOM	2900	CG	PRO	B	585	−76.395	69.773	−50.875	1.00	147.42	C
ATOM	2901	CD	PRO	B	585	−76.181	70.757	−49.746	1.00	147.59	C
ATOM	2902	C	PRO	B	585	−75.394	67.962	−48.090	1.00	146.51	C
ATOM	2903	O	PRO	B	585	−74.286	68.507	−48.215	1.00	146.59	O
ATOM	2904	N	ASN	B	586	−75.584	66.773	−47.437	1.00	140.53	N
ATOM	2905	CA	ASN	B	586	−74.557	65.960	−46.745	1.00	139.64	C
ATOM	2906	CB	ASN	B	586	−73.540	65.361	−47.762	1.00	139.67	C
ATOM	2907	CG	ASN	B	586	−73.382	63.848	−47.758	1.00	139.54	C
ATOM	2908	OD1	ASN	B	586	−72.264	63.324	−47.760	1.00	139.19	O
ATOM	2909	ND2	ASN	B	586	−74.483	63.103	−47.775	1.00	139.50	N
ATOM	2910	C	ASN	B	586	−73.854	66.757	−45.611	1.00	139.03	C
ATOM	2911	O	ASN	B	586	−72.642	66.614	−45.420	1.00	138.94	O
ATOM	2912	N	GLN	B	587	−74.640	67.573	−44.850	1.00	133.89	N
ATOM	2913	CA	GLN	B	587	−74.172	68.457	−43.772	1.00	133.19	C
ATOM	2914	CB	GLN	B	587	−74.544	69.920	−44.107	1.00	133.41	C
ATOM	2915	CG	GLN	B	587	−73.611	70.981	−43.503	1.00	134.10	C
ATOM	2916	CD	GLN	B	587	−73.858	72.385	−44.004	1.00	135.07	C
ATOM	2917	OE1	GLN	B	587	−74.969	72.928	−43.898	1.00	135.42	O
ATOM	2918	NE2	GLN	B	587	−72.812	73.011	−44.542	1.00	135.30	N
ATOM	2919	C	GLN	B	587	−74.564	68.125	−42.319	1.00	132.46	C
ATOM	2920	O	GLN	B	587	−75.651	67.611	−42.038	1.00	132.24	O
ATOM	2921	N	CYS	B	588	−73.642	68.469	−41.404	1.00	127.56	N
ATOM	2922	CA	CYS	B	588	−73.739	68.333	−39.955	1.00	126.80	C
ATOM	2923	CB	CYS	B	588	−72.441	67.765	−39.381	1.00	126.59	C
ATOM	2924	SG	CYS	B	588	−72.434	65.971	−39.116	1.00	125.32	S
ATOM	2925	C	CYS	B	588	−73.998	69.737	−39.413	1.00	126.66	C
ATOM	2926	O	CYS	B	588	−73.106	70.597	−39.478	1.00	126.58	O
ATOM	2927	N	VAL	B	589	−75.203	69.979	−38.882	1.00	125.88	N
ATOM	2928	CA	VAL	B	589	−75.524	71.301	−38.350	1.00	125.64	C
ATOM	2929	CB	VAL	B	589	−76.688	71.994	−39.099	1.00	125.70	C
ATOM	2930	CG1	VAL	B	589	−76.844	73.445	−38.646	1.00	125.90	C
ATOM	2931	CG2	VAL	B	589	−76.497	71.921	−40.615	1.00	125.82	C
ATOM	2932	C	VAL	B	589	−75.699	71.334	−36.832	1.00	125.41	C
ATOM	2933	O	VAL	B	589	−76.718	70.880	−36.312	1.00	125.19	O
ATOM	2934	N	GLY	B	590	−74.703	71.898	−36.154	1.00	127.02	N
ATOM	2935	CA	GLY	B	590	−74.688	72.066	−34.705	1.00	126.97	C
ATOM	2936	C	GLY	B	590	−74.906	73.513	−34.301	1.00	126.94	C
ATOM	2937	O	GLY	B	590	−74.917	74.401	−35.162	1.00	126.90	O
ATOM	2938	N	HIS	B	591	−75.077	73.763	−32.980	1.00	128.31	N
ATOM	2939	CA	HIS	B	591	−75.290	75.093	−32.382	1.00	128.33	C
ATOM	2940	CB	HIS	B	591	−75.465	74.964	−30.851	1.00	128.36	C
ATOM	2941	CG	HIS	B	591	−75.848	76.229	−30.138	1.00	128.50	C
ATOM	2942	ND1	HIS	B	591	−74.894	77.149	−29.728	1.00	128.48	N
ATOM	2943	CE1	HIS	B	591	−75.564	78.124	−29.135	1.00	128.57	C
ATOM	2944	NE2	HIS	B	591	−76.874	77.883	−29.131	1.00	128.60	N
ATOM	2945	CD2	HIS	B	591	−77.068	76.670	−29.754	1.00	128.45	C
ATOM	2946	C	HIS	B	591	−74.140	76.070	−32.735	1.00	128.35	C
ATOM	2947	O	HIS	B	591	−72.996	75.638	−32.916	1.00	128.27	O
ATOM	2948	N	ARG	B	592	−74.464	77.382	−32.845	1.00	130.35	N
ATOM	2949	CA	ARG	B	592	−73.526	78.465	−33.174	1.00	130.16	C
ATOM	2950	CB	ARG	B	592	−74.251	79.820	−33.346	1.00	130.23	C
ATOM	2951	CG	ARG	B	592	−75.283	80.125	−32.268	1.00	130.52	C
ATOM	2952	CD	ARG	B	592	−75.698	81.590	−32.219	1.00	131.28	C
ATOM	2953	NE	ARG	B	592	−76.802	81.788	−31.269	1.00	131.92	N
ATOM	2954	CZ	ARG	B	592	−76.657	82.148	−29.993	1.00	131.97	C
ATOM	2955	NH1	ARG	B	592	−75.446	82.385	−29.494	1.00	131.94	N
ATOM	2956	NH2	ARG	B	592	−77.723	82.283	−29.209	1.00	131.77	N
ATOM	2957	C	ARG	B	592	−72.293	78.564	−32.238	1.00	129.90	C
ATOM	2958	O	ARG	B	592	−71.166	78.662	−32.736	1.00	129.80	O
ATOM	2959	N	GLU	B	593	−72.513	78.509	−30.898	1.00	127.81	N
ATOM	2960	CA	GLU	B	593	−71.474	78.591	−29.854	1.00	127.53	C
ATOM	2961	CB	GLU	B	593	−72.107	78.883	−28.475	1.00	127.55	C
ATOM	2962	CG	GLU	B	593	−72.567	80.316	−28.243	1.00	127.44	C
ATOM	2963	CD	GLU	B	593	−72.865	80.663	−26.791	1.00	127.43	C
ATOM	2964	OE1	GLU	B	593	−74.035	80.521	−26.362	1.00	127.08	O
ATOM	2965	OE2	GLU	B	593	−71.921	81.080	−26.081	1.00	127.50	O
ATOM	2966	C	GLU	B	593	−70.550	77.346	−29.750	1.00	127.34	C
ATOM	2967	O	GLU	B	593	−69.465	77.438	−29.160	1.00	127.36	O
ATOM	2968	N	ALA	B	594	−70.987	76.191	−30.309	1.00	125.85	N
ATOM	2969	CA	ALA	B	594	−70.270	74.904	−30.279	1.00	125.30	C
ATOM	2970	CB	ALA	B	594	−71.239	73.797	−29.915	1.00	125.28	C
ATOM	2971	C	ALA	B	594	−69.558	74.534	−31.580	1.00	124.94	C
ATOM	2972	O	ALA	B	594	−70.001	74.939	−32.656	1.00	124.87	O
ATOM	2973	N	SER	B	595	−68.465	73.739	−31.475	1.00	122.91	N
ATOM	2974	CA	SER	B	595	−67.691	73.248	−32.625	1.00	122.59	C
ATOM	2975	CB	SER	B	595	−66.283	72.828	−32.211	1.00	122.36	C
ATOM	2976	OG	SER	B	595	−65.804	73.570	−31.103	1.00	122.18	O
ATOM	2977	C	SER	B	595	−68.431	72.034	−33.200	1.00	122.55	C
ATOM	2978	O	SER	B	595	−68.960	71.224	−32.432	1.00	122.50	O
ATOM	2979	N	ILE	B	596	−68.489	71.920	−34.541	1.00	122.51	N
ATOM	2980	CA	ILE	B	596	−69.152	70.812	−35.234	1.00	122.52	C
ATOM	2981	CB	ILE	B	596	−70.392	71.213	−36.108	1.00	122.49	C
ATOM	2982	CG1	ILE	B	596	−71.112	69.996	−36.722	1.00	122.49	C
ATOM	2983	CD1	ILE	B	596	−72.218	69.408	−35.909	1.00	122.57	C
ATOM	2984	CG2	ILE	B	596	−70.043	72.208	−37.194	1.00	122.93	C
ATOM	2985	C	ILE	B	596	−68.140	69.889	−35.916	1.00	122.55	C
ATOM	2986	O	ILE	B	596	−67.267	70.340	−36.662	1.00	122.43	O
ATOM	2987	N	HIS	B	597	−68.254	68.592	−35.601	1.00	123.80	N
ATOM	2988	CA	HIS	B	597	−67.429	67.504	−36.118	1.00	123.82	C
ATOM	2989	CB	HIS	B	597	−66.876	66.643	−34.975	1.00	123.73	C
ATOM	2990	CG	HIS	B	597	−66.178	67.399	−33.892	1.00	123.54	C
ATOM	2991	ND1	HIS	B	597	−64.810	67.319	−33.731	1.00	123.54	N
ATOM	2992	CE1	HIS	B	597	−64.529	68.074	−32.682	1.00	123.72	C
ATOM	2993	NE2	HIS	B	597	−65.631	68.621	−32.165	1.00	123.77	N
ATOM	2994	CD2	HIS	B	597	−66.689	68.189	−32.919	1.00	123.49	C
ATOM	2995	C	HIS	B	597	−68.322	66.643	−37.008	1.00	123.91	C
ATOM	2996	O	HIS	B	597	−69.529	66.534	−36.760	1.00	123.96	O
ATOM	2997	N	ALA	B	598	−67.737	66.040	−38.043	1.00	126.34	N
ATOM	2998	CA	ALA	B	598	−68.474	65.191	−38.969	1.00	126.61	C
ATOM	2999	CB	ALA	B	598	−68.871	65.991	−40.196	1.00	126.45	C
ATOM	3000	C	ALA	B	598	−67.612	64.022	−39.379	1.00	126.91	C
ATOM	3001	O	ALA	B	598	−66.396	64.193	−39.509	1.00	126.98	O
ATOM	3002	N	SER	B	599	−68.216	62.835	−39.584	1.00	130.56	N
ATOM	3003	CA	SER	B	599	−67.431	61.686	−40.022	1.00	130.97	C
ATOM	3004	CB	SER	B	599	−67.738	60.438	−39.210	1.00	131.14	C
ATOM	3005	OG	SER	B	599	−66.822	59.400	−39.528	1.00	132.04	O
ATOM	3006	C	SER	B	599	−67.633	61.448	−41.505	1.00	131.08	C
ATOM	3007	O	SER	B	599	−68.756	61.189	−41.947	1.00	130.93	O
ATOM	3008	N	CYS	B	600	−66.536	61.585	−42.275	1.00	136.15	N
ATOM	3009	CA	CYS	B	600	−66.507	61.421	−43.728	1.00	136.70	C
ATOM	3010	CB	CYS	B	600	−65.754	62.571	−44.403	1.00	137.12	C
ATOM	3011	SG	CYS	B	600	−66.513	64.211	−44.198	1.00	139.29	S
ATOM	3012	C	CYS	B	600	−65.893	60.079	−44.067	1.00	136.36	C
ATOM	3013	O	CYS	B	600	−64.730	59.836	−43.734	1.00	136.42	O
ATOM	3014	N	CYS	B	601	−66.665	59.207	−44.720	1.00	136.31	N
ATOM	3015	CA	CYS	B	601	−66.163	57.888	−45.071	1.00	136.05	C
ATOM	3016	CB	CYS	B	601	−66.877	56.799	−44.274	1.00	135.96	C
ATOM	3017	SG	CYS	B	601	−66.493	56.808	−42.505	1.00	135.19	S
ATOM	3018	C	CYS	B	601	−66.175	57.599	−46.557	1.00	136.06	C
ATOM	3019	O	CYS	B	601	−67.227	57.682	−47.201	1.00	136.04	O
ATOM	3020	N	HIS	B	602	−64.999	57.250	−47.104	1.00	139.94	N
ATOM	3021	CA	HIS	B	602	−64.915	56.900	−48.510	1.00	139.95	C
ATOM	3022	CB	HIS	B	602	−63.577	57.301	−49.168	1.00	140.20	C
ATOM	3023	CG	HIS	B	602	−63.501	56.998	−50.648	1.00	141.34	C
ATOM	3024	ND1	HIS	B	602	−64.637	57.006	−51.463	1.00	142.03	N
ATOM	3025	CE1	HIS	B	602	−64.212	56.698	−52.679	1.00	142.05	C
ATOM	3026	NE2	HIS	B	602	−62.890	56.501	−52.703	1.00	142.35	N
ATOM	3027	CD2	HIS	B	602	−62.425	56.689	−51.413	1.00	142.20	C
ATOM	3028	C	HIS	B	602	−65.202	55.412	−48.652	1.00	139.62	C
ATOM	3029	O	HIS	B	602	−64.468	54.562	−48.125	1.00	139.50	O
ATOM	3030	N	ALA	B	603	−66.317	55.124	−49.341	1.00	139.92	N
ATOM	3031	CA	ALA	B	603	−66.846	53.804	−49.666	1.00	139.45	C
ATOM	3032	CB	ALA	B	603	−67.448	53.142	−48.433	1.00	139.37	C
ATOM	3033	C	ALA	B	603	−67.911	54.017	−50.764	1.00	139.05	C
ATOM	3034	O	ALA	B	603	−69.043	54.427	−50.468	1.00	139.15	O
ATOM	3035	N	PRO	B	604	−67.543	53.796	−52.055	1.00	138.26	N
ATOM	3036	CA	PRO	B	604	−68.514	54.008	−53.149	1.00	137.56	C
ATOM	3037	CB	PRO	B	604	−67.654	53.930	−54.425	1.00	137.66	C
ATOM	3038	CG	PRO	B	604	−66.209	53.965	−53.954	1.00	137.98	C
ATOM	3039	CD	PRO	B	604	−66.241	53.345	−52.586	1.00	138.32	C
ATOM	3040	C	PRO	B	604	−69.671	53.007	−53.167	1.00	136.75	C
ATOM	3041	O	PRO	B	604	−70.647	53.224	−53.896	1.00	136.87	O
ATOM	3042	N	GLY	B	605	−69.552	51.938	−52.370	1.00	132.29	N
ATOM	3043	CA	GLY	B	605	−70.575	50.907	−52.240	1.00	130.75	C
ATOM	3044	C	GLY	B	605	−71.601	51.257	−51.180	1.00	129.57	C
ATOM	3045	O	GLY	B	605	−72.657	50.619	−51.101	1.00	129.70	O
ATOM	3046	N	LEU	B	606	−71.288	52.296	−50.365	1.00	124.93	N
ATOM	3047	CA	LEU	B	606	−72.087	52.803	−49.246	1.00	123.32	C
ATOM	3048	CB	LEU	B	606	−71.135	53.282	−48.127	1.00	123.34	C
ATOM	3049	CG	LEU	B	606	−71.403	52.923	−46.648	1.00	123.22	C
ATOM	3050	CD1	LEU	B	606	−71.064	54.097	−45.742	1.00	122.43	C
ATOM	3051	CD2	LEU	B	606	−72.825	52.421	−46.395	1.00	123.19	C
ATOM	3052	C	LEU	B	606	−72.996	53.963	−49.617	1.00	122.22	C
ATOM	3053	O	LEU	B	606	−72.507	54.983	−50.120	1.00	122.10	O
ATOM	3054	N	GLU	B	607	−74.310	53.820	−49.322	1.00	118.39	N
ATOM	3055	CA	GLU	B	607	−75.315	54.853	−49.553	1.00	116.97	C
ATOM	3056	CB	GLU	B	607	−76.260	54.530	−50.732	1.00	116.99	C
ATOM	3057	CG	GLU	B	607	−77.272	53.410	−50.532	1.00	117.68	C
ATOM	3058	CD	GLU	B	607	−78.624	53.643	−51.193	1.00	118.47	C
ATOM	3059	OE1	GLU	B	607	−79.321	52.643	−51.483	1.00	118.49	O
ATOM	3060	OE2	GLU	B	607	−78.992	54.821	−51.417	1.00	118.52	O
ATOM	3061	C	GLU	B	607	−76.030	55.270	−48.246	1.00	115.91	C
ATOM	3062	O	GLU	B	607	−76.739	54.465	−47.637	1.00	116.06	O
ATOM	3063	N	CYS	B	608	−75.802	56.530	−47.807	1.00	112.37	N
ATOM	3064	CA	CYS	B	608	−76.366	57.102	−46.574	1.00	110.58	C
ATOM	3065	CB	CYS	B	608	−75.259	57.654	−45.681	1.00	110.79	C
ATOM	3066	SG	CYS	B	608	−74.059	56.409	−45.131	1.00	112.17	S
ATOM	3067	C	CYS	B	608	−77.498	58.127	−46.762	1.00	108.94	C
ATOM	3068	O	CYS	B	608	−77.508	58.886	−47.732	1.00	108.93	O
ATOM	3069	N	LYS	B	609	−78.442	58.147	−45.816	1.00	100.85	N
ATOM	3070	CA	LYS	B	609	−79.581	59.057	−45.811	1.00	98.69	C
ATOM	3071	CB	LYS	B	609	−80.818	58.412	−46.448	1.00	98.51	C
ATOM	3072	CG	LYS	B	609	−81.449	57.310	−45.646	1.00	97.62	C
ATOM	3073	CD	LYS	B	609	−82.927	57.350	−45.822	1.00	97.09	C
ATOM	3074	CE	LYS	B	609	−83.510	55.972	−45.802	1.00	97.54	C
ATOM	3075	NZ	LYS	B	609	−84.954	56.009	−46.121	1.00	98.08	N
ATOM	3076	C	LYS	B	609	−79.857	59.592	−44.402	1.00	97.61	C
ATOM	3077	O	LYS	B	609	−79.117	59.264	−43.477	1.00	97.62	O
ATOM	3078	N	VAL	B	610	−80.895	60.441	−44.239	1.00	95.01	N
ATOM	3079	CA	VAL	B	610	−81.250	61.021	−42.937	1.00	93.13	C
ATOM	3080	CB	VAL	B	610	−80.857	62.524	−42.796	1.00	92.98	C
ATOM	3081	CG1	VAL	B	610	−81.313	63.089	−41.457	1.00	92.75	C
ATOM	3082	CG2	VAL	B	610	−79.350	62.739	−42.970	1.00	92.08	C
ATOM	3083	C	VAL	B	610	−82.722	60.786	−42.671	1.00	92.11	C
ATOM	3084	O	VAL	B	610	−83.506	60.775	−43.609	1.00	92.08	O
ATOM	3085	N	LYS	B	611	−83.083	60.557	−41.404	1.00	91.38	N
ATOM	3086	CA	LYS	B	611	−84.454	60.370	−40.941	1.00	90.39	C
ATOM	3087	CB	LYS	B	611	−84.782	58.907	−40.668	1.00	90.56	C
ATOM	3088	CG	LYS	B	611	−86.289	58.613	−40.749	1.00	91.05	C
ATOM	3089	CD	LYS	B	611	−86.626	57.145	−41.098	1.00	92.07	C
ATOM	3090	CE	LYS	B	611	−86.088	56.691	−42.456	1.00	92.88	C
ATOM	3091	NZ	LYS	B	611	−86.867	57.237	−43.622	1.00	93.51	N
ATOM	3092	C	LYS	B	611	−84.597	61.214	−39.687	1.00	89.60	C
ATOM	3093	O	LYS	B	611	−83.626	61.343	−38.933	1.00	89.74	O
ATOM	3094	N	GLU	B	612	−85.772	61.833	−39.483	1.00	87.15	N
ATOM	3095	CA	GLU	B	612	−86.002	62.705	−38.337	1.00	86.15	C
ATOM	3096	CB	GLU	B	612	−85.823	64.171	−38.749	1.00	86.59	C
ATOM	3097	CG	GLU	B	612	−84.395	64.674	−38.837	1.00	88.33	C
ATOM	3098	CD	GLU	B	612	−84.229	66.187	−38.948	1.00	90.95	C
ATOM	3099	OE1	GLU	B	612	−85.200	66.927	−38.645	1.00	91.46	O
ATOM	3100	OE2	GLU	B	612	−83.120	66.633	−39.340	1.00	92.27	O
ATOM	3101	C	GLU	B	612	−87.386	62.586	−37.773	1.00	84.94	C
ATOM	3102	O	GLU	B	612	−88.346	62.351	−38.505	1.00	85.08	O
ATOM	3103	N	HIS	B	613	−87.510	62.805	−36.478	1.00	80.41	N
ATOM	3104	CA	HIS	B	613	−88.797	62.818	−35.798	1.00	79.40	C
ATOM	3105	CB	HIS	B	613	−89.366	61.441	−35.482	1.00	78.55	C
ATOM	3106	CG	HIS	B	613	−90.704	61.500	−34.811	1.00	76.10	C
ATOM	3107	ND1	HIS	B	613	−90.843	61.259	−33.460	1.00	74.15	N
ATOM	3108	CE1	HIS	B	613	−92.141	61.369	−33.200	1.00	72.72	C
ATOM	3109	NE2	HIS	B	613	−92.832	61.678	−34.297	1.00	72.67	N
ATOM	3110	CD2	HIS	B	613	−91.926	61.770	−35.332	1.00	73.99	C
ATOM	3111	C	HIS	B	613	−88.613	63.585	−34.552	1.00	79.83	C
ATOM	3112	O	HIS	B	613	−87.692	63.295	−33.791	1.00	80.05	O
ATOM	3113	N	GLY	B	614	−89.459	64.585	−34.375	1.00	82.49	N
ATOM	3114	CA	GLY	B	614	−89.444	65.441	−33.208	1.00	82.79	C
ATOM	3115	C	GLY	B	614	−90.823	65.612	−32.638	1.00	83.07	C
ATOM	3116	O	GLY	B	614	−91.803	65.424	−33.362	1.00	82.78	O
ATOM	3117	N	ILE	B	615	−90.911	65.966	−31.346	1.00	88.23	N
ATOM	3118	CA	ILE	B	615	−92.196	66.213	−30.683	1.00	89.18	C
ATOM	3119	CB	ILE	B	615	−93.076	64.985	−30.329	1.00	89.23	C
ATOM	3120	CG1	ILE	B	615	−92.261	63.813	−29.798	1.00	88.59	C
ATOM	3121	CD1	ILE	B	615	−92.242	63.843	−28.398	1.00	88.33	C
ATOM	3122	CG2	ILE	B	615	−94.050	64.602	−31.489	1.00	89.10	C
ATOM	3123	C	ILE	B	615	−92.141	67.291	−29.596	1.00	89.92	C
ATOM	3124	O	ILE	B	615	−91.193	67.289	−28.815	1.00	90.14	O
ATOM	3125	N	PRO	B	616	−93.132	68.230	−29.591	1.00	92.46	N
ATOM	3126	CA	PRO	B	616	−93.155	69.352	−28.639	1.00	92.93	C
ATOM	3127	CB	PRO	B	616	−94.598	69.867	−28.758	1.00	92.90	C
ATOM	3128	CG	PRO	B	616	−95.310	68.911	−29.645	1.00	92.45	C
ATOM	3129	CD	PRO	B	616	−94.277	68.348	−30.508	1.00	92.34	C
ATOM	3130	C	PRO	B	616	−92.673	69.260	−27.175	1.00	93.54	C
ATOM	3131	O	PRO	B	616	−91.577	69.768	−26.866	1.00	93.58	O
ATOM	3132	N	ALA	B	617	−93.519	68.703	−26.269	1.00	96.94	N
ATOM	3133	CA	ALA	B	617	−93.242	68.553	−24.839	1.00	97.57	C
ATOM	3134	CB	ALA	B	617	−94.431	69.057	−24.028	1.00	97.36	C
ATOM	3135	C	ALA	B	617	−93.013	67.053	−24.597	1.00	97.97	C
ATOM	3136	O	ALA	B	617	−93.990	66.330	−24.307	1.00	98.46	O
ATOM	3137	N	PRO	B	618	−91.751	66.545	−24.766	1.00	98.47	N
ATOM	3138	CA	PRO	B	618	−91.525	65.101	−24.623	1.00	98.62	C
ATOM	3139	CB	PRO	B	618	−90.209	64.854	−25.377	1.00	98.31	C
ATOM	3140	CG	PRO	B	618	−89.803	66.158	−25.913	1.00	98.18	C
ATOM	3141	CD	PRO	B	618	−90.498	67.217	−25.140	1.00	98.25	C
ATOM	3142	C	PRO	B	618	−91.446	64.630	−23.191	1.00	98.94	C
ATOM	3143	O	PRO	B	618	−90.715	65.232	−22.386	1.00	99.07	O
ATOM	3144	N	GLN	B	619	−92.203	63.530	−22.893	1.00	100.32	N
ATOM	3145	CA	GLN	B	619	−92.267	62.858	−21.590	1.00	100.41	C
ATOM	3146	CB	GLN	B	619	−93.209	61.620	−21.646	1.00	100.77	C
ATOM	3147	CG	GLN	B	619	−94.720	61.924	−21.757	1.00	102.64	C
ATOM	3148	CD	GLN	B	619	−95.221	62.146	−23.187	1.00	105.52	C
ATOM	3149	OE1	GLN	B	619	−95.170	61.245	−24.049	1.00	106.91	O
ATOM	3150	NE2	GLN	B	619	−95.732	63.351	−23.468	1.00	105.63	N
ATOM	3151	C	GLN	B	619	−90.813	62.447	−21.227	1.00	99.99	C
ATOM	3152	O	GLN	B	619	−90.130	63.183	−20.494	1.00	100.29	O
ATOM	3153	N	GLU	B	620	−90.318	61.323	−21.796	1.00	94.10	N
ATOM	3154	CA	GLU	B	620	−88.954	60.893	−21.519	1.00	92.71	C
ATOM	3155	CB	GLU	B	620	−88.935	59.482	−20.901	1.00	92.50	C
ATOM	3156	C	GLU	B	620	−88.053	60.992	−22.752	1.00	91.86	C
ATOM	3157	O	GLU	B	620	−86.984	61.626	−22.694	1.00	91.83	O
ATOM	3158	N	GLN	B	621	−88.487	60.374	−23.872	1.00	85.55	N
ATOM	3159	CA	GLN	B	621	−87.670	60.349	−25.080	1.00	84.47	C
ATOM	3160	CB	GLN	B	621	−86.844	59.042	−25.162	1.00	84.60	C
ATOM	3161	CG	GLN	B	621	−87.462	57.832	−24.461	1.00	84.63	C
ATOM	3162	CD	GLN	B	621	−87.643	56.685	−25.402	1.00	84.43	C
ATOM	3163	OE1	GLN	B	621	−86.689	55.973	−25.708	1.00	85.62	O
ATOM	3164	NE2	GLN	B	621	−88.871	56.482	−25.882	1.00	84.34	N
ATOM	3165	C	GLN	B	621	−88.374	60.638	−26.386	1.00	83.76	C
ATOM	3166	O	GLN	B	621	−89.598	60.733	−26.423	1.00	83.59	O
ATOM	3167	N	VAL	B	622	−87.563	60.800	−27.458	1.00	79.91	N
ATOM	3168	CA	VAL	B	622	−87.932	61.064	−28.848	1.00	79.67	C
ATOM	3169	CB	VAL	B	622	−87.664	62.526	−29.281	1.00	79.63	C
ATOM	3170	CG1	VAL	B	622	−87.873	62.702	−30.771	1.00	79.21	C
ATOM	3171	CG2	VAL	B	622	−88.559	63.495	−28.516	1.00	79.49	C
ATOM	3172	C	VAL	B	622	−87.170	60.043	−29.682	1.00	79.82	C
ATOM	3173	O	VAL	B	622	−85.939	59.991	−29.653	1.00	79.77	O
ATOM	3174	N	THR	B	623	−87.927	59.218	−30.410	1.00	82.55	N
ATOM	3175	CA	THR	B	623	−87.419	58.107	−31.207	1.00	82.68	C
ATOM	3176	CB	THR	B	623	−87.976	56.814	−30.555	1.00	82.61	C
ATOM	3177	OG1	THR	B	623	−87.045	56.385	−29.562	1.00	82.15	O
ATOM	3178	CG2	THR	B	623	−88.326	55.694	−31.553	1.00	82.02	C
ATOM	3179	C	THR	B	623	−87.629	58.197	−32.723	1.00	83.06	C
ATOM	3180	O	THR	B	623	−88.686	58.617	−33.191	1.00	83.23	O
ATOM	3181	N	VAL	B	624	−86.622	57.744	−33.474	1.00	85.14	N
ATOM	3182	CA	VAL	B	624	−86.620	57.659	−34.935	1.00	85.55	C
ATOM	3183	CB	VAL	B	624	−86.190	58.982	−35.648	1.00	85.38	C
ATOM	3184	CG1	VAL	B	624	−84.702	59.294	−35.472	1.00	85.50	C
ATOM	3185	CG2	VAL	B	624	−86.563	58.962	−37.122	1.00	85.18	C
ATOM	3186	C	VAL	B	624	−85.823	56.397	−35.353	1.00	86.01	C
ATOM	3187	O	VAL	B	624	−84.642	56.262	−35.013	1.00	85.58	O
ATOM	3188	N	ALA	B	625	−86.483	55.463	−36.046	1.00	89.04	N
ATOM	3189	CA	ALA	B	625	−85.810	54.229	−36.462	1.00	90.03	C
ATOM	3190	CB	ALA	B	625	−86.573	53.019	−35.942	1.00	89.71	C
ATOM	3191	C	ALA	B	625	−85.616	54.118	−37.974	1.00	90.84	C
ATOM	3192	O	ALA	B	625	−86.465	54.600	−38.730	1.00	91.18	O
ATOM	3193	N	CYS	B	626	−84.519	53.467	−38.416	1.00	92.62	N
ATOM	3194	CA	CYS	B	626	−84.249	53.242	−39.833	1.00	93.74	C
ATOM	3195	CB	CYS	B	626	−82.845	52.686	−40.028	1.00	93.68	C
ATOM	3196	SG	CYS	B	626	−81.521	53.825	−39.563	1.00	96.55	S
ATOM	3197	C	CYS	B	626	−85.294	52.278	−40.417	1.00	94.25	C
ATOM	3198	O	CYS	B	626	−85.991	51.581	−39.670	1.00	94.23	O
ATOM	3199	N	GLU	B	627	−85.397	52.224	−41.750	1.00	99.01	N
ATOM	3200	CA	GLU	B	627	−86.313	51.280	−42.372	1.00	99.57	C
ATOM	3201	CB	GLU	B	627	−86.699	51.724	−43.779	1.00	99.82	C
ATOM	3202	CG	GLU	B	627	−87.846	52.708	−43.822	1.00	101.35	C
ATOM	3203	CD	GLU	B	627	−87.453	54.073	−44.351	1.00	103.72	C
ATOM	3204	OE1	GLU	B	627	−86.269	54.258	−44.725	1.00	104.08	O
ATOM	3205	OE2	GLU	B	627	−88.334	54.965	−44.379	1.00	105.10	O
ATOM	3206	C	GLU	B	627	−85.575	49.950	−42.474	1.00	99.72	C
ATOM	3207	O	GLU	B	627	−84.331	49.916	−42.454	1.00	99.64	O
ATOM	3208	N	GLU	B	628	−86.347	48.852	−42.602	1.00	99.87	N
ATOM	3209	CA	GLU	B	628	−85.806	47.503	−42.759	1.00	99.87	C
ATOM	3210	CB	GLU	B	628	−86.981	46.504	−42.940	1.00	100.27	C
ATOM	3211	CG	GLU	B	628	−86.774	45.326	−43.885	1.00	102.66	C
ATOM	3212	CD	GLU	B	628	−85.816	44.225	−43.459	1.00	105.44	C
ATOM	3213	OE1	GLU	B	628	−85.760	43.908	−42.246	1.00	106.67	O
ATOM	3214	OE2	GLU	B	628	−85.130	43.664	−44.348	1.00	106.45	O
ATOM	3215	C	GLU	B	628	−84.797	47.549	−43.934	1.00	99.03	C
ATOM	3216	O	GLU	B	628	−85.098	48.102	−44.990	1.00	98.78	O
ATOM	3217	N	GLY	B	629	−83.593	47.065	−43.694	1.00	97.03	N
ATOM	3218	CA	GLY	B	629	−82.544	47.072	−44.706	1.00	96.58	C
ATOM	3219	C	GLY	B	629	−81.530	48.174	−44.506	1.00	96.44	C
ATOM	3220	O	GLY	B	629	−80.403	48.111	−45.014	1.00	96.39	O
ATOM	3221	N	TRP	B	630	−81.928	49.190	−43.757	1.00	99.26	N
ATOM	3222	CA	TRP	B	630	−81.056	50.308	−43.456	1.00	99.05	C
ATOM	3223	CB	TRP	B	630	−81.851	51.611	−43.533	1.00	99.48	C
ATOM	3224	CG	TRP	B	630	−82.241	51.986	−44.934	1.00	100.47	C
ATOM	3225	CD1	TRP	B	630	−83.413	51.692	−45.576	1.00	100.68	C
ATOM	3226	NE1	TRP	B	630	−83.394	52.210	−46.852	1.00	100.42	N
ATOM	3227	CE2	TRP	B	630	−82.198	52.855	−47.054	1.00	100.71	C
ATOM	3228	CD2	TRP	B	630	−81.443	52.723	−45.868	1.00	100.98	C
ATOM	3229	CE3	TRP	B	630	−80.163	53.307	−45.809	1.00	101.56	C
ATOM	3230	CZ3	TRP	B	630	−79.684	53.996	−46.915	1.00	101.51	C
ATOM	3231	CH2	TRP	B	630	−80.444	54.095	−48.085	1.00	101.62	C
ATOM	3232	CZ2	TRP	B	630	−81.710	53.541	−48.175	1.00	101.13	C
ATOM	3233	C	TRP	B	630	−80.456	50.094	−42.074	1.00	98.40	C
ATOM	3234	O	TRP	B	630	−81.127	49.576	−41.181	1.00	98.36	O
ATOM	3235	N	THR	B	631	−79.197	50.479	−41.910	1.00	95.20	N
ATOM	3236	CA	THR	B	631	−78.443	50.347	−40.667	1.00	94.44	C
ATOM	3237	CB	THR	B	631	−77.185	49.515	−40.966	1.00	94.47	C
ATOM	3238	OG1	THR	B	631	−77.579	48.155	−41.135	1.00	94.93	O
ATOM	3239	CG2	THR	B	631	−76.114	49.624	−39.898	1.00	94.21	C
ATOM	3240	C	THR	B	631	−78.164	51.727	−40.033	1.00	93.85	C
ATOM	3241	O	THR	B	631	−77.579	52.598	−40.681	1.00	93.88	O
ATOM	3242	N	LEU	B	632	−78.569	51.919	−38.772	1.00	91.41	N
ATOM	3243	CA	LEU	B	632	−78.332	53.177	−38.074	1.00	90.60	C
ATOM	3244	CB	LEU	B	632	−79.138	53.227	−36.766	1.00	90.50	C
ATOM	3245	CG	LEU	B	632	−78.971	54.451	−35.885	1.00	89.65	C
ATOM	3246	CD1	LEU	B	632	−79.409	55.660	−36.593	1.00	89.50	C
ATOM	3247	CD2	LEU	B	632	−79.817	54.334	−34.678	1.00	89.05	C
ATOM	3248	C	LEU	B	632	−76.849	53.315	−37.798	1.00	90.39	C
ATOM	3249	O	LEU	B	632	−76.288	52.506	−37.062	1.00	90.51	O
ATOM	3250	N	THR	B	633	−76.208	54.313	−38.411	1.00	90.81	N
ATOM	3251	CA	THR	B	633	−74.772	54.565	−38.232	1.00	90.43	C
ATOM	3252	CB	THR	B	633	−74.066	54.794	−39.567	1.00	90.45	C
ATOM	3253	OG1	THR	B	633	−74.591	55.988	−40.166	1.00	91.14	O
ATOM	3254	CG2	THR	B	633	−74.184	53.604	−40.500	1.00	90.51	C
ATOM	3255	C	THR	B	633	−74.524	55.759	−37.317	1.00	90.16	C
ATOM	3256	O	THR	B	633	−73.538	55.764	−36.582	1.00	90.12	O
ATOM	3257	N	GLY	B	634	−75.394	56.763	−37.396	1.00	87.09	N
ATOM	3258	CA	GLY	B	634	−75.267	57.961	−36.581	1.00	86.65	C
ATOM	3259	C	GLY	B	634	−76.542	58.364	−35.880	1.00	86.41	C
ATOM	3260	O	GLY	B	634	−77.612	58.389	−36.502	1.00	86.54	O
ATOM	3261	N	CYS	B	635	−76.438	58.699	−34.585	1.00	82.25	N
ATOM	3262	CA	CYS	B	635	−77.609	59.131	−33.820	1.00	82.04	C
ATOM	3263	CB	CYS	B	635	−78.076	58.027	−32.879	1.00	81.41	C
ATOM	3264	SG	CYS	B	635	−79.434	58.486	−31.778	1.00	79.97	S
ATOM	3265	C	CYS	B	635	−77.254	60.442	−33.099	1.00	82.61	C
ATOM	3266	O	CYS	B	635	−76.128	60.590	−32.595	1.00	82.41	O
ATOM	3267	N	SER	B	636	−78.190	61.428	−33.153	1.00	83.71	N
ATOM	3268	CA	SER	B	636	−78.043	62.796	−32.610	1.00	84.47	C
ATOM	3269	CB	SER	B	636	−77.178	63.631	−33.551	1.00	84.28	C
ATOM	3270	OG	SER	B	636	−77.693	63.523	−34.868	1.00	84.69	O
ATOM	3271	C	SER	B	636	−79.369	63.520	−32.421	1.00	84.91	C
ATOM	3272	O	SER	B	636	−80.422	62.986	−32.751	1.00	84.87	O
ATOM	3273	N	ALA	B	637	−79.306	64.751	−31.900	1.00	87.69	N
ATOM	3274	CA	ALA	B	637	−80.478	65.601	−31.676	1.00	88.87	C
ATOM	3275	CB	ALA	B	637	−80.790	65.706	−30.192	1.00	88.44	C
ATOM	3276	C	ALA	B	637	−80.287	66.994	−32.279	1.00	89.84	C
ATOM	3277	O	ALA	B	637	−79.159	67.500	−32.334	1.00	90.01	O
ATOM	3278	N	LEU	B	638	−81.395	67.603	−32.745	1.00	95.18	N
ATOM	3279	CA	LEU	B	638	−81.383	68.934	−33.337	1.00	96.41	C
ATOM	3280	CB	LEU	B	638	−82.722	69.272	−34.006	1.00	96.25	C
ATOM	3281	CG	LEU	B	638	−82.911	68.746	−35.428	1.00	95.86	C
ATOM	3282	CD1	LEU	B	638	−84.116	69.356	−36.057	1.00	95.51	C
ATOM	3283	CD2	LEU	B	638	−81.710	69.046	−36.310	1.00	94.65	C
ATOM	3284	C	LEU	B	638	−80.990	69.951	−32.267	1.00	97.73	C
ATOM	3285	O	LEU	B	638	−81.656	70.016	−31.223	1.00	97.77	O
ATOM	3286	N	PRO	B	639	−79.864	70.688	−32.494	1.00	105.30	N
ATOM	3287	CA	PRO	B	639	−79.352	71.634	−31.482	1.00	106.33	C
ATOM	3288	CB	PRO	B	639	−78.161	72.308	−32.178	1.00	106.24	C
ATOM	3289	CG	PRO	B	639	−78.327	72.005	−33.615	1.00	105.87	C
ATOM	3290	CD	PRO	B	639	−78.974	70.662	−33.669	1.00	105.46	C
ATOM	3291	C	PRO	B	639	−80.325	72.645	−30.907	1.00	107.40	C
ATOM	3292	O	PRO	B	639	−80.205	73.000	−29.722	1.00	107.75	O
ATOM	3293	N	GLY	B	640	−81.274	73.081	−31.741	1.00	113.40	N
ATOM	3294	CA	GLY	B	640	−82.310	74.042	−31.372	1.00	114.55	C
ATOM	3295	C	GLY	B	640	−83.280	73.426	−30.393	1.00	115.12	C
ATOM	3296	O	GLY	B	640	−84.423	73.114	−30.755	1.00	115.42	O
ATOM	3297	N	THR	B	641	−82.800	73.215	−29.150	1.00	117.71	N
ATOM	3298	CA	THR	B	641	−83.559	72.584	−28.075	1.00	118.36	C
ATOM	3299	CB	THR	B	641	−83.562	71.037	−28.234	1.00	118.30	C
ATOM	3300	OG1	THR	B	641	−84.491	70.483	−27.300	1.00	118.10	O
ATOM	3301	CG2	THR	B	641	−82.167	70.408	−28.050	1.00	118.37	C
ATOM	3302	C	THR	B	641	−83.112	73.048	−26.691	1.00	118.77	C
ATOM	3303	O	THR	B	641	−82.100	73.750	−26.555	1.00	119.16	O
ATOM	3304	N	SER	B	642	−83.885	72.626	−25.671	1.00	118.42	N
ATOM	3305	CA	SER	B	642	−83.692	72.923	−24.260	1.00	118.43	C
ATOM	3306	CB	SER	B	642	−85.050	73.128	−23.585	1.00	118.78	C
ATOM	3307	OG	SER	B	642	−85.914	73.957	−24.352	1.00	119.68	O
ATOM	3308	C	SER	B	642	−82.882	71.797	−23.600	1.00	117.89	C
ATOM	3309	O	SER	B	642	−81.844	71.394	−24.144	1.00	117.93	O
ATOM	3310	N	HIS	B	643	−83.345	71.289	−22.444	1.00	114.82	N
ATOM	3311	CA	HIS	B	643	−82.631	70.240	−21.720	1.00	114.07	C
ATOM	3312	CB	HIS	B	643	−82.906	70.289	−20.189	1.00	114.71	C
ATOM	3313	CG	HIS	B	643	−81.719	69.984	−19.295	1.00	116.80	C
ATOM	3314	ND1	HIS	B	643	−80.426	70.430	−19.601	1.00	118.25	N
ATOM	3315	CE1	HIS	B	643	−79.653	70.006	−18.607	1.00	118.56	C
ATOM	3316	NE2	HIS	B	643	−80.355	69.336	−17.686	1.00	118.87	N
ATOM	3317	CD2	HIS	B	643	−81.677	69.321	−18.109	1.00	118.39	C
ATOM	3318	C	HIS	B	643	−82.757	68.829	−22.313	1.00	112.56	C
ATOM	3319	O	HIS	B	643	−83.777	68.140	−22.151	1.00	112.68	O
ATOM	3320	N	VAL	B	644	−81.695	68.422	−23.023	1.00	102.35	N
ATOM	3321	CA	VAL	B	644	−81.587	67.090	−23.585	1.00	100.09	C
ATOM	3322	CB	VAL	B	644	−81.702	66.933	−25.117	1.00	100.10	C
ATOM	3323	CG1	VAL	B	644	−82.987	67.561	−25.623	1.00	99.99	C
ATOM	3324	CG2	VAL	B	644	−80.491	67.488	−25.854	1.00	99.85	C
ATOM	3325	C	VAL	B	644	−80.366	66.454	−22.963	1.00	98.62	C
ATOM	3326	O	VAL	B	644	−79.243	66.985	−23.051	1.00	98.76	O
ATOM	3327	N	LEU	B	645	−80.619	65.347	−22.262	1.00	90.02	N
ATOM	3328	CA	LEU	B	645	−79.643	64.550	−21.532	1.00	87.53	C
ATOM	3329	CB	LEU	B	645	−80.385	63.455	−20.757	1.00	87.46	C
ATOM	3330	CG	LEU	B	645	−81.162	63.901	−19.502	1.00	86.73	C
ATOM	3331	CD1	LEU	B	645	−82.312	64.792	−19.839	1.00	86.67	C
ATOM	3332	CD2	LEU	B	645	−81.741	62.719	−18.779	1.00	86.22	C
ATOM	3333	C	LEU	B	645	−78.572	63.976	−22.465	1.00	85.94	C
ATOM	3334	O	LEU	B	645	−77.389	64.002	−22.136	1.00	85.72	O
ATOM	3335	N	GLY	B	646	−78.999	63.512	−23.633	1.00	81.27	N
ATOM	3336	CA	GLY	B	646	−78.124	62.949	−24.655	1.00	78.79	C
ATOM	3337	C	GLY	B	646	−78.847	62.091	−25.670	1.00	77.11	C
ATOM	3338	O	GLY	B	646	−80.079	62.007	−25.682	1.00	76.86	O
ATOM	3339	N	ALA	B	647	−78.075	61.445	−26.532	1.00	74.90	N
ATOM	3340	CA	ALA	B	647	−78.608	60.554	−27.563	1.00	73.60	C
ATOM	3341	CB	ALA	B	647	−78.740	61.280	−28.888	1.00	73.68	C
ATOM	3342	C	ALA	B	647	−77.744	59.328	−27.734	1.00	72.61	C
ATOM	3343	O	ALA	B	647	−76.515	59.395	−27.653	1.00	72.32	O
ATOM	3344	N	TYR	B	648	−78.402	58.202	−27.970	1.00	71.64	N
ATOM	3345	CA	TYR	B	648	−77.731	56.920	−28.182	1.00	70.40	C
ATOM	3346	CB	TYR	B	648	−77.415	56.200	−26.842	1.00	69.77	C
ATOM	3347	CG	TYR	B	648	−78.580	56.130	−25.876	1.00	67.74	C
ATOM	3348	CD1	TYR	B	648	−78.712	57.058	−24.843	1.00	66.20	C
ATOM	3349	CE1	TYR	B	648	−79.797	57.015	−23.964	1.00	64.71	C
ATOM	3350	CZ	TYR	B	648	−80.767	56.030	−24.113	1.00	64.68	C
ATOM	3351	OH	TYR	B	648	−81.835	55.960	−23.239	1.00	63.83	O
ATOM	3352	CE2	TYR	B	648	−80.647	55.092	−25.132	1.00	64.61	C
ATOM	3353	CD2	TYR	B	648	−79.555	55.145	−26.000	1.00	65.13	C
ATOM	3354	C	TYR	B	648	−78.543	56.035	−29.123	1.00	70.18	C
ATOM	3355	O	TYR	B	648	−79.767	56.174	−29.210	1.00	70.19	O
ATOM	3356	N	ALA	B	649	−77.859	55.118	−29.813	1.00	71.65	N
ATOM	3357	CA	ALA	B	649	−78.512	54.174	−30.718	1.00	71.10	C
ATOM	3358	CB	ALA	B	649	−77.614	53.899	−31.910	1.00	71.27	C
ATOM	3359	C	ALA	B	649	−78.831	52.869	−30.005	1.00	70.52	C
ATOM	3360	O	ALA	B	649	−78.006	52.355	−29.249	1.00	70.51	O
ATOM	3361	N	VAL	B	650	−80.019	52.347	−30.226	1.00	70.69	N
ATOM	3362	CA	VAL	B	650	−80.446	51.073	−29.657	1.00	70.72	C
ATOM	3363	CB	VAL	B	650	−81.517	51.182	−28.569	1.00	70.58	C
ATOM	3364	CG1	VAL	B	650	−81.723	49.839	−27.885	1.00	70.02	C
ATOM	3365	CG2	VAL	B	650	−81.146	52.245	−27.549	1.00	70.80	C
ATOM	3366	C	VAL	B	650	−80.897	50.209	−30.814	1.00	71.06	C
ATOM	3367	O	VAL	B	650	−82.092	50.194	−31.175	1.00	70.88	O
ATOM	3368	N	ASP	B	651	−79.911	49.492	−31.401	1.00	74.95	N
ATOM	3369	CA	ASP	B	651	−80.052	48.625	−32.559	1.00	75.66	C
ATOM	3370	CB	ASP	B	651	−81.277	47.685	−32.445	1.00	76.16	C
ATOM	3371	CG	ASP	B	651	−81.529	46.758	−33.626	1.00	78.41	C
ATOM	3372	OD1	ASP	B	651	−80.530	46.195	−34.180	1.00	80.78	O
ATOM	3373	OD2	ASP	B	651	−82.727	46.584	−34.003	1.00	80.71	O
ATOM	3374	C	ASP	B	651	−80.132	49.596	−33.710	1.00	75.69	C
ATOM	3375	O	ASP	B	651	−79.143	50.298	−33.950	1.00	75.69	O
ATOM	3376	N	ASN	B	652	−81.294	49.702	−34.387	1.00	77.61	N
ATOM	3377	CA	ASN	B	652	−81.461	50.629	−35.493	1.00	77.68	C
ATOM	3378	CB	ASN	B	652	−81.874	49.898	−36.775	1.00	77.48	C
ATOM	3379	CG	ASN	B	652	−80.748	49.236	−37.560	1.00	77.93	C
ATOM	3380	OD1	ASN	B	652	−79.540	49.314	−37.242	1.00	78.69	O
ATOM	3381	ND2	ASN	B	652	−81.135	48.552	−38.626	1.00	78.67	N
ATOM	3382	C	ASN	B	652	−82.435	51.728	−35.091	1.00	77.91	C
ATOM	3383	O	ASN	B	652	−83.069	52.348	−35.940	1.00	78.35	O
ATOM	3384	N	THR	B	653	−82.551	51.977	−33.791	1.00	75.16	N
ATOM	3385	CA	THR	B	653	−83.417	53.015	−33.281	1.00	75.21	C
ATOM	3386	CB	THR	B	653	−84.473	52.452	−32.330	1.00	75.26	C
ATOM	3387	OG1	THR	B	653	−85.255	51.464	−33.006	1.00	75.72	O
ATOM	3388	CG2	THR	B	653	−85.399	53.526	−31.794	1.00	74.72	C
ATOM	3389	C	THR	B	653	−82.546	54.045	−32.635	1.00	75.52	C
ATOM	3390	O	THR	B	653	−81.665	53.697	−31.861	1.00	75.87	O
ATOM	3391	N	CYS	B	654	−82.767	55.319	−32.972	1.00	76.26	N
ATOM	3392	CA	CYS	B	654	−82.038	56.437	−32.405	1.00	76.22	C
ATOM	3393	CB	CYS	B	654	−81.803	57.509	−33.454	1.00	76.68	C
ATOM	3394	SG	CYS	B	654	−81.111	59.037	−32.794	1.00	79.21	S
ATOM	3395	C	CYS	B	654	−82.871	56.956	−31.255	1.00	75.66	C
ATOM	3396	O	CYS	B	654	−84.076	57.208	−31.421	1.00	75.66	O
ATOM	3397	N	VAL	B	655	−82.248	57.048	−30.064	1.00	70.52	N
ATOM	3398	CA	VAL	B	655	−82.914	57.520	−28.847	1.00	69.96	C
ATOM	3399	CB	VAL	B	655	−82.983	56.490	−27.703	1.00	69.62	C
ATOM	3400	CG1	VAL	B	655	−83.639	57.095	−26.464	1.00	68.37	C
ATOM	3401	CG2	VAL	B	655	−83.715	55.226	−28.147	1.00	69.18	C
ATOM	3402	C	VAL	B	655	−82.292	58.801	−28.392	1.00	70.24	C
ATOM	3403	O	VAL	B	655	−81.069	58.871	−28.242	1.00	69.75	O
ATOM	3404	N	VAL	B	656	−83.151	59.819	−28.201	1.00	71.61	N
ATOM	3405	CA	VAL	B	656	−82.816	61.150	−27.714	1.00	72.11	C
ATOM	3406	CB	VAL	B	656	−83.183	62.263	−28.729	1.00	72.14	C
ATOM	3407	CG1	VAL	B	656	−83.344	63.625	−28.055	1.00	72.22	C
ATOM	3408	CG2	VAL	B	656	−82.148	62.334	−29.843	1.00	71.57	C
ATOM	3409	C	VAL	B	656	−83.560	61.248	−26.401	1.00	72.63	C
ATOM	3410	O	VAL	B	656	−84.772	61.054	−26.372	1.00	72.38	O
ATOM	3411	N	ARG	B	657	−82.825	61.480	−25.304	1.00	78.59	N
ATOM	3412	CA	ARG	B	657	−83.387	61.567	−23.953	1.00	79.74	C
ATOM	3413	CB	ARG	B	657	−82.539	60.731	−22.976	1.00	79.78	C
ATOM	3414	CG	ARG	B	657	−82.737	59.207	−23.123	1.00	80.65	C
ATOM	3415	CD	ARG	B	657	−83.820	58.623	−22.204	1.00	82.56	C
ATOM	3416	NE	ARG	B	657	−83.525	58.905	−20.795	1.00	85.35	N
ATOM	3417	CZ	ARG	B	657	−82.733	58.168	−20.003	1.00	87.81	C
ATOM	3418	NH1	ARG	B	657	−82.173	57.043	−20.459	1.00	88.85	N
ATOM	3419	NH2	ARG	B	657	−82.504	58.544	−18.748	1.00	88.39	N
ATOM	3420	C	ARG	B	657	−83.533	63.037	−23.534	1.00	80.41	C
ATOM	3421	O	ARG	B	657	−82.609	63.828	−23.747	1.00	80.41	O
ATOM	3422	N	SER	B	658	−84.706	63.407	−22.982	1.00	83.27	N
ATOM	3423	CA	SER	B	658	−85.011	64.791	−22.589	1.00	84.33	C
ATOM	3424	CB	SER	B	658	−85.972	65.406	−23.597	1.00	84.44	C
ATOM	3425	OG	SER	B	658	−87.160	64.623	−23.627	1.00	85.47	O
ATOM	3426	C	SER	B	658	−85.614	64.919	−21.181	1.00	84.82	C
ATOM	3427	O	SER	B	658	−86.333	64.018	−20.728	1.00	85.31	O
ATOM	3428	N	ARG	B	659	−85.349	66.076	−20.511	1.00	83.80	N
ATOM	3429	CA	ARG	B	659	−85.794	66.403	−19.147	1.00	83.94	C
ATOM	3430	CB	ARG	B	659	−84.813	67.394	−18.504	1.00	83.98	C
ATOM	3431	C	ARG	B	659	−87.216	66.937	−19.109	1.00	83.92	C
ATOM	3432	O	ARG	B	659	−88.139	66.240	−19.535	1.00	84.37	O
ATOM	3433	N	GLU	B	670	−90.617	74.494	−28.169	1.00	107.03	N
ATOM	3434	CA	GLU	B	670	−90.150	73.859	−29.399	1.00	107.20	C
ATOM	3435	CB	GLU	B	670	−88.867	74.517	−29.912	1.00	107.28	C
ATOM	3436	CG	GLU	B	670	−88.726	74.422	−31.425	1.00	108.21	C
ATOM	3437	CD	GLU	B	670	−87.325	74.535	−31.995	1.00	109.40	C
ATOM	3438	OE1	GLU	B	670	−86.487	75.246	−31.390	1.00	109.72	O
ATOM	3439	OE2	GLU	B	670	−87.068	73.917	−33.056	1.00	109.72	O
ATOM	3440	C	GLU	B	670	−89.976	72.318	−29.299	1.00	107.16	C
ATOM	3441	O	GLU	B	670	−89.705	71.776	−28.212	1.00	107.43	O
ATOM	3442	N	ALA	B	671	−90.138	71.624	−30.458	1.00	103.50	N
ATOM	3443	CA	ALA	B	671	−90.045	70.172	−30.584	1.00	102.63	C
ATOM	3444	CB	ALA	B	671	−90.734	69.700	−31.852	1.00	102.68	C
ATOM	3445	C	ALA	B	671	−88.626	69.671	−30.551	1.00	102.05	C
ATOM	3446	O	ALA	B	671	−87.751	70.194	−31.255	1.00	101.78	O
ATOM	3447	N	VAL	B	672	−88.409	68.639	−29.715	1.00	98.57	N
ATOM	3448	CA	VAL	B	672	−87.128	67.956	−29.538	1.00	97.51	C
ATOM	3449	CB	VAL	B	672	−87.063	67.254	−28.166	1.00	97.29	C
ATOM	3450	CG1	VAL	B	672	−85.709	66.595	−27.963	1.00	97.24	C
ATOM	3451	CG2	VAL	B	672	−87.360	68.223	−27.039	1.00	96.37	C
ATOM	3452	C	VAL	B	672	−87.071	66.945	−30.680	1.00	97.19	C
ATOM	3453	O	VAL	B	672	−87.936	66.062	−30.741	1.00	97.15	O
ATOM	3454	N	THR	B	673	−86.084	67.082	−31.590	1.00	93.85	N
ATOM	3455	CA	THR	B	673	−86.007	66.179	−32.738	1.00	93.22	C
ATOM	3456	CB	THR	B	673	−86.082	66.971	−34.055	1.00	93.20	C
ATOM	3457	OG1	THR	B	673	−87.252	67.789	−34.046	1.00	93.18	O
ATOM	3458	CG2	THR	B	673	−86.115	66.071	−35.288	1.00	93.30	C
ATOM	3459	C	THR	B	673	−84.862	65.181	−32.725	1.00	92.78	C
ATOM	3460	O	THR	B	673	−83.703	65.600	−32.638	1.00	92.70	O
ATOM	3461	N	ALA	B	674	−85.193	63.863	−32.857	1.00	85.71	N
ATOM	3462	CA	ALA	B	674	−84.223	62.776	−32.942	1.00	85.33	C
ATOM	3463	CB	ALA	B	674	−84.859	61.471	−32.509	1.00	85.28	C
ATOM	3464	C	ALA	B	674	−83.760	62.709	−34.412	1.00	85.29	C
ATOM	3465	O	ALA	B	674	−84.589	62.797	−35.317	1.00	85.26	O
ATOM	3466	N	VAL	B	675	−82.442	62.626	−34.650	1.00	81.79	N
ATOM	3467	CA	VAL	B	675	−81.863	62.631	−35.999	1.00	82.25	C
ATOM	3468	CB	VAL	B	675	−81.074	63.949	−36.260	1.00	82.10	C
ATOM	3469	CG1	VAL	B	675	−80.323	63.902	−37.582	1.00	81.84	C
ATOM	3470	CG2	VAL	B	675	−81.986	65.173	−36.207	1.00	81.53	C
ATOM	3471	C	VAL	B	675	−81.012	61.389	−36.259	1.00	82.96	C
ATOM	3472	O	VAL	B	675	−79.932	61.222	−35.671	1.00	82.87	O
ATOM	3473	N	ALA	B	676	−81.483	60.541	−37.182	1.00	83.86	N
ATOM	3474	CA	ALA	B	676	−80.804	59.298	−37.538	1.00	84.66	C
ATOM	3475	CB	ALA	B	676	−81.787	58.148	−37.422	1.00	84.58	C
ATOM	3476	C	ALA	B	676	−80.159	59.282	−38.926	1.00	85.33	C
ATOM	3477	O	ALA	B	676	−80.844	59.573	−39.898	1.00	85.57	O
ATOM	3478	N	ILE	B	677	−78.866	58.922	−39.027	1.00	85.93	N
ATOM	3479	CA	ILE	B	677	−78.177	58.793	−40.309	1.00	87.29	C
ATOM	3480	CB	ILE	B	677	−76.731	59.365	−40.279	1.00	87.10	C
ATOM	3481	CG1	ILE	B	677	−76.739	60.894	−40.163	1.00	86.31	C
ATOM	3482	CD1	ILE	B	677	−75.397	61.517	−39.806	1.00	85.43	C
ATOM	3483	CG2	ILE	B	677	−75.901	58.886	−41.506	1.00	87.10	C
ATOM	3484	C	ILE	B	677	−78.200	57.285	−40.643	1.00	88.69	C
ATOM	3485	O	ILE	B	677	−77.514	56.508	−39.976	1.00	88.82	O
ATOM	3486	N	CYS	B	678	−78.983	56.879	−41.662	1.00	95.76	N
ATOM	3487	CA	CYS	B	678	−79.116	55.479	−42.075	1.00	97.30	C
ATOM	3488	CB	CYS	B	678	−80.583	55.115	−42.238	1.00	96.90	C
ATOM	3489	SG	CYS	B	678	−81.590	55.474	−40.783	1.00	96.44	S
ATOM	3490	C	CYS	B	678	−78.311	55.090	−43.309	1.00	98.81	C
ATOM	3491	O	CYS	B	678	−78.330	55.806	−44.300	1.00	98.90	O
ATOM	3492	N	CYS	B	679	−77.630	53.935	−43.265	1.00	107.42	N
ATOM	3493	CA	CYS	B	679	−76.839	53.458	−44.401	1.00	109.62	C
ATOM	3494	CB	CYS	B	679	−75.362	53.759	−44.203	1.00	109.63	C
ATOM	3495	SG	CYS	B	679	−75.035	55.440	−43.622	1.00	112.09	S
ATOM	3496	C	CYS	B	679	−77.080	51.998	−44.779	1.00	110.70	C
ATOM	3497	O	CYS	B	679	−77.664	51.247	−43.996	1.00	110.76	O
ATOM	3498	N	ARG	B	680	−76.668	51.620	−46.014	1.00	115.73	N
ATOM	3499	CA	ARG	B	680	−76.780	50.274	−46.602	1.00	117.24	C
ATOM	3500	CB	ARG	B	680	−78.259	49.884	−46.889	1.00	117.32	C
ATOM	3501	CG	ARG	B	680	−78.910	50.627	−48.051	1.00	118.28	C
ATOM	3502	CD	ARG	B	680	−80.001	49.809	−48.728	1.00	120.20	C
ATOM	3503	NE	ARG	B	680	−80.512	50.497	−49.921	1.00	121.55	N
ATOM	3504	CZ	ARG	B	680	−81.798	50.736	−50.181	1.00	121.99	C
ATOM	3505	NH1	ARG	B	680	−82.742	50.334	−49.335	1.00	122.32	N
ATOM	3506	NH2	ARG	B	680	−82.148	51.381	−51.288	1.00	122.33	N
ATOM	3507	C	ARG	B	680	−75.906	50.131	−47.873	1.00	118.03	C
ATOM	3508	O	ARG	B	680	−75.131	51.036	−48.200	1.00	117.95	O
ATOM	3509	N	SER	B	681	−76.034	48.972	−48.568	1.00	120.44	N
ATOM	3510	CA	SER	B	681	−75.376	48.656	−49.838	1.00	121.18	C
ATOM	3511	CB	SER	B	681	−74.457	47.442	−49.711	1.00	121.11	C
ATOM	3512	OG	SER	B	681	−73.359	47.574	−50.602	1.00	121.38	O
ATOM	3513	C	SER	B	681	−76.549	48.417	−50.821	1.00	121.58	C
ATOM	3514	O	SER	B	681	−77.264	47.411	−50.695	1.00	121.71	O
ATOM	3515	N	ARG	B	682	−76.777	49.412	−51.737	1.00	120.01	N
ATOM	3516	CA	ARG	B	682	−77.837	49.537	−52.769	1.00	120.22	C
ATOM	3517	CB	ARG	B	682	−77.387	50.442	−53.933	1.00	120.08	C
ATOM	3518	C	ARG	B	682	−78.603	48.269	−53.249	1.00	120.27	C
ATOM	3519	O	ARG	B	682	−78.104	47.460	−54.034	1.00	120.40	O
TER	3520		ARG	B	682
ATOM	3521	N	THR	A	61	−42.992	55.146	−11.374	1.00	94.08	N
ATOM	3522	CA	THR	A	61	−43.825	54.985	−12.583	1.00	94.03	C
ATOM	3523	CB	THR	A	61	−43.011	55.185	−13.899	1.00	94.36	C
ATOM	3524	OG1	THR	A	61	−41.662	55.588	−13.626	1.00	95.12	O
ATOM	3525	CG2	THR	A	61	−43.697	56.150	−14.889	1.00	94.34	C
ATOM	3526	C	THR	A	61	−44.554	53.625	−12.600	1.00	93.40	C
ATOM	3527	O	THR	A	61	−45.562	53.477	−13.300	1.00	93.63	O
ATOM	3528	N	ALA	A	62	−44.025	52.632	−11.841	1.00	86.60	N
ATOM	3529	CA	ALA	A	62	−44.604	51.293	−11.751	1.00	85.19	C
ATOM	3530	CB	ALA	A	62	−43.541	50.270	−11.387	1.00	85.12	C
ATOM	3531	C	ALA	A	62	−45.728	51.292	−10.735	1.00	84.17	C
ATOM	3532	O	ALA	A	62	−45.572	51.771	−9.607	1.00	84.03	O
ATOM	3533	N	THR	A	63	−46.872	50.770	−11.152	1.00	78.31	N
ATOM	3534	CA	THR	A	63	−48.064	50.711	−10.314	1.00	77.03	C
ATOM	3535	CB	THR	A	63	−49.247	51.320	−11.047	1.00	77.14	C
ATOM	3536	OG1	THR	A	63	−49.183	50.975	−12.444	1.00	77.22	O
ATOM	3537	CG2	THR	A	63	−49.309	52.826	−10.855	1.00	77.10	C
ATOM	3538	C	THR	A	63	−48.358	49.331	−9.758	1.00	75.91	C
ATOM	3539	O	THR	A	63	−47.909	48.323	−10.298	1.00	75.80	O
ATOM	3540	N	PHE	A	64	−49.094	49.294	−8.667	1.00	69.45	N
ATOM	3541	CA	PHE	A	64	−49.457	48.047	−8.055	1.00	68.44	C
ATOM	3542	CB	PHE	A	64	−48.972	47.998	−6.617	1.00	68.44	C
ATOM	3543	CG	PHE	A	64	−49.525	46.873	−5.781	1.00	68.49	C
ATOM	3544	CD1	PHE	A	64	−48.948	45.612	−5.815	1.00	68.43	C
ATOM	3545	CE1	PHE	A	64	−49.459	44.576	−5.029	1.00	68.32	C
ATOM	3546	CZ	PHE	A	64	−50.539	44.802	−4.201	1.00	68.09	C
ATOM	3547	CE2	PHE	A	64	−51.113	46.050	−4.146	1.00	67.74	C
ATOM	3548	CD2	PHE	A	64	−50.610	47.083	−4.936	1.00	67.80	C
ATOM	3549	C	PHE	A	64	−50.961	47.864	−8.183	1.00	67.94	C
ATOM	3550	O	PHE	A	64	−51.731	48.822	−8.140	1.00	67.79	O
ATOM	3551	N	HIS	A	65	−51.371	46.616	−8.385	1.00	70.21	N
ATOM	3552	CA	HIS	A	65	−52.759	46.236	−8.570	1.00	69.19	C
ATOM	3553	CB	HIS	A	65	−53.006	45.898	−10.048	1.00	69.21	C
ATOM	3554	CG	HIS	A	65	−52.742	47.070	−10.939	1.00	70.70	C
ATOM	3555	ND1	HIS	A	65	−51.443	47.456	−11.268	1.00	72.28	N
ATOM	3556	CE1	HIS	A	65	−51.562	48.539	−12.014	1.00	71.06	C
ATOM	3557	NE2	HIS	A	65	−52.840	48.865	−12.190	1.00	71.69	N
ATOM	3558	CD2	HIS	A	65	−53.606	47.942	−11.501	1.00	71.22	C
ATOM	3559	C	HIS	A	65	−53.114	45.081	−7.683	1.00	68.59	C
ATOM	3560	O	HIS	A	65	−52.321	44.163	−7.508	1.00	68.49	O
ATOM	3561	N	ARG	A	66	−54.295	45.143	−7.099	1.00	67.78	N
ATOM	3562	CA	ARG	A	66	−54.830	44.100	−6.240	1.00	67.53	C
ATOM	3563	CB	ARG	A	66	−54.410	44.260	−4.762	1.00	67.50	C
ATOM	3564	CG	ARG	A	66	−54.777	45.560	−4.108	1.00	68.39	C
ATOM	3565	CD	ARG	A	66	−55.971	45.345	−3.237	1.00	70.95	C
ATOM	3566	NE	ARG	A	66	−56.472	46.607	−2.707	1.00	72.19	N
ATOM	3567	CZ	ARG	A	66	−57.602	46.744	−2.019	1.00	72.89	C
ATOM	3568	NH1	ARG	A	66	−58.362	45.682	−1.752	1.00	73.37	N
ATOM	3569	NH2	ARG	A	66	−57.984	47.942	−1.595	1.00	74.64	N
ATOM	3570	C	ARG	A	66	−56.332	43.981	−6.436	1.00	67.14	C
ATOM	3571	O	ARG	A	66	−56.961	44.864	−7.024	1.00	67.05	O
ATOM	3572	N	CYS	A	67	−56.902	42.877	−5.981	1.00	67.36	N
ATOM	3573	CA	CYS	A	67	−58.323	42.631	−6.127	1.00	66.60	C
ATOM	3574	CB	CYS	A	67	−58.642	41.169	−5.830	1.00	66.74	C
ATOM	3575	SG	CYS	A	67	−60.357	40.701	−6.178	1.00	67.75	S
ATOM	3576	C	CYS	A	67	−59.103	43.565	−5.237	1.00	65.89	C
ATOM	3577	O	CYS	A	67	−58.732	43.748	−4.081	1.00	65.55	O
ATOM	3578	N	ALA	A	68	−60.173	44.168	−5.780	1.00	65.52	N
ATOM	3579	CA	ALA	A	68	−61.061	45.076	−5.044	1.00	64.94	C
ATOM	3580	CB	ALA	A	68	−61.968	45.802	−6.008	1.00	64.52	C
ATOM	3581	C	ALA	A	68	−61.884	44.292	−3.995	1.00	64.88	C
ATOM	3582	O	ALA	A	68	−62.169	44.823	−2.928	1.00	64.74	O
ATOM	3583	N	LYS	A	69	−62.228	43.024	−4.286	1.00	67.62	N
ATOM	3584	CA	LYS	A	69	−62.968	42.154	−3.366	1.00	68.11	C
ATOM	3585	CB	LYS	A	69	−63.802	41.076	−4.116	1.00	68.34	C
ATOM	3586	CG	LYS	A	69	−64.420	41.527	−5.465	1.00	70.40	C
ATOM	3587	CD	LYS	A	69	−65.785	42.295	−5.349	1.00	73.07	C
ATOM	3588	CE	LYS	A	69	−66.163	43.111	−6.579	1.00	73.40	C
ATOM	3589	NZ	LYS	A	69	−67.238	44.114	−6.294	1.00	73.28	N
ATOM	3590	C	LYS	A	69	−61.946	41.533	−2.403	1.00	68.01	C
ATOM	3591	O	LYS	A	69	−61.297	40.544	−2.732	1.00	67.83	O
ATOM	3592	N	ASP	A	70	−61.781	42.142	−1.225	1.00	72.25	N
ATOM	3593	CA	ASP	A	70	−60.823	41.685	−0.221	1.00	72.93	C
ATOM	3594	CB	ASP	A	70	−60.900	42.495	1.069	1.00	73.96	C
ATOM	3595	CG	ASP	A	70	−60.314	43.895	0.917	1.00	78.57	C
ATOM	3596	OD1	ASP	A	70	−59.122	44.095	1.329	1.00	82.61	O
ATOM	3597	OD2	ASP	A	70	−61.038	44.802	0.379	1.00	81.92	O
ATOM	3598	C	ASP	A	70	−60.733	40.191	0.053	1.00	72.06	C
ATOM	3599	O	ASP	A	70	−59.614	39.696	0.074	1.00	72.62	O
ATOM	3600	N	PRO	A	71	−61.835	39.425	0.219	1.00	65.61	N
ATOM	3601	CA	PRO	A	71	−61.692	37.979	0.491	1.00	64.69	C
ATOM	3602	CB	PRO	A	71	−63.120	37.531	0.763	1.00	64.75	C
ATOM	3603	CG	PRO	A	71	−63.888	38.762	1.004	1.00	65.16	C
ATOM	3604	CD	PRO	A	71	−63.251	39.825	0.221	1.00	65.34	C
ATOM	3605	C	PRO	A	71	−61.110	37.126	−0.629	1.00	64.06	C
ATOM	3606	O	PRO	A	71	−60.814	35.951	−0.395	1.00	64.26	O
ATOM	3607	N	TRP	A	72	−60.970	37.698	−1.847	1.00	62.84	N
ATOM	3608	CA	TRP	A	72	−60.442	37.025	−3.029	1.00	61.80	C
ATOM	3609	CB	TRP	A	72	−61.200	37.473	−4.272	1.00	61.49	C
ATOM	3610	CG	TRP	A	72	−62.596	36.957	−4.323	1.00	60.52	C
ATOM	3611	CD1	TRP	A	72	−63.195	36.113	−3.434	1.00	60.19	C
ATOM	3612	NE1	TRP	A	72	−64.489	35.863	−3.815	1.00	59.75	N
ATOM	3613	CE2	TRP	A	72	−64.758	36.559	−4.967	1.00	59.41	C
ATOM	3614	CD2	TRP	A	72	−63.577	37.249	−5.323	1.00	59.63	C
ATOM	3615	CE3	TRP	A	72	−63.583	38.042	−6.481	1.00	59.30	C
ATOM	3616	CZ3	TRP	A	72	−64.748	38.123	−7.226	1.00	58.49	C
ATOM	3617	CH2	TRP	A	72	−65.891	37.403	−6.863	1.00	57.68	C
ATOM	3618	CZ2	TRP	A	72	−65.922	36.618	−5.741	1.00	57.93	C
ATOM	3619	C	TRP	A	72	−58.977	37.271	−3.205	1.00	61.81	C
ATOM	3620	O	TRP	A	72	−58.348	36.600	−4.020	1.00	61.74	O
ATOM	3621	N	ARG	A	73	−58.419	38.234	−2.453	1.00	63.78	N
ATOM	3622	CA	ARG	A	73	−56.999	38.583	−2.518	1.00	63.69	C
ATOM	3623	CB	ARG	A	73	−56.719	39.805	−1.667	1.00	63.71	C
ATOM	3624	CG	ARG	A	73	−57.297	41.081	−2.210	1.00	64.55	C
ATOM	3625	CD	ARG	A	73	−57.007	42.217	−1.260	1.00	66.07	C
ATOM	3626	NE	ARG	A	73	−55.585	42.541	−1.253	1.00	67.02	N
ATOM	3627	CZ	ARG	A	73	−55.066	43.593	−0.634	1.00	67.26	C
ATOM	3628	NH1	ARG	A	73	−53.756	43.823	−0.688	1.00	67.03	N
ATOM	3629	NH2	ARG	A	73	−55.856	44.444	0.021	1.00	68.05	N
ATOM	3630	C	ARG	A	73	−56.125	37.442	−2.039	1.00	63.44	C
ATOM	3631	O	ARG	A	73	−56.520	36.701	−1.125	1.00	63.26	O
ATOM	3632	N	LEU	A	74	−54.938	37.299	−2.660	1.00	62.91	N
ATOM	3633	CA	LEU	A	74	−53.974	36.250	−2.301	1.00	63.06	C
ATOM	3634	CB	LEU	A	74	−53.932	35.125	−3.349	1.00	62.90	C
ATOM	3635	CG	LEU	A	74	−55.224	34.373	−3.584	1.00	61.25	C
ATOM	3636	CD1	LEU	A	74	−55.053	33.386	−4.668	1.00	59.62	C
ATOM	3637	CD2	LEU	A	74	−55.713	33.711	−2.332	1.00	59.04	C
ATOM	3638	C	LEU	A	74	−52.586	36.842	−2.076	1.00	63.27	C
ATOM	3639	O	LEU	A	74	−51.678	36.573	−2.875	1.00	63.60	O
ATOM	3640	N	PRO	A	75	−52.399	37.647	−0.988	1.00	64.69	N
ATOM	3641	CA	PRO	A	75	−51.076	38.265	−0.739	1.00	64.81	C
ATOM	3642	CB	PRO	A	75	−51.294	39.086	0.528	1.00	64.47	C
ATOM	3643	CG	PRO	A	75	−52.506	38.486	1.148	1.00	64.57	C
ATOM	3644	CD	PRO	A	75	−53.370	38.037	0.053	1.00	64.42	C
ATOM	3645	C	PRO	A	75	−49.965	37.240	−0.582	1.00	64.82	C
ATOM	3646	O	PRO	A	75	−50.240	36.119	−0.168	1.00	65.20	O
ATOM	3647	N	GLY	A	76	−48.747	37.611	−0.953	1.00	65.10	N
ATOM	3648	CA	GLY	A	76	−47.627	36.689	−0.893	1.00	65.15	C
ATOM	3649	C	GLY	A	76	−47.257	36.182	−2.270	1.00	65.43	C
ATOM	3650	O	GLY	A	76	−46.132	35.730	−2.481	1.00	65.75	O
ATOM	3651	N	THR	A	77	−48.185	36.258	−3.225	1.00	66.14	N
ATOM	3652	CA	THR	A	77	−47.894	35.832	−4.588	1.00	66.17	C
ATOM	3653	CB	THR	A	77	−48.593	34.534	−4.943	1.00	66.36	C
ATOM	3654	OG1	THR	A	77	−48.498	33.644	−3.813	1.00	67.43	O
ATOM	3655	CG2	THR	A	77	−47.989	33.881	−6.188	1.00	65.71	C
ATOM	3656	C	THR	A	77	−48.193	36.989	−5.481	1.00	66.17	C
ATOM	3657	O	THR	A	77	−49.247	37.602	−5.356	1.00	66.06	O
ATOM	3658	N	TYR	A	78	−47.234	37.335	−6.338	1.00	65.71	N
ATOM	3659	CA	TYR	A	78	−47.327	38.487	−7.228	1.00	66.03	C
ATOM	3660	CB	TYR	A	78	−46.449	39.646	−6.681	1.00	65.51	C
ATOM	3661	CG	TYR	A	78	−46.823	40.011	−5.260	1.00	64.46	C
ATOM	3662	CD1	TYR	A	78	−47.766	41.000	−5.000	1.00	62.96	C
ATOM	3663	CE1	TYR	A	78	−48.169	41.290	−3.702	1.00	61.90	C
ATOM	3664	CZ	TYR	A	78	−47.643	40.571	−2.642	1.00	62.48	C
ATOM	3665	OH	TYR	A	78	−48.064	40.836	−1.367	1.00	62.90	O
ATOM	3666	CE2	TYR	A	78	−46.707	39.580	−2.871	1.00	63.20	C
ATOM	3667	CD2	TYR	A	78	−46.294	39.311	−4.175	1.00	63.76	C
ATOM	3668	C	TYR	A	78	−46.927	38.144	−8.640	1.00	67.03	C
ATOM	3669	O	TYR	A	78	−46.096	37.260	−8.858	1.00	67.43	O
ATOM	3670	N	VAL	A	79	−47.515	38.844	−9.603	1.00	66.76	N
ATOM	3671	CA	VAL	A	79	−47.203	38.667	−11.018	1.00	67.72	C
ATOM	3672	CB	VAL	A	79	−48.450	38.357	−11.887	1.00	67.49	C
ATOM	3673	CG1	VAL	A	79	−48.165	38.537	−13.373	1.00	66.92	C
ATOM	3674	CG2	VAL	A	79	−48.959	36.957	−11.613	1.00	67.53	C
ATOM	3675	C	VAL	A	79	−46.494	39.959	−11.411	1.00	68.95	C
ATOM	3676	O	VAL	A	79	−47.116	41.031	−11.473	1.00	69.13	O
ATOM	3677	N	VAL	A	80	−45.173	39.860	−11.623	1.00	68.33	N
ATOM	3678	CA	VAL	A	80	−44.388	41.016	−12.002	1.00	69.38	C
ATOM	3679	CB	VAL	A	80	−42.947	40.931	−11.485	1.00	69.16	C
ATOM	3680	CG1	VAL	A	80	−42.137	42.144	−11.942	1.00	69.16	C
ATOM	3681	CG2	VAL	A	80	−42.934	40.808	−9.964	1.00	69.15	C
ATOM	3682	C	VAL	A	80	−44.485	41.158	−13.504	1.00	70.51	C
ATOM	3683	O	VAL	A	80	−44.064	40.271	−14.242	1.00	70.63	O
ATOM	3684	N	VAL	A	81	−45.088	42.250	−13.943	1.00	71.08	N
ATOM	3685	CA	VAL	A	81	−45.278	42.520	−15.352	1.00	72.85	C
ATOM	3686	CB	VAL	A	81	−46.738	42.913	−15.672	1.00	72.46	C
ATOM	3687	CG1	VAL	A	81	−46.901	43.266	−17.136	1.00	71.97	C
ATOM	3688	CG2	VAL	A	81	−47.690	41.790	−15.294	1.00	72.64	C
ATOM	3689	C	VAL	A	81	−44.264	43.564	−15.788	1.00	74.56	C
ATOM	3690	O	VAL	A	81	−44.175	44.653	−15.203	1.00	74.54	O
ATOM	3691	N	LEU	A	82	−43.489	43.207	−16.818	1.00	80.31	N
ATOM	3692	CA	LEU	A	82	−42.454	44.045	−17.403	1.00	82.53	C
ATOM	3693	CB	LEU	A	82	−41.202	43.217	−17.733	1.00	82.15	C
ATOM	3694	CG	LEU	A	82	−40.653	42.348	−16.593	1.00	82.16	C
ATOM	3695	CD1	LEU	A	82	−39.625	41.406	−17.092	1.00	81.74	C
ATOM	3696	CD2	LEU	A	82	−40.070	43.178	−15.458	1.00	81.41	C
ATOM	3697	C	LEU	A	82	−42.980	44.810	−18.618	1.00	84.46	C
ATOM	3698	O	LEU	A	82	−43.996	44.420	−19.204	1.00	84.83	O
ATOM	3699	N	LYS	A	83	−42.301	45.919	−18.974	1.00	91.85	N
ATOM	3700	CA	LYS	A	83	−42.649	46.806	−20.083	1.00	94.25	C
ATOM	3701	CB	LYS	A	83	−41.678	47.993	−20.147	1.00	94.21	C
ATOM	3702	CG	LYS	A	83	−41.986	49.105	−19.144	1.00	95.08	C
ATOM	3703	CD	LYS	A	83	−40.695	49.669	−18.537	1.00	97.23	C
ATOM	3704	CE	LYS	A	83	−40.735	51.157	−18.255	1.00	97.94	C
ATOM	3705	NZ	LYS	A	83	−40.546	51.984	−19.491	1.00	98.59	N
ATOM	3706	C	LYS	A	83	−42.769	46.063	−21.424	1.00	95.90	C
ATOM	3707	O	LYS	A	83	−42.054	45.079	−21.642	1.00	95.76	O
ATOM	3708	N	GLU	A	84	−43.701	46.526	−22.296	1.00	102.18	N
ATOM	3709	CA	GLU	A	84	−44.037	45.957	−23.611	1.00	104.41	C
ATOM	3710	CB	GLU	A	84	−44.691	47.000	−24.543	1.00	104.70	C
ATOM	3711	CG	GLU	A	84	−46.054	46.597	−25.108	1.00	106.90	C
ATOM	3712	CD	GLU	A	84	−46.181	45.235	−25.779	1.00	109.87	C
ATOM	3713	OE1	GLU	A	84	−45.523	45.012	−26.824	1.00	111.52	O
ATOM	3714	OE2	GLU	A	84	−46.950	44.392	−25.259	1.00	110.62	O
ATOM	3715	C	GLU	A	84	−42.984	45.117	−24.364	1.00	105.41	C
ATOM	3716	O	GLU	A	84	−43.124	43.886	−24.441	1.00	105.62	O
ATOM	3717	N	GLU	A	85	−41.941	45.786	−24.914	1.00	107.79	N
ATOM	3718	CA	GLU	A	85	−40.879	45.175	−25.728	1.00	108.91	C
ATOM	3719	CB	GLU	A	85	−40.238	46.222	−26.663	1.00	109.11	C
ATOM	3720	CG	GLU	A	85	−41.150	46.605	−27.827	1.00	111.00	C
ATOM	3721	CD	GLU	A	85	−40.772	47.798	−28.696	1.00	113.16	C
ATOM	3722	OE1	GLU	A	85	−40.359	48.847	−28.145	1.00	114.02	O
ATOM	3723	OE2	GLU	A	85	−40.916	47.685	−29.938	1.00	113.67	O
ATOM	3724	C	GLU	A	85	−39.828	44.309	−25.030	1.00	109.16	C
ATOM	3725	O	GLU	A	85	−38.950	43.780	−25.710	1.00	109.04	O
ATOM	3726	N	THR	A	86	−39.924	44.140	−23.697	1.00	109.04	N
ATOM	3727	CA	THR	A	86	−38.972	43.356	−22.899	1.00	109.80	C
ATOM	3728	CB	THR	A	86	−39.355	43.350	−21.403	1.00	109.80	C
ATOM	3729	OG1	THR	A	86	−39.577	44.693	−20.962	1.00	110.29	O
ATOM	3730	CG2	THR	A	86	−38.298	42.692	−20.513	1.00	109.32	C
ATOM	3731	C	THR	A	86	−38.697	41.965	−23.462	1.00	110.40	C
ATOM	3732	O	THR	A	86	−39.616	41.260	−23.882	1.00	110.56	O
ATOM	3733	N	HIS	A	87	−37.417	41.600	−23.490	1.00	111.60	N
ATOM	3734	CA	HIS	A	87	−36.944	40.308	−23.955	1.00	112.22	C
ATOM	3735	CB	HIS	A	87	−35.651	40.479	−24.764	1.00	112.64	C
ATOM	3736	CG	HIS	A	87	−35.087	39.185	−25.249	1.00	115.04	C
ATOM	3737	ND1	HIS	A	87	−34.097	38.517	−24.538	1.00	116.61	N
ATOM	3738	CE1	HIS	A	87	−33.845	37.413	−25.224	1.00	116.85	C
ATOM	3739	NE2	HIS	A	87	−34.616	37.325	−26.312	1.00	117.28	N
ATOM	3740	CD2	HIS	A	87	−35.421	38.447	−26.334	1.00	116.55	C
ATOM	3741	C	HIS	A	87	−36.743	39.422	−22.712	1.00	111.92	C
ATOM	3742	O	HIS	A	87	−36.530	39.955	−21.617	1.00	111.91	O
ATOM	3743	N	LEU	A	88	−36.834	38.083	−22.879	1.00	108.74	N
ATOM	3744	CA	LEU	A	88	−36.707	37.080	−21.815	1.00	108.42	C
ATOM	3745	CB	LEU	A	88	−36.914	35.664	−22.370	1.00	108.37	C
ATOM	3746	CG	LEU	A	88	−36.940	34.493	−21.376	1.00	108.37	C
ATOM	3747	CD1	LEU	A	88	−37.980	34.690	−20.308	1.00	108.28	C
ATOM	3748	CD2	LEU	A	88	−37.214	33.194	−22.089	1.00	108.49	C
ATOM	3749	C	LEU	A	88	−35.449	37.179	−20.951	1.00	108.39	C
ATOM	3750	O	LEU	A	88	−35.524	36.925	−19.745	1.00	108.36	O
ATOM	3751	N	SER	A	89	−34.306	37.554	−21.554	1.00	107.40	N
ATOM	3752	CA	SER	A	89	−33.040	37.724	−20.841	1.00	107.18	C
ATOM	3753	CB	SER	A	89	−31.958	38.227	−21.791	1.00	107.30	C
ATOM	3754	OG	SER	A	89	−32.389	39.349	−22.545	1.00	107.73	O
ATOM	3755	C	SER	A	89	−33.226	38.702	−19.669	1.00	106.89	C
ATOM	3756	O	SER	A	89	−32.757	38.414	−18.572	1.00	106.96	O
ATOM	3757	N	GLN	A	90	−33.954	39.828	−19.900	1.00	105.98	N
ATOM	3758	CA	GLN	A	90	−34.269	40.851	−18.899	1.00	105.55	C
ATOM	3759	CB	GLN	A	90	−34.803	42.130	−19.540	1.00	105.69	C
ATOM	3760	CG	GLN	A	90	−33.738	42.972	−20.218	1.00	106.15	C
ATOM	3761	CD	GLN	A	90	−34.174	43.457	−21.582	1.00	106.52	C
ATOM	3762	OE1	GLN	A	90	−34.701	42.699	−22.415	1.00	106.51	O
ATOM	3763	NE2	GLN	A	90	−33.953	44.737	−21.845	1.00	106.74	N
ATOM	3764	C	GLN	A	90	−35.279	40.333	−17.894	1.00	105.10	C
ATOM	3765	O	GLN	A	90	−35.180	40.702	−16.723	1.00	105.02	O
ATOM	3766	N	SER	A	91	−36.256	39.491	−18.343	1.00	102.39	N
ATOM	3767	CA	SER	A	91	−37.274	38.889	−17.470	1.00	101.79	C
ATOM	3768	CB	SER	A	91	−38.193	37.948	−18.249	1.00	101.84	C
ATOM	3769	OG	SER	A	91	−39.238	38.596	−18.954	1.00	102.28	O
ATOM	3770	C	SER	A	91	−36.561	38.108	−16.373	1.00	101.27	C
ATOM	3771	O	SER	A	91	−36.857	38.277	−15.189	1.00	101.03	O
ATOM	3772	N	GLU	A	92	−35.586	37.287	−16.783	1.00	100.39	N
ATOM	3773	CA	GLU	A	92	−34.776	36.464	−15.894	1.00	100.06	C
ATOM	3774	CB	GLU	A	92	−34.044	35.389	−16.698	1.00	100.14	C
ATOM	3775	CG	GLU	A	92	−34.964	34.502	−17.515	1.00	101.12	C
ATOM	3776	CD	GLU	A	92	−34.249	33.372	−18.225	1.00	102.83	C
ATOM	3777	OE1	GLU	A	92	−33.476	33.651	−19.174	1.00	103.80	O
ATOM	3778	OE2	GLU	A	92	−34.457	32.204	−17.823	1.00	103.76	O
ATOM	3779	C	GLU	A	92	−33.796	37.332	−15.093	1.00	99.64	C
ATOM	3780	O	GLU	A	92	−33.559	37.054	−13.917	1.00	99.53	O
ATOM	3781	N	ARG	A	93	−33.252	38.391	−15.728	1.00	98.20	N
ATOM	3782	CA	ARG	A	93	−32.324	39.345	−15.129	1.00	97.82	C
ATOM	3783	CB	ARG	A	93	−31.948	40.416	−16.180	1.00	98.13	C
ATOM	3784	CG	ARG	A	93	−30.644	41.194	−15.937	1.00	99.80	C
ATOM	3785	CD	ARG	A	93	−30.129	41.910	−17.197	1.00	101.97	C
ATOM	3786	NE	ARG	A	93	−29.467	40.988	−18.135	1.00	103.42	N
ATOM	3787	CZ	ARG	A	93	−29.900	40.713	−19.368	1.00	104.31	C
ATOM	3788	NH1	ARG	A	93	−30.993	41.300	−19.844	1.00	104.87	N
ATOM	3789	NH2	ARG	A	93	−29.237	39.857	−20.137	1.00	104.19	N
ATOM	3790	C	ARG	A	93	−33.000	39.981	−13.894	1.00	97.21	C
ATOM	3791	O	ARG	A	93	−32.505	39.807	−12.772	1.00	96.98	O
ATOM	3792	N	THR	A	94	−34.167	40.664	−14.112	1.00	93.34	N
ATOM	3793	CA	THR	A	94	−34.986	41.337	−13.089	1.00	92.40	C
ATOM	3794	CB	THR	A	94	−36.149	42.137	−13.722	1.00	92.32	C
ATOM	3795	OG1	THR	A	94	−35.743	42.711	−14.963	1.00	91.98	O
ATOM	3796	CG2	THR	A	94	−36.642	43.246	−12.826	1.00	92.59	C
ATOM	3797	C	THR	A	94	−35.426	40.359	−11.987	1.00	91.90	C
ATOM	3798	O	THR	A	94	−35.417	40.728	−10.813	1.00	91.73	O
ATOM	3799	N	ALA	A	95	−35.776	39.111	−12.367	1.00	90.39	N
ATOM	3800	CA	ALA	A	95	−36.178	38.065	−11.428	1.00	89.91	C
ATOM	3801	CB	ALA	A	95	−36.591	36.809	−12.176	1.00	89.80	C
ATOM	3802	C	ALA	A	95	−35.030	37.763	−10.478	1.00	89.75	C
ATOM	3803	O	ALA	A	95	−35.226	37.805	−9.263	1.00	89.56	O
ATOM	3804	N	ARG	A	96	−33.819	37.503	−11.036	1.00	91.58	N
ATOM	3805	CA	ARG	A	96	−32.603	37.207	−10.270	1.00	91.34	C
ATOM	3806	CB	ARG	A	96	−31.462	36.736	−11.179	1.00	91.22	C
ATOM	3807	C	ARG	A	96	−32.214	38.424	−9.448	1.00	91.23	C
ATOM	3808	O	ARG	A	96	−31.926	38.264	−8.264	1.00	91.23	O
ATOM	3809	N	ARG	A	97	−32.279	39.640	−10.048	1.00	92.37	N
ATOM	3810	CA	ARG	A	97	−31.984	40.908	−9.365	1.00	92.44	C
ATOM	3811	CB	ARG	A	97	−32.107	42.115	−10.334	1.00	92.70	C
ATOM	3812	CG	ARG	A	97	−31.829	43.487	−9.690	1.00	94.77	C
ATOM	3813	CD	ARG	A	97	−31.046	44.479	−10.557	1.00	99.05	C
ATOM	3814	NE	ARG	A	97	−30.156	45.347	−9.762	1.00	102.58	N
ATOM	3815	CZ	ARG	A	97	−28.901	45.033	−9.409	1.00	104.00	C
ATOM	3816	NH1	ARG	A	97	−28.367	43.869	−9.779	1.00	104.30	N
ATOM	3817	NH2	ARG	A	97	−28.174	45.881	−8.685	1.00	104.49	N
ATOM	3818	C	ARG	A	97	−32.900	41.071	−8.132	1.00	92.06	C
ATOM	3819	O	ARG	A	97	−32.456	41.576	−7.090	1.00	91.94	O
ATOM	3820	N	LEU	A	98	−34.168	40.614	−8.249	1.00	89.01	N
ATOM	3821	CA	LEU	A	98	−35.133	40.692	−7.161	1.00	88.35	C
ATOM	3822	CB	LEU	A	98	−36.565	40.441	−7.675	1.00	88.23	C
ATOM	3823	CG	LEU	A	98	−37.717	40.358	−6.657	1.00	86.92	C
ATOM	3824	CD1	LEU	A	98	−37.893	41.650	−5.897	1.00	85.51	C
ATOM	3825	CD2	LEU	A	98	−38.990	39.987	−7.346	1.00	85.38	C
ATOM	3826	C	LEU	A	98	−34.767	39.743	−6.033	1.00	88.29	C
ATOM	3827	O	LEU	A	98	−34.586	40.197	−4.903	1.00	88.02	O
ATOM	3828	N	GLN	A	99	−34.634	38.440	−6.343	1.00	89.27	N
ATOM	3829	CA	GLN	A	99	−34.303	37.381	−5.382	1.00	89.54	C
ATOM	3830	CB	GLN	A	99	−33.991	36.078	−6.121	1.00	89.39	C
ATOM	3831	CG	GLN	A	99	−35.159	35.469	−6.851	1.00	89.38	C
ATOM	3832	CD	GLN	A	99	−35.074	33.967	−6.829	1.00	89.63	C
ATOM	3833	OE1	GLN	A	99	−34.580	33.333	−7.783	1.00	89.30	O
ATOM	3834	NE2	GLN	A	99	−35.562	33.360	−5.734	1.00	88.93	N
ATOM	3835	C	GLN	A	99	−33.104	37.765	−4.510	1.00	89.87	C
ATOM	3836	O	GLN	A	99	−33.076	37.461	−3.305	1.00	89.84	O
ATOM	3837	N	ALA	A	100	−32.126	38.454	−5.158	1.00	92.62	N
ATOM	3838	CA	ALA	A	100	−30.861	38.948	−4.632	1.00	92.57	C
ATOM	3839	CB	ALA	A	100	−29.977	39.414	−5.779	1.00	92.48	C
ATOM	3840	C	ALA	A	100	−31.049	40.073	−3.639	1.00	92.61	C
ATOM	3841	O	ALA	A	100	−30.585	39.950	−2.501	1.00	92.73	O
ATOM	3842	N	GLN	A	101	−31.713	41.170	−4.062	1.00	91.54	N
ATOM	3843	CA	GLN	A	101	−31.960	42.316	−3.201	1.00	91.53	C
ATOM	3844	CB	GLN	A	101	−32.680	43.415	−3.967	1.00	91.53	C
ATOM	3845	CG	GLN	A	101	−31.748	44.103	−4.951	1.00	92.66	C
ATOM	3846	CD	GLN	A	101	−32.418	45.048	−5.921	1.00	93.49	C
ATOM	3847	OE1	GLN	A	101	−33.454	45.666	−5.642	1.00	94.00	O
ATOM	3848	NE2	GLN	A	101	−31.820	45.198	−7.088	1.00	93.98	N
ATOM	3849	C	GLN	A	101	−32.727	41.902	−1.947	1.00	91.42	C
ATOM	3850	O	GLN	A	101	−32.433	42.403	−0.864	1.00	91.36	O
ATOM	3851	N	ALA	A	102	−33.656	40.943	−2.095	1.00	89.40	N
ATOM	3852	CA	ALA	A	102	−34.489	40.393	−1.032	1.00	89.26	C
ATOM	3853	CB	ALA	A	102	−35.525	39.462	−1.639	1.00	89.34	C
ATOM	3854	C	ALA	A	102	−33.670	39.643	0.016	1.00	89.33	C
ATOM	3855	O	ALA	A	102	−33.893	39.807	1.226	1.00	88.78	O
ATOM	3856	N	ALA	A	103	−32.726	38.810	−0.471	1.00	91.22	N
ATOM	3857	CA	ALA	A	103	−31.824	37.998	0.339	1.00	91.41	C
ATOM	3858	CB	ALA	A	103	−30.920	37.189	−0.559	1.00	91.23	C
ATOM	3859	C	ALA	A	103	−30.993	38.867	1.290	1.00	91.64	C
ATOM	3860	O	ALA	A	103	−30.890	38.530	2.476	1.00	91.67	O
ATOM	3861	N	ARG	A	104	−30.449	40.012	0.799	1.00	94.32	N
ATOM	3862	CA	ARG	A	104	−29.663	40.899	1.654	1.00	94.63	C
ATOM	3863	CB	ARG	A	104	−28.583	41.665	0.885	1.00	94.83	C
ATOM	3864	CG	ARG	A	104	−29.067	42.802	0.027	1.00	96.25	C
ATOM	3865	CD	ARG	A	104	−27.874	43.433	−0.654	1.00	99.40	C
ATOM	3866	NE	ARG	A	104	−27.452	42.662	−1.828	1.00	101.85	N
ATOM	3867	CZ	ARG	A	104	−27.671	43.032	−3.088	1.00	103.05	C
ATOM	3868	NH1	ARG	A	104	−28.292	44.181	−3.356	1.00	103.65	N
ATOM	3869	NH2	ARG	A	104	−27.261	42.264	−4.092	1.00	103.39	N
ATOM	3870	C	ARG	A	104	−30.469	41.734	2.686	1.00	94.43	C
ATOM	3871	O	ARG	A	104	−30.007	42.773	3.178	1.00	94.68	O
ATOM	3872	N	ARG	A	105	−31.691	41.250	3.002	1.00	92.86	N
ATOM	3873	CA	ARG	A	105	−32.636	41.790	3.982	1.00	92.14	C
ATOM	3874	CB	ARG	A	105	−33.644	42.787	3.381	1.00	91.95	C
ATOM	3875	CG	ARG	A	105	−33.428	43.105	1.915	1.00	92.08	C
ATOM	3876	CD	ARG	A	105	−33.438	44.586	1.583	1.00	92.24	C
ATOM	3877	NE	ARG	A	105	−32.759	44.822	0.305	1.00	93.09	N
ATOM	3878	CZ	ARG	A	105	−32.665	46.001	−0.304	1.00	93.45	C
ATOM	3879	NH1	ARG	A	105	−32.019	46.108	−1.462	1.00	93.87	N
ATOM	3880	NH2	ARG	A	105	−33.218	47.084	0.239	1.00	92.83	N
ATOM	3881	C	ARG	A	105	−33.305	40.591	4.655	1.00	91.76	C
ATOM	3882	O	ARG	A	105	−34.331	40.718	5.320	1.00	91.78	O
ATOM	3883	N	GLY	A	106	−32.669	39.435	4.481	1.00	92.07	N
ATOM	3884	CA	GLY	A	106	−33.080	38.152	5.033	1.00	91.54	C
ATOM	3885	C	GLY	A	106	−34.368	37.585	4.478	1.00	91.23	C
ATOM	3886	O	GLY	A	106	−35.000	36.770	5.159	1.00	91.33	O
ATOM	3887	N	TYR	A	107	−34.772	37.993	3.236	1.00	91.05	N
ATOM	3888	CA	TYR	A	107	−36.023	37.498	2.641	1.00	90.30	C
ATOM	3889	CB	TYR	A	107	−36.851	38.620	1.995	1.00	90.38	C
ATOM	3890	CG	TYR	A	107	−37.421	39.660	2.931	1.00	90.13	C
ATOM	3891	CD1	TYR	A	107	−38.543	39.389	3.706	1.00	90.22	C
ATOM	3892	CE1	TYR	A	107	−39.084	40.353	4.552	1.00	90.37	C
ATOM	3893	CZ	TYR	A	107	−38.527	41.620	4.595	1.00	90.32	C
ATOM	3894	OH	TYR	A	107	−39.056	42.597	5.402	1.00	90.92	O
ATOM	3895	CE2	TYR	A	107	−37.433	41.920	3.808	1.00	90.06	C
ATOM	3896	CD2	TYR	A	107	−36.888	40.942	2.984	1.00	90.34	C
ATOM	3897	C	TYR	A	107	−35.904	36.341	1.654	1.00	89.73	C
ATOM	3898	O	TYR	A	107	−35.287	36.483	0.584	1.00	89.59	O
ATOM	3899	N	LEU	A	108	−36.553	35.210	2.000	1.00	89.78	N
ATOM	3900	CA	LEU	A	108	−36.596	34.024	1.147	1.00	89.15	C
ATOM	3901	CB	LEU	A	108	−37.005	32.768	1.945	1.00	89.21	C
ATOM	3902	C	LEU	A	108	−37.615	34.303	0.044	1.00	88.57	C
ATOM	3903	O	LEU	A	108	−38.684	34.859	0.306	1.00	88.75	O
ATOM	3904	N	THR	A	109	−37.271	33.969	−1.194	1.00	88.76	N
ATOM	3905	CA	THR	A	109	−38.167	34.182	−2.334	1.00	87.99	C
ATOM	3906	CB	THR	A	109	−37.788	35.446	−3.139	1.00	87.90	C
ATOM	3907	OG1	THR	A	109	−36.479	35.304	−3.706	1.00	88.28	O
ATOM	3908	CG2	THR	A	109	−37.888	36.713	−2.328	1.00	87.68	C
ATOM	3909	C	THR	A	109	−38.200	32.924	−3.208	1.00	87.61	C
ATOM	3910	O	THR	A	109	−37.363	32.029	−3.042	1.00	87.87	O
ATOM	3911	N	LYS	A	110	−39.173	32.852	−4.121	1.00	84.64	N
ATOM	3912	CA	LYS	A	110	−39.291	31.738	−5.026	1.00	83.87	C
ATOM	3913	CB	LYS	A	110	−40.053	30.557	−4.399	1.00	84.18	C
ATOM	3914	CG	LYS	A	110	−39.846	29.262	−5.196	1.00	86.24	C
ATOM	3915	CD	LYS	A	110	−40.683	28.061	−4.705	1.00	88.77	C
ATOM	3916	CE	LYS	A	110	−40.382	26.772	−5.466	1.00	90.05	C
ATOM	3917	NZ	LYS	A	110	−40.771	26.822	−6.914	1.00	91.41	N
ATOM	3918	C	LYS	A	110	−39.923	32.192	−6.318	1.00	82.95	C
ATOM	3919	O	LYS	A	110	−41.078	32.611	−6.311	1.00	83.40	O
ATOM	3920	N	ILE	A	111	−39.167	32.133	−7.434	1.00	78.43	N
ATOM	3921	CA	ILE	A	111	−39.712	32.489	−8.736	1.00	77.08	C
ATOM	3922	CB	ILE	A	111	−38.652	32.868	−9.795	1.00	76.80	C
ATOM	3923	CG1	ILE	A	111	−37.712	33.990	−9.317	1.00	76.57	C
ATOM	3924	CD1	ILE	A	111	−38.290	35.430	−9.093	1.00	77.16	C
ATOM	3925	CG2	ILE	A	111	−39.300	33.187	−11.155	1.00	76.13	C
ATOM	3926	C	ILE	A	111	−40.459	31.232	−9.106	1.00	76.77	C
ATOM	3927	O	ILE	A	111	−39.839	30.180	−9.312	1.00	77.12	O
ATOM	3928	N	LEU	A	112	−41.787	31.319	−9.123	1.00	75.11	N
ATOM	3929	CA	LEU	A	112	−42.641	30.175	−9.424	1.00	74.58	C
ATOM	3930	CB	LEU	A	112	−44.014	30.333	−8.758	1.00	74.58	C
ATOM	3931	CG	LEU	A	112	−44.028	30.542	−7.254	1.00	74.49	C
ATOM	3932	CD1	LEU	A	112	−45.400	30.996	−6.785	1.00	74.48	C
ATOM	3933	CD2	LEU	A	112	−43.653	29.296	−6.541	1.00	74.31	C
ATOM	3934	C	LEU	A	112	−42.795	29.870	−10.921	1.00	74.27	C
ATOM	3935	O	LEU	A	112	−43.036	28.704	−11.278	1.00	74.36	O
ATOM	3936	N	HIS	A	113	−42.668	30.895	−11.787	1.00	70.23	N
ATOM	3937	CA	HIS	A	113	−42.822	30.737	−13.228	1.00	70.12	C
ATOM	3938	CB	HIS	A	113	−44.303	30.468	−13.557	1.00	69.91	C
ATOM	3939	CG	HIS	A	113	−44.636	30.283	−15.001	1.00	69.54	C
ATOM	3940	ND1	HIS	A	113	−44.687	31.363	−15.878	1.00	68.93	N
ATOM	3941	CE1	HIS	A	113	−45.038	30.863	−17.050	1.00	68.78	C
ATOM	3942	NE2	HIS	A	113	−45.249	29.546	−16.975	1.00	69.46	N
ATOM	3943	CD2	HIS	A	113	−45.012	29.165	−15.663	1.00	69.45	C
ATOM	3944	C	HIS	A	113	−42.332	31.997	−13.912	1.00	70.51	C
ATOM	3945	O	HIS	A	113	−42.406	33.083	−13.331	1.00	70.03	O
ATOM	3946	N	VAL	A	114	−41.808	31.843	−15.152	1.00	73.95	N
ATOM	3947	CA	VAL	A	114	−41.298	32.949	−15.962	1.00	74.60	C
ATOM	3948	CB	VAL	A	114	−39.759	32.926	−16.188	1.00	74.41	C
ATOM	3949	CG1	VAL	A	114	−39.344	33.815	−17.351	1.00	74.28	C
ATOM	3950	CG2	VAL	A	114	−39.009	33.334	−14.922	1.00	74.15	C
ATOM	3951	C	VAL	A	114	−42.111	33.067	−17.228	1.00	75.54	C
ATOM	3952	O	VAL	A	114	−42.191	32.135	−18.031	1.00	75.89	O
ATOM	3953	N	PHE	A	115	−42.731	34.227	−17.376	1.00	80.92	N
ATOM	3954	CA	PHE	A	115	−43.586	34.562	−18.486	1.00	81.92	C
ATOM	3955	CB	PHE	A	115	−44.639	35.607	−18.064	1.00	81.57	C
ATOM	3956	CG	PHE	A	115	−45.657	35.047	−17.087	1.00	80.39	C
ATOM	3957	CD1	PHE	A	115	−46.708	34.249	−17.530	1.00	79.09	C
ATOM	3958	CE1	PHE	A	115	−47.632	33.719	−16.628	1.00	78.02	C
ATOM	3959	CZ	PHE	A	115	−47.499	33.970	−15.279	1.00	77.62	C
ATOM	3960	CE2	PHE	A	115	−46.454	34.737	−14.818	1.00	78.07	C
ATOM	3961	CD2	PHE	A	115	−45.540	35.285	−15.722	1.00	78.92	C
ATOM	3962	C	PHE	A	115	−42.843	34.933	−19.751	1.00	83.07	C
ATOM	3963	O	PHE	A	115	−41.997	35.835	−19.758	1.00	83.24	O
ATOM	3964	N	HIS	A	116	−43.160	34.207	−20.824	1.00	90.64	N
ATOM	3965	CA	HIS	A	116	−42.624	34.381	−22.174	1.00	92.40	C
ATOM	3966	CB	HIS	A	116	−41.201	33.785	−22.337	1.00	93.28	C
ATOM	3967	CG	HIS	A	116	−41.077	32.299	−22.140	1.00	97.26	C
ATOM	3968	ND1	HIS	A	116	−41.478	31.674	−20.953	1.00	100.73	N
ATOM	3969	CE1	HIS	A	116	−41.215	30.384	−21.115	1.00	101.46	C
ATOM	3970	NE2	HIS	A	116	−40.660	30.144	−22.310	1.00	102.09	N
ATOM	3971	CD2	HIS	A	116	−40.558	31.361	−22.969	1.00	100.23	C
ATOM	3972	C	HIS	A	116	−43.634	33.829	−23.188	1.00	92.48	C
ATOM	3973	O	HIS	A	116	−44.050	32.662	−23.105	1.00	92.81	O
ATOM	3974	N	GLY	A	117	−44.051	34.691	−24.102	1.00	90.93	N
ATOM	3975	CA	GLY	A	117	−45.027	34.327	−25.113	1.00	90.80	C
ATOM	3976	C	GLY	A	117	−46.240	35.218	−25.019	1.00	91.00	C
ATOM	3977	O	GLY	A	117	−46.557	35.937	−25.982	1.00	91.62	O
ATOM	3978	N	LEU	A	118	−46.927	35.201	−23.852	1.00	87.58	N
ATOM	3979	CA	LEU	A	118	−48.088	36.078	−23.718	1.00	87.01	C
ATOM	3980	CB	LEU	A	118	−49.182	35.470	−22.839	1.00	87.19	C
ATOM	3981	CG	LEU	A	118	−50.491	35.037	−23.510	1.00	87.82	C
ATOM	3982	CD1	LEU	A	118	−51.568	34.849	−22.472	1.00	87.94	C
ATOM	3983	CD2	LEU	A	118	−50.967	36.030	−24.575	1.00	87.14	C
ATOM	3984	C	LEU	A	118	−47.705	37.470	−23.214	1.00	86.38	C
ATOM	3985	O	LEU	A	118	−47.981	38.459	−23.880	1.00	86.36	O
ATOM	3986	N	LEU	A	119	−47.074	37.540	−22.041	1.00	83.97	N
ATOM	3987	CA	LEU	A	119	−46.673	38.791	−21.420	1.00	83.10	C
ATOM	3988	CB	LEU	A	119	−47.568	39.056	−20.183	1.00	83.27	C
ATOM	3989	CG	LEU	A	119	−49.077	39.314	−20.409	1.00	84.36	C
ATOM	3990	CD1	LEU	A	119	−49.871	39.090	−19.137	1.00	84.64	C
ATOM	3991	CD2	LEU	A	119	−49.371	40.720	−21.008	1.00	85.48	C
ATOM	3992	C	LEU	A	119	−45.229	38.688	−20.952	1.00	82.38	C
ATOM	3993	O	LEU	A	119	−44.767	37.580	−20.689	1.00	82.51	O
ATOM	3994	N	PRO	A	120	−44.499	39.813	−20.789	1.00	79.41	N
ATOM	3995	CA	PRO	A	120	−43.127	39.709	−20.275	1.00	78.62	C
ATOM	3996	CB	PRO	A	120	−42.417	40.903	−20.935	1.00	78.79	C
ATOM	3997	CG	PRO	A	120	−43.545	41.870	−21.375	1.00	79.03	C
ATOM	3998	CD	PRO	A	120	−44.864	41.224	−21.052	1.00	79.38	C
ATOM	3999	C	PRO	A	120	−43.121	39.827	−18.745	1.00	77.86	C
ATOM	4000	O	PRO	A	120	−43.469	40.869	−18.194	1.00	77.99	O
ATOM	4001	N	GLY	A	121	−42.747	38.776	−18.051	1.00	74.71	N
ATOM	4002	CA	GLY	A	121	−42.714	38.879	−16.603	1.00	73.64	C
ATOM	4003	C	GLY	A	121	−42.383	37.594	−15.901	1.00	73.19	C
ATOM	4004	O	GLY	A	121	−41.774	36.705	−16.493	1.00	73.07	O
ATOM	4005	N	PHE	A	122	−42.783	37.497	−14.629	1.00	72.55	N
ATOM	4006	CA	PHE	A	122	−42.575	36.315	−13.794	1.00	72.16	C
ATOM	4007	CB	PHE	A	122	−41.104	36.163	−13.373	1.00	71.78	C
ATOM	4008	CG	PHE	A	122	−40.538	37.359	−12.656	1.00	70.60	C
ATOM	4009	CD1	PHE	A	122	−39.948	38.400	−13.367	1.00	69.65	C
ATOM	4010	CE1	PHE	A	122	−39.431	39.512	−12.706	1.00	69.74	C
ATOM	4011	CZ	PHE	A	122	−39.504	39.590	−11.329	1.00	69.97	C
ATOM	4012	CE2	PHE	A	122	−40.080	38.561	−10.605	1.00	69.86	C
ATOM	4013	CD2	PHE	A	122	−40.589	37.446	−11.268	1.00	70.03	C
ATOM	4014	C	PHE	A	122	−43.485	36.339	−12.575	1.00	72.41	C
ATOM	4015	O	PHE	A	122	−43.845	37.417	−12.079	1.00	72.62	O
ATOM	4016	N	LEU	A	123	−43.850	35.146	−12.102	1.00	71.35	N
ATOM	4017	CA	LEU	A	123	−44.689	34.938	−10.928	1.00	71.32	C
ATOM	4018	CB	LEU	A	123	−45.588	33.706	−11.156	1.00	71.45	C
ATOM	4019	CG	LEU	A	123	−46.407	33.184	−9.985	1.00	71.79	C
ATOM	4020	CD1	LEU	A	123	−47.567	34.116	−9.673	1.00	72.22	C
ATOM	4021	CD2	LEU	A	123	−46.943	31.817	−10.296	1.00	71.36	C
ATOM	4022	C	LEU	A	123	−43.749	34.746	−9.743	1.00	71.15	C
ATOM	4023	O	LEU	A	123	−42.853	33.910	−9.801	1.00	71.24	O
ATOM	4024	N	VAL	A	124	−43.921	35.526	−8.684	1.00	71.84	N
ATOM	4025	CA	VAL	A	124	−43.021	35.422	−7.534	1.00	71.78	C
ATOM	4026	CB	VAL	A	124	−41.969	36.576	−7.520	1.00	71.84	C
ATOM	4027	CG1	VAL	A	124	−42.624	37.963	−7.403	1.00	71.15	C
ATOM	4028	CG2	VAL	A	124	−40.911	36.361	−6.441	1.00	71.27	C
ATOM	4029	C	VAL	A	124	−43.701	35.243	−6.192	1.00	71.82	C
ATOM	4030	O	VAL	A	124	−44.545	36.053	−5.816	1.00	71.98	O
ATOM	4031	N	LYS	A	125	−43.316	34.205	−5.462	1.00	73.15	N
ATOM	4032	CA	LYS	A	125	−43.822	33.981	−4.117	1.00	73.52	C
ATOM	4033	CB	LYS	A	125	−43.860	32.480	−3.785	1.00	73.77	C
ATOM	4034	CG	LYS	A	125	−44.453	32.158	−2.419	1.00	75.03	C
ATOM	4035	CD	LYS	A	125	−44.431	30.659	−2.133	1.00	77.65	C
ATOM	4036	CE	LYS	A	125	−45.562	30.252	−1.220	1.00	78.44	C
ATOM	4037	NZ	LYS	A	125	−46.906	30.461	−1.868	1.00	80.43	N
ATOM	4038	C	LYS	A	125	−42.824	34.738	−3.213	1.00	73.44	C
ATOM	4039	O	LYS	A	125	−41.657	34.367	−3.168	1.00	73.50	O
ATOM	4040	N	MET	A	126	−43.263	35.815	−2.547	1.00	74.18	N
ATOM	4041	CA	MET	A	126	−42.411	36.649	−1.681	1.00	74.20	C
ATOM	4042	CB	MET	A	126	−41.531	37.602	−2.516	1.00	74.36	C
ATOM	4043	CG	MET	A	126	−42.316	38.391	−3.520	1.00	75.18	C
ATOM	4044	SD	MET	A	126	−41.581	39.962	−3.943	1.00	78.44	S
ATOM	4045	CE	MET	A	126	−42.995	41.032	−3.741	1.00	77.19	C
ATOM	4046	C	MET	A	126	−43.241	37.473	−0.711	1.00	74.00	C
ATOM	4047	O	MET	A	126	−44.452	37.577	−0.868	1.00	74.18	O
ATOM	4048	N	SER	A	127	−42.586	38.085	0.273	1.00	74.27	N
ATOM	4049	CA	SER	A	127	−43.271	38.900	1.260	1.00	74.17	C
ATOM	4050	CB	SER	A	127	−42.361	39.142	2.454	1.00	74.01	C
ATOM	4051	OG	SER	A	127	−42.917	40.117	3.314	1.00	73.62	O
ATOM	4052	C	SER	A	127	−43.756	40.228	0.663	1.00	74.70	C
ATOM	4053	O	SER	A	127	−43.087	40.813	−0.197	1.00	75.08	O
ATOM	4054	N	GLY	A	128	−44.916	40.688	1.132	1.00	76.07	N
ATOM	4055	CA	GLY	A	128	−45.507	41.948	0.709	1.00	75.96	C
ATOM	4056	C	GLY	A	128	−44.600	43.117	1.025	1.00	76.12	C
ATOM	4057	O	GLY	A	128	−44.691	44.161	0.382	1.00	76.50	O
ATOM	4058	N	ASP	A	129	−43.679	42.932	1.994	1.00	75.99	N
ATOM	4059	CA	ASP	A	129	−42.690	43.931	2.407	1.00	75.71	C
ATOM	4060	CB	ASP	A	129	−41.849	43.373	3.561	1.00	75.74	C
ATOM	4061	CG	ASP	A	129	−42.588	43.212	4.879	1.00	76.66	C
ATOM	4062	OD1	ASP	A	129	−43.780	43.637	4.959	1.00	77.70	O
ATOM	4063	OD2	ASP	A	129	−41.978	42.661	5.843	1.00	77.23	O
ATOM	4064	C	ASP	A	129	−41.756	44.310	1.262	1.00	75.35	C
ATOM	4065	O	ASP	A	129	−41.245	45.427	1.225	1.00	75.27	O
ATOM	4066	N	LEU	A	130	−41.532	43.372	0.334	1.00	72.31	N
ATOM	4067	CA	LEU	A	130	−40.650	43.577	−0.796	1.00	72.16	C
ATOM	4068	CB	LEU	A	130	−40.086	42.234	−1.248	1.00	72.44	C
ATOM	4069	CG	LEU	A	130	−39.214	41.518	−0.227	1.00	73.24	C
ATOM	4070	CD1	LEU	A	130	−39.243	39.998	−0.443	1.00	74.34	C
ATOM	4071	CD2	LEU	A	130	−37.794	42.090	−0.214	1.00	73.18	C
ATOM	4072	C	LEU	A	130	−41.283	44.327	−1.957	1.00	71.98	C
ATOM	4073	O	LEU	A	130	−40.645	44.495	−2.997	1.00	71.98	O
ATOM	4074	N	LEU	A	131	−42.515	44.805	−1.782	1.00	72.28	N
ATOM	4075	CA	LEU	A	131	−43.224	45.519	−2.841	1.00	72.36	C
ATOM	4076	CB	LEU	A	131	−44.713	45.607	−2.556	1.00	72.27	C
ATOM	4077	CG	LEU	A	131	−45.490	44.354	−2.851	1.00	72.00	C
ATOM	4078	CD1	LEU	A	131	−46.830	44.400	−2.152	1.00	72.02	C
ATOM	4079	CD2	LEU	A	131	−45.624	44.126	−4.382	1.00	71.72	C
ATOM	4080	C	LEU	A	131	−42.669	46.861	−3.291	1.00	72.59	C
ATOM	4081	O	LEU	A	131	−42.585	47.090	−4.495	1.00	72.42	O
ATOM	4082	N	GLU	A	132	−42.300	47.743	−2.345	1.00	74.85	N
ATOM	4083	CA	GLU	A	132	−41.749	49.072	−2.623	1.00	75.47	C
ATOM	4084	CB	GLU	A	132	−41.481	49.822	−1.313	1.00	75.52	C
ATOM	4085	CG	GLU	A	132	−40.977	51.238	−1.542	1.00	75.63	C
ATOM	4086	CD	GLU	A	132	−40.813	52.067	−0.286	1.00	76.52	C
ATOM	4087	OE1	GLU	A	132	−40.124	51.581	0.643	1.00	76.99	O
ATOM	4088	OE2	GLU	A	132	−41.367	53.195	−0.226	1.00	76.49	O
ATOM	4089	C	GLU	A	132	−40.461	48.935	−3.416	1.00	75.73	C
ATOM	4090	O	GLU	A	132	−40.226	49.689	−4.372	1.00	75.85	O
ATOM	4091	N	LEU	A	133	−39.651	47.942	−3.003	1.00	75.20	N
ATOM	4092	CA	LEU	A	133	−38.358	47.552	−3.558	1.00	75.36	C
ATOM	4093	CB	LEU	A	133	−37.824	46.454	−2.620	1.00	75.46	C
ATOM	4094	CG	LEU	A	133	−36.419	45.899	−2.779	1.00	75.90	C
ATOM	4095	CD1	LEU	A	133	−36.028	45.162	−1.510	1.00	76.47	C
ATOM	4096	CD2	LEU	A	133	−36.344	44.882	−3.913	1.00	76.30	C
ATOM	4097	C	LEU	A	133	−38.510	47.025	−5.002	1.00	75.29	C
ATOM	4098	O	LEU	A	133	−37.793	47.484	−5.891	1.00	75.23	O
ATOM	4099	N	ALA	A	134	−39.425	46.041	−5.205	1.00	73.18	N
ATOM	4100	CA	ALA	A	134	−39.725	45.403	−6.480	1.00	73.41	C
ATOM	4101	CB	ALA	A	134	−40.666	44.241	−6.271	1.00	73.33	C
ATOM	4102	C	ALA	A	134	−40.315	46.385	−7.497	1.00	73.84	C
ATOM	4103	O	ALA	A	134	−39.999	46.301	−8.690	1.00	73.72	O
ATOM	4104	N	LEU	A	135	−41.153	47.329	−7.043	1.00	74.72	N
ATOM	4105	CA	LEU	A	135	−41.733	48.309	−7.956	1.00	75.35	C
ATOM	4106	CB	LEU	A	135	−42.880	49.050	−7.283	1.00	75.03	C
ATOM	4107	CG	LEU	A	135	−44.174	48.289	−7.229	1.00	74.09	C
ATOM	4108	CD1	LEU	A	135	−44.935	48.673	−6.047	1.00	74.22	C
ATOM	4109	CD2	LEU	A	135	−45.020	48.559	−8.423	1.00	73.06	C
ATOM	4110	C	LEU	A	135	−40.663	49.285	−8.486	1.00	76.31	C
ATOM	4111	O	LEU	A	135	−40.848	49.909	−9.546	1.00	76.40	O
ATOM	4112	N	LYS	A	136	−39.530	49.390	−7.735	1.00	78.69	N
ATOM	4113	CA	LYS	A	136	−38.383	50.232	−8.049	1.00	79.02	C
ATOM	4114	CB	LYS	A	136	−37.654	50.652	−6.763	1.00	78.89	C
ATOM	4115	CG	LYS	A	136	−38.294	51.859	−6.084	1.00	79.70	C
ATOM	4116	CD	LYS	A	136	−37.604	52.235	−4.755	1.00	80.63	C
ATOM	4117	CE	LYS	A	136	−38.268	53.405	−4.035	1.00	81.81	C
ATOM	4118	NZ	LYS	A	136	−37.773	53.576	−2.632	1.00	81.67	N
ATOM	4119	C	LYS	A	136	−37.440	49.570	−9.071	1.00	79.35	C
ATOM	4120	O	LYS	A	136	−36.595	50.260	−9.640	1.00	79.86	O
ATOM	4121	N	LEU	A	137	−37.598	48.261	−9.335	1.00	78.98	N
ATOM	4122	CA	LEU	A	137	−36.766	47.543	−10.309	1.00	79.57	C
ATOM	4123	CB	LEU	A	137	−36.973	46.013	−10.249	1.00	79.67	C
ATOM	4124	CG	LEU	A	137	−36.719	45.300	−8.926	1.00	80.16	C
ATOM	4125	CD1	LEU	A	137	−37.285	43.908	−8.960	1.00	79.93	C
ATOM	4126	CD2	LEU	A	137	−35.244	45.291	−8.560	1.00	80.74	C
ATOM	4127	C	LEU	A	137	−36.988	48.020	−11.752	1.00	79.92	C
ATOM	4128	O	LEU	A	137	−38.106	48.396	−12.132	1.00	79.79	O
ATOM	4129	N	PRO	A	138	−35.927	47.997	−12.583	1.00	85.61	N
ATOM	4130	CA	PRO	A	138	−36.094	48.415	−13.981	1.00	85.93	C
ATOM	4131	CB	PRO	A	138	−34.656	48.580	−14.466	1.00	85.97	C
ATOM	4132	CG	PRO	A	138	−33.896	47.564	−13.677	1.00	86.02	C
ATOM	4133	CD	PRO	A	138	−34.531	47.583	−12.315	1.00	85.82	C
ATOM	4134	C	PRO	A	138	−36.835	47.367	−14.807	1.00	85.94	C
ATOM	4135	O	PRO	A	138	−36.753	46.152	−14.541	1.00	85.89	O
ATOM	4136	N	HIS	A	139	−37.530	47.868	−15.838	1.00	87.14	N
ATOM	4137	CA	HIS	A	139	−38.343	47.136	−16.809	1.00	87.20	C
ATOM	4138	CB	HIS	A	139	−37.661	45.869	−17.395	1.00	87.77	C
ATOM	4139	CG	HIS	A	139	−36.221	46.038	−17.807	1.00	90.16	C
ATOM	4140	ND1	HIS	A	139	−35.740	47.238	−18.334	1.00	91.35	N
ATOM	4141	CE1	HIS	A	139	−34.455	47.029	−18.573	1.00	92.08	C
ATOM	4142	NE2	HIS	A	139	−34.091	45.780	−18.259	1.00	92.76	N
ATOM	4143	CD2	HIS	A	139	−35.206	45.140	−17.768	1.00	91.72	C
ATOM	4144	C	HIS	A	139	−39.743	46.848	−16.295	1.00	86.38	C
ATOM	4145	O	HIS	A	139	−40.634	46.652	−17.113	1.00	86.53	O
ATOM	4146	N	VAL	A	140	−39.952	46.860	−14.964	1.00	82.97	N
ATOM	4147	CA	VAL	A	140	−41.242	46.617	−14.312	1.00	81.89	C
ATOM	4148	CB	VAL	A	140	−41.074	46.509	−12.780	1.00	81.92	C
ATOM	4149	CG1	VAL	A	140	−42.392	46.161	−12.109	1.00	81.92	C
ATOM	4150	CG2	VAL	A	140	−39.993	45.497	−12.411	1.00	81.73	C
ATOM	4151	C	VAL	A	140	−42.304	47.673	−14.712	1.00	81.26	C
ATOM	4152	O	VAL	A	140	−42.130	48.869	−14.454	1.00	81.13	O
ATOM	4153	N	ASP	A	141	−43.395	47.212	−15.357	1.00	80.40	N
ATOM	4154	CA	ASP	A	141	−44.498	48.058	−15.821	1.00	79.27	C
ATOM	4155	CB	ASP	A	141	−45.162	47.427	−17.057	1.00	79.20	C
ATOM	4156	CG	ASP	A	141	−46.093	48.336	−17.844	1.00	79.58	C
ATOM	4157	OD1	ASP	A	141	−46.144	49.555	−17.541	1.00	80.20	O
ATOM	4158	OD2	ASP	A	141	−46.766	47.834	−18.766	1.00	81.10	O
ATOM	4159	C	ASP	A	141	−45.503	48.266	−14.682	1.00	78.54	C
ATOM	4160	O	ASP	A	141	−45.864	49.411	−14.374	1.00	78.85	O
ATOM	4161	N	TYR	A	142	−45.948	47.135	−14.067	1.00	74.15	N
ATOM	4162	CA	TYR	A	142	−46.852	47.015	−12.924	1.00	72.68	C
ATOM	4163	CB	TYR	A	142	−48.324	47.248	−13.287	1.00	72.37	C
ATOM	4164	CG	TYR	A	142	−48.906	46.336	−14.344	1.00	71.40	C
ATOM	4165	CD1	TYR	A	142	−48.805	46.654	−15.697	1.00	70.30	C
ATOM	4166	CE1	TYR	A	142	−49.380	45.843	−16.681	1.00	70.62	C
ATOM	4167	CZ	TYR	A	142	−50.076	44.695	−16.316	1.00	70.61	C
ATOM	4168	OH	TYR	A	142	−50.623	43.913	−17.321	1.00	68.55	O
ATOM	4169	CE2	TYR	A	142	−50.212	44.369	−14.967	1.00	70.46	C
ATOM	4170	CD2	TYR	A	142	−49.636	45.196	−13.991	1.00	70.99	C
ATOM	4171	C	TYR	A	142	−46.641	45.671	−12.245	1.00	72.14	C
ATOM	4172	O	TYR	A	142	−46.001	44.789	−12.813	1.00	71.87	O
ATOM	4173	N	ILE	A	143	−47.138	45.537	−11.013	1.00	69.96	N
ATOM	4174	CA	ILE	A	143	−47.067	44.325	−10.193	1.00	69.49	C
ATOM	4175	CB	ILE	A	143	−46.063	44.457	−9.008	1.00	69.68	C
ATOM	4176	CG1	ILE	A	143	−44.666	44.972	−9.483	1.00	69.49	C
ATOM	4177	CD1	ILE	A	143	−43.375	44.443	−8.782	1.00	68.82	C
ATOM	4178	CG2	ILE	A	143	−46.013	43.161	−8.154	1.00	68.95	C
ATOM	4179	C	ILE	A	143	−48.482	44.029	−9.699	1.00	69.45	C
ATOM	4180	O	ILE	A	143	−49.113	44.897	−9.098	1.00	69.21	O
ATOM	4181	N	GLU	A	144	−48.979	42.807	−9.956	1.00	71.72	N
ATOM	4182	CA	GLU	A	144	−50.317	42.405	−9.528	1.00	71.53	C
ATOM	4183	CB	GLU	A	144	−51.202	41.960	−10.708	1.00	71.48	C
ATOM	4184	CG	GLU	A	144	−52.658	42.320	−10.459	1.00	73.34	C
ATOM	4185	CD	GLU	A	144	−53.734	41.708	−11.339	1.00	75.76	C
ATOM	4186	OE1	GLU	A	144	−53.849	42.145	−12.509	1.00	75.42	O
ATOM	4187	OE2	GLU	A	144	−54.475	40.812	−10.852	1.00	76.83	O
ATOM	4188	C	GLU	A	144	−50.307	41.347	−8.449	1.00	70.91	C
ATOM	4189	O	GLU	A	144	−49.687	40.305	−8.615	1.00	71.23	O
ATOM	4190	N	GLU	A	145	−50.998	41.610	−7.348	1.00	69.74	N
ATOM	4191	CA	GLU	A	145	−51.142	40.646	−6.271	1.00	69.59	C
ATOM	4192	CB	GLU	A	145	−51.809	41.320	−5.059	1.00	69.65	C
ATOM	4193	CG	GLU	A	145	−52.061	40.413	−3.866	1.00	71.57	C
ATOM	4194	CD	GLU	A	145	−52.590	41.153	−2.648	1.00	74.80	C
ATOM	4195	OE1	GLU	A	145	−53.829	41.212	−2.480	1.00	77.48	O
ATOM	4196	OE2	GLU	A	145	−51.765	41.678	−1.863	1.00	74.22	O
ATOM	4197	C	GLU	A	145	−52.051	39.535	−6.823	1.00	69.32	C
ATOM	4198	O	GLU	A	145	−53.051	39.824	−7.485	1.00	69.54	O
ATOM	4199	N	ASP	A	146	−51.707	38.277	−6.574	1.00	69.08	N
ATOM	4200	CA	ASP	A	146	−52.530	37.166	−7.028	1.00	68.70	C
ATOM	4201	CB	ASP	A	146	−51.882	35.831	−6.636	1.00	69.08	C
ATOM	4202	CG	ASP	A	146	−52.124	34.665	−7.594	1.00	70.22	C
ATOM	4203	OD1	ASP	A	146	−52.938	34.827	−8.551	1.00	70.06	O
ATOM	4204	OD2	ASP	A	146	−51.496	33.578	−7.388	1.00	71.69	O
ATOM	4205	C	ASP	A	146	−53.926	37.280	−6.397	1.00	68.15	C
ATOM	4206	O	ASP	A	146	−54.077	37.892	−5.329	1.00	68.20	O
ATOM	4207	N	SER	A	147	−54.946	36.735	−7.080	1.00	66.95	N
ATOM	4208	CA	SER	A	147	−56.331	36.746	−6.607	1.00	66.13	C
ATOM	4209	CB	SER	A	147	−57.129	37.895	−7.208	1.00	65.93	C
ATOM	4210	OG	SER	A	147	−56.293	38.909	−7.736	1.00	66.81	O
ATOM	4211	C	SER	A	147	−56.976	35.441	−6.993	1.00	65.51	C
ATOM	4212	O	SER	A	147	−56.466	34.728	−7.864	1.00	65.59	O
ATOM	4213	N	SER	A	148	−58.094	35.123	−6.349	1.00	62.34	N
ATOM	4214	CA	SER	A	148	−58.833	33.915	−6.614	1.00	61.23	C
ATOM	4215	CB	SER	A	148	−59.607	33.509	−5.369	1.00	61.20	C
ATOM	4216	OG	SER	A	148	−58.747	32.994	−4.365	1.00	61.41	O
ATOM	4217	C	SER	A	148	−59.803	34.109	−7.767	1.00	60.82	C
ATOM	4218	O	SER	A	148	−60.365	35.198	−7.938	1.00	61.26	O
ATOM	4219	N	VAL	A	149	−59.990	33.049	−8.563	1.00	58.81	N
ATOM	4220	CA	VAL	A	149	−60.944	32.967	−9.672	1.00	58.28	C
ATOM	4221	CB	VAL	A	149	−60.356	32.896	−11.110	1.00	58.18	C
ATOM	4222	CG1	VAL	A	149	−59.501	34.111	−11.425	1.00	57.52	C
ATOM	4223	CG2	VAL	A	149	−59.594	31.603	−11.364	1.00	58.33	C
ATOM	4224	C	VAL	A	149	−61.855	31.779	−9.329	1.00	58.22	C
ATOM	4225	O	VAL	A	149	−61.413	30.884	−8.601	1.00	58.28	O
ATOM	4226	N	PHE	A	150	−63.110	31.768	−9.804	1.00	57.53	N
ATOM	4227	CA	PHE	A	150	−64.024	30.697	−9.449	1.00	57.21	C
ATOM	4228	CB	PHE	A	150	−64.996	31.178	−8.378	1.00	56.45	C
ATOM	4229	CG	PHE	A	150	−64.355	31.762	−7.158	1.00	55.56	C
ATOM	4230	CD1	PHE	A	150	−63.975	30.952	−6.100	1.00	54.34	C
ATOM	4231	CE1	PHE	A	150	−63.397	31.504	−4.956	1.00	54.41	C
ATOM	4232	CZ	PHE	A	150	−63.176	32.864	−4.878	1.00	54.23	C
ATOM	4233	CE2	PHE	A	150	−63.537	33.677	−5.921	1.00	54.50	C
ATOM	4234	CD2	PHE	A	150	−64.146	33.132	−7.053	1.00	55.55	C
ATOM	4235	C	PHE	A	150	−64.878	30.262	−10.570	1.00	57.91	C
ATOM	4236	O	PHE	A	150	−65.321	31.089	−11.351	1.00	58.22	O
ATOM	4237	N	ALA	A	151	−65.213	28.966	−10.586	1.00	59.21	N
ATOM	4238	CA	ALA	A	151	−66.127	28.355	−11.532	1.00	59.60	C
ATOM	4239	CB	ALA	A	151	−66.339	26.901	−11.148	1.00	59.54	C
ATOM	4240	C	ALA	A	151	−67.445	29.108	−11.409	1.00	60.14	C
ATOM	4241	O	ALA	A	151	−67.848	29.444	−10.283	1.00	60.22	O
ATOM	4242	N	GLN	A	152	−68.099	29.394	−12.558	1.00	61.34	N
ATOM	4243	CA	GLN	A	152	−69.375	30.113	−12.638	1.00	61.85	C
ATOM	4244	CB	GLN	A	152	−69.204	31.376	−13.490	1.00	61.59	C
ATOM	4245	CG	GLN	A	152	−68.267	32.380	−12.889	1.00	61.62	C
ATOM	4246	CD	GLN	A	152	−68.775	32.876	−11.557	1.00	62.64	C
ATOM	4247	OE1	GLN	A	152	−69.726	33.667	−11.461	1.00	63.19	O
ATOM	4248	NE2	GLN	A	152	−68.163	32.412	−10.476	1.00	64.63	N
ATOM	4249	C	GLN	A	152	−70.545	29.222	−13.155	1.00	62.70	C
ATOM	4250	O	GLN	A	152	−71.461	29.742	−13.838	1.00	63.04	O
ATOM	4251	OXT	GLN	A	152	−70.552	27.993	−12.901	1.00	90.28	O
TER	4252		GLN	A	152
ATOM	4253	N	GLU	H	1	−66.128	−17.371	−29.550	1.00	84.16	N
ATOM	4254	CA	GLU	H	1	−67.436	−17.005	−29.032	1.00	84.28	C
ATOM	4255	CB	GLU	H	1	−68.491	−18.106	−29.309	1.00	84.57	C
ATOM	4256	CG	GLU	H	1	−68.364	−19.339	−28.418	1.00	86.38	C
ATOM	4257	CD	GLU	H	1	−69.088	−20.603	−28.841	1.00	88.58	C
ATOM	4258	OE1	GLU	H	1	−68.431	−21.670	−28.871	1.00	88.46	O
ATOM	4259	OE2	GLU	H	1	−70.308	−20.532	−29.125	1.00	89.92	O
ATOM	4260	C	GLU	H	1	−67.333	−16.729	−27.549	1.00	83.78	C
ATOM	4261	O	GLU	H	1	−66.461	−17.307	−26.870	1.00	83.95	O
ATOM	4262	N	VAL	H	2	−68.228	−15.850	−27.047	1.00	78.94	N
ATOM	4263	CA	VAL	H	2	−68.256	−15.530	−25.632	1.00	78.30	C
ATOM	4264	CB	VAL	H	2	−68.442	−14.028	−25.340	1.00	78.19	C
ATOM	4265	CG1	VAL	H	2	−68.813	−13.772	−23.882	1.00	78.05	C
ATOM	4266	CG2	VAL	H	2	−67.170	−13.270	−25.684	1.00	77.93	C
ATOM	4267	C	VAL	H	2	−69.246	−16.451	−24.938	1.00	78.07	C
ATOM	4268	O	VAL	H	2	−70.267	−16.801	−25.524	1.00	78.24	O
ATOM	4269	N	GLN	H	3	−68.914	−16.889	−23.708	1.00	77.82	N
ATOM	4270	CA	GLN	H	3	−69.763	−17.773	−22.925	1.00	77.65	C
ATOM	4271	CB	GLN	H	3	−69.436	−19.213	−23.262	1.00	78.12	C
ATOM	4272	CG	GLN	H	3	−70.619	−19.947	−23.853	1.00	80.90	C
ATOM	4273	CD	GLN	H	3	−70.144	−20.979	−24.833	1.00	84.72	C
ATOM	4274	OE1	GLN	H	3	−70.363	−20.839	−26.047	1.00	86.45	O
ATOM	4275	NE2	GLN	H	3	−69.473	−22.032	−24.330	1.00	85.45	N
ATOM	4276	C	GLN	H	3	−69.640	−17.567	−21.436	1.00	76.67	C
ATOM	4277	O	GLN	H	3	−68.525	−17.477	−20.924	1.00	76.75	O
ATOM	4278	N	LEU	H	4	−70.787	−17.506	−20.739	1.00	72.16	N
ATOM	4279	CA	LEU	H	4	−70.837	−17.368	−19.280	1.00	71.64	C
ATOM	4280	CB	LEU	H	4	−71.524	−16.069	−18.818	1.00	71.33	C
ATOM	4281	CG	LEU	H	4	−71.195	−14.757	−19.523	1.00	70.60	C
ATOM	4282	CD1	LEU	H	4	−71.913	−13.625	−18.864	1.00	70.01	C
ATOM	4283	CD2	LEU	H	4	−69.718	−14.463	−19.528	1.00	69.61	C
ATOM	4284	C	LEU	H	4	−71.535	−18.618	−18.675	1.00	71.52	C
ATOM	4285	O	LEU	H	4	−72.709	−18.888	−18.974	1.00	71.75	O
ATOM	4286	N	LEU	H	5	−70.803	−19.384	−17.846	1.00	69.57	N
ATOM	4287	CA	LEU	H	5	−71.323	−20.591	−17.235	1.00	69.42	C
ATOM	4288	CB	LEU	H	5	−70.438	−21.787	−17.545	1.00	69.66	C
ATOM	4289	CG	LEU	H	5	−70.935	−22.587	−18.733	1.00	70.41	C
ATOM	4290	CD1	LEU	H	5	−69.780	−22.973	−19.690	1.00	70.09	C
ATOM	4291	CD2	LEU	H	5	−71.834	−23.750	−18.291	1.00	70.19	C
ATOM	4292	C	LEU	H	5	−71.668	−20.530	−15.770	1.00	69.40	C
ATOM	4293	O	LEU	H	5	−70.805	−20.593	−14.907	1.00	69.27	O
ATOM	4294	N	GLU	H	6	−72.943	−20.461	−15.482	1.00	71.71	N
ATOM	4295	CA	GLU	H	6	−73.380	−20.435	−14.106	1.00	72.24	C
ATOM	4296	CB	GLU	H	6	−74.742	−19.783	−14.004	1.00	72.34	C
ATOM	4297	CG	GLU	H	6	−74.678	−18.300	−14.254	1.00	74.24	C
ATOM	4298	CD	GLU	H	6	−75.966	−17.699	−14.760	1.00	76.78	C
ATOM	4299	OE1	GLU	H	6	−76.028	−16.458	−14.856	1.00	78.16	O
ATOM	4300	OE2	GLU	H	6	−76.912	−18.459	−15.059	1.00	78.55	O
ATOM	4301	C	GLU	H	6	−73.445	−21.839	−13.519	1.00	72.29	C
ATOM	4302	O	GLU	H	6	−73.777	−22.802	−14.225	1.00	72.74	O
ATOM	4303	N	SER	H	7	−73.152	−21.946	−12.218	1.00	69.48	N
ATOM	4304	CA	SER	H	7	−73.205	−23.184	−11.462	1.00	69.09	C
ATOM	4305	CB	SER	H	7	−71.933	−23.982	−11.661	1.00	68.95	C
ATOM	4306	OG	SER	H	7	−70.817	−23.156	−11.416	1.00	69.86	O
ATOM	4307	C	SER	H	7	−73.429	−22.835	−10.005	1.00	68.98	C
ATOM	4308	O	SER	H	7	−73.028	−21.760	−9.569	1.00	69.18	O
ATOM	4309	N	GLY	H	8	−74.130	−23.692	−9.279	1.00	69.93	N
ATOM	4310	CA	GLY	H	8	−74.400	−23.446	−7.871	1.00	69.86	C
ATOM	4311	C	GLY	H	8	−75.861	−23.338	−7.508	1.00	69.99	C
ATOM	4312	O	GLY	H	8	−76.206	−23.020	−6.357	1.00	70.57	O
ATOM	4313	N	GLY	H	9	−76.723	−23.574	−8.483	1.00	70.65	N
ATOM	4314	CA	GLY	H	9	−78.159	−23.495	−8.255	1.00	70.59	C
ATOM	4315	C	GLY	H	9	−78.664	−24.743	−7.563	1.00	70.37	C
ATOM	4316	O	GLY	H	9	−78.070	−25.815	−7.714	1.00	70.41	O
ATOM	4317	N	GLY	H	10	−79.748	−24.604	−6.812	1.00	67.78	N
ATOM	4318	CA	GLY	H	10	−80.338	−25.717	−6.099	1.00	67.44	C
ATOM	4319	C	GLY	H	10	−81.143	−25.309	−4.900	1.00	67.59	C
ATOM	4320	O	GLY	H	10	−81.720	−24.214	−4.870	1.00	67.31	O
ATOM	4321	N	LEU	H	11	−81.196	−26.202	−3.904	1.00	69.83	N
ATOM	4322	CA	LEU	H	11	−81.963	−25.902	−2.713	1.00	70.67	C
ATOM	4323	CB	LEU	H	11	−82.755	−27.099	−2.219	1.00	70.63	C
ATOM	4324	CG	LEU	H	11	−84.051	−27.363	−2.918	1.00	70.82	C
ATOM	4325	CD1	LEU	H	11	−84.469	−28.777	−2.695	1.00	71.32	C
ATOM	4326	CD2	LEU	H	11	−85.144	−26.348	−2.511	1.00	71.57	C
ATOM	4327	C	LEU	H	11	−81.134	−25.361	−1.602	1.00	71.27	C
ATOM	4328	O	LEU	H	11	−80.059	−25.887	−1.300	1.00	71.33	O
ATOM	4329	N	VAL	H	12	−81.636	−24.293	−0.985	1.00	77.04	N
ATOM	4330	CA	VAL	H	12	−80.974	−23.659	0.152	1.00	77.83	C
ATOM	4331	CB	VAL	H	12	−80.394	−22.247	−0.154	1.00	77.74	C
ATOM	4332	CG1	VAL	H	12	−79.444	−21.815	0.949	1.00	77.50	C
ATOM	4333	CG2	VAL	H	12	−79.676	−22.202	−1.502	1.00	76.57	C
ATOM	4334	C	VAL	H	12	−82.020	−23.624	1.262	1.00	78.58	C
ATOM	4335	O	VAL	H	12	−83.201	−23.385	0.982	1.00	78.68	O
ATOM	4336	N	GLN	H	13	−81.603	−23.892	2.508	1.00	82.84	N
ATOM	4337	CA	GLN	H	13	−82.524	−23.873	3.644	1.00	83.70	C
ATOM	4338	CB	GLN	H	13	−81.931	−24.645	4.835	1.00	83.95	C
ATOM	4339	CG	GLN	H	13	−81.539	−26.106	4.538	1.00	86.04	C
ATOM	4340	CD	GLN	H	13	−82.707	−26.981	4.115	1.00	88.73	C
ATOM	4341	OE1	GLN	H	13	−82.682	−27.649	3.048	1.00	89.35	O
ATOM	4342	NE2	GLN	H	13	−83.766	−26.985	4.935	1.00	89.33	N
ATOM	4343	C	GLN	H	13	−82.738	−22.430	4.052	1.00	83.88	C
ATOM	4344	O	GLN	H	13	−81.774	−21.673	3.978	1.00	83.93	O
ATOM	4345	N	PRO	H	14	−83.946	−21.995	4.478	1.00	84.30	N
ATOM	4346	CA	PRO	H	14	−84.102	−20.599	4.921	1.00	84.50	C
ATOM	4347	CB	PRO	H	14	−85.560	−20.519	5.377	1.00	84.18	C
ATOM	4348	CG	PRO	H	14	−85.967	−21.904	5.600	1.00	84.55	C
ATOM	4349	CD	PRO	H	14	−85.207	−22.732	4.625	1.00	84.42	C
ATOM	4350	C	PRO	H	14	−83.101	−20.312	6.049	1.00	84.71	C
ATOM	4351	O	PRO	H	14	−82.966	−21.105	6.995	1.00	85.21	O
ATOM	4352	N	GLY	H	15	−82.351	−19.227	5.880	1.00	84.98	N
ATOM	4353	CA	GLY	H	15	−81.285	−18.815	6.782	1.00	84.47	C
ATOM	4354	C	GLY	H	15	−79.928	−19.168	6.199	1.00	84.16	C
ATOM	4355	O	GLY	H	15	−78.915	−18.539	6.533	1.00	84.38	O
ATOM	4356	N	GLY	H	16	−79.916	−20.164	5.311	1.00	82.42	N
ATOM	4357	CA	GLY	H	16	−78.720	−20.637	4.622	1.00	82.29	C
ATOM	4358	C	GLY	H	16	−78.183	−19.668	3.589	1.00	82.05	C
ATOM	4359	O	GLY	H	16	−78.700	−18.556	3.439	1.00	82.21	O
ATOM	4360	N	SER	H	17	−77.142	−20.072	2.863	1.00	80.66	N
ATOM	4361	CA	SER	H	17	−76.571	−19.159	1.888	1.00	80.48	C
ATOM	4362	CB	SER	H	17	−75.275	−18.544	2.425	1.00	80.55	C
ATOM	4363	OG	SER	H	17	−74.139	−19.386	2.286	1.00	80.34	O
ATOM	4364	C	SER	H	17	−76.367	−19.745	0.497	1.00	80.27	C
ATOM	4365	O	SER	H	17	−75.852	−20.859	0.369	1.00	80.77	O
ATOM	4366	N	LEU	H	18	−76.747	−18.988	−0.550	1.00	76.11	N
ATOM	4367	CA	LEU	H	18	−76.545	−19.440	−1.921	1.00	75.09	C
ATOM	4368	CB	LEU	H	18	−77.591	−18.880	−2.916	1.00	75.04	C
ATOM	4369	CG	LEU	H	18	−77.659	−17.363	−3.144	1.00	75.02	C
ATOM	4370	CD1	LEU	H	18	−76.848	−16.963	−4.328	1.00	75.68	C
ATOM	4371	CD2	LEU	H	18	−79.075	−16.892	−3.389	1.00	74.44	C
ATOM	4372	C	LEU	H	18	−75.139	−19.051	−2.317	1.00	74.76	C
ATOM	4373	O	LEU	H	18	−74.662	−17.972	−1.969	1.00	74.41	O
ATOM	4374	N	ARG	H	19	−74.469	−19.938	−3.019	1.00	74.61	N
ATOM	4375	CA	ARG	H	19	−73.126	−19.699	−3.480	1.00	74.54	C
ATOM	4376	CB	ARG	H	19	−72.095	−20.339	−2.549	1.00	74.56	C
ATOM	4377	CG	ARG	H	19	−72.184	−19.622	−1.214	1.00	77.55	C
ATOM	4378	CD	ARG	H	19	−71.373	−20.123	−0.058	1.00	83.29	C
ATOM	4379	NE	ARG	H	19	−69.959	−20.310	−0.377	1.00	88.54	N
ATOM	4380	CZ	ARG	H	19	−69.093	−19.351	−0.709	1.00	90.54	C
ATOM	4381	NH1	ARG	H	19	−69.494	−18.085	−0.809	1.00	88.60	N
ATOM	4382	NH2	ARG	H	19	−67.824	−19.655	−0.965	1.00	92.32	N
ATOM	4383	C	ARG	H	19	−73.095	−20.139	−4.912	1.00	74.06	C
ATOM	4384	O	ARG	H	19	−73.229	−21.330	−5.216	1.00	74.25	O
ATOM	4385	N	LEU	H	20	−73.043	−19.123	−5.804	1.00	72.96	N
ATOM	4386	CA	LEU	H	20	−73.058	−19.247	−7.263	1.00	72.22	C
ATOM	4387	CB	LEU	H	20	−74.155	−18.353	−7.833	1.00	71.98	C
ATOM	4388	CG	LEU	H	20	−75.551	−18.561	−7.313	1.00	72.09	C
ATOM	4389	CD1	LEU	H	20	−76.477	−17.556	−7.895	1.00	72.12	C
ATOM	4390	CD2	LEU	H	20	−76.073	−19.910	−7.662	1.00	73.03	C
ATOM	4391	C	LEU	H	20	−71.739	−18.889	−7.927	1.00	71.91	C
ATOM	4392	O	LEU	H	20	−70.989	−18.053	−7.424	1.00	72.10	O
ATOM	4393	N	SER	H	21	−71.471	−19.504	−9.064	1.00	70.87	N
ATOM	4394	CA	SER	H	21	−70.270	−19.236	−9.818	1.00	70.98	C
ATOM	4395	CB	SER	H	21	−69.358	−20.450	−9.838	1.00	70.95	C
ATOM	4396	OG	SER	H	21	−68.806	−20.617	−8.545	1.00	72.22	O
ATOM	4397	C	SER	H	21	−70.667	−18.909	−11.205	1.00	71.06	C
ATOM	4398	O	SER	H	21	−71.741	−19.314	−11.637	1.00	71.48	O
ATOM	4399	N	CYS	H	22	−69.800	−18.180	−11.917	1.00	72.15	N
ATOM	4400	CA	CYS	H	22	−70.004	−17.784	−13.300	1.00	71.80	C
ATOM	4401	CB	CYS	H	22	−70.666	−16.416	−13.379	1.00	71.77	C
ATOM	4402	SG	CYS	H	22	−70.891	−15.818	−15.071	1.00	73.52	S
ATOM	4403	C	CYS	H	22	−68.658	−17.809	−13.994	1.00	71.24	C
ATOM	4404	O	CYS	H	22	−67.748	−17.129	−13.552	1.00	71.34	O
ATOM	4405	N	LYS	H	23	−68.516	−18.612	−15.042	1.00	70.46	N
ATOM	4406	CA	LYS	H	23	−67.258	−18.740	−15.754	1.00	70.46	C
ATOM	4407	CB	LYS	H	23	−66.749	−20.185	−15.748	1.00	70.57	C
ATOM	4408	CG	LYS	H	23	−65.377	−20.323	−16.393	1.00	71.74	C
ATOM	4409	CD	LYS	H	23	−64.644	−21.565	−15.971	1.00	73.39	C
ATOM	4410	CE	LYS	H	23	−63.311	−21.675	−16.687	1.00	74.92	C
ATOM	4411	NZ	LYS	H	23	−62.357	−20.557	−16.371	1.00	76.84	N
ATOM	4412	C	LYS	H	23	−67.265	−18.169	−17.158	1.00	70.28	C
ATOM	4413	O	LYS	H	23	−67.860	−18.748	−18.079	1.00	70.43	O
ATOM	4414	N	ALA	H	24	−66.532	−17.064	−17.331	1.00	68.97	N
ATOM	4415	CA	ALA	H	24	−66.411	−16.386	−18.606	1.00	68.52	C
ATOM	4416	CB	ALA	H	24	−66.065	−14.937	−18.374	1.00	68.52	C
ATOM	4417	C	ALA	H	24	−65.376	−17.041	−19.532	1.00	68.37	C
ATOM	4418	O	ALA	H	24	−64.365	−17.608	−19.075	1.00	68.38	O
ATOM	4419	N	SER	H	25	−65.639	−16.951	−20.850	1.00	67.81	N
ATOM	4420	CA	SER	H	25	−64.741	−17.502	−21.852	1.00	67.76	C
ATOM	4421	CB	SER	H	25	−65.021	−18.992	−22.075	1.00	67.84	C
ATOM	4422	OG	SER	H	25	−66.129	−19.288	−22.919	1.00	68.84	O
ATOM	4423	C	SER	H	25	−64.789	−16.748	−23.172	1.00	67.61	C
ATOM	4424	O	SER	H	25	−65.830	−16.243	−23.557	1.00	67.59	O
ATOM	4425	N	GLY	H	26	−63.665	−16.714	−23.862	1.00	69.08	N
ATOM	4426	CA	GLY	H	26	−63.575	−16.119	−25.181	1.00	69.03	C
ATOM	4427	C	GLY	H	26	−63.341	−14.638	−25.287	1.00	69.20	C
ATOM	4428	O	GLY	H	26	−63.493	−14.092	−26.386	1.00	69.36	O
ATOM	4429	N	TYR	H	27	−62.995	−13.970	−24.164	1.00	69.63	N
ATOM	4430	CA	TYR	H	27	−62.726	−12.530	−24.121	1.00	69.19	C
ATOM	4431	CB	TYR	H	27	−64.031	−11.724	−23.993	1.00	69.19	C
ATOM	4432	CG	TYR	H	27	−64.705	−11.748	−22.638	1.00	68.24	C
ATOM	4433	CD1	TYR	H	27	−64.480	−10.736	−21.708	1.00	68.05	C
ATOM	4434	CE1	TYR	H	27	−65.106	−10.744	−20.461	1.00	68.69	C
ATOM	4435	CZ	TYR	H	27	−66.016	−11.747	−20.153	1.00	68.90	C
ATOM	4436	OH	TYR	H	27	−66.662	−11.746	−18.934	1.00	68.89	O
ATOM	4437	CE2	TYR	H	27	−66.286	−12.739	−21.084	1.00	68.63	C
ATOM	4438	CD2	TYR	H	27	−65.633	−12.730	−22.318	1.00	68.29	C
ATOM	4439	C	TYR	H	27	−61.719	−12.216	−23.023	1.00	69.14	C
ATOM	4440	O	TYR	H	27	−61.306	−13.141	−22.321	1.00	69.30	O
ATOM	4441	N	THR	H	28	−61.305	−10.937	−22.865	1.00	69.86	N
ATOM	4442	CA	THR	H	28	−60.364	−10.551	−21.809	1.00	69.57	C
ATOM	4443	CB	THR	H	28	−59.416	−9.454	−22.290	1.00	69.64	C
ATOM	4444	OG1	THR	H	28	−58.599	−10.020	−23.328	1.00	70.12	O
ATOM	4445	CG2	THR	H	28	−58.490	−8.947	−21.164	1.00	70.18	C
ATOM	4446	C	THR	H	28	−61.190	−10.249	−20.594	1.00	69.14	C
ATOM	4447	O	THR	H	28	−61.860	−9.228	−20.548	1.00	69.14	O
ATOM	4448	N	PHE	H	29	−61.191	−11.175	−19.641	1.00	66.46	N
ATOM	4449	CA	PHE	H	29	−61.992	−11.133	−18.418	1.00	66.27	C
ATOM	4450	CB	PHE	H	29	−61.609	−12.272	−17.465	1.00	65.85	C
ATOM	4451	CG	PHE	H	29	−62.516	−12.405	−16.266	1.00	64.34	C
ATOM	4452	CD1	PHE	H	29	−63.828	−12.828	−16.411	1.00	62.78	C
ATOM	4453	CE1	PHE	H	29	−64.669	−12.936	−15.307	1.00	62.24	C
ATOM	4454	CZ	PHE	H	29	−64.202	−12.634	−14.053	1.00	62.61	C
ATOM	4455	CE2	PHE	H	29	−62.901	−12.214	−13.883	1.00	63.53	C
ATOM	4456	CD2	PHE	H	29	−62.058	−12.100	−14.991	1.00	64.31	C
ATOM	4457	C	PHE	H	29	−62.113	−9.794	−17.703	1.00	66.91	C
ATOM	4458	O	PHE	H	29	−63.226	−9.389	−17.324	1.00	67.42	O
ATOM	4459	N	SER	H	30	−60.974	−9.101	−17.559	1.00	70.34	N
ATOM	4460	CA	SER	H	30	−60.817	−7.798	−16.892	1.00	70.63	C
ATOM	4461	CB	SER	H	30	−59.363	−7.584	−16.504	1.00	70.51	C
ATOM	4462	OG	SER	H	30	−58.532	−8.272	−17.429	1.00	71.36	O
ATOM	4463	C	SER	H	30	−61.348	−6.570	−17.645	1.00	70.64	C
ATOM	4464	O	SER	H	30	−61.698	−5.591	−16.981	1.00	71.00	O
ATOM	4465	N	SER	H	31	−61.415	−6.611	−18.999	1.00	70.40	N
ATOM	4466	CA	SER	H	31	−61.896	−5.500	−19.836	1.00	70.53	C
ATOM	4467	CB	SER	H	31	−61.750	−5.815	−21.322	1.00	70.69	C
ATOM	4468	OG	SER	H	31	−60.508	−6.406	−21.666	1.00	73.12	O
ATOM	4469	C	SER	H	31	−63.350	−5.120	−19.587	1.00	70.40	C
ATOM	4470	O	SER	H	31	−63.729	−3.961	−19.838	1.00	71.01	O
ATOM	4471	N	TYR	H	32	−64.174	−6.086	−19.129	1.00	68.08	N
ATOM	4472	CA	TYR	H	32	−65.602	−5.849	−18.906	1.00	67.28	C
ATOM	4473	CB	TYR	H	32	−66.415	−6.861	−19.719	1.00	66.88	C
ATOM	4474	CG	TYR	H	32	−66.227	−6.729	−21.207	1.00	65.13	C
ATOM	4475	CD1	TYR	H	32	−65.053	−7.163	−21.824	1.00	64.22	C
ATOM	4476	CE1	TYR	H	32	−64.867	−7.035	−23.201	1.00	63.90	C
ATOM	4477	CZ	TYR	H	32	−65.885	−6.510	−23.985	1.00	64.65	C
ATOM	4478	OH	TYR	H	32	−65.720	−6.373	−25.344	1.00	64.76	O
ATOM	4479	CE2	TYR	H	32	−67.076	−6.102	−23.394	1.00	65.21	C
ATOM	4480	CD2	TYR	H	32	−67.233	−6.204	−22.010	1.00	65.21	C
ATOM	4481	C	TYR	H	32	−65.999	−5.939	−17.443	1.00	67.37	C
ATOM	4482	O	TYR	H	32	−65.254	−6.497	−16.667	1.00	67.35	O
ATOM	4483	N	GLY	H	33	−67.157	−5.396	−17.092	1.00	65.63	N
ATOM	4484	CA	GLY	H	33	−67.692	−5.452	−15.746	1.00	66.06	C
ATOM	4485	C	GLY	H	33	−68.749	−6.530	−15.700	1.00	66.58	C
ATOM	4486	O	GLY	H	33	−69.274	−6.910	−16.749	1.00	66.80	O
ATOM	4487	N	MET	H	34	−69.065	−7.046	−14.499	1.00	66.52	N
ATOM	4488	CA	MET	H	34	−70.046	−8.104	−14.319	1.00	66.65	C
ATOM	4489	CB	MET	H	34	−69.394	−9.345	−13.737	1.00	67.09	C
ATOM	4490	CG	MET	H	34	−68.225	−9.905	−14.497	1.00	69.58	C
ATOM	4491	SD	MET	H	34	−68.573	−10.522	−16.142	1.00	75.28	S
ATOM	4492	CE	MET	H	34	−70.078	−11.560	−15.865	1.00	73.82	C
ATOM	4493	C	MET	H	34	−71.076	−7.717	−13.313	1.00	66.50	C
ATOM	4494	O	MET	H	34	−70.731	−7.254	−12.228	1.00	66.14	O
ATOM	4495	N	TYR	H	35	−72.347	−7.964	−13.641	1.00	64.67	N
ATOM	4496	CA	TYR	H	35	−73.482	−7.743	−12.760	1.00	64.82	C
ATOM	4497	CB	TYR	H	35	−74.594	−6.958	−13.494	1.00	65.00	C
ATOM	4498	CG	TYR	H	35	−74.530	−5.446	−13.399	1.00	65.80	C
ATOM	4499	CD1	TYR	H	35	−75.447	−4.732	−12.621	1.00	66.36	C
ATOM	4500	CE1	TYR	H	35	−75.405	−3.339	−12.546	1.00	66.85	C
ATOM	4501	CZ	TYR	H	35	−74.443	−2.644	−13.266	1.00	68.42	C
ATOM	4502	OH	TYR	H	35	−74.340	−1.268	−13.236	1.00	67.78	O
ATOM	4503	CE2	TYR	H	35	−73.537	−3.337	−14.058	1.00	68.00	C
ATOM	4504	CD2	TYR	H	35	−73.595	−4.725	−14.130	1.00	66.03	C
ATOM	4505	C	TYR	H	35	−74.038	−9.135	−12.369	1.00	64.88	C
ATOM	4506	O	TYR	H	35	−73.866	−10.119	−13.088	1.00	64.57	O
ATOM	4507	N	TRP	H	36	−74.697	−9.208	−11.227	1.00	65.02	N
ATOM	4508	CA	TRP	H	36	−75.374	−10.413	−10.792	1.00	65.39	C
ATOM	4509	CB	TRP	H	36	−74.875	−10.937	−9.433	1.00	65.09	C
ATOM	4510	CG	TRP	H	36	−73.758	−11.924	−9.543	1.00	64.98	C
ATOM	4511	CD1	TRP	H	36	−72.449	−11.700	−9.255	1.00	65.63	C
ATOM	4512	NE1	TRP	H	36	−71.710	−12.843	−9.467	1.00	65.37	N
ATOM	4513	CE2	TRP	H	36	−72.537	−13.828	−9.937	1.00	65.27	C
ATOM	4514	CD2	TRP	H	36	−73.844	−13.292	−9.976	1.00	65.14	C
ATOM	4515	CE3	TRP	H	36	−74.891	−14.110	−10.421	1.00	64.75	C
ATOM	4516	CZ3	TRP	H	36	−74.605	−15.413	−10.800	1.00	64.19	C
ATOM	4517	CH2	TRP	H	36	−73.296	−15.915	−10.750	1.00	63.74	C
ATOM	4518	CZ2	TRP	H	36	−72.250	−15.143	−10.321	1.00	64.26	C
ATOM	4519	C	TRP	H	36	−76.798	−9.886	−10.721	1.00	65.98	C
ATOM	4520	O	TRP	H	36	−77.055	−8.937	−9.981	1.00	66.19	O
ATOM	4521	N	VAL	H	37	−77.686	−10.396	−11.569	1.00	69.64	N
ATOM	4522	CA	VAL	H	37	−79.080	−9.940	−11.610	1.00	70.22	C
ATOM	4523	CB	VAL	H	37	−79.428	−9.296	−12.987	1.00	70.35	C
ATOM	4524	CG1	VAL	H	37	−80.856	−8.750	−13.008	1.00	70.21	C
ATOM	4525	CG2	VAL	H	37	−78.425	−8.208	−13.382	1.00	70.26	C
ATOM	4526	C	VAL	H	37	−79.956	−11.161	−11.350	1.00	70.46	C
ATOM	4527	O	VAL	H	37	−79.578	−12.261	−11.754	1.00	70.87	O
ATOM	4528	N	ARG	H	38	−81.112	−10.980	−10.694	1.00	71.70	N
ATOM	4529	CA	ARG	H	38	−82.038	−12.072	−10.437	1.00	71.83	C
ATOM	4530	CB	ARG	H	38	−82.063	−12.479	−8.962	1.00	71.52	C
ATOM	4531	CG	ARG	H	38	−82.784	−11.516	−8.019	1.00	70.95	C
ATOM	4532	CD	ARG	H	38	−82.776	−12.049	−6.600	1.00	70.37	C
ATOM	4533	NE	ARG	H	38	−83.622	−11.259	−5.700	1.00	69.30	N
ATOM	4534	CZ	ARG	H	38	−83.680	−11.458	−4.385	1.00	69.01	C
ATOM	4535	NH1	ARG	H	38	−82.938	−12.401	−3.815	1.00	69.40	N
ATOM	4536	NH2	ARG	H	38	−84.473	−10.703	−3.626	1.00	68.45	N
ATOM	4537	C	ARG	H	38	−83.424	−11.737	−10.958	1.00	72.40	C
ATOM	4538	O	ARG	H	38	−83.737	−10.563	−11.168	1.00	72.42	O
ATOM	4539	N	GLN	H	39	−84.261	−12.761	−11.175	1.00	74.58	N
ATOM	4540	CA	GLN	H	39	−85.621	−12.539	−11.653	1.00	75.17	C
ATOM	4541	CB	GLN	H	39	−85.635	−12.551	−13.173	1.00	74.95	C
ATOM	4542	CG	GLN	H	39	−86.998	−12.352	−13.788	1.00	73.81	C
ATOM	4543	CD	GLN	H	39	−86.864	−12.405	−15.275	1.00	72.62	C
ATOM	4544	OE1	GLN	H	39	−86.133	−13.251	−15.833	1.00	72.71	O
ATOM	4545	NE2	GLN	H	39	−87.566	−11.505	−15.945	1.00	71.94	N
ATOM	4546	C	GLN	H	39	−86.554	−13.585	−11.070	1.00	75.87	C
ATOM	4547	O	GLN	H	39	−86.428	−14.765	−11.400	1.00	76.00	O
ATOM	4548	N	ALA	H	40	−87.468	−13.157	−10.179	1.00	79.68	N
ATOM	4549	CA	ALA	H	40	−88.437	−14.055	−9.557	1.00	80.51	C
ATOM	4550	CB	ALA	H	40	−89.123	−13.369	−8.400	1.00	80.27	C
ATOM	4551	C	ALA	H	40	−89.450	−14.438	−10.628	1.00	81.37	C
ATOM	4552	O	ALA	H	40	−89.762	−13.580	−11.452	1.00	81.84	O
ATOM	4553	N	PRO	H	41	−89.930	−15.711	−10.671	1.00	85.05	N
ATOM	4554	CA	PRO	H	41	−90.859	−16.153	−11.737	1.00	85.30	C
ATOM	4555	CB	PRO	H	41	−91.486	−17.431	−11.164	1.00	85.19	C
ATOM	4556	CG	PRO	H	41	−90.921	−17.572	−9.757	1.00	85.38	C
ATOM	4557	CD	PRO	H	41	−89.629	−16.838	−9.771	1.00	85.27	C
ATOM	4558	C	PRO	H	41	−91.864	−15.170	−12.361	1.00	85.47	C
ATOM	4559	O	PRO	H	41	−91.797	−14.903	−13.573	1.00	85.58	O
ATOM	4560	N	GLY	H	42	−92.765	−14.631	−11.549	1.00	86.15	N
ATOM	4561	CA	GLY	H	42	−93.730	−13.665	−12.056	1.00	86.25	C
ATOM	4562	C	GLY	H	42	−93.048	−12.352	−12.411	1.00	86.19	C
ATOM	4563	O	GLY	H	42	−93.180	−11.852	−13.535	1.00	86.40	O
ATOM	4564	N	LYS	H	43	−92.278	−11.819	−11.440	1.00	82.73	N
ATOM	4565	CA	LYS	H	43	−91.509	−10.583	−11.480	1.00	81.98	C
ATOM	4566	CB	LYS	H	43	−90.766	−10.431	−10.140	1.00	82.07	C
ATOM	4567	C	LYS	H	43	−90.538	−10.346	−12.691	1.00	81.47	C
ATOM	4568	O	LYS	H	43	−90.332	−11.213	−13.556	1.00	81.20	O
ATOM	4569	N	GLY	H	44	−89.976	−9.138	−12.705	1.00	76.91	N
ATOM	4570	CA	GLY	H	44	−89.006	−8.663	−13.671	1.00	76.29	C
ATOM	4571	C	GLY	H	44	−87.603	−8.677	−13.092	1.00	75.96	C
ATOM	4572	O	GLY	H	44	−87.377	−9.231	−12.008	1.00	76.24	O
ATOM	4573	N	LEU	H	45	−86.651	−8.057	−13.813	1.00	71.99	N
ATOM	4574	CA	LEU	H	45	−85.230	−7.989	−13.471	1.00	71.27	C
ATOM	4575	CB	LEU	H	45	−84.412	−7.534	−14.691	1.00	70.96	C
ATOM	4576	CG	LEU	H	45	−84.619	−8.373	−15.941	1.00	70.10	C
ATOM	4577	CD1	LEU	H	45	−84.088	−7.696	−17.142	1.00	69.71	C
ATOM	4578	CD2	LEU	H	45	−83.974	−9.728	−15.812	1.00	69.93	C
ATOM	4579	C	LEU	H	45	−84.886	−7.181	−12.223	1.00	71.13	C
ATOM	4580	O	LEU	H	45	−85.286	−6.030	−12.107	1.00	71.44	O
ATOM	4581	N	GLU	H	46	−84.145	−7.788	−11.286	1.00	73.29	N
ATOM	4582	CA	GLU	H	46	−83.716	−7.147	−10.043	1.00	73.28	C
ATOM	4583	CB	GLU	H	46	−84.414	−7.770	−8.821	1.00	73.31	C
ATOM	4584	CG	GLU	H	46	−83.727	−7.488	−7.486	1.00	75.03	C
ATOM	4585	CD	GLU	H	46	−84.613	−7.644	−6.265	1.00	77.42	C
ATOM	4586	OE1	GLU	H	46	−84.689	−6.677	−5.471	1.00	78.48	O
ATOM	4587	OE2	GLU	H	46	−85.241	−8.720	−6.107	1.00	79.58	O
ATOM	4588	C	GLU	H	46	−82.200	−7.225	−9.934	1.00	72.99	C
ATOM	4589	O	GLU	H	46	−81.642	−8.316	−9.826	1.00	73.27	O
ATOM	4590	N	TRP	H	47	−81.522	−6.072	−9.987	1.00	71.13	N
ATOM	4591	CA	TRP	H	47	−80.064	−6.082	−9.906	1.00	70.33	C
ATOM	4592	CB	TRP	H	47	−79.464	−4.756	−10.410	1.00	70.46	C
ATOM	4593	CG	TRP	H	47	−79.220	−3.703	−9.368	1.00	70.46	C
ATOM	4594	CD1	TRP	H	47	−80.151	−2.919	−8.759	1.00	70.13	C
ATOM	4595	NE1	TRP	H	47	−79.540	−2.068	−7.863	1.00	70.12	N
ATOM	4596	CE2	TRP	H	47	−78.188	−2.281	−7.895	1.00	69.84	C
ATOM	4597	CD2	TRP	H	47	−77.948	−3.305	−8.834	1.00	70.37	C
ATOM	4598	CE3	TRP	H	47	−76.626	−3.732	−9.042	1.00	70.17	C
ATOM	4599	CZ3	TRP	H	47	−75.611	−3.129	−8.320	1.00	69.26	C
ATOM	4600	CH2	TRP	H	47	−75.884	−2.125	−7.388	1.00	67.91	C
ATOM	4601	CZ2	TRP	H	47	−77.162	−1.681	−7.167	1.00	69.50	C
ATOM	4602	C	TRP	H	47	−79.628	−6.443	−8.497	1.00	69.74	C
ATOM	4603	O	TRP	H	47	−80.275	−6.030	−7.534	1.00	69.62	O
ATOM	4604	N	ILE	H	48	−78.575	−7.253	−8.373	1.00	67.17	N
ATOM	4605	CA	ILE	H	48	−78.067	−7.669	−7.064	1.00	66.52	C
ATOM	4606	CB	ILE	H	48	−77.870	−9.212	−6.979	1.00	66.45	C
ATOM	4607	CG1	ILE	H	48	−79.214	−9.941	−7.101	1.00	66.20	C
ATOM	4608	CD1	ILE	H	48	−79.091	−11.089	−7.877	1.00	66.59	C
ATOM	4609	CG2	ILE	H	48	−77.080	−9.657	−5.735	1.00	66.23	C
ATOM	4610	C	ILE	H	48	−76.832	−6.845	−6.727	1.00	66.16	C
ATOM	4611	O	ILE	H	48	−76.856	−6.080	−5.767	1.00	65.97	O
ATOM	4612	N	GLY	H	49	−75.792	−6.990	−7.535	1.00	65.65	N
ATOM	4613	CA	GLY	H	49	−74.543	−6.282	−7.350	1.00	65.29	C
ATOM	4614	C	GLY	H	49	−73.689	−6.230	−8.598	1.00	65.45	C
ATOM	4615	O	GLY	H	49	−73.948	−6.930	−9.586	1.00	65.27	O
ATOM	4616	N	TRP	H	50	−72.642	−5.399	−8.540	1.00	66.73	N
ATOM	4617	CA	TRP	H	50	−71.678	−5.202	−9.622	1.00	66.82	C
ATOM	4618	CB	TRP	H	50	−71.910	−3.831	−10.298	1.00	66.43	C
ATOM	4619	CG	TRP	H	50	−70.814	−3.413	−11.230	1.00	63.90	C
ATOM	4620	CD1	TRP	H	50	−70.646	−3.800	−12.527	1.00	62.55	C
ATOM	4621	NE1	TRP	H	50	−69.511	−3.235	−13.050	1.00	61.58	N
ATOM	4622	CE2	TRP	H	50	−68.897	−2.487	−12.073	1.00	62.09	C
ATOM	4623	CD2	TRP	H	50	−69.698	−2.580	−10.909	1.00	62.02	C
ATOM	4624	CE3	TRP	H	50	−69.267	−1.930	−9.734	1.00	61.51	C
ATOM	4625	CZ3	TRP	H	50	−68.091	−1.193	−9.768	1.00	59.88	C
ATOM	4626	CH2	TRP	H	50	−67.316	−1.118	−10.934	1.00	60.16	C
ATOM	4627	CZ2	TRP	H	50	−67.695	−1.755	−12.100	1.00	60.79	C
ATOM	4628	C	TRP	H	50	−70.229	−5.335	−9.111	1.00	67.37	C
ATOM	4629	O	TRP	H	50	−69.966	−5.052	−7.941	1.00	67.16	O
ATOM	4630	N	ILE	H	51	−69.307	−5.748	−9.997	1.00	65.38	N
ATOM	4631	CA	ILE	H	51	−67.901	−5.890	−9.687	1.00	66.71	C
ATOM	4632	CB	ILE	H	51	−67.561	−7.267	−9.077	1.00	66.78	C
ATOM	4633	CG1	ILE	H	51	−66.179	−7.234	−8.328	1.00	66.43	C
ATOM	4634	CD1	ILE	H	51	−65.274	−8.456	−8.481	1.00	64.32	C
ATOM	4635	CG2	ILE	H	51	−67.671	−8.400	−10.138	1.00	66.18	C
ATOM	4636	C	ILE	H	51	−67.044	−5.617	−10.913	1.00	67.98	C
ATOM	4637	O	ILE	H	51	−67.364	−6.085	−12.009	1.00	68.13	O
ATOM	4638	N	ASP	H	52	−65.936	−4.884	−10.726	1.00	73.76	N
ATOM	4639	CA	ASP	H	52	−65.022	−4.621	−11.812	1.00	75.48	C
ATOM	4640	CB	ASP	H	52	−64.515	−3.183	−11.781	1.00	75.68	C
ATOM	4641	CG	ASP	H	52	−63.282	−2.949	−12.637	1.00	77.20	C
ATOM	4642	OD1	ASP	H	52	−62.384	−2.192	−12.178	1.00	78.73	O
ATOM	4643	OD2	ASP	H	52	−63.202	−3.543	−13.781	1.00	76.29	O
ATOM	4644	C	ASP	H	52	−63.879	−5.644	−11.705	1.00	76.31	C
ATOM	4645	O	ASP	H	52	−63.042	−5.534	−10.801	1.00	76.43	O
ATOM	4646	N	PRO	H	53	−63.823	−6.653	−12.614	1.00	78.05	N
ATOM	4647	CA	PRO	H	53	−62.752	−7.660	−12.543	1.00	78.76	C
ATOM	4648	CB	PRO	H	53	−63.074	−8.626	−13.689	1.00	78.77	C
ATOM	4649	CG	PRO	H	53	−64.483	−8.421	−13.982	1.00	78.29	C
ATOM	4650	CD	PRO	H	53	−64.746	−6.957	−13.720	1.00	78.12	C
ATOM	4651	C	PRO	H	53	−61.357	−7.071	−12.678	1.00	79.46	C
ATOM	4652	O	PRO	H	53	−60.378	−7.777	−12.418	1.00	80.25	O
ATOM	4653	N	GLY	H	54	−61.281	−5.799	−13.079	1.00	78.39	N
ATOM	4654	CA	GLY	H	54	−60.023	−5.083	−13.210	1.00	78.15	C
ATOM	4655	C	GLY	H	54	−59.461	−4.803	−11.832	1.00	77.68	C
ATOM	4656	O	GLY	H	54	−58.483	−5.434	−11.420	1.00	77.62	O
ATOM	4657	N	SER	H	55	−60.121	−3.897	−11.099	1.00	77.03	N
ATOM	4658	CA	SER	H	55	−59.740	−3.476	−9.757	1.00	76.83	C
ATOM	4659	CB	SER	H	55	−60.242	−2.065	−9.479	1.00	76.80	C
ATOM	4660	OG	SER	H	55	−61.658	−1.999	−9.501	1.00	77.10	O
ATOM	4661	C	SER	H	55	−60.208	−4.397	−8.646	1.00	76.83	C
ATOM	4662	O	SER	H	55	−59.390	−4.929	−7.895	1.00	77.56	O
ATOM	4663	N	GLY	H	56	−61.515	−4.563	−8.547	1.00	75.37	N
ATOM	4664	CA	GLY	H	56	−62.203	−5.325	−7.517	1.00	74.42	C
ATOM	4665	C	GLY	H	56	−63.294	−4.422	−6.966	1.00	74.06	C
ATOM	4666	O	GLY	H	56	−63.938	−4.746	−5.961	1.00	73.96	O
ATOM	4667	N	GLY	H	57	−63.480	−3.279	−7.643	1.00	70.98	N
ATOM	4668	CA	GLY	H	57	−64.487	−2.277	−7.332	1.00	70.53	C
ATOM	4669	C	GLY	H	57	−65.847	−2.934	−7.303	1.00	70.34	C
ATOM	4670	O	GLY	H	57	−66.218	−3.660	−8.226	1.00	70.61	O
ATOM	4671	N	THR	H	58	−66.588	−2.704	−6.243	1.00	68.48	N
ATOM	4672	CA	THR	H	58	−67.841	−3.386	−6.090	1.00	67.80	C
ATOM	4673	CB	THR	H	58	−67.484	−4.512	−5.112	1.00	67.50	C
ATOM	4674	OG1	THR	H	58	−67.790	−5.788	−5.635	1.00	68.57	O
ATOM	4675	CG2	THR	H	58	−67.909	−4.281	−3.694	1.00	67.36	C
ATOM	4676	C	THR	H	58	−69.012	−2.480	−5.715	1.00	67.57	C
ATOM	4677	O	THR	H	58	−68.824	−1.568	−4.922	1.00	67.91	O
ATOM	4678	N	LYS	H	59	−70.215	−2.712	−6.273	1.00	66.54	N
ATOM	4679	CA	LYS	H	59	−71.445	−1.942	−5.922	1.00	66.37	C
ATOM	4680	CB	LYS	H	59	−71.880	−0.954	−7.023	1.00	65.94	C
ATOM	4681	CG	LYS	H	59	−70.839	0.083	−7.387	1.00	65.87	C
ATOM	4682	CD	LYS	H	59	−71.473	1.258	−8.101	1.00	65.73	C
ATOM	4683	CE	LYS	H	59	−70.641	1.831	−9.224	1.00	63.88	C
ATOM	4684	NZ	LYS	H	59	−71.283	1.617	−10.566	1.00	63.65	N
ATOM	4685	C	LYS	H	59	−72.578	−2.953	−5.633	1.00	66.37	C
ATOM	4686	O	LYS	H	59	−72.665	−3.953	−6.343	1.00	66.46	O
ATOM	4687	N	TYR	H	60	−73.409	−2.725	−4.601	1.00	65.94	N
ATOM	4688	CA	TYR	H	60	−74.512	−3.641	−4.260	1.00	66.27	C
ATOM	4689	CB	TYR	H	60	−74.252	−4.386	−2.949	1.00	65.68	C
ATOM	4690	CG	TYR	H	60	−72.987	−5.203	−2.907	1.00	65.72	C
ATOM	4691	CD1	TYR	H	60	−73.000	−6.567	−3.200	1.00	66.37	C
ATOM	4692	CE1	TYR	H	60	−71.828	−7.332	−3.145	1.00	66.03	C
ATOM	4693	CZ	TYR	H	60	−70.635	−6.732	−2.776	1.00	65.40	C
ATOM	4694	OH	TYR	H	60	−69.455	−7.428	−2.716	1.00	65.30	O
ATOM	4695	CE2	TYR	H	60	−70.618	−5.390	−2.444	1.00	65.92	C
ATOM	4696	CD2	TYR	H	60	−71.786	−4.635	−2.514	1.00	65.58	C
ATOM	4697	C	TYR	H	60	−75.861	−2.946	−4.124	1.00	66.96	C
ATOM	4698	O	TYR	H	60	−75.927	−1.776	−3.747	1.00	66.93	O
ATOM	4699	N	ASN	H	61	−76.945	−3.676	−4.408	1.00	74.07	N
ATOM	4700	CA	ASN	H	61	−78.296	−3.147	−4.254	1.00	75.29	C
ATOM	4701	CB	ASN	H	61	−79.308	−4.131	−4.838	1.00	75.03	C
ATOM	4702	CG	ASN	H	61	−80.745	−3.687	−4.798	1.00	75.28	C
ATOM	4703	OD1	ASN	H	61	−81.168	−2.881	−3.969	1.00	76.17	O
ATOM	4704	ND2	ASN	H	61	−81.556	−4.221	−5.695	1.00	75.49	N
ATOM	4705	C	ASN	H	61	−78.496	−2.964	−2.728	1.00	76.55	C
ATOM	4706	O	ASN	H	61	−78.137	−3.869	−1.957	1.00	76.87	O
ATOM	4707	N	GLU	H	62	−79.025	−1.791	−2.287	1.00	79.72	N
ATOM	4708	CA	GLU	H	62	−79.246	−1.525	−0.867	1.00	80.72	C
ATOM	4709	CB	GLU	H	62	−79.777	−0.116	−0.635	1.00	80.60	C
ATOM	4710	C	GLU	H	62	−80.103	−2.614	−0.172	1.00	81.74	C
ATOM	4711	O	GLU	H	62	−79.878	−2.866	1.017	1.00	82.04	O
ATOM	4712	N	LYS	H	63	−81.036	−3.298	−0.914	1.00	83.34	N
ATOM	4713	CA	LYS	H	63	−81.869	−4.389	−0.382	1.00	84.18	C
ATOM	4714	CB	LYS	H	63	−82.757	−5.008	−1.483	1.00	83.83	C
ATOM	4715	C	LYS	H	63	−80.984	−5.473	0.302	1.00	85.07	C
ATOM	4716	O	LYS	H	63	−81.297	−5.897	1.409	1.00	85.46	O
ATOM	4717	N	PHE	H	64	−79.859	−5.868	−0.328	1.00	87.41	N
ATOM	4718	CA	PHE	H	64	−78.931	−6.878	0.200	1.00	88.13	C
ATOM	4719	CB	PHE	H	64	−78.508	−7.839	−0.932	1.00	87.91	C
ATOM	4720	CG	PHE	H	64	−79.520	−8.037	−2.037	1.00	87.18	C
ATOM	4721	CD1	PHE	H	64	−79.311	−7.497	−3.295	1.00	86.67	C
ATOM	4722	CE1	PHE	H	64	−80.249	−7.678	−4.311	1.00	85.39	C
ATOM	4723	CZ	PHE	H	64	−81.392	−8.399	−4.074	1.00	84.32	C
ATOM	4724	CE2	PHE	H	64	−81.614	−8.940	−2.836	1.00	84.40	C
ATOM	4725	CD2	PHE	H	64	−80.684	−8.757	−1.817	1.00	85.74	C
ATOM	4726	C	PHE	H	64	−77.685	−6.241	0.902	1.00	89.03	C
ATOM	4727	O	PHE	H	64	−76.527	−6.644	0.650	1.00	89.44	O
ATOM	4728	N	LYS	H	65	−77.934	−5.234	1.784	1.00	91.91	N
ATOM	4729	CA	LYS	H	65	−76.890	−4.511	2.534	1.00	91.95	C
ATOM	4730	CB	LYS	H	65	−77.490	−3.335	3.342	1.00	92.18	C
ATOM	4731	C	LYS	H	65	−76.126	−5.469	3.448	1.00	91.81	C
ATOM	4732	O	LYS	H	65	−76.642	−5.894	4.490	1.00	91.86	O
ATOM	4733	N	GLY	H	66	−74.923	−5.832	3.012	1.00	91.10	N
ATOM	4734	CA	GLY	H	66	−74.065	−6.752	3.746	1.00	90.88	C
ATOM	4735	C	GLY	H	66	−74.492	−8.201	3.618	1.00	90.89	C
ATOM	4736	O	GLY	H	66	−73.743	−9.096	4.020	1.00	91.20	O
ATOM	4737	N	LYS	H	67	−75.705	−8.450	3.056	1.00	90.67	N
ATOM	4738	CA	LYS	H	67	−76.247	−9.793	2.832	1.00	90.02	C
ATOM	4739	CB	LYS	H	67	−77.753	−9.724	2.558	1.00	89.88	C
ATOM	4740	C	LYS	H	67	−75.497	−10.467	1.667	1.00	89.63	C
ATOM	4741	O	LYS	H	67	−75.191	−11.654	1.742	1.00	89.64	O
ATOM	4742	N	ALA	H	68	−75.170	−9.683	0.615	1.00	88.82	N
ATOM	4743	CA	ALA	H	68	−74.462	−10.118	−0.595	1.00	88.21	C
ATOM	4744	CB	ALA	H	68	−75.108	−9.486	−1.819	1.00	88.14	C
ATOM	4745	C	ALA	H	68	−72.935	−9.842	−0.588	1.00	87.72	C
ATOM	4746	O	ALA	H	68	−72.471	−8.920	0.093	1.00	88.14	O
ATOM	4747	N	THR	H	69	−72.163	−10.654	−1.350	1.00	84.50	N
ATOM	4748	CA	THR	H	69	−70.708	−10.544	−1.477	1.00	83.53	C
ATOM	4749	CB	THR	H	69	−69.985	−11.394	−0.401	1.00	83.59	C
ATOM	4750	OG1	THR	H	69	−70.545	−11.172	0.899	1.00	83.87	O
ATOM	4751	CG2	THR	H	69	−68.457	−11.205	−0.407	1.00	82.58	C
ATOM	4752	C	THR	H	69	−70.303	−11.027	−2.862	1.00	83.16	C
ATOM	4753	O	THR	H	69	−70.386	−12.231	−3.146	1.00	83.89	O
ATOM	4754	N	ILE	H	70	−69.850	−10.106	−3.719	1.00	77.88	N
ATOM	4755	CA	ILE	H	70	−69.410	−10.456	−5.071	1.00	76.85	C
ATOM	4756	CB	ILE	H	70	−70.094	−9.611	−6.180	1.00	76.87	C
ATOM	4757	CG1	ILE	H	70	−71.608	−9.667	−6.025	1.00	76.68	C
ATOM	4758	CD1	ILE	H	70	−72.269	−8.566	−6.573	1.00	76.66	C
ATOM	4759	CG2	ILE	H	70	−69.696	−10.099	−7.589	1.00	76.64	C
ATOM	4760	C	ILE	H	70	−67.894	−10.426	−5.147	1.00	76.29	C
ATOM	4761	O	ILE	H	70	−67.276	−9.485	−4.649	1.00	76.21	O
ATOM	4762	N	SER	H	71	−67.303	−11.463	−5.768	1.00	73.60	N
ATOM	4763	CA	SER	H	71	−65.858	−11.583	−5.946	1.00	73.32	C
ATOM	4764	CB	SER	H	71	−65.213	−12.345	−4.791	1.00	73.02	C
ATOM	4765	OG	SER	H	71	−65.483	−13.734	−4.787	1.00	72.63	O
ATOM	4766	C	SER	H	71	−65.472	−12.142	−7.311	1.00	73.44	C
ATOM	4767	O	SER	H	71	−66.354	−12.477	−8.098	1.00	73.35	O
ATOM	4768	N	ARG	H	72	−64.170	−12.201	−7.605	1.00	75.48	N
ATOM	4769	CA	ARG	H	72	−63.661	−12.700	−8.875	1.00	76.24	C
ATOM	4770	CB	ARG	H	72	−63.371	−11.515	−9.819	1.00	76.60	C
ATOM	4771	CG	ARG	H	72	−61.963	−10.932	−9.644	1.00	78.47	C
ATOM	4772	CD	ARG	H	72	−61.921	−9.442	−9.758	1.00	82.25	C
ATOM	4773	NE	ARG	H	72	−61.252	−8.815	−8.620	1.00	83.67	N
ATOM	4774	CZ	ARG	H	72	−60.030	−8.300	−8.661	1.00	84.64	C
ATOM	4775	NH1	ARG	H	72	−59.317	−8.353	−9.783	1.00	85.32	N
ATOM	4776	NH2	ARG	H	72	−59.506	−7.731	−7.582	1.00	85.79	N
ATOM	4777	C	ARG	H	72	−62.388	−13.538	−8.670	1.00	76.09	C
ATOM	4778	O	ARG	H	72	−61.857	−13.605	−7.562	1.00	76.37	O
ATOM	4779	N	ASP	H	73	−61.883	−14.140	−9.747	1.00	77.73	N
ATOM	4780	CA	ASP	H	73	−60.662	−14.929	−9.737	1.00	77.99	C
ATOM	4781	CB	ASP	H	73	−60.971	−16.362	−9.276	1.00	78.21	C
ATOM	4782	CG	ASP	H	73	−59.812	−17.175	−8.705	1.00	78.48	C
ATOM	4783	OD1	ASP	H	73	−58.651	−16.988	−9.181	1.00	76.53	O
ATOM	4784	OD2	ASP	H	73	−60.075	−18.043	−7.806	1.00	80.10	O
ATOM	4785	C	ASP	H	73	−60.098	−14.881	−11.160	1.00	78.17	C
ATOM	4786	O	ASP	H	73	−60.113	−15.882	−11.877	1.00	77.98	O
ATOM	4787	N	ASN	H	74	−59.616	−13.692	−11.568	1.00	77.75	N
ATOM	4788	CA	ASN	H	74	−59.066	−13.424	−12.893	1.00	77.93	C
ATOM	4789	CB	ASN	H	74	−58.226	−12.155	−12.872	1.00	78.15	C
ATOM	4790	CG	ASN	H	74	−59.031	−10.887	−12.827	1.00	79.65	C
ATOM	4791	OD1	ASN	H	74	−59.705	−10.592	−11.843	1.00	81.86	O
ATOM	4792	ND2	ASN	H	74	−58.965	−10.105	−13.894	1.00	80.65	N
ATOM	4793	C	ASN	H	74	−58.281	−14.578	−13.525	1.00	77.75	C
ATOM	4794	O	ASN	H	74	−58.295	−14.729	−14.753	1.00	77.58	O
ATOM	4795	N	SER	H	75	−57.597	−15.383	−12.681	1.00	77.01	N
ATOM	4796	CA	SER	H	75	−56.783	−16.530	−13.091	1.00	76.66	C
ATOM	4797	CB	SER	H	75	−55.966	−17.040	−11.919	1.00	76.52	C
ATOM	4798	OG	SER	H	75	−56.841	−17.302	−10.835	1.00	77.70	O
ATOM	4799	C	SER	H	75	−57.635	−17.658	−13.638	1.00	76.26	C
ATOM	4800	O	SER	H	75	−57.148	−18.418	−14.476	1.00	76.65	O
ATOM	4801	N	LYS	H	76	−58.892	−17.778	−13.161	1.00	73.56	N
ATOM	4802	CA	LYS	H	76	−59.837	−18.808	−13.593	1.00	72.90	C
ATOM	4803	CB	LYS	H	76	−60.073	−19.891	−12.521	1.00	72.97	C
ATOM	4804	CG	LYS	H	76	−60.109	−19.394	−11.094	1.00	73.34	C
ATOM	4805	CD	LYS	H	76	−60.812	−20.371	−10.118	1.00	74.83	C
ATOM	4806	CE	LYS	H	76	−59.884	−21.119	−9.187	1.00	75.51	C
ATOM	4807	NZ	LYS	H	76	−59.171	−22.235	−9.885	1.00	76.07	N
ATOM	4808	C	LYS	H	76	−61.131	−18.218	−14.154	1.00	72.42	C
ATOM	4809	O	LYS	H	76	−62.174	−18.882	−14.187	1.00	72.36	O
ATOM	4810	N	ASN	H	77	−61.053	−16.942	−14.599	1.00	72.21	N
ATOM	4811	CA	ASN	H	77	−62.142	−16.171	−15.213	1.00	71.28	C
ATOM	4812	CB	ASN	H	77	−62.280	−16.601	−16.669	1.00	70.88	C
ATOM	4813	CG	ASN	H	77	−61.140	−16.232	−17.561	1.00	70.31	C
ATOM	4814	OD1	ASN	H	77	−61.354	−15.894	−18.724	1.00	70.39	O
ATOM	4815	ND2	ASN	H	77	−59.916	−16.293	−17.071	1.00	70.87	N
ATOM	4816	C	ASN	H	77	−63.491	−16.338	−14.497	1.00	71.06	C
ATOM	4817	O	ASN	H	77	−64.552	−16.213	−15.119	1.00	71.17	O
ATOM	4818	N	THR	H	78	−63.457	−16.641	−13.209	1.00	67.84	N
ATOM	4819	CA	THR	H	78	−64.706	−16.851	−12.516	1.00	67.61	C
ATOM	4820	CB	THR	H	78	−64.782	−18.234	−11.818	1.00	67.66	C
ATOM	4821	OG1	THR	H	78	−63.489	−18.573	−11.370	1.00	68.59	O
ATOM	4822	CG2	THR	H	78	−65.170	−19.328	−12.744	1.00	67.39	C
ATOM	4823	C	THR	H	78	−65.160	−15.666	−11.724	1.00	67.05	C
ATOM	4824	O	THR	H	78	−64.359	−14.867	−11.264	1.00	66.86	O
ATOM	4825	N	LEU	H	79	−66.455	−15.564	−11.581	1.00	65.03	N
ATOM	4826	CA	LEU	H	79	−67.135	−14.527	−10.853	1.00	64.84	C
ATOM	4827	CB	LEU	H	79	−68.018	−13.799	−11.856	1.00	64.81	C
ATOM	4828	CG	LEU	H	79	−68.966	−12.782	−11.324	1.00	65.04	C
ATOM	4829	CD1	LEU	H	79	−68.254	−11.520	−11.026	1.00	66.20	C
ATOM	4830	CD2	LEU	H	79	−70.119	−12.567	−12.297	1.00	64.91	C
ATOM	4831	C	LEU	H	79	−67.964	−15.271	−9.823	1.00	65.02	C
ATOM	4832	O	LEU	H	79	−68.577	−16.281	−10.162	1.00	65.22	O
ATOM	4833	N	TYR	H	80	−67.953	−14.829	−8.568	1.00	64.32	N
ATOM	4834	CA	TYR	H	80	−68.694	−15.535	−7.532	1.00	64.62	C
ATOM	4835	CB	TYR	H	80	−67.752	−16.122	−6.458	1.00	64.08	C
ATOM	4836	CG	TYR	H	80	−66.626	−17.007	−6.950	1.00	64.44	C
ATOM	4837	CD1	TYR	H	80	−65.364	−16.481	−7.220	1.00	64.70	C
ATOM	4838	CE1	TYR	H	80	−64.320	−17.289	−7.668	1.00	64.48	C
ATOM	4839	CZ	TYR	H	80	−64.520	−18.650	−7.812	1.00	65.60	C
ATOM	4840	OH	TYR	H	80	−63.491	−19.448	−8.253	1.00	66.92	O
ATOM	4841	CE2	TYR	H	80	−65.758	−19.203	−7.516	1.00	65.49	C
ATOM	4842	CD2	TYR	H	80	−66.802	−18.380	−7.093	1.00	64.95	C
ATOM	4843	C	TYR	H	80	−69.660	−14.609	−6.841	1.00	65.53	C
ATOM	4844	O	TYR	H	80	−69.348	−13.437	−6.613	1.00	65.93	O
ATOM	4845	N	LEU	H	81	−70.823	−15.144	−6.473	1.00	68.48	N
ATOM	4846	CA	LEU	H	81	−71.832	−14.431	−5.709	1.00	69.08	C
ATOM	4847	CB	LEU	H	81	−73.130	−14.187	−6.522	1.00	68.98	C
ATOM	4848	CG	LEU	H	81	−74.458	−13.954	−5.745	1.00	68.46	C
ATOM	4849	CD1	LEU	H	81	−74.497	−12.601	−5.103	1.00	67.63	C
ATOM	4850	CD2	LEU	H	81	−75.635	−14.096	−6.645	1.00	68.63	C
ATOM	4851	C	LEU	H	81	−72.114	−15.283	−4.473	1.00	69.89	C
ATOM	4852	O	LEU	H	81	−72.090	−16.521	−4.544	1.00	69.50	O
ATOM	4853	N	GLN	H	82	−72.370	−14.604	−3.347	1.00	77.02	N
ATOM	4854	CA	GLN	H	82	−72.741	−15.211	−2.086	1.00	78.47	C
ATOM	4855	CB	GLN	H	82	−71.554	−15.328	−1.145	1.00	78.56	C
ATOM	4856	CG	GLN	H	82	−71.958	−16.041	0.147	1.00	81.03	C
ATOM	4857	CD	GLN	H	82	−70.901	−16.019	1.216	1.00	83.34	C
ATOM	4858	OE1	GLN	H	82	−70.408	−17.081	1.631	1.00	84.08	O
ATOM	4859	NE2	GLN	H	82	−70.538	−14.812	1.684	1.00	84.60	N
ATOM	4860	C	GLN	H	82	−73.840	−14.384	−1.440	1.00	79.23	C
ATOM	4861	O	GLN	H	82	−73.697	−13.170	−1.306	1.00	79.44	O
ATOM	4862	N	MET	H	83	−74.924	−15.037	−1.039	1.00	79.50	N
ATOM	4863	CA	MET	H	83	−76.023	−14.364	−0.377	1.00	80.56	C
ATOM	4864	CB	MET	H	83	−77.223	−14.186	−1.301	1.00	80.59	C
ATOM	4865	CG	MET	H	83	−77.063	−13.048	−2.260	1.00	81.48	C
ATOM	4866	SD	MET	H	83	−78.606	−12.506	−3.041	1.00	83.98	S
ATOM	4867	CE	MET	H	83	−79.683	−12.206	−1.544	1.00	82.79	C
ATOM	4868	C	MET	H	83	−76.373	−15.165	0.842	1.00	81.17	C
ATOM	4869	O	MET	H	83	−76.792	−16.308	0.725	1.00	81.21	O
ATOM	4870	N	ASN	H	84	−76.171	−14.561	2.014	1.00	83.17	N
ATOM	4871	CA	ASN	H	84	−76.391	−15.144	3.332	1.00	84.11	C
ATOM	4872	CB	ASN	H	84	−75.286	−14.659	4.258	1.00	84.31	C
ATOM	4873	CG	ASN	H	84	−73.927	−14.697	3.596	1.00	85.99	C
ATOM	4874	OD1	ASN	H	84	−73.459	−15.742	3.103	1.00	87.19	O
ATOM	4875	ND2	ASN	H	84	−73.261	−13.545	3.552	1.00	88.48	N
ATOM	4876	C	ASN	H	84	−77.774	−14.819	3.899	1.00	84.38	C
ATOM	4877	O	ASN	H	84	−78.430	−13.895	3.412	1.00	84.40	O
ATOM	4878	N	SER	H	85	−78.219	−15.591	4.922	1.00	86.21	N
ATOM	4879	CA	SER	H	85	−79.510	−15.426	5.625	1.00	86.62	C
ATOM	4880	CB	SER	H	85	−79.454	−14.250	6.608	1.00	86.59	C
ATOM	4881	OG	SER	H	85	−78.255	−14.235	7.371	1.00	87.47	O
ATOM	4882	C	SER	H	85	−80.736	−15.325	4.686	1.00	86.64	C
ATOM	4883	O	SER	H	85	−81.513	−14.367	4.769	1.00	86.92	O
ATOM	4884	N	LEU	H	86	−80.904	−16.326	3.804	1.00	83.88	N
ATOM	4885	CA	LEU	H	86	−81.992	−16.360	2.828	1.00	83.85	C
ATOM	4886	CB	LEU	H	86	−81.655	−17.283	1.646	1.00	83.52	C
ATOM	4887	CG	LEU	H	86	−80.321	−17.018	0.942	1.00	82.64	C
ATOM	4888	CD1	LEU	H	86	−79.953	−18.143	0.069	1.00	80.79	C
ATOM	4889	CD2	LEU	H	86	−80.341	−15.740	0.154	1.00	82.74	C
ATOM	4890	C	LEU	H	86	−83.391	−16.631	3.388	1.00	84.25	C
ATOM	4891	O	LEU	H	86	−83.540	−17.250	4.432	1.00	84.08	O
ATOM	4892	N	ARG	H	87	−84.408	−16.117	2.692	1.00	87.49	N
ATOM	4893	CA	ARG	H	87	−85.833	−16.239	2.996	1.00	87.95	C
ATOM	4894	CB	ARG	H	87	−86.424	−14.875	3.359	1.00	88.25	C
ATOM	4895	CG	ARG	H	87	−85.590	−14.081	4.356	1.00	90.00	C
ATOM	4896	CD	ARG	H	87	−86.349	−12.904	4.913	1.00	93.13	C
ATOM	4897	NE	ARG	H	87	−86.517	−11.838	3.924	1.00	95.49	N
ATOM	4898	CZ	ARG	H	87	−86.363	−10.540	4.182	1.00	97.17	C
ATOM	4899	NH1	ARG	H	87	−86.542	−9.639	3.220	1.00	97.17	N
ATOM	4900	NH2	ARG	H	87	−86.028	−10.132	5.406	1.00	98.62	N
ATOM	4901	C	ARG	H	87	−86.476	−16.753	1.724	1.00	87.88	C
ATOM	4902	O	ARG	H	87	−85.829	−16.724	0.680	1.00	88.02	O
ATOM	4903	N	ALA	H	88	−87.727	−17.223	1.777	1.00	89.65	N
ATOM	4904	CA	ALA	H	88	−88.388	−17.752	0.580	1.00	89.55	C
ATOM	4905	CB	ALA	H	88	−89.723	−18.371	0.940	1.00	89.60	C
ATOM	4906	C	ALA	H	88	−88.531	−16.737	−0.573	1.00	89.59	C
ATOM	4907	O	ALA	H	88	−88.712	−17.146	−1.719	1.00	89.56	O
ATOM	4908	N	GLU	H	89	−88.407	−15.422	−0.274	1.00	92.07	N
ATOM	4909	CA	GLU	H	89	−88.474	−14.325	−1.253	1.00	91.99	C
ATOM	4910	CB	GLU	H	89	−88.520	−12.960	−0.564	1.00	92.37	C
ATOM	4911	CG	GLU	H	89	−89.657	−12.783	0.418	1.00	95.67	C
ATOM	4912	CD	GLU	H	89	−89.184	−12.521	1.834	1.00	100.06	C
ATOM	4913	OE1	GLU	H	89	−89.344	−13.430	2.688	1.00	101.77	O
ATOM	4914	OE2	GLU	H	89	−88.648	−11.411	2.085	1.00	101.51	O
ATOM	4915	C	GLU	H	89	−87.246	−14.337	−2.146	1.00	91.13	C
ATOM	4916	O	GLU	H	89	−87.320	−13.892	−3.296	1.00	91.47	O
ATOM	4917	N	ASP	H	90	−86.105	−14.827	−1.614	1.00	88.34	N
ATOM	4918	CA	ASP	H	90	−84.853	−14.908	−2.353	1.00	86.96	C
ATOM	4919	CB	ASP	H	90	−83.650	−14.902	−1.408	1.00	87.15	C
ATOM	4920	CG	ASP	H	90	−83.592	−13.651	−0.532	1.00	88.39	C
ATOM	4921	OD1	ASP	H	90	−83.867	−12.532	−1.056	1.00	89.29	O
ATOM	4922	OD2	ASP	H	90	−83.279	−13.783	0.679	1.00	90.20	O
ATOM	4923	C	ASP	H	90	−84.831	−16.019	−3.410	1.00	85.83	C
ATOM	4924	O	ASP	H	90	−83.819	−16.208	−4.082	1.00	85.71	O
ATOM	4925	N	THR	H	91	−85.976	−16.717	−3.596	1.00	81.43	N
ATOM	4926	CA	THR	H	91	−86.138	−17.750	−4.618	1.00	79.99	C
ATOM	4927	CB	THR	H	91	−87.349	−18.647	−4.339	1.00	80.13	C
ATOM	4928	OG1	THR	H	91	−87.316	−19.113	−2.991	1.00	80.98	O
ATOM	4929	CG2	THR	H	91	−87.457	−19.804	−5.322	1.00	78.80	C
ATOM	4930	C	THR	H	91	−86.352	−17.032	−5.938	1.00	78.71	C
ATOM	4931	O	THR	H	91	−87.298	−16.237	−6.059	1.00	78.84	O
ATOM	4932	N	ALA	H	92	−85.475	−17.309	−6.914	1.00	73.98	N
ATOM	4933	CA	ALA	H	92	−85.505	−16.731	−8.254	1.00	72.60	C
ATOM	4934	CB	ALA	H	92	−85.247	−15.231	−8.182	1.00	72.66	C
ATOM	4935	C	ALA	H	92	−84.441	−17.367	−9.120	1.00	71.70	C
ATOM	4936	O	ALA	H	92	−83.702	−18.250	−8.682	1.00	72.05	O
ATOM	4937	N	VAL	H	93	−84.360	−16.903	−10.361	1.00	68.26	N
ATOM	4938	CA	VAL	H	93	−83.351	−17.341	−11.306	1.00	66.99	C
ATOM	4939	CB	VAL	H	93	−83.925	−17.581	−12.704	1.00	66.60	C
ATOM	4940	CG1	VAL	H	93	−82.815	−17.806	−13.705	1.00	66.29	C
ATOM	4941	CG2	VAL	H	93	−84.839	−18.779	−12.672	1.00	65.83	C
ATOM	4942	C	VAL	H	93	−82.247	−16.264	−11.243	1.00	66.74	C
ATOM	4943	O	VAL	H	93	−82.529	−15.062	−11.295	1.00	66.88	O
ATOM	4944	N	TYR	H	94	−81.015	−16.707	−11.080	1.00	65.99	N
ATOM	4945	CA	TYR	H	94	−79.873	−15.853	−10.929	1.00	64.93	C
ATOM	4946	CB	TYR	H	94	−79.072	−16.318	−9.710	1.00	65.01	C
ATOM	4947	CG	TYR	H	94	−79.755	−15.960	−8.407	1.00	65.23	C
ATOM	4948	CD1	TYR	H	94	−79.333	−14.870	−7.655	1.00	64.68	C
ATOM	4949	CE1	TYR	H	94	−79.985	−14.506	−6.480	1.00	64.28	C
ATOM	4950	CZ	TYR	H	94	−81.081	−15.233	−6.046	1.00	64.51	C
ATOM	4951	OH	TYR	H	94	−81.723	−14.863	−4.893	1.00	65.03	O
ATOM	4952	CE2	TYR	H	94	−81.526	−16.321	−6.779	1.00	64.86	C
ATOM	4953	CD2	TYR	H	94	−80.859	−16.683	−7.948	1.00	65.33	C
ATOM	4954	C	TYR	H	94	−79.051	−15.838	−12.178	1.00	64.74	C
ATOM	4955	O	TYR	H	94	−78.686	−16.889	−12.708	1.00	64.40	O
ATOM	4956	N	TYR	H	95	−78.764	−14.622	−12.658	1.00	63.64	N
ATOM	4957	CA	TYR	H	95	−77.994	−14.382	−13.859	1.00	63.12	C
ATOM	4958	CB	TYR	H	95	−78.812	−13.503	−14.829	1.00	62.92	C
ATOM	4959	CG	TYR	H	95	−80.064	−14.156	−15.365	1.00	61.93	C
ATOM	4960	CD1	TYR	H	95	−80.006	−15.057	−16.429	1.00	61.03	C
ATOM	4961	CE1	TYR	H	95	−81.152	−15.685	−16.905	1.00	61.11	C
ATOM	4962	CZ	TYR	H	95	−82.384	−15.383	−16.346	1.00	61.42	C
ATOM	4963	OH	TYR	H	95	−83.528	−15.996	−16.814	1.00	61.35	O
ATOM	4964	CE2	TYR	H	95	−82.467	−14.466	−15.309	1.00	60.44	C
ATOM	4965	CD2	TYR	H	95	−81.309	−13.863	−14.824	1.00	60.20	C
ATOM	4966	C	TYR	H	95	−76.738	−13.643	−13.582	1.00	63.30	C
ATOM	4967	O	TYR	H	95	−76.719	−12.802	−12.701	1.00	63.44	O
ATOM	4968	N	CYS	H	96	−75.701	−13.910	−14.359	1.00	67.44	N
ATOM	4969	CA	CYS	H	96	−74.483	−13.120	−14.364	1.00	68.48	C
ATOM	4970	CB	CYS	H	96	−73.190	−13.894	−14.097	1.00	68.59	C
ATOM	4971	SG	CYS	H	96	−72.852	−15.230	−15.268	1.00	73.30	S
ATOM	4972	C	CYS	H	96	−74.556	−12.530	−15.791	1.00	68.14	C
ATOM	4973	O	CYS	H	96	−75.032	−13.201	−16.720	1.00	68.02	O
ATOM	4974	N	ALA	H	97	−74.221	−11.241	−15.927	1.00	67.03	N
ATOM	4975	CA	ALA	H	97	−74.282	−10.541	−17.191	1.00	66.44	C
ATOM	4976	CB	ALA	H	97	−75.520	−9.668	−17.251	1.00	66.41	C
ATOM	4977	C	ALA	H	97	−73.063	−9.706	−17.338	1.00	66.28	C
ATOM	4978	O	ALA	H	97	−72.676	−8.995	−16.413	1.00	66.42	O
ATOM	4979	N	ARG	H	98	−72.447	−9.788	−18.500	1.00	65.71	N
ATOM	4980	CA	ARG	H	98	−71.268	−9.014	−18.822	1.00	65.78	C
ATOM	4981	CB	ARG	H	98	−70.573	−9.689	−19.983	1.00	65.49	C
ATOM	4982	CG	ARG	H	98	−69.167	−9.269	−20.286	1.00	62.95	C
ATOM	4983	CD	ARG	H	98	−69.244	−9.112	−21.758	1.00	60.25	C
ATOM	4984	NE	ARG	H	98	−68.042	−9.526	−22.443	1.00	59.34	N
ATOM	4985	CZ	ARG	H	98	−67.847	−9.378	−23.752	1.00	59.47	C
ATOM	4986	NH1	ARG	H	98	−68.779	−8.817	−24.511	1.00	57.40	N
ATOM	4987	NH2	ARG	H	98	−66.713	−9.776	−24.306	1.00	59.29	N
ATOM	4988	C	ARG	H	98	−71.754	−7.628	−19.209	1.00	66.54	C
ATOM	4989	O	ARG	H	98	−72.796	−7.506	−19.850	1.00	66.86	O
ATOM	4990	N	GLU	H	99	−71.022	−6.582	−18.789	1.00	70.53	N
ATOM	4991	CA	GLU	H	99	−71.356	−5.177	−19.043	1.00	71.00	C
ATOM	4992	CB	GLU	H	99	−71.418	−4.405	−17.703	1.00	70.96	C
ATOM	4993	CG	GLU	H	99	−71.527	−2.885	−17.795	1.00	72.27	C
ATOM	4994	CD	GLU	H	99	−71.137	−2.115	−16.540	1.00	74.67	C
ATOM	4995	OE1	GLU	H	99	−71.774	−1.072	−16.248	1.00	75.05	O
ATOM	4996	OE2	GLU	H	99	−70.195	−2.560	−15.841	1.00	75.63	O
ATOM	4997	C	GLU	H	99	−70.333	−4.548	−19.946	1.00	71.25	C
ATOM	4998	O	GLU	H	99	−69.143	−4.641	−19.659	1.00	71.38	O
ATOM	4999	N	ARG	H	100	−70.792	−3.911	−21.039	1.00	72.41	N
ATOM	5000	CA	ARG	H	100	−69.919	−3.163	−21.943	1.00	72.84	C
ATOM	5001	CB	ARG	H	100	−70.354	−3.224	−23.414	1.00	72.83	C
ATOM	5002	CG	ARG	H	100	−69.329	−2.517	−24.278	1.00	72.50	C
ATOM	5003	CD	ARG	H	100	−69.664	−2.380	−25.740	1.00	72.55	C
ATOM	5004	NE	ARG	H	100	−68.761	−1.403	−26.352	1.00	73.88	N
ATOM	5005	CZ	ARG	H	100	−68.848	−0.952	−27.601	1.00	74.27	C
ATOM	5006	NH1	ARG	H	100	−69.805	−1.397	−28.413	1.00	73.63	N
ATOM	5007	NH2	ARG	H	100	−67.977	−0.057	−28.049	1.00	74.01	N
ATOM	5008	C	ARG	H	100	−70.093	−1.768	−21.397	1.00	73.26	C
ATOM	5009	O	ARG	H	100	−71.149	−1.165	−21.573	1.00	73.35	O
ATOM	5010	N	TYR	H	101	−69.107	−1.285	−20.662	1.00	75.23	N
ATOM	5011	CA	TYR	H	101	−69.181	0.023	−20.022	1.00	75.75	C
ATOM	5012	CB	TYR	H	101	−67.837	0.402	−19.426	1.00	76.28	C
ATOM	5013	CG	TYR	H	101	−67.339	−0.535	−18.344	1.00	79.85	C
ATOM	5014	CD1	TYR	H	101	−66.172	−1.282	−18.522	1.00	82.83	C
ATOM	5015	CE1	TYR	H	101	−65.661	−2.084	−17.502	1.00	84.43	C
ATOM	5016	CZ	TYR	H	101	−66.329	−2.162	−16.288	1.00	85.43	C
ATOM	5017	OH	TYR	H	101	−65.820	−2.948	−15.284	1.00	86.44	O
ATOM	5018	CE2	TYR	H	101	−67.496	−1.437	−16.089	1.00	84.58	C
ATOM	5019	CD2	TYR	H	101	−67.992	−0.626	−17.113	1.00	82.47	C
ATOM	5020	C	TYR	H	101	−69.764	1.160	−20.866	1.00	74.82	C
ATOM	5021	O	TYR	H	101	−69.277	1.443	−21.961	1.00	74.74	O
ATOM	5022	N	GLY	H	102	−70.823	1.772	−20.346	1.00	71.45	N
ATOM	5023	CA	GLY	H	102	−71.510	2.890	−20.985	1.00	70.66	C
ATOM	5024	C	GLY	H	102	−72.424	2.481	−22.117	1.00	70.17	C
ATOM	5025	O	GLY	H	102	−73.112	3.327	−22.700	1.00	70.31	O
ATOM	5026	N	TYR	H	103	−72.451	1.166	−22.417	1.00	67.53	N
ATOM	5027	CA	TYR	H	103	−73.238	0.609	−23.497	1.00	66.65	C
ATOM	5028	CB	TYR	H	103	−72.334	−0.117	−24.495	1.00	66.73	C
ATOM	5029	CG	TYR	H	103	−71.616	0.826	−25.428	1.00	67.87	C
ATOM	5030	CD1	TYR	H	103	−72.107	1.082	−26.705	1.00	68.67	C
ATOM	5031	CE1	TYR	H	103	−71.450	1.956	−27.571	1.00	67.79	C
ATOM	5032	CZ	TYR	H	103	−70.303	2.604	−27.151	1.00	67.83	C
ATOM	5033	OH	TYR	H	103	−69.666	3.479	−27.994	1.00	69.69	O
ATOM	5034	CE2	TYR	H	103	−69.808	2.381	−25.877	1.00	67.02	C
ATOM	5035	CD2	TYR	H	103	−70.454	1.481	−25.032	1.00	67.47	C
ATOM	5036	C	TYR	H	103	−74.426	−0.225	−23.116	1.00	65.83	C
ATOM	5037	O	TYR	H	103	−75.530	0.291	−23.102	1.00	65.67	O
ATOM	5038	N	TYR	H	104	−74.219	−1.512	−22.833	1.00	63.53	N
ATOM	5039	CA	TYR	H	104	−75.274	−2.500	−22.568	1.00	62.64	C
ATOM	5040	CB	TYR	H	104	−75.902	−2.908	−23.950	1.00	62.17	C
ATOM	5041	CG	TYR	H	104	−74.866	−3.054	−25.055	1.00	61.14	C
ATOM	5042	CD1	TYR	H	104	−73.904	−4.065	−25.013	1.00	61.33	C
ATOM	5043	CE1	TYR	H	104	−72.921	−4.175	−25.999	1.00	60.48	C
ATOM	5044	CZ	TYR	H	104	−72.888	−3.265	−27.041	1.00	58.82	C
ATOM	5045	OH	TYR	H	104	−71.911	−3.370	−28.007	1.00	56.93	O
ATOM	5046	CE2	TYR	H	104	−73.833	−2.249	−27.097	1.00	59.35	C
ATOM	5047	CD2	TYR	H	104	−74.813	−2.153	−26.109	1.00	60.02	C
ATOM	5048	C	TYR	H	104	−74.712	−3.786	−21.964	1.00	62.35	C
ATOM	5049	O	TYR	H	104	−73.491	−3.944	−21.821	1.00	62.32	O
ATOM	5050	N	PHE	H	105	−75.626	−4.738	−21.697	1.00	60.95	N
ATOM	5051	CA	PHE	H	105	−75.321	−6.081	−21.233	1.00	60.08	C
ATOM	5052	CB	PHE	H	105	−76.422	−6.581	−20.308	1.00	59.40	C
ATOM	5053	CG	PHE	H	105	−76.500	−5.899	−18.968	1.00	58.42	C
ATOM	5054	CD1	PHE	H	105	−77.665	−5.252	−18.564	1.00	56.91	C
ATOM	5055	CE1	PHE	H	105	−77.752	−4.655	−17.301	1.00	56.33	C
ATOM	5056	CZ	PHE	H	105	−76.677	−4.698	−16.441	1.00	56.75	C
ATOM	5057	CE2	PHE	H	105	−75.519	−5.337	−16.822	1.00	57.86	C
ATOM	5058	CD2	PHE	H	105	−75.432	−5.951	−18.079	1.00	57.85	C
ATOM	5059	C	PHE	H	105	−75.312	−6.912	−22.504	1.00	60.10	C
ATOM	5060	O	PHE	H	105	−76.378	−7.137	−23.084	1.00	60.18	O
ATOM	5061	N	ASP	H	106	−74.139	−7.310	−22.982	1.00	62.16	N
ATOM	5062	CA	ASP	H	106	−74.102	−8.089	−24.215	1.00	63.03	C
ATOM	5063	CB	ASP	H	106	−72.863	−7.804	−25.072	1.00	63.28	C
ATOM	5064	CG	ASP	H	106	−71.598	−7.570	−24.296	1.00	65.40	C
ATOM	5065	OD1	ASP	H	106	−71.564	−7.925	−23.086	1.00	67.53	O
ATOM	5066	OD2	ASP	H	106	−70.634	−7.024	−24.887	1.00	66.52	O
ATOM	5067	C	ASP	H	106	−74.312	−9.586	−24.020	1.00	63.00	C
ATOM	5068	O	ASP	H	106	−75.097	−10.196	−24.752	1.00	63.66	O
ATOM	5069	N	TYR	H	107	−73.647	−10.168	−23.027	1.00	62.37	N
ATOM	5070	CA	TYR	H	107	−73.737	−11.583	−22.724	1.00	62.23	C
ATOM	5071	CB	TYR	H	107	−72.371	−12.194	−22.904	1.00	62.04	C
ATOM	5072	CG	TYR	H	107	−71.963	−12.148	−24.360	1.00	61.88	C
ATOM	5073	CD1	TYR	H	107	−72.543	−13.003	−25.290	1.00	61.17	C
ATOM	5074	CE1	TYR	H	107	−72.181	−12.969	−26.629	1.00	61.06	C
ATOM	5075	CZ	TYR	H	107	−71.227	−12.071	−27.061	1.00	61.23	C
ATOM	5076	OH	TYR	H	107	−70.917	−12.079	−28.399	1.00	61.91	O
ATOM	5077	CE2	TYR	H	107	−70.647	−11.186	−26.160	1.00	61.81	C
ATOM	5078	CD2	TYR	H	107	−71.025	−11.223	−24.818	1.00	62.31	C
ATOM	5079	C	TYR	H	107	−74.322	−11.875	−21.359	1.00	62.66	C
ATOM	5080	O	TYR	H	107	−74.063	−11.130	−20.410	1.00	62.89	O
ATOM	5081	N	TRP	H	108	−75.144	−12.946	−21.268	1.00	63.37	N
ATOM	5082	CA	TRP	H	108	−75.808	−13.377	−20.032	1.00	63.55	C
ATOM	5083	CB	TRP	H	108	−77.321	−13.169	−20.130	1.00	63.40	C
ATOM	5084	CG	TRP	H	108	−77.792	−11.753	−20.274	1.00	63.22	C
ATOM	5085	CD1	TRP	H	108	−77.723	−10.970	−21.390	1.00	63.42	C
ATOM	5086	NE1	TRP	H	108	−78.324	−9.757	−21.155	1.00	63.16	N
ATOM	5087	CE2	TRP	H	108	−78.811	−9.742	−19.873	1.00	61.71	C
ATOM	5088	CD2	TRP	H	108	−78.521	−10.999	−19.298	1.00	62.25	C
ATOM	5089	CE3	TRP	H	108	−78.912	−11.245	−17.974	1.00	61.41	C
ATOM	5090	CZ3	TRP	H	108	−79.556	−10.244	−17.279	1.00	62.45	C
ATOM	5091	CH2	TRP	H	108	−79.838	−9.007	−17.880	1.00	61.71	C
ATOM	5092	CZ2	TRP	H	108	−79.478	−8.738	−19.173	1.00	60.73	C
ATOM	5093	C	TRP	H	108	−75.560	−14.857	−19.782	1.00	64.14	C
ATOM	5094	O	TRP	H	108	−75.353	−15.610	−20.730	1.00	64.01	O
ATOM	5095	N	GLY	H	109	−75.600	−15.271	−18.519	1.00	66.93	N
ATOM	5096	CA	GLY	H	109	−75.436	−16.674	−18.144	1.00	67.80	C
ATOM	5097	C	GLY	H	109	−76.725	−17.385	−18.497	1.00	68.72	C
ATOM	5098	O	GLY	H	109	−77.722	−16.721	−18.806	1.00	68.99	O
ATOM	5099	N	GLN	H	110	−76.726	−18.726	−18.483	1.00	71.11	N
ATOM	5100	CA	GLN	H	110	−77.903	−19.541	−18.838	1.00	71.79	C
ATOM	5101	CB	GLN	H	110	−77.539	−21.035	−18.947	1.00	72.34	C
ATOM	5102	CG	GLN	H	110	−77.089	−21.720	−17.625	1.00	75.60	C
ATOM	5103	CD	GLN	H	110	−75.597	−21.586	−17.254	1.00	80.03	C
ATOM	5104	OE1	GLN	H	110	−74.927	−20.544	−17.468	1.00	81.28	O
ATOM	5105	NE2	GLN	H	110	−75.050	−22.650	−16.662	1.00	80.71	N
ATOM	5106	C	GLN	H	110	−79.129	−19.331	−17.951	1.00	71.61	C
ATOM	5107	O	GLN	H	110	−80.256	−19.487	−18.415	1.00	71.64	O
ATOM	5108	N	GLY	H	111	−78.888	−18.964	−16.700	1.00	69.26	N
ATOM	5109	CA	GLY	H	111	−79.910	−18.755	−15.687	1.00	69.55	C
ATOM	5110	C	GLY	H	111	−79.862	−19.902	−14.703	1.00	69.85	C
ATOM	5111	O	GLY	H	111	−80.013	−21.050	−15.114	1.00	70.20	O
ATOM	5112	N	THR	H	112	−79.605	−19.619	−13.410	1.00	67.06	N
ATOM	5113	CA	THR	H	112	−79.543	−20.649	−12.355	1.00	66.93	C
ATOM	5114	CB	THR	H	112	−78.146	−20.856	−11.717	1.00	66.96	C
ATOM	5115	OG1	THR	H	112	−77.302	−19.782	−12.092	1.00	68.20	O
ATOM	5116	CG2	THR	H	112	−77.479	−22.189	−12.133	1.00	67.65	C
ATOM	5117	C	THR	H	112	−80.638	−20.458	−11.341	1.00	66.57	C
ATOM	5118	O	THR	H	112	−80.784	−19.391	−10.759	1.00	66.47	O
ATOM	5119	N	LEU	H	113	−81.422	−21.502	−11.140	1.00	66.57	N
ATOM	5120	CA	LEU	H	113	−82.509	−21.442	−10.191	1.00	66.09	C
ATOM	5121	CB	LEU	H	113	−83.640	−22.395	−10.589	1.00	65.95	C
ATOM	5122	CG	LEU	H	113	−84.753	−22.495	−9.569	1.00	66.57	C
ATOM	5123	CD1	LEU	H	113	−85.585	−21.204	−9.506	1.00	65.93	C
ATOM	5124	CD2	LEU	H	113	−85.578	−23.706	−9.806	1.00	67.95	C
ATOM	5125	C	LEU	H	113	−82.033	−21.766	−8.794	1.00	65.67	C
ATOM	5126	O	LEU	H	113	−81.336	−22.771	−8.593	1.00	65.82	O
ATOM	5127	N	VAL	H	114	−82.422	−20.921	−7.836	1.00	62.65	N
ATOM	5128	CA	VAL	H	114	−82.107	−21.118	−6.438	1.00	62.66	C
ATOM	5129	CB	VAL	H	114	−81.151	−20.031	−5.865	1.00	62.38	C
ATOM	5130	CG1	VAL	H	114	−81.011	−20.153	−4.352	1.00	61.88	C
ATOM	5131	CG2	VAL	H	114	−79.779	−20.090	−6.514	1.00	62.63	C
ATOM	5132	C	VAL	H	114	−83.477	−21.141	−5.743	1.00	63.09	C
ATOM	5133	O	VAL	H	114	−84.211	−20.145	−5.793	1.00	62.87	O
ATOM	5134	N	THR	H	115	−83.835	−22.298	−5.138	1.00	66.30	N
ATOM	5135	CA	THR	H	115	−85.096	−22.454	−4.406	1.00	66.71	C
ATOM	5136	CB	THR	H	115	−86.002	−23.586	−4.957	1.00	66.71	C
ATOM	5137	OG1	THR	H	115	−86.136	−23.455	−6.375	1.00	65.99	O
ATOM	5138	CG2	THR	H	115	−87.399	−23.542	−4.358	1.00	66.36	C
ATOM	5139	C	THR	H	115	−84.799	−22.474	−2.911	1.00	67.37	C
ATOM	5140	O	THR	H	115	−83.917	−23.222	−2.441	1.00	67.19	O
ATOM	5141	N	VAL	H	116	−85.518	−21.615	−2.178	1.00	70.14	N
ATOM	5142	CA	VAL	H	116	−85.344	−21.459	−0.735	1.00	71.22	C
ATOM	5143	CB	VAL	H	116	−85.010	−19.986	−0.351	1.00	71.13	C
ATOM	5144	CG1	VAL	H	116	−83.751	−19.498	−1.085	1.00	71.19	C
ATOM	5145	CG2	VAL	H	116	−84.834	−19.835	1.150	1.00	71.12	C
ATOM	5146	C	VAL	H	116	−86.503	−22.093	0.058	1.00	71.93	C
ATOM	5147	O	VAL	H	116	−87.568	−21.501	0.188	1.00	72.15	O
ATOM	5148	N	SER	H	117	−86.281	−23.311	0.571	1.00	75.85	N
ATOM	5149	CA	SER	H	117	−87.269	−24.072	1.325	1.00	76.81	C
ATOM	5150	CB	SER	H	117	−88.179	−24.851	0.378	1.00	76.95	C
ATOM	5151	OG	SER	H	117	−89.002	−25.799	1.043	1.00	77.25	O
ATOM	5152	C	SER	H	117	−86.648	−25.048	2.307	1.00	77.41	C
ATOM	5153	O	SER	H	117	−85.645	−25.715	2.005	1.00	77.73	O
ATOM	5154	N	SER	H	118	−87.311	−25.159	3.476	1.00	79.00	N
ATOM	5155	CA	SER	H	118	−86.988	−26.050	4.599	1.00	79.39	C
ATOM	5156	CB	SER	H	118	−87.461	−25.432	5.911	1.00	79.16	C
ATOM	5157	OG	SER	H	118	−88.754	−24.877	5.731	1.00	80.04	O
ATOM	5158	C	SER	H	118	−87.660	−27.426	4.387	1.00	79.64	C
ATOM	5159	O	SER	H	118	−87.480	−28.330	5.218	1.00	80.15	O
ATOM	5160	N	ALA	H	119	−88.417	−27.587	3.266	1.00	73.07	N
ATOM	5161	CA	ALA	H	119	−89.074	−28.836	2.926	1.00	72.98	C
ATOM	5162	CB	ALA	H	119	−90.050	−28.632	1.784	1.00	73.09	C
ATOM	5163	C	ALA	H	119	−88.066	−29.956	2.607	1.00	73.10	C
ATOM	5164	O	ALA	H	119	−86.893	−29.696	2.305	1.00	72.72	O
ATOM	5165	N	SER	H	120	−88.550	−31.209	2.716	1.00	72.01	N
ATOM	5166	CA	SER	H	120	−87.807	−32.453	2.522	1.00	72.04	C
ATOM	5167	CB	SER	H	120	−87.893	−33.299	3.782	1.00	71.83	C
ATOM	5168	OG	SER	H	120	−87.997	−32.449	4.913	1.00	72.64	O
ATOM	5169	C	SER	H	120	−88.343	−33.239	1.343	1.00	72.00	C
ATOM	5170	O	SER	H	120	−89.547	−33.176	1.060	1.00	71.77	O
ATOM	5171	N	THR	H	121	−87.434	−33.976	0.654	1.00	70.38	N
ATOM	5172	CA	THR	H	121	−87.764	−34.779	−0.515	1.00	70.68	C
ATOM	5173	CB	THR	H	121	−86.523	−35.458	−1.138	1.00	70.30	C
ATOM	5174	OG1	THR	H	121	−85.504	−34.491	−1.375	1.00	69.93	O
ATOM	5175	CG2	THR	H	121	−86.829	−36.146	−2.451	1.00	69.49	C
ATOM	5176	C	THR	H	121	−88.901	−35.717	−0.151	1.00	71.62	C
ATOM	5177	O	THR	H	121	−88.827	−36.431	0.851	1.00	72.00	O
ATOM	5178	N	LYS	H	122	−89.972	−35.653	−0.936	1.00	72.71	N
ATOM	5179	CA	LYS	H	122	−91.168	−36.441	−0.774	1.00	73.30	C
ATOM	5180	CB	LYS	H	122	−92.131	−35.708	0.189	1.00	73.06	C
ATOM	5181	CG	LYS	H	122	−93.643	−35.827	−0.089	1.00	73.63	C
ATOM	5182	CD	LYS	H	122	−94.355	−36.996	0.603	1.00	73.39	C
ATOM	5183	CE	LYS	H	122	−95.860	−36.793	0.652	1.00	73.30	C
ATOM	5184	NZ	LYS	H	122	−96.591	−37.550	−0.418	1.00	74.03	N
ATOM	5185	C	LYS	H	122	−91.754	−36.731	−2.177	1.00	74.13	C
ATOM	5186	O	LYS	H	122	−91.985	−35.802	−2.956	1.00	74.29	O
ATOM	5187	N	GLY	H	123	−91.933	−38.022	−2.490	1.00	76.46	N
ATOM	5188	CA	GLY	H	123	−92.503	−38.498	−3.745	1.00	77.46	C
ATOM	5189	C	GLY	H	123	−93.959	−38.081	−3.787	1.00	78.54	C
ATOM	5190	O	GLY	H	123	−94.538	−37.830	−2.723	1.00	78.57	O
ATOM	5191	N	PRO	H	124	−94.605	−37.960	−4.972	1.00	80.93	N
ATOM	5192	CA	PRO	H	124	−96.000	−37.518	−4.987	1.00	81.90	C
ATOM	5193	CB	PRO	H	124	−96.172	−37.027	−6.418	1.00	81.54	C
ATOM	5194	CG	PRO	H	124	−95.326	−37.916	−7.208	1.00	80.73	C
ATOM	5195	CD	PRO	H	124	−94.124	−38.210	−6.346	1.00	80.84	C
ATOM	5196	C	PRO	H	124	−97.007	−38.620	−4.701	1.00	83.35	C
ATOM	5197	O	PRO	H	124	−96.687	−39.819	−4.762	1.00	83.63	O
ATOM	5198	N	SER	H	125	−98.240	−38.183	−4.426	1.00	86.85	N
ATOM	5199	CA	SER	H	125	−99.417	−39.010	−4.201	1.00	88.24	C
ATOM	5200	CB	SER	H	125	−100.136	−38.587	−2.915	1.00	88.05	C
ATOM	5201	OG	SER	H	125	−99.245	−38.444	−1.816	1.00	88.30	O
ATOM	5202	C	SER	H	125	−100.277	−38.707	−5.446	1.00	89.31	C
ATOM	5203	O	SER	H	125	−100.723	−37.571	−5.615	1.00	89.76	O
ATOM	5204	N	VAL	H	126	−100.456	−39.694	−6.343	1.00	90.66	N
ATOM	5205	CA	VAL	H	126	−101.241	−39.522	−7.578	1.00	91.88	C
ATOM	5206	CB	VAL	H	126	−100.536	−40.090	−8.832	1.00	91.55	C
ATOM	5207	CG1	VAL	H	126	−101.344	−39.818	−10.089	1.00	91.30	C
ATOM	5208	CG2	VAL	H	126	−99.146	−39.507	−8.971	1.00	91.37	C
ATOM	5209	C	VAL	H	126	−102.703	−39.986	−7.448	1.00	93.21	C
ATOM	5210	O	VAL	H	126	−102.989	−41.177	−7.310	1.00	93.26	O
ATOM	5211	N	PHE	H	127	−103.619	−39.023	−7.514	1.00	97.08	N
ATOM	5212	CA	PHE	H	127	−105.053	−39.266	−7.430	1.00	98.63	C
ATOM	5213	CB	PHE	H	127	−105.664	−38.352	−6.381	1.00	98.32	C
ATOM	5214	CG	PHE	H	127	−105.044	−38.479	−5.018	1.00	98.24	C
ATOM	5215	CD1	PHE	H	127	−104.950	−39.715	−4.392	1.00	97.94	C
ATOM	5216	CE1	PHE	H	127	−104.411	−39.829	−3.112	1.00	98.10	C
ATOM	5217	CZ	PHE	H	127	−103.972	−38.708	−2.451	1.00	98.37	C
ATOM	5218	CE2	PHE	H	127	−104.059	−37.473	−3.056	1.00	98.37	C
ATOM	5219	CD2	PHE	H	127	−104.590	−37.361	−4.340	1.00	97.97	C
ATOM	5220	C	PHE	H	127	−105.733	−39.022	−8.783	1.00	100.17	C
ATOM	5221	O	PHE	H	127	−105.388	−38.041	−9.446	1.00	100.19	O
ATOM	5222	N	PRO	H	128	−106.701	−39.871	−9.224	1.00	105.15	N
ATOM	5223	CA	PRO	H	128	−107.348	−39.619	−10.525	1.00	106.35	C
ATOM	5224	CB	PRO	H	128	−108.033	−40.949	−10.828	1.00	106.09	C
ATOM	5225	CG	PRO	H	128	−108.388	−41.479	−9.482	1.00	105.49	C
ATOM	5226	CD	PRO	H	128	−107.246	−41.088	−8.584	1.00	105.11	C
ATOM	5227	C	PRO	H	128	−108.372	−38.485	−10.473	1.00	107.79	C
ATOM	5228	O	PRO	H	128	−108.853	−38.108	−9.396	1.00	108.04	O
ATOM	5229	N	LEU	H	129	−108.703	−37.948	−11.649	1.00	110.12	N
ATOM	5230	CA	LEU	H	129	−109.708	−36.904	−11.827	1.00	111.66	C
ATOM	5231	CB	LEU	H	129	−109.089	−35.597	−12.368	1.00	111.44	C
ATOM	5232	CG	LEU	H	129	−108.038	−34.916	−11.497	1.00	110.89	C
ATOM	5233	CD1	LEU	H	129	−107.266	−33.891	−12.296	1.00	110.21	C
ATOM	5234	CD2	LEU	H	129	−108.651	−34.321	−10.217	1.00	109.59	C
ATOM	5235	C	LEU	H	129	−110.686	−37.551	−12.809	1.00	112.94	C
ATOM	5236	O	LEU	H	129	−110.593	−37.359	−14.028	1.00	113.16	O
ATOM	5237	N	ALA	H	130	−111.573	−38.399	−12.242	1.00	116.25	N
ATOM	5238	CA	ALA	H	130	−112.592	−39.223	−12.898	1.00	117.58	C
ATOM	5239	CB	ALA	H	130	−113.404	−39.975	−11.851	1.00	117.55	C
ATOM	5240	C	ALA	H	130	−113.530	−38.511	−13.889	1.00	118.57	C
ATOM	5241	O	ALA	H	130	−114.213	−37.554	−13.498	1.00	118.42	O
ATOM	5242	N	PRO	H	131	−113.593	−38.985	−15.168	1.00	122.13	N
ATOM	5243	CA	PRO	H	131	−114.505	−38.351	−16.137	1.00	123.31	C
ATOM	5244	CB	PRO	H	131	−114.164	−39.038	−17.468	1.00	123.07	C
ATOM	5245	CG	PRO	H	131	−113.532	−40.323	−17.098	1.00	122.46	C
ATOM	5246	CD	PRO	H	131	−112.864	−40.124	−15.769	1.00	122.18	C
ATOM	5247	C	PRO	H	131	−115.957	−38.570	−15.707	1.00	124.68	C
ATOM	5248	O	PRO	H	131	−116.427	−39.716	−15.642	1.00	125.03	O
ATOM	5249	N	SER	H	132	−116.648	−37.466	−15.356	1.00	128.46	N
ATOM	5250	CA	SER	H	132	−118.036	−37.475	−14.896	1.00	129.79	C
ATOM	5251	CB	SER	H	132	−118.581	−36.055	−14.767	1.00	129.75	C
ATOM	5252	OG	SER	H	132	−118.974	−35.502	−16.015	1.00	129.83	O
ATOM	5253	C	SER	H	132	−118.948	−38.294	−15.792	1.00	130.80	C
ATOM	5254	O	SER	H	132	−118.817	−38.263	−17.026	1.00	130.81	O
ATOM	5255	N	SER	H	133	−119.871	−39.028	−15.145	1.00	135.47	N
ATOM	5256	CA	SER	H	133	−120.893	−39.875	−15.765	1.00	136.57	C
ATOM	5257	CB	SER	H	133	−121.600	−40.707	−14.693	1.00	136.61	C
ATOM	5258	OG	SER	H	133	−120.690	−41.259	−13.752	1.00	136.55	O
ATOM	5259	C	SER	H	133	−121.896	−38.958	−16.527	1.00	137.33	C
ATOM	5260	O	SER	H	133	−122.243	−39.245	−17.680	1.00	137.30	O
ATOM	5261	N	ALA	H	134	−122.313	−37.834	−15.873	1.00	140.39	N
ATOM	5262	CA	ALA	H	134	−123.211	−36.795	−16.395	1.00	141.31	C
ATOM	5263	CB	ALA	H	134	−123.830	−36.020	−15.237	1.00	141.10	C
ATOM	5264	C	ALA	H	134	−122.409	−35.838	−17.305	1.00	142.01	C
ATOM	5265	O	ALA	H	134	−121.176	−35.913	−17.327	1.00	142.33	O
ATOM	5266	N	SER	H	135	−123.104	−34.956	−18.069	1.00	145.31	N
ATOM	5267	CA	SER	H	135	−122.515	−33.965	−18.999	1.00	145.93	C
ATOM	5268	CB	SER	H	135	−121.745	−32.877	−18.238	1.00	145.96	C
ATOM	5269	OG	SER	H	135	−121.187	−31.874	−19.076	1.00	146.36	O
ATOM	5270	C	SER	H	135	−121.673	−34.557	−20.168	1.00	146.25	C
ATOM	5271	O	SER	H	135	−121.344	−33.818	−21.109	1.00	146.30	O
ATOM	5272	N	THR	H	136	−121.350	−35.883	−20.106	1.00	147.23	N
ATOM	5273	CA	THR	H	136	−120.552	−36.654	−21.078	1.00	147.51	C
ATOM	5274	CB	THR	H	136	−120.503	−38.158	−20.698	1.00	147.62	C
ATOM	5275	OG1	THR	H	136	−119.503	−38.812	−21.484	1.00	147.69	O
ATOM	5276	CG2	THR	H	136	−121.855	−38.872	−20.851	1.00	147.57	C
ATOM	5277	C	THR	H	136	−120.818	−36.342	−22.577	1.00	147.51	C
ATOM	5278	O	THR	H	136	−119.865	−36.256	−23.367	1.00	147.44	O
ATOM	5279	N	SER	H	137	−122.115	−36.144	−22.939	1.00	146.29	N
ATOM	5280	CA	SER	H	137	−122.646	−35.828	−24.276	1.00	146.19	C
ATOM	5281	CB	SER	H	137	−122.269	−34.406	−24.720	1.00	146.28	C
ATOM	5282	OG	SER	H	137	−120.871	−34.156	−24.769	1.00	146.61	O
ATOM	5283	C	SER	H	137	−122.398	−36.918	−25.353	1.00	145.85	C
ATOM	5284	O	SER	H	137	−122.723	−38.090	−25.127	1.00	145.77	O
ATOM	5285	N	GLY	H	138	−121.852	−36.505	−26.498	1.00	144.07	N
ATOM	5286	CA	GLY	H	138	−121.516	−37.350	−27.641	1.00	143.40	C
ATOM	5287	C	GLY	H	138	−120.173	−36.970	−28.240	1.00	142.93	C
ATOM	5288	O	GLY	H	138	−119.533	−37.782	−28.923	1.00	142.93	O
ATOM	5289	N	GLY	H	139	−119.759	−35.729	−27.966	1.00	140.56	N
ATOM	5290	CA	GLY	H	139	−118.500	−35.162	−28.426	1.00	139.72	C
ATOM	5291	C	GLY	H	139	−117.340	−35.626	−27.576	1.00	139.13	C
ATOM	5292	O	GLY	H	139	−117.018	−36.819	−27.566	1.00	139.16	O
ATOM	5293	N	THR	H	140	−116.719	−34.680	−26.844	1.00	135.91	N
ATOM	5294	CA	THR	H	140	−115.571	−34.936	−25.964	1.00	134.98	C
ATOM	5295	CB	THR	H	140	−114.324	−34.106	−26.390	1.00	135.14	C
ATOM	5296	OG1	THR	H	140	−114.688	−32.735	−26.576	1.00	134.94	O
ATOM	5297	CG2	THR	H	140	−113.635	−34.656	−27.649	1.00	134.96	C
ATOM	5298	C	THR	H	140	−115.892	−34.858	−24.455	1.00	134.14	C
ATOM	5299	O	THR	H	140	−116.939	−34.337	−24.050	1.00	134.03	O
ATOM	5300	N	ALA	H	141	−114.969	−35.393	−23.638	1.00	130.14	N
ATOM	5301	CA	ALA	H	141	−115.025	−35.437	−22.178	1.00	128.96	C
ATOM	5302	CB	ALA	H	141	−115.462	−36.821	−21.724	1.00	129.08	C
ATOM	5303	C	ALA	H	141	−113.639	−35.110	−21.603	1.00	128.00	C
ATOM	5304	O	ALA	H	141	−112.625	−35.341	−22.273	1.00	127.86	O
ATOM	5305	N	ALA	H	142	−113.592	−34.570	−20.370	1.00	124.07	N
ATOM	5306	CA	ALA	H	142	−112.317	−34.238	−19.735	1.00	122.79	C
ATOM	5307	CB	ALA	H	142	−112.213	−32.751	−19.459	1.00	122.91	C
ATOM	5308	C	ALA	H	142	−112.031	−35.037	−18.471	1.00	121.84	C
ATOM	5309	O	ALA	H	142	−112.859	−35.113	−17.563	1.00	121.72	O
ATOM	5310	N	LEU	H	143	−110.845	−35.643	−18.440	1.00	118.17	N
ATOM	5311	CA	LEU	H	143	−110.325	−36.452	−17.342	1.00	116.96	C
ATOM	5312	CB	LEU	H	143	−110.519	−37.958	−17.618	1.00	116.97	C
ATOM	5313	CG	LEU	H	143	−109.759	−38.579	−18.793	1.00	117.14	C
ATOM	5314	CD1	LEU	H	143	−108.530	−39.301	−18.321	1.00	117.80	C
ATOM	5315	CD2	LEU	H	143	−110.608	−39.563	−19.497	1.00	117.95	C
ATOM	5316	C	LEU	H	143	−108.845	−36.130	−17.138	1.00	115.95	C
ATOM	5317	O	LEU	H	143	−108.161	−35.694	−18.073	1.00	115.91	O
ATOM	5318	N	GLY	H	144	−108.362	−36.374	−15.933	1.00	112.56	N
ATOM	5319	CA	GLY	H	144	−106.967	−36.137	−15.605	1.00	110.59	C
ATOM	5320	C	GLY	H	144	−106.543	−36.856	−14.352	1.00	109.20	C
ATOM	5321	O	GLY	H	144	−107.200	−37.808	−13.928	1.00	109.35	O
ATOM	5322	N	CYS	H	145	−105.433	−36.418	−13.762	1.00	104.64	N
ATOM	5323	CA	CYS	H	145	−104.937	−36.963	−12.503	1.00	102.92	C
ATOM	5324	CB	CYS	H	145	−104.190	−38.296	−12.643	1.00	102.96	C
ATOM	5325	SG	CYS	H	145	−102.651	−38.216	−13.596	1.00	103.88	S
ATOM	5326	C	CYS	H	145	−104.155	−35.917	−11.747	1.00	101.35	C
ATOM	5327	O	CYS	H	145	−103.278	−35.281	−12.320	1.00	100.90	O
ATOM	5328	N	LEU	H	146	−104.545	−35.685	−10.484	1.00	97.25	N
ATOM	5329	CA	LEU	H	146	−103.920	−34.733	−9.570	1.00	95.86	C
ATOM	5330	CB	LEU	H	146	−104.934	−34.217	−8.530	1.00	95.89	C
ATOM	5331	CG	LEU	H	146	−104.393	−33.386	−7.349	1.00	96.05	C
ATOM	5332	CD1	LEU	H	146	−103.887	−32.001	−7.806	1.00	97.22	C
ATOM	5333	CD2	LEU	H	146	−105.440	−33.233	−6.263	1.00	95.05	C
ATOM	5334	C	LEU	H	146	−102.705	−35.392	−8.879	1.00	94.95	C
ATOM	5335	O	LEU	H	146	−102.849	−36.416	−8.189	1.00	94.83	O
ATOM	5336	N	VAL	H	147	−101.509	−34.790	−9.092	1.00	91.45	N
ATOM	5337	CA	VAL	H	147	−100.210	−35.192	−8.550	1.00	89.84	C
ATOM	5338	CB	VAL	H	147	−99.138	−35.042	−9.638	1.00	89.60	C
ATOM	5339	CG1	VAL	H	147	−97.805	−35.572	−9.154	1.00	90.04	C
ATOM	5340	CG2	VAL	H	147	−99.556	−35.762	−10.904	1.00	88.81	C
ATOM	5341	C	VAL	H	147	−100.003	−34.275	−7.337	1.00	89.01	C
ATOM	5342	O	VAL	H	147	−99.572	−33.133	−7.472	1.00	88.83	O
ATOM	5343	N	LYS	H	148	−100.400	−34.759	−6.162	1.00	88.49	N
ATOM	5344	CA	LYS	H	148	−100.378	−33.988	−4.925	1.00	87.97	C
ATOM	5345	CB	LYS	H	148	−101.753	−34.128	−4.213	1.00	87.92	C
ATOM	5346	CG	LYS	H	148	−102.260	−32.874	−3.503	1.00	87.57	C
ATOM	5347	CD	LYS	H	148	−102.671	−33.147	−2.062	1.00	87.09	C
ATOM	5348	CE	LYS	H	148	−103.187	−31.899	−1.371	1.00	87.40	C
ATOM	5349	NZ	LYS	H	148	−103.089	−31.965	0.119	1.00	87.10	N
ATOM	5350	C	LYS	H	148	−99.254	−34.345	−3.964	1.00	87.69	C
ATOM	5351	O	LYS	H	148	−98.770	−35.482	−3.947	1.00	87.61	O
ATOM	5352	N	ASP	H	149	−98.870	−33.353	−3.140	1.00	87.66	N
ATOM	5353	CA	ASP	H	149	−97.877	−33.460	−2.087	1.00	87.23	C
ATOM	5354	CB	ASP	H	149	−98.495	−34.184	−0.875	1.00	87.43	C
ATOM	5355	CG	ASP	H	149	−99.611	−33.408	−0.191	1.00	88.64	C
ATOM	5356	OD1	ASP	H	149	−99.662	−32.147	−0.356	1.00	89.99	O
ATOM	5357	OD2	ASP	H	149	−100.428	−34.047	0.524	1.00	89.69	O
ATOM	5358	C	ASP	H	149	−96.559	−34.084	−2.510	1.00	86.55	C
ATOM	5359	O	ASP	H	149	−96.368	−35.292	−2.350	1.00	86.72	O
ATOM	5360	N	TYR	H	150	−95.665	−33.256	−3.087	1.00	82.33	N
ATOM	5361	CA	TYR	H	150	−94.323	−33.634	−3.552	1.00	81.28	C
ATOM	5362	CB	TYR	H	150	−94.313	−34.227	−4.996	1.00	80.95	C
ATOM	5363	CG	TYR	H	150	−94.522	−33.233	−6.118	1.00	79.79	C
ATOM	5364	CD1	TYR	H	150	−93.468	−32.449	−6.590	1.00	79.35	C
ATOM	5365	CE1	TYR	H	150	−93.659	−31.499	−7.595	1.00	78.26	C
ATOM	5366	CZ	TYR	H	150	−94.914	−31.342	−8.160	1.00	77.80	C
ATOM	5367	OH	TYR	H	150	−95.084	−30.431	−9.178	1.00	76.14	O
ATOM	5368	CE2	TYR	H	150	−95.971	−32.137	−7.729	1.00	78.33	C
ATOM	5369	CD2	TYR	H	150	−95.768	−33.077	−6.714	1.00	78.62	C
ATOM	5370	C	TYR	H	150	−93.338	−32.481	−3.397	1.00	81.02	C
ATOM	5371	O	TYR	H	150	−93.745	−31.318	−3.379	1.00	80.65	O
ATOM	5372	N	PHE	H	151	−92.041	−32.808	−3.298	1.00	80.24	N
ATOM	5373	CA	PHE	H	151	−90.930	−31.858	−3.173	1.00	80.24	C
ATOM	5374	CB	PHE	H	151	−90.891	−31.234	−1.772	1.00	80.03	C
ATOM	5375	CG	PHE	H	151	−89.858	−30.152	−1.607	1.00	79.36	C
ATOM	5376	CD1	PHE	H	151	−88.574	−30.455	−1.154	1.00	78.48	C
ATOM	5377	CE1	PHE	H	151	−87.613	−29.455	−1.002	1.00	77.04	C
ATOM	5378	CZ	PHE	H	151	−87.935	−28.147	−1.286	1.00	76.80	C
ATOM	5379	CE2	PHE	H	151	−89.205	−27.825	−1.724	1.00	77.16	C
ATOM	5380	CD2	PHE	H	151	−90.163	−28.830	−1.896	1.00	77.48	C
ATOM	5381	C	PHE	H	151	−89.630	−32.607	−3.477	1.00	80.47	C
ATOM	5382	O	PHE	H	151	−89.544	−33.745	−3.037	1.00	80.63	O
ATOM	5383	N	PRO	H	152	−88.606	−32.081	−4.209	1.00	83.43	N
ATOM	5384	CA	PRO	H	152	−88.427	−30.756	−4.834	1.00	83.19	C
ATOM	5385	CB	PRO	H	152	−86.933	−30.718	−5.186	1.00	83.10	C
ATOM	5386	CG	PRO	H	152	−86.322	−31.871	−4.473	1.00	83.56	C
ATOM	5387	CD	PRO	H	152	−87.398	−32.888	−4.413	1.00	83.45	C
ATOM	5388	C	PRO	H	152	−89.355	−30.408	−5.988	1.00	83.21	C
ATOM	5389	O	PRO	H	152	−90.542	−30.634	−5.855	1.00	83.44	O
ATOM	5390	N	GLU	H	153	−88.869	−29.838	−7.092	1.00	85.80	N
ATOM	5391	CA	GLU	H	153	−89.855	−29.416	−8.056	1.00	85.87	C
ATOM	5392	CB	GLU	H	153	−89.952	−27.900	−8.138	1.00	85.58	C
ATOM	5393	CG	GLU	H	153	−91.374	−27.408	−7.948	1.00	85.41	C
ATOM	5394	CD	GLU	H	153	−92.111	−26.963	−9.195	1.00	85.00	C
ATOM	5395	OE1	GLU	H	153	−92.597	−27.837	−9.955	1.00	84.39	O
ATOM	5396	OE2	GLU	H	153	−92.222	−25.729	−9.398	1.00	84.81	O
ATOM	5397	C	GLU	H	153	−90.029	−30.019	−9.406	1.00	86.38	C
ATOM	5398	O	GLU	H	153	−91.154	−29.908	−9.891	1.00	87.16	O
ATOM	5399	N	PRO	H	154	−89.067	−30.641	−10.075	1.00	82.97	N
ATOM	5400	CA	PRO	H	154	−89.363	−31.178	−11.422	1.00	82.81	C
ATOM	5401	CB	PRO	H	154	−88.144	−31.998	−11.761	1.00	82.87	C
ATOM	5402	CG	PRO	H	154	−87.059	−31.343	−10.977	1.00	83.12	C
ATOM	5403	CD	PRO	H	154	−87.664	−30.849	−9.699	1.00	82.87	C
ATOM	5404	C	PRO	H	154	−90.708	−31.866	−11.752	1.00	82.98	C
ATOM	5405	O	PRO	H	154	−91.522	−31.184	−12.391	1.00	83.54	O
ATOM	5406	N	VAL	H	155	−90.973	−33.154	−11.339	1.00	80.51	N
ATOM	5407	CA	VAL	H	155	−92.198	−33.952	−11.670	1.00	80.32	C
ATOM	5408	CB	VAL	H	155	−93.380	−33.981	−10.663	1.00	80.32	C
ATOM	5409	CG1	VAL	H	155	−94.519	−33.072	−11.087	1.00	80.02	C
ATOM	5410	CG2	VAL	H	155	−93.909	−35.403	−10.518	1.00	81.10	C
ATOM	5411	C	VAL	H	155	−92.678	−33.935	−13.151	1.00	80.22	C
ATOM	5412	O	VAL	H	155	−93.103	−32.900	−13.645	1.00	80.15	O
ATOM	5413	N	THR	H	156	−92.635	−35.088	−13.837	1.00	82.36	N
ATOM	5414	CA	THR	H	156	−93.051	−35.181	−15.241	1.00	82.95	C
ATOM	5415	CB	THR	H	156	−91.871	−35.400	−16.183	1.00	82.72	C
ATOM	5416	OG1	THR	H	156	−91.085	−36.512	−15.749	1.00	83.41	O
ATOM	5417	CG2	THR	H	156	−91.007	−34.163	−16.312	1.00	83.21	C
ATOM	5418	C	THR	H	156	−94.217	−36.094	−15.553	1.00	83.35	C
ATOM	5419	O	THR	H	156	−94.100	−37.315	−15.448	1.00	83.44	O
ATOM	5420	N	VAL	H	157	−95.335	−35.494	−15.987	1.00	84.88	N
ATOM	5421	CA	VAL	H	157	−96.543	−36.220	−16.367	1.00	85.29	C
ATOM	5422	CB	VAL	H	157	−97.852	−35.527	−15.929	1.00	85.05	C
ATOM	5423	CG1	VAL	H	157	−99.047	−36.460	−16.116	1.00	85.24	C
ATOM	5424	CG2	VAL	H	157	−97.766	−35.038	−14.485	1.00	85.07	C
ATOM	5425	C	VAL	H	157	−96.560	−36.494	−17.862	1.00	85.97	C
ATOM	5426	O	VAL	H	157	−96.249	−35.624	−18.682	1.00	86.10	O
ATOM	5427	N	SER	H	158	−96.942	−37.713	−18.198	1.00	88.64	N
ATOM	5428	CA	SER	H	158	−97.084	−38.197	−19.559	1.00	89.64	C
ATOM	5429	CB	SER	H	158	−95.836	−38.971	−19.993	1.00	89.51	C
ATOM	5430	OG	SER	H	158	−96.025	−40.372	−20.126	1.00	88.95	O
ATOM	5431	C	SER	H	158	−98.323	−39.091	−19.553	1.00	90.56	C
ATOM	5432	O	SER	H	158	−98.538	−39.794	−18.561	1.00	90.78	O
ATOM	5433	N	TRP	H	159	−99.144	−39.060	−20.633	1.00	92.59	N
ATOM	5434	CA	TRP	H	159	−100.333	−39.907	−20.723	1.00	92.98	C
ATOM	5435	CB	TRP	H	159	−101.561	−39.104	−21.090	1.00	92.58	C
ATOM	5436	CG	TRP	H	159	−102.045	−38.260	−19.953	1.00	91.88	C
ATOM	5437	CD1	TRP	H	159	−101.611	−37.013	−19.616	1.00	91.55	C
ATOM	5438	NE1	TRP	H	159	−102.312	−36.542	−18.527	1.00	91.01	N
ATOM	5439	CE2	TRP	H	159	−103.198	−37.503	−18.119	1.00	90.69	C
ATOM	5440	CD2	TRP	H	159	−103.060	−38.602	−18.998	1.00	91.08	C
ATOM	5441	CE3	TRP	H	159	−103.876	−39.729	−18.805	1.00	90.75	C
ATOM	5442	CZ3	TRP	H	159	−104.781	−39.726	−17.754	1.00	91.05	C
ATOM	5443	CH2	TRP	H	159	−104.885	−38.627	−16.889	1.00	91.05	C
ATOM	5444	CZ2	TRP	H	159	−104.101	−37.505	−17.052	1.00	90.75	C
ATOM	5445	C	TRP	H	159	−100.114	−41.115	−21.635	1.00	93.84	C
ATOM	5446	O	TRP	H	159	−99.360	−41.028	−22.620	1.00	93.86	O
ATOM	5447	N	ASN	H	160	−100.749	−42.254	−21.261	1.00	97.57	N
ATOM	5448	CA	ASN	H	160	−100.698	−43.567	−21.922	1.00	98.31	C
ATOM	5449	CB	ASN	H	160	−101.820	−43.740	−22.950	1.00	98.36	C
ATOM	5450	CG	ASN	H	160	−103.205	−43.845	−22.348	1.00	99.33	C
ATOM	5451	OD1	ASN	H	160	−103.408	−44.390	−21.255	1.00	100.83	O
ATOM	5452	ND2	ASN	H	160	−104.203	−43.325	−23.048	1.00	100.10	N
ATOM	5453	C	ASN	H	160	−99.332	−43.897	−22.492	1.00	98.70	C
ATOM	5454	O	ASN	H	160	−99.196	−44.110	−23.694	1.00	98.51	O
ATOM	5455	N	SER	H	161	−98.311	−43.901	−21.613	1.00	100.95	N
ATOM	5456	CA	SER	H	161	−96.899	−44.191	−21.914	1.00	101.67	C
ATOM	5457	CB	SER	H	161	−96.663	−45.691	−22.072	1.00	101.66	C
ATOM	5458	OG	SER	H	161	−97.176	−46.390	−20.948	1.00	102.13	O
ATOM	5459	C	SER	H	161	−96.307	−43.382	−23.078	1.00	102.05	C
ATOM	5460	O	SER	H	161	−95.469	−43.878	−23.843	1.00	102.08	O
ATOM	5461	N	GLY	H	162	−96.748	−42.131	−23.177	1.00	103.84	N
ATOM	5462	CA	GLY	H	162	−96.291	−41.207	−24.204	1.00	104.22	C
ATOM	5463	C	GLY	H	162	−96.960	−41.387	−25.546	1.00	104.40	C
ATOM	5464	O	GLY	H	162	−96.344	−41.119	−26.583	1.00	104.66	O
ATOM	5465	N	ALA	H	163	−98.223	−41.842	−25.536	1.00	105.13	N
ATOM	5466	CA	ALA	H	163	−99.000	−42.038	−26.755	1.00	105.10	C
ATOM	5467	CB	ALA	H	163	−99.670	−43.401	−26.755	1.00	105.12	C
ATOM	5468	C	ALA	H	163	−100.036	−40.918	−26.873	1.00	104.95	C
ATOM	5469	O	ALA	H	163	−100.053	−40.227	−27.897	1.00	105.29	O
ATOM	5470	N	LEU	H	164	−100.872	−40.717	−25.829	1.00	102.14	N
ATOM	5471	CA	LEU	H	164	−101.883	−39.664	−25.819	1.00	101.80	C
ATOM	5472	CB	LEU	H	164	−103.008	−40.001	−24.814	1.00	101.61	C
ATOM	5473	CG	LEU	H	164	−103.991	−38.899	−24.407	1.00	101.38	C
ATOM	5474	CD1	LEU	H	164	−104.862	−38.446	−25.572	1.00	101.25	C
ATOM	5475	CD2	LEU	H	164	−104.847	−39.360	−23.263	1.00	100.62	C
ATOM	5476	C	LEU	H	164	−101.200	−38.296	−25.553	1.00	101.92	C
ATOM	5477	O	LEU	H	164	−100.692	−38.055	−24.450	1.00	102.13	O
ATOM	5478	N	THR	H	165	−101.171	−37.427	−26.599	1.00	102.51	N
ATOM	5479	CA	THR	H	165	−100.559	−36.088	−26.619	1.00	102.09	C
ATOM	5480	CB	THR	H	165	−99.382	−36.040	−27.600	1.00	102.06	C
ATOM	5481	OG1	THR	H	165	−99.135	−34.668	−27.916	1.00	102.39	O
ATOM	5482	CG2	THR	H	165	−99.656	−36.816	−28.901	1.00	102.11	C
ATOM	5483	C	THR	H	165	−101.542	−34.931	−26.897	1.00	101.78	C
ATOM	5484	O	THR	H	165	−101.409	−33.860	−26.296	1.00	101.69	O
ATOM	5485	N	SER	H	166	−102.483	−35.126	−27.834	1.00	100.47	N
ATOM	5486	CA	SER	H	166	−103.452	−34.095	−28.178	1.00	99.92	C
ATOM	5487	CB	SER	H	166	−104.168	−34.428	−29.484	1.00	99.96	C
ATOM	5488	OG	SER	H	166	−103.821	−33.519	−30.519	1.00	100.95	O
ATOM	5489	C	SER	H	166	−104.447	−33.894	−27.055	1.00	99.35	C
ATOM	5490	O	SER	H	166	−104.954	−34.865	−26.485	1.00	99.39	O
ATOM	5491	N	GLY	H	167	−104.692	−32.625	−26.739	1.00	98.50	N
ATOM	5492	CA	GLY	H	167	−105.620	−32.206	−25.695	1.00	97.67	C
ATOM	5493	C	GLY	H	167	−105.093	−32.351	−24.284	1.00	97.17	C
ATOM	5494	O	GLY	H	167	−105.836	−32.081	−23.340	1.00	97.21	O
ATOM	5495	N	VAL	H	168	−103.801	−32.767	−24.126	1.00	95.72	N
ATOM	5496	CA	VAL	H	168	−103.112	−32.965	−22.840	1.00	94.89	C
ATOM	5497	CB	VAL	H	168	−101.922	−33.953	−22.958	1.00	94.85	C
ATOM	5498	CG1	VAL	H	168	−101.187	−34.094	−21.632	1.00	94.65	C
ATOM	5499	CG2	VAL	H	168	−102.370	−35.317	−23.462	1.00	95.14	C
ATOM	5500	C	VAL	H	168	−102.645	−31.616	−22.294	1.00	94.37	C
ATOM	5501	O	VAL	H	168	−101.856	−30.933	−22.952	1.00	94.37	O
ATOM	5502	N	HIS	H	169	−103.114	−31.250	−21.089	1.00	91.67	N
ATOM	5503	CA	HIS	H	169	−102.761	−29.997	−20.436	1.00	91.22	C
ATOM	5504	CB	HIS	H	169	−103.975	−29.060	−20.360	1.00	91.22	C
ATOM	5505	CG	HIS	H	169	−104.261	−28.301	−21.616	1.00	91.46	C
ATOM	5506	ND1	HIS	H	169	−103.604	−28.577	−22.806	1.00	91.91	N
ATOM	5507	CE1	HIS	H	169	−104.112	−27.742	−23.700	1.00	91.47	C
ATOM	5508	NE2	HIS	H	169	−105.044	−26.954	−23.158	1.00	91.76	N
ATOM	5509	CD2	HIS	H	169	−105.152	−27.306	−21.831	1.00	91.43	C
ATOM	5510	C	HIS	H	169	−102.183	−30.178	−19.056	1.00	91.04	C
ATOM	5511	O	HIS	H	169	−102.940	−30.139	−18.074	1.00	90.98	O
ATOM	5512	N	THR	H	170	−100.839	−30.341	−18.963	1.00	89.21	N
ATOM	5513	CA	THR	H	170	−100.155	−30.465	−17.665	1.00	88.80	C
ATOM	5514	CB	THR	H	170	−98.889	−31.300	−17.749	1.00	88.65	C
ATOM	5515	OG1	THR	H	170	−99.131	−32.484	−18.516	1.00	88.62	O
ATOM	5516	CG2	THR	H	170	−98.359	−31.656	−16.376	1.00	88.55	C
ATOM	5517	C	THR	H	170	−99.927	−29.048	−17.116	1.00	88.66	C
ATOM	5518	O	THR	H	170	−99.163	−28.267	−17.694	1.00	88.44	O
ATOM	5519	N	PHE	H	171	−100.631	−28.712	−16.028	1.00	89.66	N
ATOM	5520	CA	PHE	H	171	−100.588	−27.393	−15.418	1.00	89.85	C
ATOM	5521	CB	PHE	H	171	−101.810	−27.185	−14.518	1.00	90.12	C
ATOM	5522	CG	PHE	H	171	−103.058	−26.965	−15.322	1.00	91.71	C
ATOM	5523	CD1	PHE	H	171	−103.897	−28.028	−15.638	1.00	92.97	C
ATOM	5524	CE1	PHE	H	171	−105.041	−27.833	−16.406	1.00	93.11	C
ATOM	5525	CZ	PHE	H	171	−105.350	−26.577	−16.863	1.00	93.49	C
ATOM	5526	CE2	PHE	H	171	−104.526	−25.512	−16.568	1.00	93.17	C
ATOM	5527	CD2	PHE	H	171	−103.377	−25.706	−15.806	1.00	92.71	C
ATOM	5528	C	PHE	H	171	−99.363	−27.130	−14.609	1.00	89.75	C
ATOM	5529	O	PHE	H	171	−98.851	−28.065	−13.978	1.00	90.18	O
ATOM	5530	N	PRO	H	172	−98.904	−25.849	−14.542	1.00	87.98	N
ATOM	5531	CA	PRO	H	172	−97.760	−25.525	−13.674	1.00	87.45	C
ATOM	5532	CB	PRO	H	172	−97.648	−24.001	−13.796	1.00	87.33	C
ATOM	5533	CG	PRO	H	172	−98.322	−23.665	−15.037	1.00	87.68	C
ATOM	5534	CD	PRO	H	172	−99.420	−24.639	−15.210	1.00	87.92	C
ATOM	5535	C	PRO	H	172	−98.071	−25.903	−12.220	1.00	86.77	C
ATOM	5536	O	PRO	H	172	−99.229	−25.810	−11.797	1.00	86.77	O
ATOM	5537	N	ALA	H	173	−97.053	−26.340	−11.457	1.00	83.63	N
ATOM	5538	CA	ALA	H	173	−97.233	−26.716	−10.051	1.00	83.04	C
ATOM	5539	CB	ALA	H	173	−95.950	−27.329	−9.510	1.00	82.99	C
ATOM	5540	C	ALA	H	173	−97.657	−25.522	−9.184	1.00	82.58	C
ATOM	5541	O	ALA	H	173	−97.655	−24.373	−9.636	1.00	82.40	O
ATOM	5542	N	VAL	H	174	−98.029	−25.797	−7.948	1.00	82.52	N
ATOM	5543	CA	VAL	H	174	−98.410	−24.751	−7.019	1.00	82.63	C
ATOM	5544	CB	VAL	H	174	−99.915	−24.380	−7.047	1.00	82.71	C
ATOM	5545	CG1	VAL	H	174	−100.815	−25.563	−6.700	1.00	83.00	C
ATOM	5546	CG2	VAL	H	174	−100.205	−23.192	−6.140	1.00	83.07	C
ATOM	5547	C	VAL	H	174	−97.897	−25.120	−5.657	1.00	82.53	C
ATOM	5548	O	VAL	H	174	−98.127	−26.240	−5.209	1.00	82.89	O
ATOM	5549	N	LEU	H	175	−97.177	−24.202	−5.010	1.00	81.53	N
ATOM	5550	CA	LEU	H	175	−96.615	−24.424	−3.680	1.00	81.33	C
ATOM	5551	CB	LEU	H	175	−95.444	−23.472	−3.417	1.00	80.93	C
ATOM	5552	CG	LEU	H	175	−94.733	−23.605	−2.103	1.00	80.42	C
ATOM	5553	CD1	LEU	H	175	−94.223	−25.004	−1.892	1.00	81.14	C
ATOM	5554	CD2	LEU	H	175	−93.606	−22.641	−2.031	1.00	79.66	C
ATOM	5555	C	LEU	H	175	−97.701	−24.258	−2.644	1.00	81.61	C
ATOM	5556	O	LEU	H	175	−98.313	−23.193	−2.550	1.00	81.55	O
ATOM	5557	N	GLN	H	176	−97.954	−25.321	−1.883	1.00	85.15	N
ATOM	5558	CA	GLN	H	176	−98.989	−25.317	−0.856	1.00	85.67	C
ATOM	5559	CB	GLN	H	176	−99.579	−26.711	−0.689	1.00	85.64	C
ATOM	5560	CG	GLN	H	176	−100.237	−27.269	−1.931	1.00	85.96	C
ATOM	5561	CD	GLN	H	176	−100.703	−28.657	−1.616	1.00	87.03	C
ATOM	5562	OE1	GLN	H	176	−101.887	−28.871	−1.313	1.00	88.32	O
ATOM	5563	NE2	GLN	H	176	−99.783	−29.632	−1.655	1.00	86.68	N
ATOM	5564	C	GLN	H	176	−98.428	−24.839	0.469	1.00	86.04	C
ATOM	5565	O	GLN	H	176	−97.205	−24.852	0.652	1.00	86.10	O
ATOM	5566	N	SER	H	177	−99.324	−24.426	1.399	1.00	88.86	N
ATOM	5567	CA	SER	H	177	−98.974	−23.948	2.742	1.00	89.53	C
ATOM	5568	CB	SER	H	177	−100.230	−23.631	3.542	1.00	89.52	C
ATOM	5569	OG	SER	H	177	−101.138	−24.715	3.455	1.00	90.38	O
ATOM	5570	C	SER	H	177	−98.094	−24.979	3.474	1.00	89.80	C
ATOM	5571	O	SER	H	177	−97.163	−24.593	4.193	1.00	89.96	O
ATOM	5572	N	SER	H	178	−98.353	−26.292	3.237	1.00	90.01	N
ATOM	5573	CA	SER	H	178	−97.573	−27.400	3.799	1.00	90.10	C
ATOM	5574	CB	SER	H	178	−98.120	−28.740	3.311	1.00	90.17	C
ATOM	5575	OG	SER	H	178	−98.173	−28.854	1.897	1.00	90.19	O
ATOM	5576	C	SER	H	178	−96.093	−27.261	3.414	1.00	90.15	C
ATOM	5577	O	SER	H	178	−95.216	−27.536	4.228	1.00	90.30	O
ATOM	5578	N	GLY	H	179	−95.847	−26.795	2.190	1.00	89.38	N
ATOM	5579	CA	GLY	H	179	−94.520	−26.586	1.624	1.00	89.50	C
ATOM	5580	C	GLY	H	179	−94.222	−27.558	0.504	1.00	89.56	C
ATOM	5581	O	GLY	H	179	−93.095	−27.588	−0.006	1.00	89.51	O
ATOM	5582	N	LEU	H	180	−95.249	−28.353	0.120	1.00	86.59	N
ATOM	5583	CA	LEU	H	180	−95.204	−29.364	−0.934	1.00	86.55	C
ATOM	5584	CB	LEU	H	180	−95.808	−30.690	−0.432	1.00	86.49	C
ATOM	5585	CG	LEU	H	180	−95.213	−31.355	0.829	1.00	85.74	C
ATOM	5586	CD1	LEU	H	180	−95.895	−32.655	1.095	1.00	84.95	C
ATOM	5587	CD2	LEU	H	180	−93.741	−31.644	0.678	1.00	85.10	C
ATOM	5588	C	LEU	H	180	−95.961	−28.891	−2.171	1.00	86.73	C
ATOM	5589	O	LEU	H	180	−97.032	−28.322	−2.045	1.00	86.85	O
ATOM	5590	N	TYR	H	181	−95.415	−29.126	−3.358	1.00	87.14	N
ATOM	5591	CA	TYR	H	181	−96.052	−28.716	−4.603	1.00	87.59	C
ATOM	5592	CB	TYR	H	181	−95.016	−28.595	−5.735	1.00	87.56	C
ATOM	5593	CG	TYR	H	181	−93.948	−27.568	−5.454	1.00	87.55	C
ATOM	5594	CD1	TYR	H	181	−94.132	−26.235	−5.796	1.00	87.69	C
ATOM	5595	CE1	TYR	H	181	−93.161	−25.278	−5.515	1.00	87.87	C
ATOM	5596	CZ	TYR	H	181	−91.992	−25.651	−4.873	1.00	87.74	C
ATOM	5597	OH	TYR	H	181	−91.035	−24.707	−4.584	1.00	88.45	O
ATOM	5598	CE2	TYR	H	181	−91.790	−26.973	−4.522	1.00	87.55	C
ATOM	5599	CD2	TYR	H	181	−92.767	−27.920	−4.810	1.00	87.68	C
ATOM	5600	C	TYR	H	181	−97.149	−29.678	−5.018	1.00	88.10	C
ATOM	5601	O	TYR	H	181	−97.100	−30.866	−4.684	1.00	88.23	O
ATOM	5602	N	SER	H	182	−98.136	−29.166	−5.767	1.00	91.91	N
ATOM	5603	CA	SER	H	182	−99.248	−29.952	−6.308	1.00	92.59	C
ATOM	5604	CB	SER	H	182	−100.509	−29.785	−5.470	1.00	92.69	C
ATOM	5605	OG	SER	H	182	−100.330	−30.303	−4.164	1.00	93.52	O
ATOM	5606	C	SER	H	182	−99.541	−29.520	−7.717	1.00	92.83	C
ATOM	5607	O	SER	H	182	−99.540	−28.324	−8.016	1.00	92.92	O
ATOM	5608	N	LEU	H	183	−99.775	−30.479	−8.591	1.00	94.42	N
ATOM	5609	CA	LEU	H	183	−100.126	−30.156	−9.964	1.00	95.22	C
ATOM	5610	CB	LEU	H	183	−98.948	−29.977	−10.943	1.00	95.09	C
ATOM	5611	CG	LEU	H	183	−98.157	−31.170	−11.505	1.00	94.86	C
ATOM	5612	CD1	LEU	H	183	−98.956	−31.979	−12.521	1.00	95.07	C
ATOM	5613	CD2	LEU	H	183	−96.968	−30.650	−12.264	1.00	95.32	C
ATOM	5614	C	LEU	H	183	−101.162	−31.078	−10.497	1.00	95.90	C
ATOM	5615	O	LEU	H	183	−101.322	−32.196	−10.002	1.00	96.13	O
ATOM	5616	N	SER	H	184	−101.854	−30.623	−11.521	1.00	95.87	N
ATOM	5617	CA	SER	H	184	−102.879	−31.424	−12.135	1.00	96.50	C
ATOM	5618	CB	SER	H	184	−104.260	−30.840	−11.836	1.00	96.55	C
ATOM	5619	OG	SER	H	184	−104.294	−29.427	−11.978	1.00	96.78	O
ATOM	5620	C	SER	H	184	−102.628	−31.509	−13.615	1.00	96.87	C
ATOM	5621	O	SER	H	184	−102.418	−30.487	−14.271	1.00	96.82	O
ATOM	5622	N	SER	H	185	−102.604	−32.728	−14.140	1.00	96.92	N
ATOM	5623	CA	SER	H	185	−102.465	−32.910	−15.572	1.00	97.63	C
ATOM	5624	CB	SER	H	185	−101.491	−34.018	−15.925	1.00	97.50	C
ATOM	5625	OG	SER	H	185	−101.281	−34.000	−17.329	1.00	97.39	O
ATOM	5626	C	SER	H	185	−103.862	−33.263	−16.038	1.00	98.29	C
ATOM	5627	O	SER	H	185	−104.576	−34.020	−15.365	1.00	98.57	O
ATOM	5628	N	VAL	H	186	−104.272	−32.687	−17.159	1.00	98.00	N
ATOM	5629	CA	VAL	H	186	−105.602	−32.908	−17.690	1.00	98.39	C
ATOM	5630	CB	VAL	H	186	−106.449	−31.646	−17.393	1.00	98.15	C
ATOM	5631	CG1	VAL	H	186	−106.939	−30.947	−18.653	1.00	98.29	C
ATOM	5632	CG2	VAL	H	186	−107.579	−31.941	−16.419	1.00	97.38	C
ATOM	5633	C	VAL	H	186	−105.545	−33.335	−19.166	1.00	99.17	C
ATOM	5634	O	VAL	H	186	−104.532	−33.123	−19.843	1.00	99.02	O
ATOM	5635	N	VAL	H	187	−106.617	−33.988	−19.637	1.00	101.68	N
ATOM	5636	CA	VAL	H	187	−106.742	−34.433	−21.023	1.00	102.74	C
ATOM	5637	CB	VAL	H	187	−106.004	−35.767	−21.355	1.00	102.60	C
ATOM	5638	CG1	VAL	H	187	−106.720	−36.984	−20.774	1.00	102.47	C
ATOM	5639	CG2	VAL	H	187	−105.770	−35.918	−22.853	1.00	102.04	C
ATOM	5640	C	VAL	H	187	−108.192	−34.310	−21.543	1.00	103.69	C
ATOM	5641	O	VAL	H	187	−109.132	−34.245	−20.745	1.00	103.73	O
ATOM	5642	N	THR	H	188	−108.344	−34.211	−22.880	1.00	107.37	N
ATOM	5643	CA	THR	H	188	−109.603	−34.099	−23.613	1.00	108.41	C
ATOM	5644	CB	THR	H	188	−109.767	−32.673	−24.199	1.00	108.35	C
ATOM	5645	OG1	THR	H	188	−110.529	−31.892	−23.270	1.00	107.92	O
ATOM	5646	CG2	THR	H	188	−110.414	−32.645	−25.597	1.00	108.00	C
ATOM	5647	C	THR	H	188	−109.659	−35.281	−24.573	1.00	109.45	C
ATOM	5648	O	THR	H	188	−108.768	−35.458	−25.419	1.00	109.44	O
ATOM	5649	N	VAL	H	189	−110.685	−36.121	−24.383	1.00	114.13	N
ATOM	5650	CA	VAL	H	189	−110.934	−37.340	−25.162	1.00	115.59	C
ATOM	5651	CB	VAL	H	189	−110.343	−38.638	−24.522	1.00	115.62	C
ATOM	5652	CG1	VAL	H	189	−108.822	−38.708	−24.677	1.00	115.89	C
ATOM	5653	CG2	VAL	H	189	−110.773	−38.810	−23.066	1.00	115.45	C
ATOM	5654	C	VAL	H	189	−112.427	−37.499	−25.477	1.00	116.45	C
ATOM	5655	O	VAL	H	189	−113.262	−37.061	−24.681	1.00	116.41	O
ATOM	5656	N	PRO	H	190	−112.796	−38.137	−26.609	1.00	120.19	N
ATOM	5657	CA	PRO	H	190	−114.227	−38.305	−26.893	1.00	120.99	C
ATOM	5658	CB	PRO	H	190	−114.267	−38.550	−28.402	1.00	121.02	C
ATOM	5659	CG	PRO	H	190	−112.925	−39.111	−28.741	1.00	120.60	C
ATOM	5660	CD	PRO	H	190	−111.951	−38.732	−27.671	1.00	120.17	C
ATOM	5661	C	PRO	H	190	−114.908	−39.418	−26.090	1.00	121.84	C
ATOM	5662	O	PRO	H	190	−114.259	−40.397	−25.691	1.00	121.99	O
ATOM	5663	N	SER	H	191	−116.237	−39.263	−25.865	1.00	123.47	N
ATOM	5664	CA	SER	H	191	−117.101	−40.221	−25.153	1.00	124.15	C
ATOM	5665	CB	SER	H	191	−118.450	−39.576	−24.858	1.00	124.20	C
ATOM	5666	OG	SER	H	191	−118.261	−38.280	−24.310	1.00	124.30	O
ATOM	5667	C	SER	H	191	−117.282	−41.493	−26.014	1.00	124.53	C
ATOM	5668	O	SER	H	191	−117.612	−42.568	−25.506	1.00	124.41	O
ATOM	5669	N	SER	H	192	−117.017	−41.336	−27.329	1.00	126.09	N
ATOM	5670	CA	SER	H	192	−117.054	−42.319	−28.417	1.00	126.73	C
ATOM	5671	CB	SER	H	192	−117.251	−41.599	−29.757	1.00	126.76	C
ATOM	5672	OG	SER	H	192	−116.846	−40.236	−29.760	1.00	127.04	O
ATOM	5673	C	SER	H	192	−115.799	−43.260	−28.454	1.00	127.12	C
ATOM	5674	O	SER	H	192	−115.557	−43.952	−29.454	1.00	127.14	O
ATOM	5675	N	SER	H	193	−115.018	−43.279	−27.349	1.00	127.68	N
ATOM	5676	CA	SER	H	193	−113.805	−44.088	−27.149	1.00	127.78	C
ATOM	5677	CB	SER	H	193	−112.610	−43.461	−27.873	1.00	127.70	C
ATOM	5678	OG	SER	H	193	−112.345	−42.148	−27.408	1.00	127.41	O
ATOM	5679	C	SER	H	193	−113.513	−44.240	−25.639	1.00	127.76	C
ATOM	5680	O	SER	H	193	−112.439	−44.720	−25.261	1.00	127.76	O
ATOM	5681	N	LEU	H	194	−114.488	−43.838	−24.794	1.00	126.91	N
ATOM	5682	CA	LEU	H	194	−114.439	−43.864	−23.333	1.00	126.94	C
ATOM	5683	CB	LEU	H	194	−115.735	−43.260	−22.749	1.00	126.93	C
ATOM	5684	CG	LEU	H	194	−115.625	−42.156	−21.690	1.00	126.77	C
ATOM	5685	CD1	LEU	H	194	−114.795	−40.978	−22.167	1.00	126.96	C
ATOM	5686	CD2	LEU	H	194	−115.156	−42.691	−20.368	1.00	126.40	C
ATOM	5687	C	LEU	H	194	−114.115	−45.241	−22.725	1.00	127.07	C
ATOM	5688	O	LEU	H	194	−112.938	−45.531	−22.502	1.00	127.06	O
ATOM	5689	N	GLY	H	195	−115.138	−46.067	−22.483	1.00	129.35	N
ATOM	5690	CA	GLY	H	195	−114.991	−47.405	−21.910	1.00	129.33	C
ATOM	5691	C	GLY	H	195	−114.124	−48.369	−22.705	1.00	129.46	C
ATOM	5692	O	GLY	H	195	−113.689	−49.391	−22.166	1.00	129.50	O
ATOM	5693	N	THR	H	196	−113.858	−48.040	−23.993	1.00	132.04	N
ATOM	5694	CA	THR	H	196	−113.058	−48.820	−24.960	1.00	131.92	C
ATOM	5695	CB	THR	H	196	−113.477	−48.498	−26.438	1.00	132.08	C
ATOM	5696	OG1	THR	H	196	−112.751	−47.369	−26.949	1.00	132.25	O
ATOM	5697	CG2	THR	H	196	−114.999	−48.281	−26.613	1.00	132.06	C
ATOM	5698	C	THR	H	196	−111.518	−48.784	−24.700	1.00	131.67	C
ATOM	5699	O	THR	H	196	−110.919	−49.843	−24.463	1.00	131.82	O
ATOM	5700	N	GLN	H	197	−110.895	−47.565	−24.756	1.00	129.94	N
ATOM	5701	CA	GLN	H	197	−109.460	−47.311	−24.533	1.00	129.20	C
ATOM	5702	CB	GLN	H	197	−108.927	−46.224	−25.488	1.00	129.35	C
ATOM	5703	CG	GLN	H	197	−108.355	−46.753	−26.805	1.00	130.14	C
ATOM	5704	CD	GLN	H	197	−109.414	−47.071	−27.848	1.00	131.31	C
ATOM	5705	OE1	GLN	H	197	−109.587	−48.228	−28.262	1.00	131.48	O
ATOM	5706	NE2	GLN	H	197	−110.143	−46.051	−28.303	1.00	131.48	N
ATOM	5707	C	GLN	H	197	−109.207	−46.879	−23.097	1.00	128.43	C
ATOM	5708	O	GLN	H	197	−109.925	−46.022	−22.565	1.00	128.38	O
ATOM	5709	N	THR	H	198	−108.180	−47.470	−22.474	1.00	125.73	N
ATOM	5710	CA	THR	H	198	−107.796	−47.158	−21.094	1.00	124.61	C
ATOM	5711	CB	THR	H	198	−107.122	−48.363	−20.388	1.00	124.84	C
ATOM	5712	OG1	THR	H	198	−106.301	−49.105	−21.306	1.00	124.99	O
ATOM	5713	CG2	THR	H	198	−108.135	−49.283	−19.708	1.00	124.58	C
ATOM	5714	C	THR	H	198	−106.987	−45.857	−20.999	1.00	123.61	C
ATOM	5715	O	THR	H	198	−106.191	−45.551	−21.896	1.00	123.40	O
ATOM	5716	N	TYR	H	199	−107.204	−45.094	−19.909	1.00	120.57	N
ATOM	5717	CA	TYR	H	199	−106.506	−43.832	−19.665	1.00	119.19	C
ATOM	5718	CB	TYR	H	199	−107.477	−42.643	−19.713	1.00	119.46	C
ATOM	5719	CG	TYR	H	199	−108.092	−42.453	−21.085	1.00	120.39	C
ATOM	5720	CD1	TYR	H	199	−109.468	−42.546	−21.275	1.00	120.86	C
ATOM	5721	CE1	TYR	H	199	−110.036	−42.391	−22.539	1.00	120.91	C
ATOM	5722	CZ	TYR	H	199	−109.221	−42.155	−23.635	1.00	121.46	C
ATOM	5723	OH	TYR	H	199	−109.762	−41.999	−24.888	1.00	122.60	O
ATOM	5724	CE2	TYR	H	199	−107.849	−42.073	−23.473	1.00	121.10	C
ATOM	5725	CD2	TYR	H	199	−107.293	−42.222	−22.204	1.00	120.87	C
ATOM	5726	C	TYR	H	199	−105.636	−43.860	−18.403	1.00	117.92	C
ATOM	5727	O	TYR	H	199	−106.150	−43.787	−17.280	1.00	117.83	O
ATOM	5728	N	ILE	H	200	−104.307	−44.000	−18.607	1.00	112.18	N
ATOM	5729	CA	ILE	H	200	−103.305	−44.070	−17.537	1.00	110.28	C
ATOM	5730	CB	ILE	H	200	−102.635	−45.478	−17.422	1.00	110.33	C
ATOM	5731	CG1	ILE	H	200	−101.813	−45.869	−18.686	1.00	110.02	C
ATOM	5732	CD1	ILE	H	200	−100.273	−45.895	−18.502	1.00	109.68	C
ATOM	5733	CG2	ILE	H	200	−103.663	−46.562	−17.076	1.00	109.77	C
ATOM	5734	C	ILE	H	200	−102.294	−42.915	−17.595	1.00	108.97	C
ATOM	5735	O	ILE	H	200	−101.857	−42.550	−18.690	1.00	108.81	O
ATOM	5736	N	CYS	H	201	−101.938	−42.331	−16.422	1.00	104.63	N
ATOM	5737	CA	CYS	H	201	−100.972	−41.234	−16.360	1.00	102.83	C
ATOM	5738	CB	CYS	H	201	−101.548	−39.967	−15.742	1.00	103.00	C
ATOM	5739	SG	CYS	H	201	−102.047	−40.124	−14.011	1.00	103.57	S
ATOM	5740	C	CYS	H	201	−99.664	−41.619	−15.735	1.00	101.34	C
ATOM	5741	O	CYS	H	201	−99.620	−42.123	−14.623	1.00	101.22	O
ATOM	5742	N	ASN	H	202	−98.597	−41.387	−16.472	1.00	97.30	N
ATOM	5743	CA	ASN	H	202	−97.247	−41.704	−16.069	1.00	95.57	C
ATOM	5744	CB	ASN	H	202	−96.462	−42.241	−17.251	1.00	95.80	C
ATOM	5745	CG	ASN	H	202	−97.176	−43.346	−17.972	1.00	96.46	C
ATOM	5746	OD1	ASN	H	202	−98.343	−43.214	−18.378	1.00	96.34	O
ATOM	5747	ND2	ASN	H	202	−96.477	−44.464	−18.152	1.00	98.40	N
ATOM	5748	C	ASN	H	202	−96.563	−40.507	−15.428	1.00	94.12	C
ATOM	5749	O	ASN	H	202	−96.055	−39.600	−16.099	1.00	93.94	O
ATOM	5750	N	VAL	H	203	−96.574	−40.524	−14.105	1.00	87.41	N
ATOM	5751	CA	VAL	H	203	−95.967	−39.525	−13.258	1.00	85.59	C
ATOM	5752	CB	VAL	H	203	−96.882	−39.258	−12.061	1.00	85.50	C
ATOM	5753	CG1	VAL	H	203	−96.265	−38.251	−11.108	1.00	85.70	C
ATOM	5754	CG2	VAL	H	203	−98.249	−38.784	−12.539	1.00	84.95	C
ATOM	5755	C	VAL	H	203	−94.577	−40.030	−12.858	1.00	84.64	C
ATOM	5756	O	VAL	H	203	−94.391	−41.218	−12.574	1.00	84.45	O
ATOM	5757	N	ASN	H	204	−93.588	−39.138	−12.902	1.00	83.70	N
ATOM	5758	CA	ASN	H	204	−92.224	−39.481	−12.540	1.00	82.43	C
ATOM	5759	CB	ASN	H	204	−91.418	−40.035	−13.723	1.00	82.54	C
ATOM	5760	CG	ASN	H	204	−89.922	−40.165	−13.482	1.00	83.30	C
ATOM	5761	OD1	ASN	H	204	−89.441	−40.517	−12.383	1.00	85.27	O
ATOM	5762	ND2	ASN	H	204	−89.140	−39.879	−14.517	1.00	83.81	N
ATOM	5763	C	ASN	H	204	−91.565	−38.291	−11.889	1.00	81.30	C
ATOM	5764	O	ASN	H	204	−91.286	−37.288	−12.550	1.00	81.32	O
ATOM	5765	N	HIS	H	205	−91.337	−38.414	−10.574	1.00	77.58	N
ATOM	5766	CA	HIS	H	205	−90.685	−37.427	−9.744	1.00	76.14	C
ATOM	5767	CB	HIS	H	205	−91.454	−37.230	−8.442	1.00	76.06	C
ATOM	5768	CG	HIS	H	205	−90.857	−36.229	−7.503	1.00	75.64	C
ATOM	5769	ND1	HIS	H	205	−90.239	−36.625	−6.336	1.00	76.03	N
ATOM	5770	CE1	HIS	H	205	−89.849	−35.513	−5.734	1.00	76.64	C
ATOM	5771	NE2	HIS	H	205	−90.180	−34.432	−6.441	1.00	77.05	N
ATOM	5772	CD2	HIS	H	205	−90.829	−34.877	−7.573	1.00	76.21	C
ATOM	5773	C	HIS	H	205	−89.299	−37.980	−9.517	1.00	75.44	C
ATOM	5774	O	HIS	H	205	−89.065	−38.743	−8.589	1.00	75.18	O
ATOM	5775	N	LYS	H	206	−88.385	−37.600	−10.417	1.00	73.96	N
ATOM	5776	CA	LYS	H	206	−86.979	−37.986	−10.447	1.00	73.15	C
ATOM	5777	CB	LYS	H	206	−86.281	−37.363	−11.656	1.00	73.27	C
ATOM	5778	CG	LYS	H	206	−86.794	−37.835	−13.003	1.00	74.94	C
ATOM	5779	CD	LYS	H	206	−87.115	−36.632	−13.910	1.00	78.37	C
ATOM	5780	CE	LYS	H	206	−87.147	−36.984	−15.395	1.00	79.68	C
ATOM	5781	NZ	LYS	H	206	−85.794	−37.337	−15.949	1.00	80.06	N
ATOM	5782	C	LYS	H	206	−86.209	−37.648	−9.163	1.00	72.47	C
ATOM	5783	O	LYS	H	206	−85.353	−38.461	−8.802	1.00	72.50	O
ATOM	5784	N	PRO	H	207	−86.462	−36.491	−8.455	1.00	70.56	N
ATOM	5785	CA	PRO	H	207	−85.697	−36.185	−7.225	1.00	70.13	C
ATOM	5786	CB	PRO	H	207	−86.322	−34.879	−6.743	1.00	69.80	C
ATOM	5787	CG	PRO	H	207	−86.924	−34.278	−7.905	1.00	70.09	C
ATOM	5788	CD	PRO	H	207	−87.425	−35.399	−8.735	1.00	70.58	C
ATOM	5789	C	PRO	H	207	−85.773	−37.227	−6.108	1.00	70.07	C
ATOM	5790	O	PRO	H	207	−84.820	−37.356	−5.335	1.00	69.87	O
ATOM	5791	N	SER	H	208	−86.916	−37.935	−6.018	1.00	68.21	N
ATOM	5792	CA	SER	H	208	−87.194	−38.973	−5.046	1.00	67.94	C
ATOM	5793	CB	SER	H	208	−88.539	−38.716	−4.385	1.00	67.92	C
ATOM	5794	OG	SER	H	208	−89.602	−38.909	−5.302	1.00	67.48	O
ATOM	5795	C	SER	H	208	−87.246	−40.314	−5.716	1.00	68.07	C
ATOM	5796	O	SER	H	208	−87.561	−41.284	−5.045	1.00	68.37	O
ATOM	5797	N	ASN	H	209	−86.987	−40.383	−7.039	1.00	68.59	N
ATOM	5798	CA	ASN	H	209	−87.007	−41.608	−7.863	1.00	69.03	C
ATOM	5799	CB	ASN	H	209	−85.849	−42.531	−7.490	1.00	68.43	C
ATOM	5800	CG	ASN	H	209	−85.528	−43.582	−8.510	1.00	67.30	C
ATOM	5801	OD1	ASN	H	209	−84.818	−44.533	−8.219	1.00	66.47	O
ATOM	5802	ND2	ASN	H	209	−86.032	−43.453	−9.735	1.00	66.92	N
ATOM	5803	C	ASN	H	209	−88.377	−42.353	−7.902	1.00	69.99	C
ATOM	5804	O	ASN	H	209	−88.433	−43.554	−8.197	1.00	70.02	O
ATOM	5805	N	THR	H	210	−89.471	−41.613	−7.631	1.00	72.45	N
ATOM	5806	CA	THR	H	210	−90.855	−42.086	−7.590	1.00	73.73	C
ATOM	5807	CB	THR	H	210	−91.646	−41.269	−6.551	1.00	73.38	C
ATOM	5808	OG1	THR	H	210	−91.020	−41.436	−5.287	1.00	73.71	O
ATOM	5809	CG2	THR	H	210	−93.102	−41.676	−6.445	1.00	73.49	C
ATOM	5810	C	THR	H	210	−91.535	−42.071	−8.946	1.00	74.90	C
ATOM	5811	O	THR	H	210	−92.022	−41.024	−9.360	1.00	75.20	O
ATOM	5812	N	LYS	H	211	−91.585	−43.231	−9.620	1.00	77.05	N
ATOM	5813	CA	LYS	H	211	−92.263	−43.437	−10.906	1.00	78.60	C
ATOM	5814	CB	LYS	H	211	−91.466	−44.407	−11.799	1.00	78.20	C
ATOM	5815	CG	LYS	H	211	−90.121	−43.868	−12.276	1.00	78.47	C
ATOM	5816	CD	LYS	H	211	−89.225	−44.961	−12.861	1.00	79.14	C
ATOM	5817	CE	LYS	H	211	−87.899	−45.180	−12.118	1.00	79.84	C
ATOM	5818	NZ	LYS	H	211	−88.045	−45.808	−10.756	1.00	79.07	N
ATOM	5819	C	LYS	H	211	−93.626	−44.036	−10.514	1.00	79.91	C
ATOM	5820	O	LYS	H	211	−93.659	−45.045	−9.812	1.00	80.45	O
ATOM	5821	N	VAL	H	212	−94.737	−43.412	−10.906	1.00	82.17	N
ATOM	5822	CA	VAL	H	212	−96.090	−43.875	−10.541	1.00	83.80	C
ATOM	5823	CB	VAL	H	212	−96.641	−42.980	−9.387	1.00	83.43	C
ATOM	5824	CG1	VAL	H	212	−98.161	−42.945	−9.333	1.00	82.71	C
ATOM	5825	CG2	VAL	H	212	−96.056	−43.399	−8.048	1.00	83.07	C
ATOM	5826	C	VAL	H	212	−97.043	−43.973	−11.768	1.00	85.51	C
ATOM	5827	O	VAL	H	212	−96.916	−43.183	−12.705	1.00	85.62	O
ATOM	5828	N	ASP	H	213	−97.978	−44.954	−11.767	1.00	91.75	N
ATOM	5829	CA	ASP	H	213	−98.956	−45.139	−12.847	1.00	93.82	C
ATOM	5830	CB	ASP	H	213	−98.589	−46.341	−13.728	1.00	93.63	C
ATOM	5831	CG	ASP	H	213	−97.548	−46.026	−14.798	1.00	94.16	C
ATOM	5832	OD1	ASP	H	213	−96.407	−45.655	−14.433	1.00	93.97	O
ATOM	5833	OD2	ASP	H	213	−97.872	−46.152	−15.999	1.00	95.62	O
ATOM	5834	C	ASP	H	213	−100.383	−45.216	−12.285	1.00	95.40	C
ATOM	5835	O	ASP	H	213	−100.652	−46.061	−11.428	1.00	95.72	O
ATOM	5836	N	LYS	H	214	−101.282	−44.302	−12.722	1.00	100.62	N
ATOM	5837	CA	LYS	H	214	−102.669	−44.262	−12.237	1.00	102.69	C
ATOM	5838	CB	LYS	H	214	−102.927	−43.032	−11.344	1.00	102.71	C
ATOM	5839	CG	LYS	H	214	−103.874	−43.291	−10.173	1.00	103.55	C
ATOM	5840	CD	LYS	H	214	−103.192	−44.189	−9.125	1.00	105.57	C
ATOM	5841	CE	LYS	H	214	−104.059	−44.491	−7.930	1.00	106.85	C
ATOM	5842	NZ	LYS	H	214	−103.355	−45.388	−6.978	1.00	107.17	N
ATOM	5843	C	LYS	H	214	−103.738	−44.391	−13.331	1.00	104.02	C
ATOM	5844	O	LYS	H	214	−103.780	−43.579	−14.257	1.00	104.21	O
ATOM	5845	N	LYS	H	215	−104.602	−45.424	−13.210	1.00	107.40	N
ATOM	5846	CA	LYS	H	215	−105.688	−45.687	−14.146	1.00	108.78	C
ATOM	5847	CB	LYS	H	215	−106.100	−47.176	−14.114	1.00	108.88	C
ATOM	5848	CG	LYS	H	215	−107.148	−47.597	−15.157	1.00	109.42	C
ATOM	5849	CD	LYS	H	215	−107.634	−49.047	−14.925	1.00	109.90	C
ATOM	5850	CE	LYS	H	215	−108.585	−49.581	−15.984	1.00	109.81	C
ATOM	5851	NZ	LYS	H	215	−109.153	−50.911	−15.614	1.00	109.19	N
ATOM	5852	C	LYS	H	215	−106.856	−44.787	−13.794	1.00	109.66	C
ATOM	5853	O	LYS	H	215	−107.389	−44.852	−12.682	1.00	109.51	O
ATOM	5854	N	VAL	H	216	−107.230	−43.924	−14.746	1.00	113.78	N
ATOM	5855	CA	VAL	H	216	−108.363	−43.014	−14.588	1.00	115.02	C
ATOM	5856	CB	VAL	H	216	−108.107	−41.543	−15.014	1.00	114.92	C
ATOM	5857	CG1	VAL	H	216	−109.154	−40.613	−14.400	1.00	115.00	C
ATOM	5858	CG2	VAL	H	216	−106.699	−41.087	−14.631	1.00	115.30	C
ATOM	5859	C	VAL	H	216	−109.536	−43.669	−15.330	1.00	115.97	C
ATOM	5860	O	VAL	H	216	−109.489	−43.867	−16.557	1.00	116.09	O
ATOM	5861	N	GLU	H	217	−110.555	−44.058	−14.540	1.00	117.62	N
ATOM	5862	CA	GLU	H	217	−111.782	−44.729	−14.961	1.00	118.53	C
ATOM	5863	CB	GLU	H	217	−111.995	−45.986	−14.109	1.00	118.74	C
ATOM	5864	CG	GLU	H	217	−111.067	−47.138	−14.433	1.00	119.59	C
ATOM	5865	CD	GLU	H	217	−111.166	−48.270	−13.432	1.00	120.38	C
ATOM	5866	OE1	GLU	H	217	−111.208	−49.441	−13.875	1.00	121.05	O
ATOM	5867	OE2	GLU	H	217	−111.207	−47.989	−12.209	1.00	119.83	O
ATOM	5868	C	GLU	H	217	−112.953	−43.808	−14.703	1.00	118.88	C
ATOM	5869	O	GLU	H	217	−112.821	−42.934	−13.834	1.00	118.97	O
ATOM	5870	N	PRO	H	218	−114.122	−44.009	−15.386	1.00	116.71	N
ATOM	5871	CA	PRO	H	218	−115.287	−43.133	−15.123	1.00	116.74	C
ATOM	5872	CB	PRO	H	218	−116.291	−43.519	−16.221	1.00	116.73	C
ATOM	5873	CG	PRO	H	218	−115.502	−44.323	−17.225	1.00	116.66	C
ATOM	5874	CD	PRO	H	218	−114.436	−45.003	−16.436	1.00	116.64	C
ATOM	5875	C	PRO	H	218	−115.854	−43.290	−13.704	1.00	116.70	C
ATOM	5876	O	PRO	H	218	−115.904	−44.408	−13.181	1.00	116.58	O
ATOM	5877	N	LYS	H	219	−116.237	−42.143	−13.088	1.00	113.24	N
ATOM	5878	CA	LYS	H	219	−116.788	−41.948	−11.735	1.00	113.26	C
ATOM	5879	CB	LYS	H	219	−117.941	−40.927	−11.762	1.00	113.15	C
ATOM	5880	C	LYS	H	219	−117.177	−43.217	−10.958	1.00	113.17	C
ATOM	5881	O	LYS	H	219	−116.309	−43.911	−10.428	1.00	113.03	O
TER	5882		LYS	H	219
ATOM	5883	N	GLU	L	1	−83.598	9.104	−8.215	1.00	89.00	N
ATOM	5884	CA	GLU	L	1	−83.105	8.099	−9.150	1.00	88.92	C
ATOM	5885	CB	GLU	L	1	−82.880	6.751	−8.461	1.00	89.36	C
ATOM	5886	CG	GLU	L	1	−84.070	6.181	−7.715	1.00	91.53	C
ATOM	5887	CD	GLU	L	1	−83.726	4.828	−7.121	1.00	95.85	C
ATOM	5888	OE1	GLU	L	1	−84.033	3.797	−7.766	1.00	97.73	O
ATOM	5889	OE2	GLU	L	1	−83.125	4.799	−6.020	1.00	97.18	O
ATOM	5890	C	GLU	L	1	−84.004	7.949	−10.356	1.00	88.12	C
ATOM	5891	O	GLU	L	1	−85.216	8.101	−10.217	1.00	88.16	O
ATOM	5892	N	ILE	L	2	−83.411	7.657	−11.540	1.00	80.34	N
ATOM	5893	CA	ILE	L	2	−84.157	7.483	−12.793	1.00	79.70	C
ATOM	5894	CB	ILE	L	2	−83.280	7.451	−14.089	1.00	79.60	C
ATOM	5895	CG1	ILE	L	2	−82.210	8.557	−14.067	1.00	79.33	C
ATOM	5896	CD1	ILE	L	2	−81.071	8.384	−15.048	1.00	79.74	C
ATOM	5897	CG2	ILE	L	2	−84.147	7.542	−15.369	1.00	78.97	C
ATOM	5898	C	ILE	L	2	−85.116	6.292	−12.684	1.00	79.51	C
ATOM	5899	O	ILE	L	2	−84.774	5.260	−12.087	1.00	79.69	O
ATOM	5900	N	VAL	L	3	−86.336	6.475	−13.222	1.00	75.05	N
ATOM	5901	CA	VAL	L	3	−87.387	5.480	−13.213	1.00	74.49	C
ATOM	5902	CB	VAL	L	3	−88.466	5.847	−12.180	1.00	74.17	C
ATOM	5903	CG1	VAL	L	3	−89.738	5.038	−12.386	1.00	73.26	C
ATOM	5904	CG2	VAL	L	3	−87.938	5.678	−10.762	1.00	73.55	C
ATOM	5905	C	VAL	L	3	−87.930	5.343	−14.619	1.00	74.81	C
ATOM	5906	O	VAL	L	3	−88.324	6.345	−15.213	1.00	75.07	O
ATOM	5907	N	LEU	L	4	−87.943	4.102	−15.150	1.00	76.54	N
ATOM	5908	CA	LEU	L	4	−88.444	3.802	−16.494	1.00	76.82	C
ATOM	5909	CB	LEU	L	4	−87.469	2.927	−17.283	1.00	76.43	C
ATOM	5910	CG	LEU	L	4	−86.023	3.376	−17.305	1.00	75.61	C
ATOM	5911	CD1	LEU	L	4	−85.152	2.333	−17.948	1.00	75.85	C
ATOM	5912	CD2	LEU	L	4	−85.867	4.665	−18.035	1.00	75.72	C
ATOM	5913	C	LEU	L	4	−89.832	3.173	−16.430	1.00	77.41	C
ATOM	5914	O	LEU	L	4	−90.056	2.200	−15.694	1.00	77.43	O
ATOM	5915	N	THR	L	5	−90.771	3.759	−17.190	1.00	81.19	N
ATOM	5916	CA	THR	L	5	−92.164	3.318	−17.228	1.00	81.79	C
ATOM	5917	CB	THR	L	5	−93.081	4.395	−16.653	1.00	81.50	C
ATOM	5918	OG1	THR	L	5	−92.466	4.961	−15.492	1.00	81.23	O
ATOM	5919	CG2	THR	L	5	−94.456	3.864	−16.325	1.00	81.01	C
ATOM	5920	C	THR	L	5	−92.589	2.850	−18.609	1.00	82.60	C
ATOM	5921	O	THR	L	5	−92.693	3.655	−19.545	1.00	82.60	O
ATOM	5922	N	GLN	L	6	−92.844	1.542	−18.718	1.00	86.45	N
ATOM	5923	CA	GLN	L	6	−93.272	0.915	−19.961	1.00	87.55	C
ATOM	5924	CB	GLN	L	6	−92.783	−0.532	−20.062	1.00	87.69	C
ATOM	5925	CG	GLN	L	6	−91.335	−0.717	−19.614	1.00	88.23	C
ATOM	5926	CD	GLN	L	6	−90.571	−1.688	−20.464	1.00	88.69	C
ATOM	5927	OE1	GLN	L	6	−90.813	−1.842	−21.674	1.00	89.57	O
ATOM	5928	NE2	GLN	L	6	−89.610	−2.339	−19.849	1.00	88.76	N
ATOM	5929	C	GLN	L	6	−94.794	1.027	−20.150	1.00	88.17	C
ATOM	5930	O	GLN	L	6	−95.549	0.843	−19.186	1.00	88.08	O
ATOM	5931	N	SER	L	7	−95.210	1.356	−21.406	1.00	92.93	N
ATOM	5932	CA	SER	L	7	−96.564	1.589	−21.944	1.00	93.33	C
ATOM	5933	CB	SER	L	7	−96.506	1.734	−23.455	1.00	93.66	C
ATOM	5934	OG	SER	L	7	−95.744	0.662	−24.002	1.00	94.08	O
ATOM	5935	C	SER	L	7	−97.621	0.545	−21.540	1.00	93.56	C
ATOM	5936	O	SER	L	7	−98.173	0.714	−20.438	1.00	94.05	O
ATOM	5937	N	PRO	L	8	−98.002	−0.509	−22.328	1.00	89.31	N
ATOM	5938	CA	PRO	L	8	−98.988	−1.432	−21.786	1.00	89.18	C
ATOM	5939	CB	PRO	L	8	−99.665	−1.986	−23.045	1.00	88.74	C
ATOM	5940	CG	PRO	L	8	−98.757	−1.659	−24.189	1.00	88.87	C
ATOM	5941	CD	PRO	L	8	−97.560	−0.968	−23.664	1.00	89.25	C
ATOM	5942	C	PRO	L	8	−98.220	−2.509	−21.001	1.00	89.49	C
ATOM	5943	O	PRO	L	8	−97.120	−2.908	−21.409	1.00	90.02	O
ATOM	5944	N	ALA	L	9	−98.759	−2.985	−19.873	1.00	88.96	N
ATOM	5945	CA	ALA	L	9	−98.053	−4.053	−19.169	1.00	88.68	C
ATOM	5946	CB	ALA	L	9	−98.765	−4.391	−17.872	1.00	88.39	C
ATOM	5947	C	ALA	L	9	−98.084	−5.251	−20.134	1.00	88.68	C
ATOM	5948	O	ALA	L	9	−97.112	−6.002	−20.221	1.00	89.05	O
ATOM	5949	N	THR	L	10	−99.207	−5.369	−20.898	1.00	87.79	N
ATOM	5950	CA	THR	L	10	−99.482	−6.385	−21.913	1.00	87.63	C
ATOM	5951	CB	THR	L	10	−100.425	−7.495	−21.408	1.00	87.57	C
ATOM	5952	OG1	THR	L	10	−100.164	−7.809	−20.032	1.00	87.90	O
ATOM	5953	CG2	THR	L	10	−100.347	−8.760	−22.273	1.00	87.29	C
ATOM	5954	C	THR	L	10	−100.075	−5.713	−23.137	1.00	87.50	C
ATOM	5955	O	THR	L	10	−100.917	−4.820	−23.010	1.00	87.67	O
ATOM	5956	N	LEU	L	11	−99.629	−6.162	−24.311	1.00	85.14	N
ATOM	5957	CA	LEU	L	11	−100.052	−5.694	−25.610	1.00	85.16	C
ATOM	5958	CB	LEU	L	11	−98.939	−4.864	−26.272	1.00	84.97	C
ATOM	5959	CG	LEU	L	11	−99.099	−4.581	−27.782	1.00	85.13	C
ATOM	5960	CD1	LEU	L	11	−100.036	−3.397	−28.052	1.00	84.72	C
ATOM	5961	CD2	LEU	L	11	−97.749	−4.410	−28.473	1.00	84.38	C
ATOM	5962	C	LEU	L	11	−100.430	−6.921	−26.449	1.00	85.59	C
ATOM	5963	O	LEU	L	11	−99.553	−7.668	−26.915	1.00	85.35	O
ATOM	5964	N	SER	L	12	−101.755	−7.126	−26.629	1.00	87.35	N
ATOM	5965	CA	SER	L	12	−102.331	−8.240	−27.392	1.00	87.63	C
ATOM	5966	CB	SER	L	12	−103.635	−8.699	−26.760	1.00	87.50	C
ATOM	5967	OG	SER	L	12	−103.508	−8.769	−25.348	1.00	87.38	O
ATOM	5968	C	SER	L	12	−102.526	−7.861	−28.853	1.00	88.07	C
ATOM	5969	O	SER	L	12	−103.264	−6.922	−29.161	1.00	87.95	O
ATOM	5970	N	LEU	L	13	−101.813	−8.565	−29.745	1.00	90.88	N
ATOM	5971	CA	LEU	L	13	−101.831	−8.335	−31.192	1.00	91.71	C
ATOM	5972	CB	LEU	L	13	−100.701	−7.378	−31.623	1.00	91.67	C
ATOM	5973	CG	LEU	L	13	−100.791	−5.903	−31.217	1.00	91.61	C
ATOM	5974	CD1	LEU	L	13	−102.052	−5.231	−31.759	1.00	91.18	C
ATOM	5975	CD2	LEU	L	13	−99.596	−5.163	−31.719	1.00	91.99	C
ATOM	5976	C	LEU	L	13	−101.728	−9.624	−31.998	1.00	92.38	C
ATOM	5977	O	LEU	L	13	−101.018	−10.548	−31.621	1.00	92.53	O
ATOM	5978	N	SER	L	14	−102.430	−9.669	−33.122	1.00	94.83	N
ATOM	5979	CA	SER	L	14	−102.440	−10.820	−34.029	1.00	95.63	C
ATOM	5980	CB	SER	L	14	−103.631	−10.708	−34.985	1.00	95.73	C
ATOM	5981	OG	SER	L	14	−104.781	−10.186	−34.330	1.00	96.70	O
ATOM	5982	C	SER	L	14	−101.129	−10.844	−34.826	1.00	95.79	C
ATOM	5983	O	SER	L	14	−100.555	−9.778	−35.019	1.00	95.83	O
ATOM	5984	N	PRO	L	15	−100.625	−11.998	−35.321	1.00	95.86	N
ATOM	5985	CA	PRO	L	15	−99.367	−11.968	−36.100	1.00	96.06	C
ATOM	5986	CB	PRO	L	15	−99.108	−13.443	−36.424	1.00	95.91	C
ATOM	5987	CG	PRO	L	15	−99.911	−14.201	−35.411	1.00	95.88	C
ATOM	5988	CD	PRO	L	15	−101.133	−13.376	−35.187	1.00	95.86	C
ATOM	5989	C	PRO	L	15	−99.449	−11.099	−37.359	1.00	96.26	C
ATOM	5990	O	PRO	L	15	−100.544	−10.705	−37.754	1.00	96.51	O
ATOM	5991	N	GLY	L	16	−98.295	−10.773	−37.943	1.00	98.11	N
ATOM	5992	CA	GLY	L	16	−98.181	−9.941	−39.143	1.00	98.33	C
ATOM	5993	C	GLY	L	16	−98.383	−8.449	−38.937	1.00	98.54	C
ATOM	5994	O	GLY	L	16	−97.993	−7.651	−39.799	1.00	98.67	O
ATOM	5995	N	GLU	L	17	−98.983	−8.062	−37.787	1.00	99.90	N
ATOM	5996	CA	GLU	L	17	−99.288	−6.683	−37.389	1.00	100.20	C
ATOM	5997	CB	GLU	L	17	−100.384	−6.688	−36.311	1.00	100.28	C
ATOM	5998	CG	GLU	L	17	−101.685	−7.324	−36.768	1.00	101.97	C
ATOM	5999	CD	GLU	L	17	−102.932	−6.814	−36.069	1.00	104.11	C
ATOM	6000	OE1	GLU	L	17	−103.215	−7.262	−34.930	1.00	104.25	O
ATOM	6001	OE2	GLU	L	17	−103.634	−5.966	−36.673	1.00	105.22	O
ATOM	6002	C	GLU	L	17	−98.093	−5.813	−36.901	1.00	100.05	C
ATOM	6003	O	GLU	L	17	−97.050	−6.343	−36.489	1.00	100.22	O
ATOM	6004	N	ARG	L	18	−98.274	−4.462	−36.940	1.00	98.61	N
ATOM	6005	CA	ARG	L	18	−97.294	−3.490	−36.448	1.00	97.96	C
ATOM	6006	CB	ARG	L	18	−97.411	−2.125	−37.150	1.00	98.00	C
ATOM	6007	C	ARG	L	18	−97.512	−3.364	−34.938	1.00	97.49	C
ATOM	6008	O	ARG	L	18	−98.662	−3.277	−34.478	1.00	97.17	O
ATOM	6009	N	ALA	L	19	−96.403	−3.387	−34.168	1.00	96.77	N
ATOM	6010	CA	ALA	L	19	−96.424	−3.329	−32.702	1.00	96.23	C
ATOM	6011	CB	ALA	L	19	−95.987	−4.681	−32.146	1.00	96.39	C
ATOM	6012	C	ALA	L	19	−95.547	−2.230	−32.103	1.00	95.76	C
ATOM	6013	O	ALA	L	19	−94.357	−2.166	−32.434	1.00	95.97	O
ATOM	6014	N	THR	L	20	−96.110	−1.376	−31.214	1.00	91.20	N
ATOM	6015	CA	THR	L	20	−95.293	−0.340	−30.572	1.00	90.40	C
ATOM	6016	CB	THR	L	20	−95.325	1.056	−31.230	1.00	90.54	C
ATOM	6017	OG1	THR	L	20	−96.588	1.682	−31.029	1.00	90.68	O
ATOM	6018	CG2	THR	L	20	−94.868	1.074	−32.696	1.00	89.99	C
ATOM	6019	C	THR	L	20	−95.401	−0.299	−29.058	1.00	89.89	C
ATOM	6020	O	THR	L	20	−96.507	−0.211	−28.515	1.00	89.67	O
ATOM	6021	N	ILE	L	21	−94.216	−0.348	−28.391	1.00	89.06	N
ATOM	6022	CA	ILE	L	21	−93.995	−0.313	−26.942	1.00	88.32	C
ATOM	6023	CB	ILE	L	21	−93.116	−1.528	−26.499	1.00	88.77	C
ATOM	6024	CG1	ILE	L	21	−93.768	−2.851	−26.920	1.00	88.67	C
ATOM	6025	CD1	ILE	L	21	−92.833	−3.954	−27.076	1.00	89.74	C
ATOM	6026	CG2	ILE	L	21	−92.802	−1.523	−24.965	1.00	89.13	C
ATOM	6027	C	ILE	L	21	−93.336	1.017	−26.593	1.00	87.50	C
ATOM	6028	O	ILE	L	21	−92.492	1.502	−27.343	1.00	87.42	O
ATOM	6029	N	THR	L	22	−93.711	1.580	−25.442	1.00	86.61	N
ATOM	6030	CA	THR	L	22	−93.228	2.852	−24.892	1.00	85.95	C
ATOM	6031	CB	THR	L	22	−94.429	3.829	−24.756	1.00	85.95	C
ATOM	6032	OG1	THR	L	22	−94.598	4.524	−25.986	1.00	85.76	O
ATOM	6033	CG2	THR	L	22	−94.339	4.803	−23.539	1.00	85.55	C
ATOM	6034	C	THR	L	22	−92.460	2.679	−23.572	1.00	85.64	C
ATOM	6035	O	THR	L	22	−92.794	1.806	−22.769	1.00	85.64	O
ATOM	6036	N	CYS	L	23	−91.430	3.531	−23.376	1.00	84.41	N
ATOM	6037	CA	CYS	L	23	−90.581	3.635	−22.193	1.00	83.87	C
ATOM	6038	CB	CYS	L	23	−89.210	2.993	−22.411	1.00	83.55	C
ATOM	6039	SG	CYS	L	23	−88.246	2.756	−20.884	1.00	83.84	S
ATOM	6040	C	CYS	L	23	−90.476	5.130	−21.926	1.00	83.58	C
ATOM	6041	O	CYS	L	23	−90.122	5.901	−22.825	1.00	83.61	O
ATOM	6042	N	ARG	L	24	−90.854	5.547	−20.722	1.00	86.10	N
ATOM	6043	CA	ARG	L	24	−90.808	6.952	−20.364	1.00	85.89	C
ATOM	6044	CB	ARG	L	24	−92.213	7.501	−20.108	1.00	86.58	C
ATOM	6045	CG	ARG	L	24	−92.329	9.003	−20.355	1.00	89.45	C
ATOM	6046	CD	ARG	L	24	−93.738	9.387	−20.754	1.00	93.99	C
ATOM	6047	NE	ARG	L	24	−94.140	8.740	−22.011	1.00	97.92	N
ATOM	6048	CZ	ARG	L	24	−95.395	8.676	−22.464	1.00	99.98	C
ATOM	6049	NH1	ARG	L	24	−96.391	9.220	−21.767	1.00	100.74	N
ATOM	6050	NH2	ARG	L	24	−95.661	8.067	−23.617	1.00	100.60	N
ATOM	6051	C	ARG	L	24	−89.905	7.151	−19.167	1.00	84.88	C
ATOM	6052	O	ARG	L	24	−90.261	6.760	−18.045	1.00	84.96	O
ATOM	6053	N	ALA	L	25	−88.724	7.744	−19.412	1.00	81.15	N
ATOM	6054	CA	ALA	L	25	−87.731	8.027	−18.382	1.00	79.72	C
ATOM	6055	CB	ALA	L	25	−86.380	8.312	−19.017	1.00	79.78	C
ATOM	6056	C	ALA	L	25	−88.200	9.231	−17.572	1.00	78.88	C
ATOM	6057	O	ALA	L	25	−88.784	10.167	−18.138	1.00	78.99	O
ATOM	6058	N	SER	L	26	−87.966	9.206	−16.247	1.00	76.82	N
ATOM	6059	CA	SER	L	26	−88.358	10.287	−15.348	1.00	75.42	C
ATOM	6060	CB	SER	L	26	−88.450	9.772	−13.915	1.00	75.49	C
ATOM	6061	OG	SER	L	26	−87.222	9.221	−13.472	1.00	75.52	O
ATOM	6062	C	SER	L	26	−87.406	11.488	−15.437	1.00	74.61	C
ATOM	6063	O	SER	L	26	−87.717	12.544	−14.900	1.00	74.72	O
ATOM	6064	N	GLN	L	27	−86.253	11.323	−16.107	1.00	72.38	N
ATOM	6065	CA	GLN	L	27	−85.220	12.338	−16.288	1.00	70.85	C
ATOM	6066	CB	GLN	L	27	−84.048	12.033	−15.370	1.00	71.05	C
ATOM	6067	CG	GLN	L	27	−84.312	12.084	−13.891	1.00	72.55	C
ATOM	6068	CD	GLN	L	27	−83.007	11.927	−13.147	1.00	75.22	C
ATOM	6069	OE1	GLN	L	27	−82.991	11.733	−11.922	1.00	77.67	O
ATOM	6070	NE2	GLN	L	27	−81.878	12.001	−13.860	1.00	74.71	N
ATOM	6071	C	GLN	L	27	−84.659	12.234	−17.689	1.00	69.65	C
ATOM	6072	O	GLN	L	27	−84.826	11.201	−18.338	1.00	69.54	O
ATOM	6073	N	TYR	L	28	−83.938	13.270	−18.144	1.00	67.82	N
ATOM	6074	CA	TYR	L	28	−83.315	13.256	−19.469	1.00	66.27	C
ATOM	6075	CB	TYR	L	28	−82.720	14.647	−19.814	1.00	65.44	C
ATOM	6076	CG	TYR	L	28	−82.242	14.748	−21.246	1.00	62.81	C
ATOM	6077	CD1	TYR	L	28	−83.140	14.945	−22.287	1.00	60.19	C
ATOM	6078	CE1	TYR	L	28	−82.712	15.014	−23.616	1.00	60.09	C
ATOM	6079	CZ	TYR	L	28	−81.367	14.853	−23.920	1.00	59.59	C
ATOM	6080	OH	TYR	L	28	−80.976	14.901	−25.241	1.00	59.93	O
ATOM	6081	CE2	TYR	L	28	−80.448	14.675	−22.895	1.00	59.81	C
ATOM	6082	CD2	TYR	L	28	−80.891	14.616	−21.566	1.00	61.47	C
ATOM	6083	C	TYR	L	28	−82.227	12.130	−19.499	1.00	65.99	C
ATOM	6084	O	TYR	L	28	−81.359	12.080	−18.619	1.00	65.99	O
ATOM	6085	N	VAL	L	29	−82.307	11.221	−20.474	1.00	63.65	N
ATOM	6086	CA	VAL	L	29	−81.330	10.143	−20.565	1.00	63.33	C
ATOM	6087	CB	VAL	L	29	−81.883	8.722	−20.249	1.00	63.11	C
ATOM	6088	CG1	VAL	L	29	−82.900	8.275	−21.283	1.00	62.31	C
ATOM	6089	CG2	VAL	L	29	−82.446	8.626	−18.831	1.00	62.70	C
ATOM	6090	C	VAL	L	29	−80.584	10.181	−21.876	1.00	63.57	C
ATOM	6091	O	VAL	L	29	−79.775	9.281	−22.153	1.00	63.59	O
ATOM	6092	N	GLY	L	30	−80.845	11.218	−22.662	1.00	64.62	N
ATOM	6093	CA	GLY	L	30	−80.229	11.366	−23.972	1.00	64.86	C
ATOM	6094	C	GLY	L	30	−80.687	10.222	−24.847	1.00	64.90	C
ATOM	6095	O	GLY	L	30	−81.855	9.848	−24.790	1.00	64.96	O
ATOM	6096	N	SER	L	31	−79.789	9.641	−25.626	1.00	66.85	N
ATOM	6097	CA	SER	L	31	−80.160	8.525	−26.486	1.00	67.60	C
ATOM	6098	CB	SER	L	31	−79.676	8.789	−27.908	1.00	67.46	C
ATOM	6099	OG	SER	L	31	−78.259	8.838	−27.958	1.00	68.34	O
ATOM	6100	C	SER	L	31	−79.553	7.209	−25.949	1.00	68.05	C
ATOM	6101	O	SER	L	31	−79.537	6.187	−26.654	1.00	68.16	O
ATOM	6102	N	TYR	L	32	−79.038	7.245	−24.705	1.00	68.98	N
ATOM	6103	CA	TYR	L	32	−78.390	6.098	−24.101	1.00	68.93	C
ATOM	6104	CB	TYR	L	32	−77.203	6.540	−23.233	1.00	68.85	C
ATOM	6105	CG	TYR	L	32	−76.275	7.517	−23.913	1.00	68.85	C
ATOM	6106	CD1	TYR	L	32	−75.477	7.123	−24.981	1.00	68.62	C
ATOM	6107	CE1	TYR	L	32	−74.636	8.030	−25.628	1.00	69.48	C
ATOM	6108	CZ	TYR	L	32	−74.565	9.342	−25.188	1.00	68.65	C
ATOM	6109	OH	TYR	L	32	−73.723	10.220	−25.823	1.00	68.17	O
ATOM	6110	CE2	TYR	L	32	−75.337	9.752	−24.114	1.00	69.22	C
ATOM	6111	CD2	TYR	L	32	−76.191	8.842	−23.487	1.00	69.84	C
ATOM	6112	C	TYR	L	32	−79.343	5.149	−23.374	1.00	69.13	C
ATOM	6113	O	TYR	L	32	−79.173	4.893	−22.172	1.00	69.45	O
ATOM	6114	N	LEU	L	33	−80.338	4.620	−24.111	1.00	69.39	N
ATOM	6115	CA	LEU	L	33	−81.322	3.663	−23.592	1.00	69.21	C
ATOM	6116	CB	LEU	L	33	−82.734	4.277	−23.585	1.00	68.46	C
ATOM	6117	CG	LEU	L	33	−83.871	3.332	−23.289	1.00	67.58	C
ATOM	6118	CD1	LEU	L	33	−84.932	3.981	−22.450	1.00	66.45	C
ATOM	6119	CD2	LEU	L	33	−84.435	2.734	−24.551	1.00	66.54	C
ATOM	6120	C	LEU	L	33	−81.253	2.322	−24.409	1.00	69.54	C
ATOM	6121	O	LEU	L	33	−81.075	2.353	−25.634	1.00	69.48	O
ATOM	6122	N	ASN	L	34	−81.395	1.160	−23.726	1.00	69.21	N
ATOM	6123	CA	ASN	L	34	−81.354	−0.137	−24.394	1.00	69.16	C
ATOM	6124	CB	ASN	L	34	−80.198	−0.975	−23.892	1.00	69.25	C
ATOM	6125	CG	ASN	L	34	−78.849	−0.323	−24.010	1.00	68.89	C
ATOM	6126	OD1	ASN	L	34	−78.531	0.370	−24.980	1.00	69.33	O
ATOM	6127	ND2	ASN	L	34	−78.024	−0.530	−23.008	1.00	67.82	N
ATOM	6128	C	ASN	L	34	−82.650	−0.889	−24.231	1.00	69.14	C
ATOM	6129	O	ASN	L	34	−83.387	−0.656	−23.268	1.00	69.19	O
ATOM	6130	N	TRP	L	35	−82.925	−1.789	−25.199	1.00	67.73	N
ATOM	6131	CA	TRP	L	35	−84.099	−2.654	−25.283	1.00	67.27	C
ATOM	6132	CB	TRP	L	35	−84.932	−2.329	−26.539	1.00	67.21	C
ATOM	6133	CG	TRP	L	35	−85.741	−1.060	−26.474	1.00	66.74	C
ATOM	6134	CD1	TRP	L	35	−85.421	0.143	−27.035	1.00	66.52	C
ATOM	6135	NE1	TRP	L	35	−86.415	1.068	−26.782	1.00	65.54	N
ATOM	6136	CE2	TRP	L	35	−87.413	0.463	−26.069	1.00	64.58	C
ATOM	6137	CD2	TRP	L	35	−87.026	−0.884	−25.859	1.00	64.96	C
ATOM	6138	CE3	TRP	L	35	−87.877	−1.723	−25.131	1.00	64.93	C
ATOM	6139	CZ3	TRP	L	35	−89.082	−1.206	−24.654	1.00	66.19	C
ATOM	6140	CH2	TRP	L	35	−89.442	0.131	−24.882	1.00	65.61	C
ATOM	6141	CZ2	TRP	L	35	−88.623	0.983	−25.590	1.00	64.83	C
ATOM	6142	C	TRP	L	35	−83.669	−4.127	−25.304	1.00	67.29	C
ATOM	6143	O	TRP	L	35	−82.820	−4.533	−26.114	1.00	67.16	O
ATOM	6144	N	TYR	L	36	−84.255	−4.924	−24.404	1.00	67.91	N
ATOM	6145	CA	TYR	L	36	−83.976	−6.350	−24.282	1.00	68.00	C
ATOM	6146	CB	TYR	L	36	−83.469	−6.681	−22.860	1.00	67.89	C
ATOM	6147	CG	TYR	L	36	−82.120	−6.066	−22.548	1.00	68.25	C
ATOM	6148	CD1	TYR	L	36	−82.022	−4.778	−22.030	1.00	67.50	C
ATOM	6149	CE1	TYR	L	36	−80.786	−4.178	−21.813	1.00	67.54	C
ATOM	6150	CZ	TYR	L	36	−79.624	−4.878	−22.084	1.00	67.87	C
ATOM	6151	OH	TYR	L	36	−78.406	−4.290	−21.837	1.00	68.43	O
ATOM	6152	CE2	TYR	L	36	−79.693	−6.165	−22.593	1.00	68.13	C
ATOM	6153	CD2	TYR	L	36	−80.938	−6.750	−22.825	1.00	68.33	C
ATOM	6154	C	TYR	L	36	−85.218	−7.145	−24.578	1.00	68.21	C
ATOM	6155	O	TYR	L	36	−86.330	−6.679	−24.296	1.00	68.38	O
ATOM	6156	N	GLN	L	37	−85.047	−8.355	−25.124	1.00	70.41	N
ATOM	6157	CA	GLN	L	37	−86.171	−9.249	−25.404	1.00	70.69	C
ATOM	6158	CB	GLN	L	37	−86.217	−9.637	−26.884	1.00	70.79	C
ATOM	6159	CG	GLN	L	37	−87.418	−10.520	−27.247	1.00	71.62	C
ATOM	6160	CD	GLN	L	37	−87.155	−11.323	−28.493	1.00	72.47	C
ATOM	6161	OE1	GLN	L	37	−86.164	−12.081	−28.566	1.00	72.90	O
ATOM	6162	NE2	GLN	L	37	−88.040	−11.177	−29.500	1.00	71.79	N
ATOM	6163	C	GLN	L	37	−86.013	−10.494	−24.545	1.00	70.52	C
ATOM	6164	O	GLN	L	37	−84.967	−11.132	−24.592	1.00	70.54	O
ATOM	6165	N	GLN	L	38	−87.038	−10.860	−23.775	1.00	70.53	N
ATOM	6166	CA	GLN	L	38	−86.931	−12.057	−22.949	1.00	70.45	C
ATOM	6167	CB	GLN	L	38	−86.840	−11.705	−21.480	1.00	69.65	C
ATOM	6168	CG	GLN	L	38	−86.360	−12.875	−20.682	1.00	67.53	C
ATOM	6169	CD	GLN	L	38	−86.403	−12.621	−19.208	1.00	65.49	C
ATOM	6170	OE1	GLN	L	38	−87.137	−11.746	−18.711	1.00	64.80	O
ATOM	6171	NE2	GLN	L	38	−85.617	−13.401	−18.475	1.00	64.47	N
ATOM	6172	C	GLN	L	38	−87.991	−13.132	−23.217	1.00	71.40	C
ATOM	6173	O	GLN	L	38	−89.150	−13.018	−22.787	1.00	71.38	O
ATOM	6174	N	LYS	L	39	−87.566	−14.201	−23.925	1.00	74.27	N
ATOM	6175	CA	LYS	L	39	−88.414	−15.349	−24.242	1.00	75.11	C
ATOM	6176	CB	LYS	L	39	−87.917	−16.069	−25.506	1.00	75.03	C
ATOM	6177	CG	LYS	L	39	−88.706	−15.584	−26.739	1.00	76.39	C
ATOM	6178	CD	LYS	L	39	−88.360	−16.236	−28.081	1.00	77.40	C
ATOM	6179	CE	LYS	L	39	−87.221	−15.555	−28.788	1.00	78.26	C
ATOM	6180	NZ	LYS	L	39	−85.899	−16.095	−28.348	1.00	80.80	N
ATOM	6181	C	LYS	L	39	−88.491	−16.269	−23.017	1.00	75.58	C
ATOM	6182	O	LYS	L	39	−87.502	−16.370	−22.291	1.00	75.90	O
ATOM	6183	N	PRO	L	40	−89.644	−16.914	−22.719	1.00	76.29	N
ATOM	6184	CA	PRO	L	40	−89.708	−17.786	−21.518	1.00	76.35	C
ATOM	6185	CB	PRO	L	40	−91.147	−18.292	−21.501	1.00	76.20	C
ATOM	6186	CG	PRO	L	40	−91.894	−17.355	−22.405	1.00	76.93	C
ATOM	6187	CD	PRO	L	40	−90.925	−16.909	−23.450	1.00	76.38	C
ATOM	6188	C	PRO	L	40	−88.664	−18.916	−21.460	1.00	76.28	C
ATOM	6189	O	PRO	L	40	−88.345	−19.556	−22.485	1.00	75.89	O
ATOM	6190	N	GLY	L	41	−88.107	−19.098	−20.254	1.00	75.59	N
ATOM	6191	CA	GLY	L	41	−87.064	−20.078	−19.974	1.00	75.41	C
ATOM	6192	C	GLY	L	41	−85.731	−19.660	−20.566	1.00	75.49	C
ATOM	6193	O	GLY	L	41	−84.851	−20.497	−20.835	1.00	75.64	O
ATOM	6194	N	GLN	L	42	−85.586	−18.334	−20.781	1.00	74.30	N
ATOM	6195	CA	GLN	L	42	−84.397	−17.742	−21.368	1.00	73.61	C
ATOM	6196	CB	GLN	L	42	−84.606	−17.525	−22.862	1.00	73.45	C
ATOM	6197	CG	GLN	L	42	−84.387	−18.753	−23.706	1.00	74.36	C
ATOM	6198	CD	GLN	L	42	−84.748	−18.410	−25.116	1.00	77.03	C
ATOM	6199	OE1	GLN	L	42	−84.038	−17.674	−25.821	1.00	77.97	O
ATOM	6200	NE2	GLN	L	42	−85.886	−18.913	−25.555	1.00	79.35	N
ATOM	6201	C	GLN	L	42	−84.012	−16.443	−20.711	1.00	73.06	C
ATOM	6202	O	GLN	L	42	−84.839	−15.780	−20.086	1.00	73.00	O
ATOM	6203	N	ALA	L	43	−82.740	−16.086	−20.869	1.00	70.82	N
ATOM	6204	CA	ALA	L	43	−82.159	−14.862	−20.351	1.00	70.31	C
ATOM	6205	CB	ALA	L	43	−80.642	−15.010	−20.300	1.00	70.14	C
ATOM	6206	C	ALA	L	43	−82.520	−13.713	−21.290	1.00	70.06	C
ATOM	6207	O	ALA	L	43	−82.668	−13.970	−22.495	1.00	70.12	O
ATOM	6208	N	PRO	L	44	−82.621	−12.445	−20.795	1.00	68.44	N
ATOM	6209	CA	PRO	L	44	−82.891	−11.307	−21.703	1.00	68.13	C
ATOM	6210	CB	PRO	L	44	−82.750	−10.099	−20.791	1.00	68.16	C
ATOM	6211	CG	PRO	L	44	−83.034	−10.619	−19.432	1.00	68.17	C
ATOM	6212	CD	PRO	L	44	−82.459	−11.985	−19.402	1.00	68.24	C
ATOM	6213	C	PRO	L	44	−81.876	−11.226	−22.844	1.00	68.23	C
ATOM	6214	O	PRO	L	44	−80.758	−11.726	−22.700	1.00	68.47	O
ATOM	6215	N	ARG	L	45	−82.266	−10.642	−23.989	1.00	70.66	N
ATOM	6216	CA	ARG	L	45	−81.416	−10.533	−25.184	1.00	71.08	C
ATOM	6217	CB	ARG	L	45	−81.934	−11.471	−26.279	1.00	71.21	C
ATOM	6218	CG	ARG	L	45	−81.142	−11.415	−27.568	1.00	73.90	C
ATOM	6219	CD	ARG	L	45	−81.430	−12.596	−28.471	1.00	79.03	C
ATOM	6220	NE	ARG	L	45	−80.438	−12.683	−29.554	1.00	84.54	N
ATOM	6221	CZ	ARG	L	45	−80.690	−12.402	−30.835	1.00	87.00	C
ATOM	6222	NH1	ARG	L	45	−81.918	−12.030	−31.216	1.00	87.47	N
ATOM	6223	NH2	ARG	L	45	−79.723	−12.505	−31.749	1.00	86.89	N
ATOM	6224	C	ARG	L	45	−81.367	−9.117	−25.714	1.00	70.91	C
ATOM	6225	O	ARG	L	45	−82.420	−8.556	−26.019	1.00	71.15	O
ATOM	6226	N	LEU	L	46	−80.163	−8.546	−25.857	1.00	67.97	N
ATOM	6227	CA	LEU	L	46	−80.068	−7.188	−26.379	1.00	67.99	C
ATOM	6228	CB	LEU	L	46	−78.637	−6.625	−26.287	1.00	67.90	C
ATOM	6229	CG	LEU	L	46	−78.428	−5.211	−26.816	1.00	66.29	C
ATOM	6230	CD1	LEU	L	46	−78.915	−4.190	−25.840	1.00	65.28	C
ATOM	6231	CD2	LEU	L	46	−77.002	−4.987	−27.135	1.00	65.27	C
ATOM	6232	C	LEU	L	46	−80.601	−7.154	−27.807	1.00	68.29	C
ATOM	6233	O	LEU	L	46	−80.152	−7.933	−28.653	1.00	68.46	O
ATOM	6234	N	LEU	L	47	−81.579	−6.270	−28.044	1.00	68.06	N
ATOM	6235	CA	LEU	L	47	−82.283	−6.067	−29.308	1.00	68.32	C
ATOM	6236	CB	LEU	L	47	−83.743	−5.852	−28.923	1.00	68.34	C
ATOM	6237	CG	LEU	L	47	−84.817	−6.605	−29.597	1.00	68.82	C
ATOM	6238	CD1	LEU	L	47	−84.498	−8.086	−29.676	1.00	69.06	C
ATOM	6239	CD2	LEU	L	47	−86.095	−6.363	−28.862	1.00	69.14	C
ATOM	6240	C	LEU	L	47	−81.796	−4.780	−29.959	1.00	68.67	C
ATOM	6241	O	LEU	L	47	−81.148	−4.803	−31.017	1.00	68.41	O
ATOM	6242	N	ILE	L	48	−82.145	−3.649	−29.306	1.00	69.72	N
ATOM	6243	CA	ILE	L	48	−81.815	−2.284	−29.689	1.00	70.11	C
ATOM	6244	CB	ILE	L	48	−83.112	−1.431	−29.887	1.00	70.29	C
ATOM	6245	CG1	ILE	L	48	−84.065	−2.014	−30.955	1.00	70.86	C
ATOM	6246	CD1	ILE	L	48	−83.492	−2.138	−32.379	1.00	71.97	C
ATOM	6247	CG2	ILE	L	48	−82.829	0.066	−30.109	1.00	70.03	C
ATOM	6248	C	ILE	L	48	−80.942	−1.687	−28.602	1.00	70.39	C
ATOM	6249	O	ILE	L	48	−81.302	−1.745	−27.420	1.00	70.31	O
ATOM	6250	N	TYR	L	49	−79.810	−1.099	−28.989	1.00	70.70	N
ATOM	6251	CA	TYR	L	49	−78.968	−0.435	−28.010	1.00	71.20	C
ATOM	6252	CB	TYR	L	49	−77.590	−1.069	−27.911	1.00	70.96	C
ATOM	6253	CG	TYR	L	49	−76.714	−0.865	−29.117	1.00	71.03	C
ATOM	6254	CD1	TYR	L	49	−75.752	0.141	−29.142	1.00	70.52	C
ATOM	6255	CE1	TYR	L	49	−74.926	0.328	−30.249	1.00	70.02	C
ATOM	6256	CZ	TYR	L	49	−75.042	−0.514	−31.342	1.00	71.17	C
ATOM	6257	OH	TYR	L	49	−74.224	−0.342	−32.434	1.00	73.08	O
ATOM	6258	CE2	TYR	L	49	−75.972	−1.545	−31.326	1.00	71.85	C
ATOM	6259	CD2	TYR	L	49	−76.808	−1.707	−30.220	1.00	71.13	C
ATOM	6260	C	TYR	L	49	−78.919	1.044	−28.346	1.00	71.57	C
ATOM	6261	O	TYR	L	49	−79.238	1.408	−29.469	1.00	71.66	O
ATOM	6262	N	ASP	L	50	−78.564	1.905	−27.395	1.00	74.27	N
ATOM	6263	CA	ASP	L	50	−78.497	3.349	−27.653	1.00	75.00	C
ATOM	6264	CB	ASP	L	50	−77.139	3.735	−28.250	1.00	74.83	C
ATOM	6265	CG	ASP	L	50	−75.967	3.734	−27.284	1.00	75.63	C
ATOM	6266	OD1	ASP	L	50	−76.147	3.291	−26.100	1.00	75.34	O
ATOM	6267	OD2	ASP	L	50	−74.876	4.166	−27.694	1.00	77.19	O
ATOM	6268	C	ASP	L	50	−79.668	3.901	−28.491	1.00	75.23	C
ATOM	6269	O	ASP	L	50	−79.471	4.380	−29.597	1.00	75.08	O
ATOM	6270	N	ALA	L	51	−80.886	3.792	−27.941	1.00	77.17	N
ATOM	6271	CA	ALA	L	51	−82.191	4.225	−28.464	1.00	77.67	C
ATOM	6272	CB	ALA	L	51	−82.332	5.731	−28.423	1.00	77.83	C
ATOM	6273	C	ALA	L	51	−82.707	3.685	−29.785	1.00	78.01	C
ATOM	6274	O	ALA	L	51	−83.899	3.370	−29.859	1.00	78.23	O
ATOM	6275	N	SER	L	52	−81.851	3.588	−30.815	1.00	79.08	N
ATOM	6276	CA	SER	L	52	−82.236	3.167	−32.165	1.00	79.89	C
ATOM	6277	CB	SER	L	52	−82.583	4.422	−32.960	1.00	79.80	C
ATOM	6278	OG	SER	L	52	−81.464	5.303	−32.972	1.00	80.89	O
ATOM	6279	C	SER	L	52	−81.107	2.426	−32.902	1.00	80.36	C
ATOM	6280	O	SER	L	52	−80.630	2.898	−33.927	1.00	80.53	O
ATOM	6281	N	ASN	L	53	−80.655	1.307	−32.399	1.00	79.99	N
ATOM	6282	CA	ASN	L	53	−79.569	0.605	−33.068	1.00	81.01	C
ATOM	6283	CB	ASN	L	53	−78.217	0.976	−32.453	1.00	81.07	C
ATOM	6284	CG	ASN	L	53	−77.521	2.098	−33.126	1.00	81.94	C
ATOM	6285	OD1	ASN	L	53	−77.719	3.262	−32.801	1.00	83.25	O
ATOM	6286	ND2	ASN	L	53	−76.688	1.768	−34.084	1.00	83.66	N
ATOM	6287	C	ASN	L	53	−79.799	−0.856	−32.911	1.00	81.48	C
ATOM	6288	O	ASN	L	53	−79.855	−1.332	−31.775	1.00	81.69	O
ATOM	6289	N	ARG	L	54	−79.942	−1.578	−34.030	1.00	83.24	N
ATOM	6290	CA	ARG	L	54	−80.161	−3.016	−33.967	1.00	83.75	C
ATOM	6291	CB	ARG	L	54	−80.652	−3.569	−35.300	1.00	83.62	C
ATOM	6292	CG	ARG	L	54	−82.146	−3.516	−35.411	1.00	84.05	C
ATOM	6293	CD	ARG	L	54	−82.627	−4.184	−36.662	1.00	85.38	C
ATOM	6294	NE	ARG	L	54	−82.768	−3.201	−37.726	1.00	86.77	N
ATOM	6295	CZ	ARG	L	54	−82.077	−3.221	−38.862	1.00	87.66	C
ATOM	6296	NH1	ARG	L	54	−82.265	−2.273	−39.774	1.00	88.38	N
ATOM	6297	NH2	ARG	L	54	−81.202	−4.198	−39.103	1.00	86.69	N
ATOM	6298	C	ARG	L	54	−78.886	−3.698	−33.520	1.00	84.05	C
ATOM	6299	O	ARG	L	54	−77.815	−3.445	−34.090	1.00	83.98	O
ATOM	6300	N	ALA	L	55	−78.992	−4.530	−32.472	1.00	84.40	N
ATOM	6301	CA	ALA	L	55	−77.839	−5.247	−31.952	1.00	85.14	C
ATOM	6302	CB	ALA	L	55	−78.179	−5.893	−30.624	1.00	85.11	C
ATOM	6303	C	ALA	L	55	−77.477	−6.305	−32.968	1.00	85.71	C
ATOM	6304	O	ALA	L	55	−78.351	−6.712	−33.745	1.00	85.99	O
ATOM	6305	N	THR	L	56	−76.206	−6.751	−32.979	1.00	86.17	N
ATOM	6306	CA	THR	L	56	−75.759	−7.777	−33.927	1.00	86.69	C
ATOM	6307	CB	THR	L	56	−74.278	−8.136	−33.741	1.00	86.68	C
ATOM	6308	OG1	THR	L	56	−73.521	−6.939	−33.546	1.00	87.91	O
ATOM	6309	CG2	THR	L	56	−73.711	−8.891	−34.927	1.00	86.39	C
ATOM	6310	C	THR	L	56	−76.706	−8.988	−33.974	1.00	86.77	C
ATOM	6311	O	THR	L	56	−77.074	−9.564	−32.935	1.00	86.59	O
ATOM	6312	N	GLY	L	57	−77.126	−9.299	−35.192	1.00	87.23	N
ATOM	6313	CA	GLY	L	57	−77.993	−10.423	−35.490	1.00	87.57	C
ATOM	6314	C	GLY	L	57	−79.441	−10.290	−35.096	1.00	87.78	C
ATOM	6315	O	GLY	L	57	−80.049	−11.273	−34.658	1.00	88.10	O
ATOM	6316	N	ILE	L	58	−80.016	−9.101	−35.244	1.00	87.20	N
ATOM	6317	CA	ILE	L	58	−81.425	−8.978	−34.934	1.00	87.35	C
ATOM	6318	CB	ILE	L	58	−81.811	−8.327	−33.570	1.00	87.35	C
ATOM	6319	CG1	ILE	L	58	−81.827	−6.826	−33.620	1.00	88.03	C
ATOM	6320	CD1	ILE	L	58	−83.170	−6.347	−33.346	1.00	88.97	C
ATOM	6321	CG2	ILE	L	58	−81.034	−8.853	−32.365	1.00	86.77	C
ATOM	6322	C	ILE	L	58	−82.207	−8.508	−36.187	1.00	87.67	C
ATOM	6323	O	ILE	L	58	−81.730	−7.605	−36.890	1.00	87.84	O
ATOM	6324	N	PRO	L	59	−83.368	−9.149	−36.519	1.00	89.23	N
ATOM	6325	CA	PRO	L	59	−84.122	−8.763	−37.733	1.00	88.93	C
ATOM	6326	CB	PRO	L	59	−85.388	−9.623	−37.657	1.00	89.01	C
ATOM	6327	CG	PRO	L	59	−85.468	−10.082	−36.245	1.00	89.16	C
ATOM	6328	CD	PRO	L	59	−84.048	−10.261	−35.824	1.00	89.32	C
ATOM	6329	C	PRO	L	59	−84.504	−7.301	−37.868	1.00	88.54	C
ATOM	6330	O	PRO	L	59	−84.854	−6.653	−36.870	1.00	88.42	O
ATOM	6331	N	ALA	L	60	−84.477	−6.816	−39.137	1.00	83.84	N
ATOM	6332	CA	ALA	L	60	−84.799	−5.458	−39.570	1.00	82.93	C
ATOM	6333	CB	ALA	L	60	−84.606	−5.330	−41.062	1.00	82.66	C
ATOM	6334	C	ALA	L	60	−86.193	−5.018	−39.187	1.00	82.59	C
ATOM	6335	O	ALA	L	60	−86.461	−3.816	−39.182	1.00	82.81	O
ATOM	6336	N	ARG	L	61	−87.084	−5.969	−38.843	1.00	82.13	N
ATOM	6337	CA	ARG	L	61	−88.445	−5.623	−38.435	1.00	81.73	C
ATOM	6338	CB	ARG	L	61	−89.354	−6.847	−38.462	1.00	81.85	C
ATOM	6339	CG	ARG	L	61	−89.359	−7.659	−37.194	1.00	81.26	C
ATOM	6340	CD	ARG	L	61	−90.278	−8.822	−37.413	1.00	80.17	C
ATOM	6341	NE	ARG	L	61	−89.937	−9.963	−36.570	1.00	78.82	N
ATOM	6342	CZ	ARG	L	61	−89.029	−10.886	−36.873	1.00	76.91	C
ATOM	6343	NH1	ARG	L	61	−88.341	−10.807	−38.009	1.00	76.02	N
ATOM	6344	NH2	ARG	L	61	−88.809	−11.902	−36.046	1.00	75.12	N
ATOM	6345	C	ARG	L	61	−88.481	−4.876	−37.082	1.00	81.60	C
ATOM	6346	O	ARG	L	61	−89.505	−4.278	−36.719	1.00	81.34	O
ATOM	6347	N	PHE	L	62	−87.340	−4.909	−36.361	1.00	80.86	N
ATOM	6348	CA	PHE	L	62	−87.142	−4.233	−35.085	1.00	80.77	C
ATOM	6349	CB	PHE	L	62	−86.330	−5.095	−34.126	1.00	80.82	C
ATOM	6350	CG	PHE	L	62	−87.051	−6.304	−33.582	1.00	80.99	C
ATOM	6351	CD1	PHE	L	62	−87.891	−6.194	−32.474	1.00	80.48	C
ATOM	6352	CE1	PHE	L	62	−88.549	−7.317	−31.961	1.00	80.37	C
ATOM	6353	CZ	PHE	L	62	−88.358	−8.552	−32.544	1.00	80.39	C
ATOM	6354	CE2	PHE	L	62	−87.521	−8.680	−33.637	1.00	80.11	C
ATOM	6355	CD2	PHE	L	62	−86.869	−7.558	−34.156	1.00	80.48	C
ATOM	6356	C	PHE	L	62	−86.454	−2.885	−35.304	1.00	80.72	C
ATOM	6357	O	PHE	L	62	−85.473	−2.781	−36.065	1.00	80.48	O
ATOM	6358	N	SER	L	63	−86.988	−1.842	−34.650	1.00	80.01	N
ATOM	6359	CA	SER	L	63	−86.451	−0.496	−34.796	1.00	79.87	C
ATOM	6360	CB	SER	L	63	−87.097	0.188	−35.998	1.00	79.76	C
ATOM	6361	OG	SER	L	63	−88.492	0.346	−35.794	1.00	79.38	O
ATOM	6362	C	SER	L	63	−86.716	0.313	−33.545	1.00	79.80	C
ATOM	6363	O	SER	L	63	−87.756	0.134	−32.899	1.00	80.10	O
ATOM	6364	N	GLY	L	64	−85.796	1.216	−33.233	1.00	78.03	N
ATOM	6365	CA	GLY	L	64	−85.932	2.069	−32.064	1.00	77.81	C
ATOM	6366	C	GLY	L	64	−85.979	3.545	−32.369	1.00	77.75	C
ATOM	6367	O	GLY	L	64	−85.410	4.015	−33.362	1.00	77.54	O
ATOM	6368	N	SER	L	65	−86.648	4.286	−31.498	1.00	79.48	N
ATOM	6369	CA	SER	L	65	−86.786	5.725	−31.645	1.00	79.85	C
ATOM	6370	CB	SER	L	65	−88.071	6.061	−32.395	1.00	80.07	C
ATOM	6371	OG	SER	L	65	−88.936	6.916	−31.658	1.00	81.22	O
ATOM	6372	C	SER	L	65	−86.802	6.406	−30.303	1.00	79.90	C
ATOM	6373	O	SER	L	65	−87.218	5.810	−29.299	1.00	80.21	O
ATOM	6374	N	GLY	L	66	−86.396	7.669	−30.313	1.00	80.25	N
ATOM	6375	CA	GLY	L	66	−86.375	8.510	−29.129	1.00	80.40	C
ATOM	6376	C	GLY	L	66	−85.013	9.072	−28.796	1.00	80.53	C
ATOM	6377	O	GLY	L	66	−83.974	8.600	−29.272	1.00	80.70	O
ATOM	6378	N	SER	L	67	−85.042	10.114	−27.981	1.00	81.13	N
ATOM	6379	CA	SER	L	67	−83.919	10.852	−27.414	1.00	80.80	C
ATOM	6380	CB	SER	L	67	−83.189	11.697	−28.461	1.00	80.91	C
ATOM	6381	OG	SER	L	67	−81.853	12.039	−28.110	1.00	80.63	O
ATOM	6382	C	SER	L	67	−84.608	11.712	−26.369	1.00	80.78	C
ATOM	6383	O	SER	L	67	−85.638	12.359	−26.648	1.00	80.82	O
ATOM	6384	N	GLY	L	68	−84.106	11.629	−25.152	1.00	80.25	N
ATOM	6385	CA	GLY	L	68	−84.685	12.411	−24.086	1.00	80.31	C
ATOM	6386	C	GLY	L	68	−85.363	11.660	−22.985	1.00	80.31	C
ATOM	6387	O	GLY	L	68	−84.718	11.273	−22.015	1.00	80.51	O
ATOM	6388	N	THR	L	69	−86.675	11.515	−23.100	1.00	82.51	N
ATOM	6389	CA	THR	L	69	−87.485	10.843	−22.083	1.00	82.90	C
ATOM	6390	CB	THR	L	69	−88.233	11.868	−21.213	1.00	82.86	C
ATOM	6391	OG1	THR	L	69	−88.760	12.908	−22.052	1.00	83.26	O
ATOM	6392	CG2	THR	L	69	−87.358	12.459	−20.113	1.00	82.48	C
ATOM	6393	C	THR	L	69	−88.458	9.850	−22.679	1.00	83.07	C
ATOM	6394	O	THR	L	69	−88.748	8.848	−22.029	1.00	83.38	O
ATOM	6395	N	ASP	L	70	−88.978	10.129	−23.894	1.00	81.27	N
ATOM	6396	CA	ASP	L	70	−89.936	9.260	−24.569	1.00	81.42	C
ATOM	6397	CB	ASP	L	70	−91.097	10.072	−25.179	1.00	81.76	C
ATOM	6398	CG	ASP	L	70	−92.078	10.729	−24.185	1.00	83.01	C
ATOM	6399	OD1	ASP	L	70	−91.678	10.988	−23.004	1.00	84.07	O
ATOM	6400	OD2	ASP	L	70	−93.239	11.000	−24.587	1.00	84.40	O
ATOM	6401	C	ASP	L	70	−89.221	8.380	−25.574	1.00	81.29	C
ATOM	6402	O	ASP	L	70	−88.591	8.878	−26.524	1.00	81.22	O
ATOM	6403	N	PHE	L	71	−89.282	7.055	−25.315	1.00	79.43	N
ATOM	6404	CA	PHE	L	71	−88.621	6.023	−26.116	1.00	79.47	C
ATOM	6405	CB	PHE	L	71	−87.491	5.341	−25.318	1.00	79.30	C
ATOM	6406	CG	PHE	L	71	−86.342	6.288	−25.047	1.00	79.06	C
ATOM	6407	CD1	PHE	L	71	−85.296	6.423	−25.959	1.00	78.12	C
ATOM	6408	CE1	PHE	L	71	−84.259	7.324	−25.724	1.00	77.00	C
ATOM	6409	CZ	PHE	L	71	−84.270	8.099	−24.591	1.00	77.40	C
ATOM	6410	CE2	PHE	L	71	−85.299	7.997	−23.685	1.00	77.46	C
ATOM	6411	CD2	PHE	L	71	−86.331	7.089	−23.906	1.00	78.77	C
ATOM	6412	C	PHE	L	71	−89.580	5.022	−26.738	1.00	79.78	C
ATOM	6413	O	PHE	L	71	−90.625	4.711	−26.151	1.00	79.63	O
ATOM	6414	N	THR	L	72	−89.225	4.525	−27.942	1.00	81.31	N
ATOM	6415	CA	THR	L	72	−90.081	3.603	−28.663	1.00	81.88	C
ATOM	6416	CB	THR	L	72	−91.065	4.427	−29.511	1.00	81.84	C
ATOM	6417	OG1	THR	L	72	−92.207	4.693	−28.695	1.00	81.96	O
ATOM	6418	CG2	THR	L	72	−91.477	3.749	−30.838	1.00	81.93	C
ATOM	6419	C	THR	L	72	−89.439	2.388	−29.356	1.00	82.43	C
ATOM	6420	O	THR	L	72	−88.468	2.512	−30.116	1.00	82.66	O
ATOM	6421	N	LEU	L	73	−90.034	1.210	−29.100	1.00	83.21	N
ATOM	6422	CA	LEU	L	73	−89.652	−0.054	−29.719	1.00	83.49	C
ATOM	6423	CB	LEU	L	73	−89.457	−1.179	−28.699	1.00	83.62	C
ATOM	6424	CG	LEU	L	73	−89.058	−2.517	−29.301	1.00	82.79	C
ATOM	6425	CD1	LEU	L	73	−87.582	−2.573	−29.584	1.00	82.29	C
ATOM	6426	CD2	LEU	L	73	−89.460	−3.618	−28.413	1.00	82.50	C
ATOM	6427	C	LEU	L	73	−90.770	−0.407	−30.711	1.00	83.73	C
ATOM	6428	O	LEU	L	73	−91.959	−0.372	−30.355	1.00	83.42	O
ATOM	6429	N	THR	L	74	−90.369	−0.732	−31.956	1.00	86.82	N
ATOM	6430	CA	THR	L	74	−91.277	−1.021	−33.053	1.00	87.24	C
ATOM	6431	CB	THR	L	74	−91.296	0.199	−34.006	1.00	87.18	C
ATOM	6432	OG1	THR	L	74	−91.718	1.370	−33.299	1.00	87.71	O
ATOM	6433	CG2	THR	L	74	−92.148	−0.020	−35.242	1.00	87.14	C
ATOM	6434	C	THR	L	74	−90.953	−2.305	−33.805	1.00	87.64	C
ATOM	6435	O	THR	L	74	−89.853	−2.457	−34.353	1.00	87.70	O
ATOM	6436	N	ILE	L	75	−91.949	−3.209	−33.850	1.00	89.18	N
ATOM	6437	CA	ILE	L	75	−91.918	−4.473	−34.589	1.00	89.53	C
ATOM	6438	CB	ILE	L	75	−92.331	−5.734	−33.753	1.00	89.53	C
ATOM	6439	CG1	ILE	L	75	−91.573	−5.839	−32.405	1.00	89.06	C
ATOM	6440	CD1	ILE	L	75	−92.289	−5.229	−31.167	1.00	89.50	C
ATOM	6441	CG2	ILE	L	75	−92.117	−7.001	−34.571	1.00	89.83	C
ATOM	6442	C	ILE	L	75	−92.877	−4.185	−35.761	1.00	89.77	C
ATOM	6443	O	ILE	L	75	−94.087	−4.009	−35.537	1.00	89.63	O
ATOM	6444	N	SER	L	76	−92.317	−4.061	−36.993	1.00	91.77	N
ATOM	6445	CA	SER	L	76	−93.070	−3.740	−38.216	1.00	92.22	C
ATOM	6446	CB	SER	L	76	−92.136	−3.517	−39.405	1.00	92.21	C
ATOM	6447	OG	SER	L	76	−91.592	−4.712	−39.940	1.00	92.40	O
ATOM	6448	C	SER	L	76	−94.186	−4.736	−38.535	1.00	92.44	C
ATOM	6449	O	SER	L	76	−95.344	−4.330	−38.640	1.00	92.48	O
ATOM	6450	N	SER	L	77	−93.837	−6.033	−38.661	1.00	93.86	N
ATOM	6451	CA	SER	L	77	−94.764	−7.135	−38.930	1.00	94.04	C
ATOM	6452	CB	SER	L	77	−94.588	−7.661	−40.356	1.00	94.11	C
ATOM	6453	OG	SER	L	77	−93.307	−8.246	−40.564	1.00	94.95	O
ATOM	6454	C	SER	L	77	−94.478	−8.241	−37.914	1.00	93.95	C
ATOM	6455	O	SER	L	77	−93.479	−8.965	−38.057	1.00	94.05	O
ATOM	6456	N	LEU	L	78	−95.325	−8.358	−36.873	1.00	91.52	N
ATOM	6457	CA	LEU	L	78	−95.143	−9.379	−35.846	1.00	91.26	C
ATOM	6458	CB	LEU	L	78	−96.280	−9.355	−34.816	1.00	90.85	C
ATOM	6459	CG	LEU	L	78	−96.090	−8.432	−33.626	1.00	91.04	C
ATOM	6460	CD1	LEU	L	78	−97.403	−8.180	−32.922	1.00	90.49	C
ATOM	6461	CD2	LEU	L	78	−95.079	−8.997	−32.635	1.00	90.90	C
ATOM	6462	C	LEU	L	78	−94.984	−10.795	−36.418	1.00	91.43	C
ATOM	6463	O	LEU	L	78	−95.784	−11.244	−37.252	1.00	91.64	O
ATOM	6464	N	GLU	L	79	−93.919	−11.477	−35.993	1.00	91.30	N
ATOM	6465	CA	GLU	L	79	−93.657	−12.867	−36.364	1.00	91.18	C
ATOM	6466	CB	GLU	L	79	−92.191	−13.076	−36.792	1.00	91.43	C
ATOM	6467	CG	GLU	L	79	−91.819	−12.376	−38.093	1.00	92.72	C
ATOM	6468	CD	GLU	L	79	−92.563	−12.807	−39.343	1.00	95.02	C
ATOM	6469	OE1	GLU	L	79	−92.181	−13.849	−39.923	1.00	96.62	O
ATOM	6470	OE2	GLU	L	79	−93.520	−12.106	−39.747	1.00	95.71	O
ATOM	6471	C	GLU	L	79	−94.037	−13.648	−35.090	1.00	90.77	C
ATOM	6472	O	GLU	L	79	−94.210	−13.018	−34.051	1.00	90.66	O
ATOM	6473	N	PRO	L	80	−94.246	−14.970	−35.092	1.00	91.38	N
ATOM	6474	CA	PRO	L	80	−94.642	−15.622	−33.827	1.00	91.17	C
ATOM	6475	CB	PRO	L	80	−95.162	−16.983	−34.277	1.00	90.98	C
ATOM	6476	CG	PRO	L	80	−94.416	−17.259	−35.530	1.00	91.14	C
ATOM	6477	CD	PRO	L	80	−94.137	−15.944	−36.197	1.00	91.24	C
ATOM	6478	C	PRO	L	80	−93.529	−15.710	−32.776	1.00	90.98	C
ATOM	6479	O	PRO	L	80	−93.824	−15.728	−31.579	1.00	90.95	O
ATOM	6480	N	GLU	L	81	−92.252	−15.738	−33.220	1.00	92.87	N
ATOM	6481	CA	GLU	L	81	−91.086	−15.803	−32.334	1.00	92.64	C
ATOM	6482	CB	GLU	L	81	−89.820	−16.179	−33.114	1.00	92.93	C
ATOM	6483	CG	GLU	L	81	−89.377	−15.155	−34.143	1.00	94.89	C
ATOM	6484	CD	GLU	L	81	−89.752	−15.458	−35.582	1.00	98.75	C
ATOM	6485	OE1	GLU	L	81	−88.963	−15.078	−36.483	1.00	100.80	O
ATOM	6486	OE2	GLU	L	81	−90.828	−16.065	−35.812	1.00	99.87	O
ATOM	6487	C	GLU	L	81	−90.882	−14.511	−31.519	1.00	91.98	C
ATOM	6488	O	GLU	L	81	−90.150	−14.520	−30.521	1.00	92.22	O
ATOM	6489	N	ASP	L	82	−91.546	−13.415	−31.959	1.00	89.40	N
ATOM	6490	CA	ASP	L	82	−91.539	−12.075	−31.379	1.00	87.95	C
ATOM	6491	CB	ASP	L	82	−91.895	−11.046	−32.449	1.00	87.98	C
ATOM	6492	CG	ASP	L	82	−90.926	−10.958	−33.602	1.00	88.45	C
ATOM	6493	OD1	ASP	L	82	−89.798	−11.506	−33.485	1.00	88.93	O
ATOM	6494	OD2	ASP	L	82	−91.284	−10.338	−34.620	1.00	88.57	O
ATOM	6495	C	ASP	L	82	−92.511	−11.901	−30.230	1.00	87.09	C
ATOM	6496	O	ASP	L	82	−92.614	−10.788	−29.709	1.00	87.36	O
ATOM	6497	N	PHE	L	83	−93.237	−12.953	−29.829	1.00	83.84	N
ATOM	6498	CA	PHE	L	83	−94.176	−12.805	−28.726	1.00	82.86	C
ATOM	6499	CB	PHE	L	83	−95.420	−13.661	−28.959	1.00	83.10	C
ATOM	6500	CG	PHE	L	83	−96.319	−13.096	−30.029	1.00	83.64	C
ATOM	6501	CD1	PHE	L	83	−97.359	−12.230	−29.701	1.00	83.50	C
ATOM	6502	CE1	PHE	L	83	−98.177	−11.689	−30.693	1.00	83.49	C
ATOM	6503	CZ	PHE	L	83	−97.966	−12.014	−32.016	1.00	84.02	C
ATOM	6504	CE2	PHE	L	83	−96.938	−12.869	−32.365	1.00	83.78	C
ATOM	6505	CD2	PHE	L	83	−96.117	−13.413	−31.369	1.00	83.83	C
ATOM	6506	C	PHE	L	83	−93.453	−13.101	−27.412	1.00	82.13	C
ATOM	6507	O	PHE	L	83	−93.299	−14.268	−27.028	1.00	82.31	O
ATOM	6508	N	ALA	L	84	−92.949	−12.033	−26.751	1.00	76.94	N
ATOM	6509	CA	ALA	L	84	−92.164	−12.159	−25.522	1.00	75.79	C
ATOM	6510	CB	ALA	L	84	−90.682	−12.323	−25.879	1.00	75.58	C
ATOM	6511	C	ALA	L	84	−92.334	−10.966	−24.594	1.00	75.01	C
ATOM	6512	O	ALA	L	84	−93.255	−10.160	−24.765	1.00	75.03	O
ATOM	6513	N	VAL	L	85	−91.438	−10.861	−23.600	1.00	71.29	N
ATOM	6514	CA	VAL	L	85	−91.432	−9.745	−22.678	1.00	70.32	C
ATOM	6515	CB	VAL	L	85	−91.437	−10.138	−21.183	1.00	70.16	C
ATOM	6516	CG1	VAL	L	85	−91.439	−8.908	−20.288	1.00	69.53	C
ATOM	6517	CG2	VAL	L	85	−92.651	−10.994	−20.866	1.00	69.88	C
ATOM	6518	C	VAL	L	85	−90.304	−8.797	−23.120	1.00	70.01	C
ATOM	6519	O	VAL	L	85	−89.175	−9.222	−23.397	1.00	69.49	O
ATOM	6520	N	TYR	L	86	−90.654	−7.517	−23.255	1.00	71.60	N
ATOM	6521	CA	TYR	L	86	−89.729	−6.496	−23.705	1.00	71.23	C
ATOM	6522	CB	TYR	L	86	−90.308	−5.790	−24.934	1.00	71.07	C
ATOM	6523	CG	TYR	L	86	−90.265	−6.692	−26.152	1.00	71.27	C
ATOM	6524	CD1	TYR	L	86	−91.321	−7.560	−26.446	1.00	71.96	C
ATOM	6525	CE1	TYR	L	86	−91.269	−8.413	−27.552	1.00	72.18	C
ATOM	6526	CZ	TYR	L	86	−90.142	−8.412	−28.365	1.00	72.28	C
ATOM	6527	OH	TYR	L	86	−90.035	−9.235	−29.460	1.00	72.35	O
ATOM	6528	CE2	TYR	L	86	−89.084	−7.566	−28.083	1.00	71.38	C
ATOM	6529	CD2	TYR	L	86	−89.139	−6.736	−26.969	1.00	71.38	C
ATOM	6530	C	TYR	L	86	−89.346	−5.577	−22.575	1.00	71.10	C
ATOM	6531	O	TYR	L	86	−90.215	−5.087	−21.856	1.00	70.74	O
ATOM	6532	N	TYR	L	87	−88.031	−5.404	−22.384	1.00	72.64	N
ATOM	6533	CA	TYR	L	87	−87.469	−4.603	−21.302	1.00	72.75	C
ATOM	6534	CB	TYR	L	87	−86.618	−5.511	−20.388	1.00	72.34	C
ATOM	6535	CG	TYR	L	87	−87.400	−6.389	−19.435	1.00	71.58	C
ATOM	6536	CD1	TYR	L	87	−87.502	−7.761	−19.645	1.00	70.97	C
ATOM	6537	CE1	TYR	L	87	−88.202	−8.579	−18.759	1.00	70.24	C
ATOM	6538	CZ	TYR	L	87	−88.801	−8.023	−17.642	1.00	71.79	C
ATOM	6539	OH	TYR	L	87	−89.522	−8.801	−16.773	1.00	73.47	O
ATOM	6540	CE2	TYR	L	87	−88.691	−6.665	−17.400	1.00	72.08	C
ATOM	6541	CD2	TYR	L	87	−87.982	−5.860	−18.289	1.00	72.03	C
ATOM	6542	C	TYR	L	87	−86.616	−3.414	−21.770	1.00	73.36	C
ATOM	6543	O	TYR	L	87	−85.750	−3.591	−22.628	1.00	73.54	O
ATOM	6544	N	CYS	L	88	−86.835	−2.217	−21.188	1.00	77.68	N
ATOM	6545	CA	CYS	L	88	−86.028	−1.041	−21.514	1.00	78.32	C
ATOM	6546	CB	CYS	L	88	−86.872	0.181	−21.865	1.00	78.96	C
ATOM	6547	SG	CYS	L	88	−88.008	0.730	−20.559	1.00	82.86	S
ATOM	6548	C	CYS	L	88	−85.079	−0.775	−20.355	1.00	77.79	C
ATOM	6549	O	CYS	L	88	−85.490	−0.841	−19.189	1.00	78.19	O
ATOM	6550	N	GLN	L	89	−83.803	−0.530	−20.661	1.00	70.42	N
ATOM	6551	CA	GLN	L	89	−82.794	−0.329	−19.635	1.00	69.48	C
ATOM	6552	CB	GLN	L	89	−81.862	−1.567	−19.598	1.00	69.41	C
ATOM	6553	CG	GLN	L	89	−80.596	−1.517	−18.716	1.00	68.63	C
ATOM	6554	CD	GLN	L	89	−79.316	−1.228	−19.493	1.00	68.91	C
ATOM	6555	OE1	GLN	L	89	−78.460	−0.440	−19.069	1.00	70.17	O
ATOM	6556	NE2	GLN	L	89	−79.141	−1.849	−20.646	1.00	66.41	N
ATOM	6557	C	GLN	L	89	−82.029	0.950	−19.865	1.00	69.23	C
ATOM	6558	O	GLN	L	89	−81.925	1.426	−20.997	1.00	69.03	O
ATOM	6559	N	VAL	L	90	−81.461	1.492	−18.775	1.00	68.06	N
ATOM	6560	CA	VAL	L	90	−80.656	2.706	−18.760	1.00	67.45	C
ATOM	6561	CB	VAL	L	90	−81.630	3.921	−18.668	1.00	67.12	C
ATOM	6562	CG1	VAL	L	90	−81.574	4.653	−17.333	1.00	65.60	C
ATOM	6563	CG2	VAL	L	90	−81.443	4.859	−19.837	1.00	66.82	C
ATOM	6564	C	VAL	L	90	−79.600	2.620	−17.618	1.00	67.58	C
ATOM	6565	O	VAL	L	90	−79.731	1.769	−16.729	1.00	67.28	O
ATOM	6566	N	TRP	L	91	−78.554	3.479	−17.661	1.00	68.82	N
ATOM	6567	CA	TRP	L	91	−77.536	3.549	−16.616	1.00	68.81	C
ATOM	6568	CB	TRP	L	91	−76.122	3.592	−17.187	1.00	68.19	C
ATOM	6569	CG	TRP	L	91	−75.783	2.532	−18.187	1.00	66.71	C
ATOM	6570	CD1	TRP	L	91	−75.505	2.718	−19.507	1.00	66.34	C
ATOM	6571	NE1	TRP	L	91	−75.241	1.517	−20.112	1.00	64.66	N
ATOM	6572	CE2	TRP	L	91	−75.303	0.524	−19.173	1.00	65.19	C
ATOM	6573	CD2	TRP	L	91	−75.648	1.130	−17.944	1.00	65.02	C
ATOM	6574	CE3	TRP	L	91	−75.782	0.317	−16.803	1.00	63.85	C
ATOM	6575	CZ3	TRP	L	91	−75.544	−1.041	−16.918	1.00	63.53	C
ATOM	6576	CH2	TRP	L	91	−75.188	−1.613	−18.147	1.00	64.30	C
ATOM	6577	CZ2	TRP	L	91	−75.069	−0.853	−19.289	1.00	65.06	C
ATOM	6578	C	TRP	L	91	−77.833	4.838	−15.823	1.00	69.85	C
ATOM	6579	O	TRP	L	91	−78.470	5.746	−16.355	1.00	70.18	O
ATOM	6580	N	ASP	L	92	−77.387	4.921	−14.559	1.00	75.57	N
ATOM	6581	CA	ASP	L	92	−77.627	6.045	−13.651	1.00	76.89	C
ATOM	6582	CB	ASP	L	92	−79.015	5.835	−12.988	1.00	77.25	C
ATOM	6583	CG	ASP	L	92	−79.606	6.941	−12.110	1.00	79.26	C
ATOM	6584	OD1	ASP	L	92	−80.722	6.727	−11.559	1.00	80.34	O
ATOM	6585	OD2	ASP	L	92	−78.948	8.033	−11.967	1.00	81.56	O
ATOM	6586	C	ASP	L	92	−76.487	6.084	−12.615	1.00	77.32	C
ATOM	6587	O	ASP	L	92	−75.542	5.313	−12.746	1.00	77.83	O
ATOM	6588	N	SER	L	93	−76.544	6.982	−11.610	1.00	79.15	N
ATOM	6589	CA	SER	L	93	−75.499	7.077	−10.590	1.00	79.73	C
ATOM	6590	CB	SER	L	93	−75.288	8.516	−10.152	1.00	79.60	C
ATOM	6591	OG	SER	L	93	−76.511	9.086	−9.725	1.00	79.94	O
ATOM	6592	C	SER	L	93	−75.697	6.163	−9.379	1.00	80.03	C
ATOM	6593	O	SER	L	93	−74.897	5.233	−9.249	1.00	80.11	O
ATOM	6594	N	SER	L	94	−76.748	6.441	−8.493	1.00	84.21	N
ATOM	6595	CA	SER	L	94	−77.148	5.744	−7.232	1.00	84.27	C
ATOM	6596	CB	SER	L	94	−78.393	6.365	−6.597	1.00	84.59	C
ATOM	6597	OG	SER	L	94	−79.012	5.503	−5.650	1.00	85.72	O
ATOM	6598	C	SER	L	94	−77.349	4.300	−7.562	1.00	84.06	C
ATOM	6599	O	SER	L	94	−76.424	3.532	−7.245	1.00	85.11	O
ATOM	6600	N	PRO	L	95	−78.446	3.857	−8.247	1.00	79.86	N
ATOM	6601	CA	PRO	L	95	−78.457	2.457	−8.692	1.00	78.96	C
ATOM	6602	CB	PRO	L	95	−79.941	2.139	−8.851	1.00	79.07	C
ATOM	6603	CG	PRO	L	95	−80.647	3.510	−9.000	1.00	80.00	C
ATOM	6604	CD	PRO	L	95	−79.618	4.596	−8.780	1.00	79.83	C
ATOM	6605	C	PRO	L	95	−77.667	2.548	−10.032	1.00	77.85	C
ATOM	6606	O	PRO	L	95	−77.942	3.448	−10.846	1.00	78.00	O
ATOM	6607	N	PRO	L	96	−76.603	1.761	−10.262	1.00	70.15	N
ATOM	6608	CA	PRO	L	96	−75.851	1.923	−11.509	1.00	69.43	C
ATOM	6609	CB	PRO	L	96	−74.619	1.023	−11.313	1.00	69.39	C
ATOM	6610	CG	PRO	L	96	−74.644	0.592	−9.927	1.00	69.41	C
ATOM	6611	CD	PRO	L	96	−76.042	0.682	−9.445	1.00	70.05	C
ATOM	6612	C	PRO	L	96	−76.651	1.573	−12.768	1.00	68.90	C
ATOM	6613	O	PRO	L	96	−76.341	2.061	−13.862	1.00	68.98	O
ATOM	6614	N	VAL	L	97	−77.686	0.745	−12.598	1.00	66.11	N
ATOM	6615	CA	VAL	L	97	−78.557	0.277	−13.659	1.00	65.48	C
ATOM	6616	CB	VAL	L	97	−78.293	−1.226	−13.890	1.00	65.27	C
ATOM	6617	CG1	VAL	L	97	−78.875	−2.070	−12.764	1.00	64.59	C
ATOM	6618	CG2	VAL	L	97	−78.798	−1.693	−15.259	1.00	65.12	C
ATOM	6619	C	VAL	L	97	−80.005	0.547	−13.304	1.00	65.49	C
ATOM	6620	O	VAL	L	97	−80.340	0.630	−12.131	1.00	65.64	O
ATOM	6621	N	VAL	L	98	−80.859	0.719	−14.312	1.00	67.13	N
ATOM	6622	CA	VAL	L	98	−82.298	0.927	−14.142	1.00	67.28	C
ATOM	6623	CB	VAL	L	98	−82.792	2.409	−14.141	1.00	67.09	C
ATOM	6624	CG1	VAL	L	98	−84.293	2.487	−13.853	1.00	66.37	C
ATOM	6625	CG2	VAL	L	98	−82.029	3.259	−13.133	1.00	67.24	C
ATOM	6626	C	VAL	L	98	−82.954	0.110	−15.239	1.00	67.85	C
ATOM	6627	O	VAL	L	98	−82.553	0.205	−16.409	1.00	67.78	O
ATOM	6628	N	PHE	L	99	−83.944	−0.706	−14.863	1.00	70.44	N
ATOM	6629	CA	PHE	L	99	−84.703	−1.527	−15.806	1.00	70.85	C
ATOM	6630	CB	PHE	L	99	−84.611	−3.026	−15.427	1.00	70.67	C
ATOM	6631	CG	PHE	L	99	−83.397	−3.764	−15.931	1.00	69.18	C
ATOM	6632	CD1	PHE	L	99	−82.386	−4.146	−15.060	1.00	68.29	C
ATOM	6633	CE1	PHE	L	99	−81.243	−4.810	−15.532	1.00	68.03	C
ATOM	6634	CZ	PHE	L	99	−81.128	−5.108	−16.874	1.00	67.77	C
ATOM	6635	CE2	PHE	L	99	−82.132	−4.742	−17.750	1.00	67.63	C
ATOM	6636	CD2	PHE	L	99	−83.266	−4.080	−17.278	1.00	67.90	C
ATOM	6637	C	PHE	L	99	−86.164	−1.108	−15.758	1.00	71.49	C
ATOM	6638	O	PHE	L	99	−86.664	−0.705	−14.712	1.00	71.24	O
ATOM	6639	N	GLY	L	100	−86.847	−1.233	−16.875	1.00	73.30	N
ATOM	6640	CA	GLY	L	100	−88.275	−0.956	−16.922	1.00	74.74	C
ATOM	6641	C	GLY	L	100	−89.021	−2.176	−16.395	1.00	75.62	C
ATOM	6642	O	GLY	L	100	−88.418	−3.247	−16.191	1.00	75.82	O
ATOM	6643	N	GLY	L	101	−90.325	−2.017	−16.173	1.00	77.20	N
ATOM	6644	CA	GLY	L	101	−91.194	−3.082	−15.670	1.00	78.41	C
ATOM	6645	C	GLY	L	101	−91.351	−4.249	−16.630	1.00	79.36	C
ATOM	6646	O	GLY	L	101	−91.566	−5.391	−16.204	1.00	79.33	O
ATOM	6647	N	GLY	L	102	−91.211	−3.952	−17.923	1.00	79.85	N
ATOM	6648	CA	GLY	L	102	−91.351	−4.918	−18.998	1.00	80.96	C
ATOM	6649	C	GLY	L	102	−92.736	−4.862	−19.597	1.00	81.95	C
ATOM	6650	O	GLY	L	102	−93.700	−4.480	−18.921	1.00	82.12	O
ATOM	6651	N	THR	L	103	−92.842	−5.243	−20.873	1.00	82.02	N
ATOM	6652	CA	THR	L	103	−94.110	−5.263	−21.594	1.00	82.88	C
ATOM	6653	CB	THR	L	103	−94.169	−4.102	−22.607	1.00	82.67	C
ATOM	6654	OG1	THR	L	103	−94.459	−2.902	−21.906	1.00	82.87	O
ATOM	6655	CG2	THR	L	103	−95.193	−4.313	−23.719	1.00	82.37	C
ATOM	6656	C	THR	L	103	−94.255	−6.640	−22.208	1.00	83.86	C
ATOM	6657	O	THR	L	103	−93.358	−7.072	−22.945	1.00	83.91	O
ATOM	6658	N	LYS	L	104	−95.367	−7.334	−21.899	1.00	84.99	N
ATOM	6659	CA	LYS	L	104	−95.620	−8.650	−22.460	1.00	86.22	C
ATOM	6660	CB	LYS	L	104	−96.429	−9.521	−21.486	1.00	86.41	C
ATOM	6661	CG	LYS	L	104	−96.530	−10.982	−21.928	1.00	87.85	C
ATOM	6662	CD	LYS	L	104	−97.400	−11.773	−20.983	1.00	90.43	C
ATOM	6663	CE	LYS	L	104	−98.252	−12.784	−21.725	1.00	92.63	C
ATOM	6664	NZ	LYS	L	104	−99.625	−12.928	−21.124	1.00	94.80	N
ATOM	6665	C	LYS	L	104	−96.359	−8.467	−23.780	1.00	86.73	C
ATOM	6666	O	LYS	L	104	−97.348	−7.744	−23.820	1.00	87.11	O
ATOM	6667	N	VAL	L	105	−95.869	−9.096	−24.858	1.00	87.60	N
ATOM	6668	CA	VAL	L	105	−96.499	−9.049	−26.181	1.00	88.62	C
ATOM	6669	CB	VAL	L	105	−95.529	−8.643	−27.320	1.00	88.32	C
ATOM	6670	CG1	VAL	L	105	−96.210	−8.683	−28.680	1.00	87.75	C
ATOM	6671	CG2	VAL	L	105	−94.934	−7.267	−27.067	1.00	88.51	C
ATOM	6672	C	VAL	L	105	−97.097	−10.445	−26.370	1.00	89.97	C
ATOM	6673	O	VAL	L	105	−96.359	−11.421	−26.588	1.00	90.13	O
ATOM	6674	N	GLU	L	106	−98.437	−10.530	−26.218	1.00	92.87	N
ATOM	6675	CA	GLU	L	106	−99.263	−11.740	−26.323	1.00	94.05	C
ATOM	6676	CB	GLU	L	106	−100.269	−11.748	−25.136	1.00	93.91	C
ATOM	6677	CG	GLU	L	106	−101.676	−12.282	−25.390	1.00	95.35	C
ATOM	6678	CD	GLU	L	106	−102.706	−12.100	−24.284	1.00	97.66	C
ATOM	6679	OE1	GLU	L	106	−103.918	−12.230	−24.581	1.00	98.65	O
ATOM	6680	OE2	GLU	L	106	−102.309	−11.837	−23.123	1.00	98.64	O
ATOM	6681	C	GLU	L	106	−99.950	−11.798	−27.714	1.00	94.62	C
ATOM	6682	O	GLU	L	106	−100.023	−10.774	−28.395	1.00	94.58	O
ATOM	6683	N	ILE	L	107	−100.419	−12.986	−28.144	1.00	95.83	N
ATOM	6684	CA	ILE	L	107	−101.120	−13.133	−29.426	1.00	96.60	C
ATOM	6685	CB	ILE	L	107	−100.935	−14.524	−30.095	1.00	96.59	C
ATOM	6686	CG1	ILE	L	107	−99.502	−15.040	−29.959	1.00	97.14	C
ATOM	6687	CD1	ILE	L	107	−99.405	−16.507	−29.631	1.00	99.25	C
ATOM	6688	CG2	ILE	L	107	−101.348	−14.475	−31.577	1.00	96.87	C
ATOM	6689	C	ILE	L	107	−102.607	−12.810	−29.244	1.00	96.95	C
ATOM	6690	O	ILE	L	107	−103.225	−13.346	−28.328	1.00	96.97	O
ATOM	6691	N	LYS	L	108	−103.176	−11.938	−30.108	1.00	96.98	N
ATOM	6692	CA	LYS	L	108	−104.599	−11.607	−30.058	1.00	97.38	C
ATOM	6693	CB	LYS	L	108	−104.900	−10.160	−30.481	1.00	97.23	C
ATOM	6694	C	LYS	L	108	−105.325	−12.611	−30.945	1.00	97.70	C
ATOM	6695	O	LYS	L	108	−104.957	−12.802	−32.106	1.00	97.86	O
ATOM	6696	N	ARG	L	109	−106.320	−13.293	−30.379	1.00	97.85	N
ATOM	6697	CA	ARG	L	109	−107.120	−14.292	−31.082	1.00	98.21	C
ATOM	6698	CB	ARG	L	109	−106.779	−15.722	−30.606	1.00	98.23	C
ATOM	6699	C	ARG	L	109	−108.608	−14.008	−30.891	1.00	98.48	C
ATOM	6700	O	ARG	L	109	−109.004	−13.183	−30.048	1.00	98.46	O
ATOM	6701	N	THR	L	110	−109.425	−14.704	−31.702	1.00	97.91	N
ATOM	6702	CA	THR	L	110	−110.881	−14.658	−31.715	1.00	98.06	C
ATOM	6703	CB	THR	L	110	−111.405	−15.547	−32.862	1.00	98.16	C
ATOM	6704	OG1	THR	L	110	−112.496	−16.344	−32.388	1.00	99.22	O
ATOM	6705	CG2	THR	L	110	−110.303	−16.459	−33.489	1.00	98.04	C
ATOM	6706	C	THR	L	110	−111.359	−15.063	−30.318	1.00	98.03	C
ATOM	6707	O	THR	L	110	−110.979	−16.131	−29.828	1.00	98.07	O
ATOM	6708	N	VAL	L	111	−112.132	−14.190	−29.665	1.00	96.70	N
ATOM	6709	CA	VAL	L	111	−112.642	−14.402	−28.307	1.00	97.03	C
ATOM	6710	CB	VAL	L	111	−113.562	−13.244	−27.827	1.00	97.09	C
ATOM	6711	CG1	VAL	L	111	−113.975	−13.413	−26.361	1.00	96.68	C
ATOM	6712	CG2	VAL	L	111	−112.899	−11.889	−28.048	1.00	97.07	C
ATOM	6713	C	VAL	L	111	−113.266	−15.799	−28.123	1.00	97.35	C
ATOM	6714	O	VAL	L	111	−114.399	−16.045	−28.535	1.00	97.33	O
ATOM	6715	N	ALA	L	112	−112.487	−16.715	−27.528	1.00	98.73	N
ATOM	6716	CA	ALA	L	112	−112.891	−18.095	−27.255	1.00	98.93	C
ATOM	6717	CB	ALA	L	112	−111.740	−19.049	−27.531	1.00	98.76	C
ATOM	6718	C	ALA	L	112	−113.411	−18.247	−25.814	1.00	99.15	C
ATOM	6719	O	ALA	L	112	−113.018	−17.496	−24.916	1.00	99.01	O
ATOM	6720	N	ALA	L	113	−114.331	−19.202	−25.620	1.00	101.81	N
ATOM	6721	CA	ALA	L	113	−114.977	−19.468	−24.336	1.00	102.10	C
ATOM	6722	CB	ALA	L	113	−116.492	−19.449	−24.498	1.00	102.05	C
ATOM	6723	C	ALA	L	113	−114.502	−20.788	−23.690	1.00	102.28	C
ATOM	6724	O	ALA	L	113	−114.144	−21.749	−24.405	1.00	102.06	O
ATOM	6725	N	PRO	L	114	−114.478	−20.839	−22.331	1.00	103.19	N
ATOM	6726	CA	PRO	L	114	−113.984	−22.049	−21.663	1.00	103.27	C
ATOM	6727	CB	PRO	L	114	−113.447	−21.511	−20.332	1.00	103.29	C
ATOM	6728	CG	PRO	L	114	−114.314	−20.314	−20.022	1.00	103.13	C
ATOM	6729	CD	PRO	L	114	−114.848	−19.793	−21.346	1.00	103.11	C
ATOM	6730	C	PRO	L	114	−114.993	−23.176	−21.451	1.00	103.39	C
ATOM	6731	O	PRO	L	114	−116.121	−22.949	−20.990	1.00	103.53	O
ATOM	6732	N	SER	L	115	−114.560	−24.407	−21.775	1.00	102.39	N
ATOM	6733	CA	SER	L	115	−115.326	−25.629	−21.582	1.00	102.50	C
ATOM	6734	CB	SER	L	115	−114.770	−26.762	−22.451	1.00	102.27	C
ATOM	6735	OG	SER	L	115	−114.168	−26.312	−23.655	1.00	102.46	O
ATOM	6736	C	SER	L	115	−115.063	−25.913	−20.101	1.00	102.76	C
ATOM	6737	O	SER	L	115	−113.972	−26.357	−19.774	1.00	103.38	O
ATOM	6738	N	VAL	L	116	−116.005	−25.584	−19.202	1.00	103.10	N
ATOM	6739	CA	VAL	L	116	−115.844	−25.775	−17.746	1.00	103.42	C
ATOM	6740	CB	VAL	L	116	−116.618	−24.694	−16.929	1.00	103.37	C
ATOM	6741	CG1	VAL	L	116	−116.510	−24.909	−15.417	1.00	103.06	C
ATOM	6742	CG2	VAL	L	116	−116.146	−23.289	−17.306	1.00	102.93	C
ATOM	6743	C	VAL	L	116	−116.082	−27.243	−17.276	1.00	103.88	C
ATOM	6744	O	VAL	L	116	−116.879	−27.965	−17.875	1.00	103.91	O
ATOM	6745	N	PHE	L	117	−115.334	−27.686	−16.243	1.00	103.74	N
ATOM	6746	CA	PHE	L	117	−115.403	−29.026	−15.653	1.00	104.14	C
ATOM	6747	CB	PHE	L	117	−114.356	−29.950	−16.276	1.00	103.83	C
ATOM	6748	CG	PHE	L	117	−114.546	−30.170	−17.752	1.00	103.51	C
ATOM	6749	CD1	PHE	L	117	−115.308	−31.228	−18.220	1.00	103.82	C
ATOM	6750	CE1	PHE	L	117	−115.481	−31.431	−19.594	1.00	103.88	C
ATOM	6751	CZ	PHE	L	117	−114.894	−30.572	−20.500	1.00	102.95	C
ATOM	6752	CE2	PHE	L	117	−114.135	−29.520	−20.049	1.00	102.47	C
ATOM	6753	CD2	PHE	L	117	−113.957	−29.322	−18.679	1.00	102.84	C
ATOM	6754	C	PHE	L	117	−115.221	−28.963	−14.135	1.00	104.79	C
ATOM	6755	O	PHE	L	117	−114.699	−27.976	−13.608	1.00	104.81	O
ATOM	6756	N	ILE	L	118	−115.689	−29.999	−13.429	1.00	105.72	N
ATOM	6757	CA	ILE	L	118	−115.570	−30.083	−11.973	1.00	106.31	C
ATOM	6758	CB	ILE	L	118	−116.703	−29.392	−11.157	1.00	106.17	C
ATOM	6759	CG1	ILE	L	118	−116.318	−29.259	−9.671	1.00	106.10	C
ATOM	6760	CD1	ILE	L	118	−116.971	−28.104	−8.948	1.00	105.90	C
ATOM	6761	CG2	ILE	L	118	−118.068	−30.061	−11.350	1.00	106.16	C
ATOM	6762	C	ILE	L	118	−115.273	−31.515	−11.585	1.00	106.81	C
ATOM	6763	O	ILE	L	118	−115.994	−32.425	−12.004	1.00	106.98	O
ATOM	6764	N	PHE	L	119	−114.173	−31.715	−10.838	1.00	107.59	N
ATOM	6765	CA	PHE	L	119	−113.720	−33.030	−10.400	1.00	107.97	C
ATOM	6766	CB	PHE	L	119	−112.327	−33.337	−10.936	1.00	107.73	C
ATOM	6767	CG	PHE	L	119	−112.211	−33.252	−12.437	1.00	107.44	C
ATOM	6768	CD1	PHE	L	119	−111.963	−32.035	−13.065	1.00	107.12	C
ATOM	6769	CE1	PHE	L	119	−111.832	−31.959	−14.454	1.00	107.46	C
ATOM	6770	CZ	PHE	L	119	−111.941	−33.100	−15.220	1.00	107.76	C
ATOM	6771	CE2	PHE	L	119	−112.180	−34.317	−14.613	1.00	107.82	C
ATOM	6772	CD2	PHE	L	119	−112.321	−34.390	−13.223	1.00	107.63	C
ATOM	6773	C	PHE	L	119	−113.773	−33.107	−8.885	1.00	108.58	C
ATOM	6774	O	PHE	L	119	−113.236	−32.223	−8.204	1.00	108.62	O
ATOM	6775	N	PRO	L	120	−114.453	−34.144	−8.342	1.00	109.75	N
ATOM	6776	CA	PRO	L	120	−114.597	−34.244	−6.882	1.00	110.10	C
ATOM	6777	CB	PRO	L	120	−115.986	−34.865	−6.729	1.00	110.03	C
ATOM	6778	CG	PRO	L	120	−116.210	−35.651	−8.017	1.00	109.68	C
ATOM	6779	CD	PRO	L	120	−115.169	−35.245	−9.024	1.00	109.58	C
ATOM	6780	C	PRO	L	120	−113.509	−35.063	−6.169	1.00	110.63	C
ATOM	6781	O	PRO	L	120	−112.884	−35.921	−6.813	1.00	110.39	O
ATOM	6782	N	PRO	L	121	−113.284	−34.826	−4.839	1.00	112.38	N
ATOM	6783	CA	PRO	L	121	−112.258	−35.591	−4.101	1.00	112.95	C
ATOM	6784	CB	PRO	L	121	−112.477	−35.183	−2.645	1.00	112.85	C
ATOM	6785	CG	PRO	L	121	−113.056	−33.833	−2.741	1.00	112.82	C
ATOM	6786	CD	PRO	L	121	−113.936	−33.839	−3.955	1.00	112.45	C
ATOM	6787	C	PRO	L	121	−112.342	−37.096	−4.304	1.00	113.61	C
ATOM	6788	O	PRO	L	121	−113.373	−37.733	−4.076	1.00	113.95	O
ATOM	6789	N	SER	L	122	−111.224	−37.636	−4.780	1.00	115.25	N
ATOM	6790	CA	SER	L	122	−110.957	−39.021	−5.134	1.00	115.76	C
ATOM	6791	CB	SER	L	122	−109.538	−39.115	−5.709	1.00	115.91	C
ATOM	6792	OG	SER	L	122	−109.262	−40.311	−6.419	1.00	116.00	O
ATOM	6793	C	SER	L	122	−111.161	−40.037	−3.991	1.00	116.05	C
ATOM	6794	O	SER	L	122	−111.533	−39.700	−2.859	1.00	115.84	O
ATOM	6795	N	ASP	L	123	−110.912	−41.303	−4.349	1.00	116.73	N
ATOM	6796	CA	ASP	L	123	−110.946	−42.528	−3.559	1.00	117.16	C
ATOM	6797	CB	ASP	L	123	−110.564	−43.724	−4.488	1.00	117.21	C
ATOM	6798	CG	ASP	L	123	−109.458	−43.456	−5.531	1.00	117.36	C
ATOM	6799	OD1	ASP	L	123	−108.256	−43.470	−5.152	1.00	117.15	O
ATOM	6800	OD2	ASP	L	123	−109.799	−43.244	−6.721	1.00	117.04	O
ATOM	6801	C	ASP	L	123	−109.973	−42.424	−2.361	1.00	117.43	C
ATOM	6802	O	ASP	L	123	−110.401	−42.159	−1.226	1.00	117.38	O
ATOM	6803	N	GLU	L	124	−108.659	−42.605	−2.650	1.00	115.50	N
ATOM	6804	CA	GLU	L	124	−107.540	−42.560	−1.721	1.00	115.75	C
ATOM	6805	CB	GLU	L	124	−106.249	−43.030	−2.405	1.00	115.57	C
ATOM	6806	C	GLU	L	124	−107.375	−41.165	−1.165	1.00	116.01	C
ATOM	6807	O	GLU	L	124	−106.902	−41.025	−0.037	1.00	116.10	O
ATOM	6808	N	GLN	L	125	−107.782	−40.132	−1.944	1.00	114.68	N
ATOM	6809	CA	GLN	L	125	−107.713	−38.721	−1.544	1.00	114.99	C
ATOM	6810	CB	GLN	L	125	−108.446	−37.837	−2.570	1.00	114.92	C
ATOM	6811	CG	GLN	L	125	−107.624	−36.687	−3.144	1.00	114.27	C
ATOM	6812	CD	GLN	L	125	−107.616	−35.471	−2.268	1.00	113.67	C
ATOM	6813	OE1	GLN	L	125	−108.568	−34.712	−2.245	1.00	113.40	O
ATOM	6814	NE2	GLN	L	125	−106.543	−35.261	−1.535	1.00	113.42	N
ATOM	6815	C	GLN	L	125	−108.358	−38.560	−0.166	1.00	115.37	C
ATOM	6816	O	GLN	L	125	−107.775	−37.929	0.721	1.00	115.33	O
ATOM	6817	N	LEU	L	126	−109.542	−39.176	0.015	1.00	116.16	N
ATOM	6818	CA	LEU	L	126	−110.274	−39.125	1.268	1.00	116.50	C
ATOM	6819	CB	LEU	L	126	−111.768	−39.246	1.028	1.00	116.54	C
ATOM	6820	CG	LEU	L	126	−112.405	−37.947	0.560	1.00	117.03	C
ATOM	6821	CD1	LEU	L	126	−113.452	−38.207	−0.498	1.00	117.40	C
ATOM	6822	CD2	LEU	L	126	−112.930	−37.122	1.734	1.00	116.35	C
ATOM	6823	C	LEU	L	126	−109.768	−40.117	2.295	1.00	116.62	C
ATOM	6824	O	LEU	L	126	−109.705	−39.763	3.478	1.00	116.58	O
ATOM	6825	N	LYS	L	127	−109.360	−41.341	1.848	1.00	116.04	N
ATOM	6826	CA	LYS	L	127	−108.796	−42.389	2.722	1.00	116.17	C
ATOM	6827	CB	LYS	L	127	−108.491	−43.676	1.930	1.00	115.92	C
ATOM	6828	C	LYS	L	127	−107.530	−41.864	3.449	1.00	116.32	C
ATOM	6829	O	LYS	L	127	−107.066	−42.491	4.403	1.00	116.50	O
ATOM	6830	N	SER	L	128	−107.004	−40.693	2.994	1.00	115.89	N
ATOM	6831	CA	SER	L	128	−105.839	−39.983	3.526	1.00	115.99	C
ATOM	6832	CB	SER	L	128	−104.979	−39.431	2.391	1.00	115.95	C
ATOM	6833	OG	SER	L	128	−105.498	−38.222	1.860	1.00	116.15	O
ATOM	6834	C	SER	L	128	−106.254	−38.851	4.489	1.00	116.09	C
ATOM	6835	O	SER	L	128	−105.440	−38.405	5.302	1.00	116.17	O
ATOM	6836	N	GLY	L	129	−107.498	−38.394	4.378	1.00	115.76	N
ATOM	6837	CA	GLY	L	129	−108.029	−37.348	5.242	1.00	115.83	C
ATOM	6838	C	GLY	L	129	−107.873	−35.923	4.756	1.00	115.89	C
ATOM	6839	O	GLY	L	129	−107.638	−35.014	5.560	1.00	115.86	O
ATOM	6840	N	THR	L	130	−108.023	−35.717	3.440	1.00	116.18	N
ATOM	6841	CA	THR	L	130	−107.929	−34.404	2.804	1.00	116.14	C
ATOM	6842	CB	THR	L	130	−106.470	−33.935	2.694	1.00	116.00	C
ATOM	6843	OG1	THR	L	130	−106.445	−32.519	2.542	1.00	115.74	O
ATOM	6844	CG2	THR	L	130	−105.685	−34.641	1.590	1.00	115.70	C
ATOM	6845	C	THR	L	130	−108.774	−34.374	1.530	1.00	116.34	C
ATOM	6846	O	THR	L	130	−108.796	−35.354	0.790	1.00	116.29	O
ATOM	6847	N	ALA	L	131	−109.493	−33.274	1.289	1.00	117.60	N
ATOM	6848	CA	ALA	L	131	−110.354	−33.187	0.112	1.00	117.89	C
ATOM	6849	CB	ALA	L	131	−111.803	−33.060	0.539	1.00	117.93	C
ATOM	6850	C	ALA	L	131	−109.974	−32.076	−0.872	1.00	118.00	C
ATOM	6851	O	ALA	L	131	−110.061	−30.888	−0.541	1.00	117.96	O
ATOM	6852	N	SER	L	132	−109.554	−32.479	−2.088	1.00	118.64	N
ATOM	6853	CA	SER	L	132	−109.147	−31.585	−3.170	1.00	118.99	C
ATOM	6854	CB	SER	L	132	−107.705	−31.864	−3.607	1.00	119.09	C
ATOM	6855	OG	SER	L	132	−106.716	−31.360	−2.719	1.00	119.55	O
ATOM	6856	C	SER	L	132	−110.126	−31.669	−4.353	1.00	119.16	C
ATOM	6857	O	SER	L	132	−110.204	−32.688	−5.058	1.00	119.13	O
ATOM	6858	N	VAL	L	133	−110.883	−30.575	−4.546	1.00	121.01	N
ATOM	6859	CA	VAL	L	133	−111.888	−30.410	−5.601	1.00	121.04	C
ATOM	6860	CB	VAL	L	133	−113.241	−29.885	−5.055	1.00	121.01	C
ATOM	6861	CG1	VAL	L	133	−114.409	−30.512	−5.805	1.00	120.93	C
ATOM	6862	CG2	VAL	L	133	−113.379	−30.109	−3.550	1.00	120.63	C
ATOM	6863	C	VAL	L	133	−111.316	−29.472	−6.662	1.00	121.16	C
ATOM	6864	O	VAL	L	133	−110.865	−28.368	−6.330	1.00	121.07	O
ATOM	6865	N	VAL	L	134	−111.306	−29.913	−7.929	1.00	123.41	N
ATOM	6866	CA	VAL	L	134	−110.745	−29.089	−9.000	1.00	123.87	C
ATOM	6867	CB	VAL	L	134	−109.389	−29.596	−9.575	1.00	123.85	C
ATOM	6868	CG1	VAL	L	134	−108.399	−29.935	−8.468	1.00	124.11	C
ATOM	6869	CG2	VAL	L	134	−109.573	−30.782	−10.510	1.00	124.19	C
ATOM	6870	C	VAL	L	134	−111.715	−28.622	−10.084	1.00	124.09	C
ATOM	6871	O	VAL	L	134	−112.620	−29.356	−10.470	1.00	124.11	O
ATOM	6872	N	CYS	L	135	−111.492	−27.394	−10.580	1.00	126.57	N
ATOM	6873	CA	CYS	L	135	−112.270	−26.746	−11.628	1.00	126.85	C
ATOM	6874	CB	CYS	L	135	−112.871	−25.443	−11.105	1.00	127.54	C
ATOM	6875	SG	CYS	L	135	−114.387	−24.909	−11.952	1.00	131.74	S
ATOM	6876	C	CYS	L	135	−111.368	−26.496	−12.838	1.00	125.82	C
ATOM	6877	O	CYS	L	135	−110.424	−25.711	−12.749	1.00	125.75	O
ATOM	6878	N	LEU	L	136	−111.645	−27.170	−13.952	1.00	118.46	N
ATOM	6879	CA	LEU	L	136	−110.892	−27.007	−15.186	1.00	117.54	C
ATOM	6880	CB	LEU	L	136	−110.699	−28.362	−15.885	1.00	117.36	C
ATOM	6881	CG	LEU	L	136	−110.258	−28.353	−17.364	1.00	117.14	C
ATOM	6882	CD1	LEU	L	136	−108.845	−27.832	−17.534	1.00	117.06	C
ATOM	6883	CD2	LEU	L	136	−110.347	−29.727	−17.963	1.00	116.88	C
ATOM	6884	C	LEU	L	136	−111.616	−26.017	−16.100	1.00	117.22	C
ATOM	6885	O	LEU	L	136	−112.834	−26.070	−16.223	1.00	117.23	O
ATOM	6886	N	LEU	L	137	−110.862	−25.113	−16.732	1.00	113.80	N
ATOM	6887	CA	LEU	L	137	−111.347	−24.097	−17.663	1.00	113.18	C
ATOM	6888	CB	LEU	L	137	−111.033	−22.697	−17.099	1.00	113.02	C
ATOM	6889	CG	LEU	L	137	−112.020	−22.035	−16.120	1.00	112.83	C
ATOM	6890	CD1	LEU	L	137	−112.092	−22.756	−14.777	1.00	112.58	C
ATOM	6891	CD2	LEU	L	137	−111.601	−20.602	−15.845	1.00	112.49	C
ATOM	6892	C	LEU	L	137	−110.550	−24.361	−18.944	1.00	113.02	C
ATOM	6893	O	LEU	L	137	−109.562	−23.679	−19.214	1.00	113.12	O
ATOM	6894	N	ASN	L	138	−110.943	−25.399	−19.700	1.00	111.77	N
ATOM	6895	CA	ASN	L	138	−110.253	−25.808	−20.920	1.00	111.61	C
ATOM	6896	CB	ASN	L	138	−110.601	−27.233	−21.292	1.00	111.47	C
ATOM	6897	CG	ASN	L	138	−109.505	−27.894	−22.084	1.00	111.38	C
ATOM	6898	OD1	ASN	L	138	−109.548	−27.949	−23.314	1.00	111.97	O
ATOM	6899	ND2	ASN	L	138	−108.488	−28.400	−21.401	1.00	110.73	N
ATOM	6900	C	ASN	L	138	−110.408	−24.870	−22.109	1.00	111.70	C
ATOM	6901	O	ASN	L	138	−111.489	−24.343	−22.331	1.00	111.74	O
ATOM	6902	N	ASN	L	139	−109.310	−24.671	−22.862	1.00	112.71	N
ATOM	6903	CA	ASN	L	139	−109.150	−23.835	−24.063	1.00	113.10	C
ATOM	6904	CB	ASN	L	139	−109.074	−24.695	−25.321	1.00	112.89	C
ATOM	6905	CG	ASN	L	139	−107.809	−25.512	−25.418	1.00	112.69	C
ATOM	6906	OD1	ASN	L	139	−106.698	−24.985	−25.592	1.00	113.25	O
ATOM	6907	ND2	ASN	L	139	−107.952	−26.824	−25.323	1.00	112.42	N
ATOM	6908	C	ASN	L	139	−110.022	−22.557	−24.256	1.00	113.51	C
ATOM	6909	O	ASN	L	139	−111.145	−22.634	−24.764	1.00	113.56	O
ATOM	6910	N	PHE	L	140	−109.474	−21.388	−23.869	1.00	114.58	N
ATOM	6911	CA	PHE	L	140	−110.117	−20.073	−23.982	1.00	115.21	C
ATOM	6912	CB	PHE	L	140	−110.910	−19.733	−22.710	1.00	114.98	C
ATOM	6913	CG	PHE	L	140	−110.131	−19.560	−21.427	1.00	114.30	C
ATOM	6914	CD1	PHE	L	140	−109.951	−18.301	−20.871	1.00	113.56	C
ATOM	6915	CE1	PHE	L	140	−109.252	−18.145	−19.665	1.00	113.30	C
ATOM	6916	CZ	PHE	L	140	−108.742	−19.248	−19.012	1.00	112.97	C
ATOM	6917	CE2	PHE	L	140	−108.925	−20.503	−19.544	1.00	113.00	C
ATOM	6918	CD2	PHE	L	140	−109.630	−20.662	−20.742	1.00	113.60	C
ATOM	6919	C	PHE	L	140	−109.093	−18.977	−24.336	1.00	115.99	C
ATOM	6920	O	PHE	L	140	−107.912	−19.174	−24.052	1.00	116.10	O
ATOM	6921	N	TYR	L	141	−109.521	−17.845	−24.979	1.00	120.17	N
ATOM	6922	CA	TYR	L	141	−108.566	−16.788	−25.348	1.00	121.05	C
ATOM	6923	CB	TYR	L	141	−108.589	−16.291	−26.823	1.00	120.82	C
ATOM	6924	CG	TYR	L	141	−107.750	−15.032	−26.958	1.00	120.68	C
ATOM	6925	CD1	TYR	L	141	−106.363	−15.080	−26.839	1.00	120.23	C
ATOM	6926	CE1	TYR	L	141	−105.598	−13.920	−26.835	1.00	119.92	C
ATOM	6927	CZ	TYR	L	141	−106.211	−12.689	−26.980	1.00	119.83	C
ATOM	6928	OH	TYR	L	141	−105.449	−11.549	−27.013	1.00	119.70	O
ATOM	6929	CE2	TYR	L	141	−107.589	−12.612	−27.082	1.00	120.07	C
ATOM	6930	CD2	TYR	L	141	−108.350	−13.779	−27.060	1.00	120.62	C
ATOM	6931	C	TYR	L	141	−108.327	−15.636	−24.355	1.00	121.93	C
ATOM	6932	O	TYR	L	141	−107.188	−15.543	−23.901	1.00	122.12	O
ATOM	6933	N	PRO	L	142	−109.244	−14.684	−24.062	1.00	123.73	N
ATOM	6934	CA	PRO	L	142	−108.861	−13.603	−23.124	1.00	124.38	C
ATOM	6935	CB	PRO	L	142	−110.113	−12.728	−23.040	1.00	124.21	C
ATOM	6936	CG	PRO	L	142	−110.923	−13.107	−24.228	1.00	124.05	C
ATOM	6937	CD	PRO	L	142	−110.642	−14.545	−24.504	1.00	123.75	C
ATOM	6938	C	PRO	L	142	−108.418	−14.197	−21.774	1.00	125.09	C
ATOM	6939	O	PRO	L	142	−109.144	−15.019	−21.200	1.00	125.32	O
ATOM	6940	N	ARG	L	143	−107.192	−13.856	−21.311	1.00	124.90	N
ATOM	6941	CA	ARG	L	143	−106.641	−14.409	−20.070	1.00	125.50	C
ATOM	6942	CB	ARG	L	143	−105.176	−14.017	−19.884	1.00	125.50	C
ATOM	6943	CG	ARG	L	143	−104.366	−15.117	−19.235	1.00	125.34	C
ATOM	6944	CD	ARG	L	143	−103.690	−14.659	−17.962	1.00	125.22	C
ATOM	6945	NE	ARG	L	143	−102.648	−15.606	−17.567	1.00	125.08	N
ATOM	6946	CZ	ARG	L	143	−101.400	−15.591	−18.034	1.00	125.16	C
ATOM	6947	NH1	ARG	L	143	−101.021	−14.666	−18.911	1.00	124.93	N
ATOM	6948	NH2	ARG	L	143	−100.524	−16.506	−17.634	1.00	124.72	N
ATOM	6949	C	ARG	L	143	−107.452	−14.106	−18.824	1.00	125.98	C
ATOM	6950	O	ARG	L	143	−107.460	−14.920	−17.901	1.00	125.95	O
ATOM	6951	N	GLU	L	144	−108.136	−12.949	−18.798	1.00	128.30	N
ATOM	6952	CA	GLU	L	144	−108.959	−12.548	−17.665	1.00	129.21	C
ATOM	6953	CB	GLU	L	144	−109.478	−11.103	−17.821	1.00	129.25	C
ATOM	6954	CG	GLU	L	144	−109.909	−10.468	−16.501	1.00	130.44	C
ATOM	6955	CD	GLU	L	144	−111.255	−9.759	−16.456	1.00	132.01	C
ATOM	6956	OE1	GLU	L	144	−111.271	−8.538	−16.169	1.00	132.64	O
ATOM	6957	OE2	GLU	L	144	−112.294	−10.425	−16.687	1.00	132.51	O
ATOM	6958	C	GLU	L	144	−110.108	−13.544	−17.456	1.00	129.64	C
ATOM	6959	O	GLU	L	144	−110.948	−13.736	−18.341	1.00	129.70	O
ATOM	6960	N	ALA	L	145	−110.107	−14.200	−16.290	1.00	131.03	N
ATOM	6961	CA	ALA	L	145	−111.117	−15.180	−15.884	1.00	131.73	C
ATOM	6962	CB	ALA	L	145	−110.778	−16.562	−16.436	1.00	131.51	C
ATOM	6963	C	ALA	L	145	−111.214	−15.215	−14.350	1.00	132.29	C
ATOM	6964	O	ALA	L	145	−110.184	−15.248	−13.663	1.00	132.37	O
ATOM	6965	N	LYS	L	146	−112.449	−15.182	−13.817	1.00	132.82	N
ATOM	6966	CA	LYS	L	146	−112.696	−15.209	−12.374	1.00	133.49	C
ATOM	6967	CB	LYS	L	146	−113.637	−14.067	−11.965	1.00	133.42	C
ATOM	6968	C	LYS	L	146	−113.287	−16.547	−11.963	1.00	133.99	C
ATOM	6969	O	LYS	L	146	−114.152	−17.070	−12.668	1.00	134.05	O
ATOM	6970	N	VAL	L	147	−112.806	−17.113	−10.839	1.00	133.98	N
ATOM	6971	CA	VAL	L	147	−113.292	−18.390	−10.304	1.00	134.69	C
ATOM	6972	CB	VAL	L	147	−112.411	−19.629	−10.661	1.00	134.54	C
ATOM	6973	CG1	VAL	L	147	−112.819	−20.859	−9.854	1.00	134.55	C
ATOM	6974	CG2	VAL	L	147	−112.471	−19.944	−12.152	1.00	134.47	C
ATOM	6975	C	VAL	L	147	−113.592	−18.267	−8.801	1.00	135.34	C
ATOM	6976	O	VAL	L	147	−112.688	−17.986	−8.011	1.00	135.35	O
ATOM	6977	N	GLN	L	148	−114.876	−18.465	−8.429	1.00	137.17	N
ATOM	6978	CA	GLN	L	148	−115.370	−18.427	−7.052	1.00	137.96	C
ATOM	6979	CB	GLN	L	148	−116.388	−17.291	−6.837	1.00	137.70	C
ATOM	6980	C	GLN	L	148	−115.979	−19.790	−6.736	1.00	138.61	C
ATOM	6981	O	GLN	L	148	−116.844	−20.271	−7.470	1.00	138.56	O
ATOM	6982	N	TRP	L	149	−115.491	−20.421	−5.660	1.00	141.36	N
ATOM	6983	CA	TRP	L	149	−115.938	−21.733	−5.203	1.00	142.14	C
ATOM	6984	CB	TRP	L	149	−114.788	−22.495	−4.521	1.00	142.24	C
ATOM	6985	CG	TRP	L	149	−113.731	−23.024	−5.447	1.00	142.43	C
ATOM	6986	CD1	TRP	L	149	−112.536	−22.439	−5.742	1.00	142.44	C
ATOM	6987	NE1	TRP	L	149	−111.814	−23.239	−6.596	1.00	142.71	N
ATOM	6988	CE2	TRP	L	149	−112.534	−24.376	−6.862	1.00	142.61	C
ATOM	6989	CD2	TRP	L	149	−113.748	−24.278	−6.148	1.00	142.57	C
ATOM	6990	CE3	TRP	L	149	−114.676	−25.329	−6.246	1.00	142.51	C
ATOM	6991	CZ3	TRP	L	149	−114.365	−26.424	−7.041	1.00	142.73	C
ATOM	6992	CH2	TRP	L	149	−113.153	−26.494	−7.739	1.00	142.48	C
ATOM	6993	CZ2	TRP	L	149	−112.221	−25.486	−7.661	1.00	142.42	C
ATOM	6994	C	TRP	L	149	−117.120	−21.591	−4.247	1.00	142.57	C
ATOM	6995	O	TRP	L	149	−117.033	−20.863	−3.249	1.00	142.67	O
ATOM	6996	N	LYS	L	150	−118.226	−22.295	−4.569	1.00	144.16	N
ATOM	6997	CA	LYS	L	150	−119.468	−22.302	−3.801	1.00	144.48	C
ATOM	6998	CB	LYS	L	150	−120.683	−22.049	−4.710	1.00	144.30	C
ATOM	6999	C	LYS	L	150	−119.632	−23.585	−2.988	1.00	144.77	C
ATOM	7000	O	LYS	L	150	−120.027	−24.625	−3.528	1.00	144.70	O
ATOM	7001	N	VAL	L	151	−119.311	−23.497	−1.679	1.00	146.31	N
ATOM	7002	CA	VAL	L	151	−119.412	−24.586	−0.692	1.00	146.66	C
ATOM	7003	CB	VAL	L	151	−118.294	−24.522	0.403	1.00	146.70	C
ATOM	7004	CG1	VAL	L	151	−116.953	−24.974	−0.164	1.00	146.41	C
ATOM	7005	CG2	VAL	L	151	−118.160	−23.130	1.029	1.00	146.67	C
ATOM	7006	C	VAL	L	151	−120.871	−24.606	−0.156	1.00	146.88	C
ATOM	7007	O	VAL	L	151	−121.145	−24.253	1.003	1.00	147.08	O
ATOM	7008	N	ASP	L	152	−121.801	−25.021	−1.065	1.00	146.82	N
ATOM	7009	CA	ASP	L	152	−123.271	−25.064	−0.959	1.00	146.80	C
ATOM	7010	CB	ASP	L	152	−123.897	−26.226	−0.126	1.00	146.83	C
ATOM	7011	CG	ASP	L	152	−123.537	−26.390	1.350	1.00	147.22	C
ATOM	7012	OD1	ASP	L	152	−123.286	−27.540	1.772	1.00	147.06	O
ATOM	7013	OD2	ASP	L	152	−123.542	−25.373	2.091	1.00	147.71	O
ATOM	7014	C	ASP	L	152	−123.869	−23.668	−0.765	1.00	146.65	C
ATOM	7015	O	ASP	L	152	−124.196	−23.261	0.357	1.00	146.71	O
ATOM	7016	N	ASN	L	153	−123.943	−22.914	−1.897	1.00	144.71	N
ATOM	7017	CA	ASN	L	153	−124.425	−21.528	−2.001	1.00	144.46	C
ATOM	7018	CB	ASN	L	153	−125.953	−21.439	−1.869	1.00	144.46	C
ATOM	7019	C	ASN	L	153	−123.674	−20.586	−1.028	1.00	144.28	C
ATOM	7020	O	ASN	L	153	−124.248	−19.633	−0.488	1.00	144.25	O
ATOM	7021	N	ALA	L	154	−122.372	−20.880	−0.818	1.00	143.01	N
ATOM	7022	CA	ALA	L	154	−121.464	−20.135	0.053	1.00	142.71	C
ATOM	7023	CB	ALA	L	154	−121.086	−20.977	1.267	1.00	142.72	C
ATOM	7024	C	ALA	L	154	−120.210	−19.610	−0.706	1.00	142.37	C
ATOM	7025	O	ALA	L	154	−120.130	−19.742	−1.932	1.00	142.19	O
ATOM	7026	N	LEU	L	155	−119.257	−18.993	0.023	1.00	140.88	N
ATOM	7027	CA	LEU	L	155	−118.050	−18.380	−0.536	1.00	140.44	C
ATOM	7028	CB	LEU	L	155	−117.823	−16.932	0.015	1.00	140.45	C
ATOM	7029	CG	LEU	L	155	−117.618	−16.618	1.545	1.00	140.69	C
ATOM	7030	CD1	LEU	L	155	−116.331	−17.180	2.121	1.00	140.65	C
ATOM	7031	CD2	LEU	L	155	−118.850	−16.895	2.408	1.00	140.93	C
ATOM	7032	C	LEU	L	155	−116.732	−19.183	−0.610	1.00	140.07	C
ATOM	7033	O	LEU	L	155	−116.588	−20.271	−0.034	1.00	140.03	O
ATOM	7034	N	GLN	L	156	−115.773	−18.599	−1.355	1.00	139.27	N
ATOM	7035	CA	GLN	L	156	−114.412	−19.065	−1.560	1.00	138.38	C
ATOM	7036	CB	GLN	L	156	−114.000	−18.872	−3.028	1.00	138.41	C
ATOM	7037	C	GLN	L	156	−113.579	−18.175	−0.623	1.00	137.73	C
ATOM	7038	O	GLN	L	156	−113.130	−17.093	−1.018	1.00	137.58	O
ATOM	7039	N	SER	L	157	−113.446	−18.616	0.646	1.00	136.55	N
ATOM	7040	CA	SER	L	157	−112.721	−17.929	1.721	1.00	135.68	C
ATOM	7041	CB	SER	L	157	−112.829	−18.725	3.024	1.00	135.72	C
ATOM	7042	OG	SER	L	157	−112.063	−18.164	4.078	1.00	135.84	O
ATOM	7043	C	SER	L	157	−111.255	−17.640	1.348	1.00	134.91	C
ATOM	7044	O	SER	L	157	−110.917	−16.495	1.039	1.00	134.84	O
ATOM	7045	N	GLY	L	158	−110.430	−18.685	1.368	1.00	133.80	N
ATOM	7046	CA	GLY	L	158	−109.008	−18.642	1.050	1.00	132.49	C
ATOM	7047	C	GLY	L	158	−108.431	−20.040	0.993	1.00	131.57	C
ATOM	7048	O	GLY	L	158	−107.393	−20.317	1.605	1.00	131.46	O
ATOM	7049	N	ASN	L	159	−109.134	−20.930	0.262	1.00	131.76	N
ATOM	7050	CA	ASN	L	159	−108.811	−22.342	0.056	1.00	130.80	C
ATOM	7051	CB	ASN	L	159	−109.929	−23.221	0.638	1.00	131.25	C
ATOM	7052	CG	ASN	L	159	−109.880	−23.451	2.142	1.00	132.31	C
ATOM	7053	OD1	ASN	L	159	−109.971	−24.598	2.618	1.00	133.26	O
ATOM	7054	ND2	ASN	L	159	−109.757	−22.379	2.935	1.00	132.94	N
ATOM	7055	C	ASN	L	159	−108.624	−22.653	−1.431	1.00	129.73	C
ATOM	7056	O	ASN	L	159	−108.505	−23.822	−1.804	1.00	129.65	O
ATOM	7057	N	SER	L	160	−108.591	−21.603	−2.274	1.00	127.52	N
ATOM	7058	CA	SER	L	160	−108.425	−21.704	−3.725	1.00	126.23	C
ATOM	7059	CB	SER	L	160	−109.469	−20.846	−4.446	1.00	126.30	C
ATOM	7060	OG	SER	L	160	−109.200	−20.655	−5.828	1.00	126.45	O
ATOM	7061	C	SER	L	160	−106.999	−21.339	−4.185	1.00	125.19	C
ATOM	7062	O	SER	L	160	−106.455	−20.296	−3.786	1.00	125.17	O
ATOM	7063	N	GLN	L	161	−106.411	−22.217	−5.030	1.00	121.47	N
ATOM	7064	CA	GLN	L	161	−105.083	−22.072	−5.635	1.00	119.85	C
ATOM	7065	CB	GLN	L	161	−104.056	−23.039	−5.005	1.00	119.86	C
ATOM	7066	CG	GLN	L	161	−103.506	−22.571	−3.653	1.00	118.84	C
ATOM	7067	CD	GLN	L	161	−102.328	−23.378	−3.158	1.00	117.16	C
ATOM	7068	OE1	GLN	L	161	−102.397	−24.603	−2.963	1.00	116.92	O
ATOM	7069	NE2	GLN	L	161	−101.222	−22.698	−2.921	1.00	116.03	N
ATOM	7070	C	GLN	L	161	−105.242	−22.319	−7.133	1.00	118.95	C
ATOM	7071	O	GLN	L	161	−105.766	−23.363	−7.528	1.00	118.82	O
ATOM	7072	N	GLU	L	162	−104.825	−21.345	−7.963	1.00	118.33	N
ATOM	7073	CA	GLU	L	162	−104.962	−21.418	−9.426	1.00	117.09	C
ATOM	7074	CB	GLU	L	162	−105.833	−20.264	−9.963	1.00	117.33	C
ATOM	7075	CG	GLU	L	162	−107.230	−20.213	−9.365	1.00	118.23	C
ATOM	7076	CD	GLU	L	162	−108.093	−19.008	−9.697	1.00	119.60	C
ATOM	7077	OE1	GLU	L	162	−108.981	−18.686	−8.871	1.00	120.56	O
ATOM	7078	OE2	GLU	L	162	−107.893	−18.394	−10.774	1.00	119.76	O
ATOM	7079	C	GLU	L	162	−103.644	−21.459	−10.184	1.00	115.93	C
ATOM	7080	O	GLU	L	162	−102.662	−20.845	−9.766	1.00	115.86	O
ATOM	7081	N	SER	L	163	−103.647	−22.165	−11.322	1.00	111.07	N
ATOM	7082	CA	SER	L	163	−102.489	−22.316	−12.191	1.00	109.71	C
ATOM	7083	CB	SER	L	163	−101.877	−23.692	−11.995	1.00	109.62	C
ATOM	7084	OG	SER	L	163	−100.544	−23.673	−12.462	1.00	109.51	O
ATOM	7085	C	SER	L	163	−102.920	−22.133	−13.642	1.00	108.94	C
ATOM	7086	O	SER	L	163	−103.903	−22.743	−14.060	1.00	108.88	O
ATOM	7087	N	VAL	L	164	−102.201	−21.295	−14.405	1.00	105.03	N
ATOM	7088	CA	VAL	L	164	−102.542	−21.022	−15.802	1.00	103.99	C
ATOM	7089	CB	VAL	L	164	−102.773	−19.514	−16.036	1.00	103.97	C
ATOM	7090	CG1	VAL	L	164	−103.039	−19.200	−17.514	1.00	103.77	C
ATOM	7091	CG2	VAL	L	164	−103.910	−18.992	−15.150	1.00	103.63	C
ATOM	7092	C	VAL	L	164	−101.564	−21.644	−16.792	1.00	103.53	C
ATOM	7093	O	VAL	L	164	−100.362	−21.538	−16.601	1.00	103.39	O
ATOM	7094	N	THR	L	165	−102.091	−22.274	−17.853	1.00	101.85	N
ATOM	7095	CA	THR	L	165	−101.325	−22.954	−18.890	1.00	101.44	C
ATOM	7096	CB	THR	L	165	−102.216	−23.832	−19.797	1.00	101.33	C
ATOM	7097	OG1	THR	L	165	−101.518	−25.050	−20.047	1.00	101.63	O
ATOM	7098	CG2	THR	L	165	−102.564	−23.174	−21.154	1.00	101.27	C
ATOM	7099	C	THR	L	165	−100.281	−22.150	−19.652	1.00	101.38	C
ATOM	7100	O	THR	L	165	−99.298	−22.756	−20.095	1.00	101.70	O
ATOM	7101	N	GLU	L	166	−100.472	−20.818	−19.816	1.00	99.24	N
ATOM	7102	CA	GLU	L	166	−99.572	−19.945	−20.587	1.00	98.97	C
ATOM	7103	CB	GLU	L	166	−98.098	−19.974	−20.102	1.00	98.88	C
ATOM	7104	C	GLU	L	166	−99.697	−20.306	−22.078	1.00	98.77	C
ATOM	7105	O	GLU	L	166	−99.142	−21.307	−22.528	1.00	98.60	O
ATOM	7106	N	GLN	L	167	−100.477	−19.476	−22.806	1.00	98.98	N
ATOM	7107	CA	GLN	L	167	−100.866	−19.465	−24.226	1.00	98.76	C
ATOM	7108	CB	GLN	L	167	−100.619	−18.080	−24.829	1.00	98.72	C
ATOM	7109	CG	GLN	L	167	−101.771	−17.617	−25.680	1.00	99.11	C
ATOM	7110	CD	GLN	L	167	−101.652	−16.212	−26.210	1.00	98.86	C
ATOM	7111	OE1	GLN	L	167	−100.585	−15.749	−26.632	1.00	97.98	O
ATOM	7112	NE2	GLN	L	167	−102.774	−15.509	−26.232	1.00	98.96	N
ATOM	7113	C	GLN	L	167	−100.379	−20.583	−25.164	1.00	98.55	C
ATOM	7114	O	GLN	L	167	−99.184	−20.661	−25.437	1.00	98.71	O
ATOM	7115	N	ASP	L	168	−101.315	−21.413	−25.685	1.00	99.05	N
ATOM	7116	CA	ASP	L	168	−101.028	−22.523	−26.606	1.00	99.09	C
ATOM	7117	CB	ASP	L	168	−102.317	−23.274	−26.979	1.00	99.32	C
ATOM	7118	CG	ASP	L	168	−102.104	−24.674	−27.550	1.00	99.97	C
ATOM	7119	OD1	ASP	L	168	−102.562	−25.653	−26.910	1.00	100.99	O
ATOM	7120	OD2	ASP	L	168	−101.493	−24.792	−28.649	1.00	100.34	O
ATOM	7121	C	ASP	L	168	−100.314	−22.062	−27.873	1.00	98.85	C
ATOM	7122	O	ASP	L	168	−100.550	−20.955	−28.348	1.00	98.71	O
ATOM	7123	N	SER	L	169	−99.438	−22.909	−28.415	1.00	100.81	N
ATOM	7124	CA	SER	L	169	−98.685	−22.582	−29.627	1.00	101.16	C
ATOM	7125	CB	SER	L	169	−97.451	−23.472	−29.760	1.00	101.15	C
ATOM	7126	OG	SER	L	169	−97.761	−24.820	−29.446	1.00	101.65	O
ATOM	7127	C	SER	L	169	−99.575	−22.679	−30.869	1.00	101.31	C
ATOM	7128	O	SER	L	169	−99.754	−21.678	−31.580	1.00	101.38	O
ATOM	7129	N	LYS	L	170	−100.153	−23.883	−31.102	1.00	102.36	N
ATOM	7130	CA	LYS	L	170	−101.038	−24.200	−32.217	1.00	102.39	C
ATOM	7131	CB	LYS	L	170	−101.379	−25.698	−32.216	1.00	102.24	C
ATOM	7132	C	LYS	L	170	−102.314	−23.331	−32.252	1.00	102.58	C
ATOM	7133	O	LYS	L	170	−102.579	−22.700	−33.279	1.00	102.74	O
ATOM	7134	N	ASP	L	171	−103.082	−23.269	−31.147	1.00	102.64	N
ATOM	7135	CA	ASP	L	171	−104.324	−22.495	−31.140	1.00	102.90	C
ATOM	7136	CB	ASP	L	171	−105.526	−23.442	−31.106	1.00	103.27	C
ATOM	7137	CG	ASP	L	171	−105.506	−24.392	−29.928	1.00	104.57	C
ATOM	7138	OD1	ASP	L	171	−105.745	−23.923	−28.777	1.00	104.99	O
ATOM	7139	OD2	ASP	L	171	−105.253	−25.610	−30.149	1.00	106.77	O
ATOM	7140	C	ASP	L	171	−104.471	−21.335	−30.135	1.00	102.74	C
ATOM	7141	O	ASP	L	171	−105.576	−21.073	−29.646	1.00	102.59	O
ATOM	7142	N	SER	L	172	−103.359	−20.635	−29.852	1.00	100.89	N
ATOM	7143	CA	SER	L	172	−103.227	−19.472	−28.961	1.00	100.63	C
ATOM	7144	CB	SER	L	172	−103.082	−18.200	−29.785	1.00	100.55	C
ATOM	7145	OG	SER	L	172	−101.988	−18.375	−30.673	1.00	100.64	O
ATOM	7146	C	SER	L	172	−104.216	−19.316	−27.790	1.00	100.63	C
ATOM	7147	O	SER	L	172	−104.704	−18.214	−27.521	1.00	100.47	O
ATOM	7148	N	THR	L	173	−104.472	−20.427	−27.075	1.00	101.55	N
ATOM	7149	CA	THR	L	173	−105.404	−20.472	−25.947	1.00	101.94	C
ATOM	7150	CB	THR	L	173	−106.570	−21.451	−26.219	1.00	102.01	C
ATOM	7151	OG1	THR	L	173	−106.081	−22.676	−26.772	1.00	101.82	O
ATOM	7152	CG2	THR	L	173	−107.633	−20.855	−27.104	1.00	101.98	C
ATOM	7153	C	THR	L	173	−104.772	−20.776	−24.598	1.00	102.15	C
ATOM	7154	O	THR	L	173	−103.765	−21.484	−24.518	1.00	102.13	O
ATOM	7155	N	TYR	L	174	−105.412	−20.244	−23.535	1.00	103.33	N
ATOM	7156	CA	TYR	L	174	−105.056	−20.408	−22.127	1.00	103.64	C
ATOM	7157	CB	TYR	L	174	−105.206	−19.082	−21.362	1.00	103.64	C
ATOM	7158	CG	TYR	L	174	−104.277	−17.986	−21.829	1.00	104.23	C
ATOM	7159	CD1	TYR	L	174	−104.687	−17.055	−22.777	1.00	104.83	C
ATOM	7160	CE1	TYR	L	174	−103.842	−16.032	−23.202	1.00	104.70	C
ATOM	7161	CZ	TYR	L	174	−102.566	−15.937	−22.680	1.00	104.23	C
ATOM	7162	OH	TYR	L	174	−101.722	−14.944	−23.097	1.00	104.02	O
ATOM	7163	CE2	TYR	L	174	−102.141	−16.844	−21.726	1.00	104.62	C
ATOM	7164	CD2	TYR	L	174	−102.998	−17.860	−21.304	1.00	104.52	C
ATOM	7165	C	TYR	L	174	−105.997	−21.431	−21.504	1.00	103.87	C
ATOM	7166	O	TYR	L	174	−107.064	−21.700	−22.057	1.00	104.08	O
ATOM	7167	N	SER	L	175	−105.595	−21.995	−20.347	1.00	102.93	N
ATOM	7168	CA	SER	L	175	−106.332	−22.973	−19.539	1.00	103.00	C
ATOM	7169	CB	SER	L	175	−106.041	−24.403	−19.985	1.00	102.80	C
ATOM	7170	OG	SER	L	175	−106.359	−24.591	−21.356	1.00	102.75	O
ATOM	7171	C	SER	L	175	−105.962	−22.755	−18.072	1.00	103.21	C
ATOM	7172	O	SER	L	175	−104.783	−22.635	−17.747	1.00	103.20	O
ATOM	7173	N	LEU	L	176	−106.977	−22.654	−17.203	1.00	103.24	N
ATOM	7174	CA	LEU	L	176	−106.843	−22.420	−15.768	1.00	103.52	C
ATOM	7175	CB	LEU	L	176	−107.739	−21.236	−15.365	1.00	103.27	C
ATOM	7176	CG	LEU	L	176	−107.431	−20.545	−14.039	1.00	103.20	C
ATOM	7177	CD1	LEU	L	176	−107.592	−19.051	−14.163	1.00	103.38	C
ATOM	7178	CD2	LEU	L	176	−108.324	−21.057	−12.919	1.00	102.64	C
ATOM	7179	C	LEU	L	176	−107.242	−23.673	−14.992	1.00	104.05	C
ATOM	7180	O	LEU	L	176	−108.113	−24.416	−15.435	1.00	104.03	O
ATOM	7181	N	SER	L	177	−106.604	−23.901	−13.838	1.00	106.42	N
ATOM	7182	CA	SER	L	177	−106.865	−25.033	−12.954	1.00	107.19	C
ATOM	7183	CB	SER	L	177	−105.776	−26.103	−13.103	1.00	107.15	C
ATOM	7184	OG	SER	L	177	−105.396	−26.726	−11.883	1.00	107.51	O
ATOM	7185	C	SER	L	177	−106.960	−24.511	−11.525	1.00	107.81	C
ATOM	7186	O	SER	L	177	−105.938	−24.183	−10.913	1.00	107.98	O
ATOM	7187	N	SER	L	178	−108.187	−24.401	−11.006	1.00	109.82	N
ATOM	7188	CA	SER	L	178	−108.404	−23.923	−9.640	1.00	110.68	C
ATOM	7189	CB	SER	L	178	−109.637	−23.037	−9.550	1.00	110.59	C
ATOM	7190	OG	SER	L	178	−109.580	−22.260	−8.365	1.00	110.61	O
ATOM	7191	C	SER	L	178	−108.545	−25.119	−8.723	1.00	111.35	C
ATOM	7192	O	SER	L	178	−109.106	−26.138	−9.138	1.00	111.31	O
ATOM	7193	N	THR	L	179	−108.013	−25.016	−7.490	1.00	112.95	N
ATOM	7194	CA	THR	L	179	−108.073	−26.125	−6.548	1.00	113.88	C
ATOM	7195	CB	THR	L	179	−106.758	−26.909	−6.514	1.00	113.79	C
ATOM	7196	OG1	THR	L	179	−106.386	−27.280	−7.847	1.00	113.74	O
ATOM	7197	CG2	THR	L	179	−106.834	−28.145	−5.611	1.00	113.77	C
ATOM	7198	C	THR	L	179	−108.553	−25.724	−5.182	1.00	114.71	C
ATOM	7199	O	THR	L	179	−107.882	−24.962	−4.474	1.00	114.65	O
ATOM	7200	N	LEU	L	180	−109.722	−26.275	−4.812	1.00	118.09	N
ATOM	7201	CA	LEU	L	180	−110.357	−26.055	−3.520	1.00	119.20	C
ATOM	7202	CB	LEU	L	180	−111.889	−26.053	−3.651	1.00	119.25	C
ATOM	7203	CG	LEU	L	180	−112.697	−25.644	−2.407	1.00	119.28	C
ATOM	7204	CD1	LEU	L	180	−114.165	−25.928	−2.615	1.00	119.03	C
ATOM	7205	CD2	LEU	L	180	−112.461	−24.166	−2.009	1.00	119.13	C
ATOM	7206	C	LEU	L	180	−109.866	−27.159	−2.606	1.00	119.92	C
ATOM	7207	O	LEU	L	180	−110.065	−28.345	−2.899	1.00	119.94	O
ATOM	7208	N	THR	L	181	−109.184	−26.772	−1.521	1.00	122.06	N
ATOM	7209	CA	THR	L	181	−108.604	−27.754	−0.616	1.00	123.16	C
ATOM	7210	CB	THR	L	181	−107.127	−28.063	−1.014	1.00	123.08	C
ATOM	7211	OG1	THR	L	181	−106.567	−29.038	−0.136	1.00	123.12	O
ATOM	7212	CG2	THR	L	181	−106.238	−26.818	−1.078	1.00	123.36	C
ATOM	7213	C	THR	L	181	−108.908	−27.572	0.878	1.00	123.93	C
ATOM	7214	O	THR	L	181	−108.302	−26.732	1.551	1.00	123.89	O
ATOM	7215	N	LEU	L	182	−109.843	−28.402	1.387	1.00	125.26	N
ATOM	7216	CA	LEU	L	182	−110.268	−28.455	2.796	1.00	126.41	C
ATOM	7217	CB	LEU	L	182	−111.637	−27.786	3.030	1.00	126.34	C
ATOM	7218	CG	LEU	L	182	−112.719	−28.101	2.014	1.00	126.48	C
ATOM	7219	CD1	LEU	L	182	−113.984	−28.549	2.693	1.00	126.44	C
ATOM	7220	CD2	LEU	L	182	−112.970	−26.921	1.120	1.00	126.14	C
ATOM	7221	C	LEU	L	182	−110.209	−29.909	3.360	1.00	127.14	C
ATOM	7222	O	LEU	L	182	−110.020	−30.857	2.582	1.00	127.07	O
ATOM	7223	N	SER	L	183	−110.342	−30.071	4.710	1.00	128.51	N
ATOM	7224	CA	SER	L	183	−110.276	−31.365	5.420	1.00	129.50	C
ATOM	7225	CB	SER	L	183	−110.270	−31.151	6.933	1.00	129.46	C
ATOM	7226	OG	SER	L	183	−111.490	−30.598	7.401	1.00	129.48	O
ATOM	7227	C	SER	L	183	−111.373	−32.372	5.024	1.00	130.09	C
ATOM	7228	O	SER	L	183	−112.396	−31.961	4.470	1.00	130.38	O
ATOM	7229	N	LYS	L	184	−111.155	−33.690	5.317	1.00	129.50	N
ATOM	7230	CA	LYS	L	184	−112.095	−34.801	5.041	1.00	129.96	C
ATOM	7231	CB	LYS	L	184	−111.467	−36.149	5.457	1.00	129.94	C
ATOM	7232	CG	LYS	L	184	−112.371	−37.378	5.337	1.00	130.00	C
ATOM	7233	CD	LYS	L	184	−111.722	−38.645	5.899	1.00	130.26	C
ATOM	7234	CE	LYS	L	184	−111.877	−38.816	7.398	1.00	130.53	C
ATOM	7235	NZ	LYS	L	184	−111.238	−40.069	7.891	1.00	130.87	N
ATOM	7236	C	LYS	L	184	−113.443	−34.572	5.767	1.00	130.23	C
ATOM	7237	O	LYS	L	184	−114.502	−34.925	5.229	1.00	130.35	O
ATOM	7238	N	ALA	L	185	−113.383	−33.962	6.979	1.00	128.95	N
ATOM	7239	CA	ALA	L	185	−114.520	−33.631	7.835	1.00	129.05	C
ATOM	7240	CB	ALA	L	185	−114.017	−33.124	9.179	1.00	128.94	C
ATOM	7241	C	ALA	L	185	−115.462	−32.597	7.185	1.00	129.19	C
ATOM	7242	O	ALA	L	185	−116.605	−32.936	6.863	1.00	129.18	O
ATOM	7243	N	ASP	L	186	−114.966	−31.354	6.971	1.00	128.16	N
ATOM	7244	CA	ASP	L	186	−115.687	−30.221	6.376	1.00	128.35	C
ATOM	7245	CB	ASP	L	186	−114.806	−28.953	6.347	1.00	128.45	C
ATOM	7246	CG	ASP	L	186	−114.168	−28.529	7.673	1.00	129.00	C
ATOM	7247	OD1	ASP	L	186	−114.007	−29.394	8.569	1.00	129.87	O
ATOM	7248	OD2	ASP	L	186	−113.810	−27.337	7.806	1.00	129.15	O
ATOM	7249	C	ASP	L	186	−116.305	−30.524	4.993	1.00	128.32	C
ATOM	7250	O	ASP	L	186	−117.296	−29.897	4.615	1.00	128.32	O
ATOM	7251	N	TYR	L	187	−115.733	−31.497	4.259	1.00	127.00	N
ATOM	7252	CA	TYR	L	187	−116.209	−31.924	2.945	1.00	127.07	C
ATOM	7253	CB	TYR	L	187	−115.100	−32.670	2.180	1.00	126.77	C
ATOM	7254	CG	TYR	L	187	−115.569	−33.414	0.944	1.00	125.78	C
ATOM	7255	CD1	TYR	L	187	−115.946	−32.728	−0.206	1.00	124.72	C
ATOM	7256	CE1	TYR	L	187	−116.374	−33.406	−1.348	1.00	124.08	C
ATOM	7257	CZ	TYR	L	187	−116.404	−34.790	−1.356	1.00	123.97	C
ATOM	7258	OH	TYR	L	187	−116.821	−35.459	−2.483	1.00	123.19	O
ATOM	7259	CE2	TYR	L	187	−116.021	−35.494	−0.225	1.00	124.41	C
ATOM	7260	CD2	TYR	L	187	−115.610	−34.804	0.916	1.00	125.07	C
ATOM	7261	C	TYR	L	187	−117.468	−32.791	3.070	1.00	127.53	C
ATOM	7262	O	TYR	L	187	−118.479	−32.485	2.430	1.00	127.68	O
ATOM	7263	N	GLU	L	188	−117.399	−33.880	3.883	1.00	129.18	N
ATOM	7264	CA	GLU	L	188	−118.501	−34.818	4.128	1.00	129.38	C
ATOM	7265	CB	GLU	L	188	−118.018	−36.009	4.966	1.00	129.23	C
ATOM	7266	C	GLU	L	188	−119.720	−34.118	4.776	1.00	129.63	C
ATOM	7267	O	GLU	L	188	−120.858	−34.507	4.509	1.00	129.72	O
ATOM	7268	N	LYS	L	189	−119.473	−33.061	5.588	1.00	129.95	N
ATOM	7269	CA	LYS	L	189	−120.511	−32.273	6.264	1.00	130.00	C
ATOM	7270	CB	LYS	L	189	−120.039	−31.825	7.670	1.00	129.92	C
ATOM	7271	CG	LYS	L	189	−118.929	−30.782	7.664	1.00	129.43	C
ATOM	7272	CD	LYS	L	189	−118.905	−29.927	8.907	1.00	128.46	C
ATOM	7273	CE	LYS	L	189	−118.314	−28.582	8.591	1.00	127.90	C
ATOM	7274	NZ	LYS	L	189	−118.087	−27.786	9.815	1.00	127.98	N
ATOM	7275	C	LYS	L	189	−121.069	−31.088	5.414	1.00	130.15	C
ATOM	7276	O	LYS	L	189	−121.505	−30.081	5.980	1.00	130.07	O
ATOM	7277	N	HIS	L	190	−121.065	−31.213	4.066	1.00	131.73	N
ATOM	7278	CA	HIS	L	190	−121.571	−30.175	3.149	1.00	131.90	C
ATOM	7279	CB	HIS	L	190	−120.507	−29.099	2.854	1.00	131.89	C
ATOM	7280	CG	HIS	L	190	−120.453	−27.999	3.875	1.00	132.02	C
ATOM	7281	ND1	HIS	L	190	−119.727	−28.135	5.050	1.00	132.00	N
ATOM	7282	CE1	HIS	L	190	−119.891	−26.999	5.709	1.00	131.80	C
ATOM	7283	NE2	HIS	L	190	−120.668	−26.149	5.035	1.00	131.85	N
ATOM	7284	CD2	HIS	L	190	−121.033	−26.774	3.863	1.00	132.09	C
ATOM	7285	C	HIS	L	190	−122.174	−30.772	1.865	1.00	132.01	C
ATOM	7286	O	HIS	L	190	−121.590	−31.676	1.268	1.00	131.94	O
ATOM	7287	N	LYS	L	191	−123.346	−30.255	1.450	1.00	133.19	N
ATOM	7288	CA	LYS	L	191	−124.125	−30.712	0.292	1.00	133.24	C
ATOM	7289	CB	LYS	L	191	−125.583	−30.226	0.390	1.00	133.19	C
ATOM	7290	C	LYS	L	191	−123.561	−30.517	−1.125	1.00	133.24	C
ATOM	7291	O	LYS	L	191	−122.976	−31.456	−1.677	1.00	133.17	O
ATOM	7292	N	VAL	L	192	−123.773	−29.304	−1.709	1.00	134.37	N
ATOM	7293	CA	VAL	L	192	−123.399	−28.887	−3.077	1.00	134.31	C
ATOM	7294	CB	VAL	L	192	−124.535	−28.062	−3.783	1.00	134.37	C
ATOM	7295	CG1	VAL	L	192	−125.918	−28.395	−3.228	1.00	134.20	C
ATOM	7296	CG2	VAL	L	192	−124.511	−28.243	−5.303	1.00	134.07	C
ATOM	7297	C	VAL	L	192	−122.028	−28.179	−3.199	1.00	134.22	C
ATOM	7298	O	VAL	L	192	−121.539	−27.580	−2.235	1.00	134.12	O
ATOM	7299	N	TYR	L	193	−121.430	−28.253	−4.417	1.00	133.81	N
ATOM	7300	CA	TYR	L	193	−120.149	−27.659	−4.813	1.00	133.58	C
ATOM	7301	CB	TYR	L	193	−119.001	−28.671	−4.620	1.00	133.46	C
ATOM	7302	CG	TYR	L	193	−118.739	−29.051	−3.181	1.00	133.01	C
ATOM	7303	CD1	TYR	L	193	−118.875	−30.366	−2.752	1.00	132.19	C
ATOM	7304	CE1	TYR	L	193	−118.643	−30.720	−1.424	1.00	131.86	C
ATOM	7305	CZ	TYR	L	193	−118.251	−29.752	−0.512	1.00	131.88	C
ATOM	7306	OH	TYR	L	193	−118.014	−30.081	0.802	1.00	131.77	O
ATOM	7307	CE2	TYR	L	193	−118.107	−28.437	−0.920	1.00	132.04	C
ATOM	7308	CD2	TYR	L	193	−118.345	−28.096	−2.248	1.00	132.53	C
ATOM	7309	C	TYR	L	193	−120.174	−27.183	−6.281	1.00	133.60	C
ATOM	7310	O	TYR	L	193	−120.575	−27.945	−7.169	1.00	133.62	O
ATOM	7311	N	ALA	L	194	−119.740	−25.930	−6.530	1.00	133.66	N
ATOM	7312	CA	ALA	L	194	−119.665	−25.342	−7.876	1.00	133.63	C
ATOM	7313	CB	ALA	L	194	−121.049	−24.958	−8.382	1.00	133.53	C
ATOM	7314	C	ALA	L	194	−118.735	−24.126	−7.930	1.00	133.57	C
ATOM	7315	O	ALA	L	194	−118.548	−23.429	−6.929	1.00	133.52	O
ATOM	7316	N	CYS	L	195	−118.161	−23.874	−9.113	1.00	133.43	N
ATOM	7317	CA	CYS	L	195	−117.267	−22.740	−9.350	1.00	133.34	C
ATOM	7318	CB	CYS	L	195	−115.877	−23.185	−9.815	1.00	133.14	C
ATOM	7319	SG	CYS	L	195	−115.801	−24.879	−10.473	1.00	132.53	S
ATOM	7320	C	CYS	L	195	−117.914	−21.755	−10.331	1.00	133.40	C
ATOM	7321	O	CYS	L	195	−118.453	−22.174	−11.358	1.00	133.32	O
ATOM	7322	N	GLU	L	196	−117.874	−20.455	−10.011	1.00	134.32	N
ATOM	7323	CA	GLU	L	196	−118.465	−19.444	−10.880	1.00	134.46	C
ATOM	7324	CB	GLU	L	196	−119.065	−18.302	−10.040	1.00	134.58	C
ATOM	7325	CG	GLU	L	196	−120.267	−17.617	−10.681	1.00	135.04	C
ATOM	7326	CD	GLU	L	196	−121.579	−18.381	−10.662	1.00	135.55	C
ATOM	7327	OE1	GLU	L	196	−121.760	−19.254	−9.778	1.00	135.81	O
ATOM	7328	OE2	GLU	L	196	−122.434	−18.093	−11.532	1.00	135.51	O
ATOM	7329	C	GLU	L	196	−117.416	−18.934	−11.879	1.00	134.37	C
ATOM	7330	O	GLU	L	196	−116.423	−18.340	−11.458	1.00	134.31	O
ATOM	7331	N	VAL	L	197	−117.636	−19.176	−13.196	1.00	133.36	N
ATOM	7332	CA	VAL	L	197	−116.719	−18.778	−14.283	1.00	133.27	C
ATOM	7333	CB	VAL	L	197	−116.337	−19.982	−15.188	1.00	133.17	C
ATOM	7334	CG1	VAL	L	197	−115.194	−19.624	−16.131	1.00	132.97	C
ATOM	7335	CG2	VAL	L	197	−115.984	−21.209	−14.357	1.00	133.07	C
ATOM	7336	C	VAL	L	197	−117.217	−17.552	−15.101	1.00	133.31	C
ATOM	7337	O	VAL	L	197	−118.137	−17.677	−15.917	1.00	133.28	O
ATOM	7338	N	THR	L	198	−116.575	−16.382	−14.887	1.00	133.26	N
ATOM	7339	CA	THR	L	198	−116.887	−15.099	−15.541	1.00	133.21	C
ATOM	7340	CB	THR	L	198	−116.962	−13.990	−14.468	1.00	133.25	C
ATOM	7341	OG1	THR	L	198	−117.383	−14.550	−13.215	1.00	133.25	O
ATOM	7342	CG2	THR	L	198	−117.879	−12.849	−14.872	1.00	133.03	C
ATOM	7343	C	THR	L	198	−115.863	−14.812	−16.668	1.00	133.19	C
ATOM	7344	O	THR	L	198	−114.677	−14.630	−16.373	1.00	133.08	O
ATOM	7345	N	HIS	L	199	−116.314	−14.791	−17.952	1.00	132.62	N
ATOM	7346	CA	HIS	L	199	−115.419	−14.594	−19.104	1.00	132.74	C
ATOM	7347	CB	HIS	L	199	−114.732	−15.945	−19.441	1.00	132.53	C
ATOM	7348	CG	HIS	L	199	−113.816	−15.924	−20.625	1.00	132.36	C
ATOM	7349	ND1	HIS	L	199	−112.592	−15.293	−20.576	1.00	132.07	N
ATOM	7350	CE1	HIS	L	199	−112.048	−15.482	−21.764	1.00	131.86	C
ATOM	7351	NE2	HIS	L	199	−112.843	−16.186	−22.565	1.00	132.18	N
ATOM	7352	CD2	HIS	L	199	−113.974	−16.479	−21.850	1.00	132.26	C
ATOM	7353	C	HIS	L	199	−116.057	−13.921	−20.361	1.00	133.02	C
ATOM	7354	O	HIS	L	199	−116.002	−12.693	−20.484	1.00	133.04	O
ATOM	7355	N	GLN	L	200	−116.617	−14.739	−21.297	1.00	135.50	N
ATOM	7356	CA	GLN	L	200	−117.267	−14.333	−22.548	1.00	135.70	C
ATOM	7357	CB	GLN	L	200	−116.849	−15.247	−23.719	1.00	135.56	C
ATOM	7358	C	GLN	L	200	−118.801	−14.300	−22.335	1.00	135.94	C
ATOM	7359	O	GLN	L	200	−119.373	−13.205	−22.296	1.00	135.79	O
ATOM	7360	N	GLY	L	201	−119.440	−15.467	−22.161	1.00	136.37	N
ATOM	7361	CA	GLY	L	201	−120.882	−15.553	−21.905	1.00	136.75	C
ATOM	7362	C	GLY	L	201	−121.202	−15.288	−20.440	1.00	136.97	C
ATOM	7363	O	GLY	L	201	−120.302	−15.402	−19.596	1.00	137.00	O
ATOM	7364	N	LEU	L	202	−122.472	−14.930	−20.109	1.00	134.74	N
ATOM	7365	CA	LEU	L	202	−122.867	−14.645	−18.717	1.00	134.75	C
ATOM	7366	CB	LEU	L	202	−124.283	−14.035	−18.632	1.00	134.74	C
ATOM	7367	CG	LEU	L	202	−124.427	−12.560	−18.170	1.00	134.94	C
ATOM	7368	CD1	LEU	L	202	−123.963	−12.347	−16.720	1.00	134.59	C
ATOM	7369	CD2	LEU	L	202	−123.779	−11.579	−19.147	1.00	134.83	C
ATOM	7370	C	LEU	L	202	−122.724	−15.854	−17.774	1.00	134.70	C
ATOM	7371	O	LEU	L	202	−123.054	−16.975	−18.176	1.00	134.76	O
ATOM	7372	N	SER	L	203	−122.207	−15.602	−16.531	1.00	132.85	N
ATOM	7373	CA	SER	L	203	−121.939	−16.541	−15.416	1.00	132.69	C
ATOM	7374	CB	SER	L	203	−122.407	−15.956	−14.084	1.00	132.67	C
ATOM	7375	OG	SER	L	203	−121.456	−15.053	−13.544	1.00	132.56	O
ATOM	7376	C	SER	L	203	−122.401	−18.015	−15.589	1.00	132.56	C
ATOM	7377	O	SER	L	203	−123.604	−18.287	−15.636	1.00	132.54	O
ATOM	7378	N	SER	L	204	−121.425	−18.953	−15.678	1.00	131.25	N
ATOM	7379	CA	SER	L	204	−121.638	−20.395	−15.878	1.00	130.96	C
ATOM	7380	CB	SER	L	204	−121.054	−20.820	−17.229	1.00	130.82	C
ATOM	7381	OG	SER	L	204	−120.861	−22.219	−17.363	1.00	130.49	O
ATOM	7382	C	SER	L	204	−121.140	−21.326	−14.709	1.00	130.87	C
ATOM	7383	O	SER	L	204	−119.996	−21.801	−14.776	1.00	130.88	O
ATOM	7384	N	PRO	L	205	−121.976	−21.642	−13.662	1.00	129.59	N
ATOM	7385	CA	PRO	L	205	−121.498	−22.529	−12.582	1.00	129.34	C
ATOM	7386	CB	PRO	L	205	−122.188	−21.966	−11.329	1.00	129.18	C
ATOM	7387	CG	PRO	L	205	−123.445	−21.284	−11.852	1.00	129.34	C
ATOM	7388	CD	PRO	L	205	−123.354	−21.187	−13.377	1.00	129.61	C
ATOM	7389	C	PRO	L	205	−121.783	−24.031	−12.775	1.00	129.05	C
ATOM	7390	O	PRO	L	205	−122.934	−24.470	−12.651	1.00	129.03	O
ATOM	7391	N	VAL	L	206	−120.725	−24.823	−13.066	1.00	126.14	N
ATOM	7392	CA	VAL	L	206	−120.845	−26.276	−13.214	1.00	125.92	C
ATOM	7393	CB	VAL	L	206	−119.918	−26.893	−14.300	1.00	125.90	C
ATOM	7394	CG1	VAL	L	206	−119.966	−28.417	−14.279	1.00	125.78	C
ATOM	7395	CG2	VAL	L	206	−120.302	−26.382	−15.685	1.00	125.56	C
ATOM	7396	C	VAL	L	206	−120.724	−26.885	−11.794	1.00	125.88	C
ATOM	7397	O	VAL	L	206	−119.719	−26.691	−11.099	1.00	125.71	O
ATOM	7398	N	THR	L	207	−121.805	−27.568	−11.367	1.00	124.30	N
ATOM	7399	CA	THR	L	207	−121.986	−28.167	−10.047	1.00	124.17	C
ATOM	7400	CB	THR	L	207	−123.337	−27.725	−9.471	1.00	124.15	C
ATOM	7401	C	THR	L	207	−121.831	−29.677	−9.931	1.00	124.10	C
ATOM	7402	O	THR	L	207	−121.768	−30.406	−10.930	1.00	123.98	O
ATOM	7403	N	LYS	L	208	−121.783	−30.124	−8.660	1.00	122.52	N
ATOM	7404	CA	LYS	L	208	−121.667	−31.498	−8.184	1.00	122.52	C
ATOM	7405	CB	LYS	L	208	−120.276	−32.080	−8.506	1.00	122.45	C
ATOM	7406	C	LYS	L	208	−121.901	−31.530	−6.663	1.00	122.58	C
ATOM	7407	O	LYS	L	208	−121.475	−30.621	−5.947	1.00	122.64	O
ATOM	7408	N	SER	L	209	−122.584	−32.578	−6.183	1.00	120.30	N
ATOM	7409	CA	SER	L	209	−122.872	−32.856	−4.770	1.00	120.25	C
ATOM	7410	CB	SER	L	209	−124.216	−32.272	−4.345	1.00	120.16	C
ATOM	7411	OG	SER	L	209	−125.283	−32.698	−5.173	1.00	120.24	O
ATOM	7412	C	SER	L	209	−122.830	−34.387	−4.659	1.00	120.28	C
ATOM	7413	O	SER	L	209	−123.482	−35.073	−5.458	1.00	120.26	O
ATOM	7414	N	PHE	L	210	−122.005	−34.914	−3.725	1.00	117.17	N
ATOM	7415	CA	PHE	L	210	−121.750	−36.351	−3.506	1.00	117.28	C
ATOM	7416	CB	PHE	L	210	−120.883	−36.611	−2.253	1.00	117.33	C
ATOM	7417	CG	PHE	L	210	−121.132	−35.842	−0.967	1.00	117.55	C
ATOM	7418	CD1	PHE	L	210	−120.074	−35.499	−0.128	1.00	117.54	C
ATOM	7419	CE1	PHE	L	210	−120.300	−34.825	1.076	1.00	117.48	C
ATOM	7420	CZ	PHE	L	210	−121.585	−34.509	1.459	1.00	117.93	C
ATOM	7421	CE2	PHE	L	210	−122.650	−34.837	0.646	1.00	118.09	C
ATOM	7422	CD2	PHE	L	210	−122.427	−35.521	−0.560	1.00	117.92	C
ATOM	7423	C	PHE	L	210	−122.906	−37.373	−3.653	1.00	117.31	C
ATOM	7424	O	PHE	L	210	−122.822	−38.309	−4.460	1.00	117.16	O
TER	7425		PHE	L	210
END