Crystallized LXR polypeptide in complex with a ligand and screening methods employing same

Abstract

Solved three-dimensional crystal structures of a human LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide is disclosed. Contact points between the LXR and the ligands are also disclosed. Additionally, methods of designing modulators of the biological activity of LXR, and other LXR ligand binding domain polypeptides, are also disclosed.

Description

TECHNICAL FIELD

[0002] The present invention relates generally to the structure of LXR, and more particularly to the crystalline structure of LXR in complex with a ligand. The invention further relates to methods by which modulators and ligands of a nuclear receptor, including a LXRβ can be identified.

Abbreviations
	APS	Advanced Photon Source
	cDNA	complementary DNA
	DBD	DNA binding domain
	DMSO	dimethyl sulfoxide
	DNA	deoxyribonucleic acid
	DTT	dithiothreitol
	EDTA	ethylenediaminetetraacetic acid
	EPC	24(S), 25-epoxycholesterol
	FXR	farnesoid X receptor
	HRE	hormone response element
	kDa	kilodalton(s)
	LBD	ligand binding domain
	LN2	liquid nitrogen
	LXR	liver X receptor
	LXRα	liver X receptor α
	LXRβ	liver X receptor β
	NDP	nucleotide diphosphate
	NR	nuclear receptor
	nt	nucleotide
	PCR	polymerase chain reaction
	pl	isoelectric point
	RMSD	root-mean-square deviation
	SIRAS	single isomorphous replacement anomalous
		scattering
	SPAP	secreted placental alkaline phosphatase
	SRC1	steroid receptor coactivator 1
Amino Acid Abbreviations
	Single-Letter Code	Three-Letter Code	Name
	A	Ala	Alanine
	V	Val	Valine
	L	Leu	Leucine
	I	Ile	Isoleucine
	P	Pro	Proline
	F	Phe	Phenylalanine
	W	Trp	Tryptophan
	M	Met	Methionine
	G	Gly	Glycine
	S	Ser	Serine
	T	Thr	Threonine
	C	Cys	Cysteine
	Y	Tyr	Tyrosine
	N	Asn	Asparagine
	Q	Gln	Glutamine
	D	Asp	Aspartic Acid
	E	Glu	Glutamic Acid
	K	Lys	Lysine
	R	Arg	Arginine
	H	His	Histidine

[0003]

Functionally Equivalent Codons
Amino Acid	Codons
Alanine	Ala	A	GCA GCC GCG GCU
Cysteine	Cys	C	UGC UGU
Aspartic Acid	Asp	D	GAC GAU
Glumatic acid	Glu	E	GAA GAG
Phenylalanine	Phe	F	UUC UUU
Glycine	Gly	G	GGA GGC GGG GGU
Histidine	His	H	CAC CAU
Isoleucine	Ile	I	AUA AUC AUU
Lysine	Lys	K	AAA AAG
Methionine	Met	M	AUG
Asparagine	Asn	N	AAC AAU
Proline	Pro	P	CCA CCC CCG CCU
Glutamine	Gln	Q	CAA CAG
Threonine	Thr	T	ACA ACC ACG ACU
Valine	Val	V	GUA GUC GUG GUU
Tryptophan	Trp	W	UGG
Tyrosine	Tyr	Y	UAC UAU
Leucine	Leu	L	UUA UUG CUA CUC CUG CUU
Arginine	Arg	R	AGA AGG CGA CGC CGG CGU
Serine	Ser	S	ACG AGU UCA UCC UCG UCU

BACKGROUND ART

[0004] Nuclear receptors represent a superfamily of proteins that specifically bind a physiologically relevant small molecule, such as a hormone or vitamin. As a result of a molecule binding to a nuclear receptor, the nuclear receptor changes the ability of a cell to transcribe DNA, i.e. nuclear receptors modulate the transcription of DNA. However they can also have transcription independent actions.

[0005] Unlike integral membrane receptors and membrane-associated receptors, nuclear receptors reside in either the cytoplasm or nucleus of eukaryotic cells. Thus nuclear receptors comprise a class of intracellular, soluble ligand-regulated transcription factors. Nuclear receptors include but are not limited to receptors for glucocorticoids, androgens, mineralocorticoids, progestins, estrogens, thyroid hormones, vitamin D retinoids, and icosanoids. Many nuclear receptors, identified by either sequence homology to known receptors (See, Drewes et al., (1996) Mol. Cell. Biol. 16:925-31) or based on their affinity for specific DNA binding sites in gene promoters (See, Sladek et al., Genes Dev. 4:2353-65), have unascertained ligands and are therefore termed “orphan receptors.”

[0006] Structurally, nuclear receptors are generally characterized by two distinct structural elements. First, nuclear receptors comprise a central DNA binding domain that targets the receptor to specific DNA sequences, which are known as hormone response elements (HREs). The DNA binding domains of these receptors are related in structure and sequence, and are located within the middle of the receptor. Second, the C-terminal region of nuclear receptors encompasses the ligand binding domain (LBD). Upon binding a ligand, the receptor shifts to a transcriptionally active state.

[0007] Thus, the steroid/nuclear receptor superfamily is comprised of multi-domain transcription factors that regulate transcriptional activation in response to binding small molecules. The two liver X receptors, LXRα (NR1H3) and LXRβ (NR1H2), together with the farnesoid X receptor FXR (NR1H4) form a subset of the steroid/nuclear receptor superfamily that bind oxysterols (Janowski, et al., (1999) Proc. Nat. Acad. Sci. U.S.A. 96:266-271) and bile acids (Parks et al., (1999) Science 284:1365-1368; Makishima et al., (1999) Science 284:1362-1365), respectively. This subset of receptors is involved in the regulation of genes involved in cholesterol metabolism, transport, and elimination. LXR target genes include the ATP binding cassette ABCA1, SREBP1, etc. (Lehmann et al., (1997) J. Biol. Chem. 272:3137-3140; Schultz et al., (2000) Genes Dev. 14:2831-2838; Venkateswaran et al., (2000) Proc. Nat. Acad. Sci. U.S.A. 97:12097-12102). Oxysterols as natural LXR ligands is in accordance with their role in regulating cholesterol metabolism, and this family of compounds shows clear structure activity relationships with regard to LXR activation (Lehmann et al., (1997) J. Biol. Chem. 272:3137-3140; Forman et al., (1997) Proc. Nat. Acad. Sci. U.S.A. 94:10588-10593; Spencer et al., (2001) Journal of Med. Chem. 44:886-897). One of the most potent activators of both LXR subtypes is 24(S), 25-epoxycholesterol, which is widely found in the liver (Lehmann et al., (1997) J. Biol. Chem. 272: 3137-3140).

[0008] Because of the medical interest in cholesterol regulation, LXR has also been the target for drug discovery efforts. Several LXR specific compounds have been identified, including the compound N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide (also referred to interchangeably herein as “T0901317” and “T317”) (Schultz et al., (2000) Gene Dev. 14:2831-2838), a sulfonamide steroid mimetic that is as potent in activating both LXRs than the natural ligands. These compounds have been shown to be effective in vivo in reducing serum cholesterol levels and plaque accumulation.

[0009] Unraveling the structural basis of how LXR recognizes an array of different endogenous and exogenous compounds, including both small and large ligands, is critical to understanding how compounds, such as cholesterol, are cleared from the body. Such knowledge can also improve the ability to predict and avoid dangerous drug-drug interactions.

[0010] Polypeptides, including the ligand binding domain of LXRα and the ligand binding domain of LXRβ, have a three-dimensional structure determined by the primary amino acid sequence and the environment surrounding the polypeptide. This three-dimensional structure establishes the polypeptide's activity, stability, binding affinity, binding specificity, and other biochemical attributes. Thus, knowledge of a protein's three-dimensional structure can provide much guidance in designing agents that mimic, inhibit, or improve its biological activity in soluble or membrane bound forms.

[0011] The three-dimensional structure of a polypeptide can be determined in a number of ways. Many of the most precise methods employ X-ray crystallography (See, e.g., Van Holde, (1971) Physical Biochemistry, Prentice-Hall, New Jersey, pp. 221-39). This technique relies on the ability of crystalline lattices to diffract X-rays or other forms of radiation. Diffraction experiments suitable for determining the three-dimensional structure of macromolecules typically require high-quality crystals. Unfortunately, such crystals have been unavailable for the ligand binding domain of LXR as well as many other proteins of interest. Thus, high-quality diffracting crystals of the ligand binding domain of LXR would greatly assist in the elucidation of LXR's three-dimensional structure, and would provide insight into the ligand binding properties of LXR.

[0012] Clearly, the solved crystal structure of the LXR ligand binding domain would be useful in the design of modulators of activity mediated by all LXR isoforms. Additionally, evaluation of the available sequence data has made it clear that LXR shows structural homology with the three-dimensional fold of other proteins.

[0013] A solved LXR-ligand crystal structure would provide structural details and insights necessary to design a modulator of LXR that maximizes preferred requirements for any modulator, i.e. potency and specificity. A LXR-ligand-coactivator fragment crystal structure would provide additional information. By exploiting the structural details obtained from a LXR-ligand crystal structure, or a LXR-ligand-coactivator fragment crystal structure, it would be possible to design a LXR modulator that, despite LXR's similarity with other proteins, exploits the unique structural features of LXR. A LXR modulator developed using structure-assisted design would take advantage of heretofore unknown LXR structural considerations and thus be more effective than a modulator developed using homology-based design. Potential or existent homology models cannot provide the necessary degree of specificity. A LXR modulator designed using the structural coordinates of a crystalline form of LXR would also provide a starting point for the development of modulators of other structurally similar proteins.

[0014] What is needed, therefore, is a crystallized form of a LXR LBD polypeptide, preferably in complex with a ligand. Acquisition of crystals of the LXR LBD polypeptide will permit the three dimensional structure of the LXR LBD to be determined. Knowledge of this three dimensional structure will facilitate the design of modulators of LXR activity, as well as the activity of other NRs. Such modulators can lead to therapeutic compounds to treat a wide range of conditions, including conditions associated with high serum cholesterol levels.

SUMMARY OF THE INVENTION

[0015] A crystalline form comprising a substantially pure LXR ligand binding domain polypeptide and a ligand is disclosed. Preferably, the crystalline form has lattice constants of a=60.25 Å, b=82.45 Å, c=123.18 Å, α=90°, β=90°, γ=90°. More preferably, the crystalline form is an orthogonal crystalline form. Even more preferably, the crystalline form has a space group of P21212. Still more preferably, the LXR ligand binding domain polypeptide has the amino acid sequence shown in SEQ ID NO: 8. It is also preferable that the ligand is N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide.

[0016] Yet another crystalline form comprising a substantially pure LXR ligand binding domain polypeptide, a ligand and a coactivator polypeptide is disclosed. Preferably, the crystalline form has lattice constants of a=71.17 Å, b=120.01 Å, c=147.56 Å, α=90°, β=90°, γ=90°. More preferably, the crystalline form is an orthoganol crystalline form. Even more preferably, the crystalline form has a space group of C2221. Still more preferably, the LXR ligand binding domain polypeptide has the amino acid sequence shown in SEQ ID NO: 8. It is also preferable that the ligand is is 24(S), 25-epoxycholesterol and the coactivator polypeptide comprises a SRC1 polypeptide comprising the sequence of SEQ ID NO: 9.

[0017] A method for determining the three-dimensional structure of a crystallized LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide to a resolution of about 2.8 Å or better is disclosed. In a preferred embodiment, the method comprises: (a) crystallizing a LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide to form a crystallized complex; and (b) analyzing the crystallized complex to determine the three-dimensional structure of the LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide, whereby the three-dimensional structure of a crystallized LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide is determined to a resolution of about 2.8 Å or better. It is also preferable that the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and that the coactivator polypeptide comprises a SRCI polypeptide comprising the sequence of SEQ ID NO: 9.

[0018] A method of generating a crystalline form comprising a LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide is disclosed. In a preferred embodiment, the method comprises: (a) incubating a solution comprising a LXR ligand binding domain and one or more of a ligand and a coactivator polypeptide with an equal volume of reservoir; and (b) crystallizing the LXR ligand binding domain polypeptide and one or more of a ligand and a coactivator polypeptide using the hanging drop method, whereby a crystalline form of a LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide is generated. It is also preferable that the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and that the coactivator polypeptide comprises a SRC1 polypeptide comprising the sequence of SEQ ID NO: 9.

[0019] A method of designing a modulator of a NR polypeptide is disclosed. In a preferred embodiment, the method comprises: (a) designing a potential modulator of a NR polypeptide that will make interactions with amino acids in a ligand binding site of the NR polypeptide, based upon a crystalline structure comprising a LXR ligand binding domain polypeptide in complex with a one or more of a ligand and a coactivator polypeptide; (b) synthesizing the modulator; and (c) determining whether the potential modulator modulates the activity of the NR polypeptide, whereby a modulator of a NR polypeptide is designed. It is preferable that the NR comprises a LXR and more preferably a LXRβ comprising the sequence of SEQ ID NO: 4. It is also preferable that the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and that the coactivator polypeptide comprises a SRC1 polypeptide comprising the sequence of SEQ ID NO: 9.

[0020] In an alternative embodiment, a method of designing a modulator that selectively modulates the activity of a NR polypeptide in accordance with the present invention comprises: (a) obtaining a crystalline form comprising a LXRβ ligand binding domain polypeptide in complex with one or more of a ligand and a coativator polypeptide; (b) evaluating the three-dimensional structure of the crystallized LXRβ ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide; and (c) synthesizing a potential modulator based on the three-dimensional structure of the crystallized LXRβ ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide, whereby a modulator that selectively modulates the activity of a NR polypeptide is designed. Preferably, the method further comprises contacting a NR ligand binding domain polypeptide with the potential modulator and one or more of a ligand and a coactivator polypeptide; and assaying the NR ligand binding domain polypeptide for binding of the potential modulator, for a change in activity of the NR ligand binding domain polypeptide, or both. In this embodiment, it is preferable that the NR comprises a LXR and more preferably a LXRβ comprising the sequence of SEQ ID NO: 4. It is also preferable that the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and that the coactivator polypeptide comprises a SRC1 polypeptide comprising the sequence of SEQ ID NO: 9.

[0021] A method of screening a plurality of compounds for a modulator of a NR ligand binding domain polypeptide is also disclosed. In a preferred embodiment, the method comprises: (a) providing a library of test samples; (b) contacting a crystalline form comprising a LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide with each test sample; (c) detecting an interaction between a test sample and the crystalline LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide; (d) identifying a test sample that interacts with the crystalline LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide; and (e) isolating a test sample that interacts with the crystalline LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coregulator polypeptide, whereby a plurality of compounds is screened for a modulator of a NR ligand binding domain polypeptide. In this embodiment, it is preferable that the NR comprises a LXR and more preferably a LXRβ comprising the sequence of SEQ ID NO: 4. It is also preferable that the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and that the coactivator polypeptide comprises a SRCI polypeptide comprising the sequence of SEQ ID NO: 9.

[0022] Additionally, a method for identifying a NR modulator is disclosed. IN a preferred embodiment, the method comprises: (a) providing atomic coordinates of a LXR ligand binding domain in complex with one or more of a ligand and a coactivator polypeptide to a computerized modeling system; and (b) modeling ligands that fit spatially into the binding pocket of the LXR ligand binding domain to thereby identify a NR modulator. Preferably the method further comprises identifying in an assay for NR-mediated activity a modeled ligand that increases or decreases the activity of the NR. In this embodiment, it is preferable that the NR comprises a LXR and more preferably a LXRβ comprising the sequence of SEQ ID NO: 4. It is also preferable that the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and that the coactivator polypeptide comprises a SRC1 polypeptide comprising the sequence of SEQ ID NO: 9.

[0023] In another embodiment of the present invention, a method of identifying a LXR modulator that selectively modulates the activity of a LXRβ polypeptide compared to other polypeptides is disclosed. In a preferred embodiment, the method comprises: (a) providing atomic coordinates of a LXRβ ligand binding domain in complex with one or more of a ligand and a coactivator polypeptide to a computerized modeling system; and (b) modeling a ligand that fits into the binding pocket of a LXRβ ligand binding domain and that interacts with residues of a LXRβ that are conserved among LXR subtypes to thereby identify a LXRβ modulator that selectively modulates the activity of a LXRβ polypeptide compared to other polypeptides. In this embodiment, it is preferable that the LXRβ comprises the sequence of SEQ ID NO: 4. It is also preferable that the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and that the coactivator polypeptide comprises a SRC1 polypeptide comprising the sequence of SEQ ID NO: 9. It is more preferable that the method further comprises identifying in a biological assay for LXRβ activity a modeled ligand that selectively binds to said LXRβ and increases or decreases the activity of said LXRβ.

[0024] In yet another embodiment, a method of designing a modulator of a NR polypeptide is disclosed. In a preferred embodiment, the method comprises: (a) selecting a candidate NR ligand; (b) determining which amino acid or amino acids of a NR polypeptide interact with the ligand using a three-dimensional model of a crystallized protein, the model comprising a LXRβ ligand binding domain in complex with one or more of a ligand and a coactivator polypeptide; (c) identifying in a biological assay for NR activity a degree to which the ligand modulates the activity of the NR polypeptide; (d) selecting a chemical modification of the ligand wherein the interaction between the amino acids of the NR polypeptide and the ligand is predicted to be modulated by the chemical modification; (e) synthesizing a ligand having the chemical modified to form a modified ligand; (f) contacting the modified ligand with the NR polypeptide; (g) identifying in a biological assay for NR activity a degree to which the modified ligand modulates the biological activity of the NR polypeptide; and (h) comparing the biological activity of the NR polypeptide in the presence of modified ligand with the biological activity of the NR polypeptide in the presence of the unmodified ligand, whereby a modulator of a NR polypeptide is designed. In this embodiment, it is preferable that the NR comprises a LXR and more preferably a LXRβ comprising the sequence of SEQ ID NO: 4. It is also preferable that the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and that the coactivator polypeptide comprises a SRC1 polypeptide comprising the sequence of SEQ ID NO: 9. It is additionally preferable that the the method further comprises repeating steps (a) through (f), if the biological activity of the NR polypeptide in the presence of the modified ligand varies from the biological activity of the NR polypeptide in the presence of the unmodified ligand.

[0025] Further, a method of identifying a LXR modulator that selectively modulates the biological activity of one LXR subtype compared to LXRβ is disclosed. In a preferred embodiment, the method comprises: (a) providing an atomic structure coordinate set describing a LXRβ ligand binding domain structure in complex with one or more of a ligand and a coactivator polypeptide and at least one other atomic structure coordinate set describing a LXR ligand binding domain, each ligand binding domain comprising a ligand binding site; (b) comparing the LXR atomic structure coordinate sets to identify at least one difference between the sets; (c) designing a candidate ligand predicted to interact with the difference of step (b); (d) synthesizing the candidate ligand; and (e) testing the synthesized candidate ligand for an ability to selectively modulate a LXR subtype as compared to LXRβ, whereby a LXR modulator that selectively modulates the biological activity of one LXR subtype compared to LXRβ is identified. In this embodiment, it is preferable that the LXR subtype whose biological activity is to be modulated is LXRβ and comprises the sequence of SEQ ID NO: 4. It is also preferable that the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and that the coactivator polypeptide comprises a SRC1 polypeptide comprising the sequence of SEQ ID NO: 9.

[0026] In another embodiment, a method of modeling a three-dimensional structure of a target NR in complex with one or more of a ligand and a coactivator polypeptide from a template comprising the X-ray structure of a LXR in complex with one or more of a ligand and a coactivator polypeptide is disclosed. In a preferred embodiment, the method comprises: (a) selecting an X-ray structure of a target NR LBD as a starting model for the target NR LBD; (b) manipulating the starting model for the target NR as a rigid body to superimpose its backbone atoms onto corresponding backbone atoms of a three-dimensional template structure comprising a LXR in complex with one or more of a ligand and a coactivator polypeptide to form a manipulated model; (c) making a copy of the coactivator peptide from the template structure to form a model of a coactivator polypeptide bound to a template LXR; (d) merging the model of the coactivator polypeptide into the manipulated model to form a modified model; (e) removing one or more amino acids from the modified model; and (f) optimizing side-chain conformations, whereby a three-dimensional structure of a target NR in complex with one or more of a ligand and a coactivator polypeptide is modeled from a template comprising the X-ray structure of an NR in complex with one or more of a ligand and a coactivator polypeptide. In this embodiment, it is preferable that the LXR template is LXRβ and comprises the sequence of SEQ ID NO: 4. It is also preferable that the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and that the coactivator polypeptide comprises a SRC1 polypeptide comprising the sequence of SEQ ID NO: 9.

[0027] Accordingly, it is an object of the present invention to provide a three dimensional structure of the ligand binding domain of an LXR in complex with one or more of a ligand and a coactivator polypeptide. The object is achieved in whole or in part by the present invention.

[0028] An object of the invention having been stated hereinabove, other objects will be evident as the description proceeds, when taken in connection with the accompanying Drawings and Laboratory Examples as best described hereinbelow.

BRIEF DESCRIPTION OF THE DRAWINGS

[0029] FIG. 1 is a ribbon diagram depicting the LXRβ/EPC/SRC1 dimer that formed during crystallization. LXR is gray, SRC1 is black, and EPC is light gray. The LXR dimer formed is the same in both compound complexes.

[0030] FIG. 2 is a ribbon diagram depicting an EPC molecule situated in the LXRβ binding pocket. EPC is a light gray ball and stick figure with darker oxygen atoms.

[0031] FIG. 3 is a diagram depicting residues that interact with EPC in the LXRβ binding pocket; EPC is drawn as a ball and stick figure with gray carbons and black oxygens and LXRβ is depicted as a wire frame model.

[0032] FIG. 4A is a ribbon diagram depicting the superimposition of Cα atoms of each member of the crystallized LXRβ dimer, as well as the superimposition of the ligand N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide, one molecule of which was associated with each of the LXRβ monomers. The A molecule is indicated with light ribbon, while the B molecule is indicated with darker ribbon.

[0033] FIG. 4B is a ribbon diagram depicting the position of the ligand N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide (T317) relative to helices 5, 7 and 11 of LXRβ. In this figure the superimposition of Cα atoms of each member of the crystallized LXRβ dimer, as well as a detailed view of the superimposition of the ligand, one molecule of which was associated with each of the LXRβ monomers is represented. The A molecules of both LXRβ and T317 are light colored, while the B molecules are darker.

[0034] FIG. 5 is a diagram depicting the superimposition of each LXR of the dimer (wire frame model) and the superimposition of the N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide (T317) molecule associated with each of the LXRs (ball and stick). The A molecules of LXRβ and T317 are light colored, while the B molecules are darker.

[0035] FIG. 6A is a ribbon diagram of the binding pocket of LXR demonstrating how the structure was used to identify amino acids specifically contacting EPC to design mutants. In this figure the EPC A ring extends beyond T317 and O3 and reaches into a polar pocket containing E281, E315, and R319.

[0036] FIG. 6B is a ribbon diagram of the binding pocket of LXR demonstrating how the structure was used to identify amino acids specifically contacting T317 to design mutants. In this figure the ligand T317 is shown to form a hydrogen bond with H435 and extends into a hydrophobic pocket along the beta turn containing 1327, F329, and Y335.

[0037] FIG. 7A is a bar graph depicting the effect of mutating LXR LBD pocket residues on transcriptional activity, which was determined by measuring the amount of SPAP synthesized in CV-1 cells by a transiently transfected Gal4 fusion of LXRα LBD.

[0038] FIG. 7B is a bar graph depicting the effect of mutating LXR LBD pocket residues on transcriptional activity, which was determined by measuring the amount of SPAP synthesized in CV-1 cells by a transiently transfected Gal4 fusion of LXRβ LBD.

BRIEF DESCRIPTION OF THE SEQUENCES IN THE SEQUENCE LISTING

[0039] SEQ ID NO: 1 is a DNA sequence encoding a full-length human LXRα polypeptide (Swiss-Prot Accession No. Q13133; GenBank Accession No. U22662).

[0040] SEQ ID NO: 2 is an amino acid sequence comprising a full-length human LXRα (Swiss-Prot Accession No. Q13133; GenBank Accession No. U22662).

[0041] SEQ ID NO: 3 is a DNA sequence encoding a full-length human LXRβ polypeptide (Swiss-Prot Accession No. P55055; GenBank Accession No. NM—007121).

[0042] SEQ ID NO: 4 is an amino acid sequence comprising a full-length human LXRβ (Swiss-Prot Accession No. P55055; GenBank Accession No. NM—007121).

[0043] SEQ ID NO: 5 is a DNA sequence encoding a human LXRα ligand binding domain polypeptide (Swiss-Prot Accession No. Q13133; GenBank Accession No. U22662).

[0044] SEQ ID NO: 6 is an amino acid sequence comprising a human LXRα ligand binding domain polypeptide (Swiss-Prot Accession No. Q13133; GenBank Accession No. U22662).

[0045] SEQ ID NO: 7 is a DNA sequence encoding a human LXRβ ligand binding domain polypeptide.

[0046] SEQ ID NO: 8 is an amino acid sequence comprising a human LXRβ ligand binding domain polypeptide.

[0047] SEQ ID NO: 9 is an amino acid sequence that comprises a fragment of the co-activator SRC1.

[0048] SEQ ID NO: 10 is an amino acid sequence of residues 182-419 of an RAR polypeptide that was employed in the molecular replacement solution of LXRβ.

DETAILED DESCRIPTION OF THE INVENTION

[0049] Until disclosure of the present invention presented herein, the ability to obtain crystalline forms of a LXRβ LBD has not been realized. And until disclosure of the present invention presented herein, a detailed three-dimensional crystal structure of a LXRβ polypeptide has not been solved.

[0050] In addition to providing structural information, crystalline polypeptides provide other advantages. For example, the crystallization process itself further purifies the polypeptide, and satisfies one of the classical criteria for homogeneity. In fact, crystallization frequently provides unparalleled purification quality, removing impurities that are not removed by other purification methods such as HPLC, dialysis, conventional column chromatography, etc. Moreover, crystalline polypeptides are often stable at ambient temperatures and free of protease contamination and other degradation associated with solution storage. Crystalline polypeptides can also be useful as pharmaceutical preparations. Finally, crystallization techniques in general are largely free of problems such as denaturation associated with other stabilization methods (e.g., lyophilization). Once crystallization has been accomplished, crystallographic data provides useful structural information that can assist the design of compounds that can serve as agonists or antagonists, as described herein below. In addition, the crystal structure provides information useful to map a receptor-binding domain, which could then be mimicked by a small non-peptide molecule that would serve as an antagonist or agonist.

[0051] I. Definitions

[0052] Following long-standing patent law convention, the terms “a” and “an” mean “one or more” when used in this application, including the claims.

[0053] As used herein, the term “mutation” carries its traditional connotation and means a change, inherited, naturally occurring or introduced, in a nucleic acid or polypeptide sequence, and is used in its sense as generally known to those of skill in the art.

[0054] As used herein, the term “labeled” means the attachment of a moiety, capable of detection by spectroscopic, radiologic or other methods, to a probe molecule.

[0055] As used herein, the term “target cell” refers to a cell, into which it is desired to insert a nucleic acid sequence or polypeptide, or to otherwise effect a modification from conditions known to be standard in the unmodified cell. A nucleic acid sequence introduced into a target cell can be of variable length. Additionally, a nucleic acid sequence can enter a target cell as a component of a plasmid or other vector or as a naked sequence.

[0056] As used herein, the term “transcription” means a cellular process involving the interaction of an RNA polymerase with a gene that directs the expression as RNA of the structural information present in the coding sequences of the gene. The process includes, but is not limited to the following steps: (a) the transcription initiation, (b) transcript elongation, (c) transcript splicing, (d) transcript capping, (e) transcript termination, (f) transcript polyadenylation, (g) nuclear export of the transcript, (h) transcript editing, and (i) stabilizing the transcript.

[0057] As used herein, the term “expression” generally refers to the cellular processes by which a polypeptide is produced from RNA.

[0058] As used herein, the term “transcription factor” means a cytoplasmic or nuclear protein which binds to a gene, or binds to an RNA transcript of a gene, or binds to another protein which binds to a gene or an RNA transcript or another protein which in turn binds to a gene or an RNA transcript, so as to thereby modulate expression of the gene. Such modulation can additionally be achieved by other mechanisms; the essence of a “transcription factor for a gene” pertains to a factor that alters the level of transcription of the gene in some way.

[0059] As used herein, the term “hybridization” means the binding of a probe molecule, a molecule to which a detectable moiety has been bound, to a target sample.

[0060] As used herein, the term “detecting” means confirming the presence of a target entity by observing the occurrence of a detectable signal, such as a radiologic or spectroscopic signal that will appear exclusively in the presence of the target entity.

[0061] As used herein, the term “sequencing” means determining the ordered linear sequence of nucleic acids or amino acids of a DNA or protein target sample, using conventional manual or automated laboratory techniques.

[0062] As used herein, the term “isolated” means oligonucleotides substantially free of other nucleic acids, proteins, lipids, carbohydrates or other materials with which they can be associated, such association being either in cellular material or in a synthesis medium. The term can also be applied to polypeptides, in which case the polypeptide will be substantially free of nucleic acids, carbohydrates, lipids and other undesired polypeptides.

[0063] As used herein, the term “substantially pure” means that the polynucleotide or polypeptide is substantially free of the sequences and molecules with which it is associated in its natural state, and those molecules used in the isolation procedure. The term “substantially free” means that the sample is at least 50%, preferably at least 70%, more preferably 80% and most preferably 90% free of the materials and compounds with which is it associated in nature.

[0064] As used herein, the term “primer” means a sequence comprising two or more deoxyribonucleotides or ribonucleotides, preferably more than three, and more preferably more than eight and most preferably at least about 20 nucleotides of an exonic or intronic region. Such oligonucleotides are preferably between ten and thirty bases in length.

[0065] As used herein, the term “DNA segment” means a DNA molecule that has been isolated free of total genomic DNA of a particular species. In a preferred embodiment, a DNA segment encoding a LXR polypeptide refers to a DNA segment that comprises SEQ ID NOs: 1, 3, 5, and 7, but can optionally comprise fewer or additional nucleic acids, yet is isolated away from, or purified free from, total genomic DNA of a source species, such as Homo sapiens. Included within the term “DNA segment” are DNA segments and smaller fragments of such segments, and also recombinant vectors, including, for example, plasmids, cosmids, phages, viruses, and the like.

[0066] As used herein, the phrase “enhancer-promoter” means a composite unit that contains both enhancer and promoter elements. An enhancer-promoter is operatively linked to a coding sequence that encodes at least one gene product.

[0067] As used herein, the phrase “operatively linked” means that an enhancer-promoter is connected to a coding sequence in such a way that the transcription of that coding sequence is controlled and regulated by that enhancer-promoter. Techniques for operatively linking an enhancer-promoter to a coding sequence are well known in the art; the precise orientation and location relative to a coding sequence of interest is dependent, inter alia, upon the specific nature of the enhancer-promoter.

[0068] As used herein, the terms “candidate substance” and “candidate compound” are used interchangeably and refer to a substance that is believed to interact with another moiety, for example a given ligand that is believed to interact with a complete, or a fragment of, a LXR polypeptide, and which can be subsequently evaluated for such an interaction. Representative candidate substances or compounds include “xenobiotics”, such as drugs and other therapeutic agents, carcinogens and environmental pollutants, natural products and extracts, as well as “endobiotics”, such as steroids, fatty acids and prostaglandins. Other examples of candidate compounds that can be investigated using the methods of the present invention include, but are not restricted to, agonists and antagonists of a LXR polypeptide, toxins and venoms, viral epitopes, hormones (e.g., opioid peptides, steroids, etc.), hormone receptors, peptides, enzymes, enzyme substrates, co-factors, lectins, sugars, oligonucleotides or nucleic acids, oligosaccharides, proteins, small molecules and monoclonal antibodies.

[0069] As used herein, the term “biological activity” means any observable effect flowing from interaction between a LXR polypeptide and a ligand. Representative, but non-limiting, examples of biological activity in the context of the present invention include dimerization of a LXR polypeptide and association of a LXR with a ligand, such as 24(S), 25-epoxycholesterol.

[0070] As used herein, the term “modified” means an alteration from an entity's normally occurring state. An entity can be modified by removing discrete chemical units or by adding discrete chemical units. The term “modified” encompasses detectable labels as well as those entities added as aids in purification.

[0071] As used herein, the terms “structure coordinates” and “structural coordinates” mean mathematical coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a molecule in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are used to establish the positions of the individual atoms within the unit cell of the crystal.

[0072] Those of skill in the art understand that a set of structure coordinates determined by X-ray crystallography is not without standard error. For the purpose of this invention, any set of structure coordinates for LXR or a LXR mutant that have a root mean square deviation (RMSD) from ideal of preferably no more than 1.5 Å, more preferably no more than 1.0 Å, and most preferably no more than 0.5 Å when superimposed, using the polypeptide backbone atoms, on the structure coordinates listed in Tables 2, and 3 shall be considered identical.

[0073] As used herein, the term “space group” means the arrangement of symmetry elements of a crystal.

[0074] As used herein, the term “molecular replacement” means a method that involves generating a preliminary model of the wild-type LXR ligand binding domain, or a LXR mutant crystal whose structure coordinates are unknown, by orienting and positioning a molecule whose structure coordinates are known within the unit cell of the unknown crystal so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This, in turn, can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown crystal. See, e.g., Lattman, (1985) Method Enzymol. 115: 55-77; Rossmann (ed.), (1972) The Molecular Replacement Method, Gordon & Breach, New York. Using the structure coordinates of a LXR ligand binding domain provided by the present invention, molecular replacement can be used to determine the structure coordinates of a crystalline mutant or homologue of a LXR ligand binding domain, or of a different crystal form of the LXR ligand binding domain.

[0075] As used herein, the term “isomorphous replacement” means a method of using heavy atom derivative crystals to obtain the phase information necessary to elucidate the three-dimensional structure of a native crystal (Blundell et al., (1976) Protein Crystallography, Academic Press; Otwinowski, (1991) in Isomorphous Replacement and Anomalous Scattering, (Evans & Leslie, eds.), 80-86, Daresbury Laboratory, Daresbury, United Kingdom). The phrase “heavy-atom derivatization” is synonymous with the term “isomorphous replacement.”

[0076] As used herein, the terms “β-sheet” and “beta-sheet” mean the conformation of a polypeptide chain stretched into an extended zig-zig conformation. Portions of polypeptide chains that run “parallel” all run in the same direction. Polypeptide chains that are “antiparallel” run in the opposite direction from the parallel chains.

[0077] As used herein, the terms “α-helix” and “alpha-helix” mean the conformation of a polypeptide chain wherein the polypeptide backbone is wound around the long axis of the molecule in a left-handed or right-handed direction, and the R groups of the amino acids protrude outward from the helical backbone, wherein the repeating unit of the structure is a single turnoff the helix, which extends about 0.56 nm along the long axis.

[0078] As used herein, the term “unit cell” means a basic parallelepiped shaped block. The entire volume of a crystal can be constructed by regular assembly of such blocks. Each unit cell comprises a complete representation of the unit of pattern, the repetition of which builds up the crystal. Thus, the term “unit cell” means the fundamental portion of a crystal structure that is repeated infinitely by translation in three dimensions. A unit cell is characterized by three vectors a, b, and c, not located in one plane, which form the edges of a parallelepiped. Angles α, β and γ define the angles between the vectors: angle α is the angle between vectors b and c; angle β is the angle between vectors a and c; and angle γ is the angle between vectors a and b. The entire volume of a crystal can be constructed by regular assembly of unit cells; each unit cell comprises a complete representation of the unit of pattern, the repetition of which builds up the crystal.

[0079] As used herein, the term “orthogonal unit cell” means a unit cell wherein a≠b≠c; and α=β=γ=90°. The vectors a, b and c describe the unit cell edges and the angles α, β, and γ describe the unit cell angles.

[0080] As used herein, the term “crystal lattice” means the array of points defined by the vertices of packed unit cells.

[0081] As used herein, the term “ligand binding site” and “ligand binding domain” are used interchangeably and mean that site in a polypeptide where substrate binding occurs. For human LXRβ, the ligand binding domain comprises the residues 214-462 of the full-length human LXRβ protein.

[0082] As used herein, the term “LXR” means nucleic acids encoding a liver X receptor (LXR) nuclear receptor polypeptide that can bind DNA and/or one or more ligands, and/or has the ability to form multimers. The term “LXR” includes invertebrate homologs; however, preferably, LXR nucleic acids and polypeptides are isolated from vertebrate sources. “LXR” further includes vertebrate homologs of LXR family members, including, but not limited to, mammalian and avian homologs. Representative mammalian homologs of LXR family members include, but are not limited to, murine and human homologs.

[0083] As used herein, the terms “LXR gene product”, “LXR protein”, “LXR polypeptide”, and “LXR peptide” are used interchangeably and mean peptides having amino acid sequences which are substantially identical to native amino acid sequences from an organism of interest and which are biologically active in that they comprise all or a part of the amino acid sequence of a LXR polypeptide, or cross-react with antibodies raised against a LXR polypeptide, or retain all or some of the biological activity (e.g., DNA or ligand binding ability and/or dimerization ability) of the native amino acid sequence or protein. Such biological activity can include immunogenicity.

[0084] As used herein, the terms “LXR gene product”, “LXR protein”, “LXR polypeptide”, and “LXR peptide” also include analogs of a LXR polypeptide. By “analog” is intended that a DNA or peptide sequence can contain alterations relative to the sequences disclosed herein, yet retain all or some of the biological activity of those sequences. Analogs can be derived from genomic nucleotide sequences as are disclosed herein or from other organisms, or can be created synthetically. Those skilled in the art will appreciate that other analogs, as yet undisclosed or undiscovered, can be used to design and/or construct LXR analogs. There is no need for a “LXR gene product”, “LXR protein”, “LXR polypeptide”, or “LXR peptide” to comprise all or substantially all of the amino acid sequence of a LXR polypeptide gene product. Shorter or longer sequences are anticipated to be of use in the invention; shorter sequences are herein referred to as “segments”. Thus, the terms “LXR gene product”, “LXR protein”, “LXR polypeptide”, and “LXR peptide” also include fusion, chimeric or recombinant LXR polypeptides and proteins comprising sequences of the present invention. Methods of preparing such proteins are disclosed herein and are known in the art.

[0085] As used herein, the term “polypeptide” means any polymer comprising any of the 20 protein amino acids, regardless of its size. Although “protein” is often used in reference to relatively large polypeptides, and “peptide” is often used in reference to small polypeptides, usage of these terms in the art overlaps and varies. The term “polypeptide” as used herein refers to peptides, polypeptides and proteins, unless otherwise noted. As used herein, the terms “protein”, “polypeptide” and “peptide” are used interchangeably herein when referring to a gene product.

[0086] As used herein, the term “modulate” means an increase, decrease, or other alteration of any, or all, chemical and biological activities or properties of a wild-type or mutant LXR polypeptide. The term “modulation” as used herein refers to both upregulation (i.e., activation or stimulation) and downregulation (i.e. inhibition or suppression) of a response.

[0087] As used herein, the terms “LXR gene” and “recombinant LXR gene” mean a nucleic acid molecule comprising an open reading frame encoding a LXR polypeptide of the present invention, including both exon and (optionally) intron sequences.

[0088] As used herein, the term “gene” is used for simplicity to refer to a functional protein, polypeptide or peptide encoding unit. As will be understood by those in the art, this functional term includes both genomic sequences and cDNA sequences. Preferred embodiments of genomic and cDNA sequences are disclosed herein.

[0089] As used herein, the term “DNA sequence encoding a LXR polypeptide” can refer to one or more coding sequences within a particular individual. Moreover, certain differences in nucleotide sequences can exist between individual organisms, which are called alleles. It is possible that such allelic differences might or might not result in differences in amino acid sequence of the encoded polypeptide yet still encode a protein with the same biological activity. As is well known, genes for a particular polypeptide can exist in single or multiple copies within the genome of an individual. Such duplicate genes can be identical or can have certain modifications, including nucleotide substitutions, additions or deletions, all of which still code for polypeptides having substantially the same activity.

[0090] As used herein, the term “intron” means a DNA sequence present in a given gene that is not translated into protein.

[0091] As used herein, the term “interact” means detectable interactions between molecules, such as can be detected using, for example, a yeast two hybrid assay. The term “interact” is also meant to include “binding” interactions between molecules. Interactions can, for example, be protein-protein or protein-nucleic acid in nature.

[0092] As used herein, the terms “cells,” “host cells” or “recombinant host cells” are used interchangeably and mean not only to the particular subject cell, but also to the progeny or potential progeny of such a cell. Because certain modifications can occur in succeeding generations due to either mutation or environmental influences, such progeny might not, in fact, be identical to the parent cell, but are still included within the scope of the term as used herein.

[0093] As used herein, the term “agonist” means an agent that supplements or potentiates the bioactivity of a functional LXR gene or protein, of a polypeptide encoded by a gene that is up- or down-regulated by a LXR polypeptide, and/or a polypeptide encoded by a gene that contains a LXR binding site in its promoter region.

[0094] As used herein, the term “antagonist” means an agent that decreases or inhibits the bioactivity of a functional LXR gene or protein, or that supplements or potentiates the bioactivity of a naturally occurring or engineered non-functional LXR gene or protein. Alternatively, an antagonist can decrease or inhibit the bioactivity of a functional gene or polypeptide encoded by a gene that is up- or down-regulated by a LXR polypeptide and/or contains a LXR binding site in its promoter region. An antagonist can also supplement or potentiate the bioactivity of a naturally occurring or engineered non-functional gene or polypeptide encoded by a gene that is up- or down-regulated by a LXR polypeptide, and/or contains a LXR binding site in its promoter region.

[0095] As used herein, the terms “chimeric protein” or “fusion protein” are used interchangeably and mean a fusion of a first amino acid sequence encoding a LXR polypeptide with a second amino acid sequence defining a polypeptide domain foreign to, and not homologous with, any domain of one of a LXR polypeptide. A chimeric protein can present a foreign domain that is found in an organism that also expresses the first protein, or it can be an “interspecies” or “intergenic” fusion of protein structures expressed by different kinds of organisms. In general, a fusion protein can be represented by the general formula X—LXR—Y, wherein LXR represents a portion of the protein which is derived from a LXR polypeptide, and X and Y are independently absent or represent amino acid sequences which are not related to a LXR sequence in an organism, which includes naturally occurring mutants. The term “chimeric gene” refers to a nucleic acid construct that encodes a “chimeric protein” or “fusion protein” as defined herein.

[0096] As used herein, the term “therapeutic agent” is a chemical entity intended to effectuate a change in an organism. Preferably, but not necessarily, the organism is a human being. It is not necessary that a therapeutic agent be known to effectuate a change in an organism; chemical entities that are suspected, predicted or designed to effectuate a change in an organism are therefore encompassed by the term “therapeutic agent.” The effectuated change can be of any kind, observable or unobservable, and can include, for example, a change in the biological activity of a protein.

[0097] Representative therapeutic compounds include small molecules, proteins and peptides, oligonucleotides of any length, “xenobiotics”, such as drugs and other therapeutic agents, carcinogens and environmental pollutants, natural products and extracts, as well as “endobiotics”, such as epoxycholesterols. Other examples of therapeutic agents can include, but are not restricted to, agonists and antagonists of a LXR polypeptide, toxins and venoms, viral epitopes, hormones (e.g., opioid peptides, steroids, etc.), hormone receptors, peptides, enzymes, enzyme substrates, co-factors, lectins, sugars, oligonucleotides or nucleic acids, oligosaccharides, proteins, small molecules and monoclonal antibodies.

[0098] II. Description of Tables

[0099] Table 1 is a table summarizing the crystal and data statistics obtained from the crystallized ligand binding domain of human LXR. Data on the unit cell are presented, including data on the crystal space group, unit cell dimensions, molecules per asymmetric cell and crystal resolution.

[0100] Table 2 is a table presenting the atomic coordinate data for crystallized LXRβ LBD in complex with EPC and a SRC1 peptide.

[0101] Table 3 is a table presenting the atomic coordinate data for crystallized LXRβ LBD in complex with N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide.

[0102] Table 4 is a table presenting the atomic coordinate data for human RARγ employed in the molecular replacement solution of human LXRβ ligand binding domain crystals.

[0103] III. General Considerations

[0104] The present invention will usually be applicable mutatis mutandis to all LXR polypeptides, as discussed herein, based, in part, on the patterns of LXR structure and modulation that have emerged as a consequence of determining a preferred three dimensional structure, human LXR in complex with a ligand. Generally speaking, LXR homologs and orthologs display substantial regions of amino acid homology. Additionally, the LXRs display an overall structural motif comprising three modular domains:

[0105] 1) a variable amino-terminal domain;

[0106] 2) a highly conserved DNA-binding domain (DBD); and

[0107] 3) a less conserved carboxy-terminal ligand binding domain (LBD).

[0108] The modularity of LXR permits different domains of each protein to separately accomplish different functions, although the domains can influence each other. The separate function of a domain is usually preserved when a particular domain is isolated from the remainder of the protein. Using conventional protein chemistry techniques, a modular domain can sometimes be separated from the parent protein. Using conventional molecular biology techniques, each domain can usually be separately expressed with its original function intact or, as discussed herein below, chimeric proteins comprising two different proteins can be constructed, wherein the chimeric proteins retain the properties of the individual functional domains of the respective polypeptides from which the chimeric proteins were generated.

[0109] The amino terminal domain of LXR is the least conserved of the three domains. This domain is involved in transcriptional activation and, in some cases, its uniqueness can dictate selective receptor-DNA binding and activation of target genes by LXR.

[0110] The DBD is the most conserved structure in LXR. It typically contains about 70 amino acids that fold into two zinc finger motifs, wherein a zinc ion coordinates four cysteines. The DBD generally contains two perpendicularly oriented α-helices that extend from the base of the first and second zinc fingers. The two zinc fingers function in concert along with non-zinc finger residues to direct the LXRs to specific target sites on DNA. Various amino acids in the DBD influence spacing between two half-sites (which usually comprises six nucleotides) for receptor homodimerization. The optimal spacings facilitate cooperative interactions between DBDs, and D box residues are part of the dimerization interface. Other regions of the DBD facilitate DNA-protein and protein-protein interactions required for LXR homodimerization.

[0111] The LBD is the second most highly conserved domain in these receptors. Whereas the integrity of several different LBD sub-domains is important for ligand binding, truncated molecules containing only the LBD can retain normal ligand binding activity. This domain also participates in other functions, including dimerization, nuclear translocation and transcriptional regulation activities. Importantly, this domain can bind a ligand and can undergo ligand-induced conformational changes. Ligand binding allows the activation domain to serve as an interaction site for essential co-activator proteins that function to stimulate or inhibit transcription.

[0112] The carboxy-terminal activation subdomain is in close three-dimensional proximity in the LBD to the ligand, so as to allow for ligands bound to the LBD to coordinate (or interact) with amino acid(s) in the activation subdomain. As disclosed herein, the LBD of LXR is expressed, crystallized and its three dimensional structure determined. Computational and other methods for the design of ligands to the LBD are also disclosed.

[0113] IV. Production of LXR Polypeptides

[0114] The native and mutated LXR polypeptides, and fragments thereof, of the present invention can be chemically synthesized in whole or part using techniques that are well-known in the art (See, e.g., Creighton, (1983) Proteins: Structures and Molecular Principles, W. H. Freeman & Co., New York, incorporated herein in its entirety). Alternatively, methods that are well known to those skilled in the art can be used to construct expression vectors containing a partial or the entire native or mutated LXR polypeptide coding sequence and appropriate transcriptional/translational control signals. These methods include in vitro recombinant DNA techniques, synthetic techniques and in vivo recombination/genetic recombination. See, for example, the techniques described in Sambrook et al., (1989) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, New York, and Ausubel et al., (1989) Current Protocols in Molecular Biology, Greene Publishing Associates and Wiley Interscience, New York, both incorporated herein in their entirety.

[0115] A variety of host-expression vector systems can be utilized to express a LXR coding sequence. These include but are not limited to microorganisms such as bacteria transformed with recombinant bacteriophage DNA, plasmid DNA or cosmid DNA expression vectors containing a LXR coding sequence; yeast transformed with recombinant yeast expression vectors containing a LXR coding sequence; insect cell systems infected with recombinant virus expression vectors (e.g., baculovirus) containing a LXR coding sequence; plant cell systems infected with recombinant virus expression vectors (e.g., cauliflower mosaic virus, CaMV; tobacco mosaic virus, TMV) or transformed with recombinant plasmid expression vectors (e.g., Ti plasmid) containing a LXR coding sequence; or animal cell systems. The expression elements of these systems vary in their strength and specificities.

[0116] Depending on the host/vector system utilized, any of a number of suitable transcription and translation elements, including constitutive and inducible promoters, can be used in the expression vector. For example, when cloning in bacterial systems, inducible promoters such as pL of bacteriophage λ, plac, ptrp, ptac (ptrp-lac hybrid promoter) and the like can be used. When cloning in insect cell systems, promoters such as the baculovirus polyhedrin promoter can be used. When cloning in plant cell systems, promoters derived from the genome of plant cells, such as heat shock promoters; the promoter for the small subunit of RUBISCO; the promoter for the chlorophyll a/b binding protein) or from plant viruses (e.g., the 35S RNA promoter of CaMV; the coat protein promoter of TMV) can be used. When cloning in mammalian cell systems, promoters derived from the genome of mammalian cells (e.g., metallothionein promoter) or from mammalian viruses (e.g., the adenovirus late promoter; the vaccinia virus 7.5K promoter) can be employed. When generating cell lines that contain multiple copies of the tyrosine kinase domain DNA, SV40-, BPV- and EBV-based vectors can be used with an appropriate selectable marker.

[0117] V. Formation of LXR Ligand Binding Domain Crystals

[0118] In one embodiment, the present invention provides crystals of LXR. The crystals were obtained using the methodology disclosed in the Laboratory Examples. The LXR crystals, which can be native crystals, derivative crystals or co-crystals, have orthorhombic unit cells (an orthorhombic unit cell is a unit cell wherein a≠b≠c, and wherein α=β=γ90°) and space group symmetry of P212121 in one embodiment and C2221 in another embodiment. There are two LXR molecules in the asymmetric unit related by a non-crystallographic dyad. In one LXR crystalline form, the unit cell has dimensions of a=60.25 Å, b=82.454 Å, c=123.175 Å, and α=β=γ=90°. In another LXR crystalline form, the unit cell has dimensions of a=71.166 A, b=120.012 Å, c=147.56 Å, and α=β=γ=90°.

[0119] The structure of the N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide-bound form of LXR was solved by molecular replacement using the structure of the human retinoic acid receptor γ (RARγ) as a search model (Table 4) (Renaud et al., (1995) Nature 378: 681-689; PDB ID No; 2LBD, coordinates available online at http://www.rcsb.org/pd b/). The N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl ]-benzenesulfonamide-bound form was refined to a resolution of about 2.3 Å. The structure of the EPC-bound form of LXR was solved by molecular replacement using the refined LXR subunit from the N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide-bound form as a search model. The EPC-bound form was refined to a resolution of about 2.8 Å.

[0120] The heavy atom derivatized form of the LXR LBD-ligand structure can be solved using single isomorphous replacement anomalous scattering (SIRAS) techniques and/or multiwavelength anomalous diffraction (MAD) techniques. In the SIRAS method of solving protein crystals, a derivative crystal is prepared that contains an atom that is heavier than the other atoms of the sample. Heavy atom derivative crystals are commonly prepared by soaking a crystal in a solution containing a selected heavy atom salt. For example, some heavy atom derivative crystals have been prepared by soaking a crystalline form of the protein of interest in a solution of methyl mercury chloride (MeHgCl). Another representative heavy atom that can be incorporated into a derivative crystal is iodine. Heavy atoms can associate with the protein of interest, or can be localized in a ligand that associates with a protein of interest.

[0121] Analysis of derivative crystals takes advantage of differences in the reflections from the derivative crystal as compared to the underivatized crystal. Symmetry-related reflections in the X-ray diffraction pattern, which are usually identical, are altered by the anomalous scattering contribution of the heavy atoms. The measured differences in symmetry-related reflections are used to determine the position of the heavy atoms, leading to an initial estimation of the diffraction phases, and subsequently, an electron density map is prepared. The prepared electron density map is then used to identify the position of the other atoms in the sample.

[0122] V.A. Preparation of LXR Crystals

[0123] The native and derivative co-crystals, and fragments thereof, disclosed in the present invention can be obtained by a variety of techniques, including batch, liquid bridge, dialysis, vapor diffusion and hanging drop methods (See, e.g., McPherson, (1982) Preparation and Analysis of Protein Crystals, John Wiley, New York; McPherson, (1990) Eur. J. Biochem. 189:1-23; Weber, (1991) Adv. Protein Chem. 41:1-36). In a preferred embodiment, the vapor diffusion and hanging drop methods are used for the crystallization of LXR polypeptides and fragments thereof.

[0124] In general, native crystals of the present invention are grown by dissolving substantially pure LXR LBD polypeptide or a fragment thereof in an aqueous buffer containing a precipitant at a concentration just below that necessary to precipitate the protein. Water is removed by controlled evaporation to produce precipitating conditions, which are maintained until crystal growth ceases.

[0125] In a preferred embodiment of the invention, native crystals are grown by the hanging drop method (See, e.g., McPherson, (1982) Preparation and Analysis of Protein Crystals, John Wiley, New York; McPherson, (1990) Eur. J. Biochem. 189:1-23). In this method, the polypeptide/precipitant solution is allowed to equilibrate in a closed container with a larger aqueous reservoir having a precipitant concentration optimal for producing crystals. Generally, less than about 25 μL of LXR LBD polypeptide solution is mixed with an equal volume of reservoir solution, giving a precipitant concentration about half that required for crystallization. This solution is suspended as a droplet underneath a coverslip, which is sealed onto the top of the reservoir. The sealed container is allowed to stand, until crystals grow. Crystals generally form within two to six weeks, and are suitable for data collection within approximately seven to ten weeks. Of course, those of skill in the art will recognize that the above-described crystallization procedures and conditions can be varied.

[0126] V.B. Preparation of Derivative Crystals

[0127] Derivative crystals of the present invention, e.g. heavy atom derivative crystals, can be obtained by soaking native crystals in mother liquor containing salts of heavy metal atoms. Alternatively, a ligand comprising a heavy atom can be associated with a protein, and subsequently co-crystallized. Such derivative crystals are useful for phase analysis in the solution of crystals of the present invention. This mechanism provides derivative crystals suitable for use as isomorphous replacements in determining the X-ray crystal structure of a LXR polypeptide. Additional reagents useful for the preparation of the derivative crystals of the present invention will be apparent to those of skill in the art after review of the disclosure of the present invention presented herein.

[0128] V.C. Preparation of Co-Crystals

[0129] Co-crystals of the present invention can be obtained by soaking a native crystal in mother liquor containing compounds known or predicted to bind the LBD of a LXR, or a fragment thereof. Alternatively, co-crystals can be obtained by co-crystallizing a LXR LBD polypeptide or a fragment thereof in the presence of one or more compounds known or predicted to bind the polypeptide. In a preferred embodiment of the present invention, for example, the ligand N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide is co-crystallized with LXR. In another embodiment, an epoxycholesterol is co-crystallyzed with LXR and a peptide derived from a steroid receptor coactivator (SRC).

[0130] V.D. Solving a Crystal Structure of the Present Invention

[0131] Crystal structures of the present invention can be solved using a variety of techniques including, but not limited to, isomorphous replacement anomalous scattering or molecular replacement methods. Computer software packages will also be helpful in solving a crystal structure of the present invention. Applicable software packages include but are not limited to AmoRe (Navaza & Saludjian, (1997) Method Enzymol. 276A: 581-94; AmoRe is available on the internet at various sites, such as ftp:/ftp.informatik.uni-kiel.de/pub/kiel/amore), X-PLOR™ program (Brünger, (1992) X-PLOR, Version 3.1. A System for X-ray Crystallography and NMR, Yale University Press, New Haven, Conn.; X-PLOR is available from Molecular Simulations, Inc., San Diego, Calif.), Xtal View (McRee, (1992) J. Mol. Graphics 10: 44-47; X-tal View is available from the San Diego Supercomputer Center), SHELXS 97 (Sheldrick (1990) Acta Cryst. A 46: 467; SHELX 97 is available from the Institute of Inorganic Chemistry, Georg-August-Universität, Göttingen, Germany), HEAVY (Terwilliger, Los Alamos National Laboratory) can be used and SHAKE-AND-BAKE (Hauptman, (1997) Curr. Opin. Struct. Biol. 7: 672-80; Weeks et al., (1993) Acta Cryst. D 49: 179; available from the Hauptman-Woodward Medical Research Institute, Buffalo, N.Y.). See also, Ducruix & Geige, (1992) Crystallization of Nucleic Acids and Proteins: A Practical Approach, IRL Press, Oxford, England, and references cited therein.

[0132] VI. Summary of Results for the LXR Ligand binding Domain

[0133] Three structures of the LBD of human LXR are disclosed in the present invention. First, a 2.3 Å stucture in complex with the ligand N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide is disclosed, second, a 2.8 Å structure in complex with an epoxycholesterol and a SRC pepide is disclosed.

[0134] The crystal structures of the present invention disclose important insights into how human LXR binds ligands and thus, can be useful in designing LXR ligands, including activators and inhibitors. These structures reveal that although LXR has a well defined hydrophobic pocket, the binding modes of different compounds can differ radically. A hydrogen bond with histidine 435 was found to be the only conserved polar interaction. Also, the structures revealed that filling the volume of the pocket was not necessary nor sufficient for activation of LXR.

[0135] VI.A. Overall Structure of the Human LXR Ligand Binding Domain

[0136] The LXRβ LBD had the same three-layered α-helical fold seen for other nuclear receptors (see FIG. 1). In all complex structures, the asymmetric unit contains a LXRβ homodimer, with the T317 complex and the EPC/SRC1(2) complex containing two holo molecules. Although the non-crystallographic molecules are identical sequentially, the marked structural differences observed are most likely due to crystal packing forces. The dimer interface is composed of residues in helices 7, 9, 10 and 11, as seen in other homo and heterodimer interfaces. Each homodimer comprises A and B subunits.

[0137] To understand the degree of flexibility in the LXRβ LBD, the deviation in Cα atoms in the LBD core region, comprising helices 3 to 11 was compared. The two most similar molecules were those binding EPC with the SRC peptide, having an average deviation of Cα atoms of 0.43 A RMSD. The two molecules binding the N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide compound, with an average deviation of Cα atoms of 0.6 A RMSD. Those molecules binding EPC differ from those binding the N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide compound by an average deviation of 0.65 A RMSD. In all cases, the Cα positional variance between structures increased proportionally with the distance of the residue from the homodimer interface.

[0138] The most distinguishing features of the canonical LXRβ structure are a large helix 1 (˜18 residues) and a relatively large pocket (833 Å3) compared with previously solved steroid receptors. This large binding pocket is consistent with the larger size of oxy-cholesterol derivatives compared to the sex steroids.

[0139] VI.B. The LXRβ/epoxycholesterol Complex

[0140] LXRβ with bound EPC crystallized as a dimer (see FIG. 1), with the same dimer interface seen with other nuclear receptors with EPC filling most of the pocket. The binding of EPC to LXRβ differs significantly from bound steroids observed in previously solved nuclear receptors (Brzozowski et al., (1997) Nature 389:753-758; Williams & Sigler, (1998) Nature 393:392-396; Matias et al., (2000) J. Biol. Chem. 275:26164-2617). Like other steroid receptors, EPC bound to LXRβ with the steroid A-ring oriented towards helices 3 and 4, and the D-ring and tail pointing towards helix 11 and the AF2. Although the steroid cores of progesterone, estradiol, and testosterone overlap almost perfectly when the corresponding nuclear receptor's Cα atoms are superimposed, the steroid core of EPC did not overlap that of the sex steroids when the Cα atoms of LXRβ were superimposed on those receptors. Additionally, the steroid core of EPC is flipped 180° around its long axis, so that the EPC angular methyls pointed in the opposite direction from those of other steroids, like progesterone (see FIG. 2).

[0141] The binding site for EPC was almost exclusively hydrophobic, with the only hydrophilic interaction at the end of the pocket near the A-ring ketone oxygen (O3) where LXR and the EPC O3 form a network of interactions. The O3 of EPC is positioned in a polar pocket containing Glu281, Glu315, and Arg319. The side chains of Phe 243 and Phe329 packed against the hydrophobic A ring of EPC, and pushed it against the Cp and Cy of Glu315. The steric interaction between EPC and Glu315 positioned the acid group to form a salt bridge with Arg319. This salt bridge gave Arg319 the proper orientation to form the hydrogen bond with O3 of EPC (2.6 Å). The orientation of the Glu315 acid head group was fixed by a hydrogen bond with Arg318 which was fixed to Arg319 by the peptide bond.

[0142] There is a steric interaction between the side chain of Trp457 and the EPC 24(S), 25 epoxide group. The epoxide oxygen is ˜3.2 Å from two carbons in the six-member ring of the Trp457 indole. The Trp457 indole is oriented such that the nitrogen atom is pointed away from EPC, making it impossible to form a direct hydrogen bond with the epoxide oxygen (Spencer et al., (2001) J. Med. Chem. 44: 886-897). However, the EPC epoxide oxygen is positioned to form a weak hydrogen bond with His435 (3.4 Å), explaining why a correctly positioned oxygen atom is required distal to EPC C22 to activate LXR. The interaction with the epoxide oxygen orients the His435 imidazole basic nitrogen away from the Trp457 indole, providing a hydrophobic surface for the side chain top pack against. It is possible that this indirect interaction is responsible for the Trp457 requirement observed previously, a smaller side chain cannot pack against His435. The position of the AF2 helix was stabilized by the presence of SRC located in the co-activator grove.

[0143] All residues in LXRβ lining the binding pocket that are within 5 Å of the epoxycholesterol molecule include: Asn239 and Phe243 in helix 1; Phe 268, Phe271, Thr272, Leu274, Ala275, Ser278, and Glu281 in helix 3; Ile309, Met312, Leu313, Glu315, Thr316 and Arg319 in helix4/5; Phe329 in the beta turn; Phe340 in helix 6; Leu345, Phe349, and Ile353 in helix 7; His435, Gln438, Val439, and Leu442 in helix 11, Leu449, Leu453, and Trp457 in the AF2 helix. There were several areas of unoccupied space in the binding pocket adjacent to the EPC C and D rings, proximal to Met312 and Thr316, and proximal to Ile327 and Phe340.

[0144] VI.C. The LXRβ/T317 Complex

[0145] The structure of the complex of LXRβ with compound T317 yielded two distinct LXRβ conformations, with T317 adopting both syn and gauche conformations within the relatively large binding pocket (FIGS. 4 and 5). These multiple conformations were likely present because of a combination of crystal packing forces and a low rotational energy barrier around the compound's S—N bond. When corresponding Cα atoms were superimposed, both LXRβ molecules had nearly identical conformations surrounding the hexafluoroisopropyl moiety. This part of the receptor, which comprises helices 7 through 11, also displayed the greatest degree of conservation between the two molecules in the EPC structure, presumably because the homodimer interface forced a local dyad symmetry. The only polar interaction observed was a hydrogen bond between the hexafluoro-isopropyl oxygen atom and the His435 imidazole nitrogen. This interaction was present in both copies of the molecule and is probably responsible for the tight binding and activation by this compound.

[0146] Interacting residues whose side chain conformations are conserved between the two molecules include Phe271, Thr272, Ile309, Leu345, Phe349, His435, Gln438, Val439, Leu442, Leu449, Leu453, and Trp457. Other residues that interact with both conformations of T317 include Leu274, Ala275, Ser278, Met312, Leu313, Thr316, and Ile353. Residues that interact with the gauche conformation (A molecule) but not the syn are in the beta-turn region and include Ile327, Thr328, and Phe329. This conformation of T317 fills the pocket seen in the LXRβ/EPC complex. Residues that interact with the syn conformation (B molecule) but not the gauche include residues in helices 3 and 4 that interact with the EPC A-ring, and include Phe268, Glu281, Glu315, Tyr335, and Phe340. Neither copy of T317 filled the LXRb pocket, both left significant voids in different regions of the pocket.

[0147] VI.D. Mutational Analysis of LXR Ligand Interactions

[0148] The structures of the complex of LXRβ with bound T317 and EPC revealed strikingly different protein/ligand interactions. To explore these differences, site directed mutants were made targeting specific pocket residues that interacted more directly with one compound than the other. FIG. 6A indicates that both T317 and EPC hydrogen bond with H435 (H421α). However, the gauche conformation of I317 extended into a pocket near the beta turn. This observation suggests that mutations of I327 (I313α), F329 (F315α), and Y335 (Y321α) that close off the pocket might be used to test whether this region is significant for compound binding. By contrast, O3 of EPC extended into a hydrophilic pocket (see FIG. 6B) which includes residues E281 (E267α), E315 (E301α), and R319 (R305α). Mutations in this region permit identification of the necessary polar interactions for EPC binding. The transactivation capability of gal4-fusions of wild-type and mutant LXRα and LXRβ LBDs were measured by their ability to transcribe secreted placental alkaline phosphatase (SPAP) on a UAS-tk promoter in transient transfection experiments in CV-1 cells. See Laboratory Example 4. FIGS. 7A and 7B show the effects of these mutations on the transcriptional activity of LXR. As expected, only the H435A (H421Acc) mutation completely knocked out the activity of T317, with some modulation by the Y335W mutation. Although most mutations decreased EPC activity, removing R319 (R306α) and H435 (H421α) completely abolished LXR activation, in accordance with the structure. These data agree with the structure in suggesting that the conserved arginine R319 (R305α) is the critical residue for organizing the polar interactions around EPC O3. Also in accordance with the structure, adding bulk to F329 (F329W) sterically inhibited EPC binding while decreasing bulk (F329L) did not. Although the mutational data from both LXR subtypes is similar, mutations in LXRα appear to have a greater impact than mutations in LXRβ, suggesting that the pocket is tighter.

[0149] VI.E. The Pharmacology of Oxysterols

[0150] From previous structure activity relationship studies performed on oxysterol activation of LXRα, Trp443 was found to be essential for activation. This residue is equivalent to to the Trp457 residue of LXRβ (Spencer et al., (2001) J. Med. Chem. 44:886-897). These studies also concluded that a hydrogen-bonding group on the oxysterol C24 was essential for activation. The structure of LXRβ in complex with EPC makes it clear why the tryptophan is essential, and why the epoxide group is required for activation. The conserved hydrogen bond with His435 seen in both complexes underscores its importance for activation. Only oxysterols able to make this hydrogen bond can orient H435 to form a hydrophobic complementary surface for W457, allowing the AF2 helix to pack appropriately. Smaller residues than a Trp will not interact with H435, so the hydrogen bond between the histidine and the oxysterol will not be strong enough. The structure also suggests that oxysterols without the hydrogen bonding group, like cholesterol, should bind to LXR, but will not activate transcription through the AF2. Newer binding data suggests that cholesterol and other oxysterols do bind to LXR but do not recruit co-activator, an observation that would not detected in those previous studies because it was not looked for. This property of the oxysterols is especially relevant to drug discovery efforts, since many compounds also bind tightly but do not activate LXR.

[0151] VI.F. Essential Contacts for Ligand Binding

[0152] In all four holo molecules, the ligand made contacts with residues in helices 3, 4, 5, the beta-turn, helix 11, and the AF2 helix, and was oriented in the same pocket observed for other nuclear receptors. In general, the protein ligand interface was dominated by hydrophobic contacts. The interaction with His435 is conserved in all three liganded molecules, suggesting that interactions with this residue is necessary for LXR activation, but could be different for the two different classes of ligand. This result agrees with earlier mutagenesis data, which showed that LXRα Trp443 (Trp457β) was essential for activation by oxysterols, but not by T317. The other polar residue essential for oxysterol binding was R319, with F329 required to position the oxysterol A-ring. However, in light of the tight and efficacious nature of T317, interaction with these residues is neither necessary nor sufficient for LXR activation.

[0153] Another interesting feature of the LXR/T317 complex is that the ligand does not fill the pocket. Indeed, there is enough room in the pocket for T317 to adopt multiple conformations, yet the compound bound tightly and was efficacious. Thus, although it is not applicants' desire to be bound by any theory of operation, the structures of T317 and EPC, combined with the binding data on oxysterols, imply that filling the LXR binding pocket is neither necessary nor sufficient for activation.

[0154] VI.G. Generation of Easily-Solved LXR Crystals

[0155] The present invention discloses a substantially pure LXR LBD polypeptide in crystalline form. In preferred embodiments, exemplified in the Figures and Laboratory Examples, LXR is crystallized with bound ligand(s). Crystals are formed from LXR LBD polypeptides that are usually expressed by a cell culture, such as E. coli. Bromo-, iodo- and substitutions can be included during the preparation of crystal forms and can act as heavy atom substitutions in LXR ligands and in crystals of LXR and the LXR LBD. This method can be advantageous for the phasing of the crystal, which is a crucial, and sometimes limiting, step in solving the three-dimensional structure of a crystallized entity. Thus, the need for generating the heavy metal derivatives traditionally employed in crystallography might be eliminated. After the three-dimensional structure of a LXR or LXR LBD with or without a ligand bound is determined, the resultant three-dimensional structure can be used in computational methods to design synthetic ligands for LXR and other LXR polypeptide fragments. Further activity structure relationships can be determined through routine testing, using assays disclosed herein and known in the art.

[0156] VII. Preparation of LXR Ligands

[0157] The ligand N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide (T317) has been previously described (Schultz et al., (2000) Gene Dev. 14: 2831-2838) and comprises the chemical structure: 1

[0158] The ligand 24(S), 25-epoxycholesterol (EPC) is commercially available and its utility as a ligand for LXR has been described (Lehmann, et al., (1997) J. Biol. Chem. 272(6): 3137-3140). The synthesis of this compound has also been described (Nelson et al., (1981) J. Biol. Chem. 256:1067-1068; Saucier et al., (1985) J. Biol. Chem. 260: 14571-14579). 24(S), 25-epoxycholesterol comprises the chemical structure: 2

[0159] VIII. Uses of LXR Crystals and the Three-Dimensional Structure of the Ligand Binding Domain of LXR

[0160] The LXR crystals and three-dimensional structures that form aspects of the present invention can be employed in a variety of applications. A brief discussion of several of these applications is presented hereinbelow. Additional uses for LXR crystals and the three-dimensional structures disclosed herein will be apparent to those of skill in the art upon consideration of the present disclosure.

[0161] VIII.A. Design and Development of LXR Modulators

[0162] The knowledge of the structure of the LXR ligand binding domain, an aspect of the present invention, provides a tool for investigating the mechanism of action of LXR and other LXR polypeptides in a subject. For example, various computer models, as described herein, can predict the binding of various substrate molecules to the LBD of LXR. Upon discovering that such binding in fact takes place, knowledge of the protein structure then allows design and synthesis of small molecules that mimic the functional binding of the substrate to the LBD of LXR. This is the method of “rational” drug design, further described herein.

[0163] Use of the isolated and purified LXR crystalline structure of the present invention in rational drug design is thus provided in accordance with the present invention. Additional rational drug design techniques are described in U.S. Pat. Nos. 5,834,228 and 5,872,011, incorporated herein in their entirety.

[0164] Thus, in addition to the compounds described herein, other sterically similar compounds can be formulated to mimic the key structural regions of LXRs in general, or of hLXR in particular. The generation of a structural functional equivalent can be achieved by the techniques of modeling and chemical design known to those of skill in the art and described herein. It will be understood that all such sterically similar constructs fall within the scope of the present invention.

[0165] VIII.A.1. Rational Drug Design

[0166] The three-dimensional structure of a LXR ligand binding domain is unprecedented and will greatly aid in the development of new synthetic ligands for a LXR polypeptide, such as LXR agonists and antagonists, including those that bind exclusively to any one of the LXR orthologs. In addition, LXR is well suited to modern methods, including three-dimensional structure elucidation and combinatorial chemistry, such as those disclosed in U.S. Pat. No. 5,463,564, incorporated herein by reference. Structure determination using X-ray crystallography is possible because of the solubility properties of the LXR orthologs. Computer programs that use crystallography data when practicing the present invention will enable the rational design of ligands to these receptors. Programs such as RASMOL (Biomolecular Structures Group, Glaxo Wellcome Research & Development Stevenage, Hertfordshire, UK Version 2.6, August 1995, Version 2.6.4, December 1998, Copyright ©Roger Sayle 1992-1999) can be used with the atomic structural coordinates from crystals of the present invention, crystals generated by practicing the invention or crystals used to practice the invention by generating three-dimensional models and/or determining the structures involved in ligand binding. Computer programs such as those sold under the registered trademark INSIGHT II® and such as GRASP (Nicholls et al., (1991) Proteins 11: 281-96) allow for further manipulations and the ability to introduce new structures. In addition, high throughput binding and bioactivity assays can be devised using purified recombinant protein and modern reporter gene transcription assays known to those of skill in the art in order to refine the activity of a designed ligand.

[0167] A method of identifying modulators of the activity of a LXR polypeptide using rational drug design is thus provided in accordance with the present invention. The method comprises designing a potential modulator for a LXR polypeptide of the present invention that will form non-covalent bonds with amino acids in the ligand binding cavity based upon the crystalline structure of the LXR LBD polypeptide; synthesizing the modulator; and determining whether the potential modulator modulates the activity of the LXR polypeptide. In a preferred embodiment, the modulator is designed for a LXR polypeptide. Preferably, the LXR polypeptide comprises the amino acid sequence of SEQ ID NO: 4 and the LXR LBD comprises the amino acid sequence SEQ ID NO: 8. The determination of whether the modulator modulates the biological activity of a LXR polypeptide is made in accordance with the screening methods disclosed herein, or by other screening methods known to those of skill in the art. Modulators can be synthesized using techniques known to those of ordinary skill in the art.

[0168] In an alternative embodiment, a method of designing a modulator of a LXR polypeptide in accordance with the present invention is disclosed comprising: (a) selecting a candidate LXR ligand; (b) determining which amino acid or amino acids of a LXR polypeptide interact with the ligand using a three-dimensional model of a crystallized LXR LBD; (c) identifying in a biological assay for LXR activity a degree to which the ligand modulates the activity of the LXR polypeptide; (d) selecting a chemical modification of the ligand wherein the interaction between the amino acids of the LXR polypeptide and the ligand is predicted to be modulated by the chemical modification; (e) performing the chemical modification on the ligand to form a modified ligand; (f) contacting the modified ligand with the LXR polypeptide; (g) identifying in a biological assay for LXR activity a degree to which the modified ligand modulates the biological activity of the LXR polypeptide; and (h) comparing the biological activity of the LXR polypeptide in the presence of modified ligand with the biological activity of the LXR polypeptide in the presence of the unmodified ligand, whereby a modulator of a LXR polypeptide is designed.

[0169] VIII.A.2. Methods for Using the LXR LBD Structural Coordinates for Molecular Design

[0170] For the first time, the present invention permits the use of molecular design techniques to design, select and synthesize chemical entities and compounds, including modulatory compounds, capable of binding to the ligand binding cavity or an accessory binding site of LXR and the LXR LBD, in whole or in part. Correspondingly, the present invention also provides for the application of similar techniques in the design of modulators of any LXR polypeptide.

[0171] In accordance with a preferred embodiment of the present invention, the structure coordinates of a crystalline LXR LBD can be used to design compounds that bind to a LXR LBD (preferably a LXR LBD) and alter the properties of a LXR LBD (for example, the dimerization or ligand binding ability) in different ways. One aspect of the present invention provides for the design of compounds that act as competitive inhibitors of a LXR polypeptide by binding to all, or a portion of, the binding sites on a LXR LBD. The present invention also provides for the design of compounds that can act as uncompetitive inhibitors of a LXR LBD. These compounds can bind to all, or a portion of, an accessory binding site of a LXR that is already binding its ligand and can, therefore, be more potent and less non-specific than known competitive inhibitors that compete only for the LXR ligand binding cavity. Similarly, non-competitive inhibitors that bind to and inhibit LXR LBD activity, whether or not it is bound to another chemical entity, can be designed using the LXR LBD structure coordinates of this invention.

[0172] A second design approach is to probe a LXR or LXR LBD (preferably a hLXR or hLXR LBD) crystal with molecules comprising a variety of different chemical entities to determine optimal sites for interaction between candidate LXR or LXR LBD modulators and the polypeptide. For example, high resolution X-ray diffraction data collected from crystals saturated with solvent allows the determination of the site where each type of solvent molecule adheres. Small molecules that bind tightly to those sites can then be designed, synthesized and tested for their LXR modulator activity.

[0173] Once a computationally-designed ligand is synthesized using the methods of the present invention or other methods known to those of skill in the art, assays can be used to establish its efficacy of the ligand as a modulator of LXR (preferably hLXR) activity. After such assays, the ligands can be further refined by generating intact LXR, or LXR LBD, crystals with a ligand bound to the LXR. The structure of the ligand can then be further refined using the chemical modification methods described herein and known to those of skill in the art, in order to improve the modulation activity or the binding affinity of the ligand. This process can lead to second generation ligands with improved properties.

[0174] Ligands also can be selected that modulate LXR responsive gene transcription by the method of altering the interaction of co-activators and co-repressors with their cognate LXR. For example, agonistic ligands can be selected that block or dissociate a co-repressor from interacting with the LXR, and/or that promote binding or association of a co-activator. Antagonistic ligands can be selected that block co-activator interaction and/or promote co-repressor interaction with a target receptor. Selection can be done via binding assays that screen for designed ligands having the desired modulatory properties. Preferably, interactions of a hLXR polypeptide are targeted. Suitable assays for screening that can be employed, Mutatis mutandis in the present invention, are described in published PCT international applications WO 00/037077 and WO 00/025134, incorporated herein by reference in their entirety.

[0175] VIII.A.3. Methods of Designing LXR LBD Modulator Compounds

[0176] The design of candidate substances, also referred to as “compounds” or “candidate compounds”, that bind to or inhibit LXR LBD-mediated activity according to the present invention generally involves consideration of two factors. First, the compound must be capable of physically and structurally associating with a LXR LBD. Non-covalent molecular interactions important in the association of a LXR LBD with its substrate include hydrogen bonding, van der Waals interactions and hydrophobic interactions.

[0177] Second, the compound must be able to assume a conformation that allows it to associate with a LXR LBD. Although certain portions of the compound will not directly participate in this association with a LXR LBD, those portions can still influence the overall conformation of the molecule. This, in turn, can have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of the binding site, e.g., the ligand binding cavity or an accessory binding site of a LXR LBD, or the spacing between functional groups of a compound comprising several chemical entities that directly interact with a LXR LBD.

[0178] The potential modulatory or binding effect of a chemical compound on a LXR LBD can be analyzed prior to its actual synthesis and testing by the use of computer modeling techniques that employ the coordinates of a crystalline LXR LBD polypeptide of the present invention. If the theoretical structure of the given compound suggests insufficient interaction and association between it and a LXR LBD, synthesis and testing of the compound is obviated. However, if computer modeling indicates a strong interaction, the molecule can then be synthesized and tested for its ability to bind and modulate the activity of a LXR LBD. In this manner, synthesis of unproductive or inoperative compounds can be avoided.

[0179] A modulatory or other binding compound of a LXR LBD polypeptide (preferably a hLXR LBD) can be computationally evaluated and designed via a series of steps in which chemical entities or fragments are screened and selected for their ability to associate with the individual binding sites or other areas of a crystalline LXR LBD polypeptide of the present invention.

[0180] One of several methods can be used to screen chemical entities or fragments for their ability to associate with a LXR LBD and, more particularly, with the individual binding sites of a LXR LBD, such as ligand binding cavity or an accessory binding site. This process can begin by visual inspection of, for example, the ligand binding cavity on a computer screen based on the LXR LBD atomic coordinates presented in Tables 2, 3 and 4. Selected fragments or chemical entities can then be positioned in a variety of orientations, or docked, within an individual binding site of a LXR LBD as defined herein above. Docking can be accomplished using software programs such as those available under the tradenames QUANTA™ (Molecular Simulations Inc., San Diego, Calif.) and SYBYL™ (Tripos, Inc., St. Louis, Mo.), followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARM (Brooks et al., (1983) J. Comp. Chem., 8: 132) and AMBER 5 (Case et al., (1997) AMBER 5, University of California, San Francisco; Pearlman et al., (1995) Comput. Phys. Commun. 91: 1-41).

[0181] Specialized computer programs can also assist in the process of selecting fragments or chemical entities. These include:

[0182] 1. GRID™ program, version 17 (Goodford, (1985) J. Med. Chem. 28: 849-57), which is available from Molecular Discovery Ltd., Oxford, UK;

[0183] 2. MCSS™ program (Miranker & Karplus, (1991) Proteins 11: 29-34), which is available from Molecular Simulations, Inc., San Diego, Calif.;

[0184] 3. AUTODOCK™ 3.0 program (Goodsell & Olsen, (1990) Proteins 8: 195-202), which is available from the Scripps Research Institute, La Jolla, Calif.;

[0185] 4. DOCK™ 4.0 program (Kuntz et al., (1992) J. Mol. Biol. 161: 269-88), which is available from the University of California, San Francisco, Calif.;

[0186] 5. FLEX-X™ program (See, Rarey et al., (1996) J. Comput. Aid. Mol. Des. 10:41-54), which is available from Tripos, Inc., St. Louis, Mo.;

[0187] 6. MVP program (Lambert, (1997) in Practical Application of Computer-Aided Drug Design, (Charifson, ed.) Marcel-Dekker, New York, pp. 243-303); and

[0188] 7. LUDI™ program (Bohm, (1992) J. Comput. Aid. Mol. Des. 6: 61-78), which is available from Molecular Simulations, Inc., San Diego, Calif.

[0189] Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound or modulator. Assembly can proceed by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of a LXR LBD. Manual model building using software such as QUANTA™ or SYBYL™ typically follows.

[0190] Useful programs to aid one of ordinary skill in the art in connecting the individual chemical entities or fragments include:

[0191] 1. CAVEAT™ program (Bartlett et al., (1989) Special Pub., Royal Chem. Soc. 78: 182-96), which is available from the University of California, Berkeley, Calif.;

[0192] 2. 3D database systems, such as MACCS-3D™ system program, which is available from MDL Information Systems, San Leandro, Calif. This area is reviewed in Martin, (1992) J. Med. Chem. 35: 2145-54; and

[0193] 3. HOOK™ program (Eisen et al., (1994). Proteins 19: 199-221), which is available from Molecular Simulations, Inc., San Diego, Calif.

[0194] Instead of proceeding to build a LXR LBD modulator (preferably a hLXR LBD modulator) in a step-wise fashion one fragment or chemical entity at a time as described above, modulatory or other binding compounds can be designed as a whole or de novo using the structural coordinates of a crystalline LXR LBD polypeptide of the present invention and either an empty binding site or optionally including some portion(s) of a known modulator(s). Applicable methods can employ the following software programs:

[0195] 1. LUDI™ program (Bohm, (1992) J. Comput Aid. Mol. Des. 6: 61-78), which is available from Molecular Simulations, Inc., San Diego, Calif.;

[0196] 2. LEGEND™ program (Nishibata & Itai, (1991) Tetrahedron 47: 8985); and

[0197] 3. LEAPFROG™, which is available from Tripos Associates, St. Louis, Mo.

[0198] Other molecular modeling techniques can also be employed in accordance with this invention. See, e.g., Cohen et al., (1990) J. Med. Chem. 33: 883-94. See also, Navia & Murcko, (1992) Curr. Opin. Struc. Biol. 2: 202-10; U.S. Pat. No. 6,008,033, herein incorporated by reference.

[0199] Once a compound has been designed or selected by the above methods, the efficiency with which that compound can bind to a LXR LBD can be tested and optimized by computational evaluation. By way of particular example, a compound that has been designed or selected to function as a LXR LBD modulator should also preferably traverse a volume not overlapping that occupied by the binding site when it is bound to its native ligand. Additionally, an effective LXR LBD modulator should preferably demonstrate a relatively small difference in energy between its bound and free states (i.e., a small deformation energy of binding). Thus, the most efficient LXR LBD modulators should preferably be designed with a deformation energy of binding of not greater than about 10 kcal/mole, and preferably, not greater than 7 kcal/mole. It is possible for LXR LBD modulators to interact with the polypeptide in more than one conformation that is similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free compound and the average energy of the conformations observed when the modulator binds to the polypeptide.

[0200] A compound designed or selected as binding to a LXR polypeptide (preferably a hLXR LBD polypeptide) can be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target polypeptide. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the modulator and the polypeptide when the modulator is bound to a LXR LBD preferably make a neutral or favorable contribution to the enthalpy of binding.

[0201] Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include:

[0202] 1. Gaussian 98™, which is available from Gaussian, Inc., Pittsburgh, Pa.;

[0203] 2. AMBER™ program, version 6.0, which is available from the University of California at San Francisco;

[0204] 3. QUANTA™ program, which is available from Molecular Simulations, Inc., San Diego, Calif.;

[0205] 4. CHARMm® program, which is available from Molecular Simulations, Inc., San Diego, Calif.; and

[0206] 4. INSIGHT II® program, which is available from Molecular Simulations, Inc., San Diego, Calif.

[0207] These programs can be implemented using a suitable computer system. Other hardware systems and software packages will be apparent to those skilled in the art after review of the disclosure of the present invention presented herein.

[0208] Once a LXR LBD modulating compound has been optimally selected or designed, as described above, substitutions can then be made in some of its atoms or side groups in order to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation should be avoided. Such substituted chemical compounds can then be analyzed for efficiency of fit to a LXR LBD binding site using the same computer-based approaches described in detail above.

[0209] VIII.B. Method of Screening for Chemical and Biological Modulators of the Biological Activity of LXR

[0210] A candidate substance identified according to a screening assay of LXR present invention has an ability to modulate the biological activity of a LXR polypeptide or a LXR LBD polypeptide. In a preferred embodiment, such a candidate compound can have utility in the treatment of disorders and conditions associated with the biological activity of a LXR or a LXR LBD polypeptide, including, but not limited to reducing serum levels of cholesterol and reducing arterial plaque formation and accumulation.

[0211] In a cell-free system, the method comprises the steps of establishing a control system comprising a LXR polypeptide and a ligand which is capable of binding to the polypeptide; establishing a test system comprising a LXR polypeptide, the ligand, and a candidate compound; and determining whether the candidate compound modulates the activity of the polypeptide by comparison of the test and control systems. A representative ligand comprises N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide, EPC, a peptide or a small molecule, and in this embodiment, the biological activity or property screened includes binding affinity.

[0212] In another embodiment of the invention, a form of a LXR polypeptide or a catalytic or immunogenic fragment or oligopeptide thereof, can be used for screening libraries of compounds in any of a variety of drug screening techniques. The fragment employed in such a screening can be affixed to a solid support. The formation of binding complexes, between a LXR polypeptide and the agent being tested, will be detected. In a preferred embodiment, the LXR polypeptide has an amino acid sequence of SEQ ID NO: 4. When a LXR LBD polypeptide is employed, a preferred embodiment includes a LXR polypeptide having the amino acid sequence of SEQ ID NO: 8.

[0213] Another technique for drug screening which can be used provides for high throughput screening of compounds having suitable binding affinity to the protein of interest as described in published PCT application WO 84/03564, herein incorporated by reference. In this method, as applied to a polypeptide of the present invention, large numbers of different small test compounds are synthesized on a solid substrate, such as plastic pins or some other surface. The test compounds are reacted with the polypeptide, or fragments thereof. Bound polypeptide is then detected by methods well known to those of skill in the art. The polypeptide can also be placed directly onto plates for use in the aforementioned drug screening techniques.

[0214] In yet another embodiment, a method of screening for a modulator of a LXR polypeptide or a LXR LBD polypeptide comprises: providing a library of test samples; contacting a LXR polypeptide or a LXR LBD polypeptide with each test sample; detecting an interaction between a test sample and a LXR polypeptide or a LXR LBD polypeptide; identifying a test sample that interacts with a LXR polypeptide or a LXR LBD polypeptide; and isolating a test sample that interacts with a LXR polypeptide or a LXR LBD polypeptide.

[0215] In each of the foregoing embodiments, an interaction can be detected spectrophotometrically, radiologically or immunologically. An interaction between a LXR polypeptide or a LXR LBD polypeptide and a test sample can also be quantified using methodology known to those of skill in the art. In another embodiment, the LXR polypeptide and the LXR LBD is in crystalline form.

[0216] In accordance with the present invention there is also provided a rapid and high throughput screening method that relies on the methods described above. This screening method comprises separately contacting each of a plurality of substantially identical samples with a LXR polypeptide or a LXR LBD and detecting a resulting binding complex. In such a screening method the plurality of samples preferably comprises more than about 104 samples, and more preferably comprises more than about 5×104 samples.

[0217] VIII.C. Method of Identifying Compounds Which Inhibit Ligand Binding

[0218] Using the crystal structures and ligand orientations, disclosed for the first time in the present invention, it is possible to design test compounds that inhibit binding of ligands normally bound by a LXR polypeptide.

[0219] In one aspect of the present invention, an assay method for identifying a compound that inhibits binding of a ligand to a LXR polypeptide is disclosed. A known ligand of LXR can be used in the assay method as the ligand against which the inhibition by a test compound is gauged. N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide, EPC, a SRC-dervied peptide, and combinations thereof, are preferred ligands in the assay method. The method comprises (a) incubating a LXR polypeptide with a ligand in the presence of a test inhibitor compound; (b) determining an amount of ligand that is bound to the LXR polypeptide, wherein decreased binding of ligand to the LXR polypeptide in the presence of the test inhibitor compound relative to binding in the absence of the test inhibitor compound is indicative of inhibition; and (c) identifying the test compound as an inhibitor of ligand binding if decreased ligand binding is observed. Preferably, the ligand is N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide, EPC, a SRC-dervied peptide, and combinations thereof.

[0220] In another aspect of the present invention, the disclosed assay method can be employed in the structural refinement of candidate LXR inhibitors. For example, multiple rounds of optimization can be followed by gradual structural changes in a strategy of inhibitor design. A strategy such as this is made possible by the disclosure of the coordinates of the LXR LBD and the disclosure of the orientation position of ligands of LXR, namely N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide, EPC, a SRC-dervied peptide, and combinations thereof.

[0221] IX. Design, Preparation and Structural Analysis of LXR and LXR LBD Mutants and Structural Equivalents

[0222] The present invention provides for the generation of LXR and LXR mutants (preferably hLXR and hLXR LBD mutants), and the ability to solve the crystal structures of those that crystallize. More particularly, through the provision of the three-dimensional structure of a LXR LBD, desirable sites for mutation can be identified, based on analysis of the three-dimensional LXR LBD structure coordinates provided herein.

[0223] The structure coordinates of a LXR LBD provided in accordance with the present invention also facilitate the identification of related proteins or enzymes analogous to LXR in function, structure or both, (for example, a mouse LXR), which can lead to novel therapeutic modes for treating or preventing a range of disease states, such as minimization of serum cholesterol levels and preventing the accumulation of cholesterol plaques.

[0224] IX.A. Sterically Similar Compounds

[0225] A further aspect of the present invention is that sterically similar compounds can be formulated to mimic the key portions of a LXR LBD structure. Such compounds are functional equivalents. The generation of a structural functional equivalent can be achieved by the techniques of modeling and chemical design known to those of skill in the art and described herein. Modeling and chemical design of LXR and LXR LBD structural equivalents can be based on the structure coordinates of a crystalline LXR LBD polypeptide of the present invention. It will be understood that all such sterically similar constructs fall within the scope of the present invention.

[0226] IX.B. LXR Polypeptides

[0227] The generation of chimeric LXR polypeptides is also an aspect of the present invention. Such a chimeric polypeptide can comprise a LXR LBD polypeptide or a portion of a LXR LBD, (e.g. a hLXR LBD) which is fused to a candidate polypeptide or a suitable region of the candidate polypeptide, for example a LXR expressed in mouse or other species. Throughout the present disclosure it is intended that the term “mutant” encompass not only mutants of a LXR LBD polypeptide but chimeric proteins generated using a LXR LBD as well. It is thus intended that the following discussion of mutant LXR LBDs apply mutatis mutandis to chimeric LXR and LXR LBD polypeptides and to structural equivalents thereof.

[0228] In accordance with the present invention, a mutation can be directed to a particular site or combination of sites of a wild-type LXR LBD. For example, an accessory binding site or the binding cavity can be chosen for mutagenesis. Similarly, a residue having a location on, at or near the surface of the polypeptide can be replaced, resulting in an altered surface charge of one or more charge units, as compared to the wild-type LXR and LXR LBD. Alternatively, an amino acid residue in a LXR or a LXR LBD can be chosen for replacement based on its hydrophilic or hydrophobic characteristics.

[0229] Such mutants can be characterized by any one of several different properties as compared with the wild-type LXR LBD. For example, such mutants can have an altered surface charge of one or more charge units, or can have an increase in overall stability. Other mutants can have altered substrate specificity in comparison with, or a higher specific activity than, a wild-type LXR or LXR LBD.

[0230] LXR and LXR LBD mutants of the present invention can be generated in a number of ways. For example, the wild-type sequence of a LXR or a LXR LBD can be mutated at those sites identified using this invention as desirable for mutation, by means of oligonucleotide-directed mutagenesis or other conventional methods, such as deletion. Alternatively, mutants of a LXR or a LXR LBD can be generated by the site-specific replacement of a particular amino acid with an unnaturally occurring amino acid. In addition, LXR or LXR LBD mutants can be generated through replacement of an amino acid residue, for example, a particular cysteine or methionine residue, with selenocysteine or selenomethionine. This can be achieved by growing a host organism capable of expressing either the wild-type or mutant polypeptide on a growth medium depleted of either natural cysteine or methionine (or both) but enriched in selenocysteine or selenomethionine (or both).

[0231] Mutations can be introduced into a DNA sequence coding for a LXR or a LXR LBD using synthetic oligonucleotides. These oligonucleotides contain nucleotide sequences flanking the desired mutation sites. Mutations can be generated in the full-length DNA sequence of a LXR or a LXR LBD or in any sequence coding for polypeptide fragments of a LXR or a LXR LBD.

[0232] According to the present invention, a mutated LXR or LXR LBD DNA sequence produced by the methods described above, or any alternative methods known in the art, can be expressed using an expression vector. An expression vector, as is well known to those of skill in the art, typically includes elements that permit autonomous replication in a host cell independent of the host genome, and one or more phenotypic markers for selection purposes. Either prior to or after insertion of the DNA sequences surrounding the desired LXR or LXR LBD mutant coding sequence, an expression vector also will include control sequences encoding a promoter, operator, ribosome binding site, translation initiation signal, and, optionally, a repressor gene or various activator genes and a signal for termination. In some embodiments, where secretion of the produced mutant is desired, nucleotides encoding a “signal sequence” can be inserted prior to a LXR or a LXR LBD mutant coding sequence. For expression under the direction of the control sequences, a desired DNA sequence must be operatively linked to the control sequences; that is, the sequence must have an appropriate start signal in front of the DNA sequence encoding the LXR or LXR LBD mutant, and the correct reading frame to permit expression of that sequence under the control of the control sequences and production of the desired product encoded by that LXR or LXR LBD sequence must be maintained.

[0233] Any of a wide variety of well-known available expression vectors can be useful to express a mutated LXR or LXR LBD coding sequences of this invention and generated as described in Laboratory Example 3. These expression vectors can be used in the techniques disclosed in Laboratory Examples 1 and 3 and can include, for example, vectors comprising segments of chromosomal, non-chromosomal and synthetic DNA sequences, such as various known derivatives of SV40, known bacterial plasmids, e.g., plasmids from E. coli including col E1, pCR1, pBR322, pMB9 and their derivatives, wider host range plasmids, e.g., RP4, phage DNAs, e.g., the numerous derivatives of phage λ, e.g., NM 989, and other DNA phages, e.g., M13 and filamentous single stranded DNA phages, yeast plasmids and vectors derived from combinations of plasmids and phage DNAs, such as plasmids which have been modified to employ phage DNA or other expression control sequences. In a preferred embodiment of this invention, the E. coli vector pRSETA, including a T7-based expression system, is employed.

[0234] In addition, any of a wide variety of expression control sequences-sequences that control the expression of a DNA sequence when operatively linked to it—can be used in these vectors to express the mutated DNA sequences according to this invention. Such useful expression control sequences, include, for example, the early and late promoters of SV40 for animal cells, the lac system, the trp system the TAC or TRC system, the major operator and promoter regions of phage λ, the control regions of fd coat protein, all for E. coli, the promoter for 3-phosphoglycerate kinase or other glycolytic enzymes, the promoters of acid phosphatase, e.g., Pho5, the promoters of the yeast α-mating factors for yeast, and other sequences known to control the expression of genes of prokaryotic or eukaryotic cells or their viruses, and various combinations thereof.

[0235] A wide variety of hosts are also useful for producing mutated LXR and LXR LBD polypeptides according to this invention. These hosts include, for example, bacteria, such as E. coli, Bacillus and Streptomyces, fungi, such as yeasts, and animal cells, such as CHO and COS-1 cells, plant cells, insect cells, such as Sf9 cells, and transgenic host cells.

[0236] It should be understood that not all expression vectors and expression systems function in the same way to express mutated DNA sequences of this invention, and to produce modified LXR and LXR LBD polypeptides or LXR or LXR LBD mutants. Neither do all hosts function equally well with the same expression system. One of skill in the art can, however, make a selection among these vectors, expression control sequences and hosts without undue experimentation and without departing from the scope of this invention. For example, an important consideration in selecting a vector will be the ability of the vector to replicate in a given host. The copy number of the vector, the ability to control that copy number, and the expression of any other proteins encoded by the vector, such as antibiotic markers, should also be considered.

[0237] In selecting an expression control sequence, a variety of factors should also be considered. These include, for example, the relative strength of the system, its controllability and its compatibility with the DNA sequence encoding a modified LXR or LXR LBD polypeptide of this invention, with particular regard to the formation of potential secondary and tertiary structures.

[0238] Hosts should be selected by consideration of their compatibility with the chosen vector, the toxicity of a modified LXR or LXR LBD to them, their ability to express mature products, their ability to fold proteins correctly, their fermentation requirements (if any), the ease of purification of a modified LXR or LXR LBD and safety. Within these parameters, one of skill in the art can select various vector/expression control system/host combinations that will produce useful amounts of a mutant LXR or LXR LBD. A mutant LXR or LXR LBD produced in these systems can be purified by a variety of conventional steps and strategies, including those used to purify the wild-type LXR or LXR LBD.

[0239] Once a LXR LBD mutation(s) has been generated in the desired location, such as a ligand binding or dimerization site, the mutants can be tested for any one of several properties of interest. For example, mutants can be screened for an altered charge at physiological pH. This is determined by measuring the mutant LXR or LXR LBD isoelectric point (pI) and comparing the observed value with that of the wild-type parent. Isoelectric point can be measured by gel-electrophoresis according to the method of Wellner (Wellner, (1971) Anal. Chem. 43: 597). A mutant LXR or LXR LBD polypeptide containing a replacement amino acid located at the surface of the enzyme, as provided by the structural information of this invention, can lead to an altered surface charge and an altered pl.

[0240] IX.C. Generation of an Engineered LXR or LXR LBD Mutant

[0241] In another aspect of the present invention, a unique LXR or LXR LBD polypeptide can be generated. Such a mutant can facilitate purification and can facilitate the study of the ligand binding abilities of a LXR polypeptide.

[0242] As used in the following discussion, the terms “engineered LXR”, “engineered LXR LDB”, “LXR mutant”, and “LXR LBD mutant” refers to polypeptides having amino acid sequences which contain at least one mutation in the wild-type sequence. The terms also refer to LXR and LXR LBD polypeptides which are capable of exerting a biological effect in that they comprise all or a part of the amino acid sequence of an engineered LXR or LXR LBD mutant polypeptide of the present invention, or cross-react with antibodies raised against an engineered LXR or LXR LBD mutant polypeptide, or retain all or some or an enhanced degree of the biological activity of the engineered LXR or LXR LBD mutant amino acid sequence or protein. Such biological activity can include ligand binding (e.g. EPC and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide) and co-factor binding (e.g. binding a SRC peptide), as well as reducing serum cholesterol levels and reducing accumulation of cholesterol plaques.

[0243] The terms “engineered LXR LBD” and “LXR LBD mutant” also includes analogs of an engineered LXR LBD or LXR LBD mutant polypeptide. By “analog” is intended that a DNA or polypeptide sequence can contain alterations relative to the sequences disclosed herein, yet retain all or some or an enhanced degree of the biological activity of those sequences. Analogs can be derived from genomic nucleotide sequences or from other organisms, or can be created synthetically. Those of skill in the art will appreciate that other analogs, as yet undisclosed or undiscovered, can be used to design and/or construct LXR LBD or LXR LBD mutant analogs. There is no need for an engineered LXR LBD or LXR LBD mutant polypeptide to comprise all or substantially all of the amino acid sequence of SEQ ID NOs: 6 or 8. Shorter or longer sequences are anticipated to be of use in the invention; shorter sequences are herein referred to as “segments”. Thus, the terms “engineered LXR LBD” and “LXR LBD mutant” also includes fusion, chimeric or recombinant engineered LXR LBD or LXR LBD mutant polypeptides and proteins comprising sequences of the present invention. Methods of preparing such proteins are disclosed herein above and are known in the art.

[0244] IX.D. Sequence Similarity and Identity

[0245] As used herein, the term “substantially similar” means that a particular sequence varies from nucleic acid sequence of SEQ ID NOs: 1, 3, 5, and 7, or the amino acid sequence of SEQ ID NOs: 2, 4, 6, 8 and 9 by one or more deletions, substitutions, or additions, the net effect of which is to retain at least some of biological activity of the natural gene, gene product, or sequence. Such sequences include “mutant” or “polymorphic” sequences, or sequences in Which the biological activity and/or the physical properties are altered to some degree but retains at least some or an enhanced degree of the original biological activity and/or physical properties. In determining nucleic acid sequences, all subject nucleic acid sequences capable of encoding substantially similar amino acid sequences are considered to be substantially similar to a reference nucleic acid sequence, regardless of differences in codon sequences or substitution of equivalent amino acids to create biologically functional equivalents.

[0246] IX.D.1. Sequences that are Substantially Identical to an Engineered LXR or LXR LBD Mutant Sequence of the Present Invention

[0247] Nucleic acids that are substantially identical to a nucleic acid sequence of an engineered LXR or LXR LBD mutant of the present invention, e.g. allelic variants, genetically altered versions of the gene, etc., bind to an engineered LXR or LXR LBD mutant sequence under stringent hybridization conditions. By using probes, particularly labeled probes of DNA sequences, one can isolate homologous or related genes. The source of homologous genes can be any species, e.g. primate species; rodents, such as rats and mice, canines, felines, bovines, equines, yeast, nematodes, etc.

[0248] Between mammalian species, e.g. human and mouse, homologs have substantial sequence similarity, i.e. at least 75% sequence identity between nucleotide sequences. Sequence similarity is calculated based on a reference sequence, which can be a subset of a larger sequence, such as a conserved motif, coding region, flanking region, etc. A reference sequence will usually be at least about 18 nucleotides(nt) long, more usually at least about 30 nt long, and can extend to the complete sequence that is being compared. Algorithms for sequence analysis are known in the art, such as BLAST, described in Altschul et al., (1990) J. Mol. Biol. 215: 403-10.

[0249] Percent identity or percent similarity of a DNA or peptide sequence can be determined, for example, by comparing sequence information using the GAP computer program, available from the University of Wisconsin Geneticist Computer Group. The GAP program utilizes the alignment method of Needleman et al., (1970) J. Mol. Biol. 48: 443, as revised by Smith et al., (1981) Adv. Appl. Math. 2:482. Briefly, the GAP program defines similarity as the number of aligned symbols (i.e., nucleotides or amino acids) that are similar, divided by the total number of symbols in the shorter of the two sequences. The preferred parameters for the GAP program are the default parameters, which do not impose a penalty for end gaps. See, e.g., Schwartz et al. (eds.), (1979), Atlas of Protein Sequence and Structure, National Biomedical Research Foundation, pp. 357-358, and Gribskov et al., (1986) Nucl. Acids. Res. 14: 6745.

[0250] The term “similarity” is contrasted with the term “identity”. Similarity is defined as above; “identity”, however, means a nucleic acid or amino acid sequence having the same amino acid at the same relative position in a given family member of a gene family. Homology and similarity are generally viewed as broader terms than the term identity. Biochemically similar amino acids, for example leucine/isoleucine or glutamate/aspartate, can be present at the same position—these are not identical per se, but are biochemically “similar.” As disclosed herein, these are referred to as conservative differences or conservative substitutions. This differs from a conservative mutation at the DNA level, which changes the nucleotide sequence without making a change in the encoded amino acid, e.g. TCC to TCA, both of which encode serine.

[0251] As used herein, DNA analog sequences are “substantially identical” to specific DNA sequences disclosed herein if: (a) the DNA analog sequence is derived from coding regions of the nucleic acid sequence shown in SEQ ID NOs: 1, 3, 5 and 7; or (b) the DNA analog sequence is capable of hybridization with DNA sequences of (a) under stringent conditions and which encode a biologically active LXR or LXR LBD gene product; or (c) the DNA sequences are degenerate as a result of alternative genetic code to the DNA analog sequences defined in (a) and/or (b). Substantially identical analog proteins and nucleic acids will have between about 70% and 80%, preferably between about 81% to about 90% or even more preferably between about 91% and 99% sequence identity with the corresponding sequence of the native protein or nucleic acid. Sequences having lesser degrees of identity but comparable biological activity are considered to be equivalents.

[0252] As used herein, “stringent conditions” means conditions of high stringency, for example 6×SSC, 0.2% polyvinylpyrrolidone, 0.2% Ficoll, 0.2% bovine serum albumin, 0.1% sodium dodecyl sulfate, 100 μg/ml salmon sperm DNA and 15% formamide at 68° C. For the purposes of specifying additional conditions of high stringency, preferred conditions are salt concentration of about 200 mM and temperature of about 45° C. One example of such stringent conditions is hybridization at 4×SSC, at 65° C., followed by a washing in 0.1×SSC at 65° C. for one hour. Another exemplary stringent hybridization scheme uses 50% formamide, 4×SSC at 42° C.

[0253] In contrast, nucleic acids having sequence similarity are detected by hybridization under lower stringency conditions. Thus, sequence identity can be determined by hybridization under lower stringency conditions, for example, at 50° C. or higher and 0.1×SSC (9 mM NaCl/0.9 mM sodium citrate) and the sequences will remain bound when subjected to washing at 55° C. in 1×SSC.

[0254] IX.D.2. Complementarity and Hybridization to an Engineered LXR or LXR LBD Mutant Sequence

[0255] As used herein, the term “complementary sequences” means nucleic acid sequences that are base-paired according to the standard Watson-Crick complementarity rules. The present invention also encompasses the use of nucleotide segments that are complementary to the sequences of the present invention.

[0256] Hybridization can also be used for assessing complementary sequences and/or isolating complementary nucleotide sequences. As discussed above, nucleic acid hybridization will be affected by such conditions as salt concentration, temperature, or organic solvents, in addition to the base composition, length of the complementary strands, and the number of nucleotide base mismatches between the hybridizing nucleic acids, as will be readily appreciated by those skilled in the art. Stringent temperature conditions will generally include temperatures in excess of about 30° C., typically in excess of about 37° C., and preferably in excess of about 45° C. Stringent salt conditions will ordinarily be less than about 1,000 mM, typically less than about 500 mM, and preferably less than about 200 mM. However, the combination of parameters is much more important than the measure of any single parameter. See, e.g., Wetmur & Davidson, (1968) J. Mol. Biol. 31: 349-70. Determining appropriate hybridization conditions to identify and/or isolate sequences containing high levels of homology is well known in the art. See, e.g., Sambrook et al., (1989) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor, N.Y.

[0257] IX.D.3. Functional Equivalents of an Engineered LXR or LXR LBD Mutant Nucleic Acid Sequence of the Present Invention

[0258] As used herein, the term “functionally equivalent codon” is used to refer to codons that encode the same amino acid, such as the ACG and AGU codons for serine. LXR or LXR LBD-encoding nucleic acid sequences comprising SEQ ID NOs: 1, 3, 5 and 7, which have functionally equivalent codons, are covered by the present invention. Thus, when referring to the sequence examples presented in SEQ ID NOs: 2, 4, 6 and 8, applicants contemplate substitution of functionally equivalent codons into the sequence example of SEQ ID NOs: 1, 3, 5 and 7. Thus, applicants are in possession of amino acid and nucleic acids sequences which include such substitutions but which are not set forth herein in their entirety for convenience.

[0259] It will also be understood by those of skill in the art that amino acid and nucleic acid sequences can include additional residues, such as additional N- or C-terminal amino acids or 5′ or 3′ nucleic acid sequences, and yet still be essentially as set forth in one of the sequences disclosed herein, so long as the sequence retains biological protein activity where polypeptide expression is concerned. The addition of terminal sequences particularly applies to nucleic acid sequences which can, for example, include various non-coding sequences flanking either of the 5′ or 3′ portions of the coding region or can include various internal sequences, i.e., introns, which are known to occur within genes.

[0260] IX.D.4. Biological Equivalents

[0261] The present invention envisions and includes biological equivalents of an engineered LXR or LXR LBD mutant polypeptide of the present invention. The term “biological equivalent” refers to proteins having amino acid sequences which are substantially identical to the amino acid sequence of an engineered LXR LBD mutant of the present invention and which are capable of exerting a biological effect in that they are capable of binding DNA moieties or cross-reacting with anti-LXR or LXR LBD mutant antibodies raised against an engineered mutant LXR or LXR LBD polypeptide of the present invention.

[0262] For example, certain amino acids can be substituted for other amino acids in a protein structure without appreciable loss of interactive capacity with, for example, structures in the nucleus of a cell. Since it is the interactive capacity and nature of a protein that defines that protein's biological functional activity, certain amino acid sequence substitutions can be made in a protein sequence (or the nucleic acid sequence encoding it) to obtain a protein with the same, enhanced, or antagonistic properties. Such properties can be achieved by interaction with the normal targets of the protein, but this need not be the case, and the biological activity of the invention is not limited to a particular mechanism of action. It is thus in accordance with the present invention that various changes can be made in the amino acid sequence of an engineered LXR or LXR LBD mutant polypeptide of the present invention or its underlying nucleic acid sequence without appreciable loss of biological utility or activity.

[0263] Biologically equivalent polypeptides, as used herein, are polypeptides in which certain, but not most or all, of the amino acids can be substituted. Thus, when referring to the sequence examples presented in SEQ ID NOs: 2, 4, 6, 8 and 9, applicants envision substitution of codons that encode biologically equivalent amino acids, as described herein, into the sequence examples of SEQ ID NOs: 1, 3, 5 and 7, respectively. Thus, applicants are in possession of amino acid and nucleic acids sequences which include such substitutions but which are not set forth herein in their entirety for convenience.

[0264] Alternatively, functionally equivalent proteins or peptides can be created via the application of recombinant DNA technology, in which changes in the protein structure can be engineered, based on considerations of the properties of the amino acids being exchanged, e.g. substitution of Ile for Leu. Changes designed by man can be introduced through the application of site-directed mutagenesis techniques, e.g., to introduce improvements to the antigenicity of the protein or to test an engineered LXR or LXR LBD mutant polypeptide of the present invention for its ability to modulate DNA-binding, ligand-binding or other activity, at the molecular level.

[0265] Amino acid substitutions, such as those that might be employed in modifying an engineered LXR or LXR LBD mutant polypeptide of the present invention are generally, but not necessarily, based on the relative similarity of the amino acid side-chain substituents, for example, their hydrophobicity, hydrophilicity, charge, size, and the like. An analysis of the size, shape and type of the amino acid side-chain substituents reveals that arginine, lysine and histidine are all positively charged residues; that alanine, glycine and serine are all of similar size; and that phenylalanine, tryptophan and tyrosine all have a generally similar shape. Therefore, based upon these considerations, arginine, lysine and histidine; alanine, glycine and serine; and phenylalanine, tryptophan and tyrosine; are defined herein as biologically functional equivalents. Other biologically functionally equivalent changes will be appreciated by those of skill in the art. It is implicit in the above discussion, however, that one of skill in the art can appreciate that a radical, rather than a conservative substitution is warranted in a given situation. Non-conservative substitutions in engineered mutant LXR or LXR LBD polypeptides of the present invention are also an aspect of the present invention.

[0266] In making biologically functional equivalent amino acid substitutions, the hydropathic index of amino acids can be considered. Each amino acid has been assigned a hydropathic index on the basis of their hydrophobicity and charge characteristics, these are: isoleucine (+4.5); valine (+4.2); leucine (+3.8); phenylalanine (+2.8); cysteine (+2.5); methionine (+1.9); alanine (+1.8); glycine (−-0.4); threonine (−0.7); serine (−0.8); tryptophan (−0.9); tyrosine (−1.3); proline (−1.6); histidine (−3.2); glutamate (−3.5); glutamine (−3.5); aspartate (−3.5); asparagine (−3.5); lysine (−3.9); and arginine (−4.5).

[0267] The importance of the hydropathic amino acid index in conferring interactive biological function on a protein is generally understood in the art (Kyte & Doolittle, (1982), J. Mol. Biol. 157: 105-132, incorporated herein by reference). It is known that certain amino acids can be substituted for other amino acids having a similar hydropathic index or score and still retain a similar biological activity. In making changes based upon the hydropathic index, the substitution of amino acids whose hydropathic indices are within ±2 of the original value is preferred, those which are within ±1 of the original value are particularly preferred, and those within ±0.5 of the original value are even more particularly preferred.

[0268] It is also understood in the art that the substitution of like amino acids can be made effectively on the basis of hydrophilicity. U.S. Pat. No. 4,554,101, incorporated herein by reference, states that the greatest local average hydrophilicity of a protein, as governed by the hydrophilicity of its adjacent amino acids, correlates with its immunogenicity and antigenicity, i.e. with a biological property of the protein. It is understood that an amino acid can be substituted for another having a similar hydrophilicity value and still obtain a biologically equivalent protein.

[0269] As detailed in U.S. Pat. No. 4,554,101, the following hydrophilicity values have been assigned to amino acid residues: arginine (+3.0); lysine (+3.0); aspartate (+3.0±1); glutamate (+3.0+1); serine (+0.3); asparagine (+0.2); glutamine (+0.2); glycine (0); threonine (−0.4); proline (−0.5+1); alanine (−0.5); histidine (−0.5); cysteine (−1.0); methionine (−1.3); valine (−1.5); leucine (−1.8); isoleucine (−1.8); tyrosine (−2.3); phenylalanine (−2.5); tryptophan (−3.4).

[0270] In making changes based upon similar hydrophilicity values, the substitution of amino acids whose hydrophilicity values are within ±2 of the original value is preferred, those which are within ±1 of the original value are particularly preferred, and those within ±0.5 of the original value are even more particularly preferred.

[0271] While discussion has focused on functionally equivalent polypeptides arising from amino acid changes, it will be appreciated that these changes can be effected by alteration of the encoding DNA, taking into consideration also that the genetic code is degenerate and that two or more codons can code for the same amino acid.

[0272] Thus, it will also be understood that this invention is not limited to the particular amino acid and nucleic acid sequences of SEQ ID NOs: 1-9. Recombinant vectors and isolated DNA segments can therefore variously include an engineered LXR or LXR LBD polypeptide-encoding region itself, include coding regions bearing selected alterations or modifications in the basic coding region, or include larger polypeptides which nevertheless comprise a LXR or LXR LBD polypeptide-encoding regions or can encode biologically functional equivalent proteins or polypeptides which have variant amino acid sequences. Biological activity of an engineered LXR or LXR LBD polypeptide can be determined, for example, by ligand binding assays known to those of skill in the art.

[0273] The nucleic acid segments of the present invention, regardless of the length of the coding sequence itself, can be combined with other DNA sequences, such as promoters, enhancers, polyadenylation signals, additional restriction enzyme sites, multiple cloning sites, other coding segments, and the like, such that their overall length can vary considerably. It is therefore contemplated that a nucleic acid fragment of almost any length can be employed, with the total length preferably being limited by the ease of preparation and use in the intended recombinant DNA protocol. For example, nucleic acid fragments can be prepared which include a short stretch complementary to a nucleic acid sequence set forth in SEQ ID NOs: 1, 3, 5 and 7, such as about 10 nucleotides, and which are up to 10,000 or 5,000 base pairs in length. DNA segments with total lengths of about 4,000, 3,000, 2,000, 1,000, 500, 200, 100, and about 50 base pairs in length are also useful.

[0274] The DNA segments of the present invention encompass biologically functional equivalents of engineered LXR or LXR LBD polypeptides. Such sequences can rise as a consequence of codon redundancy and functional equivalency that are known to occur naturally within nucleic acid sequences and the proteins thus encoded. Alternatively, functionally equivalent proteins or polypeptides can be created via the application of recombinant DNA technology, in which changes in the protein structure can be engineered, based on considerations of the properties of the amino acids being exchanged. Changes can be introduced through the application of site-directed mutagenesis techniques, e.g., to introduce improvements to the antigenicity of the protein or to test variants of an engineered LXR or LXR LBD mutant of the present invention in order to examine the degree of ligand binding activity, or other activity at the molecular level. Various site-directed mutagenesis techniques are known to those of skill in the art and can be employed in the present invention.

[0275] The invention further encompasses fusion proteins and peptides wherein an engineered LXR or LXR LBD mutant coding region of the present invention is aligned within the same expression unit with other proteins or peptides having desired functions, such as for purification or immunodetection purposes.

[0276] Recombinant vectors form important further aspects of the present invention. Particularly useful vectors are those in which the coding portion of the DNA segment is positioned under the control of a promoter. The promoter can be that naturally associated with a LXR gene, as can be obtained by isolating the 5′ non-coding sequences located upstream of the coding segment or exon, for example, using recombinant cloning and/or PCR technology and/or other methods known in the art, in conjunction with the compositions disclosed herein.

[0277] In other embodiments, certain advantages will be gained by positioning the coding DNA segment under the control of a recombinant, or heterologous, promoter. As used herein, a recombinant or heterologous promoter is a promoter that is not normally associated with a LXR gene in its natural environment. Such promoters can include promoters isolated from bacterial, viral, eukaryotic, or mammalian cells. Naturally, it will be important to employ a promoter that effectively directs the expression of the DNA segment in the cell type chosen for expression. The use of promoter and cell type combinations for protein expression is generally known to those of skill in the art of molecular biology (See, e.g., Sambrook et al., (1989) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, New York, specifically incorporated herein by reference). The promoters employed can be constitutive or inducible and can be used under the appropriate conditions to direct high level expression of the introduced DNA segment, such as is advantageous in the large-scale production of recombinant proteins or peptides. One preferred promoter system contemplated for use in high-level expression is a T7 promoter-based system.

[0278] X. Uses of LXR Mutants

[0279] The LXR mutants disclosed herein have a variety of applications, including in the screening of components for LXR activation using the cell-free reporter gene assay methods disclosed herein above, and using whole animal models. The LXR mutants can also be used in cell-free, cell-based and whole animal assay methods for bioavailability of compounds and for toxicology analysis. Additionally, LXR mutants can be employed in crystallizations, screening for changes in ligand activation, screening for species-specific changes in ligand activation and screening for changes in oligomerization state both with and without ligand.

[0280] XI. The Role of the Three-Dimensional Structure of the hLXR LDB in Solving Additional LXR Crystals

[0281] Because polypeptides can crystallize in more than one crystal form, the structural coordinates of a hLXR LBD, or portions thereof, as provided by the present invention, are particularly useful in solving the structure of other crystal forms of hLXR and the crystalline forms of other LXRs. The coordinates provided in the present invention can also be used to solve the structure of LXR or LXR LBD mutants (such as those described above), LXR LDB co-complexes, or of the crystalline form of any other protein with significant amino acid sequence homology to any functional domain of LXR.

[0282] XI.A. Determining the Three-Dimensional Structure of a Polypeptide Using the Three-Dimensional Structure of the hLXR LBD as a Template in Molecular Replacement

[0283] One method that can be employed for the purpose of solving additional LXR crystal structures is molecular replacement. See generally, Rossmann (ed), (1972) The Molecular Replacement Method, Gordon & Breach, New York. In the molecular replacement method, the unknown crystal structure, whether it is another crystal form of a LXR or a LXR LBD, (i.e. a LXR or a LXR LBD mutant), or a LXR or a LXR LBD polypeptide complexed with another compound (a “co-complex”), or the crystal of some other protein with significant amino acid sequence homology to any functional region of the a hLXR LBD, can be determined using the hLXR LBD structure coordinates provided in Tables 2-4. This method provides an accurate structural form for the unknown crystal more quickly and efficiently than attempting to determine such information ab initio.

[0284] In addition, in accordance with this invention, LXR or LXR mutants (preferably hLXR or hLXR LBD mutants) can be crystallized in complex with known modulators. The crystal structures of a series of such complexes can then be solved by molecular replacement and compared with that of wild-type hLXR or the wild-type hLXR LBD. Potential sites for modification within the various binding sites of the enzyme can thus be identified. This information provides an additional tool for determining the most efficient binding interactions, for example, increased hydrophobic interactions, between the hLXR LBD and a chemical entity or compound.

[0285] All of the complexes referred to in the present disclosure can be studied using X-ray diffraction techniques (See, e.g., Blundell & Johnson (1985) Method. Enzymol. 114A & 115B, (Wyckoff et al., eds.), Academic Press) and can be refined using computer software, such as the X-PLOR™ program (Brünger, (1992) X-PLOR, Version 3.1. A System for X-ray Crystallography and NMR, Yale University Press, New Haven, Conn.; X-PLOR is available from Molecular Simulations, Inc., San Diego, Calif.). This information can thus be used to optimize known classes of LXR and LXR LBD modulators, and more importantly, to design and synthesize novel classes of LXR and LXR LBD modulators.

[0286] XII. Conclusions

[0287] To aid further drug discovery efforts, the interactions involved in the binding and activation of LXR have been identified. In one aspect, the present invention discloses the atomic structures of the complexes of LXRβ with the activator T317, and the complex of LXRβ with EPC and the second LXXLL (SEQ ID NO: 9) motif (Westin et al., (1998) Nature 395:199-202) of the nuclear receptor co-activator SRC-1. These structures indicate that the LXR binding pocket is large enough to accommodate the oxysterols, and that the LXR protein is flexible enough to accommodate changes in ligand shape. As has been observed in other steroid receptor structures (Brzozowski et al., (1997) Nature 389:753-758; Williams & Sigler, (1998) Nature 393:392-396; Matias et al., (2000) J. Biol. Chem. 275:26164-2617) a relatively small number of polar interactions are responsible for determining receptor specificity, with the tight binding a result of the ligand's close fit within the hydrophobic pocket. The structure of LXRβ with EPC shows some interesting features that can be explored to fully understand the binding and activation effect. These features might be relevant for drug discovery efforts, as binding of oxysterols to LXR does not appear to be sufficient for activation. The LXRβ/T317 structure shows markedly different interactions from those with EPC, indicating that potency does not require the molecule to fill the binding pocket.

Laboratory Examples

[0288] The following Laboratory Examples have been included to illustrate preferred modes of the invention. Certain aspects of the following Laboratory Examples are described in terms of techniques and procedures found or contemplated by the present inventors to work well in the practice of the invention. These Laboratory Examples are exemplified through the use of standard laboratory practices of the inventors. In light of the present disclosure and the general level of skill in the art, those of skill will appreciate that the following Laboratory Examples are intended to be exemplary only and that numerous changes, modifications and alterations can be employed without departing from the spirit and scope of the invention.

Laboratory Example 1

LXR Expression and Purification

[0289] A minimal construct of the human LXRβ LBD (ligand binding domain) containing amino acids 214-462 and a thrombin cleavable his-tag was subcloned into the E. coli expression vector pRSETa (Invitrogen, Carlsbad, Calif.). After transforming into BL21(DE3) E. coli positive transformants were selected overnight at 37° C. on a LB plate containing 100 μg/ml carbenicilin. 3-4 colonies were selected and grown at 25° C. in 30 ml LB with 100 μg/ml carbenicilin, then used to inoculate 12×2L shaker flasks containing 1 liter of Terrific Broth II (Bio 101, Inc., Vista, Calif.) with 100 μg/ml carbenicilin at 2 ml/liter. Cultures were grown overnight at 22° C. without induction and harvested by centrifugation at 5000G for 10 min. Cell pellets were stored frozen at −80° C.

[0290] The original 12 L shaker flask purification was subsequently scaled up for fermenter growths. All steps were performed at 4° C. Cells were resuspended by adding 4× volume of NiA (25 mM imidazole pH 8.0, 150 mM NaCl, 3% 1,2 propane diol), then lysed by three passages through a cell homogenizer (APV Rannie, Copenhagen, Denmark), followed by centrifugation for 1 hour at 40,000 RPM in a Sorvall A641 to clarify the resultant solution.

[0291] The soluble protein was first purified with a 50 ml Ni+2-NTA affinity column (Qiagen, Valencia, Calif.), which was scaled up to a 150 ml column for the fermenter cultures. Cell lysate was loaded on to the pre-equilibrated column, followed by a 3-column wash with NiA, a 2-column wash with NiA with 50 mM imidazole, and eluted with a 10 column volume 50-500 mM imidazole gradient. LXR eluted at ˜300 mM imidazole. At this point, peak fractions were pooled and dialyzed against 10 mM Tris pH=8.0, 150 mM NaCl, 0.1 mM EDTA, 5% glycerol, separated into aliquots containing 30 mg of protein each, and stored frozen at −80° C.

[0292] For structural studies of protein compound complexes, protein was thawed and further purified using anion exchange with a 5 ml HiTrap HPQ column (AP Biosystems). After adding the relevant compound, his-tagged LXR was digested overnight at 4° C. with thrombin at a mass ration of 1:500. The digested protein was diluted to 25 mM salt with QO buffer (10 mM Tris pH 8.0, 0.1 mM EDTA, 5% glycerol, 5 mM DTT), and then loaded on to the pre-equilibrated anion exchange column. The column was washed with 3 columns of QO plus 30 mM NaCl followed by a 20-column 0-250 mM NaCl gradient. Complexed LXR usually eluted as a sharp peak at ˜150 mM NaCl. The eluted protein was dialyzed against 10 mM Tris pH 8.0, 0.1 mM EDTA, 5% glycerol, 5 mM DTT, 150 mM NaCl; additional compound was added, and the protein was concentrated to 12-14 mg/ml for crystallization trials.

Laboratory Example 2

Crystallization of a LXR Ligand Binding Domain

[0293] Crystallization trials were carried out using the hanging drop method by mixing 2 μl of protein solution with 2 μl of well buffer. Both the LXRβ/ligand complexes crystallized out of 10-12% PEG 3350-8000 with 0.2M salt at 40° C. Usable LXRβ/T0901317 crystals were obtained from a number of salts including NaF, KF, NaCl, KCl, Na formate, Na acetate, and K acetate. The best LXRβ/EPC (24(S), 25-epoxycholesterol) crystals were obtained with ammonium sulfate and lithium sulfate salts. All crystals took 4-6 weeks to grow. Crystals were frozen in LN2 after transferring stepwise to a cryo buffer containing the well buffer with 30% PEG 400.

Laboratory Example 3

Structure Determination

[0294] All data was obtained at the IMCA CAT 17 ID beam line at the Advanced Photon Source (APS) at a wavelength of 1 Å on a MAR CCD detector. Crystals of the LXRβ/T0901317 complex diffracted to 2.3 A, and were in the space group P212121 with unit cell parameters a=60.25 b=82.454, c=123.175. Crystals of the LXRβ/24,25 epoxycholesterol/SRC1 complex diffracted to 2.8 Å, and were in the space group C2221 with unit cell parameters a=71.17 b=120.01, c=147.56. All diffraction data was integrated and scaled using HKL2000 (Otwinowski & Minor, (1997) Method Enzymol. 276: 307-326). The LXRβ/T0901317 structure was solved by molecular replacement using the program AMoRe with a truncated monomeric form of human RARγ as a search model (Table 5). The LXRβ/EPC/SRC1 structure was solved by molecular replacement using the program AMoRe and a refined LXR A subunit from the LXRβ/T0901317 structure as a search model (Table 3).

[0295] In both complex structures there were two molecules in the asymmetric unit related by a non-crystallographic dyad. In the case of the T317 complex, the two subunits were substantially different, so non-crystallographic averaging could not be utilized. Structures were subjected to multiple rounds of building using QUANTAT™ software (Molecular Simulations Inc., San Diego, Calif.) and refined using CNX software (Molecular Simulations Inc., San Diego, Calif.).

Laboratory Example 4

Mutant Construction and Transactivation Measurements by Transient Transfection

[0296] 4.1 Plasmid Construction

[0297] Wild type and mutant LXR transactivation activity was measured in CV-1 cells. Gal4 expression constructs were prepared using the wild type or mutated ligand binding domains (LBDs) of human LXRα and LXRβ (Lehmann et al., (1997) J. Biol. Chem. 272:3137-3140). Wild type LBDs for LXRα (amino acids 164-447) and LXRβ (amino acids 155-462) were subcloned into the pSG-5 Gal4 vector as a fusion with the Gal4 DNA binding domain as KpnI-BamHI fragments. Single amino acid changes in the wild-type receptor LBD proteins were made by utilizing a two-step PCR technique with the corresponding KpnI and BamHI restriction cut sites incorporated at the 5′ and 3′ ends of the DNA fragment. The mutant DNA fragment was subcloned back in to the original pSG5-Gal4 parental vector.

[0298] A human SRC-1 construct (representing amino acids 1-1005) (Onate et al., (1995) Science 270:1354-1357) was prepared in the pSG5 expression vector (Stratagene Corp., La Jolla, Calif.). The reporter plasmid UAS-tk-SPAP was generated by insertion of five copies of a Gal4 DNA-binding element into pGl2-tk-SPAP. The β-galactosidase expression plasmid pCH110 (Pharmacia, Piscataway, N.J.) was employed as an internal control for transfection efficiency.

[0299] 4.2 Transfection and Drug Delivery

[0300] Transfection mixes contained a total of 80 ng total DNA (2 ng receptor plasmid, 8 ng UAS-tk-SPAP reporter plasmid, 7 ng SRC-1 expression plasmid, 25 ng pCH110, and 38 ng of carrier plasmid (pBluescript, Stratagene, La Jolla, Calif.) and 0.7 μl Lipofectamine (Life Technologies, Inc., Rockville, Md.) were added to each well. After 6 to 18 hours, compounds were added at a concentration of 10 μM and incubated for 18 hours prior to determination of reporter activity.

[0301] 4.3 Reporter Assays

[0302] Alkaline phosphatase activity was assayed by adding 200 μl substrate (7 mM p-nitrophenyl phosphate in 1 M diethanolamine/0.28 M sodium chloride/0.5 mM magnesium chloride, pH 9.85) to each well of the plates, incubating at room temperature, and reading absorbance at 405 nm.

[0303] β-Galactosidase normalization was performed by adding 200 μl of substrate (1.1 mg/ml o-nitrophenyl β-D-galactopyranoside, 0.13% Triton X-100 in 0.1 M sodium phosphate buffer, pH 7.2) to cell plate containing 60 μl of medium, incubating at room temperature, and reading absorbance at 405 nm.

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TABLE 1
CRYSTALLOGRAPHIC DATA AND REFINEMENT
Crystal	T317 Complex	EPC complex
Space Group	P212121		C2221
Unit Cell	a = 60.25,	b = 82.45 ,	a = 71.17	b = 120.01,
	c = 123.18		c = 147.56
	α= β= γ= 90°		α= β= γ = 90°
Resolution Range	30.-2.3		20-2.8
Observations (Unique)	308126 (27968)		126333 (15680)
Completeness	95.7 (98.7)		98.3 (99.3)
I/σ	29.8 (3.4)		11.6 (3.1)
Rmerge %	5.2 (29)		5.5 (35)
Refinement Statistics
Resolution Range	30.-2.3		20-2.8
% Rfree	7		7
Rcryst Rfree	22.1 (26.2)		21.6 (27.5)
Protein atoms	3724		4124
Ligand atoms	93		58
Water Molecules	334		101
RMSD bonds/angles	0.0085/1.675		0.0171/1.807

[0376]

TABLE 2
ATOMIC COORDINATE DATA FOR CRYSTALLIZED HUMAN LXR
IN COMPLEX WITH SRC1 and EPC
	ATOM
ATOM	TYPE	RESIDUE	PROTEIN #	#	X	Y	Z	OCC	B
1	CB	ALA	A	218	28.344	16.106	96.698	1.00	55.76
2	C	ALA	A	218	29.653	18.044	95.802	1.00	55.24
3	O	ALA	A	218	30.106	18.364	94.699	1.00	54.28
4	N	ALA	A	218	27.664	17.216	94.572	1.00	64.79
5	CA	ALA	A	218	28.265	17.434	95.930	1.00	58.73
6	N	ALA	A	219	30.314	18.224	96.938	1.00	52.70
7	CA	ALA	A	219	31.664	18.775	96.947	1.00	51.55
8	CB	ALA	A	219	31.632	20.293	97.099	1.00	46.87
9	C	ALA	A	219	32.490	18.142	98.068	1.00	51.86
10	O	ALA	A	219	31.990	17.352	98.874	1.00	55.04
11	N	LEU	A	220	33.768	18.475	98.111	1.00	51.33
12	CA	LEU	A	220	34.644	17.936	99.143	1.00	45.85
13	CB	LEU	A	220	36.098	18.230	98.786	1.00	42.81
14	CG	LEU	A	220	36.953	16.990	98.618	1.00	45.64
15	CD1	LEU	A	220	36.552	16.276	97.358	1.00	47.27
16	CD2	LEU	A	220	38.412	17.371	98.575	1.00	40.99
17	C	LEU	A	220	34.316	18.571	100.497	1.00	43.50
18	O	LEU	A	220	34.040	19.755	100.599	1.00	47.45
19	N	THR	A	221	34.328	17.777	101.546	1.00	41.43
20	CA	THR	A	221	34.062	18.325	102.870	1.00	39.33
21	CB	THR	A	221	33.764	17.233	103.878	1.00	38.56
22	OG1	THR	A	221	34.797	16.239	103.820	1.00	37.25
23	CG2	THR	A	221	32.401	16.603	103.572	1.00	15.24
24	C	THR	A	221	35.317	19.037	103.331	1.00	39.68
25	O	THR	A	221	36.431	18.689	102.928	1.00	45.38
26	N	ALA	A	222	35.152	20.045	104.166	1.00	37.55
27	CA	ALA	A	222	36.325	20.774	104.604	1.00	37.06
28	CB	ALA	A	222	35.912	21.793	105.621	1.00	38.76
29	C	ALA	A	222	37.331	19.767	105.193	1.00	32.94
30	O	ALA	A	222	38.550	19.898	105.059	1.00	28.56
31	N	ALA	A	223	36.784	18.726	105.802	1.00	27.58
32	CA	ALA	A	223	37.588	17.699	106.412	1.00	23.17
33	CB	ALA	A	223	36.696	16.774	107.142	1.00	9.46
34	C	ALA	A	223	38.372	16.964	105.339	1.00	25.13
35	O	ALA	A	223	39.596	17.006	105.347	1.00	29.33
36	N	GLN	A	224	37.662	16.300	104.426	1.00	24.64
37	CA	GLN	A	224	38.289	15.570	103.341	1.00	30.36
38	CB	GLN	A	224	37.234	15.098	102.343	1.00	22.67
39	CG	GLN	A	224	36.338	14.029	102.858	1.00	32.52
40	CD	GLN	A	224	35.492	13.449	101.760	1.00	36.79
41	OE1	GLN	A	224	34.638	14.145	101.183	1.00	33.52
42	NE2	GLN	A	224	35.726	12.171	101.447	1.00	46.08
43	C	GLN	A	224	39.342	16.409	102.589	1.00	34.36
44	O	GLN	A	224	40.468	15.970	102.294	1.00	39.02
45	N	GLU	A	225	38.968	17.618	102.238	1.00	32.23
46	CA	GLU	A	225	39.909	18.444	101.544	1.00	31.48
47	CB	GLU	A	225	39.333	19.833	101.384	1.00	42.03
48	CG	GLU	A	225	39.876	20.576	100.206	1.00	52.07
49	CD	GLU	A	225	38.993	21.761	99.842	1.00	69.24
50	OE1	GLU	A	225	37.812	21.804	100.288	1.00	68.23
51	OE2	GLU	A	225	39.477	22.643	99.098	1.00	72.72
52	C	GLU	A	225	41.187	18.495	102.360	1.00	27.39
53	O	GLU	A	225	42.255	18.255	101.831	1.00	29.04
54	N	LEU	A	226	41.053	18.777	103.656	1.00	24.43
55	CA	LEU	A	226	42.187	18.897	104.560	1.00	20.16
56	CB	LEU	A	226	41.743	19.318	105.966	1.00	19.25
57	CG	LEU	A	226	42.892	19.672	106.914	1.00	15.29
58	CD1	LEU	A	226	43.785	20.719	106.248	1.00	20.10
59	CD2	LEU	A	226	42.349	20.229	108.205	1.00	25.61
60	C	LEU	A	226	42.939	17.605	104.640	1.00	20.54
61	O	LEU	A	226	44.159	17.598	104.723	1.00	21.73
62	N	MET	A	227	42.216	16.498	104.619	1.00	18.60
63	CA	MET	A	227	42.866	15.199	104.633	1.00	16.23
64	CB	MET	A	227	41.798	14.120	104.774	1.00	9.90
65	CG	MET	A	227	42.353	12.738	104.934	1.00	22.30
66	SD	MET	A	227	42.829	12.043	103.385	1.00	30.16
67	CE	MET	A	227	41.187	11.531	102.760	1.00	36.03
68	C	MET	A	227	43.659	15.005	103.291	1.00	20.80
69	O	MET	A	227	44.838	14.659	103.298	1.00	18.00
70	N	ILE	A	228	43.006	15.230	102.143	1.00	21.23
71	CA	ILE	A	228	43.658	15.076	100.846	1.00	15.74
72	CB	ILE	A	228	42.682	15.383	99.705	1.00	18.87
73	CG2	ILE	A	228	43.387	15.298	98.377	1.00	5.25
74	CG1	ILE	A	228	41.542	14.363	99.720	1.00	12.45
75	CD1	ILE	A	228	40.681	14.448	98.519	1.00	6.20
76	C	ILE	A	228	44.895	15.947	100.733	1.00	15.29
77	O	ILE	A	228	45.887	15.530	100.143	1.00	11.10
78	N	GLN	A	229	44.838	17.164	101.276	1.00	16.77
79	CA	GLN	A	229	46.021	18.028	101.289	1.00	20.67
80	CB	GLN	A	229	45.658	19.408	101.773	1.00	16.16
81	CG	GLN	A	229	45.235	20.307	100.632	1.00	34.86
82	CD	GLN	A	229	44.291	21.436	101.072	1.00	46.19
83	OE1	GLN	A	229	44.482	22.067	102.122	1.00	34.04
84	NE2	GLN	A	229	43.261	21.689	100.261	1.00	54.62
85	C	GLN	A	229	47.082	17.389	102.215	1.00	24.70
86	O	GLN	A	229	48.253	17.317	101.879	1.00	29.53
87	N	GLN	A	230	46.649	16.908	103.373	1.00	27.75
88	CA	GLN	A	230	47.488	16.213	104.345	1.00	23.86
89	CB	GLN	A	230	46.555	15.463	105.299	1.00	40.92
90	CG	GLN	A	230	47.000	15.206	106.716	1.00	55.66
91	CD	GLN	A	230	45.786	15.006	107.676	1.00	58.41
92	OE1	GLN	A	230	44.927	15.880	107.803	1.00	52.62
93	NE2	GLN	A	230	45.731	13.865	108.341	1.00	62.25
94	C	GLN	A	230	48.313	15.171	103.567	1.00	25.51
95	O	GLN	A	230	49.552	15.245	103.525	1.00	24.06
96	N	LEU	A	231	47.625	14.202	102.943	1.00	21.46
97	CA	LEU	A	231	48.301	13.139	102.232	1.00	15.10
98	CB	LEU	A	231	47.308	12.176	101.635	1.00	16.30
99	CG	LEU	A	231	46.835	11.054	102.539	1.00	14.70
100	CD1	LEU	A	231	46.032	10.109	101.662	1.00	8.73
101	CD2	LEU	A	231	48.022	10.358	103.175	1.00	5.25
102	C	LEU	A	231	49.236	13.598	101.153	1.00	17.13
103	O	LEU	A	231	50.390	13.147	101.103	1.00	15.46
104	N	VAL	A	232	48.762	14.491	100.281	1.00	16.95
105	CA	VAL	A	232	49.618	14.966	99.196	1.00	15.39
106	CB	VAL	A	232	48.910	15.936	98.252	1.00	14.04
107	CG1	VAL	A	232	49.911	16.605	97.355	1.00	5.25
108	CG2	VAL	A	232	47.911	15.167	97.411	1.00	11.19
109	C	VAL	A	232	50.856	15.624	99.728	1.00	17.28
110	O	VAL	A	232	51.942	15.446	99.155	1.00	19.63
111	N	ALA	A	233	50.711	16.371	100.824	1.00	15.96
112	CA	ALA	A	233	51.888	17.022	101.431	1.00	18.52
113	CB	ALA	A	233	51.455	18.052	102.445	1.00	8.26
114	C	ALA	A	233	52.835	15.979	102.086	1.00	19.61
115	O	ALA	A	233	54.056	15.958	101.822	1.00	16.98
116	N	ALA	A	234	52.281	15.112	102.935	1.00	25.82
117	CA	ALA	A	234	53.113	14.071	103.562	1.00	27.97
118	CB	ALA	A	234	52.231	13.130	104.444	1.00	20.72
119	C	ALA	A	234	53.870	13.249	102.486	1.00	25.67
120	O	ALA	A	234	55.023	12.833	102.703	1.00	24.36
121	N	GLN	A	235	53.214	13.017	101.341	1.00	22.92
122	CA	GLN	A	235	53.837	12.259	100.257	1.00	25.97
123	CB	GLN	A	235	52.802	11.886	99.207	1.00	21.78
124	CG	GLN	A	235	53.336	11.420	97.871	1.00	28.41
125	CD	GLN	A	235	52.180	10.969	96.901	1.00	47.75
126	OE1	GLN	A	235	51.692	9.827	96.976	1.00	41.32
127	NE2	GLN	A	235	51.735	11.883	96.010	1.00	47.47
128	C	GLN	A	235	54.983	13.028	99.629	1.00	25.13
129	O	GLN	A	235	55.934	12.453	99.163	1.00	29.39
130	N	LEU	A	236	54.893	14.343	99.657	1.00	24.34
131	CA	LEU	A	236	55.930	15.200	99.122	1.00	20.09
132	CB	LEU	A	236	55.352	16.601	98.944	1.00	10.48
133	CG	LEU	A	236	56.263	17.528	98.144	1.00	13.40
134	CD1	LEU	A	236	56.555	16.915	96.746	1.00	5.25
135	CD2	LEU	A	236	55.580	18.860	98.025	1.00	6.03
136	C	LEU	A	236	57.137	15.249	100.103	1.00	19.25
137	O	LEU	A	236	58.314	15.081	99.728	1.00	14.99
138	N	GLN	A	237	56.842	15.478	101.370	1.00	17.73
139	CA	GLN	A	237	57.912	15.546	102.341	1.00	22.68
140	CB	GLN	A	237	57.343	16.022	103.675	1.00	26.67
141	CG	GLN	A	237	57.937	17.332	104.108	1.00	47.77
142	CD	GLN	A	237	59.451	17.329	103.931	1.00	59.33
143	OE1	GLN	A	237	60.158	16.496	104.516	1.00	65.55
144	NE2	GLN	A	237	59.953	18.246	103.110	1.00	63.55
145	C	GLN	A	237	58.711	14.241	102.527	1.00	18.77
146	O	GLN	A	237	59.930	14.258	102.665	1.00	12.71
147	N	CYS	A	238	58.019	13.107	102.503	1.00	18.52
148	CA	CYS	A	238	58.692	11.837	102.720	1.00	18.81
149	CB	CYS	A	238	57.679	10.681	102.932	1.00	10.34
150	SG	CYS	A	238	56.626	10.868	104.440	1.00	14.23
151	C	CYS	A	238	59.584	11.589	101.537	1.00	15.55
152	O	CYS	A	238	60.658	11.034	101.689	1.00	14.18
153	N	ASN	A	239	59.144	12.032	100.362	1.00	16.15
154	CA	ASN	A	239	59.940	11.852	99.160	1.00	18.70
155	CB	ASN	A	239	59.146	12.265	97.909	1.00	15.21
156	CG	ASN	A	239	59.912	11.937	96.576	1.00	26.14
157	OD1	ASN	A	239	60.150	10.771	96.255	1.00	24.57
158	ND2	ASN	A	239	60.306	12.973	95.825	1.00	12.25
159	C	ASN	A	239	61.237	12.692	99.281	1.00	21.54
160	O	ASN	A	239	62.351	12.205	99.044	1.00	20.85
161	N	LYS	A	240	61.098	13.954	99.671	1.00	25.84
162	CA	LYS	A	240	62.270	14.804	99.837	1.00	28.12
163	CB	LYS	A	240	61.852	16.198	100.326	1.00	27.47
164	CG	LYS	A	240	61.294	17.128	99.251	1.00	39.34
165	CD	LYS	A	240	61.175	18.563	99.770	1.00	42.46
166	CE	LYS	A	240	60.827	19.600	98.682	1.00	38.29
167	NZ	LYS	A	240	60.961	21.029	99.186	1.00	34.56
168	C	LYS	A	240	63.220	14.163	100.856	1.00	29.54
169	O	LYS	A	240	64.428	14.092	100.655	1.00	31.96
170	N	ARG	A	241	62.655	13.657	101.938	1.00	31.83
171	CA	ARG	A	241	63.464	13.066	102.972	1.00	36.01
172	CB	ARG	A	241	62.639	12.909	104.235	1.00	45.49
173	CG	ARG	A	241	63.457	13.137	105.514	1.00	61.86
174	CD	ARG	A	241	62.558	13.336	106.725	1.00	73.10
175	NE	ARG	A	241	61.443	12.384	106.713	1.00	80.71
176	CZ	ARG	A	241	60.173	12.713	106.481	1.00	79.67
177	NH1	ARG	A	241	59.844	13.973	106.246	1.00	80.95
178	NH2	ARG	A	241	59.228	11.780	106.485	1.00	81.60
179	C	ARG	A	241	64.143	11.746	102.643	1.00	33.51
180	O	ARG	A	241	64.879	11.214	103.447	1.00	35.57
181	N	SER	A	242	63.933	11.223	101.455	1.00	31.82
182	CA	SER	A	242	64.566	9.975	101.102	1.00	27.53
183	CB	SER	A	242	63.518	8.881	100.876	1.00	16.61
184	OG	SER	A	242	63.011	8.316	102.079	1.00	24.71
185	C	SER	A	242	65.397	10.141	99.835	1.00	31.35
186	O	SER	A	242	66.444	9.486	99.685	1.00	36.01
187	N	PHE	A	243	64.948	11.015	98.929	1.00	28.64
188	CA	PHE	A	243	65.646	11.191	97.679	1.00	28.31
189	CB	PHE	A	243	64.738	10.714	96.551	1.00	26.61
190	CG	PHE	A	243	64.560	9.208	96.505	1.00	19.50
191	CD1	PHE	A	243	65.604	8.381	96.129	1.00	26.67
192	CD2	PHE	A	243	63.368	8.621	96.873	1.00	26.29
193	CE1	PHE	A	243	65.466	6.989	96.127	1.00	28.84
194	CE2	PHE	A	243	63.220	7.219	96.872	1.00	25.73
195	CZ	PHE	A	243	64.276	6.409	96.495	1.00	22.93
196	C	PHE	A	243	66.217	12.572	97.378	1.00	33.43
197	O	PHE	A	243	66.665	12.840	96.274	1.00	33.13
198	N	SER	A	244	66.219	13.448	98.368	1.00	38.40
199	CA	SER	A	244	66.809	14.751	98.167	1.00	43.23
200	CB	SER	A	244	66.403	15.675	99.279	1.00	37.51
201	OG	SER	A	244	65.058	16.045	99.054	1.00	61.16
202	C	SER	A	244	68.316	14.621	98.159	1.00	47.85
203	O	SER	A	244	69.009	15.613	97.995	1.00	53.73
204	N	ASP	A	245	68.819	13.400	98.339	1.00	50.07
205	CA	ASP	A	245	70.258	13.149	98.349	1.00	49.87
206	CB	ASP	A	245	70.710	12.722	99.756	1.00	47.69
207	CG	ASP	A	245	70.531	13.813	100.766	1.00	47.80
208	OD1	ASP	A	245	69.384	14.271	100.958	1.00	52.92
209	OD2	ASP	A	245	71.538	14.224	101.360	1.00	48.83
210	C	ASP	A	245	70.603	12.074	97.328	1.00	50.73
211	O	ASP	A	245	70.188	10.939	97.492	1.00	54.30
212	N	GLN	A	246	71.345	12.438	96.285	1.00	49.92
213	CA	GLN	A	246	71.698	11.485	95.270	1.00	53.86
214	CB	GLN	A	246	72.615	12.156	94.241	1.00	56.38
215	CG	GLN	A	246	71.730	12.876	93.183	1.00	66.03
216	CD	GLN	A	246	72.205	14.274	92.816	1.00	65.94
217	OE1	GLN	A	246	71.536	15.012	92.082	1.00	58.93
218	NE2	GLN	A	246	73.366	14.644	93.328	1.00	69.59
219	C	GLN	A	246	72.298	10.287	95.978	1.00	52.91
220	O	GLN	A	246	73.502	10.241	96.261	1.00	58.02
221	N	PRO	A	247	71.436	9.294	96.264	1.00	49.01
222	CD	PRO	A	247	70.165	9.186	95.511	1.00	44.83
223	CA	PRO	A	247	71.769	8.053	96.969	1.00	46.95
224	CB	PRO	A	247	70.749	7.035	96.473	1.00	47.91
225	CG	PRO	A	247	69.908	7.738	95.465	1.00	47.27
226	C	PRO	A	247	73.168	7.540	96.878	1.00	49.19
227	O	PRO	A	247	73.844	7.750	95.886	1.00	46.72
228	N	ALA	A	248	73.576	6.865	97.951	1.00	52.55
229	CA	ALA	A	248	74.918	6.318	98.045	1.00	53.13
230	CB	ALA	A	248	75.411	6.320	99.511	1.00	58.29
231	C	ALA	A	248	74.928	4.917	97.499	1.00	49.47
232	O	ALA	A	248	75.440	4.005	98.150	1.00	55.81
233	N	VAL	A	249	74.408	4.759	96.290	1.00	41.18
234	CA	VAL	A	249	74.342	3.444	95.717	1.00	40.05
235	CB	VAL	A	249	72.916	3.094	95.363	1.00	39.10
236	CG1	VAL	A	249	72.026	3.387	96.522	1.00	32.01
237	CG2	VAL	A	249	72.482	3.872	94.129	1.00	38.08
238	C	VAL	A	249	75.212	3.223	94.495	1.00	40.64
239	O	VAL	A	249	75.456	4.147	93.722	1.00	41.34
240	N	THR	A	250	75.680	1.982	94.368	1.00	36.01
241	CA	THR	A	250	76.510	1.535	93.283	1.00	37.57
242	CB	THR	A	250	76.282	0.055	93.103	1.00	37.83
243	OG1	THR	A	250	76.392	−0.569	94.376	1.00	33.70
244	CG2	THR	A	250	77.301	−0.554	92.146	1.00	39.78
245	C	THR	A	250	76.104	2.262	92.013	1.00	41.06
246	O	THR	A	250	74.927	2.280	91.655	1.00	43.68
247	N	PRO	A	251	77.068	2.862	91.305	1.00	42.94
248	CD	PRO	A	251	78.386	3.265	91.818	1.00	44.90
249	CA	PRO	A	251	76.757	3.590	90.065	1.00	45.01
250	CB	PRO	A	251	78.025	4.414	89.831	1.00	40.94
251	CG	PRO	A	251	78.528	4.647	91.208	1.00	44.44
252	C	PRO	A	251	76.405	2.713	88.848	1.00	44.95
253	O	PRO	A	251	76.944	1.628	88.678	1.00	47.75
254	N	TRP	A	252	75.511	3.203	88.005	1.00	40.56
255	CA	TRP	A	252	75.147	2.469	86.826	1.00	41.27
256	CB	TRP	A	252	73.933	3.143	86.195	1.00	45.59
257	CG	TRP	A	252	73.292	2.423	85.043	1.00	42.31
258	CD2	TRP	A	252	72.337	1.352	85.129	1.00	49.14
259	CE2	TRP	A	252	71.892	1.079	83.824	1.00	49.10
260	CE3	TRP	A	252	71.836	0.578	86.183	1.00	47.81
261	CD1	TRP	A	252	73.379	2.753	83.738	1.00	36.71
262	NE1	TRP	A	252	72.534	1.965	82.993	1.00	49.62
263	CZ2	TRP	A	252	70.933	0.092	83.541	1.00	43.00
264	CZ3	TRP	A	252	70.888	−0.402	85.897	1.00	47.13
265	CH2	TRP	A	252	70.461	−0.643	84.585	1.00	34.10
266	C	TRP	A	252	76.336	2.474	85.859	1.00	42.16
267	O	TRP	A	252	76.880	3.528	85.521	1.00	39.92
268	N	PRO	A	253	76.775	1.288	85.428	1.00	44.33
269	CD	PRO	A	253	76.530	−0.001	86.089	1.00	39.51
270	CA	PRO	A	253	77.905	1.217	84.493	1.00	50.55
271	CB	PRO	A	253	78.264	−0.266	84.476	1.00	46.99
272	CG	PRO	A	253	77.769	−0.777	85.744	1.00	44.13
273	C	PRO	A	253	77.552	1.725	83.089	1.00	54.78
274	O	PRO	A	253	76.562	2.427	82.902	1.00	54.13
275	N	LEU	A	254	78.364	1.327	82.108	1.00	61.04
276	CA	LEU	A	254	78.152	1.721	80.717	1.00	65.82
277	CB	LEU	A	254	78.874	3.041	80.447	1.00	64.47
278	CG	LEU	A	254	80.379	2.884	80.214	1.00	66.62
279	CD1	LEU	A	254	80.602	2.624	78.743	1.00	61.12
280	CD2	LEU	A	254	81.118	4.131	80.633	1.00	68.68
281	C	LEU	A	254	78.630	0.649	79.705	1.00	69.59
282	O	LEU	A	254	79.495	−0.198	80.002	1.00	72.20
283	N	ALA	A	259	81.190	−4.549	77.975	1.00	75.57
284	CA	ALA	A	259	80.352	−4.942	79.099	1.00	80.27
285	CB	ALA	A	259	78.962	−5.344	78.616	1.00	81.51
286	C	ALA	A	259	80.969	−6.073	79.932	1.00	81.62
287	O	ALA	A	259	82.008	−6.638	79.582	1.00	83.94
288	N	SER	A	260	80.305	−6.447	81.017	1.00	82.06
289	CA	SER	A	260	80.905	−7.445	81.859	1.00	81.46
290	CB	SER	A	260	82.196	−6.850	82.398	1.00	84.53
291	OG	SER	A	260	82.176	−5.432	82.266	1.00	83.98
292	C	SER	A	260	80.046	−7.901	83.006	1.00	81.71
293	O	SER	A	260	78.920	−7.458	83.166	1.00	84.27
294	N	ARG	A	261	80.617	−8.782	83.816	1.00	82.01
295	CA	ARG	A	261	79.938	−9.305	84.980	1.00	81.77
296	CB	ARG	A	261	80.493	−10.693	85.311	1.00	82.72
297	CG	ARG	A	261	80.331	−11.109	86.760	1.00	84.08
298	CD	ARG	A	261	81.677	−11.377	87.407	1.00	84.50
299	NE	ARG	A	261	81.918	−10.602	88.627	1.00	82.67
300	CZ	ARG	A	261	82.978	−9.818	88.788	1.00	82.29
301	NH1	ARG	A	261	83.856	−9.715	87.813	1.00	81.99
302	NH2	ARG	A	261	83.176	−9.162	89.919	1.00	82.23
303	C	ARG	A	261	80.064	−8.366	86.181	1.00	80.36
304	O	ARG	A	261	79.656	−8.718	87.268	1.00	83.44
305	N	ASP	A	262	80.610	−7.169	85.986	1.00	79.83
306	CA	ASP	A	262	80.751	−6.212	87.090	1.00	79.82
307	CB	ASP	A	262	82.137	−5.542	87.101	1.00	83.43
308	CG	ASP	A	262	82.926	−5.858	88.369	1.00	84.30
309	OD1	ASP	A	262	83.099	−7.063	88.672	1.00	83.98
310	OD2	ASP	A	262	83.376	−4.908	89.056	1.00	83.90
311	C	ASP	A	262	79.695	−5.151	86.972	1.00	79.08
312	O	ASP	A	262	79.499	−4.362	87.878	1.00	82.58
313	N	ALA	A	263	79.017	−5.140	85.835	1.00	77.24
314	CA	ALA	A	263	77.953	−4.182	85.612	1.00	74.16
315	CB	ALA	A	263	78.086	−3.558	84.236	1.00	75.62
316	C	ALA	A	263	76.657	−4.981	85.728	1.00	71.38
317	O	ALA	A	263	75.633	−4.485	86.230	1.00	70.95
318	N	ARG	A	264	76.718	−6.239	85.300	1.00	65.44
319	CA	ARG	A	264	75.545	−7.075	85.352	1.00	64.95
320	CB	ARG	A	264	75.782	−8.370	84.582	1.00	68.61
321	CG	ARG	A	264	74.496	−9.125	84.278	1.00	77.09
322	CD	ARG	A	264	74.746	−10.578	84.014	1.00	83.87
323	NE	ARG	A	264	74.515	−11.430	85.182	1.00	84.70
324	CZ	ARG	A	264	74.299	−12.732	85.081	1.00	84.41
325	NH1	ARG	A	264	74.286	−13.282	83.883	1.00	83.98
326	NH2	ARG	A	264	74.103	−13.475	86.162	1.00	85.25
327	C	ARG	A	264	75.268	−7.371	86.816	1.00	61.13
328	O	ARG	A	264	74.145	−7.746	87.199	1.00	60.64
329	N	GLN	A	265	76.309	−7.196	87.628	1.00	57.82
330	CA	GLN	A	265	76.197	−7.443	89.058	1.00	53.76
331	CB	GLN	A	265	77.310	−8.360	89.559	1.00	57.49
332	CG	GLN	A	265	76.829	−9.357	90.602	1.00	67.60
333	CD	GLN	A	265	75.542	−10.053	90.188	1.00	75.71
334	OE1	GLN	A	265	74.446	−9.525	90.398	1.00	82.27
335	NE2	GLN	A	265	75.669	−11.227	89.573	1.00	73.63
336	C	GLN	A	265	76.202	−6.145	89.806	1.00	48.27
337	O	GLN	A	265	75.943	−6.112	90.993	1.00	50.20
338	N	GLN	A	266	76.483	−5.067	89.089	1.00	44.20
339	CA	GLN	A	266	76.457	−3.726	89.667	1.00	39.57
340	CB	GLN	A	266	77.486	−2.803	89.028	1.00	43.03
341	CG	GLN	A	266	78.772	−2.635	89.794	1.00	53.90
342	CD	GLN	A	266	79.708	−1.641	89.098	1.00	62.90
343	OE1	GLN	A	266	79.394	−0.451	89.007	1.00	60.13
344	NE2	GLN	A	266	80.851	−2.128	88.595	1.00	60.44
345	C	GLN	A	266	75.082	−3.165	89.347	1.00	36.73
346	O	GLN	A	266	74.412	−2.637	90.214	1.00	34.43
347	N	ARG	A	267	74.659	−3.291	88.090	1.00	36.08
348	CA	ARG	A	267	73.365	−2.768	87.683	1.00	34.02
349	CB	ARG	A	267	73.007	−3.181	86.271	1.00	28.42
350	CG	ARG	A	267	73.888	−2.569	85.248	1.00	32.75
351	CD	ARG	A	267	73.805	−3.337	83.932	1.00	36.45
352	NE	ARG	A	267	74.755	−2.825	82.947	1.00	46.52
353	CZ	ARG	A	267	75.042	−3.431	81.810	1.00	45.30
354	NH1	ARG	A	267	74.451	−4.573	81.518	1.00	54.30
355	NH2	ARG	A	267	75.914	−2.882	80.978	1.00	54.13
356	C	ARG	A	267	72.354	−3.321	88.616	1.00	32.85
357	O	ARG	A	267	71.542	−2.585	89.167	1.00	38.40
358	N	PHE	A	268	72.413	−4.626	88.826	1.00	29.74
359	CA	PHE	A	268	71.448	−5.243	89.716	1.00	25.18
360	CB	PHE	A	268	71.669	−6.741	89.728	1.00	26.06
361	CG	PHE	A	268	70.906	−7.460	90.784	1.00	24.07
362	CD1	PHE	A	268	71.363	−7.455	92.103	1.00	23.22
363	CD2	PHE	A	268	69.758	−8.173	90.454	1.00	16.43
364	CE1	PHE	A	268	70.688	−8.150	93.084	1.00	31.48
365	CE2	PHE	A	268	69.049	−8.895	91.427	1.00	17.72
366	CZ	PHE	A	268	69.510	−8.888	92.745	1.00	34.32
367	C	PHE	A	268	71.523	−4.668	91.131	1.00	22.70
368	O	PHE	A	268	70.494	−4.537	91.820	1.00	19.53
369	N	ALA	A	269	72.741	−4.352	91.566	1.00	15.63
370	CA	ALA	A	269	72.930	−3.772	92.891	1.00	16.25
371	CB	ALA	A	269	74.408	−3.722	93.246	1.00	5.25
372	C	ALA	A	269	72.335	−2.351	92.884	1.00	18.99
373	O	ALA	A	269	71.718	−1.906	93.883	1.00	15.16
374	N	HIS	A	270	72.489	−1.670	91.738	1.00	18.91
375	CA	HIS	A	270	71.965	−0.321	91.562	1.00	19.16
376	CB	HIS	A	270	72.239	0.177	90.133	1.00	18.47
377	CG	HIS	A	270	71.953	1.641	89.932	1.00	24.67
378	CD2	HIS	A	270	70.993	2.282	89.213	1.00	20.88
379	ND1	HIS	A	270	72.663	2.630	90.579	1.00	21.21
380	CE1	HIS	A	270	72.149	3.811	90.277	1.00	24.56
381	NE2	HIS	A	270	71.134	3.626	89.449	1.00	23.56
382	C	HIS	A	270	70.444	−0.265	91.869	1.00	20.09
383	O	HIS	A	270	69.997	0.578	92.671	1.00	19.20
384	N	PHE	A	271	69.670	−1.161	91.246	1.00	17.60
385	CA	PHE	A	271	68.235	−1.190	91.452	1.00	12.83
386	CB	PHE	A	271	67.558	−2.153	90.474	1.00	13.28
387	CG	PHE	A	271	67.365	−1.602	89.089	1.00	15.11
388	CD1	PHE	A	271	66.499	−2.201	88.224	1.00	21.67
389	CD2	PHE	A	271	68.069	−0.514	88.649	1.00	19.45
390	CE1	PHE	A	271	66.340	−1.715	86.923	1.00	33.27
391	CE2	PHE	A	271	67.921	−0.026	87.361	1.00	23.53
392	CZ	PHE	A	271	67.062	−0.622	86.500	1.00	19.54
393	C	PHE	A	271	67.934	−1.632	92.872	1.00	15.62
394	O	PHE	A	271	67.206	−0.941	93.599	1.00	13.63
395	N	THR	A	272	68.508	−2.771	93.272	1.00	17.50
396	CA	THR	A	272	68.275	−3.325	94.605	1.00	21.01
397	CB	THR	A	272	69.110	−4.569	94.864	1.00	21.69
398	OG1	THR	A	272	70.479	−4.289	94.562	1.00	21.21
399	CG2	THR	A	272	68.589	−5.712	94.031	1.00	22.74
400	C	THR	A	272	68.541	−2.339	95.728	1.00	22.06
401	O	THR	A	272	67.720	−2.256	96.694	1.00	13.99
402	N	GLU	A	273	69.659	−1.598	95.593	1.00	21.82
403	CA	GLU	A	273	70.044	−0.592	96.600	1.00	22.04
404	CB	GLU	A	273	71.505	−0.134	96.432	1.00	16.72
405	CG	GLU	A	273	72.527	−1.268	96.656	1.00	20.48
406	CD	GLU	A	273	73.954	−0.888	96.301	1.00	32.58
407	OE1	GLU	A	273	74.798	−1.820	96.156	1.00	23.16
408	OE2	GLU	A	273	74.237	0.335	96.163	1.00	34.71
409	C	GLU	A	273	69.114	0.604	96.571	1.00	18.71
410	O	GLU	A	273	68.849	1.207	97.616	1.00	20.97
411	N	LEU	A	274	68.595	0.926	95.385	1.00	16.51
412	CA	LEU	A	274	67.663	2.043	95.255	1.00	14.99
413	CB	LEU	A	274	67.495	2.463	93.796	1.00	11.12
414	CG	LEU	A	274	68.698	3.147	93.150	1.00	13.55
415	CD1	LEU	A	274	68.600	3.124	91.642	1.00	5.25
416	CD2	LEU	A	274	68.776	4.556	93.678	1.00	20.85
417	C	LEU	A	274	66.321	1.591	95.837	1.00	19.28
418	O	LEU	A	274	65.687	2.291	96.614	1.00	24.78
419	N	ALA	A	275	65.882	0.395	95.496	1.00	21.07
420	CA	ALA	A	275	64.624	−0.091	96.054	1.00	20.24
421	CB	ALA	A	275	64.417	−1.544	95.647	1.00	14.28
422	C	ALA	A	275	64.582	0.046	97.593	1.00	20.13
423	O	ALA	A	275	63.547	0.420	98.159	1.00	15.46
424	N	ILE	A	276	65.693	−0.285	98.263	1.00	20.36
425	CA	ILE	A	276	65.769	−0.177	99.725	1.00	20.48
426	CB	ILE	A	276	67.244	−0.373	100.282	1.00	22.98
427	CG2	ILE	A	276	67.357	0.091	101.688	1.00	5.25
428	CG1	ILE	A	276	67.626	−1.848	100.300	1.00	13.96
429	CD1	ILE	A	276	69.078	−2.061	100.525	1.00	5.37
430	C	ILE	A	276	65.271	1.199	100.119	1.00	22.12
431	O	ILE	A	276	64.304	1.330	100.848	1.00	26.12
432	N	ILE	A	277	65.932	2.233	99.630	1.00	21.56
433	CA	ILE	A	277	65.513	3.585	99.969	1.00	21.63
434	CB	ILE	A	277	66.224	4.638	99.059	1.00	21.92
435	CG2	ILE	A	277	65.803	6.046	99.432	1.00	6.60
436	CG1	ILE	A	277	67.733	4.455	99.182	1.00	19.32
437	CD1	ILE	A	277	68.526	5.432	98.388	1.00	18.27
438	C	ILE	A	277	64.003	3.666	99.790	1.00	22.66
439	O	ILE	A	277	63.294	4.193	100.649	1.00	23.75
440	N	SER	A	278	63.512	3.128	98.675	1.00	21.69
441	CA	SER	A	278	62.074	3.158	98.421	1.00	25.15
442	CB	SER	A	278	61.729	2.477	97.092	1.00	27.78
443	OG	SER	A	278	60.337	2.601	96.802	1.00	14.94
444	C	SER	A	278	61.270	2.518	99.583	1.00	24.56
445	O	SER	A	278	60.235	3.081	100.039	1.00	26.24
446	N	VAL	A	279	61.737	1.371	100.074	1.00	19.27
447	CA	VAL	A	279	61.048	0.764	101.194	1.00	16.83
448	CB	VAL	A	279	61.719	−0.529	101.651	1.00	9.75
449	CG1	VAL	A	279	60.929	−1.142	102.780	1.00	5.43
450	CG2	VAL	A	279	61.760	−1.491	100.509	1.00	7.30
451	C	VAL	A	279	61.004	1.741	102.366	1.00	17.92
452	O	VAL	A	279	59.959	1.894	103.019	1.00	20.05
453	N	GLN	A	280	62.118	2.432	102.616	1.00	17.87
454	CA	GLN	A	280	62.178	3.382	103.738	1.00	22.98
455	CB	GLN	A	280	63.613	3.887	103.939	1.00	22.68
456	CG	GLN	A	280	64.583	2.771	104.299	1.00	25.49
457	CD	GLN	A	280	66.035	3.158	104.103	1.00	29.97
458	OE1	GLN	A	280	66.337	4.262	103.637	1.00	39.81
459	NE2	GLN	A	280	66.951	2.246	104.459	1.00	28.32
460	C	GLN	A	280	61.232	4.566	103.550	1.00	21.90
461	O	GLN	A	280	60.701	5.078	104.521	1.00	13.34
462	N	GLU	A	281	61.018	4.977	102.292	1.00	23.40
463	CA	GLU	A	281	60.131	6.097	101.978	1.00	20.00
464	CB	GLU	A	281	60.261	6.487	100.530	1.00	14.61
465	CG	GLU	A	281	59.269	7.591	100.132	1.00	21.34
466	CD	GLU	A	281	59.364	7.998	98.655	1.00	17.98
467	OE1	GLU	A	281	58.533	8.862	98.239	1.00	23.30
468	OE2	GLU	A	281	60.253	7.464	97.918	1.00	23.51
469	C	GLU	A	281	58.705	5.622	102.209	1.00	22.73
470	O	GLU	A	281	57.868	6.333	102.846	1.00	19.39
471	N	ILE	A	282	58.425	4.420	101.679	1.00	20.62
472	CA	ILE	A	282	57.108	3.827	101.853	1.00	17.79
473	CB	ILE	A	282	57.063	2.501	101.196	1.00	12.76
474	CG2	ILE	A	282	55.928	1.682	101.785	1.00	13.17
475	CG1	ILE	A	282	56.895	2.717	99.685	1.00	10.52
476	CD1	ILE	A	282	56.885	1.414	98.819	1.00	7.32
477	C	ILE	A	282	56.740	3.700	103.347	1.00	16.55
478	O	ILE	A	282	55.686	4.193	103.791	1.00	12.54
479	N	VAL	A	283	57.614	3.063	104.126	1.00	14.35
480	CA	VAL	A	283	57.353	2.949	105.545	1.00	17.95
481	CB	VAL	A	283	58.496	2.274	106.273	1.00	11.99
482	CG1	VAL	A	283	58.266	2.361	107.794	1.00	5.25
483	CG2	VAL	A	283	58.576	0.824	105.793	1.00	11.23
484	C	VAL	A	283	57.124	4.309	106.185	1.00	20.91
485	O	VAL	A	283	56.169	4.523	106.986	1.00	23.47
486	N	ASP	A	284	58.001	5.236	105.814	1.00	23.66
487	CA	ASP	A	284	57.948	6.601	106.326	1.00	22.91
488	CB	ASP	A	284	59.182	7.355	105.841	1.00	17.43
489	CG	ASP	A	284	59.127	8.811	106.144	1.00	22.55
490	OD1	ASP	A	284	58.431	9.194	107.093	1.00	42.17
491	OD2	ASP	A	284	59.783	9.607	105.443	1.00	36.89
492	C	ASP	A	284	56.623	7.306	105.955	1.00	23.76
493	O	ASP	A	284	56.040	8.009	106.788	1.00	27.90
494	N	PHE	A	285	56.123	7.086	104.744	1.00	17.48
495	CA	PHE	A	285	54.850	7.673	104.367	1.00	19.07
496	CB	PHE	A	285	54.732	7.647	102.853	1.00	16.30
497	CG	PHE	A	285	53.383	8.069	102.346	1.00	14.98
498	CD1	PHE	A	285	52.991	9.398	102.422	1.00	13.11
499	CD2	PHE	A	285	52.499	7.135	101.819	1.00	14.66
500	CE1	PHE	A	285	51.711	9.815	101.980	1.00	14.89
501	CE2	PHE	A	285	51.214	7.526	101.367	1.00	23.01
502	CZ	PHE	A	285	50.814	8.886	101.448	1.00	5.25
503	C	PHE	A	285	53.574	6.996	104.984	1.00	23.61
504	O	PHE	A	285	52.560	7.681	105.230	1.00	22.21
505	N	ALA	A	286	53.596	5.665	105.162	1.00	23.51
506	CA	ALA	A	286	52.444	4.964	105.757	1.00	27.50
507	CB	ALA	A	286	52.641	3.449	105.744	1.00	25.14
508	C	ALA	A	286	52.272	5.429	107.205	1.00	26.35
509	O	ALA	A	286	51.171	5.387	107.743	1.00	24.23
510	N	LYS	A	287	53.376	5.856	107.812	1.00	21.64
511	CA	LYS	A	287	53.385	6.337	109.173	1.00	20.78
512	CB	LYS	A	287	54.829	6.569	109.627	1.00	32.68
513	CG	LYS	A	287	55.557	5.394	110.287	1.00	16.23
514	CD	LYS	A	287	56.916	5.890	110.820	1.00	6.38
515	CE	LYS	A	287	57.643	4.797	111.544	1.00	20.16
516	NZ	LYS	A	287	58.945	5.307	112.046	1.00	34.26
517	C	LYS	A	287	52.650	7.648	109.252	1.00	18.44
518	O	LYS	A	287	52.266	8.100	110.313	1.00	11.43
519	N	GLN	A	288	52.481	8.263	108.100	1.00	21.42
520	CA	GLN	A	288	51.810	9.553	108.006	1.00	22.66
521	CB	GLN	A	288	52.539	10.411	106.980	1.00	29.15
522	CG	GLN	A	288	54.018	10.573	107.234	1.00	42.69
523	CD	GLN	A	288	54.304	11.694	108.176	1.00	49.48
524	OE1	GLN	A	288	55.423	12.173	108.258	1.00	74.17
525	NE2	GLN	A	288	53.292	12.138	108.883	1.00	51.28
526	C	GLN	A	288	50.350	9.409	107.581	1.00	21.76
527	O	GLN	A	288	49.603	10.383	107.656	1.00	27.23
528	N	VAL	A	289	49.953	8.211	107.129	1.00	19.79
529	CA	VAL	A	289	48.580	7.973	106.681	1.00	15.70
530	CB	VAL	A	289	48.488	6.742	105.759	1.00	13.08
531	CG1	VAL	A	289	47.074	6.556	105.298	1.00	6.01
532	CG2	VAL	A	289	49.404	6.935	104.572	1.00	15.89
533	C	VAL	A	289	47.722	7.798	107.921	1.00	14.36
534	O	VAL	A	289	47.875	6.848	108.678	1.00	10.54
535	N	PRO	A	290	46.835	8.766	108.171	1.00	14.08
536	CD	PRO	A	290	46.585	9.963	107.354	1.00	17.19
537	CA	PRO	A	290	45.948	8.749	109.327	1.00	15.24
538	CB	PRO	A	290	44.921	9.810	108.977	1.00	5.72
539	CG	PRO	A	290	45.719	10.783	108.275	1.00	16.05
540	C	PRO	A	290	45.321	7.387	109.524	1.00	21.69
541	O	PRO	A	290	44.658	6.880	108.633	1.00	27.78
542	N	GLY	A	291	45.508	6.827	110.715	1.00	21.98
543	CA	GLY	A	291	44.942	5.550	111.030	1.00	16.77
544	C	GLY	A	291	45.968	4.456	111.051	1.00	23.95
545	O	GLY	A	291	45.844	3.533	111.864	1.00	27.61
546	N	PHE	A	292	46.986	4.554	110.191	1.00	23.02
547	CA	PHE	A	292	47.999	3.503	110.135	1.00	23.53
548	CB	PHE	A	292	49.080	3.824	109.096	1.00	9.73
549	CG	PHE	A	292	49.971	2.675	108.803	1.00	5.25
550	CD1	PHE	A	292	49.524	1.613	108.044	1.00	5.25
551	CD2	PHE	A	292	51.234	2.610	109.359	1.00	9.44
552	CE1	PHE	A	292	50.337	0.490	107.860	1.00	8.02
553	CE2	PHE	A	292	52.089	1.473	109.177	1.00	5.29
554	CZ	PHE	A	292	51.647	0.429	108.441	1.00	6.77
555	C	PHE	A	292	48.654	3.216	111.486	1.00	25.20
556	O	PHE	A	292	48.712	2.072	111.939	1.00	28.15
557	N	LEU	A	293	49.125	4.250	112.163	1.00	26.45
558	CA	LEU	A	293	49.793	4.021	113.451	1.00	25.06
559	CB	LEU	A	293	50.565	5.278	113.875	1.00	12.77
560	CG	LEU	A	293	51.911	5.434	113.153	1.00	13.71
561	CD1	LEU	A	293	52.619	6.647	113.686	1.00	20.57
562	CD2	LEU	A	293	52.784	4.213	113.389	1.00	17.42
563	C	LEU	A	293	48.902	3.552	114.590	1.00	26.84
564	O	LEU	A	293	49.380	3.227	115.662	1.00	27.75
565	N	GLN	A	294	47.603	3.526	114.366	1.00	28.94
566	CA	GLN	A	294	46.703	3.072	115.406	1.00	29.14
567	CB	GLN	A	294	45.335	3.721	115.199	1.00	32.40
568	CG	GLN	A	294	45.373	5.200	115.308	1.00	34.00
569	CD	GLN	A	294	44.058	5.848	114.902	1.00	47.60
570	OE1	GLN	A	294	43.968	7.088	114.834	1.00	47.41
571	NE2	GLN	A	294	43.028	5.020	114.620	1.00	31.54
572	C	GLN	A	294	46.585	1.514	115.429	1.00	29.82
573	O	GLN	A	294	46.088	0.931	116.413	1.00	27.35
574	N	LEU	A	295	47.031	0.852	114.350	1.00	24.78
575	CA	LEU	A	295	46.983	−0.605	114.275	1.00	22.06
576	CB	LEU	A	295	47.075	−1.093	112.820	1.00	15.09
577	CG	LEU	A	295	45.917	−0.816	111.856	1.00	8.95
578	CD1	LEU	A	295	46.207	−1.416	110.509	1.00	5.25
579	CD2	LEU	A	295	44.645	−1.407	112.431	1.00	7.77
580	C	LEU	A	295	48.151	−1.169	115.083	1.00	24.15
581	O	LEU	A	295	48.938	−0.432	115.679	1.00	25.53
582	N	GLY	A	296	48.250	−2.484	115.123	1.00	25.20
583	CA	GLY	A	296	49.330	−3.105	115.860	1.00	25.00
584	C	GLY	A	296	50.530	−3.319	114.947	1.00	28.85
585	O	GLY	A	296	50.389	−3.560	113.738	1.00	30.52
586	N	ARG	A	297	51.723	−3.235	115.527	1.00	27.91
587	CA	ARG	A	297	52.934	−3.416	114.771	1.00	26.54
588	CB	ARG	A	297	54.135	−3.450	115.724	1.00	26.53
589	CG	ARG	A	297	54.646	−2.058	116.142	1.00	34.70
590	CD	ARG	A	297	55.192	−1.263	114.973	1.00	43.40
591	NE	ARG	A	297	55.933	−0.085	115.407	1.00	49.04
592	CZ	ARG	A	297	55.375	1.010	115.898	1.00	44.17
593	NH1	ARG	A	297	54.064	1.073	116.017	1.00	58.77
594	NH2	ARG	A	297	56.132	2.042	116.257	1.00	42.14
595	C	ARG	A	297	52.874	−4.661	113.882	1.00	25.01
596	O	ARG	A	297	53.394	−4.663	112.766	1.00	26.94
597	N	GLU	A	298	52.218	−5.708	114.355	1.00	22.09
598	CA	GLU	A	298	52.115	−6.923	113.556	1.00	24.63
599	CB	GLU	A	298	51.327	−8.010	114.290	1.00	28.37
600	CG	GLU	A	298	51.848	−8.340	115.658	1.00	37.88
601	CD	GLU	A	298	51.292	−7.409	116.740	1.00	55.37
602	OE1	GLU	A	298	50.070	−7.452	117.028	1.00	59.05
603	OE2	GLU	A	298	52.076	−6.614	117.307	1.00	70.02
604	C	GLU	A	298	51.389	−6.558	112.273	1.00	23.66
605	O	GLU	A	298	51.927	−6.676	111.158	1.00	20.63
606	N	ASP	A	299	50.155	−6.101	112.429	1.00	19.84
607	CA	ASP	A	299	49.390	−5.712	111.253	1.00	21.20
608	CB	ASP	A	299	47.983	−5.270	111.667	1.00	16.47
609	CG	ASP	A	299	47.028	−6.459	111.883	1.00	22.01
610	OD1	ASP	A	299	47.464	−7.631	111.711	1.00	20.27
611	OD2	ASP	A	299	45.834	−6.227	112.223	1.00	17.13
612	C	ASP	A	299	50.088	−4.619	110.406	1.00	18.39
613	O	ASP	A	299	49.886	−4.542	109.198	1.00	18.30
614	N	GLN	A	300	50.916	−3.784	111.024	1.00	17.35
615	CA	GLN	A	300	51.595	−2.747	110.259	1.00	15.73
616	CB	GLN	A	300	52.376	−1.789	111.169	1.00	9.88
617	CG	GLN	A	300	51.477	−0.866	111.981	1.00	27.45
618	CD	GLN	A	300	52.229	0.097	112.877	1.00	13.50
619	OE1	GLN	A	300	51.702	0.566	113.878	1.00	23.51
620	NE2	GLN	A	300	53.458	0.379	112.530	1.00	24.69
621	C	GLN	A	300	52.565	−3.470	109.338	1.00	17.34
622	O	GLN	A	300	52.778	−3.092	108.182	1.00	18.14
623	N	ILE	A	301	53.162	−4.533	109.843	1.00	12.85
624	CA	ILE	A	301	54.101	−5.236	109.016	1.00	14.59
625	CB	ILE	A	301	54.976	−6.165	109.893	1.00	15.16
626	CG2	ILE	A	301	55.820	−7.091	109.001	1.00	5.25
627	CG1	ILE	A	301	55.793	−5.274	110.855	1.00	8.71
628	CD1	ILE	A	301	56.769	−5.993	111.737	1.00	10.92
629	C	ILE	A	301	53.384	−5.993	107.909	1.00	15.65
630	O	ILE	A	301	53.741	−5.875	106.766	1.00	12.48
631	N	ALA	A	302	52.353	−6.747	108.274	1.00	20.32
632	CA	ALA	A	302	51.576	−7.519	107.322	1.00	19.51
633	CB	ALA	A	302	50.314	−8.081	107.978	1.00	20.40
634	C	ALA	A	302	51.188	−6.645	106.161	1.00	19.30
635	O	ALA	A	302	51.409	−7.008	104.998	1.00	21.12
636	N	LEU	A	303	50.603	−5.497	106.477	1.00	16.93
637	CA	LEU	A	303	50.151	−4.565	105.447	1.00	21.31
638	CB	LEU	A	303	49.373	−3.409	106.101	1.00	13.13
639	CG	LEU	A	303	48.157	−3.919	106.854	1.00	12.92
640	CD1	LEU	A	303	47.499	−2.757	107.493	1.00	18.24
641	CD2	LEU	A	303	47.195	−4.658	105.930	1.00	5.25
642	C	LEU	A	303	51.288	−3.996	104.578	1.00	21.60
643	O	LEU	A	303	51.241	−4.018	103.347	1.00	23.50
644	N	LEU	A	304	52.313	−3.496	105.240	1.00	20.10
645	CA	LEU	A	304	53.445	−2.897	104.567	1.00	17.11
646	CB	LEU	A	304	54.343	−2.249	105.620	1.00	11.01
647	CG	LEU	A	304	54.510	−0.741	105.558	1.00	18.49
648	CD1	LEU	A	304	55.287	−0.461	104.307	1.00	44.23
649	CD2	LEU	A	304	53.181	−0.015	105.462	1.00	20.96
650	C	LEU	A	304	54.208	−3.921	103.748	1.00	16.89
651	O	LEU	A	304	54.649	−3.658	102.635	1.00	20.67
652	N	LYS	A	305	54.360	−5.109	104.288	1.00	13.73
653	CA	LYS	A	305	55.091	−6.157	103.578	1.00	19.77
654	CB	LYS	A	305	55.291	−7.356	104.527	1.00	20.81
655	CG	LYS	A	305	55.946	−8.565	103.905	1.00	13.19
656	CD	LYS	A	305	55.916	−9.726	104.870	1.00	20.63
657	CE	LYS	A	305	56.306	−11.057	104.228	1.00	12.06
658	NZ	LYS	A	305	57.703	−11.055	103.799	1.00	19.00
659	C	LYS	A	305	54.438	−6.634	102.250	1.00	21.51
660	O	LYS	A	305	55.068	−7.200	101.387	1.00	18.05
661	N	ALA	A	306	53.155	−6.410	102.087	1.00	25.21
662	CA	ALA	A	306	52.491	−6.827	100.864	1.00	23.27
663	CB	ALA	A	306	51.124	−7.438	101.174	1.00	17.32
664	C	ALA	A	306	52.298	−5.650	99.914	1.00	23.06
665	O	ALA	A	306	52.172	−5.875	98.710	1.00	24.75
666	N	SER	A	307	52.287	−4.405	100.412	1.00	16.72
667	CA	SER	A	307	52.036	−3.328	99.481	1.00	18.89
668	CB	SER	A	307	51.075	−2.280	100.087	1.00	18.39
669	OG	SER	A	307	51.577	−1.640	101.231	1.00	27.27
670	C	SER	A	307	53.252	−2.673	98.893	1.00	18.47
671	O	SER	A	307	53.137	−1.896	97.952	1.00	17.24
672	N	THR	A	308	54.418	−3.007	99.431	1.00	20.42
673	CA	THR	A	308	55.652	−2.412	98.961	1.00	20.33
674	CB	THR	A	308	56.857	−2.970	99.677	1.00	26.07
675	OG1	THR	A	308	56.723	−2.675	101.072	1.00	15.84
676	CG2	THR	A	308	58.165	−2.380	99.109	1.00	11.95
677	C	THR	A	308	55.806	−2.623	97.491	1.00	24.21
678	O	THR	A	308	55.949	−1.639	96.768	1.00	31.09
679	N	ILE	A	309	55.736	−3.865	97.008	1.00	22.05
680	CA	ILE	A	309	55.885	−4.058	95.541	1.00	21.97
681	CB	ILE	A	309	55.970	−5.540	95.155	1.00	10.57
682	CG2	ILE	A	309	54.599	−6.187	95.213	1.00	10.35
683	CG1	ILE	A	309	56.457	−5.655	93.746	1.00	11.00
684	CD1	ILE	A	309	57.624	−4.806	93.430	1.00	15.31
685	C	ILE	A	309	54.741	−3.384	94.723	1.00	24.31
686	O	ILE	A	309	54.955	−2.796	93.647	1.00	26.07
687	N	GLU	A	310	53.531	−3.417	95.257	1.00	24.15
688	CA	GLU	A	310	52.445	−2.787	94.548	1.00	25.27
689	CB	GLU	A	310	51.100	−3.217	95.156	1.00	20.97
690	CG	GLU	A	310	50.768	−4.656	94.840	1.00	23.89
691	CD	GLU	A	310	49.495	−5.121	95.467	1.00	28.73
692	OE1	GLU	A	310	48.483	−4.411	95.287	1.00	30.31
693	OE2	GLU	A	310	49.510	−6.199	96.125	1.00	29.66
694	C	GLU	A	310	52.610	−1.262	94.528	1.00	23.80
695	O	GLU	A	310	52.459	−0.630	93.456	1.00	22.71
696	N	ILE	A	311	52.925	−0.688	95.698	1.00	21.18
697	CA	ILE	A	311	53.100	0.754	95.834	1.00	17.78
698	CB	ILE	A	311	53.420	1.153	97.270	1.00	22.01
699	CG2	ILE	A	311	53.731	2.670	97.360	1.00	14.47
700	CG1	ILE	A	311	52.256	0.772	98.180	1.00	20.79
701	CD1	ILE	A	311	52.456	1.225	99.620	1.00	5.25
702	C	ILE	A	311	54.264	1.183	94.951	1.00	17.83
703	O	ILE	A	311	54.210	2.226	94.286	1.00	17.78
704	N	MET	A	312	55.310	0.367	94.914	1.00	12.27
705	CA	MET	A	312	56.447	0.689	94.053	1.00	11.78
706	CB	MET	A	312	57.513	−0.410	94.128	1.00	8.84
707	CG	MET	A	312	58.406	−0.330	95.372	1.00	8.36
708	SD	MET	A	312	59.459	−1.748	95.526	1.00	13.68
709	CE	MET	A	312	60.895	−1.101	96.293	1.00	30.13
710	C	MET	A	312	55.954	0.817	92.605	1.00	15.28
711	O	MET	A	312	56.238	1.815	91.939	1.00	14.23
712	N	LEU	A	313	55.214	−0.196	92.126	1.00	17.47
713	CA	LEU	A	313	54.678	−0.171	90.750	1.00	12.93
714	CB	LEU	A	313	53.984	−1.497	90.424	1.00	6.84
715	CG	LEU	A	313	54.946	−2.670	90.488	1.00	12.50
716	CD1	LEU	A	313	54.187	−3.949	90.340	1.00	16.17
717	CD2	LEU	A	313	55.954	−2.535	89.413	1.00	8.29
718	C	LEU	A	313	53.699	1.012	90.568	1.00	14.27
719	O	LEU	A	313	53.483	1.516	89.448	1.00	9.22
720	N	LEU	A	314	53.078	1.461	91.656	1.00	11.10
721	CA	LEU	A	314	52.211	2.593	91.465	1.00	12.84
722	CB	LEU	A	314	51.379	2.877	92.725	1.00	6.93
723	CG	LEU	A	314	50.068	2.130	92.863	1.00	6.99
724	CD1	LEU	A	314	49.457	2.319	94.173	1.00	5.25
725	CD2	LEU	A	314	49.126	2.632	91.850	1.00	7.30
726	C	LEU	A	314	53.155	3.777	91.119	1.00	12.77
727	O	LEU	A	314	52.982	4.460	90.105	1.00	11.50
728	N	GLU	A	315	54.177	3.961	91.950	1.00	11.87
729	CA	GLU	A	315	55.124	5.042	91.770	1.00	16.53
730	CB	GLU	A	315	56.120	5.039	92.932	1.00	11.89
731	CG	GLU	A	315	55.605	5.607	94.194	1.00	5.25
732	CD	GLU	A	315	55.595	7.090	94.201	1.00	10.85
733	OE1	GLU	A	315	55.182	7.702	93.176	1.00	8.77
734	OE2	GLU	A	315	55.999	7.645	95.248	1.00	17.41
735	C	GLU	A	315	55.865	4.976	90.426	1.00	16.97
736	O	GLU	A	315	56.052	6.002	89.730	1.00	17.98
737	N	THR	A	316	56.293	3.768	90.083	1.00	17.59
738	CA	THR	A	316	56.990	3.522	88.833	1.00	17.43
739	CB	THR	A	316	57.280	2.030	88.672	1.00	17.51
740	OG1	THR	A	316	57.863	1.527	89.884	1.00	30.83
741	CG2	THR	A	316	58.265	1.826	87.594	1.00	18.88
742	C	THR	A	316	56.081	4.003	87.710	1.00	11.80
743	O	THR	A	316	56.517	4.648	86.758	1.00	9.81
744	N	ALA	A	317	54.793	3.735	87.862	1.00	10.77
745	CA	ALA	A	317	53.840	4.147	86.849	1.00	16.37
746	CB	ALA	A	317	52.475	3.546	87.136	1.00	5.38
747	C	ALA	A	317	53.744	5.667	86.802	1.00	18.32
748	O	ALA	A	317	53.894	6.257	85.754	1.00	19.63
749	N	ARG	A	318	53.471	6.288	87.944	1.00	19.01
750	CA	ARG	A	318	53.340	7.728	88.018	1.00	20.43
751	CB	ARG	A	318	53.127	8.163	89.480	1.00	17.68
752	CG	ARG	A	318	53.723	9.553	89.752	1.00	26.39
753	CD	ARG	A	318	53.215	10.206	91.009	1.00	28.62
754	NE	ARG	A	318	53.609	9.530	92.240	1.00	10.50
755	CZ	ARG	A	318	53.102	9.861	93.417	1.00	16.96
756	NH1	ARG	A	318	52.228	10.843	93.456	1.00	13.30
757	NH2	ARG	A	318	53.424	9.199	94.539	1.00	11.73
758	C	ARG	A	318	54.565	8.450	87.438	1.00	22.34
759	O	ARG	A	318	54.467	9.564	86.933	1.00	21.25
760	N	ARG	A	319	55.713	7.793	87.488	1.00	21.35
761	CA	ARG	A	319	56.956	8.375	87.032	1.00	17.87
762	CB	ARG	A	319	58.045	7.931	88.022	1.00	20.75
763	CG	ARG	A	319	58.387	8.951	89.050	1.00	24.12
764	CD	ARG	A	319	58.545	8.402	90.431	1.00	17.36
765	NE	ARG	A	319	58.607	9.508	91.410	1.00	32.94
766	CZ	ARG	A	319	57.991	9.447	92.577	1.00	33.79
767	NH1	ARG	A	319	57.317	8.346	92.849	1.00	43.26
768	NH2	ARG	A	319	58.024	10.456	93.438	1.00	52.22
769	C	ARG	A	319	57.323	7.982	85.620	1.00	18.49
770	O	ARG	A	319	58.478	8.158	85.184	1.00	20.42
771	N	TYR	A	320	56.350	7.422	84.906	1.00	18.20
772	CA	TYR	A	320	56.550	6.958	83.520	1.00	14.45
773	CB	TYR	A	320	55.609	5.815	83.236	1.00	13.95
774	CG	TYR	A	320	55.706	5.312	81.847	1.00	8.19
775	CD1	TYR	A	320	54.719	5.611	80.913	1.00	8.08
776	CE1	TYR	A	320	54.753	5.056	79.620	1.00	17.06
777	CD2	TYR	A	320	56.756	4.459	81.475	1.00	19.62
778	CE2	TYR	A	320	56.819	3.888	80.178	1.00	18.44
779	CZ	TYR	A	320	55.803	4.187	79.265	1.00	17.55
780	OH	TYR	A	320	55.806	3.578	78.037	1.00	21.89
781	C	TYR	A	320	56.333	8.003	82.467	1.00	13.03
782	O	TYR	A	320	55.356	8.730	82.499	1.00	9.85
783	N	ASN	A	321	57.247	8.044	81.518	1.00	17.48
784	CA	ASN	A	321	57.208	9.010	80.425	1.00	24.17
785	CB	ASN	A	321	58.621	9.556	80.231	1.00	22.33
786	CG	ASN	A	321	58.745	10.434	79.018	1.00	35.24
787	OD1	ASN	A	321	58.104	10.210	77.977	1.00	42.91
788	ND2	ASN	A	321	59.602	11.432	79.126	1.00	40.28
789	C	ASN	A	321	56.732	8.291	79.149	1.00	30.47
790	O	ASN	A	321	57.365	7.343	78.722	1.00	30.73
791	N	HIS	A	322	55.657	8.755	78.514	1.00	34.71
792	CA	HIS	A	322	55.162	8.076	77.324	1.00	41.59
793	CB	HIS	A	322	53.701	8.431	77.059	1.00	54.29
794	CG	HIS	A	322	53.408	9.909	76.990	1.00	76.97
795	CD2	HIS	A	322	53.251	10.730	75.920	1.00	80.64
796	ND1	HIS	A	322	53.153	10.696	78.102	1.00	85.25
797	CE1	HIS	A	322	52.850	11.927	77.721	1.00	83.58
798	NE2	HIS	A	322	52.904	11.973	76.400	1.00	84.03
799	C	HIS	A	322	55.967	8.288	76.065	1.00	43.58
800	O	HIS	A	322	56.226	7.349	75.317	1.00	44.52
801	N	GLU	A	323	56.400	9.512	75.840	1.00	44.35
802	CA	GLU	A	323	57.174	9.799	74.656	1.00	46.93
803	CB	GLU	A	323	57.410	11.297	74.538	1.00	56.88
804	CG	GLU	A	323	57.359	12.013	75.886	1.00	75.19
805	CD	GLU	A	323	57.518	13.517	75.759	1.00	83.55
806	OE1	GLU	A	323	58.552	13.965	75.194	1.00	84.32
807	OE2	GLU	A	323	56.604	14.250	76.212	1.00	85.25
808	C	GLU	A	323	58.494	9.064	74.667	1.00	44.24
809	O	GLU	A	323	58.897	8.550	73.625	1.00	46.47
810	N	THR	A	324	59.148	8.979	75.833	1.00	36.96
811	CA	THR	A	324	60.461	8.325	75.921	1.00	31.82
812	CB	THR	A	324	61.419	9.124	76.811	1.00	28.94
813	OG1	THR	A	324	61.147	8.850	78.192	1.00	43.62
814	CG2	THR	A	324	61.247	10.617	76.565	1.00	42.78
815	C	THR	A	324	60.450	6.876	76.410	1.00	32.14
816	O	THR	A	324	61.486	6.156	76.345	1.00	19.90
817	N	GLU	A	325	59.260	6.449	76.848	1.00	33.70
818	CA	GLU	A	325	59.017	5.099	77.386	1.00	33.30
819	CB	GLU	A	325	59.101	4.047	76.270	1.00	39.05
820	CG	GLU	A	325	57.997	4.113	75.234	1.00	41.63
821	CD	GLU	A	325	57.894	2.822	74.473	1.00	48.98
822	OE1	GLU	A	325	57.333	1.843	75.016	1.00	67.31
823	OE2	GLU	A	325	58.402	2.755	73.344	1.00	53.65
824	C	GLU	A	325	59.966	4.711	78.541	1.00	29.19
825	O	GLU	A	325	60.150	3.541	78.819	1.00	29.37
826	N	CYS	A	326	60.543	5.708	79.210	1.00	24.41
827	CA	CYS	A	326	61.463	5.464	80.303	1.00	19.33
828	CB	CYS	A	326	62.771	6.209	80.096	1.00	19.88
829	SG	CYS	A	326	63.687	5.503	78.803	1.00	24.37
830	C	CYS	A	326	60.903	5.860	81.623	1.00	15.95
831	O	CYS	A	326	60.151	6.805	81.730	1.00	14.68
832	N	ILE	A	327	61.278	5.114	82.647	1.00	16.97
833	CA	ILE	A	327	60.772	5.412	83.970	1.00	20.52
834	CB	ILE	A	327	60.439	4.135	84.761	1.00	22.42
835	CG2	ILE	A	327	60.222	4.478	86.226	1.00	8.74
836	CG1	ILE	A	327	59.173	3.497	84.183	1.00	16.37
837	CD1	ILE	A	327	58.975	2.088	84.631	1.00	22.14
838	C	ILE	A	327	61.875	6.156	84.655	1.00	22.73
839	O	ILE	A	327	62.994	5.654	84.796	1.00	26.08
840	N	THR	A	328	61.584	7.373	85.062	1.00	19.96
841	CA	THR	A	328	62.618	8.139	85.713	1.00	19.11
842	CB	THR	A	328	62.740	9.541	85.056	1.00	11.47
843	OG1	THR	A	328	63.358	10.424	85.985	1.00	12.92
844	CG2	THR	A	328	61.417	10.084	84.701	1.00	12.27
845	C	THR	A	328	62.366	8.236	87.245	1.00	18.38
846	O	THR	A	328	61.446	8.922	87.717	1.00	14.72
847	N	PHE	A	329	63.183	7.517	88.006	1.00	16.51
848	CA	PHE	A	329	63.082	7.513	89.443	1.00	18.38
849	CB	PHE	A	329	64.105	6.547	90.027	1.00	18.29
850	CG	PHE	A	329	64.090	5.188	89.405	1.00	19.31
851	CD1	PHE	A	329	63.067	4.818	88.522	1.00	13.87
852	CD2	PHE	A	329	65.075	4.242	89.743	1.00	16.73
853	CE1	PHE	A	329	63.000	3.509	87.971	1.00	7.96
854	CE2	PHE	A	329	65.027	2.934	89.207	1.00	9.29
855	CZ	PHE	A	329	63.975	2.572	88.314	1.00	7.44
856	C	PHE	A	329	63.339	8.870	90.069	1.00	22.72
857	O	PHE	A	329	62.549	9.343	90.833	1.00	18.85
858	N	LEU	A	330	64.460	9.486	89.721	1.00	27.93
859	CA	LEU	A	330	64.873	10.747	90.316	1.00	30.76
860	CB	LEU	A	330	66.148	10.534	91.130	1.00	34.14
861	CG	LEU	A	330	66.044	10.077	92.550	1.00	29.90
862	CD1	LEU	A	330	67.392	10.061	93.207	1.00	44.27
863	CD2	LEU	A	330	65.150	11.082	93.251	1.00	53.47
864	C	LEU	A	330	65.242	11.663	89.216	1.00	35.80
865	O	LEU	A	330	64.976	11.335	88.068	1.00	34.20
866	N	LYS	A	331	65.830	12.821	89.555	1.00	39.21
867	CA	LYS	A	331	66.315	13.677	88.481	1.00	40.72
868	CB	LYS	A	331	66.344	15.172	88.848	1.00	42.67
869	CG	LYS	A	331	67.703	15.843	88.676	1.00	51.34
870	CD	LYS	A	331	67.770	16.800	87.501	1.00	53.38
871	CE	LYS	A	331	69.185	17.325	87.365	1.00	50.95
872	NZ	LYS	A	331	69.369	18.028	86.053	1.00	59.13
873	C	LYS	A	331	67.706	13.039	88.232	1.00	38.02
874	O	LYS	A	331	68.390	12.532	89.142	1.00	38.56
875	N	ASP	A	332	68.088	13.082	86.972	1.00	36.23
876	CA	ASP	A	332	69.246	12.404	86.422	1.00	35.75
877	CB	ASP	A	332	70.597	13.264	86.339	1.00	36.31
878	CG	ASP	A	332	71.188	13.706	87.656	1.00	43.37
879	OD1	ASP	A	332	72.125	13.010	88.122	1.00	55.31
880	OD2	ASP	A	332	70.770	14.763	88.198	1.00	45.32
881	C	ASP	A	332	69.377	10.932	86.923	1.00	32.13
882	O	ASP	A	332	70.442	10.431	87.220	1.00	33.64
883	N	PHE	A	333	68.241	10.219	86.921	1.00	30.11
884	CA	PHE	A	333	68.083	8.766	87.334	1.00	30.48
885	CB	PHE	A	333	67.696	8.577	88.831	1.00	19.29
886	CG	PHE	A	333	68.863	8.544	89.783	1.00	21.29
887	CD1	PHE	A	333	69.532	7.343	90.010	1.00	16.07
888	CD2	PHE	A	333	69.302	9.722	90.446	1.00	12.63
889	CE1	PHE	A	333	70.632	7.289	90.878	1.00	16.55
890	CE2	PHE	A	333	70.384	9.699	91.310	1.00	16.16
891	CZ	PHE	A	333	71.064	8.476	91.536	1.00	16.98
892	C	PHE	A	333	66.920	8.119	86.552	1.00	28.27
893	O	PHE	A	333	65.862	7.807	87.135	1.00	33.02
894	N	THR	A	334	67.139	7.860	85.270	1.00	23.48
895	CA	THR	A	334	66.115	7.295	84.392	1.00	24.00
896	CB	THR	A	334	65.828	8.337	83.276	1.00	20.94
897	OG1	THR	A	334	65.314	9.524	83.895	1.00	18.52
898	CG2	THR	A	334	64.816	7.839	82.271	1.00	17.24
899	C	THR	A	334	66.448	5.906	83.803	1.00	21.68
900	O	THR	A	334	67.595	5.599	83.563	1.00	20.97
901	N	TYR	A	335	65.442	5.071	83.581	1.00	18.64
902	CA	TYR	A	335	65.697	3.741	83.045	1.00	19.91
903	CB	TYR	A	335	65.763	2.728	84.203	1.00	18.15
904	CG	TYR	A	335	66.664	3.239	85.335	1.00	19.69
905	CD1	TYR	A	335	68.052	3.132	85.244	1.00	9.91
906	CE1	TYR	A	335	68.888	3.773	86.128	1.00	16.03
907	CD2	TYR	A	335	66.134	3.993	86.382	1.00	12.55
908	CE2	TYR	A	335	66.948	4.638	87.264	1.00	21.32
909	CZ	TYR	A	335	68.331	4.543	87.130	1.00	22.31
910	OH	TYR	A	335	69.130	5.334	87.921	1.00	14.35
911	C	TYR	A	335	64.668	3.320	81.995	1.00	21.65
912	O	TYR	A	335	63.458	3.601	82.094	1.00	25.19
913	N	SER	A	336	65.188	2.659	80.972	1.00	21.19
914	CA	SER	A	336	64.408	2.168	79.852	1.00	19.61
915	CB	SER	A	336	65.292	2.113	78.639	1.00	15.94
916	OG	SER	A	336	66.198	1.026	78.795	1.00	17.24
917	C	SER	A	336	63.993	0.751	80.156	1.00	22.31
918	O	SER	A	336	64.309	0.216	81.203	1.00	22.32
919	N	LYS	A	337	63.308	0.114	79.224	1.00	27.92
920	CA	LYS	A	337	62.927	−1.267	79.471	1.00	32.61
921	CB	LYS	A	337	61.992	−1.794	78.378	1.00	38.84
922	CG	LYS	A	337	60.512	−1.671	78.689	1.00	45.22
923	CD	LYS	A	337	59.685	−2.866	78.099	1.00	37.58
924	CE	LYS	A	337	58.528	−2.372	77.209	1.00	33.90
925	NZ	LYS	A	337	57.646	−3.499	76.797	1.00	26.57
926	C	LYS	A	337	64.220	−2.089	79.447	1.00	32.43
927	O	LYS	A	337	64.463	−2.938	80.297	1.00	31.18
928	N	ASP	A	338	65.062	−1.826	78.459	1.00	34.81
929	CA	ASP	A	338	66.281	−2.587	78.357	1.00	33.25
930	CB	ASP	A	338	67.003	−2.294	77.048	1.00	31.70
931	CG	ASP	A	338	68.258	−3.122	76.918	1.00	46.29
932	OD1	ASP	A	338	68.187	−4.373	77.017	1.00	52.08
933	OD2	ASP	A	338	69.338	−2.540	76.732	1.00	52.04
934	C	ASP	A	338	67.200	−2.355	79.561	1.00	31.99
935	O	ASP	A	338	68.063	−3.187	79.872	1.00	32.73
936	N	ASP	A	339	67.027	−1.240	80.260	1.00	29.20
937	CA	ASP	A	339	67.854	−1.030	81.439	1.00	26.90
938	CB	ASP	A	339	67.660	0.380	81.977	1.00	28.69
939	CG	ASP	A	339	68.254	1.424	81.060	1.00	29.23
940	OD1	ASP	A	339	69.450	1.260	80.684	1.00	24.71
941	OD2	ASP	A	339	67.534	2.408	80.719	1.00	32.90
942	C	ASP	A	339	67.492	−2.070	82.498	1.00	26.21
943	O	ASP	A	339	68.363	−2.587	83.209	1.00	29.03
944	N	PHE	A	340	66.196	−2.374	82.568	1.00	27.72
945	CA	PHE	A	340	65.616	−3.365	83.475	1.00	26.22
946	CB	PHE	A	340	64.096	−3.345	83.346	1.00	28.71
947	CG	PHE	A	340	63.452	−2.309	84.162	1.00	26.69
948	CD1	PHE	A	340	62.458	−2.656	85.044	1.00	24.75
949	CD2	PHE	A	340	63.870	−0.989	84.092	1.00	29.16
950	CE1	PHE	A	340	61.884	−1.703	85.865	1.00	16.74
951	CE2	PHE	A	340	63.312	−0.041	84.896	1.00	22.67
952	CZ	PHE	A	340	62.315	−0.400	85.789	1.00	25.21
953	C	PHE	A	340	66.115	−4.746	83.098	1.00	30.07
954	O	PHE	A	340	66.430	−5.561	83.970	1.00	32.54
955	N	HIS	A	341	66.178	−5.020	81.794	1.00	29.06
956	CA	HIS	A	341	66.667	−6.307	81.388	1.00	33.09
957	CB	HIS	A	341	66.523	−6.501	79.894	1.00	41.29
958	CG	HIS	A	341	66.697	−7.923	79.493	1.00	51.69
959	CD2	HIS	A	341	66.108	−9.044	79.972	1.00	62.95
960	ND1	HIS	A	341	67.639	−8.343	78.579	1.00	60.58
961	CE1	HIS	A	341	67.626	−9.664	78.516	1.00	67.99
962	NE2	HIS	A	341	66.706	−10.113	79.355	1.00	74.79
963	C	HIS	A	341	68.131	−6.416	81.781	1.00	30.10
964	O	HIS	A	341	68.564	−7.399	82.397	1.00	33.29
965	N	ARG	A	342	68.885	−5.383	81.435	1.00	26.27
966	CA	ARG	A	342	70.297	−5.350	81.751	1.00	27.76
967	CB	ARG	A	342	70.910	−4.034	81.307	1.00	21.84
968	CG	ARG	A	342	71.231	−3.988	79.842	1.00	33.15
969	CD	ARG	A	342	72.195	−2.884	79.494	1.00	37.97
970	NE	ARG	A	342	71.933	−2.375	78.148	1.00	56.61
971	CZ	ARG	A	342	71.144	−1.332	77.893	1.00	57.88
972	NH1	ARG	A	342	70.552	−0.694	78.890	1.00	63.90
973	NH2	ARG	A	342	70.934	−0.931	76.643	1.00	54.40
974	C	ARG	A	342	70.472	−5.505	83.246	1.00	32.21
975	O	ARG	A	342	71.322	−6.289	83.719	1.00	37.76
976	N	ALA	A	343	69.652	−4.761	83.989	1.00	29.12
977	CA	ALA	A	343	69.688	−4.793	85.445	1.00	26.57
978	CB	ALA	A	343	68.664	−3.819	85.987	1.00	24.89
979	C	ALA	A	343	69.483	−6.202	86.064	1.00	26.96
980	O	ALA	A	343	69.650	−6.372	87.271	1.00	25.29
981	N	GLY	A	344	69.106	−7.188	85.246	1.00	24.87
982	CA	GLY	A	344	68.944	−8.544	85.743	1.00	23.67
983	C	GLY	A	344	67.535	−9.089	85.737	1.00	27.67
984	O	GLY	A	344	67.341	−10.318	85.803	1.00	25.72
985	N	LEU	A	345	66.551	−8.188	85.650	1.00	27.49
986	CA	LEU	A	345	65.135	−8.578	85.670	1.00	24.58
987	CB	LEU	A	345	64.258	−7.342	85.811	1.00	23.55
988	CG	LEU	A	345	64.619	−6.367	86.941	1.00	15.50
989	CD1	LEU	A	345	63.839	−5.038	86.748	1.00	19.24
990	CD2	LEU	A	345	64.305	−6.978	88.234	1.00	20.63
991	C	LEU	A	345	64.671	−9.347	84.453	1.00	23.25
992	O	LEU	A	345	65.177	−9.156	83.368	1.00	23.62
993	N	GLN	A	346	63.695	−10.218	84.663	1.00	23.03
994	CA	GLN	A	346	63.075	−11.031	83.605	1.00	23.05
995	CB	GLN	A	346	62.269	−12.178	84.208	1.00	21.66
996	CG	GLN	A	346	63.072	−13.195	84.943	1.00	40.94
997	CD	GLN	A	346	62.269	−14.431	85.340	1.00	38.02
998	OE1	GLN	A	346	61.264	−14.330	86.050	1.00	26.11
999	NE2	GLN	A	346	62.719	−15.605	84.883	1.00	38.61
1000	C	GLN	A	346	62.064	−10.237	82.740	1.00	24.22
1001	O	GLN	A	346	61.293	−9.377	83.240	1.00	13.82
1002	N	VAL	A	347	62.057	−10.566	81.447	1.00	25.45
1003	CA	VAL	A	347	61.136	−9.952	80.483	1.00	24.56
1004	CB	VAL	A	347	61.344	−10.578	79.024	1.00	23.19
1005	CG1	VAL	A	347	60.788	−11.989	78.959	1.00	21.34
1006	CG2	VAL	A	347	60.655	−9.760	77.970	1.00	10.36
1007	C	VAL	A	347	59.705	−10.260	80.989	1.00	26.68
1008	O	VAL	A	347	58.768	−9.520	80.752	1.00	28.59
1009	N	GLU	A	348	59.562	−11.370	81.700	1.00	28.04
1010	CA	GLU	A	348	58.280	−11.800	82.242	1.00	26.61
1011	CB	GLU	A	348	58.448	−13.098	83.028	1.00	31.77
1012	CG	GLU	A	348	59.539	−14.015	82.550	1.00	33.06
1013	CD	GLU	A	348	59.186	−14.628	81.283	1.00	37.73
1014	OE1	GLU	A	348	58.072	−15.170	81.211	1.00	45.41
1015	OE2	GLU	A	348	60.011	−14.568	80.354	1.00	60.92
1016	C	GLU	A	348	57.744	−10.761	83.200	1.00	23.96
1017	O	GLU	A	348	56.551	−10.584	83.297	1.00	24.06
1018	N	PHE	A	349	58.646	−10.119	83.932	1.00	22.08
1019	CA	PHE	A	349	58.295	−9.085	84.910	1.00	24.53
1020	CB	PHE	A	349	59.303	−9.138	86.082	1.00	14.36
1021	CG	PHE	A	349	58.951	−8.259	87.217	1.00	9.71
1022	CD1	PHE	A	349	57.638	−8.190	87.673	1.00	16.13
1023	CD2	PHE	A	349	59.932	−7.572	87.908	1.00	14.92
1024	CE1	PHE	A	349	57.301	−7.453	88.820	1.00	5.25
1025	CE2	PHE	A	349	59.609	−6.823	89.075	1.00	13.59
1026	CZ	PHE	A	349	58.284	−6.775	89.524	1.00	7.02
1027	C	PHE	A	349	58.256	−7.659	84.283	1.00	25.25
1028	O	PHE	A	349	57.298	−6.926	84.448	1.00	23.80
1029	N	ILE	A	350	59.313	−7.294	83.565	1.00	25.82
1030	CA	ILE	A	350	59.458	−6.005	82.885	1.00	22.66
1031	CB	ILE	A	350	60.763	−6.071	82.038	1.00	22.42
1032	CG2	ILE	A	350	60.996	−4.796	81.233	1.00	14.30
1033	CG1	ILE	A	350	61.922	−6.374	82.962	1.00	10.32
1034	CD1	ILE	A	350	63.165	−6.731	82.164	1.00	13.28
1035	C	ILE	A	350	58.252	−5.582	81.982	1.00	26.39
1036	O	ILE	A	350	57.647	−4.504	82.146	1.00	19.95
1037	N	ASN	A	351	57.899	−6.418	81.012	1.00	27.99
1038	CA	ASN	A	351	56.769	−6.070	80.143	1.00	26.87
1039	CB	ASN	A	351	56.474	−7.190	79.134	1.00	20.91
1040	CG	ASN	A	351	57.688	−7.516	78.253	1.00	26.68
1041	OD1	ASN	A	351	58.301	−6.645	77.665	1.00	21.67
1042	ND2	ASN	A	351	58.030	−8.781	78.174	1.00	41.74
1043	C	ASN	A	351	55.499	−5.714	80.925	1.00	20.74
1044	O	ASN	A	351	54.935	−4.656	80.698	1.00	23.26
1045	N	PRO	A	352	55.043	−6.580	81.855	1.00	18.21
1046	CD	PRO	A	352	55.479	−7.970	82.083	1.00	12.88
1047	CA	PRO	A	352	53.830	−6.290	82.639	1.00	17.05
1048	CB	PRO	A	352	53.740	−7.479	83.592	1.00	13.45
1049	CG	PRO	A	352	54.232	−8.584	82.780	1.00	5.25
1050	C	PRO	A	352	53.872	−4.943	83.386	1.00	18.19
1051	O	PRO	A	352	52.828	−4.249	83.490	1.00	12.42
1052	N	ILE	A	353	55.059	−4.553	83.879	1.00	17.57
1053	CA	ILE	A	353	55.125	−3.280	84.574	1.00	17.31
1054	CB	ILE	A	353	56.360	−3.127	85.516	1.00	14.06
1055	CG2	ILE	A	353	57.262	−4.287	85.470	1.00	20.72
1056	CG1	ILE	A	353	57.037	−1.816	85.222	1.00	16.47
1057	CD1	ILE	A	353	58.349	−1.669	85.959	1.00	30.09
1058	C	ILE	A	353	55.043	−2.100	83.608	1.00	16.16
1059	O	ILE	A	353	54.418	−1.061	83.893	1.00	19.52
1060	N	PHE	A	354	55.623	−2.260	82.437	1.00	17.20
1061	CA	PHE	A	354	55.541	−1.161	81.496	1.00	16.87
1062	CB	PHE	A	354	56.611	−1.296	80.428	1.00	15.75
1063	CG	PHE	A	354	57.961	−0.845	80.907	1.00	26.72
1064	CD1	PHE	A	354	58.624	−1.554	81.933	1.00	26.43
1065	CD2	PHE	A	354	58.542	0.320	80.404	1.00	14.53
1066	CE1	PHE	A	354	59.839	−1.104	82.452	1.00	15.82
1067	CE2	PHE	A	354	59.759	0.781	80.915	1.00	20.30
1068	CZ	PHE	A	354	60.410	0.081	81.934	1.00	23.97
1069	C	PHE	A	354	54.164	−1.113	80.892	1.00	16.64
1070	O	PHE	A	354	53.646	−0.048	80.543	1.00	15.01
1071	N	GLU	A	355	53.538	−2.275	80.819	1.00	17.82
1072	CA	GLU	A	355	52.205	−2.313	80.279	1.00	24.65
1073	CB	GLU	A	355	51.784	−3.751	79.975	1.00	27.67
1074	CG	GLU	A	355	51.021	−3.888	78.666	1.00	54.83
1075	CD	GLU	A	355	50.285	−2.598	78.291	1.00	73.11
1076	OE1	GLU	A	355	50.069	−2.330	77.083	1.00	70.34
1077	OE2	GLU	A	355	49.912	−1.833	79.206	1.00	84.30
1078	C	GLU	A	355	51.276	−1.684	81.325	1.00	25.67
1079	O	GLU	A	355	50.267	−1.008	81.025	1.00	25.52
1080	N	PHE	A	356	51.637	−1.878	82.580	1.00	24.31
1081	CA	PHE	A	356	50.807	−1.331	83.628	1.00	21.24
1082	CB	PHE	A	356	51.186	−1.932	84.954	1.00	16.93
1083	CG	PHE	A	356	50.490	−1.315	86.093	1.00	9.37
1084	CD1	PHE	A	356	49.216	−1.697	86.425	1.00	11.26
1085	CD2	PHE	A	356	51.113	−0.325	86.834	1.00	12.62
1086	CE1	PHE	A	356	48.560	−1.097	87.490	1.00	5.27
1087	CE2	PHE	A	356	50.459	0.285	87.901	1.00	6.44
1088	CZ	PHE	A	356	49.187	−0.104	88.225	1.00	6.39
1089	C	PHE	A	356	50.980	0.152	83.699	1.00	18.18
1090	O	PHE	A	356	50.013	0.863	84.023	1.00	12.84
1091	N	SER	A	357	52.210	0.606	83.419	1.00	18.00
1092	CA	SER	A	357	52.527	2.037	83.442	1.00	20.63
1093	CB	SER	A	357	54.005	2.263	83.194	1.00	24.68
1094	OG	SER	A	357	54.765	1.848	84.302	1.00	28.70
1095	C	SER	A	357	51.721	2.819	82.408	1.00	20.09
1096	O	SER	A	357	51.288	3.946	82.673	1.00	24.68
1097	N	ARG	A	358	51.493	2.208	81.242	1.00	21.71
1098	CA	ARG	A	358	50.709	2.849	80.169	1.00	20.24
1099	CB	ARG	A	358	50.932	2.135	78.816	1.00	21.60
1100	CG	ARG	A	358	52.392	2.178	78.364	1.00	24.91
1101	CD	ARG	A	358	52.695	1.483	77.018	1.00	22.98
1102	NE	ARG	A	358	53.676	0.374	77.211	1.00	49.01
1103	CZ	ARG	A	358	53.385	−0.942	77.152	1.00	46.01
1104	NH1	ARG	A	358	52.145	−1.326	76.877	1.00	36.77
1105	NH2	ARG	A	358	54.306	−1.879	77.438	1.00	30.95
1106	C	ARG	A	358	49.240	2.855	80.533	1.00	16.71
1107	O	ARG	A	358	48.528	3.825	80.293	1.00	16.15
1108	N	ALA	A	359	48.789	1.756	81.111	1.00	15.42
1109	CA	ALA	A	359	47.401	1.699	81.547	1.00	18.48
1110	CB	ALA	A	359	47.100	0.379	82.201	1.00	23.61
1111	C	ALA	A	359	47.197	2.844	82.535	1.00	17.14
1112	O	ALA	A	359	46.214	3.581	82.437	1.00	18.07
1113	N	MET	A	360	48.147	3.008	83.455	1.00	14.89
1114	CA	MET	A	360	48.054	4.064	84.433	1.00	17.42
1115	CB	MET	A	360	49.222	3.999	85.432	1.00	17.61
1116	CG	MET	A	360	49.061	2.921	86.502	1.00	7.42
1117	SD	MET	A	360	47.353	2.918	87.350	1.00	12.36
1118	CE	MET	A	360	47.562	3.990	88.630	1.00	10.71
1119	C	MET	A	360	47.964	5.455	83.824	1.00	18.28
1120	O	MET	A	360	47.105	6.239	84.223	1.00	20.28
1121	N	ARG	A	361	48.827	5.791	82.867	1.00	23.50
1122	CA	ARG	A	361	48.727	7.123	82.279	1.00	27.99
1123	CB	ARG	A	361	49.824	7.340	81.304	1.00	24.17
1124	CG	ARG	A	361	49.598	8.583	80.524	1.00	44.39
1125	CD	ARG	A	361	50.186	8.387	79.148	1.00	59.94
1126	NE	ARG	A	361	49.637	9.089	77.971	1.00	68.19
1127	CZ	ARG	A	361	48.781	8.514	77.124	1.00	77.06
1128	NH1	ARG	A	361	48.328	7.287	77.353	1.00	83.36
1129	NH2	ARG	A	361	48.565	9.036	75.926	1.00	80.65
1130	C	ARG	A	361	47.403	7.323	81.554	1.00	33.07
1131	O	ARG	A	361	46.895	8.439	81.468	1.00	35.79
1132	N	ARG	A	362	46.845	6.227	81.040	1.00	36.68
1133	CA	ARG	A	362	45.581	6.257	80.331	1.00	35.83
1134	CB	ARG	A	362	45.220	4.855	79.858	1.00	35.29
1135	CG	ARG	A	362	45.220	4.707	78.335	1.00	44.87
1136	CD	ARG	A	362	46.405	3.842	77.844	1.00	40.38
1137	NE	ARG	A	362	46.373	2.547	78.520	1.00	42.89
1138	CZ	ARG	A	362	45.455	1.598	78.326	1.00	26.47
1139	NH1	ARG	A	362	44.502	1.775	77.469	1.00	39.65
1140	NH2	ARG	A	362	45.461	0.473	79.017	1.00	26.69
1141	C	ARG	A	362	44.457	6.806	81.203	1.00	36.78
1142	O	ARG	A	362	43.420	7.264	80.692	1.00	44.96
1143	N	LEU	A	363	44.650	6.764	82.516	1.00	29.80
1144	CA	LEU	A	363	43.626	7.256	83.418	1.00	20.73
1145	CB	LEU	A	363	43.556	6.345	84.644	1.00	21.21
1146	CG	LEU	A	363	43.163	4.913	84.314	1.00	16.69
1147	CD1	LEU	A	363	42.805	4.215	85.616	1.00	28.55
1148	CD2	LEU	A	363	41.984	4.911	83.364	1.00	15.22
1149	C	LEU	A	363	43.849	8.721	83.831	1.00	15.12
1150	O	LEU	A	363	42.945	9.375	84.411	1.00	6.97
1151	N	GLY	A	364	45.051	9.218	83.534	1.00	12.82
1152	CA	GLY	A	364	45.398	10.597	83.845	1.00	16.60
1153	C	GLY	A	364	45.244	11.000	85.292	1.00	20.61
1154	O	GLY	A	364	44.613	12.037	85.593	1.00	17.13
1155	N	LEU	A	365	45.832	10.187	86.176	1.00	17.04
1156	CA	LEU	A	365	45.768	10.460	87.593	1.00	18.84
1157	CB	LEU	A	365	46.081	9.182	88.396	1.00	27.56
1158	CG	LEU	A	365	45.349	7.845	88.116	1.00	31.11
1159	CD1	LEU	A	365	45.398	6.989	89.364	1.00	30.39
1160	CD2	LEU	A	365	43.901	8.072	87.747	1.00	34.95
1161	C	LEU	A	365	46.730	11.560	88.023	1.00	18.09
1162	O	LEU	A	365	47.822	11.706	87.504	1.00	15.59
1163	N	ASP	A	366	46.331	12.335	89.017	1.00	20.32
1164	CA	ASP	A	366	47.214	13.390	89.529	1.00	20.40
1165	CB	ASP	A	366	46.470	14.701	89.665	1.00	16.78
1166	CG	ASP	A	366	45.278	14.567	90.521	1.00	23.28
1167	OD1	ASP	A	366	45.399	13.745	91.473	1.00	15.63
1168	OD2	ASP	A	366	44.258	15.279	90.245	1.00	18.63
1169	C	ASP	A	366	47.788	13.010	90.893	1.00	22.44
1170	O	ASP	A	366	47.699	11.858	91.347	1.00	22.65
1171	N	ASP	A	367	48.350	13.990	91.570	1.00	21.06
1172	CA	ASP	A	367	48.991	13.728	92.845	1.00	19.97
1173	CB	ASP	A	367	49.820	14.962	93.171	1.00	23.70
1174	CG	ASP	A	367	50.605	15.436	91.953	1.00	33.51
1175	OD1	ASP	A	367	51.760	14.973	91.788	1.00	32.01
1176	OD2	ASP	A	367	50.043	16.231	91.133	1.00	42.88
1177	C	ASP	A	367	48.033	13.316	93.991	1.00	18.37
1178	O	ASP	A	367	48.382	12.443	94.831	1.00	13.39
1179	N	ALA	A	368	46.812	13.870	93.969	1.00	14.31
1180	CA	ALA	A	368	45.829	13.569	95.010	1.00	10.24
1181	CB	ALA	A	368	44.677	14.566	94.991	1.00	5.25
1182	C	ALA	A	368	45.278	12.183	94.839	1.00	12.43
1183	O	ALA	A	368	45.058	11.445	95.798	1.00	12.82
1184	N	GLU	A	369	45.035	11.825	93.596	1.00	13.07
1185	CA	GLU	A	369	44.465	10.518	93.299	1.00	10.95
1186	CB	GLU	A	369	43.991	10.490	91.852	1.00	10.95
1187	CG	GLU	A	369	43.173	11.761	91.522	1.00	22.49
1188	CD	GLU	A	369	42.698	11.845	90.103	1.00	22.08
1189	OE1	GLU	A	369	43.571	11.824	89.189	1.00	15.56
1190	OE2	GLU	A	369	41.452	11.923	89.933	1.00	12.69
1191	C	GLU	A	369	45.492	9.450	93.577	1.00	11.12
1192	O	GLU	A	369	45.152	8.419	94.123	1.00	13.47
1193	N	TYR	A	370	46.760	9.692	93.255	1.00	8.69
1194	CA	TYR	A	370	47.778	8.683	93.538	1.00	9.43
1195	CB	TYR	A	370	49.137	9.069	92.949	1.00	13.30
1196	CG	TYR	A	370	49.432	8.500	91.586	1.00	16.34
1197	CD1	TYR	A	370	49.209	9.234	90.429	1.00	13.30
1198	CE1	TYR	A	370	49.548	8.742	89.210	1.00	6.00
1199	CD2	TYR	A	370	49.985	7.247	91.463	1.00	21.23
1200	CE2	TYR	A	370	50.313	6.725	90.234	1.00	18.57
1201	CZ	TYR	A	370	50.101	7.469	89.103	1.00	20.19
1202	OH	TYR	A	370	50.417	6.900	87.871	1.00	19.47
1203	C	TYR	A	370	47.926	8.547	95.038	1.00	11.30
1204	O	TYR	A	370	47.928	7.480	95.575	1.00	12.12
1205	N	ALA	A	371	48.027	9.658	95.734	1.00	16.86
1206	CA	ALA	A	371	48.202	9.549	97.163	1.00	18.13
1207	CB	ALA	A	371	48.167	10.925	97.793	1.00	16.28
1208	C	ALA	A	371	47.062	8.692	97.698	1.00	19.18
1209	O	ALA	A	371	47.258	7.734	98.469	1.00	17.78
1210	N	LEU	A	372	45.856	9.055	97.277	1.00	19.78
1211	CA	LEU	A	372	44.662	8.354	97.725	1.00	19.88
1212	CB	LEU	A	372	43.394	9.032	97.187	1.00	14.68
1213	CG	LEU	A	372	42.962	10.355	97.835	1.00	19.94
1214	CD1	LEU	A	372	41.729	10.902	97.146	1.00	10.85
1215	CD2	LEU	A	372	42.651	10.108	99.298	1.00	7.68
1216	C	LEU	A	372	44.656	6.868	97.332	1.00	22.11
1217	O	LEU	A	372	44.215	6.002	98.141	1.00	22.03
1218	N	LEU	A	373	45.175	6.552	96.133	1.00	15.88
1219	CA	LEU	A	373	45.137	5.166	95.695	1.00	10.66
1220	CB	LEU	A	373	45.372	5.030	94.196	1.00	8.65
1221	CG	LEU	A	373	44.655	3.840	93.598	1.00	6.32
1222	CD1	LEU	A	373	43.285	4.260	93.208	1.00	5.25
1223	CD2	LEU	A	373	45.422	3.376	92.400	1.00	20.15
1224	C	LEU	A	373	46.136	4.329	96.433	1.00	10.85
1225	O	LEU	A	373	45.889	3.129	96.632	1.00	14.08
1226	N	ILE	A	374	47.261	4.946	96.812	1.00	5.25
1227	CA	ILE	A	374	48.303	4.281	97.562	1.00	5.25
1228	CB	ILE	A	374	49.596	5.099	97.509	1.00	6.11
1229	CG2	ILE	A	374	50.633	4.644	98.594	1.00	5.25
1230	CG1	ILE	A	374	50.210	4.921	96.129	1.00	5.25
1231	CD1	ILE	A	374	51.473	5.732	95.921	1.00	9.93
1232	C	ILE	A	374	47.800	4.089	99.012	1.00	8.80
1233	O	ILE	A	374	48.045	3.061	99.644	1.00	10.51
1234	N	ALA	A	375	47.051	5.045	99.538	1.00	11.95
1235	CA	ALA	A	375	46.522	4.857	100.879	1.00	11.55
1236	CB	ALA	A	375	45.772	6.112	101.348	1.00	18.37
1237	C	ALA	A	375	45.565	3.673	100.810	1.00	10.74
1238	O	ALA	A	375	45.736	2.692	101.512	1.00	12.44
1239	N	ILE	A	376	44.541	3.781	99.971	1.00	13.36
1240	CA	ILE	A	376	43.581	2.698	99.808	1.00	12.40
1241	CB	ILE	A	376	42.740	2.935	98.541	1.00	9.26
1242	CG2	ILE	A	376	42.041	1.644	98.135	1.00	18.71
1243	CG1	ILE	A	376	41.751	4.087	98.775	1.00	13.00
1244	CD1	ILE	A	376	40.978	4.478	97.474	1.00	17.97
1245	C	ILE	A	376	44.306	1.338	99.702	1.00	12.50
1246	O	ILE	A	376	43.886	0.343	100.249	1.00	14.22
1247	N	ASN	A	377	45.431	1.305	99.014	1.00	15.95
1248	CA	ASN	A	377	46.217	0.075	98.837	1.00	12.41
1249	CB	ASN	A	377	47.332	0.356	97.817	1.00	15.42
1250	CG	ASN	A	377	48.167	−0.873	97.487	1.00	13.49
1251	OD1	ASN	A	377	49.214	−1.104	98.085	1.00	20.76
1252	ND2	ASN	A	377	47.721	−1.650	96.522	1.00	5.51
1253	C	ASN	A	377	46.822	−0.480	100.124	1.00	12.71
1254	O	ASN	A	377	46.791	−1.665	100.344	1.00	12.86
1255	N	ILE	A	378	47.389	0.386	100.951	1.00	9.60
1256	CA	ILE	A	378	48.007	−0.007	102.208	1.00	11.48
1257	CB	ILE	A	378	48.557	1.254	102.953	1.00	13.42
1258	CG2	ILE	A	378	48.991	0.911	104.337	1.00	10.38
1259	CG1	ILE	A	378	49.731	1.847	102.176	1.00	14.54
1260	CD1	ILE	A	378	50.045	3.250	102.595	1.00	5.25
1261	C	ILE	A	378	47.018	−0.709	103.143	1.00	11.55
1262	O	ILE	A	378	47.382	−1.633	103.867	1.00	9.06
1263	N	PHE	A	379	45.775	−0.244	103.141	1.00	10.61
1264	CA	PHE	A	379	44.724	−0.812	103.989	1.00	12.29
1265	CB	PHE	A	379	43.781	0.293	104.436	1.00	7.47
1266	CG	PHE	A	379	44.440	1.315	105.268	1.00	11.02
1267	CD1	PHE	A	379	44.988	0.966	106.506	1.00	9.62
1268	CD2	PHE	A	379	44.434	2.646	104.866	1.00	11.32
1269	CE1	PHE	A	379	45.520	1.966	107.363	1.00	15.85
1270	CE2	PHE	A	379	44.951	3.653	105.686	1.00	18.67
1271	CZ	PHE	A	379	45.494	3.313	106.949	1.00	21.51
1272	C	PHE	A	379	43.914	−1.918	103.334	1.00	10.55
1273	O	PHE	A	379	42.677	−1.881	103.303	1.00	9.28
1274	N	SER	A	380	44.610	−2.909	102.810	1.00	13.88
1275	CA	SER	A	380	43.917	−4.015	102.177	1.00	17.32
1276	CB	SER	A	380	44.777	−4.563	101.039	1.00	22.85
1277	OG	SER	A	380	44.923	−3.634	99.988	1.00	11.41
1278	C	SER	A	380	43.699	−5.094	103.259	1.00	17.60
1279	O	SER	A	380	44.653	−5.748	103.690	1.00	17.72
1280	N	ALA	A	381	42.464	−5.273	103.719	1.00	17.30
1281	CA	ALA	A	381	42.195	−6.283	104.761	1.00	19.73
1282	CB	ALA	A	381	40.707	−6.274	105.140	1.00	21.74
1283	C	ALA	A	381	42.613	−7.724	104.431	1.00	18.37
1284	O	ALA	A	381	43.094	−8.438	105.304	1.00	22.04
1285	N	ASP	A	382	42.438	−8.141	103.178	1.00	14.77
1286	CA	ASP	A	382	42.754	−9.486	102.772	1.00	13.45
1287	CB	ASP	A	382	42.035	−9.807	101.457	1.00	13.39
1288	CG	ASP	A	382	42.630	−9.082	100.246	1.00	30.72
1289	OD1	ASP	A	382	43.378	−8.081	100.397	1.00	22.68
1290	OD2	ASP	A	382	42.334	−9.519	99.114	1.00	32.64
1291	C	ASP	A	382	44.238	−9.803	102.667	1.00	17.62
1292	O	ASP	A	382	44.605	−10.924	102.314	1.00	20.22
1293	N	ARG	A	383	45.110	−8.851	102.988	1.00	19.53
1294	CA	ARG	A	383	46.551	−9.137	102.878	1.00	22.22
1295	CB	ARG	A	383	47.426	−7.940	103.264	1.00	23.58
1296	CG	ARG	A	383	47.195	−6.716	102.426	1.00	35.26
1297	CD	ARG	A	383	47.697	−6.851	101.005	1.00	25.29
1298	NE	ARG	A	383	47.636	−5.552	100.332	1.00	23.14
1299	CZ	ARG	A	383	48.123	−5.319	99.126	1.00	23.43
1300	NH1	ARG	A	383	48.710	−6.289	98.461	1.00	27.91
1301	NH2	ARG	A	383	48.006	−4.121	98.580	1.00	27.85
1302	C	ARG	A	383	46.831	−10.242	103.839	1.00	18.57
1303	O	ARG	A	383	46.226	−10.305	104.920	1.00	25.15
1304	N	PRO	A	384	47.748	−11.131	103.473	1.00	16.47
1305	CD	PRO	A	384	48.511	−11.130	102.214	1.00	12.46
1306	CA	PRO	A	384	48.114	−12.259	104.335	1.00	14.68
1307	CB	PRO	A	384	49.348	−12.827	103.651	1.00	5.25
1308	CG	PRO	A	384	49.058	−12.518	102.173	1.00	5.25
1309	C	PRO	A	384	48.422	−11.868	105.799	1.00	19.79
1310	O	PRO	A	384	49.046	−10.820	106.076	1.00	27.07
1311	N	ASN	A	385	47.966	−12.706	106.729	1.00	20.14
1312	CA	ASN	A	385	48.279	−12.565	108.159	1.00	20.58
1313	CB	ASN	A	385	49.832	−12.711	108.399	1.00	20.36
1314	CG	ASN	A	385	50.474	−13.822	107.532	1.00	31.32
1315	OD1	ASN	A	385	50.776	−13.633	106.344	1.00	41.94
1316	ND2	ASN	A	385	50.647	−14.986	108.121	1.00	25.03
1317	C	ASN	A	385	47.749	−11.326	108.886	1.00	17.40
1318	O	ASN	A	385	48.181	−10.969	109.977	1.00	12.75
1319	N	VAL	A	386	46.797	−10.650	108.302	1.00	17.19
1320	CA	VAL	A	386	46.284	−9.501	109.029	1.00	17.88
1321	CB	VAL	A	386	45.340	−8.669	108.150	1.00	15.50
1322	CG1	VAL	A	386	44.750	−7.581	108.934	1.00	10.72
1323	CG2	VAL	A	386	46.087	−8.154	106.923	1.00	13.81
1324	C	VAL	A	386	45.513	−10.006	110.268	1.00	21.92
1325	O	VAL	A	386	44.720	−10.957	110.214	1.00	20.83
1326	N	GLN	A	387	45.761	−9.372	111.400	1.00	26.53
1327	CA	GLN	A	387	45.084	−9.753	112.637	1.00	30.70
1328	CB	GLN	A	387	45.891	−9.282	113.836	1.00	37.12
1329	CG	GLN	A	387	46.969	−10.223	114.318	1.00	44.09
1330	CD	GLN	A	387	47.415	−9.894	115.738	1.00	47.02
1331	OE1	GLN	A	387	48.257	−10.592	116.289	1.00	48.50
1332	NE2	GLN	A	387	46.846	−8.825	116.338	1.00	39.63
1333	C	GLN	A	387	43.685	−9.129	112.729	1.00	30.34
1334	O	GLN	A	387	42.701	−9.777	113.055	1.00	31.77
1335	N	GLU	A	388	43.619	−7.850	112.424	1.00	25.71
1336	CA	GLU	A	388	42.381	−7.135	112.477	1.00	20.29
1337	CB	GLU	A	388	42.582	−5.990	113.437	1.00	15.19
1338	CG	GLU	A	388	43.133	−6.517	114.737	1.00	19.58
1339	CD	GLU	A	388	43.239	−5.442	115.809	1.00	11.20
1340	OE1	GLU	A	388	44.330	−4.881	115.937	1.00	19.48
1341	OE2	GLU	A	388	42.246	−5.134	116.503	1.00	17.08
1342	C	GLU	A	388	41.930	−6.653	111.094	1.00	16.35
1343	O	GLU	A	388	41.896	−5.473	110.821	1.00	15.52
1344	N	PRO	A	389	41.589	−7.586	110.202	1.00	16.54
1345	CD	PRO	A	389	41.398	−9.024	110.443	1.00	16.80
1346	CA	PRO	A	389	41.146	−7.232	108.857	1.00	20.31
1347	CB	PRO	A	389	40.773	−8.579	108.250	1.00	24.57
1348	CG	PRO	A	389	40.322	−9.336	109.442	1.00	16.51
1349	C	PRO	A	389	39.984	−6.296	108.944	1.00	22.62
1350	O	PRO	A	389	40.076	−5.171	108.451	1.00	29.81
1351	N	GLY	A	390	38.905	−6.756	109.578	1.00	19.40
1352	CA	GLY	A	390	37.722	−5.926	109.734	1.00	20.42
1353	C	GLY	A	390	38.076	−4.507	110.166	1.00	21.49
1354	O	GLY	A	390	37.394	−3.523	109.865	1.00	23.11
1355	N	ARG	A	391	39.173	−4.408	110.898	1.00	22.62
1356	CA	ARG	A	391	39.645	−3.130	111.360	1.00	19.89
1357	CB	ARG	A	391	40.538	−3.343	112.583	1.00	14.12
1358	CG	ARG	A	391	40.581	−2.157	113.490	1.00	18.23
1359	CD	ARG	A	391	41.360	−2.447	114.786	1.00	13.23
1360	NE	ARG	A	391	42.102	−1.258	115.228	1.00	22.11
1361	CZ	ARG	A	391	43.090	−1.273	116.105	1.00	18.99
1362	NH1	ARG	A	391	43.462	−2.422	116.644	1.00	20.41
1363	NH2	ARG	A	391	43.689	−0.135	116.424	1.00	29.33
1364	C	ARG	A	391	40.407	−2.458	110.187	1.00	18.96
1365	O	ARG	A	391	40.183	−1.282	109.880	1.00	20.35
1366	N	VAL	A	392	41.298	−3.199	109.529	1.00	15.96
1367	CA	VAL	A	392	42.020	−2.656	108.400	1.00	17.16
1368	CB	VAL	A	392	42.878	−3.720	107.771	1.00	13.89
1369	CG1	VAL	A	392	43.494	−3.210	106.464	1.00	8.04
1370	CG2	VAL	A	392	43.951	−4.098	108.761	1.00	9.26
1371	C	VAL	A	392	41.008	−2.148	107.378	1.00	20.53
1372	O	VAL	A	392	41.144	−1.061	106.829	1.00	22.78
1373	N	GLU	A	393	39.960	−2.922	107.153	1.00	20.85
1374	CA	GLU	A	393	38.941	−2.543	106.187	1.00	24.73
1375	CB	GLU	A	393	37.948	−3.690	106.044	1.00	22.33
1376	CG	GLU	A	393	36.836	−3.509	105.029	1.00	30.78
1377	CD	GLU	A	393	35.988	−4.807	104.891	1.00	37.98
1378	OE1	GLU	A	393	34.815	−4.762	104.458	1.00	25.11
1379	OE2	GLU	A	393	36.508	−5.888	105.234	1.00	38.44
1380	C	GLU	A	393	38.241	−1.255	106.594	1.00	26.29
1381	O	GLU	A	393	37.967	−0.396	105.778	1.00	29.48
1382	N	ALA	A	394	37.967	−1.109	107.873	1.00	25.71
1383	CA	ALA	A	394	37.295	0.083	108.330	1.00	23.23
1384	CB	ALA	A	394	37.029	−0.004	109.876	1.00	5.25
1385	C	ALA	A	394	38.192	1.272	107.997	1.00	24.37
1386	O	ALA	A	394	37.699	2.322	107.552	1.00	20.89
1387	N	LEU	A	395	39.504	1.101	108.226	1.00	26.86
1388	CA	LEU	A	395	40.502	2.157	107.978	1.00	26.79
1389	CB	LEU	A	395	41.869	1.725	108.485	1.00	17.72
1390	CG	LEU	A	395	42.141	1.960	109.968	1.00	23.47
1391	CD1	LEU	A	395	43.497	1.279	110.420	1.00	6.26
1392	CD2	LEU	A	395	42.164	3.475	110.160	1.00	6.73
1393	C	LEU	A	395	40.631	2.547	106.513	1.00	31.66
1394	O	LEU	A	395	41.083	3.618	106.177	1.00	34.95
1395	N	GLN	A	396	40.185	1.688	105.624	1.00	33.84
1396	CA	GLN	A	396	40.314	1.993	104.228	1.00	29.48
1397	CB	GLN	A	396	40.298	0.680	103.433	1.00	31.37
1398	CG	GLN	A	396	40.659	0.831	101.968	1.00	30.28
1399	CD	GLN	A	396	40.428	−0.434	101.167	1.00	27.29
1400	OE1	GLN	A	396	39.296	−0.842	100.941	1.00	33.68
1401	NE2	GLN	A	396	41.501	−1.066	100.748	1.00	31.43
1402	C	GLN	A	396	39.247	2.905	103.703	1.00	27.95
1403	O	GLN	A	396	39.502	3.852	102.986	1.00	34.21
1404	N	GLN	A	397	38.033	2.606	104.075	1.00	28.79
1405	CA	GLN	A	397	36.888	3.304	103.564	1.00	27.47
1406	CB	GLN	A	397	35.665	2.707	104.272	1.00	23.47
1407	CG	GLN	A	397	35.922	1.192	104.530	1.00	28.31
1408	CD	GLN	A	397	35.505	0.226	103.395	1.00	40.98
1409	OE1	GLN	A	397	36.280	−0.668	102.997	1.00	31.54
1410	NE2	GLN	A	397	34.273	0.390	102.895	1.00	44.00
1411	C	GLN	A	397	36.913	4.804	103.523	1.00	24.58
1412	O	GLN	A	397	36.535	5.393	102.530	1.00	28.53
1413	N	PRO	A	398	37.409	5.444	104.559	1.00	23.95
1414	CD	PRO	A	398	37.715	4.894	105.881	1.00	26.73
1415	CA	PRO	A	398	37.437	6.914	104.520	1.00	23.31
1416	CB	PRO	A	398	38.221	7.287	105.775	1.00	19.47
1417	CG	PRO	A	398	37.979	6.161	106.703	1.00	37.68
1418	C	PRO	A	398	38.166	7.389	103.230	1.00	25.88
1419	O	PRO	A	398	37.798	8.397	102.623	1.00	25.59
1420	N	TYR	A	399	39.213	6.657	102.835	1.00	26.35
1421	CA	TYR	A	399	40.036	7.001	101.663	1.00	22.46
1422	CB	TYR	A	399	41.414	6.296	101.717	1.00	15.92
1423	CG	TYR	A	399	42.256	6.745	102.917	1.00	10.71
1424	CD1	TYR	A	399	42.724	8.047	103.003	1.00	15.66
1425	CE1	TYR	A	399	43.385	8.505	104.108	1.00	9.61
1426	CD2	TYR	A	399	42.497	5.898	103.989	1.00	5.25
1427	CE2	TYR	A	399	43.169	6.335	105.110	1.00	6.63
1428	CZ	TYR	A	399	43.615	7.654	105.169	1.00	17.65
1429	OH	TYR	A	399	44.307	8.110	106.287	1.00	18.05
1430	C	TYR	A	399	39.313	6.673	100.382	1.00	21.91
1431	O	TYR	A	399	39.317	7.488	99.450	1.00	17.12
1432	N	VAL	A	400	38.671	5.504	100.324	1.00	19.13
1433	CA	VAL	A	400	37.931	5.185	99.108	1.00	19.63
1434	CB	VAL	A	400	37.121	3.953	99.257	1.00	16.29
1435	CG1	VAL	A	400	36.263	3.749	98.029	1.00	13.91
1436	CG2	VAL	A	400	38.063	2.765	99.460	1.00	22.87
1437	C	VAL	A	400	37.003	6.358	98.859	1.00	25.95
1438	O	VAL	A	400	37.084	7.003	97.815	1.00	30.52
1439	N	GLU	A	401	36.147	6.663	99.836	1.00	28.51
1440	CA	GLU	A	401	35.241	7.812	99.723	1.00	28.24
1441	CB	GLU	A	401	34.688	8.215	101.081	1.00	14.53
1442	CG	GLU	A	401	33.522	7.390	101.523	1.00	45.77
1443	CD	GLU	A	401	32.410	8.230	102.120	1.00	42.44
1444	OE1	GLU	A	401	31.240	8.032	101.702	1.00	39.71
1445	OE2	GLU	A	401	32.721	9.073	102.992	1.00	43.94
1446	C	GLU	A	401	35.926	9.044	99.132	1.00	26.96
1447	O	GLU	A	401	35.481	9.581	98.112	1.00	29.78
1448	N	ALA	A	402	36.994	9.491	99.793	1.00	23.76
1449	CA	ALA	A	402	37.723	10.650	99.351	1.00	19.13
1450	CB	ALA	A	402	39.009	10.730	100.095	1.00	14.35
1451	C	ALA	A	402	37.959	10.539	97.841	1.00	22.89
1452	O	ALA	A	402	37.731	11.497	97.106	1.00	20.80
1453	N	LEU	A	403	38.369	9.360	97.365	1.00	23.41
1454	CA	LEU	A	403	38.604	9.184	95.934	1.00	20.90
1455	CB	LEU	A	403	39.263	7.845	95.665	1.00	15.78
1456	CG	LEU	A	403	39.819	7.745	94.244	1.00	7.31
1457	CD1	LEU	A	403	40.970	8.686	94.102	1.00	10.15
1458	CD2	LEU	A	403	40.244	6.321	93.975	1.00	9.87
1459	C	LEU	A	403	37.314	9.284	95.116	1.00	22.22
1460	O	LEU	A	403	37.296	9.931	94.062	1.00	20.72
1461	N	LEU	A	404	36.255	8.615	95.597	1.00	24.61
1462	CA	LEU	A	404	34.915	8.621	94.975	1.00	20.80
1463	CB	LEU	A	404	33.871	7.926	95.877	1.00	11.48
1464	CG	LEU	A	404	32.500	7.836	95.160	1.00	7.08
1465	CD1	LEU	A	404	32.690	7.079	93.867	1.00	15.09
1466	CD2	LEU	A	404	31.489	7.059	95.975	1.00	8.23
1467	C	LEU	A	404	34.444	10.062	94.760	1.00	22.50
1468	O	LEU	A	404	34.107	10.461	93.672	1.00	25.06
1469	N	SER	A	405	34.425	10.831	95.834	1.00	23.12
1470	CA	SER	A	405	34.015	12.209	95.793	1.00	20.64
1471	CB	SER	A	405	33.946	12.735	97.234	1.00	27.30
1472	OG	SER	A	405	33.432	14.056	97.321	1.00	45.53
1473	C	SER	A	405	34.963	13.058	94.950	1.00	20.08
1474	O	SER	A	405	34.521	13.960	94.283	1.00	2545
1475	N	TYR	A	406	36.258	12.768	94.982	1.00	18.80
1476	CA	TYR	A	406	37.234	13.539	94.232	1.00	14.69
1477	CB	TYR	A	406	38.635	13.072	94.548	1.00	9.34
1478	CG	TYR	A	406	39.703	13.963	93.990	1.00	14.57
1479	CD1	TYR	A	406	39.971	15.181	94.559	1.00	21.04
1480	CE1	TYR	A	406	41.052	15.975	94.109	1.00	20.89
1481	CD2	TYR	A	406	40.510	13.544	92.944	1.00	18.62
1482	CE2	TYR	A	406	41.574	14.315	92.490	1.00	15.48
1483	CZ	TYR	A	406	41.858	15.542	93.087	1.00	21.87
1484	OH	TYR	A	406	42.990	16.313	92.740	1.00	19.24
1485	C	TYR	A	406	36.984	13.351	92.760	1.00	16.56
1486	O	TYR	A	406	36.818	14.334	92.035	1.00	20.10
1487	N	THR	A	407	36.950	12.091	92.325	1.00	16.86
1488	CA	THR	A	407	36.709	11.765	90.920	1.00	16.53
1489	CB	THR	A	407	36.771	10.217	90.692	1.00	13.61
1490	OG1	THR	A	407	35.825	9.557	91.545	1.00	6.85
1491	CG2	THR	A	407	38.127	9.678	90.980	1.00	5.25
1492	C	THR	A	407	35.353	12.334	90.394	1.00	18.56
1493	O	THR	A	407	35.258	12.774	89.251	1.00	12.45
1494	N	ARG	A	408	34.319	12.323	91.234	1.00	22.92
1495	CA	ARG	A	408	33.022	12.882	90.872	1.00	27.72
1496	CB	ARG	A	408	32.055	12.823	92.050	1.00	35.75
1497	CG	ARG	A	408	31.042	11.676	92.011	1.00	46.40
1498	CD	ARG	A	408	30.033	11.897	93.119	1.00	67.06
1499	NE	ARG	A	408	29.113	10.778	93.340	1.00	78.74
1500	CZ	ARG	A	408	28.091	10.798	94.203	1.00	83.77
1501	NH1	ARG	A	408	27.838	11.878	94.937	1.00	83.98
1502	NH2	ARG	A	408	27.321	9.725	94.345	1.00	84.62
1503	C	ARG	A	408	33.190	14.357	90.464	1.00	29.46
1504	O	ARG	A	408	32.576	14.825	89.498	1.00	33.89
1505	N	ILE	A	409	34.009	15.088	91.213	1.00	25.53
1506	CA	ILE	A	409	34.298	16.482	90.918	1.00	23.48
1507	CB	ILE	A	409	35.024	17.123	92.140	1.00	24.09
1508	CG2	ILE	A	409	35.445	18.538	91.872	1.00	21.70
1509	CG1	ILE	A	409	34.096	17.139	93.334	1.00	20.16
1510	CD1	ILE	A	409	34.872	17.171	94.668	1.00	11.98
1511	C	ILE	A	409	35.193	16.628	89.647	1.00	24.10
1512	O	ILE	A	409	34.942	17.466	88.767	1.00	24.66
1513	N	LYS	A	410	36.218	15.795	89.547	1.00	20.96
1514	CA	LYS	A	410	37.128	15.876	88.442	1.00	18.34
1515	CB	LYS	A	410	38.342	15.008	88.742	1.00	18.67
1516	CG	LYS	A	410	39.498	15.178	87.782	1.00	24.94
1517	CD	LYS	A	410	40.700	14.291	88.125	1.00	26.23
1518	CE	LYS	A	410	41.936	14.709	87.307	1.00	28.36
1519	NZ	LYS	A	410	43.165	13.963	87.652	1.00	16.11
1520	C	LYS	A	410	36.543	15.551	87.053	1.00	16.91
1521	O	LYS	A	410	36.891	16.178	86.066	1.00	21.62
1522	N	ARG	A	411	35.664	14.579	86.954	1.00	14.05
1523	CA	ARG	A	411	35.084	14.241	85.653	1.00	14.43
1524	CB	ARG	A	411	35.856	13.117	84.943	1.00	14.95
1525	CG	ARG	A	411	37.215	13.516	84.372	1.00	16.11
1526	CD	ARG	A	411	37.699	12.437	83.398	1.00	22.77
1527	NE	ARG	A	411	39.073	12.656	82.949	1.00	34.57
1528	CZ	ARG	A	411	39.712	11.852	82.102	1.00	36.23
1529	NH1	ARG	A	411	39.082	10.786	81.615	1.00	31.20
1530	NH2	ARG	A	411	40.980	12.099	81.768	1.00	21.00
1531	C	ARG	A	411	33.698	13.756	85.953	1.00	14.95
1532	O	ARG	A	411	33.415	12.577	85.853	1.00	17.23
1533	N	PRO	A	412	32.802	14.674	86.324	1.00	18.27
1534	CD	PRO	A	412	32.882	16.161	86.322	1.00	19.78
1535	CA	PRO	A	412	31.454	14.197	86.633	1.00	15.45
1536	CB	PRO	A	412	30.736	15.469	87.069	1.00	12.96
1537	CG	PRO	A	412	31.447	16.581	86.230	1.00	16.38
1538	C	PRO	A	412	30.799	13.533	85.453	1.00	16.13
1539	O	PRO	A	412	29.947	12.656	85.640	1.00	18.43
1540	N	GLN	A	413	31.181	13.958	84.246	1.00	17.14
1541	CA	GLN	A	413	30.588	13.387	83.063	1.00	21.06
1542	CB	GLN	A	413	30.729	14.366	81.922	1.00	28.30
1543	CG	GLN	A	413	29.656	15.455	81.871	1.00	51.45
1544	CD	GLN	A	413	29.866	16.617	82.862	1.00	64.03
1545	OE1	GLN	A	413	30.935	17.243	82.917	1.00	65.04
1546	NE2	GLN	A	413	28.826	16.917	83.635	1.00	70.87
1547	C	GLN	A	413	31.161	11.998	82.673	1.00	24.10
1548	O	GLN	A	413	30.859	11.473	81.583	1.00	26.59
1549	N	ASP	A	414	31.953	11.391	83.572	1.00	21.34
1550	CA	ASP	A	414	32.585	10.081	83.333	1.00	17.69
1551	CB	ASP	A	414	33.993	10.273	82.720	1.00	11.40
1552	CG	ASP	A	414	34.767	8.953	82.490	1.00	17.52
1553	OD1	ASP	A	414	34.185	7.858	82.262	1.00	11.40
1554	OD2	ASP	A	414	36.017	9.024	82.505	1.00	17.55
1555	C	ASP	A	414	32.641	9.236	84.618	1.00	19.02
1556	O	ASP	A	414	33.678	8.965	85.193	1.00	15.28
1557	N	GLN	A	415	31.473	8.788	85.028	1.00	22.23
1558	CA	GLN	A	415	31.332	7.973	86.199	1.00	24.58
1559	CB	GLN	A	415	29.868	7.618	86.405	1.00	33.91
1560	CG	GLN	A	415	29.010	8.757	86.882	1.00	47.58
1561	CD	GLN	A	415	27.579	8.328	87.105	1.00	62.81
1562	OE1	GLN	A	415	26.779	9.069	87.695	1.00	61.90
1563	NE2	GLN	A	415	27.238	7.117	86.626	1.00	66.91
1564	C	GLN	A	415	32.138	6.699	86.231	1.00	25.21
1565	O	GLN	A	415	32.548	6.289	87.313	1.00	26.32
1566	N	LEU	A	416	32.361	6.053	85.087	1.00	23.46
1567	CA	LEU	A	416	33.133	4.808	85.116	1.00	23.46
1568	CB	LEU	A	416	32.895	4.021	83.845	1.00	18.13
1569	CG	LEU	A	416	31.434	3.623	83.707	1.00	21.27
1570	CD1	LEU	A	416	31.304	2.711	82.504	1.00	30.47
1571	CD2	LEU	A	416	30.965	2.901	84.982	1.00	12.71
1572	C	LEU	A	416	34.643	4.968	85.336	1.00	26.85
1573	O	LEU	A	416	35.378	3.977	85.477	1.00	26.62
1574	N	ARG	A	417	35.112	6.214	85.371	1.00	28.16
1575	CA	ARG	A	417	36.537	6.484	85.608	1.00	26.52
1576	CB	ARG	A	417	36.852	7.963	85.360	1.00	26.71
1577	CG	ARG	A	417	38.309	8.248	85.436	1.00	12.42
1578	CD	ARG	A	417	38.606	9.705	85.462	1.00	15.47
1579	NE	ARG	A	417	40.045	9.914	85.624	1.00	19.89
1580	CZ	ARG	A	417	40.610	10.604	86.617	1.00	30.02
1581	NH1	ARG	A	417	39.871	11.171	87.569	1.00	29.62
1582	NH2	ARG	A	417	41.930	10.740	86.644	1.00	26.16
1583	C	ARG	A	417	36.982	6.087	87.043	1.00	26.85
1584	O	ARG	A	417	38.138	5.729	87.262	1.00	24.07
1585	N	PHE	A	418	36.082	6.172	88.020	1.00	23.22
1586	CA	PHE	A	418	36.464	5.738	89.349	1.00	25.25
1587	CB	PHE	A	418	35.414	6.142	90.366	1.00	20.37
1588	CG	PHE	A	418	35.672	5.594	91.731	1.00	26.53
1589	CD1	PHE	A	418	36.893	5.814	92.362	1.00	28.94
1590	CD2	PHE	A	418	34.721	4.821	92.373	1.00	23.82
1591	CE1	PHE	A	418	37.165	5.259	93.611	1.00	18.88
1592	CE2	PHE	A	418	34.992	4.268	93.611	1.00	30.12
1593	CZ	PHE	A	418	36.219	4.490	94.226	1.00	24.28
1594	C	PHE	A	418	36.678	4.195	89.385	1.00	24.71
1595	O	PHE	A	418	37.649	3.691	89.976	1.00	20.41
1596	N	PRO	A	419	35.781	3.428	88.748	1.00	24.57
1597	CD	PRO	A	419	34.436	3.778	88.277	1.00	17.11
1598	CA	PRO	A	419	35.958	1.971	88.763	1.00	30.07
1599	CB	PRO	A	419	34.645	1.457	88.163	1.00	34.07
1600	CG	PRO	A	419	33.672	2.513	88.561	1.00	28.67
1601	C	PRO	A	419	37.183	1.537	87.946	1.00	31.08
1602	O	PRO	A	419	37.791	0.494	88.214	1.00	28.61
1603	N	ARG	A	420	37.535	2.326	86.931	1.00	32.83
1604	CA	ARG	A	420	38.698	1.973	86.116	1.00	29.40
1605	CB	ARG	A	420	38.885	2.953	84.965	1.00	26.01
1606	CG	ARG	A	420	38.051	2.688	83.774	1.00	15.64
1607	CD	ARG	A	420	38.357	3.783	82.682	1.00	16.77
1608	NE	ARG	A	420	37.213	3.819	81.800	1.00	32.31
1609	CZ	ARG	A	420	36.333	4.810	81.720	1.00	32.34
1610	NH1	ARG	A	420	36.464	5.912	82.454	1.00	22.18
1611	NH2	ARG	A	420	35.271	4.640	80.946	1.00	42.24
1612	C	ARG	A	420	39.909	2.045	87.046	1.00	26.85
1613	O	ARG	A	420	40.874	1.278	86.917	1.00	28.56
1614	N	MET	A	421	39.830	2.972	87.996	1.00	23.40
1615	CA	MET	A	421	40.909	3.172	88.942	1.00	22.94
1616	CB	MET	A	421	40.694	4.477	89.741	1.00	15.02
1617	CG	MET	A	421	41.658	5.548	89.351	1.00	15.86
1618	SD	MET	A	421	41.304	7.133	90.071	1.00	19.36
1619	CE	MET	A	421	40.500	8.004	88.644	1.00	23.77
1620	C	MET	A	421	41.048	1.971	89.872	1.00	20.18
1621	O	MET	A	421	42.110	1.333	89.896	1.00	18.21
1622	N	LEU	A	422	39.990	1.680	90.630	1.00	18.63
1623	CA	LEU	A	422	40.013	0.549	91.531	1.00	20.59
1624	CB	LEU	A	422	38.633	0.250	92.119	1.00	19.88
1625	CG	LEU	A	422	38.057	1.393	92.970	1.00	20.81
1626	CD1	LEU	A	422	36.812	0.964	93.694	1.00	26.59
1627	CD2	LEU	A	422	39.073	1.825	93.941	1.00	27.12
1628	C	LEU	A	422	40.513	−0.635	90.736	1.00	22.93
1629	O	LEU	A	422	41.365	−1.384	91.219	1.00	27.81
1630	N	MET	A	423	40.022	−0.794	89.511	1.00	21.99
1631	CA	MET	A	423	40.489	−1.888	88.652	1.00	23.39
1632	CB	MET	A	423	40.015	−1.632	87.207	1.00	23.04
1633	CG	MET	A	423	39.307	−2.819	86.610	1.00	34.27
1634	SD	MET	A	423	37.975	−3.396	87.683	1.00	34.89
1635	CE	MET	A	423	36.767	−2.077	87.334	1.00	35.94
1636	C	MET	A	423	42.046	−2.093	88.672	1.00	20.11
1637	O	MET	A	423	42.528	−3.222	88.577	1.00	17.25
1638	N	LYS	A	424	42.817	−1.009	88.795	1.00	17.68
1639	CA	LYS	A	424	44.271	−1.103	88.827	1.00	17.31
1640	CB	LYS	A	424	44.884	0.294	88.816	1.00	16.49
1641	CG	LYS	A	424	44.606	0.998	87.538	1.00	22.55
1642	CD	LYS	A	424	45.189	0.203	86.352	1.00	31.18
1643	CE	LYS	A	424	44.870	0.841	85.021	1.00	34.69
1644	NZ	LYS	A	424	43.422	0.627	84.683	1.00	47.10
1645	C	LYS	A	424	44.765	−1.897	90.026	1.00	16.52
1646	O	LYS	A	424	45.869	−2.485	89.989	1.00	13.57
1647	N	LEU	A	425	43.965	−1.891	91.095	1.00	14.69
1648	CA	LEU	A	425	44.294	−2.673	92.271	1.00	13.33
1649	CB	LEU	A	425	43.290	−2.400	93.397	1.00	10.78
1650	CG	LEU	A	425	43.319	−0.981	93.932	1.00	14.31
1651	CD1	LEU	A	425	42.085	−0.776	94.736	1.00	22.37
1652	CD2	LEU	A	425	44.560	−0.743	94.781	1.00	5.26
1653	C	LEU	A	425	44.251	−4.162	91.878	1.00	10.81
1654	O	LEU	A	425	44.988	−4.989	92.428	1.00	14.13
1655	N	VAL	A	426	43.378	−4.501	90.932	1.00	10.71
1656	CA	VAL	A	426	43.249	−5.878	90.490	1.00	13.91
1657	CB	VAL	A	426	42.128	−6.050	89.453	1.00	14.20
1658	CG1	VAL	A	426	42.100	−7.491	89.014	1.00	9.66
1659	CG2	VAL	A	426	40.753	−5.620	90.047	1.00	13.13
1660	C	VAL	A	426	44.569	−6.298	89.853	1.00	16.67
1661	O	VAL	A	426	45.161	−7.333	90.177	1.00	20.54
1662	N	SER	A	427	45.053	−5.463	88.957	1.00	13.21
1663	CA	SER	A	427	46.295	−5.754	88.293	1.00	14.68
1664	CB	SER	A	427	46.423	−4.782	87.146	1.00	20.09
1665	CG	SER	A	427	45.203	−4.792	86.410	1.00	20.17
1666	C	SER	A	427	47.543	−5.739	89.191	1.00	18.31
1667	O	SER	A	427	48.510	−6.495	88.914	1.00	18.50
1668	N	LEU	A	428	47.532	−4.897	90.239	1.00	16.56
1669	CA	LEU	A	428	48.670	−4.845	91.150	1.00	14.64
1670	CB	LEU	A	428	48.538	−3.709	92.179	1.00	9.37
1671	CG	LEU	A	428	48.587	−2.257	91.679	1.00	17.69
1672	CD1	LEU	A	428	48.208	−1.301	92.778	1.00	18.66
1673	CD2	LEU	A	428	49.967	−1.929	91.201	1.00	12.21
1674	C	LEU	A	428	48.832	−6.193	91.869	1.00	13.83
1675	O	LEU	A	428	49.929	−6.532	92.339	1.00	11.00
1676	N	ARG	A	429	47.758	−6.978	91.958	1.00	11.73
1677	CA	ARG	A	429	47.920	−8.256	92.630	1.00	17.81
1678	CB	ARG	A	429	46.590	−8.897	93.001	1.00	22.40
1679	CG	ARG	A	429	45.912	−8.348	94.206	1.00	9.68
1680	CD	ARG	A	429	46.815	−8.382	95.420	1.00	9.57
1681	NE	ARG	A	429	46.186	−7.536	96.441	1.00	13.29
1682	CZ	ARG	A	429	45.247	−7.954	97.279	1.00	8.67
1683	NH1	ARG	A	429	44.855	−9.209	97.261	1.00	16.20
1684	NH2	ARG	A	429	44.618	−7.101	98.053	1.00	16.87
1685	C	ARG	A	429	48.648	−9.168	91.678	1.00	22.72
1686	O	ARG	A	429	49.624	−9.814	92.064	1.00	27.52
1687	N	THR	A	430	48.178	−9.237	90.430	1.00	24.76
1688	CA	THR	A	430	48.843	−10.085	89.422	1.00	22.85
1689	CB	THR	A	430	48.187	−9.960	88.024	1.00	17.87
1690	OG1	THR	A	430	46.864	−10.525	88.069	1.00	15.01
1691	CG2	THR	A	430	49.011	−10.747	86.988	1.00	13.65
1692	C	THR	A	430	50.339	−9.712	89.333	1.00	22.44
1693	O	THR	A	430	51.227	−10.591	89.324	1.00	18.36
1694	N	LEU	A	431	50.610	−8.407	89.302	1.00	20.10
1695	CA	LEU	A	431	51.986	−7.944	89.248	1.00	19.15
1696	CB	LEU	A	431	52.032	−6.411	89.165	1.00	20.90
1697	CG	LEU	A	431	51.960	−5.865	87.725	1.00	18.63
1698	CD1	LEU	A	431	50.846	−4.891	87.630	1.00	17.52
1699	CD2	LEU	A	431	53.248	−5.193	87.356	1.00	23.80
1700	C	LEU	A	431	52.762	−8.448	90.457	1.00	17.38
1701	O	LEU	A	431	53.877	−8.911	90.333	1.00	20.17
1702	N	SER	A	432	52.148	−8.372	91.629	1.00	14.68
1703	CA	SER	A	432	52.763	−8.830	92.861	1.00	9.40
1704	CB	SER	A	432	51.801	−8.597	94.006	1.00	13.48
1705	OG	SER	A	432	52.423	−8.642	95.267	1.00	13.96
1706	C	SER	A	432	53.084	−10.315	92.737	1.00	13.39
1707	O	SER	A	432	54.115	−10.763	93.251	1.00	15.02
1708	N	SER	A	433	52.235	−11.086	92.042	1.00	13.33
1709	CA	SER	A	433	52.542	−12.518	91.866	1.00	12.64
1710	CB	SER	A	433	51.368	−13.308	91.295	1.00	12.54
1711	OG	SER	A	433	50.372	−13.577	92.249	1.00	27.96
1712	C	SER	A	433	53.710	−12.707	90.906	1.00	16.54
1713	O	SER	A	433	54.607	−13.521	91.180	1.00	19.09
1714	N	VAL	A	434	53.694	−11.961	89.790	1.00	13.12
1715	CA	VAL	A	434	54.728	−12.068	88.790	1.00	11.80
1716	CB	VAL	A	434	54.434	−11.119	87.641	1.00	21.88
1717	CG1	VAL	A	434	55.491	−11.241	86.523	1.00	34.34
1718	CG2	VAL	A	434	53.098	−11.466	87.095	1.00	23.02
1719	C	VAL	A	434	56.083	−11.765	89.401	1.00	12.40
1720	O	VAL	A	434	57.082	−12.486	89.125	1.00	5.25
1721	N	HIS	A	435	56.091	−10.710	90.235	1.00	13.26
1722	CA	HIS	A	435	57.270	−10.239	90.960	1.00	10.05
1723	CB	HIS	A	435	56.916	−9.025	91.765	1.00	10.18
1724	CG	HIS	A	435	57.873	−8.751	92.881	1.00	19.96
1725	CD2	HIS	A	435	57.754	−8.925	94.224	1.00	18.04
1726	ND1	HIS	A	435	59.117	−8.196	92.675	1.00	24.89
1727	CE1	HIS	A	435	59.718	−8.032	93.842	1.00	27.76
1728	NE2	HIS	A	435	58.912	−8.468	94.796	1.00	18.59
1729	C	HIS	A	435	57.785	−11.301	91.901	1.00	13.96
1730	O	HIS	A	435	58.962	−11.421	92.154	1.00	12.84
1731	N	SER	A	436	56.880	−12.090	92.439	1.00	22.00
1732	CA	SER	A	436	57.312	−13.147	93.328	1.00	25.75
1733	CB	SER	A	436	56.101	−13.745	94.059	1.00	18.10
1734	OG	SER	A	436	56.542	−14.368	95.254	1.00	39.95
1735	C	SER	A	436	58.043	−14.205	92.482	1.00	26.71
1736	O	SER	A	436	59.047	−14.772	92.925	1.00	29.44
1737	N	GLU	A	437	57.538	−14.459	91.271	1.00	26.62
1738	CA	GLU	A	437	58.157	−15.438	90.392	1.00	27.61
1739	CB	GLU	A	437	57.231	−15.781	89.211	1.00	32.32
1740	CG	GLU	A	437	55.970	−16.545	89.640	1.00	43.49
1741	CD	GLU	A	437	54.992	−16.826	88.517	1.00	44.02
1742	OE1	GLU	A	437	54.224	−15.916	88.110	1.00	39.81
1743	OE2	GLU	A	437	55.002	−17.978	88.033	1.00	52.54
1744	C	GLU	A	437	59.476	−14.858	89.907	1.00	30.11
1745	O	GLU	A	437	60.347	−15.573	89.446	1.00	32.93
1746	N	GLN	A	438	59.623	−13.545	90.038	1.00	29.79
1747	CA	GLN	A	438	60.845	−12.863	89.658	1.00	23.83
1748	CB	GLN	A	438	60.570	−11.387	89.459	1.00	22.03
1749	CG	GLN	A	438	61.790	−10.526	89.384	1.00	24.80
1750	CD	GLN	A	438	62.679	−10.921	88.263	1.00	23.62
1751	OE1	GLN	A	438	62.559	−10.414	87.131	1.00	17.75
1752	NE2	GLN	A	438	63.570	−11.867	88.549	1.00	10.79
1753	C	GLN	A	438	61.845	−13.042	90.788	1.00	24.89
1754	O	GLN	A	438	63.035	−13.107	90.544	1.00	25.50
1755	N	VAL	A	439	61.347	−13.111	92.025	1.00	29.45
1756	CA	VAL	A	439	62.176	−13.291	93.222	1.00	30.36
1757	CB	VAL	A	439	61.360	−13.040	94.525	1.00	31.12
1758	CG1	VAL	A	439	62.202	−13.343	95.744	1.00	35.24
1759	CG2	VAL	A	439	60.902	−11.601	94.585	1.00	28.21
1760	C	VAL	A	439	62.650	−14.736	93.238	1.00	32.10
1761	O	VAL	A	439	63.835	−15.036	93.419	1.00	34.80
1762	N	PHE	A	440	61.680	−15.618	93.062	1.00	31.65
1763	CA	PHE	A	440	61.884	−17.048	93.006	1.00	33.36
1764	CB	PHE	A	440	60.559	−17.695	92.602	1.00	43.52
1765	CG	PHE	A	440	60.697	−19.095	92.091	1.00	52.34
1766	CD1	PHE	A	440	61.337	−19.355	90.866	1.00	53.44
1767	CD2	PHE	A	440	60.253	−20.157	92.866	1.00	51.37
1768	CE1	PHE	A	440	61.542	−20.657	90.437	1.00	58.67
1769	CE2	PHE	A	440	60.453	−21.463	92.450	1.00	56.99
1770	CZ	PHE	A	440	61.102	−21.721	91.234	1.00	59.17
1771	C	PHE	A	440	62.957	−17.413	91.992	1.00	33.01
1772	O	PHE	A	440	63.773	−18.282	92.232	1.00	32.92
1773	N	ALA	A	441	62.910	−16.770	90.837	1.00	30.92
1774	CA	ALA	A	441	63.867	−17.041	89.795	1.00	33.32
1775	CB	ALA	A	441	63.280	−16.615	88.443	1.00	28.33
1776	C	ALA	A	441	65.171	−16.312	90.056	1.00	34.78
1777	O	ALA	A	441	66.236	−16.681	89.558	1.00	34.01
1778	N	LEU	A	442	65.078	−15.250	90.838	1.00	40.36
1779	CA	LEU	A	442	66.254	−14.451	91.150	1.00	40.69
1780	CB	LEU	A	442	65.871	−13.231	91.979	1.00	38.10
1781	CG	LEU	A	442	65.739	−11.948	91.209	1.00	35.38
1782	CD1	LEU	A	442	65.584	−10.865	92.176	1.00	28.28
1783	CD2	LEU	A	442	66.983	−11.755	90.407	1.00	39.43
1784	C	LEU	A	442	67.244	−15.279	91.931	1.00	43.23
1785	O	LEU	A	442	68.394	−15.408	91.548	1.00	43.93
1786	N	ARG	A	443	66.784	−15.849	93.033	1.00	45.47
1787	CA	ARG	A	443	67.651	−16.635	93.885	1.00	51.75
1788	CB	ARG	A	443	66.853	−17.149	95.070	1.00	54.53
1789	CG	ARG	A	443	65.760	−18.115	94.680	1.00	56.75
1790	CD	ARG	A	443	65.017	−18.637	95.882	1.00	69.71
1791	NE	ARG	A	443	65.428	−18.001	97.135	1.00	81.95
1792	CZ	ARG	A	443	65.400	−18.623	98.302	1.00	78.74
1793	NH1	ARG	A	443	64.987	−19.875	98.346	1.00	79.02
1794	NH2	ARG	A	443	65.783	−17.997	99.406	1.00	83.70
1795	C	ARG	A	443	68.255	−17.801	93.096	1.00	54.47
1796	O	ARG	A	443	69.404	−18.203	93.327	1.00	56.52
1797	N	LEU	A	444	67.474	−18.336	92.157	1.00	57.46
1798	CA	LEU	A	444	67.931	−19.431	91.299	1.00	56.62
1799	CB	LEU	A	444	66.830	−19.831	90.312	1.00	59.25
1800	CG	LEU	A	444	65.995	−21.008	90.831	1.00	58.14
1801	CD1	LEU	A	444	64.687	−21.069	90.096	1.00	61.54
1802	CD2	LEU	A	444	66.769	−22.284	90.629	1.00	63.49
1803	C	LEU	A	444	69.208	−19.055	90.579	1.00	54.88
1804	O	LEU	A	444	69.894	−19.897	90.078	1.00	53.96
1805	N	GLN	A	445	69.519	−17.770	90.536	1.00	60.24
1806	CA	GLN	A	445	70.760	−17.294	89.939	1.00	64.02
1807	CB	GLN	A	445	70.555	−15.973	89.182	1.00	62.89
1808	CG	GLN	A	445	70.029	−16.186	87.791	1.00	70.48
1809	CD	GLN	A	445	69.743	−14.899	87.019	1.00	79.70
1810	OE1	GLN	A	445	69.949	−13.787	87.513	1.00	83.56
1811	NE2	GLN	A	445	69.266	−15.055	85.790	1.00	75.40
1812	C	GLN	A	445	71.682	−17.052	91.137	1.00	66.51
1813	O	GLN	A	445	71.462	−17.588	92.244	1.00	61.81
1814	N	ASP	A	446	72.730	−16.262	90.925	1.00	70.85
1815	CA	ASP	A	446	73.628	−15.959	92.035	1.00	72.12
1816	CB	ASP	A	446	75.105	−15.935	91.595	1.00	76.38
1817	CG	ASP	A	446	76.046	−15.907	92.793	1.00	83.33
1818	OD1	ASP	A	446	76.229	−16.979	93.418	1.00	82.21
1819	OD2	ASP	A	446	76.572	−14.813	93.137	1.00	83.93
1820	C	ASP	A	446	73.217	−14.568	92.562	1.00	68.79
1821	O	ASP	A	446	73.930	−13.925	93.345	1.00	72.15
1822	N	LYS	A	447	72.054	−14.110	92.123	1.00	61.71
1823	CA	LYS	A	447	71.568	−12.820	92.537	1.00	56.09
1824	CB	LYS	A	447	70.763	−12.215	91.401	1.00	49.97
1825	CG	LYS	A	447	71.562	−11.250	90.572	1.00	55.67
1826	CD	LYS	A	447	71.274	−11.363	89.065	1.00	63.06
1827	CE	LYS	A	447	72.560	−11.557	88.271	1.00	63.18
1828	NZ	LYS	A	447	73.105	−12.933	88.506	1.00	72.36
1829	C	LYS	A	447	70.743	−12.903	93.822	1.00	53.51
1830	O	LYS	A	447	69.635	−13.451	93.839	1.00	52.52
1831	N	LYS	A	448	71.304	−12.377	94.907	1.00	49.20
1832	CA	LYS	A	448	70.604	−12.378	96.169	1.00	47.16
1833	CB	LYS	A	448	71.445	−13.071	97.233	1.00	49.48
1834	CG	LYS	A	448	71.046	−14.549	97.444	1.00	62.61
1835	CD	LYS	A	448	69.851	−14.716	98.413	1.00	67.54
1836	CE	LYS	A	448	68.552	−14.056	97.904	1.00	66.83
1837	NZ	LYS	A	448	68.053	−13.052	98.888	1.00	63.74
1838	C	LYS	A	448	70.210	−10.972	96.600	1.00	46.23
1839	O	LYS	A	448	70.942	−9.999	96.385	1.00	46.82
1840	N	LEU	A	449	69.025	−10.880	97.202	1.00	42.49
1841	CA	LEU	A	449	68.477	−9.606	97.658	1.00	38.18
1842	CB	LEU	A	449	66.964	−9.753	97.815	1.00	33.91
1843	CG	LEU	A	449	66.269	−10.457	96.646	1.00	36.17
1844	CD1	LEU	A	449	64.771	−10.696	96.955	1.00	10.94
1845	CD2	LEU	A	449	66.458	−9.591	95.389	1.00	35.40
1846	C	LEU	A	449	69.084	−9.118	98.969	1.00	34.08
1847	O	LEU	A	449	69.184	−9.875	99.912	1.00	40.43
1848	N	PRO	A	450	69.530	−7.857	99.034	1.00	28.11
1849	CD	PRO	A	450	69.629	−6.817	98.006	1.00	21.01
1850	CA	PRO	A	450	70.097	−7.415	100.312	1.00	27.75
1851	CB	PRO	A	450	70.333	−5.933	100.116	1.00	21.74
1852	CG	PRO	A	450	69.528	−5.608	98.846	1.00	26.89
1853	C	PRO	A	450	69.061	−7.665	101.374	1.00	30.49
1854	O	PRO	A	450	67.858	−7.637	101.071	1.00	28.32
1855	N	PRO	A	451	69.504	−7.909	102.631	1.00	32.59
1856	CD	PRO	A	451	70.885	−7.627	103.044	1.00	28.81
1857	CA	PRO	A	451	68.680	−8.187	103.821	1.00	32.25
1858	CB	PRO	A	451	69.584	−7.758	104.992	1.00	24.82
1859	CG	PRO	A	451	70.664	−6.951	104.345	1.00	23.17
1860	C	PRO	A	451	67.274	−7.569	103.909	1.00	30.85
1861	O	PRO	A	451	66.282	−8.303	104.031	1.00	33.81
1862	N	LEU	A	452	67.177	−6.245	103.862	1.00	24.53
1863	CA	LEU	A	452	65.863	−5.616	103.951	1.00	27.08
1864	CB	LEU	A	452	65.978	−4.111	103.775	1.00	30.47
1865	CG	LEU	A	452	64.687	−3.314	103.885	1.00	21.32
1866	CD1	LEU	A	452	64.116	−3.523	105.260	1.00	27.16
1867	CD2	LEU	A	452	64.959	−1.820	103.642	1.00	23.69
1868	C	LEU	A	452	64.839	−6.149	102.940	1.00	26.24
1869	O	LEU	A	452	63.734	−6.521	103.327	1.00	25.87
1870	N	LEU	A	453	65.206	−6.176	101.657	1.00	25.20
1871	CA	LEU	A	453	64.325	−6.665	100.605	1.00	24.92
1872	CB	LEU	A	453	64.973	−6.487	99.234	1.00	19.86
1873	CG	LEU	A	453	65.268	−5.025	98.933	1.00	21.10
1874	CD1	LEU	A	453	65.936	−4.836	97.561	1.00	17.34
1875	CD2	LEU	A	453	63.942	−4.295	98.975	1.00	10.81
1876	C	LEU	A	453	64.037	−8.125	100.835	1.00	26.37
1877	O	LEU	A	453	62.884	−8.565	100.836	1.00	28.39
1878	N	SER	A	454	65.110	−8.880	101.024	1.00	29.03
1879	CA	SER	A	454	65.013	−10.315	101.266	1.00	27.64
1880	CB	SER	A	454	66.397	−10.859	101.638	1.00	20.09
1881	OG	SER	A	454	66.275	−12.168	102.148	1.00	34.94
1882	C	SER	A	454	64.004	−10.660	102.377	1.00	23.26
1883	O	SER	A	454	63.401	−11.723	102.368	1.00	22.09
1884	N	GLU	A	455	63.828	−9.743	103.321	1.00	19.56
1885	CA	GLU	A	455	62.935	−9.975	104.428	1.00	20.53
1886	CB	GLU	A	455	63.162	−8.919	105.473	1.00	17.19
1887	CG	GLU	A	455	62.467	−9.149	106.738	1.00	28.76
1888	CD	GLU	A	455	62.962	−8.167	107.813	1.00	36.58
1889	OE1	GLU	A	455	64.138	−8.236	108.230	1.00	34.71
1890	OE2	GLU	A	455	62.187	−7.292	108.241	1.00	34.84
1891	C	GLU	A	455	61.523	−9.945	103.955	1.00	24.54
1892	O	GLU	A	455	60.768	−10.879	104.206	1.00	25.12
1893	N	ILE	A	456	61.187	−8.880	103.229	1.00	28.65
1894	CA	ILE	A	456	59.847	−8.657	102.688	1.00	28.59
1895	CB	ILE	A	456	59.691	−7.181	102.223	1.00	35.98
1896	CG2	ILE	A	456	58.287	−6.906	101.712	1.00	44.98
1897	CG1	ILE	A	456	59.972	−6.255	103.391	1.00	39.73
1898	CD1	ILE	A	456	60.085	−4.841	102.959	1.00	48.93
1899	C	ILE	A	456	59.473	−9.527	101.524	1.00	24.83
1900	O	ILE	A	456	58.292	−9.774	101.305	1.00	23.51
1901	N	TRP	A	457	60.480	−10.011	100.801	1.00	26.84
1902	CA	TRP	A	457	60.237	−10.789	99.594	1.00	30.79
1903	CB	TRP	A	457	60.793	−10.025	98.378	1.00	30.70
1904	CG	TRP	A	457	60.180	−8.671	98.224	1.00	26.75
1905	CD2	TRP	A	457	60.724	−7.544	97.533	1.00	25.63
1906	CE2	TRP	A	457	59.788	−6.485	97.660	1.00	28.89
1907	CE3	TRP	A	457	61.914	−7.313	96.836	1.00	17.92
1908	CD1	TRP	A	457	58.966	−8.270	98.716	1.00	21.14
1909	NE1	TRP	A	457	58.723	−6.971	98.383	1.00	16.57
1910	CZ2	TRP	A	457	59.992	−5.216	97.095	1.00	23.51
1911	CZ3	TRP	A	457	62.112	−6.066	96.283	1.00	27.28
1912	CH2	TRP	A	457	61.152	−5.024	96.423	1.00	22.51
1913	C	TRP	A	457	60.710	−12.214	99.538	1.00	31.41
1914	O	TRP	A	457	60.088	−13.063	98.892	1.00	29.63
1915	N	ASP	A	458	61.818	−12.479	100.197	1.00	32.34
1916	CA	ASP	A	458	62.337	−13.814	100.159	1.00	35.03
1917	CB	ASP	A	458	63.768	−13.824	100.670	1.00	34.90
1918	CG	ASP	A	458	64.769	−13.691	99.569	1.00	38.51
1919	OD1	ASP	A	458	64.570	−14.363	98.521	1.00	43.44
1920	OD2	ASP	A	458	65.762	−12.945	99.769	1.00	42.94
1921	C	ASP	A	458	61.482	−14.771	100.971	1.00	40.93
1922	O	ASP	A	458	60.890	−14.395	101.989	1.00	41.04
1923	N	VAL	A	459	61.392	−16.012	100.502	1.00	47.90
1924	CA	VAL	A	459	60.634	−17.040	101.215	1.00	51.13
1925	CB	VAL	A	459	60.116	−18.089	100.266	1.00	36.52
1926	CG1	VAL	A	459	59.392	−19.139	101.029	1.00	46.60
1927	CG2	VAL	A	459	59.202	−17.439	99.278	1.00	44.26
1928	C	VAL	A	459	61.599	−17.699	102.193	1.00	58.53
1929	O	VAL	A	459	62.471	−18.482	101.794	1.00	60.86
1930	N	HIS	A	460	61.454	−17.382	103.472	1.00	65.09
1931	CA	HIS	A	460	62.350	−17.948	104.474	1.00	75.10
1932	CB	HIS	A	460	63.470	−16.945	104.783	1.00	78.97
1933	CG	HIS	A	460	62.963	−15.598	105.207	1.00	83.29
1934	CD2	HIS	A	460	63.001	−14.961	106.405	1.00	85.25
1935	ND1	HIS	A	460	62.268	−14.759	104.360	1.00	84.43
1936	CE1	HIS	A	460	61.898	−13.670	105.011	1.00	78.08
1937	NE2	HIS	A	460	62.331	−13.768	106.256	1.00	85.09
1938	C	HIS	A	460	61.595	−18.282	105.751	1.00	77.65
1939	O	HIS	A	460	60.932	−17.394	106.305	1.00	80.63
1940	N	ALA	A	461	61.701	−19.539	106.205	1.00	76.94
1941	CA	ALA	A	461	61.032	−19.991	107.429	1.00	77.86
1942	CB	ALA	A	461	62.036	−20.677	108.335	1.00	68.64
1943	C	ALA	A	461	60.326	−18.851	108.198	1.00	81.03
1944	O	ALA	A	461	60.979	−17.817	108.514	1.00	84.40
1945	OT	ALA	A	461	59.108	−18.987	108.475	1.00	81.32
1946		ALA	A	461
1947	CB	ALA	B	218	19.034	7.478	89.070	1.00	43.15
1948	C	ALA	B	218	17.931	5.243	89.097	1.00	46.46
1949	O	ALA	B	218	18.818	4.400	89.085	1.00	52.84
1950	N	ALA	B	218	18.545	6.261	91.233	1.00	43.35
1951	CA	ALA	B	218	18.073	6.541	89.839	1.00	47.62
1952	N	ALA	B	219	16.788	5.128	88.454	1.00	44.52
1953	CA	ALA	B	219	16.409	3.957	87.713	1.00	41.03
1954	CB	ALA	B	219	14.932	4.005	87.422	1.00	34.92
1955	C	ALA	B	219	17.137	3.602	86.440	1.00	41.94
1956	O	ALA	B	219	17.480	4.420	85.616	1.00	44.70
1957	N	LEU	B	220	17.324	2.297	86.334	1.00	42.54
1958	CA	LEU	B	220	17.916	1.521	85.247	1.00	34.74
1959	CB	LEU	B	220	17.599	0.059	85.510	1.00	42.30
1960	CG	LEU	B	220	18.568	−0.758	86.318	1.00	37.19
1961	CD1	LEU	B	220	18.090	−2.155	86.542	1.00	46.36
1962	CD2	LEU	B	220	19.816	−0.778	85.512	1.00	47.29
1963	C	LEU	B	220	17.235	1.846	83.934	1.00	32.94
1964	O	LEU	B	220	16.066	2.210	83.879	1.00	27.71
1965	N	THR	B	221	17.947	1.664	82.847	1.00	31.90
1966	CA	THR	B	221	17.305	1.913	81.579	1.00	31.38
1967	CB	THR	B	221	18.289	2.280	80.478	1.00	27.57
1968	OG1	THR	B	221	19.084	1.137	80.152	1.00	29.79
1969	CG2	THR	B	221	19.160	3.402	80.917	1.00	17.32
1970	C	THR	B	221	16.660	0.565	81.201	1.00	33.47
1971	O	THR	B	221	16.822	−0.457	81.904	1.00	39.22
1972	N	ALA	B	222	15.915	0.569	80.103	1.00	27.17
1973	CA	ALA	B	222	15.240	−0.625	79.640	1.00	25.42
1974	CB	ALA	B	222	14.261	−0.253	78.495	1.00	10.46
1975	C	ALA	B	222	16.306	−1.579	79.145	1.00	23.41
1976	O	ALA	B	222	16.246	−2.793	79.414	1.00	20.42
1977	N	ALA	B	223	17.274	−1.013	78.424	1.00	20.88
1978	CA	ALA	B	223	18.341	−1.809	77.874	1.00	24.15
1979	CB	ALA	B	223	19.287	−0.931	77.082	1.00	20.53
1980	C	ALA	B	223	19.083	−2.542	78.993	1.00	28.88
1981	O	ALA	B	223	19.419	−3.748	78.865	1.00	28.82
1982	N	GLN	B	224	19.334	−1.826	80.093	1.00	29.60
1983	CA	GLN	B	224	20.056	−2.423	81.211	1.00	31.76
1984	CB	GLN	B	224	20.563	−1.320	82.158	1.00	27.51
1985	CG	GLN	B	224	21.613	−0.405	81.584	1.00	29.93
1986	CD	GLN	B	224	22.080	0.627	82.596	1.00	33.83
1987	OE1	GLN	B	224	21.263	1.292	83.253	1.00	25.53
1988	NE2	GLN	B	224	23.397	0.779	82.719	1.00	28.08
1989	C	GLN	B	224	19.207	−3.461	81.983	1.00	30.31
1990	O	GLN	B	224	19.723	−4.440	82.527	1.00	29.42
1991	N	GLU	B	225	17.906	−3.239	82.026	1.00	29.37
1992	CA	GLU	B	225	17.048	−4.150	82.720	1.00	30.65
1993	CB	GLU	B	225	15.651	−3.573	82.868	1.00	39.85
1994	CG	GLU	B	225	14.883	−4.208	84.022	1.00	48.26
1995	CD	GLU	B	225	13.600	−3.484	84.317	1.00	56.77
1996	OE1	GLU	B	225	13.649	−2.238	84.448	1.00	65.13
1997	OE2	GLU	B	225	12.552	−4.160	84.418	1.00	49.77
1998	C	GLU	B	225	16.993	−5.440	81.943	1.00	29.19
1999	O	GLU	B	225	17.083	−6.522	82.538	1.00	31.21
2000	N	LEU	B	226	16.850	−5.335	80.621	1.00	26.33
2001	CA	LEU	B	226	16.807	−6.527	79.779	1.00	27.01
2002	CB	LEU	B	226	16.699	−6.185	78.302	1.00	23.38
2003	CG	LEU	B	226	15.535	−6.924	77.627	1.00	31.95
2004	CD1	LEU	B	226	15.517	−8.381	78.105	1.00	34.89
2005	CD2	LEU	B	226	14.186	−6.253	78.003	1.00	29.33
2006	C	LEU	B	226	18.054	−7.349	79.967	1.00	28.78
2007	O	LEU	B	226	17.977	−8.537	80.302	1.00	32.80
2008	N	MET	B	227	19.201	−6.702	79.771	1.00	27.80
2009	CA	MET	B	227	20.515	−7.342	79.898	1.00	27.07
2010	CB	MET	B	227	21.590	−6.285	79.727	1.00	22.08
2011	CG	MET	B	227	22.970	−6.838	79.790	1.00	30.34
2012	SD	MET	B	227	23.710	−6.385	81.297	1.00	33.46
2013	CE	MET	B	227	23.478	−4.568	81.248	1.00	42.18
2014	C	MET	B	227	20.733	−8.099	81.212	1.00	26.99
2015	O	MET	B	227	21.194	−9.240	81.231	1.00	27.73
2016	N	ILE	B	228	20.393	−7.444	82.312	1.00	26.23
2017	CA	ILE	B	228	20.523	−8.043	83.633	1.00	21.67
2018	CB	ILE	B	228	20.181	−7.039	84.776	1.00	18.41
2019	CG2	ILE	B	228	20.292	−7.744	86.087	1.00	14.71
2020	CG1	ILE	B	228	21.122	−5.825	84.734	1.00	11.85
2021	CD1	ILE	B	228	20.822	−4.797	85.744	1.00	5.36
2022	C	ILE	B	228	19.582	−9.227	83.758	1.00	19.46
2023	O	ILE	B	228	19.979	−10.299	84.207	1.00	13.61
2024	N	GLN	B	229	18.336	−9.025	83.344	1.00	23.63
2025	CA	GLN	B	229	17.327	−10.080	83.409	1.00	28.46
2026	CB	GLN	B	229	15.990	−9.587	82.881	1.00	28.33
2027	CG	GLN	B	229	14.828	−10.407	83.399	1.00	38.50
2028	CD	GLN	B	229	13.560	−10.231	82.552	1.00	52.93
2029	OE1	GLN	B	229	13.351	−10.913	81.513	1.00	43.06
2030	NE2	GLN	B	229	12.713	−9.303	82.982	1.00	52.10
2031	C	GLN	B	229	17.764	−11.292	82.613	1.00	28.34
2032	O	GLN	B	229	17.600	−12.432	83.064	1.00	31.45
2033	N	GLN	B	230	18.352	−11.041	81.449	1.00	28.55
2034	CA	GLN	B	230	18.840	−12.110	80.575	1.00	33.32
2035	CB	GLN	B	230	19.151	−11.527	79.203	1.00	40.65
2036	CG	GLN	B	230	17.968	−10.761	78.647	1.00	51.44
2037	CD	GLN	B	230	18.292	−10.024	77.374	1.00	60.22
2038	OE1	GLN	B	230	19.391	−9.433	77.211	1.00	66.06
2039	NE2	GLN	B	230	17.330	−10.034	76.452	1.00	56.15
2040	C	GLN	B	230	20.081	−12.839	81.118	1.00	34.16
2041	O	GLN	B	230	20.192	−14.061	81.000	1.00	34.60
2042	N	LEU	B	231	21.022	−12.086	81.690	1.00	33.62
2043	CA	LEU	B	231	22.232	−12.672	82.247	1.00	27.03
2044	CB	LEU	B	231	23.105	−11.596	82.862	1.00	24.13
2045	CG	LEU	B	231	24.142	−10.884	82.027	1.00	30.54
2046	CD1	LEU	B	231	25.107	−10.252	83.033	1.00	39.41
2047	CD2	LEU	B	231	24.901	−11.854	81.118	1.00	21.02
2048	C	LEU	B	231	21.838	−13.656	83.331	1.00	25.58
2049	O	LEU	B	231	22.368	−14.754	83.421	1.00	24.70
2050	N	VAL	B	232	20.901	−13.252	84.172	1.00	23.19
2051	CA	VAL	B	232	20.478	−14.123	85.237	1.00	20.58
2052	CB	VAL	B	232	19.534	−13.397	86.181	1.00	19.93
2053	CG1	VAL	B	232	18.784	−14.414	87.042	1.00	6.79
2054	CG2	VAL	B	232	20.365	−12.359	87.027	1.00	5.25
2055	C	VAL	B	232	19.809	−15.346	84.658	1.00	20.54
2056	O	VAL	B	232	20.014	−16.461	85.156	1.00	24.31
2057	N	ALA	B	233	19.013	−15.145	83.609	1.00	18.87
2058	CA	ALA	B	233	18.334	−16.272	82.970	1.00	17.83
2059	CB	ALA	B	233	17.430	−15.786	81.857	1.00	13.61
2060	C	ALA	B	233	19.361	−17.247	82.416	1.00	15.43
2061	O	ALA	B	233	19.247	−18.457	82.583	1.00	15.77
2062	N	ALA	B	234	20.375	−16.701	81.763	1.00	19.63
2063	CA	ALA	B	234	21.435	−17.500	81.165	1.00	23.28
2064	CB	ALA	B	234	22.367	−16.612	80.382	1.00	17.57
2065	C	ALA	B	234	22.207	−18.240	82.254	1.00	27.69
2066	O	ALA	B	234	22.658	−19.372	82.050	1.00	34.29
2067	N	GLN	B	235	22.347	−17.626	83.421	1.00	24.90
2068	CA	GLN	B	235	23.075	−18.279	84.484	1.00	26.11
2069	CB	GLN	B	235	23.219	−17.344	85.662	1.00	30.42
2070	CG	GLN	B	235	24.135	−17.845	86.735	1.00	42.13
2071	CD	GLN	B	235	25.458	−17.067	86.789	1.00	50.21
2072	OE1	GLN	B	235	25.674	−16.205	87.680	1.00	33.87
2073	NE2	GLN	B	235	26.348	−17.351	85.819	1.00	46.88
2074	C	GLN	B	235	22.310	−19.491	84.919	1.00	26.10
2075	O	GLN	B	235	22.888	−20.519	85.235	1.00	27.29
2076	N	LEU	B	236	20.988	−19.371	84.901	1.00	28.38
2077	CA	LEU	B	236	20.123	−20.465	85.337	1.00	30.72
2078	CB	LEU	B	236	18.703	−19.945	85.664	1.00	27.81
2079	CG	LEU	B	236	17.924	−20.844	86.651	1.00	28.43
2080	CD1	LEU	B	236	18.850	−21.322	87.773	1.00	11.13
2081	CD2	LEU	B	236	16.768	−20.057	87.251	1.00	18.53
2082	C	LEU	B	236	20.043	−21.610	84.335	1.00	30.32
2083	O	LEU	B	236	20.228	−22.794	84.676	1.00	28.58
2084	N	GLN	B	237	19.783	−21.250	83.091	1.00	26.79
2085	CA	GLN	B	237	19.687	−22.249	82.069	1.00	28.98
2086	CB	GLN	B	237	19.259	−21.576	80.760	1.00	35.06
2087	CG	GLN	B	237	17.742	−21.445	80.658	1.00	47.36
2088	CD	GLN	B	237	17.128	−22.745	80.202	1.00	53.79
2089	OE1	GLN	B	237	16.011	−23.102	80.584	1.00	60.26
2090	NE2	GLN	B	237	17.872	−23.473	79.366	1.00	42.25
2091	C	GLN	B	237	20.990	−23.031	81.918	1.00	28.95
2092	O	GLN	B	237	20.979	−24.268	81.847	1.00	28.13
2093	N	CYS	B	238	22.111	−22.315	81.881	1.00	28.66
2094	CA	CYS	B	238	23.397	−22.972	81.729	1.00	29.72
2095	CB	CYS	B	238	24.507	−21.942	81.564	1.00	34.27
2096	SG	CYS	B	238	24.593	−21.236	79.948	1.00	27.05
2097	C	CYS	B	238	23.680	−23.845	82.933	1.00	26.51
2098	O	CYS	B	238	24.299	−24.913	82.819	1.00	24.18
2099	N	ASN	B	239	23.204	−23.392	84.083	1.00	24.48
2100	CA	ASN	B	239	23.413	−24.149	85.290	1.00	28.69
2101	CB	ASN	B	239	23.089	−23.285	86.518	1.00	25.28
2102	CG	ASN	B	239	23.332	−24.028	87.820	1.00	29.79
2103	OD1	ASN	B	239	24.423	−24.519	88.053	1.00	32.08
2104	ND2	ASN	B	239	22.311	−24.119	88.669	1.00	42.98
2105	C	ASN	B	239	22.548	−25.430	85.274	1.00	31.07
2106	O	ASN	B	239	22.998	−26.550	85.621	1.00	29.58
2107	N	ALA	B	240	21.303	−25.263	84.846	1.00	31.87
2108	CA	ALA	B	240	20.380	−26.392	84.803	1.00	32.86
2109	CB	ALA	B	240	18.951	−25.912	84.500	1.00	19.97
2110	C	ALA	B	240	20.833	−27.385	83.756	1.00	35.15
2111	O	ALA	B	240	20.611	−28.567	83.881	1.00	38.25
2112	N	ARG	B	241	21.495	−26.886	82.724	1.00	38.35
2113	CA	ARG	B	241	21.977	−27.692	81.605	1.00	37.53
2114	CB	ARG	B	241	22.541	−26.766	80.560	1.00	37.26
2115	CG	ARG	B	241	23.010	−27.420	79.286	1.00	40.31
2116	CD	ARG	B	241	22.676	−26.557	78.049	1.00	48.97
2117	NE	ARG	B	241	22.668	−25.105	78.299	1.00	59.22
2118	CZ	ARG	B	241	21.778	−24.271	77.761	1.00	58.75
2119	NH1	ARG	B	241	20.858	−24.767	76.952	1.00	58.70
2120	NH2	ARG	B	241	21.770	−22.967	78.066	1.00	53.27
2121	C	ARG	B	241	23.047	−28.699	81.959	1.00	39.86
2122	O	ARG	B	241	23.026	−29.840	81.534	1.00	42.08
2123	N	SER	B	242	23.981	−28.259	82.776	1.00	42.38
2124	CA	SER	B	242	25.109	−29.069	83.161	1.00	39.72
2125	CB	SER	B	242	26.323	−28.140	83.355	1.00	44.91
2126	OG	SER	B	242	26.690	−27.421	82.175	1.00	39.22
2127	C	SER	B	242	24.904	−29.917	84.394	1.00	38.57
2128	O	SER	B	242	25.572	−30.929	84.543	1.00	31.83
2129	N	PHE	B	243	23.966	−29.513	85.250	1.00	41.47
2130	CA	PHE	B	243	23.736	−30.217	86.497	1.00	42.59
2131	CB	PHE	B	243	24.229	−29.345	87.639	1.00	41.86
2132	CG	PHE	B	243	25.712	−29.064	87.593	1.00	41.55
2133	CD1	PHE	B	243	26.206	−27.924	86.946	1.00	41.40
2134	CD2	PHE	B	243	26.621	−29.956	88.201	1.00	35.89
2135	CE1	PHE	B	243	27.603	−27.672	86.904	1.00	41.54
2136	CE2	PHE	B	243	28.009	−29.724	88.167	1.00	33.17
2137	CZ	PHE	B	243	28.501	−28.575	87.515	1.00	44.01
2138	C	PHE	B	243	22.346	−30.730	86.824	1.00	44.54
2139	O	PHE	B	243	22.173	−31.408	87.815	1.00	49.89
2140	N	SER	B	244	21.355	−30.398	86.013	1.00	45.17
2141	CA	SER	B	244	20.013	−30.917	86.225	1.00	44.26
2142	CB	SER	B	244	19.172	−30.724	84.975	1.00	48.33
2143	OG	SER	B	244	18.426	−29.525	85.050	1.00	51.93
2144	C	SER	B	244	20.112	−32.402	86.496	1.00	46.85
2145	O	SER	B	244	19.657	−32.890	87.522	1.00	49.00
2146	N	ASP	B	245	20.717	−33.106	85.550	1.00	49.90
2147	CA	ASP	B	245	20.938	−34.530	85.655	1.00	52.24
2148	CB	ASP	B	245	21.253	−35.097	84.272	1.00	61.31
2149	CG	ASP	B	245	20.013	−35.253	83.453	1.00	73.36
2150	OD1	ASP	B	245	18.925	−35.317	84.092	1.00	81.72
2151	OD2	ASP	B	245	20.118	−35.316	82.203	1.00	79.76
2152	C	ASP	B	245	22.083	−34.775	86.611	1.00	49.00
2153	O	ASP	B	245	23.127	−34.151	86.512	1.00	50.73
2154	N	GLN	B	246	21.886	−35.677	87.550	1.00	45.53
2155	CA	GLN	B	246	22.928	−35.942	88.500	1.00	43.82
2156	CB	GLN	B	246	22.429	−36.961	89.497	1.00	49.76
2157	CG	GLN	B	246	23.483	−37.580	90.380	1.00	53.84
2158	CD	GLN	B	246	22.870	−37.989	91.686	1.00	54.86
2159	OE1	GLN	B	246	23.045	−39.112	92.155	1.00	55.22
2160	NE2	GLN	B	246	22.122	−37.066	92.287	1.00	56.87
2161	C	GLN	B	246	24.203	−36.419	87.837	1.00	43.71
2162	O	GLN	B	246	24.186	−37.286	86.960	1.00	44.65
2163	N	PRO	B	247	25.341	−35.853	88.252	1.00	43.54
2164	CD	PRO	B	247	25.529	−34.846	89.315	1.00	43.31
2165	CA	PRO	B	247	26.611	−36.269	87.651	1.00	43.57
2166	CB	PRO	B	247	27.665	−35.411	88.352	1.00	43.02
2167	CG	PRO	B	247	26.919	−34.345	89.074	1.00	41.73
2168	C	PRO	B	247	26.939	−37.735	87.855	1.00	45.12
2169	O	PRO	B	247	26.759	−38.268	88.954	1.00	44.37
2170	N	LYS	B	248	27.448	−38.362	86.792	1.00	48.61
2171	CA	LYS	B	248	27.897	−39.766	86.812	1.00	45.27
2172	CB	LYS	B	248	27.730	−40.391	85.424	1.00	50.09
2173	CG	LYS	B	248	26.380	−40.138	84.785	1.00	54.27
2174	CD	LYS	B	248	25.309	−41.021	85.407	1.00	37.79
2175	CE	LYS	B	248	24.054	−41.016	84.558	1.00	45.41
2176	NZ	LYS	B	248	23.084	−41.991	85.091	1.00	48.02
2177	C	LYS	B	248	29.399	−39.607	87.110	1.00	42.33
2178	O	LYS	B	248	30.246	−39.782	86.250	1.00	47.14
2179	N	VAL	B	249	29.728	−39.276	88.341	1.00	37.10
2180	CA	VAL	B	249	31.107	−39.014	88.698	1.00	33.75
2181	CB	VAL	B	249	31.175	−37.518	89.217	1.00	30.79
2182	CG1	VAL	B	249	32.573	−37.103	89.545	1.00	31.67
2183	CG2	VAL	B	249	30.612	−36.576	88.177	1.00	22.73
2184	C	VAL	B	249	31.652	−39.991	89.765	1.00	34.87
2185	O	VAL	B	249	30.892	−40.641	90.500	1.00	37.01
2186	N	THR	B	250	32.971	−40.115	89.848	1.00	32.17
2187	CA	THR	B	250	33.555	−40.935	90.902	1.00	31.48
2188	CB	THR	B	250	35.075	−40.691	91.007	1.00	30.25
2189	OG1	THR	B	250	35.711	−41.205	89.831	1.00	38.00
2190	CG2	THR	B	250	35.642	−41.378	92.248	1.00	25.30
2191	C	THR	B	250	32.870	−40.495	92.203	1.00	27.91
2192	O	THR	B	250	32.908	−39.320	92.552	1.00	26.73
2193	N	PRO	B	251	32.213	−41.425	92.922	1.00	28.52
2194	CD	PRO	B	251	32.263	−42.887	92.717	1.00	29.08
2195	CA	PRO	B	251	31.518	−41.087	94.184	1.00	28.02
2196	CB	PRO	B	251	30.795	−42.379	94.532	1.00	25.83
2197	CG	PRO	B	251	31.771	−43.428	94.058	1.00	30.66
2198	C	PRO	B	251	32.428	−40.620	95.337	1.00	24.48
2199	O	PRO	B	251	33.609	−41.024	95.405	1.00	23.99
2200	N	TRP	B	252	31.899	−39.755	96.208	1.00	19.10
2201	CA	TRP	B	252	32.685	−39.295	97.335	1.00	21.37
2202	CB	TRP	B	252	32.013	−38.096	97.975	1.00	18.10
2203	CG	TRP	B	252	32.754	−37.556	99.194	1.00	31.18
2204	CD2	TRP	B	252	33.789	−36.556	99.217	1.00	35.34
2205	CE2	TRP	B	252	34.150	−36.355	100.581	1.00	38.50
2206	CE3	TRP	B	252	34.463	−35.820	98.226	1.00	37.47
2207	CD1	TRP	B	252	32.535	−37.904	100.517	1.00	31.91
2208	NE1	TRP	B	252	33.366	−37.183	101.348	1.00	30.53
2209	CZ2	TRP	B	252	35.139	−35.424	100.969	1.00	33.94
2210	CZ3	TRP	B	252	35.453	−34.896	98.624	1.00	38.18
2211	CH2	TRP	B	252	35.779	−34.717	99.976	1.00	30.25
2212	C	TRP	B	252	32.802	−40.479	98.313	1.00	27.08
2213	O	TRP	B	252	31.830	−41.038	98.769	1.00	25.70
2214	N	PRO	B	253	34.012	−40.872	98.653	1.00	32.95
2215	CD	PRO	B	253	35.349	−40.373	98.286	1.00	42.21
2216	CA	PRO	B	253	34.082	−42.010	99.566	1.00	39.27
2217	CB	PRO	B	253	35.532	−42.483	99.409	1.00	36.35
2218	CG	PRO	B	253	36.272	−41.159	99.242	1.00	46.96
2219	C	PRO	B	253	33.752	−41.712	101.026	1.00	46.94
2220	O	PRO	B	253	33.999	−40.605	101.516	1.00	49.86
2221	N	LEU	B	254	33.216	−42.694	101.750	1.00	51.33
2222	CA	LEU	B	254	32.953	−42.526	103.192	1.00	57.46
2223	CB	LEU	B	254	31.395	−42.907	103.314	1.00	53.44
2224	CG	LEU	B	254	30.274	−42.099	102.497	1.00	56.64
2225	CD1	LEU	B	254	28.822	−42.493	102.882	1.00	52.37
2226	CD2	LEU	B	254	30.438	−40.584	102.757	1.00	56.12
2227	C	LEU	B	254	34.020	−43.213	104.160	1.00	60.78
2228	O	LEU	B	254	33.580	−43.849	105.300	1.00	64.15
2229	N	ALA	B	258	35.369	−42.937	103.834	1.00	65.16
2230	CA	ALA	B	258	36.450	−43.716	104.419	1.00	66.69
2231	CB	ALA	B	258	36.889	−44.471	103.293	1.00	72.53
2232	C	ALA	B	258	37.782	−43.192	105.164	1.00	70.13
2233	O	ALA	B	258	37.780	−42.100	105.635	1.00	71.40
2234	N	GLN	B	259	38.939	−43.934	105.136	1.00	72.67
2235	CA	GLN	B	259	40.241	−43.402	105.670	1.00	76.37
2236	CB	GLN	B	259	40.305	−43.514	107.206	1.00	68.08
2237	CG	GLN	B	259	41.502	−42.815	107.804	1.00	69.45
2238	CD	GLN	B	259	41.637	−41.366	107.330	1.00	76.44
2239	OE1	GLN	B	259	41.888	−41.087	106.147	1.00	76.42
2240	NE2	GLN	B	259	41.461	−40.438	108.254	1.00	80.79
2241	C	GLN	B	259	41.473	−44.121	105.020	1.00	79.69
2242	O	GLN	B	259	41.876	−45.192	105.497	1.00	85.25
2243	N	SER	B	260	42.110	−43.532	103.996	1.00	77.25
2244	CA	SER	B	260	43.195	−44.247	103.321	1.00	74.33
2245	CB	SER	B	260	42.564	−45.456	102.632	1.00	73.41
2246	OG	SER	B	260	43.486	−46.188	101.864	1.00	85.05
2247	C	SER	B	260	43.921	−43.391	102.287	1.00	74.57
2248	O	SER	B	260	43.700	−42.186	102.196	1.00	72.81
2249	N	ARG	B	261	44.785	−44.006	101.488	1.00	74.22
2250	CA	ARG	B	261	45.466	−43.213	100.476	1.00	74.23
2251	CB	ARG	B	261	46.889	−43.712	100.212	1.00	75.27
2252	CG	ARG	B	261	47.032	−44.508	98.959	1.00	81.06
2253	CD	ARG	B	261	48.426	−44.464	98.488	1.00	83.24
2254	NE	ARG	B	261	48.809	−43.162	97.961	1.00	78.10
2255	CZ	ARG	B	261	49.819	−43.022	97.121	1.00	74.06
2256	NH1	ARG	B	261	50.477	−44.107	96.756	1.00	72.36
2257	NH2	ARG	B	261	50.181	−41.823	96.678	1.00	73.29
2258	C	ARG	B	261	44.627	−43.306	99.208	1.00	73.70
2259	O	ARG	B	261	44.635	−42.398	98.374	1.00	75.08
2260	N	ASP	B	262	43.891	−44.410	99.080	1.00	70.69
2261	CA	ASP	B	262	43.022	−44.633	97.931	1.00	66.13
2262	CB	ASP	B	262	42.615	−46.117	97.868	1.00	73.04
2263	CG	ASP	B	262	43.741	−47.005	97.374	1.00	77.88
2264	OD1	ASP	B	262	44.905	−46.722	97.730	1.00	82.47
2265	OD2	ASP	B	262	43.468	−47.979	96.632	1.00	80.57
2266	C	ASP	B	262	41.805	−43.738	98.101	1.00	59.93
2267	O	ASP	B	262	41.185	−43.334	97.126	1.00	59.72
2268	N	ALA	B	263	41.494	−43.413	99.352	1.00	52.51
2269	CA	ALA	B	263	40.366	−42.561	99.652	1.00	47.78
2270	CB	ALA	B	263	40.012	−42.646	101.127	1.00	48.71
2271	C	ALA	B	263	40.688	−41.134	99.274	1.00	43.34
2272	O	ALA	B	263	39.812	−40.389	98.828	1.00	41.68
2273	N	ARG	B	264	41.946	−40.751	99.457	1.00	39.93
2274	CA	ARG	B	264	42.383	−39.400	99.106	1.00	43.90
2275	CB	ARG	B	264	43.821	−39.158	99.522	1.00	49.19
2276	CG	ARG	B	264	43.975	−37.848	100.271	1.00	56.17
2277	CD	ARG	B	264	45.403	−37.361	100.268	1.00	49.39
2278	NE	ARG	B	264	46.233	−37.978	101.289	1.00	46.87
2279	CZ	ARG	B	264	47.402	−38.513	101.019	1.00	56.69
2280	NH1	ARG	B	264	47.826	−38.500	99.767	1.00	62.48
2281	NH2	ARG	B	264	48.149	−39.018	101.996	1.00	66.89
2282	C	ARG	B	264	42.290	−39.200	97.599	1.00	45.41
2283	O	ARG	B	264	41.719	−38.220	97.100	1.00	46.21
2284	N	GLN	B	265	42.865	−40.138	96.868	1.00	43.29
2285	CA	GLN	B	265	42.788	−40.084	95.430	1.00	40.44
2286	CB	GLN	B	265	43.486	−41.331	94.836	1.00	51.49
2287	CG	GLN	B	265	43.962	−41.136	93.408	1.00	57.42
2288	CD	GLN	B	265	44.831	−39.884	93.300	1.00	68.00
2289	OE1	GLN	B	265	44.359	−38.806	92.939	1.00	71.18
2290	NE2	GLN	B	265	46.097	−40.019	93.653	1.00	68.29
2291	C	GLN	B	265	41.296	−40.032	94.968	1.00	38.02
2292	O	GLN	B	265	40.968	−39.357	93.981	1.00	35.36
2293	N	GLN	B	266	40.398	−40.737	95.661	1.00	30.69
2294	CA	GLN	B	266	39.022	−40.754	95.227	1.00	27.06
2295	CB	GLN	B	266	38.235	−41.787	95.990	1.00	28.96
2296	CG	GLN	B	266	37.447	−42.711	95.111	1.00	23.71
2297	CD	GLN	B	266	36.420	−43.468	95.896	1.00	21.89
2298	OE1	GLN	B	266	35.372	−42.935	96.183	1.00	21.16
2299	NE2	GLN	B	266	36.722	−44.717	96.260	1.00	30.55
2300	C	GLN	B	266	38.378	−39.415	95.419	1.00	27.40
2301	O	GLN	B	266	37.747	−38.876	94.487	1.00	29.30
2302	N	ARG	B	267	38.514	−38.877	96.631	1.00	24.33
2303	CA	ARG	B	267	37.920	−37.572	96.930	1.00	26.12
2304	CB	ARG	B	267	38.280	−37.143	98.361	1.00	25.38
2305	CG	ARG	B	267	38.071	−38.259	99.360	1.00	27.21
2306	CD	ARG	B	267	37.421	−37.794	100.678	1.00	34.15
2307	NE	ARG	B	267	38.348	−37.806	101.814	1.00	34.85
2308	CZ	ARG	B	267	38.780	−38.907	102.420	1.00	36.34
2309	NH1	ARG	B	267	38.363	−40.098	102.011	1.00	45.28
2310	NH2	ARG	B	267	39.658	−38.828	103.409	1.00	32.14
2311	C	ARG	B	267	38.491	−36.610	95.873	1.00	22.84
2312	O	ARG	B	267	37.790	−35.806	95.269	1.00	15.70
2313	N	PHE	B	268	39.785	−36.731	95.626	1.00	23.95
2314	CA	PHE	B	268	40.409	−35.895	94.613	1.00	25.07
2315	CB	PHE	B	268	41.904	−36.184	94.530	1.00	24.74
2316	CG	PHE	B	268	42.607	−35.373	93.493	1.00	25.39
2317	CD1	PHE	B	268	42.895	−35.917	92.257	1.00	16.45
2318	CD2	PHE	B	268	42.950	−34.043	93.736	1.00	27.98
2319	CE1	PHE	B	268	43.503	−35.165	91.282	1.00	11.20
2320	CE2	PHE	B	268	43.573	−33.271	92.742	1.00	14.52
2321	CZ	PHE	B	268	43.848	−33.837	91.523	1.00	14.38
2322	C	PHE	B	268	39.770	−36.089	93.229	1.00	22.23
2323	O	PHE	B	268	39.548	−35.130	92.488	1.00	24.28
2324	N	ALA	B	269	39.495	−37.330	92.865	1.00	17.72
2325	CA	ALA	B	269	38.871	−37.587	91.575	1.00	15.85
2326	CB	ALA	B	269	38.697	−39.087	91.327	1.00	8.82
2327	C	ALA	B	269	37.527	−36.913	91.601	1.00	14.49
2328	O	ALA	B	269	37.184	−36.165	90.664	1.00	13.42
2329	N	HIS	B	270	36.778	−37.160	92.684	1.00	12.69
2330	CA	HIS	B	270	35.453	−36.570	92.828	1.00	17.33
2331	CB	HIS	B	270	34.978	−36.787	94.254	1.00	8.12
2332	CG	HIS	B	270	33.552	−36.393	94.493	1.00	10.92
2333	CD2	HIS	B	270	33.006	−35.389	95.224	1.00	15.72
2334	ND1	HIS	B	270	32.491	−37.145	94.040	1.00	5.25
2335	CE1	HIS	B	270	31.359	−36.637	94.491	1.00	5.25
2336	NE2	HIS	B	270	31.643	−35.572	95.216	1.00	5.25
2337	C	HIS	B	270	35.477	−35.047	92.466	1.00	17.96
2338	O	HIS	B	270	34.770	−34.568	91.570	1.00	18.90
2339	N	PHE	B	271	36.333	−34.300	93.140	1.00	20.16
2340	CA	PHE	B	271	36.426	−32.876	92.880	1.00	23.78
2341	CB	PHE	B	271	37.450	−32.216	93.790	1.00	21.72
2342	CG	PHE	B	271	36.886	−31.701	95.056	1.00	14.87
2343	CD1	PHE	B	271	35.683	−32.169	95.537	1.00	19.48
2344	CD2	PHE	B	271	37.608	−30.792	95.821	1.00	25.55
2345	CE1	PHE	B	271	35.184	−31.742	96.799	1.00	37.20
2346	CE2	PHE	B	271	37.133	−30.354	97.076	1.00	36.95
2347	CZ	PHE	B	271	35.906	−30.839	97.570	1.00	35.14
2348	C	PHE	B	271	36.786	−32.579	91.457	1.00	22.69
2349	O	PHE	B	271	36.042	−31.890	90.800	1.00	21.96
2350	N	THR	B	272	37.917	−33.102	90.989	1.00	25.49
2351	CA	THR	B	272	38.384	−32.863	89.626	1.00	27.42
2352	CB	THR	B	272	39.608	−33.695	89.306	1.00	26.81
2353	OG1	THR	B	272	39.429	−35.012	89.825	1.00	31.00
2354	CG2	THR	B	272	40.847	−33.075	89.948	1.00	35.42
2355	C	THR	B	272	37.309	−33.174	88.612	1.00	32.00
2356	O	THR	B	272	37.042	−32.340	87.722	1.00	35.46
2357	N	GLU	B	273	36.669	−34.348	88.731	1.00	31.84
2358	CA	GLU	B	273	35.600	−34.701	87.785	1.00	28.90
2359	CB	GLU	B	273	35.083	−36.112	88.056	1.00	24.12
2360	CG	GLU	B	273	36.140	−37.185	87.911	1.00	23.98
2361	CD	GLU	B	273	35.649	−38.584	88.369	1.00	23.19
2362	OE1	GLU	B	273	36.451	−39.488	88.617	1.00	21.84
2363	OE2	GLU	B	273	34.446	−38.797	88.483	1.00	23.39
2364	C	GLU	B	273	34.434	−33.684	87.779	1.00	26.54
2365	O	GLU	B	273	33.786	−33.498	86.749	1.00	26.59
2366	N	LEU	B	274	34.177	−33.031	88.916	1.00	23.99
2367	CA	LEU	B	274	33.110	−32.034	89.008	1.00	24.74
2368	CB	LEU	B	274	32.719	−31.761	90.483	1.00	26.78
2369	CG	LEU	B	274	31.960	−32.918	91.164	1.00	32.47
2370	CD1	LEU	B	274	31.737	−32.573	92.582	1.00	35.05
2371	CD2	LEU	B	274	30.627	−33.199	90.490	1.00	12.62
2372	C	LEU	B	274	33.590	−30.756	88.334	1.00	22.06
2373	O	LEU	B	274	32.895	−30.191	87.499	1.00	23.23
2374	N	ALA	B	275	34.788	−30.318	88.701	1.00	17.79
2375	CA	ALA	B	275	35.415	−29.136	88.138	1.00	16.53
2376	CB	ALA	B	275	36.901	−29.184	88.419	1.00	13.07
2377	C	ALA	B	275	35.173	−29.077	86.633	1.00	18.81
2378	O	ALA	B	275	34.791	−28.025	86.097	1.00	16.04
2379	N	ILE	B	276	35.410	−30.213	85.965	1.00	16.66
2380	CA	ILE	B	276	35.211	−30.336	84.532	1.00	16.32
2381	CB	ILE	B	276	35.528	−31.759	84.053	1.00	13.21
2382	CG2	ILE	B	276	35.144	−31.904	82.626	1.00	5.25
2383	CG1	ILE	B	276	37.027	−32.038	84.263	1.00	15.91
2384	CD1	ILE	B	276	37.448	−33.430	83.945	1.00	13.43
2385	C	ILE	B	276	33.797	−29.959	84.104	1.00	17.75
2386	O	ILE	B	276	33.616	−29.173	83.162	1.00	18.39
2387	N	ILE	B	277	32.789	−30.504	84.779	1.00	18.95
2388	CA	ILE	B	277	31.409	−30.146	84.417	1.00	19.47
2389	CB	ILE	B	277	30.370	−30.865	85.313	1.00	13.25
2390	CG2	ILE	B	277	28.989	−30.524	84.874	1.00	5.25
2391	CG1	ILE	B	277	30.580	−32.367	85.238	1.00	17.70
2392	CD1	ILE	B	277	29.506	−33.160	85.901	1.00	18.78
2393	C	ILE	B	277	31.311	−28.627	84.646	1.00	20.85
2394	O	ILE	B	277	30.694	−27.878	83.889	1.00	19.66
2395	N	SER	B	278	31.950	−28.173	85.711	1.00	22.75
2396	CA	SER	B	278	31.931	−26.768	86.016	1.00	23.72
2397	CB	SER	B	278	32.685	−26.516	87.317	1.00	21.12
2398	OG	SER	B	278	32.715	−25.120	87.581	1.00	22.54
2399	C	SER	B	278	32.536	−25.924	84.853	1.00	25.47
2400	O	SER	B	278	31.984	−24.852	84.531	1.00	25.59
2401	N	VAL	B	279	33.649	−26.380	84.245	1.00	22.83
2402	CA	VAL	B	279	34.256	−25.631	83.142	1.00	21.95
2403	CB	VAL	B	279	35.545	−26.284	82.603	1.00	19.86
2404	CG1	VAL	B	279	36.057	−25.500	81.376	1.00	9.36
2405	CG2	VAL	B	279	36.610	−26.268	83.653	1.00	16.85
2406	C	VAL	B	279	33.263	−25.553	81.992	1.00	23.30
2407	O	VAL	B	279	33.157	−24.526	81.301	1.00	25.73
2408	N	GLN	B	280	32.525	−26.640	81.803	1.00	21.66
2409	CA	GLN	B	280	31.527	−26.697	80.766	1.00	20.75
2410	CB	GLN	B	280	30.966	−28.120	80.653	1.00	25.14
2411	CG	GLN	B	280	32.012	−29.144	80.267	1.00	22.03
2412	CD	GLN	B	280	31.458	−30.563	80.305	1.00	41.57
2413	OE1	GLN	B	280	30.340	−30.809	80.804	1.00	47.16
2414	NE2	GLN	B	280	32.236	−31.509	79.783	1.00	36.98
2415	C	GLN	B	280	30.398	−25.697	81.047	1.00	19.68
2416	O	GLN	B	280	29.809	−25.156	80.093	1.00	17.78
2417	N	GLU	B	281	30.064	−25.473	82.329	1.00	16.74
2418	CA	GLU	B	281	29.014	−24.495	82.636	1.00	16.62
2419	CB	GLU	B	281	28.607	−24.546	84.098	1.00	8.05
2420	CG	GLU	B	281	27.475	−23.574	84.423	1.00	25.22
2421	CD	GLU	B	281	27.028	−23.649	85.882	1.00	29.00
2422	OE1	GLU	B	281	26.021	−22.965	86.242	1.00	29.66
2423	OE2	GLU	B	281	27.692	−24.391	86.656	1.00	27.05
2424	C	GLU	B	281	29.545	−23.084	82.280	1.00	16.32
2425	O	GLU	B	281	28.867	−22.312	81.548	1.00	9.48
2426	N	ILE	B	282	30.755	−22.779	82.786	1.00	15.22
2427	CA	ILE	B	282	31.429	−21.515	82.531	1.00	16.61
2428	CB	ILE	B	282	32.798	−21.492	83.185	1.00	12.62
2429	CG2	ILE	B	282	33.667	−20.365	82.596	1.00	11.77
2430	CG1	ILE	B	282	32.587	−21.243	84.673	1.00	15.38
2431	CD1	ILE	B	282	33.841	−21.159	85.506	1.00	8.99
2432	C	ILE	B	282	31.550	−21.212	81.040	1.00	18.29
2433	O	ILE	B	282	31.031	−20.180	80.558	1.00	14.48
2434	N	VAL	B	283	32.252	−22.082	80.316	1.00	15.81
2435	CA	VAL	B	283	32.363	−21.908	78.874	1.00	15.19
2436	CB	VAL	B	283	33.009	−23.127	78.275	1.00	7.26
2437	CG1	VAL	B	283	32.934	−23.062	76.811	1.00	7.61
2438	CG2	VAL	B	283	34.431	−23.206	78.710	1.00	6.21
2439	C	VAL	B	283	30.951	−21.706	78.221	1.00	17.61
2440	O	VAL	B	283	30.755	−20.882	77.325	1.00	20.88
2441	N	ASP	B	284	29.966	−22.435	78.721	1.00	18.45
2442	CA	ASP	B	284	28.614	−22.388	78.210	1.00	21.25
2443	CB	ASP	B	284	27.825	−23.516	78.871	1.00	35.01
2444	CG	ASP	B	284	26.585	−23.902	78.114	1.00	40.84
2445	OD1	ASP	B	284	26.695	−24.069	76.884	1.00	58.98
2446	OD2	ASP	B	284	25.515	−24.074	78.749	1.00	47.00
2447	C	ASP	B	284	27.957	−21.054	78.497	1.00	22.42
2448	O	ASP	B	284	27.123	−20.628	77.745	1.00	25.11
2449	N	PHE	B	285	28.310	−20.419	79.607	1.00	23.18
2450	CA	PHE	B	285	27.731	−19.141	79.984	1.00	20.36
2451	CB	PHE	B	285	27.863	−18.927	81.491	1.00	15.46
2452	CG	PHE	B	285	27.184	−17.683	81.969	1.00	28.69
2453	CD1	PHE	B	285	25.779	−17.633	82.025	1.00	22.82
2454	CD2	PHE	B	285	27.931	−16.539	82.310	1.00	22.64
2455	CE1	PHE	B	285	25.129	−16.474	82.408	1.00	29.41
2456	CE2	PHE	B	285	27.287	−15.364	82.698	1.00	34.28
2457	CZ	PHE	B	285	25.883	−15.322	82.749	1.00	33.57
2458	C	PHE	B	285	28.424	−17.972	79.244	1.00	22.96
2459	O	PHE	B	285	27.771	−16.987	78.851	1.00	26.62
2460	N	ALA	B	286	29.747	−18.050	79.085	1.00	19.90
2461	CA	ALA	B	286	30.460	−17.012	78.347	1.00	19.13
2462	CB	ALA	B	286	31.948	−17.373	78.215	1.00	14.49
2463	C	ALA	B	286	29.794	−16.865	76.949	1.00	18.53
2464	O	ALA	B	286	29.433	−15.754	76.538	1.00	20.73
2465	N	LYS	B	287	29.625	−17.982	76.240	1.00	15.74
2466	CA	LYS	B	287	28.995	−17.958	74.942	1.00	21.37
2467	CB	LYS	B	287	28.667	−19.373	74.480	1.00	33.02
2468	CG	LYS	B	287	29.817	−20.189	73.913	1.00	30.82
2469	CD	LYS	B	287	29.255	−21.152	72.890	1.00	40.12
2470	CE	LYS	B	287	30.245	−22.209	72.466	1.00	44.68
2471	NZ	LYS	B	287	30.510	−23.148	73.581	1.00	37.69
2472	C	LYS	B	287	27.702	−17.157	74.953	1.00	22.71
2473	O	LYS	B	287	27.255	−16.707	73.910	1.00	22.47
2474	N	GLN	B	288	27.117	−16.967	76.138	1.00	25.38
2475	CA	GLN	B	288	25.841	−16.256	76.278	1.00	23.59
2476	CB	GLN	B	288	24.912	−17.076	77.176	1.00	24.27
2477	CG	GLN	B	288	24.675	−18.469	76.639	1.00	28.01
2478	CD	GLN	B	288	23.224	−18.774	76.525	1.00	42.38
2479	OE1	GLN	B	288	22.640	−19.488	77.363	1.00	51.37
2480	NE2	GLN	B	288	22.601	−18.212	75.498	1.00	45.89
2481	C	GLN	B	288	25.919	−14.817	76.777	1.00	20.41
2482	O	GLN	B	288	24.895	−14.098	76.809	1.00	18.32
2483	N	VAL	B	289	27.122	−14.396	77.160	1.00	17.16
2484	CA	VAL	B	289	27.303	−13.035	77.633	1.00	18.12
2485	CB	VAL	B	289	28.555	−12.911	78.503	1.00	18.92
2486	CG1	VAL	B	289	28.756	−11.468	78.863	1.00	7.11
2487	CG2	VAL	B	289	28.405	−13.791	79.757	1.00	19.44
2488	C	VAL	B	289	27.472	−12.161	76.415	1.00	19.12
2489	O	VAL	B	289	28.429	−12.304	75.657	1.00	22.10
2490	N	PRO	B	290	26.540	−11.250	76.189	1.00	17.24
2491	CD	PRO	B	290	25.445	−10.859	77.086	1.00	19.88
2492	CA	PRO	B	290	26.624	−10.359	75.022	1.00	16.50
2493	CB	PRO	B	290	25.610	−9.268	75.345	1.00	9.12
2494	CG	PRO	B	290	24.614	−9.963	76.177	1.00	15.86
2495	C	PRO	B	290	28.031	−9.776	74.811	1.00	20.18
2496	O	PRO	B	290	28.652	−9.221	75.734	1.00	19.50
2497	N	GLY	B	291	28.533	−9.899	73.589	1.00	24.22
2498	CA	GLY	B	291	29.840	−9.354	73.308	1.00	19.13
2499	C	GLY	B	291	30.901	−10.410	73.325	1.00	18.84
2500	O	GLY	B	291	31.825	−10.372	72.525	1.00	25.00
2501	N	PHE	B	292	30.768	−11.383	74.206	1.00	18.68
2502	CA	PHE	B	292	31.795	−12.397	74.250	1.00	19.53
2503	CB	PHE	B	292	31.475	−13.491	75.280	1.00	19.98
2504	CG	PHE	B	292	32.624	−14.467	75.489	1.00	16.63
2505	CD1	PHE	B	292	33.768	−14.058	76.131	1.00	7.41
2506	CD2	PHE	B	292	32.565	−15.776	75.005	1.00	19.33
2507	CE1	PHE	B	292	34.838	−14.916	76.296	1.00	14.65
2508	CE2	PHE	B	292	33.635	−16.651	75.167	1.00	16.74
2509	CZ	PHE	B	292	34.778	−16.227	75.817	1.00	15.51
2510	C	PHE	B	292	32.113	−13.051	72.913	1.00	18.23
2511	O	PHE	B	292	33.291	−13.184	72.576	1.00	19.50
2512	N	LEU	B	293	31.089	−13.479	72.162	1.00	18.86
2513	CA	LEU	B	293	31.334	−14.145	70.851	1.00	21.39
2514	CB	LEU	B	293	30.117	−14.989	70.407	1.00	12.01
2515	CG	LEU	B	293	29.913	−16.208	71.350	1.00	20.64
2516	CD1	LEU	B	293	28.598	−16.911	71.160	1.00	14.53
2517	CD2	LEU	B	293	31.060	−17.156	71.128	1.00	13.13
2518	C	LEU	B	293	31.762	−13.226	69.701	1.00	22.36
2519	O	LEU	B	293	31.917	−13.661	68.571	1.00	22.27
2520	N	GLN	B	294	31.965	−11.954	70.000	1.00	24.19
2521	CA	GLN	B	294	32.425	−11.047	68.985	1.00	27.26
2522	CB	GLN	B	294	31.917	−9.663	69.284	1.00	30.86
2523	CG	GLN	B	294	30.408	−9.595	69.201	1.00	42.01
2524	CD	GLN	B	294	29.894	−8.225	69.558	1.00	49.66
2525	OE1	GLN	B	294	28.697	−7.945	69.428	1.00	57.97
2526	NE2	GLN	B	294	30.800	−7.353	70.019	1.00	49.92
2527	C	GLN	B	294	33.955	−11.067	68.945	1.00	27.72
2528	O	GLN	B	294	34.558	−10.640	67.967	1.00	31.18
2529	N	LEU	B	295	34.586	−11.568	70.005	1.00	23.34
2530	CA	LEU	B	295	36.038	−11.637	70.045	1.00	19.78
2531	CB	LEU	B	295	36.579	−11.666	71.494	1.00	13.80
2532	CG	LEU	B	295	36.213	−10.437	72.368	1.00	20.64
2533	CD1	LEU	B	295	36.591	−10.633	73.831	1.00	16.87
2534	CD2	LEU	B	295	36.833	−9.207	71.780	1.00	5.37
2535	C	LEU	B	295	36.522	−12.861	69.286	1.00	23.15
2536	O	LEU	B	295	35.770	−13.808	69.013	1.00	27.08
2537	N	GLY	B	296	37.797	−12.829	68.930	1.00	20.51
2538	CA	GLY	B	296	38.369	−13.926	68.181	1.00	22.00
2539	C	GLY	B	296	38.613	−15.083	69.115	1.00	24.52
2540	O	GLY	B	296	38.856	−14.879	70.294	1.00	26.91
2541	N	ARG	B	297	38.544	−16.299	68.585	1.00	24.81
2542	CA	ARG	B	297	38.758	−17.494	69.369	1.00	22.38
2543	CB	ARG	B	297	38.884	−18.685	68.435	1.00	14.04
2544	CG	ARG	B	297	37.824	−19.715	68.690	1.00	27.39
2545	CD	ARG	B	297	36.525	−19.321	68.018	1.00	38.77
2546	NE	ARG	B	297	35.344	−19.780	68.741	1.00	36.12
2547	CZ	ARG	B	297	34.228	−20.166	68.148	1.00	41.67
2548	NH1	ARG	B	297	34.151	−20.165	66.833	1.00	52.02
2549	NH2	ARG	B	297	33.177	−20.513	68.876	1.00	59.39
2550	C	ARG	B	297	39.983	−17.389	70.315	1.00	22.84
2551	O	ARG	B	297	39.952	−17.875	71.470	1.00	24.28
2552	N	GLU	B	298	41.047	−16.752	69.835	1.00	20.17
2553	CA	GLU	B	298	42.249	−16.567	70.636	1.00	18.15
2554	CB	GLU	B	298	43.283	−15.806	69.799	1.00	24.82
2555	CG	GLU	B	298	43.994	−16.663	68.776	1.00	40.30
2556	CD	GLU	B	298	44.975	−17.637	69.425	1.00	59.47
2557	OE1	GLU	B	298	45.919	−17.155	70.101	1.00	73.88
2558	OE2	GLU	B	298	44.809	−18.879	69.280	1.00	61.89
2559	C	GLU	B	298	41.944	−15.827	71.965	1.00	17.48
2560	O	GLU	B	298	42.270	−16.311	73.054	1.00	15.91
2561	N	ASP	B	299	41.301	−14.664	71.865	1.00	19.09
2562	CA	ASP	B	299	40.951	−13.852	73.018	1.00	16.81
2563	CB	ASP	B	299	40.294	−12.534	72.585	1.00	21.76
2564	CG	ASP	B	299	41.279	−11.505	72.019	1.00	28.31
2565	OD1	ASP	B	299	42.310	−11.253	72.659	1.00	26.29
2566	OD2	ASP	B	299	41.011	−10.919	70.930	1.00	42.01
2567	C	ASP	B	299	39.949	−14.587	73.902	1.00	18.84
2568	O	ASP	B	299	39.937	−14.347	75.117	1.00	19.02
2569	N	GLN	B	300	39.107	−15.444	73.293	1.00	14.38
2570	CA	GLN	B	300	38.072	−16.181	74.015	1.00	14.01
2571	CB	GLN	B	300	37.160	−16.932	73.057	1.00	12.01
2572	CG	GLN	B	300	35.794	−16.406	72.996	1.00	19.29
2573	CD	GLN	B	300	35.069	−16.819	71.734	1.00	35.24
2574	OE1	GLN	B	300	35.417	−16.386	70.634	1.00	32.75
2575	NE2	GLN	B	300	34.051	−17.660	71.882	1.00	41.69
2576	C	GLN	B	300	38.695	−17.166	74.927	1.00	14.12
2577	O	GLN	B	300	38.340	−17.265	76.094	1.00	15.64
2578	N	ILE	B	301	39.629	−17.918	74.374	1.00	15.96
2579	CA	ILE	B	301	40.310	−18.921	75.151	1.00	17.05
2580	CB	ILE	B	301	41.218	−19.750	74.249	1.00	11.32
2581	CG2	ILE	B	301	42.140	−20.674	75.096	1.00	5.57
2582	CG1	ILE	B	301	40.307	−20.560	73.313	1.00	10.47
2583	CD1	ILE	B	301	40.956	−20.976	72.023	1.00	8.58
2584	C	ILE	B	301	41.073	−18.178	76.204	1.00	16.30
2585	O	ILE	B	301	40.911	−18.422	77.382	1.00	14.82
2586	N	ALA	B	302	41.904	−17.247	75.781	1.00	18.66
2587	CA	ALA	B	302	42.660	−16.459	76.764	1.00	22.11
2588	CB	ALA	B	302	43.287	−15.206	76.078	1.00	25.04
2589	C	ALA	B	302	41.803	−16.005	77.985	1.00	20.32
2590	O	ALA	B	302	42.133	−16.284	79.148	1.00	17.57
2591	N	LEU	B	303	40.713	−15.295	77.700	1.00	17.46
2592	CA	LEU	B	303	39.823	−14.803	78.741	1.00	18.81
2593	CB	LEU	B	303	38.724	−13.935	78.154	1.00	7.57
2594	CG	LEU	B	303	39.180	−12.585	77.629	1.00	7.97
2595	CD1	LEU	B	303	37.974	−11.752	77.334	1.00	15.12
2596	CD2	LEU	B	303	40.013	−11.885	78.686	1.00	15.05
2597	C	LEU	B	303	39.181	−15.880	79.613	1.00	21.50
2598	O	LEU	B	303	38.929	−15.651	80.792	1.00	23.19
2599	N	LEU	B	304	38.901	−17.046	79.038	1.00	21.15
2600	CA	LEU	B	304	38.330	−18.127	79.819	1.00	17.97
2601	CB	LEU	B	304	37.754	−19.181	78.925	1.00	16.23
2602	CG	LEU	B	304	36.346	−18.908	78.446	1.00	19.16
2603	CD1	LEU	B	304	35.689	−20.216	78.103	1.00	34.29
2604	CD2	LEU	B	304	35.582	−18.246	79.514	1.00	25.48
2605	C	LEU	B	304	39.405	−18.760	80.676	1.00	19.88
2606	O	LEU	B	304	39.251	−18.916	81.893	1.00	26.25
2607	N	LYS	B	305	40.499	−19.121	80.029	1.00	14.19
2608	CA	LYS	B	305	41.629	−19.721	80.708	1.00	17.19
2609	CB	LYS	B	305	42.858	−19.681	79.767	1.00	19.18
2610	CG	LYS	B	305	44.134	−20.300	80.336	1.00	22.69
2611	CD	LYS	B	305	45.188	−20.446	79.256	1.00	31.13
2612	CE	LYS	B	305	46.538	−20.816	79.794	1.00	42.37
2613	NZ	LYS	B	305	46.514	−22.177	80.375	1.00	54.77
2614	C	LYS	B	305	41.959	−19.070	82.070	1.00	15.90
2615	O	LYS	B	305	42.185	−19.735	83.047	1.00	19.41
2616	N	ALA	B	306	41.958	−17.760	82.145	1.00	18.52
2617	CA	ALA	B	306	42.283	−17.111	83.389	1.00	15.98
2618	CB	ALA	B	306	42.919	−15.776	83.123	1.00	11.91
2619	C	ALA	B	306	41.117	−16.914	84.322	1.00	17.98
2620	O	ALA	B	306	41.329	−16.974	85.537	1.00	19.87
2621	N	SER	B	307	39.905	−16.680	83.792	1.00	17.73
2622	CA	SER	B	307	38.739	−16.421	84.672	1.00	25.04
2623	CB	SER	B	307	37.692	−15.593	83.953	1.00	24.67
2624	OG	SER	B	307	37.262	−16.308	82.812	1.00	33.34
2625	C	SER	B	307	38.031	−17.634	85.282	1.00	25.83
2626	O	SER	B	307	37.280	−17.475	86.244	1.00	21.14
2627	N	THR	B	308	38.290	−18.819	84.710	1.00	25.98
2628	CA	THR	B	308	37.691	−20.064	85.149	1.00	18.07
2629	CB	THR	B	308	38.323	−21.269	84.467	1.00	18.27
2630	OG1	THR	B	308	38.066	−21.207	83.066	1.00	12.82
2631	CG2	THR	B	308	37.743	−22.537	85.004	1.00	15.40
2632	C	THR	B	308	37.818	−20.251	86.624	1.00	17.49
2633	O	THR	B	308	36.823	−20.354	87.332	1.00	17.50
2634	N	ILE	B	309	39.040	−20.259	87.111	1.00	15.34
2635	CA	ILE	B	309	39.235	−20.467	88.539	1.00	15.21
2636	CB	ILE	B	309	40.738	−20.482	88.886	1.00	13.09
2637	CG2	ILE	B	309	41.349	−19.105	88.725	1.00	20.27
2638	CG1	ILE	B	309	40.926	−20.891	90.312	1.00	10.55
2639	CD1	ILE	B	309	40.405	−22.213	90.598	1.00	10.98
2640	C	ILE	B	309	38.543	−19.382	89.377	1.00	19.61
2641	O	ILE	B	309	37.942	−19.662	90.437	1.00	17.36
2642	N	GLU	B	310	38.614	−18.142	88.891	1.00	21.83
2643	CA	GLU	B	310	38.024	−17.041	89.626	1.00	24.74
2644	CB	GLU	B	310	38.473	−15.713	89.017	1.00	20.41
2645	CG	GLU	B	310	39.978	−15.592	88.940	1.00	20.71
2646	CD	GLU	B	310	40.446	−14.170	88.695	1.00	21.40
2647	OE1	GLU	B	310	39.575	−13.329	88.420	1.00	21.25
2648	OE2	GLU	B	310	41.672	−13.889	88.776	1.00	15.00
2649	C	GLU	B	310	36.491	−17.137	89.712	1.00	25.09
2650	O	GLU	B	310	35.862	−16.889	90.772	1.00	27.49
2651	N	ILE	B	311	35.890	−17.510	88.595	1.00	23.06
2652	CA	ILE	B	311	34.455	−17.680	88.538	1.00	20.02
2653	CB	ILE	B	311	33.986	−18.013	87.077	1.00	22.03
2654	CG2	ILE	B	311	32.467	−18.325	87.037	1.00	24.02
2655	CG1	ILE	B	311	34.283	−16.829	86.154	1.00	13.12
2656	CD1	ILE	B	311	33.588	−16.899	84.849	1.00	5.25
2657	C	ILE	B	311	34.060	−18.830	89.497	1.00	21.66
2658	O	ILE	B	311	33.125	−18.690	90.303	1.00	19.46
2659	N	MET	B	312	34.781	−19.954	89.436	1.00	16.11
2660	CA	MET	B	312	34.459	−21.083	90.324	1.00	13.84
2661	CB	MET	B	312	35.479	−22.210	90.188	1.00	14.56
2662	CG	MET	B	312	35.628	−22.790	88.815	1.00	17.34
2663	SD	MET	B	312	36.931	−24.091	88.709	1.00	16.56
2664	CE	MET	B	312	35.811	−25.492	88.752	1.00	37.17
2665	C	MET	B	312	34.445	−20.609	91.771	1.00	14.68
2666	O	MET	B	312	33.574	−20.995	92.574	1.00	14.77
2667	N	LEU	B	313	35.423	−19.782	92.112	1.00	12.44
2668	CA	LEU	B	313	35.449	−19.255	93.465	1.00	15.01
2669	CB	LEU	B	313	36.771	−18.557	93.683	1.00	11.43
2670	CG	LEU	B	313	37.924	−19.537	93.730	1.00	13.95
2671	CD1	LEU	B	313	39.176	−18.752	93.734	1.00	24.08
2672	CD2	LEU	B	313	37.846	−20.418	94.976	1.00	5.25
2673	C	LEU	B	313	34.248	−18.304	93.730	1.00	11.72
2674	O	LEU	B	313	33.721	−18.215	94.869	1.00	5.25
2675	N	LEU	B	314	33.823	−17.588	92.684	1.00	9.59
2676	CA	LEU	B	314	32.676	−16.721	92.878	1.00	12.83
2677	CB	LEU	B	314	32.414	−15.842	91.644	1.00	7.74
2678	CG	LEU	B	314	33.346	−14.608	91.510	1.00	13.68
2679	CD1	LEU	B	314	33.382	−14.060	90.117	1.00	5.25
2680	CD2	LEU	B	314	32.889	−13.530	92.466	1.00	5.25
2681	C	LEU	B	314	31.491	−17.625	93.200	1.00	12.72
2682	O	LEU	B	314	30.765	−17.361	94.157	1.00	10.28
2683	N	GLU	B	315	31.332	−18.716	92.437	1.00	16.60
2684	CA	GLU	B	315	30.235	−19.676	92.655	1.00	19.32
2685	CB	GLU	B	315	30.249	−20.797	91.623	1.00	20.97
2686	CG	GLU	B	315	29.891	−20.418	90.256	1.00	25.79
2687	CD	GLU	B	315	28.474	−20.048	90.136	1.00	24.04
2688	OE1	GLU	B	315	27.633	−20.671	90.812	1.00	30.51
2689	OE2	GLU	B	315	28.192	−19.129	89.350	1.00	35.73
2690	C	GLU	B	315	30.401	−20.325	94.042	1.00	22.91
2691	O	GLU	B	315	29.436	−20.433	94.829	1.00	25.74
2692	N	THR	B	316	31.620	−20.783	94.330	1.00	19.17
2693	CA	THR	B	316	31.918	−21.380	95.632	1.00	16.62
2694	CB	THR	B	316	33.393	−21.538	95.830	1.00	17.06
2695	OG1	THR	B	316	33.863	−22.615	95.011	1.00	20.32
2696	CG2	THR	B	316	33.669	−21.801	97.232	1.00	14.20
2697	C	THR	B	316	31.418	−20.448	96.704	1.00	13.14
2698	O	THR	B	316	30.828	−20.897	97.644	1.00	17.68
2699	N	ALA	B	317	31.663	−19.147	96.552	1.00	12.23
2700	CA	ALA	B	317	31.184	−18.156	97.505	1.00	10.33
2701	CB	ALA	B	317	31.714	−16.784	97.158	1.00	5.89
2702	C	ALA	B	317	29.658	−18.134	97.491	1.00	13.35
2703	O	ALA	B	317	29.024	−18.231	98.537	1.00	15.23
2704	N	ARG	B	318	29.063	−18.003	96.310	1.00	14.74
2705	CA	ARG	B	318	27.610	−17.976	96.210	1.00	14.84
2706	CB	ARG	B	318	27.193	−17.799	94.741	1.00	14.50
2707	CG	ARG	B	318	25.694	−18.024	94.503	1.00	14.19
2708	CD	ARG	B	318	25.184	−17.373	93.220	1.00	25.75
2709	NE	ARG	B	318	25.755	−17.926	91.994	1.00	23.63
2710	CZ	ARG	B	318	25.484	−17.446	90.778	1.00	34.61
2711	NH1	ARG	B	318	24.653	−16.424	90.636	1.00	34.00
2712	NH2	ARG	B	318	26.059	−17.967	89.699	1.00	31.00
2713	C	ARG	B	318	26.892	−19.202	96.808	1.00	17.70
2714	O	ARG	B	318	25.785	−19.072	97.320	1.00	18.96
2715	N	ARG	B	319	27.509	−20.386	96.726	1.00	20.72
2716	CA	ARG	B	319	26.921	−21.632	97.244	1.00	16.92
2717	CB	ARG	B	319	27.303	−22.800	96.329	1.00	18.39
2718	CG	ARG	B	319	26.921	−22.642	94.898	1.00	5.97
2719	CD	ARG	B	319	25.751	−23.607	94.553	1.00	28.69
2720	NE	ARG	B	319	25.163	−23.287	93.253	1.00	11.54
2721	CZ	ARG	B	319	25.913	−22.910	92.240	1.00	24.11
2722	NH1	ARG	B	319	27.250	−22.851	92.434	1.00	16.61
2723	NH2	ARG	B	319	25.327	−22.539	91.098	1.00	21.88
2724	C	ARG	B	319	27.390	−21.940	98.677	1.00	13.41
2725	O	ARG	B	319	27.282	−23.054	99.145	1.00	14.44
2726	N	TYR	B	320	27.919	−20.938	99.359	1.00	16.42
2727	CA	TYR	B	320	28.386	−21.074	100.733	1.00	19.36
2728	CB	TYR	B	320	29.586	−20.170	100.965	1.00	17.23
2729	CG	TYR	B	320	29.990	−20.112	102.426	1.00	12.95
2730	CD1	TYR	B	320	29.587	−19.082	103.223	1.00	9.66
2731	CE1	TYR	B	320	29.974	−18.993	104.518	1.00	7.34
2732	CD2	TYR	B	320	30.802	−21.073	102.983	1.00	19.08
2733	CE2	TYR	B	320	31.200	−21.001	104.292	1.00	14.64
2734	CZ	TYR	B	320	30.785	−19.946	105.061	1.00	20.88
2735	OH	TYR	B	320	31.214	−19.801	106.379	1.00	32.48
2736	C	TYR	B	320	27.318	−20.724	101.766	1.00	22.75
2737	O	TYR	B	320	26.672	−19.655	101.670	1.00	27.48
2738	N	ASN	B	321	27.122	−21.591	102.759	1.00	23.31
2739	CA	ASN	B	321	26.109	−21.283	103.782	1.00	29.74
2740	CB	ASN	B	321	25.036	−22.398	103.883	1.00	33.20
2741	CG	ASN	B	321	25.077	−23.161	105.188	1.00	28.54
2742	OD1	ASN	B	321	24.968	−22.604	106.274	1.00	21.25
2743	ND2	ASN	B	321	25.216	−24.462	105.075	1.00	38.75
2744	C	ASN	B	321	26.817	−21.077	105.092	1.00	31.37
2745	O	ASN	B	321	27.676	−21.870	105.472	1.00	29.68
2746	N	HIS	B	322	26.451	−19.999	105.772	1.00	34.77
2747	CA	HIS	B	322	27.070	−19.642	107.033	1.00	40.14
2748	CB	HIS	B	322	26.755	−18.189	107.364	1.00	51.27
2749	CG	HIS	B	322	27.574	−17.637	108.495	1.00	68.36
2750	CD2	HIS	B	322	28.820	−17.098	108.517	1.00	75.91
2751	ND1	HIS	B	322	27.127	−17.608	109.800	1.00	75.30
2752	CE1	HIS	B	322	28.056	−17.075	110.576	1.00	77.35
2753	NE2	HIS	B	322	29.095	−16.757	109.821	1.00	81.24
2754	C	HIS	B	322	26.741	−20.512	108.234	1.00	41.26
2755	O	HIS	B	322	27.593	−20.722	109.094	1.00	42.57
2756	N	GLU	B	323	25.530	−21.040	108.310	1.00	42.04
2757	CA	GLU	B	323	25.206	−21.849	109.469	1.00	45.58
2758	CB	GLU	B	323	23.682	−22.076	109.546	1.00	44.87
2759	CG	GLU	B	323	22.973	−22.133	108.226	1.00	57.51
2760	CD	GLU	B	323	21.495	−22.487	108.369	1.00	67.14
2761	OE1	GLU	B	323	21.166	−23.373	109.195	1.00	63.90
2762	OE2	GLU	B	323	20.660	−21.893	107.643	1.00	71.98
2763	C	GLU	B	323	26.012	−23.162	109.548	1.00	43.21
2764	O	GLU	B	323	26.608	−23.476	110.581	1.00	44.00
2765	N	THR	B	324	26.060	−23.905	108.450	1.00	42.19
2766	CA	THR	B	324	26.793	−25.159	108.442	1.00	40.90
2767	CB	THR	B	324	26.243	−26.152	107.364	1.00	42.53
2768	OG1	THR	B	324	26.829	−25.852	106.089	1.00	41.85
2769	CG2	THR	B	324	24.737	−26.050	107.234	1.00	41.53
2770	C	THR	B	324	28.262	−24.893	108.101	1.00	38.75
2771	O	THR	B	324	29.147	−25.720	108.378	1.00	36.54
2772	N	GLU	B	325	28.508	−23.728	107.513	1.00	33.32
2773	CA	GLU	B	325	29.842	−23.357	107.061	1.00	33.46
2774	CB	GLU	B	325	30.856	−23.420	108.213	1.00	23.98
2775	CG	GLU	B	325	31.022	−22.081	108.892	1.00	41.70
2776	CD	GLU	B	325	31.807	−22.141	110.193	1.00	42.71
2777	OE1	GLU	B	325	33.001	−22.528	110.156	1.00	40.97
2778	OE2	GLU	B	325	31.216	−21.807	111.251	1.00	38.92
2779	C	GLU	B	325	30.295	−24.247	105.867	1.00	29.73
2780	O	GLU	B	325	31.496	−24.326	105.548	1.00	29.60
2781	N	CYS	B	326	29.329	−24.897	105.210	1.00	19.72
2782	CA	CYS	B	326	29.630	−25.738	104.068	1.00	17.47
2783	CB	CYS	B	326	28.948	−27.087	104.197	1.00	17.62
2784	SG	CYS	B	326	29.778	−28.099	105.458	1.00	19.81
2785	C	CYS	B	326	29.282	−25.132	102.735	1.00	13.98
2786	O	CYS	B	326	28.472	−24.224	102.624	1.00	14.46
2787	N	ILE	B	327	29.934	−25.641	101.713	1.00	13.56
2788	CA	ILE	B	327	29.722	−25.166	100.374	1.00	14.00
2789	CB	ILE	B	327	31.105	−24.880	99.722	1.00	21.76
2790	CG2	ILE	B	327	30.987	−24.629	98.209	1.00	15.85
2791	CG1	ILE	B	327	31.744	−23.685	100.431	1.00	19.00
2792	CD1	ILE	B	327	33.200	−23.498	100.053	1.00	30.37
2793	C	ILE	B	327	28.978	−26.277	99.640	1.00	15.70
2794	O	ILE	B	327	29.495	−27.397	99.480	1.00	17.00
2795	N	THR	B	328	27.749	−26.014	99.225	1.00	12.99
2796	CA	THR	B	328	27.042	−27.061	98.498	1.00	15.42
2797	CB	THR	B	328	25.597	−27.188	99.065	1.00	17.94
2798	OG1	THR	B	328	24.631	−27.122	97.998	1.00	16.43
2799	CG2	THR	B	328	25.363	−26.095	100.081	1.00	15.23
2800	C	THR	B	328	27.064	−26.828	96.951	1.00	14.11
2801	O	THR	B	328	26.342	−25.970	96.416	1.00	14.69
2802	N	PHE	B	329	27.913	−27.588	96.257	1.00	17.12
2803	CA	PHE	B	329	28.068	−27.515	94.785	1.00	24.47
2804	CB	PHE	B	329	28.948	−28.686	94.274	1.00	19.96
2805	CG	PHE	B	329	30.309	−28.730	94.908	1.00	11.22
2806	CD1	PHE	B	329	30.773	−27.638	95.651	1.00	16.78
2807	CD2	PHE	B	329	31.123	−29.850	94.761	1.00	17.63
2808	CE1	PHE	B	329	32.019	−27.651	96.241	1.00	12.06
2809	CE2	PHE	B	329	32.388	−29.900	95.340	1.00	14.62
2810	CZ	PHE	B	329	32.834	−28.783	96.089	1.00	25.43
2811	C	PHE	B	329	26.717	−27.505	94.071	1.00	27.50
2812	O	PHE	B	329	26.329	−26.543	93.424	1.00	31.32
2813	N	LEU	B	330	26.005	−28.603	94.162	1.00	29.49
2814	CA	LEU	B	330	24.678	−28.677	93.591	1.00	32.93
2815	CB	LEU	B	330	24.586	−29.629	92.414	1.00	20.77
2816	CG	LEU	B	330	25.611	−30.766	92.428	1.00	19.16
2817	CD1	LEU	B	330	25.156	−31.901	91.621	1.00	13.76
2818	CD2	LEU	B	330	26.910	−30.266	91.897	1.00	18.33
2819	C	LEU	B	330	24.084	−29.384	94.724	1.00	41.67
2820	O	LEU	B	330	24.790	−29.756	95.688	1.00	48.74
2821	N	LYS	B	331	22.778	−29.531	94.708	1.00	46.64
2822	CA	LYS	B	331	22.380	−30.323	95.792	1.00	51.51
2823	CB	LYS	B	331	21.170	−29.901	96.632	1.00	51.06
2824	CG	LYS	B	331	21.365	−28.780	97.591	1.00	53.95
2825	CD	LYS	B	331	20.017	−28.140	97.871	1.00	48.73
2826	CE	LYS	B	331	20.173	−26.727	98.404	1.00	48.40
2827	NZ	LYS	B	331	20.371	−25.761	97.305	1.00	47.10
2828	C	LYS	B	331	22.181	−31.688	95.570	1.00	50.52
2829	O	LYS	B	331	21.849	−32.204	94.478	1.00	46.66
2830	N	ASP	B	332	22.887	−32.032	96.624	1.00	52.67
2831	CA	ASP	B	332	23.025	−33.222	97.365	1.00	55.22
2832	CB	ASP	B	332	22.073	−34.369	96.915	1.00	59.22
2833	CG	ASP	B	332	20.592	−33.897	96.918	1.00	63.62
2834	OD1	ASP	B	332	20.155	−33.161	97.849	1.00	60.93
2835	OD2	ASP	B	332	19.873	−34.259	95.952	1.00	61.76
2836	C	ASP	B	332	24.404	−33.483	97.729	1.00	52.77
2837	O	ASP	B	332	24.697	−34.166	98.715	1.00	57.76
2838	N	PHE	B	333	25.166	−32.599	97.109	1.00	45.92
2839	CA	PHE	B	333	26.596	−32.480	97.146	1.00	42.30
2840	CB	PHE	B	333	27.042	−32.335	95.715	1.00	39.83
2841	CG	PHE	B	333	26.642	−33.497	94.836	1.00	39.89
2842	CD1	PHE	B	333	27.585	−34.434	94.498	1.00	42.14
2843	CD2	PHE	B	333	25.351	−33.645	94.339	1.00	39.58
2844	CE1	PHE	B	333	27.271	−35.506	93.681	1.00	34.24
2845	CE2	PHE	B	333	25.033	−34.713	93.526	1.00	39.73
2846	CZ	PHE	B	333	26.006	−35.644	93.199	1.00	37.98
2847	C	PHE	B	333	27.104	−31.309	97.942	1.00	40.11
2848	O	PHE	B	333	27.208	−30.199	97.420	1.00	42.42
2849	N	THR	B	334	27.449	−31.564	99.198	1.00	37.35
2850	CA	THR	B	334	27.939	−30.488	100.056	1.00	35.15
2851	CB	THR	B	334	26.935	−30.139	101.149	1.00	27.27
2852	OG1	THR	B	334	25.661	−30.006	100.544	1.00	40.46
2853	CG2	THR	B	334	27.210	−28.800	101.745	1.00	35.21
2854	C	THR	B	334	29.258	−30.878	100.676	1.00	33.56
2855	O	THR	B	334	29.553	−32.065	100.805	1.00	32.24
2856	N	TYR	B	335	30.067	−29.866	101.011	1.00	30.56
2857	CA	TYR	B	335	31.384	−30.087	101.593	1.00	23.37
2858	CB	TYR	B	335	32.419	−30.188	100.488	1.00	17.76
2859	CG	TYR	B	335	31.948	−31.134	99.385	1.00	22.34
2860	CD1	TYR	B	335	32.229	−32.504	99.434	1.00	16.82
2861	CE1	TYR	B	335	31.759	−33.364	98.477	1.00	21.70
2862	CD2	TYR	B	335	31.168	−30.671	98.338	1.00	14.59
2863	CE2	TYR	B	335	30.678	−31.533	97.389	1.00	17.96
2864	CZ	TYR	B	335	30.975	−32.868	97.452	1.00	20.27
2865	OH	TYR	B	335	30.488	−33.727	96.499	1.00	12.76
2866	C	TYR	B	335	31.769	−29.007	102.572	1.00	22.39
2867	O	TYR	B	335	31.346	−27.848	102.484	1.00	22.73
2868	N	SER	B	336	32.577	−29.444	103.519	1.00	18.36
2869	CA	SER	B	336	33.087	−28.641	104.605	1.00	17.31
2870	CB	SER	B	336	33.167	−29.511	105.826	1.00	14.17
2871	OG	SER	B	336	34.231	−30.442	105.643	1.00	5.25
2872	C	SER	B	336	34.511	−28.249	104.242	1.00	19.59
2873	O	SER	B	336	35.079	−28.790	103.331	1.00	18.34
2874	N	LYS	B	337	35.107	−27.336	104.988	1.00	24.25
2875	CA	LYS	B	337	36.472	−26.939	104.683	1.00	30.39
2876	CB	LYS	B	337	36.974	−25.910	105.704	1.00	24.85
2877	CG	LYS	B	337	38.128	−25.057	105.208	1.00	24.92
2878	CD	LYS	B	337	38.965	−24.367	106.323	1.00	10.90
2879	CE	LYS	B	337	38.155	−23.365	107.092	1.00	12.99
2880	NZ	LYS	B	337	39.074	−22.574	107.894	1.00	14.94
2881	C	LYS	B	337	37.295	−28.230	104.806	1.00	34.31
2882	O	LYS	B	337	38.262	−28.511	104.044	1.00	39.45
2883	N	ASP	B	338	36.871	−29.039	105.763	1.00	32.24
2884	CA	ASP	B	338	37.555	−30.281	106.046	1.00	29.77
2885	CB	ASP	B	338	36.851	−30.970	107.187	1.00	37.61
2886	CG	ASP	B	338	37.724	−31.967	107.868	1.00	45.54
2887	OD1	ASP	B	338	38.827	−31.553	108.301	1.00	45.53
2888	OD2	ASP	B	338	37.304	−33.153	107.970	1.00	53.47
2889	C	ASP	B	338	37.604	−31.197	104.858	1.00	25.03
2890	O	ASP	B	338	38.665	−31.776	104.560	1.00	14.70
2891	N	ASP	B	339	36.440	−31.347	104.216	1.00	20.92
2892	CA	ASP	B	339	36.335	−32.178	103.037	1.00	23.16
2893	CB	ASP	B	339	34.939	−32.097	102.433	1.00	20.17
2894	CG	ASP	B	339	33.865	−32.866	103.280	1.00	27.23
2895	OD1	ASP	B	339	34.021	−34.070	103.623	1.00	19.08
2896	OD2	ASP	B	339	32.822	−32.257	103.597	1.00	19.77
2897	C	ASP	B	339	37.397	−31.793	102.006	1.00	24.92
2898	O	ASP	B	339	37.956	−32.655	101.325	1.00	24.48
2899	N	PHE	B	340	37.721	−30.511	101.906	1.00	26.15
2900	CA	PHE	B	340	38.754	−30.115	100.952	1.00	26.11
2901	CB	PHE	B	340	38.901	−28.586	100.891	1.00	29.18
2902	CG	PHE	B	340	37.815	−27.885	100.114	1.00	28.11
2903	CD1	PHE	B	340	38.137	−26.833	99.236	1.00	22.50
2904	CD2	PHE	B	340	36.476	−28.254	100.255	1.00	14.50
2905	CE1	PHE	B	340	37.122	−26.152	98.496	1.00	9.98
2906	CE2	PHE	B	340	35.453	−27.588	99.522	1.00	12.32
2907	CZ	PHE	B	340	35.779	−26.540	98.642	1.00	14.96
2908	C	PHE	B	340	40.104	−30.744	101.346	1.00	27.23
2909	O	PHE	B	340	40.738	−31.386	100.519	1.00	21.29
2910	N	HIS	B	341	40.532	−30.546	102.601	1.00	29.89
2911	CA	HIS	B	341	41.798	−31.090	103.086	1.00	29.99
2912	CB	HIS	B	341	41.871	−31.061	104.616	1.00	40.75
2913	CG	HIS	B	341	42.227	−29.717	105.203	1.00	52.52
2914	CD2	HIS	B	341	43.428	−29.152	105.504	1.00	51.07
2915	ND1	HIS	B	341	41.274	−28.795	105.585	1.00	59.86
2916	CE1	HIS	B	341	41.866	−27.727	106.094	1.00	55.78
2917	NE2	HIS	B	341	43.175	−27.918	106.055	1.00	57.87
2918	C	HIS	B	341	41.902	−32.513	102.631	1.00	27.80
2919	O	HIS	B	341	42.897	−32.913	102.032	1.00	34.95
2920	N	ARG	B	342	40.848	−33.279	102.890	1.00	25.91
2921	CA	ARG	B	342	40.808	−34.698	102.505	1.00	21.72
2922	CB	ARG	B	342	39.530	−35.344	103.014	1.00	23.52
2923	CG	ARG	B	342	39.552	−35.591	104.518	1.00	17.95
2924	CD	ARG	B	342	38.174	−35.868	105.004	1.00	16.70
2925	NE	ARG	B	342	38.202	−36.219	106.406	1.00	35.04
2926	CZ	ARG	B	342	37.208	−35.982	107.246	1.00	44.04
2927	NH1	ARG	B	342	36.106	−35.382	106.810	1.00	44.47
2928	NH2	ARG	B	342	37.328	−36.359	108.517	1.00	59.88
2929	C	ARG	B	342	40.943	−34.976	101.036	1.00	17.70
2930	O	ARG	B	342	41.451	−36.009	100.669	1.00	12.22
2931	N	ALA	B	343	40.496	−34.037	100.206	1.00	21.91
2932	CA	ALA	B	343	40.562	−34.182	98.749	1.00	22.78
2933	CB	ALA	B	343	39.538	−33.254	98.055	1.00	10.94
2934	C	ALA	B	343	41.955	−33.853	98.261	1.00	26.32
2935	O	ALA	B	343	42.180	−33.763	97.044	1.00	31.56
2936	N	GLY	B	344	42.882	−33.674	99.211	1.00	25.61
2937	CA	GLY	B	344	44.261	−33.350	98.868	1.00	25.49
2938	C	GLY	B	344	44.617	−31.872	98.760	1.00	23.60
2939	O	GLY	B	344	45.780	−31.508	98.561	1.00	26.94
2940	N	LEU	B	345	43.631	−31.002	98.884	1.00	19.91
2941	CA	LEU	B	345	43.948	−29.597	98.832	1.00	21.14
2942	CB	LEU	B	345	42.662	−28.777	98.752	1.00	18.78
2943	CG	LEU	B	345	41.720	−29.293	97.655	1.00	18.00
2944	CD1	LEU	B	345	40.533	−28.388	97.525	1.00	16.17
2945	CD2	LEU	B	345	42.454	−29.398	96.346	1.00	17.82
2946	C	LEU	B	345	44.808	−29.150	100.031	1.00	24.55
2947	O	LEU	B	345	44.765	−29.733	101.102	1.00	24.17
2948	N	GLN	B	346	45.618	−28.121	99.801	1.00	31.30
2949	CA	GLN	B	346	46.490	−27.508	100.803	1.00	28.94
2950	CB	GLN	B	346	47.551	−26.644	100.128	1.00	29.62
2951	CG	GLN	B	346	48.427	−27.381	99.193	1.00	35.38
2952	CD	GLN	B	346	49.364	−26.444	98.485	1.00	40.33
2953	OE1	GLN	B	346	48.924	−25.417	97.959	1.00	47.15
2954	NE2	GLN	B	346	50.664	−26.781	98.460	1.00	37.94
2955	C	GLN	B	346	45.708	−26.573	101.741	1.00	27.28
2956	O	GLN	B	346	44.650	−26.030	101.411	1.00	27.98
2957	N	VAL	B	347	46.287	−26.330	102.900	1.00	24.67
2958	CA	VAL	B	347	45.646	−25.477	103.846	1.00	18.01
2959	CB	VAL	B	347	46.257	−25.722	105.278	1.00	10.17
2960	CG1	VAL	B	347	47.379	−24.760	105.559	1.00	10.52
2961	CG2	VAL	B	347	45.188	−25.644	106.323	1.00	12.51
2962	C	VAL	B	347	45.834	−24.044	103.346	1.00	17.79
2963	O	VAL	B	347	45.013	−23.175	103.577	1.00	22.76
2964	N	GLU	B	348	46.899	−23.796	102.605	1.00	17.73
2965	CA	GLU	B	348	47.163	−22.436	102.170	1.00	13.53
2966	CB	GLU	B	348	48.639	−22.295	101.753	1.00	14.31
2967	CG	GLU	B	348	49.467	−23.583	101.838	1.00	31.23
2968	CD	GLU	B	348	50.376	−23.631	103.046	1.00	44.88
2969	OE1	GLU	B	348	49.869	−23.564	104.198	1.00	51.92
2970	OE2	GLU	B	348	51.613	−23.725	102.843	1.00	50.16
2971	C	GLU	B	348	46.245	−22.001	101.060	1.00	13.72
2972	O	GLU	B	348	46.186	−20.826	100.716	1.00	15.06
2973	N	PHE	B	349	45.531	−22.950	100.476	1.00	16.82
2974	CA	PHE	B	349	44.587	−22.625	99.406	1.00	13.74
2975	CB	PHE	B	349	44.708	−23.669	98.281	1.00	18.78
2976	CG	PHE	B	349	43.740	−23.473	97.114	1.00	10.99
2977	CD1	PHE	B	349	43.459	−22.220	96.614	1.00	18.13
2978	CD2	PHE	B	349	43.132	−24.560	96.507	1.00	13.56
2979	CE1	PHE	B	349	42.573	−22.050	95.525	1.00	6.01
2980	CE2	PHE	B	349	42.255	−24.397	95.419	1.00	5.27
2981	CZ	PHE	B	349	41.981	−23.144	94.937	1.00	5.69
2982	C	PHE	B	349	43.193	−22.668	100.063	1.00	15.65
2983	O	PHE	B	349	42.428	−21.690	100.012	1.00	13.18
2984	N	ILE	B	350	42.888	−23.793	100.719	1.00	18.64
2985	CA	ILE	B	350	41.599	−24.029	101.411	1.00	15.73
2986	CB	ILE	B	350	41.711	−25.319	102.245	1.00	15.61
2987	CG2	ILE	B	350	40.518	−25.557	103.096	1.00	19.07
2988	CG1	ILE	B	350	41.814	−26.498	101.316	1.00	17.50
2989	CD1	ILE	B	350	42.135	−27.753	102.103	1.00	27.64
2990	C	ILE	B	350	41.176	−22.844	102.296	1.00	17.73
2991	O	ILE	B	350	40.153	−22.176	102.039	1.00	17.58
2992	N	ASN	B	351	41.964	−22.558	103.329	1.00	15.36
2993	CA	ASN	B	351	41.630	−21.426	104.200	1.00	21.50
2994	CB	ASN	B	351	42.773	−21.092	105.184	1.00	18.55
2995	CG	ASN	B	351	43.060	−22.266	106.118	1.00	33.34
2996	OD1	ASN	B	351	42.180	−23.130	106.341	1.00	30.31
2997	ND2	ASN	B	351	44.276	−22.324	106.657	1.00	32.74
2998	C	ASN	B	351	41.200	−20.192	103.432	1.00	17.98
2999	O	ASN	B	351	40.127	−19.675	103.672	1.00	19.95
3000	N	PRO	B	352	42.023	−19.723	102.498	1.00	17.67
3001	CD	PRO	B	352	43.393	−20.189	102.230	1.00	16.16
3002	CA	PRO	B	352	41.709	−18.543	101.689	1.00	17.00
3003	CB	PRO	B	352	42.870	−18.483	100.713	1.00	11.78
3004	CG	PRO	B	352	43.981	−18.986	101.503	1.00	13.56
3005	C	PRO	B	352	40.358	−18.651	100.942	1.00	18.90
3006	O	PRO	B	352	39.594	−17.663	100.873	1.00	15.40
3007	N	ILE	B	353	40.022	−19.835	100.415	1.00	15.19
3008	CA	ILE	B	353	38.747	−19.892	99.693	1.00	16.53
3009	CB	ILE	B	353	38.596	−21.164	98.749	1.00	13.88
3010	CG2	ILE	B	353	39.954	−21.816	98.408	1.00	26.94
3011	CG1	ILE	B	353	37.724	−22.179	99.393	1.00	33.16
3012	CD1	ILE	B	353	36.288	−21.967	99.061	1.00	45.07
3013	C	ILE	B	353	37.579	−19.748	100.646	1.00	11.77
3014	O	ILE	B	353	36.557	−19.178	100.319	1.00	17.06
3015	N	PHE	B	354	37.728	−20.236	101.856	1.00	13.84
3016	CA	PHE	B	354	36.629	−20.093	102.813	1.00	16.88
3017	CB	PHE	B	354	36.720	−21.198	103.879	1.00	14.93
3018	CG	PHE	B	354	36.075	−22.477	103.456	1.00	16.09
3019	CD1	PHE	B	354	36.685	−23.305	102.518	1.00	24.52
3020	CD2	PHE	B	354	34.824	−22.815	103.921	1.00	18.19
3021	CE1	PHE	B	354	36.057	−24.442	102.041	1.00	12.44
3022	CE2	PHE	B	354	34.177	−23.952	103.450	1.00	10.08
3023	CZ	PHE	B	354	34.797	−24.755	102.515	1.00	20.01
3024	C	PHE	B	354	36.543	−18.679	103.467	1.00	16.92
3025	O	PHE	B	354	35.533	−18.254	104.046	1.00	8.38
3026	N	GLU	B	355	37.604	−17.921	103.338	1.00	20.86
3027	CA	GLU	B	355	37.561	−16.616	103.904	1.00	24.71
3028	CB	GLU	B	355	38.979	−16.173	104.263	1.00	26.64
3029	CG	GLU	B	355	39.198	−15.870	105.748	1.00	45.42
3030	CD	GLU	B	355	40.442	−16.586	106.324	1.00	62.33
3031	OE1	GLU	B	355	40.307	−17.709	106.894	1.00	72.73
3032	OE2	GLU	B	355	41.565	−16.039	106.187	1.00	65.39
3033	C	GLU	B	355	36.916	−15.726	102.813	1.00	25.19
3034	O	GLU	B	355	36.197	−14.750	103.097	1.00	24.85
3035	N	PHE	B	356	37.148	−16.085	101.560	1.00	19.78
3036	CA	PHE	B	356	36.585	−15.306	100.472	1.00	17.79
3037	CB	PHE	B	356	37.097	−15.856	99.132	1.00	18.91
3038	CG	PHE	B	356	36.512	−15.196	97.925	1.00	14.83
3039	CD1	PHE	B	356	36.826	−13.860	97.610	1.00	5.25
3040	CD2	PHE	B	356	35.707	−15.932	97.058	1.00	9.68
3041	CE1	PHE	B	356	36.349	−13.276	96.451	1.00	5.25
3042	CE2	PHE	B	356	35.217	−15.346	95.869	1.00	12.90
3043	CZ	PHE	B	356	35.551	−14.009	95.576	1.00	7.76
3044	C	PHE	B	356	35.063	−15.423	100.525	1.00	17.85
3045	O	PHE	B	356	34.336	−14.417	100.378	1.00	13.00
3046	N	SER	B	357	34.600	−16.664	100.715	1.00	17.34
3047	CA	SER	B	357	33.182	−16.957	100.782	1.00	16.99
3048	CB	SER	B	357	32.961	−18.441	101.009	1.00	22.49
3049	OG	SER	B	357	33.091	−19.171	99.819	1.00	31.90
3050	C	SER	B	357	32.586	−16.187	101.935	1.00	16.72
3051	O	SER	B	357	31.539	−15.548	101.801	1.00	15.43
3052	N	ARG	B	358	33.255	−16.250	103.085	1.00	18.90
3053	CA	ARG	B	358	32.755	−15.521	104.240	1.00	18.40
3054	CB	ARG	B	358	33.647	−15.774	105.467	1.00	14.72
3055	CG	ARG	B	358	33.420	−17.131	106.105	1.00	7.82
3056	CD	ARG	B	358	34.071	−17.220	107.487	1.00	8.08
3057	NE	ARG	B	358	35.545	−17.239	107.462	1.00	17.36
3058	CZ	ARG	B	358	36.292	−18.310	107.173	1.00	26.94
3059	NH1	ARG	B	358	35.732	−19.490	106.876	1.00	31.94
3060	NH2	ARG	B	358	37.612	−18.205	107.178	1.00	20.34
3061	C	ARG	B	358	32.640	−14.022	103.896	1.00	15.62
3062	O	ARG	B	358	31.602	−13.371	104.137	1.00	19.53
3063	N	ALA	B	359	33.686	−13.469	103.308	1.00	12.15
3064	CA	ALA	B	359	33.619	−12.061	102.903	1.00	18.05
3065	CB	ALA	B	359	34.972	−11.565	102.396	1.00	8.61
3066	C	ALA	B	359	32.536	−11.765	101.856	1.00	19.02
3067	O	ALA	B	359	31.962	−10.688	101.883	1.00	18.91
3068	N	MET	B	360	32.254	−12.699	100.948	1.00	17.99
3069	CA	MET	B	360	31.214	−12.460	99.961	1.00	22.61
3070	CB	MET	B	360	31.225	−13.523	98.842	1.00	26.94
3071	CG	MET	B	360	32.423	−13.472	97.882	1.00	32.65
3072	SD	MET	B	360	32.647	−11.916	96.899	1.00	18.14
3073	CE	MET	B	360	31.021	−11.313	96.962	1.00	24.58
3074	C	MET	B	360	29.837	−12.462	100.634	1.00	26.84
3075	O	MET	B	360	28.944	−11.707	100.227	1.00	31.39
3076	N	ARG	B	361	29.633	−13.334	101.622	1.00	26.66
3077	CA	ARG	B	361	28.359	−13.361	102.321	1.00	27.45
3078	CB	ARG	B	361	28.368	−14.465	103.342	1.00	32.86
3079	CG	ARG	B	361	27.103	−14.454	104.197	1.00	48.02
3080	CD	ARG	B	361	27.327	−15.124	105.526	1.00	50.09
3081	NE	ARG	B	361	26.385	−14.640	106.520	1.00	53.80
3082	CZ	ARG	B	361	25.103	−14.970	106.558	1.00	61.07
3083	NH1	ARG	B	361	24.602	−15.792	105.648	1.00	49.75
3084	NH2	ARG	B	361	24.336	−14.487	107.529	1.00	70.63
3085	C	ARG	B	361	28.136	−12.011	103.039	1.00	30.85
3086	O	ARG	B	361	26.998	−11.534	103.201	1.00	28.80
3087	N	ARG	B	362	29.241	−11.413	103.479	1.00	33.49
3088	CA	ARG	B	362	29.244	−10.115	104.142	1.00	34.01
3089	CB	ARG	B	362	30.661	−9.784	104.607	1.00	41.72
3090	CG	ARG	B	362	31.017	−10.242	106.011	1.00	51.35
3091	CD	ARG	B	362	32.398	−9.709	106.379	1.00	58.26
3092	NE	ARG	B	362	33.420	−10.743	106.288	1.00	53.85
3093	CZ	ARG	B	362	34.679	−10.504	105.961	1.00	56.47
3094	NH1	ARG	B	362	35.054	−9.255	105.687	1.00	46.23
3095	NH2	ARG	B	362	35.541	−11.522	105.929	1.00	59.73
3096	C	ARG	B	362	28.764	−8.970	103.249	1.00	34.69
3097	O	ARG	B	362	28.657	−7.836	103.722	1.00	40.31
3098	N	LEU	B	363	28.525	−9.236	101.962	1.00	30.88
3099	CA	LEU	B	363	28.057	−8.179	101.042	1.00	28.18
3100	CB	LEU	B	363	28.981	−8.014	99.833	1.00	26.95
3101	CG	LEU	B	363	30.405	−7.667	100.163	1.00	27.79
3102	CD1	LEU	B	363	31.253	−7.675	98.903	1.00	32.32
3103	CD2	LEU	B	363	30.410	−6.323	100.820	1.00	30.61
3104	C	LEU	B	363	26.657	−8.448	100.550	1.00	22.85
3105	O	LEU	B	363	26.039	−7.540	99.992	1.00	21.59
3106	N	GLY	B	364	26.209	−9.693	100.747	1.00	17.08
3107	CA	GLY	B	364	24.877	−10.120	100.391	1.00	16.34
3108	C	GLY	B	364	24.509	−9.830	98.972	1.00	16.19
3109	O	GLY	B	364	23.456	−9.193	98.727	1.00	12.85
3110	N	LEU	B	365	25.367	−10.296	98.057	1.00	13.81
3111	CA	LEU	B	365	25.139	−10.118	96.630	1.00	13.79
3112	CB	LEU	B	365	26.407	−10.484	95.853	1.00	14.20
3113	CG	LEU	B	365	27.688	−9.876	96.405	1.00	21.72
3114	CD1	LEU	B	365	28.706	−9.735	95.330	1.00	31.54
3115	CD2	LEU	B	365	27.391	−8.524	96.953	1.00	39.02
3116	C	LEU	B	365	23.974	−10.995	96.179	1.00	13.42
3117	O	LEU	B	365	23.917	−12.142	96.546	1.00	13.34
3118	N	ASP	B	366	23.039	−10.443	95.394	1.00	19.07
3119	CA	ASP	B	366	21.862	−11.184	94.884	1.00	16.89
3120	CB	ASP	B	366	20.668	−10.270	94.648	1.00	13.26
3121	CG	ASP	B	366	20.962	−9.161	93.670	1.00	23.83
3122	OD1	ASP	B	366	21.482	−9.459	92.574	1.00	26.79
3123	OD2	ASP	B	366	20.653	−7.987	93.996	1.00	36.61
3124	C	ASP	B	366	22.213	−11.842	93.575	1.00	19.58
3125	O	ASP	B	366	23.296	−11.576	93.006	1.00	13.52
3126	N	ASP	B	367	21.298	−12.680	93.087	1.00	20.02
3127	CA	ASP	B	367	21.518	−13.426	91.839	1.00	22.33
3128	CB	ASP	B	367	20.271	−14.245	91.504	1.00	24.27
3129	CG	ASP	B	367	19.890	−15.194	92.616	1.00	43.14
3130	OD1	ASP	B	367	20.540	−16.280	92.703	1.00	53.43
3131	OD2	ASP	B	367	18.958	−14.843	93.413	1.00	48.18
3132	C	ASP	B	367	21.943	−12.596	90.604	1.00	19.76
3133	O	ASP	B	367	22.597	−13.127	89.719	1.00	11.62
3134	N	ALA	B	368	21.581	−11.308	90.564	1.00	19.98
3135	CA	ALA	B	368	21.918	−10.406	89.458	1.00	19.72
3136	CB	ALA	B	368	20.915	−9.338	89.372	1.00	15.55
3137	C	ALA	B	368	23.295	−9.774	89.595	1.00	22.54
3138	O	ALA	B	368	23.994	−9.511	88.596	1.00	22.54
3139	N	GLU	B	369	23.677	−9.504	90.840	1.00	23.40
3140	CA	GLU	B	369	24.980	−8.925	91.113	1.00	20.72
3141	CB	GLU	B	369	25.057	−8.470	92.564	1.00	17.66
3142	CG	GLU	B	369	23.891	−7.514	92.884	1.00	25.36
3143	CD	GLU	B	369	23.962	−6.878	94.263	1.00	29.99
3144	OE1	GLU	B	369	24.111	−7.633	95.253	1.00	26.69
3145	OE2	GLU	B	369	23.866	−5.627	94.362	1.00	16.79
3146	C	GLU	B	369	26.028	−9.960	90.769	1.00	18.11
3147	O	GLU	B	369	27.003	−9.670	90.085	1.00	20.17
3148	N	TYR	B	370	25.799	−11.195	91.178	1.00	18.30
3149	CA	TYR	B	370	26.749	−12.237	90.852	1.00	15.68
3150	CB	TYR	B	370	26.302	−13.623	91.353	1.00	19.37
3151	CG	TYR	B	370	26.827	−14.016	92.727	1.00	7.23
3152	CD1	TYR	B	370	26.032	−13.928	93.846	1.00	17.22
3153	CE1	TYR	B	370	26.514	−14.243	95.109	1.00	15.61
3154	CD2	TYR	B	370	28.116	−14.429	92.895	1.00	9.51
3155	CE2	TYR	B	370	28.614	−14.734	94.142	1.00	15.58
3156	CZ	TYR	B	370	27.819	−14.637	95.246	1.00	14.19
3157	OH	TYR	B	370	28.371	−14.858	96.486	1.00	24.16
3158	C	TYR	B	370	26.898	−12.270	89.358	1.00	12.51
3159	O	TYR	B	370	27.972	−12.022	88.827	1.00	17.46
3160	N	ALA	B	371	25.815	−12.556	88.665	1.00	11.93
3161	CA	ALA	B	371	25.889	−12.626	87.217	1.00	14.57
3162	CB	ALA	B	371	24.497	−12.590	86.620	1.00	5.25
3163	C	ALA	B	371	26.755	−11.477	86.681	1.00	17.10
3164	O	ALA	B	371	27.791	−11.716	85.993	1.00	16.34
3165	N	LEU	B	372	26.372	−10.242	87.028	1.00	17.56
3166	CA	LEU	B	372	27.135	−9.070	86.558	1.00	18.82
3167	CB	LEU	B	372	26.540	−7.775	87.107	1.00	13.33
3168	CG	LEU	B	372	25.210	−7.389	86.494	1.00	12.05
3169	CD1	LEU	B	372	24.794	−6.048	87.024	1.00	15.59
3170	CD2	LEU	B	372	25.382	−7.304	84.965	1.00	16.90
3171	C	LEU	B	372	28.625	−9.147	86.917	1.00	16.85
3172	O	LEU	B	372	29.492	−8.975	86.048	1.00	13.14
3173	N	LEU	B	373	28.910	−9.444	88.185	1.00	13.85
3174	CA	LEU	B	373	30.281	−9.548	88.629	1.00	12.62
3175	CB	LEU	B	373	30.329	−9.940	90.118	1.00	7.59
3176	CG	LEU	B	373	31.566	−9.456	90.844	1.00	8.37
3177	CD1	LEU	B	373	31.398	−7.985	91.121	1.00	9.21
3178	CD2	LEU	B	373	31.715	−10.206	92.083	1.00	5.25
3179	C	LEU	B	373	31.023	−10.587	87.762	1.00	11.70
3180	O	LEU	B	373	32.143	−10.350	87.336	1.00	13.99
3181	N	ILE	B	374	30.400	−11.735	87.504	1.00	12.16
3182	CA	ILE	B	374	31.028	−12.752	86.677	1.00	9.86
3183	CB	ILE	B	374	30.151	−14.010	86.561	1.00	5.59
3184	CG2	ILE	B	374	30.777	−15.013	85.607	1.00	5.25
3185	CG1	ILE	B	374	30.042	−14.676	87.918	1.00	10.39
3186	CD1	ILE	B	374	29.306	−16.037	87.893	1.00	7.46
3187	C	ILE	B	374	31.337	−12.221	85.259	1.00	14.32
3188	O	ILE	B	374	32.444	−12.492	84.724	1.00	11.00
3189	N	ALA	B	375	30.387	−11.479	84.658	1.00	13.12
3190	CA	ALA	B	375	30.627	−10.941	83.334	1.00	13.52
3191	CB	ALA	B	375	29.407	−10.217	82.820	1.00	20.18
3192	C	ALA	B	375	31.818	−9.980	83.427	1.00	14.33
3193	O	ALA	B	375	32.787	−10.096	82.677	1.00	19.14
3194	N	ILE	B	376	31.753	−9.030	84.351	1.00	14.01
3195	CA	ILE	B	376	32.851	−8.085	84.524	1.00	11.25
3196	CB	ILE	B	376	32.680	−7.249	85.834	1.00	8.47
3197	CG2	ILE	B	376	33.993	−6.556	86.203	1.00	13.86
3198	CG1	ILE	B	376	31.583	−6.193	85.633	1.00	7.99
3199	CD1	ILE	B	376	31.150	−5.454	86.914	1.00	12.21
3200	C	ILE	B	376	34.153	−8.860	84.581	1.00	9.44
3201	O	ILE	B	376	35.108	−8.589	83.860	1.00	11.32
3202	N	ASN	B	377	34.183	−9.848	85.452	1.00	12.26
3203	CA	ASN	B	377	35.359	−10.671	85.620	1.00	11.47
3204	CB	ASN	B	377	35.061	−11.776	86.624	1.00	9.20
3205	CG	ASN	B	377	36.219	−12.689	86.832	1.00	7.74
3206	OD1	ASN	B	377	36.523	−13.554	86.005	1.00	23.45
3207	ND2	ASN	B	377	36.886	−12.512	87.940	1.00	13.06
3208	C	ASN	B	377	35.831	−11.254	84.299	1.00	12.17
3209	O	ASN	B	377	36.985	−11.166	84.000	1.00	15.74
3210	N	ILE	B	378	34.947	−11.869	83.517	1.00	17.76
3211	CA	ILE	B	378	35.327	−12.466	82.214	1.00	16.66
3212	CB	ILE	B	378	34.124	−12.997	81.466	1.00	9.28
3213	CG2	ILE	B	378	34.549	−13.578	80.132	1.00	13.78
3214	CG1	ILE	B	378	33.475	−14.086	82.288	1.00	7.47
3215	CD1	ILE	B	378	32.276	−14.711	81.563	1.00	14.99
3216	C	ILE	B	378	36.021	−11.473	81.284	1.00	16.69
3217	O	ILE	B	378	37.026	−11.816	80.626	1.00	17.57
3218	N	PHE	B	379	35.483	−10.256	81.242	1.00	11.33
3219	CA	PHE	B	379	36.071	−9.198	80.440	1.00	16.27
3220	CB	PHE	B	379	34.967	−8.240	79.995	1.00	11.04
3221	CG	PHE	B	379	33.936	−8.871	79.063	1.00	13.52
3222	CD1	PHE	B	379	34.322	−9.497	77.873	1.00	11.53
3223	CD2	PHE	B	379	32.572	−8.842	79.391	1.00	12.09
3224	CE1	PHE	B	379	33.354	−10.109	77.000	1.00	5.76
3225	CE2	PHE	B	379	31.627	−9.420	78.570	1.00	11.76
3226	CZ	PHE	B	379	32.029	−10.073	77.341	1.00	8.68
3227	C	PHE	B	379	37.258	−8.419	81.088	1.00	14.55
3228	O	PHE	B	379	37.265	−7.178	81.133	1.00	14.20
3229	N	SER	B	380	38.258	−9.163	81.564	1.00	16.28
3230	CA	SER	B	380	39.459	−8.574	82.167	1.00	19.10
3231	CB	SER	B	380	40.137	−9.553	83.122	1.00	19.33
3232	OG	SER	B	380	39.358	−9.913	84.218	1.00	15.59
3233	C	SER	B	380	40.488	−8.236	81.063	1.00	21.09
3234	O	SER	B	380	41.286	−9.075	80.621	1.00	17.26
3235	N	ALA	B	381	40.483	−7.002	80.605	1.00	24.34
3236	CA	ALA	B	381	41.439	−6.620	79.562	1.00	25.10
3237	CB	ALA	B	381	41.296	−5.095	79.277	1.00	25.42
3238	C	ALA	B	381	42.922	−6.974	79.827	1.00	18.35
3239	O	ALA	B	381	43.728	−7.012	78.913	1.00	25.10
3240	N	ASP	B	382	43.284	−7.252	81.067	1.00	15.56
3241	CA	ASP	B	382	44.693	−7.524	81.396	1.00	18.77
3242	CB	ASP	B	382	45.111	−6.726	82.654	1.00	10.75
3243	CG	ASP	B	382	44.614	−7.355	83.958	1.00	23.74
3244	OD1	ASP	B	382	43.539	−7.994	83.980	1.00	24.72
3245	OD2	ASP	B	382	45.298	−7.202	84.991	1.00	26.03
3246	C	ASP	B	382	45.101	−8.982	81.590	1.00	20.40
3247	O	ASP	B	382	46.159	−9.260	82.165	1.00	13.95
3248	N	ARG	B	383	44.257	−9.910	81.130	1.00	26.01
3249	CA	ARG	B	383	44.552	−11.339	81.283	1.00	25.61
3250	CB	ARG	B	383	43.355	−12.220	80.901	1.00	25.21
3251	CG	ARG	B	383	42.121	−12.108	81.792	1.00	27.60
3252	CD	ARG	B	383	42.392	−12.504	83.244	1.00	31.36
3253	NE	ARG	B	383	41.145	−12.534	84.004	1.00	25.93
3254	CZ	ARG	B	383	41.066	−12.723	85.314	1.00	23.67
3255	NH1	ARG	B	383	42.182	−12.906	86.033	1.00	13.10
3256	NH2	ARG	B	383	39.855	−12.713	85.886	1.00	8.01
3257	C	ARG	B	383	45.736	−11.689	80.405	1.00	22.00
3258	O	ARG	B	383	46.011	−11.017	79.408	1.00	20.47
3259	N	PRO	B	384	46.486	−12.725	80.794	1.00	23.24
3260	CD	PRO	B	384	46.524	−13.377	82.121	1.00	20.49
3261	CA	PRO	B	384	47.644	−13.110	79.970	1.00	24.77
3262	CB	PRO	B	384	48.212	−14.336	80.704	1.00	16.49
3263	CG	PRO	B	384	47.919	−13.981	82.165	1.00	11.88
3264	C	PRO	B	384	47.252	−13.436	78.521	1.00	28.40
3265	O	PRO	B	384	46.275	−14.170	78.245	1.00	35.48
3266	N	ASN	B	385	47.998	−12.840	77.607	1.00	27.81
3267	CA	ASN	B	385	47.841	−13.074	76.202	1.00	25.50
3268	CB	ASN	B	385	48.117	−14.551	75.896	1.00	26.56
3269	CG	ASN	B	385	49.579	−14.914	76.084	1.00	29.73
3270	OD1	ASN	B	385	50.078	−15.015	77.200	1.00	25.94
3271	ND2	ASN	B	385	50.274	−15.103	74.977	1.00	42.58
3272	C	ASN	B	385	46.559	−12.664	75.558	1.00	23.58
3273	O	ASN	B	385	45.944	−13.463	74.901	1.00	30.94
3274	N	VAL	B	386	46.162	−11.418	75.726	1.00	22.19
3275	CA	VAL	B	386	44.952	−10.898	75.103	1.00	20.30
3276	CB	VAL	B	386	44.150	−10.087	76.141	1.00	20.63
3277	CG1	VAL	B	386	42.930	−9.437	75.494	1.00	11.24
3278	CG2	VAL	B	386	43.749	−11.017	77.277	1.00	13.39
3279	C	VAL	B	386	45.393	−10.003	73.923	1.00	24.43
3280	O	VAL	B	386	46.189	−9.046	74.085	1.00	26.09
3281	N	GLN	B	387	44.883	−10.303	72.732	1.00	26.72
3282	CA	GLN	B	387	45.245	−9.536	71.536	1.00	24.67
3283	CB	GLN	B	387	45.170	−10.437	70.315	1.00	33.85
3284	CG	GLN	B	387	46.258	−11.505	70.260	1.00	48.03
3285	CD	GLN	B	387	46.156	−12.422	69.054	1.00	57.45
3286	OE1	GLN	B	387	46.907	−13.398	68.963	1.00	62.38
3287	NE2	GLN	B	387	45.233	−12.118	68.119	1.00	59.65
3288	C	GLN	B	387	44.414	−8.274	71.316	1.00	20.65
3289	O	GLN	B	387	44.804	−7.346	70.616	1.00	20.76
3290	N	GLU	B	388	43.260	−8.212	71.930	1.00	17.86
3291	CA	GLU	B	388	42.499	−7.013	71.754	1.00	16.12
3292	CB	GLU	B	388	41.348	−7.271	70.804	1.00	14.57
3293	CG	GLU	B	388	41.835	−7.575	69.398	1.00	5.36
3294	CD	GLU	B	388	40.693	−7.841	68.436	1.00	12.71
3295	OE1	GLU	B	388	40.072	−8.916	68.529	1.00	29.33
3296	OE2	GLU	B	388	40.377	−6.984	67.594	1.00	32.32
3297	C	GLU	B	388	42.013	−6.445	73.076	1.00	11.41
3298	O	GLU	B	388	40.808	−6.341	73.320	1.00	13.14
3299	N	PRO	B	389	42.958	−6.055	73.938	1.00	6.71
3300	CD	PRO	B	389	44.404	−6.004	73.676	1.00	8.43
3301	CA	PRO	B	389	42.642	−5.481	75.241	1.00	14.43
3302	CB	PRO	B	389	44.008	−5.126	75.798	1.00	10.21
3303	CG	PRO	B	389	44.809	−4.909	74.567	1.00	16.14
3304	C	PRO	B	389	41.707	−4.273	75.120	1.00	22.57
3305	O	PRO	B	389	40.637	−4.222	75.761	1.00	27.08
3306	N	GLY	B	390	42.089	−3.298	74.299	1.00	25.43
3307	CA	GLY	B	390	41.218	−2.146	74.161	1.00	25.69
3308	C	GLY	B	390	39.768	−2.583	73.961	1.00	24.27
3309	O	GLY	B	390	38.809	−2.072	74.561	1.00	27.74
3310	N	ARG	B	391	39.619	−3.569	73.099	1.00	21.41
3311	CA	ARG	B	391	38.315	−4.089	72.785	1.00	18.95
3312	CB	ARG	B	391	38.449	−5.049	71.614	1.00	13.78
3313	CG	ARG	B	391	37.148	−5.406	71.026	1.00	23.30
3314	CD	ARG	B	391	37.301	−5.840	69.585	1.00	18.87
3315	NE	ARG	B	391	36.124	−6.604	69.192	1.00	14.58
3316	CZ	ARG	B	391	36.188	−7.622	68.359	1.00	28.26
3317	NH1	ARG	B	391	37.376	−7.966	67.850	1.00	32.20
3318	NH2	ARG	B	391	35.077	−8.280	68.049	1.00	40.77
3319	C	ARG	B	391	37.680	−4.759	74.004	1.00	19.06
3320	O	ARG	B	391	36.495	−4.530	74.321	1.00	19.44
3321	N	VAL	B	392	38.455	−5.589	74.697	1.00	16.37
3322	CA	VAL	B	392	37.925	−6.241	75.892	1.00	20.01
3323	CB	VAL	B	392	38.947	−7.292	76.450	1.00	23.55
3324	CG1	VAL	B	392	38.544	−7.800	77.854	1.00	25.16
3325	CG2	VAL	B	392	38.975	−8.485	75.493	1.00	22.93
3326	C	VAL	B	392	37.569	−5.165	76.960	1.00	19.85
3327	O	VAL	B	392	36.435	−5.106	77.479	1.00	17.66
3328	N	GLU	B	393	38.510	−4.280	77.260	1.00	19.42
3329	CA	GLU	B	393	38.203	−3.262	78.237	1.00	21.86
3330	CB	GLU	B	393	39.319	−2.215	78.329	1.00	21.31
3331	CG	GLU	B	393	39.323	−1.489	79.696	1.00	15.00
3332	CD	GLU	B	393	40.435	−0.488	79.825	1.00	18.00
3333	OE1	GLU	B	393	41.492	−0.681	79.209	1.00	36.45
3334	OE2	GLU	B	393	40.274	0.510	80.541	1.00	26.03
3335	C	GLU	B	393	36.870	−2.578	77.920	1.00	22.57
3336	O	GLU	B	393	36.132	−2.213	78.819	1.00	25.44
3337	N	ALA	B	394	36.531	−2.424	76.651	1.00	19.40
3338	CA	ALA	B	394	35.288	−1.766	76.340	1.00	14.16
3339	CB	ALA	B	394	35.291	−1.385	74.928	1.00	8.52
3340	C	ALA	B	394	34.094	−2.661	76.638	1.00	17.63
3341	O	ALA	B	394	33.086	−2.197	77.154	1.00	17.76
3342	N	LEU	B	395	34.186	−3.945	76.297	1.00	20.44
3343	CA	LEU	B	395	33.070	−4.870	76.557	1.00	26.34
3344	CB	LEU	B	395	33.430	−6.306	76.095	1.00	28.81
3345	CG	LEU	B	395	33.585	−6.556	74.589	1.00	30.31
3346	CD1	LEU	B	395	34.129	−7.967	74.323	1.00	19.04
3347	CD2	LEU	B	395	32.248	−6.358	73.917	1.00	18.75
3348	C	LEU	B	395	32.668	−4.890	78.039	1.00	24.18
3349	O	LEU	B	395	31.505	−4.972	78.399	1.00	24.80
3350	N	GLN	B	396	33.660	−4.785	78.898	1.00	22.89
3351	CA	GLN	B	396	33.409	−4.813	80.316	1.00	23.73
3352	CB	GLN	B	396	34.740	−5.018	81.060	1.00	18.79
3353	CG	GLN	B	396	34.581	−5.032	82.527	1.00	26.79
3354	CD	GLN	B	396	35.865	−5.097	83.232	1.00	27.74
3355	OE1	GLN	B	396	36.681	−4.191	83.117	1.00	35.13
3356	NE2	GLN	B	396	36.078	−6.174	83.979	1.00	35.02
3357	C	GLN	B	396	32.671	−3.592	80.863	1.00	23.41
3358	O	GLN	B	396	31.845	−3.714	81.759	1.00	25.74
3359	N	GLN	B	397	32.967	−2.413	80.341	1.00	20.51
3360	CA	GLN	B	397	32.300	−1.202	80.833	1.00	21.67
3361	CB	GLN	B	397	32.679	−0.005	79.956	1.00	14.93
3362	CG	GLN	B	397	34.175	0.084	79.732	1.00	33.91
3363	CD	GLN	B	397	34.957	0.475	80.982	1.00	34.76
3364	OE1	GLN	B	397	34.782	1.594	81.504	1.00	41.56
3365	NE2	GLN	B	397	35.832	−0.434	81.463	1.00	24.98
3366	C	GLN	B	397	30.748	−1.288	80.956	1.00	18.34
3367	O	GLN	B	397	30.154	−1.031	82.029	1.00	15.53
3368	N	PRO	B	398	30.082	−1.701	79.879	1.00	17.23
3369	CD	PRO	B	398	30.564	−2.367	78.652	1.00	12.02
3370	CA	PRO	B	398	28.624	−1.757	79.990	1.00	13.09
3371	CB	PRO	B	398	28.203	−2.431	78.688	1.00	13.76
3372	CG	PRO	B	398	29.363	−2.218	77.750	1.00	22.69
3373	C	PRO	B	398	28.185	−2.525	81.223	1.00	13.98
3374	O	PRO	B	398	27.182	−2.197	81.859	1.00	17.80
3375	N	TYR	B	399	28.933	−3.574	81.556	1.00	18.65
3376	CA	TYR	B	399	28.615	−4.414	82.725	1.00	19.43
3377	CB	TYR	B	399	29.343	−5.754	82.666	1.00	11.20
3378	CG	TYR	B	399	28.852	−6.615	81.555	1.00	15.79
3379	CD1	TYR	B	399	27.613	−7.241	81.641	1.00	12.49
3380	CE1	TYR	B	399	27.121	−7.990	80.583	1.00	6.49
3381	CD2	TYR	B	399	29.603	−6.760	80.380	1.00	20.08
3382	CE2	TYR	B	399	29.137	−7.490	79.322	1.00	7.84
3383	CZ	TYR	B	399	27.882	−8.114	79.419	1.00	19.70
3384	OH	TYR	B	399	27.414	−8.862	78.341	1.00	22.13
3385	C	TYR	B	399	28.980	−3.709	84.017	1.00	18.81
3386	O	TYR	B	399	28.216	−3.749	84.967	1.00	20.59
3387	N	VAL	B	400	30.131	−3.049	84.069	1.00	16.23
3388	CA	VAL	B	400	30.460	−2.334	85.297	1.00	19.14
3389	CB	VAL	B	400	31.853	−1.643	85.227	1.00	18.68
3390	CG1	VAL	B	400	31.994	−0.551	86.289	1.00	5.30
3391	CG2	VAL	B	400	32.919	−2.691	85.449	1.00	19.53
3392	C	VAL	B	400	29.384	−1.288	85.544	1.00	17.89
3393	O	VAL	B	400	28.964	−1.110	86.664	1.00	23.07
3394	N	GLU	B	401	28.911	−0.623	84.495	1.00	15.04
3395	CA	GLU	B	401	27.886	0.398	84.662	1.00	11.15
3396	CB	GLU	B	401	27.698	1.140	83.360	1.00	7.42
3397	CG	GLU	B	401	26.608	2.123	83.364	1.00	20.38
3398	CD	GLU	B	401	26.757	3.074	82.228	1.00	37.37
3399	OE1	GLU	B	401	26.867	2.620	81.057	1.00	39.44
3400	OE2	GLU	B	401	26.780	4.282	82.518	1.00	39.71
3401	C	GLU	B	401	26.557	−0.211	85.119	1.00	13.41
3402	O	GLU	B	401	25.847	0.386	85.938	1.00	12.31
3403	N	ALA	B	402	26.225	−1.404	84.623	1.00	11.22
3404	CA	ALA	B	402	24.965	−2.000	85.000	1.00	12.10
3405	CB	ALA	B	402	24.760	−3.240	84.180	1.00	15.56
3406	C	ALA	B	402	25.021	−2.304	86.519	1.00	16.14
3407	O	ALA	B	402	24.032	−2.230	87.233	1.00	16.28
3408	N	LEU	B	403	26.211	−2.608	87.018	1.00	14.33
3409	CA	LEU	B	403	26.364	−2.917	88.424	1.00	12.70
3410	CB	LEU	B	403	27.694	−3.571	88.660	1.00	14.10
3411	CG	LEU	B	403	27.950	−4.153	90.036	1.00	5.25
3412	CD1	LEU	B	403	27.039	−5.370	90.321	1.00	5.25
3413	CD2	LEU	B	403	29.407	−4.531	90.070	1.00	13.26
3414	C	LEU	B	403	26.279	−1.670	89.270	1.00	16.33
3415	O	LEU	B	403	25.606	−1.654	90.309	1.00	20.44
3416	N	LEU	B	404	26.979	−0.630	88.825	1.00	15.15
3417	CA	LEU	B	404	26.984	0.646	89.500	1.00	18.81
3418	CB	LEU	B	404	27.784	1.664	88.701	1.00	9.81
3419	CG	LEU	B	404	27.772	3.017	89.442	1.00	19.99
3420	CD1	LEU	B	404	28.565	2.881	90.769	1.00	21.31
3421	CD2	LEU	B	404	28.367	4.094	88.591	1.00	17.42
3422	C	LEU	B	404	25.567	1.200	89.713	1.00	25.26
3423	O	LEU	B	404	25.214	1.654	90.819	1.00	27.46
3424	N	SER	B	405	24.770	1.173	88.645	1.00	28.43
3425	CA	SER	B	405	23.413	1.681	88.708	1.00	30.86
3426	CB	SER	B	405	22.834	1.806	87.291	1.00	27.87
3427	OG	SER	B	405	21.426	1.931	87.341	1.00	49.84
3428	C	SER	B	405	22.572	0.760	89.589	1.00	28.69
3429	O	SER	B	405	21.738	1.217	90.362	1.00	34.53
3430	N	TYR	B	406	22.827	−0.536	89.498	1.00	25.87
3431	CA	TYR	B	406	22.091	−1.514	90.290	1.00	23.94
3432	CB	TYR	B	406	22.499	−2.918	89.855	1.00	16.25
3433	CG	TYR	B	406	21.671	−3.995	90.459	1.00	22.54
3434	CD1	TYR	B	406	20.454	−4.365	89.886	1.00	24.85
3435	CE1	TYR	B	406	19.646	−5.363	90.474	1.00	24.09
3436	CD2	TYR	B	406	22.082	−4.640	91.638	1.00	27.13
3437	CE2	TYR	B	406	21.291	−5.633	92.237	1.00	26.94
3438	CZ	TYR	B	406	20.065	−5.997	91.643	1.00	30.69
3439	OH	TYR	B	406	19.290	−7.027	92.192	1.00	26.76
3440	C	TYR	B	406	22.328	−1.357	91.802	1.00	22.98
3441	O	TYR	B	406	21.387	−1.179	92.575	1.00	22.41
3442	N	THR	B	407	23.588	−1.408	92.221	1.00	21.64
3443	CA	THR	B	407	23.910	−1.304	93.641	1.00	22.30
3444	CB	THR	B	407	25.424	−1.403	93.879	1.00	18.93
3445	OG1	THR	B	407	26.077	−0.330	93.181	1.00	20.67
3446	CG2	THR	B	407	25.967	−2.755	93.419	1.00	10.74
3447	C	THR	B	407	23.441	0.027	94.224	1.00	27.40
3448	O	THR	B	407	23.142	0.125	95.438	1.00	28.52
3449	N	ARG	B	408	23.366	1.043	93.359	1.00	25.32
3450	CA	ARG	B	408	22.941	2.364	93.778	1.00	22.43
3451	CB	ARG	B	408	23.170	3.363	92.651	1.00	18.62
3452	CG	ARG	B	408	23.166	4.801	93.095	1.00	31.32
3453	CD	ARG	B	408	24.367	5.146	93.954	1.00	39.94
3454	NE	ARG	B	408	24.314	6.530	94.424	1.00	62.46
3455	CZ	ARG	B	408	24.457	7.599	93.640	1.00	70.70
3456	NH1	ARG	B	408	24.671	7.436	92.342	1.00	71.99
3457	NH2	ARG	B	408	24.363	8.830	94.146	1.00	68.86
3458	C	ARG	B	408	21.463	2.331	94.153	1.00	25.92
3459	O	ARG	B	408	21.051	2.960	95.132	1.00	29.04
3460	N	ILE	B	409	20.671	1.594	93.380	1.00	23.14
3461	CA	ILE	B	409	19.245	1.477	93.624	1.00	24.07
3462	CB	ILE	B	409	18.549	0.982	92.334	1.00	31.63
3463	CG2	ILE	B	409	17.158	0.415	92.611	1.00	31.53
3464	CG1	ILE	B	409	18.472	2.131	91.336	1.00	27.41
3465	CD1	ILE	B	409	18.056	1.651	89.934	1.00	38.63
3466	C	ILE	B	409	18.958	0.517	94.781	1.00	29.16
3467	O	ILE	B	409	17.977	0.679	95.503	1.00	30.54
3468	N	LYS	B	410	19.820	−0.481	94.951	1.00	30.14
3469	CA	LYS	B	410	19.672	−1.457	96.019	1.00	29.72
3470	CB	LYS	B	410	20.548	−2.682	95.741	1.00	28.57
3471	CG	LYS	B	410	20.378	−3.815	96.754	1.00	34.90
3472	CD	LYS	B	410	21.126	−5.069	96.330	1.00	34.66
3473	CE	LYS	B	410	20.786	−6.234	97.205	1.00	22.65
3474	NZ	LYS	B	410	21.487	−7.471	96.748	1.00	27.10
3475	C	LYS	B	410	20.048	−0.861	97.389	1.00	27.38
3476	O	LYS	B	410	19.389	−1.134	98.380	1.00	28.37
3477	N	ARG	B	411	21.101	−0.060	97.467	1.00	23.84
3478	CA	ARG	B	411	21.446	0.510	98.773	1.00	24.63
3479	CB	ARG	B	411	22.529	−0.333	99.478	1.00	26.88
3480	CG	ARG	B	411	22.214	−1.822	99.449	1.00	31.02
3481	CD	ARG	B	411	22.225	−2.418	100.835	1.00	40.94
3482	NE	ARG	B	411	23.438	−3.184	101.133	1.00	44.64
3483	CZ	ARG	B	411	23.475	−4.259	101.923	1.00	39.45
3484	NH1	ARG	B	411	22.363	−4.700	102.486	1.00	49.81
3485	NH2	ARG	B	411	24.625	−4.880	102.173	1.00	37.84
3486	C	ARG	B	411	21.894	1.942	98.541	1.00	20.38
3487	O	ARG	B	411	23.078	2.252	98.482	1.00	26.11
3488	N	PRO	B	412	20.918	2.841	98.398	1.00	17.18
3489	CD	PRO	B	412	19.491	2.471	98.413	1.00	10.00
3490	CA	PRO	B	412	21.106	4.270	98.143	1.00	11.86
3491	CB	PRO	B	412	19.703	4.801	98.122	1.00	5.25
3492	CG	PRO	B	412	18.885	3.585	97.700	1.00	6.95
3493	C	PRO	B	412	21.933	4.941	99.151	1.00	17.42
3494	O	PRO	B	412	22.670	5.826	98.814	1.00	15.03
3495	N	GLN	B	413	21.808	4.499	100.400	1.00	27.59
3496	CA	GLN	B	413	22.542	5.104	101.502	1.00	28.72
3497	CB	GLN	B	413	21.660	5.093	102.749	1.00	40.02
3498	CG	GLN	B	413	20.436	6.039	102.688	1.00	58.84
3499	CD	GLN	B	413	19.102	5.279	102.647	1.00	73.73
3500	OE1	GLN	B	413	18.725	4.708	101.606	1.00	77.93
3501	NE2	GLN	B	413	18.398	5.240	103.789	1.00	69.98
3502	C	GLN	B	413	23.896	4.451	101.802	1.00	29.82
3503	O	GLN	B	413	24.511	4.711	102.836	1.00	37.66
3504	N	ASP	B	414	24.365	3.594	100.905	1.00	26.65
3505	CA	ASP	B	414	25.645	2.928	101.086	1.00	19.28
3506	CB	ASP	B	414	25.455	1.499	101.596	1.00	17.43
3507	CG	ASP	B	414	26.779	0.815	101.943	1.00	18.73
3508	OD1	ASP	B	414	27.805	1.519	102.103	1.00	26.26
3509	OD2	ASP	B	414	26.785	−0.421	102.075	1.00	6.65
3510	C	ASP	B	414	26.393	2.906	99.763	1.00	17.97
3511	O	ASP	B	414	26.588	1.853	99.171	1.00	13.81
3512	N	GLN	B	415	26.831	4.079	99.324	1.00	18.40
3513	CA	GLN	B	415	27.526	4.162	98.079	1.00	23.60
3514	CB	GLN	B	415	27.506	5.585	97.547	1.00	30.14
3515	CG	GLN	B	415	28.044	6.586	98.515	1.00	47.25
3516	CD	GLN	B	415	28.254	7.923	97.837	1.00	59.35
3517	OE1	GLN	B	415	27.408	8.350	97.021	1.00	57.51
3518	NE2	GLN	B	415	29.378	8.599	98.160	1.00	51.01
3519	C	GLN	B	415	28.941	3.629	98.135	1.00	22.02
3520	O	GLN	B	415	29.747	3.860	97.217	1.00	23.65
3521	N	LEU	B	416	29.265	2.914	99.200	1.00	19.34
3522	CA	LEU	B	416	30.599	2.325	99.251	1.00	20.84
3523	CB	LEU	B	416	31.280	2.641	100.572	1.00	19.15
3524	CG	LEU	B	416	31.886	4.041	100.799	1.00	25.91
3525	CD1	LEU	B	416	33.230	3.855	101.446	1.00	24.35
3526	CD2	LEU	B	416	32.101	4.795	99.502	1.00	24.30
3527	C	LEU	B	416	30.525	0.795	99.020	1.00	21.13
3528	O	LEU	B	416	31.530	0.097	98.900	1.00	17.19
3529	N	ARG	B	417	29.304	0.284	98.930	1.00	24.16
3530	CA	ARG	B	417	29.069	−1.136	98.685	1.00	21.61
3531	CB	ARG	B	417	27.565	−1.406	98.680	1.00	29.84
3532	CG	ARG	B	417	27.165	−2.819	98.393	1.00	16.14
3533	CD	ARG	B	417	25.781	−3.094	98.956	1.00	17.27
3534	NE	ARG	B	417	25.517	−4.520	98.917	1.00	19.36
3535	CZ	ARG	B	417	24.965	−5.158	97.897	1.00	21.88
3536	NH1	ARG	B	417	24.567	−4.531	96.799	1.00	24.73
3537	NH2	ARG	B	417	24.871	−6.461	97.962	1.00	26.24
3538	C	ARG	B	417	29.639	−1.467	97.316	1.00	22.39
3539	O	ARG	B	417	30.498	−2.350	97.178	1.00	19.83
3540	N	PHE	B	418	29.171	−0.757	96.288	1.00	21.46
3541	CA	PHE	B	418	29.688	−1.037	94.946	1.00	19.87
3542	CB	PHE	B	418	29.267	0.028	93.977	1.00	13.06
3543	CG	PHE	B	418	29.834	−0.152	92.643	1.00	17.77
3544	CD1	PHE	B	418	29.412	−1.212	91.841	1.00	27.33
3545	CD2	PHE	B	418	30.830	0.700	92.186	1.00	19.47
3546	CE1	PHE	B	418	29.986	−1.432	90.593	1.00	22.32
3547	CE2	PHE	B	418	31.420	0.488	90.927	1.00	19.06
3548	CZ	PHE	B	418	30.997	−0.571	90.144	1.00	27.55
3549	C	PHE	B	418	31.220	−1.189	94.909	1.00	18.37
3550	O	PHE	B	418	31.737	−2.168	94.371	1.00	20.12
3551	N	PRO	B	419	31.958	−0.242	95.505	1.00	14.48
3552	CD	PRO	B	419	31.567	1.103	95.939	1.00	12.36
3553	CA	PRO	B	419	33.410	−0.359	95.494	1.00	14.31
3554	CB	PRO	B	419	33.863	0.945	96.141	1.00	15.64
3555	CG	PRO	B	419	32.884	1.896	95.745	1.00	5.25
3556	C	PRO	B	419	33.894	−1.589	96.264	1.00	18.29
3557	O	PRO	B	419	34.961	−2.131	95.950	1.00	22.41
3558	N	ARG	B	420	33.131	−2.039	97.262	1.00	17.55
3559	CA	ARG	B	420	33.563	−3.218	98.030	1.00	18.76
3560	CB	ARG	B	420	32.657	−3.515	99.228	1.00	16.09
3561	CG	ARG	B	420	32.818	−2.592	100.389	1.00	23.27
3562	CD	ARG	B	420	32.034	−3.061	101.593	1.00	31.13
3563	NE	ARG	B	420	32.051	−2.010	102.608	1.00	53.34
3564	CZ	ARG	B	420	31.211	−0.972	102.659	1.00	53.62
3565	NH1	ARG	B	420	30.249	−0.838	101.764	1.00	45.38
3566	NH2	ARG	B	420	31.366	−0.038	103.594	1.00	56.87
3567	C	ARG	B	420	33.516	−4.405	97.092	1.00	23.08
3568	O	ARG	B	420	34.392	−5.272	97.113	1.00	25.02
3569	N	MET	B	421	32.473	−4.471	96.271	1.00	26.24
3570	CA	MET	B	421	32.392	−5.571	95.320	1.00	26.72
3571	CB	MET	B	421	31.156	−5.438	94.462	1.00	26.46
3572	CG	MET	B	421	29.952	−5.847	95.217	1.00	24.52
3573	SD	MET	B	421	28.542	−5.881	94.219	1.00	22.16
3574	CE	MET	B	421	27.317	−5.174	95.426	1.00	22.65
3575	C	MET	B	421	33.620	−5.604	94.438	1.00	26.26
3576	O	MET	B	421	34.280	−6.652	94.375	1.00	31.69
3577	N	LEU	B	422	33.927	−4.465	93.791	1.00	20.52
3578	CA	LEU	B	422	35.067	−4.356	92.919	1.00	15.96
3579	CB	LEU	B	422	35.222	−2.931	92.432	1.00	23.55
3580	CG	LEU	B	422	34.273	−2.525	91.276	1.00	25.39
3581	CD1	LEU	B	422	34.433	−1.038	90.897	1.00	23.98
3582	CD2	LEU	B	422	34.584	−3.354	90.115	1.00	26.78
3583	C	LEU	B	422	36.295	−4.815	93.652	1.00	17.24
3584	O	LEU	B	422	37.150	−5.462	93.075	1.00	15.66
3585	N	MET	B	423	36.380	−4.521	94.940	1.00	16.96
3586	CA	MET	B	423	37.537	−4.971	95.701	1.00	18.89
3587	CB	MET	B	423	37.480	−4.349	97.097	1.00	21.05
3588	CG	MET	B	423	38.772	−3.653	97.532	1.00	37.96
3589	SD	MET	B	423	39.133	−2.155	96.569	1.00	48.80
3590	CE	MET	B	423	37.726	−1.154	97.116	1.00	55.61
3591	C	MET	B	423	37.628	−6.540	95.775	1.00	19.54
3592	O	MET	B	423	38.704	−7.109	96.010	1.00	22.90
3593	N	LYS	B	424	36.511	−7.242	95.562	1.00	19.78
3594	CA	LYS	B	424	36.522	−8.709	95.587	1.00	18.28
3595	CB	LYS	B	424	35.102	−9.217	95.740	1.00	14.35
3596	CG	LYS	B	424	34.494	−8.824	97.077	1.00	19.78
3597	CD	LYS	B	424	35.192	−9.579	98.220	1.00	16.47
3598	CE	LYS	B	424	34.653	−9.192	99.592	1.00	26.47
3599	NZ	LYS	B	424	35.607	−8.267	100.347	1.00	29.05
3600	C	LYS	B	424	37.192	−9.278	94.314	1.00	19.45
3601	O	LYS	B	424	37.642	−10.432	94.275	1.00	14.12
3602	N	LEU	B	425	37.257	−8.465	93.261	1.00	20.50
3603	CA	LEU	B	425	37.945	−8.906	92.057	1.00	17.30
3604	CB	LEU	B	425	37.693	−7.970	90.891	1.00	10.42
3605	CG	LEU	B	425	36.256	−7.932	90.363	1.00	22.59
3606	CD1	LEU	B	425	36.129	−6.841	89.275	1.00	12.90
3607	CD2	LEU	B	425	35.887	−9.270	89.785	1.00	12.37
3608	C	LEU	B	425	39.429	−8.884	92.424	1.00	15.79
3609	O	LEU	B	425	40.200	−9.738	91.989	1.00	21.26
3610	N	VAL	B	426	39.830	−7.929	93.248	1.00	10.39
3611	CA	VAL	B	426	41.229	−7.853	93.642	1.00	15.67
3612	CB	VAL	B	426	41.456	−6.711	94.680	1.00	15.21
3613	CG1	VAL	B	426	42.861	−6.798	95.251	1.00	6.06
3614	CG2	VAL	B	426	41.235	−5.329	94.031	1.00	12.87
3615	C	VAL	B	426	41.655	−9.213	94.264	1.00	19.24
3616	O	VAL	B	426	42.706	−9.820	93.930	1.00	19.27
3617	N	SER	B	427	40.823	−9.702	95.166	1.00	16.66
3618	CA	SER	B	427	41.103	−10.963	95.825	1.00	17.77
3619	CB	SER	B	427	40.050	−11.220	96.864	1.00	15.50
3620	OG	SER	B	427	39.982	−10.130	97.760	1.00	28.60
3621	C	SER	B	427	41.148	−12.136	94.875	1.00	21.81
3622	O	SER	B	427	42.012	−12.995	95.008	1.00	25.86
3623	N	LEU	B	428	40.220	−12.194	93.926	1.00	19.86
3624	CA	LEU	B	428	40.257	−13.302	92.987	1.00	18.69
3625	CB	LEU	B	428	39.150	−13.169	91.930	1.00	21.55
3626	CG	LEU	B	428	37.756	−13.238	92.528	1.00	14.78
3627	CD1	LEU	B	428	36.745	−12.976	91.449	1.00	13.20
3628	CD2	LEU	B	428	37.579	−14.607	93.183	1.00	5.25
3629	C	LEU	B	428	41.621	−13.379	92.300	1.00	16.34
3630	O	LEU	B	428	42.053	−14.454	91.922	1.00	20.34
3631	N	ARG	B	429	42.292	−12.250	92.118	1.00	13.61
3632	CA	ARG	B	429	43.575	−12.319	91.481	1.00	14.98
3633	CB	ARG	B	429	44.131	−10.936	91.220	1.00	22.87
3634	CG	ARG	B	429	43.547	−10.244	90.010	1.00	17.78
3635	CD	ARG	B	429	43.500	−11.204	88.851	1.00	26.45
3636	NE	ARG	B	429	42.578	−10.691	87.848	1.00	25.15
3637	CZ	ARG	B	429	42.874	−9.711	87.008	1.00	21.97
3638	NH1	ARG	B	429	44.065	−9.153	87.042	1.00	19.57
3639	NH2	ARG	B	429	41.969	−9.278	86.147	1.00	35.54
3640	C	ARG	B	429	44.481	−13.081	92.421	1.00	16.08
3641	O	ARG	B	429	45.044	−14.111	92.057	1.00	21.79
3642	N	THR	B	430	44.621	−12.595	93.642	1.00	14.07
3643	CA	THR	B	430	45.452	−13.296	94.620	1.00	15.97
3644	CB	THR	B	430	45.339	−12.646	96.079	1.00	9.39
3645	OG1	THR	B	430	45.995	−11.357	96.080	1.00	14.87
3646	CG2	THR	B	430	46.033	−13.520	97.122	1.00	5.25
3647	C	THR	B	430	45.060	−14.795	94.676	1.00	17.85
3648	O	THR	B	430	45.911	−15.685	94.529	1.00	18.15
3649	N	LEU	B	431	43.781	−15.085	94.887	1.00	17.45
3650	CA	LEU	B	431	43.366	−16.479	94.964	1.00	16.00
3651	CB	LEU	B	431	41.852	−16.597	95.030	1.00	14.31
3652	CG	LEU	B	431	41.172	−16.422	96.386	1.00	10.47
3653	CD1	LEU	B	431	39.683	−16.470	96.162	1.00	21.26
3654	CD2	LEU	B	431	41.612	−17.516	97.342	1.00	16.24
3655	C	LEU	B	431	43.891	−17.251	93.773	1.00	16.84
3656	O	LEU	B	431	44.572	−18.284	93.947	1.00	19.07
3657	N	SER	B	432	43.593	−16.736	92.575	1.00	13.15
3658	CA	SER	B	432	44.051	−17.351	91.331	1.00	12.49
3659	CB	SER	B	432	43.841	−16.400	90.163	1.00	5.25
3660	OG	SER	B	432	44.497	−16.878	89.014	1.00	16.69
3661	C	SER	B	432	45.518	−17.704	91.466	1.00	12.52
3662	O	SER	B	432	45.979	−18.771	91.060	1.00	14.34
3663	N	SER	B	433	46.248	−16.811	92.102	1.00	12.12
3664	CA	SER	B	433	47.669	−17.032	92.326	1.00	11.06
3665	CB	SER	B	433	48.306	−15.754	92.899	1.00	7.83
3666	OG	SER	B	433	49.703	−15.834	92.934	1.00	20.00
3667	C	SER	B	433	47.909	−18.200	93.265	1.00	11.27
3668	O	SER	B	433	48.640	−19.084	92.941	1.00	17.43
3669	N	VAL	B	434	47.284	−18.201	94.432	1.00	13.16
3670	CA	VAL	B	434	47.480	−19.271	95.410	1.00	15.82
3671	CB	VAL	B	434	46.644	−19.041	96.638	1.00	13.23
3672	CG1	VAL	B	434	46.769	−20.194	97.581	1.00	28.07
3673	CG2	VAL	B	434	47.099	−17.807	97.299	1.00	19.18
3674	C	VAL	B	434	47.074	−20.602	94.821	1.00	17.34
3675	O	VAL	B	434	47.662	−21.655	95.136	1.00	15.32
3676	N	HIS	B	435	46.067	−20.539	93.955	1.00	19.92
3677	CA	HIS	B	435	45.558	−21.719	93.263	1.00	20.76
3678	CB	HIS	B	435	44.291	−21.354	92.522	1.00	16.13
3679	CG	HIS	B	435	43.938	−22.327	91.449	1.00	13.43
3680	CD2	HIS	B	435	44.084	−22.273	90.099	1.00	19.51
3681	ND1	HIS	B	435	43.386	−23.552	91.723	1.00	11.55
3682	CE1	HIS	B	435	43.199	−24.214	90.590	1.00	21.95
3683	NE2	HIS	B	435	43.617	−23.458	89.589	1.00	18.37
3684	C	HIS	B	435	46.587	−22.325	92.265	1.00	22.94
3685	O	HIS	B	435	46.665	−23.554	92.081	1.00	22.54
3686	N	SER	B	436	47.372	−21.469	91.617	1.00	22.22
3687	CA	SER	B	436	48.376	−21.988	90.703	1.00	26.24
3688	CB	SER	B	436	48.882	−20.900	89.784	1.00	16.08
3689	OG	SER	B	436	49.629	−19.982	90.515	1.00	31.23
3690	C	SER	B	436	49.517	−22.559	91.551	1.00	27.57
3691	O	SER	B	436	50.224	−23.486	91.135	1.00	31.33
3692	N	GLU	B	437	49.690	−22.026	92.755	1.00	24.78
3693	CA	GLU	B	437	50.717	−22.575	93.595	1.00	30.51
3694	CB	GLU	B	437	51.020	−21.669	94.765	1.00	32.25
3695	CG	GLU	B	437	51.777	−20.430	94.342	1.00	52.73
3696	CD	GLU	B	437	52.395	−19.681	95.513	1.00	57.67
3697	OE1	GLU	B	437	51.659	−18.973	96.260	1.00	58.28
3698	OE2	GLU	B	437	53.627	−19.813	95.688	1.00	55.84
3699	C	GLU	B	437	50.239	−23.904	94.088	1.00	30.02
3700	O	GLU	B	437	51.023	−24.686	94.598	1.00	31.65
3701	N	GLN	B	438	48.943	−24.152	93.923	1.00	29.86
3702	CA	GLN	B	438	48.350	−25.419	94.332	1.00	31.57
3703	CB	GLN	B	438	46.843	−25.222	94.617	1.00	32.61
3704	CG	GLN	B	438	46.058	−26.530	94.780	1.00	28.99
3705	CD	GLN	B	438	46.512	−27.280	95.992	1.00	18.79
3706	OE1	GLN	B	438	45.973	−27.124	97.083	1.00	7.08
3707	NE2	GLN	B	438	47.529	−28.071	95.818	1.00	14.08
3708	C	GLN	B	438	48.552	−26.473	93.204	1.00	30.40
3709	O	GLN	B	438	48.848	−27.652	93.454	1.00	20.62
3710	N	VAL	B	439	48.372	−26.026	91.963	1.00	28.89
3711	CA	VAL	B	439	48.517	−26.898	90.817	1.00	32.98
3712	CB	VAL	B	439	48.106	−26.171	89.555	1.00	28.41
3713	CG1	VAL	B	439	48.478	−26.980	88.331	1.00	29.66
3714	CG2	VAL	B	439	46.618	−25.936	89.597	1.00	31.84
3715	C	VAL	B	439	49.964	−27.352	90.721	1.00	35.16
3716	O	VAL	B	439	50.253	−28.511	90.461	1.00	37.48
3717	N	PHE	B	440	50.877	−26.425	90.930	1.00	35.36
3718	CA	PHE	B	440	52.284	−26.758	90.916	1.00	37.14
3719	CB	PHE	B	440	53.069	−25.504	91.166	1.00	42.75
3720	CG	PHE	B	440	54.504	−25.742	91.492	1.00	52.63
3721	CD1	PHE	B	440	55.000	−25.476	92.756	1.00	55.53
3722	CD2	PHE	B	440	55.385	−26.121	90.505	1.00	58.98
3723	CE1	PHE	B	440	56.369	−25.579	93.012	1.00	58.23
3724	CE2	PHE	B	440	56.751	−26.226	90.756	1.00	60.45
3725	CZ	PHE	B	440	57.240	−25.953	91.999	1.00	58.33
3726	C	PHE	B	440	52.533	−27.724	92.058	1.00	38.13
3727	O	PHE	B	440	53.277	−28.683	91.916	1.00	36.27
3728	N	ALA	B	441	51.897	−27.433	93.193	1.00	41.03
3729	CA	ALA	B	441	52.006	−28.231	94.404	1.00	38.74
3730	CB	ALA	B	441	51.241	−27.558	95.544	1.00	38.21
3731	C	ALA	B	441	51.492	−29.653	94.202	1.00	41.20
3732	O	ALA	B	441	52.049	−30.598	94.778	1.00	44.01
3733	N	LEU	B	442	50.428	−29.827	93.418	1.00	39.40
3734	CA	LEU	B	442	49.938	−31.179	93.223	1.00	45.00
3735	CB	LEU	B	442	48.402	−31.291	93.408	1.00	44.36
3736	CG	LEU	B	442	47.553	−30.244	92.704	1.00	48.78
3737	CD1	LEU	B	442	47.759	−30.335	91.219	1.00	47.07
3738	CD2	LEU	B	442	46.126	−30.447	93.039	1.00	40.98
3739	C	LEU	B	442	50.380	−31.721	91.881	1.00	49.14
3740	O	LEU	B	442	49.609	−32.344	91.144	1.00	50.63
3741	N	ARG	B	443	51.636	−31.445	91.556	1.00	51.74
3742	CA	ARG	B	443	52.214	−31.973	90.344	1.00	56.94
3743	CB	ARG	B	443	52.483	−30.893	89.301	1.00	64.35
3744	CG	ARG	B	443	53.907	−30.512	89.207	1.00	73.15
3745	CD	ARG	B	443	54.252	−29.690	87.962	1.00	75.45
3746	NE	ARG	B	443	55.411	−28.853	88.278	1.00	84.04
3747	CZ	ARG	B	443	56.364	−29.204	89.148	1.00	84.49
3748	NH1	ARG	B	443	56.292	−30.364	89.778	1.00	84.77
3749	NH2	ARG	B	443	57.396	−28.402	89.394	1.00	84.34
3750	C	ARG	B	443	53.524	−32.656	90.765	1.00	58.29
3751	O	ARG	B	443	54.010	−33.553	90.087	1.00	61.51
3752	N	LEU	B	444	54.108	−32.219	91.875	1.00	57.37
3753	CA	LEU	B	444	55.303	−32.866	92.387	1.00	56.22
3754	CB	LEU	B	444	56.356	−31.839	92.780	1.00	46.58
3755	CG	LEU	B	444	55.832	−30.667	93.566	1.00	45.81
3756	CD1	LEU	B	444	55.264	−31.114	94.891	1.00	40.63
3757	CD2	LEU	B	444	56.956	−29.725	93.812	1.00	42.09
3758	C	LEU	B	444	54.821	−33.697	93.570	1.00	60.75
3759	O	LEU	B	444	55.598	−34.344	94.288	1.00	64.57
3760	N	GLN	B	445	53.512	−33.628	93.795	1.00	63.20
3761	CA	GLN	B	445	52.894	−34.448	94.817	1.00	65.62
3762	CB	GLN	B	445	51.586	−33.855	95.304	1.00	66.95
3763	CG	GLN	B	445	51.441	−33.848	96.784	1.00	67.17
3764	CD	GLN	B	445	50.011	−33.686	97.187	1.00	78.52
3765	OE1	GLN	B	445	49.706	−33.566	98.373	1.00	83.85
3766	NE2	GLN	B	445	49.107	−33.697	96.202	1.00	75.18
3767	C	GLN	B	445	52.601	−35.594	93.843	1.00	68.02
3768	O	GLN	B	445	53.156	−35.627	92.722	1.00	70.38
3769	N	ASP	B	446	51.712	−36.510	94.195	1.00	65.55
3770	CA	ASP	B	446	51.463	−37.605	93.275	1.00	65.65
3771	CB	ASP	B	446	51.003	−38.828	94.074	1.00	68.46
3772	CG	ASP	B	446	49.491	−38.970	94.087	1.00	80.66
3773	OD1	ASP	B	446	48.821	−38.082	94.675	1.00	85.07
3774	OD2	ASP	B	446	48.973	−39.950	93.481	1.00	84.14
3775	C	ASP	B	446	50.517	−37.389	92.073	1.00	65.38
3776	O	ASP	B	446	50.828	−37.814	90.943	1.00	65.01
3777	N	LYS	B	447	49.413	−36.674	92.268	1.00	62.03
3778	CA	LYS	B	447	48.428	−36.590	91.201	1.00	57.38
3779	CB	LYS	B	447	47.075	−36.604	91.863	1.00	53.29
3780	CG	LYS	B	447	46.954	−35.520	92.915	1.00	44.15
3781	CD	LYS	B	447	46.999	−36.068	94.334	1.00	53.51
3782	CE	LYS	B	447	45.817	−36.985	94.621	1.00	51.24
3783	NZ	LYS	B	447	46.116	−37.877	95.783	1.00	46.86
3784	C	LYS	B	447	48.414	−35.564	90.054	1.00	56.84
3785	O	LYS	B	447	48.875	−34.437	90.218	1.00	56.28
3786	N	LYS	B	448	47.855	−35.977	88.904	1.00	52.56
3787	CA	LYS	B	448	47.745	−35.114	87.730	1.00	47.66
3788	CB	LYS	B	448	48.241	−35.852	86.476	1.00	52.17
3789	CG	LYS	B	448	49.387	−36.809	86.784	1.00	59.51
3790	CD	LYS	B	448	50.336	−37.016	85.619	1.00	72.25
3791	CE	LYS	B	448	51.569	−37.802	86.080	1.00	76.88
3792	NZ	LYS	B	448	52.651	−37.852	85.038	1.00	83.91
3793	C	LYS	B	448	46.272	−34.712	87.573	1.00	41.95
3794	O	LYS	B	448	45.432	−35.114	88.367	1.00	36.65
3795	N	LEU	B	449	45.964	−33.933	86.542	1.00	36.83
3796	CA	LEU	B	449	44.600	−33.475	86.317	1.00	29.86
3797	CB	LEU	B	449	44.586	−31.939	86.315	1.00	29.17
3798	CG	LEU	B	449	45.319	−31.191	87.441	1.00	21.55
3799	CD1	LEU	B	449	45.698	−29.739	87.026	1.00	13.48
3800	CD2	LEU	B	449	44.414	−31.191	88.666	1.00	25.46
3801	C	LEU	B	449	44.013	−33.966	85.001	1.00	25.36
3802	O	LEU	B	449	44.727	−34.159	84.017	1.00	20.95
3803	N	PRO	B	450	42.693	−34.159	84.959	1.00	23.78
3804	CD	PRO	B	450	41.633	−34.036	85.973	1.00	15.08
3805	CA	PRO	B	450	42.158	−34.616	83.670	1.00	24.94
3806	GB	PRO	B	450	40.642	−34.726	83.918	1.00	19.41
3807	CG	PRO	B	450	40.405	−33.860	85.110	1.00	19.53
3808	C	PRO	B	450	42.498	−33.588	82.618	1.00	27.11
3809	O	PRO	B	450	42.523	−32.384	82.933	1.00	26.09
3810	N	PRO	B	451	42.775	−34.040	81.366	1.00	29.87
3811	CD	PRO	B	451	42.281	−35.332	80.852	1.00	26.06
3812	CA	PRO	B	451	43.127	−33.160	80.233	1.00	27.77
3813	CB	PRO	B	451	42.705	−33.991	79.011	1.00	25.33
3814	CG	PRO	B	451	41.672	−34.911	79.548	1.00	28.40
3815	C	PRO	B	451	42.537	−31.742	80.216	1.00	23.36
3816	O	PRO	B	451	43.259	−30.771	80.128	1.00	27.32
3817	N	LEU	B	452	41.227	−31.635	80.298	1.00	19.34
3818	CA	LEU	B	452	40.610	−30.336	80.289	1.00	18.25
3819	CB	LEU	B	452	39.095	−30.464	80.525	1.00	14.12
3820	CG	LEU	B	452	38.325	−29.138	80.411	1.00	13.10
3821	CD1	LEU	B	452	38.711	−28.489	79.089	1.00	18.06
3822	CD2	LEU	B	452	36.855	−29.329	80.488	1.00	5.25
3823	C	LEU	B	452	41.244	−29.424	81.346	1.00	19.73
3824	O	LEU	B	452	41.904	−28.434	80.990	1.00	18.11
3825	N	LEU	B	453	41.033	−29.737	82.629	1.00	18.83
3826	CA	LEU	B	453	41.602	−28.927	83.707	1.00	19.53
3827	GB	LEU	B	453	41.444	−29.610	85.060	1.00	13.81
3828	CG	LEU	B	453	40.005	−29.927	85.467	1.00	22.28
3829	CD1	LEU	B	453	40.019	−30.669	86.841	1.00	12.32
3830	CD2	LEU	B	453	39.206	−28.627	85.529	1.00	10.46
3831	C	LEU	B	453	43.081	−28.680	83.463	1.00	22.21
3832	O	LEU	B	453	43.583	−27.565	83.690	1.00	23.09
3833	N	SER	B	454	43.770	−29.728	83.011	1.00	22.76
3834	CA	SER	B	454	45.193	−29.644	82.712	1.00	23.20
3835	CB	SER	B	454	45.702	−31.022	82.293	1.00	28.99
3836	OG	SER	B	454	47.115	−30.997	82.118	1.00	31.87
3837	C	SER	B	454	45.494	−28.593	81.591	1.00	21.00
3838	O	SER	B	454	46.543	−27.934	81.598	1.00	16.82
3839	N	GLU	B	455	44.582	−28.469	80.635	1.00	17.12
3840	CA	GLU	B	455	44.726	−27.496	79.576	1.00	24.84
3841	CB	GLU	B	455	43.526	−27.501	78.662	1.00	26.84
3842	CG	GLU	B	455	43.700	−28.184	77.353	1.00	18.84
3843	CD	GLU	B	455	42.476	−27.976	76.444	1.00	38.40
3844	OE1	GLU	B	455	42.120	−28.905	75.655	1.00	30.86
3845	OE2	GLU	B	455	41.859	−26.868	76.516	1.00	26.15
3846	C	GLU	B	455	44.794	−26.119	80.183	1.00	30.03
3847	O	GLU	B	455	45.732	−25.375	79.938	1.00	33.86
3848	N	ILE	B	456	43.788	−25.790	80.983	1.00	32.39
3849	CA	ILE	B	456	43.691	−24.492	81.643	1.00	33.77
3850	CB	ILE	B	456	42.298	−24.352	82.263	1.00	37.16
3851	CG2	ILE	B	456	42.093	−22.971	82.780	1.00	44.25
3852	CG1	ILE	B	456	41.238	−24.668	81.231	1.00	32.75
3853	CD1	ILE	B	456	39.825	−24.585	81.833	1.00	44.84
3854	C	ILE	B	456	44.703	−24.174	82.755	1.00	31.98
3855	O	ILE	B	456	45.170	−23.053	82.861	1.00	22.75
3856	N	TRP	B	457	45.057	−25.178	83.552	1.00	35.21
3857	CA	TRP	B	457	45.928	−24.959	84.705	1.00	40.82
3858	CB	TRP	B	457	45.155	−25.417	85.942	1.00	38.48
3859	CG	TRP	B	457	43.835	−24.729	86.039	1.00	22.11
3860	CD2	TRP	B	457	42.656	−25.242	86.652	1.00	19.60
3861	CE2	TRP	B	457	41.699	−24.212	86.632	1.00	19.91
3862	CE3	TRP	B	457	42.315	−26.478	87.214	1.00	16.21
3863	CD1	TRP	B	457	43.567	−23.463	85.673	1.00	5.25
3864	NE1	TRP	B	457	42.301	−23.137	86.023	1.00	9.21
3865	CZ2	TRP	B	457	40.404	−24.358	87.167	1.00	21.85
3866	CZ3	TRP	B	457	41.031	−26.639	87.748	1.00	20.82
3867	CH2	TRP	B	457	40.087	−25.578	87.717	1.00	28.52
3868	C	TRP	B	457	47.370	−25.460	84.769	1.00	43.65
3869	O	TRP	B	457	48.235	−24.810	85.323	1.00	42.42
3870	N	ASP	B	458	47.616	−26.629	84.223	1.00	49.96
3871	CA	ASP	B	458	48.943	−27.233	84.202	1.00	57.57
3872	CB	ASP	B	458	48.814	−28.592	83.517	1.00	53.25
3873	CG	ASP	B	458	48.626	−29.711	84.456	1.00	53.35
3874	OD1	ASP	B	458	48.604	−29.447	85.668	1.00	53.90
3875	OD2	ASP	B	458	48.517	−30.865	83.990	1.00	47.19
3876	C	ASP	B	458	49.880	−26.432	83.291	1.00	66.03
3877	O	ASP	B	458	51.116	−26.670	83.226	1.00	69.33
3878	N	VAL	B	459	49.313	−25.415	82.668	1.00	72.79
3879	CA	VAL	B	459	49.997	−24.823	81.543	1.00	77.10
3880	CB	VAL	B	459	49.706	−25.870	80.387	1.00	82.78
3881	CG1	VAL	B	459	49.387	−25.195	79.068	1.00	79.26
3882	CG2	VAL	B	459	50.805	−26.921	80.294	1.00	77.57
3883	C	VAL	B	459	49.287	−23.512	81.206	1.00	78.30
3884	O	VAL	B	459	48.034	−23.590	81.120	1.00	74.12
3885	OT	VAL	B	459	49.966	−22.483	80.966	1.00	85.25
3886		VAL	B	459
3887	CB	ALA	C	−3	54.311	−13.946	114.812	1.00	76.41
3888	C	ALA	C	−3	56.087	−12.625	113.749	1.00	73.80
3889	O	ALA	C	−3	57.155	−12.786	113.165	1.00	76.36
3890	N	ALA	C	−3	55.919	−12.651	116.146	1.00	69.92
3891	CA	ALA	C	−3	55.735	−13.496	114.929	1.00	71.93
3892	N	LEU	C	−2	55.158	−11.736	113.386	1.00	72.81
3893	CA	LEU	C	−2	55.342	−10.770	112.302	1.00	69.21
3894	CB	LEU	C	−2	53.991	−10.325	111.752	1.00	63.26
3895	CG	LEU	C	−2	53.533	−11.140	110.563	1.00	54.22
3896	CD1	LEU	C	−2	52.080	−10.849	110.306	1.00	49.29
3897	CD2	LEU	C	−2	54.399	−10.811	109.369	1.00	49.99
3898	C	LEU	C	−2	55.993	−9.591	113.019	1.00	69.59
3899	O	LEU	C	−2	55.292	−8.692	113.507	1.00	73.65
3900	N	ALA	C	−1	57.318	−9.580	113.095	1.00	66.78
3901	CA	ALA	C	−1	58.036	−8.509	113.802	1.00	69.32
3902	CB	ALA	C	−1	57.372	−8.206	115.172	1.00	60.13
3903	C	ALA	C	−1	59.414	−9.108	114.000	1.00	67.12
3904	O	ALA	C	−1	60.454	−8.491	113.732	1.00	71.81
3905	N	ALA	C	0	59.389	−10.329	114.513	1.00	63.04
3906	CA	ALA	C	0	60.592	−11.111	114.692	1.00	56.99
3907	CB	ALA	C	0	60.285	−12.293	115.582	1.00	51.89
3908	C	ALA	C	0	60.969	−11.582	113.261	1.00	53.09
3909	O	ALA	C	0	62.120	−11.486	112.833	1.00	48.76
3910	N	ARG	C	1	59.982	−12.037	112.493	1.00	51.49
3911	CA	ARG	C	1	60.244	−12.530	111.150	1.00	46.31
3912	CB	ARG	C	1	58.969	−13.173	110.567	1.00	53.19
3913	CG	ARG	C	1	58.887	−14.686	110.805	1.00	46.35
3914	CD	ARG	C	1	57.488	−15.191	111.211	1.00	56.12
3915	NE	ARG	C	1	56.938	−16.060	110.172	1.00	62.40
3916	CZ	ARG	C	1	56.402	−15.603	109.038	1.00	70.46
3917	NH1	ARG	C	1	56.342	−14.295	108.832	1.00	70.27
3918	NH2	ARG	C	1	55.965	−16.439	108.090	1.00	60.91
3919	C	ARG	C	1	60.752	−11.403	110.254	1.00	45.64
3920	O	ARG	C	1	61.385	−11.646	109.208	1.00	44.18
3921	N	HIS	C	2	60.520	−10.167	110.698	1.00	40.66
3922	CA	HIS	C	2	60.909	−8.991	109.926	1.00	35.21
3923	CB	HIS	C	2	59.663	−8.408	109.271	1.00	35.35
3924	CG	HIS	C	2	58.977	−9.362	108.341	1.00	36.61
3925	CD2	HIS	C	2	58.701	−9.277	107.017	1.00	39.53
3926	ND1	HIS	C	2	58.499	−10.589	108.749	1.00	39.75
3927	CE1	HIS	C	2	57.963	−11.218	107.719	1.00	47.92
3928	NE2	HIS	C	2	58.073	−10.441	106.655	1.00	45.80
3929	C	HIS	C	2	61.612	−7.918	110.743	1.00	30.30
3930	O	HIS	C	2	61.117	−6.806	110.857	1.00	23.01
3931	N	LYS	C	3	62.789	−8.257	111.263	1.00	32.28
3932	CA	LYS	C	3	63.564	−7.371	112.122	1.00	32.74
3933	CB	LYS	C	3	64.897	−8.049	112.468	1.00	39.84
3934	CG	LYS	C	3	65.426	−7.709	113.849	1.00	63.43
3935	CD	LYS	C	3	66.560	−8.657	114.292	1.00	81.08
3936	CE	LYS	C	3	67.102	−8.316	115.700	1.00	83.76
3937	NZ	LYS	C	3	68.174	−9.293	116.108	1.00	81.79
3938	C	LYS	C	3	63.793	−5.948	111.593	1.00	33.33
3939	O	LYS	C	3	63.344	−4.979	112.227	1.00	28.13
3940	N	ILE	C	4	64.470	−5.822	110.441	1.00	31.52
3941	CA	ILE	C	4	64.768	−4.505	109.868	1.00	31.05
3942	CB	ILE	C	4	65.504	−4.602	108.524	1.00	27.45
3943	CG2	ILE	C	4	65.802	−3.201	108.015	1.00	15.44
3944	CG1	ILE	C	4	66.793	−5.400	108.658	1.00	15.17
3945	CD1	ILE	C	4	67.456	−5.634	107.333	1.00	5.25
3946	C	ILE	C	4	63.487	−3.703	109.601	1.00	35.03
3947	O	ILE	C	4	63.380	−2.504	109.892	1.00	38.81
3948	N	LEU	C	5	62.501	−4.367	109.036	1.00	32.79
3949	CA	LEU	C	5	61.284	−3.666	108.760	1.00	31.98
3950	CB	LEU	C	5	60.278	−4.606	108.116	1.00	28.91
3951	CG	LEU	C	5	59.032	−3.918	107.587	1.00	21.35
3952	CD1	LEU	C	5	59.475	−3.018	106.479	1.00	27.75
3953	CD2	LEU	C	5	58.025	−4.921	107.073	1.00	28.10
3954	C	LEU	C	5	60.732	−3.127	110.055	1.00	34.05
3955	O	LEU	C	5	60.301	−1.981	110.131	1.00	37.58
3956	N	HIS	C	6	60.743	−3.959	111.089	1.00	37.37
3957	CA	HIS	C	6	60.210	−3.543	112.385	1.00	40.64
3958	CB	HIS	C	6	60.402	−4.640	113.451	1.00	45.69
3959	CG	HIS	C	6	59.721	−4.343	114.764	1.00	52.81
3960	CD2	HIS	C	6	60.134	−3.641	115.848	1.00	48.43
3961	ND1	HIS	C	6	58.425	−4.734	115.044	1.00	56.64
3962	CE1	HIS	C	6	58.071	−4.283	116.233	1.00	47.70
3963	NE2	HIS	C	6	59.091	−3.614	116.743	1.00	45.83
3964	C	HIS	C	6	60.910	−2.284	112.853	1.00	42.95
3965	O	HIS	C	6	60.257	−1.390	113.365	1.00	46.57
3966	N	ARG	C	7	62.233	−2.237	112.667	1.00	41.77
3967	CA	ARG	C	7	63.072	−1.112	113.064	1.00	39.07
3968	CB	ARG	C	7	64.536	−1.425	112.743	1.00	47.69
3969	CG	ARG	C	7	65.542	−0.516	113.444	1.00	53.50
3970	CD	ARG	C	7	66.864	−0.572	112.734	1.00	59.29
3971	NE	ARG	C	7	66.855	0.241	111.514	1.00	74.08
3972	CZ	ARG	C	7	67.445	−0.109	110.371	1.00	78.20
3973	NH1	ARG	C	7	68.084	−1.271	110.290	1.00	83.39
3974	NH2	ARG	C	7	67.427	0.721	109.320	1.00	72.71
3975	C	ARG	C	7	62.663	0.199	112.376	1.00	36.66
3976	O	ARG	C	7	62.613	1.274	113.005	1.00	34.51
3977	N	LEU	C	8	62.376	0.124	111.082	1.00	32.76
3978	CA	LEU	C	8	61.949	1.330	110.368	1.00	33.44
3979	CB	LEU	C	8	61.714	1.050	108.882	1.00	26.26
3980	CG	LEU	C	8	62.997	0.774	108.087	1.00	26.09
3981	CD1	LEU	C	8	62.728	0.308	106.677	1.00	18.55
3982	CD2	LEU	C	8	63.796	2.047	108.092	1.00	30.16
3983	C	LEU	C	8	60.678	1.904	110.965	1.00	33.67
3984	O	LEU	C	8	60.523	3.110	111.030	1.00	35.99
3985	N	LEU	C	9	59.762	1.056	111.410	1.00	31.98
3986	CA	LEU	C	9	58.538	1.589	111.984	1.00	35.05
3987	CB	LEU	C	9	57.514	0.489	112.090	1.00	25.12
3988	CG	LEU	C	9	57.147	0.051	110.716	1.00	20.67
3989	CD1	LEU	C	9	56.876	−1.425	110.711	1.00	26.48
3990	CD2	LEU	C	9	55.959	0.884	110.274	1.00	20.75
3991	C	LEU	C	9	58.717	2.244	113.349	1.00	40.45
3992	O	LEU	C	9	57.824	2.944	113.825	1.00	39.35
3993	N	GLN	C	10	59.870	2.025	113.974	1.00	46.16
3994	CA	GLN	C	10	60.125	2.585	115.300	1.00	52.79
3995	CB	GLN	C	10	60.679	1.510	116.251	1.00	49.83
3996	CG	GLN	C	10	59.666	0.491	116.727	1.00	45.94
3997	CD	GLN	C	10	60.162	−0.289	117.943	1.00	46.74
3998	OE1	GLN	C	10	61.137	−1.038	117.865	1.00	47.34
3999	NE2	GLN	C	10	59.494	−0.099	119.078	1.00	45.75
4000	C	GLN	C	10	61.081	3.770	115.293	1.00	57.32
4001	O	GLN	C	10	61.180	4.476	116.298	1.00	58.42
4002	N	GLU	C	11	61.782	3.992	114.179	1.00	60.53
4003	CA	GLU	C	11	62.709	5.114	114.127	1.00	66.82
4004	CB	GLU	C	11	63.652	5.000	112.931	1.00	64.61
4005	CG	GLU	C	11	63.118	5.565	111.627	1.00	75.77
4006	CD	GLU	C	11	64.147	5.526	110.498	1.00	80.79
4007	OE1	GLU	C	11	64.583	4.419	110.101	1.00	79.00
4008	OE2	GLU	C	11	64.529	6.611	110.004	1.00	85.25
4009	C	GLU	C	11	61.934	6.431	114.051	1.00	71.59
4010	O	GLU	C	11	62.520	7.506	114.216	1.00	74.45
4011	N	GLY	C	12	60.619	6.340	113.816	1.00	73.58
4012	CA	GLY	C	12	59.781	7.531	113.735	1.00	73.73
4013	C	GLY	C	12	59.669	8.271	115.065	1.00	73.31
4014	O	GLY	C	12	60.274	7.811	116.063	1.00	70.87
4015	OT	GLY	C	12	58.974	9.314	115.117	1.00	73.17
4016		GLY	C	12
4017	CB	ARG	D	1	46.885	−26.379	71.137	1.00	46.99
4018	CG	ARG	D	1	46.803	−25.652	69.764	1.00	48.39
4019	CD	ARG	D	1	46.249	−24.242	69.898	1.00	55.16
4020	NE	ARG	D	1	44.834	−24.129	69.566	1.00	57.32
4021	CZ	ARG	D	1	43.994	−23.298	70.171	1.00	59.78
4022	NH1	ARG	D	1	44.417	−22.515	71.155	1.00	58.58
4023	NH2	ARG	D	1	42.740	−23.226	69.759	1.00	56.99
4024	C	ARG	D	1	46.009	−25.804	73.394	1.00	52.97
4025	O	ARG	D	1	46.351	−26.313	74.496	1.00	55.64
4026	N	ARG	D	1	48.363	−25.358	72.954	1.00	43.08
4027	CA	ARG	D	1	47.013	−25.417	72.355	1.00	50.28
4028	N	HIS	D	2	44.763	−25.584	73.045	1.00	53.02
4029	CA	HIS	D	2	43.746	−25.866	73.986	1.00	47.41
4030	CB	HIS	D	2	43.273	−24.534	74.534	1.00	45.72
4031	CG	HIS	D	2	44.278	−23.864	75.434	1.00	49.31
4032	CD2	HIS	D	2	44.255	−23.654	76.776	1.00	47.68
4033	ND1	HIS	D	2	45.484	−23.349	74.995	1.00	54.30
4034	CE1	HIS	D	2	46.156	−22.857	76.026	1.00	49.22
4035	NE2	HIS	D	2	45.430	−23.032	77.120	1.00	38.45
4036	C	HIS	D	2	42.710	−26.589	73.193	1.00	48.14
4037	O	HIS	D	2	41.662	−26.036	72.884	1.00	47.23
4038	N	LYS	D	3	43.036	−27.825	72.812	1.00	46.92
4039	CA	LYS	D	3	42.103	−28.609	72.023	1.00	43.56
4040	CB	LYS	D	3	42.672	−30.006	71.775	1.00	46.80
4041	CG	LYS	D	3	43.825	−30.070	70.783	1.00	49.39
4042	CD	LYS	D	3	44.951	−30.977	71.272	1.00	60.15
4043	CE	LYS	D	3	44.485	−32.407	71.569	1.00	65.20
4044	NZ	LYS	D	3	45.623	−33.253	72.085	1.00	55.18
4045	C	LYS	D	3	40.696	−28.706	72.638	1.00	43.26
4046	O	LYS	D	3	39.721	−28.297	71.998	1.00	43.79
4047	N	ILE	D	4	40.578	−29.185	73.879	1.00	40.38
4048	CA	ILE	D	4	39.256	−29.346	74.456	1.00	39.52
4049	CB	ILE	D	4	39.312	−30.051	75.802	1.00	34.88
4050	CG2	ILE	D	4	37.906	−30.280	76.289	1.00	26.09
4051	CG1	ILE	D	4	40.057	−31.381	75.664	1.00	27.24
4052	CD1	ILE	D	4	40.402	−32.080	76.974	1.00	15.88
4053	C	ILE	D	4	38.486	−28.046	74.623	1.00	42.72
4054	O	ILE	D	4	37.365	−27.874	74.104	1.00	42.17
4055	N	LEU	D	5	39.104	−27.119	75.345	1.00	43.51
4056	CA	LEU	D	5	38.487	−25.818	75.604	1.00	41.72
4057	CB	LEU	D	5	39.492	−24.902	76.303	1.00	34.56
4058	CG	LEU	D	5	38.972	−23.526	76.646	1.00	12.80
4059	CD1	LEU	D	5	37.986	−23.667	77.770	1.00	23.18
4060	CD2	LEU	D	5	40.111	−22.651	77.080	1.00	18.96
4061	C	LEU	D	5	38.016	−25.190	74.303	1.00	41.97
4062	O	LEU	D	5	36.878	−24.766	74.163	1.00	42.53
4063	N	HIS	D	6	38.914	−25.134	73.337	1.00	46.29
4064	CA	HIS	D	6	38.587	−24.574	72.027	1.00	46.35
4065	CB	HIS	D	6	39.770	−24.777	71.085	1.00	48.78
4066	CG	HIS	D	6	39.536	−24.257	69.702	1.00	49.82
4067	CD2	HIS	D	6	40.214	−23.348	68.965	1.00	52.01
4068	ND1	HIS	D	6	38.500	−24.689	68.904	1.00	52.61
4069	CE1	HIS	D	6	38.548	−24.073	67.739	1.00	37.70
4070	NE2	HIS	D	6	39.581	−23.252	67.752	1.00	45.90
4071	C	HIS	D	6	37.369	−25.306	71.480	1.00	43.76
4072	O	HIS	D	6	36.400	−24.687	71.069	1.00	44.39
4073	N	ARG	D	7	37.449	−26.631	71.492	1.00	40.72
4074	CA	ARG	D	7	36.385	−27.490	71.019	1.00	42.50
4075	CB	ARG	D	7	36.724	−28.940	71.370	1.00	52.07
4076	CG	ARG	D	7	35.783	−29.963	70.763	1.00	60.29
4077	CD	ARG	D	7	36.198	−31.348	71.144	1.00	69.09
4078	NE	ARG	D	7	35.732	−32.356	70.195	1.00	82.74
4079	CZ	ARG	D	7	36.078	−33.641	70.259	1.00	85.02
4080	NH1	ARG	D	7	36.883	−34.044	71.232	1.00	84.76
4081	NH2	ARG	D	7	35.642	−34.516	69.345	1.00	84.04
4082	C	ARG	D	7	35.028	−27.110	71.615	1.00	41.71
4083	O	ARG	D	7	34.006	−27.079	70.917	1.00	41.93
4084	N	LEU	D	8	35.015	−26.826	72.917	1.00	40.13
4085	CA	LEU	D	8	33.780	−26.424	73.610	1.00	34.27
4086	CB	LEU	D	8	34.005	−26.284	75.111	1.00	22.98
4087	CG	LEU	D	8	34.147	−27.629	75.837	1.00	29.94
4088	CD1	LEU	D	8	34.817	−27.430	77.210	1.00	8.95
4089	CD2	LEU	D	8	32.754	−28.265	75.961	1.00	11.55
4090	C	LEU	D	8	33.263	−25.114	73.074	1.00	33.85
4091	O	LEU	D	8	32.060	−24.992	72.874	1.00	35.85
4092	N	LEU	D	9	34.163	−24.153	72.830	1.00	30.89
4093	CA	LEU	D	9	33.758	−22.867	72.308	1.00	31.74
4094	CB	LEU	D	9	34.987	−22.001	72.118	1.00	28.12
4095	CG	LEU	D	9	35.548	−21.424	73.414	1.00	28.94
4096	CD1	LEU	D	9	37.001	−20.987	73.211	1.00	30.37
4097	CD2	LEU	D	9	34.660	−20.246	73.863	1.00	24.09
4098	C	LEU	D	9	32.938	−22.970	71.013	1.00	35.76
4099	O	LEU	D	9	32.121	−22.106	70.710	1.00	31.76
4100	N	GLN	D	10	33.108	−24.049	70.265	1.00	43.66
4101	CA	GLN	D	10	32.350	−24.174	69.039	1.00	55.74
4102	CB	GLN	D	10	33.028	−25.151	68.108	1.00	53.38
4103	CG	GLN	D	10	34.255	−24.503	67.495	1.00	70.76
4104	CD	GLN	D	10	34.942	−25.365	66.456	1.00	82.40
4105	OE1	GLN	D	10	35.249	−26.535	66.706	1.00	85.25
4106	NE2	GLN	D	10	35.192	−24.791	65.282	1.00	83.74
4107	C	GLN	D	10	30.897	−24.529	69.271	1.00	63.68
4108	O	GLN	D	10	30.002	−23.797	68.811	1.00	68.67
4109	N	GLU	D	11	30.638	−25.617	69.985	1.00	67.43
4110	CA	GLU	D	11	29.249	−25.956	70.260	1.00	72.87
4111	CB	GLU	D	11	28.361	−25.659	69.036	1.00	72.17
4112	CG	GLU	D	11	28.363	−26.723	67.979	1.00	77.23
4113	CD	GLU	D	11	27.039	−26.794	67.283	1.00	77.48
4114	OE1	GLU	D	11	26.074	−26.166	67.778	1.00	82.39
4115	OE2	GLU	D	11	26.951	−27.477	66.243	1.00	84.23
4116	C	GLU	D	11	29.037	−27.402	70.720	1.00	75.56
4117	O	GLU	D	11	28.474	−28.237	69.996	1.00	78.13
4118	N	GLY	D	12	29.481	−27.709	71.933	1.00	74.76
4119	CA	GLY	D	12	29.276	−29.057	72.415	1.00	76.84
4120	C	GLY	D	12	30.267	−29.492	73.451	1.00	79.67
4121	O	GLY	D	12	31.471	−29.337	73.263	1.00	81.38
4122	N	ALA	D	13	29.748	−30.039	74.550	1.00	81.59
4123	CA	ALA	D	13	30.594	−30.530	75.638	1.00	82.83
4124	CB	ALA	D	13	29.784	−30.691	76.915	1.00	78.50
4125	C	ALA	D	13	31.237	−31.872	75.245	1.00	83.89
4126	O	ALA	D	13	30.559	−32.921	75.372	1.00	84.11
4127	OT	ALA	D	13	32.413	−31.859	74.786	1.00	85.25
4128		ALA	D	13
4129	C1	MON	E	1	62.540	2.237	92.135	1.00	23.02
4130	C2	MON	E	1	62.923	0.723	92.177	1.00	28.08
4131	C3	MON	E	1	61.083	2.417	92.743	1.00	26.18
4132	C4	MON	E	1	63.558	3.145	92.927	1.00	24.77
4133	C5	MON	E	1	61.958	−0.187	91.323	1.00	26.56
4134	C6	MON	E	1	64.314	0.292	91.658	1.00	30.49
4135	C7	MON	E	1	60.644	3.957	92.790	1.00	27.34
4136	C8	MON	E	1	60.038	1.470	92.014	1.00	19.55
4137	C9	MON	E	1	63.044	4.480	93.489	1.00	36.10
4138	C10	MON	E	1	62.683	−1.560	91.586	1.00	24.95
4139	C11	MON	E	1	60.537	−0.009	92.002	1.00	29.51
4140	C12	MON	E	1	61.841	0.186	89.786	1.00	16.20
4141	C13	MON	E	1	64.175	−1.229	91.419	1.00	18.12
4142	C14	MON	E	1	61.755	4.860	93.463	1.00	30.42
4143	C15	MON	E	1	59.373	4.137	93.699	1.00	30.42
4144	C16	MON	E	1	60.385	4.442	91.315	1.00	24.14
4145	C17	MON	E	1	62.229	−2.860	90.768	1.00	29.22
4146	C18	MON	E	1	61.404	6.156	94.244	1.00	35.00
4147	C19	MON	E	1	58.862	5.583	93.936	1.00	46.46
4148	C20	MON	E	1	62.844	−4.206	91.248	1.00	36.67
4149	C21	MON	E	1	60.689	−3.060	90.528	1.00	25.16
4150	C22	MON	E	1	59.966	6.678	94.082	1.00	52.71
4151	C23	MON	E	1	61.934	−5.259	91.890	1.00	28.32
4152	O24	MON	E	1	59.955	7.475	92.901	1.00	85.00
4153	C25	MON	E	1	62.616	−6.595	92.271	1.00	33.33
4154	C26	MON	E	1	64.049	−6.802	92.694	1.00	31.56
4155	O27	MON	E	1	62.870	−7.033	93.557	1.00	34.02
4156	C28	MON	E	1	65.035	−5.610	92.962	1.00	32.42
4157	C29	MON	E	1	64.668	−8.091	92.254	1.00	25.44
4158		MON	E	1
4159	C1	MON	F	1	33.143	−27.208	92.268	1.00	31.39
4160	C2	MON	F	1	34.685	−27.478	92.340	1.00	33.41
4161	C3	MON	F	1	32.909	−25.745	91.643	1.00	34.01
4162	C4	MON	F	1	32.368	−28.285	91.413	1.00	28.68
4163	C5	MON	F	1	35.449	−26.445	93.275	1.00	31.71
4164	C6	MON	F	1	35.179	−28.845	92.873	1.00	30.43
4165	C7	MON	F	1	31.352	−25.416	91.473	1.00	29.98
4166	C8	MON	F	1	33.719	−24.625	92.441	1.00	32.49
4167	C9	MON	F	1	31.055	−27.856	90.739	1.00	30.66
4168	C10	MON	F	1	36.887	−27.086	93.091	1.00	25.29
4169	C11	MON	F	1	35.231	−25.010	92.612	1.00	30.79
4170	C12	MON	F	1	34.930	−26.361	94.778	1.00	29.42
4171	C13	MON	F	1	36.664	−28.611	93.183	1.00	24.46
4172	C14	MON	F	1	30.589	−26.596	90.731	1.00	26.79
4173	C15	MON	F	1	31.148	−24.136	90.567	1.00	26.84
4174	C16	MON	F	1	30.744	−25.211	92.903	1.00	20.76
4175	C17	MON	F	1	38.081	−26.548	93.991	1.00	27.49
4176	C18	MON	F	1	29.330	−26.345	89.865	1.00	32.12
4177	C19	MON	F	1	29.688	−23.746	90.220	1.00	32.60
4178	C20	MON	F	1	39.496	−27.164	93.664	1.00	22.54
4179	C21	MON	F	1	38.180	−24.968	94.088	1.00	16.40
4180	C22	MON	F	1	28.700	−24.946	89.952	1.00	28.64
4181	C23	MON	F	1	40.186	−26.571	92.450	1.00	19.64
4182	O24	MON	F	1	27.766	−25.016	91.017	1.00	67.54
4183	C25	MON	F	1	41.575	−27.102	92.134	1.00	14.61
4184	C26	MON	F	1	41.899	−28.527	91.780	1.00	23.10
4185	O27	MON	F	1	42.005	−27.366	90.863	1.00	30.73
4186	C28	MON	F	1	40.778	−29.602	91.579	1.00	21.29
4187	C29	MON	F	1	43.302	−29.021	92.054	1.00	32.60
4188		MON	F	1
4189	O	HOH	W	1	28.934	−19.880	85.585	1.00	12.31
4190	O	HOH	W	2	55.303	6.531	98.855	1.00	12.91
4191	O	HOH	W	3	48.804	−3.531	102.603	1.00	16.12
4192	O	HOH	W	4	27.154	4.730	78.611	1.00	11.66
4193	O	HOH	W	5	58.488	4.566	97.443	1.00	15.31
4194	O	HOH	W	6	40.150	−3.783	102.943	1.00	16.64
4195	O	HOH	W	7	38.828	−13.399	81.631	1.00	26.36
4196	O	HOH	W	8	40.894	−5.696	85.588	1.00	23.67
4197	O	HOH	W	9	21.066	−19.167	91.749	1.00	23.16
4198	O	HOH	W	10	23.739	−13.477	73.847	1.00	27.83
4199	O	HOH	W	11	45.315	−13.580	85.785	1.00	17.40
4200	O	HOH	W	12	42.829	−3.310	82.124	1.00	13.24
4201	O	HOH	W	13	25.909	−21.766	87.993	1.00	30.21
4202	O	HOH	W	14	43.284	−12.942	99.122	1.00	34.84
4203	O	HOH	W	15	55.638	−6.539	98.489	1.00	18.17
4204	O	HOH	W	16	17.863	−15.351	90.350	1.00	35.08
4205	O	HOH	W	17	39.261	18.348	90.387	1.00	22.46
4206	O	HOH	W	18	60.616	−28.385	89.919	1.00	15.85
4207	O	HOH	W	19	61.230	9.208	103.371	1.00	16.60
4208	O	HOH	W	20	50.860	−42.107	89.699	1.00	17.48
4209	O	HOH	W	21	46.189	15.061	85.809	1.00	24.53
4210	O	HOH	W	22	52.856	8.642	98.253	1.00	36.93
4211	O	HOH	W	23	69.585	9.042	98.729	1.00	12.63
4212	O	HOH	W	24	24.849	−16.489	97.853	1.00	17.98
4213	O	HOH	W	25	16.214	−18.924	82.110	1.00	23.23
4214	O	HOH	W	26	23.966	−19.961	100.138	1.00	18.47
4215	O	HOH	W	27	30.621	2.102	77.894	1.00	26.09
4216	O	HOH	W	28	46.695	−34.723	97.299	1.00	31.88
4217	O	HOH	W	29	73.329	0.091	101.018	1.00	25.82
4218	O	HOH	W	30	57.802	11.513	84.158	1.00	28.34
4219	O	HOH	W	31	46.580	−8.461	78.008	1.00	12.33
4220	O	HOH	W	32	34.842	−5.244	107.956	1.00	31.46
4221	O	HOH	W	33	20.487	0.000	73.780	1.00	24.32
4222	O	HOH	W	34	36.203	1.678	77.127	1.00	32.71
4223	O	HOH	W	35	44.110	−31.439	104.995	1.00	33.24
4224	O	HOH	W	36	34.481	−11.772	72.134	1.00	70.97
4225	O	HOH	W	37	64.593	14.069	94.531	1.00	12.19
4226	O	HOH	W	38	40.360	0.619	76.551	1.00	23.37
4227	O	HOH	W	39	41.537	15.302	81.147	1.00	19.35
4228	O	HOH	W	40	43.053	13.888	83.764	1.00	17.50
4229	O	HOH	W	41	55.008	13.302	94.632	1.00	36.73
4230	O	HOH	W	42	48.001	−20.353	68.412	1.00	20.59
4231	O	HOH	W	43	16.865	1.283	76.436	1.00	27.34
4232	O	HOH	W	44	66.328	−9.830	75.869	1.00	18.16
4233	O	HOH	W	45	19.997	1.552	101.776	1.00	22.89
4234	O	HOH	W	46	46.772	17.189	93.223	1.00	31.59
4235	O	HOH	W	47	14.350	−13.006	73.032	1.00	41.74
4236	O	HOH	W	48	79.024	1.593	96.331	1.00	28.42
4237	O	HOH	W	49	49.770	19.140	94.124	1.00	32.22
4238	O	HOH	W	50	66.156	13.292	84.665	1.00	19.89
4239	O	HOH	W	51	51.382	−9.782	104.986	1.00	28.61
4240	O	HOH	W	52	58.197	−17.427	114.144	1.00	25.62
4241	O	HOH	W	53	55.351	14.653	106.539	1.00	38.93
4242	O	HOH	W	54	48.609	−32.570	106.727	1.00	20.34
4243	O	HOH	W	55	61.782	4.900	107.127	1.00	40.04
4244	O	HOH	W	56	74.497	−5.736	100.029	1.00	30.53
4245	O	HOH	W	57	22.456	−28.095	102.555	1.00	30.31
4246	O	HOH	W	58	20.657	−20.305	78.494	1.00	40.51
4247	O	HOH	W	59	25.060	−20.535	73.154	1.00	22.40
4248	O	HOH	W	60	53.571	−9.609	114.984	1.00	31.88
4249	O	HOH	W	61	69.559	−11.740	86.572	1.00	31.42
4250	O	HOH	W	62	51.818	2.263	74.063	1.00	29.20
4251	O	HOH	W	63	47.012	−20.795	71.045	1.00	27.78
4252	O	HOH	W	64	38.871	−10.924	69.744	1.00	35.12
4253	O	HOH	W	65	52.462	−13.956	98.987	1.00	27.92
4254	O	HOH	W	66	23.969	−22.605	99.762	1.00	32.94
4255	O	HOH	W	67	69.709	14.988	85.155	1.00	31.37
4256	O	HOH	W	68	33.026	−35.022	84.323	1.00	31.30
4257	O	HOH	W	69	16.576	−6.819	87.543	1.00	31.40
4258	O	HOH	W	70	65.039	−10.371	114.303	1.00	32.85
4259	O	HOH	W	71	22.767	−19.389	87.881	1.00	32.56
4260	O	HOH	W	72	43.815	−10.534	105.710	1.00	28.31
4261	O	HOH	W	73	45.987	13.056	105.640	1.00	31.16
4262	O	HOH	W	74	47.274	−13.091	87.837	1.00	32.00
4263	O	HOH	W	75	27.058	−15.700	98.366	1.00	32.70
4264	O	HOH	W	76	53.257	20.711	104.933	1.00	29.91
4265	O	HOH	W	77	41.043	−5.268	98.662	1.00	34.17
4266	O	HOH	W	78	44.789	−1.809	84.049	1.00	29.68
4267	O	HOH	W	79	41.310	−18.434	108.680	1.00	30.78
4268	O	HOH	W	80	38.207	11.844	105.526	1.00	32.08
4269	O	HOH	W	81	75.986	−0.830	81.601	1.00	34.96
4270	O	HOH	W	82	58.059	−18.316	88.869	1.00	33.11
4271	O	HOH	W	83	56.683	−14.479	100.385	1.00	27.89
4272	O	HOH	W	84	36.703	−25.555	86.528	1.00	36.34
4273	O	HOH	W	85	23.801	−15.167	88.443	1.00	37.39
4274	O	HOH	W	86	42.474	18.828	97.026	1.00	31.16
4275	O	HOH	W	87	48.669	−7.536	85.188	1.00	28.43
4276	O	HOH	W	88	21.591	0.859	78.322	1.00	31.94
4277	O	HOH	W	89	39.296	−33.752	80.236	1.00	30.91
4278	O	HOH	W	90	47.239	−3.382	83.812	1.00	33.55
4279	O	HOH	W	91	67.185	−20.200	93.278	1.00	38.18
4280	O	HOH	W	92	35.195	19.669	96.797	1.00	35.99
4281	O	HOH	W	93	49.803	−20.688	69.737	1.00	30.68
4282	O	HOH	W	94	64.688	−13.968	95.519	1.00	31.91
4283	O	HOH	W	95	79.308	4.287	82.277	1.00	36.78
4284	O	HOH	W	96	52.001	10.689	86.394	1.00	30.39
4285	O	HOH	W	97	62.214	9.705	94.059	1.00	31.68
4286	O	HOH	W	98	67.772	−13.671	78.429	1.00	32.38
4287	O	HOH	W	99	29.988	−3.122	102.391	1.00	35.15
4288	O	HOH	W	100	47.533	−20.550	105.577	1.00	32.36
4289	O	HOH	W	101	28.468	−35.314	99.506	1.00	31.25
4290		HOH	W	101

[0377]

TABLE 3
ATOMIC COORDINATE DATA FOR CRYSTALLIZED HUMAN LXR IN
COMPLEX WITH T317
	ATOM
ATOM	TYPE	RESIDUE	PROTEIN #	#	X	Y	Z	OCC	B
1	N	GLN	A	219	55.096	66.212	96.800	1.00	85.67
2	CA	GLN	A	219	54.529	67.185	95.712	1.00	82.61
3	CB	GLN	A	219	54.350	66.509	94.375	1.00	83.27
4	CG	GLN	A	219	54.180	67.585	93.195	1.00	85.89
5	CD	GLN	A	219	54.278	66.783	91.923	1.00	95.95
6	OE1	GLN	A	219	54.336	65.475	91.973	1.00	103.23
7	NE2	GLN	A	219	54.359	67.414	90.809	1.00	89.35
8	C	GLN	A	219	53.058	67.823	96.033	1.00	82.67
9	O	GLN	A	219	52.107	67.093	96.511	1.00	79.24
10	N	LEU	A	220	52.898	69.094	95.693	1.00	79.24
11	CA	LEU	A	220	51.820	69.917	96.065	1.00	79.91
12	CB	LEU	A	220	51.158	69.388	97.282	1.00	80.64
13	CG	LEU	A	220	49.656	69.547	97.370	1.00	84.65
14	CD1	LEU	A	220	48.849	69.361	96.088	1.00	79.69
15	CD2	LEU	A	220	49.117	68.499	98.222	1.00	77.73
16	C	LEU	A	220	52.364	71.275	96.415	1.00	78.44
17	O	LEU	A	220	52.933	71.867	95.640	1.00	79.65
18	N	THR	A	221	52.200	71.813	97.579	1.00	80.24
19	CA	THR	A	221	52.798	73.106	98.039	1.00	74.95
20	CB	THR	A	221	52.210	74.371	97.456	1.00	75.35
21	OG1	THR	A	221	50.852	74.573	97.853	1.00	71.53
22	CG2	THR	A	221	52.375	74.405	96.081	1.00	75.02
23	C	THR	A	221	52.439	73.251	99.482	1.00	73.49
24	O	THR	A	221	51.715	72.620	99.956	1.00	73.98
25	N	ALA	A	222	53.115	74.057	100.113	1.00	74.29
26	CA	ALA	A	222	53.083	74.324	101.434	1.00	73.25
27	CB	ALA	A	222	54.004	75.789	101.677	1.00	74.00
28	C	ALA	A	222	51.715	74.696	101.469	1.00	73.19
29	O	ALA	A	222	50.917	74.126	102.291	1.00	77.41
30	N	ALA	A	223	51.341	75.731	100.749	1.00	69.56
31	CA	ALA	A	223	50.011	76.343	100.979	1.00	67.22
32	CB	ALA	A	223	49.942	77.645	100.030	1.00	67.04
33	C	ALA	A	223	48.810	75.386	100.549	1.00	62.36
34	O	ALA	A	223	48.033	74.990	101.401	1.00	72.14
35	N	GLN	A	224	48.818	74.892	99.343	1.00	57.24
36	CA	GLN	A	224	47.951	73.815	99.012	1.00	54.17
37	CB	GLN	A	224	48.281	73.169	97.735	1.00	51.05
38	CG	GLN	A	224	48.294	74.054	96.470	1.00	53.95
39	CD	GLN	A	224	48.784	73.339	95.226	1.00	54.65
40	OE1	GLN	A	224	49.714	72.333	95.279	1.00	54.13
41	NE2	GLN	A	224	48.218	73.688	94.078	1.00	51.29
42	C	GLN	A	224	47.618	72.858	100.028	1.00	49.42
43	O	GLN	A	224	46.548	72.535	100.328	1.00	49.40
44	N	GLU	A	225	48.731	72.445	100.710	1.00	55.66
45	CA	GLU	A	225	48.574	71.451	101.769	1.00	55.71
46	CB	GLU	A	225	49.917	70.803	102.206	1.00	50.35
47	CG	GLU	A	225	49.846	69.389	102.481	1.00	61.55
48	CD	GLU	A	225	51.273	68.720	102.141	1.00	71.52
49	OE1	GLU	A	225	52.220	69.379	101.660	1.00	64.80
50	OE2	GLU	A	225	51.344	67.494	102.382	1.00	73.78
51	C	GLU	A	225	47.701	71.907	102.867	1.00	52.09
52	O	GLU	A	225	46.781	71.164	103.301	1.00	54.24
53	N	LEU	A	226	48.006	73.078	103.293	1.00	55.30
54	CA	LEU	A	226	47.256	73.687	104.375	1.00	63.12
55	CB	LEU	A	226	48.088	74.929	105.072	1.00	64.83
56	CG	LEU	A	226	47.422	75.271	106.441	1.00	60.16
57	CD1	LEU	A	226	48.170	74.146	107.428	1.00	71.82
58	CD2	LEU	A	226	47.731	76.481	106.932	1.00	69.43
59	C	LEU	A	226	45.854	74.173	103.963	1.00	53.65
60	O	LEU	A	226	44.871	74.165	104.661	1.00	56.35
61	N	MET	A	227	45.821	74.622	102.833	1.00	51.57
62	CA	MET	A	227	44.494	75.143	102.213	1.00	46.46
63	CB	MET	A	227	44.707	75.666	100.839	1.00	40.11
64	CG	MET	A	227	43.351	75.935	100.159	1.00	57.58
65	SD	MET	A	227	43.040	74.836	98.642	1.00	55.13
66	CE	MET	A	227	43.443	76.156	97.164	1.00	43.97
67	C	MET	A	227	43.500	73.806	102.197	1.00	46.27
68	O	MET	A	227	42.314	73.931	102.564	1.00	44.18
69	N	ILE	A	228	44.026	72.642	101.809	1.00	41.32
70	CA	ILE	A	228	43.169	71.503	101.779	1.00	46.75
71	CB	ILE	A	228	43.899	70.245	101.070	1.00	47.57
72	CG1	ILE	A	228	43.966	70.644	99.538	1.00	48.88
73	CD1	ILE	A	228	44.649	69.699	98.798	1.00	35.69
74	CG2	ILE	A	228	43.088	69.008	101.220	1.00	40.13
75	C	ILE	A	228	42.873	71.002	103.186	1.00	46.79
76	O	ILE	A	228	41.711	70.652	103.505	1.00	51.05
77	N	GLN	A	229	43.808	71.198	104.076	1.00	48.96
78	CA	GLN	A	229	43.612	70.846	105.505	1.00	48.59
79	CB	GLN	A	229	45.088	71.164	106.354	1.00	53.21
80	CG	GLN	A	229	45.941	69.894	106.483	1.00	49.89
81	CD	GLN	A	229	47.568	70.062	106.489	1.00	50.76
82	OE1	GLN	A	229	48.046	71.110	106.750	1.00	50.99
83	NE2	GLN	A	229	48.206	69.215	105.818	1.00	45.36
84	C	GLN	A	229	42.663	71.845	106.000	1.00	45.24
85	O	GLN	A	229	41.754	71.505	106.682	1.00	49.82
86	N	GLN	A	230	42.798	73.073	105.581	1.00	45.98
87	CA	GLN	A	230	41.832	74.124	105.936	1.00	47.46
88	CB	GLN	A	230	42.321	75.354	105.158	1.00	54.17
89	CG	GLN	A	230	41.872	76.768	105.720	1.00	56.74
90	CD	GLN	A	230	43.023	77.796	105.391	1.00	62.88
91	OE1	GLN	A	230	44.232	77.845	106.181	1.00	62.21
92	NE2	GLN	A	230	42.870	78.490	104.372	1.00	49.94
93	C	GLN	A	230	40.383	73.767	105.479	1.00	45.84
94	O	GLN	A	230	39.482	73.992	106.224	1.00	50.05
95	N	LEU	A	231	40.143	73.388	104.196	1.00	40.18
96	CA	LEU	A	231	38.803	73.117	103.696	1.00	36.97
97	CB	LEU	A	231	38.847	72.671	102.249	1.00	34.49
98	CG	LEU	A	231	39.003	73.787	101.287	1.00	39.49
99	CD1	LEU	A	231	39.085	73.333	99.955	1.00	32.02
100	CD2	LEU	A	231	37.892	74.819	101.569	1.00	38.12
101	C	LEU	A	231	38.331	71.856	104.456	1.00	39.71
102	O	LEU	A	231	37.235	71.863	104.897	1.00	36.04
103	N	VAL	A	232	39.238	70.801	104.575	1.00	37.04
104	CA	VAL	A	232	38.802	69.651	105.266	1.00	39.92
105	CB	VAL	A	232	39.767	68.563	105.281	1.00	41.89
106	CG1	VAL	A	232	39.460	67.424	106.242	1.00	35.24
107	CG2	VAL	A	232	39.789	67.924	103.872	1.00	34.57
108	C	VAL	A	232	38.425	69.942	106.720	1.00	40.19
109	O	VAL	A	232	37.240	69.481	107.193	1.00	37.03
110	N	ALA	A	233	39.056	70.859	107.305	1.00	39.26
111	CA	ALA	A	233	38.716	71.119	108.791	1.00	40.47
112	CB	ALA	A	233	40.043	71.949	109.543	1.00	42.60
113	C	ALA	A	233	37.408	71.881	108.792	1.00	43.83
114	O	ALA	A	233	36.576	71.750	109.707	1.00	42.76
115	N	ALA	A	234	37.222	72.791	107.913	1.00	41.01
116	CA	ALA	A	234	35.966	73.476	107.940	1.00	43.14
117	CB	ALA	A	234	35.940	74.622	106.955	1.00	36.75
118	C	ALA	A	234	34.904	72.584	107.775	1.00	43.94
119	O	ALA	A	234	33.856	72.638	108.338	1.00	46.99
120	N	GLN	A	235	35.068	71.667	106.881	1.00	47.45
121	CA	GLN	A	235	34.069	70.721	106.554	1.00	48.08
122	CB	GLN	A	235	34.546	69.825	105.467	1.00	52.03
123	CG	GLN	A	235	33.783	68.617	105.047	1.00	53.41
124	CD	GLN	A	235	34.678	67.450	104.499	1.00	52.47
125	OE1	GLN	A	235	34.652	67.038	103.328	1.00	50.48
126	NE2	GLN	A	235	35.311	66.792	105.516	1.00	54.98
127	C	GLN	A	235	33.789	69.936	107.752	1.00	53.30
128	O	GLN	A	235	32.550	69.602	107.989	1.00	55.90
129	N	LEU	A	236	34.758	69.511	108.526	1.00	50.61
130	CA	LEU	A	236	34.344	68.716	109.825	1.00	57.13
131	CB	LEU	A	236	35.603	68.079	110.441	1.00	57.67
132	CG	LEU	A	236	35.237	66.766	111.196	1.00	61.22
133	CD1	LEU	A	236	34.524	65.745	110.294	1.00	52.82
134	CD2	LEU	A	236	36.559	66.177	111.825	1.00	58.45
135	C	LEU	A	236	33.716	69.546	110.974	1.00	51.69
136	O	LEU	A	236	32.895	68.997	111.546	1.00	55.63
137	N	GLN	A	237	34.116	70.794	111.176	1.00	53.41
138	CA	GLN	A	237	33.573	71.628	112.172	1.00	58.99
139	CB	GLN	A	237	34.387	72.925	112.344	1.00	61.90
140	CG	GLN	A	237	34.237	73.820	113.590	1.00	70.99
141	CD	GLN	A	237	35.116	75.089	113.520	1.00	85.40
142	OE1	GLN	A	237	36.371	74.899	113.536	1.00	89.97
143	NE2	GLN	A	237	34.525	76.336	113.541	1.00	84.12
144	C	GLN	A	237	32.156	71.934	111.994	1.00	63.64
145	O	GLN	A	237	31.394	72.275	112.889	1.00	65.52
146	N	CYS	A	238	31.808	72.009	110.759	1.00	66.85
147	CA	CYS	A	238	30.384	72.242	110.386	1.00	70.91
148	CB	CYS	A	238	30.325	72.710	108.807	1.00	67.17
149	SG	CYS	A	238	31.327	74.207	108.665	1.00	71.62
150	C	CYS	A	238	29.541	70.943	110.485	1.00	66.87
151	O	CYS	A	238	28.518	71.003	110.575	1.00	72.18
152	N	ASN	A	239	30.100	69.844	110.273	1.00	72.55
153	CA	ASN	A	239	29.441	68.505	110.351	1.00	79.18
154	CB	ASN	A	239	30.340	67.296	109.802	1.00	77.58
155	CG	ASN	A	239	30.400	67.258	108.284	1.00	79.69
156	OD1	ASN	A	239	31.077	66.423	107.777	1.00	83.87
157	ND2	ASN	A	239	29.573	68.038	107.558	1.00	77.69
158	C	ASN	A	239	29.003	68.107	111.728	1.00	75.62
159	O	ASN	A	239	27.914	67.730	111.832	1.00	74.50
160	N	LYS	A	240	29.869	68.235	112.721	1.00	80.50
161	CA	LYS	A	240	29.464	67.794	114.144	1.00	86.13
162	CB	LYS	A	240	30.706	67.336	115.048	1.00	90.30
163	CG	LYS	A	240	30.231	66.406	116.357	1.00	94.45
164	CD	LYS	A	240	31.176	66.647	117.471	1.00	99.51
165	CE	LYS	A	240	32.269	65.606	117.395	1.00	114.82
166	NZ	LYS	A	240	32.562	65.041	115.858	1.00	114.06
167	C	LYS	A	240	28.644	68.816	114.771	1.00	85.69
168	O	LYS	A	240	27.964	68.439	115.796	1.00	89.68
169	N	ALA	A	241	28.677	70.099	114.193	1.00	87.24
170	CA	ALA	A	241	27.928	71.179	114.681	1.00	87.61
171	CB	ALA	A	241	28.294	72.335	114.124	1.00	88.25
172	C	ALA	A	241	26.500	70.745	114.193	1.00	94.00
173	O	ALA	A	241	25.570	71.490	114.394	1.00	96.99
174	N	SER	A	242	26.289	69.518	113.629	1.00	96.44
175	CA	SER	A	242	24.966	69.057	113.224	1.00	94.27
176	CB	SER	A	242	25.126	68.841	111.704	1.00	100.35
177	OG	SER	A	242	24.364	69.685	110.752	1.00	93.83
178	C	SER	A	242	24.649	67.769	113.864	1.00	93.07
179	O	SER	A	242	23.418	67.451	114.167	1.00	97.73
180	N	ALA	A	243	25.650	66.945	114.079	1.00	86.82
181	CA	ALA	A	243	25.374	65.747	114.932	1.00	86.98
182	CB	ALA	A	243	26.393	64.855	114.994	1.00	82.85
183	C	ALA	A	243	25.174	66.286	116.424	1.00	88.53
184	O	ALA	A	243	24.515	65.662	117.261	1.00	89.29
185	N	SER	A	244	25.886	67.365	116.766	1.00	87.28
186	CA	SER	A	244	25.885	67.925	118.137	1.00	87.90
187	CB	SER	A	244	27.031	68.890	118.287	1.00	84.27
188	OG	SER	A	244	28.220	68.341	117.980	1.00	83.58
189	C	SER	A	244	24.541	68.719	118.279	1.00	88.50
190	O	SER	A	244	24.130	68.910	119.279	1.00	88.97
191	N	ASP	A	245	23.948	69.122	117.150	1.00	88.90
192	CA	ASP	A	245	22.774	69.984	116.979	1.00	90.49
193	CB	ASP	A	245	22.831	71.363	116.239	1.00	86.09
194	CG	ASP	A	245	24.065	72.203	116.513	1.00	96.91
195	OD1	ASP	A	245	25.050	71.944	117.405	1.00	111.52
196	OD2	ASP	A	245	24.146	73.306	115.856	1.00	104.66
197	C	ASP	A	245	21.813	69.325	116.144	1.00	91.23
198	O	ASP	A	245	20.894	70.003	115.611	1.00	90.41
199	N	GLN	A	246	21.951	67.987	116.053	1.00	94.12
200	CA	GLN	A	246	20.851	67.266	115.352	1.00	94.06
201	CB	GLN	A	246	21.208	65.780	115.151	1.00	91.22
202	CG	GLN	A	246	19.998	65.123	114.700	1.00	87.58
203	CD	GLN	A	246	19.410	65.721	113.431	1.00	91.60
204	OE1	GLN	A	246	20.212	66.018	112.476	1.00	98.62
205	NE2	GLN	A	246	18.059	65.907	113.362	1.00	85.44
206	C	GLN	A	246	19.547	67.427	116.192	1.00	96.50
207	O	GLN	A	246	18.568	66.700	115.794	1.00	99.52
208	N	PRO	A	247	19.436	68.354	117.319	1.00	99.12
209	CA	PRO	A	247	18.094	68.308	117.993	1.00	101.73
210	CB	PRO	A	247	18.370	68.795	119.535	1.00	100.37
211	CG	PRO	A	247	19.989	69.087	119.532	1.00	96.35
212	CD	PRO	A	247	20.260	69.364	118.087	1.00	97.58
213	C	PRO	A	247	17.010	69.133	117.063	1.00	99.53
214	O	PRO	A	247	17.355	69.673	115.984	1.00	99.61
215	N	LYS	A	248	15.765	69.119	117.599	1.00	97.51
216	CA	LYS	A	248	14.676	69.814	117.113	1.00	91.20
217	CB	LYS	A	248	15.054	71.316	117.046	1.00	94.85
218	CG	LYS	A	248	16.592	71.766	116.943	1.00	97.98
219	CD	LYS	A	248	16.733	73.049	117.751	1.00	97.99
220	CE	LYS	A	248	16.110	72.909	119.070	1.00	86.59
221	NZ	LYS	A	248	17.446	72.996	119.902	1.00	101.33
222	C	LYS	A	248	14.035	69.257	115.840	1.00	85.99
223	O	LYS	A	248	13.563	70.079	115.076	1.00	87.81
224	N	VAL	A	249	13.806	67.947	115.695	1.00	78.52
225	CA	VAL	A	249	13.169	67.528	114.477	1.00	73.17
226	CB	VAL	A	249	14.142	66.871	113.498	1.00	73.37
227	CG1	VAL	A	249	14.618	65.525	114.094	1.00	79.27
228	CG2	VAL	A	249	13.499	66.651	112.317	1.00	70.29
229	C	VAL	A	249	11.941	66.663	114.641	1.00	73.94
230	O	VAL	A	249	11.781	65.828	115.543	1.00	67.47
231	N	THR	A	250	11.036	66.879	113.685	1.00	75.15
232	CA	THR	A	250	9.765	66.196	113.495	1.00	68.88
233	CB	THR	A	250	8.903	66.734	112.251	1.00	62.96
234	OG1	THR	A	250	8.354	67.933	112.477	1.00	59.52
235	CG2	THR	A	250	7.735	65.788	111.930	1.00	67.09
236	C	THR	A	250	10.091	64.666	113.423	1.00	71.32
237	O	THR	A	250	10.778	64.237	112.642	1.00	72.94
238	N	PRO	A	251	9.483	63.858	114.238	1.00	74.41
239	CA	PRO	A	251	9.750	62.512	114.198	1.00	72.78
240	CB	PRO	A	251	9.052	62.108	115.505	1.00	72.73
241	CG	PRO	A	251	8.954	63.316	116.364	1.00	69.09
242	CD	PRO	A	251	8.519	64.152	115.411	1.00	71.69
243	C	PRO	A	251	9.001	61.917	113.044	1.00	77.05
244	O	PRO	A	251	7.996	62.327	112.468	1.00	79.06
245	N	TRP	A	252	9.579	60.819	112.659	1.00	75.63
246	CA	TRP	A	252	9.071	60.047	111.528	1.00	76.35
247	CB	TRP	A	252	10.425	59.392	110.932	1.00	70.22
248	CG	TRP	A	252	10.341	58.587	109.881	1.00	55.93
249	CD1	TRP	A	252	10.066	57.235	109.857	1.00	65.14
250	NE1	TRP	A	252	10.031	56.722	108.564	1.00	61.03
251	CE2	TRP	A	252	10.278	57.810	107.707	1.00	58.03
252	CD2	TRP	A	252	10.462	58.969	108.498	1.00	54.59
253	CE3	TRP	A	252	10.596	60.178	107.878	1.00	51.44
254	CZ3	TRP	A	252	10.557	60.237	106.538	1.00	55.11
255	CH2	TRP	A	252	10.407	59.050	105.787	1.00	57.74
256	CZ2	TRP	A	252	10.237	57.844	106.405	1.00	57.19
257	C	TRP	A	252	8.133	58.878	112.057	1.00	78.02
258	O	TRP	A	252	8.477	58.241	113.199	1.00	80.22
259	N	PRO	A	253	7.117	58.530	111.261	1.00	79.55
260	CA	PRO	A	253	6.089	57.490	111.359	1.00	81.01
261	CB	PRO	A	253	5.541	57.495	109.968	1.00	77.67
262	CG	PRO	A	253	6.227	58.502	109.284	1.00	83.93
263	CD	PRO	A	253	6.718	59.510	110.314	1.00	82.51
264	C	PRO	A	253	6.428	55.966	111.829	1.00	88.29
265	O	PRO	A	253	7.520	55.359	111.483	1.00	94.15
266	N	ALA	A	254	5.573	55.304	112.625	1.00	89.95
267	CA	ALA	A	254	5.653	53.907	112.956	1.00	89.10
268	CB	ALA	A	254	4.547	53.743	113.813	1.00	92.19
269	C	ALA	A	254	5.330	53.237	111.636	1.00	92.55
270	O	ALA	A	254	5.413	51.940	111.550	1.00	89.38
271	N	GLY	A	255	4.897	54.159	110.611	1.00	93.89
272	CA	GLY	A	255	4.572	53.948	109.170	1.00	94.59
273	C	GLY	A	255	3.390	53.131	108.738	1.00	96.06
274	O	GLY	A	255	3.756	52.461	107.673	1.00	88.95
275	OXT	GLY	A	255	2.282	53.352	109.541	1.00	100.39
276	N	GLN	A	259	−0.551	53.657	105.997	1.00	100.98
277	CA	GLN	A	259	−0.692	54.510	104.638	1.00	101.82
278	CB	GLN	A	259	−1.095	53.722	103.374	1.00	103.68
279	CG	GLN	A	259	−0.017	52.868	102.666	1.00	102.32
280	CD	GLN	A	259	−0.108	51.348	102.981	1.00	109.86
281	OE1	GLN	A	259	−0.298	50.854	104.208	1.00	111.68
282	NE2	GLN	A	259	−0.018	50.545	101.859	1.00	111.42
283	C	GLN	A	259	−1.796	55.517	104.748	1.00	101.08
284	O	GLN	A	259	−2.998	55.218	104.317	1.00	102.37
285	N	SER	A	260	−1.436	56.680	105.356	1.00	97.79
286	CA	SER	A	260	−2.368	57.733	105.632	1.00	92.33
287	CB	SER	A	260	−2.273	57.895	107.119	1.00	92.61
288	OG	SER	A	260	−1.724	59.173	107.506	1.00	78.41
289	C	SER	A	260	−2.091	59.051	104.948	1.00	95.05
290	O	SER	A	260	−1.459	59.094	103.938	1.00	99.90
291	N	ARG	A	261	−2.519	60.156	105.517	1.00	94.75
292	CA	ARG	A	261	−2.360	61.518	104.997	1.00	93.13
293	CB	ARG	A	261	−3.737	62.062	104.724	1.00	94.35
294	CG	ARG	A	261	−4.900	61.003	105.277	1.00	101.94
295	CD	ARG	A	261	−6.376	61.721	105.522	1.00	101.64
296	NE	ARG	A	261	−6.597	62.608	104.359	1.00	104.47
297	CZ	ARG	A	261	−7.787	63.041	104.006	1.00	101.15
298	NH1	ARG	A	261	−8.781	62.772	104.792	1.00	102.77
299	NH2	ARG	A	261	−7.943	63.793	102.950	1.00	94.43
300	C	ARG	A	261	−1.665	62.476	105.906	1.00	90.89
301	O	ARG	A	261	−1.034	63.368	105.471	1.00	88.73
302	N	ASP	A	262	−1.868	62.289	107.191	1.00	90.00
303	CA	ASP	A	262	−1.239	63.018	108.247	1.00	87.96
304	CB	ASP	A	262	−1.906	62.624	109.569	1.00	90.25
305	CG	ASP	A	262	−1.449	63.451	110.915	1.00	98.49
306	OD1	ASP	A	262	−0.729	64.514	110.865	1.00	98.82
307	OD2	ASP	A	262	−1.884	63.091	112.109	1.00	96.43
308	C	ASP	A	262	0.289	62.562	108.232	1.00	83.28
309	O	ASP	A	262	1.166	63.340	108.472	1.00	79.22
310	N	ALA	A	263	0.501	61.324	107.911	1.00	79.80
311	CA	ALA	A	263	1.734	60.758	107.923	1.00	80.97
312	CB	ALA	A	263	1.643	59.237	107.933	1.00	80.93
313	C	ALA	A	263	2.631	61.323	106.771	1.00	82.33
314	O	ALA	A	263	3.839	61.747	107.036	1.00	78.28
315	N	ARG	A	264	1.990	61.404	105.605	1.00	81.80
316	CA	ARG	A	264	2.549	62.024	104.495	1.00	80.25
317	CB	ARG	A	264	1.761	61.997	103.248	1.00	78.27
318	CG	ARG	A	264	2.546	62.624	102.058	1.00	86.83
319	CD	ARG	A	264	2.165	62.205	100.699	1.00	85.55
320	NE	ARG	A	264	0.897	62.764	100.331	1.00	98.12
321	CZ	ARG	A	264	0.405	62.740	99.061	1.00	105.97
322	NH1	ARG	A	264	1.140	62.255	98.026	1.00	97.67
323	NH2	ARG	A	264	−0.870	63.206	98.822	1.00	112.57
324	C	ARG	A	264	3.147	63.361	104.847	1.00	81.58
325	O	ARG	A	264	4.483	63.647	104.638	1.00	83.41
326	N	GLN	A	265	2.342	64.122	105.517	1.00	79.93
327	CA	GLN	A	265	2.863	65.499	105.847	1.00	81.17
328	CB	GLN	A	265	1.635	66.454	106.366	1.00	76.97
329	CG	GLN	A	265	2.165	68.042	106.549	1.00	74.71
330	CD	GLN	A	265	2.449	68.677	105.089	1.00	84.93
331	OE1	GLN	A	265	2.513	67.904	104.022	1.00	92.74
332	NE2	GLN	A	265	2.537	69.964	104.979	1.00	82.66
333	C	GLN	A	265	4.059	65.441	106.811	1.00	73.92
334	O	GLN	A	265	4.932	66.164	106.657	1.00	70.94
335	N	GLN	A	266	3.929	64.519	107.799	1.00	73.59
336	CA	GLN	A	266	4.927	64.390	108.780	1.00	75.99
337	CB	GLN	A	266	4.713	63.205	109.660	1.00	78.43
338	CG	GLN	A	266	3.870	63.514	110.967	1.00	90.20
339	CD	GLN	A	266	3.961	62.361	111.974	1.00	95.67
340	OE1	GLN	A	266	5.119	62.116	112.694	1.00	93.72
341	NE2	GLN	A	266	2.764	61.670	112.138	1.00	85.07
342	C	GLN	A	266	6.389	64.303	108.113	1.00	72.79
343	O	GLN	A	266	7.354	64.959	108.523	1.00	68.40
344	N	ARG	A	267	6.500	63.418	107.183	1.00	71.03
345	CA	ARG	A	267	7.795	63.115	106.615	1.00	69.36
346	CB	ARG	A	267	7.878	61.736	106.087	1.00	68.79
347	CG	ARG	A	267	6.764	61.073	105.456	1.00	70.16
348	CD	ARG	A	267	6.749	59.637	105.649	1.00	68.84
349	NE	ARG	A	267	5.458	59.074	105.072	1.00	95.99
350	CZ	ARG	A	267	4.611	58.178	105.644	1.00	81.18
351	NH1	ARG	A	267	4.908	57.599	106.858	1.00	69.37
352	NH2	ARG	A	267	3.576	57.980	104.906	1.00	79.08
353	C	ARG	A	267	8.188	64.191	105.527	1.00	67.58
354	O	ARG	A	267	9.252	64.618	105.548	1.00	62.90
355	N	PHE	A	268	7.281	64.706	104.844	1.00	60.14
356	CA	PHE	A	268	7.581	65.759	104.173	1.00	57.88
357	CB	PHE	A	268	6.506	66.256	103.170	1.00	58.70
358	CG	PHE	A	268	6.780	67.668	102.543	1.00	58.81
359	CD1	PHE	A	268	6.475	68.803	103.236	1.00	55.39
360	CE1	PHE	A	268	6.467	70.043	102.736	1.00	53.30
361	CZ	PHE	A	268	7.111	70.158	101.441	1.00	62.89
362	CE2	PHE	A	268	7.479	69.081	100.800	1.00	62.35
363	CD2	PHE	A	268	7.290	67.757	101.374	1.00	58.36
364	C	PHE	A	268	8.190	66.807	104.855	1.00	57.70
365	O	PHE	A	268	9.280	67.425	104.500	1.00	58.64
366	N	ALA	A	269	7.596	67.091	105.887	1.00	56.07
367	CA	ALA	A	269	8.134	68.161	106.730	1.00	51.01
368	CB	ALA	A	269	6.867	68.463	107.890	1.00	55.80
369	C	ALA	A	269	9.366	67.877	107.323	1.00	44.97
370	O	ALA	A	269	10.056	68.732	107.752	1.00	46.96
371	N	HIS	A	270	9.506	66.632	107.587	1.00	45.75
372	CA	HIS	A	270	10.624	65.965	108.205	1.00	45.27
373	CB	HIS	A	270	10.428	64.358	108.271	1.00	39.46
374	CG	HIS	A	270	11.596	63.579	108.555	1.00	41.35
375	ND1	HIS	A	270	12.016	63.285	109.849	1.00	52.22
376	CE1	HIS	A	270	13.145	62.576	109.839	1.00	44.10
377	NE2	HIS	A	270	13.506	62.476	108.575	1.00	45.77
378	CD2	HIS	A	270	12.575	63.037	107.702	1.00	40.47
379	C	HIS	A	270	11.888	66.365	107.194	1.00	43.21
380	O	HIS	A	270	12.903	66.708	107.731	1.00	42.38
381	N	PHE	A	271	11.673	66.108	105.982	1.00	39.83
382	CA	PHE	A	271	12.588	66.267	104.971	1.00	49.60
383	CB	PHE	A	271	12.108	65.888	103.577	1.00	41.02
384	CG	PHE	A	271	12.208	64.333	103.457	1.00	45.71
385	CD1	PHE	A	271	13.357	63.618	103.931	1.00	46.76
386	CE1	PHE	A	271	13.520	62.289	103.766	1.00	45.86
387	CZ	PHE	A	271	12.552	61.512	103.235	1.00	52.48
388	CE2	PHE	A	271	11.341	62.249	102.795	1.00	53.70
389	CD2	PHE	A	271	11.333	63.686	102.941	1.00	51.87
390	C	PHE	A	271	13.106	67.901	104.921	1.00	55.37
391	O	PHE	A	271	14.338	68.174	104.794	1.00	43.89
392	N	THR	A	272	12.028	68.835	104.905	1.00	48.02
393	CA	THR	A	272	12.280	70.108	104.829	1.00	46.08
394	CB	THR	A	272	11.040	70.934	104.818	1.00	49.72
395	OG1	THR	A	272	10.377	70.754	106.059	1.00	61.56
396	CG2	THR	A	272	10.155	70.798	103.621	1.00	46.29
397	C	THR	A	272	13.104	70.535	106.046	1.00	48.09
398	O	THR	A	272	14.062	71.485	105.902	1.00	46.74
399	N	GLU	A	273	12.921	69.900	107.131	1.00	43.20
400	CA	GLU	A	273	13.665	70.298	108.300	1.00	45.93
401	CB	GLU	A	273	12.995	69.744	109.651	1.00	41.12
402	CG	GLU	A	273	11.618	70.435	109.957	1.00	51.85
403	CD	GLU	A	273	10.548	69.697	110.822	1.00	57.32
404	OE1	GLU	A	273	9.213	69.838	110.486	1.00	59.67
405	OE2	GLU	A	273	10.992	68.926	111.572	1.00	54.48
406	C	GLU	A	273	15.116	69.827	108.243	1.00	45.61
407	O	GLU	A	273	16.031	70.436	108.840	1.00	44.13
408	N	LEU	A	274	15.279	68.724	107.592	1.00	43.53
409	CA	LEU	A	274	16.710	68.181	107.376	1.00	46.73
410	CB	LEU	A	274	16.702	66.703	106.832	1.00	44.16
411	CG	LEU	A	274	16.085	65.666	107.751	1.00	47.12
412	CD1	LEU	A	274	16.213	64.321	107.207	1.00	49.05
413	CD2	LEU	A	274	16.793	65.661	109.189	1.00	53.81
414	C	LEU	A	274	17.380	69.082	106.296	1.00	37.65
415	O	LEU	A	274	18.559	69.429	106.475	1.00	40.99
416	N	ALA	A	275	16.651	69.567	105.389	1.00	36.60
417	CA	ALA	A	275	17.202	70.457	104.430	1.00	38.52
418	CB	ALA	A	275	16.224	70.659	103.268	1.00	39.37
419	C	ALA	A	275	17.691	71.778	105.001	1.00	40.85
420	O	ALA	A	275	18.752	72.357	104.671	1.00	38.61
421	N	ILE	A	276	16.877	72.342	105.919	1.00	42.17
422	CA	ILE	A	276	17.186	73.531	106.488	1.00	40.42
423	CB	ILE	A	276	15.979	73.854	107.589	1.00	44.47
424	CG1	ILE	A	276	14.852	74.498	106.855	1.00	39.46
425	CD1	ILE	A	276	13.541	74.531	107.865	1.00	41.41
426	CG2	ILE	A	276	16.526	74.936	108.670	1.00	35.38
427	C	ILE	A	276	18.506	73.478	107.236	1.00	37.69
428	O	ILE	A	276	19.269	74.309	107.080	1.00	38.14
429	N	ILE	A	277	18.699	72.477	108.088	1.00	38.21
430	CA	ILE	A	277	19.862	72.336	108.757	1.00	39.69
431	CB	ILE	A	277	19.902	71.185	109.703	1.00	39.90
432	CG1	ILE	A	277	20.708	70.218	109.290	1.00	48.55
433	CD1	ILE	A	277	22.031	70.004	110.001	1.00	41.91
434	CG2	ILE	A	277	18.381	70.692	110.105	1.00	40.45
435	C	ILE	A	277	21.048	72.223	107.854	1.00	42.32
436	O	ILE	A	277	22.135	72.732	108.134	1.00	43.22
437	N	SER	A	278	20.826	71.625	106.662	1.00	40.01
438	CA	SER	A	278	21.900	71.440	105.603	1.00	40.22
439	CB	SER	A	278	21.478	70.430	104.608	1.00	42.15
440	OG	SER	A	278	22.347	70.093	103.788	1.00	45.60
441	C	SER	A	278	22.213	72.786	104.954	1.00	39.58
442	O	SER	A	278	23.334	73.158	104.791	1.00	36.14
443	N	VAL	A	279	21.143	73.566	104.698	1.00	39.92
444	CA	VAL	A	279	21.339	74.810	104.187	1.00	38.47
445	CB	VAL	A	279	20.056	75.584	104.049	1.00	39.82
446	CG1	VAL	A	279	20.358	77.235	103.798	1.00	35.21
447	CG2	VAL	A	279	19.247	75.129	102.844	1.00	34.92
448	C	VAL	A	279	22.329	75.561	105.095	1.00	45.22
449	O	VAL	A	279	23.125	76.471	104.647	1.00	42.04
450	N	GLN	A	280	22.150	75.400	106.392	1.00	45.82
451	CA	GLN	A	280	22.964	76.151	107.344	1.00	46.04
452	CB	GLN	A	280	22.405	76.092	108.992	1.00	55.38
453	CG	GLN	A	280	21.139	76.574	109.143	1.00	62.18
454	CD	GLN	A	280	20.329	75.819	110.251	1.00	68.24
455	OE1	GLN	A	280	19.182	75.919	110.230	1.00	72.94
456	NE2	GLN	A	280	21.036	74.983	111.202	1.00	81.56
457	C	GLN	A	280	24.316	75.708	107.475	1.00	38.58
458	O	GLN	A	280	25.206	76.572	107.578	1.00	42.13
459	N	GLU	A	281	24.507	74.458	107.521	1.00	35.85
460	CA	GLU	A	281	25.926	73.894	107.421	1.00	35.48
461	CB	GLU	A	281	25.783	72.340	107.247	1.00	49.21
462	CG	GLU	A	281	27.013	71.521	107.283	1.00	46.94
463	CD	GLU	A	281	26.679	70.045	107.345	1.00	55.11
464	OE1	GLU	A	281	27.566	69.080	107.089	1.00	62.34
465	OE2	GLU	A	281	25.561	69.778	107.501	1.00	54.34
466	C	GLU	A	281	26.557	74.462	106.211	1.00	36.88
467	O	GLU	A	281	27.705	75.002	106.324	1.00	40.12
468	N	ILE	A	282	25.873	74.468	105.032	1.00	32.93
469	CA	ILE	A	282	26.483	74.937	103.824	1.00	37.10
470	CB	ILE	A	282	25.563	74.673	102.623	1.00	36.60
471	CG1	ILE	A	282	25.542	73.172	102.424	1.00	33.12
472	CD1	ILE	A	282	24.398	72.648	101.607	1.00	28.41
473	CG2	ILE	A	282	26.058	75.501	101.462	1.00	34.63
474	C	ILE	A	282	26.812	76.328	103.903	1.00	36.22
475	O	ILE	A	282	27.931	76.779	103.498	1.00	35.64
476	N	VAL	A	283	25.928	77.183	104.449	1.00	35.19
477	CA	VAL	A	283	26.314	78.657	104.550	1.00	35.61
478	CB	VAL	A	283	25.197	79.416	105.251	1.00	49.06
479	CG1	VAL	A	283	25.552	80.798	105.622	1.00	41.24
480	CG2	VAL	A	283	23.909	79.435	104.238	1.00	38.80
481	C	VAL	A	283	27.442	78.860	105.564	1.00	41.26
482	O	VAL	A	283	28.388	79.567	105.271	1.00	41.99
483	N	ASP	A	284	27.591	77.996	106.639	1.00	38.72
484	CA	ASP	A	284	28.711	78.049	107.437	1.00	38.65
485	CB	ASP	A	284	28.573	77.059	108.724	1.00	46.77
486	CG	ASP	A	284	27.750	77.687	109.857	1.00	55.54
487	OD1	ASP	A	284	27.540	78.969	109.916	1.00	60.09
488	OD2	ASP	A	284	27.147	76.899	110.567	1.00	63.52
489	C	ASP	A	284	29.957	77.605	106.801	1.00	39.66
490	O	ASP	A	284	31.004	78.247	107.049	1.00	39.55
491	N	PHE	A	285	29.933	76.487	106.050	1.00	34.06
492	CA	PHE	A	285	31.170	76.046	105.376	1.00	32.16
493	CB	PHE	A	285	30.800	74.806	104.501	1.00	32.46
494	CG	PHE	A	285	31.957	74.319	103.589	1.00	35.38
495	CD1	PHE	A	285	33.006	73.657	104.233	1.00	35.99
496	CE1	PHE	A	285	34.102	73.254	103.450	1.00	31.35
497	CZ	PHE	A	285	34.040	73.480	101.977	1.00	37.66
498	CE2	PHE	A	285	32.990	74.139	101.494	1.00	33.00
499	CD2	PHE	A	285	32.024	74.562	102.287	1.00	29.15
500	C	PHE	A	285	31.637	77.114	104.372	1.00	34.62
501	O	PHE	A	285	32.781	77.476	104.358	1.00	37.72
502	N	ALA	A	286	30.745	77.696	103.563	1.00	36.82
503	CA	ALA	A	286	31.084	78.702	102.552	1.00	36.74
504	CB	ALA	A	286	29.775	79.238	101.842	1.00	29.00
505	C	ALA	A	286	31.849	79.881	103.085	1.00	36.02
506	O	ALA	A	286	32.839	80.338	102.523	1.00	33.70
507	N	LYS	A	287	31.424	80.349	104.251	1.00	39.16
508	CA	LYS	A	287	32.048	81.465	104.851	1.00	37.96
509	CB	LYS	A	287	31.225	81.937	106.082	1.00	41.83
510	CG	LYS	A	287	29.862	82.657	105.722	1.00	45.12
511	CD	LYS	A	287	29.353	83.213	107.138	1.00	49.61
512	CE	LYS	A	287	28.172	83.922	106.877	1.00	61.11
513	NZ	LYS	A	287	27.335	84.148	108.309	1.00	63.99
514	C	LYS	A	287	33.423	81.108	105.370	1.00	42.47
515	O	LYS	A	287	34.187	81.974	105.686	1.00	43.87
516	N	GLN	A	288	33.785	79.855	105.415	1.00	37.42
517	CA	GLN	A	288	35.135	79.594	105.830	1.00	38.23
518	CB	GLN	A	288	35.120	78.300	106.750	1.00	44.53
519	CG	GLN	A	288	35.041	78.737	108.331	1.00	49.18
520	CD	GLN	A	288	34.698	77.600	109.135	1.00	64.09
521	OE1	GLN	A	288	33.359	77.135	109.051	1.00	67.22
522	NE2	GLN	A	288	35.667	76.969	109.849	1.00	52.35
523	C	GLN	A	288	36.014	79.205	104.588	1.00	41.53
524	O	GLN	A	288	37.165	78.881	104.710	1.00	37.36
525	N	VAL	A	289	35.399	79.288	103.371	1.00	37.03
526	CA	VAL	A	289	36.199	79.035	102.188	1.00	35.20
527	CB	VAL	A	289	35.351	78.477	101.018	1.00	34.98
528	CG1	VAL	A	289	36.061	78.437	99.707	1.00	27.92
529	CG2	VAL	A	289	34.811	77.046	101.400	1.00	23.48
530	C	VAL	A	289	36.982	80.255	101.840	1.00	34.92
531	O	VAL	A	289	36.453	81.265	101.702	1.00	36.02
532	N	PRO	A	290	38.322	80.172	101.764	1.00	37.23
533	CA	PRO	A	290	39.182	81.368	101.488	1.00	37.79
534	CB	PRO	A	290	40.557	80.827	101.405	1.00	33.46
535	CG	PRO	A	290	40.570	79.722	102.556	1.00	33.40
536	CD	PRO	A	290	39.192	78.974	102.164	1.00	34.43
537	C	PRO	A	290	38.794	82.090	100.251	1.00	38.43
538	O	PRO	A	290	38.684	81.423	99.169	1.00	41.81
539	N	GLY	A	291	38.546	83.337	100.306	1.00	35.20
540	CA	GLY	A	291	38.177	84.204	99.153	1.00	32.43
541	C	GLY	A	291	36.583	84.456	99.134	1.00	34.08
542	O	GLY	A	291	36.164	85.491	98.633	1.00	34.21
543	N	PHE	A	292	35.783	83.615	99.677	1.00	30.18
544	CA	PHE	A	292	34.369	83.906	99.628	1.00	32.64
545	CB	PHE	A	292	33.584	82.739	100.290	1.00	29.03
546	CG	PHE	A	292	32.075	82.790	100.082	1.00	30.95
547	CD1	PHE	A	292	31.467	82.417	98.840	1.00	29.16
548	CE1	PHE	A	292	30.172	82.389	98.678	1.00	29.51
549	CZ	PHE	A	292	29.187	82.781	99.831	1.00	29.82
550	CE2	PHE	A	292	29.833	83.315	100.964	1.00	23.75
551	CD2	PHE	A	292	31.206	83.313	101.160	1.00	26.41
552	C	PHE	A	292	33.957	85.205	100.213	1.00	36.18
553	O	PHE	A	292	32.977	85.823	99.748	1.00	37.86
554	N	LEU	A	293	34.587	85.654	101.303	1.00	41.21
555	CA	LEU	A	293	34.198	86.932	102.011	1.00	41.20
556	CB	LEU	A	293	34.586	86.881	103.397	1.00	39.17
557	CG	LEU	A	293	33.915	85.823	104.283	1.00	39.38
558	CD1	LEU	A	293	34.284	85.790	105.797	1.00	38.40
559	CD2	LEU	A	293	32.322	86.131	104.340	1.00	40.30
560	C	LEU	A	293	34.802	88.115	101.349	1.00	42.23
561	O	LEU	A	293	34.300	89.237	101.556	1.00	41.57
562	N	GLN	A	294	35.665	87.896	100.338	1.00	38.50
563	CA	GLN	A	294	36.202	89.108	99.660	1.00	38.07
564	CB	GLN	A	294	37.558	88.679	98.896	1.00	43.74
565	CG	GLN	A	294	38.741	88.503	99.899	1.00	45.87
566	CD	GLN	A	294	39.847	87.812	99.200	1.00	57.56
567	OE1	GLN	A	294	40.862	87.334	99.953	1.00	71.17
568	NE2	GLN	A	294	39.921	87.843	97.758	1.00	55.46
569	C	GLN	A	294	35.258	89.437	98.561	1.00	38.66
570	O	GLN	A	294	35.466	90.400	97.831	1.00	38.79
571	N	LEU	A	295	34.155	88.691	98.405	1.00	36.89
572	CA	LEU	A	295	33.103	89.116	97.416	1.00	31.31
573	CB	LEU	A	295	32.445	87.883	96.889	1.00	28.74
574	CG	LEU	A	295	33.323	87.020	95.927	1.00	29.80
575	CD1	LEU	A	295	32.637	85.475	95.793	1.00	25.37
576	CD2	LEU	A	295	33.453	87.750	94.464	1.00	22.18
577	C	LEU	A	295	32.165	89.985	98.121	1.00	30.65
578	O	LEU	A	295	31.913	89.837	99.395	1.00	30.96
579	N	GLY	A	296	31.419	90.721	97.364	1.00	33.64
580	CA	GLY	A	296	30.282	91.558	97.960	1.00	34.26
581	C	GLY	A	296	29.253	90.658	98.472	1.00	38.96
582	O	GLY	A	296	29.183	89.442	98.088	1.00	33.27
583	N	ARG	A	297	28.330	91.197	99.373	1.00	36.07
584	CA	ARG	A	297	27.400	90.404	99.968	1.00	31.87
585	CB	ARG	A	297	26.541	91.369	100.901	1.00	41.49
586	CG	ARG	A	297	25.152	90.646	101.517	1.00	42.67
587	CD	ARG	A	297	24.353	91.552	102.368	1.00	57.56
588	NE	ARG	A	297	22.938	91.051	102.888	1.00	57.97
589	CZ	ARG	A	297	22.911	89.948	103.622	1.00	60.51
590	NH1	ARG	A	297	24.123	89.340	103.925	1.00	56.84
591	NH2	ARG	A	297	21.759	89.300	103.920	1.00	51.82
592	C	ARG	A	297	26.495	89.884	98.843	1.00	31.57
593	O	ARG	A	297	25.980	88.825	98.896	1.00	32.83
594	N	GLU	A	298	26.102	90.797	97.920	1.00	34.95
595	CA	GLU	A	298	25.254	90.424	96.907	1.00	31.54
596	CB	GLU	A	298	25.098	91.508	95.814	1.00	36.90
597	CG	GLU	A	298	24.397	92.795	96.272	1.00	49.73
598	CD	GLU	A	298	25.378	93.783	97.000	1.00	47.92
599	OE1	GLU	A	298	26.530	93.382	97.482	1.00	41.29
600	OE2	GLU	A	298	24.864	94.893	97.235	1.00	51.31
601	C	GLU	A	298	25.800	89.071	96.190	1.00	27.71
602	O	GLU	A	298	25.030	88.123	96.026	1.00	24.56
603	N	ASP	A	299	26.978	89.108	95.749	1.00	27.21
604	CA	ASP	A	299	27.557	87.886	95.122	1.00	29.51
605	CB	ASP	A	299	28.912	88.174	94.507	1.00	27.66
606	CG	ASP	A	299	28.756	88.835	93.084	1.00	27.40
607	OD1	ASP	A	299	27.657	89.010	92.621	1.00	25.56
608	OD2	ASP	A	299	29.783	89.143	92.441	1.00	30.55
609	C	ASP	A	299	27.588	86.627	96.040	1.00	29.89
610	O	ASP	A	299	27.284	85.521	95.579	1.00	32.13
611	N	GLN	A	300	27.798	86.770	97.355	1.00	28.64
612	CA	GLN	A	300	27.835	85.720	98.203	1.00	32.43
613	CB	GLN	A	300	28.239	86.128	99.711	1.00	28.61
614	CG	GLN	A	300	29.593	86.674	99.827	1.00	32.36
615	CD	GLN	A	300	29.871	87.335	101.248	1.00	32.93
616	OE1	GLN	A	300	30.740	88.124	101.345	1.00	35.53
617	NE2	GLN	A	300	29.140	87.059	102.102	1.00	29.24
618	C	GLN	A	300	26.507	85.010	98.138	1.00	30.55
619	O	GLN	A	300	26.410	83.784	98.174	1.00	27.91
620	N	ILE	A	301	25.542	85.840	98.143	1.00	32.70
621	CA	ILE	A	301	24.073	85.277	98.165	1.00	31.27
622	CB	ILE	A	301	23.059	86.481	98.415	1.00	33.15
623	CG1	ILE	A	301	23.331	86.954	99.914	1.00	35.57
624	CD1	ILE	A	301	22.305	88.193	100.298	1.00	30.35
625	CG2	ILE	A	301	21.623	86.044	98.089	1.00	28.70
626	C	ILE	A	301	23.748	84.676	96.805	1.00	28.75
627	O	ILE	A	301	23.161	83.620	96.848	1.00	30.67
628	N	ALA	A	302	24.133	85.241	95.747	1.00	23.83
629	CA	ALA	A	302	23.746	84.638	94.490	1.00	30.56
630	CB	ALA	A	302	24.220	85.673	93.221	1.00	25.06
631	C	ALA	A	302	24.536	83.249	94.217	1.00	28.16
632	O	ALA	A	302	23.947	82.343	93.852	1.00	27.71
633	N	LEU	A	303	25.829	83.164	94.593	1.00	29.86
634	CA	LEU	A	303	26.527	81.954	94.511	1.00	31.92
635	CB	LEU	A	303	28.070	82.240	94.976	1.00	29.58
636	CG	LEU	A	303	28.750	83.153	93.983	1.00	31.40
637	CD1	LEU	A	303	30.229	83.203	94.524	1.00	31.82
638	CD2	LEU	A	303	28.685	82.579	92.531	1.00	24.33
639	C	LEU	A	303	26.019	80.903	95.445	1.00	30.24
640	O	LEU	A	303	25.844	79.752	95.063	1.00	33.92
641	N	LEU	A	304	25.633	81.290	96.655	1.00	31.43
642	CA	LEU	A	304	25.029	80.237	97.609	1.00	33.42
643	CB	LEU	A	304	24.984	80.782	98.962	1.00	29.58
644	CG	LEU	A	304	26.099	80.188	99.959	1.00	41.99
645	CD1	LEU	A	304	25.744	78.928	100.571	1.00	43.21
646	CD2	LEU	A	304	27.365	79.965	99.309	1.00	38.21
647	C	LEU	A	304	23.677	79.796	97.146	1.00	32.19
648	O	LEU	A	304	23.272	78.625	97.289	1.00	28.76
649	N	LYS	A	305	22.929	80.761	96.577	1.00	28.77
650	CA	LYS	A	305	21.523	80.408	96.180	1.00	29.45
651	CB	LYS	A	305	20.926	81.642	95.604	1.00	37.48
652	CG	LYS	A	305	19.491	81.504	95.045	1.00	42.80
653	CD	LYS	A	305	18.626	82.867	95.605	1.00	46.29
654	CE	LYS	A	305	17.714	83.286	94.535	1.00	47.99
655	NZ	LYS	A	305	16.658	82.418	94.316	1.00	47.49
656	C	LYS	A	305	21.578	79.366	94.968	1.00	29.76
657	O	LYS	A	305	20.765	78.372	94.990	1.00	29.63
658	N	ALA	A	306	22.456	79.535	94.094	1.00	24.49
659	CA	ALA	A	306	22.503	78.638	92.981	1.00	26.72
660	CB	ALA	A	306	23.216	79.225	91.740	1.00	17.94
661	C	ALA	A	306	23.301	77.341	93.404	1.00	27.93
662	O	ALA	A	306	22.931	76.218	92.857	1.00	28.47
663	N	SER	A	307	24.185	77.424	94.325	1.00	21.05
664	CA	SER	A	307	24.864	76.085	94.550	1.00	26.49
665	CB	SER	A	307	26.459	76.352	94.716	1.00	31.86
666	OG	SER	A	307	26.747	77.116	95.765	1.00	32.86
667	C	SER	A	307	24.442	75.252	95.719	1.00	26.76
668	O	SER	A	307	24.789	74.091	95.779	1.00	25.81
669	N	THR	A	308	23.483	75.743	96.543	1.00	26.28
670	CA	THR	A	308	23.022	75.056	97.654	1.00	27.51
671	CB	THR	A	308	21.941	75.893	98.398	1.00	27.16
672	OG1	THR	A	308	22.578	76.918	99.064	1.00	29.21
673	CG2	THR	A	308	21.261	74.912	99.449	1.00	17.76
674	C	THR	A	308	22.485	73.614	97.354	1.00	27.46
675	O	THR	A	308	22.802	72.648	98.066	1.00	24.75
676	N	ILE	A	309	21.545	73.538	96.378	1.00	26.93
677	CA	ILE	A	309	21.043	72.203	96.043	1.00	23.04
678	CB	ILE	A	309	19.812	72.359	94.990	1.00	26.72
679	CG1	ILE	A	309	19.084	70.966	94.795	1.00	23.33
680	CD1	ILE	A	309	18.514	70.435	96.105	1.00	23.17
681	CG2	ILE	A	309	20.331	72.855	93.642	1.00	21.02
682	C	ILE	A	309	22.120	71.257	95.486	1.00	23.12
683	O	ILE	A	309	22.134	70.091	95.714	1.00	26.33
684	N	GLU	A	310	23.059	71.822	94.742	1.00	27.82
685	CA	GLU	A	310	24.208	71.093	94.160	1.00	22.59
686	CB	GLU	A	310	24.850	72.012	93.127	1.00	25.76
687	CG	GLU	A	310	23.984	72.351	91.953	1.00	26.34
688	CD	GLU	A	310	24.749	73.174	90.841	1.00	31.59
689	OE1	GLU	A	310	25.997	73.129	90.798	1.00	21.67
690	OE2	GLU	A	310	24.134	73.847	89.993	1.00	33.55
691	C	GLU	A	310	25.192	70.623	95.160	1.00	22.68
692	O	GLU	A	310	25.596	69.488	95.185	1.00	24.16
693	N	ILE	A	311	25.417	71.433	96.209	1.00	24.92
694	CA	ILE	A	311	26.276	70.946	97.306	1.00	24.59
695	CB	ILE	A	311	26.671	72.144	98.161	1.00	27.83
696	CG1	ILE	A	311	27.596	73.082	97.376	1.00	27.28
697	CD1	ILE	A	311	28.166	74.243	98.165	1.00	28.66
698	CG2	ILE	A	311	27.445	71.689	99.477	1.00	24.31
699	C	ILE	A	311	25.603	69.910	98.096	1.00	26.73
700	O	ILE	A	311	26.163	68.877	98.518	1.00	25.76
701	N	MET	A	312	24.243	70.038	98.334	1.00	26.95
702	CA	MET	A	312	23.519	69.100	99.078	1.00	28.20
703	CB	MET	A	312	21.963	69.530	99.265	1.00	32.65
704	CG	MET	A	312	21.777	70.545	100.262	1.00	31.50
705	SD	MET	A	312	20.124	71.390	99.991	1.00	36.03
706	CE	MET	A	312	19.206	70.423	100.744	1.00	36.52
707	C	MET	A	312	23.544	67.684	98.337	1.00	25.43
708	O	MET	A	312	23.566	66.654	98.953	1.00	25.55
709	N	LEU	A	313	23.526	67.789	97.024	1.00	21.81
710	CA	LEU	A	313	23.605	66.542	96.263	1.00	21.12
711	CB	LEU	A	313	23.324	66.877	94.882	1.00	23.38
712	CG	LEU	A	313	21.760	67.105	94.603	1.00	25.11
713	CD1	LEU	A	313	21.567	67.910	93.299	1.00	19.37
714	CD2	LEU	A	313	21.209	65.754	94.499	1.00	27.49
715	C	LEU	A	313	25.053	65.882	96.420	1.00	20.35
716	O	LEU	A	313	25.151	64.736	96.646	1.00	19.92
717	N	LEU	A	314	26.069	66.745	96.347	1.00	24.80
718	CA	LEU	A	314	27.484	66.236	96.553	1.00	29.84
719	CB	LEU	A	314	28.457	67.428	96.397	1.00	24.30
720	CG	LEU	A	314	28.701	67.669	94.866	1.00	24.45
721	CD1	LEU	A	314	29.562	69.031	94.743	1.00	29.60
722	CD2	LEU	A	314	29.585	66.500	94.195	1.00	25.08
723	C	LEU	A	314	27.630	65.642	98.007	1.00	26.91
724	O	LEU	A	314	28.079	64.566	98.118	1.00	27.48
725	N	GLU	A	315	27.002	66.300	99.021	1.00	27.94
726	CA	GLU	A	315	27.090	65.741	100.410	1.00	27.46
727	CB	GLU	A	315	26.703	66.772	101.475	1.00	27.00
728	CG	GLU	A	315	27.660	67.838	101.618	1.00	35.38
729	CD	GLU	A	315	28.831	67.348	102.496	1.00	39.57
730	OE1	GLU	A	315	28.643	66.362	103.285	1.00	41.14
731	OE2	GLU	A	315	29.801	67.943	102.451	1.00	47.59
732	C	GLU	A	315	26.197	64.509	100.542	1.00	27.37
733	O	GLU	A	315	26.440	63.633	101.216	1.00	26.90
734	N	THR	A	316	25.111	64.467	99.789	1.00	29.35
735	CA	THR	A	316	24.282	63.248	99.855	1.00	25.85
736	CB	THR	A	316	22.955	63.569	98.999	1.00	25.11
737	OG1	THR	A	316	22.209	64.367	99.778	1.00	24.63
738	CG2	THR	A	316	22.277	62.300	98.644	1.00	30.27
739	C	THR	A	316	25.018	62.075	99.152	1.00	23.34
740	O	THR	A	316	25.182	61.015	99.749	1.00	25.72
741	N	ALA	A	317	25.713	62.346	97.969	1.00	21.51
742	CA	ALA	A	317	26.541	61.304	97.400	1.00	22.63
743	CB	ALA	A	317	27.287	61.849	96.075	1.00	21.57
744	C	ALA	A	317	27.720	60.896	98.383	1.00	26.32
745	O	ALA	A	317	27.894	59.724	98.569	1.00	26.21
746	N	ARG	A	318	28.285	61.849	99.070	1.00	24.26
747	CA	ARG	A	318	29.334	61.518	99.942	1.00	30.43
748	CB	ARG	A	318	30.036	62.850	100.434	1.00	28.78
749	CG	ARG	A	318	31.222	62.420	101.411	1.00	29.03
750	CD	ARG	A	318	31.994	63.794	101.741	1.00	35.38
751	NE	ARG	A	318	31.277	64.625	102.652	1.00	35.32
752	CZ	ARG	A	318	31.590	64.852	103.821	1.00	40.22
753	NH1	ARG	A	318	32.773	64.250	104.443	1.00	42.05
754	NH2	ARG	A	318	30.874	65.745	104.607	1.00	35.76
755	C	ARG	A	318	28.952	60.655	101.238	1.00	28.90
756	O	ARG	A	318	29.701	59.862	101.681	1.00	27.55
757	N	ARG	A	319	27.819	60.885	101.784	1.00	31.21
758	CA	ARG	A	319	27.401	60.142	102.999	1.00	27.42
759	CB	ARG	A	319	26.595	61.181	103.854	1.00	32.16
760	CG	ARG	A	319	27.289	62.317	104.256	1.00	37.82
761	CD	ARG	A	319	26.295	63.143	105.099	1.00	49.91
762	NE	ARG	A	319	26.949	64.323	105.979	1.00	59.32
763	CZ	ARG	A	319	27.151	65.577	105.576	1.00	60.21
764	NH1	ARG	A	319	26.781	66.044	104.383	1.00	63.33
765	NH2	ARG	A	319	27.618	66.510	106.498	1.00	67.19
766	C	ARG	A	319	26.450	58.968	102.592	1.00	28.30
767	O	ARG	A	319	25.897	58.308	103.478	1.00	31.01
768	N	TYR	A	320	26.148	58.776	101.300	1.00	26.84
769	CA	TYR	A	320	25.385	57.621	100.880	1.00	25.78
770	CB	TYR	A	320	25.175	57.653	99.428	1.00	24.29
771	CG	TYR	A	320	24.229	56.664	98.812	1.00	25.21
772	CD1	TYR	A	320	24.639	55.378	98.426	1.00	20.61
773	CE1	TYR	A	320	23.790	54.407	97.720	1.00	25.95
774	CZ	TYR	A	320	22.248	54.829	97.649	1.00	32.66
775	OH	TYR	A	320	21.501	53.957	97.050	1.00	24.66
776	CE2	TYR	A	320	21.862	56.053	97.976	1.00	21.62
777	CD2	TYR	A	320	22.843	57.025	98.602	1.00	26.81
778	C	TYR	A	320	25.805	56.288	101.364	1.00	26.52
779	O	TYR	A	320	26.968	55.930	101.180	1.00	28.23
780	N	ASN	A	321	24.941	55.500	101.837	1.00	25.11
781	CA	ASN	A	321	25.334	54.099	102.302	1.00	28.42
782	CB	ASN	A	321	24.383	53.766	103.482	1.00	28.30
783	CG	ASN	A	321	24.836	52.413	104.120	1.00	31.95
784	OD1	ASN	A	321	25.389	51.540	103.415	1.00	31.12
785	ND2	ASN	A	321	24.416	52.201	105.316	1.00	35.12
786	C	ASN	A	321	25.158	53.118	101.168	1.00	26.49
787	O	ASN	A	321	23.975	52.749	100.848	1.00	27.67
788	N	HIS	A	322	26.169	52.696	100.586	1.00	25.24
789	CA	HIS	A	322	26.128	51.761	99.497	1.00	27.12
790	CB	HIS	A	322	27.525	51.852	98.665	1.00	27.16
791	CG	HIS	A	322	27.558	53.165	97.858	1.00	29.49
792	ND1	HIS	A	322	28.192	54.312	98.266	1.00	31.90
793	CE1	HIS	A	322	28.037	55.289	97.434	1.00	26.71
794	NE2	HIS	A	322	27.244	54.797	96.472	1.00	32.75
795	CD2	HIS	A	322	26.937	53.461	96.704	1.00	26.25
796	C	HIS	A	322	26.004	50.314	99.969	1.00	31.64
797	O	HIS	A	322	25.774	49.416	99.115	1.00	32.39
798	N	GLU	A	323	26.013	50.052	101.259	1.00	27.45
799	CA	GLU	A	323	25.622	48.676	101.716	1.00	28.04
800	CB	GLU	A	323	26.154	48.463	103.239	1.00	30.66
801	CG	GLU	A	323	27.813	48.469	103.350	1.00	32.86
802	CD	GLU	A	323	28.260	48.311	104.726	1.00	37.39
803	OE1	GLU	A	323	27.438	48.232	105.689	1.00	37.69
804	OE2	GLU	A	323	29.409	48.392	104.899	1.00	40.31
805	C	GLU	A	323	24.244	48.515	101.810	1.00	30.19
806	O	GLU	A	323	23.667	47.456	101.420	1.00	31.86
807	N	THR	A	324	23.486	49.571	102.143	1.00	32.78
808	CA	THR	A	324	22.051	49.464	102.260	1.00	29.67
809	CB	THR	A	324	21.460	50.155	103.526	1.00	33.02
810	OG1	THR	A	324	21.978	51.535	103.648	1.00	34.94
811	CG2	THR	A	324	21.911	49.410	104.845	1.00	27.84
812	C	THR	A	324	21.376	50.117	101.095	1.00	34.32
813	O	THR	A	324	20.207	49.942	100.844	1.00	32.06
814	N	GLU	A	325	22.216	50.925	100.336	1.00	32.96
815	CA	GLU	A	325	21.551	51.720	99.197	1.00	30.82
816	CB	GLU	A	325	20.864	50.794	98.278	1.00	34.24
817	CG	GLU	A	325	21.772	49.654	97.698	1.00	40.03
818	CD	GLU	A	325	21.176	49.062	96.382	1.00	31.22
819	OE1	GLU	A	325	21.435	49.641	95.380	1.00	32.46
820	OE2	GLU	A	325	20.444	48.024	96.426	1.00	36.90
821	C	GLU	A	325	20.538	52.695	99.759	1.00	29.33
822	O	GLU	A	325	19.437	52.847	99.261	1.00	28.96
823	N	CYS	A	326	20.966	53.414	100.806	1.00	28.37
824	CA	CYS	A	326	20.204	54.402	101.402	1.00	33.99
825	CB	CYS	A	326	19.736	54.058	102.905	1.00	30.63
826	SG	CYS	A	326	18.387	52.785	102.879	1.00	37.75
827	C	CYS	A	326	20.850	55.806	101.400	1.00	33.40
828	O	CYS	A	326	22.066	55.910	101.595	1.00	29.29
829	N	ILE	A	327	20.013	56.857	101.324	1.00	30.10
830	CA	ILE	A	327	20.479	58.168	101.551	1.00	31.08
831	CB	ILE	A	327	19.648	59.263	100.922	1.00	35.00
832	CG1	ILE	A	327	19.922	59.335	99.456	1.00	32.21
833	CD1	ILE	A	327	18.984	60.151	98.568	1.00	38.04
834	CG2	ILE	A	327	19.824	60.608	101.766	1.00	24.53
835	C	ILE	A	327	20.560	58.271	103.081	1.00	37.38
836	O	ILE	A	327	19.615	57.873	103.805	1.00	31.19
837	N	THR	A	328	21.698	58.782	103.646	1.00	34.91
838	CA	THR	A	328	21.649	58.850	105.022	1.00	38.61
839	CB	THR	A	328	22.849	57.874	105.657	1.00	42.84
840	OG1	THR	A	328	24.111	58.423	105.337	1.00	47.71
841	CG2	THR	A	328	22.794	56.504	105.135	1.00	36.12
842	C	THR	A	328	22.028	60.302	105.495	1.00	45.59
843	O	THR	A	328	22.867	60.868	104.936	1.00	47.31
844	N	PHE	A	329	21.320	60.862	106.490	1.00	45.91
845	CA	PHE	A	329	21.630	62.013	107.122	1.00	48.86
846	CB	PHE	A	329	20.374	62.537	107.626	1.00	54.49
847	CG	PHE	A	329	20.375	64.083	107.850	1.00	57.05
848	CD1	PHE	A	329	20.773	64.668	109.142	1.00	58.41
849	CE1	PHE	A	329	20.836	65.959	109.330	1.00	53.09
850	CZ	PHE	A	329	20.472	66.792	108.224	1.00	58.19
851	CE2	PHE	A	329	20.006	66.295	107.089	1.00	59.51
852	CD2	PHE	A	329	20.038	64.861	106.864	1.00	59.08
853	C	PHE	A	329	22.544	61.989	108.310	1.00	56.52
854	O	PHE	A	329	23.478	62.853	108.405	1.00	55.51
855	N	LEU	A	330	22.599	60.870	109.145	1.00	60.17
856	CA	LEU	A	330	23.569	60.696	110.259	1.00	60.42
857	CB	LEU	A	330	22.931	61.142	111.628	1.00	65.77
858	CG	LEU	A	330	22.352	62.480	111.953	1.00	69.35
859	CD1	LEU	A	330	21.234	62.451	113.038	1.00	58.83
860	CD2	LEU	A	330	23.379	63.514	112.265	1.00	68.98
861	C	LEU	A	330	23.585	59.283	110.547	1.00	65.60
862	O	LEU	A	330	23.434	58.522	109.643	1.00	74.89
863	N	LYS	A	331	23.914	58.782	111.766	1.00	67.54
864	CA	LYS	A	331	24.161	57.267	112.064	1.00	65.86
865	CB	LYS	A	331	24.425	56.954	113.509	1.00	65.68
866	CG	LYS	A	331	24.386	55.393	113.819	1.00	65.19
867	CD	LYS	A	331	25.843	54.758	113.844	1.00	71.83
868	CE	LYS	A	331	25.926	53.704	112.636	1.00	75.49
869	NZ	LYS	A	331	27.122	52.694	112.810	1.00	69.11
870	C	LYS	A	331	22.844	56.568	111.679	1.00	68.90
871	O	LYS	A	331	22.655	55.556	110.771	1.00	73.86
872	N	ASP	A	332	21.791	57.094	112.183	1.00	65.17
873	CA	ASP	A	332	20.632	56.645	111.561	1.00	60.60
874	CB	ASP	A	332	19.713	56.336	112.511	1.00	69.63
875	CG	ASP	A	332	18.518	56.016	111.882	1.00	75.01
876	OD1	ASP	A	332	18.294	54.751	111.433	1.00	71.44
877	OD2	ASP	A	332	17.661	57.004	111.855	1.00	81.67
878	C	ASP	A	332	20.115	57.971	110.877	1.00	62.41
879	O	ASP	A	332	21.027	58.937	110.472	1.00	59.25
880	N	PHE	A	333	18.885	57.972	110.615	1.00	55.78
881	CA	PHE	A	333	18.411	59.028	109.692	1.00	53.49
882	CB	PHE	A	333	18.841	60.348	110.084	1.00	53.02
883	CG	PHE	A	333	18.261	60.740	111.480	1.00	65.51
884	CD1	PHE	A	333	16.924	61.279	111.645	1.00	60.74
885	CE1	PHE	A	333	16.361	61.547	112.836	1.00	64.61
886	CZ	PHE	A	333	17.014	61.292	114.094	1.00	63.64
887	CE2	PHE	A	333	18.384	60.674	113.944	1.00	66.77
888	CD2	PHE	A	333	18.945	60.322	112.619	1.00	60.92
889	C	PHE	A	333	18.817	58.523	108.320	1.00	50.37
890	O	PHE	A	333	19.720	59.126	107.757	1.00	53.42
891	N	THR	A	334	18.260	57.449	107.859	1.00	44.86
892	CA	THR	A	334	18.637	56.862	106.598	1.00	50.38
893	CB	THR	A	334	19.446	55.608	106.621	1.00	40.77
894	OG1	THR	A	334	18.592	54.729	107.063	1.00	49.86
895	CG2	THR	A	334	20.279	55.736	107.619	1.00	45.74
896	C	THR	A	334	17.326	56.680	105.822	1.00	45.06
897	O	THR	A	334	16.483	56.488	106.505	1.00	42.68
898	N	TYR	A	335	17.296	56.814	104.413	1.00	38.65
899	CA	TYR	A	335	16.190	56.725	103.734	1.00	34.67
900	CB	TYR	A	335	15.626	58.253	103.429	1.00	35.54
901	CG	TYR	A	335	15.684	59.043	104.542	1.00	36.77
902	CD1	TYR	A	335	14.552	58.964	105.658	1.00	44.72
903	CE1	TYR	A	335	14.500	59.789	106.758	1.00	36.72
904	CZ	TYR	A	335	15.590	60.509	107.070	1.00	38.85
905	OH	TYR	A	335	15.901	61.059	108.257	1.00	43.46
906	CE2	TYR	A	335	16.823	60.402	106.209	1.00	48.91
907	CD2	TYR	A	335	16.763	59.725	104.854	1.00	38.14
908	C	TYR	A	335	16.345	56.075	102.417	1.00	37.64
909	O	TYR	A	335	17.182	56.316	101.689	1.00	36.38
910	N	SER	A	336	15.301	55.219	102.027	1.00	39.92
911	CA	SER	A	336	15.232	54.471	100.786	1.00	36.88
912	CB	SER	A	336	14.536	53.093	101.117	1.00	35.99
913	OG	SER	A	336	13.154	53.432	101.130	1.00	42.46
914	C	SER	A	336	14.454	55.251	99.867	1.00	33.88
915	O	SER	A	336	13.945	56.283	100.248	1.00	37.82
916	N	LYS	A	337	14.434	54.855	98.650	1.00	41.15
917	CA	LYS	A	337	13.616	55.428	97.582	1.00	41.23
918	CB	LYS	A	337	13.529	54.657	96.356	1.00	36.95
919	CG	LYS	A	337	15.009	54.557	95.596	1.00	45.49
920	CD	LYS	A	337	14.894	54.356	94.258	1.00	41.74
921	CE	LYS	A	337	16.307	54.149	93.449	1.00	34.02
922	NZ	LYS	A	337	16.044	54.036	92.021	1.00	36.78
923	C	LYS	A	337	12.189	55.459	98.093	1.00	48.52
924	O	LYS	A	337	11.417	56.559	98.072	1.00	45.96
925	N	ASP	A	338	11.775	54.388	98.698	1.00	47.64
926	CA	ASP	A	338	10.467	54.351	99.250	1.00	46.38
927	CB	ASP	A	338	10.281	52.998	99.993	1.00	53.22
928	CG	ASP	A	338	8.789	52.612	100.012	1.00	64.06
929	OD1	ASP	A	338	8.167	52.411	98.833	1.00	64.38
930	OD2	ASP	A	338	8.237	52.624	101.173	1.00	66.10
931	C	ASP	A	338	10.083	55.401	100.113	1.00	46.94
932	O	ASP	A	338	8.913	55.975	99.972	1.00	45.82
933	N	ASP	A	339	10.932	55.731	101.049	1.00	47.85
934	CA	ASP	A	339	10.713	56.747	101.948	1.00	47.16
935	CB	ASP	A	339	11.729	56.874	103.045	1.00	49.83
936	CG	ASP	A	339	11.845	55.620	103.954	1.00	60.04
937	OD1	ASP	A	339	10.791	55.173	104.487	1.00	53.48
938	OD2	ASP	A	339	13.021	55.140	104.230	1.00	52.58
939	C	ASP	A	339	10.476	58.146	101.295	1.00	53.26
940	O	ASP	A	339	9.605	58.969	101.768	1.00	55.83
941	N	PHE	A	340	11.191	58.416	100.275	1.00	54.63
942	CA	PHE	A	340	11.047	59.664	99.572	1.00	55.04
943	CB	PHE	A	340	12.235	59.822	98.583	1.00	48.17
944	CG	PHE	A	340	13.503	60.320	99.262	1.00	43.47
945	CD1	PHE	A	340	13.622	61.684	99.643	1.00	46.40
946	CE1	PHE	A	340	14.746	62.234	100.336	1.00	37.14
947	CZ	PHE	A	340	15.703	61.253	100.757	1.00	43.67
948	CE2	PHE	A	340	15.586	59.964	100.282	1.00	40.75
949	CD2	PHE	A	340	14.458	59.505	99.639	1.00	39.97
950	C	PHE	A	340	9.683	59.640	98.977	1.00	57.44
951	O	PHE	A	340	9.039	60.788	98.918	1.00	60.00
952	N	ALA	A	341	9.364	58.561	98.326	1.00	52.40
953	CA	ALA	A	341	8.080	58.384	97.615	1.00	58.89
954	CB	ALA	A	341	8.005	56.891	97.006	1.00	58.65
955	C	ALA	A	341	6.931	58.616	98.619	1.00	60.38
956	O	ALA	A	341	6.067	59.406	98.483	1.00	60.21
957	N	ARG	A	342	7.087	58.039	99.749	1.00	63.11
958	CA	ARG	A	342	6.030	58.242	100.768	1.00	64.22
959	CB	ARG	A	342	6.255	57.371	101.965	1.00	61.32
960	CG	ARG	A	342	5.973	55.945	102.077	1.00	62.09
961	CD	ARG	A	342	6.818	55.614	103.454	1.00	75.15
962	NE	ARG	A	342	6.826	54.231	103.990	1.00	81.85
963	CZ	ARG	A	342	7.986	53.453	103.861	1.00	90.20
964	NH1	ARG	A	342	9.079	53.917	103.227	1.00	76.80
965	NH2	ARG	A	342	8.054	52.196	104.362	1.00	94.52
966	C	ARG	A	342	5.874	59.675	101.260	1.00	65.87
967	O	ARG	A	342	4.717	60.059	101.953	1.00	60.63
968	N	ALA	A	343	6.872	60.483	100.965	1.00	60.17
969	CA	ALA	A	343	6.584	61.826	101.407	1.00	57.27
970	CB	ALA	A	343	7.909	62.466	101.859	1.00	57.16
971	C	ALA	A	343	5.916	62.603	100.352	1.00	56.52
972	O	ALA	A	343	5.756	63.831	100.516	1.00	62.82
973	N	GLY	A	344	5.628	62.014	99.187	1.00	57.55
974	CA	GLY	A	344	4.963	62.749	98.095	1.00	57.86
975	C	GLY	A	344	5.934	63.355	97.042	1.00	65.75
976	O	GLY	A	344	5.547	64.325	96.335	1.00	66.13
977	N	LEU	A	345	7.154	62.667	96.692	1.00	62.47
978	CA	LEU	A	345	7.996	63.147	95.694	1.00	55.91
979	CB	LEU	A	345	9.295	63.261	96.392	1.00	61.92
980	CG	LEU	A	345	9.344	63.843	97.823	1.00	68.77
981	CD1	LEU	A	345	10.803	63.704	98.515	1.00	68.43
982	CD2	LEU	A	345	8.863	65.212	97.921	1.00	59.11
983	C	LEU	A	345	7.999	62.433	94.515	1.00	49.37
984	O	LEU	A	345	7.821	61.282	94.442	1.00	53.23
985	N	GLN	A	346	8.221	63.061	93.411	1.00	53.41
986	CA	GLN	A	346	8.260	62.430	92.052	1.00	55.12
987	CB	GLN	A	346	8.620	63.542	90.955	1.00	61.52
988	CG	GLN	A	346	7.597	64.461	90.620	1.00	71.32
989	CD	GLN	A	346	8.231	65.855	89.889	1.00	69.01
990	OE1	GLN	A	346	9.433	66.147	89.952	1.00	71.20
991	NE2	GLN	A	346	7.411	66.614	89.181	1.00	81.10
992	C	GLN	A	346	9.301	61.292	92.036	1.00	55.12
993	O	GLN	A	346	10.375	61.517	92.703	1.00	55.52
994	N	VAL	A	347	9.097	60.428	91.127	1.00	54.09
995	CA	VAL	A	347	10.096	59.503	90.928	1.00	58.16
996	CB	VAL	A	347	9.468	58.181	90.310	1.00	58.60
997	CG1	VAL	A	347	9.789	58.039	88.819	1.00	61.76
998	CG2	VAL	A	347	9.978	57.044	91.036	1.00	60.39
999	C	VAL	A	347	11.131	60.187	90.012	1.00	55.68
1000	O	VAL	A	347	12.265	59.797	89.921	1.00	49.89
1001	N	GLU	A	348	10.736	61.178	89.370	1.00	52.48
1002	CA	GLU	A	348	11.492	61.768	88.390	1.00	49.37
1003	CB	GLU	A	348	10.663	62.783	87.401	1.00	49.65
1004	CG	GLU	A	348	8.990	62.445	87.511	1.00	63.05
1005	CD	GLU	A	348	8.496	61.453	86.590	1.00	70.49
1006	OE1	GLU	A	348	8.720	60.141	86.764	1.00	81.28
1007	OE2	GLU	A	348	7.971	61.742	85.393	1.00	83.18
1008	C	GLU	A	348	12.614	62.639	89.157	1.00	48.56
1009	O	GLU	A	348	13.661	63.034	88.442	1.00	46.22
1010	N	PHE	A	349	12.458	62.792	90.386	1.00	41.51
1011	CA	PHE	A	349	13.435	63.585	91.173	1.00	42.56
1012	CB	PHE	A	349	12.722	64.383	92.160	1.00	35.26
1013	CG	PHE	A	349	13.570	64.980	93.173	1.00	38.81
1014	CD1	PHE	A	349	14.670	65.775	92.802	1.00	36.08
1015	CE1	PHE	A	349	15.522	66.444	93.729	1.00	31.95
1016	CZ	PHE	A	349	15.393	66.088	95.047	1.00	37.40
1017	CE2	PHE	A	349	14.315	65.302	95.471	1.00	38.65
1018	CD2	PHE	A	349	13.371	64.784	94.510	1.00	37.78
1019	C	PHE	A	349	14.222	62.503	92.001	1.00	40.40
1020	O	PHE	A	349	15.470	62.477	91.940	1.00	40.17
1021	N	ILE	A	350	13.471	61.555	92.632	1.00	39.12
1022	CA	ILE	A	350	14.005	60.622	93.405	1.00	43.56
1023	CB	ILE	A	350	12.895	59.747	93.968	1.00	44.06
1024	CG1	ILE	A	350	12.078	60.539	94.821	1.00	42.70
1025	CD1	ILE	A	350	10.586	59.645	95.281	1.00	38.43
1026	CG2	ILE	A	350	13.427	58.485	94.759	1.00	29.85
1027	C	ILE	A	350	15.130	59.579	92.719	1.00	38.73
1028	O	ILE	A	350	16.126	59.294	93.270	1.00	36.16
1029	N	ASN	A	351	14.715	59.060	91.562	1.00	33.28
1030	CA	ASN	A	351	15.622	58.280	90.866	1.00	37.86
1031	CB	ASN	A	351	15.056	57.716	89.573	1.00	33.38
1032	CG	ASN	A	351	14.137	56.437	89.867	1.00	42.08
1033	OD1	ASN	A	351	14.375	55.739	90.755	1.00	42.74
1034	ND2	ASN	A	351	13.142	56.144	88.889	1.00	40.71
1035	C	ASN	A	351	16.949	58.876	90.592	1.00	40.02
1036	O	ASN	A	351	17.994	58.406	90.937	1.00	36.40
1037	N	PRO	A	352	16.914	60.098	90.039	1.00	39.55
1038	CA	PRO	A	352	18.128	60.755	89.704	1.00	38.11
1039	CB	PRO	A	352	17.756	61.978	88.896	1.00	36.01
1040	CG	PRO	A	352	16.469	61.625	88.308	1.00	43.28
1041	CD	PRO	A	352	15.720	60.797	89.589	1.00	37.85
1042	C	PRO	A	352	19.082	61.164	90.906	1.00	32.74
1043	O	PRO	A	352	20.306	60.952	90.779	1.00	30.16
1044	N	ILE	A	353	18.538	61.191	92.104	1.00	31.77
1045	CA	ILE	A	353	19.448	61.624	93.177	1.00	32.21
1046	CB	ILE	A	353	18.830	62.379	94.299	1.00	34.16
1047	CG1	ILE	A	353	17.761	61.547	95.059	1.00	28.49
1048	CD1	ILE	A	353	17.200	62.312	96.280	1.00	25.50
1049	CG2	ILE	A	353	18.223	63.880	93.727	1.00	40.63
1050	C	ILE	A	353	20.110	60.396	93.634	1.00	35.07
1051	O	ILE	A	353	21.247	60.453	94.107	1.00	33.62
1052	N	PHE	A	354	19.363	59.302	93.704	1.00	33.04
1053	CA	PHE	A	354	19.973	57.995	94.111	1.00	37.01
1054	CB	PHE	A	354	18.983	56.887	94.218	1.00	33.54
1055	CG	PHE	A	354	18.282	56.918	95.538	1.00	34.07
1056	CD1	PHE	A	354	17.298	57.826	95.769	1.00	29.36
1057	CE1	PHE	A	354	16.642	57.859	97.051	1.00	32.83
1058	CZ	PHE	A	354	17.082	56.950	98.051	1.00	35.19
1059	CE2	PHE	A	354	18.010	56.095	97.810	1.00	36.74
1060	CD2	PHE	A	354	18.653	56.011	96.491	1.00	34.92
1061	C	PHE	A	354	21.034	57.537	92.983	1.00	36.17
1062	O	PHE	A	354	22.079	57.025	93.330	1.00	38.46
1063	N	GLU	A	355	20.729	57.777	91.739	1.00	32.99
1064	CA	GLU	A	355	21.603	57.570	90.635	1.00	31.95
1065	CB	GLU	A	355	20.849	57.683	89.349	1.00	30.61
1066	CG	GLU	A	355	21.238	56.779	88.200	1.00	45.49
1067	CD	GLU	A	355	21.419	55.196	88.539	1.00	48.90
1068	OE1	GLU	A	355	20.531	54.439	89.257	1.00	44.46
1069	OE2	GLU	A	355	22.571	54.858	88.301	1.00	47.34
1070	C	GLU	A	355	22.846	58.352	90.660	1.00	29.03
1071	O	GLU	A	355	23.939	57.950	90.316	1.00	34.92
1072	N	PHE	A	356	22.700	59.587	91.085	1.00	29.34
1073	CA	PHE	A	356	23.879	60.438	91.159	1.00	28.44
1074	CB	PHE	A	356	23.511	62.025	91.372	1.00	24.84
1075	CG	PHE	A	356	24.666	62.810	91.513	1.00	26.82
1076	CD1	PHE	A	356	25.398	63.241	90.389	1.00	20.56
1077	CE1	PHE	A	356	26.417	64.033	90.504	1.00	22.91
1078	CZ	PHE	A	356	26.735	64.591	91.746	1.00	22.03
1079	CE2	PHE	A	356	26.001	64.229	92.833	1.00	24.05
1080	CD2	PHE	A	356	24.978	63.331	92.731	1.00	21.52
1081	C	PHE	A	356	24.779	59.836	92.315	1.00	24.60
1082	O	PHE	A	356	25.987	59.838	92.144	1.00	26.66
1083	N	SER	A	357	24.215	59.596	93.391	1.00	20.88
1084	CA	SER	A	357	25.002	59.033	94.542	1.00	26.21
1085	CB	SER	A	357	24.087	58.603	95.676	1.00	26.96
1086	OG	SER	A	357	23.475	59.777	96.266	1.00	35.03
1087	C	SER	A	357	25.747	57.742	94.006	1.00	27.43
1088	O	SER	A	357	26.969	57.600	94.360	1.00	26.40
1089	N	ARG	A	358	25.134	56.946	93.210	1.00	22.54
1090	CA	ARG	A	358	25.793	55.760	92.607	1.00	28.46
1091	CB	ARG	A	358	24.843	54.824	91.803	1.00	27.12
1092	CG	ARG	A	358	23.697	54.269	92.620	1.00	31.43
1093	CD	ARG	A	358	22.934	53.389	91.651	1.00	33.88
1094	NE	ARG	A	358	23.872	52.537	91.013	1.00	43.04
1095	CZ	ARG	A	358	23.589	51.618	89.966	1.00	46.48
1096	NH1	ARG	A	358	22.381	51.806	89.350	1.00	41.56
1097	NH2	ARG	A	358	24.554	50.764	89.510	1.00	38.99
1098	C	ARG	A	358	26.993	56.041	91.707	1.00	25.01
1099	O	ARG	A	358	28.092	55.610	91.893	1.00	29.34
1100	N	ALA	A	359	26.747	56.925	90.736	1.00	27.15
1101	CA	ALA	A	359	27.774	57.289	89.826	1.00	25.84
1102	CB	ALA	A	359	27.068	58.411	88.707	1.00	29.99
1103	C	ALA	A	359	28.951	58.049	90.486	1.00	28.51
1104	O	ALA	A	359	30.109	57.815	90.086	1.00	33.57
1105	N	MET	A	360	28.681	58.972	91.463	1.00	24.05
1106	CA	MET	A	360	29.724	59.525	92.232	1.00	27.60
1107	CB	MET	A	360	29.160	60.535	93.321	1.00	23.55
1108	CG	MET	A	360	28.826	62.038	92.888	1.00	21.34
1109	SD	MET	A	360	29.972	62.957	91.915	1.00	30.06
1110	CE	MET	A	360	31.260	63.327	93.225	1.00	27.47
1111	C	MET	A	360	30.659	58.521	92.938	1.00	26.47
1112	O	MET	A	360	31.912	58.707	92.962	1.00	24.69
1113	N	ARG	A	361	30.082	57.533	93.516	1.00	25.42
1114	CA	ARG	A	361	30.820	56.539	94.212	1.00	27.69
1115	CB	ARG	A	361	29.893	55.416	94.765	1.00	25.52
1116	CG	ARG	A	361	30.639	54.373	95.441	1.00	26.92
1117	CD	ARG	A	361	31.653	54.932	96.590	1.00	30.50
1118	NE	ARG	A	361	32.360	53.943	97.240	1.00	30.09
1119	CZ	ARG	A	361	33.541	53.386	96.823	1.00	34.94
1120	NH1	ARG	A	361	34.182	53.879	95.769	1.00	27.55
1121	NH2	ARG	A	361	34.015	52.393	97.463	1.00	31.71
1122	C	ARG	A	361	31.817	55.821	93.244	1.00	29.95
1123	O	ARG	A	361	32.842	55.424	93.659	1.00	32.18
1124	N	ARG	A	362	31.499	55.806	91.915	1.00	29.17
1125	CA	ARG	A	362	32.382	55.116	90.952	1.00	32.80
1126	CB	ARG	A	362	31.749	55.079	89.592	1.00	35.25
1127	CG	ARG	A	362	30.773	53.820	89.351	1.00	44.57
1128	CD	ARG	A	362	29.771	53.880	88.402	1.00	41.11
1129	NE	ARG	A	362	30.318	54.533	87.230	1.00	62.15
1130	CZ	ARG	A	362	31.219	53.932	86.299	1.00	56.43
1131	NH1	ARG	A	362	31.790	52.909	86.664	1.00	76.32
1132	NH2	ARG	A	362	31.752	54.433	85.291	1.00	58.84
1133	C	ARG	A	362	33.715	55.888	90.842	1.00	38.96
1134	O	ARG	A	362	34.742	55.280	90.453	1.00	34.44
1135	N	LEU	A	363	33.711	57.213	91.173	1.00	35.42
1136	CA	LEU	A	363	34.936	57.932	91.121	1.00	33.23
1137	CB	LEU	A	363	34.569	59.348	90.917	1.00	31.74
1138	CG	LEU	A	363	33.942	59.767	89.493	1.00	42.89
1139	CD1	LEU	A	363	33.687	61.239	89.400	1.00	41.37
1140	CD2	LEU	A	363	34.696	59.249	88.506	1.00	40.65
1141	C	LEU	A	363	35.862	57.697	92.410	1.00	36.34
1142	O	LEU	A	363	36.930	58.187	92.423	1.00	35.01
1143	N	GLY	A	364	35.343	57.163	93.426	1.00	32.97
1144	CA	GLY	A	364	36.041	56.985	94.595	1.00	30.77
1145	C	GLY	A	364	36.681	58.169	95.246	1.00	35.17
1146	O	GLY	A	364	37.993	58.033	95.528	1.00	33.06
1147	N	LEU	A	365	36.021	59.279	95.390	1.00	29.40
1148	CA	LEU	A	365	36.470	60.445	95.940	1.00	34.74
1149	CB	LEU	A	365	35.574	61.723	95.760	1.00	29.56
1150	CG	LEU	A	365	34.993	62.073	94.350	1.00	33.44
1151	CD1	LEU	A	365	34.585	63.514	94.294	1.00	34.57
1152	CD2	LEU	A	365	35.587	61.702	93.139	1.00	32.84
1153	C	LEU	A	365	36.716	60.411	97.557	1.00	35.27
1154	O	LEU	A	365	35.915	59.695	98.275	1.00	33.84
1155	N	ASP	A	366	37.723	61.044	98.025	1.00	29.59
1156	CA	ASP	A	366	37.895	61.028	99.465	1.00	31.14
1157	CB	ASP	A	366	39.394	60.887	99.824	1.00	29.81
1158	CG	ASP	A	366	40.289	61.840	99.143	1.00	31.81
1159	OD1	ASP	A	366	39.942	63.003	98.946	1.00	34.95
1160	OD2	ASP	A	366	41.394	61.408	98.737	1.00	39.23
1161	C	ASP	A	366	37.358	62.467	100.009	1.00	31.45
1162	O	ASP	A	366	36.950	63.298	99.266	1.00	27.08
1163	N	ASP	A	367	37.498	62.663	101.256	1.00	31.37
1164	CA	ASP	A	367	37.091	63.904	101.782	1.00	36.61
1165	CB	ASP	A	367	37.230	63.889	103.412	1.00	40.07
1166	CG	ASP	A	367	36.149	62.886	104.022	1.00	46.21
1167	OD1	ASP	A	367	34.975	62.558	103.286	1.00	42.09
1168	OD2	ASP	A	367	36.222	62.655	105.136	1.00	52.17
1169	C	ASP	A	367	37.681	65.205	101.248	1.00	35.74
1170	O	ASP	A	367	36.913	66.240	101.072	1.00	33.99
1171	N	ALA	A	368	38.844	65.150	100.887	1.00	29.92
1172	CA	ALA	A	368	39.457	66.373	100.299	1.00	30.49
1173	CB	ALA	A	368	41.098	66.112	100.092	1.00	26.50
1174	C	ALA	A	368	38.911	66.620	98.895	1.00	32.62
1175	O	ALA	A	368	38.829	67.801	98.523	1.00	36.37
1176	N	GLU	A	369	38.770	65.587	98.066	1.00	24.31
1177	CA	GLU	A	369	38.356	65.818	96.845	1.00	29.00
1178	CB	GLU	A	369	38.425	64.483	95.952	1.00	22.95
1179	CG	GLU	A	369	39.908	64.031	95.886	1.00	28.00
1180	CD	GLU	A	369	40.112	62.683	95.405	1.00	29.14
1181	OE1	GLU	A	369	39.312	61.777	95.939	1.00	27.96
1182	OE2	GLU	A	369	40.793	62.490	94.321	1.00	27.55
1183	C	GLU	A	369	36.897	66.411	96.735	1.00	28.40
1184	O	GLU	A	369	36.669	67.335	95.974	1.00	27.58
1185	N	TYR	A	370	36.018	65.878	97.623	1.00	27.68
1186	CA	TYR	A	370	34.700	66.410	97.861	1.00	25.95
1187	CB	TYR	A	370	33.971	65.677	98.870	1.00	27.29
1188	CG	TYR	A	370	33.067	64.500	98.317	1.00	30.67
1189	CD1	TYR	A	370	33.375	63.179	98.520	1.00	29.65
1190	CE1	TYR	A	370	32.559	62.169	98.044	1.00	24.96
1191	CZ	TYR	A	370	31.358	62.562	97.199	1.00	31.04
1192	OH	TYR	A	370	30.639	61.580	96.641	1.00	25.30
1193	CE2	TYR	A	370	31.100	63.796	96.963	1.00	22.48
1194	CD2	TYR	A	370	31.962	64.824	97.561	1.00	31.26
1195	C	TYR	A	370	34.743	67.837	98.315	1.00	28.81
1196	O	TYR	A	370	34.090	68.730	97.663	1.00	30.56
1197	N	ALA	A	371	35.610	68.180	99.251	1.00	27.51
1198	CA	ALA	A	371	35.671	69.536	99.783	1.00	22.07
1199	CB	ALA	A	371	36.645	69.600	101.022	1.00	26.40
1200	C	ALA	A	371	36.273	70.472	98.666	1.00	26.62
1201	O	ALA	A	371	35.793	71.530	98.503	1.00	27.10
1202	N	LEU	A	372	37.245	70.024	97.843	1.00	21.94
1203	CA	LEU	A	372	37.671	70.868	96.843	1.00	22.33
1204	CB	LEU	A	372	38.927	70.434	96.173	1.00	24.56
1205	CG	LEU	A	372	40.214	70.640	97.005	1.00	33.14
1206	CD1	LEU	A	372	41.364	69.613	96.489	1.00	25.37
1207	CD2	LEU	A	372	40.639	72.052	96.915	1.00	28.88
1208	C	LEU	A	372	36.621	71.088	95.683	1.00	22.60
1209	O	LEU	A	372	36.419	72.148	95.215	1.00	21.21
1210	N	LEU	A	373	35.964	69.974	95.242	1.00	25.15
1211	CA	LEU	A	373	34.993	70.043	94.214	1.00	22.32
1212	CB	LEU	A	373	34.404	68.597	94.110	1.00	21.91
1213	CG	LEU	A	373	33.494	68.425	92.811	1.00	25.88
1214	CD1	LEU	A	373	34.350	68.939	91.548	1.00	22.43
1215	CD2	LEU	A	373	33.089	66.945	92.660	1.00	18.83
1216	C	LEU	A	373	33.799	70.997	94.727	1.00	22.27
1217	O	LEU	A	373	33.235	71.741	93.878	1.00	22.92
1218	N	ILE	A	374	33.486	70.947	95.954	1.00	23.24
1219	CA	ILE	A	374	32.401	72.000	96.536	1.00	26.23
1220	CB	ILE	A	374	32.027	71.571	97.978	1.00	26.40
1221	CG1	ILE	A	374	31.146	70.312	97.822	1.00	19.31
1222	CD1	ILE	A	374	31.024	69.456	99.267	1.00	21.34
1223	CG2	ILE	A	374	31.340	72.723	98.789	1.00	27.79
1224	C	ILE	A	374	32.924	73.408	96.489	1.00	25.86
1225	O	ILE	A	374	32.181	74.311	96.098	1.00	27.87
1226	N	ALA	A	375	34.227	73.650	96.815	1.00	24.08
1227	CA	ALA	A	375	34.790	75.051	96.714	1.00	25.33
1228	CB	ALA	A	375	36.278	75.151	97.234	1.00	31.90
1229	C	ALA	A	375	34.794	75.528	95.206	1.00	23.98
1230	O	ALA	A	375	34.462	76.633	94.933	1.00	26.40
1231	N	ILE	A	376	35.055	74.599	94.329	1.00	27.12
1232	CA	ILE	A	376	35.034	74.829	92.899	1.00	25.21
1233	CB	ILE	A	376	35.526	73.697	92.149	1.00	19.17
1234	CG1	ILE	A	376	37.047	73.693	92.273	1.00	28.94
1235	CD1	ILE	A	376	37.715	72.219	91.735	1.00	18.49
1236	CG2	ILE	A	376	35.124	73.887	90.612	1.00	21.17
1237	C	ILE	A	376	33.591	75.176	92.431	1.00	26.62
1238	O	ILE	A	376	33.341	76.138	91.676	1.00	25.78
1239	N	ASN	A	377	32.665	74.415	92.956	1.00	26.58
1240	CA	ASN	A	377	31.236	74.589	92.619	1.00	27.26
1241	CB	ASN	A	377	30.414	73.465	93.392	1.00	32.12
1242	CG	ASN	A	377	28.883	73.492	93.003	1.00	33.33
1243	OD1	ASN	A	377	28.115	74.333	93.591	1.00	34.73
1244	ND2	ASN	A	377	28.480	72.681	92.131	1.00	31.41
1245	C	ASN	A	377	30.749	75.997	93.101	1.00	26.39
1246	O	ASN	A	377	30.098	76.708	92.346	1.00	24.60
1247	N	ILE	A	378	31.087	76.406	94.348	1.00	25.57
1248	CA	ILE	A	378	30.656	77.638	94.826	1.00	24.33
1249	CB	ILE	A	378	31.257	77.879	96.311	1.00	30.38
1250	CG1	ILE	A	378	30.527	76.965	97.227	1.00	30.50
1251	CD1	ILE	A	378	31.339	76.651	98.576	1.00	18.81
1252	CG2	ILE	A	378	31.030	79.308	96.813	1.00	19.50
1253	C	ILE	A	378	31.144	78.792	93.969	1.00	25.80
1254	O	ILE	A	378	30.444	79.712	93.676	1.00	27.73
1255	N	PHE	A	379	32.372	78.795	93.503	1.00	27.64
1256	CA	PHE	A	379	32.922	79.862	92.687	1.00	24.14
1257	CB	PHE	A	379	34.452	80.154	93.022	1.00	22.61
1258	CG	PHE	A	379	34.733	80.516	94.437	1.00	24.59
1259	CD1	PHE	A	379	34.273	81.719	94.913	1.00	27.74
1260	CE1	PHE	A	379	34.674	82.266	96.127	1.00	33.61
1261	CZ	PHE	A	379	35.416	81.502	97.013	1.00	29.32
1262	CE2	PHE	A	379	35.768	80.196	96.544	1.00	30.76
1263	CD2	PHE	A	379	35.392	79.736	95.228	1.00	24.69
1264	C	PHE	A	379	32.696	79.763	91.182	1.00	30.53
1265	O	PHE	A	379	33.645	79.821	90.410	1.00	29.13
1266	N	SER	A	380	31.440	79.546	90.773	1.00	30.11
1267	CA	SER	A	380	31.049	79.544	89.382	1.00	28.70
1268	CB	SER	A	380	29.817	78.524	89.220	1.00	26.20
1269	OG	SER	A	380	30.267	77.214	89.815	1.00	25.22
1270	C	SER	A	380	30.583	80.844	88.829	1.00	25.94
1271	O	SER	A	380	29.671	81.382	89.306	1.00	27.86
1272	N	ALA	A	381	31.276	81.388	87.882	1.00	27.25
1273	CA	ALA	A	381	31.065	82.762	87.437	1.00	30.70
1274	CB	ALA	A	381	32.327	83.282	86.583	1.00	21.62
1275	C	ALA	A	381	29.755	82.911	86.622	1.00	32.31
1276	O	ALA	A	381	29.283	84.100	86.469	1.00	32.72
1277	N	ASP	A	382	29.169	81.863	86.171	1.00	29.52
1278	CA	ASP	A	382	27.968	81.981	85.348	1.00	30.16
1279	CB	ASP	A	382	28.024	80.802	84.249	1.00	33.90
1280	CG	ASP	A	382	27.902	79.417	84.934	1.00	41.16
1281	OD1	ASP	A	382	28.184	79.312	86.135	1.00	40.14
1282	OD2	ASP	A	382	27.449	78.515	84.394	1.00	50.33
1283	C	ASP	A	382	26.714	81.896	86.071	1.00	29.28
1284	O	ASP	A	382	25.666	81.833	85.479	1.00	30.47
1285	N	ARG	A	383	26.719	81.890	87.432	1.00	30.38
1286	CA	ARG	A	383	25.421	81.865	88.150	1.00	29.60
1287	CB	ARG	A	383	25.524	81.737	89.590	1.00	26.12
1288	CG	ARG	A	383	26.503	80.600	90.063	1.00	28.61
1289	CD	ARG	A	383	25.857	79.207	89.766	1.00	26.30
1290	NE	ARG	A	383	26.510	78.102	90.525	1.00	31.33
1291	CZ	ARG	A	383	26.154	76.823	90.516	1.00	32.37
1292	NH1	ARG	A	383	25.111	76.412	89.784	1.00	26.78
1293	NH2	ARG	A	383	26.843	76.032	91.264	1.00	30.05
1294	C	ARG	A	383	24.545	83.243	87.784	1.00	33.32
1295	O	ARG	A	383	25.139	84.301	87.551	1.00	38.00
1296	N	PRO	A	384	23.294	83.186	87.907	1.00	30.73
1297	CA	PRO	A	384	22.488	84.282	87.761	1.00	30.65
1298	CB	PRO	A	384	21.029	83.750	88.222	1.00	33.93
1299	CG	PRO	A	384	21.138	82.298	87.555	1.00	30.48
1300	CD	PRO	A	384	22.567	81.850	88.240	1.00	32.19
1301	C	PRO	A	384	22.735	85.434	88.723	1.00	28.49
1302	O	PRO	A	384	23.039	85.198	89.860	1.00	30.52
1303	N	ASN	A	385	22.779	86.627	88.247	1.00	33.92
1304	CA	ASN	A	385	22.909	87.850	88.864	1.00	28.88
1305	CB	ASN	A	385	21.950	87.815	89.956	1.00	39.11
1306	CG	ASN	A	385	20.556	87.667	89.404	1.00	45.66
1307	OD1	ASN	A	385	19.776	86.886	90.011	1.00	44.67
1308	ND2	ASN	A	385	20.231	88.327	88.320	1.00	37.49
1309	C	ASN	A	385	24.411	88.135	89.371	1.00	33.73
1310	O	ASN	A	385	24.598	89.183	90.049	1.00	36.83
1311	N	VAL	A	386	25.417	87.246	89.132	1.00	26.72
1312	CA	VAL	A	386	26.673	87.449	89.532	1.00	29.80
1313	CB	VAL	A	386	27.690	86.465	88.936	1.00	26.67
1314	CG1	VAL	A	386	29.086	86.871	89.073	1.00	29.15
1315	CG2	VAL	A	386	27.466	84.936	89.650	1.00	39.65
1316	C	VAL	A	386	27.173	88.968	89.082	1.00	29.38
1317	O	VAL	A	386	27.190	89.302	87.942	1.00	32.09
1318	N	GLN	A	387	27.603	89.705	90.002	1.00	28.15
1319	CA	GLN	A	387	28.024	91.166	89.544	1.00	30.91
1320	CB	GLN	A	387	27.797	92.077	90.694	1.00	31.43
1321	CG	GLN	A	387	26.434	92.007	91.257	1.00	27.96
1322	CD	GLN	A	387	26.370	93.075	92.471	1.00	34.77
1323	OE1	GLN	A	387	25.322	93.682	92.727	1.00	32.52
1324	NE2	GLN	A	387	27.419	93.109	93.204	1.00	27.17
1325	C	GLN	A	387	29.469	91.191	89.214	1.00	31.99
1326	O	GLN	A	387	29.869	91.925	88.354	1.00	31.63
1327	N	GLU	A	388	30.334	90.266	89.823	1.00	28.55
1328	CA	GLU	A	388	31.784	90.396	89.447	1.00	31.48
1329	CB	GLU	A	388	32.600	90.761	90.704	1.00	33.38
1330	CG	GLU	A	388	32.164	92.086	91.443	1.00	32.95
1331	CD	GLU	A	388	33.246	92.400	92.462	1.00	45.13
1332	OE1	GLU	A	388	33.032	92.341	93.664	1.00	37.45
1333	OE2	GLU	A	388	34.381	92.855	91.996	1.00	35.97
1334	C	GLU	A	388	32.227	88.922	88.985	1.00	31.66
1335	O	GLU	A	388	32.992	88.226	89.633	1.00	28.69
1336	N	PRO	A	389	31.764	88.550	87.802	1.00	31.67
1337	CA	PRO	A	389	32.119	87.193	87.288	1.00	33.14
1338	CB	PRO	A	389	31.345	87.202	85.757	1.00	31.36
1339	CG	PRO	A	389	31.401	88.824	85.428	1.00	30.48
1340	CD	PRO	A	389	31.011	89.459	86.763	1.00	27.05
1341	C	PRO	A	389	33.524	87.002	87.130	1.00	33.73
1342	O	PRO	A	389	33.989	85.937	87.387	1.00	34.71
1343	N	GLY	A	390	34.285	88.056	86.575	1.00	31.65
1344	CA	GLY	A	390	35.709	87.791	86.469	1.00	31.17
1345	C	GLY	A	390	36.469	87.587	87.823	1.00	31.16
1346	O	GLY	A	390	37.327	86.725	87.882	1.00	27.68
1347	N	ARG	A	391	35.986	88.273	88.926	1.00	30.04
1348	CA	ARG	A	391	36.571	87.993	90.215	1.00	30.27
1349	CB	ARG	A	391	36.059	88.919	91.287	1.00	31.81
1350	CG	ARG	A	391	36.876	88.961	92.606	1.00	36.05
1351	CD	ARG	A	391	38.301	89.717	92.397	1.00	41.83
1352	NE	ARG	A	391	39.252	88.791	91.670	1.00	44.01
1353	CZ	ARG	A	391	40.610	88.952	91.753	1.00	60.33
1354	NH1	ARG	A	391	41.184	89.957	92.544	1.00	74.34
1355	NH2	ARG	A	391	41.440	88.596	90.950	1.00	56.93
1356	C	ARG	A	391	36.244	86.563	90.653	1.00	29.49
1357	O	ARG	A	391	37.105	85.837	91.193	1.00	33.05
1358	N	VAL	A	392	34.992	86.194	90.444	1.00	29.58
1359	CA	VAL	A	392	34.548	84.837	90.857	1.00	28.07
1360	CB	VAL	A	392	33.045	84.512	90.527	1.00	25.28
1361	CG1	VAL	A	392	32.675	82.920	90.768	1.00	20.82
1362	CG2	VAL	A	392	32.179	85.402	91.408	1.00	18.99
1363	C	VAL	A	392	35.335	83.630	90.215	1.00	25.85
1364	O	VAL	A	392	35.683	82.672	90.839	1.00	24.37
1365	N	GLU	A	393	35.606	83.889	89.005	1.00	25.11
1366	CA	GLU	A	393	36.389	82.820	88.213	1.00	30.37
1367	CB	GLU	A	393	36.431	83.260	86.648	1.00	27.62
1368	CG	GLU	A	393	36.954	82.086	85.675	1.00	42.40
1369	CD	GLU	A	393	36.944	82.429	84.205	1.00	52.44
1370	OE1	GLU	A	393	37.290	83.563	83.672	1.00	54.11
1371	OE2	GLU	A	393	36.387	81.679	83.473	1.00	59.35
1372	C	GLU	A	393	37.862	82.831	88.653	1.00	24.86
1373	O	GLU	A	393	38.392	81.860	88.786	1.00	27.24
1374	N	ALA	A	394	38.392	83.974	89.054	1.00	28.71
1375	CA	ALA	A	394	39.853	83.981	89.532	1.00	27.69
1376	CB	ALA	A	394	40.413	85.489	89.467	1.00	26.95
1377	C	ALA	A	394	39.910	83.421	90.815	1.00	26.79
1378	O	ALA	A	394	40.871	82.728	91.065	1.00	37.81
1379	N	LEU	A	395	38.902	83.530	91.668	1.00	31.39
1380	CA	LEU	A	395	38.913	82.950	93.019	1.00	26.75
1381	CB	LEU	A	395	37.800	83.510	93.854	1.00	26.83
1382	CG	LEU	A	395	37.870	84.934	94.156	1.00	37.10
1383	CD1	LEU	A	395	36.675	85.476	94.959	1.00	29.87
1384	CD2	LEU	A	395	39.265	85.139	95.047	1.00	38.02
1385	C	LEU	A	395	38.691	81.426	92.890	1.00	29.53
1386	O	LEU	A	395	39.026	80.696	93.706	1.00	30.15
1387	N	GLN	A	396	38.087	80.955	91.788	1.00	30.18
1388	CA	GLN	A	396	37.872	79.548	91.564	1.00	30.65
1389	CB	GLN	A	396	36.798	79.306	90.484	1.00	26.71
1390	CG	GLN	A	396	36.379	77.817	90.332	1.00	27.41
1391	CD	GLN	A	396	35.582	77.586	89.046	1.00	30.01
1392	OE1	GLN	A	396	36.112	77.887	87.939	1.00	34.46
1393	NE2	GLN	A	396	34.449	77.071	89.157	1.00	23.49
1394	C	GLN	A	396	39.125	78.721	91.158	1.00	32.32
1395	O	GLN	A	396	39.346	77.612	91.588	1.00	31.21
1396	N	GLN	A	397	39.948	79.383	90.321	1.00	29.93
1397	CA	GLN	A	397	41.161	78.756	89.857	1.00	34.72
1398	CB	GLN	A	397	42.079	79.847	89.086	1.00	33.15
1399	CG	GLN	A	397	41.135	80.521	88.114	1.00	47.89
1400	CD	GLN	A	397	40.389	79.577	87.026	1.00	54.79
1401	OE1	GLN	A	397	40.970	78.909	86.143	1.00	56.43
1402	NE2	GLN	A	397	39.078	79.487	87.234	1.00	47.44
1403	C	GLN	A	397	42.079	78.034	90.789	1.00	31.50
1404	O	GLN	A	397	42.410	76.885	90.531	1.00	33.95
1405	N	PRO	A	398	42.488	78.652	91.901	1.00	32.17
1406	CA	PRO	A	398	43.417	77.939	92.836	1.00	33.30
1407	CB	PRO	A	398	43.694	78.885	94.123	1.00	30.34
1408	CG	PRO	A	398	43.243	80.298	93.380	1.00	33.80
1409	CD	PRO	A	398	42.194	80.090	92.358	1.00	27.53
1410	C	PRO	A	398	42.738	76.610	93.283	1.00	34.31
1411	O	PRO	A	398	43.492	75.605	93.531	1.00	37.90
1412	N	TYR	A	399	41.419	76.575	93.407	1.00	29.80
1413	CA	TYR	A	399	40.796	75.226	93.787	1.00	29.79
1414	CB	TYR	A	399	39.314	75.533	94.310	1.00	26.79
1415	CG	TYR	A	399	39.391	76.369	95.609	1.00	30.20
1416	CD1	TYR	A	399	39.850	75.877	96.821	1.00	19.91
1417	CE1	TYR	A	399	39.955	76.693	97.925	1.00	19.94
1418	CZ	TYR	A	399	39.474	78.001	97.852	1.00	28.75
1419	OH	TYR	A	399	39.610	78.833	98.939	1.00	32.92
1420	CE2	TYR	A	399	39.080	78.598	96.645	1.00	27.99
1421	CD2	TYR	A	399	39.036	77.786	95.541	1.00	32.38
1422	C	TYR	A	399	40.838	74.229	92.750	1.00	25.76
1423	O	TYR	A	399	40.948	73.086	92.974	1.00	27.61
1424	N	VAL	A	400	40.839	74.678	91.492	1.00	28.90
1425	CA	VAL	A	400	40.899	73.759	90.343	1.00	30.33
1426	CB	VAL	A	400	40.525	74.558	89.035	1.00	28.12
1427	CG1	VAL	A	400	40.625	73.575	87.823	1.00	28.59
1428	CG2	VAL	A	400	38.868	74.957	89.130	1.00	27.17
1429	C	VAL	A	400	42.343	73.282	90.248	1.00	32.13
1430	O	VAL	A	400	42.577	72.178	89.990	1.00	32.44
1431	N	GLU	A	401	43.294	74.187	90.477	1.00	34.53
1432	CA	GLU	A	401	44.728	73.837	90.461	1.00	31.84
1433	CB	GLU	A	401	45.553	75.137	90.815	1.00	35.52
1434	CG	GLU	A	401	45.554	76.108	89.776	1.00	50.30
1435	CD	GLU	A	401	46.461	77.373	90.237	1.00	71.99
1436	OE1	GLU	A	401	47.623	76.993	90.690	1.00	75.14
1437	OE2	GLU	A	401	46.044	78.745	90.202	1.00	60.74
1438	C	GLU	A	401	44.997	72.903	91.542	1.00	32.33
1439	O	GLU	A	401	45.615	71.865	91.249	1.00	33.73
1440	N	ALA	A	402	44.488	73.141	92.770	1.00	28.84
1441	CA	ALA	A	402	44.679	72.213	93.749	1.00	28.99
1442	CB	ALA	A	402	44.354	72.790	95.207	1.00	23.16
1443	C	ALA	A	402	44.135	70.909	93.551	1.00	33.91
1444	O	ALA	A	402	44.737	69.881	93.999	1.00	34.29
1445	N	LEU	A	403	42.856	70.792	93.023	1.00	31.11
1446	CA	LEU	A	403	42.286	69.471	92.813	1.00	29.68
1447	CB	LEU	A	403	40.732	69.679	92.331	1.00	31.27
1448	CG	LEU	A	403	39.888	68.502	92.054	1.00	22.85
1449	CD1	LEU	A	403	39.975	67.378	93.212	1.00	12.67
1450	CD2	LEU	A	403	38.459	68.653	91.865	1.00	30.67
1451	C	LEU	A	403	42.978	68.732	91.721	1.00	32.64
1452	O	LEU	A	403	43.081	67.511	91.743	1.00	29.24
1453	N	LEU	A	404	43.492	69.501	90.711	1.00	32.31
1454	CA	LEU	A	404	44.229	68.965	89.569	1.00	33.73
1455	CB	LEU	A	404	44.690	69.975	88.666	1.00	34.29
1456	CG	LEU	A	404	45.500	69.487	87.451	1.00	46.05
1457	CD1	LEU	A	404	45.010	68.178	86.857	1.00	46.09
1458	CD2	LEU	A	404	45.627	70.528	86.256	1.00	45.50
1459	C	LEU	A	404	45.476	68.218	90.066	1.00	41.28
1460	O	LEU	A	404	45.735	66.983	89.744	1.00	44.64
1461	N	SER	A	405	46.232	68.699	90.957	1.00	37.96
1462	CA	SER	A	405	47.467	68.220	91.476	1.00	44.39
1463	CB	SER	A	405	48.389	69.582	91.945	1.00	40.19
1464	OG	SER	A	405	48.190	69.736	93.256	1.00	52.87
1465	C	SER	A	405	47.136	67.132	92.536	1.00	43.99
1466	O	SER	A	405	47.820	66.053	92.550	1.00	42.67
1467	N	TYR	A	406	46.168	67.418	93.374	1.00	35.30
1468	CA	TYR	A	406	45.781	66.347	94.211	1.00	34.10
1469	CB	TYR	A	406	44.682	66.788	95.238	1.00	38.62
1470	CG	TYR	A	406	44.367	65.841	96.288	1.00	30.54
1471	CD1	TYR	A	406	44.805	66.098	97.590	1.00	31.56
1472	CE1	TYR	A	406	44.462	65.188	98.631	1.00	30.25
1473	CZ	TYR	A	406	43.804	64.086	98.329	1.00	26.94
1474	OH	TYR	A	406	43.423	63.233	99.436	1.00	40.42
1475	CE2	TYR	A	406	43.301	63.860	97.184	1.00	30.74
1476	CD2	TYR	A	406	43.573	64.795	96.035	1.00	26.35
1477	C	TYR	A	406	45.427	65.102	93.654	1.00	35.00
1478	O	TYR	A	406	45.805	63.964	94.172	1.00	38.25
1479	N	THR	A	407	44.775	65.109	92.611	1.00	36.43
1480	CA	THR	A	407	44.385	63.965	91.861	1.00	42.81
1481	CB	THR	A	407	43.137	64.087	90.910	1.00	32.55
1482	OG1	THR	A	407	43.410	65.212	90.049	1.00	39.85
1483	CG2	THR	A	407	41.899	64.584	91.677	1.00	40.39
1484	C	THR	A	407	45.514	63.245	91.065	1.00	42.98
1485	O	THR	A	407	45.504	62.114	90.801	1.00	42.83
1486	N	ARG	A	408	46.445	64.127	90.628	1.00	46.62
1487	CA	ARG	A	408	47.571	63.709	89.899	1.00	52.55
1488	CB	ARG	A	408	48.345	64.721	89.277	1.00	48.70
1489	CG	ARG	A	408	47.824	64.847	87.855	1.00	53.29
1490	CD	ARG	A	408	48.685	66.207	87.431	1.00	72.48
1491	NE	ARG	A	408	48.291	66.729	86.136	1.00	66.20
1492	CZ	ARG	A	408	48.839	67.847	85.647	1.00	64.96
1493	NH1	ARG	A	408	49.702	68.464	86.414	1.00	63.99
1494	NH2	ARG	A	408	48.478	68.288	84.370	1.00	69.82
1495	C	ARG	A	408	48.436	62.765	90.824	1.00	54.06
1496	O	ARG	A	408	48.991	61.713	90.391	1.00	49.02
1497	N	ILE	A	409	48.590	63.317	92.076	1.00	51.24
1498	CA	ILE	A	409	49.270	62.418	93.053	1.00	50.90
1499	CB	ILE	A	409	49.529	63.313	94.286	1.00	54.05
1500	CG1	ILE	A	409	50.683	64.440	93.999	1.00	43.61
1501	CD1	ILE	A	409	50.414	65.719	94.449	1.00	45.39
1502	CG2	ILE	A	409	49.927	62.382	95.389	1.00	51.63
1503	C	ILE	A	409	48.661	61.134	93.530	1.00	54.26
1504	O	ILE	A	409	49.247	60.038	93.741	1.00	55.05
1505	N	LYS	A	410	47.343	61.152	93.544	1.00	54.70
1506	CA	LYS	A	410	46.555	60.110	94.103	1.00	50.99
1507	CB	LYS	A	410	45.161	60.665	94.544	1.00	47.69
1508	CG	LYS	A	410	44.229	59.623	94.947	1.00	51.67
1509	CD	LYS	A	410	42.947	60.151	95.775	1.00	55.94
1510	CE	LYS	A	410	41.975	59.090	96.148	1.00	44.96
1511	NZ	LYS	A	410	41.200	59.757	97.017	1.00	44.06
1512	C	LYS	A	410	46.509	59.074	93.032	1.00	49.55
1513	O	LYS	A	410	46.378	57.845	93.352	1.00	48.08
1514	N	ARG	A	411	46.407	59.465	91.775	1.00	52.32
1515	CA	ARG	A	411	46.319	58.384	90.703	1.00	52.88
1516	CB	ARG	A	411	44.877	58.019	90.242	1.00	54.89
1517	CG	ARG	A	411	44.056	57.302	91.277	1.00	67.48
1518	CD	ARG	A	411	44.746	56.064	91.754	1.00	66.12
1519	NE	ARG	A	411	44.451	55.896	93.193	1.00	68.99
1520	CZ	ARG	A	411	43.302	55.331	93.552	1.00	61.73
1521	NH1	ARG	A	411	42.439	55.144	92.642	1.00	64.12
1522	NH2	ARG	A	411	43.153	54.891	94.794	1.00	63.60
1523	C	ARG	A	411	47.153	58.796	89.515	1.00	57.53
1524	O	ARG	A	411	46.660	59.216	88.465	1.00	56.06
1525	N	PRO	A	412	48.481	58.714	89.670	1.00	60.42
1526	CA	PRO	A	412	49.366	59.100	88.559	1.00	60.45
1527	CB	PRO	A	412	50.792	58.654	89.055	1.00	56.65
1528	CG	PRO	A	412	50.638	58.752	90.601	1.00	69.55
1529	CD	PRO	A	412	49.227	58.268	90.861	1.00	65.25
1530	C	PRO	A	412	49.000	58.556	87.306	1.00	55.68
1531	O	PRO	A	412	49.182	59.133	86.255	1.00	54.06
1532	N	GLN	A	413	48.546	57.356	87.408	1.00	59.90
1533	CA	GLN	A	413	48.240	56.659	86.032	1.00	60.25
1534	CB	GLN	A	413	48.527	55.104	86.217	1.00	67.10
1535	CG	GLN	A	413	49.979	54.905	86.732	1.00	67.59
1536	CD	GLN	A	413	51.056	55.757	86.119	1.00	69.36
1537	OE1	GLN	A	413	52.033	56.057	86.786	1.00	76.94
1538	NE2	GLN	A	413	50.872	56.187	84.846	1.00	67.53
1539	C	GLN	A	413	47.009	56.779	85.481	1.00	59.10
1540	O	GLN	A	413	46.844	56.449	84.366	1.00	60.75
1541	N	ASP	A	414	45.896	57.364	86.336	1.00	63.03
1542	CA	ASP	A	414	44.555	57.575	85.738	1.00	55.65
1543	CB	ASP	A	414	43.565	56.927	86.446	1.00	53.04
1544	CG	ASP	A	414	42.148	57.197	85.879	1.00	59.05
1545	OD1	ASP	A	414	41.969	58.000	84.911	1.00	68.82
1546	OD2	ASP	A	414	41.126	56.572	86.289	1.00	57.97
1547	C	ASP	A	414	44.407	58.993	85.552	1.00	57.26
1548	O	ASP	A	414	43.743	59.555	86.419	1.00	60.96
1549	N	GLN	A	415	44.786	59.617	84.483	1.00	53.51
1550	CA	GLN	A	415	44.736	61.024	84.480	1.00	57.02
1551	CB	GLN	A	415	45.840	61.675	83.501	1.00	59.17
1552	CG	GLN	A	415	45.684	61.102	82.123	1.00	63.39
1553	CD	GLN	A	415	46.787	61.535	81.185	1.00	69.87
1554	OE1	GLN	A	415	48.032	61.685	81.549	1.00	69.69
1555	NE2	GLN	A	415	46.370	61.784	79.954	1.00	65.81
1556	C	GLN	A	415	43.300	61.480	83.949	1.00	59.76
1557	O	GLN	A	415	43.081	62.730	83.850	1.00	56.95
1558	N	LEU	A	416	42.429	60.561	83.629	1.00	50.69
1559	CA	LEU	A	416	41.262	60.915	83.182	1.00	51.95
1560	CB	LEU	A	416	40.604	59.909	82.263	1.00	53.16
1561	CG	LEU	A	416	40.848	60.187	80.807	1.00	57.50
1562	CD1	LEU	A	416	39.912	59.258	80.067	1.00	61.02
1563	CD2	LEU	A	416	40.336	61.419	80.230	1.00	61.68
1564	C	LEU	A	416	40.167	61.107	84.453	1.00	52.06
1565	O	LEU	A	416	39.004	61.326	84.201	1.00	48.57
1566	N	ARG	A	417	40.562	60.772	85.626	1.00	46.23
1567	CA	ARG	A	417	39.677	60.700	86.771	1.00	40.89
1568	CB	ARG	A	417	40.450	60.148	87.966	1.00	42.06
1569	CG	ARG	A	417	39.657	60.063	89.207	1.00	40.87
1570	CD	ARG	A	417	40.152	58.840	90.092	1.00	39.38
1571	NE	ARG	A	417	39.531	59.057	91.418	1.00	40.68
1572	CZ	ARG	A	417	39.876	59.801	92.391	1.00	35.79
1573	NH1	ARG	A	417	40.779	60.686	92.220	1.00	36.07
1574	NH2	ARG	A	417	39.229	59.755	93.478	1.00	41.09
1575	C	ARG	A	417	39.269	62.284	87.138	1.00	42.35
1576	O	ARG	A	417	38.155	62.476	87.367	1.00	42.23
1577	N	PHE	A	418	40.200	63.278	87.055	1.00	35.97
1578	CA	PHE	A	418	40.021	64.477	87.203	1.00	35.12
1579	CB	PHE	A	418	41.315	65.336	87.179	1.00	37.25
1580	CG	PHE	A	418	41.145	66.817	87.222	1.00	39.82
1581	CD1	PHE	A	418	40.561	67.363	88.376	1.00	36.75
1582	CE1	PHE	A	418	40.412	68.729	88.477	1.00	39.66
1583	CZ	PHE	A	418	40.913	69.635	87.493	1.00	38.39
1584	CE2	PHE	A	418	41.303	69.057	86.338	1.00	41.04
1585	CD2	PHE	A	418	41.411	67.677	86.155	1.00	38.75
1586	C	PHE	A	418	38.872	65.136	86.285	1.00	36.79
1587	O	PHE	A	418	37.975	65.773	86.756	1.00	34.40
1588	N	PRO	A	419	38.976	64.989	85.010	1.00	41.06
1589	CA	PRO	A	419	37.997	65.452	84.075	1.00	39.02
1590	CB	PRO	A	419	38.398	64.915	82.750	1.00	34.83
1591	CG	PRO	A	419	39.855	64.902	82.890	1.00	42.68
1592	CD	PRO	A	419	40.183	64.401	84.281	1.00	41.24
1593	C	PRO	A	419	36.585	64.848	84.467	1.00	39.16
1594	O	PRO	A	419	35.607	65.602	84.408	1.00	33.73
1595	N	ARG	A	420	36.600	63.577	84.771	1.00	35.41
1596	CA	ARG	A	420	35.250	62.979	85.162	1.00	37.98
1597	CB	ARG	A	420	35.532	61.478	85.670	1.00	42.52
1598	CG	ARG	A	420	35.774	60.547	84.395	1.00	46.42
1599	CD	ARG	A	420	36.028	59.128	84.767	1.00	50.85
1600	NE	ARG	A	420	37.172	58.711	83.941	1.00	64.11
1601	CZ	ARG	A	420	38.362	58.028	84.512	1.00	78.99
1602	NH1	ARG	A	420	38.517	57.706	85.875	1.00	70.47
1603	NH2	ARG	A	420	39.327	57.619	83.746	1.00	75.11
1604	C	ARG	A	420	34.767	63.697	86.391	1.00	36.80
1605	O	ARG	A	420	33.562	63.836	86.490	1.00	36.70
1606	N	MET	A	421	35.663	64.164	87.317	1.00	34.00
1607	CA	MET	A	421	35.064	64.925	88.565	1.00	36.38
1608	CB	MET	A	421	36.145	65.268	89.533	1.00	37.98
1609	CG	MET	A	421	37.009	64.221	89.994	1.00	42.30
1610	SD	MET	A	421	37.806	64.611	91.524	1.00	45.58
1611	CE	MET	A	421	38.300	62.962	92.178	1.00	44.14
1612	C	MET	A	421	34.438	66.104	88.237	1.00	35.14
1613	O	MET	A	421	33.286	66.389	88.607	1.00	30.64
1614	N	LEU	A	422	35.079	66.854	87.231	1.00	33.34
1615	CA	LEU	A	422	34.470	68.084	86.637	1.00	29.82
1616	CB	LEU	A	422	35.462	68.738	85.690	1.00	26.02
1617	CG	LEU	A	422	36.710	69.286	86.396	1.00	33.75
1618	CD1	LEU	A	422	37.399	70.279	85.416	1.00	33.74
1619	CD2	LEU	A	422	36.267	70.088	87.671	1.00	29.58
1620	C	LEU	A	422	33.294	67.769	85.929	1.00	27.96
1621	O	LEU	A	422	32.279	68.609	85.861	1.00	29.14
1622	N	MET	A	423	33.275	66.662	85.239	1.00	27.82
1623	CA	MET	A	423	32.065	66.404	84.346	1.00	32.40
1624	CB	MET	A	423	32.249	65.076	83.582	1.00	34.06
1625	CG	MET	A	423	31.903	65.119	82.269	1.00	49.31
1626	SD	MET	A	423	33.373	65.419	81.082	1.00	63.59
1627	CE	MET	A	423	34.237	63.848	81.579	1.00	57.13
1628	C	MET	A	423	30.806	66.227	85.315	1.00	30.73
1629	O	MET	A	423	29.727	66.509	84.918	1.00	29.61
1630	N	LYS	A	424	31.078	65.801	86.617	1.00	27.60
1631	CA	LYS	A	424	30.029	65.769	87.539	1.00	29.41
1632	CB	LYS	A	424	30.371	65.126	88.896	1.00	32.42
1633	CG	LYS	A	424	30.825	63.645	88.773	1.00	27.50
1634	CD	LYS	A	424	29.490	62.936	88.242	1.00	36.24
1635	CE	LYS	A	424	29.832	61.415	88.133	1.00	48.83
1636	NZ	LYS	A	424	29.139	60.782	86.961	1.00	49.91
1637	C	LYS	A	424	29.406	67.122	87.734	1.00	23.61
1638	O	LYS	A	424	28.142	67.230	88.073	1.00	30.83
1639	N	LEU	A	425	30.136	68.133	87.681	1.00	24.79
1640	CA	LEU	A	425	29.623	69.505	87.924	1.00	25.47
1641	CB	LEU	A	425	30.651	70.583	87.816	1.00	28.69
1642	CG	LEU	A	425	31.803	70.454	88.879	1.00	32.43
1643	CD1	LEU	A	425	32.859	71.414	88.452	1.00	22.94
1644	CD2	LEU	A	425	31.189	70.728	90.304	1.00	21.58
1645	C	LEU	A	425	28.500	69.750	86.792	1.00	29.35
1646	O	LEU	A	425	27.584	70.593	86.996	1.00	25.35
1647	N	VAL	A	426	28.621	69.038	85.684	1.00	27.10
1648	CA	VAL	A	426	27.675	69.220	84.602	1.00	28.71
1649	CB	VAL	A	426	28.187	68.537	83.182	1.00	29.02
1650	CG1	VAL	A	426	27.146	68.755	82.165	1.00	25.81
1651	CG2	VAL	A	426	29.488	69.113	82.785	1.00	22.35
1652	C	VAL	A	426	26.371	68.567	84.961	1.00	29.59
1653	O	VAL	A	426	25.330	69.197	84.784	1.00	25.85
1654	N	SER	A	427	26.486	67.295	85.446	1.00	25.25
1655	CA	SER	A	427	25.299	66.592	85.893	1.00	31.04
1656	CB	SER	A	427	25.646	65.239	86.541	1.00	29.34
1657	OG	SER	A	427	26.386	64.519	85.593	1.00	36.53
1658	C	SER	A	427	24.489	67.358	86.989	1.00	27.83
1659	O	SER	A	427	23.282	67.360	86.996	1.00	29.96
1660	N	LEU	A	428	25.241	68.094	87.855	1.00	25.96
1661	CA	LEU	A	428	24.574	68.851	88.874	1.00	25.88
1662	CB	LEU	A	428	25.615	69.374	89.908	1.00	26.13
1663	CG	LEU	A	428	26.242	68.388	90.765	1.00	28.00
1664	CD1	LEU	A	428	27.333	68.878	91.619	1.00	25.90
1665	CD2	LEU	A	428	25.160	67.651	91.617	1.00	25.47
1666	C	LEU	A	428	23.770	70.091	88.399	1.00	25.61
1667	O	LEU	A	428	22.797	70.426	89.070	1.00	27.26
1668	N	ARG	A	429	24.030	70.643	87.309	1.00	27.67
1669	CA	ARG	A	429	23.168	71.755	86.754	1.00	28.64
1670	CB	ARG	A	429	23.846	72.372	85.395	1.00	30.85
1671	CG	ARG	A	429	25.056	73.113	85.647	1.00	32.25
1672	CD	ARG	A	429	24.907	74.244	86.805	1.00	29.00
1673	NE	ARG	A	429	26.057	74.913	87.080	1.00	26.21
1674	CZ	ARG	A	429	26.474	76.062	86.553	1.00	34.64
1675	NH1	ARG	A	429	25.821	76.717	85.593	1.00	22.70
1676	NH2	ARG	A	429	27.717	76.569	86.962	1.00	23.50
1677	C	ARG	A	429	21.885	71.086	86.288	1.00	31.30
1678	O	ARG	A	429	20.758	71.548	86.717	1.00	32.96
1679	N	THR	A	430	21.963	69.916	85.636	1.00	30.33
1680	CA	THR	A	430	20.749	69.255	85.310	1.00	30.85
1681	CB	THR	A	430	20.935	68.120	84.531	1.00	35.73
1682	OG1	THR	A	430	21.555	68.364	83.254	1.00	35.60
1683	CG2	THR	A	430	19.717	67.347	84.442	1.00	37.10
1684	C	THR	A	430	19.923	68.792	86.599	1.00	37.17
1685	O	THR	A	430	18.697	68.925	86.688	1.00	34.48
1686	N	LEU	A	431	20.643	68.327	87.662	1.00	33.01
1687	CA	LEU	A	431	19.901	67.926	88.831	1.00	28.10
1688	CB	LEU	A	431	20.828	67.144	89.785	1.00	23.96
1689	CG	LEU	A	431	21.261	65.716	89.252	1.00	29.33
1690	CD1	LEU	A	431	22.536	65.336	90.048	1.00	27.95
1691	CD2	LEU	A	431	20.226	64.748	89.638	1.00	26.21
1692	C	LEU	A	431	19.241	69.061	89.469	1.00	30.75
1693	O	LEU	A	431	18.249	68.912	90.236	1.00	28.23
1694	N	SER	A	432	19.895	70.188	89.382	1.00	31.10
1695	CA	SER	A	432	19.306	71.382	90.063	1.00	34.73
1696	CB	SER	A	432	20.276	72.655	89.682	1.00	31.90
1697	OG	SER	A	432	19.792	73.610	90.459	1.00	34.94
1698	C	SER	A	432	17.914	71.747	89.269	1.00	33.59
1699	O	SER	A	432	16.960	72.011	89.974	1.00	32.44
1700	N	SER	A	433	17.903	71.747	87.942	1.00	27.95
1701	CA	SER	A	433	16.624	71.955	87.227	1.00	38.05
1702	CB	SER	A	433	16.663	71.739	85.662	1.00	32.77
1703	OG	SER	A	433	17.766	72.432	85.101	1.00	45.13
1704	C	SER	A	433	15.583	70.841	87.730	1.00	38.67
1705	O	SER	A	433	14.416	71.170	87.950	1.00	37.74
1706	N	VAL	A	434	16.048	69.555	87.805	1.00	36.17
1707	CA	VAL	A	434	15.102	68.479	88.235	1.00	32.23
1708	CB	VAL	A	434	15.767	67.297	88.257	1.00	32.68
1709	CG1	VAL	A	434	14.919	66.195	88.855	1.00	30.28
1710	CG2	VAL	A	434	16.210	66.792	86.800	1.00	31.93
1711	C	VAL	A	434	14.580	68.830	89.507	1.00	40.04
1712	O	VAL	A	434	13.439	68.531	89.830	1.00	38.10
1713	N	HIS	A	435	15.401	69.491	90.449	1.00	32.82
1714	CA	HIS	A	435	14.960	69.548	91.844	1.00	35.99
1715	CB	HIS	A	435	16.108	70.011	92.772	1.00	24.67
1716	CG	HIS	A	435	15.727	70.667	93.947	1.00	26.20
1717	ND1	HIS	A	435	15.127	70.028	95.027	1.00	36.92
1718	CE1	HIS	A	435	14.832	70.814	96.029	1.00	22.84
1719	NE2	HIS	A	435	15.256	72.018	95.669	1.00	28.59
1720	CD2	HIS	A	435	15.802	71.988	94.347	1.00	26.08
1721	C	HIS	A	435	14.007	70.990	91.768	1.00	37.15
1722	O	HIS	A	435	13.054	70.980	92.532	1.00	38.90
1723	N	SER	A	436	14.238	71.783	90.816	1.00	38.33
1724	CA	SER	A	436	13.399	73.019	90.653	1.00	44.55
1725	CB	SER	A	436	14.019	73.975	89.619	1.00	41.13
1726	OG	SER	A	436	15.049	74.750	90.099	1.00	54.11
1727	C	SER	A	436	12.003	72.383	90.259	1.00	42.03
1728	O	SER	A	436	10.981	72.945	90.755	1.00	42.41
1729	N	GLU	A	437	11.969	71.595	89.249	1.00	40.79
1730	CA	GLU	A	437	10.738	70.900	88.892	1.00	43.47
1731	CB	GLU	A	437	11.061	69.908	87.927	1.00	43.76
1732	CG	GLU	A	437	11.464	70.697	86.621	1.00	57.34
1733	CD	GLU	A	437	11.497	69.764	85.322	1.00	72.30
1734	OE1	GLU	A	437	12.311	68.751	85.071	1.00	57.33
1735	OE2	GLU	A	437	10.572	70.092	84.521	1.00	76.33
1736	C	GLU	A	437	9.970	70.284	90.017	1.00	46.04
1737	O	GLU	A	437	8.762	70.517	90.163	1.00	44.56
1738	N	GLN	A	438	10.698	69.499	90.812	1.00	46.25
1739	CA	GLN	A	438	10.148	68.959	91.933	1.00	43.05
1740	CB	GLN	A	438	11.160	67.968	92.704	1.00	45.87
1741	CG	GLN	A	438	10.821	67.763	94.135	1.00	49.29
1742	CD	GLN	A	438	9.663	66.598	94.156	1.00	55.63
1743	OE1	GLN	A	438	9.841	65.568	93.633	1.00	55.13
1744	NE2	GLN	A	438	8.524	67.028	94.581	1.00	51.65
1745	C	GLN	A	438	9.503	69.985	92.888	1.00	47.96
1746	O	GLN	A	438	8.328	69.879	93.358	1.00	51.78
1747	N	VAL	A	439	10.245	70.999	93.193	1.00	48.20
1748	CA	VAL	A	439	9.804	72.122	94.037	1.00	50.36
1749	CB	VAL	A	439	10.729	73.174	94.141	1.00	50.79
1750	CG1	VAL	A	439	10.242	74.389	94.716	1.00	52.64
1751	CG2	VAL	A	439	11.869	72.737	95.107	1.00	50.25
1752	C	VAL	A	439	8.379	72.797	93.386	1.00	57.07
1753	O	VAL	A	439	7.540	73.118	94.051	1.00	53.27
1754	N	PHE	A	440	8.308	72.784	92.083	1.00	57.76
1755	CA	PHE	A	440	7.226	73.397	91.444	1.00	66.63
1756	CB	PHE	A	440	7.548	73.880	89.971	1.00	62.94
1757	CG	PHE	A	440	6.717	73.131	88.956	1.00	73.05
1758	CD1	PHE	A	440	6.802	71.677	88.717	1.00	85.94
1759	CE1	PHE	A	440	5.902	70.839	87.909	1.00	73.25
1760	CZ	PHE	A	440	4.927	71.551	87.287	1.00	82.27
1761	CE2	PHE	A	440	4.764	72.960	87.523	1.00	81.56
1762	CD2	PHE	A	440	5.646	73.724	88.437	1.00	82.59
1763	C	PHE	A	440	6.060	72.275	91.573	1.00	66.87
1764	O	PHE	A	440	4.931	72.840	91.922	1.00	64.21
1765	N	ALA	A	441	6.261	71.010	91.246	1.00	60.46
1766	CA	ALA	A	441	5.173	70.271	91.239	1.00	65.34
1767	CB	ALA	A	441	5.647	68.767	90.689	1.00	61.82
1768	C	ALA	A	441	4.692	70.143	92.627	1.00	67.12
1769	O	ALA	A	441	3.901	69.380	92.845	1.00	73.23
1770	N	LEU	A	442	5.249	70.810	93.570	1.00	72.33
1771	CA	LEU	A	442	4.796	70.586	94.914	1.00	76.45
1772	CB	LEU	A	442	6.039	70.402	95.873	1.00	77.74
1773	CG	LEU	A	442	6.581	68.942	95.867	1.00	83.53
1774	CD1	LEU	A	442	7.788	68.673	96.538	1.00	78.41
1775	CD2	LEU	A	442	5.497	68.191	96.563	1.00	90.49
1776	C	LEU	A	442	4.015	71.796	95.331	1.00	78.34
1777	O	LEU	A	442	3.219	71.716	96.259	1.00	71.44
1778	N	ARG	A	443	4.350	72.960	94.684	1.00	78.55
1779	CA	ARG	A	443	3.805	74.263	95.098	1.00	78.60
1780	CB	ARG	A	443	4.504	75.444	94.406	1.00	77.87
1781	CG	ARG	A	443	3.994	76.809	94.630	1.00	85.09
1782	CD	ARG	A	443	4.855	77.895	94.376	1.00	86.30
1783	NE	ARG	A	443	4.485	78.950	95.329	1.00	85.73
1784	CZ	ARG	A	443	4.723	80.182	95.006	1.00	95.54
1785	NH1	ARG	A	443	5.435	80.465	93.857	1.00	97.80
1786	NH2	ARG	A	443	4.317	81.128	95.823	1.00	102.71
1787	C	ARG	A	443	2.264	74.178	94.653	1.00	84.02
1788	O	ARG	A	443	1.404	75.220	94.901	1.00	81.88
1789	N	LEU	A	444	1.934	72.989	94.066	1.00	84.66
1790	CA	LEU	A	444	0.650	72.774	93.482	1.00	86.44
1791	CB	LEU	A	444	0.724	72.607	91.957	1.00	84.71
1792	CG	LEU	A	444	1.212	73.978	91.396	1.00	90.51
1793	CD1	LEU	A	444	1.943	73.586	90.075	1.00	93.16
1794	CD2	LEU	A	444	0.213	75.394	91.338	1.00	107.20
1795	C	LEU	A	444	0.196	71.466	94.026	1.00	84.64
1796	O	LEU	A	444	−0.162	70.680	93.258	1.00	86.26
1797	N	ALA	A	445	0.238	71.239	95.287	1.00	82.56
1798	CA	ALA	A	445	−0.176	69.949	95.812	1.00	82.67
1799	CB	ALA	A	445	0.829	68.934	95.510	1.00	78.79
1800	C	ALA	A	445	−0.464	70.183	97.356	1.00	85.71
1801	O	ALA	A	445	−0.371	69.290	98.262	1.00	80.18
1802	N	ALA	A	446	−0.832	71.475	97.600	1.00	92.16
1803	CA	ALA	A	446	−1.182	72.091	98.988	1.00	97.18
1804	CB	ALA	A	446	−2.513	71.589	99.617	1.00	99.10
1805	C	ALA	A	446	0.117	71.823	99.984	1.00	99.56
1806	O	ALA	A	446	0.058	71.252	101.258	1.00	100.00
1807	N	LYS	A	447	1.281	72.187	99.385	1.00	92.32
1808	CA	LYS	A	447	2.480	71.815	100.040	1.00	85.44
1809	CB	LYS	A	447	2.859	70.333	99.788	1.00	86.22
1810	CG	LYS	A	447	4.095	69.872	100.654	1.00	81.60
1811	CD	LYS	A	447	4.451	68.590	100.406	1.00	82.83
1812	CE	LYS	A	447	3.268	67.614	100.586	1.00	94.35
1813	NZ	LYS	A	447	3.579	66.004	100.401	1.00	95.29
1814	C	LYS	A	447	3.647	72.838	99.640	1.00	85.09
1815	O	LYS	A	447	4.149	72.846	98.461	1.00	87.81
1816	N	LYS	A	448	3.975	73.742	100.568	1.00	74.20
1817	CA	LYS	A	448	4.854	74.659	100.282	1.00	71.88
1818	CB	LYS	A	448	4.136	75.930	100.716	1.00	76.29
1819	CG	LYS	A	448	3.062	76.477	99.835	1.00	78.44
1820	CD	LYS	A	448	2.898	78.032	99.838	1.00	89.59
1821	CE	LYS	A	448	4.132	78.859	98.972	1.00	90.92
1822	NZ	LYS	A	448	4.726	80.124	99.676	1.00	78.09
1823	C	LYS	A	448	6.201	74.552	101.061	1.00	70.07
1824	O	LYS	A	448	6.299	74.181	102.250	1.00	68.77
1825	N	LEU	A	449	7.184	75.089	100.484	1.00	64.82
1826	CA	LEU	A	449	8.394	75.086	101.290	1.00	65.02
1827	CB	LEU	A	449	9.663	75.453	100.443	1.00	61.79
1828	CG	LEU	A	449	10.049	74.517	99.154	1.00	59.53
1829	CD1	LEU	A	449	10.939	75.250	98.322	1.00	56.93
1830	CD2	LEU	A	449	10.691	73.326	99.728	1.00	62.04
1831	C	LEU	A	449	8.353	75.993	102.569	1.00	61.28
1832	O	LEU	A	449	8.026	77.014	102.543	1.00	63.29
1833	N	PRO	A	450	8.901	75.553	103.645	1.00	63.84
1834	CA	PRO	A	450	8.980	76.446	104.765	1.00	58.74
1835	CB	PRO	A	450	9.770	75.580	105.907	1.00	64.22
1836	CG	PRO	A	450	10.837	74.448	104.960	1.00	57.82
1837	CD	PRO	A	450	9.913	74.288	103.764	1.00	60.43
1838	C	PRO	A	450	9.800	77.692	104.334	1.00	64.24
1839	O	PRO	A	450	10.649	77.870	103.396	1.00	67.98
1840	N	PRO	A	451	9.595	78.728	105.013	1.00	65.71
1841	CA	PRO	A	451	10.169	79.999	104.625	1.00	62.74
1842	CB	PRO	A	451	9.910	80.887	105.908	1.00	64.68
1843	CG	PRO	A	451	8.326	80.238	106.130	1.00	66.88
1844	CD	PRO	A	451	8.648	78.865	106.130	1.00	66.25
1845	C	PRO	A	451	11.679	80.077	104.296	1.00	58.54
1846	O	PRO	A	451	12.236	80.694	103.399	1.00	56.32
1847	N	LEU	A	452	12.416	79.445	105.043	1.00	58.56
1848	CA	LEU	A	452	13.817	79.391	104.748	1.00	55.44
1849	CB	LEU	A	452	14.568	78.564	105.805	1.00	61.54
1850	CG	LEU	A	452	14.894	79.450	107.096	1.00	60.59
1851	CD1	LEU	A	452	15.037	78.629	108.494	1.00	60.37
1852	CD2	LEU	A	452	16.218	80.025	106.721	1.00	55.27
1853	C	LEU	A	452	14.259	78.700	103.446	1.00	52.42
1854	O	LEU	A	452	14.980	79.281	102.671	1.00	51.12
1855	N	LEU	A	453	13.674	77.623	103.107	1.00	47.36
1856	CA	LEU	A	453	13.972	76.984	101.836	1.00	44.76
1857	CB	LEU	A	453	13.431	75.475	101.875	1.00	39.48
1858	CG	LEU	A	453	13.901	74.698	103.059	1.00	35.88
1859	CD1	LEU	A	453	13.380	73.314	103.060	1.00	35.22
1860	CD2	LEU	A	453	15.490	74.839	103.128	1.00	42.22
1861	C	LEU	A	453	13.376	77.699	100.831	1.00	46.42
1862	O	LEU	A	453	13.755	77.739	99.619	1.00	44.98
1863	N	SER	A	454	12.163	78.280	101.198	1.00	51.58
1864	CA	SER	A	454	11.330	79.070	100.141	1.00	52.68
1865	CB	SER	A	454	10.070	79.672	100.891	1.00	51.83
1866	OG	SER	A	454	9.261	80.092	99.852	1.00	53.35
1867	C	SER	A	454	12.180	80.297	99.505	1.00	45.72
1868	O	SER	A	454	12.132	80.501	98.407	1.00	44.83
1869	N	GLU	A	455	12.951	80.901	100.375	1.00	46.32
1870	CA	GLU	A	455	13.752	82.017	99.942	1.00	51.63
1871	CB	GLU	A	455	14.524	82.668	101.215	1.00	51.54
1872	CG	GLU	A	455	14.399	84.099	101.207	1.00	70.41
1873	CD	GLU	A	455	15.016	84.580	102.494	1.00	89.05
1874	OE1	GLU	A	455	14.914	83.941	103.617	1.00	85.24
1875	OE2	GLU	A	455	15.563	85.706	102.484	1.00	97.13
1876	C	GLU	A	455	14.934	81.578	98.853	1.00	58.03
1877	O	GLU	A	455	15.481	82.370	98.100	1.00	50.47
1878	N	ILE	A	456	15.328	80.264	98.862	1.00	54.73
1879	CA	ILE	A	456	16.244	79.882	97.829	1.00	49.19
1880	CB	ILE	A	456	17.125	78.697	98.531	1.00	49.97
1881	CG1	ILE	A	456	17.408	79.156	99.957	1.00	51.26
1882	CD1	ILE	A	456	18.058	77.967	100.909	1.00	50.93
1883	CG2	ILE	A	456	18.346	78.644	97.712	1.00	47.70
1884	C	ILE	A	456	15.646	79.312	96.669	1.00	45.32
1885	O	ILE	A	456	16.109	79.467	95.617	1.00	45.86
1886	N	TRP	A	457	14.580	78.515	96.847	1.00	45.70
1887	CA	TRP	A	457	14.165	77.784	95.787	1.00	49.53
1888	CB	TRP	A	457	13.930	76.402	96.205	1.00	41.00
1889	CG	TRP	A	457	15.383	75.756	96.619	1.00	45.01
1890	CD1	TRP	A	457	16.593	76.100	95.970	1.00	41.75
1891	NE1	TRP	A	457	17.484	75.291	96.470	1.00	33.91
1892	CE2	TRP	A	457	16.979	74.572	97.414	1.00	36.74
1893	CD2	TRP	A	457	15.624	74.856	97.504	1.00	30.90
1894	CE3	TRP	A	457	14.863	74.229	98.480	1.00	40.98
1895	CZ3	TRP	A	457	15.407	73.254	99.341	1.00	40.95
1896	CH2	TRP	A	457	16.852	72.924	99.238	1.00	35.65
1897	CZ2	TRP	A	457	17.657	73.666	98.320	1.00	31.70
1898	C	TRP	A	457	12.761	78.288	95.009	1.00	55.80
1899	O	TRP	A	457	12.485	77.759	94.016	1.00	61.13
1900	N	ASP	A	458	12.044	79.154	95.538	1.00	59.64
1901	CA	ASP	A	458	10.846	79.680	94.653	1.00	67.90
1902	CB	ASP	A	458	9.572	79.760	95.500	1.00	69.43
1903	CG	ASP	A	458	8.757	78.391	95.413	1.00	62.47
1904	OD1	ASP	A	458	8.323	77.972	94.165	1.00	59.31
1905	OD2	ASP	A	458	8.678	77.795	96.429	1.00	51.87
1906	C	ASP	A	458	11.166	81.042	94.253	1.00	70.30
1907	O	ASP	A	458	10.615	81.528	93.355	1.00	69.09
1908	N	VAL	A	459	12.295	81.544	94.842	1.00	77.71
1909	CA	VAL	A	459	12.847	82.884	94.547	1.00	83.82
1910	CB	VAL	A	459	14.049	83.127	95.380	1.00	82.76
1911	CG1	VAL	A	459	14.617	84.546	94.967	1.00	89.23
1912	CG2	VAL	A	459	13.473	83.256	96.861	1.00	91.03
1913	C	VAL	A	459	13.168	83.060	93.128	1.00	84.97
1914	O	VAL	A	459	14.391	82.839	92.884	1.00	89.63
1915	OXT	VAL	A	459	12.329	83.419	92.298	1.00	86.95
1916	N	GLU	B	216	58.321	62.770	80.955	1.00	104.37
1917	CA	GLU	B	216	57.234	63.800	80.512	1.00	106.06
1918	CB	GLU	B	216	57.707	65.248	80.833	1.00	105.65
1919	CG	GLU	B	216	57.269	65.820	82.137	1.00	107.76
1920	CD	GLU	B	216	58.068	67.157	82.576	1.00	116.36
1921	OE1	GLU	B	216	59.154	67.032	83.347	1.00	110.93
1922	OE2	GLU	B	216	57.626	68.366	82.222	1.00	111.71
1923	C	GLU	B	216	57.034	63.737	78.964	1.00	106.02
1924	O	GLU	B	216	56.169	62.939	78.581	1.00	104.35
1925	N	GLY	B	217	57.779	64.617	78.135	1.00	107.22
1926	CA	GLY	B	217	57.789	64.688	76.647	1.00	105.67
1927	C	GLY	B	217	56.570	64.814	75.718	1.00	104.69
1928	O	GLY	B	217	56.440	65.771	74.937	1.00	106.74
1929	N	VAL	B	218	55.757	63.783	75.659	1.00	103.69
1930	CA	VAL	B	218	54.562	63.637	74.720	1.00	98.47
1931	CB	VAL	B	218	53.360	63.434	75.491	1.00	95.36
1932	CG1	VAL	B	218	52.862	62.067	75.126	1.00	98.84
1933	CG2	VAL	B	218	53.777	63.451	77.005	1.00	102.45
1934	C	VAL	B	218	54.102	64.529	73.625	1.00	94.37
1935	O	VAL	B	218	54.296	65.746	73.595	1.00	95.73
1936	N	GLN	B	219	53.393	63.853	72.775	1.00	89.99
1937	CA	GLN	B	219	52.771	64.333	71.624	1.00	87.50
1938	CB	GLN	B	219	53.740	64.376	70.514	1.00	88.79
1939	CG	GLN	B	219	54.370	65.737	70.260	1.00	99.78
1940	CD	GLN	B	219	55.356	65.774	68.921	1.00	102.13
1941	OE1	GLN	B	219	56.064	66.782	68.670	1.00	99.81
1942	NE2	GLN	B	219	55.316	64.709	68.100	1.00	97.21
1943	C	GLN	B	219	51.646	63.288	71.208	1.00	85.61
1944	O	GLN	B	219	51.756	62.153	71.651	1.00	87.59
1945	N	LEU	B	220	50.645	63.647	70.362	1.00	80.42
1946	CA	LEU	B	220	49.566	62.830	70.020	1.00	80.74
1947	CB	LEU	B	220	48.740	63.465	68.860	1.00	76.94
1948	CG	LEU	B	220	48.068	64.785	69.106	1.00	87.28
1949	CD1	LEU	B	220	48.472	65.816	68.260	1.00	85.48
1950	CD2	LEU	B	220	46.486	64.713	69.177	1.00	91.66
1951	C	LEU	B	220	50.039	61.426	69.453	1.00	86.14
1952	O	LEU	B	220	51.322	61.268	69.015	1.00	89.45
1953	N	THR	B	221	49.049	60.549	69.211	1.00	81.01
1954	CA	THR	B	221	49.299	59.278	68.777	1.00	80.01
1955	CB	THR	B	221	48.646	58.213	69.788	1.00	76.61
1956	OG1	THR	B	221	47.242	58.289	69.709	1.00	77.41
1957	CG2	THR	B	221	49.112	58.246	71.288	1.00	74.67
1958	C	THR	B	221	48.511	59.389	67.535	1.00	79.99
1959	O	THR	B	221	47.575	60.151	67.501	1.00	82.96
1960	N	ALA	B	222	48.738	58.531	66.521	1.00	76.73
1961	CA	ALA	B	222	48.058	58.652	65.304	1.00	71.98
1962	CB	ALA	B	222	48.579	57.685	64.258	1.00	83.74
1963	C	ALA	B	222	46.762	58.321	65.405	1.00	74.83
1964	O	ALA	B	222	45.833	58.670	64.494	1.00	69.80
1965	N	ALA	B	223	46.641	57.616	66.534	1.00	75.78
1966	CA	ALA	B	223	45.280	57.295	67.007	1.00	74.74
1967	CB	ALA	B	223	45.413	56.749	68.522	1.00	73.66
1968	C	ALA	B	223	44.429	58.548	66.964	1.00	66.81
1969	O	ALA	B	223	43.410	58.789	66.227	1.00	66.52
1970	N	GLN	B	224	44.952	59.362	67.758	1.00	67.53
1971	CA	GLN	B	224	44.188	60.715	67.901	1.00	69.66
1972	CB	GLN	B	224	44.506	61.233	69.174	1.00	63.64
1973	CG	GLN	B	224	45.919	61.023	69.742	1.00	54.82
1974	CD	GLN	B	224	45.914	60.881	71.222	1.00	61.31
1975	OE1	GLN	B	224	46.978	61.214	71.967	1.00	60.03
1976	NE2	GLN	B	224	44.709	60.497	71.807	1.00	60.04
1977	C	GLN	B	224	44.141	61.725	66.676	1.00	66.55
1978	O	GLN	B	224	42.993	62.319	66.151	1.00	62.07
1979	N	GLU	B	225	45.278	61.728	66.021	1.00	70.62
1980	CA	GLU	B	225	45.190	62.593	64.761	1.00	68.19
1981	CB	GLU	B	225	46.480	62.689	64.237	1.00	77.82
1982	CG	GLU	B	225	47.079	64.105	64.057	1.00	81.01
1983	CD	GLU	B	225	48.649	64.215	64.181	1.00	70.84
1984	OE1	GLU	B	225	49.248	63.364	64.898	1.00	75.02
1985	OE2	GLU	B	225	49.263	65.156	63.577	1.00	72.57
1986	C	GLU	B	225	44.372	62.290	63.734	1.00	62.50
1987	O	GLU	B	225	43.317	63.140	63.169	1.00	60.80
1988	N	ALA	B	226	44.342	60.972	63.597	1.00	69.45
1989	CA	ALA	B	226	42.963	60.527	62.746	1.00	70.76
1990	CB	ALA	B	226	42.721	59.008	62.661	1.00	77.42
1991	C	ALA	B	226	41.982	61.171	63.218	1.00	65.26
1992	O	ALA	B	226	41.034	61.841	62.464	1.00	65.23
1993	N	MET	B	227	41.615	60.849	64.432	1.00	73.79
1994	CA	MET	B	227	40.135	61.403	64.931	1.00	58.91
1995	CB	MET	B	227	40.047	60.908	66.356	1.00	63.81
1996	CG	MET	B	227	38.792	61.642	67.072	1.00	63.60
1997	SD	MET	B	227	39.312	61.820	68.847	1.00	74.22
1998	CE	MET	B	227	40.123	60.366	69.617	1.00	64.78
1999	C	MET	B	227	40.050	62.822	64.740	1.00	53.86
2000	O	MET	B	227	38.919	63.341	64.335	1.00	58.35
2001	N	ILE	B	228	41.123	63.528	64.912	1.00	52.26
2002	CA	ILE	B	228	40.924	64.993	64.635	1.00	54.73
2003	CB	ILE	B	228	42.273	65.657	65.304	1.00	57.09
2004	CG1	ILE	B	228	42.424	65.342	66.623	1.00	54.21
2005	CD1	ILE	B	228	43.637	65.693	67.065	1.00	71.68
2006	CG2	ILE	B	228	42.290	67.084	65.280	1.00	66.30
2007	C	ILE	B	228	40.488	65.434	63.252	1.00	59.28
2008	O	ILE	B	228	39.399	66.221	63.112	1.00	55.72
2009	N	GLN	B	229	41.717	65.136	62.373	1.00	67.17
2010	CA	GLN	B	229	41.220	65.425	61.025	1.00	56.82
2011	CB	GLN	B	229	42.067	64.717	60.025	1.00	72.34
2012	CG	GLN	B	229	42.784	65.636	58.754	1.00	63.55
2013	CD	GLN	B	229	44.232	65.970	59.210	1.00	79.42
2014	OE1	GLN	B	229	44.605	67.084	59.893	1.00	79.95
2015	NE2	GLN	B	229	45.174	64.947	58.928	1.00	83.13
2016	C	GLN	B	229	39.932	65.027	60.659	1.00	53.09
2017	O	GLN	B	229	38.929	65.709	60.133	1.00	54.06
2018	N	GLN	B	230	39.742	63.883	60.942	1.00	57.65
2019	CA	GLN	B	230	38.128	63.382	60.670	1.00	62.36
2020	CB	GLN	B	230	37.940	61.858	61.286	1.00	68.75
2021	CG	GLN	B	230	36.517	61.303	61.428	1.00	66.09
2022	CD	GLN	B	230	36.302	59.984	60.740	1.00	72.78
2023	OE1	GLN	B	230	35.581	59.153	61.300	1.00	79.24
2024	NE2	GLN	B	230	36.751	59.851	59.385	1.00	79.99
2025	C	GLN	B	230	37.132	64.259	61.023	1.00	58.98
2026	O	GLN	B	230	36.234	64.761	60.243	1.00	65.60
2027	N	LEU	B	231	37.184	64.567	62.325	1.00	61.17
2028	CA	LEU	B	231	36.271	65.559	63.009	1.00	56.23
2029	CB	LEU	B	231	36.527	65.721	64.543	1.00	66.04
2030	CG	LEU	B	231	36.078	64.613	65.585	1.00	68.69
2031	CD1	LEU	B	231	36.486	65.056	66.929	1.00	57.79
2032	CD2	LEU	B	231	34.422	64.277	65.434	1.00	52.98
2033	C	LEU	B	231	36.329	66.995	62.437	1.00	54.78
2034	O	LEU	B	231	35.259	67.574	62.231	1.00	57.81
2035	N	VAL	B	232	37.321	67.640	62.034	1.00	62.54
2036	CA	VAL	B	232	37.149	69.043	61.447	1.00	66.58
2037	CB	VAL	B	232	38.485	69.812	61.477	1.00	67.20
2038	CG1	VAL	B	232	39.817	69.150	62.503	1.00	61.81
2039	CG2	VAL	B	232	38.915	69.807	60.241	1.00	79.63
2040	C	VAL	B	232	36.493	69.154	59.990	1.00	65.40
2041	O	VAL	B	232	35.559	69.981	59.698	1.00	60.73
2042	N	ALA	B	233	36.848	68.108	59.206	1.00	68.53
2043	CA	ALA	B	233	36.221	68.049	57.772	1.00	66.56
2044	CB	ALA	B	233	36.610	67.001	57.095	1.00	65.10
2045	C	ALA	B	233	34.713	68.055	57.800	1.00	73.51
2046	O	ALA	B	233	34.001	68.933	56.823	1.00	68.35
2047	N	ALA	B	234	34.180	67.208	58.815	1.00	67.41
2048	CA	ALA	B	234	32.789	67.089	58.936	1.00	68.39
2049	CB	ALA	B	234	32.406	66.087	60.009	1.00	68.31
2050	C	ALA	B	234	32.062	68.334	59.125	1.00	75.66
2051	O	ALA	B	234	30.789	68.666	58.669	1.00	79.35
2052	N	GLN	B	235	32.785	69.152	59.785	1.00	82.05
2053	CA	GLN	B	235	32.111	70.403	60.090	1.00	85.91
2054	CB	GLN	B	235	32.565	70.876	61.676	1.00	84.49
2055	CG	GLN	B	235	33.819	71.201	61.907	1.00	89.12
2056	CD	GLN	B	235	34.175	71.656	63.242	1.00	100.23
2057	OE1	GLN	B	235	35.396	72.090	63.469	1.00	93.13
2058	NE2	GLN	B	235	33.222	71.508	64.165	1.00	96.59
2059	C	GLN	B	235	32.178	71.421	59.033	1.00	83.43
2060	O	GLN	B	235	31.554	72.471	59.051	1.00	82.43
2061	N	LEU	B	236	33.072	71.063	58.122	1.00	91.29
2062	CA	LEU	B	236	33.234	71.793	56.844	1.00	89.72
2063	CB	LEU	B	236	34.558	71.576	56.363	1.00	87.89
2064	CG	LEU	B	236	35.548	72.011	57.426	1.00	95.20
2065	CD1	LEU	B	236	36.945	72.282	56.958	1.00	87.66
2066	CD2	LEU	B	236	35.131	73.303	58.312	1.00	108.16
2067	C	LEU	B	236	32.286	71.245	55.881	1.00	88.08
2068	O	LEU	B	236	31.926	71.960	55.003	1.00	93.63
2069	N	GLN	B	237	31.852	69.992	56.046	1.00	90.20
2070	CA	GLN	B	237	30.803	69.360	55.060	1.00	92.05
2071	CB	GLN	B	237	30.467	67.906	55.468	1.00	90.65
2072	CG	GLN	B	237	29.549	67.046	54.443	1.00	97.30
2073	CD	GLN	B	237	28.369	66.278	55.109	1.00	94.00
2074	OE1	GLN	B	237	28.258	65.037	55.016	1.00	103.21
2075	NE2	GLN	B	237	27.481	66.985	55.761	1.00	97.17
2076	C	GLN	B	237	29.587	70.312	55.242	1.00	90.77
2077	O	GLN	B	237	28.938	70.601	54.263	1.00	91.75
2078	N	ALA	B	238	29.372	70.672	56.527	1.00	86.00
2079	CA	ALA	B	238	28.534	71.693	57.027	1.00	90.09
2080	CB	ALA	B	238	29.561	72.807	57.626	1.00	88.02
2081	C	ALA	B	238	27.354	72.493	56.322	1.00	90.02
2082	O	ALA	B	238	26.284	72.317	56.754	1.00	90.59
2083	N	ALA	B	239	27.518	73.378	55.305	1.00	91.29
2084	CA	ALA	B	239	26.354	74.165	54.825	1.00	94.57
2085	CB	ALA	B	239	26.022	75.307	55.798	1.00	96.72
2086	C	ALA	B	239	26.437	74.827	53.438	1.00	96.93
2087	O	ALA	B	239	27.583	75.241	53.091	1.00	90.16
2088	N	ALA	B	240	25.177	75.029	52.800	1.00	96.92
2089	CA	ALA	B	240	24.941	75.529	51.426	1.00	98.11
2090	CB	ALA	B	240	23.284	75.630	51.054	1.00	99.06
2091	C	ALA	B	240	25.656	76.871	51.061	1.00	100.78
2092	O	ALA	B	240	25.725	77.284	49.807	1.00	100.97
2093	N	ALA	B	242	21.565	79.128	48.299	1.00	106.20
2094	CA	ALA	B	242	20.635	78.973	49.457	1.00	108.35
2095	CB	ALA	B	242	20.497	80.423	50.236	1.00	109.25
2096	C	ALA	B	242	19.265	78.460	49.037	1.00	106.40
2097	O	ALA	B	242	19.203	77.697	48.104	1.00	108.04
2098	N	ALA	B	243	18.207	78.966	49.715	1.00	105.11
2099	CA	ALA	B	243	16.768	78.714	49.496	1.00	101.10
2100	CB	ALA	B	243	16.502	77.309	49.423	1.00	97.27
2101	C	ALA	B	243	16.103	79.335	50.796	1.00	101.77
2102	O	ALA	B	243	16.810	79.916	51.666	1.00	101.06
2103	N	ALA	B	244	14.761	79.338	50.863	1.00	100.84
2104	CA	ALA	B	244	13.907	79.821	51.969	1.00	99.77
2105	CB	ALA	B	244	14.063	78.822	53.233	1.00	100.95
2106	C	ALA	B	244	13.795	81.316	52.457	1.00	101.34
2107	O	ALA	B	244	13.050	82.166	51.858	1.00	100.88
2108	N	ALA	B	245	14.517	81.556	53.593	1.00	102.46
2109	CA	ALA	B	245	14.675	82.740	54.351	1.00	101.68
2110	CB	ALA	B	245	15.956	83.504	53.854	1.00	103.15
2111	C	ALA	B	245	13.282	83.600	54.522	1.00	102.07
2112	O	ALA	B	245	12.242	83.072	55.091	1.00	98.13
2113	N	ALA	B	246	13.313	84.906	54.167	1.00	103.68
2114	CA	ALA	B	246	12.174	85.963	54.354	1.00	106.15
2115	CB	ALA	B	246	11.254	85.604	55.581	1.00	107.17
2116	C	ALA	B	246	12.768	87.336	54.611	1.00	103.67
2117	O	ALA	B	246	13.973	87.382	54.983	1.00	106.48
2118	N	GLN	B	266	6.953	87.068	62.544	1.00	79.67
2119	CA	GLN	B	266	7.541	87.520	61.272	1.00	87.37
2120	CB	GLN	B	266	7.673	89.025	61.102	1.00	88.42
2121	CG	GLN	B	266	6.268	89.732	60.996	1.00	98.96
2122	CD	GLN	B	266	5.890	90.602	62.314	1.00	92.78
2123	OE1	GLN	B	266	5.183	91.529	62.175	1.00	86.17
2124	NE2	GLN	B	266	6.550	90.324	63.519	1.00	92.39
2125	C	GLN	B	266	8.981	87.127	61.449	1.00	87.17
2126	O	GLN	B	266	9.512	86.310	60.885	1.00	83.42
2127	N	ALA	B	267	9.640	87.770	62.327	1.00	91.53
2128	CA	ALA	B	267	11.131	87.476	62.636	1.00	95.36
2129	CB	ALA	B	267	11.605	88.595	63.456	1.00	94.72
2130	C	ALA	B	267	11.491	86.138	63.438	1.00	92.03
2131	O	ALA	B	267	12.383	85.532	63.473	1.00	90.82
2132	N	PHE	B	268	10.539	85.702	64.144	1.00	92.21
2133	CA	PHE	B	268	10.383	84.455	64.990	1.00	86.22
2134	CB	PHE	B	268	9.005	84.449	65.761	1.00	89.59
2135	CG	PHE	B	268	8.833	83.386	66.595	1.00	90.51
2136	CD1	PHE	B	268	9.929	83.048	67.309	1.00	98.22
2137	CE1	PHE	B	268	9.897	81.943	68.142	1.00	93.68
2138	CZ	PHE	B	268	8.822	81.106	68.218	1.00	91.59
2139	CE2	PHE	B	268	7.702	81.414	67.511	1.00	94.27
2140	CD2	PHE	B	268	7.733	82.598	66.642	1.00	87.97
2141	C	PHE	B	268	10.531	83.323	64.071	1.00	84.42
2142	O	PHE	B	268	10.531	82.320	64.553	1.00	85.87
2143	N	ALA	B	269	10.425	83.506	62.776	1.00	82.21
2144	CA	ALA	B	269	10.531	82.387	61.808	1.00	79.55
2145	CB	ALA	B	269	9.447	82.574	60.559	1.00	86.99
2146	C	ALA	B	269	11.777	82.572	61.267	1.00	80.77
2147	O	ALA	B	269	12.488	81.571	60.924	1.00	80.47
2148	N	HIS	B	270	12.177	83.871	61.124	1.00	80.30
2149	CA	HIS	B	270	13.498	84.074	60.549	1.00	81.61
2150	CB	HIS	B	270	13.981	85.474	60.648	1.00	79.26
2151	CG	HIS	B	270	15.397	85.686	60.208	1.00	79.92
2152	ND1	HIS	B	270	15.858	85.338	58.935	1.00	88.96
2153	CE1	HIS	B	270	17.167	85.567	58.854	1.00	89.00
2154	NE2	HIS	B	270	17.547	86.143	59.990	1.00	80.69
2155	CD2	HIS	B	270	16.464	86.261	60.826	1.00	79.78
2156	C	HIS	B	270	14.364	83.169	61.501	1.00	77.66
2157	O	HIS	B	270	15.185	82.332	60.986	1.00	82.44
2158	N	PHE	B	271	14.167	83.269	62.823	1.00	73.18
2159	CA	PHE	B	271	15.350	82.615	63.646	1.00	80.03
2160	CB	PHE	B	271	15.176	83.094	65.106	1.00	77.22
2161	CG	PHE	B	271	16.097	84.140	65.441	1.00	84.35
2162	CD1	PHE	B	271	17.573	83.924	65.446	1.00	84.34
2163	CE1	PHE	B	271	18.374	85.069	65.878	1.00	86.87
2164	CZ	PHE	B	271	17.677	86.291	66.095	1.00	76.68
2165	CE2	PHE	B	271	16.370	86.438	65.851	1.00	77.21
2166	CD2	PHE	B	271	15.582	85.407	65.679	1.00	80.51
2167	C	PHE	B	271	15.250	81.086	63.568	1.00	75.88
2168	O	PHE	B	271	16.151	80.246	63.317	1.00	77.81
2169	N	THR	B	272	13.980	80.823	63.795	1.00	74.79
2170	CA	THR	B	272	13.200	79.536	63.756	1.00	73.99
2171	CB	THR	B	272	11.591	79.623	63.982	1.00	74.69
2172	OG1	THR	B	272	11.267	80.058	65.296	1.00	78.22
2173	CG2	THR	B	272	11.131	78.270	63.971	1.00	82.08
2174	C	THR	B	272	13.424	78.880	62.405	1.00	68.81
2175	O	THR	B	272	13.336	77.663	62.264	1.00	73.54
2176	N	GLU	B	273	13.892	79.676	61.456	1.00	68.43
2177	CA	GLU	B	273	14.180	79.135	60.200	1.00	69.62
2178	CB	GLU	B	273	13.896	80.301	59.176	1.00	73.97
2179	CG	GLU	B	273	12.639	80.045	58.219	1.00	78.18
2180	CD	GLU	B	273	12.078	81.415	57.497	1.00	78.36
2181	OE1	GLU	B	273	11.442	82.220	58.142	1.00	71.56
2182	OE2	GLU	B	273	12.284	81.645	56.297	1.00	74.81
2183	C	GLU	B	273	15.593	78.771	60.181	1.00	66.71
2184	O	GLU	B	273	16.091	77.764	59.765	1.00	64.57
2185	N	LEU	B	274	16.288	79.719	60.680	1.00	65.82
2186	CA	LEU	B	274	17.682	79.427	60.696	1.00	69.97
2187	CB	LEU	B	274	18.459	80.686	61.251	1.00	78.70
2188	CG	LEU	B	274	20.159	80.548	61.290	1.00	71.61
2189	CD1	LEU	B	274	20.909	80.170	59.963	1.00	84.54
2190	CD2	LEU	B	274	20.826	81.824	61.614	1.00	88.89
2191	C	LEU	B	274	18.164	78.304	61.694	1.00	63.14
2192	O	LEU	B	274	19.076	77.590	61.486	1.00	53.88
2193	N	ALA	B	275	17.421	78.053	62.713	1.00	63.35
2194	CA	ALA	B	275	17.751	76.963	63.565	1.00	63.41
2195	CB	ALA	B	275	16.697	77.133	64.830	1.00	61.70
2196	C	ALA	B	275	17.487	75.617	62.756	1.00	65.82
2197	O	ALA	B	275	18.409	74.716	62.871	1.00	59.36
2198	N	ILE	B	276	16.291	75.527	61.979	1.00	60.42
2199	CA	ILE	B	276	15.967	74.404	61.210	1.00	56.65
2200	CB	ILE	B	276	14.585	74.566	60.433	1.00	53.48
2201	CG1	ILE	B	276	13.491	74.529	61.520	1.00	60.73
2202	CD1	ILE	B	276	11.929	74.884	61.183	1.00	73.36
2203	CG2	ILE	B	276	14.351	73.484	59.499	1.00	46.80
2204	C	ILE	B	276	16.994	74.036	60.418	1.00	55.64
2205	O	ILE	B	276	17.098	72.909	60.058	1.00	65.41
2206	N	ILE	B	277	17.822	74.899	59.999	1.00	58.61
2207	CA	ILE	B	277	19.026	74.628	59.151	1.00	54.52
2208	CB	ILE	B	277	19.458	76.021	58.603	1.00	58.00
2209	CG1	ILE	B	277	18.132	76.618	58.041	1.00	58.20
2210	CD1	ILE	B	277	18.060	78.023	58.363	1.00	67.84
2211	CG2	ILE	B	277	20.582	75.792	57.634	1.00	62.11
2212	C	ILE	B	277	20.028	74.087	59.838	1.00	55.62
2213	O	ILE	B	277	20.757	73.255	59.425	1.00	58.46
2214	N	SER	B	278	20.165	74.668	61.119	1.00	55.68
2215	CA	SER	B	278	21.243	74.182	62.080	1.00	54.04
2216	CB	SER	B	278	21.279	74.978	63.347	1.00	61.52
2217	OG	SER	B	278	20.704	76.195	63.076	1.00	73.03
2218	C	SER	B	278	21.197	72.681	62.521	1.00	44.66
2219	O	SER	B	278	21.971	71.913	62.631	1.00	46.18
2220	N	VAL	B	279	19.911	72.306	62.666	1.00	51.44
2221	CA	VAL	B	279	19.498	70.964	63.038	1.00	49.70
2222	CB	VAL	B	279	18.252	70.872	63.069	1.00	56.96
2223	CG1	VAL	B	279	17.285	69.449	63.474	1.00	60.86
2224	CG2	VAL	B	279	17.405	71.876	64.073	1.00	58.26
2225	C	VAL	B	279	19.959	69.973	62.052	1.00	50.33
2226	O	VAL	B	279	20.198	68.818	62.507	1.00	50.44
2227	N	GLN	B	280	20.179	70.355	60.775	1.00	54.00
2228	CA	GLN	B	280	20.766	69.299	59.768	1.00	50.44
2229	CB	GLN	B	280	20.317	69.830	58.243	1.00	58.81
2230	CG	GLN	B	280	21.341	68.972	57.208	1.00	52.24
2231	CD	GLN	B	280	20.545	67.504	57.051	1.00	60.94
2232	OE1	GLN	B	280	19.444	67.460	56.472	1.00	79.31
2233	NE2	GLN	B	280	21.147	66.474	57.368	1.00	47.82
2234	C	GLN	B	280	22.137	69.264	59.730	1.00	55.32
2235	O	GLN	B	280	22.877	68.086	59.623	1.00	54.41
2236	N	GLU	B	281	22.822	70.548	59.851	1.00	57.18
2237	CA	GLU	B	281	24.342	70.372	59.794	1.00	51.39
2238	CB	GLU	B	281	24.689	71.870	59.981	1.00	60.52
2239	CG	GLU	B	281	23.537	72.847	59.755	1.00	65.49
2240	CD	GLU	B	281	23.967	74.410	60.323	1.00	81.25
2241	OE1	GLU	B	281	24.406	74.654	61.490	1.00	76.30
2242	OE2	GLU	B	281	23.880	75.392	59.525	1.00	73.76
2243	C	GLU	B	281	24.651	69.620	60.970	1.00	48.92
2244	O	GLU	B	281	25.664	69.008	61.028	1.00	56.76
2245	N	ILE	B	282	23.794	69.627	62.092	1.00	52.05
2246	CA	ILE	B	282	24.445	68.874	63.277	1.00	57.49
2247	CB	ILE	B	282	23.393	69.292	64.536	1.00	54.00
2248	CG1	ILE	B	282	23.998	70.716	65.057	1.00	54.53
2249	CD1	ILE	B	282	23.111	71.419	65.835	1.00	49.35
2250	CG2	ILE	B	282	23.495	68.340	65.377	1.00	45.45
2251	C	ILE	B	282	24.212	67.317	63.085	1.00	54.21
2252	O	ILE	B	282	25.343	66.575	63.214	1.00	53.24
2253	N	VAL	B	283	23.089	66.821	62.692	1.00	50.83
2254	CA	VAL	B	283	22.999	65.423	62.436	1.00	56.24
2255	CB	VAL	B	283	21.731	65.072	61.917	1.00	58.66
2256	CG1	VAL	B	283	21.849	63.626	61.445	1.00	54.04
2257	CG2	VAL	B	283	20.315	65.468	62.959	1.00	50.38
2258	C	VAL	B	283	23.943	64.939	61.410	1.00	56.20
2259	O	VAL	B	283	24.523	63.848	61.557	1.00	51.77
2260	N	ASP	B	284	24.292	65.778	60.472	1.00	55.22
2261	CA	ASP	B	284	25.346	65.211	59.571	1.00	64.25
2262	CB	ASP	B	284	25.303	65.906	58.091	1.00	68.50
2263	CG	ASP	B	284	24.065	65.417	57.282	1.00	68.12
2264	OD1	ASP	B	284	23.881	64.122	57.296	1.00	67.53
2265	OD2	ASP	B	284	23.246	66.294	56.739	1.00	68.04
2266	C	ASP	B	284	26.612	65.167	60.047	1.00	63.92
2267	O	ASP	B	284	27.455	64.571	59.436	1.00	62.17
2268	N	PHE	B	285	26.849	66.018	61.097	1.00	64.71
2269	CA	PHE	B	285	28.289	65.938	61.652	1.00	61.65
2270	CB	PHE	B	285	28.516	67.217	62.474	1.00	63.46
2271	CG	PHE	B	285	29.633	67.192	63.322	1.00	57.88
2272	CD1	PHE	B	285	30.710	67.208	62.677	1.00	62.04
2273	CE1	PHE	B	285	32.294	67.127	63.392	1.00	65.42
2274	CZ	PHE	B	285	32.081	67.078	64.810	1.00	70.04
2275	CE2	PHE	B	285	30.787	67.037	65.384	1.00	55.03
2276	CD2	PHE	B	285	29.605	67.142	64.725	1.00	57.34
2277	C	PHE	B	285	28.250	64.787	62.666	1.00	57.92
2278	O	PHE	B	285	29.264	64.083	62.806	1.00	54.29
2279	N	ALA	B	286	26.974	64.544	63.356	1.00	62.27
2280	CA	ALA	B	286	27.063	63.462	64.418	1.00	56.88
2281	CB	ALA	B	286	25.756	63.582	65.092	1.00	55.00
2282	C	ALA	B	286	27.280	62.110	63.683	1.00	59.47
2283	O	ALA	B	286	28.273	61.334	64.050	1.00	59.93
2284	N	LYS	B	287	26.493	61.853	62.624	1.00	62.20
2285	CA	LYS	B	287	26.665	60.564	61.794	1.00	63.29
2286	CB	LYS	B	287	25.771	60.724	60.554	1.00	55.81
2287	CG	LYS	B	287	24.319	60.987	60.852	1.00	56.80
2288	CD	LYS	B	287	23.359	61.386	59.489	1.00	70.39
2289	CE	LYS	B	287	23.158	60.140	58.561	1.00	61.74
2290	NZ	LYS	B	287	22.811	60.223	57.189	1.00	60.01
2291	C	LYS	B	287	28.031	60.319	61.490	1.00	59.19
2292	O	LYS	B	287	28.487	59.291	61.648	1.00	57.30
2293	N	GLN	B	288	28.792	61.327	61.254	1.00	57.51
2294	CA	GLN	B	288	30.344	61.122	61.058	1.00	57.22
2295	CB	GLN	B	288	30.812	62.429	60.049	1.00	61.51
2296	CG	GLN	B	288	31.229	62.044	58.542	1.00	62.61
2297	CD	GLN	B	288	32.406	61.121	58.469	1.00	76.06
2298	OE1	GLN	B	288	32.202	59.789	58.161	1.00	70.64
2299	NE2	GLN	B	288	33.658	61.690	58.793	1.00	68.17
2300	C	GLN	B	288	31.051	61.018	62.019	1.00	54.37
2301	O	GLN	B	288	32.337	61.108	61.886	1.00	61.46
2302	N	VAL	B	289	30.419	61.010	63.190	1.00	61.78
2303	CA	VAL	B	289	31.531	60.817	64.348	1.00	58.20
2304	CB	VAL	B	289	30.984	61.685	65.746	1.00	63.17
2305	CG1	VAL	B	289	32.033	61.537	66.877	1.00	56.94
2306	CG2	VAL	B	289	30.675	63.103	65.519	1.00	53.71
2307	C	VAL	B	289	31.872	59.511	64.637	1.00	56.27
2308	O	VAL	B	289	31.115	58.717	64.937	1.00	67.55
2309	N	PRO	B	290	33.036	59.135	64.777	1.00	61.39
2310	CA	PRO	B	290	33.490	57.792	65.097	1.00	60.40
2311	CB	PRO	B	290	34.896	57.881	65.238	1.00	59.76
2312	CG	PRO	B	290	35.259	59.069	64.376	1.00	57.41
2313	CD	PRO	B	290	34.169	59.982	64.687	1.00	65.61
2314	C	PRO	B	290	32.877	57.106	66.282	1.00	62.07
2315	O	PRO	B	290	33.543	57.041	67.400	1.00	63.88
2316	N	GLY	B	291	31.787	56.458	66.045	1.00	53.48
2317	CA	GLY	B	291	31.118	55.692	67.264	1.00	52.08
2318	C	GLY	B	291	29.629	55.988	67.409	1.00	47.37
2319	O	GLY	B	291	28.827	55.279	67.830	1.00	47.64
2320	N	PHE	B	292	29.260	57.143	66.788	1.00	46.97
2321	CA	PHE	B	292	27.961	57.485	66.870	1.00	48.61
2322	CB	PHE	B	292	27.816	58.865	66.348	1.00	44.81
2323	CG	PHE	B	292	26.433	59.424	66.587	1.00	44.19
2324	CD1	PHE	B	292	26.050	59.806	67.863	1.00	42.15
2325	CE1	PHE	B	292	24.867	60.284	68.073	1.00	36.36
2326	CZ	PHE	B	292	23.924	60.297	67.124	1.00	41.35
2327	CE2	PHE	B	292	24.222	59.911	65.844	1.00	44.46
2328	CD2	PHE	B	292	25.541	59.565	65.559	1.00	42.70
2329	C	PHE	B	292	26.955	56.514	66.316	1.00	56.70
2330	O	PHE	B	292	25.969	56.113	67.050	1.00	56.57
2331	N	LEU	B	293	27.131	56.163	64.973	1.00	53.68
2332	CA	LEU	B	293	26.241	55.342	64.318	1.00	53.58
2333	CB	LEU	B	293	26.435	55.479	62.811	1.00	49.24
2334	CG	LEU	B	293	25.992	56.784	62.295	1.00	53.64
2335	CD1	LEU	B	293	26.253	56.997	60.850	1.00	53.77
2336	CD2	LEU	B	293	24.184	56.923	62.401	1.00	48.39
2337	C	LEU	B	293	26.103	53.878	64.768	1.00	52.40
2338	O	LEU	B	293	25.204	53.115	64.277	1.00	52.95
2339	N	GLN	B	294	27.063	53.528	65.590	1.00	54.66
2340	CA	GLN	B	294	27.133	52.177	66.240	1.00	58.82
2341	CB	GLN	B	294	28.534	51.766	66.446	1.00	55.99
2342	CG	GLN	B	294	29.381	52.586	65.434	1.00	61.48
2343	CD	GLN	B	294	30.925	52.325	65.623	1.00	74.17
2344	OE1	GLN	B	294	31.319	51.724	66.545	1.00	75.85
2345	NE2	GLN	B	294	31.784	52.888	64.776	1.00	69.33
2346	C	GLN	B	294	26.389	52.057	67.524	1.00	58.14
2347	O	GLN	B	294	26.326	51.003	68.038	1.00	61.97
2348	N	LEU	B	295	25.691	53.044	67.947	1.00	56.46
2349	CA	LEU	B	295	25.025	52.982	69.224	1.00	61.54
2350	CB	LEU	B	295	24.900	54.500	69.876	1.00	55.24
2351	CG	LEU	B	295	26.176	55.068	70.533	1.00	50.71
2352	CD1	LEU	B	295	26.052	56.510	70.987	1.00	36.73
2353	CD2	LEU	B	295	26.341	54.250	71.781	1.00	48.13
2354	C	LEU	B	295	23.605	52.533	68.800	1.00	60.78
2355	O	LEU	B	295	23.213	52.803	67.636	1.00	59.88
2356	N	GLY	B	296	22.742	52.176	69.774	1.00	59.07
2357	CA	GLY	B	296	21.359	51.909	69.435	1.00	55.12
2358	C	GLY	B	296	20.749	53.114	68.818	1.00	62.84
2359	O	GLY	B	296	21.137	54.384	69.095	1.00	60.06
2360	N	ARG	B	297	19.716	52.882	67.977	1.00	63.08
2361	CA	ARG	B	297	19.063	54.044	67.321	1.00	62.49
2362	CB	ARG	B	297	17.986	53.603	66.339	1.00	55.91
2363	CG	ARG	B	297	16.766	54.303	66.499	1.00	61.42
2364	CD	ARG	B	297	15.836	54.353	65.183	1.00	66.08
2365	NE	ARG	B	297	16.781	54.841	64.113	1.00	83.98
2366	CZ	ARG	B	297	16.394	55.084	62.853	1.00	76.13
2367	NH1	ARG	B	297	15.378	54.775	62.444	1.00	84.00
2368	NH2	ARG	B	297	17.227	55.522	61.910	1.00	68.07
2369	C	ARG	B	297	18.499	54.957	68.436	1.00	61.26
2370	O	ARG	B	297	18.481	56.167	68.385	1.00	63.34
2371	N	GLU	B	298	18.073	54.391	69.440	1.00	58.48
2372	CA	GLU	B	298	17.405	55.199	70.428	1.00	62.30
2373	CB	GLU	B	298	16.647	54.195	71.537	1.00	57.17
2374	CG	GLU	B	298	15.169	54.174	71.324	1.00	67.57
2375	CD	GLU	B	298	14.832	53.500	69.965	1.00	80.94
2376	OE1	GLU	B	298	15.469	52.375	69.667	1.00	84.64
2377	OE2	GLU	B	298	14.023	54.023	69.092	1.00	81.00
2378	C	GLU	B	298	18.476	56.177	71.163	1.00	51.80
2379	O	GLU	B	298	18.051	57.151	71.560	1.00	49.60
2380	N	ASP	B	299	19.539	55.564	71.522	1.00	47.86
2381	CA	ASP	B	299	20.497	56.312	72.187	1.00	51.84
2382	CB	ASP	B	299	21.629	55.407	72.765	1.00	45.01
2383	CG	ASP	B	299	21.158	54.667	73.927	1.00	44.83
2384	OD1	ASP	B	299	20.149	55.035	74.559	1.00	45.60
2385	OD2	ASP	B	299	21.877	53.829	74.379	1.00	48.45
2386	C	ASP	B	299	21.047	57.463	71.272	1.00	52.94
2387	O	ASP	B	299	21.683	58.425	71.778	1.00	52.05
2388	N	GLN	B	300	20.901	57.196	69.969	1.00	50.18
2389	CA	GLN	B	300	21.413	58.153	68.979	1.00	55.61
2390	CB	GLN	B	300	21.591	57.640	67.491	1.00	52.76
2391	CG	GLN	B	300	22.617	56.690	67.374	1.00	55.34
2392	CD	GLN	B	300	22.653	56.046	65.932	1.00	63.28
2393	OE1	GLN	B	300	23.422	55.074	65.703	1.00	52.87
2394	NE2	GLN	B	300	21.958	56.692	65.000	1.00	60.94
2395	C	GLN	B	300	20.536	59.360	68.892	1.00	51.50
2396	O	GLN	B	300	21.095	60.490	69.012	1.00	53.21
2397	N	ILE	B	301	19.309	59.133	69.107	1.00	43.21
2398	CA	ILE	B	301	18.474	60.115	69.204	1.00	44.82
2399	CB	ILE	B	301	16.916	59.617	68.821	1.00	44.76
2400	CG1	ILE	B	301	15.936	60.581	69.007	1.00	41.61
2401	CD1	ILE	B	301	14.749	60.228	69.501	1.00	46.97
2402	CG2	ILE	B	301	16.727	58.642	69.732	1.00	50.79
2403	C	ILE	B	301	18.420	60.868	70.494	1.00	41.63
2404	O	ILE	B	301	18.064	62.079	70.638	1.00	35.91
2405	N	ALA	B	302	18.534	60.080	71.496	1.00	39.00
2406	CA	ALA	B	302	18.488	60.611	72.876	1.00	38.93
2407	CB	ALA	B	302	18.648	59.533	73.816	1.00	44.04
2408	C	ALA	B	302	19.757	61.609	73.031	1.00	39.30
2409	O	ALA	B	302	19.483	62.764	73.349	1.00	39.22
2410	N	LEU	B	303	20.888	61.185	72.606	1.00	38.64
2411	CA	LEU	B	303	22.029	61.991	72.654	1.00	45.39
2412	CB	LEU	B	303	23.367	61.219	72.213	1.00	42.55
2413	CG	LEU	B	303	23.701	60.032	73.096	1.00	37.97
2414	CD1	LEU	B	303	25.083	59.516	72.592	1.00	28.68
2415	CD2	LEU	B	303	23.953	60.625	74.516	1.00	29.84
2416	C	LEU	B	303	21.996	63.289	71.725	1.00	45.65
2417	O	LEU	B	303	22.299	64.460	72.187	1.00	40.78
2418	N	LEU	B	304	21.471	63.118	70.525	1.00	43.87
2419	CA	LEU	B	304	21.340	64.276	69.612	1.00	40.36
2420	CB	LEU	B	304	21.053	63.778	68.207	1.00	40.77
2421	CG	LEU	B	304	21.675	64.382	67.012	1.00	40.36
2422	CD1	LEU	B	304	23.281	64.959	67.303	1.00	54.16
2423	CD2	LEU	B	304	21.898	63.180	66.176	1.00	42.16
2424	C	LEU	B	304	20.229	65.320	70.153	1.00	38.75
2425	O	LEU	B	304	20.437	66.483	70.014	1.00	36.35
2426	N	LYS	B	305	19.163	64.828	70.594	1.00	37.85
2427	CA	LYS	B	305	18.097	65.705	71.029	1.00	45.89
2428	CB	LYS	B	305	16.814	64.982	71.652	1.00	44.35
2429	CG	LYS	B	305	15.700	64.899	70.682	1.00	61.08
2430	CD	LYS	B	305	14.407	64.197	71.605	1.00	60.08
2431	CE	LYS	B	305	13.300	64.282	70.594	1.00	64.90
2432	NZ	LYS	B	305	12.007	63.803	71.012	1.00	69.57
2433	C	LYS	B	305	18.599	66.663	72.127	1.00	46.48
2434	O	LYS	B	305	18.021	67.794	72.370	1.00	42.93
2435	N	ALA	B	306	19.386	66.009	73.098	1.00	44.50
2436	CA	ALA	B	306	19.806	66.844	74.329	1.00	40.48
2437	CB	ALA	B	306	20.225	65.957	75.470	1.00	40.95
2438	C	ALA	B	306	20.937	67.763	73.946	1.00	42.42
2439	O	ALA	B	306	21.034	68.874	74.591	1.00	41.21
2440	N	SER	B	307	21.821	67.339	72.987	1.00	38.22
2441	CA	SER	B	307	22.925	68.166	72.715	1.00	43.23
2442	CB	SER	B	307	24.204	67.314	72.686	1.00	42.01
2443	OG	SER	B	307	24.360	66.547	71.741	1.00	42.17
2444	C	SER	B	307	22.856	69.187	71.561	1.00	44.87
2445	O	SER	B	307	23.725	69.994	71.374	1.00	42.46
2446	N	THR	B	308	21.653	69.113	70.911	1.00	45.36
2447	CA	THR	B	308	21.517	69.993	69.685	1.00	45.53
2448	CB	THR	B	308	19.923	69.707	69.135	1.00	48.08
2449	OG1	THR	B	308	20.273	68.570	68.313	1.00	48.56
2450	CG2	THR	B	308	19.445	70.978	68.212	1.00	43.38
2451	C	THR	B	308	21.632	71.579	70.125	1.00	39.58
2452	O	THR	B	308	22.534	72.152	69.585	1.00	38.96
2453	N	ILE	B	309	20.758	72.042	70.902	1.00	39.26
2454	CA	ILE	B	309	20.846	73.393	71.489	1.00	37.98
2455	CB	ILE	B	309	19.882	73.642	72.397	1.00	37.29
2456	CG1	ILE	B	309	19.695	75.107	72.719	1.00	42.58
2457	CD1	ILE	B	309	19.585	75.887	71.264	1.00	48.19
2458	CG2	ILE	B	309	19.977	72.945	73.613	1.00	41.10
2459	C	ILE	B	309	22.088	73.772	72.134	1.00	41.77
2460	O	ILE	B	309	22.443	74.978	72.097	1.00	39.52
2461	N	GLU	B	310	22.977	72.761	72.526	1.00	37.45
2462	CA	GLU	B	310	24.210	73.186	73.072	1.00	39.85
2463	CB	GLU	B	310	24.799	72.120	74.300	1.00	31.33
2464	CG	GLU	B	310	23.692	71.853	75.284	1.00	33.40
2465	CD	GLU	B	310	24.089	70.879	76.384	1.00	26.27
2466	OE1	GLU	B	310	23.256	70.555	77.138	1.00	32.27
2467	OE2	GLU	B	310	25.214	70.462	76.402	1.00	33.68
2468	C	GLU	B	310	25.093	73.360	72.066	1.00	40.80
2469	O	GLU	B	310	26.168	74.152	72.192	1.00	42.61
2470	N	ILE	B	311	25.157	72.387	71.084	1.00	40.99
2471	CA	ILE	B	311	26.170	72.590	69.923	1.00	36.36
2472	CB	ILE	B	311	26.066	71.421	69.009	1.00	42.14
2473	CG1	ILE	B	311	26.191	70.196	69.587	1.00	39.35
2474	CD1	ILE	B	311	25.826	68.938	68.734	1.00	41.03
2475	CG2	ILE	B	311	27.183	71.480	67.817	1.00	43.34
2476	C	ILE	B	311	25.828	73.940	69.187	1.00	37.43
2477	O	ILE	B	311	26.810	74.547	68.730	1.00	41.57
2478	N	MET	B	312	24.620	74.369	69.197	1.00	35.81
2479	CA	MET	B	312	24.241	75.538	68.627	1.00	48.06
2480	CB	MET	B	312	22.632	75.799	68.411	1.00	50.08
2481	CG	MET	B	312	22.017	74.785	67.347	1.00	40.55
2482	SD	MET	B	312	20.256	75.219	67.641	1.00	56.76
2483	CE	MET	B	312	19.709	73.976	68.035	1.00	60.29
2484	C	MET	B	312	24.596	76.870	69.414	1.00	50.66
2485	O	MET	B	312	24.526	77.956	68.867	1.00	45.83
2486	N	LEU	B	313	24.690	76.736	70.718	1.00	44.93
2487	CA	LEU	B	313	25.178	77.734	71.666	1.00	41.55
2488	CB	LEU	B	313	24.975	77.413	73.033	1.00	29.22
2489	CG	LEU	B	313	23.619	77.798	73.316	1.00	32.64
2490	CD1	LEU	B	313	22.989	77.020	74.564	1.00	39.23
2491	CD2	LEU	B	313	23.443	79.305	73.363	1.00	30.06
2492	C	LEU	B	313	26.632	77.770	71.384	1.00	41.42
2493	O	LEU	B	313	27.115	78.864	71.203	1.00	39.31
2494	N	LEU	B	314	27.252	76.599	71.047	1.00	41.28
2495	CA	LEU	B	314	28.694	76.475	70.777	1.00	40.18
2496	CB	LEU	B	314	29.168	75.185	70.928	1.00	37.72
2497	CG	LEU	B	314	29.743	74.653	72.251	1.00	45.82
2498	CD1	LEU	B	314	30.190	73.124	72.172	1.00	36.99
2499	CD2	LEU	B	314	31.042	75.397	72.663	1.00	43.47
2500	C	LEU	B	314	29.115	77.121	69.392	1.00	54.06
2501	O	LEU	B	314	30.241	77.751	69.180	1.00	49.68
2502	N	GLU	B	315	28.345	76.790	68.346	1.00	60.26
2503	CA	GLU	B	315	28.711	77.225	66.958	1.00	57.22
2504	CB	GLU	B	315	27.789	76.349	65.926	1.00	54.82
2505	CG	GLU	B	315	28.473	74.937	65.578	1.00	47.55
2506	CD	GLU	B	315	29.959	75.061	65.018	1.00	66.56
2507	OE1	GLU	B	315	30.378	76.107	64.386	1.00	71.34
2508	OE2	GLU	B	315	30.873	74.212	65.250	1.00	66.80
2509	C	GLU	B	315	28.218	78.738	66.962	1.00	57.50
2510	O	GLU	B	315	28.795	79.532	66.191	1.00	59.15
2511	N	THR	B	316	27.217	79.105	67.678	1.00	52.78
2512	CA	THR	B	316	26.838	80.531	67.733	1.00	51.20
2513	CB	THR	B	316	25.834	80.898	68.717	1.00	57.50
2514	OG1	THR	B	316	24.441	80.632	68.221	1.00	64.56
2515	CG2	THR	B	316	25.756	82.238	69.198	1.00	52.91
2516	C	THR	B	316	27.989	81.288	68.430	1.00	57.95
2517	O	THR	B	316	28.623	82.231	67.837	1.00	61.85
2518	N	ALA	B	317	28.578	80.706	69.411	1.00	57.22
2519	CA	ALA	B	317	29.641	81.279	70.058	1.00	63.28
2520	CB	ALA	B	317	30.121	80.592	71.332	1.00	55.94
2521	C	ALA	B	317	30.798	81.416	69.076	1.00	62.31
2522	O	ALA	B	317	31.564	82.528	69.007	1.00	67.15
2523	N	ARG	B	318	31.047	80.390	68.426	1.00	61.09
2524	CA	ARG	B	318	32.295	80.537	67.603	1.00	63.74
2525	CB	ARG	B	318	32.730	79.203	67.163	1.00	64.66
2526	CG	ARG	B	318	32.441	78.894	65.959	1.00	66.74
2527	CD	ARG	B	318	33.501	77.925	65.208	1.00	70.68
2528	NE	ARG	B	318	32.930	76.486	64.841	1.00	71.26
2529	CZ	ARG	B	318	33.768	75.499	64.497	1.00	67.45
2530	NH1	ARG	B	318	34.890	75.807	64.276	1.00	67.59
2531	NH2	ARG	B	318	33.505	74.292	64.199	1.00	77.12
2532	C	ARG	B	318	32.073	81.428	66.369	1.00	64.55
2533	O	ARG	B	318	33.008	81.604	65.611	1.00	63.09
2534	N	ARG	B	319	30.860	82.095	66.351	1.00	59.57
2535	CA	ARG	B	319	30.765	82.999	65.160	1.00	68.49
2536	CB	ARG	B	319	29.473	82.521	64.326	1.00	61.30
2537	CG	ARG	B	319	30.060	81.853	63.067	1.00	69.41
2538	CD	ARG	B	319	29.235	80.581	62.763	1.00	73.24
2539	NE	ARG	B	319	30.175	79.647	62.098	1.00	75.10
2540	CZ	ARG	B	319	29.984	78.369	62.112	1.00	79.76
2541	NH1	ARG	B	319	28.933	77.857	62.748	1.00	73.63
2542	NH2	ARG	B	319	30.844	77.583	61.539	1.00	68.15
2543	C	ARG	B	319	30.514	84.508	65.637	1.00	65.44
2544	O	ARG	B	319	29.829	85.398	64.966	1.00	61.07
2545	N	TYR	B	320	30.987	84.701	66.895	1.00	63.21
2546	CA	TYR	B	320	30.819	85.999	67.487	1.00	61.59
2547	CB	TYR	B	320	30.775	85.901	68.977	1.00	58.07
2548	CG	TYR	B	320	30.812	87.230	69.711	1.00	53.02
2549	CD1	TYR	B	320	31.930	87.725	70.264	1.00	54.55
2550	CE1	TYR	B	320	31.836	88.964	70.950	1.00	53.67
2551	CZ	TYR	B	320	30.717	89.582	71.153	1.00	53.87
2552	OH	TYR	B	320	30.609	90.785	71.918	1.00	54.97
2553	CE2	TYR	B	320	29.522	88.994	70.707	1.00	56.50
2554	CD2	TYR	B	320	29.645	87.868	69.986	1.00	58.99
2555	C	TYR	B	320	31.899	86.832	67.011	1.00	55.23
2556	O	TYR	B	320	32.878	86.389	66.887	1.00	58.77
2557	N	ASN	B	321	31.580	88.000	66.684	1.00	65.16
2558	CA	ASN	B	321	32.583	89.035	66.203	1.00	67.00
2559	CB	ASN	B	321	31.783	89.909	65.073	1.00	65.00
2560	CG	ASN	B	321	32.836	90.583	64.077	1.00	68.86
2561	OD1	ASN	B	321	32.218	91.221	63.132	1.00	76.03
2562	ND2	ASN	B	321	34.315	90.514	64.302	1.00	56.08
2563	C	ASN	B	321	32.879	89.996	67.279	1.00	60.46
2564	O	ASN	B	321	31.942	90.604	67.867	1.00	65.67
2565	N	HIS	B	322	34.074	90.206	67.470	1.00	68.48
2566	CA	HIS	B	322	34.486	91.228	68.587	1.00	73.34
2567	CB	HIS	B	322	35.894	90.991	69.233	1.00	71.05
2568	CG	HIS	B	322	35.890	91.351	70.731	1.00	82.08
2569	ND1	HIS	B	322	34.747	91.147	71.589	1.00	87.14
2570	CE1	HIS	B	322	35.017	91.506	72.853	1.00	73.65
2571	NE2	HIS	B	322	36.326	91.869	72.867	1.00	80.65
2572	CD2	HIS	B	322	36.862	91.841	71.558	1.00	72.77
2573	C	HIS	B	322	34.164	92.768	68.375	1.00	66.40
2574	O	HIS	B	322	33.837	93.373	69.334	1.00	67.21
2575	N	GLU	B	323	34.174	93.291	67.174	1.00	71.21
2576	CA	GLU	B	323	33.707	94.564	67.212	1.00	77.68
2577	CB	GLU	B	323	34.541	95.721	66.906	1.00	80.99
2578	CG	GLU	B	323	34.254	96.831	68.101	1.00	81.52
2579	CD	GLU	B	323	34.486	98.300	67.726	1.00	90.73
2580	OE1	GLU	B	323	35.475	98.510	66.917	1.00	102.87
2581	OE2	GLU	B	323	33.744	99.246	68.246	1.00	91.80
2582	C	GLU	B	323	32.281	94.831	66.835	1.00	79.43
2583	O	GLU	B	323	31.626	95.785	67.535	1.00	80.47
2584	N	THR	B	324	31.741	93.954	65.982	1.00	72.14
2585	CA	THR	B	324	30.345	94.187	65.612	1.00	69.64
2586	CB	THR	B	324	29.930	93.339	64.552	1.00	67.93
2587	OG1	THR	B	324	30.970	92.349	64.445	1.00	79.89
2588	CG2	THR	B	324	30.008	94.074	63.113	1.00	72.90
2589	C	THR	B	324	29.613	93.736	66.704	1.00	71.35
2590	O	THR	B	324	28.393	93.991	66.829	1.00	70.48
2591	N	GLU	B	325	30.336	92.943	67.540	1.00	73.92
2592	CA	GLU	B	325	29.628	92.339	68.693	1.00	75.54
2593	CB	GLU	B	325	29.186	93.383	69.839	1.00	71.78
2594	CG	GLU	B	325	30.258	94.467	69.915	1.00	78.66
2595	CD	GLU	B	325	30.335	95.091	71.351	1.00	77.65
2596	OE1	GLU	B	325	29.404	95.606	71.855	1.00	79.58
2597	OE2	GLU	B	325	31.348	94.845	72.040	1.00	82.11
2598	C	GLU	B	325	28.260	91.603	68.082	1.00	70.73
2599	O	GLU	B	325	27.097	91.742	68.635	1.00	66.33
2600	N	CYS	B	326	28.494	91.022	66.965	1.00	64.52
2601	CA	CYS	B	326	27.337	90.359	66.312	1.00	67.07
2602	CB	CYS	B	326	26.830	91.209	64.945	1.00	74.74
2603	SG	CYS	B	326	25.854	92.706	65.368	1.00	68.93
2604	C	CYS	B	326	27.664	88.903	65.914	1.00	62.47
2605	O	CYS	B	326	28.803	88.540	65.629	1.00	61.32
2606	N	ILE	B	327	26.596	88.125	65.896	1.00	62.77
2607	CA	ILE	B	327	26.825	86.679	65.506	1.00	65.69
2608	CB	ILE	B	327	25.734	85.833	66.108	1.00	62.81
2609	CG1	ILE	B	327	25.699	85.979	67.621	1.00	57.04
2610	CD1	ILE	B	327	27.160	85.753	68.002	1.00	57.90
2611	CG2	ILE	B	327	25.925	84.543	65.811	1.00	56.79
2612	C	ILE	B	327	26.814	86.560	63.980	1.00	70.85
2613	O	ILE	B	327	25.808	87.044	63.339	1.00	68.43
2614	N	THR	B	328	27.826	85.849	63.444	1.00	74.31
2615	CA	THR	B	328	27.862	85.617	62.027	1.00	77.88
2616	CB	THR	B	328	29.079	85.878	61.499	1.00	76.18
2617	OG1	THR	B	328	29.054	86.699	60.193	1.00	87.07
2618	CG2	THR	B	328	29.651	84.611	61.306	1.00	69.42
2619	C	THR	B	328	27.538	84.230	61.518	1.00	86.32
2620	O	THR	B	328	27.848	83.224	62.152	1.00	88.10
2621	N	PHE	B	329	26.775	84.166	60.411	1.00	91.72
2622	CA	PHE	B	329	26.452	82.823	59.890	1.00	96.31
2623	CB	PHE	B	329	24.995	82.831	59.432	1.00	96.03
2624	CG	PHE	B	329	24.811	83.479	58.144	1.00	96.98
2625	CD1	PHE	B	329	24.808	82.750	56.887	1.00	108.83
2626	CE1	PHE	B	329	24.702	83.429	55.570	1.00	111.72
2627	CZ	PHE	B	329	24.650	84.895	55.544	1.00	114.57
2628	CE2	PHE	B	329	24.715	85.558	56.851	1.00	113.77
2629	CD2	PHE	B	329	24.787	84.778	58.122	1.00	98.68
2630	C	PHE	B	329	27.463	82.596	58.771	1.00	97.95
2631	O	PHE	B	329	28.091	81.513	58.593	1.00	102.22
2632	N	LEU	B	330	27.801	83.692	58.122	1.00	99.46
2633	CA	LEU	B	330	28.763	83.609	57.048	1.00	99.12
2634	CB	LEU	B	330	28.448	82.496	56.112	1.00	98.10
2635	CG	LEU	B	330	29.481	82.278	54.984	1.00	102.41
2636	CD1	LEU	B	330	31.027	82.287	55.382	1.00	100.19
2637	CD2	LEU	B	330	29.081	80.857	54.343	1.00	112.83
2638	C	LEU	B	330	28.849	84.952	56.309	1.00	99.47
2639	O	LEU	B	330	29.974	85.384	56.049	1.00	103.83
2640	N	LYS	B	331	27.744	85.613	55.952	1.00	96.96
2641	CA	LYS	B	331	27.831	86.934	55.298	1.00	98.37
2642	CB	LYS	B	331	27.268	86.980	53.911	1.00	102.58
2643	CG	LYS	B	331	28.113	86.052	52.923	1.00	107.93
2644	CD	LYS	B	331	27.036	85.406	51.700	1.00	105.27
2645	CE	LYS	B	331	27.842	84.412	50.674	1.00	106.60
2646	NZ	LYS	B	331	27.126	83.719	49.532	1.00	87.77
2647	C	LYS	B	331	27.040	87.899	55.991	1.00	97.46
2648	O	LYS	B	331	26.720	87.723	57.162	1.00	100.77
2649	N	ASP	B	332	26.673	88.950	55.315	1.00	95.42
2650	CA	ASP	B	332	25.895	89.988	55.948	1.00	95.39
2651	CB	ASP	B	332	25.240	90.915	54.941	1.00	99.84
2652	CG	ASP	B	332	26.248	92.060	54.549	1.00	106.41
2653	OD1	ASP	B	332	26.148	92.556	53.387	1.00	115.62
2654	OD2	ASP	B	332	27.234	92.504	55.365	1.00	109.27
2655	C	ASP	B	332	24.930	89.807	57.002	1.00	93.78
2656	O	ASP	B	332	24.788	90.634	57.997	1.00	93.30
2657	N	PHE	B	333	24.205	88.751	56.815	1.00	92.59
2658	CA	PHE	B	333	23.288	88.392	57.908	1.00	93.01
2659	CB	PHE	B	333	22.366	87.298	57.381	1.00	93.27
2660	CG	PHE	B	333	21.276	87.850	56.476	1.00	100.71
2661	CD1	PHE	B	333	21.676	88.659	55.313	1.00	104.96
2662	CE1	PHE	B	333	20.671	89.353	54.480	1.00	103.05
2663	CZ	PHE	B	333	19.148	89.224	54.829	1.00	107.06
2664	CE2	PHE	B	333	18.761	88.347	56.090	1.00	110.04
2665	CD2	PHE	B	333	19.842	87.733	56.870	1.00	102.86
2666	C	PHE	B	333	23.996	88.040	59.385	1.00	90.88
2667	O	PHE	B	333	24.298	86.882	59.697	1.00	90.25
2668	N	THR	B	334	24.154	89.078	60.185	1.00	84.40
2669	CA	THR	B	334	24.695	89.099	61.408	1.00	83.07
2670	CB	THR	B	334	26.005	89.869	61.294	1.00	83.97
2671	OG1	THR	B	334	26.424	89.498	60.004	1.00	83.93
2672	CG2	THR	B	334	27.211	89.293	62.280	1.00	86.33
2673	C	THR	B	334	23.728	89.756	62.294	1.00	82.45
2674	O	THR	B	334	22.728	90.575	61.957	1.00	80.83
2675	N	TYR	B	335	23.975	89.349	63.551	1.00	75.81
2676	CA	TYR	B	335	22.942	89.947	64.572	1.00	75.00
2677	CB	TYR	B	335	21.682	89.016	64.794	1.00	74.93
2678	CG	TYR	B	335	21.364	88.123	63.677	1.00	78.20
2679	CD1	TYR	B	335	22.187	87.145	63.030	1.00	77.22
2680	CE1	TYR	B	335	21.444	86.449	61.924	1.00	77.92
2681	CZ	TYR	B	335	20.199	86.781	61.452	1.00	70.57
2682	OH	TYR	B	335	19.742	86.051	60.284	1.00	87.36
2683	CE2	TYR	B	335	19.531	87.679	62.108	1.00	89.00
2684	CD2	TYR	B	335	20.086	88.329	63.181	1.00	91.31
2685	C	TYR	B	335	23.422	90.459	65.896	1.00	69.32
2686	O	TYR	B	335	24.454	90.253	66.261	1.00	72.11
2687	N	SER	B	336	22.610	91.199	66.547	1.00	68.57
2688	CA	SER	B	336	22.786	91.985	67.682	1.00	62.50
2689	CB	SER	B	336	22.545	93.468	67.237	1.00	62.77
2690	OG	SER	B	336	21.204	93.805	67.256	1.00	54.34
2691	C	SER	B	336	21.839	91.719	68.722	1.00	56.95
2692	O	SER	B	336	20.837	91.110	68.474	1.00	55.57
2693	N	LYS	B	337	22.245	91.980	69.906	1.00	59.06
2694	CA	LYS	B	337	21.401	91.672	71.082	1.00	65.18
2695	CB	LYS	B	337	21.981	92.085	72.472	1.00	62.25
2696	CG	LYS	B	337	23.158	91.183	72.975	1.00	75.18
2697	CD	LYS	B	337	24.128	91.873	74.164	1.00	69.42
2698	CE	LYS	B	337	23.258	92.166	75.429	1.00	82.02
2699	NZ	LYS	B	337	22.988	93.840	75.729	1.00	88.14
2700	C	LYS	B	337	19.898	92.123	70.979	1.00	65.87
2701	O	LYS	B	337	18.790	91.514	71.305	1.00	62.80
2702	N	ASP	B	338	19.841	93.263	70.436	1.00	68.89
2703	CA	ASP	B	338	18.509	93.856	70.128	1.00	66.22
2704	CB	ASP	B	338	18.759	95.420	69.801	1.00	67.25
2705	CG	ASP	B	338	19.017	96.214	71.180	1.00	78.76
2706	OD1	ASP	B	338	18.059	96.369	72.063	1.00	80.15
2707	OD2	ASP	B	338	20.106	96.727	71.473	1.00	82.82
2708	C	ASP	B	338	17.752	93.074	69.013	1.00	63.09
2709	O	ASP	B	338	16.439	92.773	69.199	1.00	62.26
2710	N	ASP	B	339	18.472	92.767	67.957	1.00	53.26
2711	CA	ASP	B	339	17.730	92.045	67.051	1.00	60.52
2712	CB	ASP	B	339	18.725	91.352	65.998	1.00	61.80
2713	CG	ASP	B	339	19.365	92.313	65.200	1.00	63.07
2714	OD1	ASP	B	339	18.679	93.307	64.790	1.00	70.88
2715	OD2	ASP	B	339	20.437	92.232	64.854	1.00	67.08
2716	C	ASP	B	339	16.863	90.880	67.818	1.00	65.06
2717	O	ASP	B	339	15.506	90.720	67.561	1.00	61.45
2718	N	PHE	B	340	17.662	90.149	68.728	1.00	61.06
2719	CA	PHE	B	340	17.220	89.050	69.494	1.00	60.32
2720	CB	PHE	B	340	18.300	88.290	70.495	1.00	56.10
2721	CG	PHE	B	340	19.434	87.535	69.783	1.00	47.88
2722	CD1	PHE	B	340	20.202	88.004	68.847	1.00	47.77
2723	CE1	PHE	B	340	21.132	87.399	68.149	1.00	45.70
2724	CZ	PHE	B	340	21.320	85.899	68.401	1.00	55.25
2725	CE2	PHE	B	340	20.409	85.312	69.255	1.00	49.14
2726	CD2	PHE	B	340	19.482	86.220	69.988	1.00	55.69
2727	C	PHE	B	340	16.017	89.484	70.175	1.00	62.83
2728	O	PHE	B	340	14.955	88.699	70.110	1.00	67.32
2729	N	HIS	B	341	16.072	90.651	70.815	1.00	64.53
2730	CA	HIS	B	341	14.814	91.067	71.551	1.00	71.00
2731	CB	HIS	B	341	15.007	92.393	72.368	1.00	72.94
2732	CG	HIS	B	341	16.122	92.302	73.297	1.00	69.49
2733	ND1	HIS	B	341	17.464	92.315	72.856	1.00	73.08
2734	CE1	HIS	B	341	18.264	92.173	73.954	1.00	78.41
2735	NE2	HIS	B	341	17.479	91.902	75.023	1.00	82.09
2736	CD2	HIS	B	341	16.126	91.990	74.616	1.00	77.34
2737	C	HIS	B	341	13.616	91.295	70.652	1.00	66.90
2738	O	HIS	B	341	12.510	90.986	71.057	1.00	60.48
2739	N	ARG	B	342	14.012	91.759	69.483	1.00	67.75
2740	CA	ARG	B	342	13.037	91.936	68.350	1.00	73.18
2741	CB	ARG	B	342	13.829	92.432	67.008	1.00	74.27
2742	CG	ARG	B	342	13.585	94.024	66.904	1.00	61.57
2743	CD	ARG	B	342	14.575	94.742	66.346	1.00	60.29
2744	NE	ARG	B	342	14.705	96.162	66.846	1.00	71.95
2745	CZ	ARG	B	342	15.904	96.835	67.255	1.00	67.30
2746	NH1	ARG	B	342	17.125	96.343	66.996	1.00	70.43
2747	NH2	ARG	B	342	15.916	98.007	67.794	1.00	68.99
2748	C	ARG	B	342	12.209	90.669	67.936	1.00	70.00
2749	O	ARG	B	342	10.877	90.653	67.865	1.00	68.24
2750	N	ALA	B	343	12.938	89.619	67.870	1.00	65.37
2751	CA	ALA	B	343	12.336	88.282	67.551	1.00	57.52
2752	CB	ALA	B	343	13.328	87.443	66.900	1.00	52.06
2753	C	ALA	B	343	11.623	87.817	68.626	1.00	60.04
2754	O	ALA	B	343	10.975	86.799	68.619	1.00	63.88
2755	N	GLY	B	344	11.558	88.588	69.693	1.00	65.13
2756	CA	GLY	B	344	10.708	88.116	70.932	1.00	63.20
2757	C	GLY	B	344	11.503	87.321	72.005	1.00	61.28
2758	O	GLY	B	344	11.032	86.873	73.056	1.00	65.97
2759	N	LEU	B	345	12.792	87.264	71.820	1.00	64.60
2760	CA	LEU	B	345	13.716	86.536	72.858	1.00	62.54
2761	CB	LEU	B	345	15.061	86.201	72.183	1.00	57.64
2762	CG	LEU	B	345	15.157	85.573	70.740	1.00	62.93
2763	CD1	LEU	B	345	16.123	84.434	70.841	1.00	76.97
2764	CD2	LEU	B	345	13.802	85.098	69.952	1.00	59.00
2765	C	LEU	B	345	13.874	87.246	73.974	1.00	63.15
2766	O	LEU	B	345	14.359	88.327	73.807	1.00	76.57
2767	N	GLN	B	346	13.552	86.790	75.143	1.00	59.15
2768	CA	GLN	B	346	13.725	87.487	76.318	1.00	64.37
2769	CB	GLN	B	346	12.880	86.738	77.398	1.00	63.91
2770	CG	GLN	B	346	13.290	85.212	77.500	1.00	73.12
2771	CD	GLN	B	346	12.419	84.464	78.569	1.00	71.74
2772	OE1	GLN	B	346	12.641	83.369	78.841	1.00	63.96
2773	NE2	GLN	B	346	11.299	85.087	79.033	1.00	70.06
2774	C	GLN	B	346	15.261	87.723	76.891	1.00	65.83
2775	O	GLN	B	346	16.065	86.955	76.681	1.00	70.72
2776	N	VAL	B	347	15.586	88.724	77.526	1.00	59.97
2777	CA	VAL	B	347	16.843	89.122	77.777	1.00	58.82
2778	CB	VAL	B	347	16.779	90.406	78.635	1.00	59.13
2779	CG1	VAL	B	347	15.764	90.275	80.040	1.00	60.73
2780	CG2	VAL	B	347	18.034	90.918	79.113	1.00	67.69
2781	C	VAL	B	347	17.480	88.087	78.667	1.00	64.04
2782	O	VAL	B	347	18.669	88.031	78.690	1.00	62.73
2783	N	GLU	B	348	16.681	87.362	79.495	1.00	61.58
2784	CA	GLU	B	348	17.082	86.396	80.301	1.00	56.15
2785	CB	GLU	B	348	15.957	85.918	81.173	1.00	61.69
2786	CG	GLU	B	348	14.512	86.339	80.411	1.00	73.26
2787	CD	GLU	B	348	13.773	87.410	81.118	1.00	67.05
2788	OE1	GLU	B	348	12.760	87.178	81.913	1.00	70.33
2789	OE2	GLU	B	348	14.273	88.437	80.948	1.00	69.87
2790	C	GLU	B	348	17.671	85.224	79.631	1.00	57.15
2791	O	GLU	B	348	18.327	84.398	80.339	1.00	59.19
2792	N	PHE	B	349	17.792	85.189	78.303	1.00	55.88
2793	CA	PHE	B	349	18.444	84.324	77.568	1.00	46.69
2794	CB	PHE	B	349	17.345	83.467	76.750	1.00	54.67
2795	CG	PHE	B	349	17.898	82.462	75.751	1.00	56.05
2796	CD1	PHE	B	349	18.897	81.521	76.196	1.00	57.34
2797	CE1	PHE	B	349	19.455	80.643	75.414	1.00	52.74
2798	CZ	PHE	B	349	19.003	80.373	74.054	1.00	53.17
2799	CE2	PHE	B	349	18.060	81.181	73.542	1.00	47.95
2800	CD2	PHE	B	349	17.487	82.349	74.549	1.00	59.50
2801	C	PHE	B	349	19.381	84.858	76.696	1.00	46.68
2802	O	PHE	B	349	20.508	84.295	76.491	1.00	49.18
2803	N	ILE	B	350	19.087	85.971	76.173	1.00	44.99
2804	CA	ILE	B	350	20.099	86.710	75.203	1.00	47.50
2805	CB	ILE	B	350	19.427	88.047	74.637	1.00	47.55
2806	CG1	ILE	B	350	18.113	87.541	73.797	1.00	48.34
2807	CD1	ILE	B	350	17.011	88.771	74.039	1.00	59.54
2808	CG2	ILE	B	350	20.235	88.800	73.720	1.00	55.42
2809	C	ILE	B	350	21.452	87.192	75.913	1.00	44.46
2810	O	ILE	B	350	22.534	86.952	75.262	1.00	45.96
2811	N	ASN	B	351	21.327	87.665	77.121	1.00	40.71
2812	CA	ASN	B	351	22.644	88.215	77.719	1.00	47.42
2813	CB	ASN	B	351	22.251	88.814	79.045	1.00	45.36
2814	CG	ASN	B	351	21.514	90.145	78.898	1.00	50.17
2815	OD1	ASN	B	351	21.495	90.817	77.832	1.00	51.44
2816	ND2	ASN	B	351	20.830	90.523	80.022	1.00	50.37
2817	C	ASN	B	351	23.588	86.934	78.059	1.00	41.66
2818	O	ASN	B	351	24.725	86.884	77.587	1.00	39.55
2819	N	PRO	B	352	22.937	85.903	78.537	1.00	36.22
2820	CA	PRO	B	352	23.682	84.683	78.700	1.00	34.72
2821	CB	PRO	B	352	22.753	83.723	79.279	1.00	36.88
2822	CG	PRO	B	352	21.811	84.653	80.164	1.00	46.71
2823	CD	PRO	B	352	21.621	85.892	79.041	1.00	35.82
2824	C	PRO	B	352	24.237	84.224	77.530	1.00	36.30
2825	O	PRO	B	352	25.419	83.761	77.383	1.00	40.39
2826	N	ILE	B	353	23.474	84.391	76.372	1.00	41.10
2827	CA	ILE	B	353	24.122	83.951	75.074	1.00	39.30
2828	CB	ILE	B	353	23.105	83.987	74.027	1.00	42.13
2829	CG1	ILE	B	353	21.891	82.903	74.260	1.00	43.94
2830	CD1	ILE	B	353	20.748	82.937	73.139	1.00	35.70
2831	CG2	ILE	B	353	23.816	83.728	72.610	1.00	32.18
2832	C	ILE	B	353	25.291	84.644	74.751	1.00	38.70
2833	O	ILE	B	353	26.320	84.176	74.244	1.00	38.63
2834	N	PHE	B	354	25.195	85.973	75.050	1.00	47.94
2835	CA	PHE	B	354	26.388	86.815	74.814	1.00	50.23
2836	CB	PHE	B	354	25.749	88.409	74.654	1.00	50.03
2837	CG	PHE	B	354	25.108	88.608	73.274	1.00	55.16
2838	CD1	PHE	B	354	23.865	88.155	73.072	1.00	55.03
2839	CE1	PHE	B	354	23.259	88.195	71.851	1.00	54.17
2840	CZ	PHE	B	354	23.881	88.570	70.739	1.00	56.66
2841	CE2	PHE	B	354	25.226	89.026	70.978	1.00	68.88
2842	CD2	PHE	B	354	25.851	88.951	72.206	1.00	45.25
2843	C	PHE	B	354	27.526	86.798	75.713	1.00	40.23
2844	O	PHE	B	354	28.733	86.925	75.321	1.00	43.29
2845	N	GLU	B	355	27.211	86.597	76.921	1.00	40.93
2846	CA	GLU	B	355	28.523	86.397	77.978	1.00	37.60
2847	CB	GLU	B	355	27.902	86.380	79.277	1.00	44.07
2848	CG	GLU	B	355	27.453	87.768	79.784	1.00	40.87
2849	CD	GLU	B	355	26.128	87.705	80.643	1.00	54.01
2850	OE1	GLU	B	355	25.652	86.568	81.136	1.00	55.64
2851	OE2	GLU	B	355	25.515	88.734	80.860	1.00	57.08
2852	C	GLU	B	355	29.098	85.076	77.698	1.00	35.92
2853	O	GLU	B	355	30.454	84.938	77.539	1.00	34.43
2854	N	PHE	B	356	28.248	84.085	77.222	1.00	36.19
2855	CA	PHE	B	356	28.898	82.751	76.709	1.00	36.57
2856	CB	PHE	B	356	27.756	81.632	76.594	1.00	35.87
2857	CG	PHE	B	356	28.340	80.354	76.177	1.00	35.72
2858	CD1	PHE	B	356	29.015	79.569	77.101	1.00	33.72
2859	CE1	PHE	B	356	29.544	78.291	76.771	1.00	39.96
2860	CZ	PHE	B	356	29.540	77.881	75.360	1.00	40.70
2861	CE2	PHE	B	356	28.833	78.674	74.387	1.00	32.50
2862	CD2	PHE	B	356	28.366	79.897	74.811	1.00	41.44
2863	C	PHE	B	356	29.852	82.882	75.662	1.00	33.57
2864	O	PHE	B	356	31.075	82.374	75.608	1.00	35.52
2865	N	SER	B	357	29.407	83.703	74.694	1.00	34.35
2866	CA	SER	B	357	30.297	83.917	73.570	1.00	33.77
2867	CB	SER	B	357	29.364	84.692	72.534	1.00	47.00
2868	OG	SER	B	357	27.969	84.212	72.666	1.00	41.44
2869	C	SER	B	357	31.489	84.718	73.839	1.00	31.31
2870	O	SER	B	357	32.573	84.504	73.262	1.00	32.90
2871	N	ARG	B	358	31.360	85.621	74.748	1.00	34.45
2872	CA	ARG	B	358	32.615	86.391	75.106	1.00	34.95
2873	CB	ARG	B	358	32.189	87.572	76.022	1.00	39.55
2874	CG	ARG	B	358	31.744	88.997	75.200	1.00	41.56
2875	CD	ARG	B	358	31.059	89.917	76.494	1.00	44.77
2876	NE	ARG	B	358	29.771	90.142	76.015	1.00	45.47
2877	CZ	ARG	B	358	28.789	90.137	76.850	1.00	49.55
2878	NH1	ARG	B	358	28.973	89.970	78.162	1.00	42.75
2879	NH2	ARG	B	358	27.510	90.492	76.442	1.00	56.37
2880	C	ARG	B	358	33.558	85.457	75.884	1.00	35.05
2881	O	ARG	B	358	34.790	85.462	75.700	1.00	35.35
2882	N	ALA	B	359	32.926	84.629	76.657	1.00	35.52
2883	CA	ALA	B	359	33.812	83.717	77.462	1.00	35.54
2884	CB	ALA	B	359	32.818	82.947	78.509	1.00	31.23
2885	C	ALA	B	359	34.462	82.680	76.523	1.00	37.97
2886	O	ALA	B	359	35.668	82.350	76.637	1.00	33.88
2887	N	MET	B	360	33.706	82.100	75.643	1.00	41.47
2888	CA	MET	B	360	34.449	81.111	74.707	1.00	36.12
2889	CB	MET	B	360	33.314	80.532	73.676	1.00	35.78
2890	CG	MET	B	360	32.295	79.532	74.412	1.00	36.49
2891	SD	MET	B	360	33.230	78.304	75.227	1.00	33.45
2892	CE	MET	B	360	33.781	77.421	73.620	1.00	44.23
2893	C	MET	B	360	35.405	81.879	74.052	1.00	38.81
2894	O	MET	B	360	36.534	81.346	73.856	1.00	38.37
2895	N	ARG	B	361	35.055	83.136	73.576	1.00	37.37
2896	CA	ARG	B	361	36.248	83.826	72.876	1.00	44.82
2897	CB	ARG	B	361	35.780	85.316	72.522	1.00	44.87
2898	CG	ARG	B	361	36.987	86.109	71.904	1.00	44.84
2899	CD	ARG	B	361	36.466	87.439	71.655	1.00	51.90
2900	NE	ARG	B	361	37.276	88.236	71.019	1.00	60.42
2901	CZ	ARG	B	361	38.134	89.185	71.515	1.00	68.73
2902	NH1	ARG	B	361	38.077	89.389	72.838	1.00	60.60
2903	NH2	ARG	B	361	38.846	90.055	70.621	1.00	78.26
2904	C	ARG	B	361	37.480	83.977	73.692	1.00	46.62
2905	O	ARG	B	361	38.727	83.585	73.269	1.00	49.98
2906	N	ARG	B	362	37.353	84.518	74.826	1.00	41.39
2907	CA	ARG	B	362	38.668	84.561	75.685	1.00	42.68
2908	CB	ARG	B	362	38.178	85.012	77.142	1.00	42.44
2909	CG	ARG	B	362	37.619	86.567	77.136	1.00	42.82
2910	CD	ARG	B	362	37.308	86.945	78.575	1.00	38.22
2911	NE	ARG	B	362	35.868	87.079	78.788	1.00	41.73
2912	CZ	ARG	B	362	35.255	86.428	79.619	1.00	38.95
2913	NH1	ARG	B	362	35.845	85.463	80.223	1.00	45.47
2914	NH2	ARG	B	362	33.998	86.508	79.660	1.00	36.14
2915	C	ARG	B	362	39.358	83.319	75.688	1.00	40.83
2916	O	ARG	B	362	40.460	83.238	76.042	1.00	48.50
2917	N	LEU	B	363	38.700	82.197	75.579	1.00	38.38
2918	CA	LEU	B	363	39.437	80.922	75.664	1.00	39.93
2919	CB	LEU	B	363	38.359	79.771	75.741	1.00	40.71
2920	CG	LEU	B	363	37.949	79.299	77.014	1.00	38.90
2921	CD1	LEU	B	363	36.937	78.240	76.961	1.00	33.87
2922	CD2	LEU	B	363	39.129	78.816	77.709	1.00	42.27
2923	C	LEU	B	363	40.232	80.692	74.366	1.00	37.22
2924	O	LEU	B	363	41.222	79.915	74.404	1.00	34.01
2925	N	GLY	B	364	39.909	81.449	73.270	1.00	39.17
2926	CA	GLY	B	364	40.736	81.431	71.959	1.00	37.89
2927	C	GLY	B	364	40.810	79.959	71.399	1.00	44.21
2928	O	GLY	B	364	41.880	79.338	71.288	1.00	40.61
2929	N	LEU	B	365	39.637	79.369	71.190	1.00	43.34
2930	CA	LEU	B	365	39.694	77.882	70.801	1.00	49.01
2931	CB	LEU	B	365	38.272	77.164	71.229	1.00	42.87
2932	CG	LEU	B	365	38.161	77.232	72.788	1.00	49.95
2933	CD1	LEU	B	365	36.743	76.607	72.908	1.00	58.47
2934	CD2	LEU	B	365	39.116	76.275	73.403	1.00	50.07
2935	C	LEU	B	365	39.830	77.676	69.298	1.00	45.16
2936	O	LEU	B	365	39.156	78.429	68.524	1.00	45.24
2937	N	ASP	B	366	40.565	76.692	69.046	1.00	48.71
2938	CA	ASP	B	366	40.787	76.030	67.592	1.00	54.79
2939	CB	ASP	B	366	41.586	74.767	67.763	1.00	51.18
2940	CG	ASP	B	366	42.955	75.100	67.351	1.00	58.96
2941	OD1	ASP	B	366	42.825	75.849	66.448	1.00	65.21
2942	OD2	ASP	B	366	44.005	74.650	67.781	1.00	53.99
2943	C	ASP	B	366	39.659	75.446	67.061	1.00	59.19
2944	O	ASP	B	366	38.335	75.346	67.602	1.00	52.59
2945	N	ASP	B	367	40.020	74.916	65.925	1.00	60.01
2946	CA	ASP	B	367	38.976	74.117	65.057	1.00	53.72
2947	CB	ASP	B	367	39.632	74.063	63.588	1.00	56.58
2948	CG	ASP	B	367	39.019	75.126	62.645	1.00	69.39
2949	OD1	ASP	B	367	38.272	76.070	63.065	1.00	68.05
2950	OD2	ASP	B	367	39.339	75.032	61.444	1.00	78.09
2951	C	ASP	B	367	38.927	72.789	65.678	1.00	43.49
2952	O	ASP	B	367	37.896	72.221	65.734	1.00	49.56
2953	N	ALA	B	368	40.048	72.270	65.943	1.00	45.38
2954	CA	ALA	B	368	40.214	71.063	66.449	1.00	50.48
2955	CB	ALA	B	368	41.596	70.645	66.677	1.00	48.33
2956	C	ALA	B	368	39.304	70.977	67.802	1.00	52.64
2957	O	ALA	B	368	38.279	70.286	67.850	1.00	48.37
2958	N	GLU	B	369	39.807	71.840	68.718	1.00	45.67
2959	CA	GLU	B	369	39.101	72.143	70.017	1.00	47.42
2960	CB	GLU	B	369	39.774	73.382	70.752	1.00	39.41
2961	CG	GLU	B	369	41.226	73.138	70.884	1.00	47.88
2962	CD	GLU	B	369	42.177	74.344	71.359	1.00	50.37
2963	OE1	GLU	B	369	41.953	75.426	70.859	1.00	49.12
2964	OE2	GLU	B	369	43.018	74.078	72.219	1.00	42.55
2965	C	GLU	B	369	37.668	72.248	69.966	1.00	43.17
2966	O	GLU	B	369	36.937	71.556	70.687	1.00	49.38
2967	N	TYR	B	370	37.148	73.057	69.116	1.00	45.99
2968	CA	TYR	B	370	35.813	73.305	69.076	1.00	47.58
2969	CB	TYR	B	370	35.422	74.286	68.072	1.00	47.27
2970	CG	TYR	B	370	35.052	75.556	68.597	1.00	52.74
2971	CD1	TYR	B	370	36.064	76.635	68.641	1.00	50.10
2972	CE1	TYR	B	370	35.624	77.936	69.314	1.00	40.35
2973	CZ	TYR	B	370	34.554	78.036	69.840	1.00	40.16
2974	OH	TYR	B	370	33.991	79.170	70.276	1.00	44.26
2975	CE2	TYR	B	370	33.424	76.804	69.704	1.00	47.37
2976	CD2	TYR	B	370	33.712	75.833	69.190	1.00	42.67
2977	C	TYR	B	370	35.030	71.874	68.684	1.00	52.99
2978	O	TYR	B	370	33.758	71.658	69.130	1.00	49.77
2979	N	ALA	B	371	35.630	71.157	67.806	1.00	47.82
2980	CA	ALA	B	371	34.831	69.961	67.295	1.00	51.98
2981	CB	ALA	B	371	35.207	69.678	65.859	1.00	45.87
2982	C	ALA	B	371	35.094	68.670	68.370	1.00	46.13
2983	O	ALA	B	371	34.180	68.036	68.544	1.00	48.06
2984	N	LEU	B	372	36.211	68.555	68.932	1.00	37.70
2985	CA	LEU	B	372	36.500	67.670	69.899	1.00	40.88
2986	CB	LEU	B	372	37.925	67.769	70.424	1.00	37.06
2987	CG	LEU	B	372	38.958	66.880	69.768	1.00	44.88
2988	CD1	LEU	B	372	40.510	67.353	70.167	1.00	41.45
2989	CD2	LEU	B	372	38.785	65.261	70.084	1.00	38.26
2990	C	LEU	B	372	35.631	67.922	71.168	1.00	43.20
2991	O	LEU	B	372	35.194	66.999	71.837	1.00	41.82
2992	N	LEU	B	373	35.309	69.225	71.411	1.00	42.24
2993	CA	LEU	B	373	34.547	69.636	72.392	1.00	41.28
2994	CB	LEU	B	373	34.686	71.195	72.706	1.00	39.69
2995	CG	LEU	B	373	33.958	71.661	74.107	1.00	41.53
2996	CD1	LEU	B	373	34.524	71.057	75.268	1.00	32.76
2997	CD2	LEU	B	373	34.319	73.192	74.271	1.00	42.23
2998	C	LEU	B	373	33.189	69.144	72.164	1.00	40.89
2999	O	LEU	B	373	32.526	68.647	73.086	1.00	36.48
3000	N	ILE	B	374	32.726	69.362	70.974	1.00	38.82
3001	CA	ILE	B	374	31.222	68.979	70.736	1.00	40.41
3002	CB	ILE	B	374	30.792	69.588	69.360	1.00	49.48
3003	CG1	ILE	B	374	30.806	71.010	69.376	1.00	40.21
3004	CD1	ILE	B	374	30.576	71.719	67.853	1.00	39.35
3005	CG2	ILE	B	374	29.433	69.176	68.783	1.00	50.16
3006	C	ILE	B	374	31.071	67.463	70.633	1.00	35.65
3007	O	ILE	B	374	30.044	67.013	70.952	1.00	37.33
3008	N	ALA	B	375	32.139	66.780	70.275	1.00	34.81
3009	CA	ALA	B	375	32.109	65.258	70.332	1.00	38.01
3010	CB	ALA	B	375	33.550	64.740	69.719	1.00	31.42
3011	C	ALA	B	375	31.850	64.791	71.650	1.00	38.73
3012	O	ALA	B	375	31.171	63.865	71.926	1.00	35.75
3013	N	ILE	B	376	32.786	65.389	72.622	1.00	41.09
3014	CA	ILE	B	376	32.744	65.055	74.022	1.00	35.50
3015	CB	ILE	B	376	33.708	65.860	74.712	1.00	33.93
3016	CG1	ILE	B	376	35.058	65.278	74.378	1.00	37.82
3017	CD1	ILE	B	376	36.260	66.085	74.970	1.00	42.61
3018	CG2	ILE	B	376	33.578	65.909	76.213	1.00	35.07
3019	C	ILE	B	376	31.215	65.433	74.518	1.00	39.39
3020	O	ILE	B	376	30.600	64.662	75.226	1.00	31.63
3021	N	ASN	B	377	30.726	66.553	73.996	1.00	33.27
3022	CA	ASN	B	377	29.481	66.963	74.402	1.00	40.51
3023	CB	ASN	B	377	29.092	68.399	73.899	1.00	35.15
3024	CG	ASN	B	377	27.785	68.831	74.341	1.00	45.99
3025	OD1	ASN	B	377	26.756	68.380	73.788	1.00	57.62
3026	ND2	ASN	B	377	27.628	69.868	75.129	1.00	42.62
3027	C	ASN	B	377	28.318	65.895	73.951	1.00	39.66
3028	O	ASN	B	377	27.426	65.579	74.639	1.00	33.22
3029	N	ILE	B	378	28.475	65.476	72.689	1.00	41.09
3030	CA	ILE	B	378	27.466	64.500	72.126	1.00	36.18
3031	CB	ILE	B	378	27.826	64.197	70.678	1.00	38.50
3032	CG1	ILE	B	378	27.152	65.256	69.760	1.00	35.97
3033	CD1	ILE	B	378	27.776	65.473	68.277	1.00	36.60
3034	CG2	ILE	B	378	27.258	62.699	70.244	1.00	33.25
3035	C	ILE	B	378	27.497	63.126	72.910	1.00	35.29
3036	O	ILE	B	378	26.423	62.693	73.370	1.00	36.52
3037	N	PHE	B	379	28.601	62.634	73.243	1.00	32.11
3038	CA	PHE	B	379	28.708	61.503	74.070	1.00	33.81
3039	CB	PHE	B	379	30.021	60.741	73.831	1.00	32.68
3040	CG	PHE	B	379	30.122	60.167	72.287	1.00	41.51
3041	CD1	PHE	B	379	29.187	59.435	71.829	1.00	38.71
3042	CE1	PHE	B	379	29.260	58.986	70.315	1.00	47.93
3043	CZ	PHE	B	379	30.147	59.236	69.593	1.00	42.87
3044	CE2	PHE	B	379	31.361	60.099	70.327	1.00	52.03
3045	CD2	PHE	B	379	31.139	60.524	71.507	1.00	40.23
3046	C	PHE	B	379	28.527	61.768	75.664	1.00	33.12
3047	O	PHE	B	379	29.455	61.342	76.400	1.00	32.97
3048	N	SER	B	380	27.448	62.253	76.030	1.00	31.16
3049	CA	SER	B	380	27.217	62.413	77.482	1.00	33.87
3050	CB	SER	B	380	26.593	63.847	77.671	1.00	35.32
3051	OG	SER	B	380	27.482	64.813	77.204	1.00	34.63
3052	C	SER	B	380	26.323	61.457	77.971	1.00	32.69
3053	O	SER	B	380	25.033	61.484	77.647	1.00	34.27
3054	N	ALA	B	381	26.835	60.585	78.833	1.00	31.35
3055	CA	ALA	B	381	26.112	59.445	79.336	1.00	36.71
3056	CB	ALA	B	381	26.981	58.621	79.982	1.00	34.88
3057	C	ALA	B	381	24.849	59.698	80.277	1.00	43.47
3058	O	ALA	B	381	23.935	58.858	80.375	1.00	39.75
3059	N	ASP	B	382	24.757	60.907	80.854	1.00	38.77
3060	CA	ASP	B	382	23.684	61.255	81.725	1.00	37.98
3061	CB	ASP	B	382	24.245	62.183	82.830	1.00	39.59
3062	CG	ASP	B	382	24.706	63.467	82.317	1.00	42.80
3063	OD1	ASP	B	382	24.785	64.393	83.147	1.00	47.40
3064	OD2	ASP	B	382	24.987	63.626	81.114	1.00	42.49
3065	C	ASP	B	382	22.458	61.983	80.969	1.00	38.07
3066	O	ASP	B	382	21.629	62.425	81.551	1.00	36.85
3067	N	ARG	B	383	22.506	61.946	79.627	1.00	33.91
3068	CA	ARG	B	383	21.389	62.586	79.022	1.00	43.30
3069	CB	ARG	B	383	21.483	62.676	77.426	1.00	38.18
3070	CG	ARG	B	383	22.666	63.403	76.929	1.00	38.53
3071	CD	ARG	B	383	22.759	64.827	77.504	1.00	35.18
3072	NE	ARG	B	383	23.761	65.525	76.860	1.00	37.54
3073	CZ	ARG	B	383	23.986	66.862	76.877	1.00	40.86
3074	NH1	ARG	B	383	23.246	67.593	77.627	1.00	31.00
3075	NH2	ARG	B	383	25.014	67.372	76.123	1.00	33.65
3076	C	ARG	B	383	20.092	61.718	79.407	1.00	41.21
3077	O	ARG	B	383	20.239	60.515	79.738	1.00	42.43
3078	N	PRO	B	384	18.965	62.322	79.384	1.00	40.98
3079	CA	PRO	B	384	17.715	61.469	79.656	1.00	42.66
3080	CB	PRO	B	384	16.564	62.496	79.569	1.00	44.34
3081	CG	PRO	B	384	17.305	63.907	79.871	1.00	38.75
3082	CD	PRO	B	384	18.605	63.775	79.084	1.00	37.14
3083	C	PRO	B	384	17.496	60.418	78.613	1.00	40.57
3084	O	PRO	B	384	17.827	60.633	77.482	1.00	40.45
3085	N	ASN	B	385	16.974	59.352	79.082	1.00	43.30
3086	CA	ASN	B	385	16.593	58.197	78.182	1.00	48.11
3087	CB	ASN	B	385	15.585	58.541	77.140	1.00	45.42
3088	CG	ASN	B	385	14.505	59.439	77.724	1.00	52.65
3089	OD1	ASN	B	385	13.873	59.126	78.665	1.00	55.72
3090	ND2	ASN	B	385	14.327	60.658	77.178	1.00	54.76
3091	C	ASN	B	385	17.816	57.479	77.451	1.00	48.64
3092	O	ASN	B	385	17.523	56.696	76.493	1.00	43.31
3093	N	VAL	B	386	19.021	57.602	77.984	1.00	41.33
3094	CA	VAL	B	386	20.060	56.863	77.388	1.00	42.45
3095	CB	VAL	B	386	21.433	57.459	77.739	1.00	41.84
3096	CG1	VAL	B	386	22.550	56.396	77.457	1.00	36.52
3097	CG2	VAL	B	386	21.585	58.739	76.787	1.00	48.51
3098	C	VAL	B	386	19.869	55.483	77.822	1.00	47.92
3099	O	VAL	B	386	19.865	55.185	78.942	1.00	52.17
3100	N	GLN	B	387	19.968	54.486	76.939	1.00	51.58
3101	CA	GLN	B	387	19.793	53.147	77.402	1.00	48.85
3102	CB	GLN	B	387	18.917	52.374	76.350	1.00	53.71
3103	CG	GLN	B	387	17.442	52.809	76.192	1.00	53.80
3104	CD	GLN	B	387	16.614	51.865	75.515	1.00	63.34
3105	OE1	GLN	B	387	16.321	50.688	76.001	1.00	66.39
3106	NE2	GLN	B	387	16.200	52.255	74.301	1.00	72.65
3107	C	GLN	B	387	20.918	52.350	77.686	1.00	51.24
3108	O	GLN	B	387	20.837	51.407	78.567	1.00	51.47
3109	N	GLU	B	388	22.116	52.752	77.087	1.00	49.23
3110	CA	GLU	B	388	23.346	52.227	77.309	1.00	44.52
3111	CB	GLU	B	388	23.934	51.490	76.035	1.00	48.85
3112	CG	GLU	B	388	22.981	50.173	75.625	1.00	58.45
3113	CD	GLU	B	388	23.286	49.659	74.132	1.00	60.60
3114	OE1	GLU	B	388	22.905	48.548	73.897	1.00	77.84
3115	OE2	GLU	B	388	23.680	50.333	73.228	1.00	61.44
3116	C	GLU	B	388	24.358	53.159	77.798	1.00	44.83
3117	O	GLU	B	388	25.470	53.409	77.170	1.00	48.61
3118	N	PRO	B	389	24.190	53.716	78.934	1.00	47.42
3119	CA	PRO	B	389	25.178	54.732	79.457	1.00	39.92
3120	CB	PRO	B	389	24.641	55.108	80.732	1.00	40.08
3121	CG	PRO	B	389	23.777	53.909	81.212	1.00	47.99
3122	CD	PRO	B	389	23.093	53.436	79.867	1.00	41.25
3123	C	PRO	B	389	26.597	54.326	79.438	1.00	42.93
3124	O	PRO	B	389	27.529	55.133	79.280	1.00	41.55
3125	N	GLY	B	390	26.883	53.146	79.869	1.00	49.43
3126	CA	GLY	B	390	28.215	52.662	80.145	1.00	43.80
3127	C	GLY	B	390	28.907	52.801	78.721	1.00	51.10
3128	O	GLY	B	390	30.087	53.361	78.713	1.00	50.45
3129	N	ARG	B	391	28.315	52.449	77.669	1.00	46.22
3130	CA	ARG	B	391	28.835	52.490	76.388	1.00	49.67
3131	CB	ARG	B	391	27.789	51.840	75.294	1.00	50.81
3132	CG	ARG	B	391	28.265	50.637	74.672	1.00	62.59
3133	CD	ARG	B	391	27.148	50.063	73.688	1.00	57.61
3134	NE	ARG	B	391	27.542	50.198	72.346	1.00	60.34
3135	CZ	ARG	B	391	26.712	49.956	71.336	1.00	65.60
3136	NH1	ARG	B	391	25.489	49.448	71.571	1.00	63.01
3137	NH2	ARG	B	391	27.137	50.044	70.028	1.00	59.69
3138	C	ARG	B	391	29.054	53.880	75.931	1.00	48.48
3139	O	ARG	B	391	30.203	54.230	75.317	1.00	49.56
3140	N	VAL	B	392	28.120	54.741	76.158	1.00	48.12
3141	CA	VAL	B	392	28.343	56.259	75.744	1.00	47.83
3142	CB	VAL	B	392	27.182	56.986	76.124	1.00	48.35
3143	CG1	VAL	B	392	27.339	58.600	75.950	1.00	45.88
3144	CG2	VAL	B	392	25.878	56.348	75.321	1.00	42.60
3145	C	VAL	B	392	29.594	56.730	76.511	1.00	43.63
3146	O	VAL	B	392	30.478	57.348	75.804	1.00	45.69
3147	N	GLU	B	393	29.745	56.411	77.768	1.00	37.90
3148	CA	GLU	B	393	30.705	56.936	78.557	1.00	42.47
3149	CB	GLU	B	393	30.552	56.493	80.014	1.00	46.80
3150	CG	GLU	B	393	31.086	57.536	81.110	1.00	52.70
3151	CD	GLU	B	393	30.912	56.905	82.636	1.00	62.94
3152	OE1	GLU	B	393	29.985	55.972	82.850	1.00	58.05
3153	OE2	GLU	B	393	31.558	57.350	83.570	1.00	57.70
3154	C	GLU	B	393	32.070	56.368	78.029	1.00	49.81
3155	O	GLU	B	393	33.100	56.998	78.094	1.00	46.21
3156	N	ALA	B	394	32.036	55.065	77.599	1.00	46.59
3157	CA	ALA	B	394	33.089	54.500	77.027	1.00	51.72
3158	CB	ALA	B	394	32.849	52.975	76.829	1.00	47.93
3159	C	ALA	B	394	33.426	55.225	75.548	1.00	49.33
3160	O	ALA	B	394	34.571	55.308	75.172	1.00	53.93
3161	N	LEU	B	395	32.512	55.542	74.841	1.00	47.24
3162	CA	LEU	B	395	32.713	56.174	73.588	1.00	47.77
3163	CB	LEU	B	395	31.375	56.420	73.002	1.00	47.27
3164	CG	LEU	B	395	30.650	55.089	72.518	1.00	52.97
3165	CD1	LEU	B	395	29.486	55.532	71.568	1.00	56.50
3166	CD2	LEU	B	395	31.633	54.369	71.629	1.00	65.08
3167	C	LEU	B	395	33.351	57.635	73.853	1.00	50.33
3168	O	LEU	B	395	34.224	57.986	73.190	1.00	43.23
3169	N	GLN	B	396	32.857	58.316	74.935	1.00	45.97
3170	CA	GLN	B	396	33.453	59.568	75.249	1.00	45.92
3171	CB	GLN	B	396	32.549	60.360	76.332	1.00	48.46
3172	CG	GLN	B	396	33.013	61.694	76.726	1.00	38.06
3173	CD	GLN	B	396	32.178	62.350	77.874	1.00	43.58
3174	OE1	GLN	B	396	31.218	63.093	77.571	1.00	37.96
3175	NE2	GLN	B	396	32.370	61.932	79.033	1.00	33.42
3176	C	GLN	B	396	34.794	59.728	75.616	1.00	39.07
3177	O	GLN	B	396	35.399	60.637	75.344	1.00	46.93
3178	N	GLN	B	397	35.306	58.840	76.278	1.00	43.51
3179	CA	GLN	B	397	36.502	58.774	76.766	1.00	45.19
3180	CB	GLN	B	397	36.753	57.518	77.438	1.00	50.22
3181	CG	GLN	B	397	38.002	57.491	78.398	1.00	53.48
3182	CD	GLN	B	397	38.113	56.049	79.202	1.00	74.85
3183	OE1	GLN	B	397	37.123	55.689	79.894	1.00	73.18
3184	NE2	GLN	B	397	39.234	55.224	78.998	1.00	69.16
3185	C	GLN	B	397	37.687	59.178	75.868	1.00	52.84
3186	O	GLN	B	397	38.635	60.070	76.246	1.00	49.93
3187	N	PRO	B	398	37.842	58.514	74.840	1.00	53.73
3188	CA	PRO	B	398	38.993	58.790	74.001	1.00	55.88
3189	CB	PRO	B	398	38.763	57.666	72.715	1.00	62.63
3190	CG	PRO	B	398	37.129	57.322	72.859	1.00	53.57
3191	CD	PRO	B	398	37.052	57.343	74.422	1.00	58.05
3192	C	PRO	B	398	38.851	60.214	73.388	1.00	52.09
3193	O	PRO	B	398	39.793	60.773	72.860	1.00	52.37
3194	N	TYR	B	399	37.751	60.840	73.430	1.00	52.85
3195	CA	TYR	B	399	37.678	62.200	72.875	1.00	50.56
3196	CB	TYR	B	399	36.329	62.567	72.524	1.00	47.48
3197	CG	TYR	B	399	35.877	61.893	71.280	1.00	58.67
3198	CD1	TYR	B	399	36.390	62.258	69.997	1.00	58.36
3199	CE1	TYR	B	399	36.185	61.595	68.906	1.00	57.41
3200	CZ	TYR	B	399	35.378	60.455	68.910	1.00	65.70
3201	OH	TYR	B	399	35.023	59.768	67.846	1.00	56.50
3202	CE2	TYR	B	399	34.729	60.113	70.174	1.00	69.32
3203	CD2	TYR	B	399	35.052	60.821	71.309	1.00	64.30
3204	C	TYR	B	399	38.168	63.070	74.069	1.00	54.09
3205	O	TYR	B	399	38.825	64.123	73.739	1.00	57.36
3206	N	VAL	B	400	37.965	62.696	75.271	1.00	45.95
3207	CA	VAL	B	400	38.468	63.498	76.324	1.00	45.82
3208	CB	VAL	B	400	37.815	63.108	77.785	1.00	38.52
3209	CG1	VAL	B	400	38.430	63.876	78.843	1.00	38.05
3210	CG2	VAL	B	400	36.331	63.403	77.774	1.00	42.03
3211	C	VAL	B	400	39.920	63.465	76.392	1.00	43.40
3212	O	VAL	B	400	40.539	64.426	76.892	1.00	41.68
3213	N	GLU	B	401	40.454	62.287	76.118	1.00	42.91
3214	CA	GLU	B	401	41.801	62.093	76.259	1.00	46.81
3215	CB	GLU	B	401	42.164	60.569	76.197	1.00	50.70
3216	CG	GLU	B	401	43.592	60.205	76.576	1.00	57.12
3217	CD	GLU	B	401	43.723	58.785	77.282	1.00	69.56
3218	OE1	GLU	B	401	43.083	57.753	76.734	1.00	72.77
3219	OE2	GLU	B	401	44.364	58.632	78.277	1.00	71.00
3220	C	GLU	B	401	42.614	62.830	75.112	1.00	43.66
3221	O	GLU	B	401	43.608	63.397	75.287	1.00	41.67
3222	N	ALA	B	402	41.947	62.883	74.025	1.00	48.95
3223	CA	ALA	B	402	42.520	63.600	72.910	1.00	51.49
3224	CB	ALA	B	402	41.662	63.395	71.667	1.00	45.05
3225	C	ALA	B	402	42.622	64.979	73.224	1.00	46.67
3226	O	ALA	B	402	43.676	65.642	72.938	1.00	47.78
3227	N	LEU	B	403	41.518	65.517	73.675	1.00	44.41
3228	CA	LEU	B	403	41.438	66.964	74.065	1.00	42.46
3229	CB	LEU	B	403	40.015	67.443	74.295	1.00	33.75
3230	CG	LEU	B	403	39.846	68.871	74.540	1.00	42.51
3231	CD1	LEU	B	403	40.537	69.597	73.404	1.00	37.35
3232	CD2	LEU	B	403	38.403	69.363	74.740	1.00	28.87
3233	C	LEU	B	403	42.509	67.341	75.098	1.00	43.11
3234	O	LEU	B	403	43.206	68.350	74.938	1.00	46.62
3235	N	LEU	B	404	42.741	66.497	76.077	1.00	43.05
3236	CA	LEU	B	404	43.682	66.687	77.057	1.00	43.92
3237	CB	LEU	B	404	43.621	65.709	78.122	1.00	42.57
3238	CG	LEU	B	404	44.754	65.651	79.179	1.00	49.81
3239	CD1	LEU	B	404	44.964	67.122	79.790	1.00	49.83
3240	CD2	LEU	B	404	44.445	64.698	80.172	1.00	53.06
3241	C	LEU	B	404	45.172	66.804	76.401	1.00	51.79
3242	O	LEU	B	404	46.052	67.766	76.669	1.00	48.42
3243	N	SER	B	405	45.506	65.747	75.777	1.00	50.35
3244	CA	SER	B	405	46.902	65.745	75.119	1.00	56.85
3245	CB	SER	B	405	47.000	64.285	74.387	1.00	48.60
3246	OG	SER	B	405	46.226	64.556	73.285	1.00	58.57
3247	C	SER	B	405	47.022	66.867	74.169	1.00	50.98
3248	O	SER	B	405	47.920	67.578	74.326	1.00	55.26
3249	N	TYR	B	406	46.086	67.082	73.349	1.00	48.23
3250	CA	TYR	B	406	46.173	68.198	72.461	1.00	51.31
3251	CB	TYR	B	406	44.919	68.339	71.790	1.00	47.60
3252	CG	TYR	B	406	44.890	69.267	70.640	1.00	59.55
3253	CD1	TYR	B	406	45.552	68.953	69.407	1.00	55.72
3254	CE1	TYR	B	406	45.630	69.909	68.299	1.00	55.02
3255	CZ	TYR	B	406	44.898	71.017	68.355	1.00	63.04
3256	OH	TYR	B	406	44.731	71.941	67.433	1.00	63.15
3257	CE2	TYR	B	406	44.115	71.303	69.606	1.00	62.97
3258	CD2	TYR	B	406	44.098	70.473	70.601	1.00	58.74
3259	C	TYR	B	406	46.444	69.486	73.174	1.00	58.44
3260	O	TYR	B	406	47.480	70.166	72.935	1.00	62.89
3261	N	THR	B	407	45.620	69.978	74.099	1.00	58.58
3262	CA	THR	B	407	45.817	71.225	74.797	1.00	48.27
3263	CB	THR	B	407	44.573	71.502	75.818	1.00	43.99
3264	OG1	THR	B	407	44.442	70.504	76.852	1.00	44.98
3265	CG2	THR	B	407	43.383	71.691	75.113	1.00	42.33
3266	C	THR	B	407	47.056	71.188	75.527	1.00	46.17
3267	O	THR	B	407	47.666	72.267	75.718	1.00	58.76
3268	N	ARG	B	408	47.555	70.144	75.977	1.00	50.52
3269	CA	ARG	B	408	48.814	70.143	76.616	1.00	57.73
3270	CB	ARG	B	408	49.161	68.795	77.190	1.00	60.99
3271	CG	ARG	B	408	49.267	68.643	78.710	1.00	65.94
3272	CD	ARG	B	408	50.252	69.792	79.272	1.00	91.42
3273	NE	ARG	B	408	51.660	69.419	79.440	1.00	88.13
3274	CZ	ARG	B	408	52.676	70.329	79.553	1.00	97.15
3275	NH1	ARG	B	408	52.483	71.701	79.541	1.00	91.28
3276	NH2	ARG	B	408	53.930	69.930	79.739	1.00	91.45
3277	C	ARG	B	408	49.940	70.584	75.468	1.00	63.60
3278	O	ARG	B	408	50.910	71.225	75.761	1.00	66.13
3279	N	ILE	B	409	49.651	70.297	74.231	1.00	59.66
3280	CA	ILE	B	409	50.375	70.830	73.100	1.00	62.29
3281	CB	ILE	B	409	50.109	69.867	71.770	1.00	57.98
3282	CG1	ILE	B	409	50.780	68.550	72.071	1.00	52.77
3283	CD1	ILE	B	409	50.198	67.240	70.873	1.00	57.84
3284	CG2	ILE	B	409	50.806	70.472	70.532	1.00	59.90
3285	C	ILE	B	409	50.166	72.217	72.767	1.00	58.83
3286	O	ILE	B	409	51.090	72.968	72.861	1.00	63.13
3287	N	LYS	B	410	48.995	72.605	72.380	1.00	56.21
3288	CA	LYS	B	410	48.801	74.031	72.085	1.00	57.56
3289	CB	LYS	B	410	47.315	74.340	71.778	1.00	61.31
3290	CG	LYS	B	410	46.801	75.771	71.712	1.00	57.24
3291	CD	LYS	B	410	45.494	75.911	71.004	1.00	54.26
3292	CE	LYS	B	410	45.245	77.070	70.613	1.00	49.91
3293	NZ	LYS	B	410	44.007	77.304	69.876	1.00	63.13
3294	C	LYS	B	410	49.321	75.022	73.028	1.00	62.14
3295	O	LYS	B	410	50.108	75.881	72.807	1.00	65.63
3296	N	ARG	B	411	48.891	74.979	74.236	1.00	68.06
3297	CA	ARG	B	411	49.301	75.944	75.310	1.00	59.35
3298	CB	ARG	B	411	48.220	76.860	75.573	1.00	55.30
3299	CG	ARG	B	411	48.481	78.414	74.976	1.00	64.39
3300	CD	ARG	B	411	47.344	78.915	74.172	1.00	56.25
3301	NE	ARG	B	411	47.810	79.128	72.848	1.00	72.33
3302	CZ	ARG	B	411	46.991	79.535	71.859	1.00	80.77
3303	NH1	ARG	B	411	45.616	79.983	72.098	1.00	76.20
3304	NH2	ARG	B	411	47.548	79.604	70.599	1.00	82.01
3305	C	ARG	B	411	49.766	75.174	76.459	1.00	61.22
3306	O	ARG	B	411	49.183	74.996	77.456	1.00	65.25
3307	N	PRO	B	412	50.972	74.672	76.397	1.00	65.47
3308	CA	PRO	B	412	51.624	73.929	77.427	1.00	56.72
3309	CB	PRO	B	412	53.026	73.570	76.677	1.00	59.83
3310	CG	PRO	B	412	53.182	74.705	75.669	1.00	49.87
3311	CD	PRO	B	412	51.812	74.717	75.070	1.00	62.38
3312	C	PRO	B	412	51.804	74.467	78.748	1.00	62.03
3313	O	PRO	B	412	52.101	73.670	79.764	1.00	62.16
3314	N	GLN	B	413	52.033	75.746	78.871	1.00	62.83
3315	CA	GLN	B	413	52.334	76.137	80.246	1.00	63.94
3316	CB	GLN	B	413	53.399	77.310	80.331	1.00	64.15
3317	CG	GLN	B	413	54.633	76.893	81.238	1.00	63.58
3318	CD	GLN	B	413	55.637	75.992	80.326	1.00	76.45
3319	OE1	GLN	B	413	56.098	74.947	80.815	1.00	71.82
3320	NE2	GLN	B	413	55.851	76.315	79.015	1.00	75.29
3321	C	GLN	B	413	50.988	76.542	80.967	1.00	65.02
3322	O	GLN	B	413	50.959	77.209	82.072	1.00	67.96
3323	N	ASP	B	414	49.921	76.361	80.290	1.00	61.61
3324	CA	ASP	B	414	48.591	76.678	80.888	1.00	55.66
3325	CB	ASP	B	414	47.875	77.673	80.044	1.00	52.94
3326	CG	ASP	B	414	46.618	78.283	80.746	1.00	58.90
3327	OD1	ASP	B	414	45.845	79.161	80.143	1.00	56.74
3328	OD2	ASP	B	414	46.388	77.828	81.913	1.00	63.67
3329	C	ASP	B	414	47.819	75.431	81.040	1.00	47.48
3330	O	ASP	B	414	47.038	75.146	80.163	1.00	48.35
3331	N	GLN	B	415	48.057	74.745	82.083	1.00	47.21
3332	CA	GLN	B	415	47.333	73.518	82.410	1.00	48.12
3333	CB	GLN	B	415	47.994	72.750	83.478	1.00	45.31
3334	CG	GLN	B	415	49.319	72.153	82.945	1.00	67.82
3335	CD	GLN	B	415	50.253	71.461	84.067	1.00	89.11
3336	OE1	GLN	B	415	51.322	70.767	83.723	1.00	85.93
3337	NE2	GLN	B	415	49.893	71.715	85.443	1.00	83.43
3338	C	GLN	B	415	45.892	73.670	82.784	1.00	49.96
3339	O	GLN	B	415	45.079	72.671	82.694	1.00	43.98
3340	N	LEU	B	416	45.501	74.945	83.123	1.00	47.10
3341	CA	LEU	B	416	43.978	75.120	83.503	1.00	46.67
3342	CB	LEU	B	416	43.862	76.220	84.464	1.00	42.24
3343	CG	LEU	B	416	44.829	76.024	85.695	1.00	46.70
3344	CD1	LEU	B	416	44.294	77.038	86.573	1.00	50.30
3345	CD2	LEU	B	416	44.747	74.612	86.360	1.00	47.05
3346	C	LEU	B	416	43.141	75.423	82.359	1.00	47.55
3347	O	LEU	B	416	41.901	75.394	82.489	1.00	46.19
3348	N	ARG	B	417	43.750	75.643	81.152	1.00	43.61
3349	CA	ARG	B	417	42.849	75.985	79.953	1.00	45.54
3350	CB	ARG	B	417	43.772	76.394	78.800	1.00	47.18
3351	CG	ARG	B	417	43.003	76.958	77.607	1.00	52.36
3352	CD	ARG	B	417	44.016	77.709	76.629	1.00	43.04
3353	NE	ARG	B	417	43.332	77.806	75.322	1.00	48.08
3354	CZ	ARG	B	417	43.399	76.764	74.337	1.00	41.87
3355	NH1	ARG	B	417	43.918	75.624	74.633	1.00	27.87
3356	NH2	ARG	B	417	42.884	77.023	73.189	1.00	42.80
3357	C	ARG	B	417	41.925	74.750	79.581	1.00	44.39
3358	O	ARG	B	417	40.805	74.921	79.177	1.00	41.74
3359	N	PHE	B	418	42.410	73.546	79.764	1.00	41.38
3360	CA	PHE	B	418	41.673	72.442	79.433	1.00	44.48
3361	CB	PHE	B	418	42.645	71.168	79.588	1.00	38.64
3362	CG	PHE	B	418	41.886	69.814	79.523	1.00	40.60
3363	CD1	PHE	B	418	41.185	69.445	78.460	1.00	46.74
3364	CE1	PHE	B	418	40.649	68.249	78.287	1.00	37.85
3365	CZ	PHE	B	418	40.741	67.416	79.212	1.00	42.90
3366	CE2	PHE	B	418	41.415	67.737	80.358	1.00	50.83
3367	CD2	PHE	B	418	41.986	68.922	80.503	1.00	45.06
3368	C	PHE	B	418	40.423	72.254	80.431	1.00	38.51
3369	O	PHE	B	418	39.257	72.212	80.003	1.00	38.19
3370	N	PRO	B	419	40.670	72.255	81.676	1.00	39.54
3371	CA	PRO	B	419	39.392	72.192	82.585	1.00	34.08
3372	CB	PRO	B	419	40.078	72.081	84.039	1.00	32.89
3373	CG	PRO	B	419	41.394	72.736	83.884	1.00	33.97
3374	CD	PRO	B	419	41.834	72.229	82.436	1.00	36.76
3375	C	PRO	B	419	38.514	73.382	82.451	1.00	33.49
3376	O	PRO	B	419	37.294	73.252	82.531	1.00	30.11
3377	N	ARG	B	420	39.024	74.565	82.149	1.00	34.06
3378	CA	ARG	B	420	38.014	75.588	81.942	1.00	40.49
3379	CB	ARG	B	420	38.491	77.117	81.933	1.00	32.76
3380	CG	ARG	B	420	39.683	77.385	81.659	1.00	56.46
3381	CD	ARG	B	420	40.184	78.915	82.102	1.00	62.86
3382	NE	ARG	B	420	41.274	79.587	81.235	1.00	64.61
3383	CZ	ARG	B	420	42.623	79.785	81.598	1.00	72.93
3384	NH1	ARG	B	420	43.135	79.398	82.846	1.00	69.01
3385	NH2	ARG	B	420	43.371	80.432	80.745	1.00	67.63
3386	C	ARG	B	420	37.183	75.268	80.668	1.00	39.24
3387	O	ARG	B	420	35.978	75.681	80.562	1.00	36.26
3388	N	MET	B	421	37.861	74.665	79.714	1.00	38.39
3389	CA	MET	B	421	37.144	74.346	78.420	1.00	37.04
3390	CB	MET	B	421	37.987	73.658	77.523	1.00	41.19
3391	CG	MET	B	421	37.969	73.936	76.045	1.00	45.40
3392	SD	MET	B	421	39.536	73.304	75.190	1.00	51.40
3393	CE	MET	B	421	40.851	74.414	75.729	1.00	49.13
3394	C	MET	B	421	35.978	73.351	78.829	1.00	37.69
3395	O	MET	B	421	34.903	73.407	78.309	1.00	32.26
3396	N	LEU	B	422	36.355	72.416	79.710	1.00	36.06
3397	CA	LEU	B	422	35.330	71.374	79.968	1.00	35.29
3398	CB	LEU	B	422	36.000	70.198	80.904	1.00	36.87
3399	CG	LEU	B	422	36.653	69.113	80.172	1.00	35.04
3400	CD1	LEU	B	422	36.781	67.981	81.004	1.00	33.56
3401	CD2	LEU	B	422	35.908	68.687	78.963	1.00	36.81
3402	C	LEU	B	422	34.253	71.997	80.830	1.00	33.87
3403	O	LEU	B	422	33.061	71.535	80.667	1.00	33.92
3404	N	MET	B	423	34.585	72.912	81.650	1.00	29.57
3405	CA	MET	B	423	33.600	73.624	82.403	1.00	32.22
3406	CB	MET	B	423	34.294	74.536	83.477	1.00	31.57
3407	CG	MET	B	423	34.735	73.357	84.683	1.00	35.36
3408	SD	MET	B	423	35.107	74.163	86.203	1.00	53.40
3409	CE	MET	B	423	36.696	74.684	85.904	1.00	64.75
3410	C	MET	B	423	32.629	74.440	81.627	1.00	35.18
3411	O	MET	B	423	31.546	74.797	82.080	1.00	33.67
3412	N	LYS	B	424	32.978	74.679	80.330	1.00	31.98
3413	CA	LYS	B	424	32.001	75.338	79.457	1.00	34.96
3414	CB	LYS	B	424	32.566	75.736	78.047	1.00	31.64
3415	CG	LYS	B	424	33.665	76.876	78.245	1.00	33.70
3416	CD	LYS	B	424	33.028	78.047	78.937	1.00	37.16
3417	CE	LYS	B	424	33.860	79.098	79.095	1.00	51.16
3418	NZ	LYS	B	424	33.356	80.056	80.511	1.00	56.80
3419	C	LYS	B	424	30.799	74.347	79.172	1.00	27.90
3420	O	LYS	B	424	29.708	74.759	78.800	1.00	32.10
3421	N	LEU	B	425	31.088	73.093	79.416	1.00	26.30
3422	CA	LEU	B	425	29.951	72.098	79.182	1.00	27.36
3423	CB	LEU	B	425	30.568	70.643	79.277	1.00	29.69
3424	CG	LEU	B	425	31.624	70.197	78.046	1.00	33.03
3425	CD1	LEU	B	425	32.018	68.907	78.317	1.00	27.54
3426	CD2	LEU	B	425	30.744	70.186	76.580	1.00	28.56
3427	C	LEU	B	425	29.064	72.274	80.333	1.00	30.48
3428	O	LEU	B	425	27.778	72.085	80.229	1.00	28.12
3429	N	VAL	B	426	29.611	72.729	81.514	1.00	25.81
3430	CA	VAL	B	426	28.680	73.006	82.672	1.00	27.78
3431	CB	VAL	B	426	29.545	73.358	84.058	1.00	22.37
3432	CG1	VAL	B	426	28.573	73.585	85.124	1.00	22.01
3433	CG2	VAL	B	426	30.318	72.211	84.478	1.00	22.98
3434	C	VAL	B	426	27.886	74.163	82.329	1.00	28.34
3435	O	VAL	B	426	26.653	74.131	82.586	1.00	28.22
3436	N	SER	B	427	28.478	75.219	81.832	1.00	25.84
3437	CA	SER	B	427	27.549	76.284	81.534	1.00	32.96
3438	CB	SER	B	427	28.249	77.696	81.257	1.00	27.16
3439	OG	SER	B	427	29.452	77.559	80.757	1.00	46.67
3440	C	SER	B	427	26.494	76.012	80.378	1.00	32.01
3441	O	SER	B	427	25.426	76.561	80.366	1.00	28.93
3442	N	LEU	B	428	26.952	75.178	79.412	1.00	32.02
3443	CA	LEU	B	428	25.988	74.865	78.278	1.00	32.40
3444	CB	LEU	B	428	26.717	73.884	77.281	1.00	27.32
3445	CG	LEU	B	428	27.761	74.628	76.300	1.00	39.39
3446	CD1	LEU	B	428	28.596	73.661	75.609	1.00	36.25
3447	CD2	LEU	B	428	26.946	75.485	75.166	1.00	33.44
3448	C	LEU	B	428	24.795	74.142	78.896	1.00	31.04
3449	O	LEU	B	428	23.657	74.287	78.397	1.00	35.47
3450	N	ARG	B	429	24.965	73.285	79.880	1.00	32.04
3451	CA	ARG	B	429	23.903	72.579	80.461	1.00	32.80
3452	CB	ARG	B	429	24.442	71.546	81.475	1.00	30.73
3453	CG	ARG	B	429	23.264	70.488	81.922	1.00	40.21
3454	CD	ARG	B	429	23.022	69.498	80.606	1.00	33.81
3455	NE	ARG	B	429	24.243	68.638	80.318	1.00	28.60
3456	CZ	ARG	B	429	24.368	67.415	80.882	1.00	32.87
3457	NH1	ARG	B	429	23.505	67.018	81.810	1.00	30.23
3458	NH2	ARG	B	429	25.267	66.574	80.457	1.00	32.14
3459	C	ARG	B	429	22.813	73.454	80.953	1.00	33.59
3460	O	ARG	B	429	21.657	73.192	80.936	1.00	37.09
3461	N	THR	B	430	23.201	74.544	81.614	1.00	38.72
3462	CA	THR	B	430	22.306	75.483	82.243	1.00	37.01
3463	CB	THR	B	430	23.120	76.468	83.049	1.00	34.12
3464	OG1	THR	B	430	23.513	75.732	84.268	1.00	38.65
3465	CG2	THR	B	430	22.217	77.724	83.460	1.00	32.93
3466	C	THR	B	430	21.592	76.362	80.972	1.00	39.46
3467	O	THR	B	430	20.447	76.527	81.004	1.00	35.20
3468	N	LEU	B	431	22.416	76.778	80.127	1.00	36.01
3469	CA	LEU	B	431	21.991	77.479	78.958	1.00	42.02
3470	CB	LEU	B	431	23.139	77.674	78.016	1.00	31.12
3471	CG	LEU	B	431	24.016	78.912	78.364	1.00	35.43
3472	CD1	LEU	B	431	25.168	78.964	77.609	1.00	34.81
3473	CD2	LEU	B	431	23.470	80.210	78.169	1.00	37.53
3474	C	LEU	B	431	20.850	76.641	78.326	1.00	43.70
3475	O	LEU	B	431	19.839	77.114	78.022	1.00	44.09
3476	N	SER	B	432	21.079	75.379	78.252	1.00	46.54
3477	CA	SER	B	432	20.086	74.518	77.706	1.00	49.15
3478	CB	SER	B	432	20.435	73.053	77.806	1.00	48.94
3479	OG	SER	B	432	19.413	72.247	77.466	1.00	45.95
3480	C	SER	B	432	18.809	74.754	78.317	1.00	49.69
3481	O	SER	B	432	17.776	74.784	77.516	1.00	54.26
3482	N	SER	B	433	18.724	74.768	79.580	1.00	47.14
3483	CA	SER	B	433	17.494	74.980	80.296	1.00	47.20
3484	CB	SER	B	433	17.739	74.865	81.794	1.00	40.62
3485	OG	SER	B	433	18.081	73.584	82.108	1.00	49.73
3486	C	SER	B	433	16.946	76.447	80.127	1.00	49.50
3487	O	SER	B	433	15.794	76.592	80.321	1.00	51.14
3488	N	VAL	B	434	17.789	77.435	79.846	1.00	49.22
3489	CA	VAL	B	434	17.229	78.708	79.746	1.00	54.55
3490	CB	VAL	B	434	18.304	79.836	79.960	1.00	54.92
3491	CG1	VAL	B	434	18.835	79.844	81.638	1.00	50.26
3492	CG2	VAL	B	434	19.391	79.488	79.048	1.00	57.15
3493	C	VAL	B	434	16.649	78.814	78.329	1.00	51.87
3494	O	VAL	B	434	15.982	79.691	78.010	1.00	51.61
3495	N	HIS	B	435	17.105	78.026	77.512	1.00	50.38
3496	CA	HIS	B	435	16.629	77.927	76.158	1.00	55.58
3497	CB	HIS	B	435	17.473	77.180	75.326	1.00	56.02
3498	CG	HIS	B	435	16.897	76.877	74.054	1.00	69.93
3499	ND1	HIS	B	435	17.388	77.444	72.810	1.00	81.64
3500	CE1	HIS	B	435	16.679	76.915	71.782	1.00	69.58
3501	NE2	HIS	B	435	15.850	75.956	72.306	1.00	62.02
3502	CD2	HIS	B	435	16.030	75.888	73.694	1.00	64.25
3503	C	HIS	B	435	15.424	77.348	76.187	1.00	59.49
3504	O	HIS	B	435	14.621	77.689	75.624	1.00	63.73
3505	N	SER	B	436	15.158	76.559	77.155	1.00	62.97
3506	CA	SER	B	436	13.838	75.852	77.250	1.00	61.17
3507	CB	SER	B	436	14.017	74.539	77.996	1.00	59.04
3508	OG	SER	B	436	12.958	74.100	78.611	1.00	57.03
3509	C	SER	B	436	12.781	76.645	77.922	1.00	64.10
3510	O	SER	B	436	11.687	76.568	77.568	1.00	69.87
3511	N	GLU	B	437	12.941	77.315	78.991	1.00	65.48
3512	CA	GLU	B	437	11.928	78.060	79.623	1.00	68.26
3513	CB	GLU	B	437	12.252	78.369	81.135	1.00	69.08
3514	CG	GLU	B	437	13.770	78.578	81.471	1.00	77.67
3515	CD	GLU	B	437	13.995	78.877	82.975	1.00	84.13
3516	OE1	GLU	B	437	12.918	79.204	83.662	1.00	96.00
3517	OE2	GLU	B	437	15.114	78.770	83.468	1.00	88.44
3518	C	GLU	B	437	11.735	79.431	78.733	1.00	69.36
3519	O	GLU	B	437	10.776	80.203	78.843	1.00	74.35
3520	N	GLN	B	438	12.603	79.707	77.908	1.00	63.83
3521	CA	GLN	B	438	12.404	80.735	77.024	1.00	61.73
3522	CB	GLN	B	438	13.664	81.035	76.242	1.00	54.68
3523	CG	GLN	B	438	13.751	81.379	74.980	1.00	53.55
3524	CD	GLN	B	438	13.375	83.010	74.543	1.00	64.01
3525	OE1	GLN	B	438	12.462	83.552	75.147	1.00	55.61
3526	NE2	GLN	B	438	14.163	83.611	73.698	1.00	54.83
3527	C	GLN	B	438	11.392	80.405	76.119	1.00	71.21
3528	O	GLN	B	438	10.254	81.176	75.834	1.00	77.04
3529	N	VAL	B	439	11.707	79.347	75.472	1.00	73.56
3530	CA	VAL	B	439	10.781	78.826	74.528	1.00	77.85
3531	CB	VAL	B	439	11.370	77.428	73.962	1.00	77.61
3532	CG1	VAL	B	439	10.095	76.647	73.195	1.00	83.57
3533	CG2	VAL	B	439	12.539	77.639	73.039	1.00	72.22
3534	C	VAL	B	439	9.319	78.686	75.069	1.00	76.34
3535	O	VAL	B	439	8.341	78.881	74.376	1.00	74.98
3536	N	PHE	B	440	9.206	78.273	76.317	1.00	79.29
3537	CA	PHE	B	440	7.996	78.110	76.985	1.00	80.16
3538	CB	PHE	B	440	8.225	77.599	78.238	1.00	78.89
3539	CG	PHE	B	440	7.054	77.724	79.098	1.00	92.23
3540	CD1	PHE	B	440	5.772	77.208	78.742	1.00	99.43
3541	CE1	PHE	B	440	4.596	77.379	79.606	1.00	98.72
3542	CZ	PHE	B	440	4.740	78.132	80.830	1.00	100.73
3543	CE2	PHE	B	440	5.999	78.723	81.122	1.00	99.88
3544	CD2	PHE	B	440	7.139	78.412	80.292	1.00	101.24
3545	C	PHE	B	440	7.379	79.541	77.198	1.00	85.20
3546	O	PHE	B	440	6.111	79.770	77.380	1.00	84.97
3547	N	ALA	B	441	8.196	80.588	77.096	1.00	86.29
3548	CA	ALA	B	441	7.624	81.976	77.265	1.00	80.96
3549	CB	ALA	B	441	8.536	82.970	77.776	1.00	74.47
3550	C	ALA	B	441	7.220	82.419	75.924	1.00	80.06
3551	O	ALA	B	441	6.132	83.160	75.872	1.00	81.05
3552	N	LEU	B	442	8.025	82.135	74.899	1.00	78.80
3553	CA	LEU	B	442	7.568	82.409	73.552	1.00	82.11
3554	CB	LEU	B	442	8.443	81.895	72.505	1.00	81.69
3555	CG	LEU	B	442	9.624	82.735	72.473	1.00	83.56
3556	CD1	LEU	B	442	10.612	82.111	71.506	1.00	80.19
3557	CD2	LEU	B	442	9.248	84.129	72.041	1.00	77.57
3558	C	LEU	B	442	6.020	81.763	73.158	1.00	85.14
3559	O	LEU	B	442	5.034	82.354	72.611	1.00	85.70
3560	N	ARG	B	443	5.815	80.602	73.482	1.00	85.53
3561	CA	ARG	B	443	4.545	80.084	73.343	1.00	87.83
3562	CB	ARG	B	443	4.619	78.683	73.798	1.00	91.21
3563	CG	ARG	B	443	3.342	77.748	73.912	1.00	98.16
3564	CD	ARG	B	443	3.700	76.185	73.899	1.00	92.87
3565	NE	ARG	B	443	4.850	75.964	72.925	1.00	93.04
3566	CZ	ARG	B	443	4.869	76.230	71.575	1.00	96.00
3567	NH1	ARG	B	443	3.705	76.661	70.926	1.00	102.88
3568	NH2	ARG	B	443	5.990	75.956	70.841	1.00	82.77
3569	C	ARG	B	443	3.639	80.845	74.249	1.00	90.37
3570	O	ARG	B	443	2.454	81.127	73.835	1.00	92.49
3571	N	ALA	B	444	4.064	81.126	75.507	1.00	93.02
3572	CA	ALA	B	444	3.244	81.840	76.538	1.00	96.93
3573	CB	ALA	B	444	3.975	82.137	77.768	1.00	95.28
3574	C	ALA	B	444	2.606	83.229	75.946	1.00	102.42
3575	O	ALA	B	444	1.426	83.696	76.300	1.00	101.79
3576	N	GLN	B	445	3.350	83.862	75.003	1.00	102.89
3577	CA	GLN	B	445	2.908	85.111	74.382	1.00	101.00
3578	CB	GLN	B	445	4.009	86.219	74.353	1.00	100.25
3579	CG	GLN	B	445	3.857	87.230	75.518	1.00	99.82
3580	CD	GLN	B	445	2.569	88.091	75.407	1.00	104.75
3581	OE1	GLN	B	445	1.973	88.471	76.447	1.00	101.58
3582	NE2	GLN	B	445	2.156	88.408	74.153	1.00	101.48
3583	C	GLN	B	445	2.285	84.948	73.003	1.00	101.79
3584	O	GLN	B	445	1.020	85.221	72.835	1.00	107.41
3585	N	ASP	B	446	3.080	84.594	72.015	1.00	98.12
3586	CA	ASP	B	446	2.583	84.498	70.639	1.00	97.10
3587	CB	ASP	B	446	3.552	85.344	69.702	1.00	95.60
3588	CG	ASP	B	446	3.395	86.855	69.975	1.00	106.20
3589	OD1	ASP	B	446	2.221	87.369	70.349	1.00	105.08
3590	OD2	ASP	B	446	4.448	87.602	69.878	1.00	103.97
3591	C	ASP	B	446	2.492	83.188	70.052	1.00	90.74
3592	O	ASP	B	446	1.567	82.679	69.995	1.00	91.91
3593	N	LYS	B	447	3.603	82.850	69.535	1.00	91.18
3594	CA	LYS	B	447	3.986	81.746	68.713	1.00	92.43
3595	CB	LYS	B	447	4.987	82.291	67.750	1.00	92.71
3596	CG	LYS	B	447	5.694	83.445	68.230	1.00	98.18
3597	CD	LYS	B	447	6.175	83.217	69.631	1.00	93.65
3598	CE	LYS	B	447	6.434	84.685	70.142	1.00	117.01
3599	NZ	LYS	B	447	5.874	85.264	71.584	1.00	106.41
3600	C	LYS	B	447	4.554	80.409	69.258	1.00	90.83
3601	O	LYS	B	447	5.379	80.381	70.262	1.00	90.09
3602	N	LYS	B	448	4.126	79.366	68.489	1.00	88.27
3603	CA	LYS	B	448	4.415	78.029	68.617	1.00	82.99
3604	CB	LYS	B	448	3.292	77.102	68.031	1.00	88.96
3605	CG	LYS	B	448	1.812	77.531	68.035	1.00	85.79
3606	CD	LYS	B	448	1.034	76.813	67.089	1.00	87.76
3607	CE	LYS	B	448	−0.305	77.719	66.689	1.00	92.06
3608	NZ	LYS	B	448	−1.490	76.757	66.440	1.00	92.58
3609	C	LYS	B	448	5.674	77.916	67.825	1.00	84.11
3610	O	LYS	B	448	6.166	78.859	67.367	1.00	82.85
3611	N	LEU	B	449	6.304	76.694	67.799	1.00	87.83
3612	CA	LEU	B	449	7.532	76.347	67.134	1.00	80.67
3613	CB	LEU	B	449	8.129	75.591	68.224	1.00	80.57
3614	CG	LEU	B	449	8.368	76.165	69.573	1.00	78.58
3615	CD1	LEU	B	449	8.768	74.939	70.442	1.00	82.07
3616	CD2	LEU	B	449	9.688	77.084	69.684	1.00	74.82
3617	C	LEU	B	449	7.267	75.353	65.939	1.00	77.71
3618	O	LEU	B	449	6.382	74.513	66.111	1.00	77.67
3619	N	PRO	B	450	8.133	75.376	64.934	1.00	71.21
3620	CA	PRO	B	450	8.214	74.509	63.793	1.00	73.98
3621	CB	PRO	B	450	9.454	74.915	63.105	1.00	68.98
3622	CG	PRO	B	450	9.464	76.294	63.381	1.00	67.90
3623	CD	PRO	B	450	9.142	76.345	64.922	1.00	69.62
3624	C	PRO	B	450	8.135	73.055	64.176	1.00	77.78
3625	O	PRO	B	450	8.994	72.666	64.840	1.00	83.46
3626	N	PRO	B	451	7.029	72.292	63.742	1.00	79.07
3627	CA	PRO	B	451	6.995	70.864	64.051	1.00	72.39
3628	CB	PRO	B	451	6.181	70.317	62.928	1.00	72.77
3629	CG	PRO	B	451	5.066	71.463	62.706	1.00	80.55
3630	CD	PRO	B	451	6.059	72.638	62.734	1.00	73.48
3631	C	PRO	B	451	8.377	70.203	64.101	1.00	69.63
3632	O	PRO	B	451	8.447	69.326	64.847	1.00	74.53
3633	N	LEU	B	452	9.267	70.673	63.327	1.00	67.85
3634	CA	LEU	B	452	10.622	70.096	63.322	1.00	68.90
3635	CB	LEU	B	452	11.275	70.644	62.138	1.00	63.66
3636	CG	LEU	B	452	12.609	69.903	62.065	1.00	67.29
3637	CD1	LEU	B	452	12.666	68.400	62.235	1.00	78.79
3638	CD2	LEU	B	452	13.805	70.222	60.707	1.00	64.79
3639	C	LEU	B	452	11.498	70.348	64.590	1.00	76.88
3640	O	LEU	B	452	12.329	69.590	65.011	1.00	76.42
3641	N	LEU	B	453	11.215	71.485	65.226	1.00	75.46
3642	CA	LEU	B	453	11.931	71.872	66.324	1.00	74.07
3643	CB	LEU	B	453	12.344	73.481	66.225	1.00	76.58
3644	CG	LEU	B	453	13.177	73.917	65.021	1.00	73.28
3645	CD1	LEU	B	453	13.359	75.377	64.905	1.00	84.76
3646	CD2	LEU	B	453	14.370	73.304	65.144	1.00	83.41
3647	C	LEU	B	453	10.997	71.555	67.373	1.00	72.22
3648	O	LEU	B	453	11.406	71.504	68.556	1.00	73.02
3649	N	SER	B	454	9.726	71.580	67.055	1.00	70.01
3650	CA	SER	B	454	8.763	71.270	68.090	1.00	73.57
3651	CB	SER	B	454	7.450	71.287	67.508	1.00	71.14
3652	OG	SER	B	454	6.551	70.409	68.142	1.00	74.80
3653	C	SER	B	454	9.104	69.817	68.646	1.00	78.17
3654	O	SER	B	454	8.730	69.476	69.704	1.00	73.62
3655	N	GLU	B	455	9.847	69.020	67.786	1.00	82.20
3656	CA	GLU	B	455	10.159	67.663	68.045	1.00	84.44
3657	CB	GLU	B	455	10.787	66.996	66.773	1.00	89.19
3658	CG	GLU	B	455	10.166	65.593	66.486	1.00	96.86
3659	CD	GLU	B	455	8.492	65.711	66.504	1.00	115.60
3660	OE1	GLU	B	455	7.775	66.633	65.744	1.00	117.40
3661	OE2	GLU	B	455	7.931	64.946	67.394	1.00	106.60
3662	C	GLU	B	455	11.219	67.481	69.107	1.00	80.43
3663	O	GLU	B	455	11.181	66.527	69.876	1.00	76.11
3664	N	ILE	B	456	12.137	68.411	69.062	1.00	75.65
3665	CA	ILE	B	456	13.198	68.334	70.069	1.00	80.83
3666	CB	ILE	B	456	14.488	68.753	69.504	1.00	78.83
3667	CG1	ILE	B	456	14.135	68.610	67.952	1.00	73.26
3668	CD1	ILE	B	456	15.216	69.380	67.297	1.00	77.02
3669	CG2	ILE	B	456	15.625	67.777	69.854	1.00	78.31
3670	C	ILE	B	456	13.115	69.203	71.185	1.00	76.42
3671	O	ILE	B	456	13.565	68.806	72.158	1.00	79.20
3672	N	TRP	B	457	12.365	70.242	71.086	1.00	71.39
3673	CA	TRP	B	457	12.292	71.151	72.176	1.00	76.38
3674	CB	TRP	B	457	12.896	72.533	71.803	1.00	68.20
3675	CG	TRP	B	457	14.232	72.476	71.499	1.00	68.30
3676	CD1	TRP	B	457	15.126	71.846	72.231	1.00	57.85
3677	NE1	TRP	B	457	16.342	71.998	71.601	1.00	64.57
3678	CE2	TRP	B	457	16.274	72.814	70.549	1.00	61.33
3679	CD2	TRP	B	457	14.970	73.180	70.458	1.00	58.63
3680	CE3	TRP	B	457	14.636	74.007	69.475	1.00	68.32
3681	CZ3	TRP	B	457	15.566	74.400	68.431	1.00	53.89
3682	CH2	TRP	B	457	16.898	74.074	68.568	1.00	59.04
3683	CZ2	TRP	B	457	17.320	73.320	69.692	1.00	60.47
3684	C	TRP	B	457	11.004	71.380	73.030	1.00	79.49
3685	O	TRP	B	457	11.014	71.998	74.102	1.00	84.07
3686	N	ASP	B	458	9.909	70.953	72.589	1.00	81.55
3687	CA	ASP	B	458	8.792	71.192	73.405	1.00	88.84
3688	CB	ASP	B	458	7.559	71.444	72.515	1.00	91.13
3689	CG	ASP	B	458	6.894	72.822	72.763	1.00	93.15
3690	OD1	ASP	B	458	6.473	73.295	71.709	1.00	89.76
3691	OD2	ASP	B	458	6.706	73.413	73.940	1.00	80.41
3692	C	ASP	B	458	8.384	70.242	74.504	1.00	94.89
3693	O	ASP	B	458	8.794	70.470	75.790	1.00	103.33
3694	N	VAL	B	459	7.573	69.231	74.181	1.00	94.94
3695	CA	VAL	B	459	7.086	68.485	75.295	1.00	101.47
3696	CB	VAL	B	459	5.754	69.037	75.851	1.00	99.71
3697	CG1	VAL	B	459	5.476	68.479	77.239	1.00	105.10
3698	CG2	VAL	B	459	5.911	70.574	76.027	1.00	109.26
3699	C	VAL	B	459	7.116	66.947	75.396	1.00	104.18
3700	O	VAL	B	459	7.313	66.156	74.438	1.00	101.60
3701	N	HIS	B	460	6.874	66.555	76.675	1.00	107.43
3702	CA	HIS	B	460	7.073	65.202	77.282	1.00	107.42
3703	CB	HIS	B	460	8.072	65.379	78.452	1.00	107.83
3704	CG	HIS	B	460	9.321	64.541	78.343	1.00	106.96
3705	ND1	HIS	B	460	9.320	63.161	78.038	1.00	106.22
3706	CE1	HIS	B	460	10.563	62.706	78.071	1.00	102.14
3707	NE2	HIS	B	460	11.360	63.731	78.314	1.00	105.06
3708	CD2	HIS	B	460	10.609	64.889	78.537	1.00	101.46
3709	C	HIS	B	460	5.855	64.306	77.786	1.00	107.54
3710	O	HIS	B	460	5.948	63.795	78.950	1.00	102.46
3711	OXT	HIS	B	460	4.828	64.047	77.024	1.00	111.13
3712	F28	MON	C	1	19.808	64.508	97.381	1.00	43.78
3713	C23	MON	C	1	19.416	65.568	97.788	1.00	45.54
3714	F26	MON	C	1	20.407	66.480	97.502	1.00	50.09
3715	F27	MON	C	1	18.437	66.125	96.966	1.00	56.18
3716	C19	MON	C	1	18.942	65.415	99.375	1.00	54.41
3717	N17	MON	C	1	18.486	66.619	99.923	1.00	52.26
3718	C16	MON	C	1	17.301	67.177	99.588	1.00	52.94
3719	C9	MON	C	1	17.046	68.586	99.514	1.00	59.65
3720	C4	MON	C	1	15.773	69.251	99.221	1.00	44.55
3721	C8	MON	C	1	16.109	66.497	99.440	1.00	58.47
3722	C3	MON	C	1	14.797	67.221	99.189	1.00	44.43
3723	C1	MON	C	1	14.619	68.582	99.044	1.00	39.54
3724	C2	MON	C	1	13.324	69.219	98.845	1.00	43.70
3725	O7	MON	C	1	13.595	70.614	98.325	1.00	42.48
3726	C6	MON	C	1	12.271	68.544	97.976	1.00	41.28
3727	F15	MON	C	1	11.230	69.333	97.783	1.00	46.95
3728	F14	MON	C	1	11.833	67.406	98.331	1.00	43.11
3729	F13	MON	C	1	12.731	68.407	96.707	1.00	43.88
3730	C5	MON	C	1	12.672	69.514	100.243	1.00	42.61
3731	F12	MON	C	1	11.527	70.162	100.099	1.00	49.55
3732	F11	MON	C	1	12.431	68.417	100.854	1.00	45.69
3733	F10	MON	C	1	13.360	70.263	101.134	1.00	39.44
3734	S18	MON	C	1	19.334	66.990	101.578	1.00	78.47
3735	O21	MON	C	1	18.906	68.160	102.353	1.00	74.53
3736	O22	MON	C	1	20.928	66.810	101.606	1.00	69.11
3737	C20	MON	C	1	18.676	65.896	102.715	1.00	59.07
3738	C24	MON	C	1	19.476	64.928	103.096	1.00	64.28
3739	C29	MON	C	1	19.096	63.952	103.934	1.00	70.23
3740	C31	MON	C	1	17.745	63.902	104.213	1.00	73.30
3741	C30	MON	C	1	16.831	64.859	103.631	1.00	67.05
3742	C25	MON	C	1	17.311	65.865	102.880	1.00	57.46
3743	F28	MON	D	1	22.651	80.942	70.764	1.00	69.44
3744	C23	MON	D	1	21.798	80.169	70.148	1.00	57.82
3745	F26	MON	D	1	22.543	79.119	70.213	1.00	62.78
3746	F27	MON	D	1	20.755	80.001	70.992	1.00	61.86
3747	C19	MON	D	1	21.215	80.654	68.630	1.00	75.45
3748	N17	MON	D	1	20.440	79.761	67.906	1.00	76.60
3749	C16	MON	D	1	19.149	79.599	68.328	1.00	68.06
3750	C9	MON	D	1	18.512	78.416	68.236	1.00	67.68
3751	C4	MON	D	1	17.186	78.252	68.702	1.00	64.13
3752	C8	MON	D	1	18.382	80.560	68.704	1.00	67.84
3753	C3	MON	D	1	17.052	80.405	69.140	1.00	71.18
3754	C1	MON	D	1	16.449	79.271	69.191	1.00	69.42
3755	C2	MON	D	1	14.956	79.086	69.415	1.00	68.85
3756	O7	MON	D	1	14.845	77.784	69.704	1.00	73.28
3757	C6	MON	D	1	14.333	80.022	70.298	1.00	73.50
3758	F15	MON	D	1	13.033	79.709	70.767	1.00	73.67
3759	F14	MON	D	1	14.461	81.177	69.631	1.00	75.64
3760	F13	MON	D	1	14.843	80.117	71.635	1.00	78.70
3761	C5	MON	D	1	14.026	79.078	68.126	1.00	65.40
3762	F12	MON	D	1	12.814	78.813	68.422	1.00	56.90
3763	F11	MON	D	1	14.145	80.191	67.512	1.00	65.11
3764	F10	MON	D	1	14.594	78.322	67.116	1.00	67.88
3765	S18	MON	D	1	20.952	79.543	66.221	1.00	91.37
3766	O21	MON	D	1	20.850	80.997	65.429	1.00	87.99
3767	O22	MON	D	1	19.809	79.087	65.442	1.00	87.36
3768	C20	MON	D	1	22.391	78.840	65.550	1.00	83.26
3769	C24	MON	D	1	22.355	78.117	64.483	1.00	84.25
3770	C29	MON	D	1	23.485	77.423	64.112	1.00	105.04
3771	C31	MON	D	1	24.753	77.652	64.776	1.00	98.94
3772	C30	MON	D	1	24.682	78.634	65.738	1.00	97.53
3773	C25	MON	D	1	23.523	79.120	66.188	1.00	88.16
3774	F28	MON	E	1	18.863	67.289	66.183	0.68	73.54
3775	C23	MON	E	1	17.901	66.491	66.389	0.68	58.02
3776	F26	MON	E	1	18.133	66.060	67.479	0.68	59.55
3777	F27	MON	E	1	16.774	67.178	66.683	0.68	68.46
3778	C19	MON	E	1	17.457	65.561	65.236	0.68	67.48
3779	N17	MON	E	1	16.984	64.432	65.323	0.68	70.21
3780	C16	MON	E	1	17.580	63.374	64.933	0.68	62.25
3781	C9	MON	E	1	17.739	63.087	63.589	0.68	61.03
3782	C4	MON	E	1	18.513	61.940	63.159	0.68	61.27
3783	C8	MON	E	1	18.041	62.421	65.826	0.68	61.34
3784	C3	MON	E	1	18.743	61.167	65.343	0.68	54.14
3785	C1	MON	E	1	18.987	60.960	64.029	0.68	52.79
3786	C2	MON	E	1	19.619	59.651	63.617	0.68	64.04
3787	O7	MON	E	1	20.348	59.164	64.675	0.68	55.74
3788	C6	MON	E	1	18.393	58.583	63.328	0.68	53.08
3789	F15	MON	E	1	19.132	57.425	63.011	0.68	57.55
3790	F14	MON	E	1	17.755	58.998	62.281	0.68	54.49
3791	F13	MON	E	1	17.552	58.341	64.329	0.68	53.53
3792	C5	MON	E	1	20.593	59.844	62.509	0.68	66.00
3793	F12	MON	E	1	21.145	58.702	62.164	0.68	71.56
3794	F11	MON	E	1	20.052	60.351	61.466	0.68	54.24
3795	F10	MON	E	1	21.505	60.695	62.917	0.68	58.61
3796	S18	MON	E	1	15.447	64.822	65.753	0.68	83.56
3797	O21	MON	E	1	14.518	65.274	64.634	0.68	93.03
3798	O22	MON	E	1	15.130	65.547	66.980	0.68	80.99
3799	C20	MON	E	1	14.228	63.373	65.915	0.68	77.88
3800	C24	MON	E	1	13.224	63.230	66.928	0.68	68.92
3801	C29	MON	E	1	12.436	62.100	67.028	0.68	73.62
3802	C31	MON	E	1	12.646	60.970	66.232	0.68	70.40
3803	C30	MON	E	1	13.636	61.041	65.250	0.68	82.63
3804	C25	MON	E	1	14.431	62.235	65.055	0.68	79.09
3805	O	HOH	W	2	28.763	91.475	95.071	1.00	39.87
3806	O	HOH	W	3	46.618	53.254	66.806	1.00	48.01
3807	O	HOH	W	4	28.768	71.285	63.182	1.00	59.05
3808	O	HOH	W	5	28.489	58.092	96.686	1.00	20.96
3809	O	HOH	W	6	33.736	54.376	64.043	1.00	59.64
3810	O	HOH	W	7	14.597	69.385	75.168	1.00	72.38
3811	O	HOH	W	8	18.802	70.558	72.353	1.00	53.73
3812	O	HOH	W	9	33.884	83.187	70.518	1.00	55.24
3813	O	HOH	W	10	22.912	96.047	71.861	1.00	55.92
3814	O	HOH	W	11	18.761	96.307	66.664	1.00	60.45
3815	O	HOH	W	12	30.903	80.413	80.693	1.00	40.55
3816	O	HOH	W	13	25.337	91.192	77.632	1.00	72.99
3817	O	HOH	W	14	34.871	85.846	83.379	1.00	46.70
3818	O	HOH	W	15	29.736	65.196	80.159	1.00	57.86
3819	O	HOH	W	16	23.629	94.190	90.119	1.00	28.94
3820	O	HOH	W	17	17.330	58.608	82.548	1.00	54.28
3821	O	HOH	W	18	34.366	59.527	79.752	1.00	55.89
3822	O	HOH	W	19	44.065	83.193	100.457	1.00	79.63
3823	O	HOH	W	20	30.075	69.132	105.305	1.00	75.54
3824	O	HOH	W	21	30.061	70.867	103.341	1.00	62.79
3825	O	HOH	W	22	14.365	58.842	111.595	1.00	56.40
3826	O	HOH	W	23	2.852	72.225	103.788	1.00	58.58
3827	O	HOH	W	24	8.238	72.237	111.123	1.00	64.18
3828	O	HOH	W	25	35.890	83.185	103.291	1.00	37.51
3829	O	HOH	W	26	40.472	81.808	96.420	1.00	50.13
3830	O	HOH	W	27	34.642	91.721	104.562	1.00	51.95
3831	O	HOH	W	28	26.151	85.227	103.132	1.00	62.19
3832	O	HOH	W	29	20.708	86.222	94.639	1.00	37.83
3833	O	HOH	W	30	20.141	75.780	95.140	1.00	28.16
3834	O	HOH	W	31	23.371	64.729	103.731	1.00	54.24
3835	O	HOH	W	32	29.196	52.130	105.039	1.00	54.15
3836	O	HOH	W	33	21.723	58.410	113.952	1.00	56.23
3837	O	HOH	W	34	14.086	56.629	108.755	1.00	64.61
3838	O	HOH	W	35	14.464	63.003	85.862	1.00	60.12
3839	O	HOH	W	36	34.911	56.785	97.989	1.00	50.01
3840	O	HOH	W	37	38.951	63.054	106.082	1.00	52.37
3841	O	HOH	W	38	31.326	77.306	84.904	1.00	45.71
3842	O	HOH	W	39	29.270	92.583	85.702	1.00	35.13
3843	O	HOH	W	40	47.229	63.071	97.529	1.00	61.45
3844	O	HOH	W	41	46.228	60.875	98.976	1.00	63.36
3845	O	HOH	W	42	40.920	51.820	95.056	1.00	57.34
3846	O	HOH	W	43	47.377	55.626	89.451	1.00	49.82
3847	O	HOH	W	44	45.228	58.061	81.927	1.00	67.31
3848	O	HOH	W	45	37.354	61.041	81.512	1.00	55.21
3849	O	HOH	W	46	26.553	61.536	86.551	1.00	48.38
3850	O	HOH	W	47	23.871	57.832	86.725	1.00	63.15
3851	O	HOH	W	48	21.351	75.888	87.379	1.00	55.36
3852	O	HOH	W	49	16.336	66.979	82.247	1.00	52.35
3853	O	HOH	W	50	20.491	78.894	89.268	1.00	49.24
3854	O	HOH	W	51	8.641	79.155	97.921	1.00	41.86
3855	O	HOH	W	52	28.754	57.106	99.998	1.00	22.16
3856	O	HOH	W	53	27.743	79.059	92.733	1.00	24.38
3857	O	HOH	W	54	25.166	51.962	95.208	1.00	28.66
3858	O	HOH	W	55	23.573	60.455	101.796	1.00	26.48
3859	O	HOH	W	56	26.250	69.724	78.744	1.00	31.75
3860	O	HOH	W	57	34.323	60.294	100.383	1.00	40.53
3861	O	HOH	W	58	27.486	72.953	88.697	1.00	28.68
3862	O	HOH	W	59	34.889	90.573	88.517	1.00	31.09
3863	O	HOH	W	60	33.283	58.848	95.676	1.00	31.39
3864	O	HOH	W	61	30.953	58.858	97.106	1.00	23.93
3865	O	HOH	W	62	22.512	52.171	95.445	1.00	27.62
3866	O	HOH	W	63	20.598	70.234	76.468	1.00	51.57
3867	O	HOH	W	64	12.319	64.060	118.862	1.00	55.13
3868	O	HOH	W	65	31.209	90.825	94.490	1.00	39.05
3869	O	HOH	W	66	23.791	79.639	85.574	1.00	41.46
3870	O	HOH	W	67	37.984	84.467	81.167	1.00	33.22
3871	O	HOH	W	68	18.599	76.019	92.910	1.00	39.06
3872	O	HOH	W	69	28.327	53.170	101.909	1.00	35.64
3873	O	HOH	W	70	17.201	75.206	88.495	1.00	43.62
3874	O	HOH	W	71	19.557	52.534	71.813	1.00	43.84
3875	O	HOH	W	72	31.383	86.335	79.832	1.00	31.19
3876	O	HOH	W	73	45.534	69.874	81.890	1.00	70.44
3877	O	HOH	W	74	23.398	78.113	87.971	1.00	41.72
3878	O	HOH	W	75	24.985	79.636	81.937	1.00	40.70
3879	O	HOH	W	76	35.214	56.538	86.573	1.00	61.87
3880	O	HOH	W	77	8.312	72.048	61.316	1.00	51.15
3881	O	HOH	W	78	54.583	67.580	79.761	1.00	92.40
3882	O	HOH	W	79	30.058	58.304	87.420	1.00	45.56
3883	O	HOH	W	80	15.658	57.937	72.486	1.00	49.88
3884	O	HOH	W	81	38.406	60.747	103.355	1.00	49.62
3885	O	HOH	W	82	45.112	73.835	79.366	1.00	57.23
3886	O	HOH	W	83	24.311	56.019	87.791	1.00	49.24
3887	O	HOH	W	84	11.054	91.063	75.823	1.00	62.21
3888	O	HOH	W	85	25.110	79.361	60.187	1.00	70.53
3889	O	HOH	W	86	21.814	61.622	88.069	1.00	45.93
3890	O	HOH	W	87	17.326	70.560	74.981	1.00	49.19
3891	O	HOH	W	88	27.869	64.366	81.736	1.00	72.04
3892	O	HOH	W	89	32.821	76.136	112.204	1.00	54.40
3893	O	HOH	W	90	33.796	83.623	82.106	1.00	54.68
3894	O	HOH	W	91	18.105	70.460	58.689	1.00	51.59
3895	O	HOH	W	92	21.706	82.125	101.976	1.00	57.32
3896	O	HOH	W	93	27.381	71.426	59.765	1.00	58.02
3897	O	HOH	W	94	27.472	55.467	86.841	1.00	49.46
3898	O	HOH	W	95	22.395	88.520	95.592	1.00	50.28
3899	O	HOH	W	96	−5.048	60.064	109.413	1.00	67.72
3900	O	HOH	W	97	14.636	51.620	97.555	1.00	72.51
3901	O	HOH	W	98	46.663	68.262	64.814	1.00	59.94
3902	O	HOH	W	99	51.526	66.481	63.513	1.00	60.60
3903	O	HOH	W	100	12.853	73.278	56.067	1.00	70.36
3904	O	HOH	W	101	17.395	50.850	69.827	1.00	51.25
3905	O	HOH	W	102	37.188	84.773	68.441	1.00	53.49
3906	O	HOH	W	103	26.301	84.156	54.117	1.00	74.97
3907	O	HOH	W	104	15.569	53.268	106.007	1.00	68.93
3908	O	HOH	W	105	11.106	82.832	80.170	1.00	52.24
3909	O	HOH	W	106	9.827	84.209	83.460	1.00	64.61
3910	O	HOH	W	107	39.542	90.057	76.485	1.00	58.59
3911	O	HOH	W	108	42.229	77.453	63.523	1.00	76.86
3912	O	HOH	W	109	27.370	67.242	78.876	1.00	41.58
3913	O	HOH	W	110	37.384	55.312	98.950	1.00	56.58
3914	O	HOH	W	111	31.815	58.721	100.040	1.00	43.21
3915	O	HOH	W	112	31.506	55.285	100.972	1.00	63.15
3916	O	HOH	W	113	38.178	54.915	91.789	1.00	58.54
3917	O	HOH	W	114	41.103	63.301	102.308	1.00	52.30
3918	O	HOH	W	115	19.518	79.361	85.632	1.00	56.13
3919	O	HOH	W	116	17.896	87.232	86.207	1.00	53.56
3920	O	HOH	W	117	13.629	61.460	82.107	1.00	53.88
3921	O	HOH	W	118	16.966	63.736	84.587	1.00	65.21
3922	O	HOH	W	119	28.949	48.535	78.225	1.00	54.95
3923	O	HOH	W	120	31.452	49.739	78.799	1.00	55.62
3924	O	HOH	W	121	19.965	71.727	82.620	1.00	60.17
3925	O	HOH	W	122	0.228	75.953	71.014	1.00	76.55
3926	O	HOH	W	123	0.158	73.725	64.810	1.00	65.34
3927	O	HOH	W	124	43.121	67.781	107.834	1.00	68.84
3928	O	HOH	W	125	42.068	71.355	112.215	1.00	71.87
3929	O	HOH	W	126	40.486	64.768	112.276	1.00	58.12
3930	O	HOH	W	127	35.045	83.128	108.243	1.00	81.25
3931	O	HOH	W	128	33.826	80.790	112.590	1.00	57.74
3932	O	HOH	W	129	30.755	80.445	110.066	1.00	68.05
3933	O	HOH	W	130	23.881	66.592	107.341	1.00	55.54
3934	O	HOH	W	131	21.181	65.654	120.113	1.00	66.27
3935	O	HOH	W	132	−1.340	56.710	98.372	1.00	70.45
3936	O	HOH	W	133	−3.291	66.354	109.085	1.00	76.45
3937	O	HOH	W	134	−0.721	72.343	105.882	1.00	90.08
3938	O	HOH	W	135	18.563	85.475	104.514	1.00	66.59
3939	O	HOH	W	136	21.187	86.326	106.734	1.00	62.94
3940	O	HOH	W	137	24.589	87.631	107.644	1.00	51.47
3941	O	HOH	W	138	25.316	87.133	104.100	1.00	69.03
3942	O	HOH	W	139	19.895	84.386	100.975	1.00	66.18
3943	O	HOH	W	140	24.239	84.741	106.617	1.00	59.66
3944	O	HOH	W	141	41.754	83.998	98.620	1.00	71.11
3945	O	HOH	W	142	32.225	59.750	103.596	1.00	56.52
3946	O	HOH	W	143	11.765	49.929	100.176	1.00	64.61
3947	O	HOH	W	144	7.717	53.143	96.964	1.00	63.33
3948	O	HOH	W	145	40.860	54.461	84.748	1.00	90.92
3949	O	HOH	W	146	15.363	84.742	107.809	1.00	64.26
3950	O	HOH	W	147	15.633	85.708	99.119	1.00	67.76
3951	O	HOH	W	148	7.601	76.855	91.970	1.00	60.58
3952	O	HOH	W	149	9.623	82.594	90.860	1.00	72.36
3953	O	HOH	W	150	24.202	89.335	92.759	1.00	43.28
3954	O	HOH	W	151	24.526	64.149	74.154	1.00	36.12
3955	O	HOH	W	152	45.473	55.901	61.786	1.00	65.50
3956	O	HOH	W	153	29.439	74.941	88.426	1.00	26.89
3957	O	HOH	W	154	37.914	91.765	66.016	1.00	90.43
3958	O	HOH	W	155	14.460	76.420	92.234	1.00	55.50
3959	O	HOH	W	156	8.236	67.697	61.549	1.00	63.32
3960	O	HOH	W	157	29.107	60.295	79.228	1.00	43.90
3961	O	HOH	W	158	26.638	76.154	60.795	1.00	58.93
3962	O	HOH	W	159	33.709	80.210	87.528	1.00	38.57
3963	O	HOH	W	160	40.715	82.585	84.782	1.00	68.42
3964	O	HOH	W	161	11.233	56.537	68.262	1.00	63.15
3965	O	HOH	W	162	21.975	64.415	85.175	1.00	40.81
3966	O	HOH	W	163	21.602	75.374	90.625	1.00	41.66
3967	O	HOH	W	164	43.202	83.556	90.439	1.00	44.45
3968	O	HOH	W	165	47.305	61.806	77.748	1.00	56.29
3969	O	HOH	W	166	16.383	73.291	75.523	1.00	44.82
3970	O	HOH	W	167	29.502	82.147	80.221	1.00	45.92
3971	O	HOH	W	168	55.133	60.635	74.223	1.00	74.10
3972	O	HOH	W	169	53.642	66.189	77.639	1.00	67.27
3973	O	HOH	W	170	32.023	76.158	86.775	1.00	50.78
3974	O	HOH	W	171	42.714	59.651	72.633	1.00	45.98
3975	O	HOH	W	172	26.008	50.088	106.857	1.00	40.13
3976	O	HOH	W	173	24.123	74.327	110.723	1.00	62.76
3977	O	HOH	W	174	43.725	70.645	61.138	1.00	66.39
3978	O	HOH	W	175	14.448	62.212	116.064	1.00	62.04
3979	O	HOH	W	176	22.321	95.254	69.714	1.00	63.47
3980	O	HOH	W	177	42.597	84.404	72.736	1.00	66.33
3981	O	HOH	W	178	39.815	56.522	94.119	1.00	51.02
3982	O	HOH	W	179	48.572	80.734	89.655	1.00	58.93
3983	O	HOH	W	180	17.082	49.172	97.561	1.00	55.92
3984	O	HOH	W	181	33.421	65.376	55.404	1.00	53.64
3985	O	HOH	W	182	30.691	93.733	74.873	1.00	60.59
3986	O	HOH	W	183	43.334	61.083	90.066	1.00	52.70
3987	O	HOH	W	184	47.929	50.409	83.769	1.00	73.41
3988	O	HOH	W	185	27.889	62.068	57.384	1.00	58.23
3989	O	HOH	W	186	2.632	58.059	112.990	1.00	55.10
3990	O	HOH	W	187	49.666	81.692	68.959	1.00	69.04
3991	O	HOH	W	188	21.840	96.023	88.622	1.00	56.16
3992	O	HOH	W	189	20.531	81.031	91.634	1.00	48.68
3993	O	HOH	W	190	13.144	52.725	91.050	1.00	74.72
3994	O	HOH	W	191	16.078	55.158	84.219	1.00	76.76
3995	O	HOH	W	192	21.973	94.500	78.308	1.00	54.35
3996	O	HOH	W	193	16.039	69.725	82.713	1.00	58.13
3997	O	HOH	W	194	29.925	92.916	101.327	1.00	55.39
3998	O	HOH	W	195	39.875	83.519	69.873	1.00	76.51
3999	O	HOH	W	196	33.547	79.050	116.541	1.00	58.96
4000	O	HOH	W	197	31.777	97.620	69.127	1.00	58.13
4001	O	HOH	W	198	19.289	81.660	108.573	1.00	54.02
4002	O	HOH	W	199	19.307	90.323	83.858	1.00	73.87
4003	O	HOH	W	200	42.438	81.165	77.189	1.00	57.30
4004	O	HOH	W	201	24.719	88.867	111.158	1.00	71.06
4005	O	HOH	W	202	14.752	82.372	79.831	1.00	50.46
4006	O	HOH	W	203	29.593	62.478	107.228	1.00	56.35
4007	O	HOH	W	204	44.276	54.216	84.906	1.00	63.06
4008	O	HOH	W	205	43.714	79.770	68.714	1.00	53.81
4009	O	HOH	W	206	10.195	74.128	58.090	1.00	67.94
4010	O	HOH	W	207	52.198	56.890	69.158	1.00	82.99
4011	O	HOH	W	208	41.501	55.621	88.559	1.00	58.64
4012	O	HOH	W	209	12.404	54.801	113.084	1.00	61.38
4013	O	HOH	W	210	20.935	85.398	102.822	1.00	59.61
4014	O	HOH	W	211	1.884	58.378	100.966	1.00	52.81
4015	O	HOH	W	212	44.292	66.241	113.852	1.00	62.95
4016	O	HOH	W	213	20.461	99.227	68.950	1.00	81.54
4017	O	HOH	W	214	54.282	63.551	95.771	1.00	73.65
4018	O	HOH	W	215	52.630	59.645	95.163	1.00	61.37
4019	O	HOH	W	216	43.847	74.747	108.470	1.00	47.79
4020	O	HOH	W	217	13.821	49.683	70.834	1.00	62.38
4021	O	HOH	W	218	30.134	58.491	54.366	1.00	60.17
4022	O	HOH	W	219	19.590	62.628	116.493	1.00	64.94
4023	O	HOH	W	220	10.033	74.052	109.418	1.00	60.61
4024	O	HOH	W	221	37.721	52.622	84.421	1.00	52.75
4025	O	HOH	W	222	4.965	79.234	106.393	1.00	54.50
4026	O	HOH	W	223	35.059	78.092	85.271	1.00	79.95
4027	O	HOH	W	224	41.104	59.402	59.846	1.00	67.70
4028	O	HOH	W	225	0.204	75.441	102.085	1.00	72.03
4029	O	HOH	W	226	27.249	75.955	121.137	1.00	96.12
4030	O	HOH	W	227	40.480	81.950	80.258	1.00	69.28
4031	O	HOH	W	228	13.904	89.137	105.643	1.00	73.36
4032	O	HOH	W	229	18.966	46.160	73.696	1.00	60.83
4033	O	HOH	W	230	25.204	95.032	76.561	1.00	55.01
4034	O	HOH	W	231	44.154	87.852	102.404	1.00	81.52
4035	O	HOH	W	232	15.734	50.286	102.580	1.00	73.57
4036	O	HOH	W	233	34.230	91.950	53.379	1.00	64.79
4037	O	HOH	W	234	34.028	88.196	54.572	1.00	76.62
4038	O	HOH	W	235	6.510	81.703	81.936	1.00	67.44
4039	O	HOH	W	236	31.250	46.769	80.109	1.00	59.73
4040	O	HOH	W	237	−4.328	66.322	104.598	1.00	72.03
4041	O	HOH	W	238	−5.175	65.411	111.235	1.00	80.31
4042	O	HOH	W	239	42.619	86.327	93.196	1.00	55.26
4043	O	HOH	W	240	53.056	58.639	77.745	1.00	67.77
4044	O	HOH	W	241	55.986	68.627	74.749	1.00	67.32
4045	O	HOH	W	242	26.578	51.838	109.039	1.00	68.47
4046	O	HOH	W	243	27.401	98.889	69.713	1.00	65.37
4047	O	HOH	W	244	38.092	57.444	100.192	1.00	67.48
4048	O	HOH	W	245	5.883	60.647	120.458	1.00	62.41
4049	O	HOH	W	246	24.874	95.610	80.166	1.00	65.09
4050	O	HOH	W	247	31.317	98.945	72.700	1.00	55.79
4051	O	HOH	W	248	42.019	81.867	65.318	1.00	64.05
4052	O	HOH	W	249	11.354	77.091	54.840	1.00	58.78
4053	O	HOH	W	250	2.257	54.062	96.344	1.00	69.03
4054	O	HOH	W	251	21.865	103.114	67.026	1.00	88.24
4055	O	HOH	W	252	25.783	79.878	112.404	1.00	71.73
4056	O	HOH	W	254	15.451	47.612	78.503	1.00	58.78
4057	O	HOH	W	255	20.013	42.200	74.057	1.00	54.88
4058	O	HOH	W	256	47.186	86.427	95.913	1.00	69.52
4059	O	HOH	W	257	42.710	86.262	96.986	1.00	69.38
4060	O	HOH	W	258	32.597	86.812	48.714	1.00	80.06
4061	O	HOH	W	259	0.686	79.870	83.804	1.00	69.66
4062	O	HOH	W	260	53.472	56.751	82.708	1.00	63.88
4063	O	HOH	W	261	8.076	56.013	119.805	1.00	75.94
4064	O	HOH	W	262	3.711	56.666	118.238	1.00	61.92
4065	O	HOH	W	263	8.577	61.095	122.359	1.00	79.31
4066	O	HOH	W	264	1.591	76.706	58.691	1.00	61.27
4067	O	HOH	W	265	9.902	70.303	56.931	1.00	64.53
4068	O	HOH	W	266	3.286	73.378	61.337	1.00	70.97
4069	O	HOH	W	267	1.544	57.048	89.873	1.00	66.17
4070	O	HOH	W	268	58.203	52.547	96.098	1.00	59.53
4071	O	HOH	W	269	55.863	59.303	86.462	1.00	86.54
4072	O	HOH	W	270	39.454	93.055	102.022	1.00	73.13
4073	O	HOH	W	271	57.151	62.618	85.040	1.00	60.06
4074	O	HOH	W	272	61.388	66.554	79.136	1.00	75.24
4075	O	HOH	W	273	16.444	65.572	76.282	1.00	48.26
4076	O	HOH	W	274	−7.019	56.050	104.617	1.00	68.20
4077	O	HOH	W	275	41.260	91.689	99.772	1.00	75.60
4078	O	HOH	W	276	7.750	72.640	69.911	1.00	65.48
4079	O	HOH	W	277	−0.534	56.593	93.766	1.00	55.74
4080	O	HOH	W	278	45.690	60.610	73.854	1.00	55.45
4081	O	HOH	W	279	43.232	79.073	98.278	1.00	68.39
4082	O	HOH	W	280	33.018	56.513	99.871	1.00	47.87
4083	O	HOH	W	281	12.875	91.417	62.202	1.00	50.60
4084	O	HOH	W	282	23.740	91.795	87.843	1.00	50.12
4085	O	HOH	W	283	33.901	87.154	60.631	1.00	57.12
4086	O	HOH	W	284	50.111	69.534	88.258	1.00	61.69
4087	O	HOH	W	285	22.172	79.896	108.037	1.00	49.77
4088	O	HOH	W	286	21.199	90.174	96.915	1.00	62.16
4089	O	HOH	W	287	41.370	77.951	75.054	1.00	93.44
4090	O	HOH	W	288	−3.670	64.205	109.234	1.00	80.74
4091	O	HOH	W	289	44.099	65.205	84.325	1.00	65.13
4092	O	HOH	W	290	18.230	84.669	98.089	1.00	73.24
4093	O	HOH	W	291	6.251	58.894	82.343	1.00	56.09
4094	O	HOH	W	292	4.533	87.103	81.626	1.00	62.59
4095	O	HOH	W	293	39.869	75.490	108.817	1.00	45.54
4096	O	HOH	W	294	23.699	54.140	107.333	1.00	46.52
4097	O	HOH	W	295	44.615	81.058	87.775	1.00	51.98
4098	O	HOH	W	296	5.134	86.562	85.564	1.00	59.40
4099	O	HOH	W	297	6.400	75.372	58.580	1.00	95.89
4100	O	HOH	W	298	15.511	101.122	67.844	1.00	83.89
4101	O	HOH	W	299	15.805	52.427	83.025	1.00	54.36
4102	O	HOH	W	300	31.021	74.527	57.113	1.00	58.88
4103	O	HOH	W	301	27.315	76.686	57.795	1.00	64.74
4104	O	HOH	X	302	16.794	73.496	92.416	1.00	43.24
4105	O	HOH	X	303	25.310	69.852	104.407	1.00	40.75
4106	O	HOH	X	304	14.601	56.696	93.871	1.00	64.02
4107	O	HOH	X	305	21.573	63.907	101.673	1.00	61.34
4108	O	HOH	X	306	47.225	61.635	66.073	1.00	72.40
4109	O	HOH	X	307	27.850	51.658	107.180	1.00	61.47
4110	O	HOH	X	308	4.828	61.226	96.660	1.00	63.69
4111	O	HOH	X	309	18.843	89.280	66.555	1.00	67.83
4112	O	HOH	X	310	31.275	70.993	63.564	1.00	76.09
4113	O	HOH	X	311	11.055	79.338	71.713	1.00	87.73
4114	O	HOH	X	312	35.732	92.142	66.782	1.00	70.59
4115	O	HOH	X	313	45.991	70.742	79.189	1.00	50.63
4116	O	HOH	X	314	42.103	62.040	87.599	1.00	58.63
4117	O	HOH	X	315	21.915	81.889	51.317	1.00	70.16
4118	O	HOH	X	316	19.123	72.199	60.303	1.00	49.30
4119	O	HOH	X	317	17.023	63.306	68.075	1.00	69.61
4120	O	HOH	X	318	20.375	72.024	116.048	1.00	68.20
4121	O	HOH	X	319	26.175	77.621	62.544	1.00	79.76
4122	O	HOH	X	320	44.798	57.627	62.912	1.00	96.29
4123	O	HOH	X	321	34.264	87.734	78.140	1.00	59.27
4124	O	HOH	X	322	36.913	85.471	83.195	1.00	68.12
4125	O	HOH	X	323	21.300	65.553	105.006	1.00	67.05
4126	O	HOH	X	324	22.477	83.111	92.028	1.00	45.27
4127	O	HOH	X	325	29.919	63.783	57.812	1.00	78.09
4128	O	HOH	X	326	21.773	58.872	81.134	1.00	50.84
4129	O	HOH	X	327	9.524	55.783	94.636	1.00	70.31
4130	O	HOH	X	328	49.945	71.633	88.156	1.00	60.20
4131	O	HOH	X	329	46.051	80.340	75.306	1.00	66.68
4132	O	HOH	X	330	19.780	53.571	86.923	1.00	52.32
4133	O	HOH	X	331	33.754	59.963	85.790	1.00	79.38
4134	O	HOH	X	332	44.741	56.622	88.452	1.00	83.35
4135	O	HOH	X	333	13.601	64.513	112.251	1.00	85.96
4136	O	HOH	X	334	24.193	61.120	87.313	1.00	54.44
4137	O	HOH	X	335	48.193	76.404	103.259	1.00	68.76
4138	O	HOH	X	336	9.407	73.167	71.266	1.00	74.67
4139	O	HOH	X	337	22.838	91.635	90.182	1.00	57.23

[0378]

TABLE 4
ATOMIC COORDINATE DATA FOR HUMAN RARγ EMPLOYED IN THE
MOLECULAR REPLACEMENT SOLUTION OF HUMAN LXR LIGAND
BINDING DOMAIN CRYSTALS
	ATOM
ATOM	TYPE	RESIDUE	PROTEIN #	#	X	Y	Z	BCC	O
1	CB	LEU	A	182	−27.418	−10.420	−1.042	1.00	32.61
2	CG	LEU	A	182	−27.812	−11.853	−0.661	1.00	33.33
3	CD1	LEU	A	182	−26.844	−12.934	−1.224	1.00	33.15
4	CD2	LEU	A	182	−27.818	−11.894	0.872	1.00	32.41
5	C	LEU	A	182	−26.797	−8.358	−2.226	1.00	31.66
6	O	LEU	A	182	−25.593	−8.099	−2.172	1.00	31.81
7	N	LEU	A	182	−26.227	−10.497	−3.276	1.00	33.77
8	CA	LEU	A	182	−27.267	−9.788	−2.446	1.00	33.01
9	N	SER	A	183	−27.741	−7.437	−2.073	1.00	30.24
10	CA	SER	A	183	−27.379	−6.058	−1.802	1.00	26.79
11	CB	SER	A	183	−28.588	−5.139	−1.923	1.00	26.27
12	OG	SER	A	183	−29.258	−5.339	−3.148	1.00	27.42
13	C	SER	A	183	−26.871	−6.058	−0.370	1.00	25.85
14	O	SER	A	183	−25.798	−5.515	−0.086	1.00	25.47
15	N	PRO	A	184	−27.599	−6.747	0.544	1.00	24.99
16	CD	PRO	A	184	−28.906	−7.426	0.422	1.00	22.22
17	CA	PRO	A	184	−27.136	−6.766	1.933	1.00	22.12
18	CB	PRO	A	184	−28.236	−7.546	2.655	1.00	23.65
19	CG	PRO	A	184	−28.899	−8.334	1.575	1.00	23.82
20	C	PRO	A	184	−25.778	−7.392	2.070	1.00	20.98
21	O	PRO	A	184	−24.944	−6.888	2.815	1.00	22.89
22	N	ALA	A	185	−25.528	−8.436	1.290	1.00	18.94
23	CA	ALA	A	185	−24.245	−9.136	1.293	1.00	17.11
24	CB	ALA	A	185	−24.290	−10.281	0.316	1.00	19.74
25	C	ALA	A	185	−23.123	−8.181	0.909	1.00	16.78
26	O	ALA	A	185	−22.072	−8.152	1.553	1.00	15.58
27	N	LEU	A	186	−23.346	−7.439	−0.171	1.00	16.27
28	CA	LEU	A	186	−22.402	−6.451	−0.636	1.00	17.77
29	CB	LEU	A	186	−22.876	−5.795	−1.931	1.00	21.12
30	CG	LEU	A	186	−22.329	−6.276	−3.281	1.00	25.48
31	CD1	LEU	A	186	−22.491	−5.150	−4.303	1.00	26.32
32	CD2	LEU	A	186	−20.847	−6.665	−3.196	1.00	26.08
33	C	LEU	A	186	−22.222	−5.354	0.407	1.00	16.80
34	O	LEU	A	186	−21.121	−4.846	0.587	1.00	17.47
35	N	GLU	A	187	−23.287	−4.971	1.090	1.00	14.83
36	CA	GLU	A	187	−23.149	−3.925	2.078	1.00	14.29
37	CB	GLU	A	187	−24.498	−3.501	2.644	1.00	13.39
38	CG	GLU	A	187	−25.438	−2.902	1.603	1.00	17.47
39	CD	GLU	A	187	−24.911	−1.645	0.907	1.00	18.66
40	OE1	GLU	A	187	−23.993	−0.982	1.433	1.00	19.34
41	OE2	GLU	A	187	−25.446	−1.303	−0.166	1.00	18.74
42	C	GLU	A	187	−22.255	−4.371	3.196	1.00	15.23
43	O	GLU	A	187	−21.495	−3.579	3.717	1.00	14.48
44	N	GLU	A	188	−22.367	−5.628	3.607	1.00	16.77
45	CA	GLU	A	188	−21.526	−6.118	4.689	1.00	19.26
46	CB	GLU	A	188	−22.175	−7.317	5.353	1.00	21.32
47	CG	GLU	A	188	−23.398	−6.845	6.134	1.00	28.68
48	CD	GLU	A	188	−24.275	−7.966	6.623	1.00	30.83
49	OE1	GLU	A	188	−25.360	−8.187	6.035	1.00	32.28
50	OE2	GLU	A	188	−23.887	−8.615	7.611	1.00	34.12
51	C	GLU	A	188	−20.061	−6.366	4.321	1.00	18.83
52	O	GLU	A	188	−19.174	−6.172	5.147	1.00	18.44
53	N	LEU	A	189	−19.805	−6.729	3.069	1.00	17.42
54	CA	LEU	A	189	−18.453	−6.953	2.591	1.00	16.55
55	CB	LEU	A	189	−18.512	−7.441	1.148	1.00	16.21
56	CG	LEU	A	189	−17.453	−8.406	0.612	1.00	17.60
57	CD1	LEU	A	189	−17.165	−8.041	−0.823	1.00	15.95
58	CD2	LEU	A	189	−16.205	−8.340	1.414	1.00	14.51
59	C	LEU	A	189	−17.728	−5.593	2.656	1.00	16.84
60	O	LEU	A	189	−16.558	−5.513	3.017	1.00	17.45
61	N	ILE	A	190	−18.449	−4.535	2.305	1.00	16.26
62	CA	ILE	A	190	−17.926	−3.189	2.322	1.00	15.67
63	CB	ILE	A	190	−18.964	−2.176	1.775	1.00	14.53
64	CG2	ILE	A	190	−18.452	−0.762	1.952	1.00	14.55
65	CG1	ILE	A	190	−19.203	−2.438	0.289	1.00	14.16
66	CD1	ILE	A	190	−20.363	−1.652	−0.369	1.00	15.08
67	C	ILE	A	190	−17.512	−2.808	3.737	1.00	16.88
68	O	ILE	A	190	−16.428	−2.271	3.952	1.00	16.52
69	N	THR	A	191	−18.379	−3.090	4.703	1.00	18.22
70	CA	THR	A	191	−18.115	−2.803	6.108	1.00	18.80
71	CB	THR	A	191	−19.328	−3.082	6.930	1.00	17.79
72	OG1	THR	A	191	−20.333	−2.147	6.560	1.00	20.38
73	CG2	THR	A	191	−19.024	−2.939	8.390	1.00	18.36
74	C	THR	A	191	−16.963	−3.623	6.653	1.00	20.64
75	O	THR	A	191	−16.101	−3.083	7.337	1.00	22.47
76	N	LYS	A	192	−16.948	−4.918	6.360	1.00	19.94
77	CA	LYS	A	192	−15.875	−5.774	6.816	1.00	20.28
78	CB	LYS	A	192	−16.162	−7.223	6.451	1.00	22.80
79	CG	LYS	A	192	−17.174	−7.832	7.439	1.00	26.17
80	CD	LYS	A	192	−17.835	−9.116	6.972	1.00	27.88
81	CE	LYS	A	192	−18.790	−9.613	8.072	1.00	29.77
82	NZ	LYS	A	192	−20.058	−10.190	7.537	1.00	32.37
83	C	LYS	A	192	−14.532	−5.312	6.288	1.00	20.29
84	O	LYS	A	192	−13.644	−4.992	7.064	1.00	21.51
85	N	VAL	A	193	−14.395	−5.201	4.976	1.00	20.89
86	CA	VAL	A	193	−13.142	−4.743	4.392	1.00	19.43
87	CB	VAL	A	193	−13.254	−4.626	2.876	1.00	20.16
88	CG1	VAL	A	193	−12.043	−3.930	2.312	1.00	20.33
89	CG2	VAL	A	193	−13.402	−6.003	2.265	1.00	16.58
90	C	VAL	A	193	−12.748	−3.400	4.988	1.00	19.77
91	O	VAL	A	193	−11.640	−3.230	5.459	1.00	20.14
92	N	SER	A	194	−13.684	−2.464	5.018	1.00	21.53
93	CA	SER	A	194	−13.438	−1.124	5.560	1.00	21.04
94	CB	SER	A	194	−14.738	−0.328	5.609	1.00	19.63
95	OG	SER	A	194	−14.496	0.998	6.016	1.00	19.69
96	C	SER	A	194	−12.812	−1.169	6.946	1.00	21.80
97	O	SER	A	194	−11.778	−0.549	7.187	1.00	21.17
98	N	LYS	A	195	−13.448	−1.919	7.840	1.00	22.99
99	CA	LYS	A	195	−13.006	−2.093	9.218	1.00	22.87
100	CB	LYS	A	195	−14.048	−2.881	10.015	1.00	23.64
101	CG	LYS	A	195	−15.116	−1.991	10.650	1.00	28.29
102	CD	LYS	A	195	−15.080	−0.578	10.043	1.00	30.25
103	CE	LYS	A	195	−16.005	0.403	10.767	1.00	32.32
104	NZ	LYS	A	195	−15.549	0.724	12.161	1.00	33.22
105	C	LYS	A	195	−11.649	−2.752	9.319	1.00	22.28
106	O	LYS	A	195	−10.822	−2.311	10.092	1.00	23.38
107	N	ALA	A	196	−11.407	−3.801	8.543	1.00	21.84
108	CA	ALA	A	196	−10.115	−4.464	8.587	1.00	21.79
109	CB	ALA	A	196	−10.096	−5.682	7.660	1.00	20.88
110	C	ALA	A	196	−9.054	−3.446	8.176	1.00	21.34
111	O	ALA	A	196	−7.982	−3.371	8.777	1.00	23.62
112	N	HIS	A	197	−9.349	−2.627	7.174	1.00	20.81
113	CA	HIS	A	197	−8.377	−1.624	6.762	1.00	20.38
114	CB	HIS	A	197	−8.776	−0.931	5.468	1.00	18.26
115	CG	HIS	A	197	−7.852	0.177	5.088	1.00	19.16
116	CD2	HIS	A	197	−7.957	1.517	5.242	1.00	17.84
117	ND1	HIS	A	197	−6.634	−0.043	4.478	1.00	19.65
118	CE1	HIS	A	197	−6.034	1.112	4.266	1.00	18.43
119	NE2	HIS	A	197	−6.817	2.073	4.718	1.00	20.25
120	C	HIS	A	197	−8.152	−0.585	7.871	1.00	21.21
121	O	HIS	A	197	−7.013	−0.296	8.243	1.00	22.59
122	N	GLN	A	198	−9.224	−0.037	8.419	1.00	21.25
123	CA	GLN	A	198	−9.070	0.951	9.463	1.00	23.59
124	CB	GLN	A	198	−10.427	1.387	9.948	1.00	26.42
125	CG	GLN	A	198	−11.141	2.386	9.083	1.00	29.27
126	CD	GLN	A	198	−12.553	2.537	9.568	1.00	30.05
127	OE1	GLN	A	198	−12.820	2.362	10.762	1.00	31.98
128	NE2	GLN	A	198	−13.485	2.764	8.647	1.00	31.27
129	C	GLN	A	198	−8.275	0.423	10.653	1.00	24.07
130	O	GLN	A	198	−7.373	1.090	11.170	1.00	25.03
131	N	GLU	A	199	−8.633	−0.777	11.089	1.00	25.01
132	CA	GLU	A	199	−7.991	−1.437	12.214	1.00	24.53
133	CB	GLU	A	199	−8.771	−2.675	12.599	1.00	24.38
134	CG	GLU	A	199	−10.086	−2.311	13.229	1.00	27.91
135	CD	GLU	A	199	−10.859	−3.511	13.707	1.00	29.06
136	OE1	GLU	A	199	−12.107	−3.480	13.615	1.00	32.53
137	OE2	GLU	A	199	−10.225	−4.477	14.194	1.00	30.26
138	C	GLU	A	199	−6.539	−1.784	12.002	1.00	23.37
139	O	GLU	A	199	−5.807	−1.883	12.963	1.00	24.39
140	N	THR	A	200	−6.114	−1.949	10.756	1.00	21.99
141	CA	THR	A	200	−4.719	−2.276	10.462	1.00	20.58
142	CB	THR	A	200	−4.624	−3.474	9.488	1.00	20.42
143	OG1	THR	A	200	−5.031	−3.059	8.169	1.00	17.20
144	CG2	THR	A	200	−5.515	−4.633	9.999	1.00	18.24
145	C	THR	A	200	−3.942	−1.086	9.872	1.00	19.62
146	O	THR	A	200	−2.761	−1.202	9.541	1.00	17.71
147	N	PHE	A	201	−4.614	0.045	9.704	1.00	20.00
148	CA	PHE	A	201	−3.958	1.220	9.161	1.00	21.05
149	CB	PHE	A	201	−3.941	1.160	7.648	1.00	22.20
150	CG	PHE	A	201	−2.984	2.112	7.024	1.00	21.15
151	CD1	PHE	A	201	−3.430	3.109	6.187	1.00	23.24
152	CD2	PHE	A	201	−1.613	1.964	7.228	1.00	24.07
153	CE1	PHE	A	201	−2.532	3.946	5.546	1.00	21.82
154	CE2	PHE	A	201	−0.703	2.792	6.593	1.00	23.53
155	CZ	PHE	A	201	−1.161	3.781	5.751	1.00	22.68
156	C	PHE	A	201	−4.619	2.521	9.560	1.00	21.47
157	O	PHE	A	201	−5.549	2.962	8.906	1.00	22.07
158	N	PRO	A	202	−4.089	3.193	10.586	1.00	23.56
159	CD	PRO	A	202	−3.018	2.664	11.445	1.00	24.92
160	CA	PRO	A	202	−4.580	4.468	11.116	1.00	23.81
161	CB	PRO	A	202	−3.570	4.784	12.206	1.00	23.88
162	CG	PRO	A	202	−3.216	3.465	12.713	1.00	25.50
163	C	PRO	A	202	−4.548	5.554	10.064	1.00	24.15
164	O	PRO	A	202	−3.584	5.647	9.294	1.00	23.02
165	N	SER	A	203	−5.588	6.381	10.028	1.00	25.14
166	CA	SER	A	203	−5.629	7.466	9.064	1.00	26.45
167	CB	SER	A	203	−7.057	7.981	8.836	1.00	26.50
168	OG	SER	A	203	−7.803	8.001	10.039	1.00	29.67
169	C	SER	A	203	−4.712	8.551	9.594	1.00	25.55
170	O	SER	A	203	−4.392	8.573	10.779	1.00	25.33
171	N	LEU	A	204	−4.238	9.405	8.698	1.00	26.68
172	CA	LEU	A	204	−3.326	10.483	9.056	1.00	28.37
173	CB	LEU	A	204	−3.110	11.361	7.828	1.00	27.72
174	CG	LEU	A	204	−1.948	12.342	7.757	1.00	27.81
175	CD1	LEU	A	204	−0.725	11.797	8.433	1.00	26.92
176	CD2	LEU	A	204	−1.676	12.614	6.300	1.00	27.54
177	C	LEU	A	204	−3.841	11.302	10.241	1.00	29.51
178	O	LEU	A	204	−3.105	11.590	11.187	1.00	30.16
179	N	CYS	A	205	−5.142	11.561	10.216	1.00	31.31
180	CA	CYS	A	205	−5.849	12.341	11.218	1.00	33.60
181	CB	CYS	A	205	−7.301	12.480	10.791	1.00	35.57
182	SG	CYS	A	205	−7.559	11.823	9.119	1.00	41.57
183	C	CYS	A	205	−5.798	11.776	12.625	1.00	33.68
184	O	CYS	A	205	−5.892	12.523	13.607	1.00	34.82
185	N	GLN	A	206	−5.690	10.459	12.730	1.00	33.19
186	CA	GLN	A	206	−5.642	9.804	14.030	1.00	32.16
187	CB	GLN	A	206	−6.136	8.359	13.887	1.00	33.06
188	CG	GLN	A	206	−5.908	7.486	15.107	1.00	32.99
189	CD	GLN	A	206	−6.222	6.034	14.849	1.00	34.01
190	OE1	GLN	A	206	−6.813	5.686	13.821	1.00	33.58
191	NE2	GLN	A	206	−5.827	5.168	15.782	1.00	34.48
192	C	GLN	A	206	−4.217	9.784	14.562	1.00	31.63
193	O	GLN	A	206	−3.975	9.430	15.719	1.00	32.61
194	N	LEU	A	207	−3.262	10.186	13.742	1.00	29.82
195	CA	LEU	A	207	−1.898	10.088	14.192	1.00	28.12
196	CB	LEU	A	207	−0.999	9.600	13.054	1.00	27.92
197	CG	LEU	A	207	−0.628	8.105	13.010	1.00	27.55
198	CD1	LEU	A	207	−1.631	7.215	13.731	1.00	27.18
199	CD2	LEU	A	207	−0.484	7.679	11.557	1.00	25.94
200	C	LEU	A	207	−1.281	11.251	14.921	1.00	26.93
201	O	LEU	A	207	−1.502	12.423	14.590	1.00	26.30
202	N	GLY	A	208	−0.609	10.893	16.010	1.00	25.66
203	CA	GLY	A	208	0.110	11.870	16.790	1.00	24.28
204	C	GLY	A	208	1.398	12.007	15.992	1.00	22.29
205	O	GLY	A	208	2.269	11.135	16.061	1.00	20.48
206	N	LYS	A	209	1.448	13.015	15.131	1.00	21.40
207	CA	LYS	A	209	2.605	13.238	14.296	1.00	21.36
208	CB	LYS	A	209	2.265	14.194	13.160	1.00	22.61
209	CG	LYS	A	209	1.457	13.511	12.069	1.00	25.95
210	CD	LYS	A	209	0.684	14.484	11.192	1.00	26.65
211	CE	LYS	A	209	1.552	15.151	10.148	1.00	27.62
212	NZ	LYS	A	209	0.683	15.849	9.151	1.00	27.27
213	C	LYS	A	209	3.783	13.742	15.076	1.00	20.75
214	O	LYS	A	209	3.620	14.478	16.042	1.00	22.12
215	N	TYR	A	210	4.955	13.210	14.747	1.00	20.02
216	CA	TYR	A	210	6.192	13.647	15.370	1.00	20.49
217	CB	TYR	A	210	6.534	12.837	16.629	1.00	18.47
218	CG	TYR	A	210	7.130	11.494	16.353	1.00	18.13
219	CD1	TYR	A	210	8.496	11.358	16.171	1.00	15.36
220	CE1	TYR	A	210	9.045	10.142	15.867	1.00	16.09
221	CD2	TYR	A	210	6.325	10.369	16.229	1.00	16.18
222	CE2	TYR	A	210	6.866	9.144	15.925	1.00	15.25
223	CZ	TYR	A	210	8.229	9.037	15.744	1.00	15.38
224	OH	TYR	A	210	8.797	7.822	15.453	1.00	16.80
225	C	TYR	A	210	7.263	13.591	14.283	1.00	19.53
226	O	TYR	A	210	7.099	12.927	13.266	1.00	19.97
227	N	THR	A	211	8.332	14.335	14.483	1.00	20.32
228	CA	THR	A	211	9.392	14.441	13.504	1.00	19.85
229	CB	THR	A	211	9.434	15.910	13.061	1.00	20.41
230	OG1	THR	A	211	9.454	16.758	14.222	1.00	22.41
231	CG2	THR	A	211	8.177	16.261	12.291	1.00	22.14
232	C	THR	A	211	10.781	13.998	13.982	1.00	20.02
233	O	THR	A	211	10.945	13.465	15.077	1.00	22.75
234	N	THR	A	212	11.774	14.147	13.117	1.00	20.00
235	CA	THR	A	212	13.150	13.829	13.447	1.00	19.89
236	CB	THR	A	212	13.567	12.417	12.996	1.00	20.40
237	OG1	THR	A	212	14.895	12.157	13.451	1.00	19.09
238	CG2	THR	A	212	13.562	12.268	11.467	1.00	18.30
239	C	THR	A	212	14.001	14.876	12.737	1.00	22.16
240	O	THR	A	212	13.544	15.506	11.771	1.00	20.36
241	N	ASN	A	213	15.201	15.139	13.261	1.00	24.37
242	CA	ASN	A	213	16.080	16.104	12.608	1.00	24.35
243	CB	ASN	A	213	16.749	17.125	13.577	1.00	24.35
244	CG	ASN	A	213	17.424	16.484	14.788	1.00	23.76
245	OD1	ASN	A	213	17.681	15.305	14.810	1.00	24.80
246	ND2	ASN	A	213	17.707	17.294	15.794	1.00	22.88
247	C	ASN	A	213	17.083	15.434	11.688	1.00	25.10
248	O	ASN	A	213	17.747	16.090	10.890	1.00	26.32
249	N	SER	A	214	17.114	14.106	11.704	1.00	24.69
250	CA	SER	A	214	18.037	13.377	10.832	1.00	25.17
251	CB	SER	A	214	17.831	11.882	10.948	1.00	25.27
252	OG	SER	A	214	18.257	11.442	12.211	1.00	25.70
253	C	SER	A	214	17.940	13.795	9.369	1.00	25.21
254	O	SER	A	214	16.844	13.925	8.821	1.00	24.04
255	N	SER	A	215	19.107	14.043	8.768	1.00	26.72
256	CA	SER	A	215	19.264	14.441	7.377	1.00	25.06
257	CB	SER	A	215	19.734	13.237	6.595	1.00	23.52
258	OG	SER	A	215	20.845	12.696	7.296	1.00	27.19
259	C	SER	A	215	18.040	15.082	6.756	1.00	24.94
260	O	SER	A	215	17.514	14.611	5.759	1.00	26.62
261	N	ALA	A	216	17.527	16.084	7.451	1.00	26.24
262	CA	ALA	A	216	16.395	16.875	7.004	1.00	27.32
263	CB	ALA	A	216	15.686	17.514	8.207	1.00	24.42
264	C	ALA	A	216	17.012	17.930	6.092	1.00	28.48
265	O	ALA	A	216	16.372	18.427	5.159	1.00	29.23
266	N	ASP	A	217	18.308	18.158	6.324	1.00	28.95
267	CA	ASP	A	217	19.169	19.109	5.620	1.00	30.21
268	CB	ASP	A	217	20.647	18.851	6.056	1.00	32.59
269	CG	ASP	A	217	21.619	20.009	5.694	1.00	33.99
270	OD1	ASP	A	217	22.382	20.458	6.603	1.00	37.14
271	OD2	ASP	A	217	21.678	20.452	4.519	1.00	33.28
272	C	ASP	A	217	19.046	18.975	4.096	1.00	28.62
273	O	ASP	A	217	18.423	19.813	3.430	1.00	27.65
274	N	HIS	A	218	19.684	17.936	3.555	1.00	27.53
275	CA	HIS	A	218	19.707	17.691	2.116	1.00	25.97
276	CB	HIS	A	218	20.895	18.410	1.486	1.00	28.45
277	CG	HIS	A	218	22.207	17.735	1.741	1.00	29.85
278	CD2	HIS	A	218	23.107	17.186	0.889	1.00	31.13
279	ND1	HIS	A	218	22.711	17.529	3.012	1.00	30.86
280	CE1	HIS	A	218	23.860	16.886	2.931	1.00	31.67
281	NE2	HIS	A	218	24.125	16.665	1.654	1.00	32.39
282	C	HIS	A	218	19.854	16.204	1.859	1.00	23.88
283	O	HIS	A	218	20.188	15.445	2.766	1.00	25.08
284	N	ARG	A	219	19.741	15.824	0.599	1.00	22.00
285	CA	ARG	A	219	19.825	14.435	0.198	1.00	22.41
286	CB	ARG	A	219	19.159	14.261	−1.166	1.00	22.50
287	CG	ARG	A	219	17.737	14.801	−1.236	1.00	22.91
288	CD	ARG	A	219	17.098	14.440	−2.571	1.00	22.98
289	NE	ARG	A	219	15.802	15.093	−2.756	1.00	22.05
290	CZ	ARG	A	219	14.916	14.760	−3.693	1.00	19.87
291	NH1	ARG	A	219	15.158	13.768	−4.544	1.00	17.44
292	NH2	ARG	A	219	13.787	15.440	−3.792	1.00	20.09
293	C	ARG	A	219	21.225	13.818	0.163	1.00	22.78
294	O	ARG	A	219	22.165	14.403	−0.377	1.00	22.77
295	N	VAL	A	220	21.352	12.643	0.766	1.00	22.75
296	CA	VAL	A	220	22.603	11.898	0.779	1.00	22.59
297	CB	VAL	A	220	23.189	11.750	2.201	1.00	22.90
298	CG1	VAL	A	220	23.673	13.119	2.722	1.00	24.17
299	CG2	VAL	A	220	22.166	11.134	3.164	1.00	20.45
300	C	VAL	A	220	22.235	10.539	0.212	1.00	24.31
301	O	VAL	A	220	21.043	10.247	0.048	1.00	26.77
302	N	GLN	A	221	23.222	9.718	−0.126	1.00	23.99
303	CA	GLN	A	221	22.932	8.402	−0.680	1.00	24.25
304	CB	GLN	A	221	24.230	7.620	−0.944	1.00	25.91
305	CG	GLN	A	221	24.002	6.223	−1.582	1.00	29.12
306	CD	GLN	A	221	25.250	5.300	−1.593	1.00	31.49
307	OE1	GLN	A	221	26.142	5.465	−2.421	1.00	34.56
308	NE2	GLN	A	221	25.276	4.299	−0.706	1.00	31.02
309	C	GLN	A	221	22.011	7.567	0.232	1.00	24.22
310	O	GLN	A	221	21.099	6.903	−0.254	1.00	25.20
311	N	LEU	A	222	22.242	7.614	1.544	1.00	23.14
312	CA	LEU	A	222	21.464	6.814	2.477	1.00	22.34
313	CB	LEU	A	222	21.858	5.351	2.255	1.00	20.04
314	CG	LEU	A	222	21.047	4.138	2.682	1.00	20.69
315	CD1	LEU	A	222	21.290	3.727	4.100	1.00	20.10
316	CD2	LEU	A	222	19.596	4.438	2.430	1.00	21.58
317	C	LEU	A	222	21.788	7.197	3.921	1.00	22.91
318	O	LEU	A	222	22.967	7.309	4.290	1.00	24.38
319	N	ASP	A	223	20.755	7.418	4.735	1.00	22.66
320	CA	ASP	A	223	20.938	7.726	6.162	1.00	21.34
321	CB	ASP	A	223	20.079	8.925	6.610	1.00	22.74
322	CG	ASP	A	223	20.221	9.238	8.126	1.00	25.18
323	OD1	ASP	A	223	20.458	10.412	8.508	1.00	26.69
324	OD2	ASP	A	223	20.059	8.320	8.955	1.00	26.37
325	C	ASP	A	223	20.531	6.443	6.889	1.00	20.74
326	O	ASP	A	223	19.359	6.054	6.915	1.00	18.76
327	N	LEU	A	224	21.518	5.782	7.463	1.00	20.18
328	CA	LEU	A	224	21.303	4.524	8.145	1.00	19.89
329	CB	LEU	A	224	22.632	3.915	8.529	1.00	21.07
330	CG	LEU	A	224	23.322	3.093	7.463	1.00	22.72
331	CD1	LEU	A	224	24.607	2.566	8.072	1.00	20.82
332	CD2	LEU	A	224	22.418	1.935	7.050	1.00	22.65
333	C	LEU	A	224	20.411	4.607	9.358	1.00	19.76
334	O	LEU	A	224	19.666	3.681	9.635	1.00	20.96
335	N	GLY	A	225	20.524	5.679	10.118	1.00	17.05
336	CA	GLY	A	225	19.673	5.807	11.268	1.00	17.01
337	C	GLY	A	225	18.243	5.835	10.775	1.00	17.46
338	O	GLY	A	225	17.377	5.228	11.381	1.00	16.42
339	N	LEU	A	226	18.025	6.481	9.628	1.00	18.64
340	CA	LEU	A	226	16.699	6.608	9.012	1.00	18.78
341	CB	LEU	A	226	16.707	7.762	8.003	1.00	18.63
342	CG	LEU	A	226	15.798	9.002	8.195	1.00	19.85
343	CD1	LEU	A	226	15.605	9.392	9.643	1.00	16.64
344	CD2	LEU	A	226	16.337	10.201	7.380	1.00	17.14
345	C	LEU	A	226	16.231	5.295	8.359	1.00	18.28
346	O	LEU	A	226	15.073	4.886	8.530	1.00	16.45
347	N	TRP	A	227	17.124	4.624	7.634	1.00	17.71
348	CA	TRP	A	227	16.776	3.352	7.015	1.00	18.68
349	CB	TRP	A	227	17.926	2.775	6.206	1.00	17.57
350	CG	TRP	A	227	17.835	1.262	6.070	1.00	16.59
351	CD2	TRP	A	227	16.919	0.501	5.253	1.00	15.32
352	CE2	TRP	A	227	17.228	−0.860	5.433	1.00	13.42
353	CE3	TRP	A	227	15.866	0.838	4.392	1.00	17.17
354	CD1	TRP	A	227	18.624	0.350	6.695	1.00	16.34
355	NE1	TRP	A	227	18.270	−0.926	6.316	1.00	15.17
356	CZ2	TRP	A	227	16.529	−1.882	4.786	1.00	13.09
357	CZ3	TRP	A	227	15.168	−0.186	3.747	1.00	15.40
358	CH2	TRP	A	227	15.505	−1.521	3.950	1.00	14.59
359	C	TRP	A	227	16.407	2.364	8.122	1.00	20.52
360	O	TRP	A	227	15.585	1.465	7.917	1.00	20.81
361	N	ASP	A	228	17.049	2.511	9.281	1.00	21.28
362	CA	ASP	A	228	16.772	1.649	10.418	1.00	21.73
363	CB	ASP	A	228	17.773	1.893	11.512	1.00	25.14
364	CG	ASP	A	228	18.798	0.815	11.570	1.00	28.26
365	OD1	ASP	A	228	19.686	0.779	10.668	1.00	29.32
366	OD2	ASP	A	228	18.682	−0.012	12.504	1.00	31.33
367	C	ASP	A	228	15.379	1.823	10.970	1.00	20.87
368	O	ASP	A	228	14.695	0.851	11.249	1.00	22.70
369	N	LYS	A	229	14.982	3.062	11.192	1.00	20.53
370	CA	LYS	A	229	13.640	3.354	11.691	1.00	19.84
371	CB	LYS	A	229	13.511	4.877	11.931	1.00	19.61
372	CG	LYS	A	229	12.162	5.331	12.479	1.00	23.06
373	CD	LYS	A	229	11.776	4.555	13.750	1.00	25.62
374	CE	LYS	A	229	10.401	4.940	14.260	1.00	25.11
375	NZ	LYS	A	229	9.907	3.921	15.249	1.00	28.39
376	C	LYS	A	229	12.643	2.889	10.614	1.00	18.28
377	O	LYS	A	229	11.662	2.210	10.902	1.00	17.81
378	N	PHE	A	230	13.016	3.159	9.362	1.00	19.38
379	CA	PHE	A	230	12.238	2.857	8.170	1.00	17.62
380	CB	PHE	A	230	12.937	3.454	6.939	1.00	16.93
381	CG	PHE	A	230	12.211	3.217	5.658	1.00	16.42
382	CD1	PHE	A	230	11.020	3.878	5.388	1.00	17.12
383	CD2	PHE	A	230	12.683	2.284	4.744	1.00	18.74
384	CE1	PHE	A	230	10.296	3.611	4.226	1.00	18.18
385	CE2	PHE	A	230	11.968	1.997	3.569	1.00	19.04
386	CZ	PHE	A	230	10.769	2.666	3.314	1.00	18.96
387	C	PHE	A	230	11.938	1.380	7.959	1.00	17.02
388	O	PHE	A	230	10.776	1.000	7.777	1.00	17.25
389	N	SER	A	231	12.971	0.551	7.992	1.00	17.74
390	CA	SER	A	231	12.810	−0.882	7.788	1.00	18.46
391	CB	SER	A	231	14.172	−1.563	7.651	1.00	18.00
392	OG	SER	A	231	15.005	−1.275	8.765	1.00	18.22
393	C	SER	A	231	12.005	−1.524	8.916	1.00	18.14
394	O	SER	A	231	11.374	−2.565	8.711	1.00	19.28
395	N	GLU	A	232	12.071	−0.931	10.109	1.00	18.65
396	CA	GLU	A	232	11.329	−1.420	11.277	1.00	18.42
397	CB	GLU	A	232	11.766	−0.685	12.541	1.00	21.44
398	CG	GLU	A	232	10.733	−0.690	13.698	1.00	24.22
399	CD	GLU	A	232	11.158	0.204	14.866	1.00	27.21
400	OE1	GLU	A	232	12.314	0.072	15.327	1.00	27.98
401	OE2	GLU	A	232	10.347	1.045	15.318	1.00	29.80
402	C	GLU	A	232	9.857	−1.149	11.035	1.00	16.09
403	O	GLU	A	232	9.031	−2.026	11.211	1.00	14.77
404	N	LEU	A	233	9.555	0.087	10.648	1.00	13.93
405	CA	LEU	A	233	8.191	0.514	10.349	1.00	13.81
406	CB	LEU	A	233	8.124	2.031	10.109	1.00	12.25
407	CG	LEU	A	233	8.385	2.956	11.314	1.00	12.32
408	CD1	LEU	A	233	8.406	4.374	10.841	1.00	12.38
409	CD2	LEU	A	233	7.341	2.789	12.399	1.00	13.65
410	C	LEU	A	233	7.646	−0.233	9.139	1.00	13.48
411	O	LEU	A	233	6.458	−0.523	9.073	1.00	15.95
412	N	ALA	A	234	8.503	−0.549	8.180	1.00	12.52
413	CA	ALA	A	234	8.049	−1.284	7.016	1.00	14.87
414	CB	ALA	A	234	9.112	−1.275	5.915	1.00	13.08
415	C	ALA	A	234	7.701	−2.729	7.459	1.00	16.06
416	O	ALA	A	234	6.619	−3.242	7.142	1.00	15.82
417	N	THR	A	235	8.578	−3.351	8.243	1.00	15.16
418	CA	THR	A	235	8.334	−4.707	8.738	1.00	15.64
419	CB	THR	A	235	9.540	−5.213	9.619	1.00	17.73
420	OG1	THR	A	235	10.662	−5.493	8.774	1.00	17.62
421	CG2	THR	A	235	9.198	−6.473	10.377	1.00	18.14
422	C	THR	A	235	7.015	−4.802	9.526	1.00	15.67
423	O	THR	A	235	6.244	−5.750	9.341	1.00	16.12
424	N	LYS	A	236	6.761	−3.838	10.400	1.00	14.40
425	CA	LYS	A	236	5.532	−3.854	11.179	1.00	15.93
426	CB	LYS	A	236	5.548	−2.778	12.264	1.00	16.01
427	CG	LYS	A	236	6.596	−2.951	13.334	1.00	21.21
428	CD	LYS	A	236	6.412	−1.894	14.419	1.00	23.81
429	CE	LYS	A	236	7.583	−1.851	15.394	1.00	24.68
430	NZ	LYS	A	236	7.749	−3.128	16.139	1.00	25.36
431	C	LYS	A	236	4.342	−3.633	10.260	1.00	14.33
432	O	LYS	A	236	3.231	−4.088	10.538	1.00	13.57
433	N	CYS	A	237	4.579	−2.938	9.156	1.00	14.60
434	CA	CYS	A	237	3.519	−2.681	8.217	1.00	16.39
435	CB	CYS	A	237	3.870	−1.561	7.234	1.00	14.97
436	SG	CYS	A	237	2.335	−0.904	6.483	1.00	17.49
437	C	CYS	A	237	3.158	−3.979	7.489	1.00	16.47
438	O	CYS	A	237	1.984	−4.327	7.360	1.00	17.24
439	N	ILE	A	238	4.170	−4.722	7.054	1.00	15.33
440	CA	ILE	A	238	3.934	−5.978	6.352	1.00	13.85
441	CB	ILE	A	238	5.264	−6.601	5.999	1.00	13.01
442	CG2	ILE	A	238	5.073	−8.038	5.514	1.00	14.88
443	CG1	ILE	A	238	5.978	−5.715	4.969	1.00	12.70
444	CD1	ILE	A	238	7.405	−6.092	4.758	1.00	10.75
445	C	ILE	A	238	3.078	−6.930	7.195	1.00	14.22
446	O	ILE	A	238	2.208	−7.642	6.691	1.00	14.79
447	N	ILE	A	239	3.359	−6.966	8.482	1.00	14.17
448	CA	ILE	A	239	2.609	−7.794	9.414	1.00	14.19
449	CB	ILE	A	239	3.238	−7.724	10.827	1.00	14.59
450	CG2	ILE	A	239	2.230	−8.068	11.870	1.00	15.96
451	CG1	ILE	A	239	4.464	−8.635	10.917	1.00	13.80
452	CD1	ILE	A	239	5.315	−8.368	12.155	1.00	13.34
453	C	ILE	A	239	1.168	−7.274	9.443	1.00	14.54
454	O	ILE	A	239	0.226	−8.057	9.452	1.00	14.16
455	N	LYS	A	240	0.988	−5.962	9.419	1.00	15.39
456	CA	LYS	A	240	−0.361	−5.415	9.427	1.00	15.53
457	CB	LYS	A	240	−0.350	−3.917	9.717	1.00	18.27
458	CG	LYS	A	240	−0.078	−3.589	11.170	1.00	21.05
459	CD	LYS	A	240	−1.336	−3.699	12.002	1.00	23.72
460	CE	LYS	A	240	−1.050	−4.179	13.432	1.00	27.33
461	NZ	LYS	A	240	−0.927	−5.697	13.537	1.00	30.09
462	C	LYS	A	240	−1.107	−5.702	8.131	1.00	15.65
463	O	LYS	A	240	−2.336	−5.785	8.139	1.00	13.48
464	N	ILE	A	241	−0.369	−5.867	7.031	1.00	14.37
465	CA	ILE	A	241	−0.977	−6.171	5.739	1.00	15.71
466	CB	ILE	A	241	−0.012	−5.897	4.560	1.00	15.46
467	CG2	ILE	A	241	−0.540	−6.514	3.275	1.00	17.68
468	CG1	ILE	A	241	0.111	−4.389	4.349	1.00	16.06
469	CD1	ILE	A	241	1.192	−3.933	3.377	1.00	17.03
470	C	ILE	A	241	−1.450	−7.630	5.746	1.00	16.21
471	O	ILE	A	241	−2.542	−7.950	5.259	1.00	15.85
472	N	VAL	A	242	−0.631	−8.505	6.332	1.00	17.19
473	CA	VAL	A	242	−0.964	−9.923	6.455	1.00	16.87
474	CB	VAL	A	242	0.180	−10.726	7.071	1.00	15.52
475	CG1	VAL	A	242	−0.310	−12.078	7.478	1.00	15.69
476	CG2	VAL	A	242	1.319	−10.848	6.068	1.00	16.20
477	C	VAL	A	242	−2.213	−10.049	7.316	1.00	16.56
478	O	VAL	A	242	−3.130	−10.786	6.968	1.00	16.69
479	N	GLU	A	243	−2.269	−9.291	8.407	1.00	16.45
480	CA	GLU	A	243	−3.451	−9.301	9.271	1.00	19.31
481	CB	GLU	A	243	−3.273	−8.371	10.468	1.00	22.56
482	CG	GLU	A	243	−4.521	−8.364	11.304	1.00	27.44
483	CD	GLU	A	243	−4.599	−7.233	12.284	1.00	31.18
484	OE1	GLU	A	243	−3.565	−6.948	12.933	1.00	33.07
485	OE2	GLU	A	243	−5.711	−6.649	12.418	1.00	33.67
486	C	GLU	A	243	−4.697	−8.839	8.500	1.00	17.64
487	O	GLU	A	243	−5.775	−9.350	8.703	1.00	14.49
488	N	PHE	A	244	−4.527	−7.799	7.686	1.00	18.29
489	CA	PHE	A	244	−5.586	−7.235	6.845	1.00	16.37
490	CB	PHE	A	244	−5.061	−6.002	6.093	1.00	17.51
491	CG	PHE	A	244	−5.971	−5.497	4.998	1.00	14.72
492	CD1	PHE	A	244	−5.638	−5.690	3.666	1.00	15.96
493	CD2	PHE	A	244	−7.121	−4.800	5.298	1.00	15.04
494	CE1	PHE	A	244	−6.439	−5.191	2.643	1.00	16.27
495	CE2	PHE	A	244	−7.934	−4.295	4.281	1.00	16.72
496	CZ	PHE	A	244	−7.595	−4.489	2.954	1.00	14.78
497	C	PHE	A	244	−6.062	−8.294	5.853	1.00	15.24
498	O	PHE	A	244	−7.264	−8.505	5.718	1.00	15.07
499	N	ALA	A	245	−5.118	−8.972	5.195	1.00	14.79
500	CA	ALA	A	245	−5.437	−10.034	4.226	1.00	14.77
501	CB	ALA	A	245	−4.147	−10.593	3.592	1.00	14.54
502	C	ALA	A	245	−6.216	−11.157	4.895	1.00	13.91
503	O	ALA	A	245	−7.220	−11.586	4.386	1.00	13.71
504	N	LYS	A	246	−5.762	−11.596	6.063	1.00	14.98
505	CA	LYS	A	246	−6.421	−12.668	6.808	1.00	16.59
506	CB	LYS	A	246	−5.658	−12.963	8.100	1.00	17.81
507	CG	LYS	A	246	−4.274	−13.575	7.925	1.00	20.05
508	CD	LYS	A	246	−4.351	−14.931	7.282	1.00	21.82
509	CE	LYS	A	246	−3.225	−15.824	7.778	1.00	23.30
510	NZ	LYS	A	246	−3.422	−17.231	7.280	1.00	26.39
511	C	LYS	A	246	−7.867	−12.341	7.184	1.00	17.03
512	O	LYS	A	246	−8.634	−13.238	7.522	1.00	16.72
513	N	ARG	A	247	−8.209	−11.054	7.186	1.00	17.90
514	CA	ARG	A	247	−9.548	−10.599	7.533	1.00	18.60
515	CB	ARG	A	247	−9.443	−9.373	8.421	1.00	20.73
516	CG	ARG	A	247	−8.784	−9.712	9.734	1.00	22.93
517	CD	ARG	A	247	−8.272	−8.510	10.443	1.00	24.91
518	NE	ARG	A	247	−9.324	−7.528	10.618	1.00	28.82
519	CZ	ARG	A	247	−9.510	−6.802	11.714	1.00	29.63
520	NH1	ARG	A	247	−8.726	−6.940	12.772	1.00	28.78
521	NH2	ARG	A	247	−10.442	−5.869	11.711	1.00	30.29
522	C	ARG	A	247	−10.488	−10.356	6.347	1.00	18.81
523	O	ARG	A	247	−11.680	−10.086	6.543	1.00	20.35
524	N	LEU	A	248	−9.973	−10.510	5.128	1.00	18.00
525	CA	LEU	A	248	−10.775	−10.339	3.931	1.00	17.53
526	CB	LEU	A	248	−9.896	−10.045	2.706	1.00	17.06
527	CG	LEU	A	248	−9.054	−8.760	2.591	1.00	15.80
528	CD1	LEU	A	248	−8.275	−8.778	1.266	1.00	12.46
529	CD2	LEU	A	248	−9.927	−7.506	2.710	1.00	14.81
530	C	LEU	A	248	−11.534	−11.646	3.713	1.00	18.26
531	O	LEU	A	248	−10.965	−12.729	3.824	1.00	17.01
532	N	PRO	A	249	−12.843	−11.567	3.419	1.00	18.73
533	CD	PRO	A	249	−13.719	−10.384	3.470	1.00	19.57
534	CA	PRO	A	249	−13.633	−12.779	3.200	1.00	19.22
535	CB	PRO	A	249	−14.977	−12.222	2.744	1.00	19.79
536	CG	PRO	A	249	−15.099	−11.016	3.621	1.00	20.52
537	C	PRO	A	249	−13.053	−13.756	2.197	1.00	19.27
538	O	PRO	A	249	−12.726	−13.387	1.075	1.00	20.55
539	N	GLY	A	250	−12.903	−15.004	2.641	1.00	20.87
540	CA	GLY	A	250	−12.401	−16.083	1.801	1.00	19.86
541	C	GLY	A	250	−10.907	−16.209	1.590	1.00	20.13
542	O	GLY	A	250	−10.454	−17.215	1.044	1.00	21.37
543	N	PHE	A	251	−10.130	−15.231	2.048	1.00	19.34
544	CA	PHE	A	251	−8.672	−15.257	1.861	1.00	19.32
545	CB	PHE	A	251	−8.036	−14.001	2.499	1.00	18.12
546	CG	PHE	A	251	−6.559	−13.903	2.297	1.00	17.10
547	CD1	PHE	A	251	−6.043	−13.423	1.094	1.00	17.68
548	CD2	PHE	A	251	−5.682	−14.368	3.277	1.00	15.40
549	CE1	PHE	A	251	−4.664	−13.414	0.859	1.00	16.47
550	CE2	PHE	A	251	−4.324	−14.365	3.060	1.00	16.00
551	CZ	PHE	A	251	−3.804	−13.891	1.850	1.00	17.36
552	C	PHE	A	251	−8.157	−16.518	2.535	1.00	18.63
553	O	PHE	A	251	−7.576	−17.418	1.921	1.00	18.89
554	N	THR	A	252	−8.505	−16.604	3.798	1.00	18.51
555	CA	THR	A	252	−8.145	−17.691	4.655	1.00	19.35
556	CB	THR	A	252	−8.678	−17.342	6.033	1.00	20.77
557	OG1	THR	A	252	−7.644	−16.680	6.767	1.00	23.36
558	CG2	THR	A	252	−9.212	−18.514	6.774	1.00	23.22
559	C	THR	A	252	−8.634	−19.033	4.132	1.00	19.84
560	O	THR	A	252	−8.220	−20.077	4.625	1.00	20.58
561	N	GLY	A	253	−9.451	−19.000	3.082	1.00	21.05
562	CA	GLY	A	253	−9.980	−20.224	2.500	1.00	20.89
563	C	GLY	A	253	−9.123	−20.789	1.383	1.00	21.46
564	O	GLY	A	253	−9.376	−21.899	0.890	1.00	21.33
565	N	LEU	A	254	−8.135	−20.011	0.948	1.00	20.37
566	CA	LEU	A	254	−7.219	−20.429	−0.116	1.00	18.42
567	CB	LEU	A	254	−6.552	−19.180	−0.708	1.00	20.47
568	CG	LEU	A	254	−7.335	−18.347	−1.725	1.00	22.68
569	CD1	LEU	A	254	−8.777	−18.338	−1.352	1.00	23.04
570	CD2	LEU	A	254	−6.780	−16.929	−1.848	1.00	22.37
571	C	LEU	A	254	−6.156	−21.355	0.502	1.00	17.86
572	O	LEU	A	254	−6.072	−21.459	1.724	1.00	16.98
573	N	SER	A	255	−5.357	−22.043	−0.300	1.00	15.32
574	CA	SER	A	255	−4.340	−22.876	0.308	1.00	16.43
575	CB	SER	A	255	−3.810	−23.881	−0.676	1.00	16.76
576	OG	SER	A	255	−3.416	−23.202	−1.825	1.00	17.59
577	C	SER	A	255	−3.199	−21.973	0.775	1.00	16.89
578	O	SER	A	255	−2.991	−20.862	0.234	1.00	15.37
579	N	ILE	A	256	−2.452	−22.465	1.760	1.00	16.17
580	CA	ILE	A	256	−1.344	−21.714	2.333	1.00	18.47
581	CB	ILE	A	256	−0.580	−22.511	3.457	1.00	17.13
582	CG2	ILE	A	256	0.288	−23.648	2.868	1.00	18.77
583	CG1	ILE	A	256	0.333	−21.575	4.219	1.00	16.65
584	CD1	ILE	A	256	−0.402	−20.528	4.973	1.00	19.69
585	C	ILE	A	256	−0.406	−21.258	1.228	1.00	18.89
586	O	ILE	A	256	0.061	−20.115	1.243	1.00	19.36
587	N	ALA	A	257	−0.169	−22.122	0.244	1.00	18.48
588	CA	ALA	A	257	0.698	−21.762	−0.874	1.00	18.14
589	CB	ALA	A	257	0.736	−22.868	−1.916	1.00	15.57
590	C	ALA	A	257	0.174	−20.487	−1.504	1.00	18.90
591	O	ALA	A	257	0.892	−19.506	−1.633	1.00	20.07
592	N	ASP	A	258	−1.109	−20.486	−1.827	1.00	19.03
593	CA	ASP	A	258	−1.721	−19.346	−2.483	1.00	18.65
594	CB	ASP	A	258	−3.141	−19.680	−2.955	1.00	20.22
595	CG	ASP	A	258	−3.160	−20.499	−4.235	1.00	21.11
596	OD1	ASP	A	258	−4.277	−20.872	−4.651	1.00	23.18
597	OD2	ASP	A	258	−2.089	−20.766	−4.825	1.00	19.47
598	C	ASP	A	258	−1.731	−18.081	−1.645	1.00	17.57
599	O	ASP	A	258	−1.435	−17.016	−2.162	1.00	16.61
600	N	GLN	A	259	−2.078	−18.195	−0.367	1.00	16.44
601	CA	GLN	A	259	−2.121	−17.036	0.510	1.00	14.15
602	CB	GLN	A	259	−2.477	−17.468	1.931	1.00	15.92
603	CG	GLN	A	259	−3.879	−18.041	2.083	1.00	15.51
604	CD	GLN	A	259	−4.215	−18.391	3.511	1.00	16.36
605	OE1	GLN	A	259	−3.718	−17.788	4.433	1.00	19.80
606	NE2	GLN	A	259	−5.080	−19.358	3.694	1.00	16.26
607	C	GLN	A	259	−0.768	−16.325	0.487	1.00	14.18
608	O	GLN	A	259	−0.714	−15.098	0.373	1.00	14.26
609	N	ILE	A	260	0.314	−17.107	0.523	1.00	13.39
610	CA	ILE	A	260	1.675	−16.582	0.509	1.00	13.11
611	CB	ILE	A	260	2.709	−17.657	0.974	1.00	11.65
612	CG2	ILE	A	260	4.122	−17.178	0.719	1.00	12.53
613	CG1	ILE	A	260	2.557	−17.892	2.498	1.00	13.30
614	CD1	ILE	A	260	3.082	−19.222	3.021	1.00	12.78
615	C	ILE	A	260	2.007	−15.992	−0.860	1.00	14.57
616	O	ILE	A	260	2.548	−14.905	−0.944	1.00	14.92
617	N	THR	A	261	1.614	−16.676	−1.927	1.00	14.56
618	CA	THR	A	261	1.845	−16.192	−3.279	1.00	15.06
619	CB	THR	A	261	1.243	−17.157	−4.306	1.00	14.24
620	OG1	THR	A	261	1.938	−18.405	−4.240	1.00	16.34
621	CG2	THR	A	261	1.330	−16.592	−5.715	1.00	15.63
622	C	THR	A	261	1.206	−14.809	−3.436	1.00	15.18
623	O	THR	A	261	1.865	−13.862	−3.848	1.00	16.32
624	N	LEU	A	262	−0.065	−14.679	−3.085	1.00	14.08
625	CA	LEU	A	262	−0.737	−13.383	−3.196	1.00	14.50
626	CB	LEU	A	262	−2.218	−13.491	−2.823	1.00	12.30
627	CG	LEU	A	262	−3.094	−14.247	−3.828	1.00	12.27
628	CD1	LEU	A	262	−4.510	−14.299	−3.279	1.00	11.50
629	CD2	LEU	A	262	−3.043	−13.549	−5.170	1.00	11.07
630	C	LEU	A	262	−0.095	−12.305	−2.333	1.00	13.40
631	O	LEU	A	262	0.019	−11.144	−2.759	1.00	12.89
632	N	LEU	A	263	0.270	−12.672	−1.113	1.00	11.86
633	CA	LEU	A	263	0.876	−11.726	−0.200	1.00	13.48
634	CB	LEU	A	263	1.063	−12.358	1.174	1.00	13.89
635	CG	LEU	A	263	−0.173	−12.363	2.061	1.00	14.62
636	CD1	LEU	A	263	0.037	−13.259	3.256	1.00	12.39
637	CD2	LEU	A	263	−0.477	−10.934	2.485	1.00	15.87
638	C	LEU	A	263	2.206	−11.248	−0.746	1.00	14.62
639	O	LEU	A	263	2.486	−10.053	−0.771	1.00	16.35
640	N	LYS	A	264	3.026	−12.168	−1.225	1.00	15.83
641	CA	LYS	A	264	4.323	−11.781	−1.779	1.00	16.21
642	CB	LYS	A	264	5.134	−13.027	−2.165	1.00	16.46
643	CG	LYS	A	264	5.888	−13.666	−0.985	1.00	16.55
644	CD	LYS	A	264	6.279	−15.099	−1.248	1.00	15.86
645	CE	LYS	A	264	7.210	−15.570	−0.144	1.00	17.98
646	NZ	LYS	A	264	8.553	−14.962	−0.342	1.00	16.92
647	C	LYS	A	264	4.180	−10.871	−2.994	1.00	15.33
648	O	LYS	A	264	4.859	−9.867	−3.106	1.00	15.30
649	N	ALA	A	265	3.274	−11.232	−3.889	1.00	14.92
650	CA	ALA	A	265	3.049	−10.486	−5.115	1.00	16.32
651	CB	ALA	A	265	2.241	−11.340	−6.070	1.00	14.20
652	C	ALA	A	265	2.418	−9.092	−4.995	1.00	16.04
653	O	ALA	A	265	2.645	−8.236	−5.850	1.00	16.12
654	N	ALA	A	266	1.644	−8.851	−3.942	1.00	15.90
655	CA	ALA	A	266	0.962	−7.557	−3.766	1.00	17.39
656	CB	ALA	A	266	−0.552	−7.781	−3.669	1.00	16.38
657	C	ALA	A	266	1.425	−6.713	−2.577	1.00	17.22
658	O	ALA	A	266	1.041	−5.543	−2.449	1.00	16.41
659	N	CYS	A	267	2.253	−7.298	−1.717	1.00	15.91
660	CA	CYS	A	267	2.710	−6.602	−0.527	1.00	17.69
661	CB	CYS	A	267	3.633	−7.493	0.281	1.00	18.90
662	SG	CYS	A	267	3.833	−6.875	1.915	1.00	23.66
663	C	CYS	A	267	3.355	−5.227	−0.756	1.00	16.15
664	O	CYS	A	267	2.985	−4.259	−0.083	1.00	14.43
665	N	LEU	A	268	4.279	−5.140	−1.715	1.00	14.38
666	CA	LEU	A	268	4.923	−3.873	−2.018	1.00	15.09
667	CB	LEU	A	268	6.069	−4.048	−3.020	1.00	14.82
668	CG	LEU	A	268	7.445	−3.400	−2.709	1.00	16.13
669	CD1	LEU	A	268	8.323	−3.377	−3.999	1.00	13.28
670	CD2	LEU	A	268	7.287	−1.984	−2.136	1.00	13.62
671	C	LEU	A	268	3.896	−2.895	−2.571	1.00	15.22
672	O	LEU	A	268	3.899	−1.722	−2.184	1.00	15.41
673	N	ASP	A	269	3.033	−3.358	−3.479	1.00	14.39
674	CA	ASP	A	269	2.001	−2.494	−4.043	1.00	14.73
675	CB	ASP	A	269	0.964	−3.300	−4.829	1.00	16.26
676	CG	ASP	A	269	1.514	−3.916	−6.104	1.00	16.52
677	OD1	ASP	A	269	0.723	−4.379	−6.947	1.00	19.84
678	OD2	ASP	A	269	2.721	−3.959	−6.281	1.00	18.78
679	C	ASP	A	269	1.268	−1.800	−2.901	1.00	16.42
680	O	ASP	A	269	1.246	−0.559	−2.817	1.00	17.01
681	N	ILE	A	270	0.714	−2.602	−1.985	1.00	16.86
682	CA	ILE	A	270	−0.061	−2.066	−0.854	1.00	16.75
683	CB	ILE	A	270	−0.784	−3.187	−0.067	1.00	16.55
684	CG2	ILE	A	270	−1.645	−2.599	1.061	1.00	16.85
685	CG1	ILE	A	270	−1.695	−3.974	−1.006	1.00	15.45
686	CD1	ILE	A	270	−2.408	−5.102	−0.308	1.00	18.34
687	C	ILE	A	270	0.752	−1.176	0.093	1.00	15.88
688	O	ILE	A	270	0.245	−0.172	0.581	1.00	16.48
689	N	LEU	A	271	2.003	−1.529	0.346	1.00	15.65
690	CA	LEU	A	271	2.860	−0.723	1.207	1.00	16.49
691	CB	LEU	A	271	4.223	−1.405	1.302	1.00	16.24
692	CG	LEU	A	271	4.857	−1.820	2.632	1.00	17.43
693	CD1	LEU	A	271	3.865	−2.078	3.723	1.00	14.58
694	CD2	LEU	A	271	5.743	−3.017	2.389	1.00	16.24
695	C	LEU	A	271	2.967	0.661	0.538	1.00	16.41
696	O	LEU	A	271	2.871	1.690	1.210	1.00	17.42
697	N	MET	A	272	3.073	0.679	−0.795	1.00	16.60
698	CA	MET	A	272	3.172	1.927	−1.559	1.00	16.79
699	CB	MET	A	272	3.575	1.666	−3.020	1.00	17.65
700	CG	MET	A	272	4.996	1.199	−3.221	1.00	18.79
701	SD	MET	A	272	6.223	2.515	−3.063	1.00	22.97
702	CE	MET	A	272	7.580	1.837	−4.003	1.00	19.64
703	C	MET	A	272	1.846	2.702	−1.524	1.00	17.44
704	O	MET	A	272	1.824	3.940	−1.380	1.00	19.90
705	N	LEU	A	273	0.733	2.007	−1.683	1.00	14.90
706	CA	LEU	A	273	−0.530	2.703	−1.632	1.00	14.87
707	CB	LEU	A	273	−1.661	1.728	−1.888	1.00	15.48
708	CG	LEU	A	273	−3.038	2.357	−1.833	1.00	16.54
709	CD1	LEU	A	273	−3.136	3.412	−2.933	1.00	17.29
710	CD2	LEU	A	273	−4.084	1.266	−2.023	1.00	15.37
711	C	LEU	A	273	−0.688	3.333	−0.249	1.00	15.34
712	O	LEU	A	273	−1.083	4.493	−0.131	1.00	15.36
713	N	ARG	A	274	−0.330	2.573	0.789	1.00	15.34
714	CA	ARG	A	274	−0.442	3.028	2.164	1.00	15.78
715	CB	ARG	A	274	−0.097	1.919	3.150	1.00	16.75
716	CG	ARG	A	274	−1.222	0.873	3.234	1.00	17.30
717	CD	ARG	A	274	−1.044	−0.105	4.365	1.00	17.86
718	NE	ARG	A	274	−2.252	−0.918	4.516	1.00	21.93
719	CZ	ARG	A	274	−2.520	−1.701	5.561	1.00	22.23
720	NH1	ARG	A	274	−1.663	−1.788	6.576	1.00	21.99
721	NH2	ARG	A	274	−3.657	−2.384	5.597	1.00	20.01
722	C	ARG	A	274	0.321	4.301	2.459	1.00	17.06
723	O	ARG	A	274	−0.306	5.279	2.816	1.00	18.66
724	N	ILE	A	275	1.645	4.349	2.279	1.00	18.51
725	CA	ILE	A	275	2.328	5.618	2.564	1.00	18.34
726	GB	ILE	A	275	3.847	5.555	2.521	1.00	18.08
727	CG2	ILE	A	275	4.420	5.601	3.927	1.00	19.84
728	CG1	ILE	A	275	4.321	4.447	1.600	1.00	18.48
729	CD1	ILE	A	275	4.510	4.949	0.201	1.00	17.63
730	C	ILE	A	275	1.878	6.778	1.680	1.00	18.77
731	O	ILE	A	275	1.843	7.911	2.154	1.00	18.87
732	N	CYS	A	276	1.522	6.504	0.419	1.00	17.07
733	CA	CYS	A	276	1.058	7.554	−0.488	1.00	16.63
734	CB	CYS	A	276	0.985	7.062	−1.931	1.00	15.81
735	SG	CYS	A	276	2.610	6.888	−2.627	1.00	22.23
736	C	CYS	A	276	−0.279	8.164	−0.058	1.00	15.45
737	O	CYS	A	276	−0.587	9.272	−0.468	1.00	15.53
738	N	THR	A	277	−1.064	7.449	0.746	1.00	13.95
739	CA	THR	A	277	−2.321	7.993	1.249	1.00	15.92
740	CB	THR	A	277	−3.363	6.887	1.545	1.00	18.17
741	OG1	THR	A	277	−2.890	6.051	2.601	1.00	20.50
742	CG2	THR	A	277	−3.591	6.023	0.314	1.00	19.00
743	C	THR	A	277	−2.054	8.816	2.520	1.00	17.31
744	O	THR	A	277	−2.917	9.560	2.984	1.00	19.20
745	N	ARG	A	278	−0.842	8.691	3.060	1.00	17.51
746	CA	ARG	A	278	−0.386	9.411	4.266	1.00	17.48
747	CB	ARG	A	278	0.459	8.455	5.101	1.00	17.18
748	CG	ARG	A	278	−0.336	7.370	5.783	1.00	16.64
749	CD	ARG	A	278	−0.683	7.825	7.175	1.00	17.73
750	NE	ARG	A	278	−1.172	6.755	8.034	1.00	17.21
751	CZ	ARG	A	278	−0.487	5.667	8.346	1.00	19.13
752	NH1	ARG	A	278	0.733	5.484	7.861	1.00	20.62
753	NH2	ARG	A	278	−1.017	4.773	9.171	1.00	20.16
754	C	ARG	A	278	0.459	10.667	3.891	1.00	16.92
755	O	ARG	A	278	1.327	11.130	4.637	1.00	16.64
756	N	TYR	A	279	0.173	11.226	2.727	1.00	17.14
757	CA	TYR	A	279	0.910	12.362	2.248	1.00	15.32
758	CB	TYR	A	279	1.208	12.142	0.784	1.00	14.96
759	CG	TYR	A	279	1.709	13.344	0.060	1.00	15.39
760	CD1	TYR	A	279	2.998	13.831	0.265	1.00	15.10
761	CE1	TYR	A	279	3.451	14.915	−0.457	1.00	15.87
762	CD2	TYR	A	279	0.898	13.977	−0.875	1.00	16.01
763	CE2	TYR	A	279	1.341	15.050	−1.591	1.00	18.57
764	CZ	TYR	A	279	2.607	15.513	−1.388	1.00	17.47
765	OH	TYR	A	279	3.019	16.564	−2.161	1.00	20.53
766	C	TYR	A	279	0.192	13.667	2.493	1.00	15.96
767	O	TYR	A	279	−1.030	13.751	2.351	1.00	15.17
768	N	THR	A	280	0.965	14.663	2.935	1.00	17.68
769	CA	THR	A	280	0.468	16.014	3.218	1.00	18.60
770	CB	THR	A	280	0.888	16.507	4.600	1.00	18.35
771	OG1	THR	A	280	0.494	15.553	5.593	1.00	19.23
772	CG2	THR	A	280	0.196	17.793	4.905	1.00	19.36
773	C	THR	A	280	1.085	16.927	2.195	1.00	18.63
774	O	THR	A	280	2.275	17.213	2.256	1.00	19.24
775	N	PRO	A	281	0.286	17.392	1.233	1.00	19.26
776	CD	PRO	A	281	−1.165	17.253	1.086	1.00	19.67
777	CA	PRO	A	281	0.791	18.273	0.201	1.00	23.13
778	CB	PRO	A	281	−0.469	18.600	−0.606	1.00	21.19
779	CG	PRO	A	281	−1.326	17.477	−0.375	1.00	19.03
780	C	PRO	A	281	1.395	19.528	0.825	1.00	27.05
781	O	PRO	A	281	2.521	19.877	0.507	1.00	29.83
782	N	GLU	A	282	0.678	20.154	1.765	1.00	29.52
783	CA	GLU	A	282	1.132	21.389	2.435	1.00	30.92
784	CB	GLU	A	282	0.188	21.733	3.623	1.00	34.18
785	CG	GLU	A	282	−0.569	23.095	3.507	1.00	37.63
786	CD	GLU	A	282	0.121	24.277	4.231	1.00	39.35
787	OE1	GLU	A	282	1.126	24.839	3.717	1.00	39.81
788	OE2	GLU	A	282	−0.365	24.656	5.320	1.00	40.91
789	C	GLU	A	282	2.602	21.384	2.907	1.00	29.16
790	O	GLU	A	282	3.380	22.301	2.610	1.00	29.44
791	N	GLN	A	283	2.967	20.336	3.629	1.00	26.73
792	CA	GLN	A	283	4.298	20.181	4.168	1.00	25.15
793	CB	GLN	A	283	4.178	19.501	5.509	1.00	25.77
794	CG	GLN	A	283	3.161	20.158	6.363	1.00	26.99
795	CD	GLN	A	283	3.640	21.516	6.757	1.00	29.54
796	OE1	GLN	A	283	4.836	21.714	7.016	1.00	30.71
797	NE2	GLN	A	283	2.728	22.477	6.793	1.00	31.58
798	C	GLN	A	283	5.197	19.326	3.301	1.00	25.04
799	O	GLN	A	283	6.388	19.230	3.583	1.00	25.52
800	N	ASP	A	284	4.625	18.687	2.276	1.00	23.29
801	CA	ASP	A	284	5.365	17.786	1.399	1.00	20.93
802	CB	ASP	A	284	6.450	18.520	0.622	1.00	21.51
803	CG	ASP	A	284	6.930	17.737	−0.581	1.00	20.88
804	OD1	ASP	A	284	6.080	17.221	−1.352	1.00	18.48
805	OD2	ASP	A	284	8.162	17.677	−0.770	1.00	20.71
806	C	ASP	A	284	5.995	16.686	2.253	1.00	19.57
807	O	ASP	A	284	7.209	16.437	2.189	1.00	17.45
808	N	THR	A	285	5.154	16.058	3.073	1.00	19.17
809	CA	THR	A	285	5.578	14.983	3.955	1.00	18.19
810	CB	THR	A	285	5.501	15.404	5.451	1.00	18.36
811	OG1	THR	A	285	4.152	15.773	5.781	1.00	17.95
812	CG2	THR	A	285	6.471	16.543	5.763	1.00	16.08
813	C	THR	A	285	4.699	13.742	3.817	1.00	17.40
814	O	THR	A	285	3.649	13.779	3.173	1.00	16.90
815	N	MET	A	286	5.163	12.654	4.429	1.00	17.39
816	CA	MET	A	286	4.462	11.375	4.498	1.00	17.47
817	CB	MET	A	286	5.031	10.337	3.509	1.00	16.08
818	CG	MET	A	286	4.692	10.646	2.053	1.00	15.31
819	SD	MET	A	286	5.340	9.441	0.905	1.00	21.84
820	CE	MET	A	286	4.558	9.994	−0.514	1.00	13.72
821	C	MET	A	286	4.609	10.893	5.951	1.00	17.11
822	O	MET	A	286	5.672	11.040	6.579	1.00	16.22
823	N	THR	A	287	3.515	10.377	6.496	1.00	15.98
824	CA	THR	A	287	3.472	9.905	7.872	1.00	15.63
825	CB	THR	A	287	2.345	10.639	8.617	1.00	14.95
826	OG1	THR	A	287	2.591	12.039	8.503	1.00	16.07
827	CG2	THR	A	287	2.291	10.260	10.098	1.00	14.81
828	C	THR	A	287	3.272	8.387	7.937	1.00	15.17
829	O	THR	A	287	2.454	7.825	7.221	1.00	14.62
830	N	PHE	A	288	4.105	7.732	8.737	1.00	15.64
831	CA	PHE	A	288	4.060	6.292	8.927	1.00	16.95
832	CB	PHE	A	288	5.463	5.770	9.263	1.00	16.87
833	CG	PHE	A	288	6.443	5.919	8.134	1.00	16.91
834	CD1	PHE	A	288	6.982	7.164	7.818	1.00	18.03
835	CD2	PHE	A	288	6.782	4.831	7.345	1.00	15.86
836	CE1	PHE	A	288	7.827	7.309	6.733	1.00	15.63
837	CE2	PHE	A	288	7.629	4.977	6.265	1.00	13.84
838	CZ	PHE	A	288	8.148	6.206	5.958	1.00	13.79
839	C	PHE	A	288	3.076	6.021	10.060	1.00	18.22
840	O	PHE	A	288	2.613	6.965	10.705	1.00	17.92
841	N	SER	A	289	2.796	4.750	10.345	1.00	18.84
842	CA	SER	A	289	1.825	4.374	11.369	1.00	18.84
843	CB	SER	A	289	1.475	2.918	11.235	1.00	18.32
844	OG	SER	A	289	0.975	2.710	9.939	1.00	20.62
845	C	SER	A	289	2.088	4.698	12.821	1.00	19.48
846	O	SER	A	289	1.194	4.553	13.642	1.00	21.03
847	N	ASP	A	290	3.308	5.090	13.167	1.00	18.56
848	CA	ASP	A	290	3.569	5.461	14.543	1.00	16.64
849	CB	ASP	A	290	4.910	4.879	15.021	1.00	19.14
850	CG	ASP	A	290	6.116	5.604	14.462	1.00	17.90
851	OD1	ASP	A	290	6.064	6.131	13.343	1.00	19.78
852	OD2	ASP	A	290	7.133	5.622	15.159	1.00	17.99
853	C	ASP	A	290	3.487	7.005	14.710	1.00	16.67
854	O	ASP	A	290	3.504	7.532	15.829	1.00	16.11
855	N	GLY	A	291	3.308	7.707	13.596	1.00	14.39
856	CA	GLY	A	291	3.227	9.155	13.627	1.00	14.41
857	C	GLY	A	291	4.476	9.773	13.034	1.00	15.52
858	O	GLY	A	291	4.473	10.956	12.721	1.00	16.88
859	N	LEU	A	292	5.544	8.993	12.869	1.00	13.32
860	CA	LEU	A	292	6.759	9.534	12.290	1.00	14.58
861	CB	LEU	A	292	7.840	8.447	12.123	1.00	14.51
862	CG	LEU	A	292	9.165	8.928	11.494	1.00	14.16
863	CD1	LEU	A	292	9.777	10.015	12.337	1.00	12.49
864	CD2	LEU	A	292	10.138	7.778	11.272	1.00	10.42
865	C	LEU	A	292	6.436	10.177	10.943	1.00	13.88
866	O	LEU	A	292	5.942	9.522	10.060	1.00	15.24
867	N	THR	A	293	6.676	11.479	10.837	1.00	14.29
868	CA	THR	A	293	6.427	12.275	9.644	1.00	14.37
869	CB	THR	A	293	5.621	13.504	10.053	1.00	16.10
870	OG1	THR	A	293	4.435	13.056	10.720	1.00	16.90
871	CG2	THR	A	293	5.259	14.356	8.851	1.00	14.68
872	C	THR	A	293	7.759	12.736	9.062	1.00	14.38
873	O	THR	A	293	8.475	13.494	9.697	1.00	14.25
874	N	LEU	A	294	8.108	12.271	7.871	1.00	14.86
875	CA	LEU	A	294	9.369	12.656	7.246	1.00	15.36
876	CB	LEU	A	294	10.135	11.418	6.803	1.00	11.39
877	CG	LEU	A	294	10.406	10.358	7.871	1.00	14.10
878	CD1	LEU	A	294	11.173	9.176	7.269	1.00	12.89
879	CD2	LEU	A	294	11.209	10.954	9.008	1.00	10.35
880	C	LEU	A	294	9.121	13.518	6.027	1.00	16.14
881	O	LEU	A	294	8.156	13.308	5.307	1.00	17.38
882	N	ASN	A	295	9.955	14.521	5.803	1.00	17.13
883	CA	ASN	A	295	9.781	15.340	4.604	1.00	17.00
884	CB	ASN	A	295	10.402	16.732	4.756	1.00	18.00
885	CG	ASN	A	295	11.907	16.705	4.955	1.00	18.40
886	OD1	ASN	A	295	12.585	15.744	4.622	1.00	19.72
887	ND2	ASN	A	295	12.435	17.787	5.494	1.00	21.69
888	C	ASN	A	295	10.362	14.588	3.412	1.00	15.70
889	O	ASN	A	295	10.872	13.477	3.573	1.00	16.12
890	N	ARG	A	296	10.265	15.163	2.217	1.00	15.71
891	CA	ARG	A	296	10.763	14.512	0.996	1.00	13.87
892	CB	ARG	A	296	10.486	15.382	−0.211	1.00	14.02
893	CG	ARG	A	296	10.843	14.721	−1.480	1.00	12.59
894	CD	ARG	A	296	10.551	15.621	−2.635	1.00	14.33
895	NE	ARG	A	296	9.137	15.980	−2.756	1.00	14.74
896	CZ	ARG	A	296	8.449	15.881	−3.887	1.00	13.62
897	NH1	ARG	A	296	9.029	15.416	−4.988	1.00	12.42
898	NH2	ARG	A	296	7.184	16.276	−3.919	1.00	13.67
899	C	ARG	A	296	12.229	14.152	1.018	1.00	15.32
900	O	ARG	A	296	12.639	13.078	0.533	1.00	16.68
901	N	THR	A	297	13.037	15.046	1.576	1.00	14.40
902	CA	THR	A	297	14.455	14.806	1.675	1.00	13.98
903	CB	THR	A	297	15.152	16.025	2.275	1.00	14.79
904	OG1	THR	A	297	15.182	17.055	1.291	1.00	16.57
905	CG2	THR	A	297	16.551	15.700	2.730	1.00	14.07
906	C	THR	A	297	14.710	13.581	2.527	1.00	14.36
907	O	THR	A	297	15.529	12.734	2.180	1.00	14.79
908	N	GLN	A	298	14.033	13.509	3.666	1.00	15.33
909	CA	GLN	A	298	14.176	12.383	4.576	1.00	15.06
910	CB	GLN	A	298	13.520	12.704	5.927	1.00	16.77
911	CG	GLN	A	298	14.257	13.756	6.743	1.00	15.29
912	CD	GLN	A	298	13.446	14.272	7.923	1.00	17.60
913	OE1	GLN	A	298	12.222	14.328	7.873	1.00	17.10
914	NE2	GLN	A	298	14.132	14.713	8.964	1.00	17.23
915	C	GLN	A	298	13.657	11.054	3.973	1.00	15.13
916	O	GLN	A	298	14.256	9.999	4.218	1.00	15.27
917	N	MET	A	299	12.561	11.082	3.201	1.00	15.38
918	CA	MET	A	299	12.076	9.848	2.564	1.00	15.55
919	CB	MET	A	299	10.863	10.093	1.703	1.00	12.60
920	CG	MET	A	299	9.663	10.434	2.476	1.00	15.70
921	SD	MET	A	299	9.234	9.124	3.549	1.00	17.19
922	CE	MET	A	299	8.349	8.002	2.467	1.00	16.80
923	C	MET	A	299	13.189	9.358	1.652	1.00	16.05
924	O	MET	A	299	13.461	8.167	1.572	1.00	17.34
925	N	HIS	A	300	13.835	10.302	0.967	1.00	16.17
926	CA	HIS	A	300	14.938	9.995	0.065	1.00	16.17
927	CB	HIS	A	300	15.429	11.282	−0.636	1.00	15.59
928	CG	HIS	A	300	16.578	11.061	−1.561	1.00	15.33
929	CD2	HIS	A	300	16.620	10.844	−2.897	1.00	17.23
930	ND1	HIS	A	300	17.885	10.994	−1.123	1.00	16.64
931	CE1	HIS	A	300	18.675	10.737	−2.149	1.00	14.56
932	NE2	HIS	A	300	17.937	10.641	−3.236	1.00	16.30
933	C	HIS	A	300	16.081	9.345	0.831	1.00	16.05
934	O	HIS	A	300	16.565	8.265	0.455	1.00	15.26
935	N	ASN	A	301	16.475	10.004	1.919	1.00	16.64
936	CA	ASN	A	301	17.573	9.576	2.778	1.00	16.77
937	CB	ASN	A	301	17.895	10.658	3.823	1.00	16.75
938	CG	ASN	A	301	18.406	11.957	3.184	1.00	20.30
939	OD1	ASN	A	301	18.804	11.967	1.999	1.00	20.59
940	ND2	ASN	A	301	18.335	13.066	3.931	1.00	18.69
941	C	ASN	A	301	17.288	8.276	3.460	1.00	16.93
942	O	ASN	A	301	18.206	7.536	3.774	1.00	17.99
943	N	ALA	A	302	16.012	7.988	3.680	1.00	17.82
944	CA	ALA	A	302	15.612	6.756	4.338	1.00	16.47
945	CB	ALA	A	302	14.205	6.884	4.842	1.00	15.77
946	C	ALA	A	302	15.760	5.503	3.469	1.00	16.21
947	O	ALA	A	302	15.642	4.398	3.961	1.00	16.49
948	N	GLY	A	303	16.016	5.665	2.180	1.00	17.15
949	CA	GLY	A	303	16.162	4.500	1.337	1.00	17.25
950	C	GLY	A	303	15.488	4.587	−0.019	1.00	18.29
951	O	GLY	A	303	15.826	3.816	−0.916	1.00	19.54
952	N	PHE	A	304	14.551	5.511	−0.204	1.00	18.25
953	CA	PHE	A	304	13.872	5.603	−1.499	1.00	18.54
954	CB	PHE	A	304	12.661	6.534	−1.435	1.00	19.40
955	CG	PHE	A	304	11.458	5.915	−0.797	1.00	18.61
956	CD1	PHE	A	304	11.297	5.929	0.581	1.00	18.46
957	CD2	PHE	A	304	10.496	5.294	−1.574	1.00	19.63
958	CE1	PHE	A	304	10.193	5.329	1.167	1.00	21.04
959	CE2	PHE	A	304	9.385	4.690	−0.991	1.00	19.15
960	CZ	PHE	A	304	9.233	4.707	0.373	1.00	18.69
961	C	PHE	A	304	14.799	6.009	−2.631	1.00	18.46
962	O	PHE	A	304	14.502	5.764	−3.795	1.00	17.98
963	N	GLY	A	305	15.905	6.656	−2.288	1.00	18.96
964	CA	GLY	A	305	16.880	7.063	−3.279	1.00	19.43
965	C	GLY	A	305	16.334	7.777	−4.501	1.00	21.11
966	O	GLY	A	305	15.509	8.673	−4.375	1.00	22.17
967	N	PRO	A	306	16.788	7.415	−5.710	1.00	20.61
968	CD	PRO	A	306	17.788	6.375	−6.011	1.00	19.86
969	CA	PRO	A	306	16.313	8.058	−6.938	1.00	21.15
970	CB	PRO	A	306	17.242	7.469	−7.992	1.00	20.67
971	CG	PRO	A	306	17.521	6.088	−7.448	1.00	21.94
972	C	PRO	A	306	14.841	7.801	−7.289	1.00	21.61
973	O	PRO	A	306	14.380	8.213	−8.353	1.00	23.28
974	N	LEU	A	307	14.094	7.179	−6.383	1.00	20.33
975	CA	LEU	A	307	12.704	6.867	−6.635	1.00	18.74
976	CB	LEU	A	307	12.469	5.399	−6.291	1.00	21.17
977	CG	LEU	A	307	11.118	4.743	−6.613	1.00	22.39
978	CD1	LEU	A	307	10.957	4.594	−8.125	1.00	23.14
979	CD2	LEU	A	307	11.022	3.392	−5.937	1.00	20.12
980	C	LEU	A	307	11.742	7.727	−5.842	1.00	18.73
981	O	LEU	A	307	10.545	7.704	−6.099	1.00	18.72
982	N	THR	A	308	12.262	8.554	−4.938	1.00	18.50
983	CA	THR	A	308	11.408	9.364	−4.086	1.00	17.36
984	CB	THR	A	308	12.168	10.000	−2.895	1.00	19.93
985	OG1	THR	A	308	12.308	11.404	−3.075	1.00	22.32
986	CG2	THR	A	308	13.514	9.432	−2.736	1.00	17.49
987	C	THR	A	308	10.517	10.405	−4.740	1.00	17.72
988	O	THR	A	308	9.407	10.655	−4.278	1.00	17.73
989	N	ASP	A	309	10.993	11.056	−5.786	1.00	18.34
990	CA	ASP	A	309	10.167	12.075	−6.434	1.00	18.34
991	CB	ASP	A	309	11.005	12.964	−7.311	1.00	19.68
992	CG	ASP	A	309	12.048	13.663	−6.536	1.00	21.80
993	OD1	ASP	A	309	13.247	13.519	−6.891	1.00	23.93
994	OD2	ASP	A	309	11.655	14.322	−5.541	1.00	22.59
995	C	ASP	A	309	9.028	11.512	−7.223	1.00	17.07
996	O	ASP	A	309	8.056	12.211	−7.439	1.00	16.35
997	N	LEU	A	310	9.221	10.299	−7.745	1.00	19.09
998	CA	LEU	A	310	8.204	9.559	−8.497	1.00	21.41
999	CB	LEU	A	310	8.793	8.312	−9.158	1.00	23.47
1000	CG	LEU	A	310	9.273	8.446	−10.593	1.00	25.11
1001	CD1	LEU	A	310	9.871	7.129	−11.041	1.00	25.39
1002	CD2	LEU	A	310	8.099	8.832	−11.480	1.00	25.87
1003	C	LEU	A	310	7.118	9.110	−7.525	1.00	20.39
1004	O	LEU	A	310	5.930	9.230	−7.812	1.00	21.79
1005	N	VAL	A	311	7.537	8.603	−6.367	1.00	18.78
1006	CA	VAL	A	311	6.592	8.172	−5.342	1.00	16.69
1007	CB	VAL	A	311	7.333	7.597	−4.124	1.00	15.13
1008	CG1	VAL	A	311	6.361	7.169	−3.020	1.00	15.45
1009	CG2	VAL	A	311	8.190	6.454	−4.575	1.00	15.80
1010	C	VAL	A	311	5.763	9.376	−4.927	1.00	14.96
1011	O	VAL	A	311	4.554	9.289	−4.840	1.00	14.98
1012	N	PHE	A	312	6.422	10.515	−4.720	1.00	16.10
1013	CA	PHE	A	312	5.744	11.749	−4.312	1.00	15.43
1014	CB	PHE	A	312	6.735	12.837	−3.932	1.00	16.20
1015	CG	PHE	A	312	7.194	12.758	−2.504	1.00	17.26
1016	CD1	PHE	A	312	8.062	11.749	−2.089	1.00	16.99
1017	CD2	PHE	A	312	6.723	13.668	−1.562	1.00	13.96
1018	CE1	PHE	A	312	8.442	11.652	−0.762	1.00	16.48
1019	CE2	PHE	A	312	7.098	13.575	−0.247	1.00	13.39
1020	CZ	PHE	A	312	7.959	12.566	0.157	1.00	15.65
1021	C	PHE	A	312	4.836	12.257	−5.385	1.00	15.11
1022	O	PHE	A	312	3.819	12.847	−5.092	1.00	16.14
1023	N	ALA	A	313	5.207	12.031	−6.633	1.00	15.74
1024	CA	ALA	A	313	4.384	12.462	−7.745	1.00	16.86
1025	CB	ALA	A	313	5.200	12.487	−9.027	1.00	18.61
1026	C	ALA	A	313	3.174	11.534	−7.873	1.00	17.47
1027	O	ALA	A	313	2.081	11.989	−8.221	1.00	17.51
1028	N	PHE	A	314	3.363	10.243	−7.592	1.00	16.65
1029	CA	PHE	A	314	2.266	9.264	−7.638	1.00	16.43
1030	CB	PHE	A	314	2.783	7.831	−7.446	1.00	16.00
1031	CG	PHE	A	314	1.683	6.812	−7.234	1.00	19.00
1032	CD1	PHE	A	314	1.002	6.270	−8.316	1.00	19.62
1033	CD2	PHE	A	314	1.262	6.460	−5.936	1.00	20.46
1034	CE1	PHE	A	314	−0.090	5.401	−8.111	1.00	20.93
1035	CE2	PHE	A	314	0.167	5.590	−5.724	1.00	21.50
1036	CZ	PHE	A	314	−0.510	5.067	−6.813	1.00	20.23
1037	C	PHE	A	314	1.284	9.602	−6.520	1.00	15.99
1038	O	PHE	A	314	0.063	9.549	−6.707	1.00	15.93
1039	N	ALA	A	315	1.827	9.928	−5.348	1.00	16.04
1040	CA	ALA	A	315	1.013	10.310	−4.198	1.00	16.36
1041	CB	ALA	A	315	1.887	10.566	−2.991	1.00	15.32
1042	C	ALA	A	315	0.211	11.555	−4.554	1.00	17.37
1043	O	ALA	A	315	−0.991	11.588	−4.352	1.00	17.22
1044	N	GLY	A	316	0.869	12.556	−5.135	1.00	17.35
1045	CA	GLY	A	316	0.170	13.772	−5.518	1.00	18.94
1046	C	GLY	A	316	−0.985	13.482	−6.461	1.00	19.73
1047	O	GLY	A	316	−2.080	14.009	−6.288	1.00	20.12
1048	N	GLN	A	317	−0.762	12.589	−7.420	1.00	20.89
1049	CA	GLN	A	317	−1.790	12.235	−8.387	1.00	21.78
1050	CB	GLN	A	317	−1.219	11.444	−9.571	1.00	24.33
1051	CG	GLN	A	317	0.083	11.942	−10.165	1.00	29.59
1052	CD	GLN	A	317	0.028	13.378	−10.618	1.00	31.66
1053	OE1	GLN	A	317	−0.293	13.660	−11.777	1.00	36.70
1054	NE2	GLN	A	317	0.406	14.296	−9.735	1.00	32.00
1055	C	GLN	A	317	−2.898	11.416	−7.753	1.00	22.05
1056	O	GLN	A	317	−3.886	11.132	−8.413	1.00	23.27
1057	N	LEU	A	318	−2.715	10.972	−6.514	1.00	20.74
1058	CA	LEU	A	318	−3.752	10.203	−5.826	1.00	21.03
1059	CB	LEU	A	318	−3.123	9.373	−4.709	1.00	22.39
1060	CG	LEU	A	318	−3.523	7.928	−4.446	1.00	23.30
1061	CD1	LEU	A	318	−3.281	7.089	−5.691	1.00	24.32
1062	CD2	LEU	A	318	−2.729	7.374	−3.269	1.00	23.64
1063	C	LEU	A	318	−4.742	11.190	−5.207	1.00	21.50
1064	O	LEU	A	318	−5.926	10.916	−5.102	1.00	21.19
1065	N	LEU	A	319	−4.248	12.365	−4.830	1.00	22.63
1066	CA	LEU	A	319	−5.070	13.400	−4.204	1.00	23.25
1067	CB	LEU	A	319	−4.273	14.686	−4.051	1.00	23.72
1068	CG	LEU	A	319	−3.003	14.592	−3.232	1.00	25.21
1069	CD1	LEU	A	319	−2.286	15.940	−3.333	1.00	27.97
1070	CD2	LEU	A	319	−3.328	14.206	−1.777	1.00	25.70
1071	C	LEU	A	319	−6.410	13.706	−4.873	1.00	23.85
1072	O	LEU	A	319	−7.439	13.673	−4.205	1.00	25.23
1073	N	PRO	A	320	−6.409	14.089	−6.174	1.00	24.07
1074	CD	PRO	A	320	−5.220	14.333	−7.024	1.00	24.33
1075	CA	PRO	A	320	−7.639	14.399	−6.918	1.00	23.26
1076	CB	PRO	A	320	−7.147	14.461	−8.359	1.00	25.29
1077	CG	PRO	A	320	−5.792	15.070	−8.216	1.00	24.51
1078	C	PRO	A	320	−8.706	13.318	−6.785	1.00	22.41
1079	O	PRO	A	320	−9.890	13.602	−6.957	1.00	22.31
1080	N	LEU	A	321	−8.282	12.074	−6.542	1.00	20.32
1081	CA	LEU	A	321	−9.218	10.976	−6.380	1.00	18.93
1082	CB	LEU	A	321	−8.507	9.622	−6.432	1.00	18.78
1083	CG	LEU	A	321	−8.308	9.035	−7.843	1.00	18.00
1084	CD1	LEU	A	321	−7.322	9.867	−8.584	1.00	20.63
1085	CD2	LEU	A	321	−7.843	7.596	−7.791	1.00	17.88
1086	C	LEU	A	321	−10.043	11.082	−5.108	1.00	19.17
1087	O	LEU	A	321	−11.062	10.410	−4.981	1.00	20.44
1088	N	GLU	A	322	−9.577	11.866	−4.143	1.00	19.27
1089	CA	GLU	A	322	−10.290	12.061	−2.867	1.00	20.00
1090	CB	GLU	A	322	−11.350	13.156	−3.000	1.00	20.61
1091	CG	GLU	A	322	−10.827	14.420	−3.641	1.00	25.44
1092	CD	GLU	A	322	−11.576	15.666	−3.219	1.00	28.32
1093	OE1	GLU	A	322	−12.037	15.749	−2.053	1.00	30.30
1094	OE2	GLU	A	322	−11.670	16.588	−4.051	1.00	30.01
1095	C	GLU	A	322	−10.954	10.800	−2.304	1.00	19.37
1096	O	GLU	A	322	−12.119	10.820	−1.932	1.00	20.57
1097	N	MET	A	323	−10.200	9.713	−2.248	1.00	18.99
1098	CA	MET	A	323	−10.670	8.441	−1.736	1.00	17.81
1099	CB	MET	A	323	−9.713	7.322	−2.174	1.00	19.71
1100	CG	MET	A	323	−9.790	6.904	−3.653	1.00	21.26
1101	SD	MET	A	323	−8.392	5.832	−4.116	1.00	22.21
1102	CE	MET	A	323	−8.757	4.374	−3.384	1.00	22.92
1103	C	MET	A	323	−10.743	8.430	−0.212	1.00	17.71
1104	O	MET	A	323	−9.899	9.034	0.475	1.00	19.02
1105	N	ASP	A	324	−11.721	7.710	0.336	1.00	16.79
1106	CA	ASP	A	324	−11.809	7.612	1.792	1.00	15.53
1107	CB	ASP	A	324	−13.250	7.787	2.304	1.00	15.59
1108	CG	ASP	A	324	−14.227	6.832	1.676	1.00	15.20
1109	OD1	ASP	A	324	−13.848	6.064	0.789	1.00	16.66
1110	OD2	ASP	A	324	−15.385	6.860	2.089	1.00	15.60
1111	C	ASP	A	324	−11.171	6.317	2.248	1.00	14.20
1112	O	ASP	A	324	−10.575	5.616	1.445	1.00	14.53
1113	N	ASP	A	325	−11.242	6.014	3.532	1.00	15.62
1114	CA	ASP	A	325	−10.639	4.791	4.059	1.00	16.98
1115	CB	ASP	A	325	−10.704	4.758	5.597	1.00	22.06
1116	CG	ASP	A	325	−9.869	5.869	6.267	1.00	27.41
1117	OD1	ASP	A	325	−8.947	6.436	5.627	1.00	28.96
1118	OD2	ASP	A	325	−10.141	6.172	7.464	1.00	31.89
1119	C	ASP	A	325	−11.263	3.503	3.494	1.00	16.36
1120	O	ASP	A	325	−10.576	2.507	3.290	1.00	16.22
1121	N	THR	A	326	−12.565	3.495	3.252	1.00	17.30
1122	CA	THR	A	326	−13.161	2.283	2.722	1.00	15.19
1123	CB	THR	A	326	−14.687	2.297	2.832	1.00	16.45
1124	OG1	THR	A	326	−15.235	3.016	1.729	1.00	23.49
1125	CG2	THR	A	326	−15.134	2.966	4.100	1.00	13.11
1126	C	THR	A	326	−12.695	2.044	1.282	1.00	13.91
1127	O	THR	A	326	−12.304	0.945	0.956	1.00	14.30
1128	N	GLU	A	327	−12.669	3.087	0.451	1.00	13.54
1129	CA	GLU	A	327	−12.217	2.993	−0.950	1.00	14.50
1130	CB	GLU	A	327	−12.342	4.337	−1.669	1.00	13.69
1131	CG	GLU	A	327	−13.739	4.596	−2.188	1.00	15.66
1132	CD	GLU	A	327	−14.061	6.070	−2.461	1.00	15.47
1133	OE1	GLU	A	327	−15.220	6.353	−2.821	1.00	15.80
1134	OE2	GLU	A	327	−13.187	6.940	−2.322	1.00	14.96
1135	C	GLU	A	327	−10.779	2.530	−1.005	1.00	13.39
1136	O	GLU	A	327	−10.410	1.699	−1.835	1.00	13.39
1137	N	THR	A	328	−9.962	3.095	−0.132	1.00	12.39
1138	CA	THR	A	328	−8.561	2.694	−0.046	1.00	14.32
1139	CB	THR	A	328	−7.788	3.598	0.931	1.00	12.84
1140	OG1	THR	A	328	−7.866	4.957	0.491	1.00	14.19
1141	CG2	THR	A	328	−6.377	3.177	1.007	1.00	12.73
1142	C	THR	A	328	−8.489	1.229	0.434	1.00	13.38
1143	O	THR	A	328	−7.683	0.436	−0.065	1.00	12.40
1144	N	GLY	A	329	−9.342	0.878	1.398	1.00	14.14
1145	CA	GLY	A	329	−9.367	−0.473	1.917	1.00	10.87
1146	C	GLY	A	329	−9.775	−1.407	0.806	1.00	11.08
1147	O	GLY	A	329	−9.111	−2.414	0.588	1.00	11.93
1148	N	LEU	A	330	−10.815	−1.037	0.061	1.00	11.42
1149	CA	LEU	A	330	−11.325	−1.851	−1.059	1.00	13.84
1150	CB	LEU	A	330	−12.663	−1.303	−1.587	1.00	11.99
1151	CG	LEU	A	330	−13.901	−1.664	−0.741	1.00	14.67
1152	CD1	LEU	A	330	−15.063	−0.697	−0.978	1.00	13.20
1153	CD2	LEU	A	330	−14.309	−3.124	−1.000	1.00	13.43
1154	C	LEU	A	330	−10.314	−1.973	−2.202	1.00	14.49
1155	O	LEU	A	330	−10.076	−3.078	−2.719	1.00	14.89
1156	N	LEU	A	331	−9.674	−0.855	−2.540	1.00	13.76
1157	CA	LEU	A	331	−8.664	−0.830	−3.586	1.00	13.42
1158	CB	LEU	A	331	−8.134	0.600	−3.768	1.00	14.33
1159	CG	LEU	A	331	−7.713	1.059	−5.173	1.00	16.95
1160	CD1	LEU	A	331	−6.203	1.142	−5.329	1.00	19.20
1161	CD2	LEU	A	331	−8.335	0.175	−6.231	1.00	17.35
1162	C	LEU	A	331	−7.531	−1.778	−3.192	1.00	12.94
1163	O	LEU	A	331	−7.024	−2.520	−4.021	1.00	12.82
1164	N	SER	A	332	−7.150	−1.775	−1.919	1.00	12.43
1165	CA	SER	A	332	−6.095	−2.686	−1.448	1.00	12.96
1166	CB	SER	A	332	−5.725	−2.391	0.004	1.00	12.28
1167	OG	SER	A	332	−5.214	−1.089	0.125	1.00	15.83
1168	C	SER	A	332	−6.506	−4.147	−1.548	1.00	12.57
1169	O	SER	A	332	−5.710	−4.987	−1.958	1.00	11.85
1170	N	ALA	A	333	−7.724	−4.461	−1.115	1.00	13.37
1171	CA	ALA	A	333	−8.223	−5.827	−1.186	1.00	12.68
1172	CB	ALA	A	333	−9.597	−5.898	−0.596	1.00	12.86
1173	C	ALA	A	333	−8.236	−6.308	−2.647	1.00	15.04
1174	O	ALA	A	333	−8.082	−7.509	−2.925	1.00	15.25
1175	N	ILE	A	334	−8.434	−5.376	−3.578	1.00	14.01
1176	CA	ILE	A	334	−8.450	−5.708	−4.987	1.00	14.07
1177	CB	ILE	A	334	−9.149	−4.598	−5.764	1.00	13.20
1178	CG2	ILE	A	334	−8.953	−4.760	−7.223	1.00	15.19
1179	CG1	ILE	A	334	−10.636	−4.641	−5.458	1.00	14.68
1180	CD1	ILE	A	334	−11.453	−3.593	−6.150	1.00	13.41
1181	C	ILE	A	334	−7.022	−6.007	−5.520	1.00	15.78
1182	O	ILE	A	334	−6.831	−6.917	−6.337	1.00	14.01
1183	N	CYS	A	335	−6.022	−5.273	−5.032	1.00	16.38
1184	CA	CYS	A	335	−4.635	−5.490	−5.457	1.00	18.88
1185	CB	CYS	A	335	−3.700	−4.394	−4.918	1.00	19.50
1186	SG	CYS	A	335	−4.015	−2.754	−5.628	1.00	25.06
1187	C	CYS	A	335	−4.110	−6.843	−5.008	1.00	18.00
1188	O	CYS	A	335	−3.390	−7.533	−5.741	1.00	18.49
1189	N	LEU	A	336	−4.489	−7.212	−3.801	1.00	18.10
1190	CA	LEU	A	336	−4.064	−8.447	−3.187	1.00	19.39
1191	CB	LEU	A	336	−4.320	−8.350	−1.698	1.00	21.55
1192	CG	LEU	A	336	−3.820	−9.468	−0.803	1.00	26.30
1193	CD1	LEU	A	336	−2.322	−9.368	−0.642	1.00	27.11
1194	CD2	LEU	A	336	−4.488	−9.295	0.550	1.00	25.31
1195	C	LEU	A	336	−4.748	−9.690	−3.750	1.00	19.53
1196	O	LEU	A	336	−4.086	−10.688	−4.073	1.00	18.48
1197	N	ILE	A	337	−6.073	−9.659	−3.834	1.00	19.32
1198	CA	ILE	A	337	−6.807	−10.811	−4.359	1.00	19.91
1199	CB	ILE	A	337	−8.156	−10.997	−3.605	1.00	19.73
1200	CG2	ILE	A	337	−8.926	−12.207	−4.130	1.00	21.03
1201	CG1	ILE	A	337	−7.854	−11.232	−2.130	1.00	18.54
1202	CD1	ILE	A	337	−9.052	−11.440	−1.328	1.00	21.98
1203	C	ILE	A	337	−6.935	−10.668	−5.888	1.00	19.55
1204	O	ILE	A	337	−7.909	−10.128	−6.431	1.00	19.70
1205	N	CYS	A	338	−5.867	−11.090	−6.551	1.00	19.24
1206	CA	CYS	A	338	−5.731	−11.026	−7.988	1.00	19.05
1207	CB	CYS	A	338	−4.568	−10.136	−8.322	1.00	18.09
1208	SG	CYS	A	338	−4.456	−9.913	−10.046	1.00	24.64
1209	C	CYS	A	338	−5.416	−12.420	−8.453	1.00	19.13
1210	O	CYS	A	338	−4.460	−13.010	−7.987	1.00	18.29
1211	N	GLY	A	339	−6.213	−12.951	−9.367	1.00	21.16
1212	CA	GLY	A	339	−5.994	−14.305	−9.827	1.00	21.28
1213	C	GLY	A	339	−4.999	−14.426	−10.946	1.00	22.01
1214	O	GLY	A	339	−4.726	−15.516	−11.433	1.00	23.62
1215	N	ASP	A	340	−4.419	−13.308	−11.332	1.00	22.60
1216	CA	ASP	A	340	−3.465	−13.326	−12.416	1.00	24.56
1217	CB	ASP	A	340	−3.737	−12.157	−13.343	1.00	26.57
1218	CG	ASP	A	340	−5.116	−12.277	−13.985	1.00	31.47
1219	OD1	ASP	A	340	−5.312	−13.227	−14.795	1.00	32.06
1220	OD2	ASP	A	340	−6.030	−11.485	−13.630	1.00	32.04
1221	C	ASP	A	340	−2.010	−13.444	−12.031	1.00	23.99
1222	O	ASP	A	340	−1.130	−13.301	−12.865	1.00	23.98
1223	N	ARG	A	341	−1.765	−13.794	−10.777	1.00	23.91
1224	CA	ARG	A	341	−0.406	−13.961	−10.310	1.00	24.57
1225	CB	ARG	A	341	−0.307	−13.885	−8.787	1.00	22.12
1226	CG	ARG	A	341	−0.986	−12.700	−8.157	1.00	23.69
1227	CD	ARG	A	341	−0.405	−11.410	−8.644	1.00	23.69
1228	NE	ARG	A	341	−0.852	−10.289	−7.830	1.00	23.18
1229	CZ	ARG	A	341	−0.271	−9.091	−7.827	1.00	24.92
1230	NH1	ARG	A	341	0.795	−8.839	−8.597	1.00	24.43
1231	NH2	ARG	A	341	−0.770	−8.134	−7.067	1.00	23.98
1232	C	ARG	A	341	0.016	−15.338	−10.754	1.00	25.19
1233	O	ARG	A	341	−0.797	−16.257	−10.871	1.00	23.68
1234	N	MET	A	342	1.303	−15.458	−11.026	1.00	28.20
1235	CA	MET	A	342	1.897	−16.712	−11.441	1.00	29.89
1236	CB	MET	A	342	3.298	−16.434	−11.964	1.00	31.90
1237	CG	MET	A	342	3.356	−15.306	−12.979	1.00	34.96
1238	SD	MET	A	342	5.057	−14.882	−13.280	1.00	38.16
1239	CE	MET	A	342	5.837	−16.599	−13.163	1.00	35.02
1240	C	MET	A	342	1.998	−17.549	−10.189	1.00	29.29
1241	O	MET	A	342	1.819	−17.034	−9.093	1.00	31.37
1242	N	ASP	A	343	2.292	−18.830	−10.347	1.00	30.14
1243	CA	ASP	A	343	2.461	−19.716	−9.202	1.00	29.67
1244	CB	ASP	A	343	3.553	−19.176	−8.253	1.00	31.20
1245	CG	ASP	A	343	4.964	−19.442	−8.758	1.00	32.74
1246	OD1	ASP	A	343	5.760	−20.023	−7.982	1.00	36.46
1247	OD2	ASP	A	343	5.281	−19.083	−9.917	1.00	33.75
1248	C	ASP	A	343	1.202	−19.984	−8.399	1.00	28.09
1249	O	ASP	A	343	1.280	−20.610	−7.344	1.00	28.84
1250	N	LEU	A	344	0.059	−19.471	−8.843	1.00	25.57
1251	CA	LEU	A	344	−1.181	−19.714	−8.136	1.00	22.21
1252	CB	LEU	A	344	−2.242	−18.714	−8.541	1.00	22.99
1253	CG	LEU	A	344	−2.162	−17.320	−7.943	1.00	21.45
1254	CD1	LEU	A	344	−3.464	−16.616	−8.305	1.00	19.98
1255	CD2	LEU	A	344	−1.996	−17.397	−6.426	1.00	20.99
1256	C	LEU	A	344	−1.683	−21.094	−8.458	1.00	22.04
1257	O	LEU	A	344	−1.693	−21.490	−9.613	1.00	22.32
1258	N	GLU	A	345	−2.113	−21.811	−7.430	1.00	21.27
1259	CA	GLU	A	345	−2.637	−23.162	−7.570	1.00	22.42
1260	CB	GLU	A	345	−2.517	−23.929	−6.248	1.00	20.74
1261	CG	GLU	A	345	−1.130	−24.139	−5.727	1.00	21.34
1262	CD	GLU	A	345	−1.110	−24.823	−4.356	1.00	22.75
1263	OE1	GLU	A	345	−0.090	−25.459	−4.020	1.00	27.68
1264	OE2	GLU	A	345	−2.083	−24.728	−3.592	1.00	22.70
1265	C	GLU	A	345	−4.112	−23.159	−7.991	1.00	23.85
1266	O	GLU	A	345	−4.566	−24.074	−8.688	1.00	25.61
1267	N	GLU	A	346	−4.872	−22.172	−7.506	1.00	23.67
1268	CA	GLU	A	346	−6.297	−22.051	−7.824	1.00	21.44
1269	CB	GLU	A	346	−7.115	−22.369	−6.586	1.00	23.93
1270	CG	GLU	A	346	−6.731	−23.661	−5.904	1.00	26.46
1271	CD	GLU	A	346	−7.759	−24.079	−4.886	1.00	27.98
1272	OE1	GLU	A	346	−8.422	−25.102	−5.131	1.00	30.36
1273	OE2	GLU	A	346	−7.931	−23.378	−3.859	1.00	29.40
1274	C	GLU	A	346	−6.621	−20.632	−8.245	1.00	20.32
1275	O	GLU	A	346	−7.343	−19.940	−7.535	1.00	18.83
1276	N	PRO	A	347	−6.183	−20.210	−9.447	1.00	19.81
1277	CD	PRO	A	347	−5.623	−20.981	−10.556	1.00	19.32
1278	CA	PRO	A	347	−6.444	−18.854	−9.912	1.00	21.05
1279	CB	PRO	A	347	−5.813	−18.831	−11.300	1.00	20.06
1280	CG	PRO	A	347	−4.854	−19.906	−11.273	1.00	18.82
1281	C	PRO	A	347	−7.907	−18.599	−10.004	1.00	22.73
1282	O	PRO	A	347	−8.349	−17.509	−9.693	1.00	24.63
1283	N	GLU	A	348	−8.658	−19.634	−10.366	1.00	25.04
1284	CA	GLU	A	348	−10.105	−19.536	−10.507	1.00	27.41
1285	CB	GLU	A	348	−10.727	−20.861	−10.990	1.00	28.57
1286	CG	GLU	A	348	−9.826	−21.704	−11.901	1.00	33.98
1287	CD	GLU	A	348	−9.147	−22.891	−11.181	1.00	34.30
1288	OE1	GLU	A	348	−8.753	−22.756	−10.002	1.00	34.12
1289	OE2	GLU	A	348	−9.025	−23.974	−11.804	1.00	36.51
1290	C	GLU	A	348	−10.762	−19.126	−9.197	1.00	26.86
1291	O	GLU	A	348	−11.687	−18.318	−9.202	1.00	28.63
1292	N	LYS	A	349	−10.307	−19.676	−8.076	1.00	25.97
1293	CA	LYS	A	349	−10.911	−19.329	−6.776	1.00	25.62
1294	CB	LYS	A	349	−10.398	−20.237	−5.647	1.00	26.61
1295	CG	LYS	A	349	−11.091	−20.003	−4.291	1.00	28.17
1296	CD	LYS	A	349	−10.565	−20.962	−3.209	1.00	29.75
1297	CE	LYS	A	349	−11.466	−21.020	−1.958	1.00	30.29
1298	NZ	LYS	A	349	−11.193	−20.025	−0.857	1.00	31.95
1299	C	LYS	A	349	−10.617	−17.889	−6.413	1.00	24.22
1300	O	LYS	A	349	−11.445	−17.199	−5.815	1.00	24.94
1301	N	VAL	A	350	−9.428	−17.436	−6.790	1.00	23.42
1302	CA	VAL	A	350	−9.020	−16.079	−6.489	1.00	19.37
1303	CB	VAL	A	350	−7.517	−15.873	−6.708	1.00	17.26
1304	CG1	VAL	A	350	−7.127	−14.526	−6.154	1.00	17.10
1305	CG2	VAL	A	350	−6.715	−16.984	−5.997	1.00	14.99
1306	C	VAL	A	350	−9.862	−15.121	−7.312	1.00	17.30
1307	O	VAL	A	350	−10.335	−14.126	−6.790	1.00	16.58
1308	N	ASP	A	351	−10.117	−15.452	−8.570	1.00	18.10
1309	CA	ASP	A	351	−10.960	−14.595	−9.410	1.00	20.96
1310	CB	ASP	A	351	−11.014	−15.106	−10.855	1.00	25.84
1311	CG	ASP	A	351	−9.711	−14.860	−11.615	1.00	30.06
1312	OD1	ASP	A	351	−8.712	−14.416	−10.998	1.00	32.95
1313	OD2	ASP	A	351	−9.688	−15.119	−12.833	1.00	33.18
1314	C	ASP	A	351	−12.380	−14.457	−8.883	1.00	19.72
1315	O	ASP	A	351	−12.999	−13.402	−9.037	1.00	19.10
1316	N	LYS	A	352	−12.894	−15.536	−8.297	1.00	20.03
1317	CA	LYS	A	352	−14.240	−15.558	−7.741	1.00	19.45
1318	CB	LYS	A	352	−14.695	−16.982	−7.410	1.00	21.58
1319	CG	LYS	A	352	−15.209	−17.769	−8.631	1.00	26.04
1320	CD	LYS	A	352	−16.394	−17.057	−9.312	1.00	29.59
1321	CE	LYS	A	352	−16.941	−17.844	−10.526	1.00	31.85
1322	NZ	LYS	A	352	−17.951	−17.067	−11.361	1.00	31.59
1323	C	LYS	A	352	−14.276	−14.715	−6.501	1.00	18.59
1324	O	LYS	A	352	−15.303	−14.120	−6.185	1.00	17.49
1325	N	LEU	A	353	−13.157	−14.671	−5.783	1.00	17.89
1326	CA	LEU	A	353	−13.071	−13.854	−4.575	1.00	18.26
1327	CB	LEU	A	353	−11.879	−14.285	−3.732	1.00	19.79
1328	CG	LEU	A	353	−12.035	−15.625	−3.050	1.00	22.37
1329	CD1	LEU	A	353	−10.676	−16.118	−2.633	1.00	22.45
1330	CD2	LEU	A	353	−12.959	−15.441	−1.860	1.00	21.09
1331	C	LEU	A	353	−12.931	−12.372	−4.914	1.00	16.10
1332	O	LEU	A	353	−13.499	−11.511	−4.264	1.00	17.51
1333	N	GLN	A	354	−12.211	−12.073	−5.972	1.00	15.53
1334	CA	GLN	A	354	−12.028	−10.686	−6.324	1.00	16.30
1335	CB	GLN	A	354	−11.011	−10.546	−7.423	1.00	18.24
1336	CG	GLN	A	354	−10.490	−9.134	−7.548	1.00	20.89
1337	CD	GLN	A	354	−9.690	−8.981	−8.788	1.00	20.24
1338	OE1	GLN	A	354	−10.152	−9.344	−9.864	1.00	20.86
1339	NE2	GLN	A	354	−8.453	−8.520	−8.650	1.00	20.85
1340	C	GLN	A	354	−13.294	−10.042	−6.777	1.00	16.79
1341	O	GLN	A	354	−13.531	−8.886	−6.460	1.00	15.54
1342	N	GLU	A	355	−14.091	−10.786	−7.544	1.00	16.68
1343	CA	GLU	A	355	−15.356	−10.278	−8.085	1.00	17.94
1344	CB	GLU	A	355	−16.217	−11.428	−8.652	1.00	20.78
1345	CG	GLU	A	355	−15.669	−12.105	−9.922	1.00	24.97
1346	CD	GLU	A	355	−16.624	−13.171	−10.526	1.00	26.48
1347	OE1	GLU	A	355	−17.825	−13.230	−10.175	1.00	26.49
1348	OE2	GLU	A	355	−16.162	−13.963	−11.372	1.00	29.34
1349	C	GLU	A	355	−16.207	−9.377	−7.153	1.00	15.27
1350	O	GLU	A	355	−16.493	−8.235	−7.498	1.00	14.44
1351	N	PRO	A	356	−16.628	−9.887	−5.979	1.00	13.16
1352	CD	PRO	A	356	−16.451	−11.225	−5.408	1.00	11.51
1353	CA	PRO	A	356	−17.431	−9.050	−5.089	1.00	12.93
1354	CB	PRO	A	356	−17.646	−9.951	−3.877	1.00	13.16
1355	CG	PRO	A	356	−17.557	−11.299	−4.424	1.00	14.47
1356	C	PRO	A	356	−16.729	−7.761	−4.691	1.00	13.27
1357	O	PRO	A	356	−17.382	−6.761	−4.405	1.00	12.63
1358	N	LEU	A	357	−15.400	−7.795	−4.637	1.00	14.63
1359	CA	LEU	A	357	−14.618	−6.619	−4.254	1.00	13.35
1360	CB	LEU	A	357	−13.155	−6.968	−4.004	1.00	12.64
1361	CG	LEU	A	357	−12.840	−7.943	−2.867	1.00	12.80
1362	CD1	LEU	A	357	−11.396	−8.349	−2.938	1.00	11.06
1363	CD2	LEU	A	357	−13.117	−7.318	−1.528	1.00	13.33
1364	C	LEU	A	357	−14.730	−5.573	−5.344	1.00	14.30
1365	O	LEU	A	357	−14.841	−4.389	−5.043	1.00	16.28
1366	N	LEU	A	358	−14.756	−5.996	−6.607	1.00	13.24
1367	CA	LEU	A	358	−14.886	−5.043	−7.693	1.00	13.47
1368	CB	LEU	A	358	−14.718	−5.699	−9.054	1.00	15.18
1369	CG	LEU	A	358	−13.305	−6.100	−9.463	1.00	18.18
1370	CD1	LEU	A	358	−13.306	−6.601	−10.894	1.00	17.71
1371	CD2	LEU	A	358	−12.410	−4.898	−9.333	1.00	17.17
1372	C	LEU	A	358	−16.258	−4.428	−7.605	1.00	13.18
1373	O	LEU	A	358	−16.415	−3.231	−7.785	1.00	14.40
1374	N	GLU	A	359	−17.260	−5.250	−7.331	1.00	12.57
1375	CA	GLU	A	359	−18.624	−4.767	−7.200	1.00	13.28
1376	CB	GLU	A	359	−19.573	−5.928	−6.986	1.00	15.79
1377	CG	GLU	A	359	−20.365	−6.303	−8.169	1.00	21.23
1378	CD	GLU	A	359	−21.319	−7.407	−7.837	1.00	25.40
1379	OE1	GLU	A	359	−22.426	−7.086	−7.341	1.00	26.24
1380	OE2	GLU	A	359	−20.947	−8.588	−8.038	1.00	27.57
1381	C	GLU	A	359	−18.807	−3.824	−6.030	1.00	11.49
1382	O	GLU	A	359	−19.479	−2.834	−6.159	1.00	12.35
1383	N	ALA	A	360	−18.303	−4.179	−4.862	1.00	11.57
1384	CA	ALA	A	360	−18.456	−3.323	−3.690	1.00	13.32
1385	CB	ALA	A	360	−17.789	−3.950	−2.471	1.00	9.99
1386	C	ALA	A	360	−17.891	−1.935	−3.935	1.00	13.88
1387	O	ALA	A	360	−18.503	−0.933	−3.544	1.00	15.74
1388	N	LEU	A	361	−16.727	−1.868	−4.586	1.00	15.15
1389	CA	LEU	A	361	−16.090	−0.577	−4.872	1.00	13.83
1390	CB	LEU	A	361	−14.648	−0.781	−5.362	1.00	14.59
1391	CG	LEU	A	361	−13.865	0.514	−5.634	1.00	14.93
1392	CD1	LEU	A	361	−13.964	1.457	−4.437	1.00	12.88
1393	CD2	LEU	A	361	−12.413	0.212	−5.963	1.00	14.12
1394	C	LEU	A	361	−16.872	0.311	−5.852	1.00	14.73
1395	O	LEU	A	361	−16.937	1.527	−5.666	1.00	16.81
1396	N	ARG	A	362	−17.418	−0.273	−6.920	1.00	14.29
1397	CA	ARG	A	362	−18.207	0.495	−7.883	1.00	13.27
1398	CB	ARG	A	362	−18.558	−0.331	−9.139	1.00	10.91
1399	CG	ARG	A	362	−19.257	0.531	−10.203	1.00	13.29
1400	CD	ARG	A	362	−19.613	−0.151	−11.539	1.00	14.88
1401	NE	ARG	A	362	−21.047	−0.012	−11.847	1.00	17.88
1402	CZ	ARG	A	362	−21.556	0.753	−12.804	1.00	15.28
1403	NH1	ARG	A	362	−20.792	1.473	−13.592	1.00	15.01
1404	NH2	ARG	A	362	−22.856	0.812	−12.955	1.00	19.91
1405	C	ARG	A	362	−19.482	1.033	−7.197	1.00	14.05
1406	O	ARG	A	362	−19.781	2.220	−7.302	1.00	13.80
1407	N	LEU	A	363	−20.189	0.173	−6.463	1.00	11.82
1408	CA	LEU	A	363	−21.393	0.572	−5.748	1.00	12.71
1409	CB	LEU	A	363	−21.974	−0.603	−4.946	1.00	13.78
1410	CG	LEU	A	363	−23.326	−0.466	−4.220	1.00	14.50
1411	CD1	LEU	A	363	−24.463	−0.468	−5.219	1.00	17.78
1412	CD2	LEU	A	363	−23.551	−1.630	−3.300	1.00	13.85
1413	C	LEU	A	363	−21.051	1.663	−4.763	1.00	12.77
1414	O	LEU	A	363	−21.666	2.723	−4.752	1.00	13.96
1415	N	TYR	A	364	−20.076	1.394	−3.906	1.00	13.26
1416	CA	TYR	A	364	−19.711	2.364	−2.910	1.00	11.50
1417	CB	TYR	A	364	−18.690	1.782	−1.951	1.00	11.85
1418	CG	TYR	A	364	−18.336	2.740	−0.849	1.00	12.80
1419	CD1	TYR	A	364	−17.235	3.582	−0.955	1.00	12.10
1420	CE1	TYR	A	364	−16.937	4.501	0.042	1.00	15.58
1421	CD2	TYR	A	364	−19.130	2.840	0.292	1.00	13.75
1422	CE2	TYR	A	364	−18.837	3.751	1.293	1.00	14.21
1423	CZ	TYR	A	364	−17.742	4.580	1.164	1.00	15.51
1424	OH	TYR	A	364	−17.452	5.489	2.159	1.00	16.22
1425	C	TYR	A	364	−19.207	3.662	−3.520	1.00	13.59
1426	O	TYR	A	364	−19.641	4.742	−3.127	1.00	13.14
1427	N	ALA	A	365	−18.344	3.573	−4.523	1.00	13.63
1428	CA	ALA	A	365	−17.776	4.777	−5.129	1.00	14.25
1429	CB	ALA	A	365	−16.678	4.386	−6.123	1.00	13.92
1430	C	ALA	A	365	−18.819	5.670	−5.804	1.00	15.83
1431	O	ALA	A	365	−18.754	6.906	−5.718	1.00	15.28
1432	N	ARG	A	366	−19.766	5.030	−6.488	1.00	15.42
1433	CA	ARG	A	366	−20.821	5.725	−7.197	1.00	16.12
1434	CB	ARG	A	366	−21.476	4.802	−8.218	1.00	14.24
1435	CG	ARG	A	366	−20.693	4.672	−9.492	1.00	15.76
1436	CD	ARG	A	366	−21.317	3.702	−10.442	1.00	18.74
1437	NE	ARG	A	366	−22.579	4.166	−11.029	1.00	21.19
1438	CZ	ARG	A	366	−22.690	4.743	−12.223	1.00	21.09
1439	NH1	ARG	A	366	−21.619	4.960	−12.975	1.00	22.65
1440	NH2	ARG	A	366	−23.889	5.049	−12.691	1.00	20.53
1441	C	ARG	A	366	−21.878	6.287	−6.264	1.00	17.46
1442	O	ARG	A	366	−22.499	7.301	−6.569	1.00	18.75
1443	N	ARG	A	367	−22.127	5.598	−5.161	1.00	17.91
1444	CA	ARG	A	367	−23.121	6.042	−4.201	1.00	17.71
1445	CB	ARG	A	367	−23.335	4.950	−3.158	1.00	17.43
1446	CG	ARG	A	367	−24.125	5.398	−1.959	1.00	18.44
1447	CD	ARG	A	367	−24.749	4.220	−1.291	1.00	16.15
1448	NE	ARG	A	367	−23.772	3.378	−0.638	1.00	19.45
1449	CZ	ARG	A	367	−23.881	2.055	−0.557	1.00	21.49
1450	NH1	ARG	A	367	−24.930	1.430	−1.101	1.00	21.68
1451	NH2	ARG	A	367	−22.951	1.354	0.081	1.00	19.07
1452	C	ARG	A	367	−22.619	7.311	−3.534	1.00	18.59
1453	O	ARG	A	367	−23.312	8.329	−3.467	1.00	20.74
1454	N	ARG	A	368	−21.363	7.268	−3.119	1.00	18.65
1455	CA	ARG	A	368	−20.736	8.373	−2.432	1.00	17.71
1456	CB	ARG	A	368	−19.380	7.901	−1.930	1.00	18.88
1457	CG	ARG	A	368	−18.756	8.689	−0.815	1.00	20.07
1458	CD	ARG	A	368	−17.317	8.249	−0.655	1.00	22.34
1459	NE	ARG	A	368	−16.541	9.337	−0.093	1.00	25.45
1460	CZ	ARG	A	368	−15.396	9.791	−0.580	1.00	24.10
1461	NH1	ARG	A	368	−14.838	9.248	−1.650	1.00	20.76
1462	NH2	ARG	A	368	−14.869	10.874	−0.037	1.00	27.70
1463	C	ARG	A	368	−20.585	9.607	−3.326	1.00	19.09
1464	O	ARG	A	368	−20.765	10.740	−2.856	1.00	21.65
1465	N	ARG	A	369	−20.248	9.399	−4.605	1.00	18.12
1466	CA	ARG	A	369	−20.035	10.499	−5.557	1.00	17.85
1467	CB	ARG	A	369	−18.552	10.745	−5.768	1.00	15.91
1468	CG	ARG	A	369	−17.929	11.408	−4.596	1.00	20.93
1469	CD	ARG	A	369	−16.478	11.608	−4.843	1.00	25.15
1470	NE	ARG	A	369	−15.753	10.347	−4.897	1.00	27.05
1471	CZ	ARG	A	369	−14.428	10.267	−4.886	1.00	27.25
1472	NH1	ARG	A	369	−13.714	11.386	−4.831	1.00	24.07
1473	NH2	ARG	A	369	−13.822	9.078	−4.884	1.00	26.35
1474	C	ARG	A	369	−20.666	10.237	−6.893	1.00	17.61
1475	O	ARG	A	369	−19.982	9.958	−7.876	1.00	18.67
1476	N	PRO	A	370	−21.982	10.373	−6.967	1.00	19.44
1477	CD	PRO	A	370	−22.940	10.698	−5.900	1.00	18.51
1478	CA	PRO	A	370	−22.663	10.127	−8.236	1.00	21.92
1479	CB	PRO	A	370	−24.137	10.116	−7.832	1.00	21.07
1480	CG	PRO	A	370	−24.175	11.062	−6.690	1.00	20.65
1481	C	PRO	A	370	−22.365	11.231	−9.229	1.00	23.55
1482	O	PRO	A	370	−22.608	11.074	−10.416	1.00	26.73
1483	N	SER	A	371	−21.823	12.336	−8.727	1.00	25.11
1484	CA	SER	A	371	−21.484	13.520	−9.528	1.00	25.30
1485	CB	SER	A	371	−21.121	14.685	−8.578	1.00	26.75
1486	OG	SER	A	371	−20.649	15.845	−9.261	1.00	30.80
1487	C	SER	A	371	−20.329	13.265	−10.472	1.00	23.45
1488	O	SER	A	371	−20.108	14.028	−11.403	1.00	23.59
1489	N	GLN	A	372	−19.569	12.214	−10.187	1.00	22.79
1490	CA	GLN	A	372	−18.393	11.869	−10.970	1.00	22.67
1491	CB	GLN	A	372	−17.132	12.276	−10.209	1.00	24.31
1492	CG	GLN	A	372	−17.377	12.709	−8.784	1.00	26.56
1493	CD	GLN	A	372	−16.694	14.015	−8.465	1.00	28.02
1494	OE1	GLN	A	372	−16.199	14.705	−9.358	1.00	28.95
1495	NE2	GLN	A	372	−16.660	14.365	−7.189	1.00	26.49
1496	C	GLN	A	372	−18.335	10.395	−11.235	1.00	21.84
1497	O	GLN	A	372	−17.688	9.657	−10.501	1.00	22.77
1498	N	PRO	A	373	−18.983	9.942	−12.308	1.00	20.20
1499	CD	PRO	A	373	−19.885	10.662	−13.221	1.00	20.33
1500	CA	PRO	A	373	−18.961	8.514	−12.599	1.00	19.96
1501	CB	PRO	A	373	−20.107	8.353	−13.598	1.00	19.66
1502	CG	PRO	A	373	−20.089	9.650	−14.330	1.00	19.46
1503	C	PRO	A	373	−17.629	7.918	−13.078	1.00	20.26
1504	O	PRO	A	373	−17.522	6.697	−13.212	1.00	21.36
1505	N	TYR	A	374	−16.603	8.740	−13.299	1.00	18.89
1506	CA	TYR	A	374	−15.318	8.179	−13.724	1.00	17.90
1507	CB	TYR	A	374	−14.520	9.128	−14.608	1.00	18.18
1508	CG	TYR	A	374	−14.912	9.124	−16.066	1.00	19.54
1509	CD1	TYR	A	374	−14.079	9.709	−17.034	1.00	20.63
1510	CE1	TYR	A	374	−14.450	9.769	−18.378	1.00	18.60
1511	CD2	TYR	A	374	−16.131	8.588	−16.485	1.00	19.14
1512	CE2	TYR	A	374	−16.515	8.639	−17.821	1.00	20.11
1513	CZ	TYR	A	374	−15.676	9.230	−18.765	1.00	19.94
1514	OH	TYR	A	374	−16.071	9.277	−20.095	1.00	20.85
1515	C	TYR	A	374	−14.435	7.763	−12.566	1.00	17.56
1516	O	TYR	A	374	−13.324	7.315	−12.797	1.00	19.32
1517	N	MET	A	375	−14.905	7.884	−11.331	1.00	16.69
1518	CA	MET	A	375	−14.079	7.510	−10.191	1.00	15.81
1519	CB	MET	A	375	−14.723	7.952	−8.875	1.00	18.75
1520	CG	MET	A	375	−13.764	8.577	−7.863	1.00	20.46
1521	SD	MET	A	375	−12.641	9.746	−8.620	1.00	23.72
1522	CE	MET	A	375	−13.665	11.177	−8.979	1.00	19.74
1523	C	MET	A	375	−13.742	6.023	−10.168	1.00	16.19
1524	O	MET	A	375	−12.567	5.661	−10.044	1.00	15.08
1525	N	PHE	A	376	−14.737	5.153	−10.350	1.00	14.22
1526	CA	PHE	A	376	−14.464	3.721	−10.328	1.00	13.87
1527	CB	PHE	A	376	−15.750	2.908	−10.462	1.00	11.39
1528	CG	PHE	A	376	−15.526	1.418	−10.474	1.00	12.73
1529	CD1	PHE	A	376	−15.875	0.660	−11.580	1.00	14.54
1530	CD2	PHE	A	376	−14.988	0.764	−9.373	1.00	11.18
1531	CE1	PHE	A	376	−15.692	−0.753	−11.587	1.00	13.62
1532	CE2	PHE	A	376	−14.803	−0.632	−9.368	1.00	12.48
1533	CZ	PHE	A	376	−15.159	−1.390	−10.476	1.00	13.31
1534	C	PHE	A	376	−13.408	3.307	−11.387	1.00	13.55
1535	O	PHE	A	376	−12.387	2.714	−11.036	1.00	13.73
1536	N	PRO	A	377	−13.626	3.622	−12.686	1.00	13.63
1537	CD	PRO	A	377	−14.737	4.288	−13.395	1.00	13.32
1538	CA	PRO	A	377	−12.578	3.197	−13.623	1.00	13.92
1539	CB	PRO	A	377	−13.147	3.583	−14.986	1.00	12.78
1540	CG	PRO	A	377	−14.104	4.694	−14.685	1.00	13.40
1541	C	PRO	A	377	−11.239	3.884	−13.338	1.00	14.19
1542	O	PRO	A	377	−10.191	3.314	−13.605	1.00	13.68
1543	N	ARG	A	378	−11.283	5.087	−12.768	1.00	15.27
1544	CA	ARG	A	378	−10.064	5.819	−12.434	1.00	16.15
1545	CB	ARG	A	378	−10.359	7.257	−12.037	1.00	16.03
1546	CG	ARG	A	378	−10.320	8.219	−13.191	1.00	18.28
1547	CD	ARG	A	378	−10.250	9.656	−12.710	1.00	21.80
1548	NE	ARG	A	378	−11.568	10.272	−12.736	1.00	28.10
1549	CZ	ARG	A	378	−11.832	11.528	−12.366	1.00	32.50
1550	NH1	ARG	A	378	−10.851	12.336	−11.937	1.00	33.14
1551	NH2	ARG	A	378	−13.101	11.957	−12.359	1.00	33.17
1552	C	ARG	A	378	−9.305	5.127	−11.320	1.00	15.75
1553	O	ARG	A	378	−8.075	5.051	−11.353	1.00	17.14
1554	N	MET	A	379	−10.017	4.611	−10.333	1.00	14.20
1555	CA	MET	A	379	−9.327	3.918	−9.256	1.00	13.79
1556	CB	MET	A	379	−10.266	3.624	−8.110	1.00	13.15
1557	CG	MET	A	379	−10.710	4.856	−7.389	1.00	17.50
1558	SD	MET	A	379	−11.892	4.387	−6.123	1.00	24.25
1559	CE	MET	A	379	−13.367	4.407	−7.010	1.00	18.04
1560	C	MET	A	379	−8.745	2.629	−9.796	1.00	13.02
1561	O	MET	A	379	−7.642	2.238	−9.443	1.00	12.63
1562	N	LEU	A	380	−9.476	1.975	−10.676	1.00	13.77
1563	CA	LEU	A	380	−8.993	0.736	−11.233	1.00	15.71
1564	CB	LEU	A	380	−10.070	0.072	−12.099	1.00	17.34
1565	CG	LEU	A	380	−11.231	−0.615	−11.377	1.00	15.40
1566	CD1	LEU	A	380	−11.922	−1.563	−12.337	1.00	13.31
1567	CD2	LEU	A	380	−10.721	−1.378	−10.168	1.00	15.23
1568	C	LEU	A	380	−7.709	0.944	−12.027	1.00	18.33
1569	O	LEU	A	380	−6.749	0.196	−11.859	1.00	19.10
1570	N	MET	A	381	−7.667	1.997	−12.843	1.00	19.87
1571	CA	MET	A	381	−6.487	2.304	−13.644	1.00	19.87
1572	CB	MET	A	381	−6.766	3.474	−14.588	1.00	20.21
1573	CG	MET	A	381	−7.115	3.027	−15.985	1.00	21.49
1574	SD	MET__	A	381	−7.724	4.398	−16.915	1.00	26.56
1575	CE	MET	A	381	−8.374	3.539	−18.385	1.00	23.61
1576	C	MET	A	381	−5.285	2.598	−12.767	1.00	18.73
1577	O	MET	A	381	−4.169	2.315	−13.160	1.00	19.04
1578	N	LYS	A	382	−5.525	3.122	−11.570	1.00	18.70
1579	CA	LYS	A	382	−4.477	3.431	−10.596	1.00	18.90
1580	CB	LYS	A	382	−5.077	4.177	−9.415	1.00	17.94
1581	CG	LYS	A	382	−5.189	5.654	−9.668	1.00	22.52
1582	CD	LYS	A	382	−3.796	6.299	−9.682	1.00	21.59
1583	CE	LYS	A	382	−3.825	7.655	−10.324	1.00	20.23
1584	NZ	LYS	A	382	−3.970	7.469	−11.795	1.00	25.12
1585	C	LYS	A	382	−3.748	2.201	−10.091	1.00	19.60
1586	O	LYS	A	382	−2.681	2.312	−9.491	1.00	20.41
1587	N	ILE	A	383	−4.352	1.031	−10.294	1.00	22.00
1588	CA	ILE	A	383	−3.773	−0.250	−9.882	1.00	21.94
1589	CB	ILE	A	383	−4.784	−1.419	−10.084	1.00	23.29
1590	CG2	ILE	A	383	−4.073	−2.772	−10.000	1.00	23.62
1591	CG1	ILE	A	383	−5.917	−1.351	−9.048	1.00	23.98
1592	CD1	ILE	A	383	−6.944	−2.494	−9.167	1.00	22.99
1593	C	ILE	A	383	−2.576	−0.487	−10.790	1.00	22.86
1594	O	ILE	A	383	−1.527	−0.967	−10.362	1.00	23.21
1595	N	THR	A	384	−2.752	−0.141	−12.056	1.00	22.20
1596	CA	THR	A	384	−1.711	−0.280	−13.045	1.00	22.77
1597	CB	THR	A	384	−2.285	−0.035	−14.462	1.00	25.21
1598	OG1	THR	A	384	−3.222	−1.089	−14.759	1.00	29.09
1599	CG2	THR	A	384	−1.189	−0.031	−15.517	1.00	27.05
1600	C	THR	A	384	−0.548	0.639	−12.712	1.00	20.89
1601	O	THR	A	384	0.598	0.195	−12.707	1.00	22.32
1602	N	ASP	A	385	−0.833	1.877	−12.315	1.00	19.55
1603	CA	ASP	A	385	0.239	2.811	−11.961	1.00	19.49
1604	CB	ASP	A	385	−0.306	4.170	−11.546	1.00	20.91
1605	CG	ASP	A	385	−1.195	4.788	−12.575	1.00	22.67
1606	OD1	ASP	A	385	−1.864	5.766	−12.208	1.00	24.97
1607	OD2	ASP	A	385	−1.230	4.326	−13.733	1.00	23.80
1608	C	ASP	A	385	1.025	2.276	−10.778	1.00	19.01
1609	O	ASP	A	385	2.255	2.278	−10.778	1.00	18.96
1610	N	LEU	A	386	0.289	1.884	−9.743	1.00	19.05
1611	CA	LEU	A	386	0.854	1.338	−8.519	1.00	18.85
1612	CB	LEU	A	386	−0.296	0.983	−7.590	1.00	19.37
1613	CG	LEU	A	386	−0.096	0.569	−6.138	1.00	21.27
1614	CD1	LEU	A	386	0.644	1.636	−5.344	1.00	19.99
1615	CD2	LEU	A	386	−1.475	0.304	−5.541	1.00	20.99
1616	C	LEU	A	386	1.759	0.125	−8.787	1.00	19.60
1617	O	LEU	A	386	2.811	−0.037	−8.167	1.00	20.22
1618	N	ARG	A	387	1.373	−0.726	−9.724	1.00	20.25
1619	CA	ARG	A	387	2.193	−1.879	−10.026	1.00	20.24
1620	CB	ARG	A	387	1.397	−2.848	−10.888	1.00	23.00
1621	CG	ARG	A	387	2.009	−4.221	−11.044	1.00	28.55
1622	CD	ARG	A	387	1.746	−4.736	−12.457	1.00	32.13
1623	NE	ARG	A	387	1.966	−3.644	−13.412	1.00	34.51
1624	CZ	ARG	A	387	1.421	−3.570	−14.622	1.00	35.87
1625	NH1	ARG	A	387	0.633	−4.546	−15.056	1.00	36.39
1626	NH2	ARG	A	387	1.554	−2.457	−15.343	1.00	36.86
1627	C	ARG	A	387	3.486	−1.392	−10.715	1.00	19.97
1628	O	ARG	A	387	4.521	−2.029	−10.607	1.00	18.77
1629	N	GLY	A	388	3.447	−0.232	−11.369	1.00	18.70
1630	CA	GLY	A	388	4.650	0.299	−12.008	1.00	18.83
1631	C	GLY	A	388	5.674	0.921	−11.037	1.00	20.22
1632	O	GLY	A	388	6.893	0.833	−11.248	1.00	15.88
1633	N	ILE	A	389	5.179	1.591	−9.991	1.00	21.33
1634	CA	ILE	A	389	6.032	2.221	−8.970	1.00	21.20
1635	CB	ILE	A	389	5.229	3.280	−8.088	1.00	22.81
1636	CG2	ILE	A	389	5.126	2.852	−6.639	1.00	23.64
1637	CG1	ILE	A	389	5.883	4.666	−8.150	1.00	22.25
1638	CD1	ILE	A	389	5.524	5.427	−9.378	1.00	21.83
1639	C	ILE	A	389	6.623	1.129	−8.083	1.00	19.67
1640	O	ILE	A	389	7.778	1.220	−7.705	1.00	19.23
1641	N	SER	A	390	5.848	0.082	−7.781	1.00	19.25
1642	CA	SER	A	390	6.333	−1.009	−6.935	1.00	19.04
1643	CB	SER	A	390	5.183	−1.882	−6.477	1.00	20.61
1644	OG	SER	A	390	4.339	−2.156	−7.562	1.00	26.93
1645	C	SER	A	390	7.407	−1.848	−7.612	1.00	18.57
1646	O	SER	A	390	8.300	−2.389	−6.946	1.00	16.78
1647	N	THR	A	391	7.326	−1.960	−8.931	1.00	18.45
1648	CA	THR	A	391	8.335	−2.696	−9.666	1.00	20.13
1649	CB	THR	A	391	7.930	−2.914	−11.066	1.00	21.93
1650	OG1	THR	A	391	7.487	−1.673	−11.621	1.00	28.62
1651	CG2	THR	A	391	6.806	−3.897	−11.099	1.00	25.50
1652	C	THR	A	391	9.587	−1.863	−9.624	1.00	20.07
1653	O	THR	A	391	10.685	−2.401	−9.524	1.00	20.66
1654	N	LYS	A	392	9.431	−0.543	−9.669	1.00	19.69
1655	CA	LYS	A	392	10.587	0.332	−9.550	1.00	20.05
1656	CB	LYS	A	392	10.250	1.755	−9.985	1.00	20.70
1657	CG	LYS	A	392	10.362	1.951	−11.486	1.00	22.58
1658	CD	LYS	A	392	9.843	3.311	−11.846	1.00	24.75
1659	CE	LYS	A	392	9.289	3.374	−13.257	1.00	26.63
1660	NZ	LYS	A	392	8.295	4.511	−13.315	1.00	28.55
1661	C	LYS	A	392	11.098	0.282	−8.094	1.00	20.04
1662	O	LYS	A	392	12.300	0.422	−7.835	1.00	20.48
1663	N	GLY	A	393	10.186	0.052	−7.151	1.00	18.91
1664	CA	GLY	A	393	10.566	−0.091	−5.753	1.00	17.90
1665	C	GLY	A	393	11.427	−1.338	−5.601	1.00	18.64
1666	O	GLY	A	393	12.451	−1.311	−4.925	1.00	20.47
1667	N	ALA	A	394	11.040	−2.420	−6.279	1.00	19.69
1668	CA	ALA	A	394	11.761	−3.689	−6.264	1.00	19.72
1669	CB	ALA	A	394	11.011	−4.696	−7.105	1.00	21.54
1670	C	ALA	A	394	13.181	−3.547	−6.789	1.00	21.85
1671	O	ALA	A	394	14.104	−4.184	−6.282	1.00	22.78
1672	N	GLU	A	395	13.337	−2.763	−7.859	1.00	24.10
1673	CA	GLU	A	395	14.640	−2.487	−8.482	1.00	24.51
1674	CB	GLU	A	395	14.466	−1.672	−9.774	1.00	26.19
1675	CG	GLU	A	395	13.910	−2.494	−10.949	1.00	31.31
1676	CD	GLU	A	395	13.717	−1.699	−12.256	1.00	33.90
1677	OE1	GLU	A	395	13.984	−0.470	−12.282	1.00	33.65
1678	OE2	GLU	A	395	13.288	−2.322	−13.263	1.00	35.18
1679	C	GLU	A	395	15.515	−1.719	−7.503	1.00	23.81
1680	O	GLU	A	395	16.715	−1.919	−7.422	1.00	23.93
1681	N	ARG	A	396	14.884	−0.851	−6.740	1.00	23.94
1682	CA	ARG	A	396	15.574	−0.056	−5.747	1.00	23.55
1683	CB	ARG	A	396	14.628	1.029	−5.216	1.00	23.99
1684	CG	ARG	A	396	15.199	1.891	−4.115	1.00	21.36
1685	CD	ARG	A	396	16.298	2.745	−4.634	1.00	21.46
1686	NE	ARG	A	396	16.917	3.454	−3.534	1.00	24.01
1687	CZ	ARG	A	396	18.222	3.656	−3.406	1.00	23.81
1688	NH1	ARG	A	396	19.078	3.195	−4.309	1.00	23.29
1689	NH2	ARG	A	396	18.661	4.380	−2.391	1.00	24.32
1690	C	ARG	A	396	16.068	−0.922	−4.594	1.00	23.72
1691	O	ARG	A	396	17.049	−0.590	−3.947	1.00	24.55
1692	N	ALA	A	397	15.368	−2.009	−4.299	1.00	24.28
1693	CA	ALA	A	397	15.783	−2.872	−3.205	1.00	23.74
1694	CB	ALA	A	397	14.741	−3.925	−2.933	1.00	24.49
1695	C	ALA	A	397	17.108	−3.507	−3.576	1.00	24.26
1696	O	ALA	A	397	17.943	−3.779	−2.721	1.00	24.86
1697	N	ILE	A	398	17.308	−3.713	−4.870	1.00	26.18
1698	CA	ILE	A	398	18.547	−4.291	−5.384	1.00	27.23
1699	CB	ILE	A	398	18.516	−4.412	−6.927	1.00	27.41
1700	CG2	ILE	A	398	19.685	−5.238	−7.416	1.00	28.46
1701	CG1	ILE	A	398	17.236	−5.109	−7.369	1.00	28.19
1702	CD1	ILE	A	398	16.999	−6.382	−6.637	1.00	29.70
1703	C	ILE	A	398	19.731	−3.406	−4.977	1.00	27.78
1704	O	ILE	A	398	20.534	−3.792	−4.100	1.00	29.44
1705	N	THR	A	399	19.819	−2.205	−5.564	1.00	27.08
1706	CA	THR	A	399	20.908	−1.293	−5.246	1.00	26.37
1707	CB	THR	A	399	20.785	0.016	−5.994	1.00	26.11
1708	OG1	THR	A	399	19.421	0.414	−6.022	1.00	28.83
1709	CG2	THR	A	399	21.235	−0.161	−7.405	1.00	29.58
1710	C	THR	A	399	20.988	−1.049	−3.755	1.00	25.99
1711	O	THR	A	399	22.079	−1.025	−3.186	1.00	26.23
1712	N	LEU	A	400	19.830	−0.935	−3.110	1.00	27.37
1713	CA	LEU	A	400	19.800	−0.723	−1.673	1.00	28.07
1714	CB	LEU	A	400	18.373	−0.640	−1.149	1.00	27.98
1715	CG	LEU	A	400	17.955	0.753	−0.667	1.00	28.69
1716	CD1	LEU	A	400	16.547	0.702	−0.104	1.00	26.86
1717	CD2	LEU	A	400	18.932	1.293	0.368	1.00	28.98
1718	C	LEU	A	400	20.527	−1.862	−0.978	1.00	28.53
1719	O	LEU	A	400	21.290	−1.630	−0.047	1.00	28.85
1720	N	LYS	A	401	20.327	−3.087	−1.447	1.00	29.09
1721	CA	LYS	A	401	21.000	−4.220	−0.839	1.00	29.71
1722	CB	LYS	A	401	20.666	−5.515	−1.561	1.00	29.44
1723	CG	LYS	A	401	19.240	−5.946	−1.356	1.00	31.48
1724	CD	LYS	A	401	18.938	−7.290	−1.989	1.00	32.04
1725	CE	LYS	A	401	17.464	−7.374	−2.329	1.00	32.74
1726	NZ	LYS	A	401	17.137	−6.437	−3.437	1.00	34.16
1727	C	LYS	A	401	22.494	−3.980	−0.852	1.00	29.99
1728	O	LYS	A	401	23.164	−4.170	0.153	1.00	29.22
1729	N	MET	A	402	23.007	−3.486	−1.971	1.00	31.43
1730	CA	MET	A	402	24.434	−3.213	−2.065	1.00	31.78
1731	CB	MET	A	402	24.795	−2.716	−3.463	1.00	34.68
1732	CG	MET	A	402	24.275	−3.512	−4.648	1.00	36.65
1733	SD	MET	A	402	24.622	−2.451	−6.136	1.00	42.97
1734	CE	MET	A	402	23.219	−2.873	−7.264	1.00	38.36
1735	C	MET	A	402	24.849	−2.125	−1.057	1.00	31.44
1736	O	MET	A	402	25.951	−2.187	−0.496	1.00	32.49
1737	N	GLU	A	403	23.970	−1.144	−0.832	1.00	29.62
1738	CA	GLU	A	403	24.246	−0.011	0.058	1.00	28.02
1739	CB	GLU	A	403	23.455	1.205	−0.415	1.00	29.18
1740	CG	GLU	A	403	23.567	1.495	−1.923	1.00	33.06
1741	CD	GLU	A	403	22.618	2.607	−2.397	1.00	35.19
1742	OE1	GLU	A	403	22.053	3.320	−1.530	1.00	36.93
1743	OE2	GLU	A	403	22.429	2.770	−3.634	1.00	35.87
1744	C	GLU	A	403	24.098	−0.145	1.592	1.00	28.19
1745	O	GLU	A	403	24.645	0.678	2.335	1.00	27.87
1746	N	ILE	A	404	23.336	−1.116	2.091	1.00	27.14
1747	CA	ILE	A	404	23.200	−1.256	3.542	1.00	25.57
1748	CB	ILE	A	404	21.799	−1.798	3.970	1.00	24.57
1749	CG2	ILE	A	404	20.743	−0.754	3.715	1.00	22.48
1750	CG1	ILE	A	404	21.495	−3.117	3.253	1.00	25.32
1751	CD1	ILE	A	404	20.172	−3.770	3.626	1.00	24.30
1752	C	ILE	A	404	24.334	−2.124	4.097	1.00	25.35
1753	O	ILE	A	404	24.850	−3.003	3.408	1.00	23.29
1754	N	PRO	A	405	24.710	−1.904	5.370	1.00	26.12
1755	CD	PRO	A	405	24.046	−0.965	6.289	1.00	26.59
1756	CA	PRO	A	405	25.782	−2.618	6.072	1.00	28.17
1757	CB	PRO	A	405	26.115	−1.661	7.203	1.00	28.59
1758	CG	PRO	A	405	24.737	−1.254	7.632	1.00	28.60
1759	C	PRO	A	405	25.365	−3.949	6.648	1.00	29.91
1760	O	PRO	A	405	26.129	−4.564	7.402	1.00	30.96
1761	N	GLY	A	406	24.124	−4.337	6.387	1.00	30.15
1762	CA	GLY	A	406	23.629	−5.599	6.880	1.00	30.34
1763	C	GLY	A	406	22.572	−6.101	5.927	1.00	30.21
1764	O	GLY	A	406	22.231	−5.395	4.973	1.00	30.98
1765	N	PRO	A	407	22.049	−7.318	6.131	1.00	29.00
1766	CD	PRO	A	407	22.190	−8.214	7.299	1.00	30.16
1767	CA	PRO	A	407	21.022	−7.804	5.215	1.00	27.77
1768	CB	PRO	A	407	20.907	−9.265	5.613	1.00	29.21
1769	CG	PRO	A	407	21.015	−9.169	7.136	1.00	29.55
1770	C	PRO	A	407	19.749	−7.047	5.567	1.00	26.71
1771	O	PRO	A	407	19.641	−6.483	6.678	1.00	27.29
1772	N	MET	A	408	18.815	−6.962	4.623	1.00	24.49
1773	CA	MET	A	408	17.553	−6.288	4.913	1.00	22.84
1774	CB	MET	A	408	16.747	−6.104	3.622	1.00	24.24
1775	CG	MET	A	408	17.429	−5.294	2.556	1.00	23.24
1776	SD	MET	A	408	16.179	−4.677	1.436	1.00	24.38
1777	CE	MET	A	408	16.887	−3.079	1.097	1.00	25.22
1778	C	MET	A	408	16.752	−7.153	5.909	1.00	20.40
1779	O	MET	A	408	17.020	−8.341	6.049	1.00	18.50
1780	N	PRO	A	409	15.801	−6.558	6.653	1.00	19.49
1781	CD	PRO	A	409	15.501	−5.124	6.731	1.00	18.87
1782	CA	PRO	A	409	14.982	−7.300	7.616	1.00	18.15
1783	CB	PRO	A	409	13.928	−6.280	7.975	1.00	19.10
1784	CG	PRO	A	409	14.729	−5.031	8.009	1.00	19.00
1785	C	PRO	A	409	14.381	−8.520	6.928	1.00	17.75
1786	O	PRO	A	409	13.974	−8.448	5.770	1.00	15.42
1787	N	PRO	A	410	14.238	−9.632	7.657	1.00	17.26
1788	CD	PRO	A	410	14.390	−9.731	9.120	1.00	16.92
1789	CA	PRO	A	410	13.695	−10.877	7.090	1.00	17.78
1790	CB	PRO	A	410	13.732	−11.844	8.287	1.00	18.05
1791	CG	PRO	A	410	13.532	−10.922	9.468	1.00	18.52
1792	C	PRO	A	410	12.335	−10.827	6.384	1.00	18.59
1793	O	PRO	A	410	12.167	−11.427	5.315	1.00	19.35
1794	N	LEU	A	411	11.365	−10.124	6.957	1.00	18.39
1795	CA	LEU	A	411	10.054	−10.045	6.335	1.00	17.77
1796	CB	LEU	A	411	9.011	−9.489	7.297	1.00	17.32
1797	CG	LEU	A	411	8.751	−10.391	8.510	1.00	18.93
1798	CD1	LEU	A	411	7.396	−10.095	9.093	1.00	15.54
1799	CD2	LEU	A	411	8.822	−11.857	8.104	1.00	19.18
1800	C	LEU	A	411	10.112	−9.237	5.065	1.00	17.72
1801	O	LEU	A	411	9.379	−9.509	4.114	1.00	19.61
1802	N	ILE	A	412	11.012	−8.262	5.030	1.00	17.15
1803	CA	ILE	A	412	11.186	−7.433	3.846	1.00	15.82
1804	CB	ILE	A	412	12.084	−6.227	4.169	1.00	15.58
1805	CG2	ILE	A	412	12.498	−5.522	2.909	1.00	15.37
1806	CG1	ILE	A	412	11.328	−5.282	5.106	1.00	13.65
1807	CD1	ILE	A	412	12.070	−4.078	5.484	1.00	14.79
1808	C	ILE	A	412	11.782	−8.300	2.740	1.00	16.91
1809	O	ILE	A	412	11.398	−8.200	1.578	1.00	17.37
1810	N	ARG	A	413	12.678	−9.205	3.112	1.00	18.84
1811	CA	ARG	A	413	13.303	−10.081	2.134	1.00	19.44
1812	CB	ARG	A	413	14.493	−10.827	2.734	1.00	21.68
1813	CG	ARG	A	413	15.609	−9.923	3.211	1.00	23.67
1814	CD	ARG	A	413	16.813	−10.744	3.637	1.00	24.61
1815	NE	ARG	A	413	17.413	−11.353	2.458	1.00	26.77
1816	CZ	ARG	A	413	18.364	−12.275	2.487	1.00	27.71
1817	NH1	ARG	A	413	18.840	−12.700	3.648	1.00	25.48
1818	NH2	ARG	A	413	18.821	−12.786	1.347	1.00	29.94
1819	C	ARG	A	413	12.307	−11.071	1.579	1.00	18.31
1820	O	ARG	A	413	12.371	−11.421	0.405	1.00	19.96
1821	N	GLU	A	414	11.422	−11.562	2.427	1.00	17.94
1822	CA	GLU	A	414	10.406	−12.501	1.987	1.00	18.28
1823	CB	GLU	A	414	9.504	−12.894	3.156	1.00	19.64
1824	CG	GLU	A	414	10.039	−14.034	3.995	1.00	19.89
1825	CD	GLU	A	414	10.209	−15.310	3.186	1.00	21.06
1826	OE1	GLU	A	414	9.301	−15.648	2.385	1.00	20.02
1827	OE2	GLU	A	414	11.254	−15.970	3.354	1.00	22.16
1828	C	GLU	A	414	9.550	−11.835	0.939	1.00	19.63
1829	O	GLU	A	414	9.261	−12.406	−0.098	1.00	19.16
1830	N	MET	A	415	9.170	−10.593	1.209	1.00	21.32
1831	CA	MET	A	415	8.322	−9.846	0.299	1.00	22.45
1832	CB	MET	A	415	7.998	−8.490	0.896	1.00	21.92
1833	CG	MET	A	415	7.351	−7.563	−0.103	1.00	22.95
1834	SD	MET	A	415	7.180	−6.000	0.638	1.00	20.83
1835	CE	MET	A	415	8.882	−5.467	0.380	1.00	18.97
1836	C	MET	A	415	8.903	−9.656	−1.085	1.00	23.05
1837	O	MET	A	415	8.177	−9.717	−2.092	1.00	22.53
1838	N	LEU	A	416	10.210	−9.395	−1.125	1.00	24.28
1839	CA	LEU	A	416	10.928	−9.167	−2.384	1.00	24.33
1840	CB	LEU	A	416	12.128	−8.217	−2.171	1.00	24.70
1841	CG	LEU	A	416	11.855	−6.810	−1.591	1.00	23.04
1842	CD1	LEU	A	416	13.139	−6.167	−1.129	1.00	24.40
1843	CD2	LEU	A	416	11.172	−5.936	−2.608	1.00	23.10
1844	C	LEU	A	416	11.347	−10.440	−3.127	1.00	25.18
1845	O	LEU	A	416	12.048	−10.363	−4.122	1.00	25.92
1846	N	GLU	A	417	11.010	−11.614	−2.597	1.00	27.78
1847	CA	GLU	A	417	11.301	−12.861	−3.310	1.00	29.15
1848	CB	GLU	A	417	11.736	−14.029	−2.393	1.00	28.98
1849	CG	GLU	A	417	12.042	−15.289	−3.239	1.00	31.22
1850	CD	GLU	A	417	12.651	−16.473	−2.495	1.00	31.45
1851	OE1	GLU	A	417	11.909	−17.412	−2.138	1.00	33.15
1852	OE2	GLU	A	417	13.883	−16.507	−2.327	1.00	30.59
1853	C	GLU	A	417	9.959	−13.188	−3.950	1.00	29.66
1854	O	GLU	A	417	9.096	−13.773	−3.316	1.00	30.13
1855	N	ASN	A	418	9.767	−12.772	−5.194	1.00	32.47
1856	CA	ASN	A	418	8.496	−13.017	−5.866	1.00	34.15
1857	CB	ASN	A	418	7.432	−12.067	−5.300	1.00	35.46
1858	CG	ASN	A	418	7.710	−10.605	−5.629	1.00	34.92
1859	OD1	ASN	A	418	8.097	−9.833	−4.759	1.00	35.44
1860	ND2	ASN	A	418	7.483	−10.215	−6.878	1.00	35.03
1861	C	ASN	A	418	8.570	−12.814	−7.381	1.00	35.01
1862	O	ASN	A	418	9.326	−11.960	−7.853	1.00	34.95
1863	N	PRO	A	419	7.773	−13.591	−8.152	1.00	34.87
1864	CD	PRO	A	419	6.936	−14.692	−7.644	1.00	35.71
1865	CA	PRO	A	419	7.697	−13.533	−9.615	1.00	35.66
1866	CB	PRO	A	419	6.731	−14.682	−9.953	1.00	35.26
1867	CG	PRO	A	419	6.908	−15.642	−8.817	1.00	35.03
1868	C	PRO	A	419	7.078	−12.196	−10.024	1.00	36.89
1869	OT1	PRO	A	419	6.055	−11.826	−9.383	1.00	38.65
1870	OT2	PRO	A	419	7.604	−11.540	−10.960	1.00	37.30
1871	C1	REA	A	500	11.617	0.766	−0.974	1.00	22.98
1872	C2	REA	A	500	12.711	−0.165	−1.544	1.00	23.95
1873	C3	REA	A	500	13.522	−0.885	−0.510	1.00	23.03
1874	C4	REA	A	500	12.706	−1.723	0.439	1.00	21.73
1875	C5	REA	A	500	11.296	−1.155	0.709	1.00	22.75
1876	C6	REA	A	500	10.782	−0.041	0.060	1.00	22.00
1877	C7	REA	A	500	9.422	0.493	0.254	1.00	21.60
1878	C8	REA	A	500	8.791	0.679	1.424	1.00	20.23
1879	C9	REA	A	500	7.449	1.141	1.670	1.00	17.02
1880	C10	REA	A	500	7.099	1.229	2.962	1.00	17.58
1881	C11	REA	A	500	5.821	1.637	3.462	1.00	18.07
1882	C12	REA	A	500	5.727	1.752	4.782	1.00	19.51
1883	C13	REA	A	500	4.536	2.128	5.483	1.00	21.00
1884	C14	REA	A	500	4.647	2.258	6.811	1.00	21.05
1885	C15	REA	A	500	3.667	2.658	7.784	1.00	20.02
1886	C16	REA	A	500	10.701	1.240	−2.118	1.00	24.14
1887	C17	REA	A	500	12.306	1.974	−0.296	1.00	21.99
1888	C18	REA	A	500	10.607	−2.018	1.769	1.00	21.60
1889	C19	REA	A	500	6.509	1.505	0.524	1.00	13.38
1890	C20	REA	A	500	3.231	2.378	4.699	1.00	22.04
1891	O1	REA	A	500	4.026	2.789	8.938	1.00	21.58
1892	O2	REA	A	500	2.508	2.885	7.461	1.00	23.03

[0379] It will be understood that various details of the invention can be changed without departing from the scope of the invention. Furthermore, the foregoing description is for the purpose of illustration only, and not for the purpose of limitation-the invention being defined by the claims.

Claims

1. A crystalline form comprising a substantially pure LXR ligand binding domain polypeptide and a ligand.

2. The crystalline form of claim 1, wherein the LXR ligand binding domain polypeptide comprises the amino acid sequence of SEQ ID NO: 8.

3. The crystalline form of claim 1, wherein the ligand is N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide.

4. The crystalline form of claim 1, wherein the ligand is 24(S), 25-epoxycholesterol.

5. The crystalline form of claim 1, wherein the crystalline form has lattice constants of a=60.25 Å, b=82.45 Å, c=123.18 Å, α=90°, β=90°, γ=90°.

6 The crystalline form of claim 1, wherein the crystalline form is an orthorhombic crystalline form.

7. The crystalline form of claim 1, wherein the crystalline form has a space group of P212121.

8. The crystalline form of claim 1, wherein the crystalline form contains two LXR ligand binding domain polypeptides in the asymmetric unit.

9. The crystalline form of claim 1, wherein the crystalline form is further characterized by the coordinates corresponding to Table 2.

10. The crystalline form of claim 1, wherein the crystalline form is such that the three-dimensional structure of the crystalline form can be determined to a resolution of about 2.8 Å or better.

11. The crystalline form of claim 1, wherein the crystalline form contains one or more atoms having a atomic weight of 40 grams/mol or greater.

12. A crystalline form comprising a substantially pure LXR ligand binding domain polypeptide, a coactivator polypeptide and a ligand.

13. The crystalline form of claim 12, wherein the LXR ligand binding domain polypeptide comprises the amino acid sequence shown of SEQ ID NO: 8.

14. The crystalline form of claim 12, wherein the ligand is 24(S), 25-epoxycholesterol, and the coactivator polypeptide is a SRC1 fragment.

15. The crystalline form of claim 12, wherein the SRC1 fragment comprises the amino acid sequence of SEQ ID NO: 9.

16. The crystalline form of claim 12, wherein the crystalline form has lattice constants selected from the group consisting of a=71.17 Å, b=120.01 Å, c=147.56 Å, α=90, β=90°, γ=90°.

17. The crystalline form of claim 12, wherein the crystalline form is an orthorhombic crystalline form.

18. The crystalline form of claim 12, wherein the crystalline form has a space group of C2221.

19. The crystalline form of claim 12, wherein the crystalline form contains two LXR ligand binding domain polypeptides and two coactivator polypeptides in the asymmetric unit.

20. The crystalline form of claim 12, wherein the crystalline form is further characterized by the coordinates corresponding to Table 3.

21. The crystalline form of claim 12, wherein the crystalline form is such that the three-dimensional structure of the crystalline form can be determined to a resolution of about 2.8 Å or better.

22. The crystalline form of claim 12, wherein the crystalline form comprises one or more atoms having a atomic weight of 40 grams/mol or greater.

23. A method for determining the three-dimensional structure of a crystallized LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide to a resolution of about 2.8 Å or better, the method comprising: (a) crystallizing a LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator fragment to form a crystallized complex; and (b) analyzing the crystallized complex to determine the three-dimensional structure of the LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide, whereby the three-dimensional structure of a crystallized LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide is determined to a resolution of about 2.8 Å or better.

24. The method of claim 23, wherein the analyzing is by X-ray diffraction.

25. The method of claim 23, wherein the crystallization is accomplished by the hanging drop vapor diffusion method, and wherein the LXR ligand binding domain polypeptide and the ligand are mixed with an equal volume of reservoir.

26. The method of claim 25, wherein the reservoir comprises 10-12% PEG3350-8000 and 0.2 M salt.

27. The method of claim 23, wherein the salt is selected from the group consisting of NaF, KF, NaCl, KCl, Na formate, Na acetate, K acetate, ammonium sulfate and lithium sulfate.

28. The method of claim 23, wherein the LXR ligand binding domain polypeptide comprises the amino acid sequence of SEQ ID NO: 8.

29. The method of claim 23, wherein the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide.

30. The method of claim 23, wherein the coactivator polypeptide is a SRC1 polypeptide.

31. The method of claim 30, wherein the SRC1 polypeptide comprises the sequence of SEQ ID NO: 9.

32. A method of generating a crystalline form comprising a LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide, the method comprising: (a) incubating a solution comprising a LXR ligand binding domain and one or more of a ligand and a coactivator polypeptide with an equal volume of reservoir; and (b) crystallizing the LXR ligand binding domain polypeptide and one or more of a ligand and a coactivator polypeptide using the hanging drop method, whereby a crystalline form of a LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide is generated.

33. The method of claim 32, wherein the LXR ligand binding domain comprises the amino acid sequence of SEQ ID NO: 8.

34. The method of claim 32, wherein the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide.

35. The method of claim 32, wherein the coactivator polypeptide comprises a SRC1 polypeptide.

36. The method of claim 35, wherein the SRC1 polypeptide comprises the sequence of SEQ ID NO: 9.

37. A crystalline form of a LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide produced by the method of claim 32.

38. A method of designing a modulator of a NR polypeptide, the method comprising: (a) designing a potential modulator of a NR polypeptide that will make interactions with amino acids in a ligand binding site of the NR polypeptide, based upon a crystalline structure comprising a LXR ligand binding domain polypeptide in complex with a one or more of a ligand and a coactivator polypeptide; (b) synthesizing the modulator; and (c) determining whether the potential modulator modulates the activity of the NR polypeptide, whereby a modulator of a NR polypeptide is designed.

39. The method of claim 38, wherein the ligand is selected from the group consisting of 24(S), 25-epoxycholesterol and N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide.

40. The method of claim 38, wherein the coactivator polypeptide comprises a SRC1 polypeptide.

41. The method of claim 38, wherein the SRC1 polypeptide comprises the sequence of SEQ ID NO: 9.

42. The method of claim 38, wherein the NR comprises a LXR.

43. The method of claim 42, wherein the LXR comprises a LXRβ.

44. The method of claim 43, wherein the LXRβ comprises the amino acid sequence of SEQ ID NO: 4.

45. The method of claim 38, wherein the ligand is selected from the group consisting of N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and 24(S), 25-epoxycholesterol.

46. A method of designing a modulator that selectively modulates the activity of a NR polypeptide compared to other polypeptides, the method comprising: (a) obtaining a crystalline form comprising a LXRβ ligand binding domain polypeptide in complex with one or more of a ligand and a coativator polypeptide; (b) evaluating the three-dimensional structure of the crystallized LXRβ ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide; and (c) synthesizing a potential modulator based on the three-dimensional structure of the crystallized LXRβ ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide, whereby a modulator that selectively modulates the activity of a NR polypeptide compared to other polypeptides is designed.

47. The method of claim 46, wherein the method further comprises contacting a NR ligand binding domain polypeptide with the potential modulator and one or more of a ligand and a coactivator polypeptide; and assaying the NR ligand binding domain polypeptide for binding of the potential modulator, for a change in activity of the NR ligand binding domain polypeptide, or both.

48. The method of claim 46, wherein the LXRβ ligand binding domain polypeptide comprises the amino acid sequence of SEQ ID NO: 8.

49. The method of claim 46, wherein the NR comprises a LXR.

50. The method of claim 49, wherein the LXR comprises LXRβ.

51. The method of claim 46, wherein the crystalline form is an orthorhombic form.

52. The method of claim 46, wherein the crystalline form is further characterized by the atomic structural coordinates of one of Table 2 and Table 3.

53. The method of claim 46, wherein the crystalline form is such that the three-dimensional structure of the crystallized LXRβ ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide can be determined to a resolution of about 2.8 Å or better.

54. The method of claim 46, wherein the coactivator polypeptide comprises a SRC1 peptide.

55. Then method of claim 54, wherein the SRC1 peptide comprises the sequence of SEQ ID NO: 9.

56. The method of claim 46, wherein the ligand is selected from the group consisting of N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and 24(S), 25-epoxycholesterol.

57. A method of screening a plurality of compounds for a modulator of a NR ligand binding domain polypeptide, the method comprising: (a) providing a library of test samples; (b) contacting a crystalline form comprising a LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide with each test sample; (c) detecting an interaction between a test sample and the crystalline LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide; (d) identifying a test sample that interacts with the crystalline LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coactivator polypeptide; and (e) isolating a test sample that interacts with the crystalline LXR ligand binding domain polypeptide in complex with one or more of a ligand and a coregulator polypeptide, whereby a plurality of compounds is screened for a modulator of a NR ligand binding domain polypeptide.

58. The method of claim 57, wherein the crystalline form is further characterized by an atomic structural coordinate set selected from the group consisting of Table 2 and Table 3.

59. The method of claim 57, wherein the LXR ligand binding domain polypeptide comprises a LXRβ ligand binding domain polypeptide.

60. The method of claim 59, wherein the LXRβ ligand binding domain polypeptide comprises the amino acid sequence of SEQ ID NO: 8.

61. The method of claim 57, wherein the test samples are bound to a substrate.

62. The method of claim 57, wherein the test samples are synthesized directly on a substrate.

63. The method of claim 57, wherein the coregulator polypeptide comprises a SRC1 polypeptide.

64. The method of claim 63, wherein the SRC1 polypeptide comprises the sequence of SEQ ID NO: 9.

65. The method of claim 57, wherein the ligand is selected from the group consisting of N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and 24(S), 25-epoxycholesterol.

66. A method for identifying a NR modulator, the method comprising: (a) providing atomic structural coordinates describing a LXR ligand binding domain in complex with one or more of a ligand and a coactivator polypeptide to a computerized modeling system; and (b) modeling ligands that fit spatially into the binding pocket of the LXR ligand binding domain to thereby identify a NR modulator.

67. The method of claim 66, wherein the method further comprises identifying in an assay for NR-mediated activity a modeled ligand that increases or decreases the activity of the NR.

68. The method of claim 66, wherein the atomic structural coordinates are selected from the group consisting of the coordinates of Table 2 and the coordinates of Table 3.

69. The method of claim 66, wherein the LXR comprises LXRβ.

70. The method of claim 66, wherein the LXRβ ligand binding domain comprises the amino acid sequence of SEQ ID NO: 8.

71. The method of claim 66, wherein the coactivator polypeptide comprises a SRC1 polypeptide.

72. The method of claim 71, wherein the SRC1 polypeptide comprises the sequence of SEQ ID NO: 9.

73. The method of claim 66, wherein the ligand is selected from the group consisting of N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and 24(S), 25-epoxycholesterol.

74. A method of identifying a LXR modulator that selectively modulates the activity of a LXRβ polypeptide compared to other polypeptides, the method comprising: (a) providing atomic structural coordinates describing a LXRβ ligand binding domain in complex with one or more of a ligand and a coactivator polypeptide to a computerized modeling system; and (b) modeling a ligand that fits into the binding pocket of a LXRβ ligand binding domain and that interacts with residues of a LXRβ that are conserved among LXR subtypes to thereby identify a LXRβ modulator that selectively modulates the activity of a LXRβ polypeptide compared to other polypeptides.

75. The method of claim 74, wherein the method further comprises identifying in a biological assay for LXRβ activity a modeled ligand that selectively binds to said LXRβ and increases or decreases the activity of said LXRβ.

76. The method of claim 74, wherein the atomic structural coordinates are selected from the group consisting of the coordinates of Table 2 and the coordinates of Table 3.

77. The method of claim 74, wherein the LXRβ ligand binding domain comprises the amino acid sequence shown in SEQ ID NO: 8.

78. The method of claim 74, wherein the coactivator polypeptide comprises a SRC1 polypeptide.

79. The method of claim 78, wherein the SRC1 polypeptide comprises the sequence of SEQ ID NO: 9.

80. The method of claim 74, wherein the ligand is selected from the group consisting of N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and 24(S), 25-epoxycholesterol.

81. A method of designing a modulator of a NR polypeptide, the method comprising: (a) selecting a candidate NR ligand; (b) determining which amino acid or amino acids of a NR polypeptide interact with the ligand using a three-dimensional model of a crystallized protein, the model comprising a LXRβ ligand binding domain in complex with one or more of a ligand and a coactivator polypeptide; (c) identifying in a biological assay for NR activity a degree to which the ligand modulates the activity of the NR polypeptide; (d) selecting a chemical modification of the ligand wherein the interaction between the amino acids of the NR polypeptide and the ligand is predicted to be modulated by the chemical modification; (e) synthesizing a ligand having the chemical modified to form a modified ligand; (f) contacting the modified ligand with the NR polypeptide; (g) identifying in a biological assay for NR activity a degree to which the modified ligand modulates the biological activity of the NR polypeptide; and (h) comparing the biological activity of the NR polypeptide in the presence of modified ligand with the biological activity of the NR polypeptide in the presence of the unmodified ligand, whereby a modulator of a NR polypeptide is designed.

82. The method of claim 81, wherein the NR polypeptide is a LXR polypeptide.

83. The method of claim 81, wherein the LXR is selected from the group consisting of a LXRα polypeptide and a LXRβ polypeptide.

84. The method of claim 83, wherein the LXRβ polypeptide has the amino acid sequence shown in SEQ ID NO: 4.

85. The method of claim 81, wherein the LXRA polypeptide comprises the amino acid sequence of SEQ ID NO: 2.

86. The method of claim 81, wherein the three-dimensional model of a crystallized protein is further characterized by atomic structural coordinates selected from the group consisting of the coordinates of Table 2 and the coordinates of Table 3.

87. The method of claim 81, wherein the coactivator polypeptide is a SRC1 polypeptide.

88. The method of claim 87, wherein the SRC1 polypeptide comprises the sequence of SEQ ID NO: 9.

89. The method of claim 81, wherein the ligand is selected from the group consisting of N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and 24(S), 25-epoxycholesterol.

90. The method of claim 81, wherein the method further comprises repeating steps (a) through (f), if the biological activity of the NR polypeptide in the presence of the modified ligand varies from the biological activity of the NR polypeptide in the presence of the unmodified ligand.

91. A method of identifying a LXR modulator that selectively modulates the biological activity of one LXR subtype compared to LXRβ, the method comprising: (a) providing an atomic structure coordinate set describing a LXRβ ligand binding domain structure in complex with one or more of a ligand and a coactivator polypeptide and at least one other atomic structure coordinate set describing a LXR ligand binding domain, each ligand binding domain comprising a ligand binding site; (b) comparing the LXR atomic structure coordinate sets to identify at least one difference between the sets; (c) designing a candidate ligand predicted to interact with the difference of step (b); (d) synthesizing the candidate ligand; and (e) testing the synthesized candidate ligand for an ability to selectively modulate a LXR subtype as compared to LXRβ, whereby a LXR modulator that selectively modulates the biological activity of one LXR subtype compared to LXRβ is identified.

92. The method of claim 91, wherein the LXR subtype whose biological activity is to be modulated comprises LXRA.

93. The method of claim 92, wherein the LXRα comprises the amino acid sequence of SEQ ID NO: 2.

94. The method of claim 91, wherein the atomic structure coordinate set describing a LXRβ ligand binding domain structure is selected from the group consisting of the coordinates of Table 2 and the coordinates of Table 3.

95. The method of claim 91, wherein the coactivator polypeptide comprises a SRC1 polypeptide.

96. The method of claim 95, wherein the SRC1 polypeptide comprises the sequence of SEQ ID NO: 9.

97. The method of claim 91, wherein the atomic structure coordinate set further describes an associated ligand.

98. The method of claim 97, wherein the ligand is selected from the group consisting of N-(2,2,2-trifluoroethyl)-N-[4-(2,2,2-trifluoro-1-hydroxy-1-trifluoromethyl-ethyl)-phenyl]-benzenesulfonamide and 24(S), 25-epoxycholesterol.

99. A method of modeling a three-dimensional structure of a target NR in complex with one or more of a ligand and a coactivator polypeptide from a template comprising the X-ray structure of a LXRβ LBD in complex with one or more of a ligand and a coactivator polypeptide, the method comprising: (a) selecting an X-ray structure of a target NR LBD as a starting model for the target NR LBD; (b) manipulating the starting model for the target NR as a rigid body to superimpose its backbone atoms onto corresponding backbone atoms of a three-dimensional template structure comprising a LXRβ in complex with one or more of a ligand and a coactivator polypeptide to form a manipulated model; (c) making a copy of the coactivator peptide from the template structure to form a model of a coactivator polypeptide bound to a template LXRβ; (d) merging the model of the coactivator polypeptide into the manipulated model to form a modified model; (e) removing one or more amino acids from the modified model; and (f) optimizing side-chain conformations, whereby a three-dimensional structure of a target NR in complex with one or more of a ligand and a coactivator polypeptide is modeled from a template comprising the X-ray structure of an NR in complex with one or more of a ligand and a coactivator polypeptide.

100. The method of claim 99, wherein the X-ray structure of a target NR LBD is a structure built by homology modeling

101. The method of claim 99, wherein the LXRβ ligand binding domain comprises the sequence of SEQ ID NO: 8.

102. The method of claim 99, wherein the coactivator polypeptide is a SRC1 polypeptide.

103. The method of claim 102, wherein the SRC1 polypeptide comprises the sequence of SEQ ID NO: 9.

104. The method of claim 99, wherein the three-dimensional template structure is a structure characterized by the coordinates selected from the group consisting of the coordinates of Table 2, the coordinates of Table 3 and the coordinates of Table 4.

105. The method of claim 99, wherein the optimizing comprises varying distance constraints.