Method of constructing three-dimensional structure of transmembrane protein

Abstract

An object of the present invention is to provide a method for constructing the steric structure of an arbitrary 7-transmembrane G-protein-coupled receptor with good precision.

Description

TECHNICAL FIELD

[0001] The present invention relates to a method for preparing the steric structure of a protein. More particularly, this invention relates to a method for preparing the steric structure of a 7-transmembrane G-protein-coupled receptor with good precision, a database and the like containing atomic coordinates defining the steric structure of a protein obtained by the method.

[0002] It is said that a 7-transmembrane G-protein-coupled receptors account for more than half of receptors which have been cloned up to now, and the method and the database and the like of the present invention are extremely useful in the field of molecular design of medicines and agricultural chemicals.

BACKGROUND ART

[0003] An approach has made it possible to construct the steric structure of a desired protein having an unknown steric structure based on information of the alignment with the desired protein wherein the alignment is obtained by utilizing information about proteins having a known steric structure. This approach is usually called homology modeling. Although the precision of the steric structure constructed by homology modeling has been remarkably improved recently, there are still many problems to be solved.

[0004] On the other hand, since a membrane protein is difficult to crystallize experimentally, it has been difficult to apply X-ray crystal diffraction which is a main stream for determining a structure in structural biology. As an attempt has been tried to determine a structure of a membrane protein with an electron microscope from a two-dimensional crystal, a structure with some extent of precision is obtained to an extent of a precision and, therefrom, it has become possible to construct a model. However, its precision has not yet reached that of single crystal diffraction by X-ray, and structural information of a loop part which is not a transmembrane region and of a side chain part of an amino acid has been poor.

[0005] Among membrane proteins, a 7-transmembrane G-protein-coupled receptor (guanine nucleotide-binding protein-coupled receptor; hereinafter this may be abbreviated as “GCPRs” or “GPCR”) is a protein which has the common nature of activating a G-protein when receives various extracellular stimulations such as calcium ion, amines, various hormones, peptides and proteins, and transmitting information into cells, which and has an important function in a living body. The common characteristics of structures of GPCRs are 7-transmembrane α helix structures and loop structures of a variety of lengths connecting them, and it is considered that these common characteristics determine the natures of GPCRs. As seen in trypsins of a serine protease having the characteristic relationship between its structure and function, also in GPCRs, it is presumed that the above-mentioned structural characteristics serve as an information transmitting mechanism.

[0006] Since GPCRs are particularly difficult to crystallize, information about their steric structures is poor. Even under this situation, regarding the model construction, for example, there are reports such as modeling combined with a site-specific mutation experiment of a CB (2) receptor (Eur J Pharmacol 2000 Jul. 28; 401 (1): 17-25), modeling combined with a site-specific mutation experiment of a CCK (1) receptor (Eur J Pharmacol 2000 Jul. 21; 400 (2-3): 185-194), a theoretical model referring to the function (Protein Eng 2000 July; 13 (7): 477-90), construction of a NK2 receptor combined with a mutation experiment (Biochem J 1999 Apr. 1; 339 (Pt 1): 55-61), modeling regarding frog rhodopsin (J Mol Biol 1998, Aug 28; 281 (4): 741-54), modeling of a transmembrane receptor combined with a site-specific mutation (Biophys J 1998 March; 74 (3): 1203-14) and the like. However, the satisfactory results have not been necessarily obtained in these modelings.

[0007] The cause why a decisive steric structure of a membrane protein has not been proposed up to now is that a membrane protein hardly becomes a single crystal due to the nature of the membrane protein orienting in a membrane of a lipid bilayer and thus it is difficult to apply X-ray diffraction. Since a membrane protein is fundamentally of α helix and there is no diversity in its steric structure, there is the background that it is difficult to determine the structure by normal approaches of NMR and a distance geometry method. For that reason, the structural information of a membrane protein is generally analyzed by electron beam diffraction of a two-dimensional crystal orienting in a membrane, but its resolution is 6 to 7 angstrom, not reaching the precision of crystal diffraction at all.

[0008] In addition, a modeling method combined with a site-specific mutation is a method of performing substitution of an amino acid at a site which is considered to be important for the activity, and examining the influence on the activity of an agonist or an antagonist. Although this method has such an advantage that detailed discussion can be made as to the surroundings of the active site, a model can not be proposed until a mutated strain of a bacterium producing a number of substituted bodies is provided, until a reaction mechanism of stimulation to GPCRs is well known and, additionally, until geometric information is obtained, and operations are troublesome and, thus, it can hardly be said that this method will give the results with good precision.

[0009] Like this, as for a membrane protein, there has been only a scarcely minute structure obtained by electron beam diffraction, or a structure from bacteriorhodopsin or the like which is not functionally equal to GPCRs, and the situation has been such that there were conventionally no choices for a reference protein. In addition, since details of a side chain of a reference protein are not determined, the situation has not been such that the performance of a software is fully displayed despite that it is possible to determine even the detailed structure of a side chain by the software. In addition, conventionally, a protein with low homology including GPCRs could not be modeled and, even when there is one experimentally determined structure, it is judged that construction of a model is impossible at an alignment stage before construction of a model in many cases.

[0010] On the other hand, it is considered that rhodopsin, one of a GPCRs family accounting for a majority of membrane proteins, is activated by light stimulation and transmits information. Recently, it has been reported that the steric structure of this protein (PDB ID:1F88) including a side chain is determined in detail by X-ray crystal analysis (Science, vol. 289, 4 August 2000, 739-745).

DISCLOSURE OF THE INVENTION

[0011] In view of the above-mentioned situation, the present invention has been achieved in order to provide a method for constructing the steric structure of arbitrary GPCRs with good precision, a database and the like of atomic coordinates defining the steric structure of GPCRs which can be utilized for molecular design of medicines and agricultural chemicals.

[0012] The present inventors have intensively studied in order to attain the above-mentioned object and, as a result, found that the precision of the steric structure model of arbitrary GPCRs can be remarkably improved by using a database of amino acid sequences of GPCRs as a profile and referring to the steric structure of rhodopsin (PDB ID:1F88), compared to the time when only a conventional structure having a different helix arrangement and not being classified into GCRDb of bacteriorhodopsin has been obtained. That is, we found that the steric structure of arbitrary GPCRs can be constructed with good precision by using the database of amino acid sequences of PCRs “GCRDb” as a motif profile of PSI-BLAST, and performing alignment referring to the steric structure of rhodopsin (PDB ID:1F88). The present invention is completed based on these findings.

[0013] That is, according to the method of the present invention, there is provided (1) a method for constructing the steric structure of a transmembrane protein, which comprises selecting a protein having the steric structure to be referred to from the known steric structures of 7-transmembrane G-protein-coupled receptors using a database of amino acid sequences of the receptors as a profile, performing alignment of a desired protein having an unknown steric structure, and producing the steric structure of the desired protein having an unknown steric structure as a G-protein-coupled receptor.

[0014] According to a preferable aspect of the present invention, there are provided (2) the method described in the above (1), wherein alignment is performed by selecting a protein having the steric structure to be referred to from a database of known steric structures of G-protein-coupled receptors, and by juxtaposing an amino acid sequence of the selected reference protein and an amino acid sequence of the desired protein; (3) the method described in (2), wherein a structure to be referred to is the steric structure of rhodopsin (PDB ID:1F88); (4) the method described in any one of the above (1) to (4), wherein the database of amino acid sequences used as a profile is selected from the group consisting of GCRDb, GPCRDB, ExPASy and ORDB; and (5) the above-mentioned method, wherein the database of amino acid sequences is used as a motif profile of PSI-BLAST.

[0015] According to a preferable aspect of the present invention, there are provided (6) the method described in above (5), wherein in the alignment performed by PSI-BLAST, the identity between a final site-specific score matrix and the reference protein is calculated as an E value and, when the E value has a value of 0.1 or smaller, the steric structure is produced, (7) the method described in any one of the above (1) to (6), wherein regarding given alignment information, re-alignment is performed in view of a combination of disulfide bonds, and the steric structure is produced based on this re-alignment information, and (8) the method described in any one of the above (1) to (7), wherein production of the steric structure comprises obtaining a coordinate from the steric structure which is referred to with respect to Cα atoms in an amino acid based on the resulting alignment information, optimizing an atomic coordinate of Cα so as to minimize an objective function, adding other atoms of a main chain to an optimized atomic coordinate of Cα to optimize an atomic coordinate of a main chain so as to minimize an objective function, and adding other atoms of a side chain to an optimized atomic coordinate of a main chain to optimize so as to minimize an objective function.

[0016] According to another aspect of the present invention, there are provided (9) an atomic coordinate defining the steric structure of a 7-transmembrane G-protein-coupled receptor obtained by the method described in any one of the above (1) to (8), (10) a computer readable recording medium in which the atomic coordinate described in the above (9) is recorded, and (11) a database, which comprises the atomic coordinate described in the above (9).

[0017] According to still another aspect of the present invention, there is provided (12) a method of presuming the function of a protein, which method comprises selecting a protein having the steric structure to be referred to from the known steric structures of 7-transmembrane G-protein-coupled receptors using a database of amino acid sequences of the receptors as a profile, performing alignment of a desired protein having the unknown structure and, when the steric structure of the desired protein can be produced, judging that the desired protein is a 7-transmembrane G-protein-coupled receptor.

[0018] According to a preferable aspect of the present invention, there is provided (13) the method described in the above (12), wherein the alignment is performed by selecting a protein having the steric structure to be referred to from a database of the known steric structures of G-protein-coupled receptors, and juxtaposing an amino acid sequence of the selected reference protein and an amino acid sequence of the desired protein, the database of amino acid sequences used as a profile is selected from the group consisting of GCRDb, CPCRDB, ExPASy and ORDB and, when alignment has a reliability of 98% or more, it is judged that the steric structure of the desired protein can be produced.

[0019] According to still another aspect of the present invention, there are provided (14) a method of designing a drug molecule, which comprises identifying, retrieving, assessing or designing a desired drug molecule based on the interaction between the steric structure of a drug candidate molecule and the steric structure of a 7-transmembrane G-protein-coupled receptor produced by using the atomic coordinate as defined in the above (9), or the atomic coordinate of the recording medium as defined in the above (10) or of the database as defined in the above (11), (15) a method for screening a medicine or an agricultural chemical, which comprises examining the activity and the safety of the drug molecule obtained by the method as defined in the above (14) as a medicine or an agricultural chemical by a desired pharmacological or physiological test, and selecting a drug molecule having the desired nature, (16) a method for manufacturing a medicine or an agricultural chemical, which comprises formulating by blending a drug molecule obtained by the method as defined in the above (15) and a pharmaceutically or agriculturally or horticulturally acceptable carrier, and (17) a drug molecule obtained by the method as defined in the above (14).

BRIEF DESCRIPTION OF THE DRAWINGS

[0020] FIG. 1 is a flowchart that shows one example of a method for constructing the steric structure of GPCRs of the present invention.

[0021] FIG. 2 is a view that shows a method for constructing a Cα atomic coordinate at the step 30. An identified part of alignment is obtained from a reference protein and, as to an absene part, minimum rmsd of overlapping of two residues having overlapped both N and C terminals is obtained from a database.

[0022] FIG. 3 is a view that shows local space homology (LSH). In calculating regarding T residue in the figure, netted (gray) residues are taken into consideration. A part surrounded by a square in an alignment at a low part of the figure is a residue pair to be considered, and a ratio at * mark is LSH. In this case, LSH is 56.2%.

[0023] FIG. 4 is a view that shows the relationship between LSH and a ratio at structurally conserved regions (SCRs). LSH is calculated from the overlapping of Cα atoms between the desired protein and the reference protein, and a ratio at SCRs is the number of residues in SCRs relative to the total number of residues of the desired protein.

[0024] FIG. 5 is a view that shows alignment of QRHUB2 (β adrenaline receptor) obtained by using 1F88 (rhodopsin) as a reference protein. In the figure, numerals on the right of QRHUB2 and 1F88 are the number of amino acids subjected to alignment in an amino acid sequence of each protein. In addition, the upper sequence indicates QRHUB2 (β adrenaline receptor) and the lower sequence indicates 1F88 (rhodopsin). An amino acid sequence of each protein is shown by a single letter symbol.

[0025] FIG. 6 is a printout of a display that shows bonding between the steric structure model constructed by the present method and an agonist (isoproterenol). The netted part in the figure indicates the agonist. A circumstance can be seen in which this agonist in R conformation is hydrogen-bonded to a receptor.

[0026] FIG. 7 is a printout of a display that shows the relative position of amino acid residues which are hydrogen-bonded to an agonist when the agonist in R form is introduced in seven α helices of a β2 adrenaline receptor in FIG. 6.

[0027] FIG. 8 is a printout of a display that shows bonding between the steric structure model constructed by the present method and an agonist (isoproterenol). The netted part in the figure indicates the agonist. A circumstance can be seen in which this agonist in S conformation is hydrogen-bonded to a receptor.

[0028] FIG. 9 is a printout of a display that shows the relative position of amino acid residues which are hydrogen-bonded to this agonist when an agonist in S form is introduced in seven α helices of a β2 adrenaline receptor in FIG. 8. A circumstance can be seen in which the hydrogen bond distance between this agonist and a receptor is instabilized to some extent due to its S comformation.

[0029] FIG. 10 is a printout of a display that shows bonding between the steric structure model constructed by the present method and an antagonist in R form (propranolol). In the figure, a netted part is an antagonist. A circumstance can be seen in which an antagonist in R form is introduced in seven α helices of a β2 adrenaline receptor.

[0030] FIG. 11 is a printout of a display that shows the relative position of amino acid residues which are hydrogen-bonded to this antagonist when an antagonist in R form is introduced in seven α helices of a β2 adrenaline receptor in FIG. 10. A circumstance can be seen in which a hydrogen bond distance between this antagonist and a receptor is extended due to its R comformation.

[0031] FIG. 12 is a printout of a display that shows bonding between the steric structure model constructed by the present method and an antagonist in S form (propranolol). In the figure, the netted part is the antagonist. A circumstance can be seen in which an antagonist in S form is introduced in seven α helices of a β2 adrenaline receptor.

[0032] FIG. 13 is a printout of a display that shows the relative position of amino acid residues which are and hydrogen-bonded to this antagonist with some inatalization when the antagonist in S form is introduced in seven α helices of a β2 adrenaline receptor in FIG. 12.

[0033] FIG. 14 is a printout of a display that shows the relative position of an antagonist (left) and an agonist (right) in a β2 adrenaline receptor in FIGS. 6 to 13. From the figure, it can be seen that an agonist and an antagonist are introduced into pockets at different positions, respectively, as expected from an experiment of site-specific mutation.

BEST MODE FOR CARRYING OUT THE INVENTION

[0034] The present invention will be explained in more detail below.

[0035] In the present invention, a “desired protein” means a protein whose complete steric structure has not been determined by X-ray crystal analysis, NMR analysis or the like and which is a subject for steric structure construction and function presumption in the present invention. This protein includes proteins whose complete steric structure has not been obtained while whose partial structure has been analyzed, proteins whose functions have been already specified as GPCRs, proteins presumed to be GPCRs, and proteins whose functions are not clear at all while their amino acid sequences are determined. “A reference protein” is a protein whose minute steric structure has been already determined by X-ray crystal analysis or NMR analysis, and which is to be referred to for alignment and optimization of an atomic coordinate. “Alignment” means obtaining of the corresponding relationship between amino acid sequences of two or more kinds of proteins, and a method therefor will be described in detail below at explanation of each step.

[0036] Then, the present invention will be explained by referring to the drawings. FIG. 1 is a flowchart that shows one example of a method for constructing the steric structure of GPCRS of the present invention.

[0037] First, at the step 10, an amino acid sequence of a desired protein (sequence) is inputted. At the step 20, a structure to be referred to is selected from database of steric structures, and alignment (juxtaposition) with an amino acid sequence of the selected reference protein is performed. At the step 30, based on information of the alignment, a coordinate with regard to a Cα atom which is one of the constituent atoms in the amino acid is obtained from the structure of the reference protein prescribed at the step 20, and an atomic coordinate of Cα is optimized so as to minimize an objective function by a simulated annealing method. At the step 40, other atoms of a main chain are added to an atomic coordinate of Cα at the step 30, followed by the optimization to minimize an objective function by a simulated annealing method. At the step 50, atoms of a side chain are added to an atomic coordinate of a main chain at the step 40, which is optimized so as to minimize an objective function by a simulated annealing method. Thus, the steric structure of GPCRs can be constructed with good precision.

[0038] Each step will be described in detail below.

[0039] Step 10: An Amino Acid Sequence of a Desired Protein

[0040] First, an amino acid sequence of a desired protein having an unknown steric structure is inputted. As the amino acid sequence used, it is particularly preferable to use sequences registered in a database as GPCRs. These sequences can be obtained from GCRDb (The G-protein-coupled Receptor Database), the details of which are described in “An Internet review: the complete neuroscientist scours the World Wide Web” Bloom FE, Science 1996; 274 (5290): 1104-9: http://www.gcrdb.uthscsa.edu/, GPCRDB: http://www.qpcr.org/7tm/, ExPASy: http://www.expasv.ch/cgi-bin/sm-gpcr.pl, ORDB: http://ycmi.med.vale.edu/senselab/ordb/ and the like.

[0041] Not only sequences registered in databases as GPCRs, but also any amino acid sequences of such as human (H. sapiens), drosophila (D. melanogaster), nematode (C. elagans), yeast (S. cerevisiae), and thalecress (A. thaliana) registered in databases such as GeneBank: ftp://ncbi.nlm.nih.gov/genbank/qenomes/, PIR: http://www-nbrf.georget own.edu/pir/(National Biomedical Research Foundation (NBRF)), Swiss Plot: http://www.expasy.ch/sprot/sprot-top.html (Swiss Institute of Bioinformatics (SIB), European Bioinfomatics Institute (EBI)), TrEMBL (URL and the administrator are both the same as those of Swiss Plot), TrEMBLNEW (URL and the administrator are both the same as those of Swiss Plot), NAD: ftp://ftp.ddbj.nig.ac.jp (Japanese DNA databank) and the like can be used. These databases are merely an example, and any databases can be used as far as they are databases in which amino acid sequences of proteins are registered.

[0042] Step 20: Database Retrieval and Sequence Alignment

[0043] After selecting a protein having a structure to be referred to from the steric structure database (Protein Data Bank) using a database of amino acid sequences of GPCRs as a profile, alignment juxtaposition) is performed between an amino acid sequence of the selected reference protein and an amino acid sequence of the desired protein. As a structure to be referred to, the steric structure of rhodopsin (PDB ID:1F88) is preferable. Hereinafter, alignment using a database of amino acid sequences as a profile may be simply referred to as “profile alignment”.

[0044] Herein, a “profile” adds information characterizing the position of a letter in a sequence to the letter. In the present invention, this means a matrix. This matrix is a round-robin combination of amino acids, and has 20*20 elements. This matrix also has meanings of information of the degree of amino acid conservation, the degree of susceptibility, and the similarity between amino acids.

[0045] As a software for performing profile alignment regarding an amino acid inputted at the step 10, it is preferable to use, for example, PSI-BLAST (Position-specific Iterated BLAST). PSI-BLAST is programmed so as to perform profile alignment. Details of PSI-BLAST are described in “Matching a protein sequence against a collection of PSI-BLAST-constructed position-specific score matrices.” Schaffer A A, Wolf Y I, Ponting C P, Koonin E V, Aravind L and Altschul S F, Bioinformatics 1999, 12, 1000-11.

[0046] Examples of an amino acid of GPCRs used as a profile include the aforementioned GCRDb, GPCRDB, ExPASy and ORDB which are public databases. These databases are used alone or as a combination thereof. Amino acid sequences of a database used as a profile is not particularly limited, but it is more preferable to use all sequences of a database used.

[0047] PSI-BLAST for performing profile alignment can be said to be a tool having the highest performance at present, for detecting a similarity of sequences. This program extracts information only from the alignment relation with significance in a database of a profile (herein, in GCRDb), and produces a site-specific score matrix of an amino acid. Then, in the interior of a program, a sequence having a high identity with a site-specific score matrix produced in place of the sequence of the desired protein is retrieved from a database, and the site-specific matrix is sequentially renewed every time until a more significant alignment is not detected. And, the identity between a final site-specific score matrix and a reference protein is calculated as the E value.

[0048] The E value quantitatively describes a random background noise present during matching between sequences. This also shows how much degree two sequences match, has the nature to decrease exponentially relative to a score, and is useful for a method of setting a significant threshold for the result. In the present invention, when the alignment has a reliability of 98% or more in general, preferably of 99% or more, it is suitable to judge that the desired protein is GPCRs and its steric structure should be so produced. In PSI-BLAST, this corresponds to when the E value statistically has a value of 0.1 or smaller in general, preferably of 0.01 or smaller.

[0049] Considering that GPCRs share the common nature of producing a disulfide bond at one position, it is preferred to perform re-alignment of GPCRs with covering all possible combinations of the disulfide bond at the position and with placing stress on the disulfide bond (SS bond) by managing parameters using a suitable alignment software, for example, the clustalW program.

[0050] As used herein, clustalW is an alignment program which enables to change a weighing function matrix and a gap penalty depending on a position on an amino acid sequence. In the present invention, since the disulfide bond is important for the steric structure as to GPCRs whose steric structures are the subject to be constructed, it is preferred to perform re-alignment after setting the weighing function such that the cysteine residue forming the disulfide bond in the alignment calculated by PSI-BLAST would match when the cysteine residue wouldn't match.

[0051] Details of ClustalW are described in Thompson, J. D., Higgins, D. G. and Gibson, T. J. (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Research, 22: 4673-4680.

[0052] That is, in re-alignment, (i) a three-dimensional structure of a protein to be referred to is preferably, for example, the aforementioned 1F88 of PDB (Protein Data Bank) (PDB ID:1F88), provided that 1F88 has an A chain and a B chain, and their coordinates have a great deficiency and are not complete, respectively. Then, it is preferable to perform modeling of the 1F88 structure using a modeling software, for example, FAMS (Journal of Molecular Graphics and Modeling 18, 258-272, 2000) and refer to the structure. (ii) A site of interest is a region of the desired protein corresponding to two parts, first site: YFVFGPTGC (SEQ ID NO.1) and second site: GWSRYIPEGMQCSCGIDYYTPHEETINNE (SEQ ID NO.2) which contains a cysteine residue. Outside of this is a secondary structure of an α helix and a β sheet in the 1F88 protein, and should not be moved respecting the alignment of PSI-BLAST. In addition, (iii) an object is to effect the matched alignments where the desired protein corresponds to C (cysteine) of the first site and C of the second site, respectively. In the first site, a secondary structure follows immediately after C, and there is little degree of freedom for changing the alignment of PSI-BLAST.

[0053] Specific preferable procedures for re-alignment are as the following (1) to (6):

[0054] (1) Definition File of Secondary Structure Part

[0055] First, a definition file for a secondary structure part of a reference protein, for example, the second site of 1F88:GWSRYIPEGMQCSCGIDYYTPHEETNNE (SEQ ID NO.2) is produced. This is for use in re-alignment for preventing a gap from entering into a secondary structure part as much as possible. Specifically, the definition file is the following form with the SwissProt file format as follows:

	ID	IF88A STANDARD;	PRT;	28AA.
	FT	STARND	13 17
	SQ	SEQUENCE	28	AA;	000000	MW;
	XXXXXXXXXXXXXXXX CRC64;
	GWSRYIPEGM	QXSCGIDYYTPHEETNNE

[0056] (2) Excision of a Part of Interest from an Original Alignment File

[0057] Then, the original alignment file is read, and the sequence of the desired protein corresponding to the second site of the reference protein 1F88: GWSRYIPEGMQCSCGIDYYTPHEETNNE (SEQ ID NO.2) is written out (excised). As described in the above (iii), since a secondary structure follows immediately after C (cysteine) in the first site, and h there is little degree of freedom for changing the alignment of PSI-BLAST, only a sequence regarding a part corresponding to the second site is excised. Upon this, a file is produced in which a position of an excised part is recorded.

[0058] (3) Variation of a Part of Interest Corresponding to a Plurality of Cysteines (Cys)

[0059] When a part of interest of the desired protein contains a plurality of Cys, for attempting as a case study, the alignment in which Cys of the reference protein are definitely corresponded to respective Cys, only one Cys of the desired protein is left as it is, and the remaining Cys are masked with X to generate sequences of a part of interest by the number of corresponding Cys.

[0060] (4) Re-Alignment Only of a Part of Interest by an Alignment Program

[0061] Regarding short parts produced in the above (1) and (2), alignment for avoiding a gap in a secondary structure is performed paying serious attention to a SS bond. Specifically, for example, the following parameters are imparted to clustalW.

General gap opening penalty     2.0
Helix part gap opening penalty  9.0
Strand part gap opening penalty 9.0
General gap extension penalty   2.0

[0062] Elements of a mutation matrix are as follows, for example, paying serious attention to a SS bond.

Consistency of Cys-Cys          99
Consistency of Trp-Trp          16
Consistency in general residues 4
Between Glu-Gln                 3
Between Asp-Aspn                3
Between Arg-Lys                 3
Other relationship              0

[0063] (5) Incorporation of a Re-Aligned Part of Interest into a Whole Alignment

[0064] Incorporation of a re-aligned part of interest into a whole alignment is performed by putting the re-alignment of a part of interest obtained in (4) into the original broad alignment of PSI-BLAST, by referring to an excised place recorded in (2) and (3). Upon this, the parts masked with X (C of GMQCS of a second site of a reference protein and, when a part of interest of the desired protein contains a plurality of Cys, Cys situated at a place other than the relevant Cys) are returned to the original sequence.

[0065] (6) Checking of a Produced Alignment

[0066] (6-1) Checking of a SS Bond

[0067] In a process of the above (4), a sequence is given paying serious attention to a SS bond, but this is relative. Here, only the alignment having effected the of consistency of Cys-Cys is extracted.

[0068] (6-2) Checking of Uniqueness

[0069] An alignment file starting from the above (2) and (3) may be consistent with the original alignment of (2) in some cases. In addition, the file may be consistent with the already modeled alignment file in some cases. Modeling by the same alignment file leaves only a unique file in order to save an amount of calculation since a great number of modeling is required at present.

[0070] (6-3) Checking of Preservation

[0071] For caution's sake, it is checked that a sequence of the desired protein of the original alignment file and that of a reference protein are consistent except for a gap. This is for preventing incorrect data due to an operation mistake from being supplied to modeling.

[0072] By the aforementioned procedures, a re-alignment is produced in view of the common characteristic of GPCRs of making a disulfide bond at one place.

[0073] Based on the above-mentioned alignment information, construction of an atomic coordinate defining the steric structure, that is, production of the steric structure is performed. A method of producing the steric structure is not particularly limited, but for example, it is preferable to construct an atomic coordinate by a method of the following steps 30 to 50. In addition, calculation times, a constant, a cutoff value and the like described in explanation of the following steps 30 to 50 show one example of parameters which are thought to be most preferable by the present inventors, and this does not limit the scope of the present invention at all.

[0074] Step 30: Construction and Optimization of an Initial Coordinate of a Cα Atom

[0075] Receiving the results of the alignment from the step 20, information about the inserted and defective amino acid residues is obtained from a reference protein. A region having no gap in which consecutive three or more residues of amino acids are corresponding in the alignment is selected and, in this region, the same Cα atom as that of the reference protein is put into the desired protein in these residue pairs. When the Cα atom has not been obtained, a coordinate is adapted from a database of a pre-made fragment (see FIG. 2). As used herein, a Cα atom means a carbon atom which is a center of a skeleton of each amino acid. A Cβatom means a carbon atom binding to a side chain side of a Cα atom. In addition, a C atom means a carbon atom of a carbonyl group.

[0076] Step 31: Construction of a Cα Atom by a Simulated Annealing Method

[0077] The Cα atom produced in the above-mentioned step 30 is optimized using a function constructed of coordinates of a reference protein using a process of simulated annealing. This objective function is as described in the following equation (1):

U Cα =U len +U ang +U pos +U vdw   (1).

[0078] Herein, Ulen relates to a distance between Cα atoms of a pair of adjacent residue and Cys residue on a sequence, and is set as in the following equation (2): 1$\begin{array}{cc}{U}_{\mathrm{len}}=K_l\sum _i{\left(D_{i,i+1}-3.8\right)}^2+K_{\mathrm{ss}}\sum _i{\left(D_i^{\mathrm{ss}}-5.4\right)}^2.& \left(2\right)\end{array}$

[0079] Herein, Di, i+1 is a distance between Cαs of a residue i and a residue i+1. DISS is a distance between pairs of Cys residues forming a disulfide bond. K1 and KSS are constants, being set at 2 and 5, respectively.

[0080] Uang is a function as a binding angle of a Cα atom, and is as in the following equation (3): 2$\begin{array}{cc}{U}_{\mathrm{ang}}=K_a\sum _i{\left({\theta }_i-{\theta }_0\right)}^2& \left(3\right)\end{array}$

[0081] Herein, θi (rad) is an angle of an ith, i+1th or i+2th residue Cα atom. θ0 is set at (100/180)·π(rad) from the X-ray structure. Ka is a constant and is set at 1.

[0082] Upos is a function regarding a position of a Cα atom, and is as in the following equation (4): 3$\begin{array}{cc}{U}_{\mathrm{pos}}=K_{\mathrm{pos}}\sum _i\frac{1}{M_i}{\&LeftDoubleBracketingBar;x_i-⟨w_i{x}_i⟩\&RightDoubleBracketingBar;}^2.& \left(4\right)\end{array}$

[0083] Herein, ∥·∥ means norm, and Mi is an average distance between Cα atoms situated at structurally equivalent positions on an alignment based on a structure. When a value of Mi can not be obtained for a residue i, a value of Mi is set at 10. Herein, it is an average coordinate of a Cα atom, and is as in the following equation (5): 4$\begin{array}{cc}⟨w_i{x}_i⟩=\frac{1}{W}\sum _j{w}_i^j{x}_i^j.& \left(5\right)\end{array}$

[0084] Herein, Xji is an atomic coordinate of Cα of an ith residue of a jth reference protein. Herein, wji is a weight of an ith residue of a jth reference protein. This weight is an important parameter for determining an approximate shape of the desired protein, and this is determined by a local value in the spatial vicinity within 12 Å of an attentioned part called Local Space Homology (LSH) (see FIG. 3). A correlation between LSH and a ratio of residue pairs present in a part in which a structure is well conserved (SCRs: Structural Conserved Regions) is very high as shown in FIG. 4. This means that, when the LSH value is high, a position of a Cα atom is statistically within 1.0 Å as compared with a reference protein structure.

[0085] Uvdw is as in the following equation (6): 5$\begin{array}{cc}{U}_{\mathrm{vdw}}=K_{\mathrm{vdw}}\sum _{i,j\left(>i+2\right)}\left\{{\left(\frac{3.8}{D_{i,j}}\right)}^{12}-{\left(\frac{3.8}{D_{i,j}}\right)}^6\right\}.& \left(6\right)\end{array}$

[0086] Herein, Kvdw is set at 0.01 (Di,j<3.2 Å) and 0.001(Di,j>3.2 Å), and has a cutoff value of 6 Å.

[0087] A Cα atom is optimized using a simulated annealing method according to the equation (1). At this optimization stage, perturbation of a Cα atom is set to be within 1.0 Å. In addition, this annealing stage is calculated every 100 times regarding all Cα atoms. And, a parameter corresponding to a temperature is reduced from 25 by 0.01 every 0.5 time, and the parameter is constant thereafter.

[0088] These great two stages, obtaining of structural information and construction of a Cα atom are repeated 10 times, and a coordinate of a Cα atom having the minimum objective function value is calculated as an optimum solution.

[0089] Step 40: Construction and Optimization of a Main Chain Atomic Coordinate

[0090] Other atoms of a main chain are added to an atomic coordinate of Cα at the step 30, and an objective function is minimized by a simulated annealing method. First, steric overlapping of Cα atoms is performed, and residues having a distance between Cα atoms of 2.5 Å or smaller are taken. Atomic coordinates of a main chain except for Cα are obtained from a coordinate of a reference protein so that a distance between Cα atoms becomes minimum and, thus, a model structure is obtained.

[0091] When there is no corresponding residue in a reference protein, atomic coordinates of a main chain are produced from a corresponding protein fragment of four residues in a database. During this process, main chain atoms of a residue i are selected from a residue having the minimum rmsd value between i−1th to i+2th Cα atoms. Upon this, at a N-terminal residue, a range of overlapping of Cα atom coordinates is from ith to i+3th and, at a C-terminal residue and a residue one before, the ranges are from i−3th to ith and from i−2th to i+1th, similarly.

[0092] Based on an objective function of main chain atoms, optimization is performed by a simulated annealing method.

[0093] An objective function is as in the following equation (7):

U main =U bond +U ang +U non-bond +U ss +U pos +U tor +U chi +U hydr   (7).

[0094] Ubond is as in the following equation (8): 6$\begin{array}{cc}{U}_{\mathrm{bond}}=K_b\sum _i{\left(b_i-b_i^0\right)}^2.& \left(8\right)\end{array}$

[0095] Herein, bi0 is a standard bond length, and is different depending on a kind of each chemical bond. Kb is a constant, and is set at 225.

[0096] Uang is a function of a bonding angle, and is as in the following equation (9): 7$\begin{array}{cc}{U}_{\mathrm{ang}}=K_a\sum _i{\left({\theta }_i-{\theta }_i^0\right)}^2.& \left(9\right)\end{array}$

[0097] Herein, θi is an ith bonding angle, and is different depending on a kind of a chemical bond. Ka is a constant, and is set at 45.

[0098] Unon-bond is a function of the non-bond interaction, and is as in the following equation (10): 8$\begin{array}{cc}{U}_{\mathrm{non}-\mathrm{bond}}=K_{\mathrm{non}}\sum _{i,j}{\epsilon }_{i,j}\left\{{\left(\frac{r_{i,j}^{*}}{r_{i,j}}\right)}^{12}-2{\left(\frac{r_{i,j}^{*}}{r_{i,j}}\right)}^6\right\}.& \left(10\right)\end{array}$

[0099] Herein, εi,j and ri,j * are constants, and are different depending on a kind of an atom.

[0100] Knon is a constant and is set at 0.25, and has cutoff of 8 Å.

[0101] USS is a function of a disulfide bond produced by the Cys residue, and is as in the following equation (11): 9$\begin{array}{cc}{U}_{\mathrm{ss}}=\sum _i\left\{{K_{C\alpha }^{\mathrm{ss}}\left(D_i^{C\alpha }-5.4\right)}^2+{K_{C\beta }^{\mathrm{ss}}\left(D_i^{C\beta }-3.8\right)}^2\right\}.& \left(11\right)\end{array}$

[0102] Herein, KSSCα and KSSCβ are constants, and are set at 7.5.

[0103] Upos is a function regarding a position of an atom, and is as in the following equation (12): 10$\begin{array}{cc}{U}_{\mathrm{pos}}=K_{\mathrm{pos}}\sum _i\frac{1}{M_i}{\&LeftDoubleBracketingBar;x_i-⟨w_i{x}_i⟩\&RightDoubleBracketingBar;}^2.& \left(12\right)\end{array}$

[0104] Herein, <WiXi> is given as in the following equation (13): 11$\begin{array}{cc}⟨w_i{x}_i⟩=\frac{1}{W}\sum _{j}w{}_i{}^{j}x_i^j.& \left(13\right)\end{array}$

[0105] <WiXi> in the equation (12) is obtained from overlapping of structures between the desired protein and the reference protein.

[0106] Kpos is a constant, and is set at 0.3.

[0107] Utor is related to a helix angle of a main chain, and is as in the following equation (14): 12$\begin{array}{cc}{U}_{\mathrm{tor}}=K_t\sum _i\sqrt{{\left({\phi }_i-{\phi }_i^0\right)}^2+{\left({\psi }_i-{\psi }_i^0\right)}^2}+K_{\omega }\sum _i{\left({\omega }_i-{\omega }_i^0\right)}^2.& \left(14\right)\end{array}$

[0108] Herein, φi0 and φi0 are let to be nearest helix angles θi and (φi on the Ramachandran map. In addition, ωi0 is let to be 0 and, only in the case of cis-Pro residue, is let to be π(radian). Kt and Kω are constants, and are let to be 10 and 50, respectively.

[0109] Uchi is related to chirality of Cα, and is as in the following equation (15): 13$\begin{array}{cc}{U}_{\mathrm{chi}}=K_{\mathrm{chi}}\sum _i{\left({\tau }_i+\frac{2}{3}\pi \right)}^2.& \left(15\right)\end{array}$

[0110] Herein, πi is a helix angle defined by N—Cα-C β-C and Kchi is let to be 50.

[0111] Uhydr is related to a hydrogen bond of a main chain conserved in homologous proteins, and is determined as in the following equation (16): 14$\begin{array}{cc}{U}_{\mathrm{hydr}}=K_{\mathrm{hydr}}\sum _{i,j}{\left(D_{i,j}^{N\text{-}O}-2.9\right)}^2.& \left(16\right)\end{array}$

[0112] A hydrogen bond is set when a distance between a N atom and a O atom is 2.9±0.5 Å.

[0113] Upon determining whether a hydrogen bond is present in a reference protein, when it is recognized that 75% or more of reference proteins are present, it is determined that a hydrogen bond is present. Khydr is a constant, and is let to be 0.6.

[0114] Optimization of main chain atoms including Cβ is performed by simulated annealing. During this annealing process, perturbation of atoms of a main chain and Cβ is let to be within 1.0 Å relative to initial positions. This annealing stage is performed 200 times on atoms of a main chain and Cβ. A parameter corresponding to a temperature starts from 50 or 25, is let to be 0.5-fold every time, and this is continued until 0.01 and, thereafter, is let to be a constant value.

[0115] In order to widely perform sampling of a steric arrangement of a main chain, according to the method of the present invention, the above-mentioned method is performed 6 times, and atomic coordinates of a main chain having the minimum objective function value are adopted as an optimum solution. And, a parameter corresponding to a temperature starts from 50 at first two times, and starts from 25 from third time.

[0116] Step 50: Construction and Optimization of Side Chain Atomic Coordinates

[0117] Construction of a side chain is roughly classified into two stages: “construction of a side chain at a structure conserved part” (step 51) and “construction of a total side chain” (step 52).

[0118] Step 51: Construction of a Side Chain at a Structure Conserved Part

[0119] Regarding calculated main chain atoms, a helix angle of a side chain is obtained from homologous proteins using the method in the previous study. Details of this method are described in “The role of played by environmental residues in side-chain torsional angles within homologous families of proteins: A new method of side chain modeling. “Ogata K and Umeyama H, Prot. Struct. Funct. Genet. 1998, 31, 255-369.

[0120] A ratio of side chains conserved in homologous proteins is calculated in this method, and, based on this information, modeling of a side chain is performed. Atomic coordinates of a side chain at a conserved site of a side chain are placed on main chain atoms. For example, when a χ1 angle of an arginine residue is conserved in homologous proteins, a coordinate of a Cγ atom can be placed and, when χ1 and χ2 angles are conserved in a Phe residue, all side chain atoms can be placed. A process of optimization of simulated annealing using the equation (7) is such that only atoms of a main chain and Cβ are performed and perturbation of atoms is within 1.0 Å. This stage of annealing atoms of a main chain and Cβ are performed 200 times. And, a parameter corresponding to a temperature starts from 25, is let to be 0.5-fold every time, and is reduced until 0.01. Unon-bond in the equation (7) is performed on main chain atoms and partially produced side chain atoms. Upon this, coordinates of side chain atoms are rendered conserved during an optimization process.

[0121] Mi and a pair of N—O in a hydrogen bond which are information of a structure are used in an optimization process. In order to obtain arrangement of main chain atoms, the above-mentioned process is repeated three times, and coordinates of minimum main chain atoms of an objective function are adopted as a calculated structure.

[0122] Step 52: Construction of a Total Side Chain

[0123] Construction of a side chain is performed under fixed main chain and Cβ atoms. This is performed by the study results disclosed in the above-mentioned Ogata K and Umeyama H, Prot. Struct. Funct. Genet. 1998, 31, 255-369 and, by using this, a precise model can be given in a short time. Then, a main chain structure is optimized by a Monte Carlo method at a low temperature, a temperature is set at 0.001 and, by using an objective function Unon-bond of the equation (7), calculation is performed at all main chain and side chain atoms. And, during optimization of N, Cα, C and Cβ atoms, coordinates of a side chain are re-arranged so as to retain a helix angle of a side chain at the optimized state. Perturbation of atoms is let to be within 0.5 Å. Then, a side chain is deleted, and the above-mentioned construction of a side chain is repeated. This process is repeated until collision of 2.4 Å atoms is diminished, and a helix angle of N—Cα-Cβ—C becomes within a range of −120±15°.

[0124] Step 60: Construction of a Final Structure

[0125] Thus, by performing steps 10 to 50, atomic coordinates defining the steric structure of GPCRs can be obtained. The resulting atomic coordinates can be appropriately used for designing drug molecules such as medicines and agricultural chemicals described later, such as by producing the steric structure model of GPCR by a suitable program which can display the steric structure, for example, BIOCES (manufactured by NEC Corporation) and the like, and by assessing this and the bonding state with various ligands (drug molecules).

[0126] Each step regarding the aforementioned construction of the steric structure can be performed by using modeling software “FAMS” developed by the present inventors. Thereby, the steric structure can be constructed with excellent precision. Herein, details of FAMS are described in Koji Ogata and Hideaki Umeyama, Journal of Molecular Graphics and Modeling 18, 258-272, 2000.

[0127] Thus, atomic coordinates defining the steric structure of an arbitrary 7-transmembrane G-protein-coupled receptor can be obtained. Herein, an atomic coordinate describes the steric structure on a three-dimensional space. That is a relative distance in mutually perpendicular three directions letting a point on a space to be an origin, and is a vector consisting of three numerals per one atom except for a hydrogen atom present in a protein.

[0128] By containment of the resulting atomic coordinates in a suitable recording medium in a prescribed computer utilizable format, a database of the steric structure of a 7-transmembrane G-protein-coupled receptor can be constructed. The database of the present invention preferably contains, for example, information of alignment between a reference protein and a desired protein together with the above-mentioned atomic coordinates. In addition, in the present invention, a database means a computer system that writes the above-mentioned atomic coordinates in a suitable recording medium, and performs retrieval according to a prescribed program. Herein, examples of a suitable recording medium include magnetic media such as floppy disc, hard disk, magnetic tape and the like; optical disc, semiconductor memory and the like such as CD-ROM, MO, CD-R, CD-RW and the like.

[0129] According to another aspect of the present invention, there is provided a method for presuming the function of a protein, which comprises selecting the steric structure to be referred to from the known steric structure of a 7-transmembrane G-protein-coupled receptor using an amino acid sequence database of the receptor as a profile, performing alignment of a desired protein having the unknown function and, when the steric structure of the desired protein can be produced, judging that the desired protein is a 7-transmembrane G-protein-coupled receptor.

[0130] In the present invention, the steric structure of the desired protein having the unknown function is constructed by the above-mentioned method and, when construction is possible, it is judged that the desired protein is GPCRs. In the present invention, preferably, alignment is performed by selecting the steric structure to be referred to from a database of the known steric structure of a G-protein-coupled receptor, and aligning an amino acid sequence of the selected reference protein and an amino acid sequence of the desired protein, an amino acid sequence database used as a profile is selected from the group consisting of GCRDb, GPCRDB, ExPASy or ORDP and, when alignment has reliability of 98% or more, it is determined that the steric structure of the desired protein can be produced. The thus obtained atomic coordinates defining the steric structure of GPCRs are included in the database of the present invention.

[0131] Then, a method for designing a drug molecule using an atomic coordinate obtained by the present method will be described.

[0132] By using all or a part of atomic coordinates defining the steric structure (hereinafter, this is abbreviated as “steric structure coordinate”) of GPCR which is a target of a drug molecule obtained by the above-mentioned method (hereinafter, this is referred to as “target GPCR”), or a database in which they are recorded, or atomic coordinates contained in a recording medium, it is possible to perform identification, retrieval, assessment or design of a drug molecule which interacts with the target GPCR (antagonist or agonist).

[0133] Identification, retrieval, assessment or design of a drug molecule is performed based on the presence or the absence and a degree of interaction between the steric structure coordinate of GPCR obtained by the present method and the steric structure coordinate of a drug molecule, in a computer in which a suitable program that can design a drug molecule operates. In the present specification, identification, retrieval, assessment, design and the like of a drug molecule is simply referred to as drug molecule design.

[0134] A computer used upon molecule design based on interaction between the steric structure coordinate of GPCR and the steric structure coordinate of a drug candidate molecule is not particularly limited as far as it is a computer that is adjusted so as to operate a suitable program. In addition, a recording medium of a computer is not particularly limited. Examples of a program used in molecular design include a computer program Insight II and the like manufactured by Molecular Simulation. In particular, by using programs such as Ludi and DOCK which are especially produced for this purpose alone or in a combination thereof, a drug molecule can be more easily identified, retrieved, assessed, or designed. In addition, assessment of docking between the steric structure coordinate of GPCR and a drug molecule can be performed, for example, by using BIOCES (version 3.10) manufactured by NEC Corporation.

[0135] Herein, whether a drug molecule is a known drug molecule or a newly synthesized drug molecule having a novel chemical structure, any drug molecules can be used in the present method as far as the steric structure thereof can be obtained. The steric structure coordinate of a drug molecule may be a coordinate obtained by any method such as X-ray crystal analysis, modeling and the like. Determined steric structure coordinates can be obtained from a suitable database, for example, CCDC (Cambridge Crystallographic Data Centre: http://www.ccdc.cam.ac.uk/) and PDB (Protein Data Bank: http://www.rcsb.org/pdb/).

[0136] Further, a drug molecule can be designed also by the method described in Japanese Patent Application Laid-Open 2000-178209. Likewise, by using the steric structure coordinate of GPCR obtained by the present method, it becomes possible to design a drug molecule by a computer, provided that the molecular designing method of the present invention is not limited to methods using these programs and procedures.

[0137] There are usually conceptionally two stages in design of a drug molecule. The first stage is to find out a lead compound, and the next stage is to optimize the lead compound. Any of the stages can be performed by using the steric structure coordinate of target GPCR by a known per se method. Thereby, an optimum medicine and agricultural chemical candidate molecule can be obtained. The thus obtained drug molecule is included in the scope of the present invention.

[0138] Medicine and agricultural chemical candidate molecules identified, retrieved, assessed or designed by the above-mentioned method can be obtained, for example, by a known per se chemical synthesizing method depending on the natures of the molecules. However, a drug molecule may be a natural compound or a synthetic compound, or may be a high-molecular compound or a low-molecular compound. The obtained medicine and agricultural chemical candidate molecules are further examined for their activity and safety by a known per se method, or by an in vitro or in vivo pharmacological or physiological test, and medicine and agricultural chemical candidate molecules having the desired nature, that is, the activity and the safety necessary as a medicine or an agricultural chemical are selected (screening), whereby, molecules which can be actually applied as a medicine or an agricultural chemical can be obtained.

[0139] Medicines or agricultural chemicals, for example, medicine molecules selected by the above-mentioned screening method can be administered alone as they are to a patient with disease which is a subject of treatment, but can be also administered by mixing 2 or more active ingredients. In addition, it is preferable to prepare the substance into a pharmaceutical composition using a pharmacologically acceptable additive for pharmacy and administer the composition. For example, the substance may be used orally as sugar-coated tablets, capsules, granules, fine granules, powders, pills, microcapsules, liposome preparations, troches, sublingual agents, solutions, elixirs, emulsions, suspensions or the like, or parenterally as injectables prepared as sterile aqueous solutions or oily solutions, suppositories, ointments, patches or the like, as necessary. These may be prepared, for example, by kneading the substance together with physiologically acceptable carrier, flavor, excipient, vehicle, preservative, stabilizer and binder in a unit dosage form required for implementing generally recognized preparations, by using the well-known methods in the art such as filling and compression. An amount of an active ingredient in these pharmaceutical compositions allows a suitable dose in an indicated range to be obtained.

[0140] When agricultural chemical molecules are actually used as an agricultural chemical, they are used by mixing with agriculturally or horticulturally acceptable carrier or diluent, additive and supplementing agent by the known method, and preparing into preparation forms (composition) which are usually used as an agricultural chemical, for example, powders, granules, hydrated agents, emulsions, water-soluble agents, flowables and the like.

EXAMPLES

[0141] The present invention will be further specifically explained by way of Examples below, but the following Examples should be regarded as helping obtain specific recognition of the present invention, and do not limit the scope of the present invention whatsoever.

Example 1

Construction of the Steric Structure of a β2 Adrenaline Receptor

[0142] According to the method described in detail in the aforementioned embodiments of the present invention, the steric structure model of a human-derived β2 adrenaline receptor was constructed, and a position into which an agonist (isoproterenol) is placed and a position into which an antagonist (propranolol) is placed were compared as follows:

[0143] Construction of the steric structure model was performed using workstation manufactured by NEC Corporation (Model: Express5800/120Rc-2, CPU:PentiumIII 933 MHz×2, OS: Red Hat Linux 6.2J, memory: 1024 Mbytes). An amino acid sequence of the desired β2 adrenalin receptor was obtained from PIR; http://www-nbrf.georgetown.edu/pir/ ID:QRHUB2. The amino acid sequence is shown in SEQ ID NO:3.

[0144] Letting an amino acid sequence of this β2 adrenaline receptor to be a sequence of the desired protein, alignment by PSI-BLAST was performed. Upon this, the full sequence 892 of GCRDb; http://www.gcrdb.uthscsa.edu/ was used as a motif profile. And, by using a structure of a B chain of PDB (http://www.rcsb.org/pdb/) ID:IF88 (rhodopsin) as the steric structure of a reference protein, alignment to this B chain was obtained. There was a dimer having the approximately same steric structure composed of an A chain and a B chain in a crystal lattice of 1F88 (rhodopsin), and the B chain was used as a structure to be referred to. In addition, there was a great defect in coordinates of the A chain and the B chain, respectively, being not complete. Modeling of the 1F88 structure was performed using modeling software “FAMS”, and that structure was referred to. An amino acid sequence of this 1F88 (rhodopsin) B chain is shown in SEQ ID NO.4.

[0145] As a result of the above-mentioned alignment, the E value calculated by PSI-BLAST was 1e-144 (minus 144 power of 10).

[0146] As described above, re-alignment was performed using a program of clutalW, paying serious attention to a disulfide bond. The resulting alignment information is shown in FIG. 5. In FIG. 5, an upper sequence denotes QRHUB2 (β adrenaline receptor), and a lower sequence denotes 1F88 (rhodopsin). As apparent from FIG. 5, homology between QRHUB2 and 1F88 was 19.6%.

[0147] Based on the thus obtained alignment information, using the modeling software “FAMS” developed by the present inventors, construction and optimization of an initial coordinate of a Cα atom, construction and optimization of a main chain atom coordinate, and construction of a total side chain were performed as in the above-mentioned steps 30 to 50, to obtain atomic coordinates defining the steric structure of QRHUB2.

[0148] The resulting atomic coordinates are shown in Table 1. Table 1 describes atomic coordinates according to the generally used format of Protein Data Bank (PDB) which is a method of expressing the steric structure (three-dimensional structure) coordinate of a protein. Table 1 describes a three-dimensional coordinate of each atom at 30th line and thereafter except the last line. ATOM on a first column indicates that this row is a row of an atomic coordinate, a second column denotes an order of the atom, a third column denotes discrimination of atoms in an amino acid residue, a fourth column denotes an amino acid residue, a fifth column denotes an amino acid number corresponding to SEQ ID No.3 (corresponding to amino acid numbers 10 to 238, 264 to 363 in SEQ ID No.3), sixth, seventh and eighth columns denote a coordinate of the atom (in an order of a-axis, b-axis and c-axis directions, in Å unit), a ninth column denotes a rate of occupation of the atom, and a tenth column denotes a temperature factor of the atom. The last line denotes the last line in this table. A part of amino acid numbers 239 to 263 in SEQ ID No.3 is an insertion sequence part for which a structure to be referred to can not be obtained. In addition, since a rate of occupation and a temperature factor of an atom can not be calculated, “0.00” are placed into ninth and tenth columns.

TABLE 1
Atomic coordinate of β2 adrenaline receptor
HEADER    mode    05 SEP. 2000 mode    AUTHOR    FAMS
SEQRES	1	329	PHE LEU LEU ALA PRO ASN ARG SER HIS ALA PRO ASP HIS
SEQRES	2	329	ASP VAL THR GLN GLN ARG ASP GLU VAL TRP VAL VAL GLY
SEQRES	3	329	MET GLY ILE VAL MET SER LEU ILE VAL LEU ALA ILE VAL
SEQRES	4	329	PHE GLY ASN VAL LEU VAL ILE THR ALA ILE ALA LYS PHE
SEQRES	5	329	GLU ARG LEU GLN THR VAL THR ASN TYR PHE ILE THR SER
SEQRES	6	329	LEU ALA CYS ALA ASP LEU VAL MET GLY LED ALA VAL VAL
SEQRES	7	329	PRO PHE GLY ALA ALA HIS ILE LEU MET LYS MET TRP THR
SEQRES	8	329	PHE GLY ASN PHE TRP CYS GLU PHE TRP THR SER ILE ASP
SEQRES	9	329	VAL LEU CYS VAL THR ALA SER ILE GLU THR LEU CYS VAL
SEQRES	10	329	ILE ALA VAL ASP ARG TYR PHE ALA ILE THR SER PRO PHE
SEQRES	11	329	LYS TYR GLN SER LEU LEU THR LYS ASN LYS ALA ARG VAL
SEQRES	12	329	ILE ILE LEU MET VAL TRP ILE VAL SER GLY LEU THR SER
SEQRES	13	329	PHE LEU PRO ILE GLN MET HIS TRP TYR ARG ALA THR HIS
SEQRES	14	329	GLN GLU ALA ILE ASN CYS TYR ALA ASN GLU THR CYS CYS
SEQRES	15	329	ASP PHE PHE THR ASN GLN ALA TYR ALA ILE ALA SER SER
SEQRES	16	329	ILE VAL SER PHE TYR VAL PRO LEU VAL ILE MET VAL PHE
SEQRES	17	329	VAL TYR SER ARG VAL PHE GLN GLU ALA LYS ARG GLN LEU
SEQRES	18	329	GLN LYS ILE ASP LYS SER GLU GLY PHE CYS LEU LYS GLU
SEQRES	19	329	HIS LYS ALA LEU LYS THR LEU GLY ILE ILE MET GLY THR
SEQRES	20	329	PHE THR LEU CYS TRP LEU PRO PHE PHE ILE VAL ASN ILE
SEQRES	21	329	VAL HIS VAL ILE GLN ASP ASN LEU ILE ARG LYS GLU VAL
SEQRES	22	329	TYR ILE LEU LEU ASN TRP ILE GLY TYR VAL ASN SER GLY
SEQRES	23	329	PHE ASN PRO LEU ILE TYR CYS ARG SER PRO ASP PHE ARG
SEQRES	24	329	ILE ALA PHE GLN GLU LEU LEU CYS LEU ARG ARG SER SER
SEQRES	25	329	LEU LYS ALA TYR GLY ASN GLY TYR SER SER ASN GLY ASN
SEQRES	26	329	THR GLY GLU GLN
SSBOND  1    CYS  97    CYS  175
ATOM	1	N	PHE	1	43.073	0.386	−20.078	0.00	0.00
ATOM	2	CA	PHE	1	41.753	−0.201	−20.163	0.00	0.00
ATOM	3	C	PHE	1	41.414	−0.419	−21.636	0.00	0.00
ATOM	4	O	PHE	1	41.225	0.577	−22.359	0.00	0.00
ATOM	5	CB	PHE	1	40.766	0.713	−19.432	0.00	0.00
ATOM	6	CG	PHE	1	39.626	−0.008	−18.812	0.00	0.00
ATOM	7	CD1	PHE	1	38.307	0.247	−19.185	0.00	0.00
ATOM	8	CD2	PHE	1	39.869	−0.865	−17.741	0.00	0.00
ATOM	9	CE1	PHE	1	37.253	−0.332	−18.502	0.00	0.00
ATOM	10	CE2	PHE	1	38.817	−1.448	−17.050	0.00	0.00
ATOM	11	CZ	PHE	1	37.506	−1.180	−17.431	0.00	0.00
ATOM	12	N	LEU	2	40.955	−1.616	−21.879	0.00	0.00
ATOM	13	CA	LEU	2	40.600	−2.066	−23.178	0.00	0.00
ATOM	14	C	LEU	2	39.522	−1.130	−23.782	0.00	0.00
ATOM	15	O	LEU	2	38.456	−0.903	−23.189	0.00	0.00
ATOM	16	CB	LEU	2	40.177	−3.558	−22.990	0.00	0.00
ATOM	17	CG	LEU	2	40.585	−4.520	−24.108	0.00	0.00
ATOM	18	CD1	LEU	2	39.574	−5.662	−24.157	0.00	0.00
ATOM	19	CD2	LEU	2	40.661	−3.884	−25.485	0.00	0.00
ATOM	20	N	LEU	3	39.652	−1.018	−25.078	0.00	0.00
ATOM	21	CA	LEU	3	38.777	−0.250	−25.976	0.00	0.00
ATOM	22	C	LEU	3	37.698	−1.167	−26.669	0.00	0.00
ATOM	23	O	LEU	3	37.353	−0.941	−27.843	0.00	0.00
ATOM	24	CB	LEU	3	39.720	0.447	−26.998	0.00	0.00
ATOM	25	CG	LEU	3	39.142	1.650	−27.822	0.00	0.00
ATOM	26	CD1	LEU	3	39.404	1.543	−29.337	0.00	0.00
ATOM	27	CD2	LEU	3	37.641	1.886	−27.688	0.00	0.00
ATOM	28	N	ALA	4	37.400	−2.343	−26.054	0.00	0.00
ATOM	29	CA	ALA	4	36.477	−3.272	−26.597	0.00	0.00
ATOM	30	C	ALA	4	35.117	−2.525	−26.707	0.00	0.00
ATOM	31	O	ALA	4	34.699	−2.282	−27.891	0.00	0.00
ATOM	32	CB	ALA	4	36.410	−4.512	−25.679	0.00	0.00
ATOM	33	N	PRO	5	34.358	−2.111	−25.644	0.00	0.00
ATOM	34	CA	PRO	5	33.084	−1.488	−25.861	0.00	0.00
ATOM	35	C	PRO	5	33.311	−0.006	−26.324	0.00	0.00
ATOM	36	O	PRO	5	32.302	0.657	−26.536	0.00	0.00
ATOM	37	CB	PRO	5	32.239	−1.431	−24.582	0.00	0.00
ATOM	38	CG	PRO	5	33.171	−2.182	−23.598	0.00	0.00
ATOM	39	CD	PRO	5	34.594	−2.101	−24.154	0.00	0.00
ATOM	40	N	ASN	6	34.520	0.564	−26.479	0.00	0.00
ATOM	41	CA	ASN	6	34.653	1.953	−27.011	0.00	0.00
ATOM	42	C	ASN	6	34.068	3.074	−26.086	0.00	0.00
ATOM	43	O	ASN	6	33.839	4.201	−26.540	0.00	0.00
ATOM	44	CB	ASN	6	34.000	2.124	−28.366	0.00	0.00
ATOM	45	CG	ASN	6	33.779	1.138	−29.437	0.00	0.00
ATOM	46	OD1	ASN	6	32.786	1.165	−30.245	0.00	0.00
ATOM	47	ND2	ASN	6	34.585	0.044	−29.583	0.00	0.00
ATOM	48	N	ARG	7	34.407	2.920	−24.839	0.00	0.00
ATOM	49	CA	ARG	7	34.120	3.835	−23.733	0.00	0.00
ATOM	50	C	ARG	7	35.410	4.653	−23.343	0.00	0.00
ATOM	51	O	ARG	7	35.233	5.799	−22.940	0.00	0.00
ATOM	52	CB	ARG	7	33.580	3.010	−22.551	0.00	0.00
ATOM	53	CG	ARG	7	33.328	3.924	−21.350	0.00	0.00
ATOM	54	CD	ARG	7	32.202	4.900	−21.560	0.00	0.00
ATOM	55	NE	ARG	7	30.908	4.251	−21.675	0.00	0.00
ATOM	56	CZ	ARG	7	29.740	4.902	−21.547	0.00	0.00
ATOM	57	NH1	ARG	7	29.675	6.216	−21.315	0.00	0.00
ATOM	58	NH2	ARG	7	28.609	4.208	−21.638	0.00	0.00
ATOM	59	N	SER	8	36.654	4.190	−23.656	0.00	0.00
ATOM	60	CA	SER	8	37.904	4.876	−23.437	0.00	0.00
ATOM	61	C	SER	8	37.932	6.234	−24.183	0.00	0.00
ATOM	62	O	SER	8	37.958	6.283	−25.421	0.00	0.00
ATOM	63	CB	SER	8	39.089	3.986	−23.904	0.00	0.00
ATOM	64	OG	SER	8	40.409	4.526	−23.618	0.00	0.00
ATOM	65	N	HIS	9	38.165	7.300	−23.402	0.00	0.00
ATOM	66	CA	HIS	9	38.329	8.653	−23.973	0.00	0.00
ATOM	67	C	HIS	9	39.745	9.163	−23.460	0.00	0.00
ATOM	68	O	HIS	9	39.917	9.246	−22.240	0.00	0.00
ATOM	69	CB	HIS	9	37.146	9.564	−23.685	0.00	0.00
ATOM	70	CG	HIS	9	37.047	10.796	−24.493	0.00	0.00
ATOM	71	ND1	HIS	9	36.064	11.704	−24.557	0.00	0.00
ATOM	72	CD2	HIS	9	37.990	11.194	−25.416	0.00	0.00
ATOM	73	CE1	HIS	9	36.376	12.602	−25.463	0.00	0.00
ATOM	74	NE2	HIS	9	37.544	12.281	−25.972	0.00	0.00
ATOM	75	N	ALA	10	40.613	9.714	−24.336	0.00	0.00
ATOM	76	CA	ALA	10	41.978	10.099	−23.914	0.00	0.00
ATOM	77	C	ALA	10	41.939	10.930	−22.615	0.00	0.00
ATOM	78	O	ALA	10	41.034	11.817	−22.560	0.00	0.00
ATOM	79	CB	ALA	10	42.624	10.929	−25.068	0.00	0.00
ATOM	80	N	PRO	11	42.636	10.598	−21.488	0.00	0.00
ATOM	81	CA	PRO	11	42.443	11.430	−20.339	0.00	0.00
ATOM	82	C	PRO	11	42.462	12.969	−20.636	0.00	0.00
ATOM	83	O	PRO	11	41.726	13.657	−19.918	0.00	0.00
ATOM	84	CB	PRO	11	43.351	11.045	−19.192	0.00	0.00
ATOM	85	CG	PRO	11	44.598	10.601	−20.045	0.00	0.00
ATOM	86	CD	PRO	11	44.017	9.941	−21.287	0.00	0.00
ATOM	87	N	ASP	12	43.185	13.472	−21.606	0.00	0.00
ATOM	88	CA	ASP	12	43.119	14.896	−21.854	0.00	0.00
ATOM	89	C	ASP	12	41.647	15.423	−22.107	0.00	0.00
ATOM	90	O	ASP	12	41.238	16.320	−21.367	0.00	0.00
ATOM	91	CB	ASP	12	44.036	15.208	−23.051	0.00	0.00
ATOM	92	CG	ASP	12	45.467	14.821	−22.771	0.00	0.00
ATOM	93	OD1	ASP	12	46.035	14.195	−23.582	0.00	0.00
ATOM	94	OD2	ASP	12	45.951	15.218	−21.705	0.00	0.00
ATOM	95	N	HIS	13	40.922	14.971	−23.139	0.00	0.00
ATOM	96	CA	HIS	13	39.565	15.432	−23.459	0.00	0.00
ATOM	97	C	HIS	13	38.527	15.140	−22.337	0.00	0.00
ATOM	98	O	HIS	13	37.979	16.107	−21.805	0.00	0.00
ATOM	99	CB	HIS	13	39.144	14.813	−24.774	0.00	0.00
ATOM	100	CG	HIS	13	39.899	15.091	−25.990	0.00	0.00
ATOM	101	ND1	HIS	13	39.346	15.454	−27.190	0.00	0.00
ATOM	102	CD2	HIS	13	41.238	15.064	−26.209	0.00	0.00
ATOM	103	CE1	HIS	13	40.314	15.638	−28.078	0.00	0.00
ATOM	104	NE2	HIS	13	41.467	15.402	−27.511	0.00	0.00
ATOM	105	N	ASP	14	38.258	13.862	−21.957	0.00	0.00
ATOM	106	CA	ASP	14	37.253	13.533	−20.930	0.00	0.00
ATOM	107	C	ASP	14	37.791	12.698	−19.741	0.00	0.00
ATOM	108	O	ASP	14	38.666	11.838	−19.929	0.00	0.00
ATOM	109	CB	ASP	14	35.903	13.055	−21.485	0.00	0.00
ATOM	110	CG	ASP	14	35.199	13.882	−22.507	0.00	0.00
ATOM	111	OD1	ASP	14	34.360	13.247	−23.276	0.00	0.00
ATOM	112	OD2	ASP	14	35.353	15.131	−22.637	0.00	0.00
ATOM	113	N	VAL	15	36.898	12.656	−18.710	0.00	0.00
ATOM	114	CA	VAL	15	37.136	12.036	−17.475	0.00	0.00
ATOM	115	C	VAL	15	37.399	10.517	−17.579	0.00	0.00
ATOM	116	O	VAL	15	36.947	9.837	−18.475	0.00	0.00
ATOM	117	CB	VAL	15	36.014	12.360	−16.536	0.00	0.00
ATOM	118	CG1	VAL	15	35.140	13.518	−16.971	0.00	0.00
ATOM	119	CG2	VAL	15	35.167	11.104	−16.240	0.00	0.00
ATOM	120	N	THR	16	38.144	10.027	−16.591	0.00	0.00
ATOM	121	CA	THR	16	38.439	8.589	−16.520	0.00	0.00
ATOM	122	C	THR	16	37.305	7.828	−15.707	0.00	0.00
ATOM	123	O	THR	16	37.664	6.837	−15.059	0.00	0.00
ATOM	124	CB	THR	16	39.934	8.199	−16.206	0.00	0.00
ATOM	125	OG1	THR	16	40.373	7.068	−17.053	0.00	0.00
ATOM	126	CG2	THR	16	40.471	7.943	−14.793	0.00	0.00
ATOM	127	N	GLN	17	36.092	8.409	−15.467	0.00	0.00
ATOM	128	CA	GLN	17	35.022	7.662	−14.758	0.00	0.00
ATOM	129	C	GLN	17	34.965	6.183	−15.162	0.00	0.00
ATOM	130	O	GLN	17	34.657	5.399	−14.270	0.00	0.00
ATOM	131	CB	GLN	17	33.586	8.287	−14.893	0.00	0.00
ATOM	132	CG	GLN	17	33.654	9.770	−14.559	0.00	0.00
ATOM	133	CD	GLN	17	34.068	9.953	−13.109	0.00	0.00
ATOM	134	OE1	GLN	17	33.406	9.484	−12.174	0.00	0.00
ATOM	135	NE2	GLN	17	35.158	10.661	−12.865	0.00	0.00
ATOM	136	N	GLN	18	34.862	5.891	−16.491	0.00	0.00
ATOM	137	CA	GLN	18	34.747	4.512	−16.869	0.00	0.00
ATOM	138	C	GLN	18	35.809	3.595	−16.138	0.00	0.00
ATOM	139	O	GLN	18	35.450	2.468	−15.813	0.00	0.00
ATOM	140	CB	GLN	18	34.920	4.249	−18.388	0.00	0.00
ATOM	141	CG	GLN	18	36.218	4.759	−19.045	0.00	0.00
ATOM	142	CD	GLN	18	37.257	3.731	−19.366	0.00	0.00
ATOM	143	OE1	GLN	18	37.392	2.667	−18.765	0.00	0.00
ATOM	144	NE2	GLN	18	38.080	4.012	−20.401	0.00	0.00
ATOM	145	N	ARG	19	37.083	4.023	−15.906	0.00	0.00
ATOM	146	CA	ARG	19	38.097	3.241	−15.140	0.00	0.00
ATOM	147	C	ARG	19	37.579	3.043	−13.679	0.00	0.00
ATOM	148	O	ARG	19	37.479	1.863	−13.285	0.00	0.00
ATOM	149	CB	ARG	19	39.523	3.759	−15.273	0.00	0.00
ATOM	150	CG	ARG	19	40.143	3.416	−16.595	0.00	0.00
ATOM	151	CD	ARG	19	41.240	4.369	−17.113	0.00	0.00
ATOM	152	NE	ARG	19	41.647	3.953	−18.459	0.00	0.00
ATOM	153	CZ	ARG	19	41.337	4.641	−19.576	0.00	0.00
ATOM	154	NH1	ARG	19	40.636	5.769	−19.498	0.00	0.00
ATOM	155	NH2	ARG	19	41.662	4.113	−20.774	0.00	0.00
ATOM	156	N	ASP	20	37.268	4.090	−12.935	0.00	0.00
ATOM	157	CA	ASP	20	36.690	3.915	−11.600	0.00	0.00
ATOM	158	C	ASP	20	35.630	5.023	−11.287	0.00	0.00
ATOM	159	O	ASP	20	35.723	6.176	−11.743	0.00	0.00
ATOM	160	CB	ASP	20	37.822	3.783	−10.606	0.00	0.00
ATOM	161	CG	ASP	20	38.595	5.053	−10.375	0.00	0.00
ATOM	162	OD1	ASP	20	38.044	6.107	−10.114	0.00	0.00
ATOM	163	OD2	ASP	20	39.837	5.007	−10.540	0.00	0.00
ATOM	164	N	GLU	21	34.700	4.679	−10.415	0.00	0.00
ATOM	165	CA	GLU	21	33.606	5.526	−10.071	0.00	0.00
ATOM	166	C	GLU	21	34.041	6.910	−9.445	0.00	0.00
ATOM	167	O	GLU	21	35.248	7.163	−9.339	0.00	0.00
ATOM	168	CB	GLU	21	32.738	4.723	−9.043	0.00	0.00
ATOM	169	CG	GLU	21	33.123	3.256	−8.825	0.00	0.00
ATOM	170	CD	GLU	21	32.520	2.472	−7.697	0.00	0.00
ATOM	171	OE1	GLU	21	33.064	1.646	−6.924	0.00	0.00
ATOM	172	OE2	GLU	21	31.270	2.655	−7.518	0.00	0.00
ATOM	173	N	VAL	22	33.169	7.904	−9.663	0.00	0.00
ATOM	174	CA	VAL	22	33.328	9.295	−9.162	0.00	0.00
ATOM	175	C	VAL	22	33.760	9.406	−7.664	0.00	0.00
ATOM	176	O	VAL	22	34.388	10.426	−7.367	0.00	0.00
ATOM	177	CB	VAL	22	31.998	10.004	−9.510	0.00	0.00
ATOM	178	CG1	VAL	22	30.860	9.381	−8.711	0.00	0.00
ATOM	179	CG2	VAL	22	32.112	11.487	−9.103	0.00	0.00
ATOM	180	N	TRP	23	33.027	8.787	−6.696	0.00	0.00
ATOM	181	CA	TRP	23	33.531	8.852	−5.337	0.00	0.00
ATOM	182	C	TRP	23	35.021	8.365	−5.294	0.00	0.00
ATOM	183	O	TRP	23	35.705	8.687	−4.312	0.00	0.00
ATOM	184	CB	TRP	23	32.668	8.048	−4.390	0.00	0.00
ATOM	185	CG	TRP	23	32.763	6.567	−4.496	0.00	0.00
ATOM	186	CD1	TRP	23	31.994	5.798	−5.290	0.00	0.00
ATOM	187	CD2	TRP	23	33.717	5.714	−3.855	0.00	0.00
ATOM	188	NE1	TRP	23	32.382	4.481	−5.168	0.00	0.00
ATOM	189	CE2	TRP	23	33.417	4.433	−4.338	0.00	0.00
ATOM	190	CE3	TRP	23	34.777	5.905	−2.952	0.00	0.00
ATOM	191	CZ2	TRP	23	34.172	3.333	−3.908	0.00	0.00
ATOM	192	CZ3	TRP	23	35.557	4.817	−2.517	0.00	0.00
ATOM	193	CH2	TRP	23	35.228	3.556	−3.021	0.00	0.00
ATOM	194	N	VAL	24	35.504	7.655	−6.351	0.00	0.00
ATOM	195	CA	VAL	24	36.836	7.229	−6.418	0.00	0.00
ATOM	196	C	VAL	24	37.702	8.493	−6.828	0.00	0.00
ATOM	197	O	VAL	24	38.714	8.260	−7.443	0.00	0.00
ATOM	198	CB	VAL	24	37.029	6.004	−7.320	0.00	0.00
ATOM	199	CG1	VAL	24	38.548	5.664	−7.451	0.00	0.00
ATOM	200	CG2	VAL	24	36.202	4.829	−6.966	0.00	0.00
ATOM	201	N	VAL	25	37.129	9.702	−6.987	0.00	0.00
ATOM	202	CA	VAL	25	38.023	10.840	−7.175	0.00	0.00
ATOM	203	C	VAL	25	38.870	10.750	−5.866	0.00	0.00
ATOM	204	O	VAL	25	39.748	9.821	−5.841	0.00	0.00
ATOM	205	CB	VAL	25	37.298	12.177	−7.417	0.00	0.00
ATOM	206	CG1	VAL	25	36.635	12.311	−8.764	0.00	0.00
ATOM	207	CG2	VAL	25	36.505	12.774	−6.310	0.00	0.00
ATOM	208	N	GLY	26	38.250	11.098	−4.694	0.00	0.00
ATOM	209	CA	GLY	26	38.795	10.938	−3.307	0.00	0.00
ATOM	210	C	GLY	26	40.361	11.172	−3.168	0.00	0.00
ATOM	211	O	GLY	26	40.894	10.843	−2.115	0.00	0.00
ATOM	212	N	MET	27	41.021	11.449	−4.261	0.00	0.00
ATOM	213	CA	MET	27	42.388	11.791	−4.408	0.00	0.00
ATOM	214	C	MET	27	42.477	13.331	−4.440	0.00	0.00
ATOM	215	O	MET	27	43.599	13.810	−4.420	0.00	0.00
ATOM	216	CB	MET	27	42.822	11.231	−5.750	0.00	0.00
ATOM	217	CG	MET	27	42.927	9.726	−5.779	0.00	0.00
ATOM	218	SD	MET	27	44.503	9.174	−5.069	0.00	0.00
ATOM	219	CE	MET	27	45.560	9.399	−6.527	0.00	0.00
ATOM	220	N	GLY	28	41.416	14.039	−4.820	0.00	0.00
ATOM	221	CA	GLY	28	41.311	15.472	−4.810	0.00	0.00
ATOM	222	C	GLY	28	41.292	15.888	−3.308	0.00	0.00
ATOM	223	O	GLY	28	41.587	17.061	−3.075	0.00	0.00
ATOM	224	N	ILE	29	40.434	15.237	−2.504	0.00	0.00
ATOM	225	CA	ILE	29	40.315	15.392	−1.034	0.00	0.00
ATOM	226	C	ILE	29	41.750	15.108	−0.437	0.00	0.00
ATOM	227	O	ILE	29	42.191	15.893	0.402	0.00	0.00
ATOM	228	CB	ILE	29	39.150	14.517	−0.452	0.00	0.00
ATOM	229	CG1	ILE	29	39.210	14.583	1.105	0.00	0.00
ATOM	230	CG2	ILE	29	39.307	12.999	−0.848	0.00	0.00
ATOM	231	CD1	ILE	29	38.727	15.958	1.665	0.00	0.00
ATOM	232	N	VAL	30	42.298	13.939	−0.711	0.00	0.00
ATOM	233	CA	VAL	30	43.643	13.534	−0.379	0.00	0.00
ATOM	234	C	VAL	30	44.676	14.603	−0.879	0.00	0.00
ATOM	235	O	VAL	30	45.661	14.801	−0.166	0.00	0.00
ATOM	236	CB	VAL	30	43.919	12.071	−0.804	0.00	0.00
ATOM	237	CG1	VAL	30	42.932	11.054	−0.159	0.00	0.00
ATOM	238	CG2	VAL	30	44.133	11.933	−2.305	0.00	0.00
ATOM	239	N	MET	31	44.600	15.005	−2.173	0.00	0.00
ATOM	240	CA	MET	31	45.440	16.108	−2.693	0.00	0.00
ATOM	241	C	MET	31	45.337	17.387	−1.831	0.00	0.00
ATOM	242	O	MET	31	46.326	18.112	−1.784	0.00	0.00
ATOM	243	CB	MET	31	45.211	16.441	−4.208	0.00	0.00
ATOM	244	CG	MET	31	45.684	15.368	−5.126	0.00	0.00
ATOM	245	SD	MET	31	47.375	14.817	−4.763	0.00	0.00
ATOM	246	CE	MET	31	48.290	16.334	−4.787	0.00	0.00
ATOM	247	N	SER	32	44.088	17.882	−1.686	0.00	0.00
ATOM	248	CA	SER	32	43.770	19.048	−0.888	0.00	0.00
ATOM	249	C	SER	32	44.547	18.975	0.463	0.00	0.00
ATOM	250	O	SER	32	45.061	20.025	0.848	0.00	0.00
ATOM	251	CB	SER	32	42.242	19.126	−0.706	0.00	0.00
ATOM	252	OG	SER	32	41.481	19.637	−1.788	0.00	0.00
ATOM	253	N	LEU	33	44.411	17.917	1.294	0.00	0.00
ATOM	254	CA	LEU	33	45.140	17.701	2.506	0.00	0.00
ATOM	255	C	LEU	33	46.690	17.860	2.286	0.00	0.00
ATOM	256	O	LEU	33	47.300	18.439	3.186	0.00	0.00
ATOM	257	CB	LEU	33	44.779	16.312	3.036	0.00	0.00
ATOM	258	CG	LEU	33	43.521	16.067	3.847	0.00	0.00
ATOM	259	CD1	LEU	33	42.327	16.943	3.499	0.00	0.00
ATOM	260	CD2	LEU	33	43.158	14.652	3.511	0.00	0.00
ATOM	261	N	ILE	34	47.348	17.141	1.332	0.00	0.00
ATOM	262	CA	ILE	34	48.774	17.315	1.001	0.00	0.00
ATOM	263	C	ILE	34	49.064	18.836	0.762	0.00	0.00
ATOM	264	O	ILE	34	49.780	19.368	1.583	0.00	0.00
ATOM	265	CB	ILE	34	49.155	16.445	−0.241	0.00	0.00
ATOM	266	CG1	ILE	34	49.439	14.983	0.179	0.00	0.00
ATOM	267	CG2	ILE	34	50.414	17.047	−0.970	0.00	0.00
ATOM	268	CD1	ILE	34	49.621	13.952	−0.963	0.00	0.00
ATOM	269	N	VAL	35	48.286	19.586	−0.065	0.00	0.00
ATOM	270	CA	VAL	35	48.409	21.059	−0.311	0.00	0.00
ATOM	271	C	VAL	35	48.439	21.835	1.055	0.00	0.00
ATOM	272	O	VAL	35	49.440	22.516	1.327	0.00	0.00
ATOM	273	CB	VAL	35	47.406	21.632	−1.382	0.00	0.00
ATOM	274	CG1	VAL	35	47.302	23.184	−1.439	0.00	0.00
ATOM	275	CG2	VAL	35	47.778	20.968	−2.758	0.00	0.00
ATOM	276	N	LEU	36	47.425	21.716	1.896	0.00	0.00
ATOM	277	CA	LEU	36	47.336	22.397	3.181	0.00	0.00
ATOM	278	C	LEU	36	48.558	22.038	4.110	0.00	0.00
ATOM	279	O	LEU	36	49.215	22.986	4.544	0.00	0.00
ATOM	280	CB	LEU	36	45.971	22.117	3.834	0.00	0.00
ATOM	281	CG	LEU	36	45.593	22.954	5.060	0.00	0.00
ATOM	282	CD1	LEU	36	45.595	24.465	4.776	0.00	0.00
ATOM	283	CD2	LEU	36	44.252	22.445	5.501	0.00	0.00
ATOM	284	N	ALA	37	48.858	20.753	4.422	0.00	0.00
ATOM	285	CA	ALA	37	50.031	20.359	5.217	0.00	0.00
ATOM	286	C	ALA	37	51.432	20.733	4.571	0.00	0.00
ATOM	287	O	ALA	37	52.292	21.121	5.351	0.00	0.00
ATOM	288	CB	ALA	37	49.903	18.854	5.489	0.00	0.00
ATOM	289	N	ILE	38	51.750	20.251	3.368	0.00	0.00
ATOM	290	CA	ILE	38	52.980	20.529	2.602	0.00	0.00
ATOM	291	C	ILE	38	53.289	22.083	2.533	0.00	0.00
ATOM	292	O	ILE	38	54.465	22.424	2.683	0.00	0.00
ATOM	293	CB	ILE	38	52.911	19.954	1.168	0.00	0.00
ATOM	294	CG1	ILE	38	52.062	20.725	0.185	0.00	0.00
ATOM	295	CG2	ILE	38	52.649	18.434	1.186	0.00	0.00
ATOM	296	CD1	ILE	38	52.006	20.193	−1.262	0.00	0.00
ATOM	297	N	VAL	39	52.315	22.992	2.240	0.00	0.00
ATOM	298	CA	VAL	39	52.524	24.429	2.267	0.00	0.00
ATOM	299	C	VAL	39	52.976	24.906	3.691	0.00	0.00
ATOM	300	O	VAL	39	54.143	25.255	3.802	0.00	0.00
ATOM	301	CB	VAL	39	51.259	25.174	1.793	0.00	0.00
ATOM	302	CG1	VAL	39	51.415	26.689	2.035	0.00	0.00
ATOM	303	CG2	VAL	39	50.982	24.940	0.328	0.00	0.00
ATOM	304	N	PHE	40	52.202	24.694	4.792	0.00	0.00
ATOM	305	CA	PHE	40	52.564	25.112	6.152	0.00	0.00
ATOM	306	C	PHE	40	53.850	24.412	6.718	0.00	0.00
ATOM	307	O	PHE	40	54.665	25.121	7.324	0.00	0.00
ATOM	308	CB	PHE	40	51.338	24.878	7.040	0.00	0.00
ATOM	309	CG	PHE	40	50.398	26.065	7.048	0.00	0.00
ATOM	310	CD1	PHE	40	50.668	27.222	6.305	0.00	0.00
ATOM	311	CD2	PHE	40	49.264	26.003	7.856	0.00	0.00
ATOM	312	CE1	PHE	40	49.815	28.317	6.371	0.00	0.00
ATOM	313	CE2	PHE	40	48.412	27.107	7.918	0.00	0.00
ATOM	314	CZ	PHE	40	48.686	28.262	7.179	0.00	0.00
ATOM	315	N	GLY	41	53.993	23.063	6.631	0.00	0.00
ATOM	316	CA	GLY	41	55.180	22.285	7.024	0.00	0.00
ATOM	317	C	GLY	41	56.512	22.798	6.425	0.00	0.00
ATOM	318	O	GLY	41	57.129	23.578	7.116	0.00	0.00
ATOM	319	N	ASN	42	56.594	22.877	5.093	0.00	0.00
ATOM	320	CA	ASN	42	57.792	23.265	4.293	0.00	0.00
ATOM	321	C	ASN	42	57.958	24.798	4.372	0.00	0.00
ATOM	322	O	ASN	42	59.012	25.199	4.835	0.00	0.00
ATOM	323	CB	ASN	42	57.500	22.770	2.902	0.00	0.00
ATOM	324	CG	ASN	42	57.785	21.337	2.647	0.00	0.00
ATOM	325	OD1	ASN	42	58.920	20.891	2.857	0.00	0.00
ATOM	326	ND2	ASN	42	56.784	20.533	2.285	0.00	0.00
ATOM	327	N	VAL	43	56.952	25.639	4.033	0.00	0.00
ATOM	328	CA	VAL	43	57.030	27.100	4.193	0.00	0.00
ATOM	329	C	VAL	43	57.552	27.464	5.619	0.00	0.00
ATOM	330	O	VAL	43	58.544	28.204	5.657	0.00	0.00
ATOM	331	CB	VAL	43	55.682	27.782	3.894	0.00	0.00
ATOM	332	CG1	VAL	43	55.568	29.204	4.437	0.00	0.00
ATOM	333	CG2	VAL	43	55.388	27.745	2.400	0.00	0.00
ATOM	334	N	LEU	44	56.889	27.059	6.728	0.00	0.00
ATOM	335	CA	LEU	44	57.389	27.306	8.090	0.00	0.00
ATOM	336	C	LEU	44	58.876	26.847	8.198	0.00	0.00
ATOM	337	O	LEU	44	59.634	27.613	8.785	0.00	0.00
ATOM	338	CB	LEU	44	56.481	26.610	9.133	0.00	0.00
ATOM	339	CG	LEU	44	57.118	26.694	10.532	0.00	0.00
ATOM	340	CD1	LEU	44	57.194	28.153	10.959	0.00	0.00
ATOM	341	CD2	LEU	44	56.281	25.913	11.508	0.00	0.00
ATOM	342	N	VAL	45	59.229	25.601	7.866	0.00	0.00
ATOM	343	CA	VAL	45	60.593	25.117	7.837	0.00	0.00
ATOM	344	C	VAL	45	61.557	26.056	7.003	0.00	0.00
ATOM	345	O	VAL	45	62.654	26.307	7.502	0.00	0.00
ATOM	346	CB	VAL	45	60.640	23.661	7.422	0.00	0.00
ATOM	347	CG1	VAL	45	62.036	23.062	7.418	0.00	0.00
ATOM	348	CG2	VAL	45	59.620	22.786	8.143	0.00	0.00
ATOM	349	N	ILE	46	61.217	26.503	5.771	0.00	0.00
ATOM	350	CA	ILE	46	62.034	27.441	5.020	0.00	0.00
ATOM	351	C	ILE	46	62.139	28.791	5.786	0.00	0.00
ATOM	352	O	ILE	46	63.279	29.249	5.902	0.00	0.00
ATOM	353	CB	ILE	46	61.552	27.527	3.540	0.00	0.00
ATOM	354	CG1	ILE	46	61.918	28.714	2.740	0.00	0.00
ATOM	355	CG2	ILE	46	60.083	27.254	3.380	0.00	0.00
ATOM	356	CD1	ILE	46	61.887	28.442	1.233	0.00	0.00
ATOM	357	N	THR	47	61.034	29.522	6.094	0.00	0.00
ATOM	358	CA	THR	47	61.131	30.729	6.902	0.00	0.00
ATOM	359	C	THR	47	62.028	30.554	8.196	0.00	0.00
ATOM	360	O	THR	47	62.634	31.550	8.590	0.00	0.00
ATOM	361	CB	THR	47	59.727	31.284	7.299	0.00	0.00
ATOM	362	OG1	THR	47	58.778	31.267	6.200	0.00	0.00
ATOM	363	CG2	THR	47	59.736	32.715	7.921	0.00	0.00
ATOM	364	N	ALA	48	61.918	29.467	8.987	0.00	0.00
ATOM	365	CA	ALA	48	62.757	29.154	10.148	0.00	0.00
ATOM	366	C	ALA	48	64.295	29.072	9.829	0.00	0.00
ATOM	367	O	ALA	48	65.030	29.710	10.590	0.00	0.00
ATOM	368	CB	ALA	48	62.185	27.881	10.783	0.00	0.00
ATOM	369	N	ILE	49	64.779	28.257	8.845	0.00	0.00
ATOM	370	CA	ILE	49	66.248	28.277	8.554	0.00	0.00
ATOM	371	C	ILE	49	66.712	29.683	8.023	0.00	0.00
ATOM	372	O	ILE	49	67.720	30.165	8.559	0.00	0.00
ATOM	373	CB	ILE	49	66.736	27.113	7.671	0.00	0.00
ATOM	374	CG1	ILE	49	66.148	25.754	8.022	0.00	0.00
ATOM	375	CG2	ILE	49	68.304	27.045	7.582	0.00	0.00
ATOM	376	CD1	ILE	49	66.548	24.575	7.114	0.00	0.00
ATOM	377	N	ALA	50	66.029	30.333	7.071	0.00	0.00
ATOM	378	CA	ALA	50	66.343	31.691	6.590	0.00	0.00
ATOM	379	C	ALA	50	66.416	32.737	7.756	0.00	0.00
ATOM	380	O	ALA	50	67.465	33.403	7.836	0.00	0.00
ATOM	381	CB	ALA	50	65.279	32.050	5.523	0.00	0.00
ATOM	382	N	LYS	51	65.372	32.949	8.560	0.00	0.00
ATOM	383	CA	LYS	51	65.443	33.901	9.677	0.00	0.00
ATOM	384	C	LYS	51	66.449	33.509	10.824	0.00	0.00
ATOM	385	O	LYS	51	67.030	34.455	11.366	0.00	0.00
ATOM	386	CB	LYS	51	64.027	34.061	10.235	0.00	0.00
ATOM	387	CG	LYS	51	63.747	35.082	11.344	0.00	0.00
ATOM	388	CD	LYS	51	62.155	35.241	11.442	0.00	0.00
ATOM	389	CE	LYS	51	61.659	35.425	10.051	0.00	0.00
ATOM	390	NZ	LYS	51	61.721	36.763	9.595	0.00	0.00
ATOM	391	N	PHE	52	66.819	32.218	11.035	0.00	0.00
ATOM	392	CA	PHE	52	67.673	31.889	12.184	0.00	0.00
ATOM	393	C	PHE	52	69.182	32.007	11.745	0.00	0.00
ATOM	394	O	PHE	52	69.649	31.199	10.924	0.00	0.00
ATOM	395	CB	PHE	52	67.169	30.460	12.505	0.00	0.00
ATOM	396	CG	PHE	52	66.297	30.478	13.789	0.00	0.00
ATOM	397	CD1	PHE	52	65.357	31.493	13.904	0.00	0.00
ATOM	398	CD2	PHE	52	66.379	29.479	14.760	0.00	0.00
ATOM	399	CE1	PHE	52	64.499	31.551	14.998	0.00	0.00
ATOM	400	CE2	PHE	52	65.499	29.512	15.863	0.00	0.00
ATOM	401	CZ	PHE	52	64.559	30.535	15.950	0.00	0.00
ATOM	402	N	GLU	53	69.838	33.121	12.141	0.00	0.00
ATOM	403	CA	GLU	53	71.224	33.483	11.772	0.00	0.00
ATOM	404	C	GLU	53	72.253	32.300	11.846	0.00	0.00
ATOM	405	O	GLU	53	72.905	32.097	10.813	0.00	0.00
ATOM	406	CB	GLU	53	71.714	34.639	12.639	0.00	0.00
ATOM	407	CG	GLU	53	71.258	35.992	12.140	0.00	0.00
ATOM	408	CD	GLU	53	71.530	37.134	13.113	0.00	0.00
ATOM	409	OE1	GLU	53	72.631	37.187	13.681	0.00	0.00
ATOM	410	OE2	GLU	53	70.624	37.956	13.302	0.00	0.00
ATOM	411	N	ARG	54	72.279	31.449	12.896	0.00	0.00
ATOM	412	CA	ARG	54	73.320	30.406	12.978	0.00	0.00
ATOM	413	C	ARG	54	72.856	28.970	12.536	0.00	0.00
ATOM	414	O	ARG	54	73.621	28.032	12.746	0.00	0.00
ATOM	415	CB	ARG	54	73.838	30.307	14.395	0.00	0.00
ATOM	416	CG	ARG	54	74.320	31.547	15.050	0.00	0.00
ATOM	417	CD	ARG	54	75.345	32.183	14.170	0.00	0.00
ATOM	418	NE	ARG	54	76.577	31.436	13.999	0.00	0.00
ATOM	419	CZ	ARG	54	77.478	31.159	14.947	0.00	0.00
ATOM	420	NH1	ARG	54	77.308	31.512	16.210	0.00	0.00
ATOM	421	NH2	ARG	54	78.551	30.420	14.622	0.00	0.00
ATOM	422	N	LEU	55	71.690	28.775	11.887	0.00	0.00
ATOM	423	CA	LEU	55	71.224	27.467	11.342	0.00	0.00
ATOM	424	C	LEU	55	71.903	27.331	9.952	0.00	0.00
ATOM	425	O	LEU	55	71.219	27.473	8.931	0.00	0.00
ATOM	426	CB	LEU	55	69.687	27.446	11.266	0.00	0.00
ATOM	427	CG	LEU	55	69.112	26.484	12.343	0.00	0.00
ATOM	428	CD1	LEU	55	69.750	26.636	13.709	0.00	0.00
ATOM	429	CD2	LEU	55	67.618	26.568	12.475	0.00	0.00
ATOM	430	N	GLN	56	73.210	27.002	9.883	0.00	0.00
ATOM	431	CA	GLN	56	74.010	26.942	8.626	0.00	0.00
ATOM	432	C	GLN	56	74.605	25.556	8.299	0.00	0.00
ATOM	433	O	GLN	56	75.197	25.468	7.220	0.00	0.00
ATOM	434	CB	GLN	56	75.130	27.966	8.827	0.00	0.00
ATOM	435	CG	GLN	56	74.724	29.415	8.955	0.00	0.00
ATOM	436	CD	GLN	56	73.896	29.994	7.840	0.00	0.00
ATOM	437	OE1	GLN	56	74.087	29.682	6.659	0.00	0.00
ATOM	438	NE2	GLN	56	72.948	30.872	8.162	0.00	0.00
ATOM	439	N	THR	57	74.518	24.524	9.178	0.00	0.00
ATOM	440	CA	THR	57	75.128	23.264	8.924	0.00	0.00
ATOM	441	C	THR	57	74.657	22.707	7.557	0.00	0.00
ATOM	442	O	THR	57	73.564	23.065	7.093	0.00	0.00
ATOM	443	CB	THR	57	74.815	22.261	10.075	0.00	0.00
ATOM	444	OG1	THR	57	73.485	21.652	9.991	0.00	0.00
ATOM	445	CG2	THR	57	74.956	22.914	11.495	0.00	0.00
ATOM	446	N	VAL	58	75.524	22.016	6.819	0.00	0.00
ATOM	447	CA	VAL	58	75.086	21.382	5.576	0.00	0.00
ATOM	448	C	VAL	58	73.712	20.657	5.759	0.00	0.00
ATOM	449	O	VAL	58	72.947	20.662	4.811	0.00	0.00
ATOM	450	CB	VAL	58	76.245	20.473	5.141	0.00	0.00
ATOM	451	CG1	VAL	58	75.900	19.381	4.113	0.00	0.00
ATOM	452	CG2	VAL	58	77.380	21.381	4.563	0.00	0.00
ATOM	453	N	THR	59	73.454	19.942	6.890	0.00	0.00
ATOM	454	CA	THR	59	72.179	19.288	7.241	0.00	0.00
ATOM	455	C	THR	59	71.018	20.323	7.216	0.00	0.00
ATOM	456	O	THR	59	69.941	19.931	6.724	0.00	0.00
ATOM	457	CB	THR	59	72.290	18.586	8.638	0.00	0.00
ATOM	458	OG1	THR	59	73.500	17.829	8.813	0.00	0.00
ATOM	459	CG2	THR	59	71.066	17.647	8.949	0.00	0.00
ATOM	460	N	ASN	60	71.046	21.394	8.015	0.00	0.00
ATOM	461	CA	ASN	60	70.020	22.454	7.954	0.00	0.00
ATOM	462	C	ASN	60	69.914	22.946	6.495	0.00	0.00
ATOM	463	O	ASN	60	68.772	23.194	6.091	0.00	0.00
ATOM	464	CB	ASN	60	70.343	23.575	8.951	0.00	0.00
ATOM	465	CG	ASN	60	70.133	23.181	10.410	0.00	0.00
ATOM	466	OD1	ASN	60	70.419	23.854	11.414	0.00	0.00
ATOM	467	ND2	ASN	60	69.588	21.981	10.594	0.00	0.00
ATOM	468	N	TYR	61	71.008	23.287	5.784	0.00	0.00
ATOM	469	CA	TYR	61	70.860	23.638	4.386	0.00	0.00
ATOM	470	C	TYR	61	70.143	22.593	3.532	0.00	0.00
ATOM	471	O	TYR	61	69.377	23.026	2.671	0.00	0.00
ATOM	472	CB	TYR	61	72.201	23.958	3.716	0.00	0.00
ATOM	473	CG	TYR	61	72.672	25.362	3.823	0.00	0.00
ATOM	474	CD1	TYR	61	71.959	26.362	3.188	0.00	0.00
ATOM	475	CD2	TYR	61	73.823	25.649	4.536	0.00	0.00
ATOM	476	CE1	TYR	61	72.399	27.664	3.268	0.00	0.00
ATOM	477	CE2	TYR	61	74.264	26.946	4.619	0.00	0.00
ATOM	478	CZ	TYR	61	73.548	27.931	3.981	0.00	0.00
ATOM	479	OH	TYR	61	73.994	29.232	4.034	0.00	0.00
ATOM	480	N	PHE	62	70.659	21.371	3.469	0.00	0.00
ATOM	481	CA	PHE	62	70.031	20.299	2.783	0.00	0.00
ATOM	482	C	PHE	62	68.487	20.433	2.997	0.00	0.00
ATOM	483	O	PHE	62	67.706	20.195	2.077	0.00	0.00
ATOM	484	CB	PHE	62	70.484	19.071	3.571	0.00	0.00
ATOM	485	CG	PHE	62	71.608	18.266	3.087	0.00	0.00
ATOM	486	CD1	PHE	62	71.725	17.825	1.770	0.00	0.00
ATOM	487	CD2	PHE	62	72.631	18.033	3.983	0.00	0.00
ATOM	488	CE1	PHE	62	72.882	17.156	1.343	0.00	0.00
ATOM	489	CE2	PHE	62	73.793	17.367	3.599	0.00	0.00
ATOM	490	CZ	PHE	62	73.899	16.939	2.265	0.00	0.00
ATOM	491	N	ILE	63	68.162	20.467	4.318	0.00	0.00
ATOM	492	CA	ILE	63	66.816	20.627	4.871	0.00	0.00
ATOM	493	C	ILE	63	66.065	21.792	4.176	0.00	0.00
ATOM	494	O	ILE	63	64.907	21.553	3.835	0.00	0.00
ATOM	495	CB	ILE	63	66.760	20.684	6.437	0.00	0.00
ATOM	496	CG1	ILE	63	66.410	19.331	7.006	0.00	0.00
ATOM	497	CG2	ILE	63	65.718	21.758	6.976	0.00	0.00
ATOM	498	CD1	ILE	63	67.215	18.884	8.242	0.00	0.00
ATOM	499	N	THR	64	66.622	23.038	4.071	0.00	0.00
ATOM	500	CA	THR	64	65.923	24.159	3.360	0.00	0.00
ATOM	501	C	THR	64	65.602	23.756	1.888	0.00	0.00
ATOM	502	O	THR	64	64.622	24.298	1.389	0.00	0.00
ATOM	503	CB	THR	64	66.630	25.566	3.308	0.00	0.00
ATOM	504	OG1	THR	64	67.414	25.876	4.440	0.00	0.00
ATOM	505	CG2	THR	64	65.519	26.672	3.144	0.00	0.00
ATOM	506	N	SER	65	66.620	23.365	1.105	0.00	0.00
ATOM	507	CA	SER	65	66.515	22.882	−0.285	0.00	0.00
ATOM	508	C	SER	65	65.246	21.985	−0.468	0.00	0.00
ATOM	509	O	SER	65	64.694	22.045	−1.574	0.00	0.00
ATOM	510	CB	SER	65	67.814	22.182	−0.704	0.00	0.00
ATOM	511	OG	SER	65	67.936	21.886	−2.083	0.00	0.00
ATOM	512	N	LEU	66	65.101	20.903	0.304	0.00	0.00
ATOM	513	CA	LEU	66	63.927	20.083	0.279	0.00	0.00
ATOM	514	C	LEU	66	62.685	20.936	0.643	0.00	0.00
ATOM	515	O	LEU	66	61.646	20.570	0.167	0.00	0.00
ATOM	516	CB	LEU	66	64.146	18.983	1.319	0.00	0.00
ATOM	517	CG	LEU	66	65.340	18.064	1.164	0.00	0.00
ATOM	518	CD1	LEU	66	65.317	17.154	2.376	0.00	0.00
ATOM	519	CD2	LEU	66	65.376	17.397	−0.202	0.00	0.00
ATOM	520	N	ALA	67	62.755	21.902	1.593	0.00	0.00
ATOM	521	CA	ALA	67	61.619	22.777	1.871	0.00	0.00
ATOM	522	C	ALA	67	61.197	23.477	0.532	0.00	0.00
ATOM	523	O	ALA	67	59.998	23.677	0.367	0.00	0.00
ATOM	524	CB	ALA	67	61.984	23.728	3.022	0.00	0.00
ATOM	525	N	CYS	68	62.125	24.149	−0.184	0.00	0.00
ATOM	526	CA	CYS	68	61.902	24.758	−1.483	0.00	0.00
ATOM	527	C	CYS	68	61.383	23.682	−2.493	0.00	0.00
ATOM	528	O	CYS	68	60.549	24.078	−3.305	0.00	0.00
ATOM	529	CB	CYS	68	63.246	25.371	−1.948	0.00	0.00
ATOM	530	SG	CYS	68	63.781	26.812	−0.973	0.00	0.00
ATOM	531	N	ALA	69	62.118	22.565	−2.742	0.00	0.00
ATOM	532	CA	ALA	69	61.679	21.451	−3.598	0.00	0.00
ATOM	533	C	ALA	69	60.227	21.037	−3.248	0.00	0.00
ATOM	534	O	ALA	69	59.416	21.135	−4.143	0.00	0.00
ATOM	535	CB	ALA	69	62.683	20.283	−3.494	0.00	0.00
ATOM	536	N	ASP	70	59.915	20.905	−1.984	0.00	0.00
ATOM	537	CA	ASP	70	58.576	20.568	−1.425	0.00	0.00
ATOM	538	C	ASP	70	57.528	21.674	−1.822	0.00	0.00
ATOM	539	O	ASP	70	56.351	21.324	−1.907	0.00	0.00
ATOM	540	CB	ASP	70	58.804	20.403	0.045	0.00	0.00
ATOM	541	CG	ASP	70	59.473	19.109	0.404	0.00	0.00
ATOM	542	OD1	ASP	70	59.912	18.352	−0.517	0.00	0.00
ATOM	543	OD2	ASP	70	59.766	18.842	1.626	0.00	0.00
ATOM	544	N	LEU	71	57.841	22.978	−1.696	0.00	0.00
ATOM	545	CA	LEU	71	56.974	24.056	−2.136	0.00	0.00
ATOM	546	C	LEU	71	56.684	23.864	−3.659	0.00	0.00
ATOM	547	O	LEU	71	55.557	24.164	−4.027	0.00	0.00
ATOM	548	CB	LEU	71	57.564	25.426	−1.840	0.00	0.00
ATOM	549	CG	LEU	71	57.746	25.748	−0.374	0.00	0.00
ATOM	550	CD1	LEU	71	58.330	27.165	−0.266	0.00	0.00
ATOM	551	CD2	LEU	71	56.360	25.708	0.283	0.00	0.00
ATOM	552	N	VAL	72	57.730	23.837	−4.517	0.00	0.00
ATOM	553	CA	VAL	72	57.679	23.569	−5.962	0.00	0.00
ATOM	554	C	VAL	72	56.673	22.374	−6.180	0.00	0.00
ATOM	555	O	VAL	72	55.878	22.483	−7.085	0.00	0.00
ATOM	556	CB	VAL	72	59.134	23.230	−6.448	0.00	0.00
ATOM	557	CG1	VAL	72	59.102	22.586	−7.880	0.00	0.00
ATOM	558	CG2	VAL	72	59.986	24.450	−6.432	0.00	0.00
ATOM	559	N	MET	73	56.793	21.254	−5.430	0.00	0.00
ATOM	560	CA	MET	73	55.899	20.123	−5.437	0.00	0.00
ATOM	561	C	MET	73	54.406	20.583	−5.354	0.00	0.00
ATOM	562	O	MET	73	53.852	20.797	−6.427	0.00	0.00
ATOM	563	CB	MET	73	56.274	19.313	−4.151	0.00	0.00
ATOM	564	CG	MET	73	57.737	18.821	−4.289	0.00	0.00
ATOM	565	SD	MET	73	58.046	17.715	−2.884	0.00	0.00
ATOM	566	CE	MET	73	57.288	16.214	−3.402	0.00	0.00
ATOM	567	N	GLY	74	54.096	21.264	−4.258	0.00	0.00
ATOM	568	CA	GLY	74	52.791	21.725	−3.868	0.00	0.00
ATOM	569	C	GLY	74	52.077	22.650	−4.840	0.00	0.00
ATOM	570	O	GLY	74	50.873	22.741	−4.686	0.00	0.00
ATOM	571	N	LEU	75	52.775	23.789	−5.096	0.00	0.00
ATOM	572	CA	LEU	75	52.356	24.815	−6.051	0.00	0.00
ATOM	573	C	LEU	75	52.496	24.411	−7.563	0.00	0.00
ATOM	574	O	LEU	75	51.766	25.018	−8.370	0.00	0.00
ATOM	575	CB	LEU	75	53.205	26.082	−5.784	0.00	0.00
ATOM	576	CG	LEU	75	52.992	26.791	−4.437	0.00	0.00
ATOM	577	CD1	LEU	75	53.866	28.026	−4.320	0.00	0.00
ATOM	578	CD2	LEU	75	51.540	27.182	−4.219	0.00	0.00
ATOM	579	N	ALA	76	53.634	23.835	−8.017	0.00	0.00
ATOM	580	CA	ALA	76	53.818	23.540	−9.422	0.00	0.00
ATOM	581	C	ALA	76	53.054	22.245	−9.915	0.00	0.00
ATOM	582	O	ALA	76	52.456	22.310	−10.991	0.00	0.00
ATOM	583	CB	ALA	76	55.296	23.583	−9.759	0.00	0.00
ATOM	584	N	VAL	77	53.247	21.068	−9.337	0.00	0.00
ATOM	585	CA	VAL	77	52.512	19.849	−9.655	0.00	0.00
ATOM	586	C	VAL	77	51.286	19.674	−8.775	0.00	0.00
ATOM	587	O	VAL	77	50.241	19.408	−9.348	0.00	0.00
ATOM	588	CB	VAL	77	53.415	18.625	−9.625	0.00	0.00
ATOM	589	CG1	VAL	77	54.599	18.651	−10.571	0.00	0.00
ATOM	590	CG2	VAL	77	53.996	18.357	−8.233	0.00	0.00
ATOM	591	N	VAL	78	51.388	20.001	−7.529	0.00	0.00
ATOM	592	CA	VAL	78	50.328	19.783	−6.625	0.00	0.00
ATOM	593	C	VAL	78	49.017	20.507	−7.078	0.00	0.00
ATOM	594	O	VAL	78	48.057	19.725	−7.315	0.00	0.00
ATOM	595	CB	VAL	78	50.717	19.856	−5.170	0.00	0.00
ATOM	596	CG1	VAL	78	49.527	19.543	−4.202	0.00	0.00
ATOM	597	CG2	VAL	78	51.960	19.158	−4.787	0.00	0.00
ATOM	598	N	PRO	79	48.813	21.853	−7.222	0.00	0.00
ATOM	599	CA	PRO	79	47.516	22.255	−7.587	0.00	0.00
ATOM	600	C	PRO	79	47.038	21.553	−8.890	0.00	0.00
ATOM	601	O	PRO	79	45.834	21.535	−9.108	0.00	0.00
ATOM	602	CB	PRO	79	47.378	23.815	−7.791	0.00	0.00
ATOM	603	CG	PRO	79	48.830	24.251	−7.527	0.00	0.00
ATOM	604	CD	PRO	79	49.721	23.085	−7.224	0.00	0.00
ATOM	605	N	PHE	80	47.929	21.268	−9.810	0.00	0.00
ATOM	606	CA	PHE	80	47.668	20.504	−11.022	0.00	0.00
ATOM	607	C	PHE	80	46.922	19.188	−10.797	0.00	0.00
ATOM	608	O	PHE	80	45.723	19.187	−11.069	0.00	0.00
ATOM	609	CB	PHE	80	48.990	20.376	−11.801	0.00	0.00
ATOM	610	CG	PHE	80	49.405	21.419	−12.763	0.00	0.00
ATOM	611	CD1	PHE	80	50.305	21.070	−13.793	0.00	0.00
ATOM	612	CD2	PHE	80	48.907	22.720	−12.714	0.00	0.00
ATOM	613	CE1	PHE	80	50.746	22.039	−14.671	0.00	0.00
ATOM	614	CE2	PHE	80	49.323	23.694	−13.621	0.00	0.00
ATOM	615	CZ	PHE	80	50.228	23.329	−14.629	0.00	0.00
ATOM	616	N	GLY	81	47.479	18.285	−10.045	0.00	0.00
ATOM	617	CA	GLY	81	46.890	17.015	−9.659	0.00	0.00
ATOM	618	C	GLY	81	45.477	17.246	−8.974	0.00	0.00
ATOM	619	O	GLY	81	44.649	16.387	−9.158	0.00	0.00
ATOM	620	N	ALA	82	45.337	18.201	−8.017	0.00	0.00
ATOM	621	CA	ALA	82	44.100	18.608	−7.364	0.00	0.00
ATOM	622	C	ALA	82	42.976	18.981	−8.373	0.00	0.00
ATOM	623	O	ALA	82	41.993	18.260	−8.360	0.00	0.00
ATOM	624	CB	ALA	82	44.435	19.755	−6.399	0.00	0.00
ATOM	625	N	ALA	83	43.136	19.965	−9.268	0.00	0.00
ATOM	626	CA	ALA	83	42.141	20.304	−10.312	0.00	0.00
ATOM	627	C	ALA	83	41.828	19.077	−11.268	0.00	0.00
ATOM	628	O	ALA	83	40.811	19.103	−11.971	0.00	0.00
ATOM	629	CB	ALA	83	42.650	21.550	−11.054	0.00	0.00
ATOM	630	N	HIS	84	42.891	18.376	−11.576	0.00	0.00
ATOM	631	CA	HIS	84	42.958	17.165	−12.398	0.00	0.00
ATOM	632	C	HIS	84	42.028	16.030	−11.809	0.00	0.00
ATOM	633	O	HIS	84	41.235	15.500	−12.565	0.00	0.00
ATOM	634	CB	HIS	84	44.382	16.640	−12.463	0.00	0.00
ATOM	635	CG	HIS	84	44.760	15.548	−13.463	0.00	0.00
ATOM	636	ND1	HIS	84	44.935	15.646	−14.803	0.00	0.00
ATOM	637	CD2	HIS	84	44.994	14.210	−13.119	0.00	0.00
ATOM	638	CE1	HIS	84	45.264	14.440	−15.259	0.00	0.00
ATOM	639	NE2	HIS	84	45.296	13.589	−14.240	0.00	0.00
ATOM	640	N	ILE	85	42.346	15.531	−10.644	0.00	0.00
ATOM	641	CA	ILE	85	41.509	14.569	−9.975	0.00	0.00
ATOM	642	C	ILE	85	40.053	15.091	−9.816	0.00	0.00
ATOM	643	O	ILE	85	39.108	14.292	−9.698	0.00	0.00
ATOM	644	CB	ILE	85	42.022	14.229	−8.542	0.00	0.00
ATOM	645	CG1	ILE	85	43.554	13.922	−8.531	0.00	0.00
ATOM	646	CG2	ILE	85	41.268	12.935	−7.991	0.00	0.00
ATOM	647	CD1	ILE	85	44.279	13.738	−7.202	0.00	0.00
ATOM	648	N	LEU	86	39.926	16.424	−9.611	0.00	0.00
ATOM	649	CA	LEU	86	38.609	17.112	−9.540	0.00	0.00
ATOM	650	C	LEU	86	37.823	16.861	−10.867	0.00	0.00
ATOM	651	O	LEU	86	36.620	16.648	−10.742	0.00	0.00
ATOM	652	CB	LEU	86	38.735	18.596	−9.181	0.00	0.00
ATOM	653	CG	LEU	86	39.164	18.771	−7.733	0.00	0.00
ATOM	654	CD1	LEU	86	39.621	20.240	−7.600	0.00	0.00
ATOM	655	CD2	LEU	86	37.928	18.518	−6.870	0.00	0.00
ATOM	656	N	MET	87	38.436	16.928	−12.084	0.00	0.00
ATOM	657	CA	MET	87	37.655	16.568	−13.299	0.00	0.00
ATOM	658	C	MET	87	37.911	15.103	−13.854	0.00	0.00
ATOM	659	O	MET	87	37.087	14.667	−14.659	0.00	0.00
ATOM	660	CB	MET	87	37.960	17.651	−14.309	0.00	0.00
ATOM	661	CG	MET	87	37.282	18.980	−13.996	0.00	0.00
ATOM	662	SD	MET	87	35.620	18.906	−13.432	0.00	0.00
ATOM	663	CE	MET	87	34.771	18.066	−14.859	0.00	0.00
ATOM	664	N	LYS	88	38.614	14.263	−13.045	0.00	0.00
ATOM	665	CA	LYS	88	39.049	12.872	−13.345	0.00	0.00
ATOM	666	C	LYS	88	39.857	12.716	−14.618	0.00	0.00
ATOM	667	O	LYS	88	40.062	11.530	−15.008	0.00	0.00
ATOM	668	CB	LYS	88	37.959	11.882	−13.158	0.00	0.00
ATOM	669	CG	LYS	88	38.262	10.416	−13.094	0.00	0.00
ATOM	670	CD	LYS	88	38.756	10.031	−11.699	0.00	0.00
ATOM	671	CE	LYS	88	37.640	10.036	−10.635	0.00	0.00
ATOM	672	NZ	LYS	88	36.697	8.934	−10.803	0.00	0.00
ATOM	673	N	MET	89	40.835	13.607	−14.726	0.00	0.00
ATOM	674	CA	MET	89	41.588	13.659	−15.977	0.00	0.00
ATOM	675	C	MET	89	42.569	14.781	−16.113	0.00	0.00
ATOM	676	O	MET	89	42.388	15.689	−15.315	0.00	0.00
ATOM	677	CB	MET	89	40.620	14.185	−16.906	0.00	0.00
ATOM	678	CG	MET	89	39.791	15.253	−17.061	0.00	0.00
ATOM	679	SD	MET	89	38.239	15.215	−18.089	0.00	0.00
ATOM	680	CE	MET	89	37.447	16.632	−17.336	0.00	0.00
ATOM	681	N	TRP	90	43.046	15.075	−17.322	0.00	0.00
ATOM	682	CA	TRP	90	43.870	16.271	−17.376	0.00	0.00
ATOM	683	C	TRP	90	43.157	17.473	−18.127	0.00	0.00
ATOM	684	O	TRP	90	43.256	17.525	−19.355	0.00	0.00
ATOM	685	CB	TRP	90	45.035	15.810	−18.252	0.00	0.00
ATOM	686	CG	TRP	90	46.280	15.330	−17.500	0.00	0.00
ATOM	687	CD1	TRP	90	46.622	14.011	−17.620	0.00	0.00
ATOM	688	CD2	TRP	90	47.086	15.997	−16.588	0.00	0.00
ATOM	689	NE1	TRP	90	47.629	13.833	−16.787	0.00	0.00
ATOM	690	CE2	TRP	90	47.934	14.985	−16.163	0.00	0.00
ATOM	691	CE3	TRP	90	47.243	17.267	−16.067	0.00	0.00
ATOM	692	CZ2	TRP	90	48.911	15.211	−15.222	0.00	0.00
ATOM	693	CZ3	TRP	90	48.227	17.498	−15.122	0.00	0.00
ATOM	694	CH2	TRP	90	49.061	16.482	−14.708	0.00	0.00
ATOM	695	N	THR	91	42.186	18.199	−17.532	0.00	0.00
ATOM	696	CA	THR	91	41.525	19.409	−18.104	0.00	0.00
ATOM	697	C	THR	91	42.543	20.439	−18.731	0.00	0.00
ATOM	698	O	THR	91	42.223	20.924	−19.822	0.00	0.00
ATOM	699	CB	THR	91	40.683	20.109	−16.980	0.00	0.00
ATOM	700	OG1	THR	91	39.722	19.201	−16.374	0.00	0.00
ATOM	701	CG2	THR	91	40.033	21.465	−17.357	0.00	0.00
ATOM	702	N	PHE	92	43.801	20.601	−18.218	0.00	0.00
ATOM	703	CA	PHE	92	44.763	21.604	−18.739	0.00	0.00
ATOM	704	C	PHE	92	45.739	21.075	−19.868	0.00	0.00
ATOM	705	O	PHE	92	46.684	21.818	−20.202	0.00	0.00
ATOM	706	CB	PHE	92	45.489	22.310	−17.588	0.00	0.00
ATOM	707	CG	PHE	92	44.619	22.895	−16.507	0.00	0.00
ATOM	708	CD1	PHE	92	43.531	23.683	−16.857	0.00	0.00
ATOM	709	CD2	PHE	92	44.911	22.684	−15.182	0.00	0.00
ATOM	710	CE1	PHE	92	42.767	24.242	−15.861	0.00	0.00
ATOM	711	CE2	PHE	92	44.140	23.247	−14.196	0.00	0.00
ATOM	712	CZ	PHE	92	43.063	24.031	−14.529	0.00	0.00
ATOM	713	N	GLY	93	45.474	19.943	−20.558	0.00	0.00
ATOM	714	CA	GLY	93	46.323	19.501	−21.684	0.00	0.00
ATOM	715	C	GLY	93	47.591	18.760	−21.176	0.00	0.00
ATOM	716	O	GLY	93	47.600	18.306	−20.027	0.00	0.00
ATOM	717	N	ASN	94	48.385	18.193	−22.085	0.00	0.00
ATOM	718	CA	ASN	94	49.652	17.570	−21.646	0.00	0.00
ATOM	719	C	ASN	94	50.538	18.566	−20.791	0.00	0.00
ATOM	720	O	ASN	94	51.581	18.103	−20.350	0.00	0.00
ATOM	721	CB	ASN	94	50.435	17.120	−22.880	0.00	0.00
ATOM	722	CG	ASN	94	49.988	15.808	−23.443	0.00	0.00
ATOM	723	OD1	ASN	94	50.879	15.087	−23.971	0.00	0.00
ATOM	724	ND2	ASN	94	48.838	15.363	−23.064	0.00	0.00
ATOM	725	N	PHE	95	50.495	19.898	−21.086	0.00	0.00
ATOM	726	CA	PHE	95	51.204	20.883	−20.275	0.00	0.00
ATOM	727	C	PHE	95	50.808	20.740	−18.792	0.00	0.00
ATOM	728	O	PHE	95	51.649	21.040	−17.959	0.00	0.00
ATOM	729	CB	PHE	95	50.854	22.312	−20.793	0.00	0.00
ATOM	730	CG	PHE	95	51.129	22.563	−22.264	0.00	0.00
ATOM	731	CD1	PHE	95	52.366	22.194	−22.828	0.00	0.00
ATOM	732	CD2	PHE	95	50.213	23.229	−23.065	0.00	0.00
ATOM	733	CE1	PHE	95	52.598	22.522	−24.146	0.00	0.00
ATOM	734	CE2	PHE	95	50.470	23.565	−24.370	0.00	0.00
ATOM	735	CZ	PHE	95	51.678	23.174	−24.937	0.00	0.00
ATOM	736	N	TRP	96	49.605	20.216	−18.469	0.00	0.00
ATOM	737	CA	TRP	96	49.185	20.011	−17.147	0.00	0.00
ATOM	738	C	TRP	96	49.967	18.697	−16.740	0.00	0.00
ATOM	739	O	TRP	96	50.722	18.721	−15.744	0.00	0.00
ATOM	740	CB	TRP	96	47.644	20.024	−17.218	0.00	0.00
ATOM	741	CG	TRP	96	47.053	20.008	−15.764	0.00	0.00
ATOM	742	CD1	TRP	96	47.715	20.551	−14.701	0.00	0.00
ATOM	743	CD2	TRP	96	45.770	19.628	−15.445	0.00	0.00
ATOM	744	NE1	TRP	96	46.862	20.533	−13.727	0.00	0.00
ATOM	745	CE2	TRP	96	45.692	19.997	−14.112	0.00	0.00
ATOM	746	CE3	TRP	96	44.686	19.042	−16.056	0.00	0.00
ATOM	747	CZ2	TRP	96	44.544	19.797	−13.368	0.00	0.00
ATOM	748	CZ3	TRP	96	43.534	18.843	−15.308	0.00	0.00
ATOM	749	CH2	TRP	96	43.461	19.220	−13.971	0.00	0.00
ATOM	750	N	CYS	97	49.987	17.655	−17.604	0.00	0.00
ATOM	751	CA	CYS	97	50.725	16.429	−17.401	0.00	0.00
ATOM	752	C	CYS	97	52.245	16.736	−17.168	0.00	0.00
ATOM	753	O	CYS	97	52.633	16.626	−16.014	0.00	0.00
ATOM	754	CB	CYS	97	50.428	15.492	−18.525	0.00	0.00
ATOM	755	SG	CYS	97	51.381	13.975	−18.578	0.00	0.00
ATOM	756	N	GLU	98	52.879	17.602	−17.987	0.00	0.00
ATOM	757	CA	GLU	98	54.245	18.070	−17.865	0.00	0.00
ATOM	758	C	GLU	98	54.545	18.732	−16.505	0.00	0.00
ATOM	759	O	GLU	98	55.623	18.429	−15.996	0.00	0.00
ATOM	760	CB	GLU	98	54.557	19.032	−19.023	0.00	0.00
ATOM	761	CG	GLU	98	54.864	18.271	−20.301	0.00	0.00
ATOM	762	CD	GLU	98	54.979	19.029	−21.579	0.00	0.00
ATOM	763	OE1	GLU	98	55.744	18.638	−22.463	0.00	0.00
ATOM	764	OE2	GLU	98	54.173	19.993	−21.663	0.00	0.00
ATOM	765	N	PHE	99	53.811	19.759	−16.056	0.00	0.00
ATOM	766	CA	PHE	99	54.094	20.249	−14.742	0.00	0.00
ATOM	767	C	PHE	99	53.884	19.218	−13.604	0.00	0.00
ATOM	768	O	PHE	99	54.907	18.768	−13.170	0.00	0.00
ATOM	769	CB	PHE	99	53.285	21.488	−14.493	0.00	0.00
ATOM	770	CG	PHE	99	53.606	22.791	−15.057	0.00	0.00
ATOM	771	CD1	PHE	99	52.961	23.287	−16.189	0.00	0.00
ATOM	772	CD2	PHE	99	54.631	23.594	−14.505	0.00	0.00
ATOM	773	CE1	PHE	99	53.274	24.513	−16.781	0.00	0.00
ATOM	774	CE2	PHE	99	54.965	24.803	−15.088	0.00	0.00
ATOM	775	CZ	PHE	99	54.280	25.277	−16.208	0.00	0.00
ATOM	776	N	TRP	100	52.784	18.419	−13.607	0.00	0.00
ATOM	777	CA	TRP	100	52.538	17.527	−12.479	0.00	0.00
ATOM	778	C	TRP	100	53.638	16.415	−12.443	0.00	0.00
ATOM	779	O	TRP	100	53.840	15.885	−11.364	0.00	0.00
ATOM	780	CB	TRP	100	51.061	17.129	−12.291	0.00	0.00
ATOM	781	CG	TRP	100	50.775	15.985	−11.326	0.00	0.00
ATOM	782	CD1	TRP	100	50.257	14.801	−11.764	0.00	0.00
ATOM	783	CD2	TRP	100	50.829	16.054	−9.952	0.00	0.00
ATOM	784	NE1	TRP	100	49.964	14.125	−10.688	0.00	0.00
ATOM	785	CE2	TRP	100	50.280	14.818	−9.587	0.00	0.00
ATOM	786	CE3	TRP	100	51.240	16.960	−8.964	0.00	0.00
ATOM	787	CZ2	TRP	100	50.135	14.476	−8.242	0.00	0.00
ATOM	788	CZ3	TRP	100	51.096	16.612	−7.617	0.00	0.00
ATOM	789	CH2	TRP	100	50.547	15.379	−17.259	0.00	0.00
ATOM	790	N	THR	101	54.096	15.831	−13.586	0.00	0.00
ATOM	791	CA	THR	101	55.199	14.829	−13.645	0.00	0.00
ATOM	792	C	THR	101	56.541	15.514	−13.136	0.00	0.00
ATOM	793	O	THR	101	57.270	14.858	−12.411	0.00	0.00
ATOM	794	CB	THR	101	55.487	14.330	−15.114	0.00	0.00
ATOM	795	OG1	THR	101	56.617	14.807	−15.774	0.00	0.00
ATOM	796	CG2	THR	101	54.249	14.399	−16.034	0.00	0.00
ATOM	797	N	SER	102	56.977	16.562	−13.891	0.00	0.00
ATOM	798	CA	SER	102	58.230	17.288	−13.695	0.00	0.00
ATOM	799	C	SER	102	58.493	17.726	−12.252	0.00	0.00
ATOM	800	O	SER	102	59.643	18.049	−12.004	0.00	0.00
ATOM	801	CB	SER	102	58.290	18.541	−14.597	0.00	0.00
ATOM	802	OG	SER	102	57.326	19.604	−14.314	0.00	0.00
ATOM	803	N	ILE	103	57.498	18.194	−11.504	0.00	0.00
ATOM	804	CA	ILE	103	57.805	18.592	−10.129	0.00	0.00
ATOM	805	C	ILE	103	57.642	17.333	−9.192	0.00	0.00
ATOM	806	O	ILE	103	58.307	17.340	−8.200	0.00	0.00
ATOM	807	CB	ILE	103	56.927	19.793	−9.660	0.00	0.00
ATOM	808	CG1	ILE	103	56.867	21.005	−10.559	0.00	0.00
ATOM	809	CG2	ILE	103	57.038	20.140	−8.128	0.00	0.00
ATOM	810	CD1	ILE	103	58.118	21.867	−10.467	0.00	0.00
ATOM	811	N	ASP	104	56.814	16.307	−9.549	0.00	0.00
ATOM	812	CA	ASP	104	56.778	15.101	−8.699	0.00	0.00
ATOM	813	C	ASP	104	58.226	14.467	−8.795	0.00	0.00
ATOM	814	O	ASP	104	58.541	13.694	−7.856	0.00	0.00
ATOM	815	CB	ASP	104	55.674	14.064	−9.083	0.00	0.00
ATOM	816	CG	ASP	104	56.166	12.599	−9.100	0.00	0.00
ATOM	817	OD1	ASP	104	57.343	12.261	−8.980	0.00	0.00
ATOM	818	OD2	ASP	104	56.699	12.249	−10.146	0.00	0.00
ATOM	819	N	VAL	105	58.786	14.256	−9.999	0.00	0.00
ATOM	820	CA	VAL	105	60.153	13.771	−10.254	0.00	0.00
ATOM	821	C	VAL	105	61.193	14.809	−9.731	0.00	0.00
ATOM	822	O	VAL	105	62.197	14.345	−9.219	0.00	0.00
ATOM	823	CB	VAL	105	60.394	13.461	−11.753	0.00	0.00
ATOM	824	CG1	VAL	105	61.719	12.731	−12.116	0.00	0.00
ATOM	825	CG2	VAL	105	59.213	12.710	−12.348	0.00	0.00
ATOM	826	N	LEU	106	61.182	16.101	−10.177	0.00	0.00
ATOM	827	CA	LEU	106	62.138	17.132	−9.695	0.00	0.00
ATOM	828	C	LEU	106	62.276	17.070	−8.133	0.00	0.00
ATOM	829	O	LEU	106	63.369	17.421	−7.669	0.00	0.00
ATOM	830	CB	LEU	106	61.697	18.542	−10.136	0.00	0.00
ATOM	831	CG	LEU	106	62.609	19.695	−9.718	0.00	0.00
ATOM	832	CD1	LEU	106	63.952	19.564	−10.420	0.00	0.00
ATOM	833	CD2	LEU	106	61.976	21.041	−10.005	0.00	0.00
ATOM	834	N	CYS	107	61.177	17.064	−7.378	0.00	0.00
ATOM	835	CA	CYS	107	61.166	16.951	−5.934	0.00	0.00
ATOM	836	C	CYS	107	61.858	15.619	−5.442	0.00	0.00
ATOM	837	O	CYS	107	62.426	15.683	−4.358	0.00	0.00
ATOM	838	CB	CYS	107	59.715	17.074	−5.552	0.00	0.00
ATOM	839	SG	CYS	107	58.552	15.718	−5.932	0.00	0.00
ATOM	840	N	VAL	108	61.441	14.446	−5.908	0.00	0.00
ATOM	841	CA	VAL	108	61.990	13.169	−5.539	0.00	0.00
ATOM	842	C	VAL	108	63.511	13.138	−5.808	0.00	0.00
ATOM	843	O	VAL	108	64.173	12.308	−5.153	0.00	0.00
ATOM	844	CB	VAL	108	61.216	12.105	−6.342	0.00	0.00
ATOM	845	CG1	VAL	108	61.931	10.740	−6.173	0.00	0.00
ATOM	846	CG2	VAL	108	59.787	11.961	−5.804	0.00	0.00
ATOM	847	N	THR	109	63.825	13.360	−7.095	0.00	0.00
ATOM	848	CA	THR	109	65.172	13.475	−7.545	0.00	0.00
ATOM	849	C	THR	109	65.960	14.396	−6.661	0.00	0.00
ATOM	850	O	THR	109	67.131	14.080	−6.469	0.00	0.00
ATOM	851	CB	THR	109	65.313	13.934	−9.044	0.00	0.00
ATOM	852	OG1	THR	109	64.849	15.322	−9.254	0.00	0.00
ATOM	853	CG2	THR	109	64.839	12.860	−10.004	0.00	0.00
ATOM	854	N	ALA	110	65.516	15.665	−6.497	0.00	0.00
ATOM	855	CA	ALA	110	66.155	16.591	−5.576	0.00	0.00
ATOM	856	C	ALA	110	66.255	15.873	−4.194	0.00	0.00
ATOM	857	O	ALA	110	67.276	16.076	−3.556	0.00	0.00
ATOM	858	CB	ALA	110	65.408	17.935	−5.515	0.00	0.00
ATOM	859	N	SER	111	65.236	15.077	−3.746	0.00	0.00
ATOM	860	CA	SER	111	65.227	14.269	−2.529	0.00	0.00
ATOM	861	C	SER	111	66.295	13.114	−2.570	0.00	0.00
ATOM	862	O	SER	111	66.920	12.929	−1.525	0.00	0.00
ATOM	863	CB	SER	111	63.818	13.726	−2.274	0.00	0.00
ATOM	864	OG	SER	111	62.863	14.656	−1.786	0.00	0.00
ATOM	865	N	ILE	112	66.285	12.165	−3.551	0.00	0.00
ATOM	866	CA	ILE	112	67.334	11.114	−3.636	0.00	0.00
ATOM	867	C	ILE	112	68.779	11.694	−3.829	0.00	0.00
ATOM	868	O	ILE	112	69.693	11.056	−3.308	0.00	0.00
ATOM	869	CB	ILE	112	66.898	10.050	−4.695	0.00	0.00
ATOM	870	CG1	ILE	112	67.645	8.707	−4.422	0.00	0.00
ATOM	871	CG2	ILE	112	67.059	10.589	−6.130	0.00	0.00
ATOM	872	CD1	ILE	112	67.444	7.643	−5.511	0.00	0.00
ATOM	873	N	GLU	113	69.000	12.773	−4.601	0.00	0.00
ATOM	874	CA	GLU	113	70.311	13.372	−4.746	0.00	0.00
ATOM	875	C	GLU	113	70.751	14.076	−3.406	0.00	0.00
ATOM	876	O	GLU	113	71.967	14.174	−3.217	0.00	0.00
ATOM	877	CB	GLU	113	70.229	14.416	−5.878	0.00	0.00
ATOM	878	CG	GLU	113	70.477	13.968	−7.305	0.00	0.00
ATOM	879	CD	GLU	113	71.163	12.635	−7.313	0.00	0.00
ATOM	880	OE1	GLU	113	70.737	11.633	−7.846	0.00	0.00
ATOM	881	OE2	GLU	113	72.203	12.723	−6.630	0.00	0.00
ATOM	882	N	THR	114	69.871	14.816	−2.700	0.00	0.00
ATOM	883	CA	THR	114	70.150	15.420	−1.399	0.00	0.00
ATOM	884	C	THR	114	70.643	14.297	−0.442	0.00	0.00
ATOM	885	O	THR	114	71.465	14.642	0.413	0.00	0.00
ATOM	886	CB	THR	114	68.951	16.274	−0.884	0.00	0.00
ATOM	887	OG1	THR	114	69.270	17.185	0.202	0.00	0.00
ATOM	888	CG2	THR	114	67.600	15.671	−0.696	0.00	0.00
ATOM	889	N	LEU	115	69.983	13.126	−0.388	0.00	0.00
ATOM	890	CA	LEU	115	70.445	11.994	0.402	0.00	0.00
ATOM	891	C	LEU	115	71.899	11.624	−0.004	0.00	0.00
ATOM	892	O	LEU	115	72.579	11.041	0.858	0.00	0.00
ATOM	893	CB	LEU	115	69.493	10.830	0.166	0.00	0.00
ATOM	894	CG	LEU	115	68.152	10.983	0.836	0.00	0.00
ATOM	895	CD1	LEU	115	67.237	9.771	0.651	0.00	0.00
ATOM	896	CD2	LEU	115	68.250	11.198	2.346	0.00	0.00
ATOM	897	N	CYS	116	72.286	11.660	−1.293	0.00	0.00
ATOM	898	CA	CYS	116	73.668	11.408	−1.755	0.00	0.00
ATOM	899	C	CYS	116	74.596	12.440	−1.068	0.00	0.00
ATOM	900	O	CYS	116	75.490	11.995	−0.365	0.00	0.00
ATOM	901	CB	CYS	116	73.797	11.419	−3.275	0.00	0.00
ATOM	902	SG	CYS	116	75.530	11.348	−3.777	0.00	0.00
ATOM	903	N	VAL	117	74.299	13.684	−1.141	0.00	0.00
ATOM	904	CA	VAL	117	75.167	14.619	−0.418	0.00	0.00
ATOM	905	C	VAL	117	75.291	14.292	1.060	0.00	0.00
ATOM	906	O	VAL	117	76.414	14.462	1.571	0.00	0.00
ATOM	907	CB	VAL	117	74.769	16.096	−0.607	0.00	0.00
ATOM	908	CG1	VAL	117	75.598	17.039	0.227	0.00	0.00
ATOM	909	CG2	VAL	117	74.706	16.504	−2.058	0.00	0.00
ATOM	910	N	ILE	118	74.148	14.231	1.752	0.00	0.00
ATOM	911	CA	ILE	118	74.120	13.901	3.157	0.00	0.00
ATOM	912	C	ILE	118	74.972	12.690	3.547	0.00	0.00
ATOM	913	O	ILE	118	75.595	12.812	4.610	0.00	0.00
ATOM	914	CB	ILE	118	72.633	13.622	3.493	0.00	0.00
ATOM	915	CG1	ILE	118	71.823	14.882	3.577	0.00	0.00
ATOM	916	CG2	ILE	118	72.533	12.995	4.913	0.00	0.00
ATOM	917	CD1	ILE	118	70.275	14.737	3.570	0.00	0.00
ATOM	918	N	ALA	119	74.753	11.501	2.984	0.00	0.00
ATOM	919	CA	ALA	119	75.521	10.310	3.193	0.00	0.00
ATOM	920	C	ALA	119	77.043	10.591	3.206	0.00	0.00
ATOM	921	O	ALA	119	77.679	10.162	4.163	0.00	0.00
ATOM	922	CB	ALA	119	75.108	9.254	2.142	0.00	0.00
ATOM	923	N	VAL	120	77.635	11.167	2.145	0.00	0.00
ATOM	924	CA	VAL	120	79.070	11.568	2.079	0.00	0.00
ATOM	925	C	VAL	120	79.413	12.579	3.207	0.00	0.00
ATOM	926	O	VAL	120	80.571	12.565	3.614	0.00	0.00
ATOM	927	CB	VAL	120	79.427	12.188	0.717	0.00	0.00
ATOM	928	CG1	VAL	120	80.872	12.662	0.544	0.00	0.00
ATOM	929	CG2	VAL	120	79.086	11.320	−0.468	0.00	0.00
ATOM	930	N	ASP	121	78.549	13.579	3.461	0.00	0.00
ATOM	931	CA	ASP	121	78.766	14.500	4.557	0.00	0.00
ATOM	932	C	ASP	121	78.988	13.688	5.883	0.00	0.00
ATOM	933	O	ASP	121	79.942	14.049	6.576	0.00	0.00
ATOM	934	CB	ASP	121	77.635	15.519	4.591	0.00	0.00
ATOM	935	CG	ASP	121	77.951	16.731	5.370	0.00	0.00
ATOM	936	OD1	ASP	121	79.163	16.803	5.650	0.00	0.00
ATOM	937	OD2	ASP	121	77.082	17.535	5.712	0.00	0.00
ATOM	938	N	ARG	122	78.040	12.839	6.355	0.00	0.00
ATOM	939	CA	ARG	122	78.207	11.978	7.529	0.00	0.00
ATOM	940	C	ARG	122	79.440	11.028	7.420	0.00	0.00
ATOM	941	O	ARG	122	79.798	10.489	8.459	0.00	0.00
ATOM	942	CB	ARG	122	76.924	11.348	8.039	0.00	0.00
ATOM	943	CG	ARG	122	75.687	12.159	8.261	0.00	0.00
ATOM	944	CD	ARG	122	75.843	13.430	9.133	0.00	0.00
ATOM	945	NE	ARG	122	76.220	14.653	8.409	0.00	0.00
ATOM	946	CZ	ARG	122	75.826	15.885	8.799	0.00	0.00
ATOM	947	NH1	ARG	122	75.074	16.078	9.884	0.00	0.00
ATOM	948	NH2	ARG	122	76.189	16.966	8.101	0.00	0.00
ATOM	949	N	TYR	123	79.859	10.558	6.204	0.00	0.00
ATOM	950	CA	TYR	123	81.049	9.753	5.968	0.00	0.00
ATOM	951	C	TYR	123	82.288	10.614	6.317	0.00	0.00
ATOM	952	O	TYR	123	82.879	10.316	7.360	0.00	0.00
ATOM	953	CB	TYR	123	81.120	9.261	4.533	0.00	0.00
ATOM	954	CG	TYR	123	82.321	8.407	4.234	0.00	0.00
ATOM	955	CD1	TYR	123	82.330	7.060	4.602	0.00	0.00
ATOM	956	CD2	TYR	123	83.456	8.936	3.622	0.00	0.00
ATOM	957	CE1	TYR	123	83.431	6.260	4.379	0.00	0.00
ATOM	958	CE2	TYR	123	84.564	8.142	3.390	0.00	0.00
ATOM	959	CZ	TYR	123	84.543	6.802	3.773	0.00	0.00
ATOM	960	OH	TYR	123	85.632	5.992	3.549	0.00	0.00
ATOM	961	N	PHE	124	82.526	11.773	5.665	0.00	0.00
ATOM	962	CA	PHE	124	83.617	12.690	5.992	0.00	0.00
ATOM	963	C	PHE	124	83.653	13.056	7.515	0.00	0.00
ATOM	964	O	PHE	124	84.752	12.987	8.077	0.00	0.00
ATOM	965	CB	PHE	124	83.501	13.938	5.138	0.00	0.00
ATOM	966	CG	PHE	124	83.784	13.818	3.671	0.00	0.00
ATOM	967	CD1	PHE	124	84.853	13.053	3.210	0.00	0.00
ATOM	968	CD2	PHE	124	83.013	14.534	2.770	0.00	0.00
ATOM	969	CE1	PHE	124	85.154	12.994	1.841	0.00	0.00
ATOM	970	CE2	PHE	124	83.269	14.475	1.386	0.00	0.00
ATOM	971	CZ	PHE	124	84.334	13.673	0.940	0.00	0.00
ATOM	972	N	ALA	125	82.551	13.485	8.129	0.00	0.00
ATOM	973	CA	ALA	125	82.450	13.854	9.541	0.00	0.00
ATOM	974	C	ALA	125	82.577	12.638	10.541	0.00	0.00
ATOM	975	O	ALA	125	83.512	12.706	11.351	0.00	0.00
ATOM	976	CB	ALA	125	81.124	14.613	9.708	0.00	0.00
ATOM	977	N	ILE	126	81.724	11.612	10.503	0.00	0.00
ATOM	978	CA	ILE	126	81.675	10.489	11.428	0.00	0.00
ATOM	979	C	ILE	126	82.649	9.309	11.082	0.00	0.00
ATOM	980	O	ILE	126	83.173	8.760	12.042	0.00	0.00
ATOM	981	CB	ILE	126	80.185	10.023	11.506	0.00	0.00
ATOM	982	CG1	ILE	126	79.238	11.203	11.707	0.00	0.00
ATOM	983	CG2	ILE	126	79.967	8.876	12.534	0.00	0.00
ATOM	984	CD1	ILE	126	77.798	10.883	11.185	0.00	0.00
ATOM	985	N	THR	127	82.737	8.759	9.833	0.00	0.00
ATOM	986	CA	THR	127	83.734	7.704	9.468	0.00	0.00
ATOM	987	C	THR	127	85.221	8.238	9.633	0.00	0.00
ATOM	988	O	THR	127	86.114	7.399	9.803	0.00	0.00
ATOM	989	CB	THR	127	83.404	7.037	8.085	0.00	0.00
ATOM	990	OG1	THR	127	82.073	6.422	8.089	0.00	0.00
ATOM	991	CG2	THR	127	84.462	5.941	7.748	0.00	0.00
ATOM	992	N	SER	128	85.346	9.526	10.025	0.00	0.00
ATOM	993	CA	SER	128	86.559	10.230	10.268	0.00	0.00
ATOM	994	C	SER	128	87.536	10.270	9.077	0.00	0.00
ATOM	995	O	SER	128	88.728	10.428	9.357	0.00	0.00
ATOM	996	CB	SER	128	87.230	9.596	11.492	0.00	0.00
ATOM	997	OG	SER	128	86.518	9.491	12.695	0.00	0.00
ATOM	998	N	PRO	129	87.124	10.335	7.774	0.00	0.00
ATOM	999	CA	PRO	129	88.092	10.475	6.707	0.00	0.00
ATOM	1000	C	PRO	129	88.773	11.905	6.768	0.00	0.00
ATOM	1001	O	PRO	129	88.502	12.723	7.646	0.00	0.00
ATOM	1002	CB	PRO	129	87.433	10.181	5.307	0.00	0.00
ATOM	1003	CG	PRO	129	85.933	10.303	5.665	0.00	0.00
ATOM	1004	CD	PRO	129	85.739	10.164	7.155	0.00	0.00
ATOM	1005	N	PHE	130	89.412	12.196	5.637	0.00	0.00
ATOM	1006	CA	PHE	130	90.233	13.323	5.403	0.00	0.00
ATOM	1007	C	PHE	130	91.324	13.284	6.513	0.00	0.00
ATOM	1008	O	PHE	130	91.857	12.160	6.716	0.00	0.00
ATOM	1009	CB	PHE	130	89.441	14.572	5.319	0.00	0.00
ATOM	1010	CG	PHE	130	89.016	15.047	4.005	0.00	0.00
ATOM	1011	CD1	PHE	130	88.232	14.217	3.216	0.00	0.00
ATOM	1012	CD2	PHE	130	89.337	16.313	3.521	0.00	0.00
ATOM	1013	CE1	PHE	130	87.765	14.601	1.970	0.00	0.00
ATOM	1014	CE2	PHE	130	88.886	16.741	2.273	0.00	0.00
ATOM	1015	CZ	PHE	130	88.103	15.876	1.515	0.00	0.00
ATOM	1016	N	LYS	131	91.942	14.333	6.873	0.00	0.00
ATOM	1017	CA	LYS	131	92.906	14.276	7.987	0.00	0.00
ATOM	1018	C	LYS	131	93.203	15.687	8.526	0.00	0.00
ATOM	1019	O	LYS	131	93.553	15.750	9.718	0.00	0.00
ATOM	1020	CB	LYS	131	94.165	13.458	7.631	0.00	0.00
ATOM	1021	CG	LYS	131	95.046	13.905	6.493	0.00	0.00
ATOM	1022	CD	LYS	131	96.315	13.128	6.784	0.00	0.00
ATOM	1023	CE	LYS	131	97.259	13.103	5.596	0.00	0.00
ATOM	1024	NZ	LYS	131	98.543	12.573	6.028	0.00	0.00
ATOM	1025	N	TYR	132	93.659	16.525	7.543	0.00	0.00
ATOM	1026	CA	TYR	132	94.073	17.831	7.924	0.00	0.00
ATOM	1027	C	TYR	132	92.842	18.705	8.212	0.00	0.00
ATOM	1028	O	TYR	132	92.453	19.571	7.419	0.00	0.00
ATOM	1029	CB	TYR	132	94.985	18.438	6.842	0.00	0.00
ATOM	1030	CG	TYR	132	95.949	19.482	7.410	0.00	0.00
ATOM	1031	CD1	TYR	132	95.872	20.813	6.970	0.00	0.00
ATOM	1032	CD2	TYR	132	96.943	19.210	8.365	0.00	0.00
ATOM	1033	CE1	TYR	132	96.770	21.807	7.381	0.00	0.00
ATOM	1034	CE2	TYR	132	97.853	20.179	8.801	0.00	0.00
ATOM	1035	CZ	TYR	132	97.779	21.491	8.302	0.00	0.00
ATOM	1036	OH	TYR	132	98.676	22.453	8.660	0.00	0.00
ATOM	1037	N	GLN	133	92.138	18.248	9.240	0.00	0.00
ATOM	1038	CA	GLN	133	91.018	18.854	9.828	0.00	0.00
ATOM	1039	C	GLN	133	89.976	19.469	8.797	0.00	0.00
ATOM	1040	O	GLN	133	89.541	20.605	9.064	0.00	0.00
ATOM	1041	CB	GLN	133	91.574	19.853	10.849	0.00	0.00
ATOM	1042	CG	GLN	133	92.221	21.074	10.257	0.00	0.00
ATOM	1043	CD	GLN	133	92.996	21.792	11.345	0.00	0.00
ATOM	1044	OE1	GLN	133	93.344	22.968	11.218	0.00	0.00
ATOM	1045	NE2	GLN	133	93.336	21.157	12.454	0.00	0.00
ATOM	1046	N	SER	134	89.390	18.713	7.853	0.00	0.00
ATOM	1047	CA	SER	134	88.367	19.342	6.961	0.00	0.00
ATOM	1048	C	SER	134	86.948	19.406	7.645	0.00	0.00
ATOM	1049	O	SER	134	86.437	18.338	8.020	0.00	0.00
ATOM	1050	CB	SER	134	88.185	18.534	5.679	0.00	0.00
ATOM	1051	OG	SER	134	87.903	17.158	5.817	0.00	0.00
ATOM	1052	N	LEU	135	86.343	20.593	7.908	0.00	0.00
ATOM	1053	CA	LEU	135	84.986	20.686	8.449	0.00	0.00
ATOM	1054	C	LEU	135	83.978	21.632	7.663	0.00	0.00
ATOM	1055	O	LEU	135	84.002	22.856	7.858	0.00	0.00
ATOM	1056	CB	LEU	135	85.059	21.148	9.908	0.00	0.00
ATOM	1057	CG	LEU	135	83.661	21.190	10.628	0.00	0.00
ATOM	1058	CD1	LEU	135	83.021	19.795	10.637	0.00	0.00
ATOM	1059	CD2	LEU	135	83.842	21.695	12.048	0.00	0.00
ATOM	1060	N	LEU	136	83.400	21.126	6.543	0.00	0.00
ATOM	1061	CA	LEU	136	82.356	21.714	5.654	0.00	0.00
ATOM	1062	C	LEU	136	82.240	23.262	5.735	0.00	0.00
ATOM	1063	O	LEU	136	83.253	23.882	5.435	0.00	0.00
ATOM	1064	CB	LEU	136	81.075	21.036	5.993	0.00	0.00
ATOM	1065	CG	LEU	136	80.619	19.641	5.823	0.00	0.00
ATOM	1066	CD1	LEU	136	79.383	19.419	6.657	0.00	0.00
ATOM	1067	CD2	LEU	136	80.358	19.272	4.384	0.00	0.00
ATOM	1068	N	THR	137	81.030	23.867	5.532	0.00	0.00
ATOM	1069	CA	THR	137	80.694	25.318	5.666	0.00	0.00
ATOM	1070	C	THR	137	79.420	25.517	4.839	0.00	0.00
ATOM	1071	O	THR	137	78.557	24.637	4.730	0.00	0.00
ATOM	1072	CB	THR	137	81.795	26.387	5.306	0.00	0.00
ATOM	1073	OG1	THR	137	82.122	26.317	3.857	0.00	0.00
ATOM	1074	CG2	THR	137	82.912	26.327	6.306	0.00	0.00
ATOM	1075	N	LYS	138	79.086	26.774	4.709	0.00	0.00
ATOM	1076	CA	LYS	138	77.993	27.296	3.904	0.00	0.00
ATOM	1077	C	LYS	138	78.325	26.967	2.391	0.00	0.00
ATOM	1078	O	LYS	138	77.375	26.719	1.664	0.00	0.00
ATOM	1079	CB	LYS	138	78.023	28.822	4.135	0.00	0.00
ATOM	1080	CG	LYS	138	77.173	29.184	5.353	0.00	0.00
ATOM	1081	CD	LYS	138	76.874	30.674	5.437	0.00	0.00
ATOM	1082	CE	LYS	138	76.812	31.202	6.901	0.00	0.00
ATOM	1083	NZ	LYS	138	78.150	31.653	7.456	0.00	0.00
ATOM	1084	N	ASN	139	79.511	27.430	1.899	0.00	0.00
ATOM	1085	CA	ASN	139	79.969	27.231	0.550	0.00	0.00
ATOM	1086	C	ASN	139	79.905	25.729	0.037	0.00	0.00
ATOM	1087	O	ASN	139	79.597	25.547	−1.139	0.00	0.00
ATOM	1088	CB	ASN	139	81.236	28.015	0.183	0.00	0.00
ATOM	1089	CG	ASN	139	82.349	27.691	1.208	0.00	0.00
ATOM	1090	OD1	ASN	139	82.352	28.376	2.259	0.00	0.00
ATOM	1091	ND2	ASN	139	83.199	26.710	0.999	0.00	0.00
ATOM	1092	N	LYS	140	80.445	24.709	0.754	0.00	0.00
ATOM	1093	CA	LYS	140	80.326	23.249	0.435	0.00	0.00
ATOM	1094	C	LYS	140	78.793	22.868	0.384	0.00	0.00
ATOM	1095	O	LYS	140	78.457	22.067	−0.465	0.00	0.00
ATOM	1096	CB	LYS	140	81.089	22.373	1.426	0.00	0.00
ATOM	1097	CG	LYS	140	82.495	22.623	1.885	0.00	0.00
ATOM	1098	CD	LYS	140	83.473	21.961	0.898	0.00	0.00
ATOM	1099	CE	LYS	140	84.897	22.455	1.072	0.00	0.00
ATOM	1100	NZ	LYS	140	85.704	21.656	0.070	0.00	0.00
ATOM	1101	N	ALA	141	77.998	23.281	1.381	0.00	0.00
ATOM	1102	CA	ALA	141	76.555	23.120	1.464	0.00	0.00
ATOM	1103	C	ALA	141	75.877	23.676	0.146	0.00	0.00
ATOM	1104	O	ALA	141	74.754	23.247	−0.092	0.00	0.00
ATOM	1105	CB	ALA	141	76.040	23.850	2.716	0.00	0.00
ATOM	1106	N	ARG	142	76.258	24.862	−0.403	0.00	0.00
ATOM	1107	CA	ARG	142	75.758	25.401	−1.671	0.00	0.00
ATOM	1108	C	ARG	142	76.288	24.480	−2.833	0.00	0.00
ATOM	1109	O	ARG	142	75.710	24.586	−3.910	0.00	0.00
ATOM	1110	CB	ARG	142	76.189	26.877	−1.904	0.00	0.00
ATOM	1111	CG	ARG	142	75.685	27.464	−3.272	0.00	0.00
ATOM	1112	CD	ARG	142	74.172	27.451	−3.325	0.00	0.00
ATOM	1113	NE	ARG	142	73.773	28.183	−4.523	0.00	0.00
ATOM	1114	CZ	ARG	142	73.578	29.502	−4.551	0.00	0.00
ATOM	1115	NH1	ARG	142	73.721	30.238	−3.451	0.00	0.00
ATOM	1116	NH2	ARG	142	73.242	30.048	−5.718	0.00	0.00
ATOM	1117	N	VAL	143	77.539	23.956	−2.810	0.00	0.00
ATOM	1118	CA	VAL	143	78.058	23.010	−3.803	0.00	0.00
ATOM	1119	C	VAL	143	77.146	21.756	−3.867	0.00	0.00
ATOM	1120	O	VAL	143	77.005	21.265	−4.966	0.00	0.00
ATOM	1121	CB	VAL	143	79.529	22.650	−3.522	0.00	0.00
ATOM	1122	CG1	VAL	143	79.992	21.496	−4.403	0.00	0.00
ATOM	1123	CG2	VAL	143	80.444	23.863	−3.618	0.00	0.00
ATOM	1124	N	ILE	144	76.784	21.121	−2.753	0.00	0.00
ATOM	1125	CA	ILE	144	75.871	20.018	−2.668	0.00	0.00
ATOM	1126	C	ILE	144	74.396	20.377	−3.069	0.00	0.00
ATOM	1127	O	ILE	144	73.710	19.462	−3.507	0.00	0.00
ATOM	1128	CB	ILE	144	76.030	19.338	−1.262	0.00	0.00
ATOM	1129	CG1	ILE	144	75.955	20.321	−0.084	0.00	0.00
ATOM	1130	CG2	ILE	144	77.319	18.476	−1.197	0.00	0.00
ATOM	1131	CD1	ILE	144	75.655	19.620	1.286	0.00	0.00
ATOM	1132	N	ILE	145	73.790	21.504	−2.598	0.00	0.00
ATOM	1133	CA	ILE	145	72.468	21.974	−2.985	0.00	0.00
ATOM	1134	C	ILE	145	72.537	22.281	−4.534	0.00	0.00
ATOM	1135	O	ILE	145	71.513	22.105	−5.192	0.00	0.00
ATOM	1136	CB	ILE	145	71.867	23.141	−2.122	0.00	0.00
ATOM	1137	CG1	ILE	145	71.196	22.653	−0.784	0.00	0.00
ATOM	1138	CG2	ILE	145	70.718	23.933	−2.859	0.00	0.00
ATOM	1139	CD1	ILE	145	70.965	23.783	0.260	0.00	0.00
ATOM	1140	N	LEU	146	73.496	23.088	−5.044	0.00	0.00
ATOM	1141	CA	LEU	146	73.700	23.348	−6.479	0.00	0.00
ATOM	1142	C	LEU	146	73.816	21.999	−7.245	0.00	0.00
ATOM	1143	O	LEU	146	73.073	21.828	−8.213	0.00	0.00
ATOM	1144	CB	LEU	146	74.906	24.256	−6.738	0.00	0.00
ATOM	1145	CG	LEU	146	75.209	24.584	−8.196	0.00	0.00
ATOM	1146	CD1	LEU	146	74.077	25.426	−8.764	0.00	0.00
ATOM	1147	CD2	LEU	146	76.540	25.290	−8.348	0.00	0.00
ATOM	1148	N	MET	147	74.654	21.048	−6.790	0.00	0.00
ATOM	1149	CA	MET	147	74.786	19.722	−7.338	0.00	0.00
ATOM	1150	C	MET	147	73.445	18.924	−7.294	0.00	0.00
ATOM	1151	O	MET	147	73.185	18.247	−8.295	0.00	0.00
ATOM	1152	CB	MET	147	75.928	19.018	−6.589	0.00	0.00
ATOM	1153	CG	MET	147	75.850	17.518	−6.809	0.00	0.00
ATOM	1154	SD	MET	147	77.118	16.743	−5.821	0.00	0.00
ATOM	1155	CE	MET	147	78.101	16.256	−7.187	0.00	0.00
ATOM	1156	N	VAL	148	72.669	18.911	−6.190	0.00	0.00
ATOM	1157	CA	VAL	148	71.389	18.229	−6.189	0.00	0.00
ATOM	1158	C	VAL	148	70.479	18.726	−7.366	0.00	0.00
ATOM	1159	O	VAL	148	69.728	17.883	−7.844	0.00	0.00
ATOM	1160	CB	VAL	148	70.720	18.239	−4.802	0.00	0.00
ATOM	1161	CG1	VAL	148	71.533	17.505	−3.740	0.00	0.00
ATOM	1162	CG2	VAL	148	70.359	19.674	−4.394	0.00	0.00
ATOM	1163	N	TRP	149	70.187	20.036	−7.496	0.00	0.00
ATOM	1164	CA	TRP	149	69.448	20.603	−8.599	0.00	0.00
ATOM	1165	C	TRP	149	69.992	20.141	−9.985	0.00	0.00
ATOM	1166	O	TRP	149	69.160	20.098	−10.899	0.00	0.00
ATOM	1167	CB	TRP	149	69.479	22.113	−8.499	0.00	0.00
ATOM	1168	CG	TRP	149	68.602	22.778	−7.514	0.00	0.00
ATOM	1169	CD1	TRP	149	68.840	22.953	−6.178	0.00	0.00
ATOM	1170	CD2	TRP	149	67.319	23.365	−7.777	0.00	0.00
ATOM	1171	NE1	TRP	149	67.784	23.629	−5.572	0.00	0.00
ATOM	1172	CE2	TRP	149	66.848	23.888	−6.545	0.00	0.00
ATOM	1173	CE3	TRP	149	66.547	23.515	−8.924	0.00	0.00
ATOM	1174	CZ2	TRP	149	65.624	24.541	−6.444	0.00	0.00
ATOM	1175	CZ3	TRP	149	65.324	24.146	−8.825	0.00	0.00
ATOM	1176	CH2	TRP	149	64.878	24.659	−7.615	0.00	0.00
ATOM	1177	N	ILE	150	71.311	20.225	−10.275	0.00	0.00
ATOM	1178	CA	ILE	150	71.825	19.705	−11.512	0.00	0.00
ATOM	1179	C	ILE	150	71.385	18.232	−11.749	0.00	0.00
ATOM	1180	O	ILE	150	71.025	17.944	−12.889	0.00	0.00
ATOM	1181	CB	ILE	150	73.385	19.823	−11.568	0.00	0.00
ATOM	1182	CG1	ILE	150	73.924	21.225	−11.346	0.00	0.00
ATOM	1183	CG2	ILE	150	73.951	19.323	−12.935	0.00	0.00
ATOM	1184	CD1	ILE	150	75.439	21.137	−11.044	0.00	0.00
ATOM	1185	N	VAL	151	71.712	17.257	−10.882	0.00	0.00
ATOM	1186	CA	VAL	151	71.310	15.871	−11.121	0.00	0.00
ATOM	1187	C	VAL	151	69.751	15.692	−11.153	0.00	0.00
ATOM	1188	O	VAL	151	69.326	14.763	−11.854	0.00	0.00
ATOM	1189	CB	VAL	151	71.990	14.872	−10.198	0.00	0.00
ATOM	1190	CG1	VAL	151	71.490	13.431	−10.275	0.00	0.00
ATOM	1191	CG2	VAL	151	73.478	15.016	−10.190	0.00	0.00
ATOM	1192	N	SER	152	68.958	16.244	−10.213	0.00	0.00
ATOM	1193	CA	SER	152	67.514	16.173	−10.293	0.00	0.00
ATOM	1194	C	SER	152	66.999	16.703	−11.659	0.00	0.00
ATOM	1195	O	SER	152	65.934	16.247	−12.084	0.00	0.00
ATOM	1196	CB	SER	152	67.021	17.108	−9.211	0.00	0.00
ATOM	1197	OG	SER	152	67.112	18.506	−9.380	0.00	0.00
ATOM	1198	N	GLY	153	67.488	17.903	−12.070	0.00	0.00
ATOM	1199	CA	GLY	153	67.223	18.518	−13.331	0.00	0.00
ATOM	1200	C	GLY	153	67.565	17.555	−14.478	0.00	0.00
ATOM	1201	O	GLY	153	66.837	17.561	−15.460	0.00	0.00
ATOM	1202	N	LEU	154	68.752	16.944	−14.485	0.00	0.00
ATOM	1203	CA	LEU	154	69.164	15.935	−15.451	0.00	0.00
ATOM	1204	C	LEU	154	68.039	14.851	−15.634	0.00	0.00
ATOM	1205	O	LEU	154	67.363	14.957	−16.641	0.00	0.00
ATOM	1206	CB	LEU	154	70.432	15.388	−14.907	0.00	0.00
ATOM	1207	CG	LEU	154	71.298	14.293	−15.421	0.00	0.00
ATOM	1208	CD1	LEU	154	70.537	12.958	−15.552	0.00	0.00
ATOM	1209	CD2	LEU	154	71.873	14.658	−16.799	0.00	0.00
ATOM	1210	N	THR	155	67.541	14.182	−14.559	0.00	0.00
ATOM	1211	CA	THR	155	66.568	13.105	−14.633	0.00	0.00
ATOM	1212	C	THR	155	65.176	13.583	−15.212	0.00	0.00
ATOM	1213	O	THR	155	64.808	13.101	−16.278	0.00	0.00
ATOM	1214	CB	THR	155	66.472	12.515	−13.196	0.00	0.00
ATOM	1215	OG1	THR	155	67.702	11.884	−12.752	0.00	0.00
ATOM	1216	CG2	THR	155	65.282	11.510	−13.166	0.00	0.00
ATOM	1217	N	SER	156	64.526	14.641	−14.694	0.00	0.00
ATOM	1218	CA	SER	156	63.173	15.097	−15.101	0.00	0.00
ATOM	1219	C	SER	156	63.145	16.097	−16.300	0.00	0.00
ATOM	1220	O	SER	156	62.032	16.247	−16.850	0.00	0.00
ATOM	1221	CB	SER	156	62.543	15.725	−13.848	0.00	0.00
ATOM	1222	OG	SER	156	63.112	16.913	−13.318	0.00	0.00
ATOM	1223	N	PHE	157	64.010	17.121	−16.337	0.00	0.00
ATOM	1224	CA	PHE	157	64.070	18.017	−17.525	0.00	0.00
ATOM	1225	C	PHE	157	63.996	17.212	−18.847	0.00	0.00
ATOM	1226	O	PHE	157	63.479	17.799	−19.820	0.00	0.00
ATOM	1227	CB	PHE	157	65.284	18.948	−17.417	0.00	0.00
ATOM	1228	CG	PHE	157	65.486	19.799	−18.667	0.00	0.00
ATOM	1229	CD1	PHE	157	64.673	20.896	−18.875	0.00	0.00
ATOM	1230	CD2	PHE	157	66.464	19.489	−19.591	0.00	0.00
ATOM	1231	CE1	PHE	157	64.842	21.664	−20.000	0.00	0.00
ATOM	1232	CE2	PHE	157	66.625	20.269	−20.720	0.00	0.00
ATOM	1233	CZ	PHE	157	65.810	21.357	−20.926	0.00	0.00
ATOM	1234	N	LEU	158	64.568	16.006	−18.947	0.00	0.00
ATOM	1235	CA	LEU	158	64.627	15.178	−20.116	0.00	0.00
ATOM	1236	C	LEU	158	63.267	14.919	−20.769	0.00	0.00
ATOM	1237	O	LEU	158	63.162	15.293	−21.931	0.00	0.00
ATOM	1238	CB	LEU	158	65.386	13.916	−19.870	0.00	0.00
ATOM	1239	CG	LEU	158	66.636	13.880	−19.076	0.00	0.00
ATOM	1240	CD1	LEU	158	66.946	12.438	−18.637	0.00	0.00
ATOM	1241	CD2	LEU	158	67.724	14.481	−19.912	0.00	0.00
ATOM	1242	N	PRO	159	62.236	14.264	−20.152	0.00	0.00
ATOM	1243	CA	PRO	159	61.055	14.057	−20.917	0.00	0.00
ATOM	1244	C	PRO	159	60.487	15.351	−21.586	0.00	0.00
ATOM	1245	O	PRO	159	59.764	15.170	−22.537	0.00	0.00
ATOM	1246	CB	PRO	159	60.030	13.299	−20.015	0.00	0.00
ATOM	1247	CG	PRO	159	60.466	13.762	−18.573	0.00	0.00
ATOM	1248	CD	PRO	159	61.922	14.162	−18.675	0.00	0.00
ATOM	1249	N	ILE	160	60.340	16.503	−20.887	0.00	0.00
ATOM	1250	CA	ILE	160	59.812	17.704	−21.609	0.00	0.00
ATOM	1251	C	ILE	160	60.605	17.968	−22.926	0.00	0.00
ATOM	1252	O	ILE	160	59.955	17.977	−23.969	0.00	0.00
ATOM	1253	CB	ILE	160	59.797	19.021	−20.762	0.00	0.00
ATOM	1254	CG1	ILE	160	58.789	18.889	−19.608	0.00	0.00
ATOM	1255	CG2	ILE	160	59.482	20.267	−21.672	0.00	0.00
ATOM	1256	CD1	ILE	160	58.618	20.116	−18.691	0.00	0.00
ATOM	1257	N	GLN	161	61.950	18.049	−22.922	0.00	0.00
ATOM	1258	CA	GLN	161	62.810	18.298	−24.090	0.00	0.00
ATOM	1259	C	GLN	161	63.031	17.005	−24.918	0.00	0.00
ATOM	1260	O	GLN	161	63.983	16.256	−24.683	0.00	0.00
ATOM	1261	CB	GLN	161	64.119	18.937	−23.632	0.00	0.00
ATOM	1262	CG	GLN	161	64.938	19.448	−24.835	0.00	0.00
ATOM	1263	CD	GLN	161	66.422	19.469	−24.639	0.00	0.00
ATOM	1264	OE1	GLN	161	66.997	19.469	−23.554	0.00	0.00
ATOM	1265	NE2	GLN	161	67.121	19.459	−25.807	0.00	0.00
ATOM	1266	N	MET	162	62.348	17.028	−26.053	0.00	0.00
ATOM	1267	CA	MET	162	62.245	15.948	−27.040	0.00	0.00
ATOM	1268	C	MET	162	61.839	14.598	−26.367	0.00	0.00
ATOM	1269	O	MET	162	61.861	13.576	−27.070	0.00	0.00
ATOM	1270	CB	MET	162	63.552	15.847	−27.838	0.00	0.00
ATOM	1271	CG	MET	162	63.986	17.239	−28.345	0.00	0.00
ATOM	1272	SD	MET	162	63.029	17.571	−29.840	0.00	0.00
ATOM	1273	CE	MET	162	63.690	19.114	−30.489	0.00	0.00
ATOM	1274	N	HIS	163	61.170	14.678	−25.195	0.00	0.00
ATOM	1275	CA	HIS	163	60.629	13.543	−24.484	0.00	0.00
ATOM	1276	C	HIS	163	61.816	12.526	−24.347	0.00	0.00
ATOM	1277	O	HIS	163	61.816	11.656	−25.276	0.00	0.00
ATOM	1278	CB	HIS	163	59.452	13.084	−25.324	0.00	0.00
ATOM	1279	CG	HIS	163	58.194	13.821	−24.989	0.00	0.00
ATOM	1280	ND1	HIS	163	57.029	13.256	−24.501	0.00	0.00
ATOM	1281	CD2	HIS	163	57.950	15.161	−25.091	0.00	0.00
ATOM	1282	CE1	HIS	163	56.120	14.244	−24.400	0.00	0.00
ATOM	1283	NE2	HIS	163	56.639	15.400	−24.679	0.00	0.00
ATOM	1284	N	TRP	164	63.022	12.908	−23.827	0.00	0.00
ATOM	1285	CA	TRP	164	63.883	11.795	−23.609	0.00	0.00
ATOM	1286	C	TRP	164	62.859	10.988	−22.729	0.00	0.00
ATOM	1287	O	TRP	164	62.382	11.526	−21.720	0.00	0.00
ATOM	1288	CB	TRP	164	65.221	12.146	−22.981	0.00	0.00
ATOM	1289	CG	TRP	164	66.215	11.049	−23.091	0.00	0.00
ATOM	1290	CD1	TRP	164	66.175	9.966	−23.933	0.00	0.00
ATOM	1291	CD2	TRP	164	67.394	10.895	−22.291	0.00	0.00
ATOM	1292	NE1	TRP	164	67.249	9.139	−23.689	0.00	0.00
ATOM	1293	CE2	TRP	164	68.013	9.684	−22.688	0.00	0.00
ATOM	1294	CE3	TRP	164	67.982	11.653	−21.269	0.00	0.00
ATOM	1295	CZ2	TRP	164	69.189	9.216	−22.094	0.00	0.00
ATOM	1296	CZ3	TRP	164	69.142	11.188	−20.681	0.00	0.00
ATOM	1297	CH2	TRP	164	69.737	9.978	−21.094	0.00	0.00
ATOM	1298	N	TYR	165	62.251	9.990	−23.297	0.00	0.00
ATOM	1299	CA	TYR	165	61.150	9.255	−22.749	0.00	0.00
ATOM	1300	C	TYR	165	59.969	10.319	−22.761	0.00	0.00
ATOM	1301	O	TYR	165	59.694	10.799	−23.849	0.00	0.00
ATOM	1302	CB	TYR	165	61.378	8.508	−21.415	0.00	0.00
ATOM	1303	CG	TYR	165	61.070	9.315	−20.200	0.00	0.00
ATOM	1304	CD1	TYR	165	59.816	9.147	−19.601	0.00	0.00
ATOM	1305	CD2	TYR	165	62.084	10.139	−19.637	0.00	0.00
ATOM	1306	CE1	TYR	165	59.522	9.856	−18.427	0.00	0.00
ATOM	1307	CE2	TYR	165	61.758	10.818	−18.415	0.00	0.00
ATOM	1308	CZ	TYR	165	60.502	10.672	−17.872	0.00	0.00
ATOM	1309	OH	TYR	165	60.189	11.329	−16.710	0.00	0.00
ATOM	1310	N	ARG	166	59.031	10.400	−21.769	0.00	0.00
ATOM	1311	CA	ARG	166	57.887	11.357	−21.841	0.00	0.00
ATOM	1312	C	ARG	166	57.049	11.484	−20.508	0.00	0.00
ATOM	1313	O	ARG	166	56.975	10.518	−19.742	0.00	0.00
ATOM	1314	CB	ARG	166	56.910	10.805	−22.914	0.00	0.00
ATOM	1315	CG	ARG	166	56.518	9.394	−22.681	0.00	0.00
ATOM	1316	CD	ARG	166	55.152	8.979	−23.067	0.00	0.00
ATOM	1317	NE	ARG	166	55.003	8.503	−24.402	0.00	0.00
ATOM	1318	CZ	ARG	166	54.167	7.507	−24.678	0.00	0.00
ATOM	1319	NH1	ARG	166	53.443	6.865	−23.764	0.00	0.00
ATOM	1320	NH2	ARG	166	53.933	7.240	−25.955	0.00	0.00
ATOM	1321	N	ALA	167	56.192	12.498	−20.476	0.00	0.00
ATOM	1322	CA	ALA	167	55.243	12.749	−19.394	0.00	0.00
ATOM	1323	C	ALA	167	53.833	12.230	−19.848	0.00	0.00
ATOM	1324	O	ALA	167	53.296	12.701	−20.854	0.00	0.00
ATOM	1325	CB	ALA	167	55.233	14.257	−19.132	0.00	0.00
ATOM	1326	N	THR	168	53.444	11.045	−19.340	0.00	0.00
ATOM	1327	CA	THR	168	52.130	10.421	−19.544	0.00	0.00
ATOM	1328	C	THR	168	51.461	10.222	−18.126	0.00	0.00
ATOM	1329	O	THR	168	52.117	9.675	−17.232	0.00	0.00
ATOM	1330	CB	THR	168	52.268	9.125	−20.420	0.00	0.00
ATOM	1331	OG1	THR	168	51.005	8.631	−20.938	0.00	0.00
ATOM	1332	CG2	THR	168	53.002	7.973	−19.687	0.00	0.00
ATOM	1333	N	HIS	169	50.156	10.039	−18.162	0.00	0.00
ATOM	1334	CA	HIS	169	49.234	9.927	−16.992	0.00	0.00
ATOM	1335	C	HIS	169	49.137	8.493	−16.322	0.00	0.00
ATOM	1336	O	HIS	169	49.429	7.520	−17.025	0.00	0.00
ATOM	1337	CB	HIS	169	47.835	10.257	−17.561	0.00	0.00
ATOM	1338	CG	HIS	169	47.359	9.347	−18.666	0.00	0.00
ATOM	1339	ND1	HIS	169	47.572	9.655	−20.008	0.00	0.00
ATOM	1340	CD2	HIS	169	46.724	8.148	−18.647	0.00	0.00
ATOM	1341	CE1	HIS	169	47.077	8.671	−20.738	0.00	0.00
ATOM	1342	NE2	HIS	169	46.569	7.764	−19.940	0.00	0.00
ATOM	1343	N	GLN	170	48.562	8.340	−15.097	0.00	0.00
ATOM	1344	CA	GLN	170	48.363	6.995	−14.497	0.00	0.00
ATOM	1345	C	GLN	170	46.822	6.648	−14.459	0.00	0.00
ATOM	1346	O	GLN	170	46.415	5.923	−15.362	0.00	0.00
ATOM	1347	CB	GLN	170	49.011	6.969	−13.160	0.00	0.00
ATOM	1348	CG	GLN	170	48.706	8.057	−12.229	0.00	0.00
ATOM	1349	CD	GLN	170	49.500	7.898	−10.966	0.00	0.00
ATOM	1350	OE1	GLN	170	50.636	8.378	−10.871	0.00	0.00
ATOM	1351	NE2	GLN	170	48.938	7.170	−9.997	0.00	0.00
ATOM	1352	N	GLU	171	45.994	6.953	−13.416	0.00	0.00
ATOM	1353	CA	GLU	171	44.504	6.819	−13.444	0.00	0.00
ATOM	1354	C	GLU	171	43.985	8.168	−14.008	0.00	0.00
ATOM	1355	O	GLU	171	42.909	8.639	−13.617	0.00	0.00
ATOM	1356	CB	GLU	171	43.995	6.773	−12.015	0.00	0.00
ATOM	1357	CG	GLU	171	44.527	7.725	−10.986	0.00	0.00
ATOM	1358	CD	GLU	171	43.952	7.627	−9.671	0.00	0.00
ATOM	1359	OE1	GLU	171	44.714	8.195	−8.888	0.00	0.00
ATOM	1360	OE2	GLU	171	42.809	7.181	−9.196	0.00	0.00
ATOM	1361	N	ALA	172	44.476	8.513	−15.167	0.00	0.00
ATOM	1362	CA	ALA	172	44.180	9.811	−15.750	0.00	0.00
ATOM	1363	C	ALA	172	44.234	10.923	−14.615	0.00	0.00
ATOM	1364	O	ALA	172	43.353	11.810	−14.677	0.00	0.00
ATOM	1365	CB	ALA	172	42.820	9.727	−16.461	0.00	0.00
ATOM	1366	N	ILE	173	45.089	10.783	−13.624	0.00	0.00
ATOM	1367	CA	ILE	173	45.277	11.664	−12.455	0.00	0.00
ATOM	1368	C	ILE	173	46.743	12.104	−12.232	0.00	0.00
ATOM	1369	O	ILE	173	46.971	13.200	−11.640	0.00	0.00
ATOM	1370	CB	ILE	173	44.658	11.116	−11.140	0.00	0.00
ATOM	1371	CG1	ILE	173	43.103	11.105	−11.296	0.00	0.00
ATOM	1372	CG2	ILE	173	45.045	11.857	−9.849	0.00	0.00
ATOM	1373	CD1	ILE	173	42.433	10.015	−10.434	0.00	0.00
ATOM	1374	N	ASN	174	47.753	11.415	−12.843	0.00	0.00
ATOM	1375	CA	ASN	174	49.105	11.798	−12.562	0.00	0.00
ATOM	1376	C	ASN	174	50.016	11.334	−13.707	0.00	0.00
ATOM	1377	O	ASN	174	50.269	10.139	−13.819	0.00	0.00
ATOM	1378	CB	ASN	174	49.544	11.002	−11.302	0.00	0.00
ATOM	1379	CG	ASN	174	50.988	10.972	−10.923	0.00	0.00
ATOM	1380	OD1	ASN	174	51.828	10.527	−11.731	0.00	0.00
ATOM	1381	ND2	ASN	174	51.368	11.437	−9.752	0.00	0.00
ATOM	1382	N	CYS	175	50.950	12.176	−13.938	0.00	0.00
ATOM	1383	CA	CYS	175	52.003	11.899	−14.937	0.00	0.00
ATOM	1384	C	CYS	175	53.397	11.625	−14.346	0.00	0.00
ATOM	1385	O	CYS	175	53.787	12.104	−13.275	0.00	0.00
ATOM	1386	CB	CYS	175	52.018	12.948	−16.035	0.00	0.00
ATOM	1387	SG	CYS	175	50.563	13.014	−17.024	0.00	0.00
ATOM	1388	N	TYR	176	54.137	10.840	−15.158	0.00	0.00
ATOM	1389	CA	TYR	176	55.496	10.410	−14.930	0.00	0.00
ATOM	1390	C	TYR	176	55.920	9.579	−16.213	0.00	0.00
ATOM	1391	O	TYR	176	55.703	10.032	−17.355	0.00	0.00
ATOM	1392	CB	TYR	176	55.67	19.762	−13.508	0.00	0.00
ATOM	1393	CG	TYR	176	57.129	9.219	−13.443	0.00	0.00
ATOM	1394	CD1	TYR	176	58.136	10.146	−13.197	0.00	0.00
ATOM	1395	CD2	TYR	176	57.445	7.863	−13.509	0.00	0.00
ATOM	1396	CE1	TYR	176	59.455	9.730	−13.015	0.00	0.00
ATOM	1397	CE2	TYR	176	58.766	7.439	−13.331	0.00	0.00
ATOM	1398	CZ	TYR	176	59.774	8.373	−13.078	0.00	0.00
ATOM	1399	OH	TYR	176	61.088	7.975	−12.850	0.00	0.00
ATOM	1400	N	ALA	177	56.821	8.590	−16.032	0.00	0.00
ATOM	1401	CA	ALA	177	57.395	7.772	−17.032	0.00	0.00
ATOM	1402	C	ALA	177	56.322	7.156	−18.000	0.00	0.00
ATOM	1403	O	ALA	177	55.290	6.672	−17.536	0.00	0.00
ATOM	1404	CB	ALA	177	58.252	6.729	−16.295	0.00	0.00
ATOM	1405	N	ASN	178	56.870	6.642	−19.090	0.00	0.00
ATOM	1406	CA	ASN	178	56.211	6.151	−20.336	0.00	0.00
ATOM	1407	C	ASN	178	55.139	4.979	−20.379	0.00	0.00
ATOM	1408	O	ASN	178	53.979	5.333	−20.553	0.00	0.00
ATOM	1409	CB	ASN	178	57.336	5.907	−21.279	0.00	0.00
ATOM	1410	CG	ASN	178	57.867	4.418	−21.201	0.00	0.00
ATOM	1411	OD1	ASN	178	57.617	3.541	−22.027	0.00	0.00
ATOM	1412	ND2	ASN	178	58.600	4.106	−20.140	0.00	0.00
ATOM	1413	N	GLU	179	55.461	3.669	−20.530	0.00	0.00
ATOM	1414	CA	GLU	179	54.462	2.575	−20.747	0.00	0.00
ATOM	1415	C	GLU	179	54.183	2.215	−22.255	0.00	0.00
ATOM	1416	O	GLU	179	53.412	1.262	−22.476	0.00	0.00
ATOM	1417	CB	GLU	179	53.138	2.788	−19.965	0.00	0.00
ATOM	1418	CG	GLU	179	53.288	2.758	−18.428	0.00	0.00
ATOM	1419	CD	GLU	179	51.951	2.966	−17.833	0.00	0.00
ATOM	1420	OE1	GLU	179	50.905	3.254	−18.403	0.00	0.00
ATOM	1421	OE2	GLU	179	51.914	2.573	−16.610	0.00	0.00
ATOM	1422	N	THR	180	54.961	2.704	−23.239	0.00	0.00
ATOM	1423	CA	THR	180	54.877	2.372	−24.659	0.00	0.00
ATOM	1424	C	THR	180	56.327	2.461	−25.191	0.00	0.00
ATOM	1425	O	THR	180	57.014	3.468	−24.913	0.00	0.00
ATOM	1426	CB	THR	180	53.925	3.295	−25.476	0.00	0.00
ATOM	1427	OG1	THR	180	54.490	4.644	−25.636	0.00	0.00
ATOM	1428	CG2	THR	180	52.513	3.389	−24.894	0.00	0.00
ATOM	1429	N	CYS	181	56.792	1.423	−25.905	0.00	0.00
ATOM	1430	CA	CYS	181	58.126	1.502	−26.519	0.00	0.00
ATOM	1431	C	CYS	181	58.362	2.935	−27.116	0.00	0.00
ATOM	1432	O	CYS	181	59.325	3.554	−26.652	0.00	0.00
ATOM	1433	CB	CYS	181	58.313	0.370	−27.547	0.00	0.00
ATOM	1434	SG	CYS	181	59.819	0.712	−28.515	0.00	0.00
ATOM	1435	N	CYS	182	57.463	3.513	−27.919	0.00	0.00
ATOM	1436	CA	CYS	182	57.591	4.869	−28.411	0.00	0.00
ATOM	1437	C	CYS	182	58.968	5.101	−29.103	0.00	0.00
ATOM	1438	O	CYS	182	59.784	5.844	−28.541	0.00	0.00
ATOM	1439	CB	CYS	182	57.261	5.896	−27.337	0.00	0.00
ATOM	1440	SG	CYS	182	56.750	7.500	−28.058	0.00	0.00
ATOM	1441	N	ASP	183	59.361	4.224	−30.073	0.00	0.00
ATOM	1442	CA	ASP	183	60.652	4.296	−30.767	0.00	0.00
ATOM	1443	C	ASP	183	61.065	5.756	−31.153	0.00	0.00
ATOM	1444	O	ASP	183	62.276	5.992	−31.116	0.00	0.00
ATOM	1445	CB	ASP	183	60.520	3.343	−31.918	0.00	0.00
ATOM	1446	CG	ASP	183	60.336	3.577	−33.367	0.00	0.00
ATOM	1447	OD1	ASP	183	60.764	2.631	−34.200	0.00	0.00
ATOM	1448	OD2	ASP	183	59.795	4.594	−33.942	0.00	0.00
ATOM	1449	N	PHE	184	60.180	6.619	−31.722	0.00	0.00
ATOM	1450	CA	PHE	184	60.452	8.026	−32.021	0.00	0.00
ATOM	1451	C	PHE	184	61.160	8.739	−30.823	0.00	0.00
ATOM	1452	O	PHE	184	62.276	9.227	−31.038	0.00	0.00
ATOM	1453	CB	PHE	184	59.147	8.722	−32.442	0.00	0.00
ATOM	1454	CG	PHE	184	59.347	10.072	−33.102	0.00	0.00
ATOM	1455	CD1	PHE	184	60.114	10.115	−34.265	0.00	0.00
ATOM	1456	CD2	PHE	184	58.773	11.234	−32.488	0.00	0.00
ATOM	1457	CE1	PHE	184	60.293	11.374	−34.869	0.00	0.00
ATOM	1458	CE2	PHE	184	59.053	12.437	−33.105	0.00	0.00
ATOM	1459	CZ	PHE	184	59.741	12.580	−34.265	0.00	0.00
ATOM	1460	N	PHE	185	60.626	8.715	−29.587	0.00	0.00
ATOM	1461	CA	PHE	185	61.187	9.437	−28.413	0.00	0.00
ATOM	1462	C	PHE	185	62.133	8.581	−27.498	0.00	0.00
ATOM	1463	O	PHE	185	62.673	9.155	−26.543	0.00	0.00
ATOM	1464	CB	PHE	185	60.015	9.997	−27.612	0.00	0.00
ATOM	1465	CG	PHE	185	59.121	10.914	−28.391	0.00	0.00
ATOM	1466	CD1	PHE	185	59.597	12.241	−28.559	0.00	0.00
ATOM	1467	CD2	PHE	185	57.928	10.510	−28.993	0.00	0.00
ATOM	1468	CE1	PHE	185	58.793	13.119	−29.350	0.00	0.00
ATOM	1469	CE2	PHE	185	57.167	11.396	−29.763	0.00	0.00
ATOM	1470	CZ	PHE	185	57.603	12.719	−29.943	0.00	0.00
ATOM	1471	N	THR	186	62.465	7.332	−27.833	0.00	0.00
ATOM	1472	CA	THR	186	63.421	6.452	−27.121	0.00	0.00
ATOM	1473	C	THR	186	63.129	6.250	−25.598	0.00	0.00
ATOM	1474	O	THR	186	63.852	6.830	−24.779	0.00	0.00
ATOM	1475	CB	THR	186	64.930	6.695	−27.510	0.00	0.00
ATOM	1476	OG1	THR	186	65.970	6.484	−26.535	0.00	0.00
ATOM	1477	CG2	THR	186	65.151	7.860	−28.424	0.00	0.00
ATOM	1478	N	ASN	187	61.915	5.863	−25.257	0.00	0.00
ATOM	1479	CA	ASN	187	61.395	5.692	−23.887	0.00	0.00
ATOM	1480	C	ASN	187	62.252	4.623	−23.104	0.00	0.00
ATOM	1481	O	ASN	187	62.358	4.788	−21.892	0.00	0.00
ATOM	1482	CB	ASN	187	59.949	5.375	−24.110	0.00	0.00
ATOM	1483	CG	ASN	187	59.050	6.548	−24.023	0.00	0.00
ATOM	1484	OD1	ASN	187	58.435	6.871	−25.018	0.00	0.00
ATOM	1485	ND2	ASN	187	59.027	7.259	−22.908	0.00	0.00
ATOM	1486	N	GLN	188	62.464	3.380	−23.641	0.00	0.00
ATOM	1487	CA	GLN	188	63.324	2.342	−23.058	0.00	0.00
ATOM	1488	C	GLN	188	64.761	2.883	−22.757	0.00	0.00
ATOM	1489	O	GLN	188	65.273	2.536	−21.698	0.00	0.00
ATOM	1490	CB	GLN	188	63.319	1.130	−24.006	0.00	0.00
ATOM	1491	CG	GLN	188	64.136	−0.035	−23.399	0.00	0.00
ATOM	1492	CD	GLN	188	64.113	−1.202	−24.371	0.00	0.00
ATOM	1493	OE1	GLN	188	64.145	−0.998	−25.583	0.00	0.00
ATOM	1494	NE2	GLN	188	64.034	−2.400	−23.811	0.00	0.00
ATOM	1495	N	ALA	189	65.487	3.471	−23.744	0.00	0.00
ATOM	1496	CA	ALA	189	66.797	4.079	−23.483	0.00	0.00
ATOM	1497	C	ALA	189	66.644	5.078	−22.301	0.00	0.00
ATOM	1498	O	ALA	189	67.593	5.130	−21.527	0.00	0.00
ATOM	1499	CB	ALA	189	67.475	4.650	−24.719	0.00	0.00
ATOM	1500	N	TYR	190	65.634	5.986	−22.264	0.00	0.00
ATOM	1501	CA	TYR	190	65.543	6.800	−21.038	0.00	0.00
ATOM	1502	C	TYR	190	65.364	5.930	−19.762	0.00	0.00
ATOM	1503	O	TYR	190	65.923	6.341	−18.766	0.00	0.00
ATOM	1504	CB	TYR	190	64.426	7.798	−21.030	0.00	0.00
ATOM	1505	CG	TYR	190	64.314	8.646	−19.817	0.00	0.00
ATOM	1506	CD1	TYR	190	63.557	8.064	−18.795	0.00	0.00
ATOM	1507	CD2	TYR	190	64.992	9.866	−19.627	0.00	0.00
ATOM	1508	CE1	TYR	190	63.418	8.717	−17.572	0.00	0.00
ATOM	1509	CE2	TYR	190	64.872	10.496	−18.397	0.00	0.00
ATOM	1510	CZ	TYR	190	64.073	9.938	−17.403	0.00	0.00
ATOM	1511	OH	TYR	190	63.892	10.585	−16.167	0.00	0.00
ATOM	1512	N	ALA	191	64.291	5.111	−19.669	0.00	0.00
ATOM	1513	CA	ALA	191	63.971	4.236	−18.553	0.00	0.00
ATOM	1514	C	ALA	191	65.233	3.535	−17.982	0.00	0.00
ATOM	1515	O	ALA	191	65.266	3.395	−16.761	0.00	0.00
ATOM	1516	CB	ALA	191	62.889	3.247	−19.015	0.00	0.00
ATOM	1517	N	ILE	192	66.094	2.889	−18.783	0.00	0.00
ATOM	1518	CA	ILE	192	67.349	2.290	−18.353	0.00	0.00
ATOM	1519	C	ILE	192	68.275	3.404	−17.802	0.00	0.00
ATOM	1520	O	ILE	192	68.830	3.175	−16.713	0.00	0.00
ATOM	1521	CB	ILE	192	67.941	1.506	−19.537	0.00	0.00
ATOM	1522	CG1	ILE	192	67.026	0.387	−20.006	0.00	0.00
ATOM	1523	CG2	ILE	192	69.320	0.927	−19.109	0.00	0.00
ATOM	1524	CD1	ILE	192	66.973	−0.924	−19.203	0.00	0.00
ATOM	1525	N	ALA	193	68.621	4.442	−18.589	0.00	0.00
ATOM	1526	CA	ALA	193	69.397	5.573	−18.105	0.00	0.00
ATOM	1527	C	ALA	193	68.837	6.064	−16.710	0.00	0.00
ATOM	1528	O	ALA	193	69.674	6.273	−15.827	0.00	0.00
ATOM	1529	CB	ALA	193	69.401	6.670	−19.178	0.00	0.00
ATOM	1530	N	SER	194	67.523	6.339	−16.532	0.00	0.00
ATOM	1531	CA	SER	194	66.933	6.820	−15.270	0.00	0.00
ATOM	1532	C	SER	194	67.095	5.801	−14.097	0.00	0.00
ATOM	1533	O	SER	194	67.325	6.287	−12.982	0.00	0.00
ATOM	1534	CB	SER	194	65.437	7.169	−15.518	0.00	0.00
ATOM	1535	OG	SER	194	64.562	6.019	−15.438	0.00	0.00
ATOM	1536	N	SER	195	66.618	4.542	−14.211	0.00	0.00
ATOM	1537	CA	SER	195	66.850	3.552	−13.175	0.00	0.00
ATOM	1538	C	SER	195	68.365	3.454	−12.836	0.00	0.00
ATOM	1539	O	SER	195	68.726	4.016	−11.820	0.00	0.00
ATOM	1540	CB	SER	195	66.251	2.189	−13.572	0.00	0.00
ATOM	1541	OG	SER	195	64.837	2.058	−13.615	0.00	0.00
ATOM	1542	N	ILE	196	69.251	3.077	−13.806	0.00	0.00
ATOM	1543	CA	ILE	196	70.663	2.938	−13.423	0.00	0.00
ATOM	1544	C	ILE	196	71.288	4.228	−12.826	0.00	0.00
ATOM	1545	O	ILE	196	71.397	4.245	−11.627	0.00	0.00
ATOM	1546	CB	ILE	196	71.490	2.383	−14.598	0.00	0.00
ATOM	1547	CG1	ILE	196	71.042	1.022	−15.008	0.00	0.00
ATOM	1548	CG2	ILE	196	72.966	2.291	−14.248	0.00	0.00
ATOM	1549	CD1	ILE	196	71.199	0.687	−16.493	0.00	0.00
ATOM	1550	N	VAL	197	71.349	5.358	−13.574	0.00	0.00
ATOM	1551	CA	VAL	197	71.986	6.535	−12.982	0.00	0.00
ATOM	1552	C	VAL	197	71.254	7.108	−11.698	0.00	0.00
ATOM	1553	O	VAL	197	71.990	7.589	−10.831	0.00	0.00
ATOM	1554	CB	VAL	197	72.100	7.610	−14.077	0.00	0.00
ATOM	1555	CG1	VAL	197	72.870	8.834	−13.555	0.00	0.00
ATOM	1556	CG2	VAL	197	72.739	7.091	−15.352	0.00	0.00
ATOM	1557	N	SER	198	69.952	7.510	−11.746	0.00	0.00
ATOM	1558	CA	SER	198	69.241	8.064	−10.608	0.00	0.00
ATOM	1559	C	SER	198	68.981	7.012	−9.470	0.00	0.00
ATOM	1560	O	SER	198	69.046	7.442	−8.321	0.00	0.00
ATOM	1561	CB	SER	198	67.951	8.737	−11.117	0.00	0.00
ATOM	1562	OG	SER	198	67.105	9.256	−10.086	0.00	0.00
ATOM	1563	N	PHE	199	68.175	5.976	−9.759	0.00	0.00
ATOM	1564	CA	PHE	199	67.726	4.953	−8.827	0.00	0.00
ATOM	1565	C	PHE	199	68.837	4.031	−8.287	0.00	0.00
ATOM	1566	O	PHE	199	69.305	4.341	−7.198	0.00	0.00
ATOM	1567	CB	PHE	199	66.576	4.224	−9.526	0.00	0.00
ATOM	1568	CG	PHE	199	65.813	3.155	−8.857	0.00	0.00
ATOM	1569	CD1	PHE	199	65.366	3.283	−7.537	0.00	0.00
ATOM	1570	CD2	PHE	199	65.478	1.977	−9.545	0.00	0.00
ATOM	1571	CE1	PHE	199	64.590	2.292	−6.929	0.00	0.00
ATOM	1572	CE2	PHE	199	64.734	0.993	−8.956	0.00	0.00
ATOM	1573	CZ	PHE	199	64.291	1.129	−7.635	0.00	0.00
ATOM	1574	N	TYR	200	69.474	3.203	−9.142	0.00	0.00
ATOM	1575	CA	TYR	200	70.564	2.308	−8.735	0.00	0.00
ATOM	1576	C	TYR	200	71.787	3.103	−8.234	0.00	0.00
ATOM	1577	O	TYR	200	72.272	2.749	−7.158	0.00	0.00
ATOM	1578	CB	TYR	200	70.997	1.337	−9.842	0.00	0.00
ATOM	1579	CG	TYR	200	69.870	0.408	−10.215	0.00	0.00
ATOM	1580	CD1	TYR	200	68.774	0.835	−10.976	0.00	0.00
ATOM	1581	CD2	TYR	200	69.886	−0.909	−9.751	0.00	0.00
ATOM	1582	CE1	TYR	200	67.733	−0.060	−11.296	0.00	0.00
ATOM	1583	CE2	TYR	200	68.876	−1.792	−10.081	0.00	0.00
ATOM	1584	CZ	TYR	200	67.788	−1.361	−10.822	0.00	0.00
ATOM	1585	OH	TYR	200	66.837	−2.309	−11.092	0.00	0.00
ATOM	1586	N	VAL	201	72.168	4.255	−8.837	0.00	0.00
ATOM	1587	CA	VAL	201	73.396	4.995	−8.449	0.00	0.00
ATOM	1588	C	VAL	201	73.404	5.665	−7.086	0.00	0.00
ATOM	1589	O	VAL	201	74.041	5.039	−6.227	0.00	0.00
ATOM	1590	CB	VAL	201	73.935	5.897	−9.518	0.00	0.00
ATOM	1591	CG1	VAL	201	75.323	6.414	−9.212	0.00	0.00
ATOM	1592	CG2	VAL	201	73.890	5.318	−10.913	0.00	0.00
ATOM	1593	N	PRO	202	72.822	6.862	−6.773	0.00	0.00
ATOM	1594	CA	PRO	202	72.894	7.226	−5.411	0.00	0.00
ATOM	1595	C	PRO	202	72.394	6.118	−4.403	0.00	0.00
ATOM	1596	O	PRO	202	72.895	6.154	−3.286	0.00	0.00
ATOM	1597	CB	PRO	202	72.194	8.565	−5.125	0.00	0.00
ATOM	1598	CG	PRO	202	71.388	8.800	−6.412	0.00	0.00
ATOM	1599	CD	PRO	202	71.990	7.913	−7.499	0.00	0.00
ATOM	1600	N	LEU	203	71.350	5.315	−4.702	0.00	0.00
ATOM	1601	CA	LEU	203	70.983	4.268	−3.724	0.00	0.00
ATOM	1602	C	LEU	203	72.237	3.507	−3.178	0.00	0.00
ATOM	1603	O	LEU	203	72.267	3.308	−1.979	0.00	0.00
ATOM	1604	CB	LEU	203	69.921	3.300	−4.251	0.00	0.00
ATOM	1605	CG	LEU	203	68.509	3.843	−4.341	0.00	0.00
ATOM	1606	CD1	LEU	203	67.589	2.759	−4.922	0.00	0.00
ATOM	1607	CD2	LEU	203	68.012	4.320	−2.977	0.00	0.00
ATOM	1608	N	VAL	204	73.033	2.873	−4.038	0.00	0.00
ATOM	1609	CA	VAL	204	74.277	2.167	−3.716	0.00	0.00
ATOM	1610	C	VAL	204	75.342	3.152	−3.125	0.00	0.00
ATOM	1611	O	VAL	204	76.155	2.654	−2.355	0.00	0.00
ATOM	1612	CB	VAL	204	74.623	1.416	−4.946	0.00	0.00
ATOM	1613	CG1	VAL	204	75.915	1.545	−5.539	0.00	0.00
ATOM	1614	CG2	VAL	204	73.895	0.127	−5.163	0.00	0.00
ATOM	1615	N	ILE	205	75.546	4.379	−3.659	0.00	0.00
ATOM	1616	CA	ILE	205	76.480	5.352	−3.028	0.00	0.00
ATOM	1617	C	ILE	205	76.015	5.548	−1.535	0.00	0.00
ATOM	1618	O	ILE	205	76.881	5.466	−0.669	0.00	0.00
ATOM	1619	CB	ILE	205	76.524	6.686	−3.862	0.00	0.00
ATOM	1620	CG1	ILE	205	77.243	6.488	−5.232	0.00	0.00
ATOM	1621	CG2	ILE	205	77.120	7.895	−3.067	0.00	0.00
ATOM	1622	CD1	ILE	205	77.130	7.859	−6.035	0.00	0.00
ATOM	1623	N	MET	206	74.706	5.797	−1.220	0.00	0.00
ATOM	1624	CA	MET	206	74.139	5.898	0.118	0.00	0.00
ATOM	1625	C	MET	206	74.392	4.610	0.971	0.00	0.00
ATOM	1626	O	MET	206	74.759	4.786	2.142	0.00	0.00
ATOM	1627	CB	MET	206	72.626	6.115	−0.067	0.00	0.00
ATOM	1628	CG	MET	206	72.303	7.434	−0.695	0.00	0.00
ATOM	1629	SD	MET	206	70.583	7.581	−1.269	0.00	0.00
ATOM	1630	CE	MET	206	69.725	7.523	0.310	0.00	0.00
ATOM	1631	N	VAL	207	73.937	3.402	0.535	0.00	0.00
ATOM	1632	CA	VAL	207	74.154	2.102	1.196	0.00	0.00
ATOM	1633	C	VAL	207	75.676	1.848	1.486	0.00	0.00
ATOM	1634	O	VAL	207	75.919	1.207	2.504	0.00	0.00
ATOM	1635	CB	VAL	207	73.489	1.019	0.345	0.00	0.00
ATOM	1636	CG1	VAL	207	73.640	−0.377	0.865	0.00	0.00
ATOM	1637	CG2	VAL	207	72.003	1.234	0.262	0.00	0.00
ATOM	1638	N	PHE	208	76.617	2.067	0.547	0.00	0.00
ATOM	1639	CA	PHE	208	78.047	1.795	0.661	0.00	0.00
ATOM	1640	C	PHE	208	78.642	2.727	1.803	0.00	0.00
ATOM	1641	O	PHE	208	79.508	2.200	2.525	0.00	0.00
ATOM	1642	CB	PHE	208	78.644	1.998	−0.753	0.00	0.00
ATOM	1643	CG	PHE	208	80.103	1.526	−0.967	0.00	0.00
ATOM	1644	CD1	PHE	208	80.473	0.279	−0.430	0.00	0.00
ATOM	1645	CD2	PHE	208	80.968	2.246	−1.729	0.00	0.00
ATOM	1646	CE1	PHE	208	81.792	−0.169	−0.604	0.00	0.00
ATOM	1647	CE2	PHE	208	82.287	1.798	−1.904	0.00	0.00
ATOM	1648	CZ	PHE	208	82.740	0.631	−1.364	0.00	0.00
ATOM	1649	N	VAL	209	78.523	4.078	1.753	0.00	0.00
ATOM	1650	CA	VAL	209	78.948	4.989	2.806	0.00	0.00
ATOM	1651	C	VAL	209	78.434	4.450	4.186	0.00	0.00
ATOM	1652	O	VAL	209	79.261	4.410	5.095	0.00	0.00
ATOM	1653	CB	VAL	209	78.462	6.451	2.533	0.00	0.00
ATOM	1654	CG1	VAL	209	78.838	7.390	3.658	0.00	0.00
ATOM	1655	CG2	VAL	209	78.953	6.972	1.175	0.00	0.00
ATOM	1656	N	TYR	210	77.102	4.258	4.384	0.00	0.00
ATOM	1657	CA	TYR	210	76.500	3.667	5.588	0.00	0.00
ATOM	1658	C	TYR	210	77.178	2.303	5.953	0.00	0.00
ATOM	1659	O	TYR	210	77.310	2.083	7.156	0.00	0.00
ATOM	1660	CB	TYR	210	74.966	3.491	5.424	0.00	0.00
ATOM	1661	CG	TYR	210	74.411	2.584	6.544	0.00	0.00
ATOM	1662	CD1	TYR	210	74.170	3.127	7.813	0.00	0.00
ATOM	1663	CD2	TYR	210	74.161	1.227	6.301	0.00	0.00
ATOM	1664	CE1	TYR	210	73.651	2.333	8.842	0.00	0.00
ATOM	1665	CE2	TYR	210	73.683	0.414	7.332	0.00	0.00
ATOM	1666	CZ	TYR	210	73.432	0.971	8.591	0.00	0.00
ATOM	1667	OH	TYR	210	72.969	0.164	9.591	0.00	0.00
ATOM	1668	N	SER	211	77.429	1.363	5.013	0.00	0.00
ATOM	1669	CA	SER	211	78.160	0.127	5.335	0.00	0.00
ATOM	1670	C	SER	211	79.514	0.467	6.068	0.00	0.00
ATOM	1671	O	SER	211	79.869	−0.299	6.964	0.00	0.00
ATOM	1672	CB	SER	211	78.381	−0.661	4.034	0.00	0.00
ATOM	1673	OG	SER	211	77.277	−1.409	3.530	0.00	0.00
ATOM	1674	N	ARG	212	80.358	1.425	5.572	0.00	0.00
ATOM	1675	CA	ARG	212	81.583	1.873	6.236	0.00	0.00
ATOM	1676	C	ARG	212	81.300	2.628	7.582	0.00	0.00
ATOM	1677	O	ARG	212	82.124	2.472	8.489	0.00	0.00
ATOM	1678	CB	ARG	212	82.602	2.513	5.317	0.00	0.00
ATOM	1679	CG	ARG	212	83.051	1.759	4.118	0.00	0.00
ATOM	1680	CD	ARG	212	84.006	2.667	3.259	0.00	0.00
ATOM	1681	NE	ARG	212	83.337	3.826	2.683	0.00	0.00
ATOM	1682	CZ	ARG	212	82.532	3.749	1.619	0.00	0.00
ATOM	1683	NH1	ARG	212	82.313	2.600	0.972	0.00	0.00
ATOM	1684	NH2	ARG	212	81.786	4.813	1.299	0.00	0.00
ATOM	1685	N	VAL	213	80.337	3.586	7.670	0.00	0.00
ATOM	1686	CA	VAL	213	79.950	4.258	8.926	0.00	0.00
ATOM	1687	C	VAL	213	79.649	3.222	10.076	0.00	0.00
ATOM	1688	O	VAL	213	79.668	3.654	11.232	0.00	0.00
ATOM	1689	CB	VAL	213	78.688	5.111	8.631	0.00	0.00
ATOM	1690	CG1	VAL	213	77.985	5.787	9.777	0.00	0.00
ATOM	1691	CG2	VAL	213	79.006	6.128	7.519	0.00	0.00
ATOM	1692	N	PHE	214	79.191	1.980	9.796	0.00	0.00
ATOM	1693	CA	PHE	214	78.971	0.905	10.743	0.00	0.00
ATOM	1694	C	PHE	214	80.115	0.842	11.802	0.00	0.00
ATOM	1695	O	PHE	214	79.779	0.484	12.931	0.00	0.00
ATOM	1696	CB	PHE	214	78.910	−0.426	9.974	0.00	0.00
ATOM	1697	CG	PHE	214	78.678	−1.631	10.873	0.00	0.00
ATOM	1698	CD1	PHE	214	77.428	−1.794	11.490	0.00	0.00
ATOM	1699	CD2	PHE	214	79.690	−2.558	11.093	0.00	0.00
ATOM	1700	CE1	PHE	214	77.189	−2.897	12.315	0.00	0.00
ATOM	1701	CE2	PHE	214	79.454	−3.682	11.899	0.00	0.00
ATOM	1702	CZ	PHE	214	78.199	−3.841	12.502	0.00	0.00
ATOM	1703	N	GLN	215	81.425	1.030	11.451	0.00	0.00
ATOM	1704	CA	GLN	215	82.468	1.067	12.491	0.00	0.00
ATOM	1705	C	GLN	215	82.074	2.093	13.589	0.00	0.00
ATOM	1706	O	GLN	215	82.067	1.679	14.761	0.00	0.00
ATOM	1707	CB	GLN	215	83.900	1.452	11.968	0.00	0.00
ATOM	1708	CG	GLN	215	84.911	1.980	13.051	0.00	0.00
ATOM	1709	CD	GLN	215	85.353	0.838	13.980	0.00	0.00
ATOM	1710	OE1	GLN	215	86.020	−0.152	13.358	0.00	0.00
ATOM	1711	NE2	GLN	215	85.070	0.910	15.279	0.00	0.00
ATOM	1712	N	GLU	216	81.969	3.362	13.300	0.00	0.00
ATOM	1713	CA	GLU	216	81.655	4.429	14.283	0.00	0.00
ATOM	1714	C	GLU	216	80.268	4.227	14.995	0.00	0.00
ATOM	1715	O	GLU	216	80.300	3.933	16.191	0.00	0.00
ATOM	1716	CB	GLU	216	81.855	5.817	13.692	0.00	0.00
ATOM	1717	CG	GLU	216	81.404	7.059	14.462	0.00	0.00
ATOM	1718	CD	GLU	216	82.539	7.480	15.416	0.00	0.00
ATOM	1719	OE1	GLU	216	83.129	6.648	16.104	0.00	0.00
ATOM	1720	OE2	GLU	216	82.767	8.704	15.326	0.00	0.00
ATOM	1721	N	ALA	217	79.095	4.319	14.295	0.00	0.00
ATOM	1722	CA	ALA	217	77.771	4.051	14.891	0.00	0.00
ATOM	1723	C	ALA	217	77.010	2.946	14.061	0.00	0.00
ATOM	1724	O	ALA	217	76.568	3.180	12.939	0.00	0.00
ATOM	1725	CB	ALA	217	76.979	5.371	14.958	0.00	0.00
ATOM	1726	N	LYS	218	77.117	1.712	14.561	0.00	0.00
ATOM	1727	CA	LYS	218	76.512	0.568	13.887	0.00	0.00
ATOM	1728	C	LYS	218	74.946	0.719	13.717	0.00	0.00
ATOM	1729	O	LYS	218	74.543	0.981	12.573	0.00	0.00
ATOM	1730	CB	LYS	218	76.798	−0.721	14.702	0.00	0.00
ATOM	1731	CG	LYS	218	78.235	−0.952	15.075	0.00	0.00
ATOM	1732	CD	LYS	218	78.323	−1.936	16.240	0.00	0.00
ATOM	1733	CE	LYS	218	79.713	−1.947	16.864	0.00	0.00
ATOM	1734	NZ	LYS	218	79.773	−2.788	18.090	0.00	0.00
ATOM	1735	N	ARG	219	74.170	0.717	14.812	0.00	0.00
ATOM	1736	CA	ARG	219	72.728	0.926	14.717	0.00	0.00
ATOM	1737	C	ARG	219	72.107	1.677	15.892	0.00	0.00
ATOM	1738	O	ARG	219	70.871	1.796	15.860	0.00	0.00
ATOM	1739	CB	ARG	219	72.118	−0.485	14.624	0.00	0.00
ATOM	1740	CG	ARG	219	72.018	−1.272	15.936	0.00	0.00
ATOM	1741	CD	ARG	219	71.848	−2.724	15.524	0.00	0.00
ATOM	1742	NE	ARG	219	70.681	−3.343	16.145	0.00	0.00
ATOM	1743	CZ	ARG	219	70.759	−4.639	16.592	0.00	0.00
ATOM	1744	NH1	ARG	219	71.928	−5.378	16.432	0.00	0.00
ATOM	1745	NH2	ARG	219	69.657	−5.179	17.190	0.00	0.00
ATOM	1746	N	GLN	220	72.873	2.426	16.721	0.00	0.00
ATOM	1747	CA	GLN	220	72.243	3.014	17.864	0.00	0.00
ATOM	1748	C	GLN	220	72.785	4.370	18.259	0.00	0.00
ATOM	1749	O	GLN	220	74.001	4.612	18.253	0.00	0.00
ATOM	1750	CB	GLN	220	72.464	2.087	19.065	0.00	0.00
ATOM	1751	CG	GLN	220	71.968	0.673	18.971	0.00	0.00
ATOM	1752	CD	GLN	220	71.879	−0.216	20.219	0.00	0.00
ATOM	1753	OE1	GLN	220	71.791	0.357	21.311	0.00	0.00
ATOM	1754	NE2	GLN	220	71.834	−1.566	20.089	0.00	0.00
ATOM	1755	N	LEU	221	71.847	5.278	18.273	0.00	0.00
ATOM	1756	CA	LEU	221	71.978	6.632	18.682	0.00	0.00
ATOM	1757	C	LEU	221	71.074	6.698	19.974	0.00	0.00
ATOM	1758	O	LEU	221	69.901	7.073	19.829	0.00	0.00
ATOM	1759	CB	LEU	221	71.369	7.321	17.486	0.00	0.00
ATOM	1760	CG	LEU	221	72.215	7.670	16.271	0.00	0.00
ATOM	1761	CD1	LEU	221	73.702	7.858	16.486	0.00	0.00
ATOM	1762	CD2	LEU	221	71.820	6.499	15.385	0.00	0.00
ATOM	1763	N	GLN	222	71.590	6.541	21.195	0.00	0.00
ATOM	1764	CA	GLN	222	70.667	6.502	22.376	0.00	0.00
ATOM	1765	C	GLN	222	70.481	7.859	23.094	0.00	0.00
ATOM	1766	O	GLN	222	69.370	8.050	23.609	0.00	0.00
ATOM	1767	CB	GLN	222	71.203	5.416	23.333	0.00	0.00
ATOM	1768	CG	GLN	222	71.127	4.002	22.762	0.00	0.00
ATOM	1769	CD	GLN	222	69.739	3.338	22.638	0.00	0.00
ATOM	1770	OE1	GLN	222	69.660	2.166	22.199	0.00	0.00
ATOM	1771	NE2	GLN	222	68.665	3.984	22.990	0.00	0.00
ATOM	1772	N	LYS	223	71.512	8.708	23.252	0.00	0.00
ATOM	1773	CA	LYS	223	71.287	9.956	23.961	0.00	0.00
ATOM	1774	C	LYS	223	70.445	10.868	23.043	0.00	0.00
ATOM	1775	O	LYS	223	71.019	11.634	22.284	0.00	0.00
ATOM	1776	CB	LYS	223	72.621	10.547	24.424	0.00	0.00
ATOM	1777	CG	LYS	223	72.424	11.808	25.243	0.00	0.00
ATOM	1778	CD	LYS	223	73.743	12.229	25.842	0.00	0.00
ATOM	1779	CE	LYS	223	73.517	12.587	27.304	0.00	0.00
ATOM	1780	NZ	LYS	223	73.190	11.412	28.104	0.00	0.00
ATOM	1781	N	ILE	224	69.244	11.178	23.517	0.00	0.00
ATOM	1782	CA	ILE	224	68.296	11.956	22.722	0.00	0.00
ATOM	1783	C	ILE	224	68.725	13.453	22.496	0.00	0.00
ATOM	1784	O	ILE	224	68.221	14.006	21.517	0.00	0.00
ATOM	1785	CB	ILE	224	66.907	11.792	23.357	0.00	0.00
ATOM	1786	CG1	ILE	224	65.811	12.285	22.414	0.00	0.00
ATOM	1787	CG2	ILE	224	66.871	12.596	24.680	0.00	0.00
ATOM	1788	CD1	ILE	224	64.378	11.908	22.825	0.00	0.00
ATOM	1789	N	ASP	225	69.274	14.198	23.498	0.00	0.00
ATOM	1790	CA	ASP	225	69.560	15.635	23.200	0.00	0.00
ATOM	1791	C	ASP	225	70.484	15.778	21.942	0.00	0.00
ATOM	1792	O	ASP	225	69.968	16.252	20.940	0.00	0.00
ATOM	1793	CB	ASP	225	70.186	16.372	24.381	0.00	0.00
ATOM	1794	CG	ASP	225	69.318	16.402	25.578	0.00	0.00
ATOM	1795	OD1	ASP	225	68.135	16.851	25.307	0.00	0.00
ATOM	1796	OD2	ASP	225	69.630	16.047	26.726	0.00	0.00
ATOM	1797	N	LYS	226	71.842	15.724	22.076	0.00	0.00
ATOM	1798	CA	LYS	226	72.787	15.746	20.947	0.00	0.00
ATOM	1799	C	LYS	226	72.520	16.935	19.952	0.00	0.00
ATOM	1800	O	LYS	226	72.165	16.685	18.794	0.00	0.00
ATOM	1801	CB	LYS	226	72.554	14.394	20.384	0.00	0.00
ATOM	1802	CG	LYS	226	73.076	13.223	21.127	0.00	0.00
ATOM	1803	CD	LYS	226	73.295	12.026	20.221	0.00	0.00
ATOM	1804	CE	LYS	226	71.994	11.483	19.686	0.00	0.00
ATOM	1805	NZ	LYS	226	72.138	10.297	18.846	0.00	0.00
ATOM	1806	N	SER	227	72.325	18.177	20.471	0.00	0.00
ATOM	1807	CA	SER	227	72.140	19.391	19.681	0.00	0.00
ATOM	1808	C	SER	227	73.322	20.294	19.904	0.00	0.00
ATOM	1809	O	SER	227	73.232	21.248	20.724	0.00	0.00
ATOM	1810	CB	SER	227	70.855	20.078	20.015	0.00	0.00
ATOM	1811	OG	SER	227	69.647	19.476	19.624	0.00	0.00
ATOM	1812	N	GLU	228	74.203	20.256	18.956	0.00	0.00
ATOM	1813	CA	GLU	228	75.463	21.033	18.908	0.00	0.00
ATOM	1814	C	GLU	228	76.154	21.062	20.319	0.00	0.00
ATOM	1815	O	GLU	228	77.168	21.770	20.410	0.00	0.00
ATOM	1816	CB	GLU	228	75.101	22.480	18.526	0.00	0.00
ATOM	1817	CG	GLU	228	75.104	22.696	17.054	0.00	0.00
ATOM	1818	CD	GLU	228	76.197	22.309	16.184	0.00	0.00
ATOM	1819	OE1	GLU	228	77.253	23.022	16.105	0.00	0.00
ATOM	1820	OE2	GLU	228	76.044	21.186	15.472	0.00	0.00
ATOM	1821	N	GLY	229	75.957	20.074	21.221	0.00	0.00
ATOM	1822	CA	GLY	229	76.550	20.073	22.572	0.00	0.00
ATOM	1823	C	GLY	229	77.855	19.218	22.726	0.00	0.00
ATOM	1824	O	GLY	229	78.746	19.729	23.401	0.00	0.00
ATOM	1825	N	PHE	230	78.075	18.133	21.940	0.00	0.00
ATOM	1826	CA	PHE	230	79.253	17.277	22.092	0.00	0.00
ATOM	1827	C	PHE	230	79.369	16.271	20.897	0.00	0.00
ATOM	1828	O	PHE	230	78.778	16.546	19.859	0.00	0.00
ATOM	1829	CB	PHE	230	79.190	16.576	23.499	0.00	0.00
ATOM	1830	CG	PHE	230	80.326	15.542	23.641	0.00	0.00
ATOM	1831	CD1	PHE	230	80.212	14.224	23.202	0.00	0.00
ATOM	1832	CD2	PHE	230	81.520	15.937	24.223	0.00	0.00
ATOM	1833	CE1	PHE	230	81.266	13.325	23.338	0.00	0.00
ATOM	1834	CE2	PHE	230	82.570	15.039	24.361	0.00	0.00
ATOM	1835	CZ	PHE	230	82.439	13.731	23.915	0.00	0.00
ATOM	1836	N	CYS	231	80.544	15.636	20.828	0.00	0.00
ATOM	1837	CA	CYS	231	80.698	14.598	19.787	0.00	0.00
ATOM	1838	C	CYS	231	79.396	13.722	19.636	0.00	0.00
ATOM	1839	O	CYS	231	79.150	13.270	18.514	0.00	0.00
ATOM	1840	CB	CYS	231	81.908	13.691	20.025	0.00	0.00
ATOM	1841	SG	CYS	231	83.387	14.505	20.626	0.00	0.00
ATOM	1842	N	LEU	232	78.651	13.376	20.710	0.00	0.00
ATOM	1843	CA	LEU	232	77.372	12.649	20.637	0.00	0.00
ATOM	1844	C	LEU	232	76.293	13.328	19.719	0.00	0.00
ATOM	1845	O	LEU	232	75.622	12.590	19.054	0.00	0.00
ATOM	1846	CB	LEU	232	76.895	12.539	22.078	0.00	0.00
ATOM	1847	CG	LEU	232	77.182	11.299	22.871	0.00	0.00
ATOM	1848	CD1	LEU	232	78.637	10.921	22.981	0.00	0.00
ATOM	1849	CD2	LEU	232	76.608	11.362	24.329	0.00	0.00
ATOM	1850	N	LYS	233	76.158	14.671	19.665	0.00	0.00
ATOM	1851	CA	LYS	233	75.220	15.345	18.754	0.00	0.00
ATOM	1852	C	LYS	233	75.276	14.759	17.282	0.00	0.00
ATOM	1853	O	LYS	233	74.204	14.756	16.670	0.00	0.00
ATOM	1854	CB	LYS	233	75.486	16.863	18.709	0.00	0.00
ATOM	1855	CG	LYS	233	76.815	17.208	18.100	0.00	0.00
ATOM	1856	CD	LYS	233	77.120	18.669	17.932	0.00	0.00
ATOM	1857	CE	LYS	233	78.502	18.528	17.289	0.00	0.00
ATOM	1858	NZ	LYS	233	79.249	19.768	17.279	0.00	0.00
ATOM	1859	N	GLU	234	76.460	14.621	16.616	0.00	0.00
ATOM	1860	CA	GLU	234	76.566	13.976	15.277	0.00	0.00
ATOM	1861	C	GLU	234	75.746	12.633	15.161	0.00	0.00
ATOM	1862	O	GLU	234	75.680	12.119	14.051	0.00	0.00
ATOM	1863	CB	GLU	234	78.062	13.786	14.983	0.00	0.00
ATOM	1864	CG	GLU	234	78.884	15.041	14.735	0.00	0.00
ATOM	1865	CD	GLU	234	78.351	16.011	13.723	0.00	0.00
ATOM	1866	OE1	GLU	234	78.282	17.229	13.831	0.00	0.00
ATOM	1867	OE2	GLU	234	77.886	15.473	12.617	0.00	0.00
ATOM	1868	N	HIS	235	75.730	11.887	16.270	0.00	0.00
ATOM	1869	CA	HIS	235	75.002	10.647	16.476	0.00	0.00
ATOM	1870	C	HIS	235	73.483	10.871	16.164	0.00	0.00
ATOM	1871	O	HIS	235	73.065	10.338	15.138	0.00	0.00
ATOM	1872	CB	HIS	235	75.340	10.228	17.952	0.00	0.00
ATOM	1873	CG	HIS	235	75.482	8.723	18.295	0.00	0.00
ATOM	1874	ND1	HIS	235	74.898	8.154	19.433	0.00	0.00
ATOM	1875	CD2	HIS	235	76.174	7.703	17.703	0.00	0.00
ATOM	1876	CE1	HIS	235	75.242	6.878	19.493	0.00	0.00
ATOM	1877	NE2	HIS	235	76.002	6.594	18.471	0.00	0.00
ATOM	1878	N	LYS	236	72.846	11.965	16.668	0.00	0.00
ATOM	1879	CA	LYS	236	71.452	12.276	16.418	0.00	0.00
ATOM	1880	C	LYS	236	71.284	12.725	14.933	0.00	0.00
ATOM	1881	O	LYS	236	70.254	12.373	14.360	0.00	0.00
ATOM	1882	CB	LYS	236	71.030	13.259	17.447	0.00	0.00
ATOM	1883	CG	LYS	236	69.625	13.716	17.422	0.00	0.00
ATOM	1884	CD	LYS	236	69.408	14.442	18.733	0.00	0.00
ATOM	1885	CE	LYS	236	67.951	14.774	18.890	0.00	0.00
ATOM	1886	NZ	LYS	236	67.202	13.545	18.715	0.00	0.00
ATOM	1887	N	ALA	237	72.147	13.607	14.402	0.00	0.00
ATOM	1888	CA	ALA	237	72.160	14.020	13.024	0.00	0.00
ATOM	1889	C	ALA	237	72.320	12.753	12.108	0.00	0.00
ATOM	1890	O	ALA	237	71.665	12.739	11.080	0.00	0.00
ATOM	1891	CB	ALA	237	73.279	15.046	12.831	0.00	0.00
ATOM	1892	N	LEU	238	73.303	11.837	12.341	0.00	0.00
ATOM	1893	CA	LEU	238	73.480	10.580	11.595	0.00	0.00
ATOM	1894	C	LEU	238	72.217	9.686	11.651	0.00	0.00
ATOM	1895	O	LEU	238	71.878	9.172	10.589	0.00	0.00
ATOM	1896	CB	LEU	238	74.717	9.788	12.115	0.00	0.00
ATOM	1897	CG	LEU	238	75.012	8.424	11.447	0.00	0.00
ATOM	1898	CD1	LEU	238	75.346	8.568	9.963	0.00	0.00
ATOM	1899	CD2	LEU	238	76.123	7.662	12.177	0.00	0.00
ATOM	1900	N	LYS	239	71.727	9.216	12.832	0.00	0.00
ATOM	1901	CA	LYS	239	70.470	8.451	12.918	0.00	0.00
ATOM	1902	C	LYS	239	69.354	9.133	12.089	0.00	0.00
ATOM	1903	O	LYS	239	68.581	8.383	11.499	0.00	0.00
ATOM	1904	CB	LYS	239	69.949	8.370	14.349	0.00	0.00
ATOM	1905	CG	LYS	239	68.826	7.425	14.652	0.00	0.00
ATOM	1906	CD	LYS	239	68.584	7.194	16.136	0.00	0.00
ATOM	1907	CE	LYS	239	67.935	5.846	16.428	0.00	0.00
ATOM	1908	NZ	LYS	239	68.024	5.406	17.844	0.00	0.00
ATOM	1909	N	THR	240	69.017	10.422	12.336	0.00	0.00
ATOM	1910	CA	THR	240	68.054	11.244	11.577	0.00	0.00
ATOM	1911	C	THR	240	68.254	11.093	10.042	0.00	0.00
ATOM	1912	O	THR	240	67.252	10.807	9.403	0.00	0.00
ATOM	1913	CB	THR	240	67.934	12.712	12.119	0.00	0.00
ATOM	1914	OG1	THR	240	67.546	12.744	13.533	0.00	0.00
ATOM	1915	CG2	THR	240	66.905	13.528	11.291	0.00	0.00
ATOM	1916	N	LEU	241	69.426	11.385	9.461	0.00	0.00
ATOM	1917	CA	LEU	241	69.717	11.198	8.022	0.00	0.00
ATOM	1918	C	LEU	241	69.502	9.703	7.573	0.00	0.00
ATOM	1919	O	LEU	241	69.173	9.534	6.400	0.00	0.00
ATOM	1920	CB	LEU	241	71.161	11.677	7.834	0.00	0.00
ATOM	1921	CG	LEU	241	71.289	13.196	8.072	0.00	0.00
ATOM	1922	CD1	LEU	241	72.747	13.625	7.860	0.00	0.00
ATOM	1923	CD2	LEU	241	70.450	13.899	7.116	0.00	0.00
ATOM	1924	N	GLY	242	69.875	8.688	8.382	0.00	0.00
ATOM	1925	CA	GLY	242	69.632	7.271	8.117	0.00	0.00
ATOM	1926	C	GLY	242	68.102	7.081	7.972	0.00	0.00
ATOM	1927	O	GLY	242	67.714	6.279	7.113	0.00	0.00
ATOM	1928	N	ILE	243	67.325	7.439	9.017	0.00	0.00
ATOM	1929	CA	ILE	243	65.884	7.418	8.994	0.00	0.00
ATOM	1930	C	ILE	243	65.387	8.209	7.722	0.00	0.00
ATOM	1931	O	ILE	243	64.332	7.830	7.218	0.00	0.00
ATOM	1932	CB	ILE	243	65.254	7.933	10.319	0.00	0.00
ATOM	1933	CG1	ILE	243	65.394	6.822	11.394	0.00	0.00
ATOM	1934	CG2	ILE	243	63.732	8.264	10.111	0.00	0.00
ATOM	1935	CD1	ILE	243	64.436	5.632	11.111	0.00	0.00
ATOM	1936	N	ILE	244	65.957	9.397	7.354	0.00	0.00
ATOM	1937	CA	ILE	244	65.533	10.064	6.081	0.00	0.00
ATOM	1938	C	ILE	244	65.472	9.022	4.911	0.00	0.00
ATOM	1939	O	ILE	244	64.460	9.009	4.213	0.00	0.00
ATOM	1940	CB	ILE	244	66.443	11.250	5.744	0.00	0.00
ATOM	1941	CG1	ILE	244	66.457	12.250	6.869	0.00	0.00
ATOM	1942	CG2	ILE	244	66.055	11.857	4.401	0.00	0.00
ATOM	1943	CD1	ILE	244	67.431	13.459	6.665	0.00	0.00
ATOM	1944	N	MET	245	66.554	8.258	4.646	0.00	0.00
ATOM	1945	CA	MET	245	66.611	7.177	3.656	0.00	0.00
ATOM	1946	C	MET	245	65.463	6.125	3.788	0.00	0.00
ATOM	1947	O	MET	245	65.105	5.585	2.734	0.00	0.00
ATOM	1948	CB	MET	245	67.909	6.422	3.900	0.00	0.00
ATOM	1949	CG	MET	245	69.188	7.090	3.600	0.00	0.00
ATOM	1950	SD	MET	245	70.635	5.990	3.860	0.00	0.00
ATOM	1951	CE	MET	245	70.024	4.891	5.129	0.00	0.00
ATOM	1952	N	GLY	246	65.224	5.553	5.000	0.00	0.00
ATOM	1953	CA	GLY	246	64.176	4.614	5.296	0.00	0.00
ATOM	1954	C	GLY	246	62.810	5.182	4.849	0.00	0.00
ATOM	1955	O	GLY	246	62.079	4.397	4.265	0.00	0.00
ATOM	1956	N	THR	247	62.391	6.396	5.249	0.00	0.00
ATOM	1957	CA	THR	247	61.152	6.999	4.760	0.00	0.00
ATOM	1958	C	THR	247	61.114	7.133	3.184	0.00	0.00
ATOM	1959	O	THR	247	59.995	7.101	2.676	0.00	0.00
ATOM	1960	CB	THR	247	60.821	8.295	5.558	0.00	0.00
ATOM	1961	OG1	THR	247	60.599	8.072	6.963	0.00	0.00
ATOM	1962	CG2	THR	247	59.561	9.047	5.009	0.00	0.00
ATOM	1963	N	PHE	248	62.181	7.619	2.483	0.00	0.00
ATOM	1964	CA	PHE	248	62.283	7.689	1.019	0.00	0.00
ATOM	1965	C	PHE	248	62.141	6.270	0.390	0.00	0.00
ATOM	1966	O	PHE	248	61.611	6.231	−0.718	0.00	0.00
ATOM	1967	CB	PHE	248	63.578	8.394	0.547	0.00	0.00
ATOM	1968	CG	PHE	248	63.643	8.542	−0.993	0.00	0.00
ATOM	1969	CD1	PHE	248	63.342	9.754	−1.525	0.00	0.00
ATOM	1970	CD2	PHE	248	63.976	7.501	−1.851	0.00	0.00
ATOM	1971	CE1	PHE	248	63.364	9.932	−2.899	0.00	0.00
ATOM	1972	CE2	PHE	248	63.994	7.670	−3.209	0.00	0.00
ATOM	1973	CZ	PHE	248	63.685	8.893	−3.746	0.00	0.00
ATOM	1974	N	THR	249	62.881	5.225	0.837	0.00	0.00
ATOM	1975	CA	THR	249	62.639	3.889	0.294	0.00	0.00
ATOM	1976	C	THR	249	61.140	3.474	0.608	0.00	0.00
ATOM	1977	O	THR	249	60.476	3.164	−0.333	0.00	0.00
ATOM	1978	CB	THR	249	63.542	2.807	0.942	0.00	0.00
ATOM	1979	OG1	THR	249	63.556	2.703	2.337	0.00	0.00
ATOM	1980	CG2	THR	249	64.967	2.852	0.359	0.00	0.00
ATOM	1981	N	LEU	250	60.535	3.833	1.766	0.00	0.00
ATOM	1982	CA	LEU	250	59.089	3.514	1.999	0.00	0.00
ATOM	1983	C	LEU	250	58.184	4.200	0.938	0.00	0.00
ATOM	1984	O	LEU	250	57.451	3.508	0.232	0.00	0.00
ATOM	1985	CB	LEU	250	58.617	3.868	3.412	0.00	0.00
ATOM	1986	CG	LEU	250	59.394	3.135	4.496	0.00	0.00
ATOM	1987	CD1	LEU	250	59.159	3.911	5.774	0.00	0.00
ATOM	1988	CD2	LEU	250	58.856	1.718	4.637	0.00	0.00
ATOM	1989	N	CYS	251	58.416	5.496	0.732	0.00	0.00
ATOM	1990	CA	CYS	251	57.702	6.381	−0.195	0.00	0.00
ATOM	1991	C	CYS	251	57.973	6.022	−1.683	0.00	0.00
ATOM	1992	O	CYS	251	56.957	5.925	−2.429	0.00	0.00
ATOM	1993	CB	CYS	251	58.210	7.804	0.147	0.00	0.00
ATOM	1994	SG	CYS	251	56.967	9.048	−0.365	0.00	0.00
ATOM	1995	N	TRP	252	59.219	5.627	−2.004	0.00	0.00
ATOM	1996	CA	TRP	252	59.540	5.384	−3.419	0.00	0.00
ATOM	1997	C	TRP	252	60.035	3.907	−3.734	0.00	0.00
ATOM	1998	O	TRP	252	60.434	3.640	−4.906	0.00	0.00
ATOM	1999	CB	TRP	252	60.418	6.430	−4.031	0.00	0.00
ATOM	2000	CG	TRP	252	59.918	7.793	−3.916	0.00	0.00
ATOM	2001	CD1	TRP	252	60.406	8.823	−3.138	0.00	0.00
ATOM	2002	CD2	TRP	252	58.804	8.318	−4.641	0.00	0.00
ATOM	2003	NE1	TRP	252	59.674	9.954	−3.384	0.00	0.00
ATOM	2004	CE2	TRP	252	58.704	9.696	−4.293	0.00	0.00
ATOM	2005	CE3	TRP	252	57.895	7.783	−5.542	0.00	0.00
ATOM	2006	CZ2	TRP	252	57.703	10.499	−4.798	0.00	0.00
ATOM	2007	CZ3	TRP	252	56.919	8.610	−6.081	0.00	0.00
ATOM	2008	CH2	TRP	252	56.792	9.950	−5.689	0.00	0.00
ATOM	2009	N	LEU	253	59.663	2.949	−2.829	0.00	0.00
ATOM	2010	CA	LEU	253	59.877	1.552	−2.972	0.00	0.00
ATOM	2011	C	LEU	253	58.747	1.036	−3.962	0.00	0.00
ATOM	2012	O	LEU	253	59.069	1.000	−5.173	0.00	0.00
ATOM	2013	CB	LEU	253	60.088	0.734	−1.724	0.00	0.00
ATOM	2014	CG	LEU	253	61.482	0.397	−1.296	0.00	0.00
ATOM	2015	CD1	LEU	253	62.515	1.477	−1.534	0.00	0.00
ATOM	2016	CD2	LEU	253	61.469	0.209	0.195	0.00	0.00
ATOM	2017	N	PRO	254	57.474	0.690	−3.614	0.00	0.00
ATOM	2018	CA	PRO	254	56.600	0.329	−4.653	0.00	0.00
ATOM	2019	C	PRO	254	56.466	1.439	−5.672	0.00	0.00
ATOM	2020	O	PRO	254	56.260	1.057	−6.803	0.00	0.00
ATOM	2021	CB	PRO	254	55.326	−0.071	−3.974	0.00	0.00
ATOM	2022	CG	PRO	254	55.371	0.541	−2.581	0.00	0.00
ATOM	2023	CD	PRO	254	56.810	0.501	−2.259	0.00	0.00
ATOM	2024	N	PHE	255	56.677	2.738	−5.398	0.00	0.00
ATOM	2025	CA	PHE	255	56.605	3.648	−6.580	0.00	0.00
ATOM	2026	C	PHE	255	57.504	3.134	−7.753	0.00	0.00
ATOM	2027	O	PHE	255	57.048	3.178	−8.905	0.00	0.00
ATOM	2028	CB	PHE	255	57.198	5.002	−6.210	0.00	0.00
ATOM	2029	CG	PHE	255	57.293	5.981	−7.333	0.00	0.00
ATOM	2030	CD1	PHE	255	56.136	6.558	−7.872	0.00	0.00
ATOM	2031	CD2	PHE	255	58.493	6.174	−7.994	0.00	0.00
ATOM	2032	CE1	PHE	255	56.232	7.387	−8.977	0.00	0.00
ATOM	2033	CE2	PHE	255	58.617	6.958	−9.139	0.00	0.00
ATOM	2034	CZ	PHE	255	57.435	7.577	−9.640	0.00	0.00
ATOM	2035	N	PHE	256	58.830	2.954	−7.528	0.00	0.00
ATOM	2036	CA	PHE	256	59.804	2.430	−8.467	0.00	0.00
ATOM	2037	C	PHE	256	59.561	0.962	−8.906	0.00	0.00
ATOM	2038	O	PHE	256	60.112	0.620	−9.939	0.00	0.00
ATOM	2039	CB	PHE	256	61.214	2.630	−7.922	0.00	0.00
ATOM	2040	CG	PHE	256	61.768	3.984	−8.074	0.00	0.00
ATOM	2041	CD1	PHE	256	61.787	4.593	−9.319	0.00	0.00
ATOM	2042	CD2	PHE	256	62.272	4.643	−6.943	0.00	0.00
ATOM	2043	CE1	PHE	256	62.310	5.879	−9.470	0.00	0.00
ATOM	2044	CE2	PHE	256	62.781	5.933	−7.093	0.00	0.00
ATOM	2045	CZ	PHE	256	62.789	6.552	−8.336	0.00	0.00
ATOM	2046	N	ILE	257	59.384	0.018	−7.931	0.00	0.00
ATOM	2047	CA	ILE	257	59.046	−1.381	−8.133	0.00	0.00
ATOM	2048	C	ILE	257	57.835	−1.541	−9.090	0.00	0.00
ATOM	2049	O	ILE	257	57.949	−2.411	−9.955	0.00	0.00
ATOM	2050	CB	ILE	257	58.807	−2.085	−6.762	0.00	0.00
ATOM	2051	CG1	ILE	257	59.915	−1.949	−5.745	0.00	0.00
ATOM	2052	CG2	ILE	257	58.470	−3.590	−6.977	0.00	0.00
ATOM	2053	CD1	ILE	257	61.331	−2.125	−6.288	0.00	0.00
ATOM	2054	N	VAL	258	56.639	−0.952	−8.828	0.00	0.00
ATOM	2055	CA	VAL	258	55.514	−1.027	−9.805	0.00	0.00
ATOM	2056	C	VAL	258	56.003	−0.361	−11.144	0.00	0.00
ATOM	2057	O	VAL	258	55.726	−0.917	−12.209	0.00	0.00
ATOM	2058	CB	VAL	258	54.271	−0.286	−9.388	0.00	0.00
ATOM	2059	CG1	VAL	258	54.532	1.103	−8.878	0.00	0.00
ATOM	2060	CG2	VAL	258	53.183	−0.322	−10.405	0.00	0.00
ATOM	2061	N	ASN	259	56.702	0.816	−11.101	0.00	0.00
ATOM	2062	CA	ASN	259	57.291	1.494	−12.204	0.00	0.00
ATOM	2063	C	ASN	259	58.186	0.546	−13.083	0.00	0.00
ATOM	2064	O	ASN	259	57.886	0.442	−14.279	0.00	0.00
ATOM	2065	CB	ASN	259	58.203	2.499	−11.597	0.00	0.00
ATOM	2066	CG	ASN	259	58.225	3.852	−12.139	0.00	0.00
ATOM	2067	OD1	ASN	259	57.496	4.781	−11.768	0.00	0.00
ATOM	2068	ND2	ASN	259	59.179	3.827	−13.078	0.00	0.00
ATOM	2069	N	ILE	260	59.248	−0.082	−12.525	0.00	0.00
ATOM	2070	CA	ILE	260	60.084	−1.045	−13.199	0.00	0.00
ATOM	2071	C	ILE	260	59.271	−2.286	−13.726	0.00	0.00
ATOM	2072	O	ILE	260	59.590	−2.724	−14.833	0.00	0.00
ATOM	2073	CB	ILE	260	61.278	−1.376	−12.289	0.00	0.00
ATOM	2074	CG1	ILE	260	62.308	−2.224	−13.020	0.00	0.00
ATOM	2075	CG2	ILE	260	60.834	−2.101	−11.011	0.00	0.00
ATOM	2076	CD1	ILE	260	63.592	−2.510	−12.232	0.00	0.00
ATOM	2077	N	VAL	261	58.281	−2.862	−12.977	0.00	0.00
ATOM	2078	CA	VAL	261	57.429	−3.972	−13.439	0.00	0.00
ATOM	2079	C	VAL	261	56.699	−3.568	−14.761	0.00	0.00
ATOM	2080	O	VAL	261	56.798	−4.369	−15.698	0.00	0.00
ATOM	2081	CB	VAL	261	56.453	−4.456	−12.329	0.00	0.00
ATOM	2082	CG1	VAL	261	55.244	−5.148	−13.031	0.00	0.00
ATOM	2083	CG2	VAL	261	57.031	−5.617	−11.498	0.00	0.00
ATOM	2084	N	HIS	262	55.883	−2.490	−14.813	0.00	0.00
ATOM	2085	CA	HIS	262	55.264	−2.017	−16.064	0.00	0.00
ATOM	2086	C	HIS	262	56.318	−1.981	−17.240	0.00	0.00
ATOM	2087	O	HIS	262	55.930	−2.430	−18.313	0.00	0.00
ATOM	2088	CB	HIS	262	54.586	−0.653	−15.922	0.00	0.00
ATOM	2089	CG	HIS	262	53.465	−0.653	−14.942	0.00	0.00
ATOM	2090	ND1	HIS	262	52.252	−1.253	−15.135	0.00	0.00
ATOM	2091	CD2	HIS	262	53.411	−0.044	−13.715	0.00	0.00
ATOM	2092	CE1	HIS	262	51.513	−1.059	−14.063	0.00	0.00
ATOM	2093	NE2	HIS	262	52.174	−0.311	−13.192	0.00	0.00
ATOM	2094	N	VAL	263	57.475	−1.291	−17.132	0.00	0.00
ATOM	2095	CA	VAL	263	58.504	−1.174	−18.171	0.00	0.00
ATOM	2096	C	VAL	263	58.952	−2.564	−18.769	0.00	0.00
ATOM	2097	O	VAL	263	59.024	−2.617	−20.006	0.00	0.00
ATOM	2098	CB	VAL	263	59.703	−0.370	−17.619	0.00	0.00
ATOM	2099	CG1	VAL	263	60.929	−0.613	−18.479	0.00	0.00
ATOM	2100	CG2	VAL	263	59.359	1.091	−17.482	0.00	0.00
ATOM	2101	N	ILE	264	59.446	−3.546	−17.983	0.00	0.00
ATOM	2102	CA	ILE	264	59.781	−4.824	−18.639	0.00	0.00
ATOM	2103	C	ILE	264	58.498	−5.462	−19.314	0.00	0.00
ATOM	2104	O	ILE	264	58.587	−5.772	−20.504	0.00	0.00
ATOM	2105	CB	ILE	264	60.426	−5.898	−17.684	0.00	0.00
ATOM	2106	CG1	ILE	264	59.896	−5.787	−16.273	0.00	0.00
ATOM	2107	CG2	ILE	264	61.941	−6.266	−17.727	0.00	0.00
ATOM	2108	CD1	ILE	264	59.531	−7.266	−15.829	0.00	0.00
ATOM	2109	N	GLN	265	57.406	−5.786	−18.583	0.00	0.00
ATOM	2110	CA	GLN	265	56.161	−6.286	−19.136	0.00	0.00
ATOM	2111	C	GLN	265	55.269	−5.107	−19.555	0.00	0.00
ATOM	2112	O	GLN	265	54.469	−4.595	−18.754	0.00	0.00
ATOM	2113	CB	GLN	265	55.466	−7.159	−18.088	0.00	0.00
ATOM	2114	CG	GLN	265	56.191	−8.295	−17.424	0.00	0.00
ATOM	2115	CD	GLN	265	55.386	−8.854	−16.258	0.00	0.00
ATOM	2116	OE1	GLN	265	56.010	−9.102	−15.217	0.00	0.00
ATOM	2117	NE2	GLN	265	54.096	−9.079	−16.523	0.00	0.00
ATOM	2118	N	ASP	266	55.279	−4.882	−20.866	0.00	0.00
ATOM	2119	CA	ASP	266	54.460	−3.901	−21.513	0.00	0.00
ATOM	2120	C	ASP	266	53.108	−4.546	−21.958	0.00	0.00
ATOM	2121	O	ASP	266	53.111	−5.571	−22.639	0.00	0.00
ATOM	2122	CB	ASP	266	55.217	−3.311	−22.695	0.00	0.00
ATOM	2123	CG	ASP	266	56.391	−2.495	−22.240	0.00	0.00
ATOM	2124	OD1	ASP	266	56.395	−2.006	−21.116	0.00	0.00
ATOM	2125	OD2	ASP	266	57.321	−2.301	−23.013	0.00	0.00
ATOM	2126	N	ASN	267	52.084	−3.679	−21.996	0.00	0.00
ATOM	2127	CA	ASN	267	50.686	−4.000	−22.423	0.00	0.00
ATOM	2128	C	ASN	267	49.938	−5.072	−21.522	0.00	0.00
ATOM	2129	O	ASN	267	49.060	−5.779	−22.040	0.00	0.00
ATOM	2130	CB	ASN	267	50.656	−4.439	−23.912	0.00	0.00
ATOM	2131	CG	ASN	267	49.227	−4.372	−24.498	0.00	0.00
ATOM	2132	OD1	ASN	267	48.538	−3.417	−24.205	0.00	0.00
ATOM	2133	ND2	ASN	267	48.764	−5.361	−25.281	0.00	0.00
ATOM	2134	N	LEU	268	50.117	−5.110	−20.172	0.00	0.00
ATOM	2135	CA	LEU	268	49.394	−5.994	−19.281	0.00	0.00
ATOM	2136	C	LEU	268	49.129	−5.163	−17.967	0.00	0.00
ATOM	2137	O	LEU	268	50.049	−5.165	−17.138	0.00	0.00
ATOM	2138	CB	LEU	268	50.281	−7.216	−19.078	0.00	0.00
ATOM	2139	CG	LEU	268	49.764	−8.542	−18.611	0.00	0.00
ATOM	2140	CD1	LEU	268	50.880	−9.519	−18.873	0.00	0.00
ATOM	2141	CD2	LEU	268	49.393	−8.558	−17.128	0.00	0.00
ATOM	2142	N	ILE	269	47.864	−4.788	−17.614	0.00	0.00
ATOM	2143	CA	ILE	269	47.620	−4.054	−16.330	0.00	0.00
ATOM	2144	C	ILE	269	46.155	−3.503	−16.056	0.00	0.00
ATOM	2145	O	ILE	269	45.328	−3.444	−16.975	0.00	0.00
ATOM	2146	CB	ILE	269	48.672	−2.891	−16.204	0.00	0.00
ATOM	2147	CG1	ILE	269	48.741	−2.397	−14.710	0.00	0.00
ATOM	2148	CG2	ILE	269	48.235	−1.706	−17.018	0.00	0.00
ATOM	2149	CD1	ILE	269	49.210	−3.445	−13.712	0.00	0.00
ATOM	2150	N	ARG	270	45.859	−2.948	−14.842	0.00	0.00
ATOM	2151	CA	ARG	270	44.603	−2.293	−14.405	0.00	0.00
ATOM	2152	C	ARG	270	44.962	−0.869	−13.817	0.00	0.00
ATOM	2153	O	ARG	270	45.980	−0.762	−13.111	0.00	0.00
ATOM	2154	CB	ARG	270	43.936	−3.164	−13.328	0.00	0.00
ATOM	2155	CG	ARG	270	43.393	−4.473	−13.856	0.00	0.00
ATOM	2156	CD	ARG	270	42.279	−4.306	−14.815	0.00	0.00
ATOM	2157	NE	ARG	270	41.726	−5.580	−15.169	0.00	0.00
ATOM	2158	CZ	ARG	270	42.262	−6.381	−16.089	0.00	0.00
ATOM	2159	NH1	ARG	270	43.403	−6.110	−16.693	0.00	0.00
ATOM	2160	NH2	ARG	270	41.657	−7.523	−16.395	0.00	0.00
ATOM	2161	N	LYS	271	44.125	0.185	−13.973	0.00	0.00
ATOM	2162	CA	LYS	271	44.416	1.561	−13.510	0.00	0.00
ATOM	2163	C	LYS	271	44.773	1.678	−12.002	0.00	0.00
ATOM	2164	O	LYS	271	45.869	2.179	−11.752	0.00	0.00
ATOM	2165	CB	LYS	271	43.461	2.619	−14.049	0.00	0.00
ATOM	2166	CG	LYS	271	43.163	2.502	−15.516	0.00	0.00
ATOM	2167	CD	LYS	271	44.546	2.468	−16.218	0.00	0.00
ATOM	2168	CE	LYS	271	44.433	2.347	−17.748	0.00	0.00
ATOM	2169	NZ	LYS	271	45.606	1.513	−18.235	0.00	0.00
ATOM	2170	N	GLU	272	43.947	1.255	−11.060	0.00	0.00
ATOM	2171	CA	GLU	272	44.236	1.442	−9.627	0.00	0.00
ATOM	2172	C	GLU	272	45.627	0.880	−9.156	0.00	0.00
ATOM	2173	O	GLU	272	46.103	1.418	−8.159	0.00	0.00
ATOM	2174	CB	GLU	272	43.110	0.758	−8.824	0.00	0.00
ATOM	2175	CG	GLU	272	41.677	1.022	−9.237	0.00	0.00
ATOM	2176	CD	GLU	272	40.660	1.121	−8.126	0.00	0.00
ATOM	2177	OE1	GLU	272	41.090	1.356	−6.943	0.00	0.00
ATOM	2178	OE2	GLU	272	39.477	0.964	−8.364	0.00	0.00
ATOM	2179	N	VAL	273	46.131	−0.275	−9.652	0.00	0.00
ATOM	2180	CA	VAL	273	47.490	−0.780	−9.305	0.00	0.00
ATOM	2181	C	VAL	273	48.607	0.346	−9.340	0.00	0.00
ATOM	2182	O	VAL	273	49.265	0.508	−8.312	0.00	0.00
ATOM	2183	CB	VAL	273	47.811	−1.941	−10.258	0.00	0.00
ATOM	2184	CG1	VAL	273	49.118	−2.681	−9.908	0.00	0.00
ATOM	2185	CG2	VAL	273	46.675	−2.962	−10.214	0.00	0.00
ATOM	2186	N	TYR	274	48.750	1.172	−10.416	0.00	0.00
ATOM	2187	CA	TYR	274	49.801	2.204	−10.573	0.00	0.00
ATOM	2188	C	TYR	274	49.445	3.491	−9.714	0.00	0.00
ATOM	2189	O	TYR	274	50.315	3.880	−8.946	0.00	0.00
ATOM	2190	CB	TYR	274	50.052	2.444	−12.087	0.00	0.00
ATOM	2191	CG	TYR	274	51.061	3.556	−12.314	0.00	0.00
ATOM	2192	CD1	TYR	274	50.661	4.809	−12.783	0.00	0.00
ATOM	2193	CD2	TYR	274	52.405	3.283	−12.085	0.00	0.00
ATOM	2194	CE1	TYR	274	51.634	5.778	−12.981	0.00	0.00
ATOM	2195	CE2	TYR	274	53.372	4.263	−12.290	0.00	0.00
ATOM	2196	CZ	TYR	274	52.966	5.509	−12.743	0.00	0.00
ATOM	2197	OH	TYR	274	53.985	6.424	−12.940	0.00	0.00
ATOM	2198	N	ILE	275	48.134	3.768	−9.441	0.00	0.00
ATOM	2199	CA	ILE	275	47.616	4.863	−8.586	0.00	0.00
ATOM	2200	C	ILE	275	48.221	4.817	−7.166	0.00	0.00
ATOM	2201	O	ILE	275	48.543	5.876	−6.636	0.00	0.00
ATOM	2202	CB	ILE	275	46.068	4.638	−8.425	0.00	0.00
ATOM	2203	CG1	ILE	275	45.354	4.632	−9.818	0.00	0.00
ATOM	2204	CG2	ILE	275	45.490	5.833	−7.559	0.00	0.00
ATOM	2205	CD1	ILE	275	43.787	4.754	−9.902	0.00	0.00
ATOM	2206	N	LEU	276	47.982	3.678	−6.487	0.00	0.00
ATOM	2207	CA	LEU	276	48.335	3.434	−5.062	0.00	0.00
ATOM	2208	C	LEU	276	49.703	3.956	−4.655	0.00	0.00
ATOM	2209	O	LEU	276	49.706	5.034	−4.073	0.00	0.00
ATOM	2210	CB	LEU	276	48.215	1.934	−4.779	0.00	0.00
ATOM	2211	CG	LEU	276	47.026	1.100	−5.128	0.00	0.00
ATOM	2212	CD1	LEU	276	47.317	−0.335	−4.697	0.00	0.00
ATOM	2213	CD2	LEU	276	45.786	1.594	−4.442	0.00	0.00
ATOM	2214	N	LEU	277	50.769	3.602	−5.284	0.00	0.00
ATOM	2215	CA	LEU	277	52.137	3.906	−4.909	0.00	0.00
ATOM	2216	C	LEU	277	52.586	5.292	−5.470	0.00	0.00
ATOM	2217	O	LEU	277	53.652	5.771	−5.064	0.00	0.00
ATOM	2218	CB	LEU	277	52.954	2.835	−5.540	0.00	0.00
ATOM	2219	CG	LEU	277	52.675	1.390	−5.424	0.00	0.00
ATOM	2220	CD1	LEU	277	53.594	0.494	−6.231	0.00	0.00
ATOM	2221	CD2	LEU	277	52.724	0.948	−3.973	0.00	0.00
ATOM	2222	N	ASN	278	51.996	5.703	−6.625	0.00	0.00
ATOM	2223	CA	ASN	278	52.233	7.003	−7.206	0.00	0.00
ATOM	2224	C	ASN	278	51.671	8.090	−6.259	0.00	0.00
ATOM	2225	O	ASN	278	52.444	9.000	−5.928	0.00	0.00
ATOM	2226	CB	ASN	278	51.558	6.984	−8.564	0.00	0.00
ATOM	2227	CG	ASN	278	52.413	6.323	−9.663	0.00	0.00
ATOM	2228	OD1	ASN	278	51.945	5.392	−10.335	0.00	0.00
ATOM	2229	ND2	ASN	278	53.668	6.733	−9.843	0.00	0.00
ATOM	2230	N	TRP	279	50.348	8.099	−5.942	0.00	0.00
ATOM	2231	CA	TRP	279	49.706	8.997	−4.951	0.00	0.00
ATOM	2232	C	TRP	279	50.449	8.788	−3.592	0.00	0.00
ATOM	2233	O	TRP	279	50.661	9.755	−2.908	0.00	0.00
ATOM	2234	CB	TRP	279	48.212	8.785	−4.804	0.00	0.00
ATOM	2235	CG	TRP	279	47.576	9.902	−3.997	0.00	0.00
ATOM	2236	CD1	TRP	279	47.004	11.047	−4.433	0.00	0.00
ATOM	2237	CD2	TRP	279	47.541	9.963	−2.558	0.00	0.00
ATOM	2238	NE1	TRP	279	46.622	11.838	−3.378	0.00	0.00
ATOM	2239	CE2	TRP	279	46.989	11.203	−2.221	0.00	0.00
ATOM	2240	CE3	TRP	279	47.932	9.051	−1.556	0.00	0.00
ATOM	2241	CZ2	TRP	279	46.795	11.570	−0.882	0.00	0.00
ATOM	2242	CZ3	TRP	279	47.802	9.446	−0.218	0.00	0.00
ATOM	2243	CH2	TRP	279	47.192	10.677	0.103	0.00	0.00
ATOM	2244	N	ILE	280	50.515	7.549	−3.012	0.00	0.00
ATOM	2245	CA	ILE	280	51.164	7.399	−1.670	0.00	0.00
ATOM	2246	C	ILE	280	52.581	8.079	−1.668	0.00	0.00
ATOM	2247	O	ILE	280	52.952	8.603	−0.619	0.00	0.00
ATOM	2248	CB	ILE	280	51.175	5.963	−1.124	0.00	0.00
ATOM	2249	CG1	ILE	280	52.028	5.758	0.112	0.00	0.00
ATOM	2250	CG2	ILE	280	51.781	5.015	−2.185	0.00	0.00
ATOM	2251	CD1	ILE	280	51.440	6.342	1.392	0.00	0.00
ATOM	2252	N	GLY	281	53.409	7.985	−2.729	0.00	0.00
ATOM	2253	CA	GLY	281	54.721	8.646	−2.810	0.00	0.00
ATOM	2254	C	GLY	281	54.671	10.215	−2.731	0.00	0.00
ATOM	2255	O	GLY	281	55.716	10.838	−2.924	0.00	0.00
ATOM	2256	N	TYR	282	53.489	10.801	−2.785	0.00	0.00
ATOM	2257	CA	TYR	282	53.226	12.249	−2.859	0.00	0.00
ATOM	2258	C	TYR	282	53.560	12.824	−1.417	0.00	0.00
ATOM	2259	O	TYR	282	53.796	14.044	−1.345	0.00	0.00
ATOM	2260	CB	TYR	282	51.673	12.226	−3.085	0.00	0.00
ATOM	2261	CG	TYR	282	51.023	12.220	−4.482	0.00	0.00
ATOM	2262	CD1	TYR	282	51.693	11.956	−5.685	0.00	0.00
ATOM	2263	CD2	TYR	282	49.639	12.471	−4.586	0.00	0.00
ATOM	2264	CE1	TYR	282	51.046	11.916	−6.915	0.00	0.00
ATOM	2265	CE2	TYR	282	48.933	12.432	−5.806	0.00	0.00
ATOM	2266	CZ	TYR	282	49.666	12.144	−6.968	0.00	0.00
ATOM	2267	OH	TYR	282	49.040	12.089	−8.170	0.00	0.00
ATOM	2268	N	VAL	283	53.349	12.058	−0.311	0.00	0.00
ATOM	2269	CA	VAL	283	53.713	12.452	1.002	0.00	0.00
ATOM	2270	C	VAL	283	55.246	12.774	1.024	0.00	0.00
ATOM	2271	O	VAL	283	55.699	13.121	2.117	0.00	0.00
ATOM	2272	CB	VAL	283	53.302	11.357	1.993	0.00	0.00
ATOM	2273	CG1	VAL	283	51.790	11.130	1.989	0.00	0.00
ATOM	2274	CG2	VAL	283	54.021	10.039	1.731	0.00	0.00
ATOM	2275	N	ASN	284	56.079	12.321	0.036	0.00	0.00
ATOM	2276	CA	ASN	284	57.465	12.684	−0.024	0.00	0.00
ATOM	2277	C	ASN	284	57.656	14.230	0.261	0.00	0.00
ATOM	2278	O	ASN	284	58.733	14.585	0.742	0.00	0.00
ATOM	2279	CB	ASN	284	58.096	12.408	−1.409	0.00	0.00
ATOM	2280	CG	ASN	284	57.358	13.050	−2.551	0.00	0.00
ATOM	2281	OD1	ASN	284	56.326	13.699	−2.484	0.00	0.00
ATOM	2282	ND2	ASN	284	57.976	12.963	−3.703	0.00	0.00
ATOM	2283	N	SER	285	56.875	15.122	−0.396	0.00	0.00
ATOM	2284	CA	SER	285	56.903	16.549	−0.264	0.00	0.00
ATOM	2285	C	SER	285	56.839	16.908	1.241	0.00	0.00
ATOM	2286	O	SER	285	57.919	17.014	1.809	0.00	0.00
ATOM	2287	CB	SER	285	55.716	17.282	−0.966	0.00	0.00
ATOM	2288	OG	SER	285	55.092	18.389	−0.295	0.00	0.00
ATOM	2289	N	GLY	286	55.795	16.460	1.927	0.00	0.00
ATOM	2290	CA	GLY	286	55.564	16.802	3.281	0.00	0.00
ATOM	2291	C	GLY	286	56.404	16.070	4.366	0.00	0.00
ATOM	2292	O	GLY	286	56.732	16.750	5.343	0.00	0.00
ATOM	2293	N	PHE	287	56.912	14.841	4.154	0.00	0.00
ATOM	2294	CA	PHE	287	57.622	14.062	5.182	0.00	0.00
ATOM	2295	C	PHE	287	58.989	14.647	5.571	0.00	0.00
ATOM	2296	O	PHE	287	59.435	14.349	6.678	0.00	0.00
ATOM	2297	CB	PHE	287	57.874	12.617	4.806	0.00	0.00
ATOM	2298	CG	PHE	287	58.932	12.240	3.839	0.00	0.00
ATOM	2299	CD1	PHE	287	58.734	12.463	2.457	0.00	0.00
ATOM	2300	CD2	PHE	287	60.143	11.724	4.305	0.00	0.00
ATOM	2301	CE1	PHE	287	59.755	12.127	1.560	0.00	0.00
ATOM	2302	CE2	PHE	287	61.164	11.389	3.398	0.00	0.00
ATOM	2303	CZ	PHE	287	60.962	11.597	2.016	0.00	0.00
ATOM	2304	N	ASN	288	59.687	15.347	4.653	0.00	0.00
ATOM	2305	CA	ASN	288	60.984	15.838	4.903	0.00	0.00
ATOM	2306	C	ASN	288	61.089	16.686	6.212	0.00	0.00
ATOM	2307	O	ASN	288	61.870	16.258	7.081	0.00	0.00
ATOM	2308	CB	ASN	288	61.354	16.617	3.680	0.00	0.00
ATOM	2309	CG	ASN	288	61.940	15.785	2.589	0.00	0.00
ATOM	2310	OD1	ASN	288	63.134	15.559	2.557	0.00	0.00
ATOM	2311	ND2	ASN	288	61.272	15.263	1.571	0.00	0.00
ATOM	2312	N	PRO	289	60.503	17.913	6.415	0.00	0.00
ATOM	2313	CA	PRO	289	60.673	18.524	7.718	0.00	0.00
ATOM	2314	C	PRO	289	59.952	17.695	8.855	0.00	0.00
ATOM	2315	O	PRO	289	60.210	18.045	10.012	0.00	0.00
ATOM	2316	CB	PRO	289	60.041	19.901	7.648	0.00	0.00
ATOM	2317	CG	PRO	289	60.239	20.300	6.145	0.00	0.00
ATOM	2318	CD	PRO	289	60.154	19.011	5.382	0.00	0.00
ATOM	2319	N	LEU	290	58.827	16.979	8.599	0.00	0.00
ATOM	2320	CA	LEU	290	58.241	16.136	9.655	0.00	0.00
ATOM	2321	C	LEU	290	59.349	15.322	10.400	0.00	0.00
ATOM	2322	O	LEU	290	59.169	15.107	11.613	0.00	0.00
ATOM	2323	CB	LEU	290	57.148	15.233	9.108	0.00	0.00
ATOM	2324	CG	LEU	290	56.015	15.864	8.342	0.00	0.00
ATOM	2325	CD1	LEU	290	55.058	14.757	7.868	0.00	0.00
ATOM	2326	CD2	LEU	290	55.223	16.827	9.223	0.00	0.00
ATOM	2327	N	ILE	291	60.291	14.685	9.651	0.00	0.00
ATOM	2328	CA	ILE	291	61.409	13.990	10.251	0.00	0.00
ATOM	2329	C	ILE	291	62.342	14.914	11.131	0.00	0.00
ATOM	2330	O	ILE	291	63.009	14.329	11.996	0.00	0.00
ATOM	2331	CB	ILE	291	62.214	13.293	9.106	0.00	0.00
ATOM	2332	CG1	ILE	291	61.299	12.232	8.421	0.00	0.00
ATOM	2333	CG2	ILE	291	63.538	12.630	9.634	0.00	0.00
ATOM	2334	CD1	ILE	291	62.003	11.632	7.161	0.00	0.00
ATOM	2335	N	TYR	292	62.176	16.257	11.159	0.00	0.00
ATOM	2336	CA	TYR	292	63.060	17.077	12.003	0.00	0.00
ATOM	2337	C	TYR	292	62.685	17.023	13.546	0.00	0.00
ATOM	2338	O	TYR	292	63.146	17.817	14.349	0.00	0.00
ATOM	2339	CB	TYR	292	63.100	18.487	11.322	0.00	0.00
ATOM	2340	CG	TYR	292	64.441	19.164	11.676	0.00	0.00
ATOM	2341	CD1	TYR	292	64.670	19.539	12.977	0.00	0.00
ATOM	2342	CD2	TYR	292	65.459	19.314	10.731	0.00	0.00
ATOM	2343	CE1	TYR	292	65.865	20.064	13.372	0.00	0.00
ATOM	2344	CE2	TYR	292	66.677	19.849	11.120	0.00	0.00
ATOM	2345	CZ	TYR	292	66.860	20.211	12.459	0.00	0.00
ATOM	2346	OH	TYR	292	68.024	20.730	12.993	0.00	0.00
ATOM	2347	N	CYS	293	61.609	16.254	13.885	0.00	0.00
ATOM	2348	CA	CYS	293	61.156	15.906	15.268	0.00	0.00
ATOM	2349	C	CYS	293	62.382	15.353	16.066	0.00	0.00
ATOM	2350	O	CYS	293	62.369	15.384	17.293	0.00	0.00
ATOM	2351	CB	CYS	293	59.860	15.010	15.326	0.00	0.00
ATOM	2352	SG	CYS	293	58.480	16.041	16.011	0.00	0.00
ATOM	2353	N	ARG	294	63.359	14.741	15.346	0.00	0.00
ATOM	2354	CA	ARG	294	64.587	14.227	15.842	0.00	0.00
ATOM	2355	C	ARG	294	65.719	15.315	16.077	0.00	0.00
ATOM	2356	O	ARG	294	66.871	14.859	16.297	0.00	0.00
ATOM	2357	CB	ARG	294	65.022	13.178	14.810	0.00	0.00
ATOM	2358	CG	ARG	294	64.114	12.025	14.548	0.00	0.00
ATOM	2359	CD	ARG	294	63.528	11.319	15.771	0.00	0.00
ATOM	2360	NE	ARG	294	64.516	10.399	16.275	0.00	0.00
ATOM	2361	CZ	ARG	294	64.983	10.419	17.492	0.00	0.00
ATOM	2362	NH1	ARG	294	64.572	11.257	18.401	0.00	0.00
ATOM	2363	NH2	ARG	294	65.903	9.557	17.797	0.00	0.00
ATOM	2364	N	SER	295	65.600	16.611	15.807	0.00	0.00
ATOM	2365	CA	SER	295	66.760	17.457	16.187	0.00	0.00
ATOM	2366	C	SER	295	66.261	18.523	17.141	0.00	0.00
ATOM	2367	O	SER	295	65.771	19.526	16.619	0.00	0.00
ATOM	2368	CB	SER	295	67.307	17.985	14.905	0.00	0.00
ATOM	2369	OG	SER	295	68.527	18.521	14.611	0.00	0.00
ATOM	2370	N	PRO	296	66.431	18.481	18.494	0.00	0.00
ATOM	2371	CA	PRO	296	65.960	19.644	19.221	0.00	0.00
ATOM	2372	C	PRO	296	66.698	20.907	18.800	0.00	0.00
ATOM	2373	O	PRO	296	66.236	21.960	19.234	0.00	0.00
ATOM	2374	CB	PRO	296	66.166	19.516	20.762	0.00	0.00
ATOM	2375	CG	PRO	296	67.030	18.319	20.791	0.00	0.00
ATOM	2376	CD	PRO	296	67.054	17.519	19.458	0.00	0.00
ATOM	2377	N	ASP	297	67.808	20.910	18.009	0.00	0.00
ATOM	2378	CA	ASP	297	68.351	22.227	17.581	0.00	0.00
ATOM	2379	C	ASP	297	67.282	23.057	16.788	0.00	0.00
ATOM	2380	O	ASP	297	67.032	24.199	17.174	0.00	0.00
ATOM	2381	CB	ASP	297	69.638	21.952	16.784	0.00	0.00
ATOM	2382	CG	ASP	297	70.446	23.184	16.410	0.00	0.00
ATOM	2383	OD1	ASP	297	69.919	24.229	16.061	0.00	0.00
ATOM	2384	OD2	ASP	297	71.660	23.077	16.488	0.00	0.00
ATOM	2385	N	PHE	298	66.727	22.582	15.630	0.00	0.00
ATOM	2386	CA	PHE	298	65.651	23.239	14.838	0.00	0.00
ATOM	2387	C	PHE	298	64.318	23.282	15.583	0.00	0.00
ATOM	2388	O	PHE	298	63.574	24.189	15.267	0.00	0.00
ATOM	2389	CB	PHE	298	65.485	22.706	13.441	0.00	0.00
ATOM	2390	CG	PHE	298	64.597	23.488	12.539	0.00	0.00
ATOM	2391	CD1	PHE	298	63.355	22.956	12.173	0.00	0.00
ATOM	2392	CD2	PHE	298	64.948	24.766	12.091	0.00	0.00
ATOM	2393	CE1	PHE	298	62.485	23.667	11.345	0.00	0.00
ATOM	2394	CE2	PHE	298	64.097	25.506	11.251	0.00	0.00
ATOM	2395	CZ	PHE	298	62.852	24.936	10.884	0.00	0.00
ATOM	2396	N	ARG	299	63.763	22.110	15.990	0.00	0.00
ATOM	2397	CA	ARG	299	62.545	22.183	16.797	0.00	0.00
ATOM	2398	C	ARG	299	62.565	23.296	17.864	0.00	0.00
ATOM	2399	O	ARG	299	61.515	23.934	17.985	0.00	0.00
ATOM	2400	CB	ARG	299	62.093	20.863	17.378	0.00	0.00
ATOM	2401	CG	ARG	299	60.677	20.767	17.804	0.00	0.00
ATOM	2402	CD	ARG	299	60.299	19.327	18.181	0.00	0.00
ATOM	2403	NE	ARG	299	58.932	19.361	18.627	0.00	0.00
ATOM	2404	CZ	ARG	299	57.915	19.224	17.783	0.00	0.00
ATOM	2405	NH1	ARG	299	58.067	19.018	16.487	0.00	0.00
ATOM	2406	NH2	ARG	299	56.690	19.488	18.221	0.00	0.00
ATOM	2407	N	ILE	300	63.569	23.380	18.791	0.00	0.00
ATOM	2408	CA	ILE	300	63.611	24.528	19.734	0.00	0.00
ATOM	2409	C	ILE	300	63.586	25.893	18.950	0.00	0.00
ATOM	2410	O	ILE	300	63.016	26.840	19.511	0.00	0.00
ATOM	2411	CB	ILE	300	64.762	24.377	20.773	0.00	0.00
ATOM	2412	CG1	ILE	300	64.493	25.285	22.012	0.00	0.00
ATOM	2413	CG2	ILE	300	66.152	24.667	20.162	0.00	0.00
ATOM	2414	CD1	ILE	300	65.538	25.020	23.115	0.00	0.00
ATOM	2415	N	ALA	301	64.238	26.045	17.779	0.00	0.00
ATOM	2416	CA	ALA	301	64.211	27.191	16.930	0.00	0.00
ATOM	2417	C	ALA	301	62.782	27.423	16.286	0.00	0.00
ATOM	2418	O	ALA	301	62.426	28.618	16.175	0.00	0.00
ATOM	2419	CB	ALA	301	65.210	26.859	15.785	0.00	0.00
ATOM	2420	N	PHE	302	62.065	26.409	15.708	0.00	0.00
ATOM	2421	CA	PHE	302	60.714	26.833	15.240	0.00	0.00
ATOM	2422	C	PHE	302	59.801	27.261	16.410	0.00	0.00
ATOM	2423	O	PHE	302	58.830	27.948	16.099	0.00	0.00
ATOM	2424	CB	PHE	302	60.075	25.893	14.194	0.00	0.00
ATOM	2425	CG	PHE	302	59.848	24.468	14.770	0.00	0.00
ATOM	2426	CD1	PHE	302	60.754	23.474	14.424	0.00	0.00
ATOM	2427	CD2	PHE	302	58.746	24.177	15.569	0.00	0.00
ATOM	2428	CE1	PHE	302	60.542	22.187	14.889	0.00	0.00
ATOM	2429	CE2	PHE	302	58.560	22.889	16.020	0.00	0.00
ATOM	2430	CZ	PHE	302	59.455	21.893	15.683	0.00	0.00
ATOM	2431	N	GLN	303	59.904	26.698	17.634	0.00	0.00
ATOM	2432	CA	GLN	303	59.123	27.146	18.813	0.00	0.00
ATOM	2433	C	GLN	303	59.517	28.620	19.138	0.00	0.00
ATOM	2434	O	GLN	303	58.661	29.365	19.632	0.00	0.00
ATOM	2435	CB	GLN	303	59.365	26.232	20.010	0.00	0.00
ATOM	2436	CG	GLN	303	58.873	24.828	19.752	0.00	0.00
ATOM	2437	CD	GLN	303	59.077	23.945	20.967	0.00	0.00
ATOM	2438	OE1	GLN	303	58.269	23.987	21.885	0.00	0.00
ATOM	2439	NE2	GLN	303	60.152	23.186	20.988	0.00	0.00
ATOM	2440	N	GLU	304	60.794	29.003	19.007	0.00	0.00
ATOM	2441	CA	GLU	304	61.303	30.354	19.170	0.00	0.00
ATOM	2442	C	GLU	304	60.581	31.341	18.184	0.00	0.00
ATOM	2443	O	GLU	304	60.492	32.513	18.544	0.00	0.00
ATOM	2444	CB	GLU	304	62.814	30.381	19.090	0.00	0.00
ATOM	2445	CG	GLU	304	63.478	31.639	19.595	0.00	0.00
ATOM	2446	CD	GLU	304	63.473	31.839	21.066	0.00	0.00
ATOM	2447	OE1	GLU	304	63.507	32.913	21.649	0.00	0.00
ATOM	2448	OE2	GLU	304	63.513	30.768	21.725	0.00	0.00
ATOM	2449	N	LEU	305	60.516	31.021	16.860	0.00	0.00
ATOM	2450	CA	LEU	305	59.767	31.857	15.900	0.00	0.00
ATOM	2451	C	LEU	305	58.256	31.822	16.170	0.00	0.00
ATOM	2452	O	LEU	305	57.667	32.907	16.090	0.00	0.00
ATOM	2453	CB	LEU	305	60.008	31.530	14.376	0.00	0.00
ATOM	2454	CG	LEU	305	59.184	32.344	13.310	0.00	0.00
ATOM	2455	CD1	LEU	305	59.606	33.796	13.228	0.00	0.00
ATOM	2456	CD2	LEU	305	59.407	31.680	11.935	0.00	0.00
ATOM	2457	N	LEU	306	57.599	30.636	16.264	0.00	0.00
ATOM	2458	CA	LEU	306	56.146	30.615	16.525	0.00	0.00
ATOM	2459	C	LEU	306	55.799	31.622	17.698	0.00	0.00
ATOM	2460	O	LEU	306	54.863	32.405	17.497	0.00	0.00
ATOM	2461	CB	LEU	306	55.637	29.179	16.733	0.00	0.00
ATOM	2462	CG	LEU	306	55.784	28.300	15.503	0.00	0.00
ATOM	2463	CD1	LEU	306	55.370	26.899	15.867	0.00	0.00
ATOM	2464	CD2	LEU	306	54.919	28.815	14.366	0.00	0.00
ATOM	2465	N	CYS	307	56.347	31.433	18.898	0.00	0.00
ATOM	2466	CA	CYS	307	56.116	32.388	19.902	0.00	0.00
ATOM	2467	C	CYS	307	57.186	33.428	19.641	0.00	0.00
ATOM	2468	O	CYS	307	58.354	33.106	19.927	0.00	0.00
ATOM	2469	CB	CYS	307	56.230	31.815	21.309	0.00	0.00
ATOM	2470	SG	CYS	307	54.827	30.888	21.901	0.00	0.00
ATOM	2471	N	LEU	308	56.863	34.660	19.313	0.00	0.00
ATOM	2472	CA	LEU	308	57.935	35.567	18.975	0.00	0.00
ATOM	2473	C	LEU	308	58.904	35.717	20.173	0.00	0.00
ATOM	2474	O	LEU	308	58.567	36.270	21.235	0.00	0.00
ATOM	2475	CB	LEU	308	57.351	36.943	18.658	0.00	0.00
ATOM	2476	CG	LEU	308	56.351	36.951	17.547	0.00	0.00
ATOM	2477	CD1	LEU	308	55.967	38.398	17.216	0.00	0.00
ATOM	2478	CD2	LEU	308	56.936	36.272	16.295	0.00	0.00
ATOM	2479	N	ARG	309	60.121	35.353	19.863	0.00	0.00
ATOM	2480	CA	ARG	309	61.301	35.437	20.713	0.00	0.00
ATOM	2481	C	ARG	309	61.201	34.837	22.150	0.00	0.00
ATOM	2482	O	ARG	309	62.158	35.080	22.905	0.00	0.00
ATOM	2483	CB	ARG	309	61.427	36.995	20.897	0.00	0.00
ATOM	2484	CG	ARG	309	61.330	37.803	19.646	0.00	0.00
ATOM	2485	CD	ARG	309	61.623	39.285	19.834	0.00	0.00
ATOM	2486	NE	ARG	309	62.987	39.543	20.307	0.00	0.00
ATOM	2487	CZ	ARG	309	64.045	39.626	19.496	0.00	0.00
ATOM	2488	NH1	ARG	309	63.906	39.463	18.172	0.00	0.00
ATOM	2489	NH2	ARG	309	65.293	39.875	19.918	0.00	0.00
ATOM	2490	N	ARG	310	60.416	33.778	22.419	0.00	0.00
ATOM	2491	CA	ARG	310	60.238	33.280	23.776	0.00	0.00
ATOM	2492	C	ARG	310	60.046	31.748	23.834	0.00	0.00
ATOM	2493	O	ARG	310	59.157	31.206	23.159	0.00	0.00
ATOM	2494	CB	ARG	310	58.993	33.952	24.356	0.00	0.00
ATOM	2495	CG	ARG	310	59.138	35.402	24.730	0.00	0.00
ATOM	2496	CD	ARG	310	57.772	36.041	25.028	0.00	0.00
ATOM	2497	NE	ARG	310	57.075	35.512	26.208	0.00	0.00
ATOM	2498	CZ	ARG	310	57.353	35.859	27.475	0.00	0.00
ATOM	2499	NH1	ARG	310	56.596	35.415	28.479	0.00	0.00
ATOM	2500	NH2	ARG	310	58.379	36.646	27.770	0.00	0.00
ATOM	2501	N	SER	311	60.830	31.111	24.681	0.00	0.00
ATOM	2502	CA	SER	311	60.739	29.678	24.960	0.00	0.00
ATOM	2503	C	SER	311	60.478	29.493	26.481	0.00	0.00
ATOM	2504	O	SER	311	61.083	30.235	27.281	0.00	0.00
ATOM	2505	CB	SER	311	62.046	28.975	24.529	0.00	0.00
ATOM	2506	OG	SER	311	62.082	27.568	24.804	0.00	0.00
ATOM	2507	N	SER	312	59.574	28.548	26.855	0.00	0.00
ATOM	2508	CA	SER	312	59.250	28.452	28.274	0.00	0.00
ATOM	2509	C	SER	312	60.290	27.586	29.083	0.00	0.00
ATOM	2510	O	SER	312	59.838	26.876	30.006	0.00	0.00
ATOM	2511	CB	SER	312	57.822	27.866	28.324	0.00	0.00
ATOM	2512	OG	SER	312	56.866	28.432	27.441	0.00	0.00
ATOM	2513	N	LEU	313	61.479	28.196	29.207	0.00	0.00
ATOM	2514	CA	LEU	313	62.666	27.715	29.860	0.00	0.00
ATOM	2515	C	LEU	313	63.651	28.918	29.867	0.00	0.00
ATOM	2516	O	LEU	313	63.540	29.839	29.011	0.00	0.00
ATOM	2517	CB	LEU	313	63.248	26.479	29.131	0.00	0.00
ATOM	2518	CG	LEU	313	62.667	25.083	29.286	0.00	0.00
ATOM	2519	CD1	LEU	313	61.711	24.789	30.426	0.00	0.00
ATOM	2520	CD2	LEU	313	62.075	24.639	27.976	0.00	0.00
ATOM	2521	N	LYS	314	64.725	28.877	30.661	0.00	0.00
ATOM	2522	CA	LYS	314	65.674	29.977	30.551	0.00	0.00
ATOM	2523	C	LYS	314	66.544	29.936	29.259	0.00	0.00
ATOM	2524	O	LYS	314	67.164	30.972	28.998	0.00	0.00
ATOM	2525	CB	LYS	314	66.557	29.897	31.815	0.00	0.00
ATOM	2526	CG	LYS	314	65.847	30.215	33.122	0.00	0.00
ATOM	2527	CD	LYS	314	65.146	31.579	33.225	0.00	0.00
ATOM	2528	CE	LYS	314	64.150	31.544	34.398	0.00	0.00
ATOM	2529	NZ	LYS	314	63.338	32.757	34.503	0.00	0.00
ATOM	2530	N	ALA	315	66.407	28.939	28.348	0.00	0.00
ATOM	2531	CA	ALA	315	67.281	28.832	27.199	0.00	0.00
ATOM	2532	C	ALA	315	68.770	28.840	27.725	0.00	0.00
ATOM	2533	O	ALA	315	69.664	29.342	27.033	0.00	0.00
ATOM	2534	CB	ALA	315	66.978	29.922	26.178	0.00	0.00
ATOM	2535	N	TYR	316	69.035	28.128	28.852	0.00	0.00
ATOM	2536	CA	TYR	316	70.279	28.007	29.503	0.00	0.00
ATOM	2537	C	TYR	316	71.174	27.242	28.525	0.00	0.00
ATOM	2538	O	TYR	316	70.711	26.194	28.026	0.00	0.00
ATOM	2539	CB	TYR	316	70.033	27.327	30.847	0.00	0.00
ATOM	2540	CG	TYR	316	71.171	27.314	31.819	0.00	0.00
ATOM	2541	CD1	TYR	316	72.071	26.266	31.818	0.00	0.00
ATOM	2542	CD2	TYR	316	71.237	28.298	32.783	0.00	0.00
ATOM	2543	CE1	TYR	316	73.049	26.174	32.798	0.00	0.00
ATOM	2544	CE2	TYR	316	72.216	28.211	33.772	0.00	0.00
ATOM	2545	CZ	TYR	316	73.102	27.153	33.760	0.00	0.00
ATOM	2546	OH	TYR	316	74.061	27.036	34.726	0.00	0.00
ATOM	2547	N	GLY	317	72.482	27.401	28.684	0.00	0.00
ATOM	2548	CA	GLY	317	73.328	26.788	27.720	0.00	0.00
ATOM	2549	C	GLY	317	73.384	25.252	27.813	0.00	0.00
ATOM	2550	O	GLY	317	74.343	24.732	28.392	0.00	0.00
ATOM	2551	N	ASN	318	72.837	24.746	26.765	0.00	0.00
ATOM	2552	CA	ASN	318	72.720	23.385	26.324	0.00	0.00
ATOM	2553	C	ASN	318	72.034	23.469	24.919	0.00	0.00
ATOM	2554	O	ASN	318	70.982	24.167	24.862	0.00	0.00
ATOM	2555	CB	ASN	318	71.880	22.515	27.271	0.00	0.00
ATOM	2556	CG	ASN	318	72.541	22.233	28.577	0.00	0.00
ATOM	2557	OD1	ASN	318	71.839	22.169	29.579	0.00	0.00
ATOM	2558	ND2	ASN	318	73.857	22.123	28.649	0.00	0.00
ATOM	2559	N	GLY	319	72.190	22.504	24.017	0.00	0.00
ATOM	2560	CA	GLY	319	71.492	22.665	22.753	0.00	0.00
ATOM	2561	C	GLY	319	71.934	24.051	22.171	0.00	0.00
ATOM	2562	O	GLY	319	71.027	24.887	22.035	0.00	0.00
ATOM	2563	N	TYR	320	73.239	24.353	21.979	0.00	0.00
ATOM	2564	CA	TYR	320	73.773	25.621	21.548	0.00	0.00
ATOM	2565	C	TYR	320	72.730	26.352	20.695	0.00	0.00
ATOM	2566	O	TYR	320	72.457	25.975	19.542	0.00	0.00
ATOM	2567	CB	TYR	320	75.123	25.390	20.841	0.00	0.00
ATOM	2568	CG	TYR	320	76.327	25.649	21.751	0.00	0.00
ATOM	2569	CD1	TYR	320	77.566	25.900	21.202	0.00	0.00
ATOM	2570	CD2	TYR	320	76.182	25.565	23.118	0.00	0.00
ATOM	2571	CE1	TYR	320	78.676	26.054	22.021	0.00	0.00
ATOM	2572	CE2	TYR	320	77.285	25.721	23.947	0.00	0.00
ATOM	2573	CZ	TYR	320	78.532	25.961	23.393	0.00	0.00
ATOM	2574	OH	TYR	320	79.679	26.091	24.244	0.00	0.00
ATOM	2575	N	SER	321	72.426	27.546	21.202	0.00	0.00
ATOM	2576	CA	SER	321	71.390	28.398	20.647	0.00	0.00
ATOM	2577	C	SER	321	71.956	29.150	19.439	0.00	0.00
ATOM	2578	O	SER	321	72.508	30.242	19.539	0.00	0.00
ATOM	2579	CB	SER	321	70.831	29.297	21.761	0.00	0.00
ATOM	2580	OG	SER	321	69.425	29.191	22.005	0.00	0.00
ATOM	2581	N	SER	322	71.553	28.628	18.308	0.00	0.00
ATOM	2582	CA	SER	322	71.906	29.091	16.982	0.00	0.00
ATOM	2583	C	SER	322	70.747	29.807	16.199	0.00	0.00
ATOM	2584	O	SER	322	70.860	29.872	14.974	0.00	0.00
ATOM	2585	CB	SER	322	72.510	27.862	16.286	0.00	0.00
ATOM	2586	OG	SER	322	71.613	26.757	16.125	0.00	0.00
ATOM	2587	N	ASN	323	69.613	30.058	16.761	0.00	0.00
ATOM	2588	CA	ASN	323	68.567	30.779	16.162	0.00	0.00
ATOM	2589	C	ASN	323	69.027	32.252	16.015	0.00	0.00
ATOM	2590	O	ASN	323	69.981	32.711	16.699	0.00	0.00
ATOM	2591	CB	ASN	323	67.461	30.781	17.191	0.00	0.00
ATOM	2592	CG	ASN	323	67.177	29.878	18.342	0.00	0.00
ATOM	2593	OD1	ASN	323	67.757	28.790	18.677	0.00	0.00
ATOM	2594	ND2	ASN	323	66.351	30.336	19.312	0.00	0.00
ATOM	2595	N	GLY	324	68.393	32.982	15.113	0.00	0.00
ATOM	2596	CA	GLY	324	68.742	34.412	15.039	0.00	0.00
ATOM	2597	C	GLY	324	68.606	35.080	16.445	0.00	0.00
ATOM	2598	O	GLY	324	69.173	36.167	16.597	0.00	0.00
ATOM	2599	N	ASN	325	67.569	34.696	17.211	0.00	0.00
ATOM	2600	CA	ASN	325	67.299	35.108	18.553	0.00	0.00
ATOM	2601	C	ASN	325	68.175	34.289	19.555	0.00	0.00
ATOM	2602	O	ASN	325	68.598	33.160	19.247	0.00	0.00
ATOM	2603	CB	ASN	325	65.835	34.723	18.792	0.00	0.00
ATOM	2604	CG	ASN	325	64.857	35.706	18.178	0.00	0.00
ATOM	2605	OD1	ASN	325	63.634	35.526	18.329	0.00	0.00
ATOM	2606	ND2	ASN	325	65.214	36.745	17.401	0.00	0.00
ATOM	2607	N	THR	326	68.206	34.714	20.817	0.00	0.00
ATOM	2608	CA	THR	326	68.895	34.008	21.922	0.00	0.00
ATOM	2609	C	THR	326	70.413	33.767	21.675	0.00	0.00
ATOM	2610	O	THR	326	70.793	32.678	21.201	0.00	0.00
ATOM	2611	CB	THR	326	68.151	32.674	22.275	0.00	0.00
ATOM	2612	OG1	THR	326	66.717	32.785	22.294	0.00	0.00
ATOM	2613	CG2	THR	326	68.626	32.016	23.614	0.00	0.00
ATOM	2614	N	GLY	327	71.182	34.874	21.579	0.00	0.00
ATOM	2615	CA	GLY	327	72.611	34.764	21.424	0.00	0.00
ATOM	2616	C	GLY	327	73.096	34.584	19.965	0.00	0.00
ATOM	2617	O	GLY	327	73.803	33.587	19.755	0.00	0.00
ATOM	2618	N	GLU	328	72.479	35.240	18.940	0.00	0.00
ATOM	2619	CA	GLU	328	72.913	35.171	17.564	0.00	0.00
ATOM	2620	C	GLU	328	74.480	35.212	17.396	0.00	0.00
ATOM	2621	O	GLU	328	74.920	34.645	16.395	0.00	0.00
ATOM	2622	CB	GLU	328	72.166	36.287	16.824	0.00	0.00
ATOM	2623	CG	GLU	328	72.969	37.630	16.948	0.00	0.00
ATOM	2624	CD	GLU	328	72.145	38.850	16.655	0.00	0.00
ATOM	2625	OE1	GLU	328	72.117	39.178	15.440	0.00	0.00
ATOM	2626	OE2	GLU	328	71.563	39.479	17.538	0.00	0.00
ATOM	2627	N	GLN	329	75.254	36.040	18.150	0.00	0.00
ATOM	2628	CA	GLN	329	76.717	36.092	18.148	0.00	0.00
ATOM	2629	C	GLN	329	77.347	34.799	17.577	0.00	0.00
ATOM	2630	O	GLN	329	77.228	33.699	18.114	0.00	0.00
ATOM	2631	CB	GLN	329	77.241	36.291	19.567	0.00	0.00
ATOM	2632	CG	GLN	329	76.507	37.286	20.443	0.00	0.00
ATOM	2633	CD	GLN	329	75.835	38.541	19.964	0.00	0.00
ATOM	2634	OE1	GLN	329	76.479	39.546	19.598	0.00	0.00
ATOM	2635	NE2	GLN	329	74.458	38.613	20.013	0.00	0.00
ATOM	2636	OXT	GLN	329	77.961	34.937	16.519	0.00	0.00
TER	2637	GLN		329
END

[0149] Based on the resulting atomic coordinates, the steric structure model of QRHUB2 (β2 adrenaline receptor) was produced using BIOCES (version 3.10) manufactured by NEC Corporation, and a position into which the agonist (isoproterenol) is placed and a position into which the antagonist (propranolol) is placed were compared. The results are shown in FIGS. 6 to 14.

[0150] From FIGS. 6 to 9, it is seen that this antagonist (isoproterenol) has optical isomers (R isomer and S isomer), and the R isomer binds with the receptor better. From FIGS. 10 to 13, it is seen that a position of antagonist (propranolol) binding is clearly different from a position of agonist (isopretenol) binding.

[0151] FIG. 14 shows relative arrangement in the receptor of the antagonist (propranolol) (left) and the agonist (isoproterenol) (right) in the β2 adrenaline receptor obtained from the above-mentioned model. From FIG. 14, it is seen that the agonist and the antagonist are introduced into pockets at different positions, respectively, as predicted from an experiment of site-specific mutation.

Example 2

Construction of Steric Structures of Amino Acid Sequences Registered in GCRDb, GPCRDB, ExPASy and ORDB

[0152] Regarding amino acid sequences of all GPCRs registered in GCRDb, GPCRDB, ExPASy and ORDB, atomic coordinates defining the steric structure were obtained using 1F88 as a reference protein as in Example 1. Each amino acid sequence was obtained from GCRDb: http://www.gcrdb.uthscsa.edu/, GPCRDB: http://www.gpcr.org/7tm/, ExPASy: http://www.expasv.ch/cqi-bin/sm-qpcr.pl, ORDB: http://ycmi.med.yale.edu/senselab/ordb/. In alignments of these amino acid sequences, the E values calculated by PSI-BLAST were as follows:

	TABLE 2
	1e−3˜	1e−11˜	1e−51˜	1e−100
	1e−10	1e−50	1e−100	or less	Total
	GCRDb	5	71	709	46	831
	GPCRDB	0	0	13	570	583
	ExPASY	0	15	44	318	377
	ORDB	0	78	232	107	417

[0153] There was one E value of 0.001 (1e-3) or more in GPCRDB and ORDB, respectively, and these were removed from the Table 2. Therefore, the number of GPCRs for which the steric structure was produced was as follows: GCRDb:831, GPCRDB:584, ORDB:418, ExPASY:377 (total: 2210).

Example 3

Construction of Steric Structures of Amino Acid Sequences Registered in GeneBank

[0154] Regarding sequences of human, Drosophila, nematode, yeast, thearecress and the like registered in databases such as GeneBank and the like, atomic coordinates defining the steric structure were obtained as in Example 1. Alignment was performed by employing PSAI-BLAST and using 1F88 as a reference protein as in Example 1 and, when the E value was 0.1 or less, it was judged to be GPCRs. Sequences of Drosophila, nematode, yeast and thearecress were obtained from GeneBank: ftp://ncbi.nlm.nih.gov/qenbank/genomes/, and a sequence of human was obtained from ftp://ftp.expasy.ch/databases/swiss-prot/special selection/human.seq, http://cdna.ims.u-tokyo.ac.jp/.

[0155] The numbers of sequences for which construction of the steric structure was performed are as follows:

	TABLE 3
	Registered	Total	Overlapped
	sequence	ORF	ORF	Non-overlapped
	number	number	number	ORF number
Human	6032	272	156	116
Drosophila	14100	147	5	142
Nematode	15808	541	19	522
Thearecress	403	5	0	5
Yeast	6295	5	1	4

[0156] In Table 3, the “registered sequence number” denotes the number of all sequences registered in databases, the “total ORF number” denotes the number of all ORFs (Open Reading Frame) which were determined to be GPCRs, the “overlapped ORF number” denotes the number of ORFs overlapped with sequences of the above four databases (GCRDb, GPCRDb, ORDB, ExPASy), and the “non-overlapped ORF number” denotes the number of ORFs which were not overlapped with sequences of the above-mentioned four databases and were newly determined to be GPCRs, and for which atomic coordinates defining the steric structure were obtained.

Example 4

Construction of Steric Structures of Amino Acid Sequences Registered in PIR, SwissPlot and DAD

[0157] Further, sequences were obtained from PIR: http://www-nbrf.georgetown.edu/pir/, Swiss Plot: http://www.expasy.ch/sprot/sprot-top.html, TrEMBL: http://www.expasy.ch/sprot/sprot-top.html, TrEMBLNEW: http://www.expasy.ch/sprot/sprot-top.html, DAD: ftp://ftp.ddbj.nig.ac.jp, and atomic coordinates defining the steric structure were obtained as in Example 1. Alignment was performed employing PSAI-BLAST and using 1F88 as a reference protein as in Example 1 and, when the E value was 0.1 or less, it was determined to be GPCRs.

[0158] The number of sequences registered in each database are as follows:

TABLE 4
PIR 65       182,162
SWISSPROT 39 87,252
TrEMBL 14    296,917
TrEMBLNEW    71,201
DAD 12       514,763

[0159] Regarding the foregoing total 1,152,295, the number of sequences from which overlapping is omitted is 481,870 and, among them, 5,335 sequences were determined to be GPCRs. Among them, the number of sequences from which overlapping with the above-mentioned four databases (GCRDb, GPCRDb, ORDB, ExPASy) are omitted was 3,475 and, regarding them, atomic coordinates defining the steric structure were obtained.

[0160] The present invention has been explained in detail by referring to specific embodiments, but it would be apparent to a person skilled in the art that various variations and modifications can be made without departing from the spirit and the scope of the present invention.

[0161] The present application is based on Japanese Patent Application (Patent Application No.2000-279155) filed on Sep. 14, 2000 and Japanese Patent Application (Patent Application No. 2000-350378) filed on Nov. 17, 2000, the entire content of which is incorporated herein by reference.

INDUSTRIAL APPLICABILITY

[0162] The excellent points of the present invention compared with the previous methods are as follows:

[0163] (1) Alignment is performed by using the amino acid sequence database “GCRDb” as a profile, a model of an arbitrary G-protein-coupled receptor is produced, for example, based on the steric structure of rhodopsin (PDB ID:1F88), models of a 7-transmembrane a helix structure which is the common nature of GPCRs structures and loop structures of a variety of lengths connecting them are reproduced, whereby, the function of GCRDb serving as an information transmitting mechanism can be presumed.

[0164] (2) In particular, by using a crystal structure of rhodopsin (PDB ID:1F88) as a reference protein, it becomes possible to remarkably improve the steric structure model in a precision, although only structures having different helix arrangements which are not classified into GCRDb of bacteriorhodopsin could be obtained previously.

[0165] (3) The amino acid sequence database “GCRDb” contains only amino acid sequences of GPCRs and, by using alignment software, for example, PSI-BLAST as a motif profile, it is possible to produce a model even when homology is low (20% or less) as compared with PDB:1F88 and, at the same time, suitable alignment is provided regarding arbitrary GPCRs, and an excellent method which does not give unnecessary alignment is provided regarding amino acid sequences other than GPCRs. Previously, it has been said that when homology is reduced to 20% or less, there is a possibility that a structure greatly differs and, therefore, this is a limit of homology modeling (Chochia, C. and Lesk, A. M., EMBO J. 5, 823-826 (1986)). However, a structure of seven helices arrangement of GPCRs obtained by the present method is well conserved, showing that this can be the steric structure model which is reliable in generation of drugs.

[0166] (4) In particular, the modeling software “FAMS” developed by the present inventors adopts an algorism for calculating structures similar to those of natural proteins, from proteins having high homology to proteins having low homology, and from a main chain to a side chain of an amino acid and, by performing modeling based on 1F88 which is a detailed steric structure coordinate present in PDB experimentally obtained using this, the reproductivity of a side chain of GPCRs has been remarkably improved.

[0167] (5) The database of the present invention contains atomic coordinates defining steric structures of GPCRs obtained from almost all sequences which can be currently obtained, of human, Drosophila, nematode, thearecress, yeast and the like, and proteins having presumed function of GPCRs, and is a database covering steric structures of almost all GPCRs.

[0168] As described above, the present method is a method which can construct the steric structure of arbitrary GPCRs with good precision, and the database of the present invention containing atomic coordinates defining the thus obtained GPCRs steric structures is extremely useful for designing, in particular, drug molecules such as medicines, agricultural chemicals and the like.

Claims

1. A method for constructing the steric structure of a transmembrane protein, comprising: selecting a protein having the steric structure to be referred to from the known steric structures of 7-transmembrane G-protein-coupled receptors using a database of amino acid sequences of the receptors as a profile; performing alignment of a desired protein having an unknown steric structure and, based on the alignment information; and producing the steric structure of the desired protein having an unknown steric structure as a G-protein-coupled receptor.

2. The method according to claim 1, wherein the performing alignment includes selecting a protein having the steric structure to be referred to from a database of known steric structures of G-protein-coupled receptors, and juxtaposing an amino acid sequence of the selected reference protein and an amino acid sequence of the desired protein.

3. The method according to claim 2, wherein the steric structure to be referred to is the steric structure of rhodopsin (PDB ID:1F88).

4. The method according to any one of claims 1 to 3, wherein the database of amino acid sequences to be used as a profile is selected from the group consisting of GCRDb, GPCRDB, ExPASy and ORDB.

5. The method according to any one of claims 1 to 4, wherein the database of amino acid sequences is used as a motif profile of PSI-BLAST.

6. The method according to claim 5, wherein in the alignment performed by PSI-BLAST, the identity between a final site-specific score matrix and the reference protein are calculated as an E value and the production of the steric structure is performed when the E value has a value of 0.1 or less.

7. The method according to any one of claims 1 to 6, further comprising performing re-alignment is so as to the given alignment information, in view of a combination of a disulfide bond and, the producing of the steric structure is performed based on the re-alignment information.

8. The method according to any one of claims 1 to 7, wherein the producing comprises: obtaining a coordinate with regard to a Cα atom in an amino acid from the steric structure to be referred to based on the resulting alignment information; optimizing an atomic coordinate of Cα so as to minimize an objective function; adding other atoms of a main chain to the optimized atomic coordinate of Cα to optimize an atomic coordinate of the main chain so as to minimize an objective function; and adding other atoms of a side chain to the optimized atomic coordinate of the main chain to optimize so as to minimize an objective function.

9. An atomic coordinate defining the steric structure of a 7-transmembrane G-protein-coupled receptor obtained by the method according to any one of claims 1 to 8.

10. A computer readable recording medium in which the atomic coordinate according to claim 9 is recorded.

11. A database comprising the atomic coordinate according to claim 9.

12. A method for presuming the function of a protein, comprising: selecting a protein having the steric structure to be referred to from the known steric structures of 7-transmembrane G-protein-coupled receptors using a database of amino acid sequences of the receptors as a profile; performing alignment of a desired protein having an unknown function; and judging that the desired protein is a 7-transmembrane G-protein-coupled receptor when the steric structure of the desired protein can be produced.

13. The method according to claim 12, wherein the performing alignment comprises: selecting the steric structure to be referred to from a database of the known steric structures of G-protein-coupled receptors; juxtaposing an amino acid sequence of the selected reference protein and an amino acid sequence of the desired protein, the database of amino acid sequences used as a profile is selected from the group consisting of GCRDb, GPCRDB, ExPASy and ORDB; and judging that the steric structure of the desired protein can be produced when the alignment has reliability of 98% or more.

14. A method for designing a drug molecule, comprising: identifying, retrieving, assessing or designing a desired drug molecule based on the interaction between the steric structure of a drug candidate molecule and the steric structure of a 7-transmembrane G-protein-coupled receptor produced by using the atomic coordinate according to claim 9, or the atomic coordinate of the recording medium according to claim 10 or the atomic coordinate of the database according to claim 11.

15. A method for screening a medicine or an agricultural chemical, comprising: examining the drug molecule obtained by the method according to claim 14 for its activity and safety as a medicine or an agricultural chemical by a desired pharmacological or physiological test; and selecting a drug molecule having the desired nature.

16. A method for manufacturing a medicine or an agricultural chemical, comprising: formulating by blending the drug molecule obtained by the method according to claim 15 and a pharmaceutically or agriculturally or horticulturally acceptable carrier.

17. A drug molecule obtained by the method according to claim 14.