# Patent

## Title
Isolated peptides having phospholipase inhibitory activity

## Abstract

The invention provides for isolated peptides having phospholipase inhibitory activity, polypeptides comprising phospholipase inhibitory activity and lipases capable of being inhibited by the isolated peptides and/or polypeptides comprising phospholipase inhibitory activity. The invention also relates to nucleic acid constructs, recombinant expression vectors, and recombinant host cells comprising the polynucleotides as well as methods for producing and using the peptides and the polypeptides having lipase inhibitory activity.

## Background
CROSS-REFERENCE TO RELATED APPLICATIONS
This application claims priority or the benefit under 35 U.S.C. 119 of European application no. 08155438.8 filed Apr. 30, 2008 and U.S. provisional application No. 61/050,317 filed May 5, 2008, the contents of which are fully incorporated herein by reference.


REFERENCE TO SEQUENCE LISTING
This application contains a sequence listing in computer readable form. The computer readable form is incorporated herein by reference.
FIELD OF THE INVENTION
The present invention relates to the field of lipases. In particular, it relates to isolated peptides having phospholipase inhibitory activity and isolated polynucleotides encoding the peptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods for producing and using the peptides. It furthermore relates to polypeptides having phospholipase inhibitory activity and lipases capable of being inhibited by such peptides and/or polypeptides.
BACKGROUND OF THE INVENTION
Lipases (EC 3.1.1.3) hydrolyze ester bonds of triacylglycerols and catalyze esterification and transesterification (acidolysis, alcoholysis, and interesterification) in a non-aqueous system. Some lipases, such as phospholipases, hydrolyze ester bonds in phospholipids which are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids. A 26 amino acid C-terminal peptide of Fusarium heterosporum phospholipase was described by Nagao et al., 1998, J. Biochem. 124:1124-29 to play an important role in increasing the thermostability of the lipase without the peptide having an effect on the enzymatic activity.
In light of the broad use of lipids such as e.g. as digestives, for the production of flavours, in dough and baked products of dough, as diagnostic reagents, ingredients of detergent, as catalysts of optical resolutions, etc. it would be desirable to have a mean of controlling the enzymatic activity of lipases. Furthermore, control of the lipolytic activity is desirable from a production point of view due to the option of making enzyme productions that are reproducible regarding their enzymatic activity.
SUMMARY OF THE INVENTION
It is an object of the present invention to provide peptides having lipase inhibitory activity and polynucleotides encoding the peptides, as well as nucleic acid constructs, vectors, and host cells comprising the polynucleotides and methods for producing and using the peptides. It is furthermore an object of the invention to provide polypeptides having lipase inhibitory activity and lipases capable of being inhibited by such peptides and/or polypeptides.
The present invention relates to an isolated peptide having phospholipase inhibitory activity, selected from: (a) an isolated peptide comprising an amino acid sequence having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or 100% identity to the residues 289-310 of SEQ ID NO: 1 or the residues 154-175 of SEQ ID. NO: 9; (b) an isolated peptide encoded by a polynucleotide that hybridizes under medium stringency conditions or high stringency conditions with a peptide coding sequence of SEQ ID NO: 1 or the complementary stand of said peptide coding sequence of SEQ ID NO: 1; (c) an isolated peptide encoded by a polynucleotide comprising a nucleotide sequence having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or 100% identity to the residues 289-310 of SEQ ID NO: 1; or (d) an isolated peptide comprising a motif with the following amino acid sequence: M1T2D3X4X5L6E7X8K9L10N11X12Y13V14X15X16D17X18E19Y20X21K22 (SEQ ID NO: 32) where X4, X5, X8, X12, X15, X16, X18, and X21 independently may be any amino acid, wherein the size of the peptide is less than 60 amino acids (aa).
The present invention also relates to polypeptides comprising the peptide and a lipase, wherein said lipase has a phospholipase activity below 50 PHLU/mg, below 45 PHLU/mg, below 40 PHLU/mg, below 35 PHLU/mg, below 30 PHLU/mg, blow 25 PHLU/mg, below 20 PHLU/mg, below 15 PHLU/mg, below 10 PHLU/mg, below 5 PHLU/mg or below 1 PHLU/mg, and/or shows no phospholipase activity in a plate assay.
The present invention also relates to polypeptides having phospholipase inhibitory activity, wherein a parent protein with at least three solvent accessible residues of an alpha-helix localized at the surface of said protein has been amended in the alpha-helix at at least one of the solvent accessible residues corresponding to position D3, L6, L10, Y13, V14, D17, and X21 and/or the edge residues corresponding to position E7, K9, N11, X18, and Y20 of the motif.
The present invention also relates to isolated polynucleotide's, nucleic acid constructs, recombinant expression vectors, recombinant host cells comprising the peptides or the polypeptides and methods of producing the isolated peptides or polypeptides having phospholipase inhibitory activity.
The present invention also relates to use of the peptides or the polypeptides for inhibiting the enzymatic activity of a lipase upon binding of the peptides or the polypeptides to said lipase.
The present invention also relates to lipases having a phospholipase activity below 50 PHLU/mg, below 45 PHLU/mg, below 40 PHLU/mg, below 35 PHLU/mg, below 30 PHLU/mg, blow 25 PHLU/mg, below 20 PHLU/mg, below 15 PHLU/mg, below 10 PHLU/mg, below 5 PHLU/mg or below 1 PHLU/mg, and/or shows no phospholipase activity in a plate assay which is capable of being inhibited by the peptide, wherein said lipase comprises at least one alteration which independently is an insertion, a deletion or a substitution, whereby the activity of said lipase is inhibited upon binding of at least one of (a) the isolated peptide having phospholipase inhibitory activity; or (b) the peptide having phospholipase inhibitory activity comprised in the polypeptide.



BRIEF DESCRIPTION OF THE FIGURES
FIG. 1 shows the sequence alignment of phospholipases to F. oxysporum 
FIG. 2 shows alpha-beta and all-alpha protein sequences
FIG. 3 shows the solvent accessibility of the residues from the F. oxysporum alpha-helix
FIG. 4 shows a crystal of GZEL
FIG. 5 shows a typical diffraction pattern of GZEL crystals
FIG. 6 shows a peptide induced change of the FoL PI
FIG. 7 shows Monellin variant 1, MON1 and Monellin variant 2, MON2 sequences
FIG. 8 shows the change in initial reaction rate for various peptides
FIG. 9 shows the change in % inhibition for various peptides and lipases



SEQUENCE LIST
SEQ ID No. 1: Fusarium oxysporum, FoL
SEQ ID No. 2: Fusarium graminearium 
SEQ ID No. 3: Nectria lipase 1
SEQ ID No. 4: Nectria lipase 2
SEQ ID No. 5: Fusarium heterosporum 
SEQ ID No. 6: Fusarium semitectum. 
SEQ ID No. 7: Fusarium solani LipC
SEQ ID No. 8: Fusarium solani LipD
SEQ ID No. 9: Thermomyces lanuginosus, TLL
SEQ ID No. 10: Fusarium venenatum PLA2, FVPLA2
SEQ ID No. 11: Plectasin
SEQ ID No. 12: Monellin
SEQ ID No. 13: Protegrin
SEQ ID No. 14: Barnase
SEQ ID No. 15: Cystatins
SEQ ID No. 16: Apolipoprotein E
Definitions
Phospholipase activity: The term “phospholipase activity” is defined herein as a phospholipolytic (EC number 3.1.1.4) activity that converts phospholipids into fatty acids and other lipophilic substances. For purposes of the present invention, phospholipase activity is determined according to the procedures described for PHLU and the plate assay described in the paragraph “Materials and Methods” below.
Phospholipase inhibitory activity: The term “phospholipase inhibitory activity” is defined herein as the activity that inhibits the phospholipase activity. The peptides of the present invention have at least 20%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, or 100% of the phospholipase inhibitory activity of the mature polypeptide of SEQ ID NO: 1.
Isolated peptide/polypeptide: The term “isolated peptide” or “isolated polypeptide” as used herein refers to a peptide or a polypeptide respectively that is isolated from a source. In certain aspects, the peptide/polypeptide is at least 1% pure, at least 5% pure, at least 10% pure, at least 20% pure, at least 40% pure, at least 60% pure, at least 80% pure, or at least 90% pure, as determined by SDS-PAGE or HPLC. Peptide purity is determined by HPLC.
Identity: The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “identity”. For purposes of the present invention, the degree of identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends in Genetics 16: 276-277), preferably version 3.0.0 or later. The optional parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of Needle labeled “longest identity” (obtained using the −nobrief option) is used as the percent identity and is calculated as follows: (Identical Residues×100)/(Length of Alignment−Total Number of Gaps in Alignment). For purposes of the present invention, the degree of identity between two deoxyribonucleotide sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), preferably version 3.0.0 or later. The optional parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EDNA-FULL (EMBOSS version of NCBI NUC4.4) substitution matrix. The output of Needle labeled “longest identity” (obtained using the −nobrief option) is used as the percent identity and is calculated as follows: (Identical Deoxyribonucleotides×100)/(Length of Alignment−Total Number of Gaps in Alignment).
Homologous sequence: The term “homologous sequence” is defined herein as a predicted protein that gives an E value (or expectancy score) of less than 0.001 in a tfasty search (Pearson, W. R., 1999, in Bioinformatics Methods and Protocols, S. Misener and S. A. Krawetz, ed., pp. 185-219). The degree of homology may be suitably determined by means of computer programs known in the art, such as GAP provided in the GCG program package (Program Manual for the Wisconsin Package, Version 8, August 1994, Genetics Computer Group, 575 Science Drive, Madison, Wis., USA 53711) (Needleman, S. B. and Wunsch, C. D., (1970), Journal of Molecular Biology, 48, 443-45). In the present invention, corresponding (or homologous) positions in the lipase sequences of Fusarium graminearium, Nectria lipase, Fusarium solani, Fusarium semitectum, Fusarium oxysporum, Fusarium heterosporum, and Thermomyces lanoginosus (synonym: Humicola lanuginose) are defined by the alignment shown in FIG. 1. To find the homologous positions in lipase sequences not shown in the alignment, the sequence of interest is aligned to the sequences shown in FIG. 1. The new sequence is aligned to the present alignment in FIG. 1 by using the GAP alignment to the most homologous sequence found by the GAP program. The following settings are used for polypeptide sequence comparison: GAP creation penalty of 3.0 and GAP extension penalty of 0.1.
Isolated polynucleotide: The term “isolated polynucleotide” as used herein refers to a polynucleotide that is isolated from a source. In certain aspects, the polynucleotide is at least 1% pure, at least 5% pure, at least 10% pure, at least 20% pure, at least 40% pure, at least 60% pure, at least 80% pure, or at least 90% pure, as determined by agarose electrophoresis.
Coding sequence: When used herein the term “coding sequence” means a nucleotide sequence, which directly specifies the amino acid sequence of its protein product. The boundaries of the coding sequence are generally determined by an open reading frame, which usually begins with the ATG start codon or alternative start codons such as GTG and TTG and ends with a stop codon such as TAA, TAG, and TGA. The coding sequence may be a DNA, cDNA, synthetic or recombinant nucleotide sequence.
Nucleic acid construct: The term “nucleic acid construct” as used herein refers to a nucleic acid molecule, either single- or double-stranded, which is isolated from a naturally occurring gene or which is modified to contain segments of nucleic acids in a manner that would not otherwise exist in nature or which is synthetic. The term nucleic acid construct is synonymous with the term “expression cassette” when the nucleic acid construct contains the control sequences required for expression of a coding sequence of the present invention.
Control sequences: The term “control sequences” is defined herein to include all components necessary for the expression of a polynucleotide encoding a polypeptide of the present invention. Each control sequence may be native or foreign to the nucleotide sequence encoding the polypeptide or native or foreign to each other. Such control sequences include, but are not limited to, a leader, polyadenylation sequence, pro-peptide sequence, promoter, signal peptide sequence, and transcription terminator. At a minimum, the control sequences include a promoter, and transcriptional and translational stop signals. The control sequences may be provided with linkers for the purpose of introducing specific restriction sites facilitating ligation of the control sequences with the coding region of the nucleotide sequence encoding a polypeptide.
Operably linked: The term “operably linked” denotes herein a configuration in which a control sequence is placed at an appropriate position relative to the coding sequence of the polynucleotide sequence such that the control sequence directs the expression of the coding sequence of a polypeptide.
Expression: The term “expression” includes any step involved in the production of the polypeptide including, but not limited to, transcription, post-transcriptional modification, translation, post-translational modification, and secretion.
Expression vector: The term “expression vector” is defined herein as a linear or circular DNA molecule that comprises a polynucleotide encoding a polypeptide of the present invention and is operably linked to additional nucleotides that provide for its expression.
Host cell: The term “host cell”, as used herein, includes any cell type that is susceptible to transformation, transfection, transduction, and the like with a nucleic acid construct or expression vector comprising a polynucleotide of the present invention.
Alteration: The term “alteration” means herein any chemical alteration of the polypeptide consisting of the mature polypeptide of SEQ ID NO: 1; or a homologous sequence thereof; as well as genetic manipulation of the DNA encoding such a polypeptide. The alteration can be a substitution, a deletion and/or an insertion of one or more (several) amino acids as well as replacements of one or more (several) amino acid side chains. In describing the amended amino acid sequences according to the invention, the following nomenclature is used for ease of reference: “Original amino acid:position:substituted amino acid(s)”. According to this nomenclature, for instance the substitution of glutamic acid (E) for glycine (G) in position 195 is shown as G195E. A deletion of glycine in the same position is shown as G195*, and insertion of an additional amino acid residue such as lysine (K) is shown as G195GK. Where a specific lipase contains a “deletion” in comparison with other lipases and an insertion is made in such a position this is indicated as *36D for insertion of an aspartic acid (D) in position 36. Multiple mutations are separated by pluses, i.e.: R170Y+G195E, representing mutations in positions 170 and 195 substituting tyrosine (Y) and glutamic acid (E) for arginine (R) and glycine (G), respectively. X231 indicates the amino acid in a parent polypeptide corresponding to position 231, when applying the described alignment procedure. X231R indicates that the amino acid is replaced with R. For SEQ ID NO: 2 X is T, and X231R thus indicates a substitution of T in position 231 with R. Where the amino acid in a position (e.g. 231) may be substituted by another amino acid selected from a group of amino acids, e.g. the group consisting of R and P and Y, this will be indicated by X231R/P/Y. In all cases, the accepted IUPAC single letter or triple letter amino acid abbreviation is employed.
Whether a given amino acid residue is on the surface of the enzyme may be determined according to W. Kabsch and C. Sander (1983). Biopolymers 22, pp. 2577-2637. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features, for example if its solvent accessible surface as calculated with the program DSSP is over 30 Å2.
DETAILED DESCRIPTION OF THE INVENTION
The inventors have found that a peptide, which may be isolated from the C-terminal of Fusarium oxysporum or Fusarium graminearium (Gibberella zeae) is able to bind to the lipase. They have furthermore shown that the peptide of Fusarium oxysporum has phospholipase inhibitory activity. It is thus suggested that a similar C-terminal peptide isolated from any suitable phospholipase such as e.g., Nectria lipase, Nectria haematococca (Fusarium eumartii), Fusarium solani, Fusarium culmorum, Fusarium semitectum and Fusarium heterosporum, may be used for inhibiting phospholipase activity.
In a first aspect, the invention relates to an isolated peptide having phospholipase inhibitory activity, selected from: (a) an isolated peptide comprising an amino acid sequence having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or 100% identity to the residues 289-310 of SEQ ID NO: 1 or the residues 154-175 of SEQ ID. NO: 9; (b) an isolated peptide encoded by a polynucleotide that hybridizes under medium stringency conditions or high stringency conditions with a peptide coding sequence of SEQ ID NO: 1 or the complementary stand of said peptide coding sequence of SEQ ID NO: 1; (c) an isolated peptide encoded by a polynucleotide comprising a nucleotide sequence having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or 100% identity to the residues 289-310 of SEQ ID NO: 1; or (d) an isolated peptide comprising a motif with the following amino acid sequence: M1T2D3X4X5L6E7X8K9L10N11X12Y13V14X15X16D17X18E19Y20X21K22 (SEQ ID NO: 32) where X4, X5, X8, X12, X15, X16, X18, and X21 independently may be any amino acid, wherein the size of the peptide is less than 60 amino acids (aa).
In another aspect, the invention relates to the peptide which has a length of less than 55 aa, less than 50 aa, less than 45 aa, less than 40 aa, less than 35 aa, or less than 30 aa.
In another aspect, the invention relates to the peptide which has a length of at least 15 aa, at least 20 aa, or at least 25 aa.
In another aspect, the invention relates to the peptide wherein said peptide has a secondary structure of an alpha-helix.
In another aspect, the invention relates to the peptide wherein the amino acid at each of the positions X4, X5, X8, X12, X15, X16, X18, and X21 present in the motif independently are selected whereby X4 is A or E; X5 is E or Q; X8 is K or A; X12 is S or N; X15 is E, Q or A; X16 is L or M; X18 is K or Q; and X21 is I or V.
The peptide of Fusarium oxysporum lipase (FoL) may be altered to improve or reduce the capacity of said peptide of inhibiting the lipase. Examples of such alterations are shown in Table 1.







TABLE 1







Alterations in the peptide having phospholipase inhibitory activity


derived from Fusarium oxysporum lipase corresponding to


residues 289-310 of SEQ ID NO: 1 to obtain an improved or


reduced inhibition of the wild type lipase by the changed peptide.











Original amino acid
Improved inhibition
Reduced inhibition






D291
D291E




L294

L294A



E295
E295T, S




K297
K297R




L298

L298A



N299
N299D, E




Y301
Y301W




D305

D305A



K306
K306R




Y308
Y308E, D




V309
V309I, N, Q









In another aspect, the invention relates to the peptide which compared to SEQ ID NO: 1 comprises at least one amino acid substitution at a position corresponding to FoL residues D291; L294; E295; K297; L298; N299; Y301; D305; K306; Y308; or V309.
In another aspect, the invention relates to the peptide which compared to SEQ ID NO: 1 comprises at least one amino acid substitution corresponding to FoL residues D291E; L294A; E295T,S; K297R; L298A; N299D,E; Y301W; D305A; K306R; Y308E,D; or V309I,N,Q.
It is contemplated that alterations in the peptide in some cases may result in a change and in other cases may result in no change in the binding between peptide and lipase. A change may lead to improved or reduced binding which accordingly may result in improved or reduced inhibition of the lipase by the peptide.
The interaction between the peptide and the lipase may in addition to the alterations in the peptide also be influenced by changes in the lipase. Such alterations may contribute to an improved inhibition or a reduced inhibition. Examples of alterations in the amino acid sequence of the Fusarium oxysporum lipase is shown in Table 2.







TABLE 2







Alterations in the Fusarium oxysporum lipase corresponding to


residues 1-316 of SEQ ID NO: 1 to obtain an improved or reduced


inhibition of the changed lipase by the wild type peptide.











Original amino acid
Improved inhibition
Reduced inhibition






L92
L92D, E
L92W



R96

R96E, D, A



L203

L203W, K, M



I207
I207D, E




R211

R211H



L243

L243W, K



L250
L250D, E
L250R



L252
L252S, T









In another aspect, the invention relates to an isolated polynucleotide encoding the peptide.
In another aspect, the invention relates to a nucleic acid construct comprising the polynucleotide operationally linked to at least one control sequence that directs the production of the peptide in an expression host.
In another aspect, the invention relates to a recombinant expression vector comprising the nucleic acid construct.
In another aspect, the invention relates to a recombinant host cell comprising the nucleic acid construct or the recombinant expression vector.
In another aspect, the invention relates to a method of preparing the isolated peptide comprising the steps: (a) cultivating a host cell comprising the nucleic acid construct comprising the polynucleotide encoding at least one copy of the peptide under conditions conductive for production of the peptide; and (b) recovering the peptide.
Alternatively the peptides of the invention may be prepared by in vitro synthesis, using conventional methods as known in the art. Various commercial synthetic apparatuses are available, for example automated synthesizers by Applied Biosystems Inc., Beckman, etc. By using synthesizers, naturally occurring amino acids may be substituted with unnatural amino acids, particularly D-isomers (or D-forms) e.g. D-alanine and D-isoleucine, diastereoisomers, side chains having different lengths or functionalities, and the like. The particular sequence and the manner of preparation will be determined by convenience, economics, purity required, and the like.
The peptides may also be isolated and purified in accordance with conventional methods of recombinant synthesis. A lysate may be prepared of the expression host and the lysate purified using HPLC, exclusion chromatography, gel electrophoresis, affinity chromatography, or other purification technique. For the most part, the compositions which are used will comprise at least 20% by weight of the desired product, more usually at least about 75% by weight, preferably at least about 95% by weight, and for therapeutic purposes, usually at least about 99.5% by weight, in relation to contaminants related to the method of preparation of the product and its purification. Usually, the percentages will be based upon total protein.
In another aspect, the invention relates to use of the peptide for inhibiting the enzymatic activity of a lipase upon binding of the peptide to said lipase.
Some lipases which are not classified as phospholipases and it is desirable to derive a variant with phospholipase activity from a parent lipolytic enzyme having no or very little phospholipase activity, e.g. corresponding to a ratio of phospholipase activity to lipase activity below or below 50 PHLU/mg, below 45 PHLU/mg, below 40 PHLU/mg, below 35 PHLU/mg, below 30 PHLU/mg, blow 25 PHLU/mg, below 20 PHLU/mg, below 15 PHLU/mg, below 10 PHLU/mg, below 5 PHLU/mg or below 1 PHLU/mg, and/or shows no phospholipase activity in a plate assay.
In a further aspect, the invention relates to a polypeptide comprising the peptide and a lipase, wherein said lipase has a phospholipase activity below 50 PHLU/mg, below 45 PHLU/mg, below 40 PHLU/mg, below 35 PHLU/mg, below 30 PHLU/mg, blow 25 PHLU/mg, below 20 PHLU/mg, below 15 PHLU/mg, below 10 PHLU/mg, below 5 PHLU/mg or below 1 PHLU/mg, and/or shows no phospholipase activity in a plate assay.
In another aspect, the invention relates to the polypeptide comprising a lipase which is at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or 100% identical to Thermomyces lanuginosus (SEQ ID NO: 9).
Lipases which do not naturally comprise a peptide having inhibitory activity may be altered for the purpose of obtaining lipase variants that are inhibited by the isolated peptide of the invention. These lipase variants may be inhibited by either of (a) the isolated peptide, (b) the peptide which is attached to such lipase variants or (c) a polypeptide comprising peptides having inhibitory activity. The binding interaction between the peptide and the lipase variants may be further modified by amending the amino acid sequence of the peptide.
Thermomyces lanuginosus lipase (TLL) has essentially no phospholipase activity and there is currently no information indicating that this lipase comprises any C- or N-terminal peptides to control and/or inhibit its activity. This lipase has a structure that makes it suitable for introducing amino acid alterations that will render TLL susceptible for binding of the Fusarium oxysporum lipase (FoL) peptide and thereby inhibiting its lipolytic activity. Examples of such alterations are disclosed in Table 3 (A). The interaction of TLL and isolated peptides of the invention may further be optimized by introduction of alterations in the peptide. Examples of alterations in the C-terminal peptide of the FoL are shown in Table 3 (B).







TABLE 3







(A) Alterations in the Thermomyces lanuginosus lipase (TLL)


corresponding to residues 1-269 of SEQ ID NO: 9 to generate a


lipase that is inhibited by the wild type FoL peptide, and (B)


Alterations in the peptide having phospholipase inhibitory activity


derived from Fusarium oxysporum lipase (FoL) corresponding


to residues 288-317 of SEQ ID NO: 1 to obtain an improved


inhibition of TLL.











(B)



(A)
Alterations in the



Alterations in TLL
FoL peptide






E87R
L294V



I90L
Q303N, T



G91T
M304A, S, G



I202P
K306A



R209L




E210I




T244L




Substitution of the TLL residues 248-255




(NQPNIP-DI) (SEQ ID NO: 19) with the 




FoL residues 246-254 (NGGTLGLDI)




(SEQ ID NO: 20)




Substitution of the TLL residues 248-253




(NQPNIP) (SEQ ID NO: 21)




with the FoL residues 247-252




(GGTLGL) (SEQ ID NO: 22)









It is contemplated that where TLL residues is substituted with FoL residues all the residues may be substituted, or alternatively at least one residue selected from the TLL sequence may be substituted with the corresponding residue selected from the FoL sequence according to the following alignments:













Alignment A
Alignment B








N Q P N I P - D I—
N Q P N I P



(SEQ ID NO: 19)




N G G T L G L D I
G G T L G L



(SEQ ID NO: 20)









In another aspect, the invention relates to the polypeptide wherein the lipase comprises at least one alteration which independently is an insertion, a deletion or a substitution.
In another aspect, the invention relates to the polypeptide wherein the at least one alteration of the lipase comprises one or more amino acid substitutions corresponding to the residues E87R, I90L, G91T, I202P, R209L, E210I, or T244L of Thermomyces lanuginosus (SEQ ID NO: 9).
In another aspect, the invention relates to the polypeptide wherein the lipase comprises a substitution of the residues corresponding to 248-255 of Thermomyces lanuginosus (SEQ ID NO: 9) with the residues 246-254 of Fusarium oxysporum (SEQ ID NO: 1), or 248-253 of Thermomyces lanuginosus (SEQ ID NO: 9) with the residues 247-252 of Fusarium oxysporum (SEQ ID NO: 1).
In a further aspect, the invention relates to a polypeptide having phospholipase inhibitory activity, wherein a protein with at least three solvent accessible residues of an alpha-helix localized at the surface of said protein has been amended in the alpha-helix at at least one of the solvent accessible residues corresponding to position D3, L6, L10, Y13, V14, D17, and X21 and/or the edge residues corresponding to position E7, K9, N11, X18, and Y20 of the motif of the invention as described.
In another aspect, the invention relates to the polypeptide wherein the protein has an amino acid sequence which is at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or 100% identical to the Plectasin (SEQ ID NO: 11); Monellin (SEQ ID NO: 12); Protegrin (SEQ ID NO: 13); Barnase (SEQ ID NO: 14); Cytostatins (SEQ ID NO: 15); or Apolipoprotein E (SEQ ID NO: 16).
Proteins suitable for generating a polypeptide having phospholipase inhibitory activity must comprise at least one alpha-helix which is exposed to the surface of the protein. It is necessary that the some of the amino acids comprised in the alpha helix are solvent accessible to be able to bind to a lipase and exert its inhibitory effect. The size of the alpha helix may be 22 amino acids or 20, 18, 16, 14, 12, or 10 amino acids. In addition to the at least one alpha-helix other secondary structure elements such as e.g. beta-strands may be present. Based on their secondary structures three main groups of proteins may be defined: an All-alpha group, an all beta-group and an Alpha-beta group. FIG. 2 shows examples of proteins belonging to the Alpha-beta group such as e.g. plectasin, monellin, protegrin, barnase, and cystatins and examples of proteins belonging to the All-alpha group such as apolipoprotein E. The amino acid sequence are shown in the second line and the first line refers to the secondary structure as calculated by the programme Dictionary of Secondary Structure Prediction (DSSP) where a/A indicate alpha-helices and b/B indicate beta-strands.
The alpha-helix of the phospholipase inhibitory peptide may be superimposed and aligned with the alpha-helix of the selected protein (underlined) in a two-step procedure as illustrated below for monellin:
Select the direction, either parallel or anti-parallel of the sequences to be aligned,




Once the direction is selected there are several possibilities of aligning the sequences of the alpha-helices. The most optimal alignment is the one comprising the maximum length in common and the minimum number of troubles (clashes).




After identifying the most optimal alignment, modifications in the protein alpha-helix may be made to change the amino acid residues to the alpha-helix of the phospholipase inhibitory peptide. An example is shown in FIG. 3 wherein the peptide of Fol is drawn to illustrate which part of the alpha-helix and which amino acid residues are facing the enzyme and which is facing the solvent. In particular, residues that are facing the surface of the scaffold protein and are solvent accessible and accordingly may be involved in the contact and in the inhibition of a lipase must be considered. These residues are corresponding to position D3, L6, L10, Y13, V14, D17, and X21 of the motif: M1T2D3X4X5L6E7X8K9L10N11X12Y13V14X15 X16D17X18E19Y20X21K22. Optionally, residues that are found at the edge of the surface of the protein and are potentially solvent accessible and accordingly may be involved in the contact and in the inhibition of a lipase should also be considered. These residues are corresponding to position E7, K9, N11, X18, and Y20 of the motif.
Finally, parts outside the alpha-helix in the protein are analyzed to identify if there are other and/or new clashes that may affect binding of the alpha-helix of the scaffold protein to the lipase or affect the accommodation of the alpha-helix within the protein. Such residues are then optionally changed to maximize the phospholipase inhibitory effect. These are the mutations outside the helix.
In another aspect, the invention relates to a method of preparing the polypeptide of the invention comprising a step of attaching the peptide to a lipase, wherein said lipase has a phospholipase activity below 50 PHLU/mg, below 45 PHLU/mg, below 40 PHLU/mg, below 35 PHLU/mg, below 30 PHLU/mg, blow 25 PHLU/mg, below 20 PHLU/mg, below 15 PHLU/mg, below 10 PHLU/mg, below 5 PHLU/mg or below 1 PHLU/mg, and/or shows no phospholipase activity in a plate assay.
In another aspect, the invention relates to a method of preparing a polypeptide comprising the steps: (a) selecting a protein having an alpha-helix localized at the surface of the protein whereby at least three, at least four, at least five, or at least six residues of said alpha-helix is solvent accessible; (b) aligning the alpha-helix of the protein with the peptide; (c) identifying the residues in the alpha-helix of the protein that are solvent accessible corresponding to position D3, L6, L10, Y13, V14, D17, and X21 of the motif; (d) altering at least one, at least two, at least three, at least four, at least five, at least six or at least seven of the amino acids in the protein identified in step (c); (e) testing the polypeptide for phospholipase inhibitory activity; (f) selecting the polypeptide having phospholipase inhibitory activity; and (g) producing the polypeptide selected in (f).
In another aspect, the invention relates to the method further identifying in step (c) the residues in the alpha-helix of the protein that are potentially solvent accessible corresponding to position E7, K9, N11, X18, and Y20 of the motif.
In another aspect, the invention relates to the method further comprising a step of making at least one alteration at one or more positions in the protein.
In another aspect, the invention relates to use of the polypeptide, for inhibiting the enzymatic activity of a lipase upon binding of the peptide comprised in the polypeptide to said lipase.
In a further aspect, the invention relates to a lipase having a phospholipase activity below 50 PHLU/mg, below 45 PHLU/mg, below 40 PHLU/mg, below 35 PHLU/mg, below 30 PHLU/mg, blow 25 PHLU/mg, below 20 PHLU/mg, below 15 PHLU/mg, below 10 PHLU/mg, below 5 PHLU/mg or below 1 PHLU/mg, and/or shows no phospholipase activity in a plate assay which is capable of being inhibited by the peptide, wherein said lipase comprises at least one alteration which independently is an insertion, a deletion or a substitution, whereby the activity of said lipase is inhibited upon binding of at least one of (a) the isolated peptide having phospholipase inhibitory activity; or (b) the peptide having phospholipase inhibitory activity comprised in the polypeptide.
In another aspect, the invention relates to the lipase wherein said lipase is at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 97%, or 100% identical to Thermomyces lanuginosus (SEQ ID. NO: 9).
In another aspect, the invention relates to the lipase wherein the at least one alteration is a substitution corresponding to the residues L92; R96; L203; I207; R211; L243; L250; or L252 of Thermomyces lanuginosus (SEQ ID NO: 9).
In another aspect, the invention relates to the lipase wherein the at least one alteration is a substitution corresponding to the residues L92D,E,W; R96E,D,A; L203W,K,M; I207D,E; R211 H; L243W,K L250D,E,R; and L252S,T of Thermomyces lanuginosus (SEQ ID NO: 9).
Materials and Methods
Phospholipase Activity (PHLU)
Phospholipase activity (PHLU) is measured as the release of free fatty acids from lecithin. 50 μl 4% L-alpha-phosphatidylcholine (plant lecithin from Avanti), 5 mM CaCl2 in 50 mM HEPES, pH 7 is added 50 μl enzyme solution diluted to an appropriate concentration in 50 mM HEPES, pH 7. The samples are incubated for 10 min at 30° C. and the reaction stopped at 95° C. for 5 min prior to centrifugation (5 min at 7000 rpm). Free fatty acids are determined using the NEFA C kit from Wako Chemicals GmbH; 25 μl reaction mixture is added 250 μl Reagent A and incubated 10 min at 37° C. Then 500 μl Reagent B is added and the sample is incubated again, 10 min at 37° C. The absorption at 550 nm is measured using an HP 8452A diode array spectrophotometer. Samples are run in at least in duplicates. Substrate and enzyme blinds (preheated enzyme samples (10 min at 95° C.)+substrate) are included. Oleic acid is used as a fatty acid standard. 1 PHLU equals the amount of enzyme capable of releasing 1 μmol of free fatty acid/min at these conditions. Specific phospholipase activity (PHLU/mg) is calculated at the phospholipase activity (PHLU) per amount protein (mg).
Plate assay: 50 ml 2% agarose is dissolved by heating in purified water for 5 minutes and subsequently cooled to 60-63° C. 50 ml 2% plant L-alpha-Phosphatidylcholine 95% in 0.2M NaOAc, 10 mM CaCl2, pH 5.5 at 60° C. in 30 min. is blended for 15 sec. with ultrathorax. Equal volumes of 2% agarose and 2% Lecithin are mixed. 250 μl 4 mg/ml crystal violet in purified water is added as indicator. The mixture is poured into appropriate petri dishes (e.g. 30 ml in 14 cm Ø dish), and appropriate holes (3-5 mm) are made in the agar for application of enzyme solution. The enzyme sample is diluted to a concentration corresponding to OD280=0.5 and 10 microliter and applied into holes in the agarose/lecithin-matrix. Plates are incubated at 30° C. and reaction zones in the plates are identified after approximately 4-5 hours and/or after approximately 20 hours incubation. The Humicola lanuginosa lipase is used as a control, and the presence of a larger clearing zone than the control is taken as a positive result for phospholipase activity.
EXAMPLES
The present invention is further described by the following examples that should not be construed as limiting the scope of the invention.
Example 1
GZEL Crystal Structure
Protein expression and purification: The Gibberella zeae/Fusarium graminearum lipase (GZEL) gene was amplified by PCR and further confirmed by sequencing. Then the GZEL gene was expressed in yeast with a significant protein band shown on SDS-PAGE after Comassie staining. And the activity was detected against the olive oil/Bright Green plate at pH 7. The positive candidate clones showed dark green zones around the holes.
The culture supernatant separated from cells by centrifugation and the pH of supernatant was adjusted to pH 7.0. The supernatant was then filtrated and applied into Ni-Sepharose FF equilibrated with 25 mM Tris-HCl at pH 7.0 with 0.3 M NaCl. The target protein was eluted by imidazole at a gradient from 0M to 1M. Fractions from the column were analyzed for activity. Fractions with enzyme activity were pooled and concentrated. Then the samples were loaded into a gel filtration column Superdex 75 equilibrated by 25 mM Tris-HCl at pH 8.0 with 0.15 M NaCl. The eluted active lipase was concentrated and dialyzed with 25 mM Tris-HCl at pH 8.0. The lipase was checked by SDS-PAGE and the pure fractions were prepared for crystallization trails.
Crystallization: The freshly prepared protein was concentrated to 10 mg/ml and crystallized by the hanging drop vapor diffusion method at 291K. The initial crystallization conditions were screened using several Crystal Screen Kits (Hampton Research screen kit 1 and 2, Index screen kit, MembFac screen kit). One microliter of protein solution was mixed with 1 microliter of reservoir solution and equilibrated against 200 microliter of reservoir solution. Small crystals could be found in many different conditions within three days. Many of the crystals are hollow sticks and have poor diffraction quality. Fine shaped and good quality crystals were selected from the condition with 0.2 M Ammonium Sulfate, 0.1 M Bis-Tris (pH 5.5), 25% w/v PEG3350 within 2-4 days (see FIG. 3), which can reach their final volumes of about 50*50*200 micrometer with the space group P212121.
Data collection and processing: A 2.8 Å resolution set of diffraction data sets were collected at 100K from a single GZEL derivative crystal using an in-house Rigaku MM-007 generator and a Mar345dtb detector. The beam was focused by osmic mirrors. For a more detailed analysis, flash-cooled crystals were used. Crystals were immersed in cryoprotectant for 5-10 sec., picked up with a loop and flash-cooled in a stream of nitrogen gas cooled to 100K. The cryoprotectant was prepared by adding 25% glycerol to the mother liquor reservoir. The crystal form belongs to space group P212121 (a=78.4, b=91.0, c=195.8, α=β=γ=90°) with four GZEL molecules per asymmetric unit and a VM of 2.6 Å3 Da-1 (Matthews 1968), corresponding to a solvent content of 48%. Processing of diffraction images and scaling of the integrated intensities were performed using the HKL2000 software package (Otwinowski et al. 1997).
Results: Initially, although we have obtained dozens of GZEL crystals in many conditions of the screening kits, they are unsuitable for X-ray diffraction. Many of the crystals are hollow fibre. Therefore, further crystallization optimization was performed and better crystals were obtained in the following condition: 0.2 M Ammonium Sulfate, 0.1 M Bis-Tris, pH 5.5, 25% w/v PEG3350. Drops containing 2 μl protein solution and 2 μl of reservoir solution were equilibrated against 200 microliter of reservoir solution. Crystals grown from the optimized reservoir solution (0.2 M Ammonium Sulfate, 0.1 M Bis-Tris, pH 5.5, 25% w/v PEG3350) were more suitable for X-ray diffraction and diffracted to 2.8 Å. A set of data was subsequently collected from one single crystal (see FIG. 4 showing a typical diffraction pattern of GZEL crystals. The exposure time was 300 seconds, detector distance was 150 millimeter and oscillation range per frame was 10). There are four molecules per asymmetric unit. Complete datacollection statistics are given in Table 4. The structure of GZEL has been determined and is disclosed in appendix 1.
References: Matthews, B. W., Solvent content of protein crystals. J. Mol. Biol., 1968. 33: p. 491-497. Otwinowski, Z. and W. Minor, Processing of X-ray diffraction data collected in oscillation mode, in Macromolecular Crystallography, part A, C. W. Carter Jr. and R. M. Sweet, Editors. 1997, Academic Press. p. 307-326.







TABLE 4





Data collection and processing statistics. Rmerge = 100Σ|Ii − <I>|/ΣIi,


where Ii is the intensity of the observation.


















Space group
P212121,



Unit-cell parameters
a = 78.4 Å, b = 91.0 Å, c = 195.8 Å,




α = β = γ = 90°.



Resolution range (Å)
50.0-2.8 (2.9-2.8)a 



Total reflections
326163



Unique reflections
 34080



Average I/σ (I)
9.6 (8.0)a



Rmerge (%)
10.1 (48.0)a



Data completeness(%)
97.7 (92.3)a









Example 2
Peptide Binding to GZEL
There are four GZEL-peptide complexes in the asymmetric unit of the crystal structure. The four complexes were refined independently from each other. They constitute four different entities. In this four different complexes the peptide sits in exactly the same way with respect to the lipase core domain, see Table 5 below. This provides another set of evidence for a specific binding of the peptide to the lipase core.







TABLE 5







GZEL-peptide C_alpha root mean square deviation upon


optimal superimposion. An in-house program designed superimpose


optimally two sets of protein atomic coordinates was used on each


of the four GZEL-peptide pairs. The entries on the table show the


residual (root mean square deviation) of the C_alpha


atoms upon superimposion in Angstroms.












A
B
C
D
















A
0.00
0.44
0.52
0.51



B
0.44
0.00
0.49
0.47



C
0.52
0.49
0.00
0.48



D
0.51
0.47
0.48
0.00









Example 3
Preparation of FoL Devoid of Peptide for Binding Experiments
FoL was purified from a Pilot fermentation LVF 57 UF concentrate PPW6523. PPW6523 was 0.22 μm filtered and loaded onto a butyl-sepharose fast flow column, washed with 1.8M NH4acetate and eluted with MilliQ H2O. Datasheet on purified FoL: 2003-04317-01. On an isoelectric focusing gel IEF pH 3-10 (Novex precast) 20070628 the sample gave a single band. N-terminal sequencing of the band showed only one sequence—the expected FoL N-terminus showing that C-terminal peptide was not bound.
Example 4
Inhibition Assay
The substrate used for these experiments was para-nitropenyl (p-NP) butyrate purchased from Sigma Aldrich. A substrate stock solution was prepared by adding 18 μL of p-NP Butyrate to 1 ml of 2-propanol giving a 100 mM stock solution. The working solution was prepared by diluting 10 μL stock solution in final volume of 1 ml 50 mM Tris pH 7 buffer. 45 μL of the FoL 1 mg/ml in 50 mM Tris buffer pH 7 was preincubated with two concentrations of the peptide and control was carried out in absence of peptide using the same buffer. After pre-incubation for 5 minutes at room temperature the enzyme solution was diluted in 50 mM Tris pH 7 buffer and 100 μL diluted enzyme solution was mixed with the 100 μL substrate solution and reaction was followed in microtiter plate spectrophotometer under constant shaking at room temperature. Table 6 below shows the color development over time monitored at A405 (every 30 sec. for 10 minutes) of p-nitrophenol, one of the degradation products of p-NP butyrate, liberated by the enzyme which was preincubated with the peptide in two different concentrations and a control which was treated exactly the same way in the absence of peptide.







TABLE 6







Data for the activity of FoL enzyme with and without peptide. The


activity of FoL demonstrated that addition of the peptide caused


an inhibition of the activity, determined as a reduced color


development. FoL with peptide gave the lowest color


development, whereas FoL with 5x diluted peptide had a higher


color development, whereas the control sample, FoL with water,


had the highest color development.










Time
45 μL FoL +
45 μL FoL +
45 μL FoL +


(seconds)
5 μL peptide
5 μL 5x diluted peptide
5 μL MilliQ water













0
0.03
0.05
0.06


30
0.18
0.12
0.19


60
0.22
0.23
0.28


90
0.29
0.32
0.38


120
0.38
0.42
0.49


150
0.45
0.52
0.59


180
0.54
0.60
0.70


210
0.62
0.69
0.81


240
0.70
0.79
0.91


270
0.77
0.88
1.00


300
0.83
0.96
1.08


330
0.89
1.03
1.15


360
0.95
1.09
1.21


390
1.00
1.15
1.27


420
1.06
1.22
1.33


450
1.10
1.26
1.37


480
1.15
1.31
1.41


510
1.19
1.36
1.45


540
1.23
1.40
1.49


570
1.27
1.43
1.52


600
1.30
1.47
1.55









Example 5
Isoelectric Point Measurements
The samples prepared in Example 4 were loaded to a Nowex gel IEF 3-10. Lane 1: Marker. Lane 2: Sample 1 (10 μL). Lane 3: Sample 1 (20 μL). Lane 4: Sample 2 (10 μL). Lane 5: Sample 2 (20 μL). Lane 6: Sample 3 (10 μL). Lane 7: Sample 3 (20 μL). A photo of the gel is shown in FIG. 6. The gel revealed that addition of the peptide caused a change in pl due to bands (lane 6 and 7) which had a lower pl than samples with peptide (lane 2-5). This is a clear indication of binding of the peptide to the enzyme.
Example 6
Activity of TLL and FoL in a Lecithin Plate Assay
A lecithin plate without Triton-X 100 was prepared as described in the Materials and Methods. The same amounts based on ODA280 of purified TLL and FoL was added to the holes: TLL to the two top holes, FoL to the two bottom holes; left holes (lower concentration, ODA280 equal to 0.2); right holes (higher concentration, ODA280 equal to 0.5). After 20 hours of incubation FoL exhibited a 7/10 mm clearing zone at the lower/higher concentration. TLL did not show a clearing zone.







TABLE 7







Lecithin plate assay. Clearing zone diameter after 20 hours incubation


measured in mm (milimeters). The enzymes were dosed equally


based on ODA280.









ODA280
TLL
FoL





0.2
0 mm
 7 mm


0.5
0 mm
10 mm









Example 7
How to Modify the Alpha-Helix in Monellin to Generate a Polypeptide Having Phospholipase Inhibitory Activity
The recently solved structure of the Fusarium graminearum, also known as Gibberella zeae, phospholipase has shown that the C-terminal peptide normally cleaved for maturation of the enzyme was present in the structure. This peptide adopts an alpha-helical structure and packs against the catalytic domain of the phospholipase. The peptide has been shown to inhibit the phospholipase activity against small esters.
Monellin is a sugar tasting protein from the African serendipity berry. The structure of Monellin consists of a long partially exposed alpha-helix packed perpendicularly against a 5-stranded beta-sheet. The presence of the solvent accessible alpha-helix makes the protein well suited for the purpose of modifying the alpha-helix in the attempt of transferring the inhibitory properties of the C-terminal peptide of the Fusarium oxysporum lipase (FoL), which is a very close homologue of Fusarium graminearum lipase (FGL). Two different Monellin variants were designed as FoL inhibitors.
Variant summary: Two variants were found after analyzing all the possible ways of superimposing the C-terminal peptide alpha-helix of FoL onto the alpha-helix of Monellin. In selection of the variants the visual inspection focused on; a) maximizing the alignment of the alpha-helix of Monellin with the C-terminal peptide residues that interact with the catalytic domain of the lipase; and b) minimizing the conflicts of other parts of Monellin with the catalytic domain. Two different possibilities of superimposing the helices either matching the N to C-terminal direction (parallel) or inverting it (anti-parallel) were identified.
Sequence/structure: The sequence of Monellin used on this study is shown in FIG. 2 (second line) together with the secondary structure (first line) as calculated by the program Dictionary of Secondary Structure Prediction (DSSP) published by W. Kabsch and C. Sander, Biopolymers (1983) 22:2577-2637. The b/B refer to beta-strands, the a/A refer to alpha-helices. The RCSB PDB file used for the superpositions was 1IV7.
Variants: Two Monellin variants were the result of this study. They are described in what follows.
MON1 variant: When the superposition where of the lipase peptide alpha-helix is aligned parallel to the Monellin alpha-helix the amino acid substitutions F11E+Q13K+N14L+L15V+K17Y+F18V+N24Y+K25V+I74A+E77R+R82G+R83G are to be made. These substitutions will mimic the interaction of the peptide with the lipase catalytic domain and eliminate possible conflicts of the remaining parts of the molecules. The complete sequence of MON1 is shown in FIG. 6 where the substituted amino acids are boldfaced in red. It may be necessary to change P10 into a leucine (P10L) but it is foreseen that this change will be detrimental to the overall stability of Monellin.
MON2 variant: When the superposition of the lipase peptide alpha-helix is aligned anti-parallel to the Monellin alpha-helix the amino acid substitutions F11Y+Q13N+N14L+K17A+F18L+K25H+F34V+R81G+R84G are to be made. These substitutions will mimic the interaction of the lipase peptide with the lipase catalytic domain and eliminate possible conflicts of the remaining parts of the molecule. The complete sequence of MON2 is shown in FIG. 7 where the substituted amino-acids are boldfaced in red.
Example 8
Inhibitory Effect of Various Peptides on FoL Wildtype and FoL Variant I207E
Enzyme assay: The substrate used for these experiments was para-nitropenyl (p-NP) butyrate (N9876 Sigma Aldrich). A substrate stock solution was prepared by adding 18 μL of p-NP butyrate to 1 ml of 2-propanol giving a 100 mM stock solution. The working solution was prepared by diluting 500 μL stock solution in final volume of 50 mL 500 mM phosphate pH 7, 0.4% triton X-100. 40 μL of the enzyme 38 ng/mL in 500 mM phosphate pH 7, 0.4% triton X-100, was pre-incubated with 20 μL of peptide having various concentrations giving peptide/lipase ratios from 0.5 to 1000 increasing with a factor of 2 through 12 steps. An enzyme substrate blank containing 60 μL was included. After pre-incubation in minimum 15 minutes, 100 μL of substrate was added and the reaction was followed in microtiter plate spectrophotometer (SPECTRAmax PLUS 384 from Molecular Devices) after an initial shaking (5 sec.) at room temperature. Colour development over time was monitored at A405 (every 20 sec. for 30 minutes), measuring p-nitrophenol, one of the degradation products of p-NP butyrate, liberated by the hydrolysis.
Initial reaction rates (determined as the linear initial slope of A405 plotted against time) were plotted against the logarithm to the inhibitor/lipase ratio. From the following model IC50 values were determined:




  
    v
    0
  
  =
  
    
      v
      max
    
    ❘
    
      
        v
        min
      
      
        1
        +
        
          10
          
            
              
                [
                peptide
                ]
              
              
                [
                enzyme
                ]
              
            
            -
            
              IC
              50
            
          
        
      
    
  




v0 is the initial reaction rate, vmax is the maximum rate, vmin is the minimum reaction rate and IC50 is the half maximal inhibitory concentration. GraphPad Prism (v.5.00, Mar. 12, 2007) from GraphPad Software, Inc. was used for regression.
% Inhibition is the percentage reduction in initial reaction rate where 0% inhibition is defined as the initial reaction rate without peptide.







TABLE 8







Peptide sequences tested. Synthetic peptides HPLC


purified (>85% purity) were obtained from TAG


Copenhagen A/S.











Name
Design
Sequence






P0
Wildtype
ATMTDAELEKKLNSYVQMDKEYVKNNQARS





(SEQ ID NO: 23)


 



P1
D291E
ATMTEAELEKKLNSYVQMDKEYVKNNQARS





(SEQ ID NO: 24)


 



P2
E295T
ATMTDAELTKKLNSYVQMDKEYVKNNQARS





(SEQ ID NO: 25)


 



P3
K297R
ATMTDAELEKRLNSYVQMDKEYVKNNQARS





(SEQ ID NO: 26)


 



P4
Y308E
ATMTDAELEKKLNSYVQMDKEEVKNNQARS





(SEQ ID NO: 27)


 



 P1′
D305A
ATMTDAELEKKLNSYVQMAKEYVKNNQARS





(SEQ ID NO: 28)
















TABLE 9







The determined IC50 values













Name
P0
P1
P2
P3
P4
P1′





FOL
913
Very low
Very low
1561
No
No


wt
 (555-1501)
inhibition*
inhibition*
 (644-3782)
inhibition
inhibition


FOL I207E
 2871
1009
782
 301
Very low
No


variant
 (208-397)2
(440-2314)
(505-1210)
(214-403)
inhibition*
inhibition





1IC50 value (half maximal inhibitory concentration).


295% Confidence interval.


*IC50 > highest peptide excess tested






Results: FIG. 8 shows how the initial reaction rates are altered by various peptide concentrations (A & B). Assuming 0% inhibition for the lowest concentration of peptide it is clear from (C) when plotting the curves for P0 that the FoL variant: I207E was better at binding the peptide than the wildtype enzyme.
Example 9
Inhibitory Effect of Various Peptides on TLL Wildtype and TLL Variants
Enzyme assay: As described above. Peptides P11 and P13 were tested in concentrations giving peptide/lipase ratios from 5 to 5000 increasing with a factor of 2 through 10 steps. Peptide P12 was tested in concentrations giving peptide/lipase ratios from 6 to 6000 increasing with a factor of 2 through 10 steps.







TABLE 10







Peptide sequences tested











Name
Design
Sequence






P11
L294V
ATMTDAEVEKKLNSYVQMDKEYVKNNQARS





(SEQ ID NO: 29)


 



P12
Q303N
ATMTDAELEKKLNSYVNMDKEYVKNNQARS





(SEQ ID NO: 30)


 



P13
K306A
ATMTDAELEKKLNSYVQMDAEYVKNNQARS





(SEQ ID NO: 31)
















TABLE 11







IC50 values for TLL variant N248G/Q249G/


P250T/N251L/I252G/P253L










TLL variant
P11
P12
P13





N248G/Q249G/P250T/N251L/
Very low
16881
1716


I252G/P253L
inhibition*
(496-5745)2
(1403-2098)





1IC50 value (half maximal inhibitory concentration).


295% Confidence interval.


*IC50 > highest peptide excess tested






Results: FIG. 9 shows how the % inhibition is altered by various peptide concentrations (peptide blank is 0% inhibition).







APPENDIX 1





Coordinates in Protein Data Bank (PDB) format of GZEL.
























ATOM
1
CB
ALA
1
26.829
24.911
33.431
1.00
46.79


ATOM
2
C
ALA
1
28.010
24.831
31.273
1.00
51.75


ATOM
3
O
ALA
1
29.048
25.242
30.748
1.00
55.66


ATOM
4
N
ALA
1
29.275
24.764
33.312
1.00
48.96


ATOM
5
CA
ALA
1
28.005
24.323
32.689
1.00
49.44


ATOM
6
N
VAL
2
26.838
24.818
30.659
1.00
49.20


ATOM
7
CA
VAL
2
26.701
25.297
29.297
1.00
46.02


ATOM
8
CB
VAL
2
26.195
24.190
28.377
1.00
44.99


ATOM
9
CG1
VAL
2
26.187
24.670
26.943
1.00
43.38


ATOM
10
CG2
VAL
2
27.093
22.967
28.534
1.00
40.91


ATOM
11
C
VAL
2
25.705
26.444
29.321
1.00
45.79


ATOM
12
O
VAL
2
24.830
26.501
30.192
1.00
46.48


ATOM
13
N
SER
3
25.844
27.373
28.382
1.00
45.59


ATOM
14
CA
SER
3
24.951
28.533
28.326
1.00
45.63


ATOM
15
CB
SER
3
25.543
29.692
29.138
1.00
46.98


ATOM
16
OG
SER
3
24.691
30.821
29.139
1.00
50.89


ATOM
17
C
SER
3
24.738
28.971
26.886
1.00
42.84


ATOM
18
O
SER
3
25.100
28.256
25.949
1.00
46.23


ATOM
19
N
VAL
4
24.148
30.143
26.703
1.00
38.57


ATOM
20
CA
VAL
4
23.901
30.633
25.356
1.00
37.41


ATOM
21
CB
VAL
4
22.400
30.871
25.136
1.00
36.17


ATOM
22
CG1
VAL
4
21.933
32.057
25.965
1.00
34.74


ATOM
23
CG2
VAL
4
22.125
31.071
23.661
1.00
35.04


ATOM
24
C
VAL
4
24.671
31.941
25.171
1.00
36.25


ATOM
25
O
VAL
4
25.036
32.593
26.163
1.00
34.50


ATOM
26
N
SER
5
24.935
32.322
23.918
1.00
34.33


ATOM
27
CA
SER
5
25.664
33.559
23.655
1.00
34.34


ATOM
28
CB
SER
5
27.076
33.268
23.179
1.00
30.08


ATOM
29
OG
SER
5
27.086
32.928
21.806
1.00
23.67


ATOM
30
C
SER
5
25.032
34.490
22.627
1.00
35.94


ATOM
31
O
SER
5
24.066
34.149
21.921
1.00
38.21


ATOM
32
N
THR
6
25.631
35.668
22.536
1.00
35.10


ATOM
33
CA
THR
6
25.194
36.693
21.625
1.00
33.67


ATOM
34
CB
THR
6
26.131
37.887
21.716
1.00
33.12


ATOM
35
OG1
THR
6
25.661
38.744
22.755
1.00
33.18


ATOM
36
CG2
THR
6
26.203
38.662
20.385
1.00
34.10


ATOM
37
C
THR
6
25.198
36.161
20.219
1.00
34.02


ATOM
38
O
THR
6
24.183
36.172
19.528
1.00
37.02


ATOM
39
N
THR
7
26.360
35.692
19.801
1.00
36.77


ATOM
40
CA
THR
7
26.506
35.158
18.474
1.00
37.15


ATOM
41
CB
THR
7
27.972
35.059
18.119
1.00
38.00


ATOM
42
OG1
THR
7
28.138
34.070
17.104
1.00
42.94


ATOM
43
CG2
THR
7
28.796
34.694
19.333
1.00
35.45


ATOM
44
C
THR
7
25.850
33.788
18.346
1.00
37.14


ATOM
45
O
THR
7
25.545
33.333
17.241
1.00
35.92


ATOM
46
N
ASP
8
25.655
33.121
19.479
1.00
35.56


ATOM
47
CA
ASP
8
25.005
31.824
19.478
1.00
36.26


ATOM
48
CB
ASP
8
25.069
31.157
20.859
1.00
37.91


ATOM
49
CG
ASP
8
26.118
30.044
20.930
1.00
42.07


ATOM
50
OD1
ASP
8
26.845
29.821
19.926
1.00
42.80


ATOM
51
OD2
ASP
8
26.207
29.385
21.992
1.00
40.71


ATOM
52
C
ASP
8
23.565
32.055
19.084
1.00
34.39


ATOM
53
O
ASP
8
23.020
31.297
18.295
1.00
32.33


ATOM
54
N
PHE
9
22.956
33.110
19.612
1.00
33.82


ATOM
55
CA
PHE
9
21.576
33.396
19.262
1.00
34.15


ATOM
56
CB
PHE
9
21.000
34.468
20.165
1.00
32.06


ATOM
57
CG
PHE
9
19.502
34.518
20.138
1.00
31.29


ATOM
58
CD1
PHE
9
18.766
33.459
20.656
1.00
29.36


ATOM
59
CD2
PHE
9
18.827
35.611
19.581
1.00
30.22


ATOM
60
CE1
PHE
9
17.367
33.478
20.631
1.00
31.11


ATOM
61
CE2
PHE
9
17.453
35.651
19.544
1.00
31.35


ATOM
62
CZ
PHE
9
16.705
34.571
20.072
1.00
34.10


ATOM
63
C
PHE
9
21.463
33.865
17.817
1.00
35.20


ATOM
64
O
PHE
9
20.526
33.515
17.095
1.00
37.15


ATOM
65
N
GLY
10
22.430
34.674
17.406
1.00
35.16


ATOM
66
CA
GLY
10
22.443
35.182
16.049
1.00
34.12


ATOM
67
C
GLY
10
22.435
34.027
15.085
1.00
31.88


ATOM
68
O
GLY
10
21.608
33.975
14.180
1.00
31.31


ATOM
69
N
ASN
11
23.367
33.098
15.289
1.00
32.62


ATOM
70
CA
ASN
11
23.474
31.915
14.446
1.00
32.09


ATOM
71
CB
ASN
11
24.500
30.936
15.000
1.00
30.29


ATOM
72
CG
ASN
11
25.918
31.372
14.715
1.00
27.15


ATOM
73
OD1
ASN
11
26.167
32.066
13.732
1.00
25.09


ATOM
74
ND2
ASN
11
26.855
30.960
15.560
1.00
20.33


ATOM
75
C
ASN
11
22.148
31.206
14.360
1.00
32.33


ATOM
76
O
ASN
11
21.715
30.830
13.262
1.00
34.04


ATOM
77
N
PHE
12
21.524
31.021
15.527
1.00
30.36


ATOM
78
CA
PHE
12
20.215
30.371
15.624
1.00
32.00


ATOM
79
CB
PHE
12
19.626
30.516
17.051
1.00
29.79


ATOM
80
CG
PHE
12
20.365
29.735
18.124
1.00
24.06


ATOM
81
CD1
PHE
12
21.479
28.953
17.813
1.00
24.09


ATOM
82
CD2
PHE
12
19.955
29.795
19.464
1.00
22.95


ATOM
83
CE1
PHE
12
22.165
28.254
18.817
1.00
20.49


ATOM
84
CE2
PHE
12
20.659
29.079
20.467
1.00
21.55


ATOM
85
CZ
PHE
12
21.754
28.321
20.123
1.00
20.63


ATOM
86
C
PHE
12
19.276
31.053
14.613
1.00
31.42


ATOM
87
O
PHE
12
18.788
30.434
13.656
1.00
33.69


ATOM
88
N
LYS
13
19.056
32.343
14.824
1.00
28.13


ATOM
89
CA
LYS
13
18.178
33.097
13.968
1.00
24.06


ATOM
90
CB
LYS
13
18.120
34.542
14.443
1.00
24.85


ATOM
91
CG
LYS
13
17.469
34.664
15.785
1.00
26.16


ATOM
92
CD
LYS
13
17.143
36.111
16.115
1.00
31.82


ATOM
93
CE
LYS
13
16.040
36.686
15.214
1.00
34.72


ATOM
94
NZ
LYS
13
15.847
38.173
15.401
1.00
35.98


ATOM
95
C
LYS
13
18.612
33.053
12.532
1.00
21.70


ATOM
96
O
LYS
13
17.809
33.258
11.617
1.00
23.96


ATOM
97
N
PHE
14
19.882
32.787
12.311
1.00
22.50


ATOM
98
CA
PHE
14
20.338
32.800
10.948
1.00
22.03


ATOM
99
CB
PHE
14
21.809
33.188
10.876
1.00
20.84


ATOM
100
CG
PHE
14
22.375
33.054
9.508
1.00
23.35


ATOM
101
CD1
PHE
14
21.949
33.893
8.479
1.00
16.32


ATOM
102
CD2
PHE
14
23.269
32.027
9.212
1.00
25.22


ATOM
103
CE1
PHE
14
22.398
33.700
7.183
1.00
20.53


ATOM
104
CE2
PHE
14
23.722
31.836
7.895
1.00
24.23


ATOM
105
CZ
PHE
14
23.286
32.668
6.892
1.00
23.06


ATOM
106
C
PHE
14
20.155
31.508
10.185
1.00
20.08


ATOM
107
O
PHE
14
19.757
31.528
9.014
1.00
18.56


ATOM
108
N
TYR
15
20.469
30.388
10.820
1.00
22.14


ATOM
109
CA
TYR
15
20.383
29.145
10.100
1.00
28.79


ATOM
110
CB
TYR
15
21.181
28.078
10.854
1.00
28.20


ATOM
111
CG
TYR
15
22.677
28.326
10.692
1.00
29.94


ATOM
112
CD1
TYR
15
23.498
28.492
11.792
1.00
31.99


ATOM
113
CE1
TYR
15
24.884
28.755
11.653
1.00
32.66


ATOM
114
CD2
TYR
15
23.259
28.430
9.428
1.00
31.55


ATOM
115
CE2
TYR
15
24.628
28.692
9.269
1.00
33.72


ATOM
116
CZ
TYR
15
25.442
28.850
10.394
1.00
33.86


ATOM
117
OH
TYR
15
26.807
29.062
10.294
1.00
28.91


ATOM
118
C
TYR
15
18.997
28.681
9.672
1.00
30.43


ATOM
119
O
TYR
15
18.874
28.025
8.639
1.00
28.40


ATOM
120
N
ILE
16
17.944
29.024
10.409
1.00
30.41


ATOM
121
CA
ILE
16
16.630
28.580
9.957
1.00
30.84


ATOM
122
CB
ILE
16
15.471
29.079
10.830
1.00
31.23


ATOM
123
CG2
ILE
16
14.975
27.958
11.664
1.00
28.44


ATOM
124
CG1
ILE
16
15.886
30.291
11.656
1.00
32.82


ATOM
125
CD1
ILE
16
15.349
31.590
11.107
1.00
33.34


ATOM
126
C
ILE
16
16.366
29.035
8.540
1.00
31.82


ATOM
127
O
ILE
16
15.580
28.419
7.830
1.00
34.26


ATOM
128
N
GLN
17
17.016
30.108
8.105
1.00
30.85


ATOM
129
CA
GLN
17
16.775
30.575
6.742
1.00
28.53


ATOM
130
CB
GLN
17
17.574
31.858
6.463
1.00
30.13


ATOM
131
CG
GLN
17
17.234
32.992
7.473
1.00
30.83


ATOM
132
CD
GLN
17
17.579
34.397
6.964
1.00
32.84


ATOM
133
OE1
GLN
17
17.582
35.348
7.733
1.00
28.29


ATOM
134
NE2
GLN
17
17.854
34.528
5.664
1.00
34.81


ATOM
135
C
GLN
17
17.122
29.456
5.772
1.00
26.12


ATOM
136
O
GLN
17
16.461
29.257
4.771
1.00
22.90


ATOM
137
N
HIS
18
18.157
28.699
6.096
1.00
24.71


ATOM
138
CA
HIS
18
18.554
27.574
5.260
1.00
26.07


ATOM
139
CB
HIS
18
19.952
27.134
5.596
1.00
25.26


ATOM
140
CG
HIS
18
20.996
27.922
4.894
1.00
26.41


ATOM
141
CD2
HIS
18
21.394
27.907
3.603
1.00
25.37


ATOM
142
ND1
HIS
18
21.798
28.835
5.538
1.00
28.88


ATOM
143
CE1
HIS
18
22.659
29.344
4.672
1.00
29.96


ATOM
144
NE2
HIS
18
22.433
28.795
3.491
1.00
28.73


ATOM
145
C
HIS
18
17.624
26.408
5.465
1.00
27.02


ATOM
146
O
HIS
18
17.345
25.655
4.534
1.00
27.11


ATOM
147
N
GLY
19
17.148
26.252
6.693
1.00
28.43


ATOM
148
CA
GLY
19
16.217
25.178
6.943
1.00
29.45


ATOM
149
C
GLY
19
14.979
25.390
6.083
1.00
31.53


ATOM
150
O
GLY
19
14.518
24.461
5.417
1.00
34.43


ATOM
151
N
ALA
20
14.464
26.624
6.090
1.00
28.21


ATOM
152
CA
ALA
20
13.268
27.022
5.339
1.00
28.35


ATOM
153
CB
ALA
20
12.785
28.396
5.826
1.00
26.16


ATOM
154
C
ALA
20
13.547
27.086
3.842
1.00
29.16


ATOM
155
O
ALA
20
12.654
26.891
3.004
1.00
33.64


ATOM
156
N
ALA
21
14.798
27.390
3.520
1.00
27.87


ATOM
157
CA
ALA
21
15.241
27.493
2.145
1.00
25.44


ATOM
158
CB
ALA
21
16.668
28.040
2.104
1.00
19.43


ATOM
159
C
ALA
21
15.187
26.105
1.511
1.00
26.54


ATOM
160
O
ALA
21
14.754
25.954
0.365
1.00
29.36


ATOM
161
N
ALA
22
15.620
25.092
2.263
1.00
27.19


ATOM
162
CA
ALA
22
15.639
23.730
1.758
1.00
28.51


ATOM
163
CB
ALA
22
15.989
22.789
2.858
1.00
26.37


ATOM
164
C
ALA
22
14.276
23.376
1.184
1.00
32.45


ATOM
165
O
ALA
22
14.164
22.491
0.317
1.00
33.17


ATOM
166
N
TYR
23
13.250
24.079
1.669
1.00
34.80


ATOM
167
CA
TYR
23
11.878
23.856
1.240
1.00
35.46


ATOM
168
CB
TYR
23
10.900
24.500
2.230
1.00
31.16


ATOM
169
CG
TYR
23
10.567
23.607
3.423
1.00
31.27


ATOM
170
CD1
TYR
23
9.927
22.370
3.254
1.00
29.95


ATOM
171
CE1
TYR
23
9.624
21.533
4.367
1.00
24.00


ATOM
172
CD2
TYR
23
10.901
23.987
4.718
1.00
28.94


ATOM
173
CE2
TYR
23
10.615
23.163
5.817
1.00
27.14


ATOM
174
CZ
TYR
23
9.979
21.948
5.642
1.00
24.07


ATOM
175
OH
TYR
23
9.709
21.174
6.755
1.00
30.00


ATOM
176
C
TYR
23
11.574
24.334
−0.171
1.00
38.29


ATOM
177
O
TYR
23
10.434
24.227
−0.628
1.00
39.77


ATOM
178
N
CYS
24
12.566
24.873
−0.867
1.00
40.13


ATOM
179
CA
CYS
24
12.300
25.303
−2.227
1.00
43.23


ATOM
180
C
CYS
24
13.517
25.301
−3.116
1.00
42.88


ATOM
181
O
CYS
24
13.401
25.294
−4.330
1.00
42.12


ATOM
182
CB
CYS
24
11.628
26.679
−2.240
1.00
47.63


ATOM
183
SG
CYS
24
12.447
27.997
−1.288
1.00
56.39


ATOM
184
N
ASN
25
14.691
25.287
−2.514
1.00
42.45


ATOM
185
CA
ASN
25
15.906
25.271
−3.304
1.00
44.76


ATOM
186
CB
ASN
25
16.952
26.149
−2.642
1.00
43.87


ATOM
187
CG
ASN
25
16.533
27.586
−2.612
1.00
48.58


ATOM
188
OD1
ASN
25
15.624
27.974
−1.875
1.00
48.53


ATOM
189
ND2
ASN
25
17.171
28.391
−3.443
1.00
52.09


ATOM
190
C
ASN
25
16.412
23.852
−3.460
1.00
45.88


ATOM
191
O
ASN
25
17.475
23.613
−4.039
1.00
46.08


ATOM
192
N
SER
26
15.610
22.917
−2.965
1.00
48.46


ATOM
193
CA
SER
26
15.940
21.509
−2.998
1.00
49.56


ATOM
194
CB
SER
26
14.972
20.760
−2.085
1.00
51.09


ATOM
195
OG
SER
26
13.680
21.347
−2.136
1.00
54.46


ATOM
196
C
SER
26
15.885
20.973
−4.417
1.00
48.64


ATOM
197
O
SER
26
16.054
19.769
−4.651
1.00
46.39


ATOM
198
N
GLU
27
15.665
21.886
−5.359
1.00
48.70


ATOM
199
CA
GLU
27
15.558
21.526
−6.754
1.00
47.85


ATOM
200
CB
GLU
27
14.123
21.687
−7.187
1.00
50.86


ATOM
201
CG
GLU
27
13.741
20.727
−8.260
1.00
54.11


ATOM
202
CD
GLU
27
13.588
19.339
−7.708
1.00
53.46


ATOM
203
OE1
GLU
27
12.499
19.046
−7.165
1.00
48.31


ATOM
204
OE2
GLU
27
14.565
18.558
−7.799
1.00
55.78


ATOM
205
C
GLU
27
16.426
22.410
−7.623
1.00
46.15


ATOM
206
O
GLU
27
16.583
22.165
−8.818
1.00
45.46


ATOM
207
N
ALA
28
16.979
23.448
−7.010
1.00
45.36


ATOM
208
CA
ALA
28
17.821
24.404
−7.712
1.00
45.38


ATOM
209
CB
ALA
28
18.254
25.493
−6.762
1.00
46.93


ATOM
210
C
ALA
28
19.040
23.804
−8.395
1.00
45.46


ATOM
211
O
ALA
28
19.693
22.904
−7.868
1.00
45.96


ATOM
212
N
PRO
29
19.361
24.314
−9.593
1.00
43.34


ATOM
213
CD
PRO
29
18.585
25.318
−10.336
1.00
43.59


ATOM
214
CA
PRO
29
20.499
23.860
−10.392
1.00
39.84


ATOM
215
CB
PRO
29
20.199
24.422
−11.789
1.00
40.87


ATOM
216
CG
PRO
29
18.731
24.809
−11.738
1.00
43.29


ATOM
217
C
PRO
29
21.768
24.456
−9.814
1.00
36.35


ATOM
218
O
PRO
29
21.745
25.532
−9.218
1.00
32.62


ATOM
219
N
ALA
30
22.879
23.760
−9.981
1.00
34.74


ATOM
220
CA
ALA
30
24.118
24.291
−9.462
1.00
40.14


ATOM
221
CB
ALA
30
25.293
23.443
−9.913
1.00
39.49


ATOM
222
C
ALA
30
24.224
25.704
−10.015
1.00
43.07


ATOM
223
O
ALA
30
23.557
26.041
−10.999
1.00
45.14


ATOM
224
N
GLY
31
25.039
26.532
−9.366
1.00
43.67


ATOM
225
CA
GLY
31
25.209
27.903
−9.812
1.00
44.09


ATOM
226
C
GLY
31
24.044
28.817
−9.486
1.00
45.12


ATOM
227
O
GLY
31
24.216
30.036
−9.426
1.00
45.37


ATOM
228
N
ALA
32
22.861
28.236
−9.275
1.00
45.29


ATOM
229
CA
ALA
32
21.663
29.012
−8.942
1.00
44.96


ATOM
230
CB
ALA
32
20.427
28.091
−8.837
1.00
46.26


ATOM
231
C
ALA
32
21.874
29.754
−7.626
1.00
44.27


ATOM
232
O
ALA
32
22.799
29.449
−6.871
1.00
45.48


ATOM
233
N
LYS
33
21.014
30.731
−7.362
1.00
44.05


ATOM
234
CA
LYS
33
21.096
31.530
−6.147
1.00
43.46


ATOM
235
CB
LYS
33
20.903
33.007
−6.469
1.00
45.85


ATOM
236
CG
LYS
33
21.975
33.588
−7.362
1.00
46.87


ATOM
237
CD
LYS
33
23.287
33.640
−6.609
1.00
48.03


ATOM
238
CE
LYS
33
24.349
34.400
−7.378
1.00
48.31


ATOM
239
NZ
LYS
33
25.524
34.723
−6.507
1.00
47.98


ATOM
240
C
LYS
33
20.041
31.120
−5.157
1.00
42.61


ATOM
241
O
LYS
33
18.853
31.089
−5.472
1.00
44.51


ATOM
242
N
VAL
34
20.480
30.820
−3.947
1.00
41.96


ATOM
243
CA
VAL
34
19.559
30.423
−2.906
1.00
40.22


ATOM
244
CB
VAL
34
20.314
30.132
−1.607
1.00
39.03


ATOM
245
CG1
VAL
34
19.333
29.774
−0.516
1.00
39.34


ATOM
246
CG2
VAL
34
21.301
28.982
−1.835
1.00
37.52


ATOM
247
C
VAL
34
18.553
31.554
−2.731
1.00
41.33


ATOM
248
O
VAL
34
18.917
32.711
−2.492
1.00
41.11


ATOM
249
N
THR
35
17.284
31.206
−2.879
1.00
43.13


ATOM
250
CA
THR
35
16.242
32.187
−2.801
1.00
46.82


ATOM
251
CB
THR
35
15.904
32.677
−4.215
1.00
48.83


ATOM
252
OG1
THR
35
15.010
33.792
−4.143
1.00
55.17


ATOM
253
CG2
THR
35
15.253
31.559
−4.996
1.00
48.30


ATOM
254
C
THR
35
14.987
31.629
−2.153
1.00
47.64


ATOM
255
O
THR
35
14.723
30.432
−2.197
1.00
50.05


ATOM
256
N
CYS
36
14.209
32.525
−1.561
1.00
47.99


ATOM
257
CA
CYS
36
12.974
32.160
−0.895
1.00
47.27


ATOM
258
C
CYS
36
11.993
33.270
−1.071
1.00
49.06


ATOM
259
O
CYS
36
12.351
34.443
−1.147
1.00
51.86


ATOM
260
CB
CYS
36
13.206
31.961
0.599
1.00
47.51


ATOM
261
SG
CYS
36
14.721
31.004
0.946
1.00
46.80


ATOM
262
N
SER
37
10.738
32.873
−1.122
1.00
50.29


ATOM
263
CA
SER
37
9.657
33.811
−1.253
1.00
51.64


ATOM
264
CB
SER
37
8.606
33.282
−2.224
1.00
51.71


ATOM
265
OG
SER
37
7.920
32.176
−1.671
1.00
51.99


ATOM
266
C
SER
37
9.047
33.954
0.132
1.00
52.79


ATOM
267
O
SER
37
9.227
33.081
1.009
1.00
54.99


ATOM
268
N
GLY
38
8.313
35.049
0.319
1.00
52.11


ATOM
269
CA
GLY
38
7.683
35.300
1.601
1.00
47.78


ATOM
270
C
GLY
38
8.741
35.668
2.616
1.00
46.33


ATOM
271
O
GLY
38
8.597
35.336
3.799
1.00
41.87


ATOM
272
N
ASN
39
9.794
36.347
2.142
1.00
46.02


ATOM
273
CA
ASN
39
10.905
36.774
2.986
1.00
43.85


ATOM
274
CB
ASN
39
10.435
37.873
3.941
1.00
47.51


ATOM
275
CG
ASN
39
11.282
39.114
3.842
1.00
54.53


ATOM
276
OD1
ASN
39
12.286
39.258
4.551
1.00
56.71


ATOM
277
ND2
ASN
39
10.902
40.017
2.938
1.00
55.69


ATOM
278
C
ASN
39
11.422
35.574
3.762
1.00
41.94


ATOM
279
O
ASN
39
11.950
35.703
4.881
1.00
38.41


ATOM
280
N
GLY
40
11.274
34.406
3.143
1.00
41.26


ATOM
281
CA
GLY
40
11.689
33.183
3.785
1.00
39.14


ATOM
282
C
GLY
40
13.131
33.124
4.234
1.00
37.57


ATOM
283
O
GLY
40
13.427
32.461
5.228
1.00
38.05


ATOM
284
N
CYS
41
14.025
33.809
3.521
1.00
37.14


ATOM
285
CA
CYS
41
15.449
33.756
3.851
1.00
36.29


ATOM
286
C
CYS
41
16.257
34.924
3.300
1.00
37.23


ATOM
287
O
CYS
41
17.256
34.731
2.617
1.00
36.42


ATOM
288
CB
CYS
41
16.028
32.456
3.305
1.00
33.97


ATOM
289
SG
CYS
41
16.100
32.411
1.482
1.00
36.33


ATOM
290
N
PRO
42
15.850
36.153
3.621
1.00
38.20


ATOM
291
CD
PRO
42
14.779
36.487
4.576
1.00
39.84


ATOM
292
CA
PRO
42
16.540
37.356
3.148
1.00
38.13


ATOM
293
CB
PRO
42
15.715
38.485
3.766
1.00
37.35


ATOM
294
CG
PRO
42
15.177
37.862
5.027
1.00
37.04


ATOM
295
C
PRO
42
18.047
37.480
3.424
1.00
38.39


ATOM
296
O
PRO
42
18.790
37.903
2.548
1.00
38.45


ATOM
297
N
THR
43
18.504
37.126
4.622
1.00
38.67


ATOM
298
CA
THR
43
19.931
37.235
4.932
1.00
38.85


ATOM
299
CB
THR
43
20.251
36.818
6.395
1.00
36.92


ATOM
300
OG1
THR
43
19.613
37.727
7.299
1.00
37.95


ATOM
301
CG2
THR
43
21.753
36.853
6.653
1.00
33.96


ATOM
302
C
THR
43
20.686
36.334
3.993
1.00
38.46


ATOM
303
O
THR
43
21.789
36.636
3.556
1.00
39.61


ATOM
304
N
VAL
44
20.081
35.209
3.684
1.00
38.02


ATOM
305
CA
VAL
44
20.730
34.302
2.792
1.00
39.52


ATOM
306
CB
VAL
44
19.982
32.988
2.750
1.00
36.82


ATOM
307
CG1
VAL
44
20.601
32.105
1.712
1.00
37.04


ATOM
308
CG2
VAL
44
20.028
32.321
4.106
1.00
36.16


ATOM
309
C
VAL
44
20.794
34.949
1.412
1.00
43.60


ATOM
310
O
VAL
44
21.843
34.950
0.771
1.00
41.94


ATOM
311
N
GLN
45
19.682
35.516
0.957
1.00
47.86


ATOM
312
CA
GLN
45
19.684
36.166
−0.347
1.00
50.53


ATOM
313
CB
GLN
45
18.267
36.548
−0.780
1.00
46.99


ATOM
314
CG
GLN
45
17.327
35.370
−0.912
1.00
49.29


ATOM
315
CD
GLN
45
15.924
35.790
−1.305
1.00
50.89


ATOM
316
OE1
GLN
45
15.396
36.774
−0.795
1.00
54.31


ATOM
317
NE2
GLN
45
15.311
35.044
−2.205
1.00
47.74


ATOM
318
C
GLN
45
20.568
37.405
−0.289
1.00
52.82


ATOM
319
O
GLN
45
21.341
37.667
−1.207
1.00
54.98


ATOM
320
N
SER
46
20.462
38.164
0.795
1.00
54.53


ATOM
321
CA
SER
46
21.278
39.360
0.946
1.00
54.05


ATOM
322
CB
SER
46
21.162
39.907
2.356
1.00
52.75


ATOM
323
OG
SER
46
22.332
40.647
2.655
1.00
52.40


ATOM
324
C
SER
46
22.737
39.045
0.667
1.00
53.72


ATOM
325
O
SER
46
23.455
39.812
0.033
1.00
52.04


ATOM
326
N
ASN
47
23.170
37.907
1.180
1.00
54.08


ATOM
327
CA
ASN
47
24.524
37.462
0.975
1.00
54.09


ATOM
328
CB
ASN
47
24.926
36.519
2.094
1.00
52.99


ATOM
329
CG
ASN
47
24.669
37.109
3.446
1.00
55.12


ATOM
330
OD1
ASN
47
24.826
36.447
4.464
1.00
55.92


ATOM
331
ND2
ASN
47
24.267
38.376
3.470
1.00
56.97


ATOM
332
C
ASN
47
24.483
36.722
−0.335
1.00
55.62


ATOM
333
O
ASN
47
23.409
36.481
−0.895
1.00
55.92


ATOM
334
N
GLY
48
25.651
36.338
−0.815
1.00
55.14


ATOM
335
CA
GLY
48
25.706
35.629
−2.071
1.00
53.83


ATOM
336
C
GLY
48
25.619
34.127
−1.991
1.00
51.96


ATOM
337
O
GLY
48
26.424
33.435
−2.596
1.00
54.44


ATOM
338
N
ALA
49
24.632
33.615
−1.269
1.00
49.83


ATOM
339
CA
ALA
49
24.465
32.166
−1.130
1.00
47.17


ATOM
340
CB
ALA
49
23.393
31.863
−0.106
1.00
44.77


ATOM
341
C
ALA
49
24.108
31.506
−2.458
1.00
45.91


ATOM
342
O
ALA
49
23.130
31.879
−3.108
1.00
44.92


ATOM
343
N
THR
50
24.895
30.513
−2.855
1.00
44.61


ATOM
344
CA
THR
50
24.658
29.827
−4.119
1.00
45.57


ATOM
345
CB
THR
50
25.711
30.252
−5.137
1.00
44.64


ATOM
346
OG1
THR
50
27.016
30.057
−4.572
1.00
48.93


ATOM
347
CG2
THR
50
25.543
31.714
−5.484
1.00
44.18


ATOM
348
C
THR
50
24.689
28.303
−3.973
1.00
44.90


ATOM
349
O
THR
50
25.323
27.774
−3.058
1.00
47.41


ATOM
350
N
ILE
51
24.001
27.606
−4.878
1.00
41.51


ATOM
351
CA
ILE
51
23.939
26.147
−4.854
1.00
40.26


ATOM
352
CB
ILE
51
22.705
25.608
−5.608
1.00
40.04


ATOM
353
CG2
ILE
51
22.656
24.083
−5.524
1.00
40.44


ATOM
354
CG1
ILE
51
21.431
26.191
−5.012
1.00
44.06


ATOM
355
CD1
ILE
51
20.980
27.438
−5.720
1.00
43.76


ATOM
356
C
ILE
51
25.155
25.502
−5.491
1.00
39.87


ATOM
357
O
ILE
51
25.649
25.955
−6.523
1.00
42.31


ATOM
358
N
VAL
52
25.631
24.429
−4.877
1.00
38.22


ATOM
359
CA
VAL
52
26.763
23.712
−5.415
1.00
35.17


ATOM
360
CB
VAL
52
27.711
23.308
−4.299
1.00
33.49


ATOM
361
CG1
VAL
52
28.920
22.570
−4.869
1.00
34.02


ATOM
362
CG2
VAL
52
28.152
24.553
−3.549
1.00
29.71


ATOM
363
C
VAL
52
26.144
22.485
−6.076
1.00
35.33


ATOM
364
O
VAL
52
26.728
21.887
−7.001
1.00
36.26


ATOM
365
N
ALA
53
24.936
22.144
−5.619
1.00
35.25


ATOM
366
CA
ALA
53
24.194
21.003
−6.152
1.00
35.42


ATOM
367
CB
ALA
53
25.073
19.748
−6.117
1.00
31.66


ATOM
368
C
ALA
53
22.951
20.793
−5.293
1.00
33.55


ATOM
369
O
ALA
53
22.942
21.153
−4.115
1.00
35.15


ATOM
370
N
SER
54
21.890
20.247
−5.874
1.00
32.33


ATOM
371
CA
SER
54
20.688
19.973
−5.084
1.00
31.79


ATOM
372
CB
SER
54
19.502
20.832
−5.524
1.00
30.57


ATOM
373
OG
SER
54
19.105
20.503
−6.840
1.00
37.05


ATOM
374
C
SER
54
20.383
18.505
−5.309
1.00
31.23


ATOM
375
O
SER
54
20.939
17.883
−6.230
1.00
27.55


ATOM
376
N
PHE
55
19.501
17.939
−4.500
1.00
32.84


ATOM
377
CA
PHE
55
19.243
16.526
−4.654
1.00
35.43


ATOM
378
CB
PHE
55
20.399
15.741
−4.053
1.00
35.14


ATOM
379
CG
PHE
55
20.922
16.322
−2.761
1.00
32.14


ATOM
380
CD1
PHE
55
22.222
16.856
−2.704
1.00
29.42


ATOM
381
CD2
PHE
55
20.155
16.305
−1.599
1.00
30.22


ATOM
382
CE1
PHE
55
22.745
17.352
−1.520
1.00
25.73


ATOM
383
CE2
PHE
55
20.693
16.810
−0.398
1.00
31.85


ATOM
384
CZ
PHE
55
21.978
17.325
−0.368
1.00
29.09


ATOM
385
C
PHE
55
17.979
16.116
−3.975
1.00
35.04


ATOM
386
O
PHE
55
17.518
16.777
−3.037
1.00
39.64


ATOM
387
N
THR
56
17.429
15.000
−4.436
1.00
29.99


ATOM
388
CA
THR
56
16.191
14.488
−3.864
1.00
28.55


ATOM
389
CB
THR
56
14.945
15.096
−4.590
1.00
27.79


ATOM
390
OG1
THR
56
14.733
14.425
−5.844
1.00
23.97


ATOM
391
CG2
THR
56
15.178
16.600
−4.870
1.00
21.19


ATOM
392
C
THR
56
16.129
12.958
−3.945
1.00
27.76


ATOM
393
O
THR
56
16.540
12.352
−4.945
1.00
27.35


ATOM
394
N
GLY
57
15.659
12.336
−2.869
1.00
27.18


ATOM
395
CA
GLY
57
15.530
10.890
−2.856
1.00
28.45


ATOM
396
C
GLY
57
14.097
10.554
−3.204
1.00
29.19


ATOM
397
O
GLY
57
13.209
10.576
−2.352
1.00
28.30


ATOM
398
N
SER
58
13.874
10.243
−4.475
1.00
31.31


ATOM
399
CA
SER
58
12.547
9.912
−4.978
1.00
34.45


ATOM
400
CB
SER
58
12.654
9.347
−6.397
1.00
38.20


ATOM
401
OG
SER
58
11.381
9.224
−7.010
1.00
44.69


ATOM
402
C
SER
58
11.858
8.901
−4.076
1.00
33.61


ATOM
403
O
SER
58
10.735
9.126
−3.620
1.00
34.55


ATOM
404
N
LYS
59
12.535
7.796
−3.810
1.00
34.29


ATOM
405
CA
LYS
59
11.974
6.761
−2.968
1.00
34.68


ATOM
406
CB
LYS
59
12.943
5.587
−2.921
1.00
36.22


ATOM
407
CG
LYS
59
12.562
4.459
−1.966
1.00
38.49


ATOM
408
CD
LYS
59
13.605
3.338
−2.000
1.00
48.21


ATOM
409
CE
LYS
59
13.141
2.110
−1.216
1.00
54.13


ATOM
410
NZ
LYS
59
14.126
0.972
−1.246
1.00
54.56


ATOM
411
C
LYS
59
11.644
7.199
−1.549
1.00
33.98


ATOM
412
O
LYS
59
10.735
6.654
−0.921
1.00
39.25


ATOM
413
N
THR
60
12.352
8.193
−1.033
1.00
32.34


ATOM
414
CA
THR
60
12.114
8.569
0.347
1.00
29.15


ATOM
415
CB
THR
60
13.426
8.369
1.109
1.00
27.10


ATOM
416
OG1
THR
60
13.175
7.767
2.378
1.00
23.98


ATOM
417
CG2
THR
60
14.143
9.696
1.268
1.00
29.07


ATOM
418
C
THR
60
11.520
9.963
0.636
1.00
30.25


ATOM
419
O
THR
60
11.184
10.270
1.779
1.00
28.21


ATOM
420
N
GLY
61
11.381
10.804
−0.384
1.00
30.45


ATOM
421
CA
GLY
61
10.815
12.119
−0.148
1.00
29.54


ATOM
422
C
GLY
61
11.822
13.108
0.398
1.00
31.39


ATOM
423
O
GLY
61
11.553
14.299
0.458
1.00
34.11


ATOM
424
N
ILE
62
12.989
12.640
0.808
1.00
29.86


ATOM
425
CA
ILE
62
13.961
13.583
1.294
1.00
28.85


ATOM
426
CB
ILE
62
15.203
12.887
1.857
1.00
29.86


ATOM
427
CG2
ILE
62
15.952
12.192
0.729
1.00
30.75


ATOM
428
CG1
ILE
62
16.091
13.922
2.572
1.00
30.47


ATOM
429
CD1
ILE
62
15.475
14.557
3.844
1.00
24.98


ATOM
430
C
ILE
62
14.373
14.495
0.140
1.00
30.26


ATOM
431
O
ILE
62
14.013
14.278
−1.018
1.00
30.97


ATOM
432
N
GLY
63
15.130
15.526
0.481
1.00
29.70


ATOM
433
CA
GLY
63
15.599
16.488
−0.492
1.00
29.18


ATOM
434
C
GLY
63
16.466
17.450
0.281
1.00
30.92


ATOM
435
O
GLY
63
16.366
17.524
1.516
1.00
32.28


ATOM
436
N
GLY
64
17.309
18.186
−0.437
1.00
30.23


ATOM
437
CA
GLY
64
18.192
19.141
0.201
1.00
31.31


ATOM
438
C
GLY
64
19.222
19.699
−0.759
1.00
32.75


ATOM
439
O
GLY
64
19.257
19.312
−1.937
1.00
35.66


ATOM
440
N
TYR
65
20.084
20.579
−0.251
1.00
31.95


ATOM
441
CA
TYR
65
21.113
21.206
−1.075
1.00
32.66


ATOM
442
CB
TYR
65
20.546
22.488
−1.709
1.00
34.11


ATOM
443
CG
TYR
65
20.241
23.601
−0.703
1.00
30.58


ATOM
444
CD1
TYR
65
21.260
24.429
−0.204
1.00
29.89


ATOM
445
CE1
TYR
65
20.991
25.404
0.765
1.00
31.16


ATOM
446
CD2
TYR
65
18.946
23.791
−0.203
1.00
31.70


ATOM
447
CE2
TYR
65
18.682
24.762
0.767
1.00
31.85


ATOM
448
CZ
TYR
65
19.704
25.567
1.251
1.00
33.02


ATOM
449
OH
TYR
65
19.436
26.519
2.234
1.00
30.17


ATOM
450
C
TYR
65
22.384
21.544
−0.295
1.00
31.93


ATOM
451
O
TYR
65
22.420
21.458
0.946
1.00
33.75


ATOM
452
N
VAL
66
23.425
21.898
−1.050
1.00
31.26


ATOM
453
CA
VAL
66
24.730
22.308
−0.519
1.00
29.99


ATOM
454
CB
VAL
66
25.879
21.384
−0.995
1.00
25.14


ATOM
455
CG1
VAL
66
27.229
21.928
−0.486
1.00
19.75


ATOM
456
CG2
VAL
66
25.653
19.983
−0.517
1.00
19.11


ATOM
457
C
VAL
66
24.977
23.683
−1.138
1.00
32.47


ATOM
458
O
VAL
66
24.944
23.819
−2.378
1.00
34.11


ATOM
459
N
ALA
67
25.229
24.688
−0.297
1.00
34.55


ATOM
460
CA
ALA
67
25.456
26.034
−0.794
1.00
36.86


ATOM
461
CB
ALA
67
24.248
26.883
−0.501
1.00
37.43


ATOM
462
C
ALA
67
26.691
26.686
−0.205
1.00
38.04


ATOM
463
O
ALA
67
27.185
26.266
0.847
1.00
37.89


ATOM
464
N
THR
68
27.142
27.746
−0.877
1.00
38.87


ATOM
465
CA
THR
68
28.320
28.515
−0.477
1.00
41.49


ATOM
466
CB
THR
68
29.374
28.482
−1.555
1.00
40.24


ATOM
467
OG1
THR
68
28.781
28.909
−2.786
1.00
39.38


ATOM
468
CG2
THR
68
29.916
27.078
−1.695
1.00
37.17


ATOM
469
C
THR
68
27.974
29.971
−0.209
1.00
44.07


ATOM
470
O
THR
68
27.303
30.619
−1.007
1.00
45.44


ATOM
471
N
ASP
69
28.481
30.476
0.914
1.00
46.41


ATOM
472
CA
ASP
69
28.240
31.844
1.379
1.00
48.43


ATOM
473
CB
ASP
69
27.760
31.808
2.834
1.00
52.61


ATOM
474
CG
ASP
69
26.780
32.927
3.167
1.00
56.38


ATOM
475
OD1
ASP
69
27.148
34.118
3.048
1.00
56.17


ATOM
476
OD2
ASP
69
25.634
32.602
3.556
1.00
58.58


ATOM
477
C
ASP
69
29.493
32.716
1.294
1.00
48.33


ATOM
478
O
ASP
69
30.354
32.686
2.182
1.00
49.35


ATOM
479
N
PRO
70
29.611
33.507
0.221
1.00
46.85


ATOM
480
CD
PRO
70
28.598
33.759
−0.816
1.00
45.47


ATOM
481
CA
PRO
70
30.773
34.384
0.052
1.00
47.08


ATOM
482
CB
PRO
70
30.425
35.181
−1.210
1.00
46.69


ATOM
483
CG
PRO
70
28.929
35.155
−1.241
1.00
45.84


ATOM
484
C
PRO
70
30.991
35.281
1.276
1.00
47.53


ATOM
485
O
PRO
70
32.110
35.455
1.749
1.00
47.58


ATOM
486
N
THR
71
29.895
35.833
1.782
1.00
46.80


ATOM
487
CA
THR
71
29.901
36.723
2.938
1.00
45.48


ATOM
488
CB
THR
71
28.501
37.315
3.177
1.00
43.99


ATOM
489
OG1
THR
71
28.104
38.086
2.041
1.00
40.66


ATOM
490
CG2
THR
71
28.497
38.181
4.408
1.00
43.58


ATOM
491
C
THR
71
30.312
36.029
4.231
1.00
45.79


ATOM
492
O
THR
71
31.178
36.506
4.960
1.00
45.02


ATOM
493
N
ARG
72
29.671
34.904
4.521
1.00
46.99


ATOM
494
CA
ARG
72
29.954
34.171
5.746
1.00
47.70


ATOM
495
CB
ARG
72
28.724
33.384
6.159
1.00
48.08


ATOM
496
CG
ARG
72
27.681
34.206
6.859
1.00
48.15


ATOM
497
CD
ARG
72
26.521
33.312
7.196
1.00
46.29


ATOM
498
NE
ARG
72
25.995
33.592
8.524
1.00
46.49


ATOM
499
CZ
ARG
72
26.452
33.057
9.651
1.00
44.95


ATOM
500
NH1
ARG
72
27.457
32.193
9.625
1.00
50.14


ATOM
501
NH2
ARG
72
25.905
33.400
10.809
1.00
41.99


ATOM
502
C
ARG
72
31.143
33.217
5.681
1.00
46.99


ATOM
503
O
ARG
72
31.549
32.655
6.709
1.00
44.85


ATOM
504
N
LYS
73
31.698
33.035
4.484
1.00
46.91


ATOM
505
CA
LYS
73
32.822
32.128
4.308
1.00
46.89


ATOM
506
CB
LYS
73
34.098
32.703
4.929
1.00
51.74


ATOM
507
CG
LYS
73
34.809
33.782
4.112
1.00
57.40


ATOM
508
CD
LYS
73
36.162
34.081
4.783
1.00
63.05


ATOM
509
CE
LYS
73
37.203
34.577
3.777
1.00
67.22


ATOM
510
NZ
LYS
73
38.607
34.596
4.319
1.00
69.40


ATOM
511
C
LYS
73
32.516
30.792
4.968
1.00
44.83


ATOM
512
O
LYS
73
33.140
30.419
5.969
1.00
42.64


ATOM
513
N
GLU
74
31.544
30.081
4.409
1.00
42.80


ATOM
514
CA
GLU
74
31.164
28.781
4.926
1.00
41.44


ATOM
515
CB
GLU
74
30.311
28.923
6.191
1.00
41.39


ATOM
516
CG
GLU
74
28.989
29.654
5.992
1.00
40.80


ATOM
517
CD
GLU
74
28.215
29.819
7.295
1.00
41.18


ATOM
518
OE1
GLU
74
26.988
30.036
7.239
1.00
37.73


ATOM
519
OE2
GLU
74
28.831
29.738
8.376
1.00
41.62


ATOM
520
C
GLU
74
30.393
27.999
3.876
1.00
39.97


ATOM
521
O
GLU
74
30.014
28.534
2.825
1.00
39.67


ATOM
522
N
ILE
75
30.181
26.723
4.179
1.00
37.40


ATOM
523
CA
ILE
75
29.464
25.807
3.309
1.00
33.79


ATOM
524
CB
ILE
75
30.418
24.715
2.753
1.00
33.51


ATOM
525
CG2
ILE
75
29.679
23.821
1.766
1.00
33.40


ATOM
526
CG1
ILE
75
31.626
25.362
2.062
1.00
34.17


ATOM
527
CD1
ILE
75
32.723
24.362
1.645
1.00
32.76


ATOM
528
C
ILE
75
28.394
25.135
4.157
1.00
31.88


ATOM
529
O
ILE
75
28.711
24.432
5.127
1.00
30.16


ATOM
530
N
VAL
76
27.130
25.354
3.806
1.00
29.47


ATOM
531
CA
VAL
76
26.043
24.736
4.571
1.00
30.29


ATOM
532
CB
VAL
76
24.930
25.758
4.986
1.00
29.82


ATOM
533
CG1
VAL
76
25.539
27.145
5.281
1.00
25.34


ATOM
534
CG2
VAL
76
23.870
25.815
3.913
1.00
29.32


ATOM
535
C
VAL
76
25.363
23.627
3.767
1.00
29.05


ATOM
536
O
VAL
76
25.384
23.655
2.523
1.00
32.60


ATOM
537
N
VAL
77
24.757
22.668
4.484
1.00
29.82


ATOM
538
CA
VAL
77
24.037
21.517
3.879
1.00
29.11


ATOM
539
CB
VAL
77
24.688
20.162
4.261
1.00
27.37


ATOM
540
CG1
VAL
77
24.313
19.102
3.250
1.00
24.87


ATOM
541
CG2
VAL
77
26.179
20.302
4.359
1.00
25.61


ATOM
542
C
VAL
77
22.619
21.486
4.429
1.00
28.13


ATOM
543
O
VAL
77
22.412
21.080
5.576
1.00
29.04


ATOM
544
N
SER
78
21.649
21.894
3.618
1.00
27.68


ATOM
545
CA
SER
78
20.267
21.957
4.083
1.00
29.69


ATOM
546
CB
SER
78
19.669
23.313
3.737
1.00
29.26


ATOM
547
OG
SER
78
20.187
24.292
4.582
1.00
35.26


ATOM
548
C
SER
78
19.333
20.870
3.580
1.00
28.37


ATOM
549
O
SER
78
19.176
20.652
2.375
1.00
32.05


ATOM
550
N
PHE
79
18.686
20.195
4.509
1.00
26.09


ATOM
551
CA
PHE
79
17.774
19.148
4.120
1.00
27.58


ATOM
552
CB
PHE
79
18.086
17.899
4.894
1.00
27.89


ATOM
553
CG
PHE
79
19.512
17.483
4.792
1.00
23.20


ATOM
554
CD1
PHE
79
20.499
18.090
5.561
1.00
23.22


ATOM
555
CD2
PHE
79
19.868
16.445
3.954
1.00
22.33


ATOM
556
CE1
PHE
79
21.813
17.649
5.495
1.00
23.58


ATOM
557
CE2
PHE
79
21.172
16.006
3.886
1.00
21.16


ATOM
558
CZ
PHE
79
22.143
16.605
4.659
1.00
22.90


ATOM
559
C
PHE
79
16.411
19.660
4.471
1.00
30.97


ATOM
560
O
PHE
79
16.260
20.394
5.467
1.00
31.30


ATOM
561
N
ARG
80
15.419
19.272
3.675
1.00
34.09


ATOM
562
CA
ARG
80
14.069
19.757
3.884
1.00
37.31


ATOM
563
CB
ARG
80
13.423
20.015
2.541
1.00
39.96


ATOM
564
CG
ARG
80
13.054
18.739
1.827
1.00
44.84


ATOM
565
CD
ARG
80
12.388
19.015
0.509
1.00
43.90


ATOM
566
NE
ARG
80
11.986
17.775
−0.140
1.00
44.13


ATOM
567
CZ
ARG
80
11.652
17.692
−1.421
1.00
47.81


ATOM
568
NH1
ARG
80
11.673
18.779
−2.185
1.00
47.38


ATOM
569
NH2
ARG
80
11.308
16.522
−1.943
1.00
50.47


ATOM
570
C
ARG
80
13.176
18.819
4.674
1.00
38.95


ATOM
571
O
ARG
80
13.176
17.603
4.441
1.00
38.69


ATOM
572
N
GLY
81
12.381
19.397
5.573
1.00
40.20


ATOM
573
CA
GLY
81
11.482
18.604
6.393
1.00
42.83


ATOM
574
C
GLY
81
10.232
18.077
5.687
1.00
45.60


ATOM
575
O
GLY
81
10.196
17.974
4.443
1.00
46.04


ATOM
576
N
SER
82
9.207
17.739
6.475
1.00
48.26


ATOM
577
CA
SER
82
7.961
17.210
5.937
1.00
51.78


ATOM
578
CB
SER
82
7.335
16.244
6.947
1.00
53.73


ATOM
579
OG
SER
82
6.254
15.513
6.393
1.00
58.63


ATOM
580
C
SER
82
6.998
18.348
5.632
1.00
53.53


ATOM
581
O
SER
82
6.751
19.219
6.471
1.00
54.68


ATOM
582
N
ILE
83
6.464
18.339
4.420
1.00
52.86


ATOM
583
CA
ILE
83
5.522
19.355
4.003
1.00
52.55


ATOM
584
CB
ILE
83
5.488
19.443
2.479
1.00
53.58


ATOM
585
CG2
ILE
83
6.841
19.896
1.979
1.00
53.86


ATOM
586
CG1
ILE
83
5.133
18.077
1.885
1.00
53.41


ATOM
587
CD1
ILE
83
5.129
18.011
0.381
1.00
53.83


ATOM
588
C
ILE
83
4.157
18.946
4.527
1.00
52.26


ATOM
589
O
ILE
83
3.168
19.677
4.375
1.00
51.93


ATOM
590
N
ASN
84
4.122
17.770
5.153
1.00
48.94


ATOM
591
CA
ASN
84
2.888
17.229
5.711
1.00
46.21


ATOM
592
CB
ASN
84
2.353
16.135
4.805
1.00
46.90


ATOM
593
CG
ASN
84
0.855
15.998
4.902
1.00
49.97


ATOM
594
OD1
ASN
84
0.271
16.163
5.985
1.00
51.10


ATOM
595
ND2
ASN
84
0.213
15.695
3.765
1.00
46.93


ATOM
596
C
ASN
84
3.133
16.649
7.097
1.00
44.37


ATOM
597
O
ASN
84
2.867
15.489
7.354
1.00
44.26


ATOM
598
N
ILE
85
3.629
17.473
8.001
1.00
38.99


ATOM
599
CA
ILE
85
3.945
17.006
9.341
1.00
33.20


ATOM
600
CB
ILE
85
4.619
18.087
10.145
1.00
28.90


ATOM
601
CG2
ILE
85
3.577
19.113
10.608
1.00
27.23


ATOM
602
CG1
ILE
85
5.455
17.418
11.242
1.00
25.20


ATOM
603
CD1
ILE
85
6.778
16.808
10.681
1.00
20.62


ATOM
604
C
ILE
85
2.826
16.453
10.207
1.00
32.57


ATOM
605
O
ILE
85
3.035
15.504
10.955
1.00
32.52


ATOM
606
N
ARG
86
1.641
17.037
10.143
1.00
35.06


ATOM
607
CA
ARG
86
0.577
16.497
10.963
1.00
38.21


ATOM
608
CB
ARG
86
−0.723
17.259
10.755
1.00
42.23


ATOM
609
CG
ARG
86
−1.836
16.354
10.257
1.00
51.70


ATOM
610
CD
ARG
86
−3.214
16.998
10.318
1.00
54.87


ATOM
611
NE
ARG
86
−4.172
16.168
11.047
1.00
53.16


ATOM
612
CZ
ARG
86
−4.345
16.211
12.362
1.00
54.60


ATOM
613
NH1
ARG
86
−3.623
17.049
13.092
1.00
54.61


ATOM
614
NH2
ARG
86
−5.237
15.419
12.944
1.00
52.09


ATOM
615
C
ARG
86
0.410
15.056
10.502
1.00
38.35


ATOM
616
O
ARG
86
0.181
14.158
11.289
1.00
37.91


ATOM
617
N
ASN
87
0.543
14.844
9.205
1.00
39.43


ATOM
618
CA
ASN
87
0.421
13.510
8.652
1.00
41.29


ATOM
619
CB
ASN
87
0.679
13.544
7.145
1.00
45.33


ATOM
620
CG
ASN
87
0.464
12.198
6.486
1.00
48.42


ATOM
621
OD1
ASN
87
0.764
12.021
5.305
1.00
48.98


ATOM
622
ND2
ASN
87
−0.065
11.239
7.245
1.00
50.03


ATOM
623
C
ASN
87
1.425
12.569
9.312
1.00
39.38


ATOM
624
O
ASN
87
1.049
11.532
9.870
1.00
40.50


ATOM
625
N
TRP
88
2.701
12.951
9.236
1.00
38.35


ATOM
626
CA
TRP
88
3.797
12.170
9.792
1.00
33.00


ATOM
627
CB
TRP
88
5.113
12.961
9.750
1.00
28.10


ATOM
628
CG
TRP
88
6.309
12.112
10.132
1.00
28.88


ATOM
629
CD2
TRP
88
6.975
12.066
11.400
1.00
23.66


ATOM
630
CE2
TRP
88
7.932
11.005
11.333
1.00
24.60


ATOM
631
CE3
TRP
88
6.859
12.808
12.589
1.00
24.28


ATOM
632
CD1
TRP
88
6.878
11.128
9.373
1.00
28.94


ATOM
633
NE1
TRP
88
7.850
10.452
10.085
1.00
22.39


ATOM
634
CZ2
TRP
88
8.765
10.672
12.416
1.00
23.76


ATOM
635
CZ3
TRP
88
7.697
12.478
13.675
1.00
25.97


ATOM
636
CH2
TRP
88
8.636
11.413
13.572
1.00
24.75


ATOM
637
C
TRP
88
3.509
11.800
11.228
1.00
33.22


ATOM
638
O
TRP
88
3.827
10.697
11.681
1.00
34.17


ATOM
639
N
LEU
89
2.919
12.731
11.957
1.00
33.69


ATOM
640
CA
LEU
89
2.629
12.450
13.334
1.00
35.69


ATOM
641
CB
LEU
89
2.199
13.726
14.056
1.00
34.51


ATOM
642
CG
LEU
89
3.267
14.770
14.425
1.00
31.52


ATOM
643
CD1
LEU
89
2.615
15.814
15.303
1.00
31.01


ATOM
644
CD2
LEU
89
4.415
14.153
15.183
1.00
27.75


ATOM
645
C
LEU
89
1.570
11.372
13.464
1.00
37.12


ATOM
646
O
LEU
89
1.710
10.463
14.264
1.00
42.41


ATOM
647
N
THR
90
0.513
11.444
12.676
1.00
35.52


ATOM
648
CA
THR
90
−0.531
10.444
12.799
1.00
33.89


ATOM
649
CB
THR
90
−1.687
10.772
11.895
1.00
32.79


ATOM
650
OG1
THR
90
−1.228
10.778
10.538
1.00
29.17


ATOM
651
CG2
THR
90
−2.254
12.129
12.274
1.00
31.57


ATOM
652
C
THR
90
−0.053
9.039
12.484
1.00
34.21


ATOM
653
O
THR
90
−0.640
8.065
12.958
1.00
34.70


ATOM
654
N
ASN
91
1.009
8.933
11.694
1.00
33.44


ATOM
655
CA
ASN
91
1.540
7.628
11.326
1.00
34.05


ATOM
656
CB
ASN
91
2.364
7.747
10.067
1.00
34.95


ATOM
657
CG
ASN
91
1.503
7.962
8.866
1.00
40.50


ATOM
658
OD1
ASN
91
1.972
8.382
7.816
1.00
44.74


ATOM
659
ND2
ASN
91
0.213
7.666
9.011
1.00
45.23


ATOM
660
C
ASN
91
2.354
6.954
12.389
1.00
33.80


ATOM
661
O
ASN
91
2.441
5.731
12.403
1.00
34.95


ATOM
662
N
LEU
92
2.945
7.751
13.275
1.00
34.11


ATOM
663
CA
LEU
92
3.774
7.242
14.370
1.00
34.02


ATOM
664
CB
LEU
92
2.956
6.320
15.281
1.00
33.05


ATOM
665
CG
LEU
92
1.686
7.011
15.761
1.00
31.66


ATOM
666
CD1
LEU
92
0.976
6.160
16.793
1.00
28.13


ATOM
667
CD2
LEU
92
2.073
8.343
16.363
1.00
34.00


ATOM
668
C
LEU
92
5.005
6.488
13.878
1.00
35.56


ATOM
669
O
LEU
92
5.248
5.342
14.288
1.00
34.71


ATOM
670
N
ASP
93
5.774
7.139
13.014
1.00
36.76


ATOM
671
CA
ASP
93
6.973
6.547
12.451
1.00
37.90


ATOM
672
CB
ASP
93
7.515
7.500
11.393
1.00
38.96


ATOM
673
CG
ASP
93
8.548
6.850
10.505
1.00
42.87


ATOM
674
OD1
ASP
93
9.435
6.144
11.044
1.00
43.52


ATOM
675
OD2
ASP
93
8.474
7.044
9.266
1.00
41.91


ATOM
676
C
ASP
93
8.016
6.325
13.555
1.00
38.75


ATOM
677
O
ASP
93
8.795
7.234
13.849
1.00
38.67


ATOM
678
N
PHE
94
8.052
5.131
14.146
1.00
37.65


ATOM
679
CA
PHE
94
9.001
4.886
15.217
1.00
36.97


ATOM
680
CB
PHE
94
8.246
4.562
16.488
1.00
33.98


ATOM
681
CG
PHE
94
7.409
5.684
16.988
1.00
36.52


ATOM
682
CD1
PHE
94
6.436
5.455
17.943
1.00
34.84


ATOM
683
CD2
PHE
94
7.621
6.981
16.537
1.00
37.51


ATOM
684
CE1
PHE
94
5.681
6.496
18.450
1.00
36.25


ATOM
685
CE2
PHE
94
6.874
8.046
17.032
1.00
39.25


ATOM
686
CZ
PHE
94
5.894
7.800
18.002
1.00
39.66


ATOM
687
C
PHE
94
10.042
3.804
14.992
1.00
35.93


ATOM
688
O
PHE
94
11.111
3.828
15.619
1.00
34.66


ATOM
689
N
ASP
95
9.755
2.861
14.110
1.00
33.05


ATOM
690
CA
ASP
95
10.693
1.789
13.893
1.00
32.72


ATOM
691
CB
ASP
95
10.241
1.010
12.705
1.00
33.93


ATOM
692
CG
ASP
95
8.985
0.249
13.001
1.00
38.39


ATOM
693
OD1
ASP
95
8.254
0.678
13.919
1.00
36.80


ATOM
694
OD2
ASP
95
8.719
−0.770
12.331
1.00
38.25


ATOM
695
C
ASP
95
12.137
2.191
13.759
1.00
33.61


ATOM
696
O
ASP
95
12.480
3.217
13.188
1.00
32.88


ATOM
697
N
GLN
96
13.004
1.368
14.311
1.00
32.68


ATOM
698
CA
GLN
96
14.394
1.698
14.224
1.00
33.14


ATOM
699
CB
GLN
96
14.902
2.281
15.537
1.00
31.37


ATOM
700
CG
GLN
96
15.216
1.274
16.638
1.00
32.76


ATOM
701
CD
GLN
96
15.964
1.910
17.834
1.00
33.37


ATOM
702
OE1
GLN
96
15.507
2.895
18.410
1.00
29.23


ATOM
703
NE2
GLN
96
17.108
1.338
18.203
1.00
32.04


ATOM
704
C
GLN
96
15.293
0.574
13.808
1.00
35.47


ATOM
705
O
GLN
96
15.246
−0.536
14.324
1.00
32.06


ATOM
706
N
ASP
97
16.116
0.904
12.830
1.00
37.28


ATOM
707
CA
ASP
97
17.110
0.002
12.296
1.00
39.67


ATOM
708
CB
ASP
97
17.446
0.371
10.858
1.00
39.54


ATOM
709
CG
ASP
97
16.723
−0.484
9.871
1.00
42.24


ATOM
710
OD1
ASP
97
16.978
−0.344
8.656
1.00
43.67


ATOM
711
OD2
ASP
97
15.897
−1.305
10.318
1.00
48.30


ATOM
712
C
ASP
97
18.369
0.129
13.121
1.00
39.69


ATOM
713
O
ASP
97
18.495
1.016
13.964
1.00
41.13


ATOM
714
N
GLU
98
19.305
−0.764
12.859
1.00
37.69


ATOM
715
CA
GLU
98
20.550
−0.728
13.566
1.00
36.93


ATOM
716
CB
GLU
98
21.158
−2.108
13.605
1.00
39.43


ATOM
717
CG
GLU
98
20.107
−3.147
13.842
1.00
45.29


ATOM
718
CD
GLU
98
20.688
−4.508
14.065
1.00
50.89


ATOM
719
OE1
GLU
98
19.909
−5.488
14.117
1.00
52.97


ATOM
720
OE2
GLU
98
21.925
−4.597
14.191
1.00
54.27


ATOM
721
C
GLU
98
21.418
0.206
12.765
1.00
33.23


ATOM
722
O
GLU
98
21.154
0.454
11.584
1.00
32.06


ATOM
723
N
CYS
99
22.450
0.743
13.400
1.00
32.71


ATOM
724
CA
CYS
99
23.351
1.665
12.722
1.00
34.26


ATOM
725
C
CYS
99
24.782
1.212
13.008
1.00
34.77


ATOM
726
O
CYS
99
25.023
0.504
13.991
1.00
34.87


ATOM
727
CB
CYS
99
23.106
3.078
13.232
1.00
34.11


ATOM
728
SG
CYS
99
24.557
3.884
13.952
1.00
42.37


ATOM
729
N
SER
100
25.729
1.587
12.153
1.00
36.04


ATOM
730
CA
SER
100
27.114
1.170
12.362
1.00
35.94


ATOM
731
CB
SER
100
27.615
0.358
11.161
1.00
34.65


ATOM
732
OG
SER
100
27.789
1.156
9.992
1.00
36.00


ATOM
733
C
SER
100
28.042
2.355
12.599
1.00
38.47


ATOM
734
O
SER
100
29.095
2.473
11.960
1.00
41.79


ATOM
735
N
LEU
101
27.653
3.231
13.518
1.00
37.61


ATOM
736
CA
LEU
101
28.451
4.405
13.822
1.00
36.68


ATOM
737
CB
LEU
101
27.554
5.635
13.906
1.00
37.98


ATOM
738
CG
LEU
101
27.063
6.258
12.595
1.00
37.48


ATOM
739
CD1
LEU
101
25.893
7.176
12.923
1.00
36.78


ATOM
740
CD2
LEU
101
28.187
7.031
11.888
1.00
37.90


ATOM
741
C
LEU
101
29.163
4.187
15.145
1.00
34.88


ATOM
742
O
LEU
101
30.266
4.728
15.380
1.00
32.30


ATOM
743
N
THR
102
28.527
3.388
15.999
1.00
33.47


ATOM
744
CA
THR
102
29.081
3.077
17.302
1.00
37.75


ATOM
745
CB
THR
102
28.696
4.148
18.342
1.00
37.45


ATOM
746
OG1
THR
102
29.294
5.394
17.975
1.00
42.24


ATOM
747
CG2
THR
102
29.187
3.760
19.748
1.00
37.29


ATOM
748
C
THR
102
28.526
1.738
17.737
1.00
39.39


ATOM
749
O
THR
102
27.515
1.267
17.189
1.00
43.35


ATOM
750
N
SER
103
29.196
1.127
18.708
1.00
39.79


ATOM
751
CA
SER
103
28.766
−0.149
19.226
1.00
41.28


ATOM
752
CB
SER
103
29.656
−0.555
20.386
1.00
42.67


ATOM
753
OG
SER
103
29.204
−1.767
20.957
1.00
45.02


ATOM
754
C
SER
103
27.326
−0.085
19.708
1.00
39.98


ATOM
755
O
SER
103
26.935
0.866
20.384
1.00
41.43


ATOM
756
N
GLY
104
26.544
−1.104
19.366
1.00
38.48


ATOM
757
CA
GLY
104
25.156
−1.144
19.796
1.00
38.43


ATOM
758
C
GLY
104
24.331
0.069
19.411
1.00
36.76


ATOM
759
O
GLY
104
23.406
0.449
20.137
1.00
34.83


ATOM
760
N
CYS
105
24.652
0.649
18.254
1.00
36.77


ATOM
761
CA
CYS
105
23.970
1.838
17.733
1.00
35.81


ATOM
762
C
CYS
105
22.632
1.565
17.036
1.00
34.27


ATOM
763
O
CYS
105
22.562
0.759
16.086
1.00
35.72


ATOM
764
CB
CYS
105
24.904
2.575
16.759
1.00
37.31


ATOM
765
SG
CYS
105
24.192
4.053
15.956
1.00
41.61


ATOM
766
N
GLY
106
21.580
2.241
17.513
1.00
32.57


ATOM
767
CA
GLY
106
20.264
2.088
16.918
1.00
29.70


ATOM
768
C
GLY
106
19.841
3.398
16.282
1.00
28.51


ATOM
769
O
GLY
106
20.227
4.469
16.751
1.00
24.97


ATOM
770
N
VAL
107
19.043
3.323
15.222
1.00
27.72


ATOM
771
CA
VAL
107
18.612
4.522
14.529
1.00
25.88


ATOM
772
CB
VAL
107
19.608
4.900
13.424
1.00
24.77


ATOM
773
CG1
VAL
107
19.527
3.891
12.307
1.00
24.43


ATOM
774
CG2
VAL
107
19.328
6.308
12.927
1.00
27.27


ATOM
775
C
VAL
107
17.240
4.345
13.906
1.00
26.16


ATOM
776
O
VAL
107
16.821
3.226
13.586
1.00
26.91


ATOM
777
N
HIS
108
16.561
5.481
13.751
1.00
22.68


ATOM
778
CA
HIS
108
15.239
5.558
13.176
1.00
21.88


ATOM
779
CB
HIS
108
14.657
6.930
13.459
1.00
18.95


ATOM
780
CG
HIS
108
13.354
7.185
12.773
1.00
18.23


ATOM
781
CD2
HIS
108
12.114
7.404
13.274
1.00
16.34


ATOM
782
ND1
HIS
108
13.233
7.242
11.399
1.00
15.06


ATOM
783
CE1
HIS
108
11.971
7.486
11.084
1.00
16.78


ATOM
784
NE2
HIS
108
11.272
7.588
12.203
1.00
18.04


ATOM
785
C
HIS
108
15.336
5.338
11.687
1.00
24.47


ATOM
786
O
HIS
108
15.754
6.225
10.945
1.00
28.53


ATOM
787
N
SER
109
14.933
4.151
11.259
1.00
26.53


ATOM
788
CA
SER
109
14.971
3.767
9.846
1.00
26.33


ATOM
789
CB
SER
109
13.901
2.718
9.596
1.00
25.81


ATOM
790
OG
SER
109
14.122
1.617
10.464
1.00
30.40


ATOM
791
C
SER
109
14.800
4.902
8.855
1.00
24.40


ATOM
792
O
SER
109
15.747
5.278
8.155
1.00
23.43


ATOM
793
N
GLY
110
13.575
5.416
8.805
1.00
23.31


ATOM
794
CA
GLY
110
13.244
6.506
7.921
1.00
25.96


ATOM
795
C
GLY
110
14.392
7.453
7.742
1.00
26.60


ATOM
796
O
GLY
110
15.010
7.515
6.689
1.00
27.43


ATOM
797
N
PHE
111
14.693
8.183
8.798
1.00
24.09


ATOM
798
CA
PHE
111
15.773
9.159
8.742
1.00
23.35


ATOM
799
CB
PHE
111
16.105
9.663
10.139
1.00
22.88


ATOM
800
CG
PHE
111
14.912
10.175
10.893
1.00
20.11


ATOM
801
CD1
PHE
111
13.822
10.729
10.213
1.00
16.75


ATOM
802
CD2
PHE
111
14.885
10.152
12.287
1.00
17.31


ATOM
803
CE1
PHE
111
12.731
11.251
10.926
1.00
17.67


ATOM
804
CE2
PHE
111
13.797
10.676
12.986
1.00
19.96


ATOM
805
CZ
PHE
111
12.731
11.221
12.308
1.00
19.28


ATOM
806
C
PHE
111
17.031
8.596
8.086
1.00
24.50


ATOM
807
O
PHE
111
17.600
9.218
7.188
1.00
23.12


ATOM
808
N
GLN
112
17.452
7.407
8.501
1.00
24.02


ATOM
809
CA
GLN
112
18.649
6.815
7.921
1.00
26.60


ATOM
810
CB
GLN
112
19.051
5.555
8.677
1.00
26.33


ATOM
811
CG
GLN
112
20.212
4.850
8.021
1.00
26.25


ATOM
812
CD
GLN
112
21.011
4.000
8.981
1.00
29.74


ATOM
813
OE1
GLN
112
21.443
2.894
8.639
1.00
35.31


ATOM
814
NE2
GLN
112
21.243
4.519
10.180
1.00
34.04


ATOM
815
C
GLN
112
18.516
6.488
6.435
1.00
27.78


ATOM
816
O
GLN
112
19.436
6.745
5.647
1.00
29.45


ATOM
817
N
ASN
113
17.371
5.938
6.041
1.00
28.08


ATOM
818
CA
ASN
113
17.175
5.596
4.639
1.00
28.43


ATOM
819
CB
ASN
113
15.839
4.901
4.424
1.00
28.41


ATOM
820
CG
ASN
113
15.871
3.451
4.863
1.00
30.04


ATOM
821
OD1
ASN
113
16.792
2.700
4.496
1.00
30.46


ATOM
822
ND2
ASN
113
14.865
3.040
5.643
1.00
28.40


ATOM
823
C
ASN
113
17.233
6.841
3.803
1.00
28.99


ATOM
824
O
ASN
113
17.865
6.880
2.759
1.00
33.51


ATOM
825
N
ALA
114
16.554
7.869
4.279
1.00
28.45


ATOM
826
CA
ALA
114
16.527
9.145
3.583
1.00
27.49


ATOM
827
CB
ALA
114
15.801
10.171
4.405
1.00
26.03


ATOM
828
C
ALA
114
17.950
9.609
3.343
1.00
27.35


ATOM
829
O
ALA
114
18.299
10.023
2.241
1.00
29.80


ATOM
830
N
TRP
115
18.767
9.532
4.391
1.00
23.62


ATOM
831
CA
TRP
115
20.155
9.952
4.323
1.00
21.51


ATOM
832
CB
TRP
115
20.875
9.730
5.652
1.00
21.64


ATOM
833
CG
TRP
115
22.372
9.888
5.533
1.00
20.35


ATOM
834
CD2
TRP
115
23.087
10.970
4.903
1.00
19.79


ATOM
835
CE2
TRP
115
24.474
10.687
5.036
1.00
18.85


ATOM
836
CE3
TRP
115
22.691
12.146
4.247
1.00
17.80


ATOM
837
CD1
TRP
115
23.321
9.029
5.998
1.00
20.04


ATOM
838
NE1
TRP
115
24.593
9.500
5.700
1.00
17.55


ATOM
839
CZ2
TRP
115
25.456
11.537
4.543
1.00
17.95


ATOM
840
CZ3
TRP
115
23.672
12.994
3.756
1.00
18.83


ATOM
841
CH2
TRP
115
25.042
12.681
3.909
1.00
21.55


ATOM
842
C
TRP
115
20.868
9.144
3.295
1.00
23.16


ATOM
843
O
TRP
115
21.623
9.663
2.471
1.00
27.46


ATOM
844
N
ASN
116
20.658
7.846
3.386
1.00
23.42


ATOM
845
CA
ASN
116
21.304
6.953
2.465
1.00
24.21


ATOM
846
CB
ASN
116
21.030
5.516
2.849
1.00
24.03


ATOM
847
CG
ASN
116
21.676
5.150
4.132
1.00
29.29


ATOM
848
OD1
ASN
116
22.717
5.687
4.481
1.00
31.97


ATOM
849
ND2
ASN
116
21.080
4.218
4.844
1.00
33.01


ATOM
850
C
ASN
116
20.836
7.172
1.052
1.00
23.56


ATOM
851
O
ASN
116
21.567
6.937
0.093
1.00
22.94


ATOM
852
N
GLU
117
19.604
7.614
0.897
1.00
20.73


ATOM
853
CA
GLU
117
19.146
7.772
−0.454
1.00
22.57


ATOM
854
CB
GLU
117
17.640
8.002
−0.509
1.00
21.79


ATOM
855
CG
GLU
117
17.137
7.876
−1.925
1.00
27.82


ATOM
856
CD
GLU
117
15.642
7.790
−2.017
1.00
28.18


ATOM
857
OE1
GLU
117
15.136
7.453
−3.110
1.00
28.56


ATOM
858
OE2
GLU
117
14.979
8.066
−1.000
1.00
27.41


ATOM
859
C
GLU
117
19.849
8.891
−1.180
1.00
22.98


ATOM
860
O
GLU
117
19.907
8.890
−2.413
1.00
22.77


ATOM
861
N
ILE
118
20.433
9.812
−0.421
1.00
24.29


ATOM
862
CA
ILE
118
21.056
10.989
−1.017
1.00
24.36


ATOM
863
CB
ILE
118
20.160
12.210
−0.739
1.00
23.50


ATOM
864
CG2
ILE
118
18.679
11.913
−1.178
1.00
17.72


ATOM
865
CG1
ILE
118
20.229
12.521
0.768
1.00
23.92


ATOM
866
CD1
ILE
118
19.649
13.873
1.188
1.00
24.45


ATOM
867
C
ILE
118
22.470
11.302
−0.500
1.00
27.82


ATOM
868
O
ILE
118
23.083
12.301
−0.893
1.00
27.76


ATOM
869
N
SER
119
22.989
10.455
0.384
1.00
28.69


ATOM
870
CA
SER
119
24.321
10.676
0.972
1.00
31.82


ATOM
871
CB
SER
119
24.707
9.487
1.842
1.00
31.79


ATOM
872
OG
SER
119
24.796
8.321
1.064
1.00
31.33


ATOM
873
C
SER
119
25.459
10.952
−0.015
1.00
31.63


ATOM
874
O
SER
119
26.269
11.845
0.191
1.00
32.58


ATOM
875
N
ALA
120
25.508
10.187
−1.095
1.00
30.64


ATOM
876
CA
ALA
120
26.563
10.324
−2.104
1.00
31.31


ATOM
877
CB
ALA
120
26.414
9.246
−3.178
1.00
32.77


ATOM
878
C
ALA
120
26.633
11.678
−2.769
1.00
30.92


ATOM
879
O
ALA
120
27.681
12.311
−2.810
1.00
32.49


ATOM
880
N
ALA
121
25.499
12.115
−3.290
1.00
28.48


ATOM
881
CA
ALA
121
25.396
13.411
−3.954
1.00
23.95


ATOM
882
CB
ALA
121
24.007
13.605
−4.511
1.00
22.70


ATOM
883
C
ALA
121
25.681
14.490
−2.958
1.00
23.32


ATOM
884
O
ALA
121
26.352
15.466
−3.250
1.00
20.59


ATOM
885
N
ALA
122
25.151
14.282
−1.765
1.00
23.65


ATOM
886
CA
ALA
122
25.323
15.216
−0.668
1.00
25.49


ATOM
887
CB
ALA
122
24.650
14.670
0.571
1.00
25.06


ATOM
888
C
ALA
122
26.803
15.400
−0.407
1.00
26.41


ATOM
889
O
ALA
122
27.327
16.507
−0.423
1.00
24.84


ATOM
890
N
THR
123
27.481
14.285
−0.194
1.00
24.70


ATOM
891
CA
THR
123
28.904
14.297
0.068
1.00
26.60


ATOM
892
CB
THR
123
29.406
12.912
0.185
1.00
26.27


ATOM
893
OG1
THR
123
28.622
12.238
1.168
1.00
28.89


ATOM
894
CG2
THR
123
30.873
12.916
0.569
1.00
23.09


ATOM
895
C
THR
123
29.748
14.970
−0.989
1.00
29.08


ATOM
896
O
THR
123
30.545
15.869
−0.698
1.00
29.71


ATOM
897
N
ALA
124
29.591
14.494
−2.213
1.00
29.51


ATOM
898
CA
ALA
124
30.335
15.033
−3.317
1.00
30.04


ATOM
899
CB
ALA
124
29.850
14.428
−4.590
1.00
28.86


ATOM
900
C
ALA
124
30.214
16.536
−3.384
1.00
31.99


ATOM
901
O
ALA
124
31.229
17.231
−3.494
1.00
32.89


ATOM
902
N
ALA
125
28.978
17.032
−3.324
1.00
32.86


ATOM
903
CA
ALA
125
28.732
18.470
−3.390
1.00
32.71


ATOM
904
CB
ALA
125
27.257
18.762
−3.214
1.00
29.72


ATOM
905
C
ALA
125
29.548
19.196
−2.316
1.00
36.27


ATOM
906
O
ALA
125
30.168
20.230
−2.585
1.00
38.52


ATOM
907
N
VAL
126
29.556
18.648
−1.106
1.00
37.28


ATOM
908
CA
VAL
126
30.299
19.247
−0.015
1.00
37.15


ATOM
909
CB
VAL
126
30.080
18.467
1.271
1.00
35.30


ATOM
910
CG1
VAL
126
30.905
19.081
2.376
1.00
31.71


ATOM
911
CG2
VAL
126
28.620
18.467
1.628
1.00
37.20


ATOM
912
C
VAL
126
31.788
19.281
−0.316
1.00
39.89


ATOM
913
O
VAL
126
32.500
20.211
0.078
1.00
39.87


ATOM
914
N
ALA
127
32.263
18.246
−0.997
1.00
41.11


ATOM
915
CA
ALA
127
33.666
18.176
−1.340
1.00
41.91


ATOM
916
CB
ALA
127
33.964
16.836
−1.939
1.00
38.95


ATOM
917
C
ALA
127
33.971
19.272
−2.336
1.00
42.35


ATOM
918
O
ALA
127
34.782
20.147
−2.112
1.00
43.45


ATOM
919
N
LYS
128
33.270
19.189
−3.449
1.00
42.74


ATOM
920
CA
LYS
128
33.376
20.124
−4.552
1.00
45.06


ATOM
921
CB
LYS
128
32.173
19.946
−5.493
1.00
46.03


ATOM
922
CG
LYS
128
32.162
20.899
−6.664
1.00
45.30


ATOM
923
CD
LYS
128
31.018
20.569
−7.617
1.00
43.76


ATOM
924
CE
LYS
128
31.086
21.435
−8.866
1.00
42.90


ATOM
925
NZ
LYS
128
30.055
21.041
−9.865
1.00
47.44


ATOM
926
C
LYS
128
33.445
21.580
−4.124
1.00
47.18


ATOM
927
O
LYS
128
34.218
22.365
−4.688
1.00
48.16


ATOM
928
N
ALA
129
32.619
21.947
−3.149
1.00
46.89


ATOM
929
CA
ALA
129
32.568
23.327
−2.681
1.00
48.47


ATOM
930
CB
ALA
129
31.176
23.649
−2.202
1.00
50.70


ATOM
931
C
ALA
129
33.556
23.554
−1.564
1.00
48.47


ATOM
932
O
ALA
129
33.724
24.664
−1.069
1.00
49.52


ATOM
933
N
ARG
130
34.216
22.481
−1.173
1.00
47.79


ATOM
934
CA
ARG
130
35.177
22.533
−0.091
1.00
47.18


ATOM
935
CB
ARG
130
35.056
21.238
0.708
1.00
46.27


ATOM
936
CG
ARG
130
35.996
21.101
1.866
1.00
45.34


ATOM
937
CD
ARG
130
35.303
21.237
3.216
1.00
45.42


ATOM
938
NE
ARG
130
36.154
20.722
4.292
1.00
46.95


ATOM
939
CZ
ARG
130
36.532
19.446
4.379
1.00
47.21


ATOM
940
NH1
ARG
130
36.125
18.578
3.455
1.00
49.67


ATOM
941
NH2
ARG
130
37.316
19.030
5.374
1.00
47.17


ATOM
942
C
ARG
130
36.569
22.695
−0.688
1.00
47.32


ATOM
943
O
ARG
130
37.481
23.265
−0.085
1.00
46.83


ATOM
944
N
LYS
131
36.699
22.182
−1.900
1.00
47.02


ATOM
945
CA
LYS
131
37.927
22.234
−2.665
1.00
47.60


ATOM
946
CB
LYS
131
37.898
21.096
−3.683
1.00
48.24


ATOM
947
CG
LYS
131
38.905
21.171
−4.797
1.00
49.97


ATOM
948
CD
LYS
131
38.712
20.006
−5.773
1.00
51.12


ATOM
949
CE
LYS
131
39.616
20.100
−7.012
1.00
54.18


ATOM
950
NZ
LYS
131
41.091
20.138
−6.750
1.00
52.50


ATOM
951
C
LYS
131
37.935
23.590
−3.358
1.00
46.50


ATOM
952
O
LYS
131
38.974
24.205
−3.565
1.00
45.65


ATOM
953
N
ALA
132
36.745
24.057
−3.703
1.00
46.55


ATOM
954
CA
ALA
132
36.596
25.338
−4.366
1.00
46.83


ATOM
955
CB
ALA
132
35.250
25.412
−5.040
1.00
46.52


ATOM
956
C
ALA
132
36.734
26.481
−3.392
1.00
47.29


ATOM
957
O
ALA
132
37.140
27.564
−3.742
1.00
48.72


ATOM
958
N
ASN
133
36.393
26.237
−2.149
1.00
47.56


ATOM
959
CA
ASN
133
36.475
27.290
−1.167
1.00
47.89


ATOM
960
CB
ASN
133
35.073
27.831
−0.904
1.00
47.13


ATOM
961
CG
ASN
133
34.379
28.258
−2.180
1.00
44.88


ATOM
962
OD1
ASN
133
34.762
29.251
−2.797
1.00
46.01


ATOM
963
ND2
ASN
133
33.365
27.501
−2.594
1.00
42.65


ATOM
964
C
ASN
133
37.088
26.709
0.084
1.00
51.35


ATOM
965
O
ASN
133
36.428
26.587
1.115
1.00
54.41


ATOM
966
N
PRO
134
38.379
26.354
0.004
1.00
52.07


ATOM
967
CD
PRO
134
39.241
26.711
−1.139
1.00
51.41


ATOM
968
CA
PRO
134
39.175
25.765
1.082
1.00
51.27


ATOM
969
CB
PRO
134
40.543
25.589
0.429
1.00
50.94


ATOM
970
CG
PRO
134
40.598
26.756
−0.500
1.00
53.24


ATOM
971
C
PRO
134
39.248
26.523
2.416
1.00
52.11


ATOM
972
O
PRO
134
39.540
25.917
3.452
1.00
54.28


ATOM
973
N
SER
135
38.995
27.829
2.417
1.00
51.79


ATOM
974
CA
SER
135
39.048
28.568
3.681
1.00
49.81


ATOM
975
CB
SER
135
39.238
30.065
3.427
1.00
48.81


ATOM
976
OG
SER
135
38.140
30.602
2.716
1.00
44.30


ATOM
977
C
SER
135
37.760
28.354
4.469
1.00
48.48


ATOM
978
O
SER
135
37.769
28.345
5.707
1.00
48.39


ATOM
979
N
PHE
136
36.660
28.178
3.734
1.00
46.17


ATOM
980
CA
PHE
136
35.320
27.980
4.295
1.00
44.62


ATOM
981
CB
PHE
136
34.335
27.829
3.135
1.00
44.25


ATOM
982
CG
PHE
136
34.154
29.083
2.324
1.00
43.96


ATOM
983
CD1
PHE
136
35.249
29.862
1.966
1.00
44.47


ATOM
984
CD2
PHE
136
32.883
29.499
1.930
1.00
45.10


ATOM
985
CE1
PHE
136
35.079
31.039
1.232
1.00
45.46


ATOM
986
CE2
PHE
136
32.707
30.675
1.195
1.00
47.14


ATOM
987
CZ
PHE
136
33.805
31.443
0.850
1.00
46.31


ATOM
988
C
PHE
136
35.167
26.799
5.266
1.00
43.26


ATOM
989
O
PHE
136
35.839
25.768
5.133
1.00
42.48


ATOM
990
N
LYS
137
34.298
26.969
6.259
1.00
42.74


ATOM
991
CA
LYS
137
34.016
25.918
7.240
1.00
45.31


ATOM
992
CB
LYS
137
33.944
26.514
8.642
1.00
47.43


ATOM
993
CG
LYS
137
33.075
27.753
8.724
1.00
50.73


ATOM
994
CD
LYS
137
33.088
28.321
10.120
1.00
54.00


ATOM
995
CE
LYS
137
32.294
29.614
10.197
1.00
56.52


ATOM
996
NZ
LYS
137
32.838
30.691
9.310
1.00
54.83


ATOM
997
C
LYS
137
32.664
25.315
6.843
1.00
43.52


ATOM
998
O
LYS
137
31.980
25.863
5.978
1.00
43.49


ATOM
999
N
VAL
138
32.271
24.207
7.467
1.00
40.21


ATOM
1000
CA
VAL
138
31.014
23.569
7.100
1.00
39.86


ATOM
1001
CB
VAL
138
31.236
22.126
6.677
1.00
39.80


ATOM
1002
CG1
VAL
138
30.044
21.660
5.858
1.00
37.32


ATOM
1003
CG2
VAL
138
32.524
21.995
5.912
1.00
38.61


ATOM
1004
C
VAL
138
29.934
23.540
8.169
1.00
38.40


ATOM
1005
O
VAL
138
30.222
23.430
9.357
1.00
39.54


ATOM
1006
N
VAL
139
28.685
23.595
7.715
1.00
36.50


ATOM
1007
CA
VAL
139
27.528
23.559
8.596
1.00
38.24


ATOM
1008
CB
VAL
139
26.933
24.956
8.791
1.00
39.41


ATOM
1009
CG1
VAL
139
25.652
24.858
9.596
1.00
38.25


ATOM
1010
CG2
VAL
139
27.942
25.850
9.487
1.00
40.77


ATOM
1011
C
VAL
139
26.437
22.642
8.051
1.00
36.49


ATOM
1012
O
VAL
139
26.124
22.650
6.866
1.00
39.45


ATOM
1013
N
SER
140
25.835
21.869
8.937
1.00
32.14


ATOM
1014
CA
SER
140
24.792
20.936
8.552
1.00
29.04


ATOM
1015
CB
SER
140
25.181
19.543
9.042
1.00
24.02


ATOM
1016
OG
SER
140
24.210
18.589
8.703
1.00
29.12


ATOM
1017
C
SER
140
23.510
21.413
9.222
1.00
28.02


ATOM
1018
O
SER
140
23.397
21.358
10.441
1.00
27.82


ATOM
1019
N
VAL
141
22.553
21.874
8.417
1.00
27.82


ATOM
1020
CA
VAL
141
21.281
22.399
8.907
1.00
30.87


ATOM
1021
CB
VAL
141
21.111
23.883
8.420
1.00
29.90


ATOM
1022
CG1
VAL
141
19.865
24.527
9.022
1.00
28.75


ATOM
1023
CG2
VAL
141
22.348
24.679
8.798
1.00
33.17


ATOM
1024
C
VAL
141
20.074
21.550
8.485
1.00
33.03


ATOM
1025
O
VAL
141
20.176
20.659
7.644
1.00
35.84


ATOM
1026
N
GLY
142
18.933
21.848
9.104
1.00
32.70


ATOM
1027
CA
GLY
142
17.686
21.152
8.838
1.00
30.09


ATOM
1028
C
GLY
142
16.645
21.396
9.923
1.00
29.65


ATOM
1029
O
GLY
142
16.960
21.411
11.111
1.00
31.37


ATOM
1030
N
HIS
143
15.399
21.590
9.496
1.00
26.39


ATOM
1031
CA
HIS
143
14.269
21.829
10.399
1.00
19.33


ATOM
1032
CB
HIS
143
13.491
23.102
10.017
1.00
19.62


ATOM
1033
CG
HIS
143
12.026
23.054
10.359
1.00
20.09


ATOM
1034
CD2
HIS
143
11.352
23.478
11.459
1.00
18.21


ATOM
1035
ND1
HIS
143
11.070
22.536
9.506
1.00
21.83


ATOM
1036
CE1
HIS
143
9.872
22.646
10.062
1.00
21.18


ATOM
1037
NE2
HIS
143
10.017
23.216
11.248
1.00
20.26


ATOM
1038
C
HIS
143
13.315
20.672
10.321
1.00
18.40


ATOM
1039
O
HIS
143
13.069
20.129
9.238
1.00
19.89


ATOM
1040
N
SER
144
12.751
20.312
11.464
1.00
17.17


ATOM
1041
CA
SER
144
11.805
19.233
11.467
1.00
16.24


ATOM
1042
CB
SER
144
10.818
19.452
10.328
1.00
13.89


ATOM
1043
OG
SER
144
9.608
18.743
10.515
1.00
21.42


ATOM
1044
C
SER
144
12.578
17.950
11.231
1.00
17.37


ATOM
1045
O
SER
144
13.698
17.746
11.721
1.00
17.35


ATOM
1046
N
LEU
145
11.965
17.085
10.448
1.00
14.63


ATOM
1047
CA
LEU
145
12.564
15.820
10.130
1.00
16.67


ATOM
1048
CB
LEU
145
11.613
14.995
9.247
1.00
14.08


ATOM
1049
CG
LEU
145
10.177
14.808
9.767
1.00
15.88


ATOM
1050
CD1
LEU
145
9.389
13.779
8.946
1.00
11.76


ATOM
1051
CD2
LEU
145
10.246
14.399
11.216
1.00
14.25


ATOM
1052
C
LEU
145
13.834
16.173
9.373
1.00
19.50


ATOM
1053
O
LEU
145
14.886
15.546
9.557
1.00
18.82


ATOM
1054
N
GLY
146
13.733
17.204
8.537
1.00
19.28


ATOM
1055
CA
GLY
146
14.882
17.635
7.770
1.00
21.26


ATOM
1056
C
GLY
146
16.006
17.826
8.753
1.00
21.58


ATOM
1057
O
GLY
146
17.161
17.608
8.433
1.00
24.44


ATOM
1058
N
GLY
147
15.657
18.254
9.962
1.00
20.38


ATOM
1059
CA
GLY
147
16.656
18.427
11.002
1.00
22.70


ATOM
1060
C
GLY
147
17.203
17.074
11.425
1.00
23.22


ATOM
1061
O
GLY
147
18.411
16.899
11.618
1.00
17.17


ATOM
1062
N
ALA
148
16.295
16.107
11.569
1.00
24.83


ATOM
1063
CA
ALA
148
16.682
14.750
11.955
1.00
26.11


ATOM
1064
CB
ALA
148
15.499
13.795
11.842
1.00
26.21


ATOM
1065
C
ALA
148
17.789
14.310
11.024
1.00
26.98


ATOM
1066
O
ALA
148
18.944
14.236
11.415
1.00
26.77


ATOM
1067
N
VAL
149
17.420
14.043
9.780
1.00
29.05


ATOM
1068
CA
VAL
149
18.370
13.642
8.754
1.00
30.78


ATOM
1069
CB
VAL
149
17.720
13.723
7.356
1.00
29.50


ATOM
1070
CG1
VAL
149
17.139
15.107
7.141
1.00
36.38


ATOM
1071
CG2
VAL
149
18.757
13.417
6.271
1.00
28.41


ATOM
1072
C
VAL
149
19.631
14.520
8.758
1.00
32.09


ATOM
1073
O
VAL
149
20.733
14.040
8.502
1.00
35.50


ATOM
1074
N
ALA
150
19.476
15.808
9.052
1.00
31.81


ATOM
1075
CA
ALA
150
20.627
16.720
9.050
1.00
31.91


ATOM
1076
CB
ALA
150
20.188
18.142
9.407
1.00
31.19


ATOM
1077
C
ALA
150
21.692
16.249
10.029
1.00
31.31


ATOM
1078
O
ALA
150
22.876
16.480
9.838
1.00
31.99


ATOM
1079
N
THR
151
21.262
15.571
11.075
1.00
31.04


ATOM
1080
CA
THR
151
22.188
15.092
12.070
1.00
30.45


ATOM
1081
CB
THR
151
21.442
14.612
13.316
1.00
31.26


ATOM
1082
OG1
THR
151
20.654
15.683
13.847
1.00
35.05


ATOM
1083
CG2
THR
151
22.430
14.179
14.369
1.00
31.46


ATOM
1084
C
THR
151
23.070
13.961
11.573
1.00
30.95


ATOM
1085
O
THR
151
24.291
14.020
11.709
1.00
30.80


ATOM
1086
N
LEU
152
22.459
12.917
11.024
1.00
30.43


ATOM
1087
CA
LEU
152
23.224
11.771
10.522
1.00
31.80


ATOM
1088
CB
LEU
152
22.307
10.750
9.829
1.00
25.27


ATOM
1089
CG
LEU
152
21.276
10.058
10.721
1.00
19.74


ATOM
1090
CD1
LEU
152
20.542
8.952
10.000
1.00
19.66


ATOM
1091
CD2
LEU
152
22.004
9.488
11.878
1.00
19.81


ATOM
1092
C
LEU
152
24.246
12.282
9.527
1.00
33.94


ATOM
1093
O
LEU
152
25.437
11.976
9.593
1.00
35.31


ATOM
1094
N
ALA
153
23.754
13.101
8.617
1.00
33.85


ATOM
1095
CA
ALA
153
24.590
13.692
7.597
1.00
33.67


ATOM
1096
CB
ALA
153
23.795
14.716
6.823
1.00
36.30


ATOM
1097
C
ALA
153
25.798
14.339
8.247
1.00
32.20


ATOM
1098
O
ALA
153
26.896
14.239
7.745
1.00
33.42


ATOM
1099
N
GLY
154
25.596
14.994
9.381
1.00
33.09


ATOM
1100
CA
GLY
154
26.712
15.630
10.048
1.00
33.71


ATOM
1101
C
GLY
154
27.637
14.570
10.590
1.00
34.42


ATOM
1102
O
GLY
154
28.830
14.546
10.293
1.00
34.11


ATOM
1103
N
ALA
155
27.065
13.682
11.394
1.00
35.16


ATOM
1104
CA
ALA
155
27.815
12.602
12.020
1.00
37.79


ATOM
1105
CB
ALA
155
26.855
11.612
12.635
1.00
36.39


ATOM
1106
C
ALA
155
28.685
11.902
10.991
1.00
37.41


ATOM
1107
O
ALA
155
29.902
11.805
11.120
1.00
36.20


ATOM
1108
N
ASN
156
28.030
11.406
9.960
1.00
37.07


ATOM
1109
CA
ASN
156
28.730
10.721
8.917
1.00
36.66


ATOM
1110
CB
ASN
156
27.715
10.144
7.937
1.00
35.94


ATOM
1111
CG
ASN
156
27.170
8.813
8.410
1.00
37.19


ATOM
1112
OD1
ASN
156
27.823
7.782
8.257
1.00
41.36


ATOM
1113
ND2
ASN
156
25.986
8.828
9.007
1.00
38.22


ATOM
1114
C
ASN
156
29.732
11.640
8.235
1.00
38.00


ATOM
1115
O
ASN
156
30.905
11.295
8.117
1.00
39.70


ATOM
1116
N
LEU
157
29.302
12.825
7.815
1.00
36.33


ATOM
1117
CA
LEU
157
30.231
13.721
7.125
1.00
30.00


ATOM
1118
CB
LEU
157
29.610
15.104
6.865
1.00
26.41


ATOM
1119
CG
LEU
157
29.181
15.474
5.424
1.00
26.33


ATOM
1120
CD1
LEU
157
30.071
14.777
4.412
1.00
24.41


ATOM
1121
CD2
LEU
157
27.761
15.069
5.167
1.00
26.08


ATOM
1122
C
LEU
157
31.477
13.857
7.973
1.00
30.24


ATOM
1123
O
LEU
157
32.600
13.744
7.491
1.00
29.89


ATOM
1124
N
ARG
158
31.255
14.058
9.261
1.00
29.77


ATOM
1125
CA
ARG
158
32.345
14.195
10.194
1.00
32.79


ATOM
1126
CB
ARG
158
31.820
14.192
11.645
1.00
33.07


ATOM
1127
CG
ARG
158
30.861
15.331
12.023
1.00
32.85


ATOM
1128
CD
ARG
158
31.088
15.717
13.489
1.00
35.95


ATOM
1129
NE
ARG
158
29.886
16.070
14.260
1.00
38.94


ATOM
1130
CZ
ARG
158
29.346
17.287
14.342
1.00
39.79


ATOM
1131
NH1
ARG
158
28.259
17.469
15.082
1.00
32.39


ATOM
1132
NH2
ARG
158
29.875
18.323
13.686
1.00
40.89


ATOM
1133
C
ARG
158
33.320
13.037
9.998
1.00
35.98


ATOM
1134
O
ARG
158
34.485
13.250
9.709
1.00
40.19


ATOM
1135
N
ILE
159
32.835
11.805
10.136
1.00
36.99


ATOM
1136
CA
ILE
159
33.708
10.632
10.014
1.00
36.27


ATOM
1137
CB
ILE
159
32.963
9.267
10.118
1.00
36.24


ATOM
1138
CG2
ILE
159
32.042
9.259
11.325
1.00
30.70


ATOM
1139
CG1
ILE
159
32.157
8.994
8.855
1.00
41.45


ATOM
1140
CD1
ILE
159
31.199
7.805
9.010
1.00
48.56


ATOM
1141
C
ILE
159
34.394
10.661
8.692
1.00
37.10


ATOM
1142
O
ILE
159
35.466
10.073
8.528
1.00
39.04


ATOM
1143
N
GLY
160
33.759
11.341
7.744
1.00
39.77


ATOM
1144
CA
GLY
160
34.332
11.467
6.421
1.00
45.59


ATOM
1145
C
GLY
160
35.558
12.367
6.464
1.00
49.14


ATOM
1146
O
GLY
160
36.290
12.512
5.491
1.00
49.04


ATOM
1147
N
GLY
161
35.797
12.974
7.614
1.00
49.77


ATOM
1148
CA
GLY
161
36.940
13.847
7.732
1.00
49.94


ATOM
1149
C
GLY
161
36.429
15.241
7.928
1.00
48.63


ATOM
1150
O
GLY
161
36.604
15.837
8.982
1.00
51.78


ATOM
1151
N
THR
162
35.758
15.752
6.914
1.00
45.61


ATOM
1152
CA
THR
162
35.227
17.098
6.992
1.00
43.42


ATOM
1153
CB
THR
162
34.318
17.391
5.828
1.00
43.68


ATOM
1154
OG1
THR
162
33.204
18.157
6.298
1.00
46.49


ATOM
1155
CG2
THR
162
33.854
16.105
5.195
1.00
44.15


ATOM
1156
C
THR
162
34.454
17.394
8.273
1.00
42.04


ATOM
1157
O
THR
162
33.408
16.801
8.550
1.00
40.79


ATOM
1158
N
PRO
163
34.988
18.311
9.082
1.00
41.64


ATOM
1159
CD
PRO
163
36.376
18.797
8.979
1.00
39.68


ATOM
1160
CA
PRO
163
34.380
18.718
10.346
1.00
42.23


ATOM
1161
CB
PRO
163
35.560
19.279
11.134
1.00
43.75


ATOM
1162
CG
PRO
163
36.438
19.839
10.054
1.00
44.13


ATOM
1163
C
PRO
163
33.229
19.703
10.165
1.00
40.16


ATOM
1164
O
PRO
163
33.223
20.565
9.275
1.00
37.11


ATOM
1165
N
LEU
164
32.267
19.559
11.067
1.00
40.42


ATOM
1166
CA
LEU
164
31.031
20.322
11.051
1.00
38.72


ATOM
1167
CB
LEU
164
29.883
19.434
10.632
1.00
35.75


ATOM
1168
CG
LEU
164
29.691
19.202
9.166
1.00
33.13


ATOM
1169
CD1
LEU
164
28.838
17.977
9.033
1.00
37.44


ATOM
1170
CD2
LEU
164
29.047
20.412
8.519
1.00
29.26


ATOM
1171
C
LEU
164
30.579
20.917
12.349
1.00
38.94


ATOM
1172
O
LEU
164
31.271
20.888
13.368
1.00
42.10


ATOM
1173
N
ASP
165
29.346
21.407
12.258
1.00
40.82


ATOM
1174
CA
ASP
165
28.593
22.013
13.326
1.00
39.97


ATOM
1175
CB
ASP
165
28.921
23.491
13.494
1.00
41.99


ATOM
1176
CG
ASP
165
29.864
23.743
14.638
1.00
45.08


ATOM
1177
OD1
ASP
165
29.907
22.907
15.571
1.00
47.09


ATOM
1178
OD2
ASP
165
30.550
24.786
14.610
1.00
46.42


ATOM
1179
C
ASP
165
27.193
21.882
12.776
1.00
38.60


ATOM
1180
O
ASP
165
26.868
22.451
11.732
1.00
40.54


ATOM
1181
N
ILE
166
26.368
21.124
13.486
1.00
33.75


ATOM
1182
CA
ILE
166
24.983
20.891
13.096
1.00
30.12


ATOM
1183
CB
ILE
166
24.577
19.449
13.398
1.00
27.81


ATOM
1184
CG2
ILE
166
23.165
19.180
12.900
1.00
28.09


ATOM
1185
CG1
ILE
166
25.580
18.499
12.731
1.00
27.25


ATOM
1186
CD1
ILE
166
25.524
17.076
13.276
1.00
16.32


ATOM
1187
C
ILE
166
24.012
21.806
13.813
1.00
28.19


ATOM
1188
O
ILE
166
24.072
21.950
15.037
1.00
28.70


ATOM
1189
N
TYR
167
23.120
22.409
13.030
1.00
26.22


ATOM
1190
CA
TYR
167
22.085
23.310
13.529
1.00
29.29


ATOM
1191
CB
TYR
167
22.225
24.703
12.915
1.00
29.15


ATOM
1192
CG
TYR
167
23.295
25.581
13.541
1.00
29.82


ATOM
1193
CD1
TYR
167
24.634
25.451
13.193
1.00
31.46


ATOM
1194
CE1
TYR
167
25.618
26.271
13.778
1.00
33.38


ATOM
1195
CD2
TYR
167
22.956
26.547
14.490
1.00
31.23


ATOM
1196
CE2
TYR
167
23.917
27.362
15.082
1.00
31.33


ATOM
1197
CZ
TYR
167
25.250
27.224
14.726
1.00
32.94


ATOM
1198
OH
TYR
167
26.198
28.032
15.329
1.00
33.66


ATOM
1199
C
TYR
167
20.713
22.756
13.155
1.00
30.93


ATOM
1200
O
TYR
167
20.380
22.642
11.977
1.00
31.73


ATOM
1201
N
THR
168
19.917
22.429
14.163
1.00
33.46


ATOM
1202
CA
THR
168
18.592
21.866
13.950
1.00
34.18


ATOM
1203
CB
THR
168
18.564
20.428
14.427
1.00
34.56


ATOM
1204
OG1
THR
168
19.567
20.266
15.439
1.00
36.47


ATOM
1205
CG2
THR
168
18.855
19.470
13.274
1.00
35.43


ATOM
1206
C
THR
168
17.494
22.643
14.659
1.00
34.34


ATOM
1207
O
THR
168
17.718
23.310
15.667
1.00
37.07


ATOM
1208
N
TYR
169
16.294
22.535
14.106
1.00
33.59


ATOM
1209
CA
TYR
169
15.132
23.227
14.615
1.00
31.03


ATOM
1210
CB
TYR
169
14.839
24.434
13.726
1.00
26.08


ATOM
1211
CG
TYR
169
16.037
25.332
13.525
1.00
27.60


ATOM
1212
CD1
TYR
169
17.109
24.930
12.739
1.00
30.90


ATOM
1213
CE1
TYR
169
18.217
25.762
12.533
1.00
31.53


ATOM
1214
CD2
TYR
169
16.094
26.587
14.112
1.00
28.88


ATOM
1215
CE2
TYR
169
17.191
27.438
13.916
1.00
31.16


ATOM
1216
CZ
TYR
169
18.254
27.023
13.116
1.00
33.28


ATOM
1217
OH
TYR
169
19.323
27.867
12.846
1.00
32.19


ATOM
1218
C
TYR
169
13.924
22.322
14.662
1.00
32.69


ATOM
1219
O
TYR
169
13.402
21.904
13.631
1.00
31.23


ATOM
1220
N
GLY
170
13.486
22.034
15.879
1.00
32.73


ATOM
1221
CA
GLY
170
12.320
21.196
16.067
1.00
31.89


ATOM
1222
C
GLY
170
12.510
19.828
15.448
1.00
31.16


ATOM
1223
O
GLY
170
11.592
19.282
14.834
1.00
30.48


ATOM
1224
N
SER
171
13.709
19.271
15.601
1.00
29.94


ATOM
1225
CA
SER
171
13.999
17.953
15.043
1.00
29.41


ATOM
1226
CB
SER
171
15.504
17.797
14.760
1.00
31.96


ATOM
1227
OG
SER
171
16.189
17.109
15.813
1.00
28.95


ATOM
1228
C
SER
171
13.568
16.897
16.050
1.00
27.43


ATOM
1229
O
SER
171
13.529
17.136
17.262
1.00
30.66


ATOM
1230
N
PRO
172
13.209
15.723
15.565
1.00
24.19


ATOM
1231
CD
PRO
172
12.982
15.315
14.175
1.00
24.16


ATOM
1232
CA
PRO
172
12.799
14.693
16.513
1.00
25.27


ATOM
1233
CB
PRO
172
11.906
13.802
15.667
1.00
22.48


ATOM
1234
CG
PRO
172
12.570
13.861
14.337
1.00
26.34


ATOM
1235
C
PRO
172
14.071
13.995
17.006
1.00
26.93


ATOM
1236
O
PRO
172
15.165
14.277
16.481
1.00
25.21


ATOM
1237
N
ARG
173
13.950
13.122
18.015
1.00
24.87


ATOM
1238
CA
ARG
173
15.117
12.387
18.509
1.00
19.89


ATOM
1239
CB
ARG
173
14.741
11.481
19.651
1.00
16.72


ATOM
1240
CG
ARG
173
14.075
12.137
20.827
1.00
13.01


ATOM
1241
CD
ARG
173
14.184
11.214
22.011
1.00
18.41


ATOM
1242
NE
ARG
173
13.775
11.943
23.200
1.00
22.47


ATOM
1243
CZ
ARG
173
12.516
12.251
23.482
1.00
22.00


ATOM
1244
NH1
ARG
173
12.229
12.936
24.577
1.00
18.05


ATOM
1245
NH2
ARG
173
11.545
11.841
22.684
1.00
23.39


ATOM
1246
C
ARG
173
15.482
11.515
17.327
1.00
20.52


ATOM
1247
O
ARG
173
14.565
11.012
16.689
1.00
21.15


ATOM
1248
N
VAL
174
16.770
11.306
17.024
1.00
22.47


ATOM
1249
CA
VAL
174
17.135
10.497
15.827
1.00
25.15


ATOM
1250
CB
VAL
174
18.144
11.313
14.881
1.00
23.04


ATOM
1251
CG1
VAL
174
18.336
12.735
15.425
1.00
22.73


ATOM
1252
CG2
VAL
174
19.469
10.612
14.772
1.00
24.59


ATOM
1253
C
VAL
174
17.621
9.020
16.017
1.00
26.28


ATOM
1254
O
VAL
174
17.560
8.223
15.067
1.00
26.79


ATOM
1255
N
GLY
175
18.063
8.650
17.225
1.00
30.71


ATOM
1256
CA
GLY
175
18.513
7.281
17.478
1.00
32.37


ATOM
1257
C
GLY
175
18.428
6.893
18.942
1.00
32.98


ATOM
1258
O
GLY
175
17.602
7.406
19.686
1.00
35.87


ATOM
1259
N
ASN
176
19.285
5.971
19.359
1.00
30.86


ATOM
1260
CA
ASN
176
19.302
5.535
20.747
1.00
31.73


ATOM
1261
CB
ASN
176
19.361
4.007
20.873
1.00
28.19


ATOM
1262
CG
ASN
176
20.700
3.408
20.428
1.00
30.78


ATOM
1263
OD1
ASN
176
20.915
2.203
20.552
1.00
28.67


ATOM
1264
ND2
ASN
176
21.592
4.238
19.907
1.00
35.19


ATOM
1265
C
ASN
176
20.475
6.123
21.488
1.00
32.41


ATOM
1266
O
ASN
176
21.370
6.776
20.926
1.00
32.01


ATOM
1267
N
THR
177
20.452
5.888
22.779
1.00
31.20


ATOM
1268
CA
THR
177
21.497
6.359
23.660
1.00
35.00


ATOM
1269
CB
THR
177
21.510
5.478
24.861
1.00
33.97


ATOM
1270
OG1
THR
177
20.534
4.443
24.654
1.00
40.81


ATOM
1271
CG2
THR
177
21.141
6.276
26.090
1.00
34.76


ATOM
1272
C
THR
177
22.889
6.430
23.069
1.00
36.41


ATOM
1273
O
THR
177
23.475
7.492
23.025
1.00
38.30


ATOM
1274
N
GLN
178
23.423
5.309
22.605
1.00
36.58


ATOM
1275
CA
GLN
178
24.776
5.343
22.045
1.00
38.33


ATOM
1276
CB
GLN
178
25.380
3.928
21.855
1.00
37.70


ATOM
1277
CG
GLN
178
24.401
2.867
21.458
1.00
37.39


ATOM
1278
CD
GLN
178
23.795
2.165
22.668
1.00
38.56


ATOM
1279
OE1
GLN
178
24.497
1.494
23.415
1.00
37.40


ATOM
1280
NE2
GLN
178
22.486
2.312
22.857
1.00
36.48


ATOM
1281
C
GLN
178
24.882
6.124
20.748
1.00
36.06


ATOM
1282
O
GLN
178
25.936
6.708
20.448
1.00
35.15


ATOM
1283
N
LEU
179
23.821
6.163
19.963
1.00
31.34


ATOM
1284
CA
LEU
179
23.972
6.929
18.753
1.00
31.50


ATOM
1285
CB
LEU
179
22.786
6.691
17.840
1.00
28.66


ATOM
1286
CG
LEU
179
22.690
7.609
16.631
1.00
27.94


ATOM
1287
CD1
LEU
179
23.680
7.207
15.572
1.00
29.06


ATOM
1288
CD2
LEU
179
21.302
7.507
16.072
1.00
33.99


ATOM
1289
C
LEU
179
24.061
8.405
19.175
1.00
34.01


ATOM
1290
O
LEU
179
25.032
9.111
18.845
1.00
33.60


ATOM
1291
N
ALA
180
23.061
8.856
19.935
1.00
34.29


ATOM
1292
CA
ALA
180
23.013
10.245
20.375
1.00
34.25


ATOM
1293
CB
ALA
180
21.878
10.440
21.312
1.00
31.38


ATOM
1294
C
ALA
180
24.291
10.650
21.067
1.00
35.98


ATOM
1295
O
ALA
180
24.757
11.779
20.946
1.00
39.76


ATOM
1296
N
ALA
181
24.831
9.722
21.836
1.00
34.88


ATOM
1297
CA
ALA
181
26.039
9.966
22.583
1.00
31.64


ATOM
1298
CB
ALA
181
26.369
8.771
23.380
1.00
28.24


ATOM
1299
C
ALA
181
27.139
10.249
21.632
1.00
32.31


ATOM
1300
O
ALA
181
27.818
11.261
21.713
1.00
30.45


ATOM
1301
N
PHE
182
27.311
9.311
20.729
1.00
33.84


ATOM
1302
CA
PHE
182
28.338
9.409
19.721
1.00
37.67


ATOM
1303
CB
PHE
182
28.038
8.399
18.634
1.00
35.24


ATOM
1304
CG
PHE
182
29.006
8.421
17.513
1.00
32.23


ATOM
1305
CD1
PHE
182
28.581
8.744
16.230
1.00
35.37


ATOM
1306
CD2
PHE
182
30.325
8.027
17.709
1.00
31.11


ATOM
1307
CE1
PHE
182
29.453
8.658
15.150
1.00
35.57


ATOM
1308
CE2
PHE
182
31.203
7.937
16.629
1.00
32.35


ATOM
1309
CZ
PHE
182
30.764
8.252
15.351
1.00
34.57


ATOM
1310
C
PHE
182
28.412
10.809
19.123
1.00
40.35


ATOM
1311
O
PHE
182
29.431
11.500
19.216
1.00
40.89


ATOM
1312
N
VAL
183
27.308
11.226
18.527
1.00
38.30


ATOM
1313
CA
VAL
183
27.235
12.529
17.917
1.00
39.18


ATOM
1314
CB
VAL
183
25.866
12.741
17.393
1.00
40.72


ATOM
1315
CG1
VAL
183
25.790
14.058
16.649
1.00
39.25


ATOM
1316
CG2
VAL
183
25.507
11.552
16.530
1.00
37.39


ATOM
1317
C
VAL
183
27.534
13.621
18.919
1.00
38.88


ATOM
1318
O
VAL
183
28.213
14.600
18.622
1.00
39.49


ATOM
1319
N
SER
184
27.014
13.457
20.119
1.00
37.57


ATOM
1320
CA
SER
184
27.251
14.452
21.126
1.00
37.92


ATOM
1321
CB
SER
184
26.554
14.053
22.413
1.00
34.90


ATOM
1322
OG
SER
184
25.169
14.191
22.253
1.00
31.35


ATOM
1323
C
SER
184
28.740
14.599
21.370
1.00
40.95


ATOM
1324
O
SER
184
29.262
15.713
21.453
1.00
43.53


ATOM
1325
N
ASN
185
29.417
13.463
21.459
1.00
42.49


ATOM
1326
CA
ASN
185
30.838
13.428
21.749
1.00
43.30


ATOM
1327
CB
ASN
185
31.129
12.154
22.478
1.00
46.28


ATOM
1328
CG
ASN
185
30.120
11.904
23.542
1.00
51.12


ATOM
1329
OD1
ASN
185
29.977
12.708
24.455
1.00
51.56


ATOM
1330
ND2
ASN
185
29.390
10.809
23.430
1.00
56.16


ATOM
1331
C
ASN
185
31.714
13.526
20.554
1.00
43.01


ATOM
1332
O
ASN
185
32.880
13.173
20.592
1.00
43.68


ATOM
1333
N
GLN
186
31.137
13.981
19.469
1.00
39.81


ATOM
1334
CA
GLN
186
31.917
14.138
18.283
1.00
39.03


ATOM
1335
CB
GLN
186
31.058
13.959
17.041
1.00
39.39


ATOM
1336
CG
GLN
186
31.029
12.570
16.476
1.00
36.32


ATOM
1337
CD
GLN
186
30.509
12.574
15.068
1.00
35.86


ATOM
1338
OE1
GLN
186
30.888
11.732
14.255
1.00
39.13


ATOM
1339
NE2
GLN
186
29.627
13.522
14.764
1.00
35.55


ATOM
1340
C
GLN
186
32.454
15.541
18.324
1.00
39.42


ATOM
1341
O
GLN
186
31.866
16.437
18.926
1.00
41.40


ATOM
1342
N
ALA
187
33.605
15.724
17.710
1.00
38.62


ATOM
1343
CA
ALA
187
34.194
17.042
17.666
1.00
38.34


ATOM
1344
CB
ALA
187
35.438
17.030
16.788
1.00
37.50


ATOM
1345
C
ALA
187
33.118
17.938
17.069
1.00
39.50


ATOM
1346
O
ALA
187
32.374
17.532
16.150
1.00
38.37


ATOM
1347
N
GLY
188
33.012
19.146
17.615
1.00
39.42


ATOM
1348
CA
GLY
188
32.009
20.067
17.114
1.00
38.11


ATOM
1349
C
GLY
188
30.737
20.118
17.950
1.00
35.77


ATOM
1350
O
GLY
188
30.613
19.421
18.987
1.00
35.70


ATOM
1351
N
GLY
189
29.789
20.939
17.500
1.00
33.30


ATOM
1352
CA
GLY
189
28.548
21.082
18.230
1.00
34.89


ATOM
1353
C
GLY
189
27.280
20.762
17.472
1.00
35.30


ATOM
1354
O
GLY
189
27.213
20.843
16.233
1.00
36.66


ATOM
1355
N
GLU
190
26.271
20.397
18.261
1.00
34.26


ATOM
1356
CA
GLU
190
24.926
20.036
17.802
1.00
30.13


ATOM
1357
CB
GLU
190
24.568
18.609
18.250
1.00
29.94


ATOM
1358
CG
GLU
190
25.555
17.509
17.877
1.00
30.77


ATOM
1359
CD
GLU
190
26.936
17.697
18.461
1.00
32.53


ATOM
1360
OE1
GLU
190
27.052
17.995
19.673
1.00
34.56


ATOM
1361
OE2
GLU
190
27.905
17.523
17.695
1.00
32.05


ATOM
1362
C
GLU
190
23.988
20.987
18.552
1.00
25.52


ATOM
1363
O
GLU
190
23.506
20.631
19.645
1.00
25.60


ATOM
1364
N
TYR
191
23.747
22.178
18.012
1.00
23.84


ATOM
1365
CA
TYR
191
22.868
23.104
18.689
1.00
26.80


ATOM
1366
CB
TYR
191
23.167
24.539
18.295
1.00
29.71


ATOM
1367
CG
TYR
191
24.614
24.924
18.207
1.00
32.88


ATOM
1368
CD1
TYR
191
25.198
25.723
19.184
1.00
33.47


ATOM
1369
CE1
TYR
191
26.526
26.132
19.071
1.00
33.90


ATOM
1370
CD2
TYR
191
25.390
24.537
17.119
1.00
35.22


ATOM
1371
CE2
TYR
191
26.702
24.938
16.997
1.00
38.47


ATOM
1372
CZ
TYR
191
27.265
25.737
17.967
1.00
37.34


ATOM
1373
OH
TYR
191
28.561
26.167
17.795
1.00
41.52


ATOM
1374
C
TYR
191
21.482
22.789
18.188
1.00
27.01


ATOM
1375
O
TYR
191
21.111
23.265
17.118
1.00
30.00


ATOM
1376
N
ARG
192
20.721
21.970
18.912
1.00
23.47


ATOM
1377
CA
ARG
192
19.363
21.697
18.466
1.00
23.80


ATOM
1378
CB
ARG
192
18.966
20.213
18.555
1.00
23.43


ATOM
1379
CG
ARG
192
18.894
19.585
19.917
1.00
26.56


ATOM
1380
CD
ARG
192
18.227
18.215
19.805
1.00
29.50


ATOM
1381
NE
ARG
192
17.268
17.990
20.884
1.00
30.31


ATOM
1382
CZ
ARG
192
17.598
17.672
22.130
1.00
32.33


ATOM
1383
NH1
ARG
192
16.654
17.501
23.046
1.00
33.74


ATOM
1384
NH2
ARG
192
18.863
17.492
22.449
1.00
35.07


ATOM
1385
C
ARG
192
18.448
22.558
19.290
1.00
22.85


ATOM
1386
O
ARG
192
18.488
22.540
20.542
1.00
22.61


ATOM
1387
N
VAL
193
17.670
23.352
18.554
1.00
20.52


ATOM
1388
CA
VAL
193
16.726
24.306
19.117
1.00
24.71


ATOM
1389
CB
VAL
193
16.760
25.635
18.307
1.00
25.59


ATOM
1390
CG1
VAL
193
15.771
26.629
18.888
1.00
23.22


ATOM
1391
CG2
VAL
193
18.191
26.227
18.280
1.00
26.47


ATOM
1392
C
VAL
193
15.284
23.782
19.106
1.00
28.05


ATOM
1393
O
VAL
193
14.845
23.158
18.111
1.00
32.43


ATOM
1394
N
THR
194
14.564
24.055
20.205
1.00
29.93


ATOM
1395
CA
THR
194
13.166
23.659
20.383
1.00
32.80


ATOM
1396
CB
THR
194
13.009
22.586
21.494
1.00
33.39


ATOM
1397
OG1
THR
194
13.570
23.052
22.734
1.00
34.60


ATOM
1398
CG2
THR
194
13.700
21.316
21.074
1.00
35.77


ATOM
1399
C
THR
194
12.253
24.844
20.728
1.00
33.73


ATOM
1400
O
THR
194
12.623
25.790
21.432
1.00
34.75


ATOM
1401
N
ASN
195
11.022
24.762
20.258
1.00
33.87


ATOM
1402
CA
ASN
195
10.076
25.835
20.492
1.00
36.33


ATOM
1403
CB
ASN
195
9.586
26.345
19.132
1.00
36.77


ATOM
1404
CG
ASN
195
8.726
27.574
19.232
1.00
37.55


ATOM
1405
OD1
ASN
195
8.810
28.352
20.193
1.00
32.92


ATOM
1406
ND2
ASN
195
7.896
27.773
18.213
1.00
33.28


ATOM
1407
C
ASN
195
8.911
25.443
21.395
1.00
36.22


ATOM
1408
O
ASN
195
8.031
24.664
21.002
1.00
33.64


ATOM
1409
N
ALA
196
8.931
25.979
22.617
1.00
37.74


ATOM
1410
CA
ALA
196
7.864
25.730
23.592
1.00
39.36


ATOM
1411
CB
ALA
196
6.670
26.666
23.303
1.00
42.05


ATOM
1412
C
ALA
196
7.377
24.271
23.670
1.00
40.34


ATOM
1413
O
ALA
196
8.135
23.373
24.112
1.00
43.70


ATOM
1414
N
LYS
197
6.117
24.049
23.265
1.00
38.99


ATOM
1415
CA
LYS
197
5.503
22.726
23.292
1.00
35.84


ATOM
1416
CB
LYS
197
4.137
22.823
23.920
1.00
33.03


ATOM
1417
CG
LYS
197
4.182
23.206
25.348
1.00
36.10


ATOM
1418
CD
LYS
197
2.794
23.473
25.836
1.00
37.51


ATOM
1419
CE
LYS
197
2.783
23.551
27.342
1.00
39.85


ATOM
1420
NZ
LYS
197
3.163
22.223
27.944
1.00
43.96


ATOM
1421
C
LYS
197
5.366
22.066
21.930
1.00
36.67


ATOM
1422
O
LYS
197
4.373
21.373
21.679
1.00
38.07


ATOM
1423
N
ASP
198
6.351
22.295
21.055
1.00
34.49


ATOM
1424
CA
ASP
198
6.384
21.686
19.717
1.00
32.29


ATOM
1425
CB
ASP
198
7.708
22.032
19.013
1.00
29.09


ATOM
1426
CG
ASP
198
7.882
21.302
17.701
1.00
26.03


ATOM
1427
OD1
ASP
198
7.062
20.409
17.414
1.00
23.23


ATOM
1428
OD2
ASP
198
8.845
21.615
16.969
1.00
21.49


ATOM
1429
C
ASP
198
6.333
20.180
20.033
1.00
33.21


ATOM
1430
O
ASP
198
7.153
19.676
20.809
1.00
36.31


ATOM
1431
N
PRO
199
5.384
19.438
19.442
1.00
31.90


ATOM
1432
CD
PRO
199
4.208
19.890
18.679
1.00
33.69


ATOM
1433
CA
PRO
199
5.302
18.004
19.740
1.00
31.80


ATOM
1434
CB
PRO
199
3.859
17.676
19.408
1.00
30.13


ATOM
1435
CG
PRO
199
3.581
18.575
18.252
1.00
30.92


ATOM
1436
C
PRO
199
6.266
17.016
19.090
1.00
34.31


ATOM
1437
O
PRO
199
6.313
15.856
19.490
1.00
37.03


ATOM
1438
N
VAL
200
7.038
17.451
18.102
1.00
32.02


ATOM
1439
CA
VAL
200
7.952
16.525
17.429
1.00
33.55


ATOM
1440
CB
VAL
200
8.140
16.879
15.896
1.00
31.45


ATOM
1441
CG1
VAL
200
7.679
18.286
15.609
1.00
26.24


ATOM
1442
CG2
VAL
200
9.603
16.708
15.471
1.00
26.07


ATOM
1443
C
VAL
200
9.314
16.342
18.080
1.00
36.82


ATOM
1444
O
VAL
200
9.900
15.254
18.026
1.00
36.73


ATOM
1445
N
PRO
201
9.843
17.398
18.704
1.00
39.43


ATOM
1446
CD
PRO
201
9.432
18.809
18.677
1.00
40.66


ATOM
1447
CA
PRO
201
11.152
17.259
19.341
1.00
38.84


ATOM
1448
CB
PRO
201
11.466
18.682
19.778
1.00
35.83


ATOM
1449
CG
PRO
201
10.765
19.504
18.729
1.00
38.37


ATOM
1450
C
PRO
201
11.121
16.280
20.507
1.00
38.72


ATOM
1451
O
PRO
201
12.136
16.029
21.137
1.00
41.44


ATOM
1452
N
ARG
202
9.944
15.735
20.791
1.00
38.20


ATOM
1453
CA
ARG
202
9.810
14.778
21.865
1.00
33.59


ATOM
1454
CB
ARG
202
8.833
15.287
22.943
1.00
31.21


ATOM
1455
CG
ARG
202
7.619
16.100
22.527
1.00
26.21


ATOM
1456
CD
ARG
202
6.651
16.096
23.704
1.00
28.07


ATOM
1457
NE
ARG
202
5.721
17.221
23.771
1.00
32.08


ATOM
1458
CZ
ARG
202
4.543
17.282
23.145
1.00
31.23


ATOM
1459
NH1
ARG
202
3.782
18.357
23.293
1.00
33.90


ATOM
1460
NH2
ARG
202
4.112
16.286
22.372
1.00
30.66


ATOM
1461
C
ARG
202
9.406
13.419
21.309
1.00
32.52


ATOM
1462
O
ARG
202
8.807
12.575
22.004
1.00
35.11


ATOM
1463
N
LEU
203
9.773
13.204
20.048
1.00
29.82


ATOM
1464
CA
LEU
203
9.481
11.946
19.380
1.00
25.27


ATOM
1465
CB
LEU
203
8.263
12.104
18.460
1.00
24.76


ATOM
1466
CG
LEU
203
6.964
12.372
19.219
1.00
25.85


ATOM
1467
CD1
LEU
203
5.883
12.703
18.207
1.00
20.27


ATOM
1468
CD2
LEU
203
6.585
11.156
20.109
1.00
19.33


ATOM
1469
C
LEU
203
10.706
11.514
18.572
1.00
21.60


ATOM
1470
O
LEU
203
11.471
12.352
18.074
1.00
19.99


ATOM
1471
N
PRO
204
10.948
10.200
18.489
1.00
18.93


ATOM
1472
CD
PRO
204
11.765
9.581
17.427
1.00
17.45


ATOM
1473
CA
PRO
204
10.098
9.203
19.144
1.00
20.16


ATOM
1474
CB
PRO
204
10.572
7.888
18.516
1.00
21.98


ATOM
1475
CG
PRO
204
11.007
8.301
17.141
1.00
16.12


ATOM
1476
C
PRO
204
10.234
9.215
20.685
1.00
18.91


ATOM
1477
O
PRO
204
11.176
9.789
21.239
1.00
15.54


ATOM
1478
N
PRO
205
9.299
8.554
21.388
1.00
19.35


ATOM
1479
CD
PRO
205
8.213
7.738
20.823
1.00
20.56


ATOM
1480
CA
PRO
205
9.278
8.477
22.850
1.00
21.21


ATOM
1481
CB
PRO
205
8.091
7.555
23.131
1.00
19.58


ATOM
1482
CG
PRO
205
7.212
7.756
21.945
1.00
19.74


ATOM
1483
C
PRO
205
10.561
7.919
23.442
1.00
24.31


ATOM
1484
O
PRO
205
11.210
7.055
22.842
1.00
27.43


ATOM
1485
N
LEU
206
10.924
8.411
24.624
1.00
24.15


ATOM
1486
CA
LEU
206
12.115
7.908
25.284
1.00
26.76


ATOM
1487
CB
LEU
206
12.329
8.538
26.663
1.00
25.72


ATOM
1488
CG
LEU
206
12.816
9.977
26.831
1.00
28.25


ATOM
1489
CD1
LEU
206
13.274
10.191
28.268
1.00
26.97


ATOM
1490
CD2
LEU
206
13.970
10.252
25.873
1.00
29.72


ATOM
1491
C
LEU
206
11.864
6.431
25.493
1.00
28.70


ATOM
1492
O
LEU
206
12.751
5.607
25.218
1.00
32.61


ATOM
1493
N
ILE
207
10.654
6.101
25.968
1.00
30.14


ATOM
1494
CA
ILE
207
10.296
4.714
26.248
1.00
31.14


ATOM
1495
CB
ILE
207
8.799
4.556
26.569
1.00
28.18


ATOM
1496
CG2
ILE
207
8.463
5.299
27.868
1.00
26.68


ATOM
1497
CG1
ILE
207
7.966
5.038
25.387
1.00
26.98


ATOM
1498
CD1
ILE
207
6.479
4.718
25.510
1.00
32.66


ATOM
1499
C
ILE
207
10.653
3.767
25.103
1.00
33.97


ATOM
1500
O
ILE
207
10.739
2.543
25.309
1.00
34.93


ATOM
1501
N
PHE
208
10.864
4.317
23.904
1.00
34.47


ATOM
1502
CA
PHE
208
11.213
3.473
22.771
1.00
33.35


ATOM
1503
CB
PHE
208
10.242
3.743
21.597
1.00
33.97


ATOM
1504
CG
PHE
208
8.801
3.322
21.882
1.00
37.81


ATOM
1505
CD1
PHE
208
7.728
4.050
21.361
1.00
36.85


ATOM
1506
CD2
PHE
208
8.518
2.225
22.716
1.00
38.73


ATOM
1507
CE1
PHE
208
6.393
3.706
21.672
1.00
35.52


ATOM
1508
CE2
PHE
208
7.182
1.871
23.032
1.00
38.10


ATOM
1509
CZ
PHE
208
6.124
2.623
22.504
1.00
37.46


ATOM
1510
C
PHE
208
12.702
3.627
22.394
1.00
30.91


ATOM
1511
O
PHE
208
13.085
3.557
21.230
1.00
33.03


ATOM
1512
N
GLY
209
13.530
3.813
23.422
1.00
27.41


ATOM
1513
CA
GLY
209
14.977
3.902
23.270
1.00
27.70


ATOM
1514
C
GLY
209
15.564
5.177
22.712
1.00
29.53


ATOM
1515
O
GLY
209
16.769
5.436
22.851
1.00
29.48


ATOM
1516
N
TYR
210
14.718
5.962
22.055
1.00
29.56


ATOM
1517
CA
TYR
210
15.154
7.198
21.451
1.00
29.10


ATOM
1518
CB
TYR
210
14.054
7.729
20.544
1.00
28.00


ATOM
1519
CG
TYR
210
13.904
6.928
19.253
1.00
28.06


ATOM
1520
CD1
TYR
210
14.611
7.283
18.093
1.00
26.44


ATOM
1521
CE1
TYR
210
14.454
6.564
16.884
1.00
25.01


ATOM
1522
CD2
TYR
210
13.043
5.829
19.181
1.00
22.49


ATOM
1523
CE2
TYR
210
12.881
5.099
17.980
1.00
24.49


ATOM
1524
CZ
TYR
210
13.585
5.477
16.839
1.00
26.12


ATOM
1525
OH
TYR
210
13.400
4.789
15.654
1.00
28.95


ATOM
1526
C
TYR
210
15.564
8.211
22.506
1.00
30.17


ATOM
1527
O
TYR
210
14.879
8.419
23.530
1.00
31.17


ATOM
1528
N
ARG
211
16.716
8.818
22.230
1.00
29.17


ATOM
1529
CA
ARG
211
17.357
9.805
23.082
1.00
27.79


ATOM
1530
CB
ARG
211
18.591
9.177
23.707
1.00
26.76


ATOM
1531
CG
ARG
211
18.308
7.871
24.418
1.00
30.07


ATOM
1532
CD
ARG
211
17.554
8.140
25.688
1.00
28.13


ATOM
1533
NE
ARG
211
16.471
7.194
25.872
1.00
31.44


ATOM
1534
CZ
ARG
211
16.342
6.426
26.945
1.00
37.43


ATOM
1535
NH1
ARG
211
17.240
6.511
27.912
1.00
38.25


ATOM
1536
NH2
ARG
211
15.323
5.576
27.053
1.00
39.38


ATOM
1537
C
ARG
211
17.789
10.976
22.206
1.00
29.96


ATOM
1538
O
ARG
211
17.767
10.860
20.969
1.00
35.98


ATOM
1539
N
HIS
212
18.196
12.080
22.837
1.00
28.81


ATOM
1540
CA
HIS
212
18.632
13.264
22.116
1.00
27.59


ATOM
1541
CB
HIS
212
17.826
14.468
22.586
1.00
25.29


ATOM
1542
CG
HIS
212
16.632
14.782
21.733
1.00
21.16


ATOM
1543
CD2
HIS
212
15.329
14.985
22.051
1.00
18.56


ATOM
1544
ND1
HIS
212
16.727
14.996
20.374
1.00
19.29


ATOM
1545
CE1
HIS
212
15.538
15.314
19.892
1.00
19.37


ATOM
1546
NE2
HIS
212
14.671
15.313
20.889
1.00
18.19


ATOM
1547
C
HIS
212
20.115
13.592
22.258
1.00
29.89


ATOM
1548
O
HIS
212
20.858
12.902
22.948
1.00
32.67


ATOM
1549
N
THR
213
20.533
14.653
21.568
1.00
32.51


ATOM
1550
CA
THR
213
21.915
15.151
21.609
1.00
34.41


ATOM
1551
CB
THR
213
22.434
15.671
20.251
1.00
35.45


ATOM
1552
OG1
THR
213
21.376
16.357
19.565
1.00
36.52


ATOM
1553
CG2
THR
213
22.991
14.545
19.421
1.00
38.69


ATOM
1554
C
THR
213
21.929
16.359
22.518
1.00
35.02


ATOM
1555
O
THR
213
21.008
17.165
22.518
1.00
33.04


ATOM
1556
N
SER
214
22.998
16.511
23.266
1.00
35.79


ATOM
1557
CA
SER
214
23.068
17.627
24.161
1.00
37.40


ATOM
1558
CB
SER
214
23.556
17.122
25.514
1.00
37.51


ATOM
1559
OG
SER
214
23.560
18.133
26.501
1.00
42.60


ATOM
1560
C
SER
214
23.990
18.694
23.575
1.00
37.69


ATOM
1561
O
SER
214
24.931
18.390
22.842
1.00
39.04


ATOM
1562
N
PRO
215
23.699
19.968
23.857
1.00
36.66


ATOM
1563
CD
PRO
215
24.595
21.111
23.606
1.00
36.17


ATOM
1564
CA
PRO
215
22.562
20.383
24.677
1.00
35.16


ATOM
1565
CB
PRO
215
23.032
21.699
25.252
1.00
34.57


ATOM
1566
CG
PRO
215
23.761
22.286
24.085
1.00
34.47


ATOM
1567
C
PRO
215
21.286
20.568
23.879
1.00
35.43


ATOM
1568
O
PRO
215
21.129
20.049
22.773
1.00
34.55


ATOM
1569
N
GLU
216
20.389
21.341
24.469
1.00
36.14


ATOM
1570
CA
GLU
216
19.101
21.651
23.885
1.00
35.35


ATOM
1571
CB
GLU
216
18.015
20.782
24.504
1.00
34.93


ATOM
1572
CG
GLU
216
16.632
21.260
24.130
1.00
31.58


ATOM
1573
CD
GLU
216
15.537
20.628
24.973
1.00
34.98


ATOM
1574
OE1
GLU
216
15.723
19.485
25.463
1.00
41.04


ATOM
1575
OE2
GLU
216
14.474
21.272
25.133
1.00
34.46


ATOM
1576
C
GLU
216
18.804
23.099
24.211
1.00
33.66


ATOM
1577
O
GLU
216
18.693
23.478
25.375
1.00
32.94


ATOM
1578
N
TYR
217
18.686
23.913
23.179
1.00
33.09


ATOM
1579
CA
TYR
217
18.392
25.326
23.361
1.00
34.95


ATOM
1580
CB
TYR
217
19.200
26.134
22.364
1.00
34.01


ATOM
1581
CG
TYR
217
20.689
25.910
22.489
1.00
35.10


ATOM
1582
CD1
TYR
217
21.300
24.776
21.947
1.00
35.08


ATOM
1583
CE1
TYR
217
22.681
24.583
22.053
1.00
33.58


ATOM
1584
CD2
TYR
217
21.495
26.841
23.148
1.00
36.42


ATOM
1585
CE2
TYR
217
22.869
26.653
23.263
1.00
33.49


ATOM
1586
CZ
TYR
217
23.453
25.523
22.710
1.00
32.43


ATOM
1587
OH
TYR
217
24.803
25.332
22.805
1.00
31.62


ATOM
1588
C
TYR
217
16.904
25.537
23.158
1.00
35.97


ATOM
1589
O
TYR
217
16.422
25.725
22.050
1.00
37.11


ATOM
1590
N
TRP
218
16.175
25.475
24.260
1.00
33.94


ATOM
1591
CA
TRP
218
14.720
25.597
24.245
1.00
33.34


ATOM
1592
CB
TRP
218
14.125
24.729
25.356
1.00
35.12


ATOM
1593
CG
TRP
218
12.660
24.733
25.456
1.00
31.18


ATOM
1594
CD2
TRP
218
11.908
24.884
26.658
1.00
27.18


ATOM
1595
CE2
TRP
218
10.545
24.649
26.342
1.00
27.19


ATOM
1596
CE3
TRP
218
12.252
25.190
27.981
1.00
26.15


ATOM
1597
CD1
TRP
218
11.755
24.437
24.467
1.00
32.33


ATOM
1598
NE1
TRP
218
10.474
24.377
24.997
1.00
29.27


ATOM
1599
CZ2
TRP
218
9.536
24.706
27.299
1.00
23.07


ATOM
1600
CZ3
TRP
218
11.253
25.246
28.925
1.00
28.57


ATOM
1601
CH2
TRP
218
9.909
25.005
28.582
1.00
27.07


ATOM
1602
C
TRP
218
14.215
27.006
24.385
1.00
32.24


ATOM
1603
O
TRP
218
14.706
27.785
25.218
1.00
30.36


ATOM
1604
N
LEU
219
13.223
27.316
23.553
1.00
32.03


ATOM
1605
CA
LEU
219
12.606
28.635
23.539
1.00
30.96


ATOM
1606
CB
LEU
219
12.153
28.992
22.130
1.00
24.86


ATOM
1607
CG
LEU
219
13.219
29.035
21.047
1.00
22.19


ATOM
1608
CD1
LEU
219
12.604
29.413
19.702
1.00
23.26


ATOM
1609
CD2
LEU
219
14.294
30.024
21.451
1.00
23.32


ATOM
1610
C
LEU
219
11.413
28.623
24.477
1.00
32.11


ATOM
1611
O
LEU
219
10.383
28.003
24.199
1.00
31.03


ATOM
1612
N
SER
220
11.574
29.320
25.591
1.00
34.19


ATOM
1613
CA
SER
220
10.558
29.391
26.622
1.00
38.20


ATOM
1614
CB
SER
220
11.232
29.675
27.975
1.00
40.51


ATOM
1615
OG
SER
220
10.283
29.951
28.990
1.00
42.19


ATOM
1616
C
SER
220
9.519
30.468
26.290
1.00
41.27


ATOM
1617
O
SER
220
9.816
31.686
26.314
1.00
43.55


ATOM
1618
N
GLY
221
8.309
30.004
25.974
1.00
42.71


ATOM
1619
CA
GLY
221
7.228
30.901
25.630
1.00
44.34


ATOM
1620
C
GLY
221
5.993
30.125
25.231
1.00
47.07


ATOM
1621
O
GLY
221
5.641
29.130
25.880
1.00
48.33


ATOM
1622
N
SER
222
5.335
30.570
24.162
1.00
47.78


ATOM
1623
CA
SER
222
4.119
29.914
23.686
1.00
48.39


ATOM
1624
CB
SER
222
2.896
30.819
23.912
1.00
48.99


ATOM
1625
OG
SER
222
3.179
32.187
23.647
1.00
46.46


ATOM
1626
C
SER
222
4.209
29.520
22.208
1.00
51.09


ATOM
1627
O
SER
222
4.290
28.326
21.861
1.00
55.36


ATOM
1628
N
ASP
223
4.181
30.530
21.340
1.00
51.73


ATOM
1629
CA
ASP
223
4.269
30.334
19.895
1.00
51.72


ATOM
1630
CB
ASP
223
3.077
29.475
19.432
1.00
46.28


ATOM
1631
CG
ASP
223
2.848
29.517
17.926
1.00
44.22


ATOM
1632
OD1
ASP
223
3.763
29.198
17.126
1.00
46.70


ATOM
1633
OD2
ASP
223
1.719
29.867
17.539
1.00
38.38


ATOM
1634
C
ASP
223
4.337
31.703
19.161
1.00
54.87


ATOM
1635
O
ASP
223
3.716
32.693
19.587
1.00
55.13


ATOM
1636
N
LYS
224
5.158
31.733
18.104
1.00
56.32


ATOM
1637
CA
LYS
224
5.412
32.878
17.221
1.00
53.02


ATOM
1638
CB
LYS
224
4.626
34.108
17.650
1.00
52.74


ATOM
1639
CG
LYS
224
3.137
33.957
17.404
1.00
56.80


ATOM
1640
CD
LYS
224
2.804
33.708
15.933
1.00
57.03


ATOM
1641
CE
LYS
224
1.290
33.534
15.740
1.00
53.19


ATOM
1642
NZ
LYS
224
0.831
33.475
14.322
1.00
50.36


ATOM
1643
C
LYS
224
6.880
33.251
16.992
1.00
50.71


ATOM
1644
O
LYS
224
7.801
32.547
17.395
1.00
49.91


ATOM
1645
N
ILE
225
7.077
34.397
16.364
1.00
48.53


ATOM
1646
CA
ILE
225
8.392
34.884
15.931
1.00
48.98


ATOM
1647
CB
ILE
225
8.157
35.792
14.699
1.00
47.91


ATOM
1648
CG2
ILE
225
9.461
36.175
14.035
1.00
50.91


ATOM
1649
CG1
ILE
225
7.292
35.068
13.686
1.00
50.09


ATOM
1650
CD1
ILE
225
6.841
35.963
12.570
1.00
52.31


ATOM
1651
C
ILE
225
9.461
35.593
16.803
1.00
48.42


ATOM
1652
O
ILE
225
10.666
35.340
16.627
1.00
47.48


ATOM
1653
N
ASP
226
9.046
36.449
17.733
1.00
46.35


ATOM
1654
CA
ASP
226
9.998
37.258
18.509
1.00
42.89


ATOM
1655
CB
ASP
226
9.318
38.569
18.839
1.00
44.72


ATOM
1656
CG
ASP
226
8.058
38.357
19.657
1.00
50.94


ATOM
1657
OD1
ASP
226
7.807
37.187
20.044
1.00
51.85


ATOM
1658
OD2
ASP
226
7.327
39.343
19.919
1.00
51.91


ATOM
1659
C
ASP
226
10.749
36.823
19.770
1.00
40.29


ATOM
1660
O
ASP
226
10.907
37.650
20.674
1.00
36.29


ATOM
1661
N
TYR
227
11.241
35.592
19.864
1.00
38.05


ATOM
1662
CA
TYR
227
11.970
35.268
21.087
1.00
35.65


ATOM
1663
CB
TYR
227
12.205
33.787
21.223
1.00
31.14


ATOM
1664
CG
TYR
227
10.979
32.944
21.408
1.00
23.94


ATOM
1665
CD1
TYR
227
10.268
32.458
20.310
1.00
22.52


ATOM
1666
CE1
TYR
227
9.253
31.538
20.467
1.00
18.28


ATOM
1667
CD2
TYR
227
10.619
32.502
22.673
1.00
22.37


ATOM
1668
CE2
TYR
227
9.607
31.579
22.834
1.00
20.84


ATOM
1669
CZ
TYR
227
8.937
31.099
21.724
1.00
20.72


ATOM
1670
OH
TYR
227
7.991
30.116
21.863
1.00
24.72


ATOM
1671
C
TYR
227
13.324
35.961
21.059
1.00
34.93


ATOM
1672
O
TYR
227
13.749
36.474
20.012
1.00
35.23


ATOM
1673
N
THR
228
14.002
35.971
22.207
1.00
33.89


ATOM
1674
CA
THR
228
15.312
36.619
22.306
1.00
33.29


ATOM
1675
CB
THR
228
15.188
38.000
22.909
1.00
29.80


ATOM
1676
OG1
THR
228
14.804
37.879
24.284
1.00
24.02


ATOM
1677
CG2
THR
228
14.135
38.777
22.157
1.00
22.64


ATOM
1678
C
THR
228
16.226
35.795
23.189
1.00
34.79


ATOM
1679
O
THR
228
15.765
34.869
23.840
1.00
38.39


ATOM
1680
N
ILE
229
17.509
36.142
23.241
1.00
34.44


ATOM
1681
CA
ILE
229
18.451
35.355
24.030
1.00
37.75


ATOM
1682
CB
ILE
229
19.835
36.044
24.181
1.00
39.09


ATOM
1683
CG2
ILE
229
20.937
34.987
23.989
1.00
32.52


ATOM
1684
CG1
ILE
229
19.995
37.178
23.154
1.00
42.61


ATOM
1685
CD1
ILE
229
21.396
37.800
23.068
1.00
45.25


ATOM
1686
C
ILE
229
17.932
35.044
25.414
1.00
39.33


ATOM
1687
O
ILE
229
18.148
33.960
25.952
1.00
39.91


ATOM
1688
N
ASN
230
17.195
35.991
25.971
1.00
42.05


ATOM
1689
CA
ASN
230
16.663
35.840
27.318
1.00
43.15


ATOM
1690
CB
ASN
230
16.427
37.216
27.905
1.00
44.81


ATOM
1691
CG
ASN
230
17.722
37.982
28.064
1.00
46.86


ATOM
1692
OD1
ASN
230
17.718
39.201
28.182
1.00
44.52


ATOM
1693
ND2
ASN
230
18.849
37.258
28.079
1.00
48.08


ATOM
1694
C
ASN
230
15.428
34.990
27.469
1.00
42.18


ATOM
1695
O
ASN
230
14.925
34.809
28.572
1.00
41.84


ATOM
1696
N
ASP
231
14.938
34.470
26.358
1.00
40.88


ATOM
1697
CA
ASP
231
13.763
33.623
26.385
1.00
40.09


ATOM
1698
CB
ASP
231
12.848
33.968
25.219
1.00
44.81


ATOM
1699
CG
ASP
231
12.537
35.435
25.148
1.00
45.26


ATOM
1700
OD1
ASP
231
12.038
35.875
24.085
1.00
43.82


ATOM
1701
OD2
ASP
231
12.793
36.137
26.153
1.00
48.49


ATOM
1702
C
ASP
231
14.259
32.200
26.220
1.00
38.80


ATOM
1703
O
ASP
231
13.479
31.276
26.031
1.00
36.46


ATOM
1704
N
VAL
232
15.574
32.029
26.263
1.00
37.12


ATOM
1705
CA
VAL
232
16.147
30.706
26.100
1.00
36.25


ATOM
1706
CB
VAL
232
17.434
30.762
25.227
1.00
34.82


ATOM
1707
CG1
VAL
232
18.128
29.393
25.227
1.00
30.44


ATOM
1708
CG2
VAL
232
17.070
31.144
23.803
1.00
30.02


ATOM
1709
C
VAL
232
16.449
29.999
27.428
1.00
37.79


ATOM
1710
O
VAL
232
16.680
30.642
28.469
1.00
39.93


ATOM
1711
N
LYS
233
16.400
28.668
27.384
1.00
37.60


ATOM
1712
CA
LYS
233
16.703
27.827
28.532
1.00
36.16


ATOM
1713
CB
LYS
233
15.435
27.145
29.060
1.00
37.40


ATOM
1714
CG
LYS
233
14.297
28.080
29.473
1.00
39.89


ATOM
1715
CD
LYS
233
14.501
28.672
30.863
1.00
43.04


ATOM
1716
CE
LYS
233
13.258
29.447
31.323
1.00
46.34


ATOM
1717
NZ
LYS
233
11.986
28.648
31.284
1.00
47.35


ATOM
1718
C
LYS
233
17.658
26.776
27.955
1.00
37.10


ATOM
1719
O
LYS
233
17.608
26.484
26.757
1.00
40.45


ATOM
1720
N
VAL
234
18.520
26.213
28.795
1.00
35.45


ATOM
1721
CA
VAL
234
19.472
25.203
28.346
1.00
31.04


ATOM
1722
CB
VAL
234
20.904
25.760
28.310
1.00
27.95


ATOM
1723
CG1
VAL
234
21.888
24.667
27.894
1.00
27.27


ATOM
1724
CG2
VAL
234
20.965
26.936
27.354
1.00
25.26


ATOM
1725
C
VAL
234
19.438
23.990
29.257
1.00
32.55


ATOM
1726
O
VAL
234
19.851
24.045
30.425
1.00
33.04


ATOM
1727
N
CYS
235
18.938
22.895
28.694
1.00
35.25


ATOM
1728
CA
CYS
235
18.781
21.619
29.391
1.00
38.31


ATOM
1729
C
CYS
235
19.860
20.670
28.841
1.00
37.75


ATOM
1730
O
CYS
235
20.025
20.522
27.620
1.00
39.24


ATOM
1731
CB
CYS
235
17.342
21.121
29.116
1.00
36.40


ATOM
1732
SG
CYS
235
16.413
22.533
28.396
1.00
49.33


ATOM
1733
N
GLU
236
20.631
20.055
29.732
1.00
37.70


ATOM
1734
CA
GLU
236
21.677
19.147
29.274
1.00
37.30


ATOM
1735
CB
GLU
236
23.026
19.544
29.886
1.00
35.33


ATOM
1736
CG
GLU
236
23.437
21.008
29.670
1.00
38.61


ATOM
1737
CD
GLU
236
24.837
21.314
30.211
1.00
37.96


ATOM
1738
OE1
GLU
236
25.080
22.448
30.690
1.00
34.90


ATOM
1739
OE2
GLU
236
25.699
20.416
30.147
1.00
34.80


ATOM
1740
C
GLU
236
21.332
17.687
29.612
1.00
37.87


ATOM
1741
O
GLU
236
20.639
17.415
30.606
1.00
40.11


ATOM
1742
N
GLY
237
21.785
16.753
28.769
1.00
36.80


ATOM
1743
CA
GLY
237
21.513
15.337
28.998
1.00
32.73


ATOM
1744
C
GLY
237
20.680
14.648
27.905
1.00
30.90


ATOM
1745
O
GLY
237
19.797
15.260
27.294
1.00
29.19


ATOM
1746
N
ALA
238
20.954
13.361
27.688
1.00
32.95


ATOM
1747
CA
ALA
238
20.284
12.512
26.691
1.00
32.90


ATOM
1748
CB
ALA
238
20.903
11.097
26.705
1.00
31.25


ATOM
1749
C
ALA
238
18.788
12.396
26.924
1.00
34.16


ATOM
1750
O
ALA
238
17.994
12.484
25.972
1.00
37.39


ATOM
1751
N
ALA
239
18.426
12.178
28.194
1.00
32.51


ATOM
1752
CA
ALA
239
17.028
12.037
28.623
1.00
33.61


ATOM
1753
CB
ALA
239
16.777
10.624
29.152
1.00
30.52


ATOM
1754
C
ALA
239
16.661
13.076
29.691
1.00
33.09


ATOM
1755
O
ALA
239
16.689
12.802
30.887
1.00
38.01


ATOM
1756
N
ASN
240
16.314
14.271
29.229
1.00
29.73


ATOM
1757
CA
ASN
240
15.958
15.402
30.079
1.00
28.09


ATOM
1758
CB
ASN
240
17.042
16.481
29.956
1.00
28.69


ATOM
1759
CG
ASN
240
16.675
17.762
30.674
1.00
29.76


ATOM
1760
OD1
ASN
240
15.498
18.095
30.837
1.00
29.65


ATOM
1761
ND2
ASN
240
17.682
18.498
31.097
1.00
32.23


ATOM
1762
C
ASN
240
14.614
15.959
29.593
1.00
27.56


ATOM
1763
O
ASN
240
14.485
16.335
28.421
1.00
32.63


ATOM
1764
N
LEU
241
13.622
16.051
30.473
1.00
25.68


ATOM
1765
CA
LEU
241
12.315
16.546
30.048
1.00
25.18


ATOM
1766
CB
LEU
241
11.268
15.505
30.374
1.00
20.15


ATOM
1767
CG
LEU
241
11.654
14.108
29.910
1.00
20.13


ATOM
1768
CD1
LEU
241
10.667
13.096
30.438
1.00
19.46


ATOM
1769
CD2
LEU
241
11.712
14.082
28.394
1.00
7.75


ATOM
1770
C
LEU
241
11.957
17.837
30.735
1.00
28.61


ATOM
1771
O
LEU
241
10.792
18.178
30.881
1.00
31.35


ATOM
1772
N
GLN
242
12.974
18.550
31.177
1.00
31.34


ATOM
1773
CA
GLN
242
12.761
19.798
31.875
1.00
31.71


ATOM
1774
CB
GLN
242
14.002
20.174
32.671
1.00
32.22


ATOM
1775
CG
GLN
242
14.327
19.140
33.687
1.00
35.19


ATOM
1776
CD
GLN
242
13.107
18.781
34.520
1.00
36.20


ATOM
1777
OE1
GLN
242
12.710
19.531
35.413
1.00
38.50


ATOM
1778
NE2
GLN
242
12.503
17.634
34.225
1.00
37.34


ATOM
1779
C
GLN
242
12.478
20.864
30.863
1.00
31.94


ATOM
1780
O
GLN
242
12.335
22.027
31.213
1.00
33.10


ATOM
1781
N
CYS
243
12.386
20.468
29.604
1.00
34.24


ATOM
1782
CA
CYS
243
12.139
21.444
28.583
1.00
35.22


ATOM
1783
C
CYS
243
11.105
21.019
27.577
1.00
34.96


ATOM
1784
O
CYS
243
9.971
20.709
27.949
1.00
34.17


ATOM
1785
CB
CYS
243
13.470
21.795
27.949
1.00
37.75


ATOM
1786
SG
CYS
243
14.547
22.600
29.193
1.00
41.04


ATOM
1787
N
ASN
244
11.465
21.029
26.301
1.00
32.89


ATOM
1788
CA
ASN
244
10.493
20.637
25.280
1.00
32.64


ATOM
1789
CB
ASN
244
11.122
20.572
23.886
1.00
32.57


ATOM
1790
CG
ASN
244
10.185
19.952
22.854
1.00
30.96


ATOM
1791
OD1
ASN
244
10.293
18.757
22.521
1.00
27.02


ATOM
1792
ND2
ASN
244
9.245
20.759
22.352
1.00
27.59


ATOM
1793
C
ASN
244
9.911
19.277
25.623
1.00
34.40


ATOM
1794
O
ASN
244
8.724
19.175
25.935
1.00
36.59


ATOM
1795
N
GLY
245
10.741
18.235
25.548
1.00
33.08


ATOM
1796
CA
GLY
245
10.274
16.910
25.907
1.00
30.30


ATOM
1797
C
GLY
245
9.784
17.150
27.307
1.00
30.36


ATOM
1798
O
GLY
245
10.491
17.757
28.110
1.00
32.61


ATOM
1799
N
GLY
246
8.584
16.696
27.616
1.00
29.59


ATOM
1800
CA
GLY
246
8.062
16.949
28.942
1.00
29.91


ATOM
1801
C
GLY
246
6.897
17.915
28.813
1.00
30.92


ATOM
1802
O
GLY
246
6.141
18.122
29.771
1.00
28.51


ATOM
1803
N
THR
247
6.751
18.512
27.626
1.00
31.78


ATOM
1804
CA
THR
247
5.646
19.431
27.364
1.00
32.55


ATOM
1805
CB
THR
247
6.039
20.521
26.378
1.00
29.13


ATOM
1806
OG1
THR
247
6.538
19.917
25.181
1.00
34.76


ATOM
1807
CG2
THR
247
7.099
21.402
26.966
1.00
28.24


ATOM
1808
C
THR
247
4.496
18.637
26.748
1.00
35.15


ATOM
1809
O
THR
247
4.673
17.468
26.373
1.00
32.84


ATOM
1810
N
LEU
248
3.329
19.273
26.629
1.00
37.01


ATOM
1811
CA
LEU
248
2.164
18.600
26.070
1.00
36.63


ATOM
1812
CB
LEU
248
1.197
18.251
27.191
1.00
31.69


ATOM
1813
CG
LEU
248
1.729
17.092
28.023
1.00
30.56


ATOM
1814
CD1
LEU
248
0.903
16.929
29.279
1.00
27.80


ATOM
1815
CD2
LEU
248
1.715
15.829
27.176
1.00
26.69


ATOM
1816
C
LEU
248
1.433
19.380
24.990
1.00
37.81


ATOM
1817
O
LEU
248
1.881
20.452
24.550
1.00
38.54


ATOM
1818
N
GLY
249
0.314
18.818
24.541
1.00
38.01


ATOM
1819
CA
GLY
249
−0.462
19.488
23.520
1.00
39.37


ATOM
1820
C
GLY
249
−0.059
19.107
22.106
1.00
38.76


ATOM
1821
O
GLY
249
0.797
18.238
21.873
1.00
37.04


ATOM
1822
N
LEU
250
−0.679
19.795
21.159
1.00
38.22


ATOM
1823
CA
LEU
250
−0.458
19.553
19.755
1.00
38.05


ATOM
1824
CB
LEU
250
−1.698
18.844
19.208
1.00
35.50


ATOM
1825
CG
LEU
250
−1.516
17.814
18.109
1.00
33.40


ATOM
1826
CD1
LEU
250
−2.861
17.207
17.780
1.00
36.98


ATOM
1827
CD2
LEU
250
−0.908
18.472
16.897
1.00
34.84


ATOM
1828
C
LEU
250
−0.265
20.916
19.091
1.00
36.02


ATOM
1829
O
LEU
250
−0.939
21.238
18.099
1.00
36.86


ATOM
1830
N
ASP
251
0.667
21.703
19.629
1.00
34.80


ATOM
1831
CA
ASP
251
0.918
23.027
19.088
1.00
33.81


ATOM
1832
CB
ASP
251
1.550
23.921
20.160
1.00
31.99


ATOM
1833
CG
ASP
251
1.572
25.398
19.764
1.00
33.18


ATOM
1834
OD1
ASP
251
2.033
26.236
20.581
1.00
31.63


ATOM
1835
OD2
ASP
251
1.131
25.724
18.638
1.00
35.47


ATOM
1836
C
ASP
251
1.804
22.963
17.847
1.00
33.35


ATOM
1837
O
ASP
251
2.873
23.571
17.806
1.00
36.22


ATOM
1838
N
ILE
252
1.336
22.233
16.836
1.00
32.44


ATOM
1839
CA
ILE
252
2.057
22.086
15.582
1.00
32.27


ATOM
1840
CB
ILE
252
1.186
21.361
14.523
1.00
33.71


ATOM
1841
CG2
ILE
252
1.772
21.563
13.132
1.00
33.09


ATOM
1842
CG1
ILE
252
1.076
19.862
14.853
1.00
35.60


ATOM
1843
CD1
ILE
252
0.206
19.058
13.909
1.00
35.69


ATOM
1844
C
ILE
252
2.481
23.443
15.028
1.00
33.10


ATOM
1845
O
ILE
252
3.450
23.533
14.270
1.00
36.41


ATOM
1846
N
ASP
253
1.762
24.496
15.402
1.00
33.30


ATOM
1847
CA
ASP
253
2.099
25.833
14.936
1.00
31.11


ATOM
1848
CB
ASP
253
1.158
26.854
15.557
1.00
30.03


ATOM
1849
CG
ASP
253
0.521
27.751
14.520
1.00
34.22


ATOM
1850
OD1
ASP
253
−0.079
28.786
14.894
1.00
36.89


ATOM
1851
OD2
ASP
253
0.619
27.415
13.320
1.00
37.40


ATOM
1852
C
ASP
253
3.528
26.169
15.348
1.00
29.66


ATOM
1853
O
ASP
253
4.332
26.690
14.566
1.00
28.81


ATOM
1854
N
ALA
254
3.817
25.855
16.603
1.00
26.55


ATOM
1855
CA
ALA
254
5.115
26.091
17.184
1.00
25.62


ATOM
1856
CB
ALA
254
5.140
25.564
18.598
1.00
20.85


ATOM
1857
C
ALA
254
6.196
25.405
16.345
1.00
29.11


ATOM
1858
O
ALA
254
7.213
26.018
15.997
1.00
31.34


ATOM
1859
N
HIS
255
5.986
24.137
16.013
1.00
27.36


ATOM
1860
CA
HIS
255
6.973
23.410
15.231
1.00
26.27


ATOM
1861
CB
HIS
255
6.428
22.033
14.880
1.00
24.83


ATOM
1862
CG
HIS
255
7.341
21.223
14.017
1.00
24.24


ATOM
1863
CD2
HIS
255
7.154
20.674
12.790
1.00
23.27


ATOM
1864
ND1
HIS
255
8.627
20.897
14.390
1.00
24.00


ATOM
1865
CE1
HIS
255
9.193
20.185
13.431
1.00
21.55


ATOM
1866
NE2
HIS
255
8.322
20.035
12.449
1.00
17.44


ATOM
1867
C
HIS
255
7.255
24.204
13.962
1.00
28.52


ATOM
1868
O
HIS
255
8.409
24.258
13.494
1.00
28.00


ATOM
1869
N
LEU
256
6.199
24.835
13.435
1.00
28.61


ATOM
1870
CA
LEU
256
6.265
25.621
12.207
1.00
28.55


ATOM
1871
CB
LEU
256
4.896
25.596
11.554
1.00
29.17


ATOM
1872
CG
LEU
256
4.695
24.226
10.899
1.00
33.99


ATOM
1873
CD1
LEU
256
3.236
23.981
10.647
1.00
38.97


ATOM
1874
CD2
LEU
256
5.494
24.144
9.599
1.00
35.28


ATOM
1875
C
LEU
256
6.749
27.045
12.359
1.00
29.39


ATOM
1876
O
LEU
256
6.735
27.824
11.410
1.00
31.07


ATOM
1877
N
HIS
257
7.185
27.371
13.567
1.00
29.83


ATOM
1878
CA
HIS
257
7.673
28.705
13.884
1.00
29.56


ATOM
1879
CB
HIS
257
6.605
29.480
14.656
1.00
32.53


ATOM
1880
CG
HIS
257
5.426
29.866
13.824
1.00
33.82


ATOM
1881
CD2
HIS
257
4.196
29.316
13.713
1.00
30.44


ATOM
1882
ND1
HIS
257
5.454
30.929
12.945
1.00
33.02


ATOM
1883
CE1
HIS
257
4.289
31.017
12.329
1.00
29.43


ATOM
1884
NE2
HIS
257
3.508
30.048
12.778
1.00
28.63


ATOM
1885
C
HIS
257
8.952
28.740
14.698
1.00
28.51


ATOM
1886
O
HIS
257
8.903
28.655
15.927
1.00
29.13


ATOM
1887
N
TYR
258
10.085
28.896
14.011
1.00
27.00


ATOM
1888
CA
TYR
258
11.407
29.000
14.646
1.00
25.03


ATOM
1889
CB
TYR
258
12.267
27.784
14.273
1.00
19.74


ATOM
1890
CG
TYR
258
11.874
26.563
15.076
1.00
17.11


ATOM
1891
CD1
TYR
258
10.716
25.851
14.768
1.00
17.80


ATOM
1892
CE1
TYR
258
10.301
24.765
15.565
1.00
19.70


ATOM
1893
CD2
TYR
258
12.617
26.158
16.197
1.00
15.62


ATOM
1894
CE2
TYR
258
12.216
25.074
16.977
1.00
18.52


ATOM
1895
CZ
TYR
258
11.060
24.380
16.660
1.00
21.26


ATOM
1896
OH
TYR
258
10.683
23.269
17.405
1.00
21.26


ATOM
1897
C
TYR
258
12.117
30.332
14.287
1.00
25.34


ATOM
1898
O
TYR
258
12.913
30.416
13.329
1.00
23.81


ATOM
1899
N
PHE
259
11.800
31.373
15.063
1.00
27.51


ATOM
1900
CA
PHE
259
12.347
32.716
14.846
1.00
30.42


ATOM
1901
CB
PHE
259
13.842
32.655
14.522
1.00
26.75


ATOM
1902
CG
PHE
259
14.682
32.157
15.645
1.00
27.90


ATOM
1903
CD1
PHE
259
14.429
32.559
16.958
1.00
30.40


ATOM
1904
CD2
PHE
259
15.769
31.325
15.401
1.00
29.77


ATOM
1905
CE1
PHE
259
15.247
32.145
18.006
1.00
31.66


ATOM
1906
CE2
PHE
259
16.604
30.904
16.472
1.00
25.94


ATOM
1907
CZ
PHE
259
16.335
31.317
17.760
1.00
27.26


ATOM
1908
C
PHE
259
11.610
33.315
13.658
1.00
32.76


ATOM
1909
O
PHE
259
11.661
34.518
13.400
1.00
35.13


ATOM
1910
N
GLN
260
10.913
32.462
12.932
1.00
31.61


ATOM
1911
CA
GLN
260
10.214
32.941
11.782
1.00
31.13


ATOM
1912
CB
GLN
260
11.229
33.310
10.703
1.00
27.17


ATOM
1913
CG
GLN
260
11.710
32.116
9.873
1.00
25.63


ATOM
1914
CD
GLN
260
12.849
32.468
8.940
1.00
26.16


ATOM
1915
OE1
GLN
260
13.064
31.793
7.937
1.00
27.34


ATOM
1916
NE2
GLN
260
13.598
33.520
9.275
1.00
31.37


ATOM
1917
C
GLN
260
9.352
31.798
11.323
1.00
34.49


ATOM
1918
O
GLN
260
9.301
30.750
11.950
1.00
35.38


ATOM
1919
N
ALA
261
8.657
32.008
10.218
1.00
36.41


ATOM
1920
CA
ALA
261
7.805
30.973
9.660
1.00
37.19


ATOM
1921
CB
ALA
261
6.737
31.591
8.766
1.00
34.82


ATOM
1922
C
ALA
261
8.657
29.993
8.852
1.00
40.12


ATOM
1923
O
ALA
261
9.423
30.386
7.961
1.00
37.41


ATOM
1924
N
THR
262
8.526
28.717
9.194
1.00
43.36


ATOM
1925
CA
THR
262
9.231
27.613
8.539
1.00
44.18


ATOM
1926
CB
THR
262
8.924
26.319
9.285
1.00
43.35


ATOM
1927
OG1
THR
262
9.612
26.303
10.537
1.00
44.23


ATOM
1928
CG2
THR
262
9.289
25.118
8.449
1.00
42.27


ATOM
1929
C
THR
262
8.739
27.416
7.097
1.00
46.97


ATOM
1930
O
THR
262
9.505
27.391
6.130
1.00
44.95


ATOM
1931
N
ASP
263
7.425
27.248
7.013
1.00
49.53


ATOM
1932
CA
ASP
263
6.660
27.035
5.798
1.00
48.98


ATOM
1933
CB
ASP
263
5.238
26.685
6.223
1.00
47.39


ATOM
1934
CG
ASP
263
4.644
27.730
7.170
1.00
50.68


ATOM
1935
OD1
ASP
263
5.279
28.036
8.199
1.00
51.25


ATOM
1936
OD2
ASP
263
3.542
28.255
6.887
1.00
53.12


ATOM
1937
C
ASP
263
6.635
28.246
4.847
1.00
49.91


ATOM
1938
O
ASP
263
5.878
28.258
3.876
1.00
50.87


ATOM
1939
N
ALA
264
7.464
29.253
5.107
1.00
48.36


ATOM
1940
CA
ALA
264
7.471
30.450
4.265
1.00
47.66


ATOM
1941
CB
ALA
264
8.601
31.406
4.678
1.00
46.98


ATOM
1942
C
ALA
264
7.615
30.083
2.797
1.00
48.80


ATOM
1943
O
ALA
264
6.810
30.519
1.961
1.00
46.94


ATOM
1944
N
CYS
265
8.621
29.261
2.488
1.00
52.02


ATOM
1945
CA
CYS
265
8.858
28.862
1.107
1.00
52.57


ATOM
1946
C
CYS
265
8.071
27.619
0.660
1.00
53.21


ATOM
1947
O
CYS
265
8.410
27.015
−0.352
1.00
52.62


ATOM
1948
CB
CYS
265
10.356
28.641
0.894
1.00
51.98


ATOM
1949
SG
CYS
265
10.914
29.221
−0.736
1.00
62.77


ATOM
1950
N
SER
266
7.016
27.256
1.397
1.00
55.18


ATOM
1951
CA
SER
266
6.186
26.076
1.094
1.00
55.25


ATOM
1952
CB
SER
266
5.315
26.296
−0.163
1.00
55.01


ATOM
1953
OG
SER
266
6.059
26.313
−1.376
1.00
53.51


ATOM
1954
C
SER
266
7.013
24.807
0.920
1.00
57.82


ATOM
1955
O
SER
266
6.771
23.800
1.592
1.00
58.50


ATOM
1956
N
THR
288
−5.104
10.709
9.431
1.00
69.17


ATOM
1957
CA
THR
288
−6.163
9.702
9.336
1.00
68.04


ATOM
1958
CB
THR
288
−5.575
8.326
8.904
1.00
69.10


ATOM
1959
OG1
THR
288
−4.241
8.190
9.427
1.00
71.00


ATOM
1960
CG2
THR
288
−5.550
8.209
7.381
1.00
66.83


ATOM
1961
C
THR
288
−6.897
9.563
10.669
1.00
66.62


ATOM
1962
O
THR
288
−7.678
8.635
10.867
1.00
67.87


ATOM
1963
N
MET
289
−6.637
10.504
11.573
1.00
63.79


ATOM
1964
CA
MET
289
−7.267
10.517
12.887
1.00
59.84


ATOM
1965
CB
MET
289
−6.376
9.822
13.911
1.00
60.37


ATOM
1966
CG
MET
289
−5.070
10.549
14.185
1.00
58.53


ATOM
1967
SD
MET
289
−4.097
9.750
15.488
1.00
55.89


ATOM
1968
CE
MET
289
−3.213
8.434
14.513
1.00
53.56


ATOM
1969
C
MET
289
−7.504
11.958
13.308
1.00
56.91


ATOM
1970
O
MET
289
−6.766
12.851
12.911
1.00
56.23


ATOM
1971
N
THR
290
−8.523
12.178
14.128
1.00
55.14


ATOM
1972
CA
THR
290
−8.862
13.526
14.563
1.00
55.59


ATOM
1973
CB
THR
290
−10.041
13.530
15.540
1.00
55.73


ATOM
1974
OG1
THR
290
−9.587
13.157
16.847
1.00
56.69


ATOM
1975
CG2
THR
290
−11.103
12.551
15.081
1.00
57.65


ATOM
1976
C
THR
290
−7.722
14.275
15.228
1.00
55.10


ATOM
1977
O
THR
290
−6.549
13.938
15.071
1.00
57.70


ATOM
1978
N
ASP
291
−8.086
15.311
15.969
1.00
53.52


ATOM
1979
CA
ASP
291
−7.113
16.122
16.666
1.00
53.03


ATOM
1980
CB
ASP
291
−7.539
17.584
16.604
1.00
53.76


ATOM
1981
CG
ASP
291
−6.579
18.435
15.798
1.00
53.50


ATOM
1982
OD1
ASP
291
−6.217
18.039
14.670
1.00
54.08


ATOM
1983
OD2
ASP
291
−6.186
19.509
16.294
1.00
53.04


ATOM
1984
C
ASP
291
−7.032
15.648
18.108
1.00
53.15


ATOM
1985
O
ASP
291
−5.974
15.205
18.567
1.00
50.18


ATOM
1986
N
ALA
292
−8.164
15.732
18.807
1.00
54.12


ATOM
1987
CA
ALA
292
−8.254
15.306
20.201
1.00
53.85


ATOM
1988
CB
ALA
292
−9.705
15.131
20.603
1.00
55.19


ATOM
1989
C
ALA
292
−7.540
13.988
20.293
1.00
52.42


ATOM
1990
O
ALA
292
−6.840
13.687
21.244
1.00
53.42


ATOM
1991
N
GLU
293
−7.749
13.198
19.264
1.00
52.24


ATOM
1992
CA
GLU
293
−7.121
11.906
19.160
1.00
55.82


ATOM
1993
CB
GLU
293
−7.529
11.259
17.837
1.00
59.67


ATOM
1994
CG
GLU
293
−6.842
9.964
17.550
1.00
64.61


ATOM
1995
CD
GLU
293
−7.295
8.872
18.483
1.00
67.82


ATOM
1996
OE1
GLU
293
−7.070
9.000
19.708
1.00
67.87


ATOM
1997
OE2
GLU
293
−7.883
7.886
17.987
1.00
70.08


ATOM
1998
C
GLU
293
−5.602
12.064
19.218
1.00
54.54


ATOM
1999
O
GLU
293
−4.964
11.753
20.230
1.00
52.29


ATOM
2000
N
LEU
294
−5.034
12.569
18.127
1.00
52.22


ATOM
2001
CA
LEU
294
−3.594
12.745
18.036
1.00
49.88


ATOM
2002
CB
LEU
294
−3.213
13.548
16.782
1.00
46.75


ATOM
2003
CG
LEU
294
−1.734
13.465
16.357
1.00
46.25


ATOM
2004
CD1
LEU
294
−1.411
12.023
15.956
1.00
41.73


ATOM
2005
CD2
LEU
294
−1.450
14.414
15.187
1.00
45.50


ATOM
2006
C
LEU
294
−3.012
13.418
19.262
1.00
49.36


ATOM
2007
O
LEU
294
−1.936
13.061
19.715
1.00
48.76


ATOM
2008
N
GLU
295
−3.714
14.397
19.810
1.00
49.05


ATOM
2009
CA
GLU
295
−3.183
15.071
20.981
1.00
47.81


ATOM
2010
CB
GLU
295
−4.094
16.204
21.408
1.00
48.38


ATOM
2011
CG
GLU
295
−3.765
16.655
22.787
1.00
50.22


ATOM
2012
CD
GLU
295
−4.643
17.782
23.219
1.00
52.29


ATOM
2013
OE1
GLU
295
−4.536
18.869
22.617
1.00
54.49


ATOM
2014
OE2
GLU
295
−5.450
17.580
24.154
1.00
52.86


ATOM
2015
C
GLU
295
−3.055
14.084
22.126
1.00
46.68


ATOM
2016
O
GLU
295
−2.019
14.009
22.801
1.00
45.14


ATOM
2017
N
LYS
296
−4.129
13.341
22.352
1.00
45.98


ATOM
2018
CA
LYS
296
−4.123
12.365
23.405
1.00
47.29


ATOM
2019
CB
LYS
296
−5.454
11.633
23.432
1.00
47.12


ATOM
2020
CG
LYS
296
−6.558
12.517
23.981
1.00
47.16


ATOM
2021
CD
LYS
296
−7.900
11.809
24.010
1.00
50.91


ATOM
2022
CE
LYS
296
−8.985
12.717
24.580
1.00
49.77


ATOM
2023
NZ
LYS
296
−10.319
12.055
24.645
1.00
50.40


ATOM
2024
C
LYS
296
−2.963
11.411
23.204
1.00
45.67


ATOM
2025
O
LYS
296
−2.025
11.405
24.001
1.00
45.50


ATOM
2026
N
LYS
297
−3.007
10.620
22.141
1.00
45.96


ATOM
2027
CA
LYS
297
−1.927
9.678
21.894
1.00
46.33


ATOM
2028
CB
LYS
297
−1.922
9.248
20.447
1.00
45.64


ATOM
2029
CG
LYS
297
−3.017
8.264
20.143
1.00
49.76


ATOM
2030
CD
LYS
297
−3.095
7.965
18.652
1.00
52.12


ATOM
2031
CE
LYS
297
−4.241
7.000
18.307
1.00
53.58


ATOM
2032
NZ
LYS
297
−4.433
6.842
16.829
1.00
55.41


ATOM
2033
C
LYS
297
−0.578
10.252
22.236
1.00
45.70


ATOM
2034
O
LYS
297
0.164
9.692
23.040
1.00
45.62


ATOM
2035
N
LEU
298
−0.275
11.392
21.639
1.00
43.91


ATOM
2036
CA
LEU
298
0.997
12.035
21.873
1.00
43.35


ATOM
2037
CB
LEU
298
1.104
13.280
21.030
1.00
42.24


ATOM
2038
CG
LEU
298
1.281
12.939
19.560
1.00
42.32


ATOM
2039
CD1
LEU
298
1.715
14.203
18.864
1.00
40.59


ATOM
2040
CD2
LEU
298
2.330
11.824
19.372
1.00
39.55


ATOM
2041
C
LEU
298
1.257
12.381
23.307
1.00
43.14


ATOM
2042
O
LEU
298
2.360
12.228
23.806
1.00
43.84


ATOM
2043
N
ASN
299
0.231
12.869
23.970
1.00
42.30


ATOM
2044
CA
ASN
299
0.369
13.215
25.367
1.00
40.09


ATOM
2045
CB
ASN
299
−0.987
13.640
25.937
1.00
39.75


ATOM
2046
CG
ASN
299
−1.236
15.126
25.817
1.00
39.45


ATOM
2047
OD1
ASN
299
−0.602
15.841
25.020
1.00
36.52


ATOM
2048
ND2
ASN
299
−2.182
15.604
26.610
1.00
39.54


ATOM
2049
C
ASN
299
0.845
11.952
26.061
1.00
39.47


ATOM
2050
O
ASN
299
1.896
11.917
26.688
1.00
39.95


ATOM
2051
N
SER
300
0.030
10.915
25.909
1.00
36.98


ATOM
2052
CA
SER
300
0.255
9.596
26.477
1.00
32.52


ATOM
2053
CB
SER
300
−0.477
8.546
25.651
1.00
32.63


ATOM
2054
OG
SER
300
0.327
7.392
25.490
1.00
40.74


ATOM
2055
C
SER
300
1.725
9.242
26.529
1.00
31.83


ATOM
2056
O
SER
300
2.242
8.833
27.582
1.00
26.37


ATOM
2057
N
TYR
301
2.382
9.392
25.381
1.00
32.44


ATOM
2058
CA
TYR
301
3.793
9.096
25.255
1.00
33.17


ATOM
2059
CB
TYR
301
4.245
9.455
23.850
1.00
31.08


ATOM
2060
CG
TYR
301
3.738
8.476
22.832
1.00
31.92


ATOM
2061
CD1
TYR
301
3.218
8.903
21.611
1.00
34.78


ATOM
2062
CE1
TYR
301
2.692
7.981
20.684
1.00
35.21


ATOM
2063
CD2
TYR
301
3.737
7.109
23.108
1.00
32.63


ATOM
2064
CE2
TYR
301
3.220
6.183
22.202
1.00
33.64


ATOM
2065
CZ
TYR
301
2.693
6.625
20.993
1.00
36.58


ATOM
2066
OH
TYR
301
2.122
5.720
20.122
1.00
42.92


ATOM
2067
C
TYR
301
4.650
9.814
26.289
1.00
33.19


ATOM
2068
O
TYR
301
5.382
9.169
27.062
1.00
33.66


ATOM
2069
N
VAL
302
4.551
11.146
26.291
1.00
31.53


ATOM
2070
CA
VAL
302
5.309
11.986
27.207
1.00
31.88


ATOM
2071
CB
VAL
302
5.184
13.516
26.830
1.00
30.64


ATOM
2072
CG1
VAL
302
3.806
13.804
26.245
1.00
34.62


ATOM
2073
CG2
VAL
302
5.425
14.390
28.033
1.00
28.18


ATOM
2074
C
VAL
302
4.872
11.714
28.638
1.00
34.16


ATOM
2075
O
VAL
302
5.579
12.060
29.582
1.00
35.35


ATOM
2076
N
GLU
303
3.725
11.075
28.822
1.00
37.44


ATOM
2077
CA
GLU
303
3.322
10.774
30.182
1.00
38.93


ATOM
2078
CB
GLU
303
1.814
10.559
30.249
1.00
41.44


ATOM
2079
CG
GLU
303
1.131
11.315
31.410
1.00
48.53


ATOM
2080
CD
GLU
303
1.164
12.848
31.252
1.00
53.98


ATOM
2081
OE1
GLU
303
0.499
13.392
30.337
1.00
55.14


ATOM
2082
OE2
GLU
303
1.861
13.520
32.046
1.00
56.20


ATOM
2083
C
GLU
303
4.094
9.512
30.572
1.00
38.83


ATOM
2084
O
GLU
303
4.418
9.294
31.745
1.00
41.64


ATOM
2085
N
MET
304
4.405
8.693
29.570
1.00
37.27


ATOM
2086
CA
MET
304
5.155
7.467
29.801
1.00
35.94


ATOM
2087
CB
MET
304
4.953
6.478
28.650
1.00
31.52


ATOM
2088
CG
MET
304
3.579
5.858
28.595
1.00
31.49


ATOM
2089
SD
MET
304
3.184
4.590
29.827
1.00
28.57


ATOM
2090
CE
MET
304
2.746
5.557
31.251
1.00
29.07


ATOM
2091
C
MET
304
6.632
7.809
29.934
1.00
37.54


ATOM
2092
O
MET
304
7.336
7.256
30.778
1.00
37.89


ATOM
2093
N
ASP
305
7.099
8.729
29.098
1.00
36.62


ATOM
2094
CA
ASP
305
8.494
9.138
29.142
1.00
36.97


ATOM
2095
CB
ASP
305
8.789
10.139
28.020
1.00
35.93


ATOM
2096
CG
ASP
305
8.797
9.478
26.641
1.00
35.21


ATOM
2097
OD1
ASP
305
9.366
8.364
26.550
1.00
26.08


ATOM
2098
OD2
ASP
305
8.256
10.063
25.663
1.00
35.03


ATOM
2099
C
ASP
305
8.830
9.727
30.507
1.00
36.38


ATOM
2100
O
ASP
305
9.907
9.521
31.037
1.00
36.84


ATOM
2101
N
LYS
306
7.878
10.407
31.112
1.00
34.64


ATOM
2102
CA
LYS
306
8.121
10.992
32.416
1.00
35.44


ATOM
2103
CB
LYS
306
7.036
12.016
32.739
1.00
34.65


ATOM
2104
CG
LYS
306
7.286
13.335
32.039
1.00
35.30


ATOM
2105
CD
LYS
306
6.029
14.155
31.857
1.00
42.10


ATOM
2106
CE
LYS
306
5.507
14.747
33.147
1.00
45.04


ATOM
2107
NZ
LYS
306
4.285
15.551
32.855
1.00
48.24


ATOM
2108
C
LYS
306
8.178
9.927
33.488
1.00
35.92


ATOM
2109
O
LYS
306
9.026
9.975
34.392
1.00
34.83


ATOM
2110
N
GLU
307
7.281
8.955
33.369
1.00
38.05


ATOM
2111
CA
GLU
307
7.209
7.871
34.334
1.00
41.32


ATOM
2112
CB
GLU
307
6.007
6.986
34.035
1.00
41.96


ATOM
2113
CG
GLU
307
5.559
6.166
35.230
1.00
44.27


ATOM
2114
CD
GLU
307
4.739
4.938
34.841
1.00
44.72


ATOM
2115
OE1
GLU
307
3.890
5.025
33.925
1.00
42.09


ATOM
2116
OE2
GLU
307
4.938
3.876
35.470
1.00
46.86


ATOM
2117
C
GLU
307
8.478
7.042
34.251
1.00
40.66


ATOM
2118
O
GLU
307
8.914
6.445
35.227
1.00
39.62


ATOM
2119
N
TYR
308
9.040
6.993
33.050
1.00
39.89


ATOM
2120
CA
TYR
308
10.271
6.265
32.795
1.00
38.66


ATOM
2121
CB
TYR
308
10.647
6.328
31.306
1.00
38.72


ATOM
2122
CG
TYR
308
11.998
5.698
30.995
1.00
35.82


ATOM
2123
CD1
TYR
308
12.092
4.412
30.447
1.00
34.01


ATOM
2124
CE1
TYR
308
13.326
3.802
30.244
1.00
33.27


ATOM
2125
CD2
TYR
308
13.186
6.354
31.323
1.00
35.59


ATOM
2126
CE2
TYR
308
14.430
5.744
31.126
1.00
35.52


ATOM
2127
CZ
TYR
308
14.494
4.468
30.592
1.00
35.24


ATOM
2128
OH
TYR
308
15.722
3.846
30.457
1.00
32.71


ATOM
2129
C
TYR
308
11.344
6.968
33.597
1.00
38.16


ATOM
2130
O
TYR
308
11.987
6.384
34.466
1.00
42.33


ATOM
2131
N
ILE
309
11.546
8.236
33.279
1.00
34.53


ATOM
2132
CA
ILE
309
12.539
9.008
33.978
1.00
33.96


ATOM
2133
CB
ILE
309
12.485
10.482
33.553
1.00
31.45


ATOM
2134
CG2
ILE
309
12.843
11.392
34.737
1.00
28.90


ATOM
2135
CG1
ILE
309
13.412
10.670
32.339
1.00
30.32


ATOM
2136
CD1
ILE
309
13.436
12.066
31.764
1.00
34.28


ATOM
2137
C
ILE
309
12.345
8.877
35.466
1.00
35.18


ATOM
2138
O
ILE
309
13.295
8.668
36.212
1.00
33.45


ATOM
2139
N
LYS
310
11.103
8.981
35.897
1.00
38.85


ATOM
2140
CA
LYS
310
10.825
8.872
37.313
1.00
39.29


ATOM
2141
CB
LYS
310
9.323
8.894
37.541
1.00
37.16


ATOM
2142
CG
LYS
310
8.964
8.558
38.953
1.00
35.69


ATOM
2143
CD
LYS
310
7.641
7.848
38.996
1.00
38.63


ATOM
2144
CE
LYS
310
7.527
7.081
40.307
1.00
39.65


ATOM
2145
NZ
LYS
310
6.351
6.171
40.381
1.00
44.93


ATOM
2146
C
LYS
310
11.403
7.596
37.902
1.00
38.47


ATOM
2147
O
LYS
310
12.210
7.610
38.830
1.00
38.54


ATOM
2148
N
THR
311
10.972
6.491
37.330
1.00
38.54


ATOM
2149
CA
THR
311
11.370
5.180
37.784
1.00
38.10


ATOM
2150
CB
THR
311
10.551
4.112
37.056
1.00
37.44


ATOM
2151
OG1
THR
311
10.847
2.832
37.622
1.00
42.06


ATOM
2152
CG2
THR
311
10.868
4.114
35.559
1.00
33.19


ATOM
2153
C
THR
311
12.842
4.828
37.666
1.00
36.98


ATOM
2154
O
THR
311
13.253
3.757
38.093
1.00
38.27


ATOM
2155
N
HIS
312
13.637
5.724
37.102
1.00
36.25


ATOM
2156
CA
HIS
312
15.071
5.476
36.940
1.00
36.32


ATOM
2157
CB
HIS
312
15.442
5.505
35.455
1.00
36.87


ATOM
2158
CG
HIS
312
14.998
4.294
34.693
1.00
42.97


ATOM
2159
CD2
HIS
312
13.776
3.730
34.531
1.00
46.21


ATOM
2160
ND1
HIS
312
15.876
3.515
33.971
1.00
43.74


ATOM
2161
CE1
HIS
312
15.217
2.522
33.396
1.00
45.94


ATOM
2162
NE2
HIS
312
13.939
2.630
33.719
1.00
48.05


ATOM
2163
C
HIS
312
15.893
6.520
37.693
1.00
34.17


ATOM
2164
O
HIS
312
17.119
6.534
37.654
1.00
29.16


ATOM
2165
N
ALA
313
15.195
7.398
38.389
1.00
34.95


ATOM
2166
CA
ALA
313
15.841
8.461
39.137
1.00
37.67


ATOM
2167
CB
ALA
313
14.808
9.133
40.053
1.00
33.12


ATOM
2168
C
ALA
313
17.077
8.046
39.945
1.00
36.45


ATOM
2169
O
ALA
313
18.137
8.654
39.811
1.00
35.64


ATOM
2170
N
SER
314
16.935
7.006
40.763
1.00
35.30


ATOM
2171
CA
SER
314
18.004
6.519
41.636
1.00
34.86


ATOM
2172
CB
SER
314
17.387
5.751
42.799
1.00
32.67


ATOM
2173
OG
SER
314
16.772
4.571
42.292
1.00
37.73


ATOM
2174
C
SER
314
19.021
5.598
40.964
1.00
34.47


ATOM
2175
O
SER
314
19.721
4.842
41.648
1.00
35.60


ATOM
2176
N
ARG
315
19.110
5.661
39.643
1.00
34.13


ATOM
2177
CA
ARG
315
20.026
4.801
38.923
1.00
33.01


ATOM
2178
CB
ARG
315
19.315
4.214
37.709
1.00
30.87


ATOM
2179
CG
ARG
315
18.160
3.289
38.078
1.00
33.01


ATOM
2180
CD
ARG
315
18.596
1.841
38.115
1.00
30.79


ATOM
2181
NE
ARG
315
18.950
1.363
36.782
1.00
27.06


ATOM
2182
CZ
ARG
315
20.135
0.871
36.456
1.00
23.56


ATOM
2183
NH1
ARG
315
21.079
0.788
37.372
1.00
19.72


ATOM
2184
NH2
ARG
315
20.368
0.476
35.214
1.00
19.00


ATOM
2185
C
ARG
315
21.316
5.486
38.508
1.00
36.88


ATOM
2186
O
ARG
315
21.687
6.530
39.056
1.00
33.34


ATOM
2187
N
SER
316
21.992
4.873
37.533
1.00
42.86


ATOM
2188
CA
SER
316
23.281
5.337
36.997
1.00
44.60


ATOM
2189
CB
SER
316
23.248
6.850
36.667
1.00
45.66


ATOM
2190
OG
SER
316
24.311
7.227
35.802
1.00
45.23


ATOM
2191
C
SER
316
24.329
5.034
38.070
1.00
44.35


ATOM
2192
O
SER
316
25.091
4.052
37.885
1.00
46.99


ATOM
2193
OXT
SER
316
24.345
5.751
39.093
1.00
40.99

## Claims

1. An isolated peptide having phospholipase inhibitory activity, wherein the peptide has a length of at least 15 amino acids and less than 40 amino acids and the peptide is selected from the group consisting of:
a) a peptide having at least 65% identity to residues 289-310 of SEQ ID NO: 1 or residues 154-175 of SEQ ID. NO: 10; and
b) a peptide comprising a motif with the following amino acid sequence (SEQ ID NO: 32):








Met Thr Asp Xaa Xaa Leu Glu Xaa Lys Leu Asn Xaa Tyr


                5                   10


 


Val Xaa Xaa Asp Xaa Glu Tyr Xaa Lys


    15                  20






wherein Xaa at positions 4, 5, 8, 12, 15, 16, 18, and 21 are independently any amino acid.

2. The peptide of claim 1, which has at least 70% identity to residues 289-310 of SEQ ID NO: 1 or residues 154-175 of SEQ ID. NO: 10.

3. The peptide of claim 1, which has at least 75% identity to residues 289-310 of SEQ ID NO: 1 or residues 154-175 of SEQ ID. NO: 10.

4. The peptide of claim 1, which has at least 80% identity to residues 289-310 of SEQ ID NO: 1 or residues 154-175 of SEQ ID. NO: 10.

5. The peptide of claim 1, which has at least 85% identity to residues 289-310 of SEQ ID NO: 1 or residues 154-175 of SEQ ID. NO: 10.

6. The peptide of claim 1, which has at least 90% identity to residues 289-310 of SEQ ID NO: 1 or residues 154-175 of SEQ ID. NO: 10.

7. The peptide of claim 1, which has at least 95% identity to residues 289-310 of SEQ ID NO: 1 or residues 154-175 of SEQ ID. NO: 10.

8. The peptide of claim 1, which has at least 97% identity to residues 289-310 of SEQ ID NO: 1 or residues 154-175 of SEQ ID. NO: 10.

9. The peptide of claim 1, which has 100% identity to residues 289-310 of SEQ ID NO: 1 or residues 154-175 of SEQ ID. NO: 10.

10. The peptide of claim 6, which has a length of less than 35 amino acids.

11. The peptide of claim 6, which has a length of less than 30 amino acids.

12. The peptide of claim 6, which has a length of at least 20 amino acids.

13. The peptide of claim 6, which has a length of at least 25 amino acids.

14. The peptide of claim 1, having a secondary structure of an alpha helix.

15. The peptide of claim 1, which comprises the motif wherein
Xaa at position 4 is A or E;
Xaa at position 5 is E or Q;
Xaa at position 8 is K or A;
Xaa at position 12 is S or N;
Xaa at position 15 is E, Q or A;
Xaa at position 16 is L or M;
Xaa at position 18 is K or Q; and/or
Xaa at position 21 is I or V.

16. The peptide of claim 1, which comprises at least one amino acid substitution at a position corresponding to position D291; L294; E295; K297; L298; N299; Y301; D305; K306; Y308; or V309 of SEQ ID NO: 1.

17. The peptide according to claim 16, wherein the at least one amino acid substitution is selected from the group consisting of D291E; L294A; E295T,S; K297R; L298A; N299D,E; Y301W; D305A; K306R; Y308E,D; and V309I,N,Q.

18. A polypeptide comprising a lipase and the peptide of claim 1 as a C-terminal extension, wherein the polypeptide has a phospholipase activity below 50 PHLU/mg in a plate assay.

19. The polypeptide of claim 18, wherein the lipase has at least 75% identity to SEQ ID NO: 9.

20. The polypeptide of claim 18, wherein the lipase has at least 80% identity to SEQ ID NO: 9.

21. The polypeptide of claim 18, wherein the lipase has at least 85% identity to SEQ ID NO: 9.

22. The polypeptide of claim 18, wherein the lipase has at least 90% identity to SEQ ID NO: 9.

23. The polypeptide of claim 18, wherein the lipase has at least 95% identity to SEQ ID NO: 9.