# Patent

## Title
Method for preparing maltogenic alpha-amylase variants

## Abstract

The inventors have modified the amino acid sequence of a maltogenic alpha-amylase to obtain variants with improved properties, based on the three-dimensional structure of the maltogenic alpha-amylase Novamyl. The variants have altered physicochemical properties, e.g. an altered pH optimum, improved thermostability, increased specific activity, an altered cleavage pattern or an increased ability to reduce retrogradation of starch or staling of bread.

## Background
CROSS-REFERENCE TO RELATED APPLICATIONS
This application is a continuation of U.S. application Ser. No. 12/413,758 filed on Mar. 30, 2009 (now U.S. Pat. No. 7,908,094), which is a continuation of U.S. application Ser. No. 11/037,573 (abandoned) filed on Jan. 18, 2005, which is a continuation of U.S. application Ser. No. 09/607,142 (now U.S. Pat. No. 6,876,932) filed Jun. 29, 2000, which is a divisional of U.S. application Ser. No. 09/386,607 (now U.S. Pat. No. 6,162,628), filed Aug. 31, 1999, which is a continuation in part of PCT/DK99/00088, filed Feb. 26, 1999 which claims priority or the benefit under 35 U.S.C. 119 of Danish application no. 98/00269, filed Feb. 27, 1998 and U.S. Provisional application No. 60/077,795, filed Mar. 12, 1998, the contents of which are fully incorporated herein by reference.


FIELD OF THE INVENTION
The present invention relates to variants of maltogenic amylase and to methods of constructing such variants.
BACKGROUND OF THE INVENTION
Maltogenic alpha-amylase (glucan 1,4-α-maltohydrolase, E.C. 3.2.1.133) is able to hydrolyze amylose and amylopectin to maltose in the alpha-configuration, and is also able to hydrolyze maltotriose as well as cyclodextrin.
A maltogenic alpha-amylase from Bacillus (EP 120 693) is commercially available under the trade name Novamyl® (product of Novo Nordisk A/S, Denmark) and is widely used in the baking industry as an anti-staling agent due to its ability to reduce retrogradation of starch (WO 91/04669). It is most active at 60-70° C. (Christophersen, C., et al., 1997, Starch, vol. 50, No. 1, 39-45).
Novamyl® shares several characteristics with cyclodextrin glucanotransferases (CGTases), including sequence homology (Henrissat B., Bairoch A. 1996) and formation of transglycosylation products (Christophersen, C., et al., 1997, Starch, vol. 50, No. 1, 39-45). Cyclomaltodextrin glucanotransferase (E.C. 2.4.1.19), also designated cyclodextrin glucanotransferase or cyclodextrin glycosyltransferase, abbreviated herein as CGTase, catalyses the conversion of starch and similar substrates into cyclomaltodextrins via an intramolecular transglycosylation reaction, thereby forming cyclomaltodextrins (or CD) of various sizes.
CGTases are widely distributed and from several different bacterial sources, including Bacillus, Brevibacterium, Clostridium, Corynebacterium, Klebsiella, Micrococcus, Thermoanaerobacter and Thermoanaerobacterium have been extensively described in the literature. A CGTase produced by Thermoanaerobacter sp. has been reported in Norman B E, Jørgensen S T; Denpun Kaqaku 1992 39 99-106, and WO 89/03421, and the amino acid sequence has been disclosed in WO 96/33267. The sequence of CGTases from Thermoanaerobacterium thermosulfurigenes and from Bacillus circulansis available on the Internet (SCOP or PDF home pages) as pdf file 1 CIU, and the sequence of a CGTase from B. circulans is available as pdf file 1CDG.
Tachibana, Y., Journal of Fermentation and Bioengineering, 83 (6), 540-548 (1997) describes the cloning and expression of a CGTase. Variants of CGTases have been described by Kim, Y. H., Biochemistry and Molecular Biology International, 41 (2), 227-234 (1997); Sin K-A, Journal of Biotechnology, 32 (3), 283-288 (1994); D Penning a, Biochemistry, 34 (10), 3368-3376 (1995); and WO 96/33267.
Recently, the tertiary structure of several CGTases have been reported. Hofman et al. [Hofman B E, Bender H, Schultz G E; J. Mol. Biol. 1989 209 793-800] and Klein & Schulz [Klein C, Schulz G E; J. Mol. Biol. 1991 217 737-750] report the tertiary structure of a CGTase derived from Bacillus circulans Strain 8, Kubota et al. [Kubota M, Matsuura Y, Sakai S and Katsube Y; Denpun Kaqaku 1991 38 141-146] report the tertiary structure of a CGTase derived from Bacillus stearothermophilus TC-91, Lawson et al. [Lawson C L, van Montfort R, Strokopytov B, Rozeboom H J, Kalk K H, de Vries G E, Penning a D, Dijkhuizen L, and Dijkstra B W; J. Mol. Biol. 1994 236 590-600] report the tertiary structure of a CGTase derived from Bacillus circulans Strain 251, Strokopytov et al. [Strokopytov B, Penning a D, Rozeboom H J; Kalk K H, Dijkhuizen L and Dijkstra B W; Biochemistry 1995 34 2234-2240] report the tertiary structure of a CGTase derived from Bacillus circulans Strain 251, which CGTase has been complexed with acarbose, an effective CGTase inhibitor, and Knegtel et al. [Knegtel R M A, Wind R D, Rozeboom H J, Kalk K H, Buitelaar R M, Dijkhuizen L and Dijkstra B W; J. Mol. Biol. 1996 256 611-622] report the tertiary structure of a CGTase derived from Thermoanaerobacterium thermosulfurigenes. 



BRIEF DESCRIPTION OF THE FIGURE
FIG. 1 shows the plasmid pLBei010, which contains the Bacillus stearothermophilus maltogenic amylase gene.



DETAILED DISCLOSURE OF THE INVENTION
The inventors have found that the anti-staling effect of a maltogenic amylase can be improved by using a variant having increased thermostability. Further, they found that such a variant improves the softness of baked products in the initial period after baking, particularly the first 24 hours after baking, so that the baked product has improved softness, both when eaten on the same day and when stored for several days after baking.
Accordingly, the invention provides a polypeptide which:
a) has maltogenic amylase activity;
b) has at least 70% identity to SEQ ID NO: 2,
c) has optimum maltogenic amylase activity in the range pH 3.5-7.0 (preferably 4-5.5), and
d) shows a residual maltogenic amylase activity of at least 25% after incubation with 1 mM Ca++ at pH 4.3, 80° C. for 15 minutes.
The inventors found that thermostable variants can be prepared by random DNA mutagenesis followed by screening for thermostable variants. Thus, the invention also provides a method of preparing a maltogenic amylase variant having improved anti-staling properties, which method comprises
a) subjecting a DNA sequence encoding the maltogenic amylase to random mutagenesis,
b) expressing the mutated DNA sequence obtained in step (a) in a host cell, and
c) screening for host cells expressing a mutated maltogenic amylase which shows a higher thermostability, and
d) preparing the mutated maltogenic amylase expressed by the host cells.
Further, the inventors have modified the amino acid sequence of a maltogenic alpha-amylase to obtain variants with improved properties, based on the three-dimensional structure of the maltogenic alpha-amylase Novamyl. The variants have altered physicochemical properties, e.g. an altered pH optimum, improved thermostability, increased specific activity, an altered cleavage pattern or an increased ability to reduce retrogradation of starch or staling of bread.
Accordingly, the present invention provides a method of constructing a variant of a parent maltogenic alpha-amylase, wherein the variant has at least one altered property as compared to said parent maltogenic alpha-amylase, which method comprises:
i) analyzing the structure of the maltogenic alpha-amylase to identify, on the basis of an evaluation of structural considerations, at least one amino acid residue or at least one structural region of the maltogenic alpha-amylase, which is of relevance for altering said property;
ii) constructing a variant of the maltogenic alpha-amylase, which as compared to the parent, has been modified in the amino acid residue or structural part identified in i) so as to alter said property; and
iii) testing the resulting maltogenic alpha-amylase variant for said property.
The property which may be altered by the above methods of the present invention may be, e.g., stability, pH dependent activity, ability to reduce retrogradation of starch or staling of bread, specific activity, or substrate specificity. Thus, the variant may have, e.g., increased thermostability or higher activity at a lower pH an altered pH optimum, improved thermostability, increased specific activity or increased ability to reduce retrogradation of starch or staling of bread
In still further aspects the invention relates to variants of a maltogenic alpha-amylase, the DNA encoding such variants and methods of preparing the variants. Finally, the invention relates to the use of the variants for various industrial purposes, in particular baking.
DETAILED DISCLOSURE OF THE INVENTION
Maltogenic Alpha-Amylase
The maltogenic alpha-amylase is an enzyme classified in EC 3.2.1.133. The enzymatic activity does not require a non-reducing end on the substrate and the primary enzymatic activity results in the degradation of amylopectin and amylose to maltose and longer maltodextrins. It is able to hydrolyze amylose and amylopectin to maltose in the alpha-configuration, and is also able to hydrolyze maltotriose as well as cyclodextrin.
A particularly preferred maltogenic alpha-amylase is the amylase cloned from Bacillus as described in EP 120 693 (hereinafter referred to as Novamyl). Novamyl has the amino acid sequence set forth in amino acids 1-686 of SEQ ID NO: 2. Novamyl is encoded in the gene harbored in the Bacillus strain NCIB 11837 which has the nucleic acid sequence set forth in SEQ ID NO:1. The three-dimensional structure of Novamyl is described below.
In general, a preferred maltogenic alpha-amylase should have one or more of the following properties:
i) a three dimensional structural homology to Novamyl,
ii) an amino acid sequence having at least 70% identity to SEQ ID NO: 2, preferably at least 80% or 90%, e.g. 95% or 98%,
iii) a DNA sequence which hybridizes to the DNA sequence set forth in SEQ ID NO:1 or to the DNA sequence encoding Novamyl harbored in the Bacillus strain NCIB 11837;
iv) a calcium binding site comprising a coordination equivalent to a backbone carbonyl atom from Asn77, sidechain atom OE2 and OE1 from Glu102, a sidechain atom OD1 from Asp79, a sidechain atom OD1 from Asp76, and a sidechain atom OE1 from Glu101, and one water molecule WAT V21, atom OW0, wherein the positions are as shown in Appendix 1;
v) a sequence of five amino acids corresponding to Pro-Ala-Gly-Phe-Ser in a position equivalent to residues 191-195 in the amino acid sequence shown in SEQ ID NO: 2; and
The structural homology referred to above in i) is based on other sequence homologies, hydrophobic cluster analysis or by reverse threading (Huber, T; Torda, A E, PROTEIN SCIENCE Vol. 7, No. 1 pp. 142-149 (1998)) and which by any of these methods is predicted to have the same tertiary structure as Novamyl, wherein the tertiary structure refers to the overall folding or the folding of Domains A, B, and C, more preferably including Domain D, and most preferably including Domain E. Alternatively, a structural alignment between Novamyl and a maltogenic alpha-amylase may be used to identify equivalent positions.
The calcium binding site referred to above in iv) is based on a calcium binding site identified in the three-dimensional structure of Novamyl, and is discussed below in the section “Calcium binding sites.”
The “equivalent position” referred to above in v) is based on amino acid or DNA sequence alignment or structural homology using methods known in the art.
Three-Dimensional Structure of Maltogenic Alpha-Amylase
Novamyl was used to elucidate the three-dimensional structure forming the basis for the present invention.
The structure of Novamyl was solved in accordance with the principle for x-ray crystallographic methods, for example, as given in X-Ray Structure Determination, Stout, G. K. and Jensen, L. H., John Wiley & Sons, Inc. NY, 1989.
The structural coordinates for the solved crystal structure of Novamyl at 2.2 Å resolution using the isomorphous replacement method are given in standard PDB format (Protein Data Bank, Brookhaven National Laboratory, Brookhaven, Conn.) as set forth in Appendix 1. It is to be understood that Appendix 1 forms part of the present application. In the context of Appendix 1, the following abbreviations are used: CA refers to calcium ion or alpha-carbon atom of the polypeptide backbone, WAT refers to water or to calcium, MAL refers to maltose, HEX refers to a carbohydrate unit of a substrate analogue, and SUL refers to a sulfate ion.
Amino acid residues of the enzyme are identified herein by their respective one- or three-letter amino acid code.
The structure of said maltogenic alpha-amylase is made up of five globular domains, ordered A, B, C, D and E. The domains can be defined as being residues 1-132 and 204-403 for Domain A, residues 133-203 for Domain B, residues 404-496 for Domain C, residues 497-579 for Domain D, and residues 580-686 for Domain E, wherein the numbering refers to the amino acid sequence in SEQ ID NO: 2. Features of Domains A, B, and C of particular interest are described below.
Domain A
Domain A is the largest domain and contains the active site which comprises a cluster of three amino acid residues, D329, D228 and E256, spatially arranged at the bottom of a cleft in the surface of the enzyme. The structure of Domain A shows an overall fold in common with the α-amylases for which the structure is known, viz. the (beta/alpha) 8 barrel with eight central beta strands (numbered 1-8) and eight flanking a-helices. The β-barrel is defined by McGregor op. cit. The C-terminal end of the beta strand 1 is connected to helix 1 by a loop denoted loop 1 and an identical pattern is found for the other loops, although the loops show some variation in size and some can be quite extensive.
The eight central beta-strands in the (beta/alpha) 8 barrel superimpose reasonably well with the known structures of CGTases. This part of the structure, including the close surroundings of the active site located at the C-terminal end of the beta-strands, shows a high degree of identity with CGTases.
In contrast, the loops connecting the beta-strands and alpha helices display a high degree of variation from the known structures of CGTases. These loops constitute the structural context of the active site, and the majority of the contacts to the substrate is found among residues located in these loops. Distinguishing characteristics such as substrate specificity, substrate binding, pH activity profile, substrate cleavage pattern, and the like, are determined by specific amino acids and the positions they occupy in these loops. In Novamyl Domain A contains two calcium binding sites, one of which is homologous to the calcium binding site in CGTases; the other is unique to Novamyl. The structure of the calcium binding site is discussed further below in the section “Calcium binding sites.”
Domain B
Domain B, also referred to as loop 3 of the (beta/alpha) 8 barrel, in comprises amino acid residues 133-203 of the amino acid sequence shown in SEQ ID NO: 2. The structure is partially homologous to the structure of Domain B in CGTases, the most striking difference being the presence of a five amino acid insert corresponding to positions 191-195 in the amino acid sequence shown in SEQ ID NO: 2 which is not found in the CGTases. This insert is spatially positioned close to the active site residues and in close contact to the substrate.
Domain C
Domain C in Novamyl comprises amino acid residues 404-496 of the amino acid sequence shown in SEQ ID NO: 2. Domain C is composed entirely of β-strands which form a single 8-stranded sheet structure that folds back on itself, and thus may be described as a β-sandwich structure. One part of the β-sheet forms the interface to Domain A.
Calcium Binding Sites
The structure of the maltogenic alpha-amylase exhibits three calcium-binding sites; that is, three calcium ions are found to be present in the structure. In common with most of the known family 13 structures, one calcium ion, WAT 693 in Appendix 1, is located between the A and B domains. This calcium ion is coordinated by a backbone carbonyl atom from Gln184 and His232, sidechain atoms OD2 and OD1 from Asp198, a sidechain atom OD1 from Asn131, and three water molecules WAT V1, WAT V5 and WAT V8.
A second calcium ion is located in the A domain and is common to CGTases, but not found in α-amylases. The calcium ion WAT 694 is coordinated by a backbone carbonyl atom from Gly48 and Asp23, sidechain atom OD2 from Asp50, a sidechain atom OD1 from Asp21, a sidechain atom OD1 from Asn26, and a sidechain atom OD1 from Asn27, and one water molecule WAT V62.
The third calcium ion is located in the A Domain and is unique to Novamyl. The calcium ion is WAT 692 and the coordination comprises a backbone carbonyl atom from Asn77, sidechain atom OE2 and OE1 from Glu102, a sidechain atom OD1 from Asp79, a sidechain atom OD1 from Asp76, and a sidechain atom OE1 from Glu101, and one water molecule WAT V21.
Substrate Binding Site
Parts of the loop discussed above in the context of domains A and B are of particular interest for substrate interaction and active site reactivity. In particular, in domain A, residues 37-45 in loop 1, residues 261-266 in loop 5, residues 327-330 in loop 7 and residues 370-376 in loop 8; in domain B, residues 135-145 in loop 3, residues 173-180 and 188-196 in loop 3, wherein residue positions correspond to the amino acids in the amino acid sequence in SEQ ID NO: 2.
Without being limited to any theory, it is presently believed that binding between a substrate and an enzyme is supported by favorable interactions found within a sphere of 4 to 6 Å between the substrate molecule and the enzyme, such as hydrogen bonds and/or strong electrostatic interaction. The following residues of Novamyl (SEQ ID NO: 2), are within a distance of 6 Å of the substrate HEX and thus believed to be involved in interactions with said substrate:
44, 89, 90, 92, 93, 127, 129, 132, 135, 177, 178, 188, 191, 194, 196, 226, 228, 229, 230, 231, 232, 256, 258-261, 288, 328, 329, 371, 372, 373, 376, and 690.
The following residues of Novamyl are within a distance of 4 Å of the substrate HEX and thus believed to be involved in interactions with said substrate:
90, 92, 93, 129, 132, 177, 188, 189, 190, 191, 196, 226, 228, 229, 231, 232, 256, 258, 259, 260, 261, 328, 329, 372, 376, and 690.
Homology Building of Novamyl®
The structure of the Novamyl® was model built on the structure disclosed in Appendix 1 herein. The structure of other maltogenic alpha-amylases may be built analogously.
A model structure of a maltogenic alpha-amylase can be built using the Homology program or a comparable program, eg., Modeller (both from Molecular Simulations, Inc., San Diego, Calif.). The principle is to align the sequence of the maltogenic alpha-amylase with the known structure with that of the maltogenic alpha-amylase for which a model structure is to be constructed. The structurally conserved regions can then be built on the basis of consensus sequences. In areas lacking homology, loop structures can be inserted, or sequences can be deleted with subsequent bonding of the necessary residues using, e.g., the program Homology. Subsequent relaxing and optimization of the structure should be done using either Homology or another molecular simulation program, e.g., CHARMm from Molecular Simulations.
Methods for Designing Novel Maltogenic Alpha-Amylase Variants
In a first aspect, the invention relates to a method of constructing a variant of a parent maltogenic alpha-amylase, wherein said variant has at least one altered property as compared to said parent α-amylase, which method comprises:
i) analyzing the structure of the maltogenic alpha-amylase to identify at least one amino acid or structural region of said α-amylase, which, on the basis of structural or functional considerations, is determined to be of relevance for altering said property of the parent maltogenic alpha-amylase;
ii) constructing a variant of the maltogenic alpha-amylase, which as compared to the parent, has been modified in the amino acid residue or structural region identified in i) has been modified so as to alter said property; and
iii) testing the resulting variant for said property.
The structural part which is identified in step i) of the method of the invention may be composed of one amino acid residue. However, normally the structural part comprises more than one amino acid residue, typically constituting one of the above parts of the maltogenic alpha-amylase structure such as one of the A, B, C, D or E domains, an interface between any of these domains, a calcium binding site, a loop structure, the substrate binding site, or the like.
The structural or functional considerations may involve an analysis of the relevant structure or structural part and its contemplated impact on the function of the enzyme. For example, an analysis of the functional differences between maltogenic alpha-amylase and the various CGTases may be used for assigning certain properties of Novamyl to certain parts of the Novamyl structure or to contemplate such relationship. For instance, differences in the pattern or structure of loops surrounding the active site may result in differences in access to the active site of the substrate and thus differences in substrate specificity and/or cleavage pattern.
Furthermore, parts of a maltogenic alpha-amylase involved in substrate binding, and thus, for example, substrate specificity and/or cleavage, calcium ion binding, important, for example, for the calcium dependency of the enzyme, and the like, have been identified (vide infra).
The modification of an amino acid residue or structural region is typically accomplished by suitable modifications of a DNA sequence encoding the parent enzyme in question. The modification may be substitution, deletion or insertion of an amino acid residue or a structural part.
The property to be modified may be stability (e.g. thermostability), pH dependent activity, substrate specificity, specific activity or ability to reduce retrogradation of starch or staling of bread. Thus, the altered property may be an altered specific activity at a given pH and/or an altered substrate specificity, such as an altered pattern of substrate cleavage or an altered pattern of substrate inhibition.
In step ii) of the method according to the invention the part of the structure to be identified is preferably one which in the folded enzyme is believed to be in contact with the substrate (cf, the disclosure above in the section entitled “Substrate Binding Site”) or involved in substrate specificity and/or cleavage pattern, and/or one which is in contact with one of the calcium ions and/or one, which is contributing to the pH or temperature profile of the enzyme, or is otherwise responsible for the properties of the maltogenic alpha-amylase.
Described in the following are specific types of variants which have been designed by use of the method of the invention.
The variants of the invention may comprise additional modifications in addition to the modifications described herein. The variants preferably have an amino acid having more than 70% identity with SEQ ID NO: 2, preferably more than 80%, particularly more than 90%, especially more than 95%, e.g. more than 98%.
Maltogenic Alpha-Amylase Variants with Altered pH Dependent Activity Profile
The pH dependent activity profile can be changed by changing the pKa of residues within 10 Å of the active site residues of the maltogenic alpha-amylase. Changing the pKa of the active site residues is achieved, e.g., by changing the electrostatic interaction or hydrophobic interaction between functional groups of amino acid side chains of a given amino acid residue and its close surroundings. To obtain a higher activity at a higher pH, negatively charged residues are placed near a hydrogen donor acid, whereas positively charged residues placed near a nucleophilic acid will result in higher activity at low pH. Also, a decrease in the pKa can be obtained by reducing the accessibility of water or increasing hydrophobicity of the environment.
Thus, another aspect of the present invention relates to a variant of a parent maltogenic alpha-amylase, in which the variant has an altered pH dependent activity profile as compared to the parent, wherein the variant may be obtained by the following method:
i) identifying an amino acid residue within 15 Å from an active site residue of a maltogenic alpha-amylase in the three-dimensional structure of said parent maltogenic alpha-amylase, in particular 10 Å from an active site residue, wherein said amino acid residue is contemplated to be involved in electrostatic or hydrophobic interactions with an active site residue;
ii) substituting, in the structure, said amino acid residue with an amino acid residue which changes the electrostatic and/or hydrophobic surroundings of an active site residue, and evaluating the accommodation of the amino acid residue in the structure,
iii) optionally repeating step i) and/or ii) recursively until an amino acid substitution has been identified which is accommodated into the structure,
iv) constructing a maltogenic alpha-amylase variant resulting from steps i) and ii), and optionally iii), and testing the pH dependent enzymatic activity of said variant.
In a preferred embodiment, the variant of a maltogenic alpha-amylase having an altered pH dependent activity profile as compared to the parent maltogenic alpha-amylase comprises a modification of an amino acid residue corresponding to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 2:
D127, V129, F188, A229, Y258, V281, F284, T288, N327, M330, G370, N371, and D372,
L71, S72, V74, L75, L78, T80, L81, G83, T84, D85, N86, T87, G88, Y89, H90, G91, T94, R95, D96, F97, I174, S175, N176, D178, D179, R180, Y181, E182, A183, Q184, K186, N187, F188, T189, D190, A192, G193, F194, S195, L196.
In more preferred embodiment, the variant comprises a modification corresponding to one or more of the following modifications in the amino acid sequence set forth in SEQ ID NO: 2:
D127N/L, V129S/T/G/V, F188E/K/H, A229S/T/G/V, Y258E/D/K/R/F/N, V281 L/T, F284K/H/D/E/Y, T288E/K/R, N327D, M330L/F/I/D/E/K, G370N, N371 D/E/G/K, and D372N/V,
L71I, S72C, V74I, L75N/D/Q/1N, L78N/I, T80I/L/V/S/N/G, L811N/S/T/N/Q/K/H, G83A/S/T/N/Q/E/D/R/H/L, T84S/A/N/D/G, D85A/T/S/N/G, N86Q/E/D/Y/H/K, T87S/I, G88A/S/T, Y89F, H90N/Q/K, G91A/S/T, T94N/D/A/M/V/I, R95K/Q, D96N/V/Q/I, F97Y, I174N/Q/L, S175T/A/N/D, N176S/T/H/Q/P, D178N/Q/E/K/H, D179Y/N/H, R180W, Y181R/F/C/L, E182D, A183S/C/G, Q184E, K186R, N187Q/E/L/F/H/K/V/L, F188Y/L/I/H/N, T189N/D/A/S/H/Y/G, D190E/Q/H/N/K, A192T/D/E/N/K, G193A/S/T, F194Y, S195N/D/E/R/K/G, L196I.
Similar modifications may be introduced in equivalent positions of other maltogenic alpha-amylases. Variants of particular interest have a combination of one or more of the above with any of the other modifications disclosed herein.
Maltogenic Alpha-Amylase Variants with Altered Stability
A variant with improved stability (typically increased stability) may be obtained by stabilization of calcium binding, substitution with proline, substitution of histidine with another amino acid, introduction of an interdomain disulfide bond, removal of a deamidation site, altering a hydrogen bond contact, filling in an internal structural cavity with one or more amino acids with bulkier side groups, introduction of interdomain interactions, altering charge distribution, helix capping, or introduction of a salt bridge.
Calcium Binding
The invention provides a variant of a parent maltogenic alpha-amylase, which has an altered stability due to an altered stabilization of calcium (Ca2+) binding. The enzyme variant may have altered thermostability or pH dependent stability, or it may have maltogenic alpha-amylase activity in the presence of a lower concentration of calcium ion. It is presently believed that amino acid residues located within 10 Å from a calcium ion are involved in or are of importance for the Ca2+ binding capability of the enzyme.
The amino acid residues found within a distance of 10 Å from the Ca2+ binding sites of the maltogenic alpha-amylase with the amino acid sequence set forth in SEQ ID NO: 2 were determined as described in Example 2 and are as follows:
16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28 29, 30, 31, 32, 33, 35, 36, 40, 46, 47, 48, 49, 50, 51, 52, 53, 54, 56, 73, 74, 75, 76, 77, 78, 79, 80, 81, 87, 88, 89, 91, 93, 94, 95, 96, 99, 100, 101, 102, 103, 104, 105, 109, 129, 130, 131, 132, 133, 134, 145, 150, 167, 168, 169, 170, 171, 172, 174, 177, 180, 181, 182, 183, 184, 185, 186, 187, 188, 189, 196, 197, 198, 199, 200, 201, 202, 206, 210, 228, 229, 230, 231, 232, 233, 234, 235, 237, 378, and 637.
In order to construct a variant according to this aspect of the invention it is desirable to substitute at least one of the above mentioned amino acid residues, which is determined to be involved in a non-optimal calcium binding, with any other amino acid residue which improves the Ca2+ binding affinity of the variant enzyme. Accordingly, another aspect of the invention relates to a method of constructing a variant of a parent maltogenic alpha-amylase wherein said variant has a stabilised Ca2+ binding as compared to said parent, which method comprises:
i) identifying an amino acid residue within 10 Å from a Ca2+ binding site of a maltogenic alpha-amylase in a model of the three-dimensional structure of said α-amylase which, from structural or functional considerations, is determined to be responsible for a non-optimal calcium ion interaction;
ii) constructing a variant in which said amino acid residue is substituted with another amino acid residue which, from structural or functional considerations, is determined to be important for establishing an altered Ca2+ binding affinity; and
iii) testing the Ca2+ binding of the resulting maltogenic alpha-amylase variant.
Substituting an amino acid residue responsible for non-optimal calcium ion interaction with another residue may alter a calcium ion binding interaction of the enzyme. For instance, the amino acid residue in question may be selected on the basis of one or more of the following objectives:
a) to obtain an improved interaction between a calcium ion and an amino acid residue as identified from the structure of the maltogenic alpha-amylase. For instance, if the amino acid residue in question is exposed to a surrounding solvent, it may be advantageous to increase the shielding of said amino acid residue from the solvent so as to stabilize the interaction between said amino acid residue and a calcium ion. This can be achieved by substituting said residue, or an amino acid residue in the vicinity of said residue contributing to the shielding, with an amino acid residue with a bulkier side group or which otherwise results in an improved shielding effect.
b) to stabilize a calcium binding site, for instance by stabilizing the structure of the maltogenic alpha-amylase, e.g. by stabilizing the contacts between two or more of the five domains or stabilizing one or more of the individual domains as such. This may, e.g., be achieved by providing for a better coordination to amino acid side chains, which may, e.g., be obtained by substituting an N residue with a D residue and/or a Q residue with an E residue, e.g. within 10 Å, and preferably within 3 or 4 Å, of a calcium binding site.
c) to improve the coordination between the calcium ion and the calcium binding residues, e.g., by improving the interaction between the ion and the coordinating residues or increasing the number of sidechain coordinations by substituting a coordinating water with an amino acid sidechain.
d) replace water by a coordinating calcium amino acid residue.
Preferably, the amino acid residue to be modified is located within 8 Å of a Ca2+ ion, preferably within 5 Å of a Ca2+ ion. The amino acid residues within 8 Å and 5 Å, respectively, may easily be identified by an analogous method used for identifying amino acid residues within 10 Å (cf. Example 2).
In a preferred embodiment, the variant of a maltogenic alpha-amylase having an altered Ca2+ binding as compared to the parent maltogenic alpha-amylase comprises a substitution of an amino acid residue corresponding to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 2:
D17, A30, S32, R95, H103, N131, Q201, I174, and/or H169,
V74, L75, L78, T80, L81, T87, G88, Y89, H90, G91, T94, R95, D96, F97, Y167, F168, H169, H170, N171, G172, D173, 1174, S175, N176, D178, D179, R180, Y181, E182, A183, Q184, K186, N187, F188, T189.
In more preferred embodiment, the variant of a maltogenic alpha-amylase comprises a substitution corresponding to one or more of the following substitutions in the amino acid sequence set forth in SEQ ID NO: 2:
D17E/Q, A30M/L/A/V/I/E/Q, S32D/E/N/Q, R95M/L/A/V/I/E/Q, H103Y/N/Q/D/E, N131D, Q201E, I174E/Q, and H169N/D/E/Q
V74I, L75N/D/Q/1N, L78N/I, T80I/L/V/S/N/G, L81I/V/S/T/N/Q/K/H, T87S/I, G88A/S/T, Y89F, H90N/Q/K, G91A/S/T, T94N/D/A/M/V/I, R95K/Q, D96N/V/Q/I, F97Y, Y167F/R/C, F168Y, H169N/Q/K, H170N/Q/K, N171D/E/Q/H/R/K/G, G172A/T/S, D173N/S/T/Y/R/G, I174 N/Q/L, S175T/A/N/D, N176S/T/H/Q/P, D178N/Q/E/K/H, D179Y/N/H, R180W, Y181R/F/C/L, E182D, A183S/C/G, Q184E, K186R, N187Q/E/L/F/H/K/V/L, F188Y/L/I/H/N, T189N/D/A/S/H/Y/G.
In another preferred embodiment of the invention with respect to altering the Ca2+ binding of a maltogenic alpha-amylase the partial sequence N28-P29-A30-K31-S32-Y33-G34 as set forth in SEQ ID NO: 2 is modified.
Similar substitutions may be introduced in equivalent positions of other maltogenic alpha-amylases. Modifications of particular interest are any combination of one or more of the above with any of the other modifications disclosed herein.
Other Substitutions
Variants with improved stability of the enzyme can be achieved by improving existing or introducing new interdomain and intradomain contacts. Such improved stability can be achieved by the modifications listed below.
The maltogenic alpha-amylase having the amino acid sequence shown in SEQ ID NO: 2 may be stabilized by the introduction of one or more interdomain disulfide bonds. Accordingly, another preferred embodiment of the present invention relates to a variant of a parent maltogenic alpha-amylase which has improved stability and at least one more interdomain disulfide bridge as compared to said parent, wherein said variant comprises a modification in a position corresponding to at least one of the following pairs of positions in SEQ ID NO: 2:
G236+S583, G618+R272, T252+V433 and/or A348+V487.
In a more preferred embodiment, the substitution corresponds to at least one of the following pairs:
G236C+S583C, G618C+R272c, T252C+V433C and/or A348C+V487C.
Another preferred embodiment of the invention relates to a variant of a parent maltogenic alpha-amylase which has an improved stability and an altered interdomain interaction as compared to said parent, wherein said variant comprises a substitution in a position corresponding at least one of the following sets of positions in SEQ ID NO: 2:
i) F143, F194, L78;
ii) A341, A348, L398, I415, T439, L464, L465;
iii) L557;
iv) S240, L268;
v) Q208, L628;
vi) F427, Q500, N507, M508, S573; and
vii) 1510, V620.
In a more preferred embodiment, the substitution corresponds to at least one of the following sets:
i) F143Y, F194Y, L78Y/F/W/E/Q;
ii) A341S/D/N, A348V/I/L, L398E/Q/N/D, 1415E/Q, T439D/E/Q/N, L464D/E,
L465D/E/N/Q/R/K;
iii) L557Q/E/N/D;
iv) S240D/E/N/Q, L268D/E/N/Q/R/K;
v) Q208D/E/Q, L628E/Q/N/D;
vi) F427E/Q/R/K/Y, Q500Y, N507Q/E/D, M508K/R/E/Q, S573D/E/N/Q; and/or
vii) I510D/E/N/Q/S, V620D/E/N/Q.
Another preferred embodiment of the invention relates to a variant of a parent maltogenic alpha-amylase which has an improved stability and one or more salt bridges as compared to said parent, wherein said variant comprises a substitution in a position corresponding at least one of the following sets of positions in SEQ ID NO: 2:
N106, N320 and Q624.
In a more preferred embodiment, the variant of a maltogenic alpha-amylase comprises a substitution corresponding to the following substitutions in the amino acid sequence set forth in SEQ ID NO: 2:
N106R, N320E/D and/or Q624E.
Another embodiment of the invention relates to a variant of a parent maltogenic alpha-amylase which has an improved stability and wherein said variant comprises a substitution in a position corresponding at least one of the following sets of positions in SEQ ID NO: 2:
K40, V74, S141, T142, F188, N234, K249, D261, D261, L268, V279, N342, G397, A403, K425, S442, S479, S493, T494, S495, A496, S497, A498, Q500, K520, A555 and N595.
In a more preferred embodiment, the variant of a maltogenic alpha-amylase comprises a substitution corresponding to one or more of the following substitutions with proline in the amino acid sequence set forth in SEQ ID NO: 2:
V74P, 5141 P, N234P, K249P, L268P, V279P, N342P, G397P, A403P, S442P, S479P, S493P, T494P, S495P, A496P, S497P, A498P, Q500P, and/or A555P.
Other preferred substitutions are K40R, T142A, F1881/L, D261G, K425E, K520R, and/or N5951.
Analogously, it may be preferred that one or more histidine residues present in the parent maltogenic alpha-amylase is or are substituted with a non-histidine residues such as Y, V I, L, F, M, E, Q, N, or D. Accordingly, in another preferred embodiment, the variant of a maltogenic alpha-amylase comprises a substitution of an amino acid residue corresponding to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 2:
H103, H220, and H344
In a more preferred embodiment, the variant of a maltogenic alpha-amylase comprises a substitution corresponding to one or more of the following substitutions in the amino acid sequence set forth in SEQ ID NO: 2:
H103Y/V/I/L/F/Y, H220Y/L/M, and H344E/Q/N/D/Y.
It may be preferred that one or more asparagine or glutamine residues present in the parent maltogenic alpha-amylase is or are substituted with a residue lacking the amide on the side chain. Accordingly, in another preferred embodiment, the variant of a Novamyl-like comprises a substitution of an amino acid residue corresponding to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 2:
Q13, N26, N77, N86, N99, Q119, N120, N131, N152, N171, N176, N187, Q201, N203, N234, Q247, N266, N275, N276, N280, N287, Q299, N320, N327, N342, Q365, N371, N375, N401, N436, N454, N468, N474, Q500, N507, N513, Q526, N575, Q581, N621, Q624 and N664.
In more preferred embodiment, the variant of a maltogenic alpha-amylase comprises a substitution corresponding to one or more of the following substitutions in the amino acid sequence set forth in SEQ ID NO: 2:
Q13S/T/A/V/L/I/F/M, N26S/T/A/V/L/I, N77S/T/A/V/L/I, N86S/T/A/V/L/I, N99T/S/V/L, Q119T/S, N120S/T/A/V/L/I, N131S/T/A/V/L/I, N152T/S/V/L, N171Y/D/S/T, N176S/T/A/V/L/I, N187S/T/A/V/L/I, Q201S/T/A/V/L/I/F/M, N203 D/S/T/A/V/L/I, N234S/T/A/V/L/I, Q247S/T/A/V/L/I/F/M, N266S/T/A/V/L/I, N275S/T/A/V/L/I, N276S/T/A/V/L/I, N280S/T/A/V/L/I, N287S/T/A/V/L/I, Q299 L/T/S, N320S/T/A/V/L/I, N327S/T/A/V/L/I, N342S/T/A/V/L/I, Q365S/T/A/V/L/I, N371S/T/A/V/L/I, N375S/T/A/V/L/1, N401S/T/A/V/L/I, N436S/T/A/V/L/I, N454 D/S/T/A/V/L/I, N468D/S/T/A/V/L/I, N474D/S/T/A/V/L/I, Q500S/T/A/V/L/I/F/M, N507S/T/A/V/L/I, N513S/T/A/V/L/I, Q526 D/S/T/A/V/L/I, N575S/T/A/V/L/I, Q581 S/T/A/V/L/I/F/M, N621S/T/A/V/L/I Q624S/T/A/V/L/I/F/M and N664D/S/T/A/V/L/I.
Another embodiment of the invention relates to a variant of a parent maltogenic alpha-amylase which has improved stability and improved hydrogen bond contacts as compared to said parent, wherein said variant comprises a modification in a position corresponding to one or more of the following positions in SEQ ID NO: 2:
I16, L35, M45, P73, D76, D79, A192, I100, A148, A163+G172, L268, V281, D285, L321, F297, N305, K316, S573, A341, M378, A381, F389, A483, A486, I510, A564, F586, K589, F636, K645, A629, and/or T681.
In a preferred embodiment, the modification corresponds to one or more of the following:
I16T/D/N, L35Q, M45K, P73Q, D76E, D79E/Y, A192S/D/N, I100T/S/D/N/E/Q, A148D/N/E/Q/S/T/R/K, A163Y+G172S/D/N, L268R/K, V281/Q, D285R/K, L321Q, F297N/D/Q/E, N305K/R, K316N/D, S573N/D, A341R/K, M378R/K, A381S/D/N, F389Y, A483S/D/N, A486Q/E, I510R/K, A564S/D/N, F586S/D/N, K589S/D/Q/N, F636Y, K645T, A629N/D/E/Q, and/or T681D/N/E/Q/S.
Similar substitutions may be introduced in equivalent positions of other maltogenic alpha-amylases. Substitutions of particular interest are any combination of one or more of the above with any of the other modifications disclosed herein.
Before actually constructing a maltogenic alpha-amylase variant to achieve any of the above objectives, it may be convenient to evaluate whether or not the contemplated amino acid modification can be accommodated into the maltogenic alpha-amylase structure, e.g. into a model of the three-dimensional structure of the parent maltogenic alpha-amylase.
Maltogenic Alpha-Amylase Variants with Altered Thermostability and/or Altered Temperature Dependent Activity Profile
The invention further relates to a variant of a parent maltogenic alpha-amylase, which results from substitution, deletion or insertion of one or more amino acid residues so as to obtain a variant having an altered thermostability or temperature dependent activity profile.
The structure of the maltogenic alpha-amylase contains a number of unique internal cavities which may contain water and a number of crevices. In order to increase the thermostability of the polypeptide it may be desirable to reduce the number or size of cavities and crevices, e.g., by introducing one or more hydrophobic contacts, preferably achieved by introducing amino acids with bulkier side groups in the vicinity or surroundings of the cavity. For instance, the amino acid residues to be modified are those which are involved in the formation of the cavity.
Accordingly, in a further aspect the present invention relates to a method of increasing the thermostability and/or altering the temperature dependent activity profile of a parent maltogenic alpha-amylase, which method comprises:
i) identifying an internal cavity or a crevice of the parent maltogenic alpha-amylase in the three-dimensional structure of said polypeptide;
ii) substituting, in the structure, one or more amino acid residues in the neighbourhood of the cavity or crevice identified in step i) with another amino acid residue which, from structural or functional considerations, is determined to increase the hydrophobic interaction and to fill out or reduce the size of the cavity or crevice; and
iii) constructing a variant of the parent maltogenic alpha-amylase resulting from step ii) and testing the thermostability and/or temperature dependent activity of the variant.
The structure identified in Appendix 1 may be used for identifying the cavity or crevice of the parent maltogenic alpha-amylase.
It will be understood that the cavity or crevice is identified by the amino acid residues surrounding said cavity or crevice, and that modification of said amino acid residues are of importance for filling or reducing the size of said cavity or crevice. Preferably, the modification is a substitution with a bulkier amino acid residue, i.e. one with a greater side chain volume. For example, all the amino acids are bulkier than Gly, whereas Tyr and Trp are bulkier than Phe. The particular amino acid residues referred to below are those which in a crystal structure have been found to flank the cavity or crevice in question.
In a preferred embodiment, the variant of a maltogenic alpha-amylase, in order to fill, either completely or partly, cavities located internally in the structure, comprises a substitution of an amino acid residue corresponding to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 2:
L51, L75, L78, G88, G91, T94, V114, I125, V126, T134, G157, L217, S235, G236, V254, V279, V281, L286, V289, 1290, V308, L321, I325, D326, L343, F349, S353, 1359, 1405, L448, Q449, L452, 1470, G509, V515, S583, G625, L627, L628 and A670.
L71, S72, V74, L75, L78, T80, L81, G83, T84, D85, N86, T87, G88, Y89, H90, G91, T94, R95, D96, F97, Y167, F168, H169, H170, N171, G172, D173, I174, S175, N176, D178, D179, R180, Y181, E182, A183, Q184, K186, N187, F188, T189, D190, A192, G193, F194, S195, L196.
In a more preferred embodiment, the variant of a maltogenic alpha-amylase comprises one or more substitutions corresponding to the following substitutions in the amino acid sequence set forth in SEQ ID NO: 2:
L217 in combination with L75 (e.g. L217F/Y in combination with L75F/Y), L51W, L75F/Y, L78I, G88A/V/T, G91T/S/V/N, T94V/I/L, V114V/I/L, I125L/M/F/Y/W, V126I/L, T134V/I/L/M/F/V/W, G157A/V/I/L, L217V/I/M/F/Y/W, S235I/L/M/F/Y/W, G236A/V/I/L/M/F/Y/W, V254I/L/M/F/Y/W, V279M/I/L/F, V281I/L/M/F/Y/W, L286F, V289I/L/R, I290M/L/F, V308I/L/M/F/Y/W, L321I/M/F/Y/W, I325L/M/F/Y/W, D326E/Q, L343M/F/Y/W, F349W/Y, S353V/I/L, I359L/M/F/Y/W, I405M/L/Y/F/W, L448Y, Q449Y, L452M/Y/F/W, I470M/L/F, G509A/V/I/L/M/S/T/D/N, V515I/L, S583V/I/L/V, G625A/V/I/L/M/F/Y/W, L627M/F/Y, L628M/I/F/Y/W and A670V/I/L/M/F/Y/W,
L71I, S72C, V74I, L75N/D/Q/I/V, L78N/I, T80I/L/V/S/N/G, L81I/V/S/T/N/Q/K/H, G83A/S/T/N/Q/E/D/R/H/L, T84S/A/N/D/G, D85A/T/S/N/G, N86Q/E/D/Y/H/K, T87S/I, G88A/S/T, Y89F, H90N/Q/K, G91A/S/T, T94N/D/A/M/V/I, R95K/Q, D96N/V/Q/I, F97Y, Y167F/R/C, F168Y, H169N/Q/K, H170N/Q/K, N171D/E/Q/H/R/K/G, G172A/T/S, D173N/S/T/Y/R/G, I174 N/Q/L, S175T/A/N/D, N176S/T/H/Q/P, D178N/Q/E/K/H, D179Y/N/H, R180W, Y181R/F/C/L, E182D, A183S/C/G, Q184E, K186R, N187Q/E/L/F/H/K/V/L, F188Y/L/I/H/N, T189N/D/A/S/H/Y/G, D190E/Q/H/N/K, A192T/D/E/N/K, G193A/S/T, F194Y, S195N/D/E/R/K/G, L191I.
Similar substitutions may be introduced in equivalent positions of other maltogenic alpha-amylases. Variants of particular interest have a combination of one or more of the above with any of the other modifications disclosed herein.
Maltogenic Alpha-Amylase Variants with an Altered Cleavage Pattern
One aim of the present invention is to change the degradation characteristics of a maltogenic alpha-amylase. Thus, Novamyl hydrolyzes starch to form predominantly maltose (G2) and a small amount of glucose (G1), but virtually no higher oligosaccharides (G3+). It may be desirable to change this cleavage pattern, e.g. so as to form higher amounts of higher oligosaccharides, such as maltotriose (G3), maltotetraose (G4) and maltopentaose (G5).
A variant of a parent maltogenic alpha-amylase in which the substrate cleavage pattern is altered as compared to said parent may be constructed by a method which comprises:
i) identifying the substrate binding area of the parent maltogenic alpha-amylase in a model of the three-dimensional structure, e.g. within a sphere of 4 Å from the substrate binding site as defined in the section above entitled “Substrate Binding Site”;
ii) substituting in the model one or more amino acid residues of the substrate binding area of the cleft identified in i) which is or are believed to be responsible for the cleavage pattern of the parent with another amino acid residue which from structural or functional considerations is believed to result in an altered substrate cleavage pattern, or deleting one or more amino acid residues of the substrate binding area contemplated to introduce favorable interactions to the substrate or adding one or more amino acid residues to the substrate binding area contemplated to introduce favorable interactions to the substrate; and
iii) constructing a maltogenic alpha-amylase variant resulting from step ii) and testing the substrate cleavage pattern of the variant.
Accordingly, another aspect of the invention relates to a variant of a parent maltogenic alpha-amylase which has an altered substrate binding site as compared to said parent, which variant comprises a modification in a position corresponding to one or both of the following positions in SEQ ID NO: 2:
V281 and/or A629.
In a preferred embodiment, the variant comprises a modification corresponding to:
V281Q and/or A629N/D/E/Q.
Similar modifications may be introduced in equivalent positions of other maltogenic alpha-amylases. Substitutions of particular interest are any combination of one or both of the above with any of the other modifications disclosed herein.
Maltogenic Alpha-Amylase Variants with Improved Ability to Reduce Retrogradation of Starch and/or Staling of Bread
The invention provides maltogenic alpha-amylase variants having improved ability to reduce the retrogradation of starch and/or the staling of bread. Preferred variants comprise a modification at one or more positions corresponding to the following amino acid residues in SEQ ID NO: 2:
A30, K40, N115, T142, F188, T189, P191, A192, G193, F194, S195, D261, N327, K425, K520 and N595.
In a more preferred embodiment, the variant comprises one or more modifications corresponding to the following in SEQ ID NO: 2:
A30D, K40R, N115D, T142A, F188L, T189Y, Δ (191-195), D261G, D261G, N327S, K425E, K520R and N595I.
Determination of Residues within 10 Å from Calcium Ions
The coordinates of Appendix 1 are read into the INSIGHT program (BIOSYM Technologies). The spatial coordinates are presented showing the bonds between the atoms. The ions are presented as well as the water atoms. The part of the program package for creating subsets was used to create a 10 Å subset around the calcium ions in the structure by using the command ZONE. All residues identified as having an atom within the designated 10 Å distance from a calcium ion are compiled and listed by using the command LIST MOLECULE. By giving the ions the name “VAT CA” in the coordinate file, a 10 Å sphere around all atoms called “VAT CA” is compiled. The specific residues identified in this manner are given further above in the section entitled “Calcium binding”.
Determination of Cavities
The solved structure of Novamyl with the structural coordinates set forth in Appendix 1 reveals many internal crevices and cavities. When analysing for such cavities the Connolly program is normally used (Lee, B. and Richards, F. M. (1971) J. Mol. Biol. 55:379-400). The program uses a probe with radius to search the external and internal surface of the protein. The smallest crevice observable in this way has the probe radius.
To analyse the solved structure a modified version of the Connolly program included in the program of INSIGHT was used. In the first step, the water molecules and the ions were removed by unmerging these atoms from the solved structure. By using the command MOLECULE SURFACE SOLVENT the solvent accessible surface area was calculated for all atoms and residues using a probe radius of 1.4 Å, and displayed graphically together with the model of the solved structure. The internal cavities are then seen as dot surfaces with no connections to the external surface.
Suggestions for specific modifications to fill out the cavities are given above in the section entitled “Variants with altered thermostability and/or altered temperature dependent activity profile”). By using the homology built structures or/and comparisons based on sequence alignment, mutations for homologous structures of maltogenic alpha-amylases can be made.
Nomenclature for Amino Acid Modifications
The nomenclature used herein for defining mutations is essentially as described in WO 92/05249. Thus, F188H indicates a substitution of the amino acid F (Phe) in position 188 with the amino acid H(H is). V129S/T/G/V indicates a substitution of V129 with S, T, G or V. Δ (191-195) or Δ (191-195) indicates a deletion of amino acids in positions 191-195. 192-A-193 indicates an insertion of A between amino acids 192 and 193.
Polypeptide Sequence Identity
For purposes of the present invention, the degree of identity may be suitably determined according to the method described in Needleman, S. B. and Wunsch, C. D., (1970), Journal of Molecular Biology, 48, 443-45, with the following settings for polypeptide sequence comparison: GAP creation penalty of 3.0 and GAP extension penalty of 0.1. The determination may be done by means of a computer program known 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).
The variants of the invention have an amino acid identity with amino acids 1-686 of SEQ ID NO: 2 of at least 70%, preferably at least 80%, e.g. at least 90%, particularly at least 95% or at least 98%.
Hybridization
Suitable experimental conditions for determining hybridization between a nucleotide probe and a homologous DNA or RNA sequence involves presoaking of the filter containing the DNA fragments or RNA to hybridize in 5×SSC (sodium chloride/sodium citrate, Sambrook, et al., 1989) for 10 min, and prehybridization of the filter in a solution of 5×SSC, 5×Denhardt's solution (Sambrook, et al., 1989), 0.5% SDS and 100 μg/ml of denatured sonicated salmon sperm DNA (Sambrook, et al., 1989), followed by hybridization in the same solution containing a random-primed (Feinberg, A. P. and Vogelstein, B. (1983) Anal. Biochem. 132:6-13), 32P-dCTP-labeled (specific activity >1×109 cpm/μg) probe for 12 hours at ca. 45° C. The filter is then washed twice for 30 minutes in 2×SSC, 0.5% SDS at least 55° C. (low stringency), preferably at least 60° C. (medium stringency), more preferably at least 65° C. (medium/high stringency), more preferably at least 70° C. (high stringency), even more preferably at least 75° C. (very high stringency).
Molecules which hybridize to the oligonucleotide probe under these conditions are detected by exposure to x-ray film.
Methods of Preparing Variants of Maltogenic Alpha-Amylases
Cloning a DNA Sequence Encoding a Novamyl-Like Polypeptide
The DNA sequence encoding a parent maltogenic alpha-amylase may be isolated from any cell or microorganism producing the maltogenic alpha-amylase in question, using various methods well known in the art, for example, from the Bacillus strain NCIB 11837.
First, a genomic DNA and/or cDNA library should be constructed using chromosomal DNA or messenger RNA from the organism that produces the maltogenic alpha-amylase to be studied. Then, if the amino acid sequence of the α-amylase is known, homologous, labelled oligonucleotide probes may be synthesised and used to identify maltogenic alpha-amylase-encoding clones from a genomic library prepared from the organism in question. Alternatively, a labelled oligonucleotide probe containing sequences homologous to a known α-amylase gene could be used as a probe to identify maltogenic alpha-amylase-encoding clones, using hybridization and washing conditions of lower stringency.
Another method for identifying maltogenic alpha-amylase-encoding clones involves inserting fragments of genomic DNA into an expression vector, such as a plasmid, transforming α-amylase negative bacteria with the resulting genomic DNA library, and then plating the transformed bacteria onto agar containing a substrate for maltogenic alpha-amylase, thereby allowing clones expressing maltogenic alpha-amylase activity to be identified.
Alternatively, the DNA sequence encoding the enzyme may be prepared synthetically by established standard methods, e.g. the phosphoroamidite method described by S. L. Beaucage and M. H. Caruthers (1981) or the method described by Matthes et al. (1984). In the phosphoroamidite method, oligonucleotides are synthesized, e.g. in an automatic DNA synthesizer, purified, annealed, ligated and cloned in appropriate vectors.
Finally, the DNA sequence may be of mixed genomic and synthetic origin, mixed synthetic and cDNA origin or mixed genomic and cDNA origin, prepared by ligating fragments of synthetic, genomic or cDNA origin, wherein the fragments correspond to various parts of the entire DNA sequence, in accordance with techniques well known in the art. The DNA sequence may also be prepared by polymerase chain reaction (PCR) using specific primers, for instance as described in U.S. Pat. No. 4,683,202 or R. K. Saiki et al. (1988).
Site-Directed Mutagenesis
Once a maltogenic alpha-amylase-encoding DNA sequence has been isolated, and desirable sites for modification identified, modifications may be introduced using synthetic oligonucleotides. These oligonucleotides contain nucleotide sequences flanking the desired modification sites; mutant nucleotides are inserted during oligonucleotide synthesis. In a specific method, a single-stranded gap of DNA, bridging the maltogenic alpha-amylase-encoding sequence, is created in a vector carrying the maltogenic alpha-amylase gene. Then the synthetic nucleotide, bearing the desired modification, is annealed to a homologous portion of the single-stranded DNA. The remaining gap is then filled in with DNA polymerase I (Klenow fragment) and the construct is ligated using T4 ligase. A specific example of this method is described in Morinaga et al. (1984). U.S. Pat. No. 4,760,025 discloses the introduction of oligonucleotides encoding multiple modifications by performing minor alterations of the cassette. However, an even greater variety of modifications can be introduced at any one time by the Morinaga method because a multitude of oligonucleotides, of various lengths, can be introduced.
Another method of introducing modifications into a maltogenic alpha-amylase-encoding DNA sequences is described in Nelson and Long (1989). It involves a 3-step generation of a PCR fragment containing the desired modification introduced by using a chemically synthesized DNA strand as one of the primers in the PCR reactions. From the PCR-generated fragment, a DNA fragment carrying the modification may be isolated by cleavage with restriction endonucleases and reinserted into an expression plasmid.
Random Mutagenesis
Random mutagenesis is suitably performed either as localised or region-specific random mutagenesis in at least three parts of the gene translating to the amino acid sequence shown in question, or within the whole gene.
The random mutagenesis of a DNA sequence encoding a parent maltogenic alpha-amylase may be conveniently performed by use of any method known in the art.
In relation to the above, a further aspect of the present invention relates to a method for generating a variant of a parent Novamyl-like α-amylase, wherein the variant exhibits increased stability at low pH and at low calcium concentration relative to the parent, the method comprising:
(a) subjecting a DNA sequence encoding the parent Novamyl-like α-amylase to random mutagenesis,
(b) expressing the mutated DNA sequence obtained in step (a) in a host cell, and
(c) screening for host cells expressing a Novamyl-like α-amylase variant which has an altered property relative to the parent Novamyl-like α-amylase.
Step (a) of the above method of the invention is preferably performed using doped primers, as described in the working examples herein (vide infra).
For instance, the random mutagenesis may be performed by use of a suitable physical or chemical mutagenizing agent, by use of a suitable oligonucleotide, or by subjecting the DNA sequence to PCR generated mutagenesis. Furthermore, the random mutagenesis may be performed by use of any combination of these mutagenizing agents. The mutagenizing agent may, e.g., be one which induces transitions, transversions, inversions, scrambling, deletions, and/or insertions.
Examples of a physical or chemical mutagenizing agent suitable for the present purpose include ultraviolet (UV) irradiation, hydroxylamine, N-methyl-N′-nitro-N-nitrosoguanidine (MNNG), O-methyl hydroxylamine, nitrous acid, ethyl methane sulphonate (EMS), sodium bisulphite, formic acid, and nucleotide analogues. When such agents are used, the mutagenesis is typically performed by incubating the DNA sequence encoding the parent enzyme to be mutagenized in the presence of the mutagenizing agent of choice under suitable conditions for the mutagenesis to take place, and selecting for mutated DNA having the desired properties.
When the mutagenesis is performed by the use of an oligonucleotide, the oligonucleotide may be doped or spiked with the three non-parent nucleotides during the synthesis of the oligonucleotide at the positions which are to be changed. The doping or spiking may be done so that codons for unwanted amino acids are avoided. The doped or spiked oligonucleotide can be incorporated into the DNA encoding the maltogenic alpha-amylase enzyme by any published technique, using e.g. PCR, LCR or any DNA polymerase and ligase as deemed appropriate.
Preferably, the doping is carried out using “constant random doping”, in which the percentage of wild-type and modification in each position is predefined. Furthermore, the doping may be directed toward a preference for the introduction of certain nucleotides, and thereby a preference for the introduction of one or more specific amino acid residues. The doping may be made, e.g., so as to allow for the introduction of 90% wild type and 10% modifications in each position. An additional consideration in the choice of a doping scheme is based on genetic as well as protein-structural constraints. The doping scheme may be made by using the DOPE program which, inter alia, ensures that introduction of stop codons is avoided.
When PCR-generated mutagenesis is used, either a chemically treated or non-treated gene encoding a parent maltogenic alpha-amylase enzyme is subjected to PCR under conditions that increase the misincorporation of nucleotides (Deshler 1992; Leung et al., Technique, Vol. 1, 1989, pp. 11-15).
A mutator strain of E. coli (Fowler et al., Molec. Gen. Genet., 133, 1974, pp. 179-191), S. cereviseae or any other microbial organism may be used for the random mutagenesis of the DNA encoding the maltogenic alpha-amylase by, e.g., transforming a plasmid containing the parent enzyme into the mutator strain, growing the mutator strain with the plasmid and isolating the mutated plasmid from the mutator strain. The mutated plasmid may be subsequently transformed into the expression organism.
The DNA sequence to be mutagenized may be conveniently present in a genomic or cDNA library prepared from an organism expressing the parent maltogenic alpha-amylase. Alternatively, the DNA sequence may be present on a suitable vector such as a plasmid or a bacteriophage, which as such may be incubated with or otherwise exposed to the mutagenising agent. The DNA to be mutagenized may also be present in a host cell either by being integrated in the genome of said cell or by being present on a vector harbored in the cell. Finally, the DNA to be mutagenized may be in isolated form. It will be understood that the DNA sequence to be subjected to random mutagenesis is preferably a cDNA or a genomic DNA sequence.
In some cases it may be convenient to amplify the mutated DNA sequence prior to performing the expression step b) or the screening step c). Such amplification may be performed in accordance with methods known in the art, the presently preferred method being PCR-generated amplification using oligonucleotide primers prepared on the basis of the DNA or amino acid sequence of the parent enzyme.
Subsequent to the incubation with or exposure to the mutagenising agent, the mutated DNA is expressed by culturing a suitable host cell carrying the DNA sequence under conditions allowing expression to take place. The host cell used for this purpose may be one which has been transformed with the mutated DNA sequence, optionally present on a vector, or one which was carried the DNA sequence encoding the parent enzyme during the mutagenesis treatment. Examples of suitable host cells are the following: gram positive bacteria such as Bacillus subtilis, Bacillus lichenifonnis, Bacillus lentus, Bacillus brevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacillus lautus, Bacillus megaterium, Bacillus thuringiensis, Streptomyces lividans or Streptomyces murinus; and gram negative bacteria such as E. coli. 
The mutated DNA sequence may further comprise a DNA sequence encoding functions permitting expression of the mutated DNA sequence.
Localized Random Mutagenesis
The random mutagenesis may be advantageously localized to a part of the parent maltogenic alpha-amylase in question. This may, e.g., be advantageous when certain regions of the enzyme have been identified to be of particular importance for a given property of the enzyme, and when modified are expected to result in a variant having improved properties. Such regions may normally be identified when the tertiary structure of the parent enzyme has been elucidated and related to the function of the enzyme.
The localized, or region-specific, random mutagenesis is conveniently performed by use of PCR generated mutagenesis techniques as described above or any other suitable technique known in the art. Alternatively, the DNA sequence encoding the part of the DNA sequence to be modified may be isolated, e.g., by insertion into a suitable vector, and said part may be subsequently subjected to mutagenesis by use of any of the mutagenesis methods discussed above.
For region-specific random mutagenesis with a view to improving the stability of calcium binding of a parent maltogenic alpha-amylase, codon positions corresponding to the following amino acid residues from the amino acid sequence set forth in SEQ ID NO: 2 may appropriately be targeted:
Residues:Regions:
16-33, 35-36, 40: 16-40
46-54, 56: 46-56
73-81: 73-81
87-89, 91, 93-96, 99-105, 109: 87-109
129-134, (145, 150): 129-134
167-172, 174, 177, 180-189: 167-189
196-202, 206-210: 196-210
228-235, 237: 228-237
378
637
With a view to achieving improved binding of a substrate, i.e., improved binding of a carbohydrate species, such as amylose or amylopectin, by a maltogenic alpha-amylase variant with a modified, e.g. higher, substrate specificity and/or a modified, e.g. higher, specificity with respect to cleavage, i.e. hydrolysis, of the substrate, it appears that the following codon positions in the following regions of the amino acid sequence shown in SEQ ID NO: 2, may particularly appropriately be targeted for modification by region-specific mutagenesis:
70-97, 127-143, 174-198, 226-233, 255-270, 282-292, 324-331, 370-376.
For region-specific random mutagenesis with a view to altering the substrate specificity and/or the pH dependent activity profile, the following regions of SEQ ID NO: 2 may be targeted: 70-97, 174-198.
For random mutagenesis with a view to improving the thermostability, the residues and regions described above may be targeted, particularly those described for altering stability, filling internal holes, improved Ca binding, interdomain and intradomain contacts, helix capping, proline substitution, and histidine substitution. In addition, the following regions may be targeted with a view to improving the thermostability: 70-109, 167-200. Also, any amino acid residue which is substituted in a variant having improved thermostability may be targeted, e.g. those in the following positions: 115, 342, 387, 422, 425, 483, 520, 594 and 600.
General Method for Random Mutagenesis by Use of the Dope Program
The random mutagenesis may be carried out by the following steps:
1. Select regions of interest for modification in the parent enzyme
2. Decide on mutation sites and non-mutated sites in the selected region
3. Decide on which kind of mutations should be carried out, e.g. with respect to the desired stability and/or performance of the variant to be constructed
4. Select structurally reasonable mutations
5. Adjust the residues selected by step 3 with regard to step 4.
6. Analyse by use of a suitable dope algorithm the nucleotide distribution.
7. If necessary, adjust the wanted residues to genetic code realism, e.g. taking into account constraints resulting from the genetic code, e.g. in order to avoid introduction of stop codons; the skilled person will be aware that some codon combinations cannot be used in practice and will need to be adapted
8. Make primers
9. Perform random mutagenesis by use of the primers
10. Select resulting α-amylase variants by screening for the desired improved properties.
Suitable dope algorithms for use in step 6 are well known in the art. One such algorithm is described by Tomandl, D. et al., 1997, Journal of Computer-Aided Molecular Design 11:29-38. Another algorithm is DOPE (Jensen, L J, Andersen, K V, Svendsen, A, and Kretzschmar, T (1998) Nucleic Acids Research 26:697-702).
Expression of Maltogenic Alpha-Amylase Variants
The construction of the variant of interest is accomplished by cultivating a microorganism comprising a DNA sequence encoding the variant under conditions which are conducive for producing the variant, and optionally subsequently recovering the variant from the resulting culture broth. This is described in detail further below.
According to the invention, a DNA sequence encoding the variant produced by methods described above, or by any alternative methods known in the art, can be expressed, in the form of a protein or polypeptide, using an expression vector which typically includes control sequences encoding a promoter, operator, ribosome binding site, translation initiation signal, and, optionally, a repressor gene or various activator genes.
The recombinant expression vector carrying the DNA sequence encoding an maltogenic alpha-amylase variant of the invention may be any vector which may conveniently be subjected to recombinant DNA procedures, and the choice of vector will often depend on the host cell into which it is to be introduced. Thus, the vector may be an autonomously replicating vector, i.e. a vector which exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g. a plasmid, a bacteriophage or an extrachromosomal element, minichromosome or an artificial chromosome. Alternatively, the vector may be one which, when introduced into a host cell, is integrated into the host cell genome and replicated together with the chromosome(s) into which it has been integrated.
In the vector, the DNA sequence should be operably connected to a suitable promoter sequence. The promoter may be any DNA sequence which shows transcriptional activity in the host cell of choice and may be derived from genes encoding proteins either homologous or heterologous to the host cell. Examples of suitable promoters for directing the transcription of the DNA sequence encoding a maltogenic alpha-amylase variant of the invention, especially in a bacterial host, are the promoter of the lac operon of E. coli, the Streptomyces coelicolor agarase gene dagA promoters, the promoters of the Bacillus lichenifonnis α-amylase gene (amyL), the promoters of the Bacillus stearothermophilus maltogenic amylase gene (amyM), the promoters of the Bacillus amyloliquefaciens α-amylase (amyQ), the promoters of the Bacillus subtilis xylA and xylB genes, etc. For transcription in a fungal host, examples of useful promoters are those derived from the gene encoding A. oryzae TAKA amylase, Rhizomucor miehei aspartic proteinase, A. niger neutral α-amylase, A. niger acid stable α-amylase, A. niger glucoamylase, Rhizomucor miehei lipase, A. oryzae alkaline protease, A. oryzae triose phosphate isomerase or A. nidulans acetamidase.
The expression vector of the invention may also comprise a suitable transcription terminator and, in eukaryotes, polyadenylation sequences operably connected to the DNA sequence encoding the maltogenic alpha-amylase variant of the invention. Termination and polyadenylation sequences may suitably be derived from the same sources as the promoter.
The vector may further comprise a DNA sequence enabling the vector to replicate in the host cell in question. Examples of such sequences are the origins of replication of plasmids pUC19, pACYC177, pUB110, pE194, pAMB1 and pIJ702.
The vector may also comprise a selectable marker, e.g. a gene the product of which complements a defect in the host cell, such as the dal genes from B. subtilis or B. lichenifonnis, or one which confers antibiotic resistance such as ampicillin, kanamycin, chloramphenicol or tetracycline resistance. Furthermore, the vector may comprise Aspergillus selection markers such as amdS, argB, niaD and sC, a marker giving rise to hygromycin resistance, or the selection may be accomplished by co-transformation, e.g. as described in WO 91/17243.
While intracellular expression may be advantageous in some respects, e.g. when using certain bacteria as host cells, it is generally preferred that the expression is extracellular. In general, the Bacillus α-amylases mentioned herein comprise a preregion permitting secretion of the expressed protease into the culture medium. If desirable, this preregion may be replaced by a different preregion or signal sequence, conveniently accomplished by substitution of the DNA sequences encoding the respective preregions.
The procedures used to ligate the DNA construct of the invention encoding maltogenic alpha-amylase variant, the promoter, terminator and other elements, respectively, and to insert them into suitable vectors containing the information necessary for replication, are well known to persons skilled in the art (cf., for instance, Sambrook et al. (1989)).
The cell of the invention, either comprising a DNA construct or an expression vector of the invention as defined above, is advantageously used as a host cell in the recombinant production of a maltogenic alpha-amylase variant of the invention. The cell may be transformed with the DNA construct of the invention encoding the variant, conveniently by integrating the DNA construct (in one or more copies) in the host chromosome. This integration is generally considered to be an advantage as the DNA sequence is more likely to be stably maintained in the cell. Integration of the DNA constructs into the host chromosome may be performed according to conventional methods, e.g. by homologous or heterologous recombination. Alternatively, the cell may be transformed with an expression vector as described above in connection with the different types of host cells.
The cell of the invention may be a cell of a higher organism such as a mammal or an insect, but is preferably a microbial cell, e.g. a bacterial or a fungal (including yeast) cell.
Examples of suitable bacteria are gram positive bacteria such as Bacillus subtilis, Bacillus lichenifonnis, Bacillus lentus, Bacillus brevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacillus lautus, Bacillus megaterium, Bacillus thuringiensis, or Streptomyces lividans or Streptomyces murinus, or gram negative bacteria such as E. coli. The transformation of the bacteria may, for instance, be effected by protoplast transformation or by using competent cells in a manner known per se.
The yeast organism may favourably be selected from a species of Saccharomyces or Schizosaccharomyces, e.g. Saccharomyces cerevisiae. The filamentous fungus may advantageously belong to a species of Aspergillus, e.g. Aspergillus oryzae or Aspergillus niger. Fungal cells may be transformed by a process involving protoplast formation and transformation of the protoplasts followed by regeneration of the cell wall in a manner known per se. A suitable procedure for transformation of Aspergillus host cells is described in EP 238 023.
In a yet further aspect, the present invention relates to a method of producing a maltogenic alpha-amylase variant of the invention, which method comprises cultivating a host cell as described above under conditions conducive to the production of the variant and recovering the variant from the cells and/or culture medium.
The medium used to cultivate the cells may be any conventional medium suitable for growing the host cell in question and obtaining expression of the maltogenic alpha-amylase variant of the invention. Suitable media are available from commercial suppliers or may be prepared according to published recipes (e.g. as described in catalogues of the American Type Culture Collection).
The maltogenic alpha-amylase variant secreted from the host cells may conveniently be recovered from the culture medium by well-known procedures, including separating the cells from the medium by centrifugation or filtration, and precipitating proteinaceous components of the medium by means of a salt such as ammonium sulfate, followed by the use of chromatographic procedures such as ion exchange chromatography, affinity chromatography, or the like.
Testing of Maltogenic Alpha-Amylase Variants
Maltogenic alpha-amylase variants produced by any of the methods described above may be tested, either prior to or after purification, for amylolytic activity in a screening assay which measures the ability of the variant to degrade starch. The screening in step 10 in the above-mentioned random mutagenesis method of the invention may be conveniently performed by use of a filter assay based on the following procedure: A microorganism capable of expressing the mutated maltogenic alpha-amylase of interest is incubated on a suitable medium and under suitable conditions for secretion of the enzyme, the medium being covered with two filters comprising a protein-binding filter placed under a second filter exhibiting a low protein binding capability. The microorganism is grown on the second, top filter. Subsequent to the incubation, the bottom protein-binding filter comprising enzymes secreted from the microorganism is separated from the second filter comprising the microorganism. The protein-binding filter is then subjected to screening for the desired enzymatic activity, and the corresponding microbial colonies present on the second filter are identified. The first filter used for binding the enzymatic activity may be any protein-binding filter, e.g., nylon or nitrocellulose. The second filter carrying the colonies of the expression organism may be any filter that has no or low affinity for binding proteins, e.g., cellulose acetate or DuraporeTM.
Screening consists of treating the first filter to which the secreted protein is bound with a substrate that allows detection of the α-amylase activity. The enzymatic activity may be detected by a dye, fluorescence, precipitation, pH indicator, IR-absorbance or any other known technique for detection of enzymatic activity. The detecting compound may be immobilized by any immobilizing agent e.g. agarose, agar, gelatine, polyacrylamide, starch, filter paper, cloth; or any combination of immobilizing agents. For example, α-amylase activity can be detected by Cibacron Red labelled amylopectin, which is immobilized in agarose. α-amylase activity on this substrate produces zones on the plate with reduced red color intensity.
To screen for variants with increased stability, the filter with bound maltogenic alpha-amylase variants can be pretreated prior to the detection step described above to inactivate variants that do not have improved stability relative to the parent maltogenic alpha-amylase. This inactivation step may consist of, but is not limited to, incubation at elevated temperatures in the presence of a buffered solution at any pH from pH 2 to 12, and/or in a buffer containing another compound known or thought to contribute to altered stability e.g., surfactants, EDTA, EGTA, wheat flour components, or any other relevant additives. Filters so treated for a specified time are then rinsed briefly in deionized water and placed on plates for activity detection as described above. The conditions are chosen such that stabilized variants show increased enzymatic activity relative to the parent after incubation on the detection media.
To screen for variants with altered thermostability, filters with bound variants are incubated in buffer at a given pH (e.g., in the range from pH 2-12) at an elevated temperature (e.g., in the range from 50°-110° C.) for a time period (e.g., from 1-20 minutes) to inactivate nearly all of the parent maltogenic alpha-amylase, rinsed in water, then placed directly on a detection plate containing immobilized Cibacron Red labelled amylopectin and incubated until activity is detectable. Similarly, pH dependent stability can be screened for by adjusting the pH of the buffer in the above inactivation step such that the parent maltogenic alpha-amylase is inactivated, thereby allowing detection of only those variants with increased stability at the pH in question. To screen for variants with increased calcium-dependent stability calcium chelators, such as ethylene glycol-bis(β-aminoethyl ether) N,N,N′,N′-tetraacetic acid (EGTA), is added to the inactivation buffer at a concentration such that the parent maltogenic alpha-amylase is inactivated under conditions further defined, such as buffer pH, temperature or a specified length of incubation.
The variants of the invention may be suitably tested by assaying the starch-degrading activity of the variant, for instance by growing host cells transformed with a DNA sequence encoding a variant on a starch-containing agarose plate and identifying starch-degrading host cells as described above. Further testing in regard to altered properties, including specific activity, substrate specificity, cleavage pattern, thermoactivation, thermostability, pH dependent activity or optimum, pH dependent stability, temperature dependent activity or optimum, transglycosylation activity, stability, and any other parameter of interest, may be performed on purified variants in accordance with methods known in the art as described below.
Degradation of β-Limit Dextrin by Maltogenic Alpha-Amylase:
Another important parameter in the evaluation of the substrate specificity of maltogenic alpha-amylase variants may be the degree to which such enzymes are capable of degrading starch that has been exhaustively treated with the exoglycosylase β-amylase. To screen for variants which show patterns of degradation on such a substrate differing from the patterns produced by the parent maltogenic alpha-amylase the following assay is performed: β-limit dextrin is prepared by incubating 25 ml 1% amylopectin in Mcllvane buffer (48.5 mM citrate and 193 mM sodium phosphate pH 5.0) with 24 μg/ml β-amylase overnight at 30° C. Unhydrolysed amylopectin (i.e., β-limit dextrin) is precipitated with 1 volume 98% ethanol, washed and redissolved in water. 1 ml β-limit dextrin is incubated with 18 μl enzymes (at 2.2 mg/ml) and 100 μl 0.2 M citrate-phosphate pH 5.0 for 2 hrs at 30° C. and analysed by HPLC as described above. Total hydrolysis of β-limit dextrin is carried out in 2M HCl at 95° C. The concentration of reducing ends is measured by methods known in the art.
Calcium Binding Affinity
Unfolding of maltogenic alpha-amylases by exposure to heat or to denaturants such as guanidine hydrochloride is accompanied by a decrease in fluorescence, and oss of calcium ions leads to unfolding. Thus, the affinity of a maltogenic alpha-amylase variant for calcium can be measured by fluorescence measurements before and after incubation of the variant (e.g., at a concentration of 10 mg/ml) in a buffer (e.g., 50 mM HEPES, pH 7) with different concentrations of calcium (e.g., in the range from 1 mM-100 mM) or of EGTA (e.g., in the range from 1-1000 mM) for a sufficiently long period of time (such as 22 hours at 55° C.).
The measured fluorescence, F, is composed of contributions form the folded and unfolded forms of the enzyme. The following equation can be derived to describe the dependence of F on calcium concentration ([Ca]):

F=[Ca]/(Kdiss+[Ca])(aN−bN log ([Ca]))+Kdiss/(Kdiss+[Ca])(aU−bU log ([Ca]))

where aN is the fluorescence of the native (folded) form of the enzyme, bN is the linear dependence of aN on the logarithm of the calcium concentration (as observed experimentally), aU is the fluorescence of the unfolded form and bU is the linear dependence of aU on the logarithm of the calcium concentration. Kdiss is the apparent calcium binding constant for an equilibrium process as follows:

Kdiss 

N—Ca<<U+Ca(N=native enzyme; U=unfolded enzyme)

In fact, unfolding proceeds extremely slowly and is irreversible. The rate of unfolding is dependent on calcium concentration, and such dependency for a given enzyme provides a measure of the calcium binding affinity of the enzyme. By defining a standard set of reaction conditions (e.g., 22 hours at 55° C.), a meaningful comparison of Kdiss for different maltogenic alpha-amylase variants can be made.
INDUSTRIAL APPLICATIONS
The maltogenic alpha-amylase variants of the invention possesses valuable properties which may be advantageously used in various industrial applications. In particular, the enzyme finds potential application for retarding or preventing retrogradation, and thus the staling, of starch based food such as common in the baking industry.
The variant may be used for the preparation of bread and other bread products in accordance with conventional techniques known in the art.
It is believed that the modification of the starch fraction by use of the present invention results in increased volume in baked products and improved organoleptic qualities, such as flavour, mouth feel, palatability, aroma and crust colour.
The maltogenic alpha-amylase variant may be used as the only enzyme or as a major enzymatic activity in combination with one or more additional enzymes, such as xylanase, lipase, glucose oxidase and other oxidoreductases, or an amylolytic enzyme.
The enzyme variants of the invention also find industrial applicability as a component in washing, dishwashing and hard-surface cleaning detergent compositions. Some variants are particularly useful in a process for the manufacture of linear oligosaccharides, or in the production of sweeteners and ethanol from starch, and/or for textile desizing. Conditions for conventional starch conversion processes, including starch liquefaction and/or saccharification processes, are described in, e.g., U.S. Pat. No. 3,912,590 and in EP patent publications Nos. 252,730 and 63,909.
The invention is further illustrated with reference to the following examples which are not intended to be in any way limiting to the scope of the invention as claimed.
Determination of Maltogenic Amylase in MANU
One Maltogenic Amylase Novo Unit (MANU) is the amount of enzyme which under standard will cleave one μmol maltotriose per minute. The standard conditions are 10 mg/ml maltotriose, 37° C., pH 5.0, 30 minutes reaction time.
The pH dependence is found by repeating this measurement at the same conditions, but at different pH values.
EXAMPLES
Example 1
Construction of a Variant of Novamyl with Altered pH Dependent Activity
Novamyl is expressed in Bacillus subtilis from a plasmid denoted herein as pLBei010. This plasmid contains amyM in which the expression of amyM is directed by its own promoter and the complete gene encoding Novamyl, e.g., as contained in the strain DSM 11837. The plasmid contains the origin of replication, ori, from plasmid pUB110 and an kanamycin resistance marker for selection purposes. pLBei010 is shown in FIG. 1.
Primer Sequences
Site directed mutants of Novamyl were constructed by the megaprimer method essentially as described by Kammann et al. (1989). Briefly, a mutagenic oligonucleotide primer is used together in a PCR reaction with a suitable opposite DNA strand end primer to create a preliminary PCR product. This product is then used as a megaprimer together with another opposite DNA strand end primer to create a double-stranded DNA product. The product of the final PCR reaction was routinely used to replace a corresponding DNA fragment in the pLBei010 plasmid by standard cloning procedures. Mutants were transformed directly into Bacillus subtilis strain SHa273, a derivative of Bacillus subtilis 168 which is apr−, npr−, amyE−, amyR2− and prepared by methods known in the art.
Oligonucleotide primers used in the construction of described variants are as listed below:
Variant Sequence (5′→3′)
F188H: SEQ ID NO: 3
F188E: SEQ ID NO: 4
F284E: SEQ ID NO: 5
F284D: SEQ ID NO: 6
F284K: SEQ ID NO: 7
N327D: SEQ ID NO: 8
Variant Sequence (3′→5′)
T288K: SEQ ID NO: 9
T288R: SEQ ID NO: 10
Aspartate variants of F284, T288 and N327 were obtained using primer A189 (SEQ ID NO: 11) and B649 (SEQ ID NO: 12) as end-primers.
F188-variants F188L, T189Y were obtained using primer A82 (SEQ ID NO: 13) and B346 (SEQ ID NO: 14) as end-primers.
PCR products with the desired modification(s) were purified, digested with appropriate enzymes, separated by agarose gel electrophoresis and extracted, ethanol precipitated in the presence of glycogen, resuspended in H2O, ligated to pLBei010 which had been digested with the same appropriate enzymes, and transformed into Bacillus subtilis SHa273. Transformants were checked for size by colony PCR and for the insertion or removal of specific restriction sites by restriction enzyme digestion. Positive colonies were verified by DNA sequencing methods as described in the art.
Fermentation
The B. subtilis SHa273 mutant clones were grown overnight on LB-Kana (10 μg/ml)—Starch plates at 37° C. The colonies from the plate were resuspended in 10 ml Luria broth. One-sixth of each of the suspensions were inoculated into a 500 ml shake flasks containing 100 ml PS-1 media, a soy meal/sucrose-based media, kanamycin for a final concentration of 10 μg/ml and 100 μl 5M NaOH. The pH was adjusted to 7.5 with NaOH before inoculation. The cultures were incubated for five days at 30° C. with shaking at 270-300 rpm.
Enzyme Purification
Large particles from the media were removed by flocculation before affinity chromatography. Superfloc C521 (American Cyamide Company) was used as the cationic flocculant and Superfloc A130 (American Cyamide Company) as the anionic flocculant.
The culture suspension was diluted 1:1 with deionized water and the pH was adjusted to approx. 7.5. A volume of 0.01 ml of 50 w/w % CaCl2 per ml diluted culture was added during stirring. A volume of 0.015 ml of 20w/w % Na-aluminate per ml diluted culture was titrated with 20% formic acid, while keeping the pH between 7 and 8. While stirring 0.025 ml 10 v/v % of C521 per ml diluted culture was added, followed by 0.05 ml 1 w/v % A130 per ml diluted culture, or until flocculation was observed. The solution was centrifuged at 4500 rpm for 30 minutes. Filtration was performed using a filter of pore size of 0.45 μm to exclude larger particles and any remaining bacteria. The filtered solution was stored at −20° C.
Immobilization of α-Cyclodextrin to DSV-Aqarose
One hundred mg of α-cylcodextrin of molecular weight 972.86 g/mol (Fluka 28705) was dissolved in 20 ml coupling buffer (0.5M Na2CO3, pH 11). Ten ml of DSV-agarose (Mini-Leak, Medium 10-20 mmol/l of divinyl sulfone activated agarose (Kem-En-Tec) was washed thoroughly with deionized water, then dried by suction and transferred to the α-cyclodextrin solution. After the mixture had stirred for 24 hr at ambient temperature, the gel was washed with deionized water, followed by 0.5M KHCO3. The gel was transferred to the blocking buffer (20 ml 0.5M KHCO3+1 ml mercaptoethanol), stirred for 2 hr at ambient temperature, then washed with deionized water.
Affinity Chromatography
The variants were purified by affinity chromatography using the Pharmacia FPLC System. A 0.04 volume of 1M Na-acetate pH 5 was added to the filtrate obtained by flocculation to adjust pH and CaCl2 was added to a final concentration of 10−10 M. The solution was filtered and degassed. A Pharmacia XK16 column was prepared with ten ml of the immobilised α-cyclodextrin, then equilibrated in the equilibration buffer (25 mM Na-acetate pH 5) by washing with approximately 10 times the column volume. The filtrate was applied to the XK16 column, which was then washed with the equilibration buffer until protein could no longer be detected in the washing buffer. The column was washed with the equilibration buffer containing 0.5M NaCl to elute nonspecific material, followed by another wash with 2-3 times the column volume of the equilibration buffer. All washings were performed using a flow rate of 10 ml/min. Specifically bound material was eluted using a solution of 2% α-cyclodextrin in the wash buffer and collected using the Pharmacia Liquid Chromatography Collector LCC-500 Plus using a flow rate of 5 ml/min.
Example 2
pH Dependent Activity of Variants
The variants prepared in the preceding Example were tested for activity at various pH values as follows.
A colorimetric glucose oxidase-peroxidase assay for liberated glucose from maltotriose or amylopectin was used to determine the pH activity profiles of the enzyme variants (Glucose/GOD-Perid® Method, Boehringer Mannheim, Indianapolis Ind.). Activity was assayed in a buffer of 25 mM citrate-phosphate, 0.1 mM CaCl2 at pH values of 2, 2.5, 3, 3.5, 4, 4.5, 5, 5.5, 6, 6.5, 7, 7.5, 8 and 8.6. The buffer pH was adjusted using NaOH and enzymes were diluted in 25 mM citrate-phosphate buffer pH 5. Measurements were taken in duplicate to obtain an average value. All values are relative to the pH at which the highest level of activity is seen.
The results, shown in the table below, indicate that each of the variants has an alteration in the pH dependent activity profile when compared to the parent Novamyl®. The highest level of activity for each variant is designated 100% and the activity of that variant measured at the other indicated pH values is a relative percentage of that maximum.













pH





















Modifications
2.0
2.5
3.0
3.5
4.0
4.5
5.0
5.5
6.0
6.5
7.0
7.5
8.0
8.6
























None (parent)
0
0
0
8
47
80
100
95
91
80
66
39
35
30


F188H
1
0
0
1
3
29
77
99
100
88
59
39
31
27


F188E
0
0
0
2
27
62
89
100
93
71
46
28
20
18


T288R
0
0
0
8
51
77
94
100
86
73
50
34
27
12


N327D
1
1
7
27
67
95
100
98
77
33
19
11
5
0









Further, a number of Novamyl variants were tested for activity at pH 4.0 and 5.0, taking the activity of Novamyl at the same pH as 100%. The activity was determined by hydrolysis of maltotriose (10 mg/ml) at 60° C., 50 mM sodium acetate, 1 mM CaCl2. The results are expressed as the ratio between activity at pH 5.0 and pH 4.0:














Modifications
pH 5.0/pH 4.0



















N131D
0.24



I174Q
0.31



G397P
0.40



H103Y
0.40



Δ 262-266
0.47



T142A + D261G + T288P + Q449R
0.50



S32Q
0.53



S32D
0.55



T142A + D261G
0.62



G370N + N371G
0.66



S32N
0.68



N176S
0.79



D17E
0.80



None (parent)
1



Δ 191
1.39



192-A-193
1.61



I174E
1.80



192-A-G-193
1.90



Δ 192
2.22



F188L + D261G + T288P
2.47










The results demonstrate that variants with a higher or lower pH optimum can be obtained according to the invention.
Example 3
Thermostability of Variants
Incubation at 80° C.
The thermostability of a number of Novamyl variants was tested by incubating an aqueous solution at 80° C., pH 4.3, 50 mM acetate buffer, 1 mM CaCl2, and measuring the residual amylase activity at various times. The parent enzyme, Novamyl, was included for comparison. The results are expressed as residual activity at various times in percent of initial activity:


















5
10
15
20
25


Variant
0
min.
min.
min.
min.
min.





















None (parent)
100
23
9
3
1
0


A197P + D261G + T288P +
100
36
28
14
16
9


N342S


A30D + K40R + D261G
100
38
24
15
13
10


T288K
100
64
31
18
7
4


T142A + N327S + K425E +
100
47
39
25
19
11


K520R + N595I


T142A + D261G + T288P +
100
45
36
27
16
9


Q449R


K40R + F188L + D261G +
100
56
48
40
36
30


A483T


F188L + V336L + T525A
100
63
49
48
52
47


F188I + Y422F + I660V
100
71
60
51
43
38


N115D + F188L
100
73
60
51
44
39


F188L + D261G + T288P
100
60
67
66
63
67


F188L + D261G + T288P +
100
66
72
73
75
78


A483T


N26S + F188L + D261G +
100
80
80
82
84
84


T288P + T594A + I600V


N26S + T80A + F188L +
100
80
75
82
83
87


D261G + T288P + R291L









The above data show a clearly improved thermostability for the variants compared to the parent amylase. Thus, after 15 minutes incubation at 80° C., a number of variants show at least 25% residual activity, and some even show at least 50% residual activity, whereas the parent enzyme has essentially lost its activity.
Incubation at 85° C.
The Novamyl variant S32E was tested by incubation with 1 mM Ca++ at 85° C. for 15 minutes. The variant showed a residual activity of 48% whereas the parent enzyme (Novamyl) showed 32% residual activity at the same conditions.
Incubation at 90° C.
Four variants and the parent enzyme were tested by incubating at 90° C., pH 5.0, 50 mM acetate buffer, 1 mM CaCl2, and measuring the residual activity. The results were as follows:














Variant
0
10 min.
20 min.
30 min.



















None (parent)
100
5
0
0


F188L + D261G + T288P
100
70
41
28


N26S + F188L + D261G +
100
71
54
39


T288P + T594A + I600V


N26S + T80A + F188L +
100
43
26
13


D261G + T288P + R291L


F188L + D261G + T288P + A483T
100
54
39
26









The variants show a clearly improved thermostability. Thus, the variants retain more than 10% (or even more than 20%) relative activity after 30 minutes incubation at 90° C., whereas the parent enzyme loses all activity after 20 minutes.
DSC
Further, the thermostability was tested for some Novamyl variants by DSC (differential scanning calorimetry) at pH values in the range 4.0-5.5. Again, the parent amylase was included for comparison. The results are expressed as the denaturation temperature (Tm) at the given pH:














Modifications
pH 4.0
pH 4.3
pH 5.0
pH 5.5







None (parent)
64° C.
79° C.
83° C.
88° C.


N115D + F188L

86° C.

92° C.


T142A + N327S + K425E +



93° C.


K520R + N595I


F188L + D261G + T288P
75° C.

95° C.









The results show improved thermostability for each variant. One variant shows an improvement of more than 10° C. at pH 4.0 and 5.5.
Example 4
Specific Activity of Variants
Amylase activity was determined by a colorimetric measurement after action on Phadebas tablets at pH 5.0 and 60° C. The results for two Novamyl variants, relative to Novamyl were as follows.














Modifications
Relative amylase activity









None (parent)
100



192-A-193
110



Δ (191-195)
300










The specific activity was further tested by action on maltotriose at pH 4.0, 60° C. by the MANU method described above. The results showed that the variant G370N, N371G has a maltotriose activity of 106% compared to Novamyl.
Example 5
Inhibition of Retrogradation
The efficiency of Novamyl and Novamyl variants to inhibit retrogradation was determined as follows:
730 mg of 50% (w/w) amylopectin slurry in 0.1 M sodium acetate, at a selected pH (3.7, 4.3 or 5.5) was mixed with 20 μl of an enzyme sample, and the mixture was incubated in a sealed ampoule for 1 hour at 40° C., followed by incubation at 100° C. for 1 hour in order to gelatinize the samples. The sample was then aged for 7 days at room temperature to allow recrystallization of the amylopectin. A control without enzyme was included.
After aging, DSC was performed on the sample by scanning from 5° C. to 95° C. at a constant scan rate of 90° C./hour. The area under the first endothermic peak in the thermogram was taken to represent the amount of retrograded amylopectin, and the relative inhibition of retrogradation was taken as the area reduction (in %) relative to the control without enzyme.
In the table below, the efficiency of the enzyme is expressed as the ratio of the relative inhibition of retrogradation to the enzyme dosage (in MANU/ml):

















Relative



pH
Modifications
MANU/ml
inhibition
Efficiency



















3.7
A30D + K40R + D261G
0.23
0.38
1.7


3.7
T142A + N327S + K425E +
0.07
0.29
4.1



K520R +N595I


3.7
None (parent)
0.27
0.38
1.4


4.3
N115D + F188L
0.01
0.18
18


4.3
None (parent)
0.27
0.43
1.6


5.5
Δ (191-195) + F188L + T189Y
0.02
0.12
6


5.5
Δ (191-195)
0.02
0.14
7


5.5
Δ (191-195)
0.05
0.31
6.2


5.5
N115D + F188L
0.01
0.39
39


5.5
T142A + D261G
0.14
0.53
3.8


5.5
None (parent)
0.27
0.49
1.8









The results demonstrate that a number of variants are more efficient than the parent amylase to inhibit retrogradation.
Example 6
Anti-Staling Effect of Variants
Bread was made by an European Straight Dough method (wheat flour, water, yeast, salt, sugar, ascorbic acid) or from a wheat sour dough (acidified with “Ireks ferdigsauer” from Balchem Co.) with or without addition of enzymes, and loaves were baked in lidded pans, to avoid volume effects. pH in the dough was measured by blending 10 g of the mixed dough with 100 ml of deionised water for 30 min before measurement of pH in the suspension. The bread was allowed to cool for 2 hours, and the texture was analyzed by a Texture Analyser TA-XT2 from Stable Micro Systems. The remaining loaves were then wrapped in plastic bags and stored at room temperature for texture analysis after 1, 4 and 7 days.
The texture analysis of each loaf was done by cutting 4 slices; the force was measured at 25% compression (P1), at 40% compression (P2) and after keeping 40% compression constant for 30 sec. (P3). P1 was taken as the firmness (in grams), and the ratio (P3/P2) was taken as the elasticity of the crumb. The extent of retrogradation after 7 days storage was determined by DSC as described in Example 7.
European Straight Dough (pH5.5-6.0)
A Novamyl variant (T142A+N327S+K425E+K520R+N5951) was tested at dosages in the range of 0-2 mg enzyme/kg flour, and the parent enzyme (Novamyl) was used for comparison.
The following results were obtained for elasticity (P3/P2) after two hours and 7 days and firmness (P1) after 7 days:















Dosage
Elasticity
Elasticity
Elasticity


Enzyme
mg/kg flour
2 hours
1 day
7 days







None
0
0.69
0.60
0.44


Parent
1
0.62
0.60
0.55



2
0.58
0.57
0.54


Variant
1
0.65
0.62
0.56



2
0.63
0.61
0.58

























Dosage
Firmness (P1)



Enzyme
mg/kg flour
after 7 days




















None
0
2267



Parent
1
1192




2
1113



Variant
1
1022




2
905










The results after two hours and 1 day show that at equal dosages, the variant gives a better elasticity than the parent enzyme. The results after 7 days show that the variant at dosages of 1-2 mg/kg gives a softer crumb (lower firmness and higher elasticity) than the parent enzyme at the same dosage. Thus, the variant has a better anti-staling effect throughout a 7-day storage period.
Sour Dough (pH Approx. 4.5)
A Novamyl variant (F188L+D261G+T288P) was tested in sour dough, and the parent enzyme (Novamyl) was used for comparison. The following results were obtained for firmness (P1) after 7 days. elasticity (P3/P2) after 4 and 7 days and retrogradation after 7 days:
















Dosage
Firmness (P1)



Enzyme
mg/kg flour
after 7 days




















None
0
2590



Parent
1
2031




3
1912




13
1570



Variant
1
1436




3
1226



























Dosage
Elasticity
Elasticity



Enzyme
mg/kg flour
4 days
7 days





















None
0
0.49
0.47



Parent
1
0.51
0.52




3
0.53
0.51




13
0.53
0.51



Variant
1
0.59
0.57




3
0.57
0.58


























Dosage
Retrogradation, 7 days



Enzyme
mg/kg flour
(relative to control)




















None
0
100%



Parent
1
100%




3
63%




13
32%



Variant
1
46%




3
20%










The results show that the variant has a markedly improved effect on texture evaluated as firmness and elasticity in sour dough at pH 4.5. A dosage of 1-3 mg/kg of the variant is superior to 13 mg/kg of the parent enzyme on all parameters tested, and the elasticity achieved with the variant cannot be matched by the parent enzyme at any dosage.
pH-Profile in Wheat-Flour Bread (pH Approx. 4.4; 4.9; and 5.5)
The Novamyl variant (F188L+D261G+T288P) was further tested in acidified wheat flour bread to measure the function over a broader pH range in baking application, while maintaining a comparable recipe. The parent enzyme (Novamyl) was used for comparison. Dosage of the parent enzyme was changed at the various pH to compensate for the lower activity of the parent enzyme at lower pH. The following results were obtained for firmness (P1) and elasticity (P3/P2) after 0 (=2 hours), 1, 3 and 7 days.














Dosage
Firmness













pH
Enzyme
mg/kg flour
0 days
1 day
3 days
7 days
















pH 4.4
None
0
450
1144
1945
3020



Variant
0.5
392
939
1386
1664



Parent
15
870
1206
1220
1511



Parent
1
586
1127
2005
2312


pH 4.9
None
0
330
764
1536
2005



Variant
0.5
287
687
767
1096



Parent
7
570
1075
984
1057



Parent
0.5
373
784
1170
1642


pH 5.5
None
0
217
711
1123
1382



Variant
0.5
315
447
712
846



Parent
3.5
431
629
666
718



Parent
0.5
381
599
630
922























Dosage
Elasticity













pH
Enzyme
mg/kg flour
0 days
1 day
3 days
7 days
















pH 4.4
None
0
0.70
0.61
0.53
0.48



Variant
0.5
0.70
0.63
0.59
0.56



Parent
15
0.53
0.50
0.52
0.51



Parent
1
0.65
0.60
0.55
0.51


pH 4.9
None
0
0.71
0.64
0.55
0.49



Variant
0.5
0.70
0.65
0.63
0.60



Parent
7
0.56
0.52
0.54
0.54



Parent
0.5
0.67
0.61
0.58
0.54


pH 5.5
None
0
0.70
0.61
0.56
0.51



Variant
0.5
0.68
0.64
0.61
0.60



Parent
3.5
0.58
0.56
0.57
0.57



Parent
0.5
0.63
0.61
0.62
0.58









It is clearly observed, that the variant is much improved compared to the parent at all pH, and especially at lower pH. The elasticity is higher, and the crumb stays more soft over the measured time span.
Four Variants Tested in Wheat Sourdough Compared to Parent Enzyme
Four Novamyl variants were tested in another test series of acidified wheat flour bread to determine the performance in sourdough baking application. pH in the bread and dough was measured to be in the interval 4.30-4.40. The parent enzyme (Novamyl) was used for comparison. Dosage of the parent enzyme was chosen at 1 and 13 mg/kg flour, much higher than the variants, as we have experienced that this is needed to see effect of the parent enzyme in this specific application. The firmness (P1) and elasticity (P3/P2) were determined after 1, 3 and 7 days, and the extent of retrogradation after 7 days storage was determined as described above.














Dosage




mg/kg
Firmness











Enzyme
flour
1 day
3 days
7 days














None
0
789
1624
2054


Parent
1
745
1107
1685



13
722
967
1205


N26S + F188L + D261G + T288P +
0.5
716
1170
1518


T594A + I600V
3
847
895
1188


F188L + D261G + T288P
0.5
689
1054
1457


A197P + D261G + T288P + N342S
0.5
638
1114
1631


F188L + D261G + T288P + A483T
0.5
643
983
1562



3
660
804
953























Dosage




mg/kg
Elasticity











Enzyme
flour
1 day
3 days
7 days














None
0
0.63
0.55
0.48


Parent
1
0.64
0.57
0.49



13
0.57
0.56
0.53


N26S + F188L + D261G + T288P +
0.5
0.63
0.56
0.50


T594A + I600V
3
0.61
0.59
0.57


F188L + D261G + T288P
0.5
0.64
0.58
0.53


A197P + D261G + T288P + N342S
0.5
0.64
0.57
0.50


F188L + D261G + T288P + A483T
0.5
0.65
0.58
0.53



3
0.63
0.60
0.58























Retrogradation,



Dosage
7 days


Enzyme
mg/kg flour
(relative to control)

















None
0
100%


Parent
1
67%



13
21%


N26S + F188L + D261G + T288P +
0.5
72%


T594A + I600V
3
18%


F188L + D261G + T288P
0.5
53%


A197P + D261G + T288P + N342S
0.5
59%


F188L + D261G + T288P + A483T
0.5
43%



3
10%









For antistaling (fresh-keeping) it is particularly important, that the bread is soft and elastic after several days storage. Therefore, most weight should be put on the textural properties after 7 days of storage. It is clearly observed, that the variants are much improved compared to the parent. The elasticity is higher, and the crumb stays more soft.
Example 7
Cleavage Pattern of Variants
The cleavage pattern in starch hydrolysis was compared for two variants and the parent enzyme, Novamyl.
The results below indicate % by weight of each oligosacccharide (G1-G8) formed after 24 hours incubation in 1% (w/v) starch using 50 mM sodium acetate, 1 mM CaCl2, pH 5.0 at 50° C. The oligosaccharides were identified and quantitated using HPLC.













Oligosaccharide
Parent
Δ (191-195)
N115D + F188L


















G8
—
1.7
—


G7
—
2.6
—


G6
—
7.5
1.4


G5
—
10.1
2.1


G4
—
21.1
11.3


G3
—
28.7
10.7


G2
96.5
28.3
61.9


G1
3.5
—
12.6









The results demonstrate a significantly altered cleavage pattern. Novamyl after 24 hours produces mainly maltose and virtually no higher oligosaccharides. In contrast, the two variants produce significant amounts of maltotriose and higher oligosaccharides.
Example 8
Substrate Specificity of Variants
The activity of variants was tested on two different substrates: glucose release from maltotriose and color release from Phadebas colored starch. The parent enzyme (Novamyl) was tested for comparison. The measurements were made at pH 5, and each activity was expressed relative to the parent enzyme. The ratio of activities on the two substrates was found to be as follows:












Activity ratio


Variant
Starch/maltotriose







Parent enzyme
1.0


F188L, D261G, T288P
3.6


N26S + F188L, D261G, T288P, T594A, I600V
5.5


N26S, T80A, F188L, D261G, T288P, R291L
1.9


A197P, D261G, T288P, N342S
1.5


T142A, D261G, T288P, Q449R
2.5


F188L, D261G, T288P, A483T
2.5









It is seen that the 6 variants have an increased activity on starch relative to maltotriose.
REFERENCES CITED


    Klein, C., et al., Biochemistry 1992, 31, 8740-8746,
    Mizuno, H., et al., J. Mol. Biol. (1993) 234, 1282-1283,
    Chang, C., et al, J. Mol. Biol. (1993) 229, 235-238,
    Larson, S. B., J. Mol. Biol. (1994) 235, 1560-1584,
    Lawson, C. L., J. Mol. Biol. (1994) 236, 590-600,
    Qian, M., et al., J. Mol. Biol. (1993) 231, 785-799,
    Brady, R. L., et al., Acta Crystallogr. sect. B, 47, 527-535,
    Swift, H. J., et al., Acta Crystallogr. sect. B, 47, 535-544
    A. Kadziola, Ph.D. Thesis: “An alpha-amylase from Barley and its Complex with a Substrate Analogue Inhibitor Studied by X-ray Crystallography”, Department of Chemistry University of Copenhagen 1993
    MacGregor, E. A., Food Hydrocolloids, 1987, Vol. 1, No. 5-6, p.
    B. Diderichsen and L. Christiansen, Cloning of a maltogenic α-amylase from Bacillus stearothermophilus, FEMS Microbiol. letters: 56: pp. 53-60 (1988)
    Hudson et al., Practical Immunology, Third edition (1989), Blackwell Scientific Publications,
    Sambrook et al., Molecular Cloning: A Laboratory Manual, 2nd Ed., Cold Spring Harbor, 1989
    S. L. Beaucage and M. H. Caruthers, Tetrahedron Letters 22, 1981, pp. 1859-1869
    Matthes et al., The EMBO J. 3, 1984, pp. 801-805.
    R. K. Saiki et al., Science 239, 1988, pp. 487-491.
    Morinaga et al., (1984, Biotechnology 2:646-639)
    Nelson and Long, Analytical Biochemistry 180, 1989, pp. 147-151
    Hunkapiller et al., 1984, Nature 310:105-111
    R. Higuchi, B. Krummel, and R. K. Saiki (1988). A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucl. Acids Res. 16:7351-7367.
    Dubnau et al., 1971, J. Mol. Biol. 56, pp. 209-221.
    Gryczan et al., 1978, J. Bacteriol. 134, pp. 318-329.
    S. D. Erlich, 1977, Proc. Natl. Acad. Sci. 74, pp. 1680-1682.
    Boel et al., 1990, Biochemistry 29, pp. 6244-6249.
    Kammann, M Laufs, J Schell, J and Gronnenborn, B (1989) Nucleic Acids Research 20:4937-4938.









TABLE 1





Atom Coordinates from the Crystal Structure of NOVAMYL

























1
N
SER
A
1
10.254
56.595
38.175
1.00
15.64
7


2
CA
SER
A
1
11.216
55.462
37.898
1.00
15.87
6


3
C
SER
A
1
12.466
55.723
38.726
1.00
14.53
6


4
O
SER
A
1
12.585
56.773
39.369
1.00
15.99
8


5
CB
SER
A
1
11.527
55.345
36.397
1.00
21.54
6


6
OG
SER
A
1
12.305
56.503
36.045
1.00
20.33
8


7
N
SER
A
2
13.466
54.795
38.551
1.00
18.07
7


8
CA
SER
A
2
14.705
55.061
39.291
1.00
19.33
6


9
C
SER
A
2
15.621
56.069
38.559
1.00
15.87
6


10
O
SER
A
2
16.573
56.563
39.209
1.00
16.73
8


11
CB
SER
A
2
15.490
53.735
39.422
1.00
26.53
6


12
OG
SER
A
2
15.918
53.392
38.123
1.00
21.07
8


13
N
SER
A
3
15.136
56.545
37.384
1.00
12.71
7


14
CA
SER
A
3
15.956
57.522
36.680
1.00
13.38
6


15
C
SER
A
3
15.873
58.916
37.316
1.00
12.57
6


16
O
SER
A
3
16.759
59.749
37.029
1.00
15.22
8


17
CB
SER
A
3
15.434
57.682
35.219
1.00
16.30
6


18
OG
SER
A
3
15.593
56.381
34.568
1.00
23.61
8


19
N
ALA
A
4
14.811
59.222
38.050
1.00
10.88
7


20
CA
ALA
A
4
14.574
60.623
38.384
1.00
11.38
6


21
C
ALA
A
4
15.599
61.115
39.409
1.00
12.81
6


22
O
ALA
A
4
15.888
62.314
39.355
1.00
12.58
8


23
CB
ALA
A
4
13.132
60.682
38.956
1.00
14.28
6


24
N
SER
A
5
15.968
60.306
40.380
1.00
13.21
7


25
CA
SER
A
5
16.905
60.780
41.427
1.00
14.29
6


26
C
SER
A
5
18.163
59.941
41.357
1.00
16.01
6


27
O
SER
A
5
18.053
58.724
41.237
1.00
16.41
8


28
CB
SER
A
5
16.218
60.613
42.785
1.00
15.57
6


29
OG
SER
A
5
17.193
60.855
43.843
1.00
13.17
8


30
N
VAL
A
6
19.340
60.530
41.476
1.00
10.07
7


31
CA
VAL
A
6
20.589
59.751
41.567
1.00
10.13
6


32
C
VAL
A
6
21.169
59.955
42.963
1.00
10.99
6


33
O
VAL
A
6
22.349
59.685
43.172
1.00
10.81
8


34
CB
VAL
A
6
21.639
60.160
40.513
1.00
13.85
6


35
CG1
VAL
A
6
21.002
59.694
39.148
1.00
15.29
6


36
CG2
VAL
A
6
21.874
61.656
40.459
1.00
12.12
6


37
N
LYS
A
7
20.369
60.349
43.964
1.00
10.30
7


38
CA
LYS
A
7
20.901
60.604
45.331
1.00
9.78
6


39
C
LYS
A
7
21.508
59.360
46.015
1.00
12.06
6


40
O
LYS
A
7
22.382
59.560
46.857
1.00
12.59
8


41
CB
LYS
A
7
19.830
61.187
46.264
1.00
11.40
6


42
CG
LYS
A
7
19.414
62.588
45.680
1.00
12.09
6


43
CD
LYS
A
7
18.160
63.123
46.350
1.00
9.80
6


44
CE
LYS
A
7
17.698
64.488
45.795
1.00
10.87
6


45
NZ
LYS
A
7
17.114
64.187
44.425
1.00
11.38
7


46
N
GLY
A
8
21.036
58.214
45.577
1.00
13.10
7


47
CA
GLY
A
8
21.604
56.982
46.166
1.00
12.31
6


48
C
GLY
A
8
22.718
56.358
45.340
1.00
14.02
6


49
O
GLY
A
8
23.109
55.205
45.579
1.00
13.36
8


50
N
ASP
A
9
23.133
57.048
44.293
1.00
11.90
7


51
CA
ASP
A
9
24.049
56.447
43.319
1.00
11.74
6


52
C
ASP
A
9
25.478
56.996
43.442
1.00
10.18
6


106
CB
ILE
A
15
37.192
59.653
28.343
1.00
10.73
6


107
CG1
ILE
A
15
37.106
60.975
29.131
1.00
11.86
6


108
CG2
ILE
A
15
37.626
60.014
26.904
1.00
12.56
6


109
CD1
ILE
A
15
36.181
62.091
28.574
1.00
15.42
6


110
N
ILE
A
16
34.926
57.450
26.561
1.00
10.37
7


111
CA
ILE
A
16
34.728
56.178
25.868
1.00
11.03
6


112
C
ILE
A
16
35.990
55.729
25.099
1.00
12.23
6


113
O
ILE
A
16
36.342
54.511
25.184
1.00
11.07
8


114
CB
ILE
A
16
33.578
56.292
24.863
1.00
10.56
6


115
CG1
ILE
A
16
32.240
56.387
25.709
1.00
11.92
6


116
CG2
ILE
A
16
33.444
55.053
23.953
1.00
11.18
6


117
CD1
ILE
A
16
31.115
56.958
24.823
1.00
13.67
6


118
N
ASP
A
17
36.565
56.624
24.314
1.00
10.08
7


119
CA
ASP
A
17
37.730
56.165
23.518
1.00
8.61
6


120
C
ASP
A
17
38.911
55.693
24.346
1.00
10.86
6


121
O
ASP
A
17
39.777
54.987
23.831
1.00
11.03
8


122
CB
ASP
A
17
38.184
57.422
22.675
1.00
11.30
6


123
CG
ASP
A
17
39.380
57.017
21.755
1.00
9.77
6


124
OD1
ASP
A
17
39.105
56.206
20.852
1.00
11.65
8


125
OD2
ASP
A
17
40.480
57.562
21.970
1.00
11.48
8


126
N
ARG
A
18
38.972
55.999
25.646
1.00
9.54
7


127
CA
ARG
A
18
40.113
55.719
26.527
1.00
8.38
6


128
C
ARG
A
18
39.826
54.720
27.608
1.00
9.97
6


129
O
ARG
A
18
40.643
54.490
28.501
1.00
13.32
8


130
CB
ARG
A
18
40.537
57.083
27.137
1.00
11.02
6


131
CG
ARG
A
18
40.931
58.139
26.063
1.00
9.63
6


132
CD
ARG
A
18
42.135
57.721
25.237
1.00
9.86
6


133
NE
ARG
A
18
42.280
58.523
23.969
1.00
10.16
7


134
CZ
ARG
A
18
43.103
59.578
23.903
1.00
13.46
6


135
NH1
ARG
A
18
43.748
60.063
24.966
1.00
12.03
7


136
NH2
ARG
A
18
43.350
60.181
22.725
1.00
10.43
7


137
N
PHE
A
19
38.648
54.007
27.497
1.00
11.25
7


138
CA
PHE
A
19
38.296
53.057
28.601
1.00
10.13
6


139
C
PHE
A
19
38.543
51.614
28.192
1.00
12.61
6


140
O
PHE
A
19
39.528
51.024
28.677
1.00
12.51
8


141
CB
PHE
A
19
36.798
53.294
28.945
1.00
13.20
6


142
CG
PHE
A
19
36.342
52.543
30.189
1.00
12.09
6


143
CD1
PHE
A
19
36.849
52.908
31.423
1.00
12.96
6


144
CD2
PHE
A
19
35.472
51.447
30.058
1.00
13.30
6


145
CE1
PHE
A
19
36.500
52.187
32.563
1.00
16.46
6


146
CE2
PHE
A
19
35.184
50.719
31.215
1.00
12.02
6


147
CZ
PHE
A
19
35.638
51.089
32.482
1.00
11.98
6


148
N
TYR
A
20
37.844
51.054
27.199
1.00
11.48
7


149
CA
TYR
A
20
38.154
49.694
26.772
1.00
11.40
6


150
C
TYR
A
20
37.730
49.476
25.321
1.00
10.89
6


151
O
TYR
A
20
36.593
49.813
24.934
1.00
11.80
8


152
CB
TYR
A
20
37.417
48.696
27.719
1.00
12.88
6


153
CG
TYR
A
20
37.927
47.270
27.504
1.00
13.88
6


154
CD1
TYR
A
20
39.216
46.968
27.943
1.00
14.05
6


155
CD2
TYR
A
20
37.160
46.285
26.932
1.00
15.80
6


156
CE1
TYR
A
20
39.717
45.678
27.800
1.00
16.74
6


157
CE2
TYR
A
20
37.658
44.982
26.795
1.00
19.32
6


158
CZ
TYR
A
20
38.935
44.710
27.214
1.00
19.70
6


159
OH
TYR
A
20
39.458
43.422
27.062
1.00
22.69
8


160
N
ASP
A
21
38.662
48.893
24.586
1.00
13.46
7


161
CA
ASP
A
21
38.414
48.628
23.134
1.00
14.35
6


162
C
ASP
A
21
37.754
47.226
23.097
1.00
14.61
6


163
O
ASP
A
21
38.426
46.196
23.063
1.00
13.84
8


164
CB
ASP
A
21
39.746
48.665
22.413
1.00
14.54
6


165
CG
ASP
A
21
39.678
48.444
20.909
1.00
17.30
6


166
OD1
ASP
A
21
38.565
48.288
20.425
1.00
12.67
8


167
OD2
ASP
A
21
40.759
48.450
20.282
1.00
15.87
8


168
N
GLY
A
22
36.430
47.219
23.040
1.00
12.11
7


169
CA
GLY
A
22
35.683
45.934
23.110
1.00
15.21
6


170
C
GLY
A
22
35.482
45.410
21.664
1.00
18.33
6


171
O
GLY
A
22
35.034
44.264
21.516
1.00
17.21
8


172
N
ASP
A
23
35.786
46.189
20.639
1.00
13.30
7


173
CA
ASP
A
23
35.505
45.770
19.261
1.00
14.68
6


174
C
ASP
A
23
36.634
46.389
18.425
1.00
14.54
6


175
O
ASP
A
23
36.570
47.597
18.138
1.00
13.39
8


176
CB
ASP
A
23
34.163
46.271
18.762
1.00
13.59
6


177
CG
ASP
A
23
33.889
45.785
17.319
1.00
16.74
6


178
OD1
ASP
A
23
34.805
45.200
16.750
1.00
17.96
8


179
OD2
ASP
A
23
32.782
46.058
16.872
1.00
16.43
8


180
N
THR
A
24
37.681
45.659
18.083
1.00
15.02
7


181
CA
THR
A
24
38.769
46.308
17.340
1.00
16.37
6


182
C
THR
A
24
38.381
46.606
15.923
1.00
15.39
6


183
O
THR
A
24
39.124
47.376
15.252
1.00
16.40
8


184
CB
THR
A
24
40.033
45.402
17.367
1.00
18.68
6


185
OG1
THR
A
24
39.710
44.147
16.673
1.00
17.99
8


186
CG2
THR
A
24
40.478
45.112
18.772
1.00
22.45
6


187
N
THR
A
25
37.228
46.150
15.423
1.00
16.09
7


188
CA
THR
A
25
36.864
46.330
14.019
1.00
16.07
6


189
C
THR
A
25
36.349
47.743
13.724
1.00
16.52
6


190
O
THR
A
25
36.215
48.013
12.538
1.00
20.25
8


191
CB
THR
A
25
35.780
45.366
13.475
1.00
20.06
6


192
OG1
THR
A
25
34.475
45.532
14.010
1.00
18.04
8


193
CG2
THR
A
25
36.248
43.924
13.739
1.00
21.26
6


194
N
ASN
A
26
36.066
48.509
14.802
1.00
13.98
7


195
CA
ASN
A
26
35.577
49.871
14.471
1.00
12.49
6


196
C
ASN
A
26
36.689
50.862
14.772
1.00
13.05
6


197
O
ASN
A
26
36.435
52.053
14.825
1.00
11.58
8


198
CB
ASN
A
26
34.283
50.103
15.246
1.00
13.85
6


199
CG
ASN
A
26
34.435
49.981
16.739
1.00
15.62
6


200
OD1
ASN
A
26
35.558
50.066
17.224
1.00
12.89
8


201
ND2
ASN
A
26
33.339
49.796
17.497
1.00
16.36
7


202
N
ASN
A
27
37.946
50.401
14.890
1.00
14.79
7


203
CA
ASN
A
27
38.972
51.353
15.290
1.00
12.19
6


204
C
ASN
A
27
39.404
52.337
14.189
1.00
13.62
6


205
O
ASN
A
27
39.775
53.461
14.499
1.00
14.13
8


206
CB
ASN
A
27
40.235
50.575
15.662
1.00
12.10
6


207
CG
ASN
A
27
40.150
49.884
17.001
1.00
15.80
6


208
OD1
ASN
A
27
39.065
49.932
17.554
1.00
12.92
8


209
ND2
ASN
A
27
41.187
49.291
17.571
1.00
15.14
7


210
N
ASN
A
28
39.211
51.954
12.920
1.00
14.26
7


211
CA
ASN
A
28
39.604
52.918
11.854
1.00
15.71
6


212
C
ASN
A
28
38.672
52.705
10.661
1.00
14.39
6


213
O
ASN
A
28
39.059
52.148
9.622
1.00
16.82
8


214
CB
ASN
A
28
41.036
52.497
11.478
1.00
13.79
6


215
CG
ASN
A
28
41.790
53.538
10.656
1.00
21.29
6


216
OD1
ASN
A
28
41.391
54.685
10.535
1.00
17.46
8


217
ND2
ASN
A
28
42.936
53.086
10.108
1.00
24.72
7


218
N
PRO
A
29
37.442
53.154
10.790
1.00
15.04
7


219
CA
PRO
A
29
36.430
52.993
9.742
1.00
17.37
6


220
C
PRO
A
29
36.734
53.802
8.507
1.00
18.08
6


221
O
PRO
A
29
37.259
54.906
8.580
1.00
16.51
8


222
CB
PRO
A
29
35.087
53.483
10.312
1.00
17.71
6


223
CG
PRO
A
29
35.394
53.615
11.787
1.00
17.95
6


224
CD
PRO
A
29
36.907
53.841
11.957
1.00
15.54
6


225
N
ALA
A
30
36.329
53.244
7.331
1.00
16.99
7


226
CA
ALA
A
30
36.533
54.024
6.117
1.00
19.06
6


227
C
ALA
A
30
35.841
55.375
6.161
1.00
16.15
6


228
O
ALA
A
30
36.398
56.355
5.599
1.00
18.27
8


229
CB
ALA
A
30
35.998
53.268
4.880
1.00
21.27
6


230
N
LYS
A
31
34.697
55.514
6.833
1.00
15.01
7


231
CA
LYS
A
31
34.012
56.812
6.886
1.00
14.64
6


232
C
LYS
A
31
34.944
57.908
7.416
1.00
15.07
6


233
O
LYS
A
31
34.722
59.094
7.172
1.00
14.25
8


234
CB
LYS
A
31
32.771
56.667
7.818
1.00
13.99
6


235
CG
LYS
A
31
31.981
57.980
8.050
1.00
13.23
6


236
CD
LYS
A
31
30.617
57.569
8.669
1.00
16.17
6


237
CE
LYS
A
31
29.763
58.766
9.053
1.00
14.65
6


238
NZ
LYS
A
31
30.427
59.568
10.156
1.00
12.05
7


239
N
SER
A
32
35.822
57.610
8.364
1.00
16.27
7


240
CA
SER
A
32
36.675
58.587
9.038
1.00
14.39
6


241
C
SER
A
32
38.087
57.989
9.161
1.00
17.62
6


242
O
SER
A
32
38.770
57.968
10.193
1.00
17.19
8


243
CB
SER
A
32
36.100
58.851
10.460
1.00
12.32
6


244
OG
SER
A
32
35.874
57.664
11.167
1.00
12.92
8


245
N
TYR
A
33
38.596
57.524
8.010
1.00
14.71
7


246
CA
TYR
A
33
39.875
56.801
8.045
1.00
15.23
6


247
C
TYR
A
33
41.051
57.676
8.444
1.00
14.94
6


248
O
TYR
A
33
41.042
58.848
8.023
1.00
17.62
8


249
CB
TYR
A
33
40.075
56.295
6.582
1.00
18.09
6


250
CG
TYR
A
33
41.166
55.254
6.536
1.00
20.46
6


251
CD1
TYR
A
33
40.982
53.978
7.004
1.00
26.95
6


252
CD2
TYR
A
33
42.408
55.618
6.002
1.00
31.14
6


253
CE1
TYR
A
33
41.994
53.027
6.944
1.00
33.56
6


254
CE2
TYR
A
33
43.422
54.670
5.943
1.00
31.30
6


255
CZ
TYR
A
33
43.210
53.409
6.402
1.00
33.88
6


256
OH
TYR
A
33
44.235
52.483
6.334
1.00
44.90
8


257
N
GLY
A
34
42.039
57.105
9.114
1.00
12.92
7


258
CA
GLY
A
34
43.281
57.836
9.403
1.00
14.92
6


259
C
GLY
A
34
43.255
58.672
10.686
1.00
15.08
6


260
O
GLY
A
34
44.274
59.342
10.956
1.00
15.24
8


261
N
LEU
A
35
42.253
58.417
11.548
1.00
12.52
7


262
CA
LEU
A
35
42.215
59.140
12.846
1.00
11.02
6


263
C
LEU
A
35
42.519
58.271
14.028
1.00
15.01
6


264
O
LEU
A
35
42.472
58.755
15.182
1.00
14.18
8


265
CB
LEU
A
35
40.784
59.737
13.090
1.00
10.53
6


266
CG
LEU
A
35
40.170
60.460
11.891
1.00
12.89
6


267
CD1
LEU
A
35
38.783
61.033
12.240
1.00
13.47
6


268
CD2
LEU
A
35
41.090
61.613
11.433
1.00
15.36
6


269
N
TYR
A
36
43.025
57.036
13.757
1.00
13.30
7


270
CA
TYR
A
36
43.335
56.061
14.796
1.00
13.00
6


271
C
TYR
A
36
44.826
55.913
15.032
1.00
15.18
6


272
O
TYR
A
36
45.610
55.855
14.049
1.00
15.86
8


273
CB
TYR
A
36
42.749
54.728
14.291
1.00
13.61
6


274
CG
TYR
A
36
43.149
53.492
15.076
1.00
12.30
6


275
CD1
TYR
A
36
42.927
53.383
16.454
1.00
14.21
6


276
CD2
TYR
A
36
43.807
52.460
14.391
1.00
16.88
6


277
CE1
TYR
A
36
43.317
52.206
17.122
1.00
14.97
6


278
CE2
TYR
A
36
44.182
51.320
15.075
1.00
19.02
6


279
CZ
TYR
A
36
43.930
51.206
16.416
1.00
17.90
6


280
OH
TYR
A
36
44.299
50.063
17.135
1.00
18.88
8


281
N
ASP
A
37
45.211
55.848
16.289
1.00
12.45
7


282
CA
ASP
A
37
46.646
55.624
16.621
1.00
12.80
6


283
C
ASP
A
37
46.700
54.350
17.441
1.00
14.03
6


284
O
ASP
A
37
46.507
54.281
18.673
1.00
13.32
8


285
CB
ASP
A
37
47.120
56.834
17.463
1.00
13.46
6


286
CG
ASP
A
37
48.543
56.543
17.991
1.00
20.57
6


287
OD1
ASP
A
37
49.278
55.720
17.366
1.00
17.00
8


288
OD2
ASP
A
37
48.902
57.113
19.028
1.00
17.32
8


289
N
PRO
A
38
47.163
53.245
16.821
1.00
15.62
7


290
CA
PRO
A
38
47.375
52.024
17.548
1.00
15.67
6


291
C
PRO
A
38
48.484
52.056
18.558
1.00
15.69
6


292
O
PRO
A
38
48.513
51.189
19.436
1.00
18.95
8


293
CB
PRO
A
38
47.669
50.946
16.450
1.00
17.01
6


294
CG
PRO
A
38
48.367
51.843
15.437
1.00
18.68
6


295
CD
PRO
A
38
47.570
53.192
15.409
1.00
18.22
6


296
N
THR
A
39
49.385
53.031
18.514
1.00
15.60
7


297
CA
THR
A
39
50.469
53.080
19.499
1.00
14.85
6


298
C
THR
A
39
50.126
53.773
20.822
1.00
17.68
6


299
O
THR
A
39
50.961
53.777
21.719
1.00
17.01
8


300
CB
THR
A
39
51.692
53.847
18.947
1.00
19.14
6


301
OG1
THR
A
39
51.503
55.239
18.723
1.00
16.66
8


302
CG2
THR
A
39
52.083
53.233
17.573
1.00
22.20
6


303
N
LYS
A
40
48.983
54.487
20.832
1.00
14.93
7


304
CA
LYS
A
40
48.588
55.225
22.041
1.00
14.22
6


305
C
LYS
A
40
49.736
56.141
22.483
1.00
17.80
6


306
O
LYS
A
40
50.009
56.348
23.685
1.00
17.78
8


307
CB
LYS
A
40
48.104
54.324
23.207
1.00
19.03
6


308
CG
LYS
A
40
47.023
53.320
22.775
1.00
18.65
6


309
CD
LYS
A
40
46.535
52.543
24.031
1.00
21.38
6


310
CE
LYS
A
40
45.432
51.573
23.590
1.00
22.34
6


311
NZ
LYS
A
40
45.883
50.563
22.605
1.00
21.85
7


312
N
SER
A
41
50.307
56.831
21.475
1.00
16.33
7


313
CA
SER
A
41
51.307
57.853
21.746
1.00
17.21
6


314
C
SER
A
41
50.929
59.210
21.203
1.00
16.87
6


315
O
SER
A
41
51.606
60.250
21.492
1.00
16.04
8


316
CB
SER
A
41
52.714
57.429
21.198
1.00
17.96
6


317
OG
SER
A
41
52.625
57.387
19.782
1.00
20.42
8


318
N
LYS
A
42
49.895
59.315
20.388
1.00
13.73
7


319
CA
LYS
A
42
49.446
60.589
19.836
1.00
12.77
6


320
C
LYS
A
42
48.152
60.921
20.603
1.00
13.20
6


321
O
LYS
A
42
47.111
60.351
20.317
1.00
12.98
8


322
CB
LYS
A
42
49.193
60.477
18.321
1.00
14.60
6


323
CG
LYS
A
42
50.523
60.079
17.606
1.00
19.41
6


324
CD
LYS
A
42
50.228
60.163
16.078
1.00
25.03
6


325
CE
LYS
A
42
51.611
60.340
15.395
1.00
34.65
6


326
NZ
LYS
A
42
52.071
58.949
15.130
1.00
41.02
7


327
N
TRP
A
43
48.256
61.858
21.565
1.00
11.08
7


328
CA
TRP
A
43
47.235
61.925
22.643
1.00
13.35
6


329
C
TRP
A
43
45.915
62.494
22.162
1.00
11.08
6


330
O
TRP
A
43
45.002
62.429
22.997
1.00
13.47
8


331
CB
TRP
A
43
47.831
62.848
23.743
1.00
14.15
6


332
CG
TRP
A
43
48.739
61.957
24.592
1.00
12.91
6


333
CD1
TRP
A
43
50.014
61.590
24.338
1.00
14.88
6


334
CD2
TRP
A
43
48.362
61.357
25.845
1.00
12.18
6


335
NE1
TRP
A
43
50.507
60.770
25.364
1.00
16.61
7


336
CE2
TRP
A
43
49.467
60.633
26.297
1.00
17.08
6


337
CE3
TRP
A
43
47.186
61.367
26.617
1.00
13.97
6


338
CZ2
TRP
A
43
49.497
59.891
27.501
1.00
19.44
6


339
CZ3
TRP
A
43
47.223
60.644
27.814
1.00
14.34
6


340
CH2
TRP
A
43
48.333
59.925
28.265
1.00
15.92
6


341
N
LYS
A
44
45.846
63.088
20.972
1.00
11.78
7


342
CA
LYS
A
44
44.532
63.606
20.529
1.00
10.59
6


343
C
LYS
A
44
43.959
62.797
19.362
1.00
11.15
6


344
O
LYS
A
44
43.021
63.227
18.707
1.00
11.48
8


345
CB
LYS
A
44
44.647
65.112
20.097
1.00
11.58
6


346
CG
LYS
A
44
45.053
65.911
21.382
1.00
11.48
6


347
CD
LYS
A
44
44.928
67.435
21.011
1.00
12.19
6


348
CE
LYS
A
44
45.254
68.171
22.334
1.00
15.83
6


349
NZ
LYS
A
44
45.125
69.681
22.068
1.00
18.92
7


350
N
MET
A
45
44.473
61.576
19.114
1.00
10.42
7


351
CA
MET
A
45
43.881
60.686
18.112
1.00
12.24
6


352
C
MET
A
45
42.952
59.664
18.768
1.00
11.36
6


353
O
MET
A
45
43.011
59.512
19.985
1.00
12.88
8


354
CB
MET
A
45
45.028
59.874
17.442
1.00
13.26
6


355
CG
AMET
A
45
46.067
60.710
16.692
0.50
14.78
6


356
SD
AMET
A
45
45.379
61.237
15.135
0.50
13.95
16


357
CE
AMET
A
45
45.728
60.040
13.903
0.50
12.41
6


355
CG
BMET
A
45
45.776
60.960
16.619
0.50
11.59
6


356
SD
BMET
A
45
46.918
60.290
15.431
0.50
16.20
16


357
CE
BMET
A
45
45.864
59.453
14.271
0.50
18.11
6


358
N
TYR
A
46
42.122
58.961
17.976
1.00
10.91
7


359
CA
TYR
A
46
41.356
57.880
18.584
1.00
13.29
6


360
C
TYR
A
46
42.263
56.691
18.938
1.00
13.10
6


361
O
TYR
A
46
43.076
56.318
18.094
1.00
12.46
8


362
CB
TYR
A
46
40.258
57.364
17.660
1.00
12.44
6


363
CG
TYR
A
46
39.031
58.210
17.416
1.00
13.02
6


364
CD1
TYR
A
46
39.075
59.210
16.436
1.00
11.30
6


365
CD2
TYR
A
46
37.846
57.978
18.105
1.00
12.45
6


366
CE1
TYR
A
46
37.940
59.997
16.146
1.00
12.75
6


367
CE2
TYR
A
46
36.683
58.746
17.838
1.00
9.77
6


368
CZ
TYR
A
46
36.789
59.707
16.881
1.00
10.60
6


369
OH
TYR
A
46
35.703
60.490
16.547
1.00
11.65
8


370
N
TRP
A
47
42.097
56.222
20.188
1.00
9.67
7


371
CA
TRP
A
47
42.866
55.089
20.664
1.00
11.50
6


372
C
TRP
A
47
42.065
53.770
20.579
1.00
12.29
6


373
O
TRP
A
47
42.633
52.676
20.711
1.00
12.20
8


374
CB
TRP
A
47
43.430
55.285
22.077
1.00
12.80
6


375
CG
TRP
A
47
44.548
56.316
22.086
1.00
10.46
6


376
CD1
TRP
A
47
45.068
57.007
21.037
1.00
11.88
6


377
CD2
TRP
A
47
45.300
56.687
23.218
1.00
10.01
6


378
NE1
TRP
A
47
46.060
57.853
21.485
1.00
11.36
7


379
CE2
TRP
A
47
46.219
57.700
22.820
1.00
12.07
6


380
CE3
TRP
A
47
45.198
56.392
24.603
1.00
12.09
6


381
CZ2
TRP
A
47
47.103
58.301
23.715
1.00
13.05
6


382
CZ3
TRP
A
47
46.072
56.974
25.484
1.00
15.07
6


383
CH2
TRP
A
47
47.002
57.939
25.033
1.00
16.33
6


384
N
GLY
A
48
40.752
53.875
20.442
1.00
10.96
7


385
CA
GLY
A
48
39.995
52.631
20.097
1.00
11.53
6


386
C
GLY
A
48
38.960
52.197
21.106
1.00
11.03
6


387
O
GLY
A
48
38.208
51.215
20.845
1.00
12.01
8


388
N
GLY
A
49
38.834
52.862
22.221
1.00
12.42
7


389
CA
GLY
A
49
37.789
52.443
23.230
1.00
12.08
6


390
C
GLY
A
49
36.451
52.679
22.614
1.00
9.81
6


391
O
GLY
A
49
36.173
53.629
21.880
1.00
10.92
8


392
N
ASP
A
50
35.433
51.851
23.065
1.00
10.42
7


393
CA
ASP
A
50
34.135
51.985
22.429
1.00
11.91
6


394
C
ASP
A
50
32.977
51.516
23.344
1.00
11.85
6


395
O
ASP
A
50
33.188
51.228
24.489
1.00
12.76
8


396
CB
ASP
A
50
34.148
51.188
21.094
1.00
10.66
6


397
CG
ASP
A
50
34.693
49.790
21.327
1.00
14.50
6


398
OD1
ASP
A
50
34.446
49.184
22.384
1.00
11.19
8


399
OD2
ASP
A
50
35.425
49.205
20.532
1.00
11.87
8


400
N
LEU
A
51
31.762
51.615
22.778
1.00
11.80
7


401
CA
LEU
A
51
30.580
51.320
23.617
1.00
11.32
6


402
C
LEU
A
51
30.568
49.843
23.973
1.00
13.43
6


403
O
LEU
A
51
30.145
49.499
25.090
1.00
11.80
8


404
CB
LEU
A
51
29.272
51.662
22.869
1.00
12.03
6


405
CG
LEU
A
51
29.178
53.205
22.638
1.00
11.71
6


406
CD1
LEU
A
51
28.036
53.389
21.666
1.00
13.88
6


407
CD2
LEU
A
51
28.915
53.930
23.954
1.00
15.76
6


408
N
GLU
A
52
30.942
48.987
23.037
1.00
12.67
7


409
CA
GLU
A
52
30.995
47.541
23.443
1.00
12.25
6


410
C
GLU
A
52
32.024
47.239
24.516
1.00
12.73
6


411
O
GLU
A
52
31.816
46.375
25.382
1.00
13.32
8


412
CB
GLU
A
52
31.182
46.786
22.122
1.00
16.82
6


413
CG
GLU
A
52
31.390
45.298
22.295
1.00
22.57
6


414
CD
GLU
A
52
30.227
44.545
22.992
1.00
12.69
6


415
OE1
GLU
A
52
29.097
45.029
23.005
1.00
17.98
8


416
OE2
GLU
A
52
30.680
43.475
23.419
1.00
16.49
8


417
N
GLY
A
53
33.114
48.012
24.628
1.00
12.03
7


418
CA
GLY
A
53
34.108
47.857
25.680
1.00
13.18
6


419
C
GLY
A
53
33.471
48.292
27.005
1.00
12.67
6


420
O
GLY
A
53
33.737
47.586
28.000
1.00
11.91
8


421
N
VAL
A
54
32.653
49.355
27.005
1.00
11.80
7


422
CA
VAL
A
54
31.996
49.680
28.280
1.00
10.05
6


423
C
VAL
A
54
31.078
48.502
28.715
1.00
12.37
6


424
O
VAL
A
54
31.055
48.111
29.879
1.00
12.15
8


425
CB
VAL
A
54
31.154
50.947
28.220
1.00
11.03
6


426
CG1
VAL
A
54
30.449
51.255
29.552
1.00
13.86
6


427
CG2
VAL
A
54
32.100
52.143
27.853
1.00
11.86
6


428
N
ARG
A
55
30.387
47.952
27.708
1.00
9.95
7


429
CA
ARG
A
55
29.382
46.875
28.101
1.00
13.29
6


430
C
ARG
A
55
30.112
45.671
28.652
1.00
12.91
6


431
O
ARG
A
55
29.684
44.943
29.596
1.00
13.96
8


432
CB
ARG
A
55
28.627
46.458
26.819
1.00
13.43
6


433
CG
ARG
A
55
27.364
45.611
27.165
1.00
13.64
6


434
CD
ARG
A
55
26.723
44.974
25.877
1.00
13.15
6


435
NE
ARG
A
55
27.745
44.040
25.358
1.00
13.30
7


436
CZ
ARG
A
55
28.117
42.905
25.921
1.00
14.35
6


437
NH1
ARG
A
55
27.475
42.404
27.011
1.00
15.82
7


438
NH2
ARG
A
55
29.125
42.171
25.446
1.00
17.12
7


439
N
GLN
A
56
31.265
45.354
28.031
1.00
11.75
7


440
CA
GLN
A
56
32.050
44.171
28.503
1.00
12.69
6


441
C
GLN
A
56
32.530
44.339
29.945
1.00
14.76
6


442
O
GLN
A
56
32.895
43.338
30.611
1.00
15.16
8


443
CB
GLN
A
56
33.249
43.948
27.536
1.00
12.12
6


444
CG
GLN
A
56
32.718
43.310
26.223
1.00
12.45
6


445
CD
GLN
A
56
33.748
43.189
25.110
1.00
18.74
6


446
OE1
GLN
A
56
33.441
43.161
23.879
1.00
21.22
8


447
NE2
GLN
A
56
34.957
43.066
25.540
1.00
13.29
7


448
N
LYS
A
57
32.816
45.574
30.355
1.00
13.93
7


449
CA
LYS
A
57
33.243
45.881
31.703
1.00
11.77
6


450
C
LYS
A
57
32.146
46.200
32.702
1.00
13.05
6


451
O
LYS
A
57
32.397
46.651
33.834
1.00
12.11
8


452
CB
LYS
A
57
34.240
47.112
31.625
1.00
12.27
6


453
CG
LYS
A
57
35.508
46.752
30.818
1.00
13.15
6


454
CD
LYS
A
57
36.167
45.442
31.318
1.00
13.38
6


455
CE
LYS
A
57
37.577
45.277
30.729
1.00
16.88
6


456
NZ
LYS
A
57
38.170
43.960
31.261
1.00
17.21
7


457
N
LEU
A
58
30.883
45.891
32.388
1.00
12.90
7


458
CA
LEU
A
58
29.789
46.048
33.338
1.00
14.31
6


459
C
LEU
A
58
29.981
45.299
34.668
1.00
12.68
6


460
O
LEU
A
58
29.737
45.865
35.732
1.00
13.94
8


461
CB
LEU
A
58
28.407
45.779
32.723
1.00
12.52
6


462
CG
LEU
A
58
27.963
46.878
31.718
1.00
12.14
6


463
CD1
LEU
A
58
26.709
46.366
30.943
1.00
14.87
6


464
CD2
LEU
A
58
27.586
48.136
32.488
1.00
15.84
6


465
N
PRO
A
59
30.555
44.107
34.670
1.00
13.13
7


466
CA
PRO
A
59
30.776
43.396
35.937
1.00
14.64
6


467
C
PRO
A
59
31.759
44.139
36.827
1.00
14.63
6


468
O
PRO
A
59
31.532
44.250
38.038
1.00
15.79
8


469
CB
PRO
A
59
31.436
42.034
35.525
1.00
15.40
6


470
CG
PRO
A
59
30.719
41.845
34.161
1.00
16.79
6


471
CD
PRO
A
59
30.807
43.247
33.514
1.00
16.71
6


472
N
TYR
A
60
32.806
44.717
36.210
1.00
12.89
7


473
CA
TYR
A
60
33.789
45.511
36.994
1.00
12.47
6


474
C
TYR
A
60
33.072
46.731
37.584
1.00
12.64
6


475
O
TYR
A
60
33.237
46.994
38.797
1.00
13.63
8


476
CB
TYR
A
60
34.918
45.920
36.026
1.00
12.16
6


477
CG
TYR
A
60
35.856
46.938
36.667
1.00
12.17
6


478
CD1
TYR
A
60
36.917
46.528
37.462
1.00
13.23
6


479
CD2
TYR
A
60
35.602
48.293
36.453
1.00
12.24
6


480
CE1
TYR
A
60
37.730
47.509
38.049
1.00
12.99
6


481
CE2
TYR
A
60
36.438
49.268
37.022
1.00
14.93
6


482
CZ
TYR
A
60
37.473
48.852
37.823
1.00
14.75
6


483
OH
TYR
A
60
38.287
49.782
38.464
1.00
13.93
8


484
N
LEU
A
61
32.298
47.410
36.735
1.00
11.74
7


485
CA
LEU
A
61
31.622
48.610
37.225
1.00
11.91
6


486
C
LEU
A
61
30.570
48.316
38.272
1.00
14.11
6


487
O
LEU
A
61
30.508
49.022
39.283
1.00
13.33
8


488
CB
LEU
A
61
30.993
49.382
36.051
1.00
12.06
6


489
CG
LEU
A
61
32.030
49.809
34.992
1.00
13.18
6


490
CD1
LEU
A
61
31.263
50.310
33.753
1.00
15.35
6


491
CD2
LEU
A
61
32.865
50.971
35.605
1.00
16.34
6


492
N
LYS
A
62
29.850
47.217
38.162
1.00
12.47
7


493
CA
LYS
A
62
28.890
46.844
39.202
1.00
13.25
6


494
C
LYS
A
62
29.614
46.558
40.535
1.00
13.60
6


495
O
LYS
A
62
29.149
47.032
41.576
1.00
15.97
8


496
CB
LYS
A
62
28.117
45.588
38.730
1.00
14.71
6


497
CG
LYS
A
62
27.011
45.263
39.764
1.00
17.27
6


498
CD
LYS
A
62
25.908
44.363
39.223
1.00
30.17
6


499
CE
LYS
A
62
24.879
44.088
40.343
1.00
25.52
6


500
NZ
LYS
A
62
23.887
45.203
40.515
1.00
24.63
7


501
N
GLN
A
63
30.722
45.781
40.455
1.00
12.05
7


502
CA
GLN
A
63
31.437
45.448
41.660
1.00
10.80
6


503
C
GLN
A
63
32.010
46.705
42.325
1.00
13.71
6


504
O
GLN
A
63
32.200
46.751
43.544
1.00
13.66
8


505
CB
AGLN
A
63
32.582
44.501
41.262
0.66
17.93
6


506
CG
AGLN
A
63
32.178
43.092
40.865
0.66
27.01
6


507
CD
AGLN
A
63
33.421
42.362
40.343
0.66
35.95
6


508
OE1
AGLN
A
63
34.283
42.022
41.149
0.66
40.99
8


509
NE2
AGLN
A
63
33.525
42.128
39.043
0.66
36.04
7


505
CB
BGLN
A
63
32.511
44.387
41.345
0.33
7.59
6


506
CG
BGLN
A
63
33.072
43.793
42.621
0.33
8.29
6


507
CD
BGLN
A
63
34.234
42.824
42.408
0.33
8.28
6


508
OE1
BGLN
A
63
34.480
42.416
41.279
0.33
14.24
8


509
NE2
BGLN
A
63
34.884
42.519
43.537
0.33
12.44
7


510
N
LEU
A
64
32.481
47.646
41.498
1.00
10.99
7


511
CA
LEU
A
64
32.993
48.909
42.087
1.00
15.73
6


512
C
LEU
A
64
31.893
49.656
42.837
1.00
14.21
6


513
O
LEU
A
64
32.253
50.516
43.659
1.00
14.81
8


514
CB
LEU
A
64
33.536
49.777
40.930
1.00
14.15
6


515
CG
LEU
A
64
34.050
51.201
41.274
1.00
13.04
6


516
CD1
LEU
A
64
35.177
51.132
42.303
1.00
12.46
6


517
CD2
LEU
A
64
34.587
51.825
39.963
1.00
12.70
6


518
N
GLY
A
65
30.605
49.492
42.566
1.00
14.23
7


519
CA
GLY
A
65
29.537
50.247
43.205
1.00
13.78
6


520
C
GLY
A
65
28.987
51.337
42.311
1.00
14.56
6


521
O
GLY
A
65
28.207
52.222
42.758
1.00
13.13
8


522
N
VAL
A
66
29.343
51.265
41.014
1.00
12.13
7


523
CA
VAL
A
66
28.773
52.267
40.114
1.00
10.77
6


524
C
VAL
A
66
27.297
52.007
39.842
1.00
13.82
6


525
O
VAL
A
66
26.933
50.836
39.617
1.00
13.38
8


526
CB
VAL
A
66
29.491
52.192
38.744
1.00
11.10
6


527
CG1
VAL
A
66
28.892
53.220
37.731
1.00
12.12
6


528
CG2
VAL
A
66
30.961
52.489
38.974
1.00
14.48
6


529
N
THR
A
67
26.431
53.016
39.992
1.00
10.70
7


530
CA
THR
A
67
25.022
52.822
39.675
1.00
12.22
6


531
C
THR
A
67
24.526
53.737
38.565
1.00
13.77
6


532
O
THR
A
67
23.404
53.538
38.103
1.00
13.29
8


533
CB
THR
A
67
24.072
52.926
40.898
1.00
14.25
6


534
OG1
THR
A
67
24.680
53.791
41.874
1.00
13.89
8


535
CG2
THR
A
67
24.085
51.519
41.584
1.00
14.96
6


536
N
THR
A
68
25.351
54.723
38.156
1.00
12.63
7


537
CA
THR
A
68
25.042
55.479
36.914
1.00
10.68
6


538
C
THR
A
68
26.379
55.684
36.193
1.00
9.37
6


539
O
THR
A
68
27.313
56.214
36.775
1.00
11.86
8


540
CB
THR
A
68
24.388
56.837
37.236
1.00
13.89
6


541
OG1
THR
A
68
23.094
56.649
37.793
1.00
13.19
8


542
CG2
THR
A
68
24.269
57.734
35.965
1.00
14.32
6


543
N
ILE
A
69
26.394
55.287
34.896
1.00
9.42
7


544
CA
ILE
A
69
27.605
55.600
34.073
1.00
8.17
6


545
C
ILE
A
69
27.249
56.897
33.377
1.00
11.16
6


546
O
ILE
A
69
26.200
57.080
32.734
1.00
12.50
8


547
CB
ILE
A
69
27.714
54.510
32.986
1.00
12.66
6


548
CG1
ILE
A
69
28.160
53.214
33.736
1.00
14.05
6


549
CG2
ILE
A
69
28.737
54.893
31.900
1.00
11.22
6


550
CD1
ILE
A
69
27.937
52.008
32.775
1.00
13.93
6


551
N
TRP
A
70
28.196
57.872
33.425
1.00
9.74
7


552
CA
TRP
A
70
28.095
59.093
32.600
1.00
10.34
6


553
C
TRP
A
70
28.991
58.790
31.403
1.00
11.63
6


554
O
TRP
A
70
30.214
58.751
31.558
1.00
11.51
8


555
CB
TRP
A
70
28.494
60.327
33.441
1.00
9.83
6


556
CG
TRP
A
70
28.954
61.558
32.738
1.00
8.81
6


557
CD1
TRP
A
70
29.050
61.770
31.360
1.00
13.03
6


558
CD2
TRP
A
70
29.591
62.698
33.356
1.00
10.57
6


559
NE1
TRP
A
70
29.645
63.016
31.118
1.00
12.41
7


560
CE2
TRP
A
70
30.017
63.558
32.338
1.00
10.48
6


561
CE3
TRP
A
70
29.830
63.007
34.699
1.00
12.18
6


562
CZ2
TRP
A
70
30.721
64.729
32.587
1.00
9.61
6


563
CZ3
TRP
A
70
30.426
64.234
34.950
1.00
11.62
6


564
CH2
TRP
A
70
30.896
65.061
33.914
1.00
13.98
6


565
N
LEU
A
71
28.373
58.542
30.225
1.00
10.83
7


566
CA
LEU
A
71
29.219
58.311
29.023
1.00
11.92
6


567
C
LEU
A
71
29.585
59.691
28.439
1.00
10.49
6


568
O
LEU
A
71
28.669
60.552
28.276
1.00
10.64
8


569
CB
LEU
A
71
28.342
57.617
27.923
1.00
11.13
6


570
CG
LEU
A
71
27.991
56.159
28.240
1.00
11.31
6


571
CD1
LEU
A
71
27.073
55.665
27.096
1.00
10.98
6


572
CD2
LEU
A
71
29.253
55.314
28.322
1.00
11.96
6


573
N
SER
A
72
30.870
59.865
28.066
1.00
10.17
7


574
CA
SER
A
72
31.250
60.995
27.218
1.00
9.81
6


575
C
SER
A
72
30.455
60.988
25.920
1.00
11.22
6


576
O
SER
A
72
29.733
60.011
25.572
1.00
10.33
8


577
CB
SER
A
72
32.773
60.898
26.944
1.00
10.62
6


578
OG
SER
A
72
33.092
59.694
26.237
1.00
11.62
8


579
N
PRO
A
73
30.447
62.034
25.128
1.00
11.10
7


580
CA
PRO
A
73
29.427
62.188
24.048
1.00
11.86
6


581
C
PRO
A
73
29.521
61.057
23.042
1.00
13.54
6


582
O
PRO
A
73
30.653
60.649
22.674
1.00
11.75
8


583
CB
PRO
A
73
29.672
63.563
23.414
1.00
10.32
6


584
CG
PRO
A
73
30.360
64.313
24.557
1.00
10.23
6


585
CD
PRO
A
73
31.228
63.286
25.358
1.00
11.09
6


586
N
VAL
A
74
28.345
60.538
22.623
1.00
11.02
7


587
CA
VAL
A
74
28.351
59.338
21.794
1.00
9.14
6


588
C
VAL
A
74
27.998
59.628
20.344
1.00
9.79
6


589
O
VAL
A
74
28.041
58.700
19.549
1.00
10.96
8


590
CB
VAL
A
74
27.260
58.313
22.311
1.00
9.29
6


591
CG1
VAL
A
74
27.541
57.935
23.780
1.00
11.66
6


592
CG2
VAL
A
74
25.882
58.894
22.161
1.00
10.26
6


593
N
LEU
A
75
27.708
60.912
19.980
1.00
10.62
7


594
CA
LEU
A
75
27.182
61.136
18.619
1.00
10.48
6


595
C
LEU
A
75
28.305
61.464
17.620
1.00
12.02
6


596
O
LEU
A
75
29.436
61.678
18.016
1.00
11.28
8


597
CB
LEU
A
75
26.111
62.279
18.660
1.00
10.81
6


598
CG
LEU
A
75
24.952
61.966
19.634
1.00
11.49
6


599
CD1
LEU
A
75
24.074
63.178
19.911
1.00
11.47
6


600
CD2
LEU
A
75
24.074
60.864
18.960
1.00
11.05
6


601
N
ASP
A
76
27.958
61.296
16.347
1.00
10.11
7


602
CA
ASP
A
76
29.020
61.292
15.299
1.00
9.23
6


603
C
ASP
A
76
29.821
62.605
15.351
1.00
9.60
6


604
O
ASP
A
76
29.263
63.683
15.155
1.00
11.11
8


605
CB
ASP
A
76
28.264
61.153
13.979
1.00
9.89
6


606
CG
ASP
A
76
29.177
61.079
12.745
1.00
12.56
6


607
OD1
ASP
A
76
30.380
60.856
12.895
1.00
12.97
8


608
OD2
ASP
A
76
28.617
61.239
11.641
1.00
11.97
8


609
N
ASN
A
77
31.131
62.435
15.524
1.00
9.80
7


610
CA
ASN
A
77
32.043
63.570
15.534
1.00
9.86
6


611
C
ASN
A
77
32.766
63.691
14.180
1.00
10.69
6


612
O
ASN
A
77
32.797
62.759
13.385
1.00
10.51
8


613
CB
ASN
A
77
33.117
63.370
16.619
1.00
10.13
6


614
CG
ASN
A
77
32.685
63.988
17.945
1.00
13.40
6


615
OD1
ASN
A
77
33.515
64.636
18.600
1.00
10.92
8


616
ND2
ASN
A
77
31.412
63.908
18.341
1.00
11.73
7


617
N
LEU
A
78
33.296
64.886
13.967
1.00
10.62
7


618
CA
LEU
A
78
34.240
65.195
12.866
1.00
11.24
6


619
C
LEU
A
78
34.929
63.977
12.309
1.00
8.87
6


620
O
LEU
A
78
35.632
63.257
13.026
1.00
12.04
8


621
CB
LEU
A
78
35.257
66.197
13.506
1.00
9.81
6


622
CG
LEU
A
78
36.289
66.679
12.399
1.00
9.30
6


623
CD1
LEU
A
78
35.622
67.597
11.418
1.00
11.34
6


624
CD2
LEU
A
78
37.382
67.439
13.176
1.00
13.04
6


625
N
ASP
A
79
34.801
63.867
10.945
1.00
11.36
7


626
CA
ASP
A
79
35.393
62.670
10.348
1.00
9.32
6


627
C
ASP
A
79
36.754
62.947
9.688
1.00
12.70
6


628
O
ASP
A
79
37.275
62.042
9.026
1.00
14.30
8


629
CB
ASP
A
79
34.468
62.189
9.168
1.00
14.19
6


630
CG
ASP
A
79
33.217
61.518
9.658
1.00
15.14
6


631
OD1
ASP
A
79
33.208
61.150
10.841
1.00
12.50
8


632
OD2
ASP
A
79
32.239
61.307
8.931
1.00
12.26
8


633
N
THR
A
80
37.307
64.115
9.950
1.00
12.57
7


634
CA
THR
A
80
38.652
64.479
9.456
1.00
14.13
6


635
C
THR
A
80
39.521
64.930
10.635
1.00
13.16
6


636
O
THR
A
80
39.072
64.981
11.769
1.00
12.58
8


637
CB
THR
A
80
38.583
65.712
8.534
1.00
14.19
6


638
OG1
THR
A
80
38.265
66.927
9.264
1.00
15.46
8


639
CG2
THR
A
80
37.593
65.645
7.372
1.00
19.78
6


640
N
LEU
A
81
40.809
65.216
10.327
1.00
13.37
7


641
CA
LEU
A
81
41.651
65.864
11.341
1.00
10.22
6


642
C
LEU
A
81
41.263
67.297
11.488
1.00
12.10
6


643
O
LEU
A
81
40.635
67.900
10.595
1.00
12.72
8


644
CB
LEU
A
81
43.143
65.818
10.830
1.00
10.42
6


645
CG
LEU
A
81
43.643
64.345
10.809
1.00
15.27
6


646
CD1
LEU
A
81
44.897
64.351
9.927
1.00
21.14
6


647
CD2
LEU
A
81
44.059
63.885
12.244
1.00
14.05
6


648
N
ALA
A
82
41.647
67.888
12.629
1.00
11.74
7


649
CA
ALA
A
82
41.548
69.320
12.798
1.00
13.34
6


650
C
ALA
A
82
42.941
69.801
13.202
1.00
12.91
6


651
O
ALA
A
82
43.208
70.247
14.316
1.00
11.11
8


652
CB
ALA
A
82
40.566
69.586
13.989
1.00
14.40
6


653
N
GLY
A
83
43.811
69.835
12.180
1.00
12.89
7


654
CA
GLY
A
83
45.245
70.145
12.484
1.00
11.52
6


655
C
GLY
A
83
45.960
68.860
12.923
1.00
12.02
6


656
O
GLY
A
83
45.405
67.737
13.060
1.00
11.47
8


657
N
THR
A
84
47.262
68.987
13.230
1.00
12.31
7


658
CA
THR
A
84
48.160
67.879
13.444
1.00
11.91
6


659
C
THR
A
84
47.716
66.883
14.496
1.00
10.74
6


660
O
THR
A
84
47.554
67.213
15.687
1.00
11.33
8


661
CB
THR
A
84
49.570
68.477
13.888
1.00
10.32
6


662
OG1
THR
A
84
49.942
69.432
12.873
1.00
12.17
8


663
CG2
THR
A
84
50.533
67.298
14.074
1.00
13.58
6


664
N
ASP
A
85
47.462
65.652
14.019
1.00
12.06
7


665
CA
ASP
A
85
47.117
64.552
14.933
1.00
10.80
6


666
C
ASP
A
85
45.981
64.902
15.894
1.00
12.31
6


667
O
ASP
A
85
45.986
64.416
17.030
1.00
13.43
8


668
CB
ASP
A
85
48.356
64.077
15.747
1.00
14.44
6


669
CG
ASP
A
85
49.500
63.600
14.831
1.00
22.31
6


670
OD1
ASP
A
85
49.284
63.065
13.744
1.00
14.91
8


671
OD2
ASP
A
85
50.645
63.782
15.275
1.00
23.25
8


672
N
ASN
A
86
45.024
65.712
15.418
1.00
10.53
7


673
CA
ASN
A
86
44.024
66.196
16.401
1.00
10.12
6


674
C
ASN
A
86
42.644
65.784
15.880
1.00
9.75
6


675
O
ASN
A
86
42.241
66.073
14.747
1.00
12.30
8


676
CB
ASN
A
86
44.190
67.732
16.468
1.00
11.52
6


677
CG
ASN
A
86
43.470
68.295
17.677
1.00
13.68
6


678
OD1
ASN
A
86
42.743
67.535
18.341
1.00
14.08
8


679
ND2
ASN
A
86
43.644
69.546
18.063
1.00
15.21
7


680
N
THR
A
87
41.877
65.099
16.705
1.00
10.11
7


681
CA
THR
A
87
40.619
64.459
16.251
1.00
10.70
6


682
C
THR
A
87
39.525
64.643
17.317
1.00
11.84
6


683
O
THR
A
87
39.764
65.021
18.471
1.00
11.11
8


684
CB
THR
A
87
40.745
62.924
16.124
1.00
12.30
6


685
OG1
THR
A
87
40.840
62.298
17.444
1.00
11.34
8


686
CG2
THR
A
87
41.961
62.467
15.375
1.00
11.19
6


687
N
GLY
A
88
38.307
64.357
16.903
1.00
11.28
7


688
CA
GLY
A
88
37.184
64.329
17.887
1.00
10.27
6


689
C
GLY
A
88
37.107
63.063
18.721
1.00
10.54
6


690
O
GLY
A
88
35.954
62.712
19.121
1.00
10.21
8


691
N
TYR
A
89
38.196
62.404
19.087
1.00
10.33
7


692
CA
TYR
A
89
38.134
61.241
19.955
1.00
10.06
6


693
C
TYR
A
89
37.314
61.476
21.204
1.00
11.70
6


694
O
TYR
A
89
36.760
60.489
21.732
1.00
11.42
8


695
CB
TYR
A
89
39.564
60.769
20.316
1.00
9.10
6


696
CG
TYR
A
89
40.152
61.653
21.412
1.00
11.07
6


697
CD1
TYR
A
89
40.732
62.857
21.106
1.00
10.61
6


698
CD2
TYR
A
89
40.058
61.256
22.750
1.00
9.12
6


699
CE1
TYR
A
89
41.243
63.688
22.115
1.00
9.21
6


700
CE2
TYR
A
89
40.505
62.054
23.777
1.00
11.90
6


701
CZ
TYR
A
89
41.098
63.267
23.443
1.00
10.92
6


702
OH
TYR
A
89
41.593
64.126
24.411
1.00
10.82
8


703
N
HIS
A
90
37.283
62.703
21.748
1.00
10.85
7


704
CA
HIS
A
90
36.623
62.983
23.011
1.00
9.54
6


705
C
HIS
A
90
35.095
63.104
22.837
1.00
7.69
6


706
O
HIS
A
90
34.392
63.040
23.856
1.00
9.02
8


707
CB
HIS
A
90
37.178
64.338
23.555
1.00
10.73
6


708
CG
HIS
A
90
37.294
65.403
22.507
1.00
11.48
6


709
ND1
HIS
A
90
36.210
66.035
21.926
1.00
9.73
7


710
CD2
HIS
A
90
38.405
65.898
21.906
1.00
8.93
6


711
CE1
HIS
A
90
36.686
66.903
21.010
1.00
10.94
6


712
NE2
HIS
A
90
37.988
66.862
20.995
1.00
10.18
7


713
N
GLY
A
91
34.616
63.356
21.629
1.00
9.66
7


714
CA
GLY
A
91
33.143
63.393
21.404
1.00
9.79
6


715
C
GLY
A
91
32.505
64.768
21.395
1.00
10.82
6


716
O
GLY
A
91
31.287
64.916
21.102
1.00
11.09
8


717
N
TYR
A
92
33.288
65.840
21.633
1.00
10.15
7


718
CA
TYR
A
92
32.653
67.152
21.753
1.00
10.44
6


719
C
TYR
A
92
32.556
67.935
20.459
1.00
8.85
6


720
O
TYR
A
92
32.132
69.141
20.520
1.00
9.64
8


721
CB
TYR
A
92
33.461
67.977
22.837
1.00
10.08
6


722
CG
TYR
A
92
33.217
67.385
24.219
1.00
10.98
6


723
CD1
TYR
A
92
32.091
67.719
24.974
1.00
10.25
6


724
CD2
TYR
A
92
34.112
66.472
24.730
1.00
10.46
6


725
CE1
TYR
A
92
31.905
67.143
26.247
1.00
10.96
6


726
CE2
TYR
A
92
33.932
65.888
25.983
1.00
14.14
6


727
CZ
TYR
A
92
32.829
66.237
26.715
1.00
11.56
6


728
OH
TYR
A
92
32.648
65.665
27.970
1.00
12.31
8


729
N
TRP
A
93
32.968
67.343
19.345
1.00
10.19
7


730
CA
TRP
A
93
32.914
68.040
18.039
1.00
11.73
6


731
C
TRP
A
93
31.949
67.307
17.103
1.00
9.84
6


732
O
TRP
A
93
32.336
66.443
16.294
1.00
10.83
8


733
CB
TRP
A
93
34.322
68.024
17.415
1.00
12.42
6


734
CG
TRP
A
93
35.359
68.775
18.253
1.00
11.75
6


735
CD1
TRP
A
93
35.181
69.659
19.258
1.00
12.58
6


736
CD2
TRP
A
93
36.786
68.657
18.020
1.00
11.96
6


737
NE1
TRP
A
93
36.448
70.120
19.694
1.00
13.60
7


738
CE2
TRP
A
93
37.397
69.501
18.932
1.00
14.78
6


739
CE3
TRP
A
93
37.559
67.884
17.130
1.00
13.74
6


740
CZ2
TRP
A
93
38.808
69.626
19.040
1.00
15.96
6


741
CZ3
TRP
A
93
38.959
68.021
17.209
1.00
10.95
6


742
CH2
TRP
A
93
39.526
68.880
18.171
1.00
9.91
6


743
N
THR
A
94
30.669
67.534
17.237
1.00
10.45
7


744
CA
THR
A
94
29.603
66.690
16.661
1.00
9.91
6


745
C
THR
A
94
29.244
67.242
15.270
1.00
11.32
6


746
O
THR
A
94
28.854
68.415
15.074
1.00
11.48
8


747
CB
THR
A
94
28.302
66.837
17.495
1.00
9.85
6


748
OG1
THR
A
94
28.643
66.563
18.891
1.00
11.49
8


749
CG2
THR
A
94
27.263
65.739
17.079
1.00
11.23
6


750
N
ARG
A
95
29.315
66.299
14.292
1.00
10.33
7


751
CA
ARG
A
95
28.819
66.623
12.945
1.00
11.51
6


752
C
ARG
A
95
27.382
66.123
12.703
1.00
13.19
6


753
O
ARG
A
95
26.834
66.523
11.700
1.00
12.00
8


754
CB
ARG
A
95
29.766
65.999
11.920
1.00
12.95
6


755
CG
ARG
A
95
29.739
64.437
11.900
1.00
9.03
6


756
CD
ARG
A
95
30.894
63.964
11.008
1.00
12.99
6


757
NE
ARG
A
95
30.917
64.346
9.584
1.00
13.10
7


758
CZ
ARG
A
95
30.216
63.680
8.633
1.00
13.74
6


759
NH1
ARG
A
95
29.307
62.746
8.918
1.00
13.30
7


760
NH2
ARG
A
95
30.477
64.026
7.380
1.00
15.12
7


761
N
ASP
A
96
26.880
65.176
13.503
1.00
11.44
7


762
CA
ASP
A
96
25.536
64.640
13.218
1.00
11.75
6


763
C
ASP
A
96
24.977
64.166
14.570
1.00
10.37
6


764
O
ASP
A
96
25.448
63.154
15.091
1.00
12.67
8


765
CB
ASP
A
96
25.622
63.467
12.217
1.00
10.69
6


766
CG
ASP
A
96
24.238
63.012
11.732
1.00
14.77
6


767
OD1
ASP
A
96
23.229
63.251
12.412
1.00
11.10
8


768
OD2
ASP
A
96
24.218
62.343
10.651
1.00
15.82
8


769
N
PHE
A
97
24.007
64.989
15.033
1.00
9.84
7


770
CA
PHE
A
97
23.482
64.615
16.377
1.00
10.91
6


771
C
PHE
A
97
22.504
63.426
16.336
1.00
13.19
6


772
O
PHE
A
97
21.945
63.125
17.373
1.00
13.15
8


773
CB
PHE
A
97
22.818
65.844
16.982
1.00
10.58
6


774
CG
PHE
A
97
23.783
66.935
17.422
1.00
14.29
6


775
CD1
PHE
A
97
24.438
67.807
16.532
1.00
13.03
6


776
CD2
PHE
A
97
23.979
67.062
18.799
1.00
13.39
6


777
CE1
PHE
A
97
25.321
68.786
17.067
1.00
11.37
6


778
CE2
PHE
A
97
24.780
68.073
19.296
1.00
9.92
6


779
CZ
PHE
A
97
25.489
68.930
18.467
1.00
9.67
6


780
N
LYS
A
98
22.220
62.889
15.152
1.00
11.59
7


781
CA
LYS
A
98
21.249
61.786
15.105
1.00
10.99
6


782
C
LYS
A
98
21.893
60.424
14.982
1.00
13.58
6


783
O
LYS
A
98
21.136
59.437
14.991
1.00
14.00
8


784
CB
LYS
A
98
20.375
61.999
13.835
1.00
10.72
6


785
CG
LYS
A
98
19.595
63.337
13.915
1.00
11.63
6


786
CD
LYS
A
98
18.627
63.408
15.091
1.00
16.21
6


787
CE
LYS
A
98
17.808
64.707
15.036
1.00
16.03
6


788
NZ
LYS
A
98
16.876
64.605
13.828
1.00
15.90
7


789
N
GLN
A
99
23.233
60.336
14.853
1.00
9.90
7


790
CA
GLN
A
99
23.900
59.079
14.613
1.00
11.53
6


791
C
GLN
A
99
25.042
58.866
15.625
1.00
12.11
6


792
O
GLN
A
99
25.610
59.842
16.118
1.00
13.41
8


793
CB
GLN
A
99
24.657
58.975
13.225
1.00
13.31
6


794
CG
GLN
A
99
23.575
58.962
12.137
1.00
20.81
6


795
CD
GLN
A
99
24.005
57.830
11.187
1.00
47.61
6


796
OE1
GLN
A
99
23.966
56.639
11.540
1.00
38.44
8


797
NE2
GLN
A
99
24.435
58.330
10.031
1.00
51.18
7


798
N
ILE
A
100
25.139
57.581
16.003
1.00
11.97
7


799
CA
ILE
A
100
26.265
57.291
16.916
1.00
9.69
6


800
C
ILE
A
100
27.586
57.395
16.160
1.00
11.29
6


801
O
ILE
A
100
27.744
57.032
14.974
1.00
13.58
8


802
CB
ILE
A
100
26.080
55.834
17.385
1.00
11.20
6


803
CG1
ILE
A
100
24.767
55.651
18.197
1.00
13.05
6


804
CG2
ILE
A
100
27.229
55.284
18.240
1.00
10.14
6


805
CD1
ILE
A
100
24.692
56.541
19.489
1.00
13.82
6


806
N
GLU
A
101
28.607
57.861
16.898
1.00
11.66
7


807
CA
GLU
A
101
29.968
57.886
16.322
1.00
11.19
6


808
C
GLU
A
101
30.443
56.478
15.956
1.00
11.88
6


809
O
GLU
A
101
30.430
55.545
16.758
1.00
12.38
8


810
CB
GLU
A
101
30.918
58.478
17.400
1.00
11.53
6


811
CG
GLU
A
101
32.427
58.256
17.126
1.00
10.12
6


812
CD
GLU
A
101
32.796
58.791
15.715
1.00
10.82
6


813
OE1
GLU
A
101
32.328
59.903
15.389
1.00
11.74
8


814
OE2
GLU
A
101
33.577
58.059
15.099
1.00
12.29
8


815
N
GLU
A
102
30.874
56.411
14.662
1.00
12.51
7


816
CA
GLU
A
102
31.192
55.081
14.116
1.00
11.29
6


817
C
GLU
A
102
32.387
54.443
14.766
1.00
12.50
6


818
O
GLU
A
102
32.460
53.176
14.813
1.00
11.57
8


819
CB
GLU
A
102
31.402
55.182
12.553
1.00
11.80
6


820
CG
GLU
A
102
32.656
55.982
12.107
1.00
12.52
6


821
CD
GLU
A
102
32.465
57.475
12.181
1.00
12.69
6


822
OE1
GLU
A
102
31.368
58.018
12.431
1.00
14.09
8


823
OE2
GLU
A
102
33.493
58.174
11.930
1.00
15.94
8


824
N
HIS
A
103
33.391
55.145
15.324
1.00
9.73
7


825
CA
HIS
A
103
34.429
54.494
16.120
1.00
9.99
6


826
C
HIS
A
103
33.862
53.874
17.376
1.00
11.88
6


827
O
HIS
A
103
34.531
52.943
17.864
1.00
12.86
8


828
CB
HIS
A
103
35.470
55.578
16.584
1.00
12.93
6


829
CG
HIS
A
103
36.364
56.049
15.481
1.00
11.28
6


830
ND1
HIS
A
103
36.015
57.085
14.639
1.00
12.54
7


831
CD2
HIS
A
103
37.595
55.655
15.123
1.00
14.43
6


832
CE1
HIS
A
103
37.021
57.288
13.749
1.00
13.58
6


833
NE2
HIS
A
103
37.965
56.434
14.054
1.00
13.95
7


834
N
PHE
A
104
32.662
54.253
17.819
1.00
9.60
7


835
CA
PHE
A
104
32.171
53.727
19.103
1.00
10.30
6


836
C
PHE
A
104
31.116
52.625
18.924
1.00
13.76
6


837
O
PHE
A
104
30.969
51.851
19.894
1.00
13.23
8


838
CB
PHE
A
104
31.583
54.855
19.953
1.00
10.00
6


839
CG
PHE
A
104
32.587
55.933
20.330
1.00
13.59
6


840
CD1
PHE
A
104
33.954
55.782
20.204
1.00
11.92
6


841
CD2
PHE
A
104
32.082
57.130
20.834
1.00
13.49
6


842
CE1
PHE
A
104
34.854
56.802
20.561
1.00
12.32
6


843
CE2
PHE
A
104
32.981
58.161
21.193
1.00
11.48
6


844
CZ
PHE
A
104
34.365
58.005
21.053
1.00
13.46
6


845
N
GLY
A
105
30.491
52.584
17.759
1.00
14.42
7


846
CA
GLY
A
105
29.462
51.533
17.546
1.00
16.52
6


847
C
GLY
A
105
28.362
52.143
16.670
1.00
17.63
6


848
O
GLY
A
105
28.624
53.104
15.927
1.00
14.43
8


849
N
ASN
A
106
27.169
51.558
16.664
1.00
14.15
7


850
CA
ASN
A
106
26.017
52.150
15.960
1.00
11.27
6


851
C
ASN
A
106
24.864
52.149
16.958
1.00
13.27
6


852
O
ASN
A
106
25.081
51.890
18.174
1.00
13.00
8


853
CB
ASN
A
106
25.756
51.332
14.677
1.00
13.55
6


854
CG
ASN
A
106
25.465
49.876
14.958
1.00
18.28
6


855
OD1
ASN
A
106
25.093
49.459
16.033
1.00
17.05
8


856
ND2
ASN
A
106
25.576
49.021
13.910
1.00
22.96
7


857
N
TRP
A
107
23.668
52.508
16.525
1.00
12.62
7


858
CA
TRP
A
107
22.554
52.559
17.465
1.00
13.67
6


859
C
TRP
A
107
22.296
51.203
18.121
1.00
14.10
6


860
O
TRP
A
107
21.827
51.121
19.274
1.00
14.66
8


861
CB
TRP
A
107
21.268
53.087
16.802
1.00
14.53
6


862
CG
TRP
A
107
21.256
54.576
16.836
1.00
16.29
6


863
CD1
TRP
A
107
21.351
55.357
15.696
1.00
17.56
6


864
CD2
TRP
A
107
21.131
55.454
17.949
1.00
15.71
6


865
NE1
TRP
A
107
21.279
56.677
16.088
1.00
16.73
7


866
CE2
TRP
A
107
21.186
56.759
17.451
1.00
14.24
6


867
CE3
TRP
A
107
20.995
55.256
19.345
1.00
13.30
6


868
CZ2
TRP
A
107
21.082
57.915
18.240
1.00
14.74
6


869
CZ3
TRP
A
107
20.919
56.410
20.131
1.00
16.80
6


870
CH2
TRP
A
107
20.927
57.717
19.596
1.00
13.00
6


871
N
THR
A
108
22.439
50.097
17.351
1.00
14.29
7


872
CA
THR
A
108
22.316
48.792
18.020
1.00
14.34
6


873
C
THR
A
108
23.305
48.617
19.154
1.00
16.18
6


874
O
THR
A
108
22.945
48.095
20.224
1.00
14.57
8


875
CB
THR
A
108
22.508
47.669
16.969
1.00
16.38
6


876
OG1
THR
A
108
21.473
47.841
16.005
1.00
18.39
8


877
CG2
THR
A
108
22.386
46.276
17.600
1.00
20.41
6


878
N
THR
A
109
24.581
49.043
18.959
1.00
12.36
7


879
CA
THR
A
109
25.556
48.897
20.029
1.00
13.35
6


880
C
THR
A
109
25.149
49.732
21.248
1.00
12.11
6


881
O
THR
A
109
25.318
49.282
22.382
1.00
12.78
8


882
CB
THR
A
109
26.960
49.404
19.545
1.00
13.85
6


883
OG1
THR
A
109
27.201
49.021
18.155
1.00
14.22
8


884
CG2
THR
A
109
28.048
48.783
20.429
1.00
15.14
6


885
N
PHE
A
110
24.673
50.945
20.982
1.00
12.96
7


886
CA
PHE
A
110
24.247
51.800
22.126
1.00
12.43
6


887
C
PHE
A
110
23.058
51.137
22.830
1.00
13.48
6


888
O
PHE
A
110
23.061
51.036
24.060
1.00
12.36
8


889
CB
PHE
A
110
23.823
53.160
21.525
1.00
14.28
6


890
CG
PHE
A
110
23.320
54.128
22.611
1.00
15.08
6


891
CD1
PHE
A
110
24.190
54.941
23.252
1.00
13.29
6


892
CD2
PHE
A
110
21.975
54.202
22.913
1.00
14.29
6


893
CE1
PHE
A
110
23.764
55.850
24.247
1.00
13.20
6


894
CE2
PHE
A
110
21.487
55.055
23.876
1.00
12.89
6


895
CZ
PHE
A
110
22.377
55.898
24.558
1.00
13.20
6


896
N
ASP
A
111
22.056
50.645
22.065
1.00
13.15
7


897
CA
ASP
A
111
20.916
49.993
22.755
1.00
12.63
6


898
C
ASP
A
111
21.337
48.770
23.517
1.00
14.08
6


899
O
ASP
A
111
20.917
48.606
24.698
1.00
14.41
8


900
CB
ASP
A
111
19.966
49.513
21.610
1.00
13.40
6


901
CG
ASP
A
111
19.224
50.603
20.937
1.00
18.96
6


902
OD1
ASP
A
111
19.343
51.768
21.305
1.00
17.72
8


903
OD2
ASP
A
111
18.498
50.291
19.945
1.00
18.78
8


904
N
THR
A
112
22.284
48.006
22.997
1.00
13.38
7


905
CA
THR
A
112
22.756
46.828
23.718
1.00
14.87
6


906
C
THR
A
112
23.450
47.184
25.017
1.00
14.48
6


907
O
THR
A
112
23.224
46.583
26.069
1.00
15.04
8


908
CB
THR
A
112
23.680
45.966
22.829
1.00
15.99
6


909
OG1
THR
A
112
22.844
45.644
21.711
1.00
16.67
8


910
CG2
THR
A
112
24.006
44.662
23.576
1.00
18.86
6


911
N
LEU
A
113
24.321
48.221
24.968
1.00
11.85
7


912
CA
LEU
A
113
24.982
48.631
26.219
1.00
12.44
6


913
C
LEU
A
113
23.992
49.138
27.242
1.00
12.26
6


914
O
LEU
A
113
24.057
48.793
28.403
1.00
12.86
8


915
CB
LEU
A
113
25.988
49.772
25.811
1.00
10.14
6


916
CG
LEU
A
113
26.404
50.629
27.037
1.00
13.26
6


917
CD1
LEU
A
113
27.184
49.772
28.040
1.00
13.59
6


918
CD2
LEU
A
113
27.295
51.825
26.664
1.00
12.75
6


919
N
VAL
A
114
23.020
49.971
26.823
1.00
11.82
7


920
CA
VAL
A
114
22.073
50.545
27.762
1.00
12.84
6


921
C
VAL
A
114
21.215
49.449
28.384
1.00
13.48
6


922
O
VAL
A
114
20.973
49.402
29.577
1.00
13.54
8


923
CB
VAL
A
114
21.264
51.680
27.090
1.00
13.71
6


924
CG1
VAL
A
114
20.144
52.091
28.032
1.00
18.18
6


925
CG2
VAL
A
114
22.209
52.885
26.815
1.00
15.06
6


926
N
ASN
A
115
20.760
48.534
27.512
1.00
13.50
7


927
CA
ASN
A
115
19.912
47.430
28.013
1.00
11.60
6


928
C
ASN
A
115
20.678
46.553
28.961
1.00
12.99
6


929
O
ASN
A
115
20.121
46.160
29.987
1.00
15.11
8


930
CB
ASN
A
115
19.372
46.637
26.820
1.00
15.99
6


931
CG
ASN
A
115
18.200
47.261
26.118
1.00
22.41
6


932
OD1
ASN
A
115
18.061
47.131
24.868
1.00
26.38
8


933
ND2
ASN
A
115
17.304
47.937
26.823
1.00
22.30
7


934
N
ASP
A
116
21.940
46.229
28.669
1.00
12.94
7


935
CA
ASP
A
116
22.731
45.386
29.561
1.00
12.20
6


936
C
ASP
A
116
23.087
46.144
30.835
1.00
12.69
6


937
O
ASP
A
116
23.070
45.584
31.933
1.00
12.40
8


938
CB
ASP
A
116
23.989
44.814
28.887
1.00
13.19
6


939
CG
ASP
A
116
23.648
43.698
27.896
1.00
19.33
6


940
OD1
ASP
A
116
22.461
43.487
27.582
1.00
23.80
8


941
OD2
ASP
A
116
24.583
42.967
27.460
1.00
22.90
8


942
N
ALA
A
117
23.342
47.453
30.753
1.00
12.25
7


943
CA
ALA
A
117
23.561
48.208
32.005
1.00
12.13
6


944
C
ALA
A
117
22.314
48.146
32.878
1.00
10.66
6


945
O
ALA
A
117
22.425
47.887
34.083
1.00
12.92
8


946
CB
ALA
A
117
23.877
49.692
31.625
1.00
13.05
6


947
N
HIS
A
118
21.149
48.403
32.291
1.00
12.02
7


948
CA
HIS
A
118
19.948
48.334
33.131
1.00
10.66
6


949
C
HIS
A
118
19.727
46.929
33.683
1.00
12.65
6


950
O
HIS
A
118
19.267
46.870
34.838
1.00
14.87
8


951
CB
HIS
A
118
18.714
48.622
32.200
1.00
10.79
6


952
CG
HIS
A
118
18.691
50.088
31.789
1.00
11.37
6


953
ND1
HIS
A
118
17.881
50.557
30.773
1.00
14.86
7


954
CD2
HIS
A
118
19.340
51.157
32.359
1.00
13.69
6


955
CE1
HIS
A
118
18.020
51.897
30.708
1.00
15.91
6


956
NE2
HIS
A
118
18.912
52.260
31.644
1.00
11.99
7


957
N
GLN
A
119
20.028
45.871
32.935
1.00
11.93
7


958
CA
GLN
A
119
19.843
44.545
33.592
1.00
12.22
6


959
C
GLN
A
119
20.770
44.412
34.781
1.00
15.02
6


960
O
GLN
A
119
20.519
43.615
35.694
1.00
15.33
8


961
CB
GLN
A
119
20.340
43.445
32.620
1.00
16.20
6


962
CG
GLN
A
119
19.327
43.169
31.521
1.00
17.09
6


963
CD
GLN
A
119
20.028
41.969
30.765
1.00
21.33
6


964
OE1
GLN
A
119
20.575
41.051
31.363
1.00
29.71
8


965
NE2
GLN
A
119
19.985
42.085
29.522
1.00
20.93
7


966
N
ASN
A
120
21.939
45.127
34.806
1.00
15.33
7


967
CA
ASN
A
120
22.853
45.072
35.932
1.00
16.39
6


968
C
ASN
A
120
22.541
46.148
36.970
1.00
14.25
6


969
O
ASN
A
120
23.358
46.337
37.876
1.00
15.65
8


970
CB
ASN
A
120
24.337
45.189
35.481
1.00
12.26
6


971
CG
ASN
A
120
24.753
43.901
34.799
1.00
20.80
6


972
OD1
ASN
A
120
24.778
43.805
33.576
1.00
23.34
8


973
ND2
ASN
A
120
25.076
42.912
35.627
1.00
18.29
7


974
N
GLY
A
121
21.398
46.801
36.951
1.00
13.35
7


975
CA
GLY
A
121
20.994
47.834
37.885
1.00
16.91
6


976
C
GLY
A
121
21.840
49.129
37.772
1.00
13.99
6


977
O
GLY
A
121
21.866
49.890
38.747
1.00
15.35
8


978
N
ILE
A
122
22.262
49.397
36.527
1.00
12.67
7


979
CA
ILE
A
122
23.128
50.569
36.322
1.00
13.01
6


980
C
ILE
A
122
22.464
51.454
35.289
1.00
13.96
6


981
O
ILE
A
122
22.075
50.945
34.227
1.00
12.86
8


982
CB
ILE
A
122
24.556
50.129
35.886
1.00
12.06
6


983
CG1
ILE
A
122
25.320
49.424
37.040
1.00
15.35
6


984
CG2
ILE
A
122
25.415
51.348
35.506
1.00
13.36
6


985
CD1
ILE
A
122
26.569
48.709
36.465
1.00
15.31
6


986
N
LYS
A
123
22.344
52.752
35.609
1.00
11.45
7


987
CA
LYS
A
123
21.767
53.718
34.652
1.00
11.74
6


988
C
LYS
A
123
22.865
54.362
33.786
1.00
11.74
6


989
O
LYS
A
123
24.052
54.129
34.057
1.00
11.17
8


990
CB
LYS
A
123
21.051
54.811
35.457
1.00
11.34
6


991
CG
LYS
A
123
19.832
54.205
36.163
1.00
12.23
6


992
CD
LYS
A
123
18.994
55.310
36.815
1.00
16.30
6


993
CE
LYS
A
123
19.601
56.014
38.025
1.00
21.38
6


994
NZ
LYS
A
123
20.133
55.054
39.000
1.00
25.83
7


995
N
VAL
A
124
22.372
54.936
32.656
1.00
9.54
7


996
CA
VAL
A
124
23.343
55.533
31.740
1.00
9.53
6


997
C
VAL
A
124
22.856
56.954
31.460
1.00
12.31
6


998
O
VAL
A
124
21.723
57.168
30.990
1.00
12.23
8


999
CB
VAL
A
124
23.372
54.748
30.408
1.00
12.71
6


1000
CG1
VAL
A
124
24.327
55.480
29.398
1.00
12.93
6


1001
CG2
VAL
A
124
23.875
53.313
30.661
1.00
11.85
6


1002
N
ILE
A
125
23.726
57.937
31.756
1.00
10.85
7


1003
CA
ILE
A
125
23.419
59.311
31.352
1.00
10.22
6


1004
C
ILE
A
125
24.430
59.676
30.232
1.00
11.59
6


1005
O
ILE
A
125
25.549
59.113
30.220
1.00
12.11
8


1006
CB
ILE
A
125
23.403
60.385
32.474
1.00
10.25
6


1007
CG1
ILE
A
125
24.811
60.531
33.089
1.00
13.12
6


1008
CG2
ILE
A
125
22.304
60.035
33.484
1.00
9.99
6


1009
CD1
ILE
A
125
24.770
61.746
34.084
1.00
17.03
6


1010
N
VAL
A
126
23.971
60.450
29.252
1.00
9.62
7


1011
CA
VAL
A
126
24.864
60.725
28.102
1.00
10.33
6


1012
C
VAL
A
126
25.247
62.207
28.081
1.00
12.61
6


1013
O
VAL
A
126
24.413
63.080
28.254
1.00
11.41
8


1014
CB
VAL
A
126
24.039
60.356
26.823
1.00
11.44
6


1015
CG1
VAL
A
126
24.892
60.704
25.575
1.00
12.92
6


1016
CG2
VAL
A
126
23.704
58.883
26.856
1.00
11.52
6


1017
N
ASP
A
127
26.535
62.445
27.771
1.00
8.46
7


1018
CA
ASP
A
127
27.011
63.870
27.661
1.00
9.67
6


1019
C
ASP
A
127
26.509
64.374
26.283
1.00
10.71
6


1020
O
ASP
A
127
26.837
63.710
25.279
1.00
11.36
8


1021
CB
ASP
A
127
28.552
63.719
27.694
1.00
9.91
6


1022
CG
ASP
A
127
29.305
64.951
28.135
1.00
11.94
6


1023
OD1
ASP
A
127
28.822
66.041
27.747
1.00
11.17
8


1024
OD2
ASP
A
127
30.335
64.880
28.865
1.00
10.63
8


1025
N
PHE
A
128
25.802
65.484
26.325
1.00
8.41
7


1026
CA
PHE
A
128
25.134
65.952
25.077
1.00
9.40
6


1027
C
PHE
A
128
25.609
67.394
24.887
1.00
9.48
6


1028
O
PHE
A
128
25.752
68.163
25.858
1.00
10.67
8


1029
CB
PHE
A
128
23.609
66.006
25.437
1.00
9.59
6


1030
CG
PHE
A
128
22.760
66.405
24.223
1.00
8.93
6


1031
CD1
PHE
A
128
22.719
65.597
23.104
1.00
12.26
6


1032
CD2
PHE
A
128
22.095
67.627
24.315
1.00
10.12
6


1033
CE1
PHE
A
128
21.907
66.014
22.027
1.00
12.04
6


1034
CE2
PHE
A
128
21.325
67.993
23.183
1.00
10.05
6


1035
CZ
PHE
A
128
21.229
67.218
22.070
1.00
10.20
6


1036
N
VAL
A
129
25.985
67.736
23.647
1.00
8.13
7


1037
CA
VAL
A
129
26.851
68.932
23.398
1.00
9.78
6


1038
C
VAL
A
129
26.171
69.845
22.412
1.00
9.18
6


1039
O
VAL
A
129
26.494
70.026
21.210
1.00
10.74
8


1040
CB
VAL
A
129
28.178
68.381
22.804
1.00
11.28
6


1041
CG1
VAL
A
129
29.206
69.539
22.719
1.00
12.02
6


1042
CG2
VAL
A
129
28.829
67.246
23.590
1.00
10.62
6


1043
N
PRO
A
130
25.165
70.638
22.855
1.00
10.64
7


1044
CA
PRO
A
130
24.341
71.474
21.986
1.00
10.69
6


1045
C
PRO
A
130
24.946
72.802
21.588
1.00
11.36
6


1046
O
PRO
A
130
24.336
73.565
20.814
1.00
11.49
8


1047
CB
PRO
A
130
22.983
71.673
22.735
1.00
10.77
6


1048
CG
PRO
A
130
23.480
71.602
24.189
1.00
12.02
6


1049
CD
PRO
A
130
24.593
70.514
24.205
1.00
11.44
6


1050
N
ASN
A
131
26.107
73.181
22.144
1.00
9.48
7


1051
CA
ASN
A
131
26.687
74.481
21.859
1.00
10.43
6


1052
C
ASN
A
131
27.244
74.637
20.438
1.00
11.66
6


1053
O
ASN
A
131
27.256
75.724
19.881
1.00
11.65
8


1054
CB
ASN
A
131
27.756
74.902
22.877
1.00
10.94
6


1055
CG
ASN
A
131
28.233
76.316
22.592
1.00
10.72
6


1056
OD1
ASN
A
131
27.396
77.205
22.783
1.00
10.02
8


1057
ND2
ASN
A
131
29.516
76.447
22.224
1.00
10.08
7


1058
N
HIS
A
132
27.676
73.513
19.855
1.00
10.71
7


1059
CA
HIS
A
132
28.476
73.726
18.632
1.00
9.32
6


1060
C
HIS
A
132
28.552
72.441
17.845
1.00
9.83
6


1061
O
HIS
A
132
28.256
71.362
18.361
1.00
12.46
8


1062
CB
HIS
A
132
29.896
74.227
19.005
1.00
11.52
6


1063
CG
HIS
A
132
30.560
73.394
20.080
1.00
10.70
6


1064
ND1
HIS
A
132
30.616
73.869
21.372
1.00
11.00
7


1065
CD2
HIS
A
132
31.084
72.152
20.032
1.00
9.99
6


1066
CE1
HIS
A
132
31.189
72.945
22.154
1.00
12.39
6


1067
NE2
HIS
A
132
31.445
71.929
21.368
1.00
10.00
7


1068
N
SER
A
133
28.999
72.608
16.584
1.00
10.23
7


1069
CA
SER
A
133
29.365
71.428
15.787
1.00
10.30
6


1070
C
SER
A
133
30.876
71.239
15.861
1.00
11.64
6


1071
O
SER
A
133
31.319
70.652
16.863
1.00
11.94
8


1072
CB
SER
A
133
28.807
71.514
14.344
1.00
10.65
6


1073
OG
SER
A
133
29.342
72.683
13.700
1.00
11.57
8


1074
N
THR
A
134
31.611
71.535
14.805
1.00
11.30
7


1075
CA
THR
A
134
33.034
71.082
14.740
1.00
10.51
6


1076
C
THR
A
134
33.959
72.251
14.424
1.00
8.56
6


1077
O
THR
A
134
33.553
73.376
14.121
1.00
10.40
8


1078
CB
THR
A
134
33.119
70.005
13.630
1.00
9.65
6


1079
OG1
THR
A
134
32.559
70.596
12.429
1.00
11.51
8


1080
CG2
THR
A
134
32.295
68.752
13.956
1.00
11.00
6


1081
N
PRO
A
135
35.256
71.959
14.489
1.00
10.51
7


1082
CA
PRO
A
135
36.320
72.955
14.289
1.00
12.33
6


1083
C
PRO
A
135
36.264
73.606
12.899
1.00
12.27
6


1084
O
PRO
A
135
36.014
72.968
11.868
1.00
13.19
8


1085
CB
PRO
A
135
37.627
72.145
14.405
1.00
11.11
6


1086
CG
PRO
A
135
37.241
71.129
15.486
1.00
11.56
6


1087
CD
PRO
A
135
35.809
70.746
15.111
1.00
11.98
6


1088
N
PHE
A
136
36.500
74.966
12.885
1.00
10.88
7


1089
CA
PHE
A
136
36.606
75.628
11.597
1.00
11.37
6


1090
C
PHE
A
136
37.536
76.830
11.718
1.00
11.99
6


1091
O
PHE
A
136
37.856
77.248
12.827
1.00
12.95
8


1092
CB
PHE
A
136
35.176
76.074
11.125
1.00
13.36
6


1093
CG
PHE
A
136
34.690
77.341
11.793
1.00
15.31
6


1094
CD1
PHE
A
136
34.201
77.311
13.100
1.00
12.18
6


1095
CD2
PHE
A
136
34.801
78.565
11.134
1.00
13.24
6


1096
CE1
PHE
A
136
33.813
78.477
13.738
1.00
13.44
6


1097
CE2
PHE
A
136
34.451
79.741
11.779
1.00
12.17
6


1098
CZ
PHE
A
136
33.903
79.708
13.087
1.00
15.41
6


1099
N
LYS
A
137
38.037
77.258
10.547
1.00
11.70
7


1100
CA
LYS
A
137
38.710
78.567
10.479
1.00
10.33
6


1101
C
LYS
A
137
37.859
79.484
9.618
1.00
13.10
6


1102
O
LYS
A
137
37.493
79.111
8.490
1.00
12.91
8


1103
CB
LYS
A
137
40.060
78.360
9.724
1.00
17.76
6


1104
CG
LYS
A
137
41.153
77.554
10.411
1.00
19.69
6


1105
CD
LYS
A
137
41.439
78.049
11.810
1.00
22.72
6


1106
CE
LYS
A
137
42.145
79.366
12.006
1.00
31.41
6


1107
NZ
LYS
A
137
43.212
79.771
11.035
1.00
25.39
7


1108
N
ALA
A
138
37.657
80.688
10.158
1.00
12.09
7


1109
CA
ALA
A
138
36.683
81.510
9.375
1.00
12.57
6


1110
C
ALA
A
138
37.267
81.873
8.017
1.00
14.60
6


1111
O
ALA
A
138
36.469
82.176
7.094
1.00
14.01
8


1112
CB
ALA
A
138
36.410
82.806
10.148
1.00
15.45
6


1113
N
ASN
A
139
38.597
81.986
7.900
1.00
13.25
7


1114
CA
ASN
A
139
39.165
82.359
6.608
1.00
14.41
6


1115
C
ASN
A
139
39.444
81.212
5.682
1.00
14.25
6


1116
O
ASN
A
139
40.047
81.349
4.562
1.00
14.82
8


1117
CB
ASN
A
139
40.443
83.188
6.852
1.00
16.78
6


1118
CG
ASN
A
139
41.666
82.292
7.083
1.00
22.27
6


1119
OD1
ASN
A
139
41.484
81.167
7.486
1.00
25.66
8


1120
ND2
ASN
A
139
42.853
82.762
6.773
1.00
21.53
7


1121
N
ASP
A
140
39.150
79.955
6.052
1.00
14.76
7


1122
CA
ASP
A
140
39.433
78.835
5.203
1.00
13.60
6


1123
C
ASP
A
140
38.470
77.674
5.337
1.00
16.09
6


1124
O
ASP
A
140
38.607
76.905
6.339
1.00
13.95
8


1125
CB
ASP
A
140
40.885
78.382
5.557
1.00
12.14
6


1126
CG
ASP
A
140
41.331
77.260
4.643
1.00
16.87
6


1127
OD1
ASP
A
140
40.616
76.705
3.810
1.00
17.82
8


1128
OD2
ASP
A
140
42.569
76.954
4.814
1.00
25.09
8


1129
N
SER
A
141
37.529
77.555
4.414
1.00
15.21
7


1130
CA
SER
A
141
36.508
76.520
4.501
1.00
16.63
6


1131
C
SER
A
141
37.048
75.092
4.285
1.00
17.44
6


1132
O
SER
A
141
36.349
74.129
4.607
1.00
18.28
8


1133
CB
SER
A
141
35.372
76.746
3.493
1.00
19.52
6


1134
OG
SER
A
141
35.867
76.579
2.144
1.00
16.38
8


1135
N
THR
A
142
38.302
74.958
3.839
1.00
14.08
7


1136
CA
THR
A
142
38.889
73.615
3.649
1.00
15.63
6


1137
C
THR
A
142
39.445
73.036
4.933
1.00
16.91
6


1138
O
THR
A
142
39.798
71.840
4.961
1.00
15.67
8


1139
CB
THR
A
142
40.105
73.658
2.622
1.00
16.69
6


1140
OG1
THR
A
142
41.261
74.288
3.211
1.00
18.35
8


1141
CG2
THR
A
142
39.653
74.352
1.368
1.00
25.03
6


1142
N
PHE
A
143
39.533
73.874
6.007
1.00
15.48
7


1143
CA
PHE
A
143
40.027
73.314
7.285
1.00
12.99
6


1144
C
PHE
A
143
38.953
72.384
7.908
1.00
14.57
6


1145
O
PHE
A
143
37.807
72.837
8.026
1.00
12.49
8


1146
CB
PHE
A
143
40.412
74.481
8.238
1.00
14.72
6


1147
CG
PHE
A
143
40.905
73.939
9.546
1.00
13.33
6


1148
CD1
PHE
A
143
42.192
73.454
9.669
1.00
14.66
6


1149
CD2
PHE
A
143
40.054
73.908
10.679
1.00
10.60
6


1150
CE1
PHE
A
143
42.677
72.946
10.878
1.00
14.87
6


1151
CE2
PHE
A
143
40.556
73.381
11.849
1.00
12.09
6


1152
CZ
PHE
A
143
41.842
72.912
11.975
1.00
16.30
6


1153
N
ALA
A
144
39.342
71.174
8.264
1.00
14.83
7


1154
CA
ALA
A
144
38.380
70.250
8.884
1.00
14.49
6


1155
C
ALA
A
144
37.165
70.136
7.976
1.00
14.94
6


1156
O
ALA
A
144
37.369
69.878
6.784
1.00
13.97
8


1157
CB
ALA
A
144
37.990
70.683
10.323
1.00
12.28
6


1158
N
GLU
A
145
35.942
70.135
8.506
1.00
11.43
7


1159
CA
GLU
A
145
34.744
70.061
7.645
1.00
10.19
6


1160
C
GLU
A
145
34.063
71.386
7.520
1.00
10.66
6


1161
O
GLU
A
145
32.824
71.513
7.266
1.00
11.84
8


1162
CB
GLU
A
145
33.771
68.943
8.180
1.00
11.91
6


1163
CG
GLU
A
145
34.408
67.577
8.042
1.00
11.68
6


1164
CD
GLU
A
145
33.591
66.467
8.697
1.00
15.77
6


1165
OE1
GLU
A
145
32.530
66.660
9.208
1.00
20.95
8


1166
OE2
GLU
A
145
34.122
65.351
8.743
1.00
21.22
8


1167
N
GLY
A
146
34.677
72.533
7.898
1.00
12.55
7


1168
CA
GLY
A
146
34.021
73.826
7.783
1.00
12.03
6


1169
C
GLY
A
146
32.799
73.976
8.739
1.00
15.18
6


1170
O
GLY
A
146
32.025
74.880
8.511
1.00
13.95
8


1171
N
GLY
A
147
32.774
73.157
9.790
1.00
12.57
7


1172
CA
GLY
A
147
31.639
73.265
10.703
1.00
12.28
6


1173
C
GLY
A
147
30.439
72.415
10.267
1.00
14.09
6


1174
O
GLY
A
147
29.372
72.644
10.903
1.00
11.87
8


1175
N
ALA
A
148
30.552
71.583
9.258
1.00
11.40
7


1176
CA
ALA
A
148
29.343
70.942
8.707
1.00
13.48
6


1177
C
ALA
A
148
28.495
70.132
9.729
1.00
11.58
6


1178
O
ALA
A
148
29.025
69.390
10.557
1.00
12.14
8


1179
CB
ALA
A
148
29.861
69.927
7.660
1.00
14.52
6


1180
N
LEU
A
149
27.188
70.305
9.543
1.00
12.19
7


1181
CA
LEU
A
149
26.192
69.594
10.365
1.00
10.39
6


1182
C
LEU
A
149
25.298
68.798
9.407
1.00
10.91
6


1183
O
LEU
A
149
24.907
69.311
8.313
1.00
14.52
8


1184
CB
LEU
A
149
25.345
70.684
11.028
1.00
10.56
6


1185
CG
LEU
A
149
24.344
70.222
12.098
1.00
14.34
6


1186
CD1
LEU
A
149
25.067
69.618
13.294
1.00
16.21
6


1187
CD2
LEU
A
149
23.436
71.409
12.447
1.00
15.60
6


1188
N
TYR
A
150
25.047
67.560
9.836
1.00
12.69
7


1189
CA
TYR
A
150
24.178
66.675
9.057
1.00
11.91
6


1190
C
TYR
A
150
23.007
66.234
9.957
1.00
13.54
6


1191
O
TYR
A
150
23.116
66.203
11.188
1.00
12.53
8


1192
CB
TYR
A
150
24.945
65.392
8.671
1.00
12.62
6


1193
CG
TYR
A
150
26.104
65.699
7.694
1.00
10.80
6


1194
CD1
TYR
A
150
27.275
66.240
8.185
1.00
13.28
6


1195
CD2
TYR
A
150
25.983
65.330
6.359
1.00
14.10
6


1196
CE1
TYR
A
150
28.295
66.545
7.273
1.00
14.81
6


1197
CE2
TYR
A
150
27.004
65.609
5.479
1.00
17.28
6


1198
CZ
TYR
A
150
28.139
66.206
5.959
1.00
17.89
6


1199
OH
TYR
A
150
29.227
66.444
5.082
1.00
18.31
8


1200
N
ASN
A
151
21.932
65.787
9.288
1.00
11.59
7


1201
CA
ASN
A
151
20.774
65.261
10.048
1.00
13.13
6


1202
C
ASN
A
151
20.582
63.801
9.659
1.00
14.46
6


1203
O
ASN
A
151
20.020
63.527
8.595
1.00
15.41
8


1204
CB
ASN
A
151
19.542
66.068
9.633
1.00
12.78
6


1205
CG
ASN
A
151
18.280
65.607
10.386
1.00
15.85
6


1206
OD1
ASN
A
151
18.376
65.084
11.460
1.00
14.91
8


1207
ND2
ASN
A
151
17.115
65.851
9.790
1.00
23.13
7


1208
N
ASN
A
152
21.153
62.881
10.455
1.00
11.88
7


1209
CA
ASN
A
152
21.160
61.460
10.056
1.00
12.91
6


1210
C
ASN
A
152
21.628
61.265
8.619
1.00
17.10
6


1211
O
ASN
A
152
21.059
60.495
7.804
1.00
18.15
8


1212
CB
ASN
A
152
19.763
60.894
10.305
1.00
15.18
6


1213
CG
ASN
A
152
19.772
59.363
10.289
1.00
28.25
6


1214
OD1
ASN
A
152
20.803
58.741
10.579
1.00
25.62
8


1215
ND2
ASN
A
152
18.647
58.722
9.925
1.00
26.09
7


1216
N
GLY
A
153
22.797
61.857
8.344
1.00
11.86
7


1217
CA
GLY
A
153
23.494
61.698
7.061
1.00
15.63
6


1218
C
GLY
A
153
23.096
62.727
6.007
1.00
17.70
6


1219
O
GLY
A
153
23.819
62.836
4.994
1.00
16.41
8


1220
N
THR
A
154
21.975
63.414
6.209
1.00
13.77
7


1221
CA
THR
A
154
21.535
64.406
5.220
1.00
14.28
6


1222
C
THR
A
154
22.181
65.781
5.538
1.00
14.24
6


1223
O
THR
A
154
22.048
66.264
6.650
1.00
15.31
8


1224
CB
THR
A
154
20.008
64.592
5.212
1.00
21.10
6


1225
OG1
THR
A
154
19.488
63.334
4.709
1.00
20.66
8


1226
CG2
THR
A
154
19.569
65.711
4.260
1.00
21.99
6


1227
N
TYR
A
155
22.977
66.280
4.566
1.00
14.57
7


1228
CA
TYR
A
155
23.613
67.573
4.928
1.00
15.65
6


1229
C
TYR
A
155
22.652
68.698
5.184
1.00
17.55
6


1230
O
TYR
A
155
21.639
68.912
4.487
1.00
16.44
8


1231
CB
TYR
A
155
24.440
67.984
3.678
1.00
16.08
6


1232
CG
TYR
A
155
25.238
69.243
3.820
1.00
16.71
6


1233
CD1
TYR
A
155
26.324
69.277
4.693
1.00
16.20
6


1234
CD2
TYR
A
155
24.989
70.381
3.075
1.00
16.54
6


1235
CE1
TYR
A
155
27.139
70.407
4.789
1.00
16.44
6


1236
CE2
TYR
A
155
25.773
71.530
3.162
1.00
14.17
6


1237
CZ
TYR
A
155
26.843
71.515
4.015
1.00
16.83
6


1238
OH
TYR
A
155
27.673
72.601
4.142
1.00
15.80
8


1239
N
MET
A
156
22.895
69.456
6.272
1.00
12.36
7


1240
CA
MET
A
156
22.120
70.658
6.595
1.00
12.72
6


1241
C
MET
A
156
22.877
71.939
6.202
1.00
14.70
6


1242
O
MET
A
156
22.290
72.876
5.628
1.00
14.86
8


1243
CB
MET
A
156
21.886
70.683
8.141
1.00
14.72
6


1244
CG
MET
A
156
21.045
69.510
8.543
1.00
13.16
6


1245
SD
MET
A
156
20.812
69.391
10.354
1.00
16.44
16


1246
CE
MET
A
156
19.828
70.788
10.735
1.00
16.14
6


1247
N
GLY
A
157
24.138
72.003
6.634
1.00
15.28
7


1248
CA
GLY
A
157
24.888
73.257
6.260
1.00
12.22
6


1249
C
GLY
A
157
26.169
73.337
7.061
1.00
15.29
6


1250
O
GLY
A
157
26.402
72.513
7.965
1.00
13.96
8


1251
N
ASN
A
158
26.981
74.369
6.736
1.00
13.19
7


1252
CA
ASN
A
158
28.205
74.586
7.485
1.00
12.06
6


1253
C
ASN
A
158
28.353
76.085
7.759
1.00
8.80
6


1254
O
ASN
A
158
27.377
76.850
7.583
1.00
11.73
8


1255
CB
ASN
A
158
29.438
73.957
6.787
1.00
12.79
6


1256
CG
ASN
A
158
29.783
74.647
5.457
1.00
16.08
6


1257
OD1
ASN
A
158
29.311
75.727
5.160
1.00
12.69
8


1258
ND2
ASN
A
158
30.650
74.060
4.603
1.00
20.88
7


1259
N
TYR
A
159
29.559
76.484
8.260
1.00
10.67
7


1260
CA
TYR
A
159
29.714
77.924
8.640
1.00
11.67
6


1261
C
TYR
A
159
29.665
78.827
7.432
1.00
12.87
6


1262
O
TYR
A
159
29.444
80.029
7.605
1.00
12.70
8


1263
CB
TYR
A
159
31.055
78.072
9.434
1.00
11.86
6


1264
CG
TYR
A
159
31.171
79.475
10.063
1.00
11.61
6


1265
CD1
TYR
A
159
30.414
79.868
11.149
1.00
14.86
6


1266
CD2
TYR
A
159
31.962
80.402
9.380
1.00
13.87
6


1267
CE1
TYR
A
159
30.576
81.181
11.600
1.00
15.19
6


1268
CE2
TYR
A
159
32.069
81.716
9.811
1.00
19.88
6


1269
CZ
TYR
A
159
31.387
82.088
10.926
1.00
16.15
6


1270
OH
TYR
A
159
31.377
83.383
11.432
1.00
16.24
8


1271
N
PHE
A
160
29.904
78.307
6.253
1.00
13.52
7


1272
CA
PHE
A
160
30.073
79.126
5.029
1.00
12.84
6


1273
C
PHE
A
160
28.855
79.182
4.153
1.00
12.34
6


1274
O
PHE
A
160
28.803
80.101
3.300
1.00
14.63
8


1275
CB
PHE
A
160
31.228
78.421
4.234
1.00
12.99
6


1276
CG
PHE
A
160
32.504
78.508
5.080
1.00
14.21
6


1277
CD1
PHE
A
160
33.310
79.662
4.935
1.00
12.64
6


1278
CD2
PHE
A
160
32.804
77.488
5.965
1.00
12.84
6


1279
CE1
PHE
A
160
34.466
79.772
5.737
1.00
14.91
6


1280
CE2
PHE
A
160
33.940
77.621
6.761
1.00
14.27
6


1281
CZ
PHE
A
160
34.769
78.740
6.653
1.00
13.93
6


1282
N
ASP
A
161
27.917
78.220
4.232
1.00
14.16
7


1283
CA
ASP
A
161
26.731
78.329
3.371
1.00
14.46
6


1284
C
ASP
A
161
25.486
78.622
4.217
1.00
14.25
6


1285
O
ASP
A
161
24.375
78.215
3.808
1.00
15.23
8


1286
CB
ASP
A
161
26.557
77.031
2.565
1.00
12.66
6


1287
CG
ASP
A
161
26.500
75.766
3.373
1.00
15.72
6


1288
OD1
ASP
A
161
26.191
75.896
4.579
1.00
13.04
8


1289
OD2
ASP
A
161
26.767
74.716
2.766
1.00
20.26
8


1290
N
ASP
A
162
25.656
79.460
5.227
1.00
13.84
7


1291
CA
ASP
A
162
24.557
79.667
6.196
1.00
14.60
6


1292
C
ASP
A
162
23.787
80.939
5.979
1.00
16.54
6


1293
O
ASP
A
162
22.840
81.252
6.726
1.00
18.25
8


1294
CB
ASP
A
162
25.253
79.785
7.584
1.00
12.11
6


1295
CG
ASP
A
162
24.264
79.524
8.717
1.00
13.12
6


1296
OD1
ASP
A
162
23.408
78.624
8.551
1.00
12.76
8


1297
OD2
ASP
A
162
24.417
80.201
9.775
1.00
12.76
8


1298
N
ALA
A
163
24.109
81.725
4.949
1.00
16.09
7


1299
CA
ALA
A
163
23.428
83.019
4.792
1.00
16.11
6


1300
C
ALA
A
163
21.914
82.901
4.848
1.00
17.25
6


1301
O
ALA
A
163
21.341
83.825
5.467
1.00
24.30
8


1302
CB
ALA
A
163
23.828
83.609
3.414
1.00
19.57
6


1303
N
THR
A
164
21.317
81.987
4.145
1.00
19.25
7


1304
CA
THR
A
164
19.845
81.973
4.121
1.00
24.11
6


1305
C
THR
A
164
19.237
81.014
5.149
1.00
25.86
6


1306
O
THR
A
164
18.055
80.605
5.002
1.00
25.38
8


1307
CB
THR
A
164
19.384
81.502
2.723
1.00
21.33
6


1308
OG1
THR
A
164
19.834
80.146
2.496
1.00
29.22
8


1309
CG2
THR
A
164
20.062
82.359
1.658
1.00
32.67
6


1310
N
LYS
A
165
20.086
80.431
6.008
1.00
19.16
7


1311
CA
LYS
A
165
19.577
79.430
6.929
1.00
16.62
6


1312
C
LYS
A
165
19.714
79.888
8.391
1.00
18.03
6


1313
O
LYS
A
165
18.735
79.767
9.173
1.00
17.25
8


1314
CB
LYS
A
165
20.423
78.140
6.826
1.00
13.80
6


1315
CG
LYS
A
165
20.215
77.497
5.423
1.00
21.49
6


1316
CD
LYS
A
165
20.913
76.186
5.334
1.00
30.47
6


1317
CE
LYS
A
165
22.394
76.297
5.245
1.00
26.09
6


1318
NZ
LYS
A
165
23.067
75.308
4.349
1.00
18.44
7


1319
N
GLY
A
166
20.839
80.499
8.700
1.00
14.27
7


1320
CA
GLY
A
166
21.048
81.024
10.082
1.00
14.43
6


1321
C
GLY
A
166
21.103
79.863
11.109
1.00
14.80
6


1322
O
GLY
A
166
20.730
80.096
12.287
1.00
14.92
8


1323
N
TYR
A
167
21.732
78.765
10.734
1.00
12.78
7


1324
CA
TYR
A
167
21.882
77.692
11.732
1.00
12.54
6


1325
C
TYR
A
167
22.991
78.009
12.739
1.00
12.62
6


1326
O
TYR
A
167
23.085
77.349
13.776
1.00
11.78
8


1327
CB
TYR
A
167
22.226
76.374
11.022
1.00
10.92
6


1328
CG
TYR
A
167
21.127
75.836
10.103
1.00
14.63
6


1329
CD1
TYR
A
167
19.810
76.232
10.291
1.00
13.59
6


1330
CD2
TYR
A
167
21.490
74.921
9.121
1.00
15.06
6


1331
CE1
TYR
A
167
18.836
75.722
9.421
1.00
13.53
6


1332
CE2
TYR
A
167
20.503
74.385
8.254
1.00
12.93
6


1333
CZ
TYR
A
167
19.211
74.809
8.469
1.00
15.10
6


1334
OH
TYR
A
167
18.235
74.289
7.594
1.00
18.52
8


1335
N
PHE
A
168
23.963
78.870
12.342
1.00
11.36
7


1336
CA
PHE
A
168
25.072
79.208
13.244
1.00
11.20
6


1337
C
PHE
A
168
25.097
80.677
13.551
1.00
12.02
6


1338
O
PHE
A
168
24.515
81.539
12.854
1.00
11.21
8


1339
CB
PHE
A
168
26.432
78.934
12.493
1.00
13.41
6


1340
CG
PHE
A
168
26.552
77.459
12.174
1.00
11.52
6


1341
CD1
PHE
A
168
27.044
76.583
13.130
1.00
10.63
6


1342
CD2
PHE
A
168
26.171
77.007
10.899
1.00
13.81
6


1343
CE1
PHE
A
168
27.122
75.214
12.765
1.00
12.04
6


1344
CE2
PHE
A
168
26.250
75.639
10.574
1.00
12.05
6


1345
CZ
PHE
A
168
26.752
74.751
11.518
1.00
12.13
6


1346
N
HIS
A
169
25.665
81.067
14.709
1.00
11.43
7


1347
CA
HIS
A
169
25.979
82.473
14.979
1.00
12.52
6


1348
C
HIS
A
169
27.266
82.836
14.195
1.00
11.69
6


1349
O
HIS
A
169
28.109
82.035
13.921
1.00
11.66
8


1350
CB
HIS
A
169
26.361
82.658
16.482
1.00
11.57
6


1351
CG
HIS
A
169
25.157
82.347
17.376
1.00
11.97
6


1352
ND1
HIS
A
169
25.403
81.657
18.588
1.00
11.36
7


1353
CD2
HIS
A
169
23.838
82.604
17.274
1.00
11.55
6


1354
CE1
HIS
A
169
24.195
81.518
19.195
1.00
12.02
6


1355
NE2
HIS
A
169
23.233
82.111
18.427
1.00
10.80
7


1356
N
HIS
A
170
27.295
84.147
13.797
1.00
11.77
7


1357
CA
HIS
A
170
28.474
84.629
13.015
1.00
12.20
6


1358
C
HIS
A
170
29.029
85.872
13.672
1.00
14.93
6


1359
O
HIS
A
170
29.174
86.974
13.053
1.00
16.92
8


1360
CB
HIS
A
170
28.083
84.949
11.533
1.00
13.28
6


1361
CG
HIS
A
170
27.535
83.698
10.888
1.00
12.02
6


1362
ND1
HIS
A
170
28.327
82.925
10.069
1.00
15.51
7


1363
CD2
HIS
A
170
26.306
83.088
10.915
1.00
13.12
6


1364
CE1
HIS
A
170
27.639
81.863
9.689
1.00
16.69
6


1365
NE2
HIS
A
170
26.409
81.953
10.156
1.00
13.32
7


1366
N
ASN
A
171
29.387
85.778
14.962
1.00
12.58
7


1367
CA
ASN
A
171
29.735
86.967
15.733
1.00
12.76
6


1368
C
ASN
A
171
31.201
87.040
16.147
1.00
13.34
6


1369
O
ASN
A
171
31.554
87.947
16.949
1.00
17.31
8


1370
CB
ASN
A
171
28.916
86.961
17.054
1.00
13.40
6


1371
CG
ASN
A
171
27.430
86.948
16.719
1.00
17.12
6


1372
OD1
ASN
A
171
26.595
86.168
17.252
1.00
16.54
8


1373
ND2
ASN
A
171
27.046
87.866
15.861
1.00
12.82
7


1374
N
GLY
A
172
32.013
86.197
15.601
1.00
13.14
7


1375
CA
GLY
A
172
33.444
86.166
15.964
1.00
15.42
6


1376
C
GLY
A
172
33.728
85.275
17.210
1.00
16.69
6


1377
O
GLY
A
172
32.817
84.706
17.722
1.00
14.98
8


1378
N
ASP
A
173
34.993
85.180
17.526
1.00
14.76
7


1379
CA
ASP
A
173
35.473
84.346
18.622
1.00
12.93
6


1380
C
ASP
A
173
35.292
84.996
19.976
1.00
12.76
6


1381
O
ASP
A
173
35.410
86.248
20.131
1.00
11.79
8


1382
CB
ASP
A
173
36.980
84.152
18.369
1.00
14.28
6


1383
CG
ASP
A
173
37.273
83.139
17.268
1.00
24.98
6


1384
OD1
ASP
A
173
36.398
82.387
16.822
1.00
17.11
8


1385
OD2
ASP
A
173
38.451
83.124
16.815
1.00
23.71
8


1386
N
ILE
A
174
35.073
84.127
20.969
1.00
12.58
7


1387
CA
ILE
A
174
35.136
84.670
22.362
1.00
11.65
6


1388
C
ILE
A
174
36.500
85.307
22.646
1.00
14.87
6


1389
O
ILE
A
174
37.508
84.670
22.337
1.00
15.09
8


1390
CB
ILE
A
174
34.896
83.495
23.357
1.00
13.27
6


1391
CG1
ILE
A
174
33.431
83.005
23.177
1.00
10.95
6


1392
CG2
ILE
A
174
35.145
84.016
24.806
1.00
12.74
6


1393
CD1
ILE
A
174
33.220
81.690
24.000
1.00
11.77
6


1394
N
SER
A
175
36.441
86.493
23.260
1.00
14.22
7


1395
CA
SER
A
175
37.710
87.093
23.770
1.00
16.89
6


1396
C
SER
A
175
37.712
87.131
25.291
1.00
18.02
6


1397
O
SER
A
175
38.617
86.587
25.938
1.00
19.20
8


1398
CB
SER
A
175
37.868
88.470
23.138
1.00
17.86
6


1399
OG
SER
A
175
39.049
89.044
23.724
1.00
24.28
8


1400
N
ASN
A
176
36.650
87.662
25.854
1.00
14.39
7


1401
CA
ASN
A
176
36.515
87.678
27.336
1.00
13.41
6


1402
C
ASN
A
176
35.511
86.561
27.678
1.00
12.76
6


1403
O
ASN
A
176
34.286
86.760
27.482
1.00
13.43
8


1404
CB
ASN
A
176
35.898
89.032
27.724
1.00
15.61
6


1405
CG
ASN
A
176
35.749
89.123
29.243
1.00
17.91
6


1406
OD1
ASN
A
176
35.963
88.166
29.982
1.00
15.18
8


1407
ND2
ASN
A
176
35.402
90.347
29.694
1.00
22.13
7


1408
N
TRP
A
177
36.085
85.465
28.237
1.00
14.29
7


1409
CA
TRP
A
177
35.172
84.361
28.558
1.00
13.39
6


1410
C
TRP
A
177
34.248
84.677
29.724
1.00
15.05
6


1411
O
TRP
A
177
33.279
83.898
29.909
1.00
14.25
8


1412
CB
TRP
A
177
36.054
83.145
28.953
1.00
16.12
6


1413
CG
TRP
A
177
36.712
82.559
27.721
1.00
14.43
6


1414
CD1
TRP
A
177
37.745
83.101
26.998
1.00
16.58
6


1415
CD2
TRP
A
177
36.399
81.291
27.142
1.00
13.92
6


1416
NE1
TRP
A
177
38.070
82.235
25.940
1.00
18.57
7


1417
CE2
TRP
A
177
37.234
81.131
26.014
1.00
18.68
6


1418
CE3
TRP
A
177
35.437
80.298
27.392
1.00
17.34
6


1419
CZ2
TRP
A
177
37.148
80.031
25.169
1.00
14.28
6


1420
CZ3
TRP
A
177
35.379
79.182
26.574
1.00
17.20
6


1421
CH2
TRP
A
177
36.253
79.045
25.441
1.00
18.00
6


1422
N
ASP
A
178
34.477
85.795
30.469
1.00
12.43
7


1423
CA
ASP
A
178
33.507
86.126
31.517
1.00
11.08
6


1424
C
ASP
A
178
32.454
87.115
31.053
1.00
12.88
6


1425
O
ASP
A
178
31.586
87.420
31.881
1.00
15.73
8


1426
CB
ASP
A
178
34.243
86.717
32.739
1.00
17.78
6


1427
CG
ASP
A
178
35.201
85.739
33.362
1.00
24.33
6


1428
OD1
ASP
A
178
34.916
84.535
33.440
1.00
18.07
8


1429
OD2
ASP
A
178
36.317
86.155
33.777
1.00
24.77
8


1430
N
ASP
A
179
32.527
87.608
29.810
1.00
11.79
7


1431
CA
ASP
A
179
31.448
88.502
29.357
1.00
11.42
6


1432
C
ASP
A
179
30.292
87.603
28.903
1.00
12.33
6


1433
O
ASP
A
179
30.537
86.725
28.067
1.00
12.08
8


1434
CB
ASP
A
179
31.997
89.341
28.184
1.00
15.43
6


1435
CG
ASP
A
179
30.831
90.225
27.763
1.00
18.80
6


1436
OD1
ASP
A
179
30.462
91.232
28.431
1.00
20.56
8


1437
OD2
ASP
A
179
30.213
89.893
26.753
1.00
13.51
8


1438
N
ARG
A
180
29.115
87.768
29.477
1.00
13.02
7


1439
CA
ARG
A
180
28.057
86.771
29.205
1.00
11.54
6


1440
C
ARG
A
180
27.585
86.833
27.757
1.00
10.36
6


1441
O
ARG
A
180
27.261
85.746
27.225
1.00
11.27
8


1442
CB
ARG
A
180
26.893
87.051
30.172
1.00
13.31
6


1443
CG
ARG
A
180
27.286
86.796
31.654
1.00
12.49
6


1444
CD
ARG
A
180
27.797
85.340
31.899
1.00
10.75
6


1445
NE
ARG
A
180
26.694
84.389
31.571
1.00
11.38
7


1446
CZ
ARG
A
180
26.896
83.305
30.812
1.00
11.55
6


1447
NH1
ARG
A
180
28.090
82.893
30.359
1.00
11.21
7


1448
NH2
ARG
A
180
25.769
82.597
30.589
1.00
13.64
7


1449
N
TYR
A
181
27.508
87.990
27.113
1.00
10.51
7


1450
CA
TYR
A
181
27.104
87.980
25.688
1.00
10.68
6


1451
C
TYR
A
181
28.195
87.277
24.870
1.00
11.14
6


1452
O
TYR
A
181
27.826
86.403
24.044
1.00
10.66
8


1453
CB
TYR
A
181
26.915
89.446
25.196
1.00
12.30
6


1454
CG
TYR
A
181
26.645
89.417
23.698
1.00
12.16
6


1455
CD1
TYR
A
181
25.446
89.009
23.179
1.00
13.07
6


1456
CD2
TYR
A
181
27.712
89.736
22.837
1.00
15.09
6


1457
CE1
TYR
A
181
25.242
88.936
21.808
1.00
18.03
6


1458
CE2
TYR
A
181
27.510
89.688
21.457
1.00
16.90
6


1459
CZ
TYR
A
181
26.275
89.265
20.988
1.00
19.76
6


1460
OH
TYR
A
181
26.097
89.156
19.614
1.00
17.30
8


1461
N
GLU
A
182
29.473
87.528
25.083
1.00
13.50
7


1462
CA
GLU
A
182
30.468
86.836
24.265
1.00
12.35
6


1463
C
GLU
A
182
30.442
85.311
24.504
1.00
10.45
6


1464
O
GLU
A
182
30.482
84.533
23.582
1.00
11.45
8


1465
CB
GLU
A
182
31.939
87.266
24.571
1.00
10.48
6


1466
CG
GLU
A
182
32.131
88.769
24.214
1.00
12.66
6


1467
CD
GLU
A
182
33.640
89.046
24.246
1.00
19.30
6


1468
OE1
GLU
A
182
34.487
88.229
23.958
1.00
15.48
8


1469
OE2
GLU
A
182
34.009
90.199
24.690
1.00
30.95
8


1470
N
ALA
A
183
30.314
84.945
25.796
1.00
10.17
7


1471
CA
ALA
A
183
30.436
83.521
26.110
1.00
11.02
6


1472
C
ALA
A
183
29.302
82.709
25.471
1.00
11.67
6


1473
O
ALA
A
183
29.555
81.542
25.197
1.00
10.91
8


1474
CB
ALA
A
183
30.290
83.352
27.664
1.00
11.34
6


1475
N
GLN
A
184
28.196
83.381
25.172
1.00
10.70
7


1476
CA
GLN
A
184
27.046
82.624
24.601
1.00
8.62
6


1477
C
GLN
A
184
26.939
82.844
23.102
1.00
10.69
6


1478
O
GLN
A
184
26.509
81.913
22.388
1.00
10.72
8


1479
CB
GLN
A
184
25.772
83.078
25.330
1.00
12.35
6


1480
CG
GLN
A
184
25.730
82.584
26.785
1.00
9.80
6


1481
CD
GLN
A
184
24.603
83.315
27.538
1.00
12.56
6


1482
OE1
GLN
A
184
24.739
84.527
27.890
1.00
15.21
8


1483
NE2
GLN
A
184
23.536
82.580
27.775
1.00
8.78
7


1484
N
TRP
A
185
27.186
84.018
22.585
1.00
11.90
7


1485
CA
TRP
A
185
26.968
84.285
21.148
1.00
9.74
6


1486
C
TRP
A
185
28.252
84.298
20.318
1.00
10.30
6


1487
O
TRP
A
185
28.093
84.277
19.065
1.00
11.67
8


1488
CB
TRP
A
185
26.201
85.647
20.965
1.00
12.61
6


1489
CG
TRP
A
185
24.696
85.390
21.039
1.00
10.95
6


1490
CD1
TRP
A
185
23.863
85.166
19.989
1.00
12.59
6


1491
CD2
TRP
A
185
23.898
85.345
22.226
1.00
12.07
6


1492
NE1
TRP
A
185
22.561
84.887
20.428
1.00
14.15
7


1493
CE2
TRP
A
185
22.600
85.003
21.805
1.00
13.63
6


1494
CE3
TRP
A
185
24.154
85.530
23.587
1.00
13.34
6


1495
CZ2
TRP
A
185
21.534
84.846
22.703
1.00
14.01
6


1496
CZ3
TRP
A
185
23.083
85.361
24.494
1.00
14.75
6


1497
CH2
TRP
A
185
21.812
85.004
24.035
1.00
13.91
6


1498
N
LYS
A
186
29.413
84.254
20.924
1.00
11.31
7


1499
CA
LYS
A
186
30.655
84.170
20.127
1.00
12.29
6


1500
C
LYS
A
186
31.228
82.764
20.238
1.00
14.72
6


1501
O
LYS
A
186
30.718
81.896
20.981
1.00
12.47
8


1502
CB
LYS
A
186
31.682
85.224
20.582
1.00
11.09
6


1503
CG
LYS
A
186
31.145
86.646
20.243
1.00
14.74
6


1504
CD
LYS
A
186
32.295
87.655
20.601
1.00
14.53
6


1505
CE
LYS
A
186
31.688
89.051
20.286
1.00
20.29
6


1506
NZ
LYS
A
186
32.744
89.943
19.726
1.00
28.67
7


1507
N
ASN
A
187
32.217
82.446
19.379
1.00
13.16
7


1508
CA
ASN
A
187
32.653
81.074
19.195
1.00
13.22
6


1509
C
ASN
A
187
33.587
80.604
20.314
1.00
15.43
6


1510
O
ASN
A
187
34.587
81.250
20.646
1.00
12.76
8


1511
CB
ASN
A
187
33.386
80.850
17.862
1.00
12.72
6


1512
CG
ASN
A
187
32.673
81.537
16.697
1.00
18.84
6


1513
OD1
ASN
A
187
31.447
81.456
16.631
1.00
15.46
8


1514
ND2
ASN
A
187
33.426
82.219
15.839
1.00
16.94
7


1515
N
PHE
A
188
33.369
79.356
20.719
1.00
11.91
7


1516
CA
PHE
A
188
34.321
78.658
21.604
1.00
10.93
6


1517
C
PHE
A
188
35.600
78.457
20.806
1.00
13.95
6


1518
O
PHE
A
188
35.534
78.128
19.632
1.00
13.55
8


1519
CB
PHE
A
188
33.682
77.259
21.822
1.00
11.05
6


1520
CG
PHE
A
188
34.177
76.552
23.071
1.00
11.08
6


1521
CD1
PHE
A
188
35.431
75.953
23.060
1.00
14.39
6


1522
CD2
PHE
A
188
33.364
76.492
24.194
1.00
14.52
6


1523
CE1
PHE
A
188
35.865
75.309
24.204
1.00
15.63
6


1524
CE2
PHE
A
188
33.821
75.818
25.327
1.00
14.28
6


1525
CZ
PHE
A
188
35.081
75.233
25.350
1.00
12.75
6


1526
N
THR
A
189
36.737
78.710
21.504
1.00
11.89
7


1527
CA
THR
A
189
38.000
78.578
20.769
1.00
11.77
6


1528
C
THR
A
189
38.851
77.524
21.457
1.00
13.65
6


1529
O
THR
A
189
38.630
77.149
22.589
1.00
14.67
8


1530
CB
THR
A
189
38.826
79.904
20.788
1.00
12.56
6


1531
OG1
THR
A
189
39.066
80.215
22.180
1.00
15.52
8


1532
CG2
THR
A
189
38.012
81.045
20.136
1.00
13.79
6


1533
N
ASP
A
190
39.773
76.961
20.639
1.00
11.10
7


1534
CA
ASP
A
190
40.736
75.985
21.186
1.00
11.48
6


1535
C
ASP
A
190
42.109
76.575
20.929
1.00
11.63
6


1536
O
ASP
A
190
42.403
77.103
19.861
1.00
13.03
8


1537
CB
ASP
A
190
40.530
74.703
20.365
1.00
11.07
6


1538
CG
ASP
A
190
41.445
73.591
20.781
1.00
12.55
6


1539
OD1
ASP
A
190
42.691
73.716
20.943
1.00
14.12
8


1540
OD2
ASP
A
190
40.937
72.422
20.956
1.00
14.32
8


1541
N
PRO
A
191
43.013
76.539
21.885
1.00
12.39
7


1542
CA
PRO
A
191
44.344
77.094
21.756
1.00
16.15
6


1543
C
PRO
A
191
45.205
76.488
20.648
1.00
17.03
6


1544
O
PRO
A
191
46.194
77.139
20.258
1.00
17.33
8


1545
CB
PRO
A
191
45.077
76.806
23.067
1.00
15.82
6


1546
CG
PRO
A
191
43.951
76.489
24.024
1.00
19.99
6


1547
CD
PRO
A
191
42.769
75.960
23.220
1.00
15.14
6


1548
N
ALA
A
192
44.778
75.374
20.102
1.00
12.41
7


1549
CA
ALA
A
192
45.446
74.851
18.871
1.00
16.29
6


1550
C
ALA
A
192
45.279
75.807
17.697
1.00
21.11
6


1551
O
ALA
A
192
46.014
75.779
16.675
1.00
19.85
8


1552
CB
ALA
A
192
44.978
73.466
18.579
1.00
20.48
6


1553
N
GLY
A
193
44.317
76.695
17.671
1.00
16.93
7


1554
CA
GLY
A
193
44.199
77.733
16.641
1.00
17.03
6


1555
C
GLY
A
193
42.919
77.582
15.819
1.00
17.85
6


1556
O
GLY
A
193
42.991
77.960
14.651
1.00
17.03
8


1557
N
PHE
A
194
41.888
76.955
16.373
1.00
13.47
7


1558
CA
PHE
A
194
40.612
76.976
15.567
1.00
11.84
6


1559
C
PHE
A
194
39.441
77.265
16.536
1.00
11.03
6


1560
O
PHE
A
194
39.621
77.423
17.750
1.00
11.69
8


1561
CB
PHE
A
194
40.411
75.629
14.855
1.00
10.98
6


1562
CG
PHE
A
194
40.568
74.412
15.767
1.00
11.46
6


1563
CD1
PHE
A
194
39.545
74.063
16.649
1.00
11.56
6


1564
CD2
PHE
A
194
41.707
73.656
15.747
1.00
15.24
6


1565
CE1
PHE
A
194
39.688
72.942
17.460
1.00
11.26
6


1566
CE2
PHE
A
194
41.871
72.533
16.574
1.00
12.49
6


1567
CZ
PHE
A
194
40.860
72.181
17.450
1.00
12.03
6


1568
N
SER
A
195
38.283
77.497
15.895
1.00
10.73
7


1569
CA
SER
A
195
37.097
77.782
16.704
1.00
11.52
6


1570
C
SER
A
195
36.081
76.649
16.423
1.00
11.92
6


1571
O
SER
A
195
36.284
75.902
15.519
1.00
10.36
8


1572
CB
SER
A
195
36.416
79.059
16.186
1.00
16.30
6


1573
OG
SER
A
195
37.442
80.119
16.216
1.00
22.79
8


1574
N
LEU
A
196
35.060
76.594
17.262
1.00
12.22
7


1575
CA
LEU
A
196
34.007
75.622
17.060
1.00
12.16
6


1576
C
LEU
A
196
32.756
76.384
16.584
1.00
7.60
6


1577
O
LEU
A
196
32.364
77.416
17.112
1.00
13.16
8


1578
CB
LEU
A
196
33.660
74.883
18.410
1.00
10.95
6


1579
CG
LEU
A
196
34.880
74.298
19.107
1.00
10.75
6


1580
CD1
LEU
A
196
34.439
73.454
20.334
1.00
11.59
6


1581
CD2
LEU
A
196
35.719
73.384
18.134
1.00
12.48
6


1582
N
ALA
A
197
32.139
75.877
15.481
1.00
9.97
7


1583
CA
ALA
A
197
30.995
76.637
14.905
1.00
10.64
6


1584
C
ALA
A
197
29.788
76.658
15.830
1.00
14.16
6


1585
O
ALA
A
197
29.362
75.622
16.314
1.00
11.22
8


1586
CB
ALA
A
197
30.629
75.928
13.565
1.00
10.95
6


1587
N
ASP
A
198
29.429
77.869
16.236
1.00
10.28
7


1588
CA
ASP
A
198
28.459
78.009
17.350
1.00
10.50
6


1589
C
ASP
A
198
27.030
77.880
16.795
1.00
11.99
6


1590
O
ASP
A
198
26.607
78.731
15.993
1.00
13.33
8


1591
CB
ASP
A
198
28.744
79.433
17.900
1.00
12.29
6


1592
CG
ASP
A
198
28.236
79.529
19.353
1.00
10.72
6


1593
OD1
ASP
A
198
28.683
78.683
20.172
1.00
11.33
8


1594
OD2
ASP
A
198
27.401
80.452
19.671
1.00
10.45
8


1595
N
LEU
A
199
26.310
76.847
17.247
1.00
10.29
7


1596
CA
LEU
A
199
24.927
76.690
16.763
1.00
8.80
6


1597
C
LEU
A
199
24.086
77.821
17.321
1.00
9.88
6


1598
O
LEU
A
199
24.246
78.320
18.449
1.00
11.27
8


1599
CB
LEU
A
199
24.452
75.296
17.279
1.00
9.52
6


1600
CG
LEU
A
199
25.178
74.135
16.526
1.00
10.88
6


1601
CD1
LEU
A
199
24.799
72.879
17.321
1.00
12.59
6


1602
CD2
LEU
A
199
24.658
74.045
15.071
1.00
14.19
6


1603
N
SER
A
200
23.024
78.144
16.505
1.00
11.57
7


1604
CA
SER
A
200
22.055
79.160
16.950
1.00
10.26
6


1605
C
SER
A
200
20.810
78.424
17.499
1.00
11.50
6


1606
O
SER
A
200
19.994
77.917
16.741
1.00
11.79
8


1607
CB
SER
A
200
21.636
80.012
15.731
1.00
14.77
6


1608
OG
SER
A
200
20.723
81.011
16.249
1.00
13.69
8


1609
N
GLN
A
201
20.786
78.294
18.837
1.00
10.61
7


1610
CA
GLN
A
201
19.599
77.668
19.473
1.00
11.55
6


1611
C
GLN
A
201
18.421
78.648
19.371
1.00
11.79
6


1612
O
GLN
A
201
17.305
78.161
19.700
1.00
12.43
8


1613
CB
GLN
A
201
19.852
77.359
20.969
1.00
11.94
6


1614
CG
GLN
A
201
21.042
76.370
21.151
1.00
10.05
6


1615
CD
GLN
A
201
22.393
77.086
21.126
1.00
10.84
6


1616
OE1
GLN
A
201
22.499
78.298
21.208
1.00
11.60
8


1617
NE2
GLN
A
201
23.465
76.231
21.079
1.00
9.83
7


1618
N
GLU
A
202
18.590
79.860
18.862
1.00
10.41
7


1619
CA
GLU
A
202
17.434
80.763
18.667
1.00
11.55
6


1620
C
GLU
A
202
16.849
80.531
17.277
1.00
14.51
6


1621
O
GLU
A
202
15.856
81.166
16.903
1.00
16.57
8


1622
CB
GLU
A
202
17.877
82.226
18.875
1.00
10.69
6


1623
CG
GLU
A
202
18.522
82.442
20.252
1.00
9.01
6


1624
CD
GLU
A
202
20.002
82.069
20.330
1.00
12.78
6


1625
OE1
GLU
A
202
20.680
82.031
19.299
1.00
16.62
8


1626
OE2
GLU
A
202
20.457
81.782
21.434
1.00
12.31
8


1627
N
ASN
A
203
17.507
79.704
16.435
1.00
11.04
7


1628
CA
ASN
A
203
16.939
79.318
15.142
1.00
10.64
6


1629
C
ASN
A
203
16.020
78.098
15.372
1.00
13.48
6


1630
O
ASN
A
203
16.441
77.148
16.008
1.00
12.81
8


1631
CB
ASN
A
203
18.105
78.892
14.217
1.00
11.71
6


1632
CG
ASN
A
203
17.604
78.307
12.930
1.00
15.36
6


1633
OD1
ASN
A
203
17.271
77.124
12.838
1.00
15.37
8


1634
ND2
ASN
A
203
17.611
79.108
11.829
1.00
15.33
7


1635
N
GLY
A
204
14.797
78.219
14.831
1.00
13.94
7


1636
CA
GLY
A
204
13.813
77.115
15.175
1.00
14.96
6


1637
C
GLY
A
204
14.202
75.766
14.593
1.00
12.98
6


1638
O
GLY
A
204
13.891
74.775
15.243
1.00
14.33
8


1639
N
THR
A
205
14.802
75.705
13.401
1.00
11.88
7


1640
CA
THR
A
205
15.279
74.405
12.894
1.00
12.45
6


1641
C
THR
A
205
16.275
73.780
13.856
1.00
11.35
6


1642
O
THR
A
205
16.161
72.621
14.172
1.00
11.84
8


1643
CB
THR
A
205
15.866
74.603
11.497
1.00
14.40
6


1644
OG1
THR
A
205
14.760
75.060
10.662
1.00
18.35
8


1645
CG2
THR
A
205
16.344
73.256
10.930
1.00
16.31
6


1646
N
ILE
A
206
17.295
74.586
14.188
1.00
10.89
7


1647
CA
ILE
A
206
18.330
73.996
15.081
1.00
10.54
6


1648
C
ILE
A
206
17.736
73.689
16.457
1.00
9.48
6


1649
O
ILE
A
206
18.081
72.638
17.051
1.00
10.61
8


1650
CB
ILE
A
206
19.481
75.017
15.212
1.00
9.16
6


1651
CG1
ILE
A
206
20.193
75.155
13.844
1.00
12.29
6


1652
CG2
ILE
A
206
20.550
74.624
16.273
1.00
11.91
6


1653
CD1
ILE
A
206
20.691
73.847
13.218
1.00
12.69
6


1654
N
ALA
A
207
16.912
74.562
17.021
1.00
10.30
7


1655
CA
ALA
A
207
16.350
74.185
18.339
1.00
12.45
6


1656
C
ALA
A
207
15.583
72.871
18.311
1.00
12.96
6


1657
O
ALA
A
207
15.714
72.053
19.217
1.00
13.37
8


1658
CB
ALA
A
207
15.511
75.359
18.883
1.00
13.30
6


1659
N
GLN
A
208
14.749
72.676
17.282
1.00
10.55
7


1660
CA
GLN
A
208
13.968
71.431
17.236
1.00
11.60
6


1661
C
GLN
A
208
14.842
70.256
16.877
1.00
14.22
6


1662
O
GLN
A
208
14.627
69.200
17.426
1.00
11.79
8


1663
CB
GLN
A
208
12.869
71.573
16.136
1.00
13.62
6


1664
CG
GLN
A
208
11.847
70.429
16.197
1.00
14.37
6


1665
CD
GLN
A
208
11.089
70.392
17.513
1.00
15.09
6


1666
OE1
GLN
A
208
10.565
71.371
17.957
1.00
14.67
8


1667
NE2
GLN
A
208
11.168
69.230
18.180
1.00
14.23
7


1668
N
TYR
A
209
15.876
70.454
16.062
1.00
11.41
7


1669
CA
TYR
A
209
16.807
69.372
15.724
1.00
10.71
6


1670
C
TYR
A
209
17.570
68.930
16.979
1.00
10.31
6


1671
O
TYR
A
209
17.634
67.727
17.231
1.00
11.12
8


1672
CB
TYR
A
209
17.840
69.989
14.743
1.00
11.54
6


1673
CG
TYR
A
209
19.072
69.148
14.457
1.00
12.56
6


1674
CD1
TYR
A
209
19.031
68.083
13.584
1.00
11.38
6


1675
CD2
TYR
A
209
20.269
69.485
15.060
1.00
12.87
6


1676
CE1
TYR
A
209
20.184
67.341
13.286
1.00
16.27
6


1677
CE2
TYR
A
209
21.432
68.739
14.794
1.00
13.55
6


1678
CZ
TYR
A
209
21.368
67.676
13.915
1.00
13.50
6


1679
OH
TYR
A
209
22.527
66.968
13.654
1.00
14.21
8


1680
N
LEU
A
210
17.985
69.883
17.821
1.00
10.88
7


1681
CA
LEU
A
210
18.731
69.461
19.027
1.00
10.76
6


1682
C
LEU
A
210
17.776
68.829
20.049
1.00
11.52
6


1683
O
LEU
A
210
18.178
67.863
20.687
1.00
11.55
8


1684
CB
LEU
A
210
19.388
70.688
19.713
1.00
10.40
6


1685
CG
LEU
A
210
20.603
71.237
18.893
1.00
10.20
6


1686
CD1
LEU
A
210
20.918
72.628
19.480
1.00
12.47
6


1687
CD2
LEU
A
210
21.766
70.260
18.920
1.00
13.21
6


1688
N
THR
A
211
16.539
69.327
20.069
1.00
9.66
7


1689
CA
THR
A
211
15.520
68.689
20.933
1.00
11.98
6


1690
C
THR
A
211
15.294
67.272
20.496
1.00
11.93
6


1691
O
THR
A
211
15.311
66.354
21.335
1.00
11.42
8


1692
CB
THR
A
211
14.193
69.502
20.889
1.00
12.29
6


1693
OG1
THR
A
211
14.488
70.842
21.373
1.00
11.73
8


1694
CG2
THR
A
211
13.137
68.832
21.808
1.00
10.37
6


1695
N
ASP
A
212
15.071
67.084
19.170
1.00
12.47
7


1696
CA
ASP
A
212
14.813
65.738
18.671
1.00
10.73
6


1697
C
ASP
A
212
15.998
64.812
18.997
1.00
12.42
6


1698
O
ASP
A
212
15.748
63.598
19.194
1.00
12.22
8


1699
CB
ASP
A
212
14.605
65.829
17.159
1.00
12.33
6


1700
CG
ASP
A
212
13.253
66.477
16.797
1.00
15.18
6


1701
OD1
ASP
A
212
12.379
66.643
17.667
1.00
13.61
8


1702
OD2
ASP
A
212
13.100
66.828
15.585
1.00
14.64
8


1703
N
ALA
A
213
17.230
65.326
18.830
1.00
10.02
7


1704
CA
ALA
A
213
18.376
64.422
19.084
1.00
10.72
6


1705
C
ALA
A
213
18.422
64.023
20.552
1.00
10.18
6


1706
O
ALA
A
213
18.819
62.882
20.861
1.00
11.96
8


1707
CB
ALA
A
213
19.679
65.163
18.735
1.00
10.83
6


1708
N
ALA
A
214
18.155
64.970
21.448
1.00
12.55
7


1709
CA
ALA
A
214
18.185
64.599
22.892
1.00
10.81
6


1710
C
ALA
A
214
17.073
63.631
23.235
1.00
11.35
6


1711
O
ALA
A
214
17.246
62.667
23.953
1.00
12.75
8


1712
CB
ALA
A
214
18.038
65.876
23.757
1.00
10.21
6


1713
N
VAL
A
215
15.885
63.854
22.677
1.00
10.82
7


1714
CA
VAL
A
215
14.724
62.923
22.875
1.00
11.60
6


1715
C
VAL
A
215
15.035
61.577
22.302
1.00
13.68
6


1716
O
VAL
A
215
14.673
60.552
22.903
1.00
15.03
8


1717
CB
VAL
A
215
13.462
63.523
22.283
1.00
14.89
6


1718
CG1
VAL
A
215
12.285
62.514
22.234
1.00
16.68
6


1719
CG2
VAL
A
215
12.982
64.740
23.099
1.00
15.78
6


1720
N
GLN
A
216
15.759
61.496
21.193
1.00
12.25
7


1721
CA
GLN
A
216
16.153
60.192
20.632
1.00
13.52
6


1722
C
GLN
A
216
17.023
59.404
21.577
1.00
13.62
6


1723
O
GLN
A
216
16.864
58.192
21.706
1.00
12.75
8


1724
CB
GLN
A
216
16.814
60.382
19.232
1.00
12.82
6


1725
CG
GLN
A
216
17.225
59.032
18.639
1.00
14.36
6


1726
CD
GLN
A
216
17.856
59.162
17.261
1.00
18.32
6


1727
OE1
GLN
A
216
18.762
59.976
16.980
1.00
21.98
8


1728
NE2
GLN
A
216
17.392
58.348
16.335
1.00
19.07
7


1729
N
LEU
A
217
17.996
60.043
22.269
1.00
11.16
7


1730
CA
LEU
A
217
18.781
59.317
23.261
1.00
11.02
6


1731
C
LEU
A
217
17.885
58.756
24.396
1.00
10.47
6


1732
O
LEU
A
217
18.106
57.631
24.754
1.00
13.19
8


1733
CB
LEU
A
217
19.847
60.252
23.876
1.00
12.00
6


1734
CG
LEU
A
217
20.974
60.577
22.859
1.00
10.07
6


1735
CD1
LEU
A
217
21.770
61.789
23.418
1.00
10.56
6


1736
CD2
LEU
A
217
21.953
59.383
22.787
1.00
12.18
6


1737
N
VAL
A
218
16.940
59.584
24.844
1.00
10.50
7


1738
CA
VAL
A
218
16.027
59.030
25.884
1.00
14.12
6


1739
C
VAL
A
218
15.114
57.918
25.304
1.00
12.90
6


1740
O
VAL
A
218
14.914
56.898
25.978
1.00
14.29
8


1741
CB
VAL
A
218
15.121
60.168
26.376
1.00
11.91
6


1742
CG1
VAL
A
218
14.131
59.671
27.428
1.00
14.89
6


1743
CG2
VAL
A
218
16.045
61.169
27.107
1.00
14.59
6


1744
N
ALA
A
219
14.717
57.992
24.051
1.00
14.93
7


1745
CA
ALA
A
219
13.868
56.915
23.478
1.00
14.21
6


1746
C
ALA
A
219
14.647
55.619
23.377
1.00
16.64
6


1747
O
ALA
A
219
14.072
54.517
23.401
1.00
14.94
8


1748
CB
ALA
A
219
13.379
57.270
22.059
1.00
15.54
6


1749
N
HIS
A
220
15.959
55.702
23.258
1.00
12.54
7


1750
CA
HIS
A
220
16.853
54.570
23.215
1.00
14.41
6


1751
C
HIS
A
220
17.305
54.124
24.611
1.00
12.25
6


1752
O
HIS
A
220
18.194
53.243
24.711
1.00
13.99
8


1753
CB
HIS
A
220
18.055
54.802
22.293
1.00
11.69
6


1754
CG
HIS
A
220
17.630
54.760
20.840
1.00
14.69
6


1755
ND1
HIS
A
220
17.984
53.694
20.064
1.00
14.71
7


1756
CD2
HIS
A
220
16.928
55.624
20.077
1.00
16.42
6


1757
CE1
HIS
A
220
17.518
53.916
18.823
1.00
16.42
6


1758
NE2
HIS
A
220
16.855
55.077
18.794
1.00
17.85
7


1759
N
GLY
A
221
16.735
54.666
25.655
1.00
11.47
7


1760
CA
GLY
A
221
16.964
54.129
26.999
1.00
11.21
6


1761
C
GLY
A
221
17.655
55.060
27.965
1.00
13.22
6


1762
O
GLY
A
221
17.875
54.635
29.095
1.00
13.24
8


1763
N
ALA
A
222
18.297
56.111
27.426
1.00
12.29
7


1764
CA
ALA
A
222
19.139
56.912
28.356
1.00
14.03
6


1765
C
ALA
A
222
18.325
57.381
29.553
1.00
13.32
6


1766
O
ALA
A
222
17.138
57.794
29.459
1.00
10.61
8


1767
CB
ALA
A
222
19.700
58.136
27.618
1.00
12.95
6


1768
N
ASP
A
223
19.009
57.376
30.709
1.00
11.67
7


1769
CA
ASP
A
223
18.391
57.768
31.951
1.00
10.83
6


1770
C
ASP
A
223
18.621
59.249
32.306
1.00
12.58
6


1771
O
ASP
A
223
18.116
59.667
33.356
1.00
11.47
8


1772
CB
ASP
A
223
18.997
56.964
33.123
1.00
9.67
6


1773
CG
ASP
A
223
18.744
55.469
32.925
1.00
12.72
6


1774
OD1
ASP
A
223
17.554
55.095
33.224
1.00
15.35
8


1775
OD2
ASP
A
223
19.610
54.686
32.482
1.00
10.77
8


1776
N
GLY
A
224
19.186
59.972
31.348
1.00
11.00
7


1777
CA
GLY
A
224
19.393
61.413
31.651
1.00
11.62
6


1778
C
GLY
A
224
20.641
61.861
30.809
1.00
9.62
6


1779
O
GLY
A
224
21.069
61.107
29.928
1.00
9.69
8


1780
N
LEU
A
225
20.869
63.123
30.983
1.00
10.32
7


1781
CA
LEU
A
225
21.962
63.749
30.177
1.00
9.63
6


1782
C
LEU
A
225
22.828
64.566
31.128
1.00
10.99
6


1783
O
LEU
A
225
22.356
65.110
32.097
1.00
10.86
8


1784
CB
LEU
A
225
21.389
64.780
29.172
1.00
9.89
6


1785
CG
LEU
A
225
20.424
64.212
28.122
1.00
10.00
6


1786
CD1
LEU
A
225
19.806
65.361
27.279
1.00
12.69
6


1787
CD2
LEU
A
225
21.003
63.092
27.243
1.00
13.97
6


1788
N
ARG
A
226
24.135
64.671
30.790
1.00
10.52
7


1789
CA
ARG
A
226
24.993
65.777
31.295
1.00
9.01
6


1790
C
ARG
A
226
25.093
66.744
30.110
1.00
10.97
6


1791
O
ARG
A
226
25.628
66.348
29.083
1.00
10.94
8


1792
CB
ARG
A
226
26.337
65.159
31.691
1.00
9.10
6


1793
CG
ARG
A
226
27.381
66.213
32.158
1.00
8.52
6


1794
CD
ARG
A
226
28.248
66.648
30.956
1.00
9.82
6


1795
NE
ARG
A
226
29.438
67.400
31.425
1.00
9.22
7


1796
CZ
ARG
A
226
30.251
68.074
30.592
1.00
9.27
6


1797
NH1
ARG
A
226
29.978
68.191
29.289
1.00
9.46
7


1798
NH2
ARG
A
226
31.311
68.687
31.114
1.00
10.94
7


1799
N
ILE
A
227
24.590
67.940
30.262
1.00
10.46
7


1800
CA
ILE
A
227
24.553
68.901
29.124
1.00
7.87
6


1801
C
ILE
A
227
25.807
69.751
29.238
1.00
8.86
6


1802
O
ILE
A
227
26.042
70.450
30.199
1.00
11.29
8


1803
CB
ILE
A
227
23.295
69.783
29.269
1.00
9.62
6


1804
CG1
ILE
A
227
22.096
68.814
29.378
1.00
10.28
6


1805
CG2
ILE
A
227
23.196
70.601
27.964
1.00
11.21
6


1806
CD1
ILE
A
227
20.743
69.547
29.412
1.00
15.31
6


1807
N
ASP
A
228
26.544
69.672
28.125
1.00
9.30
7


1808
CA
ASP
A
228
27.846
70.399
28.079
1.00
9.30
6


1809
C
ASP
A
228
27.672
71.915
27.904
1.00
9.50
6


1810
O
ASP
A
228
26.757
72.338
27.189
1.00
9.88
8


1811
CB
ASP
A
228
28.521
69.865
26.769
1.00
9.23
6


1812
CG
ASP
A
228
29.904
70.442
26.587
1.00
10.24
6


1813
OD1
ASP
A
228
30.725
70.228
27.505
1.00
10.28
8


1814
OD2
ASP
A
228
30.208
71.128
25.574
1.00
9.89
8


1815
N
ALA
A
229
28.575
72.633
28.582
1.00
8.93
7


1816
CA
ALA
A
229
28.745
74.068
28.257
1.00
9.72
6


1817
C
ALA
A
229
27.455
74.868
28.324
1.00
10.58
6


1818
O
ALA
A
229
27.123
75.695
27.464
1.00
10.73
8


1819
CB
ALA
A
229
29.355
74.180
26.841
1.00
9.90
6


1820
N
VAL
A
230
26.729
74.708
29.487
1.00
9.05
7


1821
CA
VAL
A
230
25.421
75.392
29.548
1.00
9.09
6


1822
C
VAL
A
230
25.547
76.905
29.753
1.00
10.83
6


1823
O
VAL
A
230
24.587
77.636
29.573
1.00
12.48
8


1824
CB
VAL
A
230
24.469
74.836
30.634
1.00
10.80
6


1825
CG1
VAL
A
230
24.119
73.389
30.262
1.00
9.84
6


1826
CG2
VAL
A
230
25.084
74.934
32.047
1.00
11.19
6


1827
N
LYS
A
231
26.753
77.312
30.189
1.00
9.10
7


1828
CA
LYS
A
231
26.988
78.763
30.234
1.00
7.91
6


1829
C
LYS
A
231
27.304
79.391
28.883
1.00
11.01
6


1830
O
LYS
A
231
27.398
80.604
28.809
1.00
13.02
8


1831
CB
LYS
A
231
28.173
79.043
31.209
1.00
10.48
6


1832
CG
LYS
A
231
29.567
78.801
30.602
1.00
10.63
6


1833
CD
LYS
A
231
30.599
78.817
31.758
1.00
13.70
6


1834
CE
LYS
A
231
30.937
80.205
32.236
1.00
13.75
6


1835
NZ
LYS
A
231
32.215
80.157
33.104
1.00
11.49
7


1836
N
HIS
A
232
27.364
78.589
27.814
1.00
9.37
7


1837
CA
HIS
A
232
27.744
79.081
26.480
1.00
12.72
6


1838
C
HIS
A
232
26.576
79.044
25.537
1.00
12.48
6


1839
O
HIS
A
232
26.698
79.505
24.388
1.00
9.62
8


1840
CB
HIS
A
232
28.849
78.129
25.915
1.00
9.94
6


1841
CG
HIS
A
232
30.145
78.345
26.709
1.00
9.35
6


1842
ND1
HIS
A
232
30.780
79.598
26.674
1.00
11.03
7


1843
CD2
HIS
A
232
30.803
77.530
27.554
1.00
11.85
6


1844
CE1
HIS
A
232
31.838
79.483
27.513
1.00
12.22
6


1845
NE2
HIS
A
232
31.882
78.243
28.049
1.00
11.68
7


1846
N
PHE
A
233
25.342
78.757
25.941
1.00
9.67
7


1847
CA
PHE
A
233
24.165
78.957
25.062
1.00
10.57
6


1848
C
PHE
A
233
23.015
79.437
25.991
1.00
9.21
6


1849
O
PHE
A
233
23.073
79.254
27.225
1.00
11.50
8


1850
CB
PHE
A
233
23.792
77.705
24.296
1.00
9.50
6


1851
CG
PHE
A
233
23.382
76.523
25.145
1.00
10.66
6


1852
CD1
PHE
A
233
24.335
75.588
25.559
1.00
12.13
6


1853
CD2
PHE
A
233
22.023
76.331
25.466
1.00
11.40
6


1854
CE1
PHE
A
233
23.982
74.503
26.347
1.00
12.18
6


1855
CE2
PHE
A
233
21.642
75.219
26.237
1.00
10.50
6


1856
CZ
PHE
A
233
22.629
74.340
26.657
1.00
11.82
6


1857
N
ASN
A
234
22.051
80.148
25.349
1.00
12.13
7


1858
CA
ASN
A
234
21.093
80.799
26.253
1.00
8.31
6


1859
C
ASN
A
234
20.367
79.859
27.214
1.00
9.45
6


1860
O
ASN
A
234
20.112
78.722
26.829
1.00
9.94
8


1861
CB
ASN
A
234
20.132
81.662
25.369
1.00
10.71
6


1862
CG
ASN
A
234
18.981
80.871
24.740
1.00
12.93
6


1863
OD1
ASN
A
234
18.070
80.516
25.519
1.00
12.50
8


1864
ND2
ASN
A
234
18.975
80.590
23.448
1.00
10.79
7


1865
N
SER
A
235
20.023
80.451
28.374
1.00
10.78
7


1866
CA
SER
A
235
19.401
79.586
29.396
1.00
8.67
6


1867
C
SER
A
235
17.906
79.375
29.177
1.00
11.06
6


1868
O
SER
A
235
17.399
78.402
29.759
1.00
11.56
8


1869
CB
ASER
A
235
19.594
80.196
30.792
0.60
11.41
6


1870
OG
ASER
A
235
20.974
80.269
31.098
0.60
10.81
8


1869
CB
BSER
A
235
19.679
80.067
30.817
0.40
10.03
6


1870
OG
BSER
A
235
19.311
81.423
30.914
0.40
7.85
8


1871
N
GLY
A
236
17.301
80.140
28.312
1.00
10.81
7


1872
CA
GLY
A
236
15.906
79.857
27.882
1.00
11.83
6


1873
C
GLY
A
236
15.821
78.448
27.289
1.00
12.34
6


1874
O
GLY
A
236
14.942
77.638
27.552
1.00
11.07
8


1875
N
PHE
A
237
16.742
78.158
26.370
1.00
10.75
7


1876
CA
PHE
A
237
16.793
76.864
25.702
1.00
9.60
6


1877
C
PHE
A
237
17.034
75.738
26.715
1.00
10.90
6


1878
O
PHE
A
237
16.476
74.641
26.526
1.00
10.74
8


1879
CB
PHE
A
237
17.714
76.891
24.467
1.00
12.14
6


1880
CG
PHE
A
237
17.642
75.595
23.691
1.00
12.02
6


1881
CD1
PHE
A
237
16.442
75.242
23.048
1.00
12.55
6


1882
CD2
PHE
A
237
18.751
74.740
23.659
1.00
11.64
6


1883
CE1
PHE
A
237
16.367
74.046
22.358
1.00
12.60
6


1884
CE2
PHE
A
237
18.634
73.533
22.952
1.00
11.39
6


1885
CZ
PHE
A
237
17.468
73.200
22.301
1.00
13.43
6


1886
N
SER
A
238
17.965
75.939
27.658
1.00
10.56
7


1887
CA
SER
A
238
18.119
74.844
28.637
1.00
11.43
6


1888
C
SER
A
238
16.762
74.489
29.289
1.00
10.24
6


1889
O
SER
A
238
16.416
73.312
29.442
1.00
10.58
8


1890
CB
SER
A
238
19.069
75.303
29.776
1.00
11.86
6


1891
OG
SER
A
238
20.432
75.070
29.404
1.00
12.16
8


1892
N
LYS
A
239
16.053
75.523
29.757
1.00
10.06
7


1893
CA
LYS
A
239
14.749
75.262
30.433
1.00
10.43
6


1894
C
LYS
A
239
13.712
74.684
29.505
1.00
10.95
6


1895
O
LYS
A
239
13.006
73.718
29.879
1.00
11.91
8


1896
CB
LYS
A
239
14.259
76.598
31.123
1.00
8.56
6


1897
CG
LYS
A
239
12.889
76.329
31.861
1.00
12.08
6


1898
CD
LYS
A
239
12.577
77.644
32.648
1.00
11.14
6


1899
CE
LYS
A
239
11.131
77.442
33.240
1.00
11.14
6


1900
NZ
LYS
A
239
10.797
78.668
34.098
1.00
10.40
7


1901
N
SER
A
240
13.600
75.153
28.279
1.00
9.61
7


1902
CA
SER
A
240
12.611
74.583
27.330
1.00
9.08
6


1903
C
SER
A
240
13.006
73.207
26.957
1.00
10.90
6


1904
O
SER
A
240
12.160
72.320
26.790
1.00
10.77
8


1905
CB
SER
A
240
12.560
75.572
26.136
1.00
11.38
6


1906
OG
SER
A
240
11.488
75.039
25.266
1.00
12.68
8


1907
N
LEU
A
241
14.300
72.896
26.747
1.00
10.43
7


1908
CA
LEU
A
241
14.726
71.560
26.389
1.00
10.29
6


1909
C
LEU
A
241
14.420
70.599
27.539
1.00
11.73
6


1910
O
LEU
A
241
13.924
69.507
27.303
1.00
11.15
8


1911
CB
LEU
A
241
16.255
71.582
26.077
1.00
10.07
6


1912
CG
LEU
A
241
16.816
70.170
25.829
1.00
12.71
6


1913
CD1
LEU
A
241
16.205
69.502
24.577
1.00
13.39
6


1914
CD2
LEU
A
241
18.333
70.350
25.611
1.00
12.90
6


1915
N
ALA
A
242
14.710
71.055
28.778
1.00
11.25
7


1916
CA
ALA
A
242
14.427
70.181
29.912
1.00
10.06
6


1917
C
ALA
A
242
12.923
69.852
29.969
1.00
10.68
6


1918
O
ALA
A
242
12.565
68.703
30.215
1.00
10.97
8


1919
CB
ALA
A
242
14.910
70.889
31.196
1.00
10.49
6


1920
N
ASP
A
243
12.062
70.870
29.712
1.00
10.40
7


1921
CA
ASP
A
243
10.609
70.595
29.694
1.00
11.54
6


1922
C
ASP
A
243
10.365
69.448
28.700
1.00
12.78
6


1923
O
ASP
A
243
9.636
68.474
29.006
1.00
12.31
8


1924
CB
ASP
A
243
9.930
71.904
29.186
1.00
11.95
6


1925
CG
ASP
A
243
8.507
71.717
28.674
1.00
13.21
6


1926
OD1
ASP
A
243
7.668
71.113
29.422
1.00
12.98
8


1927
OD2
ASP
A
243
8.223
72.178
27.546
1.00
12.92
8


1928
N
LYS
A
244
10.825
69.536
27.451
1.00
10.42
7


1929
CA
LYS
A
244
10.523
68.449
26.484
1.00
10.94
6


1930
C
LYS
A
244
10.997
67.097
26.998
1.00
13.31
6


1931
O
LYS
A
244
10.349
66.061
26.763
1.00
12.24
8


1932
CB
LYS
A
244
11.232
68.728
25.122
1.00
11.69
6


1933
CG
LYS
A
244
10.924
70.142
24.580
1.00
14.16
6


1934
CD
LYS
A
244
9.398
70.400
24.483
1.00
13.14
6


1935
CE
LYS
A
244
9.129
71.869
24.133
1.00
13.82
6


1936
NZ
LYS
A
244
9.582
72.780
25.269
1.00
12.11
7


1937
N
LEU
A
245
12.213
67.068
27.593
1.00
11.20
7


1938
CA
LEU
A
245
12.730
65.762
28.039
1.00
11.98
6


1939
C
LEU
A
245
11.936
65.200
29.205
1.00
12.96
6


1940
O
LEU
A
245
11.665
63.996
29.219
1.00
12.16
8


1941
CB
LEU
A
245
14.221
65.961
28.461
1.00
10.88
6


1942
CG
LEU
A
245
15.091
66.282
27.206
1.00
15.60
6


1943
CD1
LEU
A
245
16.493
66.701
27.692
1.00
14.87
6


1944
CD2
LEU
A
245
15.227
65.052
26.282
1.00
19.24
6


1945
N
TYR
A
246
11.480
66.037
30.136
1.00
11.31
7


1946
CA
TYR
A
246
10.676
65.529
31.258
1.00
11.13
6


1947
C
TYR
A
246
9.294
65.090
30.770
1.00
11.59
6


1948
O
TYR
A
246
8.674
64.306
31.500
1.00
13.03
8


1949
CB
TYR
A
246
10.582
66.586
32.359
1.00
12.53
6


1950
CG
TYR
A
246
11.928
66.907
32.995
1.00
9.85
6


1951
CD1
TYR
A
246
12.882
65.941
33.210
1.00
11.79
6


1952
CD2
TYR
A
246
12.163
68.228
33.408
1.00
10.52
6


1953
CE1
TYR
A
246
14.103
66.245
33.830
1.00
11.71
6


1954
CE2
TYR
A
246
13.379
68.569
34.021
1.00
10.59
6


1955
CZ
TYR
A
246
14.319
67.562
34.208
1.00
11.60
6


1956
OH
TYR
A
246
15.536
67.856
34.816
1.00
11.49
8


1957
N
GLN
A
247
8.769
65.623
29.672
1.00
12.54
7


1958
CA
GLN
A
247
7.501
65.088
29.112
1.00
13.07
6


1959
C
GLN
A
247
7.677
63.690
28.587
1.00
13.75
6


1960
O
GLN
A
247
6.712
62.875
28.651
1.00
16.16
8


1961
CB
GLN
A
247
7.016
66.001
27.940
1.00
12.33
6


1962
CG
GLN
A
247
6.530
67.357
28.518
1.00
13.62
6


1963
CD
GLN
A
247
6.016
68.220
27.397
1.00
16.89
6


1964
OE1
GLN
A
247
5.355
67.699
26.462
1.00
18.89
8


1965
NE2
GLN
A
247
6.372
69.518
27.387
1.00
14.76
7


1966
N
LYS
A
248
8.881
63.349
28.162
1.00
14.17
7


1967
CA
LYS
A
248
9.163
61.979
27.702
1.00
15.18
6


1968
C
LYS
A
248
9.328
61.000
28.836
1.00
15.52
6


1969
O
LYS
A
248
8.839
59.868
28.746
1.00
16.45
8


1970
CB
ALYS
A
248
10.397
61.994
26.793
0.50
13.40
6


1971
CG
ALYS
A
248
10.116
62.793
25.528
0.50
14.14
6


1972
CD
ALYS
A
248
8.958
62.165
24.749
0.50
17.69
6


1973
CE
ALYS
A
248
8.449
63.068
23.657
0.50
18.41
6


1974
NZ
ALYS
A
248
7.682
62.378
22.577
0.50
25.68
7


1970
CB
BLYS
A
248
10.414
62.030
26.816
0.50
17.60
6


1971
CG
BLYS
A
248
10.840
60.676
26.292
0.50
22.20
6


1972
CD
BLYS
A
248
11.561
60.755
24.977
0.50
29.85
6


1973
CE
BLYS
A
248
11.495
59.497
24.150
0.50
18.09
6


1974
NZ
BLYS
A
248
10.779
58.367
24.885
0.50
21.86
7


1975
N
LYS
A
249
10.131
61.400
29.830
1.00
12.97
7


1976
CA
LYS
A
249
10.424
60.442
30.917
1.00
14.04
6


1977
C
LYS
A
249
10.983
61.213
32.084
1.00
11.94
6


1978
O
LYS
A
249
11.520
62.316
31.876
1.00
13.26
8


1979
CB
LYS
A
249
11.514
59.423
30.462
1.00
15.09
6


1980
CG
LYS
A
249
11.674
58.358
31.542
1.00
15.17
6


1981
CD
LYS
A
249
12.552
57.175
31.147
1.00
23.08
6


1982
CE
LYS
A
249
12.451
56.111
32.249
1.00
27.89
6


1983
NZ
LYS
A
249
13.149
54.836
31.875
1.00
36.10
7


1984
N
ASP
A
250
10.870
60.678
33.288
1.00
11.41
7


1985
CA
ASP
A
250
11.406
61.336
34.494
1.00
12.04
6


1986
C
ASP
A
250
12.918
61.011
34.626
1.00
11.51
6


1987
O
ASP
A
250
13.348
60.354
35.546
1.00
13.89
8


1988
CB
ASP
A
250
10.638
60.891
35.728
1.00
11.54
6


1989
CG
ASP
A
250
10.618
59.405
36.030
1.00
15.08
6


1990
OD1
ASP
A
250
10.695
58.618
35.085
1.00
15.58
8


1991
OD2
ASP
A
250
10.448
59.027
37.224
1.00
15.73
8


1992
N
ILE
A
251
13.644
61.541
33.607
1.00
11.19
7


1993
CA
ILE
A
251
15.093
61.346
33.593
1.00
12.04
6


1994
C
ILE
A
251
15.777
62.413
34.467
1.00
12.14
6


1995
O
ILE
A
251
15.148
63.303
34.990
1.00
13.37
8


1996
CB
ILE
A
251
15.610
61.331
32.164
1.00
15.29
6


1997
CG1
ILE
A
251
14.988
62.477
31.361
1.00
23.77
6


1998
CG2
ILE
A
251
15.204
60.064
31.402
1.00
16.73
6


1999
CD1
ILE
A
251
15.645
63.784
31.503
1.00
25.03
6


2000
N
PHE
A
252
17.122
62.248
34.639
1.00
9.99
7


2001
CA
PHE
A
252
17.885
63.182
35.420
1.00
9.59
6


2002
C
PHE
A
252
18.690
64.105
34.501
1.00
11.26
6


2003
O
PHE
A
252
19.347
63.587
33.596
1.00
12.38
8


2004
CB
PHE
A
252
18.916
62.372
36.275
1.00
13.00
6


2005
CG
PHE
A
252
19.748
63.290
37.145
1.00
11.27
6


2006
CD1
PHE
A
252
19.182
63.951
38.241
1.00
12.24
6


2007
CD2
PHE
A
252
21.094
63.494
36.838
1.00
12.52
6


2008
CE1
PHE
A
252
19.907
64.802
39.029
1.00
11.05
6


2009
CE2
PHE
A
252
21.843
64.327
37.664
1.00
11.26
6


2010
CZ
PHE
A
252
21.263
65.031
38.750
1.00
10.84
6


2011
N
LEU
A
253
18.740
65.389
34.772
1.00
12.09
7


2012
CA
LEU
A
253
19.592
66.278
33.936
1.00
9.30
6


2013
C
LEU
A
253
20.498
67.083
34.913
1.00
9.94
6


2014
O
LEU
A
253
20.094
67.647
35.914
1.00
11.26
8


2015
CB
LEU
A
253
18.694
67.378
33.282
1.00
8.72
6


2016
CG
LEU
A
253
17.749
66.766
32.216
1.00
10.91
6


2017
CD1
LEU
A
253
16.881
67.891
31.562
1.00
10.35
6


2018
CD2
LEU
A
253
18.508
66.051
31.089
1.00
12.13
6


2019
N
VAL
A
254
21.761
67.179
34.422
1.00
11.23
7


2020
CA
VAL
A
254
22.750
68.015
35.077
1.00
11.09
6


2021
C
VAL
A
254
23.423
68.807
33.921
1.00
10.26
6


2022
O
VAL
A
254
23.707
68.196
32.892
1.00
10.32
8


2023
CB
VAL
A
254
23.722
67.184
35.947
1.00
9.61
6


2024
CG1
VAL
A
254
24.552
66.161
35.161
1.00
10.99
6


2025
CG2
VAL
A
254
24.688
68.131
36.685
1.00
11.22
6


2026
N
GLY
A
255
23.762
70.047
34.194
1.00
10.96
7


2027
CA
GLY
A
255
24.492
70.879
33.243
1.00
11.43
6


2028
C
GLY
A
255
25.877
71.193
33.731
1.00
11.23
6


2029
O
GLY
A
255
26.095
71.404
34.967
1.00
10.31
8


2030
N
GLU
A
256
26.828
71.308
32.765
1.00
10.72
7


2031
CA
GLU
A
256
28.159
71.786
33.187
1.00
10.84
6


2032
C
GLU
A
256
28.236
73.315
33.013
1.00
11.33
6


2033
O
GLU
A
256
28.295
73.820
31.871
1.00
10.36
8


2034
CB
GLU
A
256
29.172
71.178
32.167
1.00
10.52
6


2035
CG
GLU
A
256
30.603
71.617
32.605
1.00
10.70
6


2036
CD
GLU
A
256
31.442
72.059
31.414
1.00
11.32
6


2037
OE1
GLU
A
256
30.925
72.467
30.347
1.00
10.78
8


2038
OE2
GLU
A
256
32.696
71.998
31.517
1.00
11.88
8


2039
N
TRP
A
257
28.173
74.038
34.120
1.00
9.79
7


2040
CA
TRP
A
257
28.409
75.480
34.158
1.00
9.57
6


2041
C
TRP
A
257
29.798
75.608
34.799
1.00
10.84
6


2042
O
TRP
A
257
29.908
75.560
36.037
1.00
10.82
8


2043
CB
TRP
A
257
27.301
76.175
34.997
1.00
9.83
6


2044
CG
TRP
A
257
27.449
77.700
34.854
1.00
8.59
6


2045
CD1
TRP
A
257
28.566
78.442
35.196
1.00
12.90
6


2046
CD2
TRP
A
257
26.431
78.592
34.412
1.00
10.35
6


2047
NE1
TRP
A
257
28.295
79.753
34.937
1.00
12.55
7


2048
CE2
TRP
A
257
27.020
79.891
34.459
1.00
12.29
6


2049
CE3
TRP
A
257
25.124
78.425
33.946
1.00
13.94
6


2050
CZ2
TRP
A
257
26.317
81.041
34.055
1.00
10.73
6


2051
CZ3
TRP
A
257
24.385
79.544
33.527
1.00
13.32
6


2052
CH2
TRP
A
257
25.026
80.793
33.599
1.00
11.64
6


2053
N
TYR
A
258
30.831
75.725
33.986
1.00
11.79
7


2054
CA
TYR
A
258
32.211
75.619
34.524
1.00
11.80
6


2055
C
TYR
A
258
32.527
76.859
35.355
1.00
12.06
6


2056
O
TYR
A
258
32.370
77.988
34.869
1.00
13.57
8


2057
CB
TYR
A
258
33.189
75.508
33.335
1.00
11.31
6


2058
CG
TYR
A
258
34.562
74.978
33.723
1.00
11.97
6


2059
CD1
TYR
A
258
35.452
75.687
34.524
1.00
13.71
6


2060
CD2
TYR
A
258
34.932
73.734
33.234
1.00
11.78
6


2061
CE1
TYR
A
258
36.707
75.160
34.859
1.00
15.77
6


2062
CE2
TYR
A
258
36.179
73.226
33.564
1.00
13.38
6


2063
CZ
TYR
A
258
37.037
73.908
34.376
1.00
16.44
6


2064
OH
TYR
A
258
38.277
73.304
34.631
1.00
20.59
8


2065
N
GLY
A
259
33.030
76.605
36.550
1.00
9.86
7


2066
CA
GLY
A
259
33.584
77.705
37.361
1.00
12.24
6


2067
C
GLY
A
259
32.510
78.690
37.891
1.00
11.55
6


2068
O
GLY
A
259
31.417
78.276
38.227
1.00
12.61
8


2069
N
ASP
A
260
32.921
79.963
37.891
1.00
11.45
7


2070
CA
ASP
A
260
32.064
81.004
38.486
1.00
10.59
6


2071
C
ASP
A
260
31.718
80.614
39.947
1.00
12.08
6


2072
O
ASP
A
260
30.554
80.528
40.317
1.00
11.34
8


2073
CB
ASP
A
260
30.792
81.286
37.665
1.00
13.01
6


2074
CG
ASP
A
260
31.160
81.807
36.269
1.00
16.43
6


2075
OD1
ASP
A
260
32.136
82.593
36.148
1.00
13.58
8


2076
OD2
ASP
A
260
30.486
81.502
35.274
1.00
14.47
8


2077
N
ASP
A
261
32.812
80.528
40.708
1.00
10.89
7


2078
CA
ASP
A
261
32.709
80.239
42.158
1.00
13.96
6


2079
C
ASP
A
261
32.059
81.369
42.936
1.00
12.00
6


2080
O
ASP
A
261
31.920
82.528
42.502
1.00
13.08
8


2081
CB
ASP
A
261
34.125
79.875
42.610
1.00
17.34
6


2082
CG
ASP
A
261
34.615
78.518
42.074
1.00
18.47
6


2083
OD1
ASP
A
261
33.990
77.881
41.181
1.00
22.23
8


2084
OD2
ASP
A
261
35.642
78.035
42.569
1.00
20.46
8


2085
N
PRO
A
262
31.751
81.124
44.230
1.00
11.36
7


2086
CA
PRO
A
262
31.155
82.197
45.033
1.00
13.50
6


2087
C
PRO
A
262
32.085
83.428
45.042
1.00
15.27
6


2088
O
PRO
A
262
33.325
83.254
45.078
1.00
17.80
8


2089
CB
PRO
A
262
30.973
81.583
46.445
1.00
14.74
6


2090
CG
PRO
A
262
30.818
80.086
46.071
1.00
13.76
6


2091
CD
PRO
A
262
31.873
79.856
44.938
1.00
11.66
6


2092
N
GLY
A
263
31.385
84.560
45.069
1.00
20.11
7


2093
CA
GLY
A
263
32.178
85.810
45.091
1.00
20.82
6


2094
C
GLY
A
263
32.444
86.343
43.693
1.00
22.93
6


2095
O
GLY
A
263
33.030
87.433
43.565
1.00
26.12
8


2096
N
THR
A
264
32.204
85.581
42.640
1.00
16.30
7


2097
CA
THR
A
264
32.579
85.990
41.270
1.00
15.29
6


2098
C
THR
A
264
31.378
86.647
40.599
1.00
14.14
6


2099
O
THR
A
264
30.225
86.490
41.019
1.00
15.14
8


2100
CB
THR
A
264
33.154
84.890
40.377
1.00
17.00
6


2101
OG1
THR
A
264
32.185
83.864
40.214
1.00
17.20
8


2102
CG2
THR
A
264
34.455
84.302
40.998
1.00
18.53
6


2103
N
ALA
A
265
31.684
87.407
39.536
1.00
14.47
7


2104
CA
ALA
A
265
30.579
88.206
38.957
1.00
16.68
6


2105
C
ALA
A
265
29.455
87.387
38.348
1.00
14.50
6


2106
O
ALA
A
265
28.315
87.921
38.316
1.00
15.71
8


2107
CB
ALA
A
265
31.153
89.034
37.793
1.00
18.93
6


2108
N
ASN
A
266
29.808
86.186
37.837
1.00
11.26
7


2109
CA
ASN
A
266
28.739
85.402
37.199
1.00
12.93
6


2110
C
ASN
A
266
28.140
84.338
38.110
1.00
13.52
6


2111
O
ASN
A
266
27.364
83.484
37.632
1.00
11.82
8


2112
CB
ASN
A
266
29.289
84.792
35.855
1.00
15.03
6


2113
CG
ASN
A
266
29.632
85.944
34.889
1.00
15.26
6


2114
OD1
ASN
A
266
28.938
86.955
34.822
1.00
13.24
8


2115
ND2
ASN
A
266
30.698
85.797
34.146
1.00
14.64
7


2116
N
HIS
A
267
28.621
84.306
39.353
1.00
12.23
7


2117
CA
HIS
A
267
28.106
83.276
40.271
1.00
13.10
6


2118
C
HIS
A
267
26.596
83.276
40.469
1.00
13.44
6


2119
O
HIS
A
267
25.999
82.182
40.399
1.00
12.11
8


2120
CB
HIS
A
267
28.852
83.439
41.616
1.00
10.82
6


2121
CG
HIS
A
267
28.469
82.306
42.563
1.00
12.37
6


2122
ND1
HIS
A
267
28.877
81.020
42.410
1.00
11.65
7


2123
CD2
HIS
A
267
27.637
82.360
43.640
1.00
15.29
6


2124
CE1
HIS
A
267
28.355
80.278
43.375
1.00
12.97
6


2125
NE2
HIS
A
267
27.608
81.080
44.153
1.00
11.63
7


2126
N
LEU
A
268
26.001
84.430
40.726
1.00
10.81
7


2127
CA
LEU
A
268
24.548
84.455
40.988
1.00
13.40
6


2128
C
LEU
A
268
23.766
83.997
39.768
1.00
11.02
6


2129
O
LEU
A
268
22.745
83.268
39.957
1.00
12.74
8


2130
CB
LEU
A
268
24.169
85.889
41.374
1.00
14.95
6


2131
CG
LEU
A
268
22.599
86.052
41.471
1.00
19.99
6


2132
CD1
LEU
A
268
22.040
85.151
42.563
1.00
24.25
6


2133
CD2
LEU
A
268
22.298
87.536
41.677
1.00
25.18
6


2134
N
GLU
A
269
24.210
84.274
38.549
1.00
11.51
7


2135
CA
GLU
A
269
23.495
83.760
37.381
1.00
11.81
6


2136
C
GLU
A
269
23.525
82.221
37.386
1.00
10.11
6


2137
O
GLU
A
269
22.512
81.596
37.067
1.00
11.07
8


2138
CB
GLU
A
269
24.190
84.360
36.122
1.00
13.26
6


2139
CG
GLU
A
269
23.490
83.803
34.867
1.00
11.45
6


2140
CD
GLU
A
269
24.122
84.417
33.582
1.00
13.11
6


2141
OE1
GLU
A
269
24.906
85.369
33.643
1.00
12.92
8


2142
OE2
GLU
A
269
23.720
83.906
32.525
1.00
12.17
8


2143
N
LYS
A
270
24.678
81.608
37.720
1.00
9.00
7


2144
CA
LYS
A
270
24.754
80.156
37.787
1.00
9.72
6


2145
C
LYS
A
270
23.806
79.578
38.862
1.00
10.98
6


2146
O
LYS
A
270
23.079
78.613
38.609
1.00
10.64
8


2147
CB
LYS
A
270
26.221
79.709
38.063
1.00
10.49
6


2148
CG
LYS
A
270
26.259
78.174
38.299
1.00
10.05
6


2149
CD
LYS
A
270
27.725
77.682
38.502
1.00
8.77
6


2150
CE
LYS
A
270
28.236
78.181
39.869
1.00
9.57
6


2151
NZ
LYS
A
270
29.600
77.515
40.161
1.00
11.56
7


2152
N
VAL
A
271
23.765
80.218
40.038
1.00
11.90
7


2153
CA
VAL
A
271
22.847
79.712
41.105
1.00
10.97
6


2154
C
VAL
A
271
21.392
79.835
40.608
1.00
10.81
6


2155
O
VAL
A
271
20.583
78.951
40.827
1.00
11.67
8


2156
CB
VAL
A
271
23.044
80.608
42.346
1.00
13.53
6


2157
CG1
VAL
A
271
22.016
80.248
43.435
1.00
12.11
6


2158
CG2
VAL
A
271
24.455
80.307
42.888
1.00
12.46
6


2159
N
ARG
A
272
21.064
80.978
39.983
1.00
11.20
7


2160
CA
ARG
A
272
19.668
81.127
39.458
1.00
11.53
6


2161
C
ARG
A
272
19.328
80.041
38.439
1.00
10.29
6


2162
O
ARG
A
272
18.208
79.506
38.389
1.00
11.34
8


2163
CB
ARG
A
272
19.462
82.540
38.859
1.00
9.74
6


2164
CG
ARG
A
272
19.220
83.552
40.027
1.00
11.97
6


2165
CD
ARG
A
272
19.405
85.000
39.483
1.00
10.96
6


2166
NE
ARG
A
272
18.600
85.394
38.306
1.00
12.10
7


2167
CZ
ARG
A
272
17.297
85.759
38.377
1.00
14.61
6


2168
NH1
ARG
A
272
16.541
85.765
39.493
1.00
12.14
7


2169
NH2
ARG
A
272
16.734
86.132
37.232
1.00
12.07
7


2170
N
TYR
A
273
20.329
79.790
37.553
1.00
10.33
7


2171
CA
TYR
A
273
20.116
78.669
36.589
1.00
11.57
6


2172
C
TYR
A
273
19.882
77.355
37.328
1.00
9.14
6


2173
O
TYR
A
273
18.931
76.590
36.993
1.00
12.29
8


2174
CB
TYR
A
273
21.415
78.569
35.742
1.00
9.07
6


2175
CG
TYR
A
273
21.388
77.445
34.693
1.00
8.78
6


2176
CD1
TYR
A
273
21.708
76.144
35.110
1.00
11.52
6


2177
CD2
TYR
A
273
21.054
77.630
33.363
1.00
9.55
6


2178
CE1
TYR
A
273
21.663
75.071
34.218
1.00
9.62
6


2179
CE2
TYR
A
273
21.087
76.577
32.482
1.00
8.45
6


2180
CZ
TYR
A
273
21.366
75.301
32.885
1.00
10.47
6


2181
OH
TYR
A
273
21.365
74.258
31.956
1.00
11.35
8


2182
N
ALA
A
274
20.678
77.001
38.308
1.00
10.68
7


2183
CA
ALA
A
274
20.449
75.697
39.008
1.00
10.66
6


2184
C
ALA
A
274
19.062
75.725
39.677
1.00
10.79
6


2185
O
ALA
A
274
18.478
74.649
39.796
1.00
11.53
8


2186
CB
ALA
A
274
21.539
75.560
40.092
1.00
12.82
6


2187
N
ASN
A
275
18.692
76.887
40.217
1.00
11.15
7


2188
CA
ASN
A
275
17.443
76.882
40.998
1.00
11.26
6


2189
C
ASN
A
275
16.199
77.051
40.131
1.00
10.88
6


2190
O
ASN
A
275
15.082
76.705
40.606
1.00
11.83
8


2191
CB
ASN
A
275
17.490
78.056
42.004
1.00
11.31
6


2192
CG
ASN
A
275
18.495
77.768
43.107
1.00
11.97
6


2193
OD1
ASN
A
275
18.987
76.661
43.214
1.00
12.55
8


2194
ND2
ASN
A
275
18.759
78.816
43.934
1.00
12.55
7


2195
N
ASN
A
276
16.322
77.453
38.842
1.00
11.20
7


2196
CA
ASN
A
276
15.129
77.705
38.045
1.00
12.25
6


2197
C
ASN
A
276
15.023
76.992
36.720
1.00
14.18
6


2198
O
ASN
A
276
13.932
76.820
36.165
1.00
11.89
8


2199
CB
ASN
A
276
15.134
79.197
37.632
1.00
9.94
6


2200
CG
ASN
A
276
14.629
80.023
38.806
1.00
14.75
6


2201
OD1
ASN
A
276
13.365
80.089
38.826
1.00
16.83
8


2202
ND2
ASN
A
276
15.551
80.529
39.612
1.00
16.12
7


2203
N
SER
A
277
16.151
76.504
36.173
1.00
10.52
7


2204
CA
SER
A
277
16.064
75.974
34.811
1.00
11.82
6


2205
C
SER
A
277
15.497
74.585
34.678
1.00
11.16
6


2206
O
SER
A
277
15.204
74.178
33.545
1.00
12.16
8


2207
CB
SER
A
277
17.502
75.911
34.204
1.00
11.66
6


2208
OG
SER
A
277
18.257
74.877
34.872
1.00
12.14
8


2209
N
GLY
A
278
15.371
73.851
35.795
1.00
11.36
7


2210
CA
GLY
A
278
15.051
72.411
35.697
1.00
11.40
6


2211
C
GLY
A
278
16.263
71.565
35.375
1.00
11.97
6


2212
O
GLY
A
278
16.115
70.348
35.279
1.00
13.61
8


2213
N
VAL
A
279
17.442
72.180
35.342
1.00
12.14
7


2214
CA
VAL
A
279
18.673
71.427
35.090
1.00
10.48
6


2215
C
VAL
A
279
19.552
71.645
36.348
1.00
11.31
6


2216
O
VAL
A
279
19.814
72.782
36.732
1.00
12.60
8


2217
CB
VAL
A
279
19.362
71.989
33.830
1.00
11.56
6


2218
CG1
VAL
A
279
20.628
71.191
33.543
1.00
10.87
6


2219
CG2
VAL
A
279
18.429
71.824
32.592
1.00
13.38
6


2220
N
ASN
A
280
20.053
70.556
36.919
1.00
10.03
7


2221
CA
ASN
A
280
20.918
70.714
38.122
1.00
10.49
6


2222
C
ASN
A
280
22.294
71.095
37.572
1.00
13.05
6


2223
O
ASN
A
280
22.506
71.116
36.365
1.00
12.57
8


2224
CB
ASN
A
280
20.968
69.368
38.864
1.00
11.26
6


2225
CG
ASN
A
280
19.492
69.056
39.263
1.00
9.85
6


2226
OD1
ASN
A
280
18.839
69.805
39.990
1.00
10.91
8


2227
ND2
ASN
A
280
18.974
67.913
38.787
1.00
10.65
7


2228
N
VAL
A
281
23.262
71.312
38.492
1.00
11.45
7


2229
CA
VAL
A
281
24.622
71.621
37.977
1.00
9.71
6


2230
C
VAL
A
281
25.671
70.782
38.660
1.00
11.24
6


2231
O
VAL
A
281
25.581
70.318
39.799
1.00
11.15
8


2232
CB
VAL
A
281
25.013
73.104
38.187
1.00
9.82
6


2233
CG1
VAL
A
281
24.019
74.024
37.397
1.00
10.47
6


2234
CG2
VAL
A
281
25.038
73.569
39.638
1.00
11.52
6


2235
N
LEU
A
282
26.786
70.675
37.904
1.00
9.31
7


2236
CA
LEU
A
282
28.031
70.087
38.460
1.00
10.27
6


2237
C
LEU
A
282
28.631
71.063
39.476
1.00
11.17
6


2238
O
LEU
A
282
28.577
72.295
39.298
1.00
12.65
8


2239
CB
LEU
A
282
29.022
69.883
37.283
1.00
10.13
6


2240
CG
LEU
A
282
28.650
68.558
36.538
1.00
11.97
6


2241
CD1
LEU
A
282
29.159
68.726
35.102
1.00
16.51
6


2242
CD2
LEU
A
282
29.314
67.351
37.196
1.00
12.93
6


2243
N
ASP
A
283
29.128
70.458
40.581
1.00
9.33
7


2244
CA
ASP
A
283
29.503
71.304
41.764
1.00
11.76
6


2245
C
ASP
A
283
30.935
71.778
41.696
1.00
11.31
6


2246
O
ASP
A
283
31.877
71.275
42.316
1.00
11.22
8


2247
CB
ASP
A
283
29.212
70.451
43.014
1.00
8.73
6


2248
CG
ASP
A
283
29.282
71.343
44.271
1.00
11.60
6


2249
OD1
ASP
A
283
29.655
72.526
44.259
1.00
10.06
8


2250
OD2
ASP
A
283
28.866
70.758
45.290
1.00
11.95
8


2251
N
PHE
A
284
31.108
72.815
40.834
1.00
10.41
7


2252
CA
PHE
A
284
32.439
73.424
40.731
1.00
10.33
6


2253
C
PHE
A
284
32.746
74.271
41.966
1.00
11.21
6


2254
O
PHE
A
284
33.941
74.331
42.313
1.00
12.52
8


2255
CB
PHE
A
284
32.509
74.409
39.517
1.00
10.51
6


2256
CG
PHE
A
284
32.750
73.575
38.227
1.00
10.01
6


2257
CD1
PHE
A
284
31.725
72.991
37.520
1.00
11.07
6


2258
CD2
PHE
A
284
34.073
73.416
37.765
1.00
11.57
6


2259
CE1
PHE
A
284
31.925
72.232
36.386
1.00
12.29
6


2260
CE2
PHE
A
284
34.292
72.665
36.596
1.00
11.45
6


2261
CZ
PHE
A
284
33.234
72.085
35.903
1.00
9.72
6


2262
N
ASP
A
285
31.729
74.753
42.687
1.00
9.13
7


2263
CA
ASP
A
285
32.061
75.575
43.882
1.00
10.61
6


2264
C
ASP
A
285
32.799
74.670
44.885
1.00
10.95
6


2265
O
ASP
A
285
33.806
75.092
45.468
1.00
11.00
8


2266
CB
ASP
A
285
30.773
76.068
44.545
1.00
9.55
6


2267
CG
ASP
A
285
29.979
77.042
43.692
1.00
10.92
6


2268
OD1
ASP
A
285
30.499
77.631
42.710
1.00
12.04
8


2269
OD2
ASP
A
285
28.773
77.214
44.043
1.00
12.59
8


2270
N
LEU
A
286
32.248
73.464
45.128
1.00
10.30
7


2271
CA
LEU
A
286
32.959
72.569
46.061
1.00
9.08
6


2272
C
LEU
A
286
34.219
71.940
45.505
1.00
9.26
6


2273
O
LEU
A
286
35.179
71.757
46.238
1.00
11.04
8


2274
CB
LEU
A
286
31.968
71.419
46.481
1.00
9.12
6


2275
CG
LEU
A
286
32.367
70.697
47.790
1.00
10.68
6


2276
CD1
LEU
A
286
32.357
71.580
49.023
1.00
15.93
6


2277
CD2
LEU
A
286
31.384
69.510
47.999
1.00
13.68
6


2278
N
ASN
A
287
34.226
71.683
44.168
1.00
9.32
7


2279
CA
ASN
A
287
35.441
71.091
43.586
1.00
10.65
6


2280
C
ASN
A
287
36.687
71.937
43.872
1.00
9.75
6


2281
O
ASN
A
287
37.751
71.401
44.184
1.00
10.35
8


2282
CB
ASN
A
287
35.269
71.000
42.039
1.00
8.74
6


2283
CG
ASN
A
287
36.571
70.507
41.392
1.00
11.79
6


2284
OD1
ASN
A
287
37.171
71.318
40.654
1.00
11.65
8


2285
ND2
ASN
A
287
36.866
69.245
41.597
1.00
9.92
7


2286
N
THR
A
288
36.588
73.275
43.719
1.00
9.52
7


2287
CA
THR
A
288
37.769
74.106
43.907
1.00
11.58
6


2288
C
THR
A
288
38.367
73.906
45.292
1.00
10.74
6


2289
O
THR
A
288
39.593
73.741
45.486
1.00
13.25
8


2290
CB
THR
A
288
37.365
75.596
43.745
1.00
15.82
6


2291
OG1
THR
A
288
36.906
75.753
42.397
1.00
16.55
8


2292
CG2
THR
A
288
38.641
76.459
43.984
1.00
14.43
6


2293
N
VAL
A
289
37.440
73.847
46.268
1.00
8.64
7


2294
CA
VAL
A
289
37.915
73.732
47.655
1.00
8.82
6


2295
C
VAL
A
289
38.401
72.341
47.985
1.00
11.04
6


2296
O
VAL
A
289
39.438
72.184
48.642
1.00
11.67
8


2297
CB
VAL
A
289
36.780
74.237
48.605
1.00
11.02
6


2298
CG1
VAL
A
289
37.297
74.258
50.051
1.00
10.38
6


2299
CG2
VAL
A
289
36.323
75.632
48.191
1.00
11.61
6


2300
N
ILE
A
290
37.764
71.287
47.430
1.00
9.86
7


2301
CA
ILE
A
290
38.262
69.911
47.642
1.00
8.30
6


2302
C
ILE
A
290
39.715
69.830
47.144
1.00
12.22
6


2303
O
ILE
A
290
40.554
69.251
47.806
1.00
10.89
8


2304
CB
ILE
A
290
37.342
68.979
46.851
1.00
9.93
6


2305
CG1
ILE
A
290
36.004
68.833
47.591
1.00
11.46
6


2306
CG2
ILE
A
290
38.025
67.579
46.690
1.00
11.35
6


2307
CD1
ILE
A
290
34.964
68.108
46.700
1.00
11.71
6


2308
N
ARG
A
291
39.969
70.386
45.940
1.00
11.21
7


2309
CA
ARG
A
291
41.352
70.246
45.455
1.00
10.67
6


2310
C
ARG
A
291
42.343
71.071
46.293
1.00
9.59
6


2311
O
ARG
A
291
43.481
70.627
46.380
1.00
12.39
8


2312
CB
ARG
A
291
41.308
70.770
43.991
1.00
10.96
6


2313
CG
ARG
A
291
40.602
69.717
43.110
1.00
11.39
6


2314
CD
ARG
A
291
40.480
70.173
41.647
1.00
11.11
6


2315
NE
ARG
A
291
41.729
70.343
40.907
1.00
11.15
7


2316
CZ
ARG
A
291
42.225
69.361
40.109
1.00
12.12
6


2317
NH1
ARG
A
291
41.706
68.126
40.068
1.00
11.32
7


2318
NH2
ARG
A
291
43.322
69.593
39.363
1.00
12.38
7


2319
N
ASN
A
292
41.972
72.204
46.801
1.00
12.65
7


2320
CA
ASN
A
292
42.894
73.001
47.653
1.00
11.32
6


2321
C
ASN
A
292
42.983
72.376
49.051
1.00
11.68
6


2322
O
ASN
A
292
44.074
72.565
49.634
1.00
11.50
8


2323
CB
ASN
A
292
42.408
74.471
47.750
1.00
11.01
6


2324
CG
ASN
A
292
42.593
75.238
46.379
1.00
14.57
6


2325
OD1
ASN
A
292
43.466
74.831
45.665
1.00
19.84
8


2326
ND2
ASN
A
292
41.735
76.242
46.267
1.00
18.55
7


2327
N
VAL
A
293
42.009
71.574
49.542
1.00
10.40
7


2328
CA
VAL
A
293
42.157
71.075
50.940
1.00
10.24
6


2329
C
VAL
A
293
42.861
69.743
50.969
1.00
11.21
6


2330
O
VAL
A
293
43.748
69.520
51.783
1.00
11.98
8


2331
CB
VAL
A
293
40.703
70.961
51.499
1.00
10.95
6


2332
CG1
VAL
A
293
40.707
70.175
52.820
1.00
12.97
6


2333
CG2
VAL
A
293
40.153
72.364
51.736
1.00
13.88
6


2334
N
PHE
A
294
42.479
68.858
50.033
1.00
11.12
7


2335
CA
PHE
A
294
43.106
67.537
49.960
1.00
11.38
6


2336
C
PHE
A
294
44.255
67.464
48.964
1.00
11.51
6


2337
O
PHE
A
294
45.095
66.540
49.093
1.00
11.86
8


2338
CB
PHE
A
294
42.063
66.455
49.553
1.00
11.70
6


2339
CG
PHE
A
294
40.936
66.334
50.584
1.00
11.57
6


2340
CD1
PHE
A
294
41.178
65.683
51.808
1.00
11.48
6


2341
CD2
PHE
A
294
39.707
66.865
50.295
1.00
13.60
6


2342
CE1
PHE
A
294
40.133
65.579
52.724
1.00
12.41
6


2343
CE2
PHE
A
294
38.662
66.762
51.232
1.00
13.36
6


2344
CZ
PHE
A
294
38.880
66.104
52.463
1.00
13.22
6


2345
N
GLY
A
295
44.295
68.355
47.976
1.00
11.76
7


2346
CA
GLY
A
295
45.328
68.234
46.907
1.00
12.36
6


2347
C
GLY
A
295
46.504
69.187
47.187
1.00
10.85
6


2348
O
GLY
A
295
47.547
68.676
47.612
1.00
13.29
8


2349
N
THR
A
296
46.271
70.499
46.990
1.00
10.00
7


2350
CA
THR
A
296
47.441
71.394
47.123
1.00
11.19
6


2351
C
THR
A
296
47.675
71.894
48.549
1.00
13.50
6


2352
O
THR
A
296
48.755
72.436
48.874
1.00
12.22
8


2353
CB
THR
A
296
47.162
72.647
46.253
1.00
11.65
6


2354
OG1
THR
A
296
46.005
73.276
46.812
1.00
15.42
8


2355
CG2
THR
A
296
46.976
72.308
44.770
1.00
13.16
6


2356
N
PHE
A
297
46.760
71.647
49.472
1.00
11.24
7


2357
CA
PHE
A
297
46.917
72.026
50.881
1.00
12.10
6


2358
C
PHE
A
297
47.104
73.543
50.984
1.00
17.18
6


2359
O
PHE
A
297
47.719
74.035
51.952
1.00
17.61
8


2360
CB
PHE
A
297
48.052
71.271
51.610
1.00
11.80
6


2361
CG
PHE
A
297
47.630
69.924
52.199
1.00
14.38
6


2362
CD1
PHE
A
297
47.153
68.917
51.385
1.00
13.09
6


2363
CD2
PHE
A
297
47.760
69.711
53.565
1.00
11.70
6


2364
CE1
PHE
A
297
46.821
67.656
51.854
1.00
12.95
6


2365
CE2
PHE
A
297
47.438
68.444
54.064
1.00
12.92
6


2366
CZ
PHE
A
297
46.948
67.450
53.231
1.00
11.87
6


2367
N
THR
A
298
46.411
74.322
50.183
1.00
13.51
7


2368
CA
THR
A
298
46.398
75.773
50.270
1.00
13.52
6


2369
C
THR
A
298
45.131
76.303
50.925
1.00
13.29
6


2370
O
THR
A
298
45.018
77.505
51.220
1.00
15.14
8


2371
CB
THR
A
298
46.488
76.437
48.870
1.00
13.68
6


2372
OG1
THR
A
298
45.446
75.982
48.035
1.00
12.95
8


2373
CG2
THR
A
298
47.869
76.059
48.250
1.00
15.45
6


2374
N
GLN
A
299
44.162
75.400
51.194
1.00
10.17
7


2375
CA
GLN
A
299
43.009
75.785
51.975
1.00
13.00
6


2376
C
GLN
A
299
42.852
74.738
53.114
1.00
14.72
6


2377
O
GLN
A
299
43.624
73.753
53.094
1.00
14.92
8


2378
CB
GLN
A
299
41.654
75.808
51.214
1.00
11.79
6


2379
CG
GLN
A
299
41.692
77.072
50.299
1.00
14.80
6


2380
CD
GLN
A
299
40.301
77.320
49.668
1.00
16.23
6


2381
OE1
GLN
A
299
39.959
76.525
48.827
1.00
15.11
8


2382
NE2
GLN
A
299
39.635
78.376
50.107
1.00
17.75
7


2383
N
THR
A
300
42.031
75.020
54.106
1.00
13.71
7


2384
CA
THR
A
300
41.924
74.106
55.252
1.00
11.61
6


2385
C
THR
A
300
40.518
73.485
55.355
1.00
14.08
6


2386
O
THR
A
300
39.580
73.874
54.644
1.00
11.91
8


2387
CB
THR
A
300
42.152
74.850
56.601
1.00
15.34
6


2388
OG1
THR
A
300
41.116
75.771
56.804
1.00
15.70
8


2389
CG2
THR
A
300
43.511
75.587
56.464
1.00
16.98
6


2390
N
MET
A
301
40.337
72.672
56.443
1.00
11.88
7


2391
CA
MET
A
301
38.977
72.123
56.650
1.00
12.22
6


2392
C
MET
A
301
37.972
73.216
56.994
1.00
12.44
6


2393
O
MET
A
301
36.791
73.075
56.691
1.00
11.03
8


2394
CB
MET
A
301
38.935
71.065
57.800
1.00
12.80
6


2395
CG
MET
A
301
39.707
69.787
57.393
1.00
11.05
6


2396
SD
MET
A
301
39.027
69.014
55.895
1.00
12.28
16


2397
CE
MET
A
301
39.724
67.366
56.047
1.00
14.34
6


2398
N
TYR
A
302
38.408
74.374
57.555
1.00
12.00
7


2399
CA
TYR
A
302
37.462
75.453
57.759
1.00
10.79
6


2400
C
TYR
A
302
36.898
75.974
56.430
1.00
11.89
6


2401
O
TYR
A
302
35.694
76.181
56.325
1.00
12.65
8


2402
CB
TYR
A
302
38.131
76.626
58.505
1.00
10.20
6


2403
CG
TYR
A
302
38.409
76.271
59.983
1.00
11.51
6


2404
CD1
TYR
A
302
37.375
76.197
60.914
1.00
16.19
6


2405
CD2
TYR
A
302
39.739
76.057
60.344
1.00
17.97
6


2406
CE1
TYR
A
302
37.736
75.884
62.236
1.00
18.06
6


2407
CE2
TYR
A
302
40.062
75.723
61.683
1.00
15.93
6


2408
CZ
TYR
A
302
39.029
75.670
62.567
1.00
19.00
6


2409
OH
TYR
A
302
39.409
75.355
63.905
1.00
21.46
8


2410
N
ASP
A
303
37.763
76.026
55.418
1.00
13.06
7


2411
CA
ASP
A
303
37.256
76.434
54.104
1.00
12.54
6


2412
C
ASP
A
303
36.285
75.409
53.492
1.00
11.88
6


2413
O
ASP
A
303
35.330
75.782
52.785
1.00
13.46
8


2414
CB
ASP
A
303
38.419
76.666
53.133
1.00
10.93
6


2415
CG
ASP
A
303
39.386
77.734
53.654
1.00
14.78
6


2416
OD1
ASP
A
303
38.879
78.877
53.849
1.00
13.77
8


2417
OD2
ASP
A
303
40.573
77.435
53.832
1.00
13.10
8


2418
N
LEU
A
304
36.602
74.152
53.720
1.00
11.36
7


2419
CA
LEU
A
304
35.713
73.086
53.156
1.00
11.06
6


2420
C
LEU
A
304
34.348
73.181
53.841
1.00
12.95
6


2421
O
LEU
A
304
33.315
73.111
53.155
1.00
11.60
8


2422
CB
LEU
A
304
36.393
71.742
53.367
1.00
10.48
6


2423
CG
LEU
A
304
35.687
70.566
52.633
1.00
11.09
6


2424
CD1
LEU
A
304
35.737
70.797
51.112
1.00
12.57
6


2425
CD2
LEU
A
304
36.397
69.248
52.971
1.00
12.54
6


2426
N
ASN
A
305
34.290
73.255
55.180
1.00
11.76
7


2427
CA
ASN
A
305
32.999
73.422
55.887
1.00
12.74
6


2428
C
ASN
A
305
32.308
74.720
55.479
1.00
11.54
6


2429
O
ASN
A
305
31.100
74.673
55.259
1.00
13.50
8


2430
CB
ASN
A
305
33.331
73.448
57.405
1.00
12.22
6


2431
CG
ASN
A
305
32.014
73.551
58.210
1.00
12.84
6


2432
OD1
ASN
A
305
31.174
72.669
58.097
1.00
13.98
8


2433
ND2
ASN
A
305
31.910
74.651
58.967
1.00
17.24
7


2434
N
ASN
A
306
33.061
75.772
55.272
1.00
11.86
7


2435
CA
ASN
A
306
32.418
77.036
54.848
1.00
12.68
6


2436
C
ASN
A
306
31.740
76.830
53.499
1.00
13.44
6


2437
O
ASN
A
306
30.672
77.409
53.225
1.00
13.40
8


2438
CB
ASN
A
306
33.438
78.176
54.774
1.00
12.13
6


2439
CG
ASN
A
306
33.863
78.686
56.143
1.00
20.79
6


2440
OD1
ASN
A
306
33.275
78.499
57.233
1.00
23.19
8


2441
ND2
ASN
A
306
34.959
79.477
56.155
1.00
24.17
7


2442
N
MET
A
307
32.405
76.105
52.589
1.00
11.55
7


2443
CA
MET
A
307
31.750
75.915
51.254
1.00
11.38
6


2444
C
MET
A
307
30.590
74.957
51.272
1.00
12.48
6


2445
O
MET
A
307
29.639
75.156
50.512
1.00
13.10
8


2446
CB
MET
A
307
32.849
75.431
50.252
1.00
12.11
6


2447
CG
MET
A
307
32.375
75.462
48.767
1.00
12.14
6


2448
SD
MET
A
307
31.759
77.075
48.246
1.00
12.77
16


2449
CE
MET
A
307
33.282
78.010
48.324
1.00
13.86
6


2450
N
VAL
A
308
30.592
73.951
52.152
1.00
10.38
7


2451
CA
VAL
A
308
29.383
73.136
52.340
1.00
10.10
6


2452
C
VAL
A
308
28.272
74.049
52.822
1.00
11.64
6


2453
O
VAL
A
308
27.153
73.974
52.321
1.00
13.14
8


2454
CB
VAL
A
308
29.712
72.052
53.406
1.00
13.16
6


2455
CG1
VAL
A
308
28.388
71.356
53.770
1.00
14.05
6


2456
CG2
VAL
A
308
30.641
71.038
52.727
1.00
13.08
6


2457
N
ASN
A
309
28.541
74.952
53.784
1.00
12.04
7


2458
CA
ASN
A
309
27.479
75.848
54.264
1.00
12.56
6


2459
C
ASN
A
309
27.073
76.824
53.176
1.00
13.56
6


2460
O
ASN
A
309
25.875
77.017
53.030
1.00
15.38
8


2461
CB
ASN
A
309
27.997
76.680
55.470
1.00
14.00
6


2462
CG
ASN
A
309
28.109
75.761
56.684
1.00
20.56
6


2463
OD1
ASN
A
309
27.432
74.725
56.748
1.00
26.71
8


2464
ND2
ASN
A
309
28.967
76.208
57.595
1.00
21.18
7


2465
N
GLN
A
310
27.970
77.423
52.426
1.00
14.28
7


2466
CA
GLN
A
310
27.549
78.422
51.422
1.00
13.95
6


2467
C
GLN
A
310
26.734
77.754
50.319
1.00
13.50
6


2468
O
GLN
A
310
25.672
78.286
49.942
1.00
14.03
8


2469
CB
GLN
A
310
28.821
79.123
50.869
1.00
14.99
6


2470
CG
GLN
A
310
28.507
80.214
49.859
1.00
21.08
6


2471
CD
GLN
A
310
29.734
81.169
49.819
1.00
21.08
6


2472
OE1
GLN
A
310
30.875
80.762
50.019
1.00
25.61
8


2473
NE2
GLN
A
310
29.417
82.401
49.600
1.00
25.23
7


2474
N
THR
A
311
27.238
76.630
49.792
1.00
11.65
7


2475
CA
THR
A
311
26.432
75.983
48.711
1.00
11.52
6


2476
C
THR
A
311
25.089
75.459
49.257
1.00
12.57
6


2477
O
THR
A
311
24.039
75.572
48.599
1.00
13.81
8


2478
CB
THR
A
311
27.143
74.754
48.142
1.00
12.52
6


2479
OG1
THR
A
311
27.593
73.909
49.194
1.00
13.67
8


2480
CG2
THR
A
311
28.426
75.250
47.375
1.00
14.32
6


2481
N
GLY
A
312
25.096
75.107
50.561
1.00
11.69
7


2482
CA
GLY
A
312
23.812
74.642
51.137
1.00
14.78
6


2483
C
GLY
A
312
22.800
75.792
51.223
1.00
14.32
6


2484
O
GLY
A
312
21.573
75.473
51.276
1.00
16.33
8


2485
N
ASN
A
313
23.320
76.998
51.476
1.00
13.08
7


2486
CA
ASN
A
313
22.392
78.108
51.535
1.00
13.20
6


2487
C
ASN
A
313
21.980
78.575
50.150
1.00
14.89
6


2488
O
ASN
A
313
20.827
79.097
50.014
1.00
20.75
8


2489
CB
ASN
A
313
23.155
79.260
52.204
1.00
19.18
6


2490
CG
ASN
A
313
23.210
79.024
53.718
1.00
30.91
6


2491
OD1
ASN
A
313
22.384
78.310
54.281
1.00
30.04
8


2492
ND2
ASN
A
313
24.152
79.691
54.360
1.00
31.03
7


2493
N
GLU
A
314
22.802
78.394
49.111
1.00
12.83
7


2494
CA
GLU
A
314
22.396
79.060
47.822
1.00
11.95
6


2495
C
GLU
A
314
21.621
78.137
46.889
1.00
13.20
6


2496
O
GLU
A
314
20.733
78.689
46.175
1.00
13.02
8


2497
CB
GLU
A
314
23.753
79.394
47.117
1.00
10.17
6


2498
CG
GLU
A
314
24.503
80.510
47.842
1.00
12.02
6


2499
CD
GLU
A
314
25.715
80.987
46.985
1.00
15.94
6


2500
OE1
GLU
A
314
26.285
80.206
46.232
1.00
15.22
8


2501
OE2
GLU
A
314
26.164
82.100
47.284
1.00
24.00
8


2502
N
TYR
A
315
21.992
76.840
46.892
1.00
11.76
7


2503
CA
TYR
A
315
21.297
75.979
45.885
1.00
10.85
6


2504
C
TYR
A
315
20.032
75.368
46.506
1.00
12.73
6


2505
O
TYR
A
315
20.140
74.648
47.510
1.00
12.47
8


2506
CB
TYR
A
315
22.265
74.838
45.494
1.00
12.39
6


2507
CG
TYR
A
315
23.437
75.394
44.699
1.00
10.41
6


2508
CD1
TYR
A
315
23.270
75.610
43.316
1.00
11.23
6


2509
CD2
TYR
A
315
24.613
75.785
45.297
1.00
12.52
6


2510
CE1
TYR
A
315
24.333
76.166
42.586
1.00
12.92
6


2511
CE2
TYR
A
315
25.686
76.350
44.563
1.00
10.90
6


2512
CZ
TYR
A
315
25.510
76.507
43.187
1.00
12.76
6


2513
OH
TYR
A
315
26.595
77.056
42.517
1.00
13.74
8


2514
N
LYS
A
316
18.895
75.634
45.861
1.00
11.54
7


2515
CA
LYS
A
316
17.638
75.080
46.395
1.00
14.39
6


2516
C
LYS
A
316
17.578
73.555
46.454
1.00
15.27
6


2517
O
LYS
A
316
17.175
72.963
47.475
1.00
14.60
8


2518
CB
LYS
A
316
16.496
75.595
45.485
1.00
14.77
6


2519
CG
LYS
A
316
15.139
75.068
46.091
1.00
18.12
6


2520
CD
LYS
A
316
13.982
75.856
45.565
1.00
22.24
6


2521
CE
LYS
A
316
12.683
75.166
46.061
1.00
19.23
6


2522
NZ
LYS
A
316
12.432
75.635
47.468
1.00
22.20
7


2523
N
TYR
A
317
18.227
72.953
45.457
1.00
13.10
7


2524
CA
TYR
A
317
18.316
71.483
45.445
1.00
11.39
6


2525
C
TYR
A
317
19.805
71.123
45.506
1.00
10.31
6


2526
O
TYR
A
317
20.410
70.491
44.637
1.00
12.52
8


2527
CB
TYR
A
317
17.652
70.893
44.157
1.00
12.53
6


2528
CG
TYR
A
317
16.221
71.387
44.004
1.00
13.61
6


2529
CD1
TYR
A
317
15.272
70.932
44.915
1.00
14.65
6


2530
CD2
TYR
A
317
15.800
72.280
43.030
1.00
14.34
6


2531
CE1
TYR
A
317
13.938
71.366
44.811
1.00
13.78
6


2532
CE2
TYR
A
317
14.511
72.767
42.890
1.00
12.10
6


2533
CZ
TYR
A
317
13.604
72.246
43.832
1.00
15.19
6


2534
OH
TYR
A
317
12.275
72.682
43.733
1.00
14.53
8


2535
N
LYS
A
318
20.375
71.463
46.702
1.00
11.46
7


2536
CA
LYS
A
318
21.821
71.130
46.865
1.00
10.64
6


2537
C
LYS
A
318
22.053
69.651
46.865
1.00
10.21
6


2538
O
LYS
A
318
23.133
69.145
46.529
1.00
10.36
8


2539
CB
LYS
A
318
22.408
71.772
48.141
1.00
9.85
6


2540
CG
LYS
A
318
21.843
71.211
49.451
1.00
13.57
6


2541
CD
LYS
A
318
20.619
72.105
49.820
1.00
19.29
6


2542
CE
LYS
A
318
20.309
72.064
51.345
1.00
19.13
6


2543
NZ
LYS
A
318
19.066
72.819
51.636
1.00
20.57
7


2544
N
GLU
A
319
21.044
68.796
47.174
1.00
9.32
7


2545
CA
GLU
A
319
21.217
67.359
47.096
1.00
11.07
6


2546
C
GLU
A
319
21.164
66.802
45.667
1.00
12.26
6


2547
O
GLU
A
319
21.469
65.627
45.504
1.00
11.85
8


2548
CB
GLU
A
319
20.021
66.636
47.827
1.00
12.74
6


2549
CG
GLU
A
319
19.998
67.027
49.320
1.00
15.35
6


2550
CD
GLU
A
319
19.346
68.353
49.656
1.00
19.53
6


2551
OE1
GLU
A
319
18.645
68.996
48.818
1.00
14.20
8


2552
OE2
GLU
A
319
19.503
68.829
50.839
1.00
14.17
8


2553
N
ASN
A
320
21.033
67.681
44.664
1.00
9.38
7


2554
CA
ASN
A
320
21.155
67.324
43.285
1.00
9.77
6


2555
C
ASN
A
320
22.454
67.819
42.636
1.00
12.36
6


2556
O
ASN
A
320
22.736
67.591
41.442
1.00
10.93
8


2557
CB
ASN
A
320
19.995
67.901
42.402
1.00
10.57
6


2558
CG
ASN
A
320
18.660
67.290
42.784
1.00
14.03
6


2559
OD1
ASN
A
320
18.619
66.275
43.445
1.00
13.17
8


2560
ND2
ASN
A
320
17.558
67.901
42.323
1.00
10.64
7


2561
N
LEU
A
321
23.285
68.499
43.422
1.00
10.68
7


2562
CA
LEU
A
321
24.610
68.918
42.896
1.00
10.60
6


2563
C
LEU
A
321
25.415
67.643
42.685
1.00
10.70
6


2564
O
LEU
A
321
25.448
66.685
43.452
1.00
11.96
8


2565
CB
LEU
A
321
25.299
69.733
44.024
1.00
9.53
6


2566
CG
LEU
A
321
24.761
71.176
44.124
1.00
9.68
6


2567
CD1
LEU
A
321
25.310
71.820
45.415
1.00
13.05
6


2568
CD2
LEU
A
321
25.183
72.064
42.930
1.00
9.85
6


2569
N
ILE
A
322
26.185
67.671
41.566
1.00
9.04
7


2570
CA
ILE
A
322
27.014
66.478
41.265
1.00
9.68
6


2571
C
ILE
A
322
28.477
66.821
41.584
1.00
11.13
6


2572
O
ILE
A
322
29.071
67.716
40.935
1.00
10.40
8


2573
CB
ILE
A
322
26.872
66.118
39.767
1.00
10.10
6


2574
CG1
ILE
A
322
25.387
65.842
39.384
1.00
9.96
6


2575
CG2
ILE
A
322
27.793
64.954
39.396
1.00
12.80
6


2576
CD1
ILE
A
322
24.773
64.698
40.258
1.00
9.05
6


2577
N
THR
A
323
29.019
66.133
42.594
1.00
9.87
7


2578
CA
THR
A
323
30.333
66.524
43.130
1.00
8.82
6


2579
C
THR
A
323
31.433
65.704
42.453
1.00
9.73
6


2580
O
THR
A
323
31.218
64.628
41.902
1.00
10.64
8


2581
CB
THR
A
323
30.364
66.302
44.652
1.00
10.77
6


2582
OG1
THR
A
323
30.009
64.919
44.887
1.00
10.73
8


2583
CG2
THR
A
323
29.314
67.237
45.318
1.00
10.06
6


2584
N
PHE
A
324
32.660
66.234
42.559
1.00
9.44
7


2585
CA
PHE
A
324
33.784
65.582
41.880
1.00
10.80
6


2586
C
PHE
A
324
35.086
66.205
42.385
1.00
9.58
6


2587
O
PHE
A
324
35.086
67.375
42.805
1.00
10.73
8


2588
CB
PHE
A
324
33.716
65.698
40.286
1.00
9.57
6


2589
CG
PHE
A
324
33.638
67.122
39.817
1.00
9.02
6


2590
CD1
PHE
A
324
32.421
67.817
39.810
1.00
11.94
6


2591
CD2
PHE
A
324
34.798
67.746
39.354
1.00
11.07
6


2592
CE1
PHE
A
324
32.321
69.142
39.380
1.00
11.10
6


2593
CE2
PHE
A
324
34.683
69.083
38.926
1.00
11.33
6


2594
CZ
PHE
A
324
33.498
69.788
38.931
1.00
13.68
6


2595
N
ILE
A
325
36.137
65.385
42.285
1.00
9.28
7


2596
CA
ILE
A
325
37.469
65.879
42.710
1.00
9.24
6


2597
C
ILE
A
325
38.277
66.277
41.480
1.00
9.67
6


2598
O
ILE
A
325
39.255
67.116
41.645
1.00
10.76
8


2599
CB
AILE
A
325
38.211
64.869
43.596
0.60
11.75
6


2600
CG1
AILE
A
325
38.779
63.705
42.764
0.60
10.90
6


2601
CG2
AILE
A
325
37.288
64.325
44.695
0.60
12.60
6


2602
CD1
AILE
A
325
39.550
62.693
43.585
0.60
10.36
6


2599
CB
BILE
A
325
38.139
64.627
43.330
0.40
12.90
6


2600
CG1
BILE
A
325
37.386
64.127
44.568
0.40
10.36
6


2601
CG2
BILE
A
325
39.604
64.862
43.640
0.40
10.82
6


2602
CD1
BILE
A
325
37.571
62.651
44.847
0.40
13.69
6


2603
N
ASP
A
326
38.028
65.680
40.350
1.00
9.63
7


2604
CA
ASP
A
326
38.762
65.987
39.107
1.00
10.15
6


2605
C
ASP
A
326
37.813
65.625
37.964
1.00
11.71
6


2606
O
ASP
A
326
36.678
65.102
38.209
1.00
10.86
8


2607
CB
ASP
A
326
40.149
65.323
39.050
1.00
12.00
6


2608
CG
ASP
A
326
40.166
63.807
39.089
1.00
12.49
6


2609
OD1
ASP
A
326
39.080
63.207
38.870
1.00
12.13
8


2610
OD2
ASP
A
326
41.228
63.200
39.354
1.00
11.72
8


2611
N
ASN
A
327
38.279
65.749
36.731
1.00
9.05
7


2612
CA
ASN
A
327
37.486
65.359
35.569
1.00
10.52
6


2613
C
ASN
A
327
38.334
65.556
34.352
1.00
9.98
6


2614
O
ASN
A
327
39.573
65.686
34.478
1.00
11.19
8


2615
CB
ASN
A
327
36.177
66.162
35.432
1.00
11.56
6


2616
CG
ASN
A
327
36.351
67.636
35.121
1.00
12.65
6


2617
OD1
ASN
A
327
37.355
68.106
34.634
1.00
11.48
8


2618
ND2
ASN
A
327
35.314
68.376
35.463
1.00
8.99
7


2619
N
HIS
A
328
37.802
65.385
33.178
1.00
9.23
7


2620
CA
HIS
A
328
38.599
65.393
31.958
1.00
11.14
6


2621
C
HIS
A
328
39.037
66.779
31.471
1.00
11.62
6


2622
O
HIS
A
328
39.744
66.836
30.450
1.00
11.55
8


2623
CB
HIS
A
328
37.726
64.740
30.844
1.00
10.61
6


2624
CG
HIS
A
328
36.511
65.577
30.526
1.00
9.76
6


2625
ND1
HIS
A
328
35.652
65.938
31.572
1.00
11.58
7


2626
CD2
HIS
A
328
36.012
66.093
29.370
1.00
11.35
6


2627
CE1
HIS
A
328
34.648
66.668
31.066
1.00
12.44
6


2628
NE2
HIS
A
328
34.853
66.756
29.733
1.00
11.88
7


2629
N
ASP
A
329
38.746
67.808
32.263
1.00
8.48
7


2630
CA
ASP
A
329
39.181
69.155
31.893
1.00
9.03
6


2631
C
ASP
A
329
40.073
69.793
32.960
1.00
12.15
6


2632
O
ASP
A
329
40.388
71.012
32.883
1.00
12.94
8


2633
CB
ASP
A
329
37.955
70.091
31.837
1.00
11.03
6


2634
CG
ASP
A
329
37.069
69.815
30.620
1.00
11.95
6


2635
OD1
ASP
A
329
37.477
69.188
29.617
1.00
11.39
8


2636
OD2
ASP
A
329
35.891
70.243
30.712
1.00
11.11
8


2637
N
MET
A
330
40.568
68.936
33.857
1.00
11.19
7


2638
CA
MET
A
330
41.533
69.433
34.857
1.00
9.36
6


2639
C
MET
A
330
42.537
68.330
35.211
1.00
9.51
6


2640
O
MET
A
330
42.224
67.156
34.927
1.00
11.47
8


2641
CB
MET
A
330
40.858
70.015
36.111
1.00
13.17
6


2642
CG
MET
A
330
40.005
68.973
36.857
1.00
11.23
6


2643
SD
MET
A
330
39.087
69.743
38.236
1.00
12.96
16


2644
CE
MET
A
330
37.923
70.706
37.364
1.00
13.78
6


2645
N
SER
A
331
43.702
68.680
35.765
1.00
10.04
7


2646
CA
SER
A
331
44.650
67.618
36.030
1.00
9.86
6


2647
C
SER
A
331
44.130
66.557
37.020
1.00
11.24
6


2648
O
SER
A
331
43.295
66.892
37.858
1.00
11.71
8


2649
CB
SER
A
331
46.009
68.207
36.629
1.00
11.21
6


2650
OG
SER
A
331
45.623
68.981
37.793
1.00
14.33
8


2651
N
ARG
A
332
44.540
65.321
36.833
1.00
11.49
7


2652
CA
ARG
A
332
44.057
64.272
37.749
1.00
11.49
6


2653
C
ARG
A
332
44.499
64.603
39.189
1.00
11.63
6


2654
O
ARG
A
332
45.591
65.103
39.412
1.00
12.21
8


2655
CB
ARG
A
332
44.667
62.914
37.387
1.00
13.45
6


2656
CG
ARG
A
332
43.997
62.516
36.049
1.00
16.61
6


2657
CD
ARG
A
332
43.560
61.101
36.061
1.00
20.26
6


2658
NE
ARG
A
332
43.017
60.592
34.777
1.00
15.50
7


2659
CZ
ARG
A
332
41.965
59.753
34.882
1.00
12.48
6


2660
NH1
ARG
A
332
41.546
59.388
36.094
1.00
10.61
7


2661
NH2
ARG
A
332
41.440
59.251
33.741
1.00
10.74
7


2662
N
PHE
A
333
43.654
64.168
40.153
1.00
9.55
7


2663
CA
PHE
A
333
44.019
64.431
41.533
1.00
10.54
6


2664
C
PHE
A
333
45.461
63.976
41.852
1.00
12.40
6


2665
O
PHE
A
333
46.170
64.709
42.515
1.00
13.01
8


2666
CB
PHE
A
333
43.007
63.676
42.481
1.00
11.67
6


2667
CG
PHE
A
333
43.365
64.006
43.958
1.00
12.76
6


2668
CD1
PHE
A
333
44.315
63.230
44.587
1.00
15.62
6


2669
CD2
PHE
A
333
42.718
65.041
44.556
1.00
18.86
6


2670
CE1
PHE
A
333
44.651
63.513
45.905
1.00
19.61
6


2671
CE2
PHE
A
333
43.014
65.342
45.906
1.00
15.77
6


2672
CZ
PHE
A
333
43.978
64.561
46.492
1.00
16.46
6


2673
N
LEU
A
334
45.825
62.763
41.462
1.00
10.49
7


2674
CA
LEU
A
334
47.183
62.257
41.835
1.00
14.60
6


2675
C
LEU
A
334
48.303
63.035
41.167
1.00
12.74
6


2676
O
LEU
A
334
49.456
62.864
41.627
1.00
13.05
8


2677
CB
LEU
A
334
47.269
60.748
41.476
1.00
13.94
6


2678
CG
LEU
A
334
46.461
59.910
42.484
1.00
13.29
6


2679
CD1
LEU
A
334
46.488
58.447
41.969
1.00
14.98
6


2680
CD2
LEU
A
334
47.045
59.905
43.909
1.00
13.51
6


2681
N
SER
A
335
48.014
63.857
40.144
1.00
11.98
7


2682
CA
SER
A
335
49.117
64.732
39.639
1.00
11.30
6


2683
C
SER
A
335
49.115
66.026
40.421
1.00
15.22
6


2684
O
SER
A
335
50.159
66.664
40.438
1.00
18.21
8


2685
CB
SER
A
335
48.843
65.113
38.179
1.00
14.88
6


2686
OG
SER
A
335
49.221
63.920
37.436
1.00
17.27
8


2687
N
VAL
A
336
48.041
66.315
41.169
1.00
11.92
7


2688
CA
VAL
A
336
48.092
67.455
42.094
1.00
14.73
6


2689
C
VAL
A
336
48.805
67.064
43.392
1.00
15.20
6


2690
O
VAL
A
336
49.593
67.825
43.962
1.00
16.13
8


2691
CB
VAL
A
336
46.691
67.970
42.447
1.00
14.37
6


2692
CG1
VAL
A
336
46.646
69.120
43.441
1.00
16.05
6


2693
CG2
VAL
A
336
45.970
68.386
41.154
1.00
18.05
6


2694
N
ASN
A
337
48.525
65.866
43.852
1.00
13.19
7


2695
CA
ASN
A
337
49.114
65.389
45.132
1.00
12.41
6


2696
C
ASN
A
337
49.153
63.870
44.976
1.00
12.10
6


2697
O
ASN
A
337
48.082
63.178
44.865
1.00
11.76
8


2698
CB
ASN
A
337
48.141
65.756
46.272
1.00
11.12
6


2699
CG
ASN
A
337
48.570
65.206
47.621
1.00
13.14
6


2700
OD1
ASN
A
337
49.572
64.466
47.738
1.00
12.58
8


2701
ND2
ASN
A
337
47.865
65.514
48.694
1.00
11.19
7


2702
N
SER
A
338
50.364
63.275
44.939
1.00
9.71
7


2703
CA
SER
A
338
50.477
61.849
44.747
1.00
13.36
6


2704
C
SER
A
338
50.257
60.983
45.993
1.00
11.43
6


2705
O
SER
A
338
50.294
59.759
45.858
1.00
14.29
8


2706
CB
SER
A
338
51.884
61.461
44.225
1.00
17.19
6


2707
OG
SER
A
338
52.871
61.883
45.154
1.00
17.12
8


2708
N
ASN
A
339
49.847
61.610
47.095
1.00
13.33
7


2709
CA
ASN
A
339
49.601
60.788
48.297
1.00
12.26
6


2710
C
ASN
A
339
48.267
60.043
48.193
1.00
12.82
6


2711
O
ASN
A
339
47.246
60.732
48.134
1.00
12.55
8


2712
CB
ASN
A
339
49.554
61.769
49.485
1.00
10.37
6


2713
CG
ASN
A
339
49.516
60.949
50.787
1.00
18.65
6


2714
OD1
ASN
A
339
48.403
60.509
51.110
1.00
19.28
8


2715
ND2
ASN
A
339
50.648
60.809
51.502
1.00
18.28
7


2716
N
LYS
A
340
48.283
58.708
48.148
1.00
12.73
7


2717
CA
LYS
A
340
47.008
58.021
47.941
1.00
11.20
6


2718
C
LYS
A
340
46.077
58.134
49.122
1.00
13.56
6


2719
O
LYS
A
340
44.859
58.103
48.906
1.00
12.11
8


2720
CB
LYS
A
340
47.345
56.523
47.665
1.00
12.59
6


2721
CG
LYS
A
340
48.006
56.401
46.279
1.00
12.90
6


2722
CD
LYS
A
340
48.318
54.903
46.055
1.00
18.47
6


2723
CE
LYS
A
340
48.937
54.658
44.699
1.00
18.65
6


2724
NZ
LYS
A
340
50.377
55.099
44.564
1.00
22.63
7


2725
N
ALA
A
341
46.585
58.363
50.345
1.00
12.85
7


2726
CA
ALA
A
341
45.626
58.557
51.453
1.00
14.45
6


2727
C
ALA
A
341
44.835
59.830
51.239
1.00
13.48
6


2728
O
ALA
A
341
43.661
59.855
51.568
1.00
11.31
8


2729
CB
ALA
A
341
46.346
58.628
52.806
1.00
15.23
6


2730
N
ASN
A
342
45.459
60.911
50.731
1.00
10.37
7


2731
CA
ASN
A
342
44.717
62.126
50.470
1.00
10.38
6


2732
C
ASN
A
342
43.687
61.897
49.359
1.00
10.62
6


2733
O
ASN
A
342
42.560
62.477
49.439
1.00
12.01
8


2734
CB
ASN
A
342
45.708
63.276
50.141
1.00
11.46
6


2735
CG
ASN
A
342
46.519
63.737
51.351
1.00
13.17
6


2736
OD1
ASN
A
342
47.710
64.044
51.127
1.00
12.82
8


2737
ND2
ASN
A
342
45.888
63.859
52.516
1.00
12.05
7


2738
N
LEU
A
343
44.001
61.049
48.344
1.00
10.66
7


2739
CA
LEU
A
343
42.953
60.715
47.377
1.00
10.18
6


2740
C
LEU
A
343
41.810
59.935
48.039
1.00
12.28
6


2741
O
LEU
A
343
40.635
60.288
47.781
1.00
11.44
8


2742
CB
LEU
A
343
43.581
59.854
46.229
1.00
10.02
6


2743
CG
LEU
A
343
42.546
59.182
45.295
1.00
10.27
6


2744
CD1
LEU
A
343
41.847
60.288
44.550
1.00
13.59
6


2745
CD2
LEU
A
343
43.309
58.294
44.283
1.00
12.64
6


2746
N
HIS
A
344
42.173
58.977
48.898
1.00
11.47
7


2747
CA
HIS
A
344
41.093
58.185
49.570
1.00
11.49
6


2748
C
HIS
A
344
40.189
59.122
50.370
1.00
13.40
6


2749
O
HIS
A
344
38.951
58.916
50.500
1.00
12.11
8


2750
CB
HIS
A
344
41.731
57.075
50.439
1.00
9.09
6


2751
CG
HIS
A
344
42.520
56.064
49.656
1.00
10.04
6


2752
ND1
HIS
A
344
43.612
55.436
50.199
1.00
12.75
7


2753
CD2
HIS
A
344
42.363
55.580
48.370
1.00
11.63
6


2754
CE1
HIS
A
344
44.114
54.612
49.289
1.00
10.72
6


2755
NE2
HIS
A
344
43.393
54.662
48.157
1.00
12.61
7


2756
N
GLN
A
345
40.834
60.100
51.024
1.00
10.53
7


2757
CA
GLN
A
345
40.049
61.036
51.831
1.00
10.43
6


2758
C
GLN
A
345
39.077
61.899
51.008
1.00
10.42
6


2759
O
GLN
A
345
37.888
62.067
51.324
1.00
10.38
8


2760
CB
GLN
A
345
40.996
62.012
52.564
1.00
11.01
6


2761
CG
GLN
A
345
41.847
61.258
53.641
1.00
9.73
6


2762
CD
GLN
A
345
43.142
62.041
53.786
1.00
10.78
6


2763
OE1
GLN
A
345
43.232
63.196
53.279
1.00
12.69
8


2764
NE2
GLN
A
345
44.170
61.448
54.428
1.00
12.87
7


2765
N
ALA
A
346
39.590
62.418
49.883
1.00
11.81
7


2766
CA
ALA
A
346
38.762
63.250
48.987
1.00
10.44
6


2767
C
ALA
A
346
37.604
62.379
48.462
1.00
11.17
6


2768
O
ALA
A
346
36.473
62.887
48.339
1.00
11.30
8


2769
CB
ALA
A
346
39.595
63.827
47.829
1.00
9.34
6


2770
N
LEU
A
347
37.895
61.107
48.079
1.00
12.34
7


2771
CA
LEU
A
347
36.809
60.261
47.589
1.00
11.12
6


2772
C
LEU
A
347
35.777
59.999
48.733
1.00
9.98
6


2773
O
LEU
A
347
34.567
60.087
48.466
1.00
11.63
8


2774
CB
LEU
A
347
37.367
58.885
47.187
1.00
11.26
6


2775
CG
LEU
A
347
38.146
58.913
45.840
1.00
14.75
6


2776
CD1
LEU
A
347
38.829
57.574
45.530
1.00
13.09
6


2777
CD2
LEU
A
347
37.132
59.197
44.722
1.00
15.41
6


2778
N
ALA
A
348
36.304
59.764
49.955
1.00
10.14
7


2779
CA
ALA
A
348
35.269
59.479
51.003
1.00
10.67
6


2780
C
ALA
A
348
34.432
60.725
51.273
1.00
12.22
6


2781
O
ALA
A
348
33.231
60.600
51.534
1.00
11.88
8


2782
CB
ALA
A
348
36.008
59.130
52.310
1.00
10.16
6


2783
N
PHE
A
349
35.026
61.922
51.160
1.00
10.08
7


2784
CA
PHE
A
349
34.258
63.149
51.330
1.00
10.26
6


2785
C
PHE
A
349
33.120
63.213
50.282
1.00
9.67
6


2786
O
PHE
A
349
31.942
63.422
50.717
1.00
11.25
8


2787
CB
PHE
A
349
35.270
64.348
51.200
1.00
9.92
6


2788
CG
PHE
A
349
34.515
65.659
51.357
1.00
8.60
6


2789
CD1
PHE
A
349
34.016
66.030
52.605
1.00
11.80
6


2790
CD2
PHE
A
349
34.340
66.526
50.249
1.00
11.51
6


2791
CE1
PHE
A
349
33.296
67.247
52.714
1.00
11.90
6


2792
CE2
PHE
A
349
33.638
67.709
50.409
1.00
10.49
6


2793
CZ
PHE
A
349
33.069
68.068
51.660
1.00
12.88
6


2794
N
ILE
A
350
33.411
63.030
49.005
1.00
8.49
7


2795
CA
ILE
A
350
32.257
63.124
48.089
1.00
10.97
6


2796
C
ILE
A
350
31.361
61.899
48.158
1.00
11.48
6


2797
O
ILE
A
350
30.139
62.115
47.958
1.00
11.30
8


2798
CB
ILE
A
350
32.676
63.380
46.605
1.00
11.26
6


2799
CG1
ILE
A
350
33.451
62.279
45.983
1.00
11.16
6


2800
CG2
ILE
A
350
33.429
64.742
46.556
1.00
12.07
6


2801
CD1
ILE
A
350
33.748
62.454
44.463
1.00
9.59
6


2802
N
LEU
A
351
31.873
60.731
48.548
1.00
9.78
7


2803
CA
LEU
A
351
30.930
59.601
48.655
1.00
9.90
6


2804
C
LEU
A
351
29.956
59.782
49.809
1.00
11.10
6


2805
O
LEU
A
351
28.888
59.122
49.698
1.00
11.60
8


2806
CB
LEU
A
351
31.813
58.349
48.879
1.00
11.35
6


2807
CG
LEU
A
351
32.492
57.907
47.564
1.00
10.64
6


2808
CD1
LEU
A
351
33.679
56.944
47.822
1.00
12.51
6


2809
CD2
LEU
A
351
31.500
57.262
46.595
1.00
13.68
6


2810
N
THR
A
352
30.267
60.590
50.850
1.00
9.74
7


2811
CA
THR
A
352
29.310
60.657
51.960
1.00
11.34
6


2812
C
THR
A
352
28.658
62.022
52.149
1.00
12.86
6


2813
O
THR
A
352
27.822
62.214
53.022
1.00
13.09
8


2814
CB
THR
A
352
30.099
60.375
53.296
1.00
11.44
6


2815
OG1
THR
A
352
31.244
61.234
53.420
1.00
11.08
8


2816
CG2
THR
A
352
30.607
58.939
53.324
1.00
9.52
6


2817
N
SER
A
353
29.100
63.028
51.368
1.00
10.03
7


2818
CA
SER
A
353
28.530
64.357
51.432
1.00
10.73
6


2819
C
SER
A
353
27.299
64.574
50.536
1.00
9.28
6


2820
O
SER
A
353
26.990
63.688
49.726
1.00
13.31
8


2821
CB
SER
A
353
29.607
65.403
51.012
1.00
12.91
6


2822
OG
SER
A
353
30.626
65.402
52.045
1.00
12.40
8


2823
N
ARG
A
354
26.646
65.741
50.754
1.00
10.25
7


2824
CA
ARG
A
354
25.379
65.920
50.024
1.00
10.03
6


2825
C
ARG
A
354
25.611
65.997
48.533
1.00
10.84
6


2826
O
ARG
A
354
26.704
66.369
48.085
1.00
11.59
8


2827
CB
ARG
A
354
24.669
67.185
50.545
1.00
10.71
6


2828
CG
ARG
A
354
25.099
68.504
49.838
1.00
11.61
6


2829
CD
ARG
A
354
26.535
68.853
50.229
1.00
12.49
6


2830
NE
ARG
A
354
26.964
70.130
49.548
1.00
12.69
7


2831
CZ
ARG
A
354
27.455
70.157
48.317
1.00
12.54
6


2832
NH1
ARG
A
354
27.638
69.113
47.497
1.00
12.15
7


2833
NH2
ARG
A
354
27.867
71.370
47.894
1.00
11.14
7


2834
N
GLY
A
355
24.542
65.707
47.780
1.00
11.00
7


2835
CA
GLY
A
355
24.624
65.584
46.318
1.00
10.49
6


2836
C
GLY
A
355
25.149
64.196
45.929
1.00
13.18
6


2837
O
GLY
A
355
25.154
63.299
46.788
1.00
15.74
8


2838
N
THR
A
356
25.546
64.007
44.688
1.00
10.24
7


2839
CA
THR
A
356
25.885
62.648
44.202
1.00
10.01
6


2840
C
THR
A
356
27.279
62.722
43.581
1.00
10.67
6


2841
O
THR
A
356
27.512
63.621
42.769
1.00
10.61
8


2842
CB
THR
A
356
24.908
62.301
43.066
1.00
13.21
6


2843
OG1
THR
A
356
23.622
62.052
43.698
1.00
11.93
8


2844
CG2
THR
A
356
25.332
60.948
42.433
1.00
11.53
6


2845
N
PRO
A
357
28.184
61.868
43.967
1.00
10.42
7


2846
CA
PRO
A
357
29.564
61.929
43.493
1.00
10.52
6


2847
C
PRO
A
357
29.689
61.366
42.092
1.00
11.14
6


2848
O
PRO
A
357
29.074
60.379
41.752
1.00
11.48
8


2849
CB
PRO
A
357
30.340
61.021
44.494
1.00
10.57
6


2850
CG
PRO
A
357
29.245
59.991
44.834
1.00
11.58
6


2851
CD
PRO
A
357
27.914
60.760
44.914
1.00
10.88
6


2852
N
SER
A
358
30.508
62.051
41.293
1.00
8.23
7


2853
CA
SER
A
358
31.003
61.558
40.001
1.00
9.73
6


2854
C
SER
A
358
32.509
61.272
40.069
1.00
10.56
6


2855
O
SER
A
358
33.323
62.183
40.331
1.00
11.97
8


2856
CB
SER
A
358
30.768
62.634
38.921
1.00
12.36
6


2857
OG
SER
A
358
31.301
62.159
37.653
1.00
13.42
8


2858
N
ILE
A
359
32.813
59.992
39.915
1.00
9.37
7


2859
CA
ILE
A
359
34.234
59.557
39.927
1.00
9.47
6


2860
C
ILE
A
359
34.703
59.350
38.492
1.00
12.04
6


2861
O
ILE
A
359
34.101
58.730
37.647
1.00
11.59
8


2862
CB
ILE
A
359
34.313
58.205
40.671
1.00
11.89
6


2863
CG1
ILE
A
359
33.858
58.478
42.145
1.00
14.90
6


2864
CG2
ILE
A
359
35.727
57.624
40.550
1.00
12.39
6


2865
CD1
ILE
A
359
33.936
57.155
42.925
1.00
22.17
6


2866
N
TYR
A
360
35.810
60.088
38.176
1.00
9.52
7


2867
CA
TYR
A
360
36.364
60.076
36.807
1.00
8.41
6


2868
C
TYR
A
360
37.027
58.709
36.636
1.00
9.86
6


2869
O
TYR
A
360
37.780
58.227
37.510
1.00
10.81
8


2870
CB
TYR
A
360
37.399
61.247
36.796
1.00
9.51
6


2871
CG
TYR
A
360
37.935
61.510
35.363
1.00
9.64
6


2872
CD1
TYR
A
360
37.191
61.428
34.206
1.00
10.11
6


2873
CD2
TYR
A
360
39.279
61.882
35.294
1.00
9.54
6


2874
CE1
TYR
A
360
37.818
61.650
32.960
1.00
10.79
6


2875
CE2
TYR
A
360
39.927
62.148
34.066
1.00
10.73
6


2876
CZ
TYR
A
360
39.153
62.044
32.937
1.00
11.36
6


2877
OH
TYR
A
360
39.712
62.217
31.670
1.00
10.12
8


2878
N
TYR
A
361
36.808
58.146
35.418
1.00
10.09
7


2879
CA
TYR
A
361
37.279
56.773
35.210
1.00
10.66
6


2880
C
TYR
A
361
38.748
56.616
35.593
1.00
11.54
6


2881
O
TYR
A
361
39.556
57.488
35.297
1.00
11.37
8


2882
CB
TYR
A
361
37.051
56.287
33.730
1.00
9.71
6


2883
CG
TYR
A
361
38.086
56.846
32.765
1.00
10.50
6


2884
CD1
TYR
A
361
37.937
58.150
32.332
1.00
10.91
6


2885
CD2
TYR
A
361
39.176
56.052
32.383
1.00
10.62
6


2886
CE1
TYR
A
361
38.913
58.715
31.480
1.00
10.92
6


2887
CE2
TYR
A
361
40.155
56.601
31.520
1.00
9.87
6


2888
CZ
TYR
A
361
39.988
57.930
31.139
1.00
12.35
6


2889
OH
TYR
A
361
40.982
58.482
30.297
1.00
11.60
8


2890
N
GLY
A
362
39.069
55.475
36.171
1.00
11.61
7


2891
CA
GLY
A
362
40.454
55.099
36.513
1.00
12.01
6


2892
C
GLY
A
362
40.997
55.744
37.772
1.00
11.04
6


2893
O
GLY
A
362
42.168
55.431
38.093
1.00
12.36
8


2894
N
THR
A
363
40.222
56.614
38.446
1.00
12.35
7


2895
CA
THR
A
363
40.676
57.169
39.736
1.00
11.24
6


2896
C
THR
A
363
41.033
56.009
40.693
1.00
11.33
6


2897
O
THR
A
363
42.072
56.074
41.376
1.00
12.29
8


2898
CB
THR
A
363
39.528
57.957
40.387
1.00
11.07
6


2899
OG1
THR
A
363
39.248
59.065
39.494
1.00
12.04
8


2900
CG2
THR
A
363
40.024
58.554
41.730
1.00
11.22
6


2901
N
GLU
A
364
40.221
54.961
40.670
1.00
11.97
7


2902
CA
GLU
A
364
40.379
53.835
41.610
1.00
11.29
6


2903
C
GLU
A
364
41.520
52.938
41.198
1.00
12.77
6


2904
O
GLU
A
364
41.845
51.968
41.915
1.00
14.39
8


2905
CB
GLU
A
364
38.994
53.093
41.712
1.00
10.27
6


2906
CG
GLU
A
364
38.652
52.265
40.469
1.00
11.76
6


2907
CD
GLU
A
364
38.139
53.001
39.248
1.00
15.28
6


2908
OE1
GLU
A
364
38.072
54.257
39.239
1.00
13.43
8


2909
OE2
GLU
A
364
37.813
52.343
38.247
1.00
11.75
8


2910
N
GLN
A
365
42.046
53.105
39.993
1.00
10.80
7


2911
CA
GLN
A
365
43.256
52.398
39.542
1.00
11.28
6


2912
C
GLN
A
365
44.462
53.305
39.629
1.00
12.82
6


2913
O
GLN
A
365
45.606
52.953
39.219
1.00
12.70
8


2914
CB
GLN
A
365
43.138
51.923
38.088
1.00
12.65
6


2915
CG
GLN
A
365
41.964
50.951
37.828
1.00
9.91
6


2916
CD
GLN
A
365
42.043
49.690
38.693
1.00
14.70
6


2917
OE1
GLN
A
365
41.016
49.200
39.269
1.00
17.54
8


2918
NE2
GLN
A
365
43.204
49.142
38.847
1.00
12.05
7


2919
N
TYR
A
366
44.317
54.426
40.333
1.00
10.84
7


2920
CA
TYR
A
366
45.443
55.357
40.582
1.00
10.38
6


2921
C
TYR
A
366
46.039
55.921
39.308
1.00
13.18
6


2922
O
TYR
A
366
47.248
56.182
39.205
1.00
14.90
8


2923
CB
TYR
A
366
46.547
54.753
41.514
1.00
11.57
6


2924
CG
TYR
A
366
45.872
54.326
42.813
1.00
11.25
6


2925
CD1
TYR
A
366
45.270
55.215
43.707
1.00
14.66
6


2926
CD2
TYR
A
366
45.942
52.977
43.139
1.00
13.34
6


2927
CE1
TYR
A
366
44.653
54.747
44.882
1.00
15.95
6


2928
CE2
TYR
A
366
45.361
52.494
44.332
1.00
14.89
6


2929
CZ
TYR
A
366
44.711
53.395
45.154
1.00
12.93
6


2930
OH
TYR
A
366
44.118
52.939
46.302
1.00
12.26
8


2931
N
MET
A
367
45.147
56.315
38.357
1.00
12.15
7


2932
CA
MET
A
367
45.700
56.998
37.181
1.00
10.89
6


2933
C
MET
A
367
46.195
58.365
37.586
1.00
14.58
6


2934
O
MET
A
367
45.501
59.019
38.383
1.00
14.18
8


2935
CB
MET
A
367
44.602
57.163
36.115
1.00
11.31
6


2936
CG
MET
A
367
44.316
55.810
35.397
1.00
11.19
6


2937
SD
MET
A
367
42.994
56.012
34.139
1.00
13.40
16


2938
CE
MET
A
367
43.986
56.859
32.873
1.00
13.82
6


2939
N
ALA
A
368
47.271
58.817
36.904
1.00
12.72
7


2940
CA
ALA
A
368
47.689
60.193
37.152
1.00
14.30
6


2941
C
ALA
A
368
47.745
60.849
35.754
1.00
14.06
6


2942
O
ALA
A
368
47.702
60.187
34.694
1.00
19.49
8


2943
CB
ALA
A
368
49.047
60.184
37.904
1.00
15.40
6


2944
N
GLY
A
369
47.908
62.152
35.729
1.00
14.57
7


2945
CA
GLY
A
369
48.101
62.780
34.408
1.00
15.04
6


2946
C
GLY
A
369
47.715
64.242
34.571
1.00
16.47
6


2947
O
GLY
A
369
46.895
64.643
35.433
1.00
13.93
8


2948
N
GLY
A
370
48.524
65.045
33.872
1.00
12.36
7


2949
CA
GLY
A
370
48.282
66.487
33.864
1.00
15.60
6


2950
C
GLY
A
370
47.034
66.898
33.102
1.00
14.31
6


2951
O
GLY
A
370
46.202
66.015
32.888
1.00
18.42
8


2952
N
ASN
A
371
46.994
68.167
32.710
1.00
14.57
7


2953
CA
ASN
A
371
45.708
68.579
32.081
1.00
14.92
6


2954
C
ASN
A
371
45.594
68.064
30.645
1.00
14.23
6


2955
O
ASN
A
371
46.556
67.570
30.084
1.00
14.23
8


2956
CB
AASN
A
371
45.420
70.051
32.240
0.60
23.78
6


2957
CG
AASN
A
371
43.956
70.451
32.279
0.60
25.40
6


2958
OD1
AASN
A
371
43.002
69.778
31.899
0.60
11.28
8


2959
ND2
AASN
A
371
43.728
71.695
32.756
0.60
26.08
7


2956
CB
BASN
A
371
45.872
70.115
31.871
0.40
16.79
6


2957
CG
BASN
A
371
44.590
70.670
32.513
0.40
29.87
6


2958
OD1
BASN
A
371
43.560
70.829
31.849
0.40
28.56
8


2959
ND2
BASN
A
371
44.801
70.909
33.793
0.40
23.38
7


2960
N
ASP
A
372
44.373
68.230
30.152
1.00
12.86
7


2961
CA
ASP
A
372
44.018
67.780
28.792
1.00
12.97
6


2962
C
ASP
A
372
45.054
67.942
27.745
1.00
12.07
6


2963
O
ASP
A
372
45.503
69.093
27.614
1.00
13.32
8


2964
CB
ASP
A
372
42.737
68.624
28.451
1.00
10.31
6


2965
CG
ASP
A
372
42.153
68.351
27.084
1.00
11.02
6


2966
OD1
ASP
A
372
42.556
67.384
26.464
1.00
12.81
8


2967
OD2
ASP
A
372
41.293
69.190
26.659
1.00
12.58
8


2968
N
PRO
A
373
45.561
66.874
27.151
1.00
11.77
7


2969
CA
PRO
A
373
44.932
65.582
26.928
1.00
11.70
6


2970
C
PRO
A
373
45.436
64.544
27.918
1.00
11.76
6


2971
O
PRO
A
373
45.014
63.392
27.879
1.00
11.30
8


2972
CB
PRO
A
373
45.237
65.136
25.475
1.00
10.91
6


2973
CG
PRO
A
373
46.632
65.755
25.353
1.00
14.12
6


2974
CD
PRO
A
373
46.484
67.082
26.040
1.00
13.69
6


2975
N
TYR
A
374
46.374
64.933
28.815
1.00
9.68
7


2976
CA
TYR
A
374
47.139
63.921
29.579
1.00
10.60
6


2977
C
TYR
A
374
46.381
63.338
30.741
1.00
11.01
6


2978
O
TYR
A
374
46.896
62.356
31.346
1.00
12.41
8


2979
CB
TYR
A
374
48.493
64.515
30.101
1.00
12.69
6


2980
CG
TYR
A
374
49.258
65.009
28.884
1.00
14.15
6


2981
CD1
TYR
A
374
49.738
64.107
27.954
1.00
14.25
6


2982
CD2
TYR
A
374
49.457
66.382
28.664
1.00
19.98
6


2983
CE1
TYR
A
374
50.385
64.536
26.798
1.00
19.01
6


2984
CE2
TYR
A
374
50.125
66.791
27.525
1.00
18.34
6


2985
CZ
TYR
A
374
50.572
65.893
26.613
1.00
21.81
6


2986
OH
TYR
A
374
51.271
66.349
25.492
1.00
24.57
8


2987
N
ASN
A
375
45.203
63.895
31.004
1.00
10.61
7


2988
CA
ASN
A
375
44.295
63.320
31.991
1.00
9.59
6


2989
C
ASN
A
375
43.275
62.353
31.357
1.00
11.84
6


2990
O
ASN
A
375
42.406
61.795
32.073
1.00
12.18
8


2991
CB
ASN
A
375
43.489
64.456
32.649
1.00
10.84
6


2992
CG
ASN
A
375
42.822
65.356
31.632
1.00
13.47
6


2993
OD1
ASN
A
375
42.889
65.147
30.378
1.00
14.66
8


2994
ND2
ASN
A
375
42.188
66.403
32.155
1.00
11.13
7


2995
N
ARG
A
376
43.519
62.009
30.071
1.00
11.23
7


2996
CA
ARG
A
376
42.622
61.074
29.366
1.00
12.81
6


2997
C
ARG
A
376
43.410
59.886
28.872
1.00
11.47
6


2998
O
ARG
A
376
43.286
59.389
27.744
1.00
11.36
8


2999
CB
ARG
A
376
41.975
61.789
28.128
1.00
11.93
6


3000
CG
ARG
A
376
41.111
62.997
28.659
1.00
11.44
6


3001
CD
ARG
A
376
40.908
63.980
27.521
1.00
13.66
6


3002
NE
ARG
A
376
40.177
65.214
28.005
1.00
13.05
7


3003
CZ
ARG
A
376
39.567
66.011
27.137
1.00
11.35
6


3004
NH1
ARG
A
376
39.569
65.752
25.825
1.00
9.57
7


3005
NH2
ARG
A
376
38.944
67.071
27.646
1.00
10.95
7


3006
N
GLY
A
377
44.270
59.361
29.749
1.00
9.89
7


3007
CA
GLY
A
377
45.084
58.173
29.407
1.00
10.61
6


3008
C
GLY
A
377
44.162
56.943
29.297
1.00
11.99
6


3009
O
GLY
A
377
42.974
56.949
29.658
1.00
10.52
8


3010
N
MET
A
378
44.783
55.861
28.718
1.00
12.46
7


3011
CA
MET
A
378
43.968
54.622
28.638
1.00
11.69
6


3012
C
MET
A
378
43.777
54.021
30.032
1.00
11.73
6


3013
O
MET
A
378
44.769
53.836
30.804
1.00
12.80
8


3014
CB
MET
A
378
44.714
53.606
27.749
1.00
13.64
6


3015
CG
MET
A
378
43.750
52.572
27.113
1.00
12.65
6


3016
SD
MET
A
378
42.871
53.357
25.713
1.00
14.01
16


3017
CE
MET
A
378
41.543
52.139
25.530
1.00
15.94
6


3018
N
MET
A
379
42.575
53.515
30.324
1.00
11.68
7


3019
CA
MET
A
379
42.364
52.843
31.637
1.00
11.67
6


3020
C
MET
A
379
43.364
51.711
31.705
1.00
14.11
6


3021
O
MET
A
379
43.463
50.864
30.812
1.00
12.85
8


3022
CB
MET
A
379
40.896
52.323
31.558
1.00
12.77
6


3023
CG
MET
A
379
40.572
51.443
32.790
1.00
13.09
6


3024
SD
MET
A
379
40.355
52.467
34.277
1.00
13.28
16


3025
CE
MET
A
379
39.369
51.269
35.254
1.00
13.26
6


3026
N
PRO
A
380
44.193
51.636
32.750
1.00
12.95
7


3027
CA
PRO
A
380
45.398
50.827
32.726
1.00
14.01
6


3028
C
PRO
A
380
45.170
49.402
33.204
1.00
17.99
6


3029
O
PRO
A
380
46.005
48.554
32.914
1.00
17.24
8


3030
CB
PRO
A
380
46.384
51.501
33.699
1.00
14.68
6


3031
CG
PRO
A
380
45.418
52.190
34.636
1.00
16.71
6


3032
CD
PRO
A
380
44.300
52.693
33.751
1.00
14.00
6


3033
N
ALA
A
381
44.099
49.232
33.975
1.00
15.78
7


3034
CA
ALA
A
381
43.895
47.955
34.625
1.00
13.86
6


3035
C
ALA
A
381
42.477
47.891
35.190
1.00
13.98
6


3036
O
ALA
A
381
41.859
48.952
35.215
1.00
13.69
8


3037
CB
ALA
A
381
44.854
47.608
35.761
1.00
17.52
6


3038
N
PHE
A
382
42.029
46.671
35.497
1.00
14.05
7


3039
CA
PHE
A
382
40.701
46.466
36.094
1.00
12.60
6


3040
C
PHE
A
382
40.791
45.644
37.393
1.00
12.68
6


3041
O
PHE
A
382
39.963
44.765
37.641
1.00
15.80
8


3042
CB
PHE
A
382
39.742
45.806
35.052
1.00
15.36
6


3043
CG
PHE
A
382
39.619
46.669
33.826
1.00
14.57
6


3044
CD1
PHE
A
382
40.475
46.629
32.737
1.00
14.43
6


3045
CD2
PHE
A
382
38.572
47.618
33.775
1.00
16.09
6


3046
CE1
PHE
A
382
40.327
47.480
31.670
1.00
17.87
6


3047
CE2
PHE
A
382
38.414
48.469
32.699
1.00
12.38
6


3048
CZ
PHE
A
382
39.293
48.395
31.613
1.00
15.80
6


3049
N
ASP
A
383
41.721
46.138
38.224
1.00
13.84
7


3050
CA
ASP
A
383
42.065
45.402
39.467
1.00
15.38
6


3051
C
ASP
A
383
41.067
45.732
40.552
1.00
15.05
6


3052
O
ASP
A
383
40.864
46.868
40.943
1.00
16.64
8


3053
CB
ASP
A
383
43.457
45.826
39.901
1.00
13.18
6


3054
CG
ASP
A
383
44.015
45.155
41.165
1.00
18.89
6


3055
OD1
ASP
A
383
43.286
44.428
41.805
1.00
20.99
8


3056
OD2
ASP
A
383
45.229
45.408
41.363
1.00
21.43
8


3057
N
THR
A
384
40.302
44.680
40.950
1.00
13.75
7


3058
CA
THR
A
384
39.215
44.894
41.930
1.00
12.49
6


3059
C
THR
A
384
39.773
44.871
43.345
1.00
13.78
6


3060
O
THR
A
384
38.951
44.852
44.298
1.00
18.13
8


3061
CB
THR
A
384
38.098
43.831
41.755
1.00
16.42
6


3062
OG1
THR
A
384
38.725
42.525
41.937
1.00
18.75
8


3063
CG2
THR
A
384
37.515
43.943
40.342
1.00
20.28
6


3064
N
THR
A
385
41.088
44.832
43.573
1.00
14.37
7


3065
CA
THR
A
385
41.648
44.691
44.906
1.00
16.71
6


3066
C
THR
A
385
42.313
45.974
45.424
1.00
16.63
6


3067
O
THR
A
385
42.873
45.952
46.539
1.00
14.22
8


3068
CB
THR
A
385
42.693
43.546
45.009
1.00
19.15
6


3069
OG1
THR
A
385
43.883
43.878
44.288
1.00
17.99
8


3070
CG2
THR
A
385
42.075
42.234
44.541
1.00
24.33
6


3071
N
THR
A
386
42.254
47.039
44.606
1.00
14.92
7


3072
CA
THR
A
386
42.952
48.254
45.131
1.00
13.63
6


3073
C
THR
A
386
42.175
48.801
46.328
1.00
11.22
6


3074
O
THR
A
386
40.990
48.649
46.478
1.00
12.74
8


3075
CB
THR
A
386
43.101
49.344
44.054
1.00
13.50
6


3076
OG1
THR
A
386
41.805
49.919
43.822
1.00
12.14
8


3077
CG2
THR
A
386
43.656
48.809
42.719
1.00
17.62
6


3078
N
THR
A
387
42.886
49.552
47.184
1.00
14.21
7


3079
CA
THR
A
387
42.237
50.167
48.316
1.00
11.44
6


3080
C
THR
A
387
41.127
51.134
47.887
1.00
12.54
6


3081
O
THR
A
387
40.045
51.113
48.437
1.00
12.57
8


3082
CB
THR
A
387
43.277
50.926
49.145
1.00
17.16
6


3083
OG1
THR
A
387
44.177
49.939
49.669
1.00
15.42
8


3084
CG2
THR
A
387
42.644
51.724
50.273
1.00
14.27
6


3085
N
ALA
A
388
41.441
51.910
46.838
1.00
13.30
7


3086
CA
ALA
A
388
40.376
52.785
46.360
1.00
10.83
6


3087
C
ALA
A
388
39.162
52.083
45.808
1.00
12.23
6


3088
O
ALA
A
388
38.030
52.497
46.001
1.00
11.44
8


3089
CB
ALA
A
388
40.968
53.700
45.239
1.00
10.26
6


3090
N
PHE
A
389
39.347
50.956
45.084
1.00
12.53
7


3091
CA
PHE
A
389
38.202
50.182
44.579
1.00
13.64
6


3092
C
PHE
A
389
37.361
49.746
45.779
1.00
13.47
6


3093
O
PHE
A
389
36.157
49.895
45.789
1.00
12.37
8


3094
CB
PHE
A
389
38.766
48.975
43.763
1.00
11.46
6


3095
CG
PHE
A
389
37.627
48.178
43.141
1.00
12.01
6


3096
CD1
PHE
A
389
36.936
47.248
43.916
1.00
16.87
6


3097
CD2
PHE
A
389
37.375
48.299
41.777
1.00
14.39
6


3098
CE1
PHE
A
389
35.869
46.515
43.383
1.00
14.50
6


3099
CE2
PHE
A
389
36.340
47.536
41.216
1.00
12.44
6


3100
CZ
PHE
A
389
35.646
46.648
42.031
1.00
13.69
6


3101
N
LYS
A
390
38.053
49.160
46.775
1.00
12.03
7


3102
CA
LYS
A
390
37.303
48.672
47.936
1.00
12.63
6


3103
C
LYS
A
390
36.544
49.767
48.699
1.00
14.75
6


3104
O
LYS
A
390
35.438
49.556
49.197
1.00
12.66
8


3105
CB
LYS
A
390
38.291
48.000
48.917
1.00
12.06
6


3106
CG
LYS
A
390
38.798
46.712
48.243
1.00
15.90
6


3107
CD
LYS
A
390
39.589
45.970
49.325
1.00
25.81
6


3108
CE
LYS
A
390
40.980
46.524
49.440
1.00
29.79
6


3109
NZ
LYS
A
390
41.835
45.465
50.107
1.00
41.01
7


3110
N
GLU
A
391
37.256
50.908
48.782
1.00
11.21
7


3111
CA
GLU
A
391
36.636
52.048
49.475
1.00
11.43
6


3112
C
GLU
A
391
35.375
52.482
48.742
1.00
12.51
6


3113
O
GLU
A
391
34.300
52.735
49.337
1.00
10.64
8


3114
CB
GLU
A
391
37.670
53.223
49.487
1.00
10.44
6


3115
CG
GLU
A
391
36.957
54.519
49.997
1.00
10.67
6


3116
CD
GLU
A
391
37.870
55.744
49.810
1.00
12.38
6


3117
OE1
GLU
A
391
38.974
55.628
49.226
1.00
13.12
8


3118
OE2
GLU
A
391
37.458
56.841
50.284
1.00
12.94
8


3119
N
VAL
A
392
35.455
52.675
47.403
1.00
11.36
7


3120
CA
VAL
A
392
34.279
53.176
46.653
1.00
12.25
6


3121
C
VAL
A
392
33.156
52.128
46.716
1.00
12.76
6


3122
O
VAL
A
392
31.968
52.481
46.930
1.00
12.77
8


3123
CB
VAL
A
392
34.667
53.410
45.175
1.00
14.39
6


3124
CG1
VAL
A
392
33.434
53.661
44.296
1.00
13.75
6


3125
CG2
VAL
A
392
35.702
54.570
45.061
1.00
12.07
6


3126
N
SER
A
393
33.487
50.846
46.628
1.00
10.90
7


3127
CA
SER
A
393
32.426
49.822
46.686
1.00
12.19
6


3128
C
SER
A
393
31.708
49.782
48.021
1.00
10.96
6


3129
O
SER
A
393
30.469
49.774
48.186
1.00
12.48
8


3130
CB
SER
A
393
33.059
48.431
46.394
1.00
12.79
6


3131
OG
SER
A
393
31.944
47.538
46.423
1.00
19.93
8


3132
N
THR
A
394
32.493
49.942
49.099
1.00
11.04
7


3133
CA
THR
A
394
31.920
49.922
50.445
1.00
12.34
6


3134
C
THR
A
394
31.061
51.130
50.682
1.00
11.80
6


3135
O
THR
A
394
29.935
51.097
51.169
1.00
11.63
8


3136
CB
THR
A
394
33.039
49.889
51.509
1.00
12.40
6


3137
OG1
THR
A
394
33.699
48.614
51.401
1.00
14.67
8


3138
CG2
THR
A
394
32.443
50.011
52.927
1.00
14.84
6


3139
N
LEU
A
395
31.600
52.334
50.322
1.00
12.76
7


3140
CA
LEU
A
395
30.858
53.558
50.592
1.00
11.35
6


3141
C
LEU
A
395
29.666
53.709
49.624
1.00
10.18
6


3142
O
LEU
A
395
28.676
54.373
49.976
1.00
11.69
8


3143
CB
LEU
A
395
31.784
54.804
50.604
1.00
13.30
6


3144
CG
LEU
A
395
32.795
54.745
51.811
1.00
12.96
6


3145
CD1
LEU
A
395
33.641
56.019
51.748
1.00
13.55
6


3146
CD2
LEU
A
395
32.059
54.747
53.145
1.00
14.45
6


3147
N
ALA
A
396
29.852
53.116
48.444
1.00
11.70
7


3148
CA
ALA
A
396
28.636
53.182
47.557
1.00
12.78
6


3149
C
ALA
A
396
27.498
52.378
48.163
1.00
13.72
6


3150
O
ALA
A
396
26.345
52.797
48.075
1.00
10.99
8


3151
CB
ALA
A
396
29.035
52.530
46.203
1.00
12.34
6


3152
N
GLY
A
397
27.797
51.244
48.825
1.00
11.86
7


3153
CA
GLY
A
397
26.710
50.490
49.510
1.00
12.95
6


3154
C
GLY
A
397
26.096
51.295
50.656
1.00
12.93
6


3155
O
GLY
A
397
24.865
51.276
50.842
1.00
15.22
8


3156
N
LEU
A
398
26.948
52.018
51.404
1.00
12.12
7


3157
CA
LEU
A
398
26.336
52.833
52.491
1.00
10.40
6


3158
C
LEU
A
398
25.388
53.871
51.900
1.00
13.47
6


3159
O
LEU
A
398
24.310
54.166
52.434
1.00
13.29
8


3160
CB
LEU
A
398
27.503
53.525
53.229
1.00
10.78
6


3161
CG
LEU
A
398
26.999
54.426
54.353
1.00
11.76
6


3162
CD1
LEU
A
398
26.326
53.660
55.479
1.00
15.25
6


3163
CD2
LEU
A
398
28.230
55.206
54.909
1.00
16.57
6


3164
N
ARG
A
399
25.832
54.478
50.754
1.00
11.98
7


3165
CA
ARG
A
399
24.988
55.539
50.164
1.00
12.52
6


3166
C
ARG
A
399
23.712
54.952
49.579
1.00
13.24
6


3167
O
ARG
A
399
22.661
55.603
49.688
1.00
14.42
8


3168
CB
ARG
A
399
25.789
56.271
49.068
1.00
11.24
6


3169
CG
ARG
A
399
24.974
57.205
48.158
1.00
11.40
6


3170
CD
ARG
A
399
25.933
57.875
47.182
1.00
11.42
6


3171
NE
ARG
A
399
26.620
59.029
47.799
1.00
10.92
7


3172
CZ
ARG
A
399
26.193
60.279
47.877
1.00
14.21
6


3173
NH1
ARG
A
399
24.965
60.565
47.446
1.00
10.96
7


3174
NH2
ARG
A
399
26.954
61.245
48.436
1.00
11.76
7


3175
N
ARG
A
400
23.713
53.697
49.131
1.00
12.24
7


3176
CA
ARG
A
400
22.456
53.111
48.675
1.00
12.96
6


3177
C
ARG
A
400
21.533
52.789
49.852
1.00
13.71
6


3178
O
ARG
A
400
20.311
52.762
49.629
1.00
17.33
8


3179
CB
ARG
A
400
22.748
51.783
47.930
1.00
14.09
6


3180
CG
ARG
A
400
23.460
51.918
46.578
1.00
14.91
6


3181
CD
ARG
A
400
23.412
50.634
45.761
1.00
16.08
6


3182
NE
ARG
A
400
24.141
49.517
46.399
1.00
14.78
7


3183
CZ
ARG
A
400
25.452
49.279
46.343
1.00
14.12
6


3184
NH1
ARG
A
400
26.214
50.128
45.640
1.00
15.84
7


3185
NH2
ARG
A
400
25.957
48.216
46.978
1.00
16.89
7


3186
N
ASN
A
401
22.154
52.394
50.972
1.00
14.24
7


3187
CA
ASN
A
401
21.271
51.879
52.060
1.00
14.18
6


3188
C
ASN
A
401
20.967
52.828
53.189
1.00
15.56
6


3189
O
ASN
A
401
19.976
52.564
53.935
1.00
17.91
8


3190
CB
ASN
A
401
21.990
50.632
52.590
1.00
16.43
6


3191
CG
ASN
A
401
21.827
49.617
51.404
1.00
25.29
6


3192
OD1
ASN
A
401
22.805
49.256
50.797
1.00
33.03
8


3193
ND2
ASN
A
401
20.619
49.215
51.102
1.00
40.20
7


3194
N
ASN
A
402
21.705
53.948
53.373
1.00
13.76
7


3195
CA
ASN
A
402
21.449
54.851
54.506
1.00
13.71
6


3196
C
ASN
A
402
20.938
56.175
53.980
1.00
14.67
6


3197
O
ASN
A
402
21.601
56.923
53.249
1.00
13.53
8


3198
CB
ASN
A
402
22.753
55.036
55.311
1.00
13.24
6


3199
CG
ASN
A
402
22.397
55.744
56.604
1.00
14.53
6


3200
OD1
ASN
A
402
21.722
56.787
56.564
1.00
14.56
8


3201
ND2
ASN
A
402
22.839
55.186
57.762
1.00
11.48
7


3202
N
ALA
A
403
19.633
56.460
54.202
1.00
12.55
7


3203
CA
ALA
A
403
19.017
57.672
53.679
1.00
12.81
6


3204
C
ALA
A
403
19.622
58.961
54.144
1.00
14.88
6


3205
O
ALA
A
403
19.421
59.958
53.422
1.00
13.18
8


3206
CB
ALA
A
403
17.511
57.608
54.092
1.00
12.99
6


3207
N
ALA
A
404
20.407
58.945
55.229
1.00
11.82
7


3208
CA
ALA
A
404
21.107
60.187
55.611
1.00
11.98
6


3209
C
ALA
A
404
22.095
60.641
54.524
1.00
11.49
6


3210
O
ALA
A
404
22.259
61.857
54.383
1.00
12.58
8


3211
CB
ALA
A
404
21.874
60.008
56.930
1.00
15.02
6


3212
N
ILE
A
405
22.707
59.716
53.830
1.00
11.27
7


3213
CA
ILE
A
405
23.702
60.168
52.791
1.00
11.62
6


3214
C
ILE
A
405
22.936
60.722
51.581
1.00
13.21
6


3215
O
ILE
A
405
23.353
61.696
50.964
1.00
12.14
8


3216
CB
ILE
A
405
24.538
58.973
52.331
1.00
14.54
6


3217
CG1
ILE
A
405
25.425
58.253
53.392
1.00
15.40
6


3218
CG2
ILE
A
405
25.511
59.410
51.202
1.00
11.30
6


3219
CD1
ILE
A
405
26.170
59.266
54.247
1.00
17.36
6


3220
N
GLN
A
406
21.759
60.152
51.297
1.00
11.32
7


3221
CA
GLN
A
406
20.992
60.545
50.107
1.00
11.87
6


3222
C
GLN
A
406
20.335
61.902
50.300
1.00
14.28
6


3223
O
GLN
A
406
20.265
62.707
49.360
1.00
11.82
8


3224
CB
GLN
A
406
19.875
59.494
49.869
1.00
12.00
6


3225
CG
GLN
A
406
20.511
58.136
49.549
1.00
12.17
6


3226
CD
GLN
A
406
19.521
56.983
49.392
1.00
22.22
6


3227
OE1
GLN
A
406
19.847
55.775
49.395
1.00
20.31
8


3228
NE2
GLN
A
406
18.272
57.356
49.223
1.00
24.04
7


3229
N
TYR
A
407
19.757
62.154
51.499
1.00
13.05
7


3230
CA
TYR
A
407
18.848
63.261
51.702
1.00
13.56
6


3231
C
TYR
A
407
19.168
64.182
52.885
1.00
10.35
6


3232
O
TYR
A
407
18.463
65.190
53.047
1.00
12.85
8


3233
CB
TYR
A
407
17.440
62.678
52.068
1.00
14.06
6


3234
CG
TYR
A
407
16.935
61.567
51.144
1.00
12.51
6


3235
CD1
TYR
A
407
16.929
61.748
49.759
1.00
11.68
6


3236
CD2
TYR
A
407
16.397
60.418
51.708
1.00
11.57
6


3237
CE1
TYR
A
407
16.441
60.742
48.918
1.00
12.71
6


3238
CE2
TYR
A
407
15.910
59.420
50.894
1.00
14.60
6


3239
CZ
TYR
A
407
15.933
59.595
49.515
1.00
15.50
6


3240
OH
TYR
A
407
15.433
58.598
48.707
1.00
15.89
8


3241
N
GLY
A
408
20.152
63.743
53.678
1.00
12.31
7


3242
CA
GLY
A
408
20.277
64.361
55.005
1.00
14.17
6


3243
C
GLY
A
408
20.830
65.790
55.030
1.00
13.76
6


3244
O
GLY
A
408
21.566
66.253
54.133
1.00
13.31
8


3245
N
THR
A
409
20.636
66.393
56.207
1.00
12.33
7


3246
CA
THR
A
409
21.322
67.645
56.558
1.00
14.50
6


3247
C
THR
A
409
22.822
67.370
56.707
1.00
13.72
6


3248
O
THR
A
409
23.222
66.229
56.777
1.00
12.71
8


3249
CB
THR
A
409
20.812
68.210
57.928
1.00
16.13
6


3250
OG1
THR
A
409
20.849
67.169
58.916
1.00
16.69
8


3251
CG2
THR
A
409
19.360
68.677
57.762
1.00
18.70
6


3252
N
THR
A
410
23.605
68.449
56.790
1.00
12.28
7


3253
CA
THR
A
410
25.062
68.261
57.141
1.00
12.15
6


3254
C
THR
A
410
25.332
69.229
58.321
1.00
12.71
6


3255
O
THR
A
410
25.041
70.423
58.225
1.00
13.99
8


3256
CB
THR
A
410
25.943
68.740
55.952
1.00
11.34
6


3257
OG1
THR
A
410
25.541
67.959
54.786
1.00
13.77
8


3258
CG2
THR
A
410
27.425
68.392
56.192
1.00
13.33
6


3259
N
THR
A
411
25.996
68.665
59.342
1.00
12.78
7


3260
CA
THR
A
411
26.301
69.430
60.568
1.00
12.27
6


3261
C
THR
A
411
27.765
69.192
60.919
1.00
13.51
6


3262
O
THR
A
411
28.168
68.039
61.036
1.00
14.10
8


3263
CB
THR
A
411
25.386
68.891
61.718
1.00
13.83
6


3264
OG1
THR
A
411
24.000
69.120
61.364
1.00
15.26
8


3265
CG2
THR
A
411
25.620
69.676
62.991
1.00
17.79
6


3266
N
GLN
A
412
28.501
70.302
61.110
1.00
12.74
7


3267
CA
GLN
A
412
29.899
70.153
61.592
1.00
13.61
6


3268
C
GLN
A
412
29.894
69.765
63.062
1.00
13.43
6


3269
O
GLN
A
412
29.218
70.451
63.824
1.00
15.64
8


3270
CB
GLN
A
412
30.556
71.523
61.335
1.00
14.70
6


3271
CG
GLN
A
412
31.999
71.615
61.876
1.00
22.99
6


3272
CD
GLN
A
412
31.918
72.168
63.334
1.00
22.07
6


3273
OE1
GLN
A
412
32.409
71.438
64.163
1.00
19.41
8


3274
NE2
GLN
A
412
31.358
73.310
63.633
1.00
25.10
7


3275
N
ARG
A
413
30.694
68.721
63.330
1.00
11.94
7


3276
CA
ARG
A
413
30.768
68.223
64.700
1.00
11.40
6


3277
C
ARG
A
413
32.184
68.430
65.276
1.00
12.19
6


3278
O
ARG
A
413
32.263
68.482
66.510
1.00
12.20
8


3279
CB
ARG
A
413
30.356
66.756
64.815
1.00
16.20
6


3280
CG
ARG
A
413
28.840
66.557
64.562
1.00
13.09
6


3281
CD
ARG
A
413
27.968
67.296
65.579
1.00
13.13
6


3282
NE
ARG
A
413
26.611
66.668
65.580
1.00
14.79
7


3283
CZ
ARG
A
413
25.684
66.909
66.515
1.00
19.43
6


3284
NH1
ARG
A
413
25.974
67.784
67.503
1.00
16.73
7


3285
NH2
ARG
A
413
24.529
66.233
66.470
1.00
18.22
7


3286
N
TRP
A
414
33.228
68.466
64.474
1.00
11.18
7


3287
CA
TRP
A
414
34.548
68.752
65.082
1.00
12.61
6


3288
C
TRP
A
414
35.444
69.243
63.947
1.00
13.80
6


3289
O
TRP
A
414
35.295
68.712
62.833
1.00
13.58
8


3290
CB
TRP
A
414
35.121
67.438
65.651
1.00
14.04
6


3291
CG
TRP
A
414
36.181
67.603
66.709
1.00
14.49
6


3292
CD1
TRP
A
414
35.921
67.473
68.075
1.00
15.45
6


3293
CD2
TRP
A
414
37.583
67.864
66.591
1.00
15.74
6


3294
NE1
TRP
A
414
37.112
67.622
68.773
1.00
16.17
7


3295
CE2
TRP
A
414
38.123
67.884
67.898
1.00
15.43
6


3296
CE3
TRP
A
414
38.421
68.101
65.507
1.00
14.89
6


3297
CZ2
TRP
A
414
39.489
68.090
68.138
1.00
20.21
6


3298
CZ3
TRP
A
414
39.805
68.279
65.725
1.00
15.42
6


3299
CH2
TRP
A
414
40.310
68.296
67.066
1.00
17.01
6


3300
N
ILE
A
415
36.215
70.337
64.186
1.00
12.40
7


3301
CA
ILE
A
415
37.012
70.828
63.038
1.00
11.33
6


3302
C
ILE
A
415
38.296
71.491
63.524
1.00
15.04
6


3303
O
ILE
A
415
38.300
72.134
64.600
1.00
15.39
8


3304
CB
ILE
A
415
36.153
71.827
62.253
1.00
15.29
6


3305
CG1
ILE
A
415
36.843
72.197
60.923
1.00
15.07
6


3306
CG2
ILE
A
415
35.782
73.061
63.054
1.00
20.69
6


3307
CD1
ILE
A
415
35.862
72.686
59.854
1.00
18.18
6


3308
N
ASN
A
416
39.349
71.266
62.797
1.00
13.47
7


3309
CA
ASN
A
416
40.517
72.152
62.912
1.00
14.63
6


3310
C
ASN
A
416
41.103
72.198
61.526
1.00
13.17
6


3311
O
ASN
A
416
40.399
71.879
60.536
1.00
12.76
8


3312
CB
ASN
A
416
41.480
71.607
63.994
1.00
14.61
6


3313
CG
ASN
A
416
42.250
70.394
63.669
1.00
16.07
6


3314
OD1
ASN
A
416
42.180
69.778
62.591
1.00
12.99
8


3315
ND2
ASN
A
416
43.129
69.947
64.597
1.00
16.12
7


3316
N
ASN
A
417
42.356
72.644
61.313
1.00
13.23
7


3317
CA
ASN
A
417
42.755
72.836
59.907
1.00
13.30
6


3318
C
ASN
A
417
42.767
71.526
59.103
1.00
13.34
6


3319
O
ASN
A
417
42.621
71.524
57.886
1.00
12.55
8


3320
CB
ASN
A
417
44.185
73.410
59.931
1.00
16.87
6


3321
CG
ASN
A
417
44.190
74.929
59.999
1.00
23.81
6


3322
OD1
ASN
A
417
43.170
75.585
60.178
1.00
21.65
8


3323
ND2
ASN
A
417
45.415
75.482
59.839
1.00
24.48
7


3324
N
ASP
A
418
43.109
70.439
59.874
1.00
12.62
7


3325
CA
ASP
A
418
43.295
69.150
59.209
1.00
10.76
6


3326
C
ASP
A
418
42.126
68.157
59.319
1.00
12.08
6


3327
O
ASP
A
418
42.093
67.177
58.533
1.00
11.98
8


3328
CB
ASP
A
418
44.520
68.478
59.846
1.00
13.38
6


3329
CG
ASP
A
418
45.842
69.080
59.483
1.00
16.78
6


3330
OD1
ASP
A
418
46.040
69.609
58.372
1.00
13.55
8


3331
OD2
ASP
A
418
46.759
69.017
60.342
1.00
13.98
8


3332
N
VAL
A
419
41.304
68.369
60.363
1.00
11.52
7


3333
CA
VAL
A
419
40.281
67.366
60.644
1.00
10.52
6


3334
C
VAL
A
419
38.910
67.958
60.419
1.00
12.12
6


3335
O
VAL
A
419
38.606
69.052
60.846
1.00
12.25
8


3336
CB
VAL
A
419
40.384
66.958
62.145
1.00
11.46
6


3337
CG1
VAL
A
419
39.231
65.959
62.481
1.00
11.88
6


3338
CG2
VAL
A
419
41.737
66.266
62.444
1.00
12.56
6


3339
N
TYR
A
420
38.034
67.172
59.764
1.00
11.92
7


3340
CA
TYR
A
420
36.628
67.548
59.636
1.00
10.72
6


3341
C
TYR
A
420
35.772
66.328
59.977
1.00
10.50
6


3342
O
TYR
A
420
35.908
65.254
59.383
1.00
13.20
8


3343
CB
TYR
A
420
36.410
67.866
58.138
1.00
9.44
6


3344
CG
TYR
A
420
35.063
68.583
57.856
1.00
10.31
6


3345
CD1
TYR
A
420
34.258
69.238
58.754
1.00
13.30
6


3346
CD2
TYR
A
420
34.669
68.523
56.512
1.00
13.25
6


3347
CE1
TYR
A
420
33.045
69.865
58.379
1.00
11.70
6


3348
CE2
TYR
A
420
33.476
69.131
56.115
1.00
14.40
6


3349
CZ
TYR
A
420
32.692
69.780
57.021
1.00
15.49
6


3350
OH
TYR
A
420
31.503
70.412
56.683
1.00
15.26
8


3351
N
ILE
A
421
35.000
66.508
61.075
1.00
11.61
7


3352
CA
ILE
A
421
34.037
65.462
61.458
1.00
9.13
6


3353
C
ILE
A
421
32.649
66.076
61.282
1.00
10.90
6


3354
O
ILE
A
421
32.379
67.148
61.788
1.00
13.13
8


3355
CB
ILE
A
421
34.238
64.997
62.941
1.00
11.03
6


3356
CG1
ILE
A
421
35.689
64.584
63.133
1.00
11.76
6


3357
CG2
ILE
A
421
33.251
63.841
63.198
1.00
14.22
6


3358
CD1
ILE
A
421
35.980
63.871
64.484
1.00
14.70
6


3359
N
TYR
A
422
31.889
65.498
60.276
1.00
10.51
7


3360
CA
TYR
A
422
30.571
66.072
60.004
1.00
11.77
6


3361
C
TYR
A
422
29.510
64.963
60.053
1.00
11.33
6


3362
O
TYR
A
422
29.877
63.774
59.986
1.00
11.55
8


3363
CB
TYR
A
422
30.570
66.791
58.623
1.00
11.55
6


3364
CG
TYR
A
422
31.000
65.881
57.458
1.00
12.40
6


3365
CD1
TYR
A
422
30.094
65.103
56.724
1.00
11.81
6


3366
CD2
TYR
A
422
32.354
65.851
57.140
1.00
11.72
6


3367
CE1
TYR
A
422
30.559
64.305
55.668
1.00
12.09
6


3368
CE2
TYR
A
422
32.853
65.051
56.094
1.00
11.73
6


3369
CZ
TYR
A
422
31.935
64.298
55.377
1.00
13.04
6


3370
OH
TYR
A
422
32.365
63.520
54.338
1.00
11.43
8


3371
N
GLU
A
423
28.257
65.380
60.139
1.00
11.98
7


3372
CA
GLU
A
423
27.202
64.378
60.362
1.00
11.04
6


3373
C
GLU
A
423
26.064
64.598
59.383
1.00
11.74
6


3374
O
GLU
A
423
25.644
65.748
59.205
1.00
13.56
8


3375
CB
GLU
A
423
26.633
64.609
61.806
1.00
14.91
6


3376
CG
GLU
A
423
25.731
63.465
62.258
1.00
12.27
6


3377
CD
GLU
A
423
25.459
63.688
63.796
1.00
13.28
6


3378
OE1
GLU
A
423
24.947
64.750
64.099
1.00
18.28
8


3379
OE2
GLU
A
423
25.800
62.682
64.408
1.00
17.49
8


3380
N
ARG
A
424
25.648
63.541
58.699
1.00
12.31
7


3381
CA
ARG
A
424
24.457
63.621
57.847
1.00
11.64
6


3382
C
ARG
A
424
23.268
63.035
58.643
1.00
13.19
6


3383
O
ARG
A
424
23.515
62.077
59.367
1.00
13.04
8


3384
CB
ARG
A
424
24.665
62.689
56.620
1.00
10.72
6


3385
CG
ARG
A
424
25.961
63.049
55.805
1.00
10.81
6


3386
CD
ARG
A
424
25.862
64.465
55.212
1.00
11.09
6


3387
NE
ARG
A
424
24.666
64.721
54.412
1.00
10.91
7


3388
CZ
ARG
A
424
24.420
64.168
53.207
1.00
11.39
6


3389
NH1
ARG
A
424
25.240
63.308
52.620
1.00
10.62
7


3390
NH2
ARG
A
424
23.239
64.512
52.596
1.00
10.78
7


3391
N
LYS
A
425
22.068
63.623
58.542
1.00
11.90
7


3392
CA
LYS
A
425
20.937
63.080
59.290
1.00
11.75
6


3393
C
LYS
A
425
19.685
63.233
58.443
1.00
15.39
6


3394
O
LYS
A
425
19.444
64.340
58.036
1.00
14.23
8


3395
CB
LYS
A
425
20.801
63.854
60.626
1.00
13.68
6


3396
CG
LYS
A
425
19.617
63.271
61.494
1.00
14.44
6


3397
CD
LYS
A
425
19.721
63.992
62.863
1.00
19.53
6


3398
CE
LYS
A
425
18.739
63.342
63.856
1.00
20.97
6


3399
NZ
LYS
A
425
17.322
63.663
63.509
1.00
23.72
7


3400
N
PHE
A
426
18.908
62.144
58.357
1.00
12.33
7


3401
CA
PHE
A
426
17.583
62.238
57.709
1.00
12.03
6


3402
C
PHE
A
426
16.651
61.481
58.706
1.00
11.05
6


3403
O
PHE
A
426
16.657
60.252
58.693
1.00
13.03
8


3404
CB
PHE
A
426
17.608
61.450
56.397
1.00
13.23
6


3405
CG
PHE
A
426
16.260
61.449
55.699
1.00
12.58
6


3406
CD1
PHE
A
426
15.838
62.659
55.147
1.00
14.04
6


3407
CD2
PHE
A
426
15.515
60.300
55.571
1.00
14.55
6


3408
CE1
PHE
A
426
14.594
62.715
54.490
1.00
13.58
6


3409
CE2
PHE
A
426
14.264
60.345
54.906
1.00
15.67
6


3410
CZ
PHE
A
426
13.839
61.552
54.398
1.00
15.62
6


3411
N
PHE
A
427
15.916
62.357
59.408
1.00
14.34
7


3412
CA
PHE
A
427
15.024
61.773
60.490
1.00
16.20
6


3413
C
PHE
A
427
15.781
60.836
61.400
1.00
17.32
6


3414
O
PHE
A
427
16.737
61.354
62.070
1.00
19.10
8


3415
CB
PHE
A
427
13.772
61.132
59.840
1.00
18.52
6


3416
CG
PHE
A
427
12.888
62.175
59.193
1.00
17.73
6


3417
CD1
PHE
A
427
11.972
62.918
59.905
1.00
21.55
6


3418
CD2
PHE
A
427
13.018
62.396
57.830
1.00
14.51
6


3419
CE1
PHE
A
427
11.188
63.858
59.276
1.00
18.85
6


3420
CE2
PHE
A
427
12.246
63.336
57.185
1.00
16.68
6


3421
CZ
PHE
A
427
11.311
64.087
57.906
1.00
19.85
6


3422
N
ASN
A
428
15.546
59.522
61.442
1.00
15.71
7


3423
CA
ASN
A
428
16.284
58.735
62.433
1.00
17.74
6


3424
C
ASN
A
428
17.573
58.173
61.837
1.00
18.72
6


3425
O
ASN
A
428
18.307
57.587
62.639
1.00
17.57
8


3426
CB
ASN
A
428
15.484
57.591
63.008
1.00
22.35
6


3427
CG
ASN
A
428
14.267
58.214
63.733
1.00
36.36
6


3428
OD1
ASN
A
428
14.452
59.092
64.570
1.00
38.45
8


3429
ND2
ASN
A
428
13.103
57.735
63.325
1.00
44.64
7


3430
N
ASP
A
429
17.867
58.370
60.547
1.00
15.06
7


3431
CA
ASP
A
429
19.091
57.810
59.986
1.00
14.19
6


3432
C
ASP
A
429
20.222
58.816
60.103
1.00
11.55
6


3433
O
ASP
A
429
20.026
60.024
59.967
1.00
13.16
8


3434
CB
ASP
A
429
18.927
57.501
58.471
1.00
12.81
6


3435
CG
ASP
A
429
17.766
56.561
58.255
1.00
28.25
6


3436
OD1
ASP
A
429
17.727
55.530
58.940
1.00
20.84
8


3437
OD2
ASP
A
429
16.804
56.870
57.490
1.00
27.47
8


3438
N
VAL
A
430
21.384
58.297
60.600
1.00
12.85
7


3439
CA
VAL
A
430
22.502
59.192
60.876
1.00
11.51
6


3440
C
VAL
A
430
23.816
58.621
60.371
1.00
13.31
6


3441
O
VAL
A
430
23.993
57.405
60.522
1.00
12.49
8


3442
CB
VAL
A
430
22.632
59.315
62.427
1.00
14.21
6


3443
CG1
VAL
A
430
23.828
60.233
62.734
1.00
14.56
6


3444
CG2
VAL
A
430
21.373
59.955
63.033
1.00
14.79
6


3445
N
VAL
A
431
24.721
59.432
59.826
1.00
12.54
7


3446
CA
VAL
A
431
26.043
58.933
59.434
1.00
11.58
6


3447
C
VAL
A
431
27.051
59.978
59.912
1.00
11.43
6


3448
O
VAL
A
431
26.847
61.129
59.603
1.00
12.12
8


3449
CB
VAL
A
431
26.250
58.685
57.905
1.00
12.54
6


3450
CG1
VAL
A
431
27.698
58.199
57.615
1.00
10.81
6


3451
CG2
VAL
A
431
25.254
57.657
57.400
1.00
13.14
6


3452
N
LEU
A
432
27.976
59.557
60.800
1.00
10.48
7


3453
CA
LEU
A
432
29.015
60.512
61.285
1.00
11.27
6


3454
C
LEU
A
432
30.317
60.140
60.583
1.00
11.12
6


3455
O
LEU
A
432
30.708
58.961
60.577
1.00
13.28
8


3456
CB
LEU
A
432
29.087
60.224
62.831
1.00
11.86
6


3457
CG
LEU
A
432
30.033
61.205
63.562
1.00
11.74
6


3458
CD1
LEU
A
432
29.574
62.643
63.510
1.00
11.18
6


3459
CD2
LEU
A
432
30.119
60.744
65.044
1.00
14.23
6


3460
N
VAL
A
433
30.987
61.141
59.978
1.00
11.73
7


3461
CA
VAL
A
433
32.162
60.867
59.131
1.00
9.07
6


3462
C
VAL
A
433
33.328
61.667
59.702
1.00
9.49
6


3463
O
VAL
A
433
33.158
62.864
59.844
1.00
10.58
8


3464
CB
VAL
A
433
31.899
61.334
57.674
1.00
10.62
6


3465
CG1
VAL
A
433
33.173
61.088
56.812
1.00
11.05
6


3466
CG2
VAL
A
433
30.693
60.564
57.072
1.00
11.15
6


3467
N
ALA
A
434
34.455
61.000
60.017
1.00
10.65
7


3468
CA
ALA
A
434
35.643
61.757
60.409
1.00
10.07
6


3469
C
ALA
A
434
36.742
61.603
59.363
1.00
11.73
6


3470
O
ALA
A
434
37.030
60.489
58.924
1.00
11.96
8


3471
CB
ALA
A
434
36.199
61.171
61.742
1.00
10.24
6


3472
N
ILE
A
435
37.345
62.744
58.992
1.00
10.23
7


3473
CA
ILE
A
435
38.438
62.741
58.008
1.00
8.82
6


3474
C
ILE
A
435
39.571
63.587
58.558
1.00
10.58
6


3475
O
ILE
A
435
39.366
64.734
58.922
1.00
10.88
8


3476
CB
ILE
A
435
37.961
63.408
56.674
1.00
10.84
6


3477
CG1
ILE
A
435
36.749
62.608
56.120
1.00
11.49
6


3478
CG2
ILE
A
435
39.146
63.352
55.689
1.00
10.37
6


3479
CD1
ILE
A
435
36.230
63.228
54.758
1.00
13.59
6


3480
N
ASN
A
436
40.741
62.933
58.596
1.00
10.83
7


3481
CA
ASN
A
436
41.963
63.646
58.943
1.00
11.64
6


3482
C
ASN
A
436
42.852
63.653
57.715
1.00
9.83
6


3483
O
ASN
A
436
43.367
62.621
57.309
1.00
12.85
8


3484
CB
ASN
A
436
42.711
62.821
60.036
1.00
12.59
6


3485
CG
ASN
A
436
44.030
63.480
60.383
1.00
12.87
6


3486
OD1
ASN
A
436
44.422
64.602
60.026
1.00
13.07
8


3487
ND2
ASN
A
436
44.789
62.721
61.224
1.00
13.56
7


3488
N
ARG
A
437
43.055
64.891
57.181
1.00
10.03
7


3489
CA
ARG
A
437
43.878
64.887
55.958
1.00
9.39
6


3490
C
ARG
A
437
45.362
64.725
56.267
1.00
10.71
6


3491
O
ARG
A
437
46.117
64.552
55.310
1.00
12.32
8


3492
CB
ARG
A
437
43.673
66.201
55.161
1.00
12.80
6


3493
CG
ARG
A
437
44.296
67.415
55.869
1.00
13.58
6


3494
CD
ARG
A
437
44.031
68.719
55.043
1.00
11.13
6


3495
NE
ARG
A
437
44.772
69.847
55.738
1.00
10.90
7


3496
CZ
ARG
A
437
44.957
71.046
55.195
1.00
14.88
6


3497
NH1
ARG
A
437
44.521
71.299
53.948
1.00
11.67
7


3498
NH2
ARG
A
437
45.406
72.058
55.947
1.00
13.84
7


3499
N
ASN
A
438
45.779
65.035
57.513
1.00
11.11
7


3500
CA
ASN
A
438
47.255
65.048
57.734
1.00
12.20
6


3501
C
ASN
A
438
47.780
63.623
57.869
1.00
13.73
6


3502
O
ASN
A
438
47.440
62.900
58.830
1.00
12.56
8


3503
CB
ASN
A
438
47.474
65.787
59.071
1.00
13.49
6


3504
CG
ASN
A
438
48.921
66.167
59.255
1.00
13.92
6


3505
OD1
ASN
A
438
49.775
65.335
58.985
1.00
15.45
8


3506
ND2
ASN
A
438
49.263
67.376
59.700
1.00
13.51
7


3507
N
THR
A
439
48.650
63.224
56.949
1.00
11.49
7


3508
CA
THR
A
439
49.087
61.822
56.883
1.00
12.77
6


3509
C
THR
A
439
50.271
61.585
57.846
1.00
14.69
6


3510
O
THR
A
439
50.750
60.450
57.917
1.00
16.23
8


3511
CB
THR
A
439
49.518
61.431
55.456
1.00
16.48
6


3512
OG1
THR
A
439
50.542
62.330
54.990
1.00
17.73
8


3513
CG2
THR
A
439
48.284
61.611
54.554
1.00
15.47
6


3514
N
GLN
A
440
50.666
62.669
58.501
1.00
14.00
7


3515
CA
GLN
A
440
51.778
62.467
59.481
1.00
16.61
6


3516
C
GLN
A
440
51.339
62.729
60.910
1.00
19.80
6


3517
O
GLN
A
440
52.198
62.543
61.812
1.00
18.55
8


3518
CB
GLN
A
440
52.905
63.422
59.081
1.00
23.60
6


3519
CG
GLN
A
440
53.543
62.971
57.761
1.00
37.17
6


3520
CD
GLN
A
440
54.248
61.634
57.810
1.00
48.48
6


3521
OE1
GLN
A
440
55.292
61.462
58.444
1.00
57.64
8


3522
NE2
GLN
A
440
53.729
60.605
57.127
1.00
54.59
7


3523
N
SER
A
441
50.115
63.161
61.192
1.00
13.09
7


3524
CA
SER
A
441
49.738
63.516
62.559
1.00
13.14
6


3525
C
SER
A
441
48.481
62.739
62.958
1.00
18.60
6


3526
O
SER
A
441
47.524
62.718
62.168
1.00
15.27
8


3527
CB
SER
A
441
49.451
65.025
62.702
1.00
16.00
6


3528
OG
SER
A
441
50.658
65.770
62.516
1.00
17.34
8


3529
N
SER
A
442
48.417
62.251
64.198
1.00
13.46
7


3530
CA
SER
A
442
47.177
61.703
64.730
1.00
13.64
6


3531
C
SER
A
442
46.581
62.835
65.599
1.00
14.33
6


3532
O
SER
A
442
47.366
63.761
65.974
1.00
15.22
8


3533
CB
SER
A
442
47.452
60.598
65.791
1.00
15.48
6


3534
OG
SER
A
442
48.033
59.420
65.203
1.00
19.49
8


3535
N
TYR
A
443
45.302
62.845
65.817
1.00
13.24
7


3536
CA
TYR
A
443
44.693
63.886
66.694
1.00
12.26
6


3537
C
TYR
A
443
43.877
63.156
67.749
1.00
14.89
6


3538
O
TYR
A
443
43.032
62.293
67.451
1.00
14.44
8


3539
CB
TYR
A
443
43.772
64.824
65.860
1.00
13.59
6


3540
CG
TYR
A
443
44.592
65.807
65.009
1.00
10.92
6


3541
CD1
TYR
A
443
45.124
66.940
65.629
1.00
12.95
6


3542
CD2
TYR
A
443
44.836
65.549
63.667
1.00
12.89
6


3543
CE1
TYR
A
443
45.908
67.843
64.882
1.00
11.89
6


3544
CE2
TYR
A
443
45.595
66.474
62.914
1.00
11.54
6


3545
CZ
TYR
A
443
46.107
67.595
63.551
1.00
12.16
6


3546
OH
TYR
A
443
46.871
68.508
62.811
1.00
15.42
8


3547
N
SER
A
444
43.976
63.663
69.008
1.00
14.60
7


3548
CA
SER
A
444
43.034
63.232
70.040
1.00
14.67
6


3549
C
SER
A
444
41.698
64.002
69.912
1.00
13.95
6


3550
O
SER
A
444
41.739
65.229
69.879
1.00
16.35
8


3551
CB
SER
A
444
43.620
63.684
71.418
1.00
17.27
6


3552
OG
SER
A
444
44.701
62.764
71.733
1.00
18.88
8


3553
N
ILE
A
445
40.628
63.265
69.758
1.00
15.00
7


3554
CA
ILE
A
445
39.303
63.892
69.559
1.00
13.10
6


3555
C
ILE
A
445
38.498
63.757
70.863
1.00
14.11
6


3556
O
ILE
A
445
37.935
62.703
71.131
1.00
17.51
8


3557
CB
ILE
A
445
38.537
63.188
68.403
1.00
14.59
6


3558
CG1
ILE
A
445
39.386
63.120
67.136
1.00
15.39
6


3559
CG2
ILE
A
445
37.159
63.906
68.223
1.00
16.44
6


3560
CD1
ILE
A
445
39.772
64.500
66.533
1.00
15.53
6


3561
N
SER
A
446
38.309
64.925
71.501
1.00
15.73
7


3562
CA
SER
A
446
37.450
65.018
72.680
1.00
16.64
6


3563
C
SER
A
446
36.394
66.091
72.415
1.00
18.39
6


3564
O
SER
A
446
36.592
67.021
71.653
1.00
18.43
8


3565
CB
SER
A
446
38.248
65.398
73.972
1.00
18.77
6


3566
OG
SER
A
446
38.784
66.689
73.750
1.00
24.38
8


3567
N
GLY
A
447
35.263
65.958
73.091
1.00
19.05
7


3568
CA
GLY
A
447
34.169
66.916
73.050
1.00
17.05
6


3569
C
GLY
A
447
33.253
66.660
71.829
1.00
20.26
6


3570
O
GLY
A
447
32.491
67.554
71.467
1.00
19.38
8


3571
N
LEU
A
448
33.487
65.502
71.171
1.00
13.94
7


3572
CA
LEU
A
448
32.625
65.262
69.967
1.00
15.40
6


3573
C
LEU
A
448
31.245
64.853
70.386
1.00
16.78
6


3574
O
LEU
A
448
31.018
63.906
71.155
1.00
17.47
8


3575
CB
LEU
A
448
33.312
64.155
69.144
1.00
14.08
6


3576
CG
LEU
A
448
32.578
63.628
67.903
1.00
15.34
6


3577
CD1
LEU
A
448
32.403
64.740
66.845
1.00
16.18
6


3578
CD2
LEU
A
448
33.283
62.449
67.256
1.00
13.42
6


3579
N
GLN
A
449
30.221
65.509
69.814
1.00
13.16
7


3580
CA
GLN
A
449
28.812
65.224
70.018
1.00
14.91
6


3581
C
GLN
A
449
28.209
64.630
68.734
1.00
16.76
6


3582
O
GLN
A
449
28.754
64.827
67.645
1.00
13.94
8


3583
CB
AGLN
A
449
28.054
66.486
70.470
0.50
18.23
6


3584
CG
AGLN
A
449
28.884
67.206
71.540
0.50
24.01
6


3585
CD
AGLN
A
449
28.211
68.188
72.449
0.50
23.44
6


3586
OE1
AGLN
A
449
28.812
68.606
73.455
0.50
32.55
8


3587
NE2
AGLN
A
449
26.984
68.573
72.134
0.50
32.22
7


3583
CB
BGLN
A
449
27.974
66.473
70.339
0.50
13.26
6


3584
CG
BGLN
A
449
28.536
67.122
71.620
0.50
17.72
6


3585
CD
BGLN
A
449
28.037
66.396
72.844
0.50
16.00
6


3586
OE1
BGLN
A
449
28.776
65.702
73.511
0.50
22.43
8


3587
NE2
BGLN
A
449
26.759
66.550
73.145
0.50
23.34
7


3588
N
THR
A
450
27.085
63.965
68.897
1.00
15.61
7


3589
CA
THR
A
450
26.481
63.264
67.761
1.00
13.97
6


3590
C
THR
A
450
24.998
63.001
67.994
1.00
16.43
6


3591
O
THR
A
450
24.528
62.925
69.160
1.00
16.61
8


3592
CB
THR
A
450
27.216
61.912
67.566
1.00
15.00
6


3593
OG1
THR
A
450
26.686
61.176
66.471
1.00
15.07
8


3594
CG2
THR
A
450
27.007
61.016
68.814
1.00
18.27
6


3595
N
ALA
A
451
24.286
62.806
66.886
1.00
15.10
7


3596
CA
ALA
A
451
22.898
62.330
66.941
1.00
16.96
6


3597
C
ALA
A
451
22.799
60.830
66.879
1.00
15.04
6


3598
O
ALA
A
451
21.681
60.282
66.900
1.00
15.44
8


3599
CB
ALA
A
451
22.212
62.946
65.681
1.00
16.26
6


3600
N
LEU
A
452
23.929
60.083
66.788
1.00
14.57
7


3601
CA
LEU
A
452
23.803
58.623
66.814
1.00
12.45
6


3602
C
LEU
A
452
23.170
58.200
68.158
1.00
17.32
6


3603
O
LEU
A
452
23.505
58.727
69.218
1.00
17.00
8


3604
CB
LEU
A
452
25.201
57.989
66.779
1.00
14.27
6


3605
CG
LEU
A
452
25.854
58.082
65.380
1.00
14.43
6


3606
CD1
LEU
A
452
27.344
57.716
65.610
1.00
13.81
6


3607
CD2
LEU
A
452
25.263
57.102
64.375
1.00
14.40
6


3608
N
PRO
A
453
22.383
57.163
68.080
1.00
16.12
7


3609
CA
PRO
A
453
21.808
56.539
69.305
1.00
18.87
6


3610
C
PRO
A
453
22.936
55.882
70.090
1.00
19.68
6


3611
O
PRO
A
453
24.039
55.532
69.686
1.00
18.19
8


3612
CB
PRO
A
453
20.796
55.523
68.880
1.00
20.41
6


3613
CG
PRO
A
453
20.615
55.743
67.392
1.00
21.35
6


3614
CD
PRO
A
453
21.806
56.582
66.872
1.00
16.78
6


3615
N
ASN
A
454
22.619
55.684
71.406
1.00
14.58
7


3616
CA
ASN
A
454
23.630
55.025
72.244
1.00
14.89
6


3617
C
ASN
A
454
24.085
53.704
71.712
1.00
18.47
6


3618
O
ASN
A
454
23.320
52.881
71.168
1.00
17.84
8


3619
CB
ASN
A
454
22.851
54.705
73.573
1.00
17.80
6


3620
CG
ASN
A
454
22.656
55.933
74.421
1.00
24.08
6


3621
OD1
ASN
A
454
23.071
57.055
74.201
1.00
19.24
8


3622
ND2
ASN
A
454
21.941
55.757
75.554
1.00
24.42
7


3623
N
GLY
A
455
25.378
53.451
71.950
1.00
17.75
7


3624
CA
GLY
A
455
25.919
52.156
71.553
1.00
20.13
6


3625
C
GLY
A
455
27.422
52.289
71.172
1.00
17.39
6


3626
O
GLY
A
455
27.899
53.393
71.080
1.00
19.07
8


3627
N
SER
A
456
27.916
51.112
70.814
1.00
18.37
7


3628
CA
SER
A
456
29.286
51.073
70.261
1.00
17.34
6


3629
C
SER
A
456
29.173
50.927
68.725
1.00
17.80
6


3630
O
SER
A
456
28.322
50.199
68.220
1.00
20.53
8


3631
CB
SER
A
456
29.916
49.747
70.778
1.00
22.39
6


3632
OG
SER
A
456
30.178
49.998
72.161
1.00
30.42
8


3633
N
TYR
A
457
30.024
51.683
68.013
1.00
15.08
7


3634
CA
TYR
A
457
29.941
51.627
66.559
1.00
13.18
6


3635
C
TYR
A
457
31.301
51.229
65.961
1.00
14.20
6


3636
O
TYR
A
457
32.257
51.915
66.259
1.00
16.66
8


3637
CB
TYR
A
457
29.564
53.017
65.941
1.00
17.47
6


3638
CG
TYR
A
457
28.122
53.387
66.241
1.00
15.26
6


3639
CD1
TYR
A
457
27.799
53.933
67.497
1.00
15.37
6


3640
CD2
TYR
A
457
27.077
53.174
65.325
1.00
16.16
6


3641
CE1
TYR
A
457
26.521
54.297
67.873
1.00
15.82
6


3642
CE2
TYR
A
457
25.768
53.516
65.671
1.00
15.99
6


3643
CZ
TYR
A
457
25.523
54.070
66.928
1.00
16.37
6


3644
OH
TYR
A
457
24.210
54.401
67.218
1.00
16.11
8


3645
N
ALA
A
458
31.329
50.211
65.128
1.00
14.59
7


3646
CA
ALA
A
458
32.601
49.943
64.445
1.00
17.03
6


3647
C
ALA
A
458
32.686
50.915
63.247
1.00
14.66
6


3648
O
ALA
A
458
31.654
51.326
62.731
1.00
14.84
8


3649
CB
ALA
A
458
32.638
48.538
63.857
1.00
17.50
6


3650
N
ASP
A
459
33.942
51.128
62.831
1.00
13.42
7


3651
CA
ASP
A
459
34.082
51.858
61.521
1.00
11.91
6


3652
C
ASP
A
459
33.472
51.048
60.410
1.00
12.75
6


3653
O
ASP
A
459
33.679
49.834
60.222
1.00
13.42
8


3654
CB
ASP
A
459
35.567
52.007
61.258
1.00
12.66
6


3655
CG
ASP
A
459
35.984
52.522
59.876
1.00
13.56
6


3656
OD1
ASP
A
459
35.143
53.232
59.328
1.00
12.36
8


3657
OD2
ASP
A
459
37.109
52.170
59.441
1.00
14.11
8


3658
N
TYR
A
460
32.581
51.730
59.662
1.00
11.96
7


3659
CA
TYR
A
460
31.927
51.022
58.513
1.00
13.29
6


3660
C
TYR
A
460
32.905
50.541
57.467
1.00
16.04
6


3661
O
TYR
A
460
32.617
49.627
56.683
1.00
15.32
8


3662
CB
TYR
A
460
30.909
52.021
57.931
1.00
13.60
6


3663
CG
TYR
A
460
29.970
51.418
56.899
1.00
13.06
6


3664
CD1
TYR
A
460
28.809
50.815
57.400
1.00
11.63
6


3665
CD2
TYR
A
460
30.215
51.365
55.532
1.00
16.49
6


3666
CE1
TYR
A
460
27.838
50.274
56.514
1.00
15.86
6


3667
CE2
TYR
A
460
29.278
50.783
54.662
1.00
15.66
6


3668
CZ
TYR
A
460
28.098
50.257
55.165
1.00
17.45
6


3669
OH
TYR
A
460
27.209
49.696
54.262
1.00
16.44
8


3670
N
LEU
A
461
34.057
51.242
57.374
1.00
13.04
7


3671
CA
LEU
A
461
35.137
50.814
56.424
1.00
13.89
6


3672
C
LEU
A
461
36.026
49.742
57.023
1.00
14.71
6


3673
O
LEU
A
461
36.992
49.331
56.369
1.00
13.39
8


3674
CB
LEU
A
461
35.968
52.115
56.171
1.00
13.08
6


3675
CG
LEU
A
461
35.299
53.075
55.149
1.00
13.44
6


3676
CD1
LEU
A
461
35.968
54.453
55.284
1.00
14.44
6


3677
CD2
LEU
A
461
35.485
52.526
53.743
1.00
16.37
6


3678
N
SER
A
462
35.746
49.218
58.222
1.00
15.11
7


3679
CA
SER
A
462
36.521
48.122
58.810
1.00
16.17
6


3680
C
SER
A
462
38.011
48.422
58.907
1.00
17.10
6


3681
O
SER
A
462
38.878
47.546
58.763
1.00
16.40
8


3682
CB
SER
A
462
36.316
46.813
57.987
1.00
19.17
6


3683
OG
SER
A
462
34.914
46.479
57.974
1.00
20.76
8


3684
N
GLY
A
463
38.369
49.689
59.115
1.00
13.98
7


3685
CA
GLY
A
463
39.781
50.089
59.271
1.00
14.97
6


3686
C
GLY
A
463
40.533
50.140
57.949
1.00
15.42
6


3687
O
GLY
A
463
41.745
50.387
57.984
1.00
15.84
8


3688
N
LEU
A
464
39.816
50.043
56.808
1.00
12.86
7


3689
CA
LEU
A
464
40.559
50.113
55.525
1.00
10.93
6


3690
C
LEU
A
464
41.370
51.420
55.427
1.00
12.62
6


3691
O
LEU
A
464
42.484
51.408
54.854
1.00
14.36
8


3692
CB
LEU
A
464
39.487
50.148
54.402
1.00
13.24
6


3693
CG
LEU
A
464
40.083
50.223
52.969
1.00
14.42
6


3694
CD1
LEU
A
464
40.800
48.892
52.620
1.00
15.93
6


3695
CD2
LEU
A
464
38.971
50.469
51.967
1.00
14.00
6


3696
N
LEU
A
465
40.797
52.526
55.872
1.00
11.79
7


3697
CA
LEU
A
465
41.473
53.824
55.761
1.00
12.51
6


3698
C
LEU
A
465
41.953
54.319
57.114
1.00
13.32
6


3699
O
LEU
A
465
41.873
55.518
57.401
1.00
16.12
8


3700
CB
LEU
A
465
40.510
54.894
55.130
1.00
12.90
6


3701
CG
LEU
A
465
40.090
54.441
53.714
1.00
12.88
6


3702
CD1
LEU
A
465
39.162
55.509
53.111
1.00
14.96
6


3703
CD2
LEU
A
465
41.263
54.191
52.777
1.00
14.83
6


3704
N
GLY
A
466
42.237
53.348
58.043
1.00
14.06
7


3705
CA
GLY
A
466
42.789
53.800
59.336
1.00
14.74
6


3706
C
GLY
A
466
41.735
54.095
60.400
1.00
14.06
6


3707
O
GLY
A
466
42.061
54.643
61.479
1.00
15.13
8


3708
N
GLY
A
467
40.451
53.817
60.125
1.00
13.86
7


3709
CA
GLY
A
467
39.357
54.137
61.045
1.00
11.80
6


3710
C
GLY
A
467
39.321
53.244
62.311
1.00
14.35
6


3711
O
GLY
A
467
40.083
52.261
62.394
1.00
16.59
8


3712
N
ASN
A
468
38.509
53.696
63.236
1.00
15.29
7


3713
CA
ASN
A
468
38.483
53.050
64.569
1.00
14.61
6


3714
C
ASN
A
468
37.007
52.960
64.963
1.00
15.14
6


3715
O
ASN
A
468
36.145
53.679
64.418
1.00
15.07
8


3716
CB
ASN
A
468
39.253
54.012
65.515
1.00
16.45
6


3717
CG
ASN
A
468
38.730
55.429
65.538
1.00
17.15
6


3718
OD1
ASN
A
468
39.013
56.375
64.739
1.00
19.92
8


3719
ND2
ASN
A
468
37.812
55.710
66.490
1.00
16.39
7


3720
N
GLY
A
469
36.787
52.285
66.076
1.00
16.49
7


3721
CA
GLY
A
469
35.415
52.189
66.624
1.00
16.85
6


3722
C
GLY
A
469
35.261
53.309
67.640
1.00
14.55
6


3723
O
GLY
A
469
36.191
53.919
68.176
1.00
17.51
8


3724
N
ILE
A
470
33.976
53.624
67.954
1.00
14.83
7


3725
CA
ILE
A
470
33.623
54.650
68.921
1.00
14.09
6


3726
C
ILE
A
470
32.518
54.102
69.860
1.00
13.92
6


3727
O
ILE
A
470
31.867
53.108
69.553
1.00
19.57
8


3728
CB
ILE
A
470
33.155
56.004
68.368
1.00
16.37
6


3729
CG1
ILE
A
470
31.948
55.753
67.429
1.00
17.51
6


3730
CG2
ILE
A
470
34.319
56.652
67.581
1.00
16.76
6


3731
CD1
ILE
A
470
31.315
57.104
67.032
1.00
15.78
6


3732
N
SER
A
471
32.408
54.804
70.980
1.00
15.71
7


3733
CA
SER
A
471
31.268
54.477
71.903
1.00
14.51
6


3734
C
SER
A
471
30.497
55.755
72.165
1.00
14.83
6


3735
O
SER
A
471
31.107
56.814
72.402
1.00
17.55
8


3736
CB
SER
A
471
32.024
54.018
73.220
1.00
22.00
6


3737
OG
SER
A
471
30.967
53.933
74.176
1.00
27.40
8


3738
N
VAL
A
472
29.172
55.712
72.054
1.00
14.69
7


3739
CA
VAL
A
472
28.298
56.834
72.186
1.00
14.15
6


3740
C
VAL
A
472
27.380
56.696
73.425
1.00
15.07
6


3741
O
VAL
A
472
26.764
55.638
73.563
1.00
19.05
8


3742
CB
VAL
A
472
27.433
56.903
70.900
1.00
15.53
6


3743
CG1
VAL
A
472
26.446
58.057
70.970
1.00
14.81
6


3744
CG2
VAL
A
472
28.376
57.153
69.691
1.00
18.40
6


3745
N
SER
A
473
27.351
57.767
74.184
1.00
15.80
7


3746
CA
SER
A
473
26.386
57.736
75.312
1.00
16.44
6


3747
C
SER
A
473
25.711
59.073
75.420
1.00
16.40
6


3748
O
SER
A
473
26.435
60.084
75.548
1.00
19.98
8


3749
CB
SER
A
473
27.214
57.446
76.594
1.00
21.00
6


3750
OG
SER
A
473
26.284
57.573
77.686
1.00
31.70
8


3751
N
ASN
A
474
24.396
59.107
75.308
1.00
18.40
7


3752
CA
ASN
A
474
23.632
60.348
75.444
1.00
19.45
6


3753
C
ASN
A
474
24.194
61.523
74.646
1.00
19.99
6


3754
O
ASN
A
474
24.363
62.658
75.103
1.00
15.86
8


3755
CB
ASN
A
474
23.685
60.707
76.968
1.00
22.35
6


3756
CG
ASN
A
474
22.991
59.572
77.722
1.00
31.24
6


3757
OD1
ASN
A
474
22.086
58.887
77.191
1.00
33.57
8


3758
ND2
ASN
A
474
23.579
59.303
78.890
1.00
32.67
7


3759
N
GLY
A
475
24.452
61.223
73.341
1.00
17.78
7


3760
CA
GLY
A
475
24.866
62.311
72.438
1.00
20.56
6


3761
C
GLY
A
475
26.369
62.573
72.430
1.00
18.34
6


3762
O
GLY
A
475
26.807
63.464
71.690
1.00
20.59
8


3763
N
SER
A
476
27.146
61.894
73.305
1.00
18.39
7


3764
CA
SER
A
476
28.563
62.222
73.451
1.00
14.26
6


3765
C
SER
A
476
29.384
61.026
72.974
1.00
17.38
6


3766
O
SER
A
476
29.103
59.902
73.358
1.00
18.38
8


3767
CB
ASER
A
476
28.931
62.557
74.900
0.70
19.66
6


3768
OG
ASER
A
476
28.330
63.803
75.257
0.70
22.12
8


3767
CB
BSER
A
476
28.870
62.465
74.932
0.30
18.16
6


3768
OG
BSER
A
476
30.220
62.822
75.127
0.30
20.85
8


3769
N
VAL
A
477
30.430
61.284
72.188
1.00
15.08
7


3770
CA
VAL
A
477
31.322
60.248
71.766
1.00
16.01
6


3771
C
VAL
A
477
32.549
60.211
72.699
1.00
14.42
6


3772
O
VAL
A
477
33.117
61.277
72.913
1.00
16.73
8


3773
CB
VAL
A
477
31.852
60.539
70.320
1.00
12.17
6


3774
CG1
VAL
A
477
32.718
59.377
69.872
1.00
15.08
6


3775
CG2
VAL
A
477
30.665
60.682
69.389
1.00
13.12
6


3776
N
ALA
A
478
32.802
59.035
73.236
1.00
17.39
7


3777
CA
ALA
A
478
33.956
58.962
74.181
1.00
17.45
6


3778
C
ALA
A
478
35.248
59.401
73.501
1.00
19.79
6


3779
O
ALA
A
478
35.398
59.204
72.298
1.00
15.95
8


3780
CB
ALA
A
478
34.031
57.543
74.731
1.00
18.76
6


3781
N
SER
A
479
36.152
60.069
74.181
1.00
15.72
7


3782
CA
SER
A
479
37.405
60.518
73.501
1.00
17.20
6


3783
C
SER
A
479
38.170
59.392
72.855
1.00
16.18
6


3784
O
SER
A
479
38.177
58.231
73.329
1.00
16.38
8


3785
CB
SER
A
479
38.262
61.218
74.569
1.00
23.12
6


3786
OG
SER
A
479
37.554
62.348
75.047
1.00
22.40
8


3787
N
PHE
A
480
38.774
59.656
71.674
1.00
16.00
7


3788
CA
PHE
A
480
39.449
58.638
70.881
1.00
15.01
6


3789
C
PHE
A
480
40.575
59.308
70.092
1.00
14.53
6


3790
O
PHE
A
480
40.568
60.548
70.019
1.00
17.08
8


3791
CB
PHE
A
480
38.538
57.834
69.938
1.00
14.92
6


3792
CG
PHE
A
480
37.888
58.695
68.846
1.00
15.98
6


3793
CD1
PHE
A
480
36.748
59.437
69.087
1.00
14.48
6


3794
CD2
PHE
A
480
38.493
58.728
67.589
1.00
14.19
6


3795
CE1
PHE
A
480
36.160
60.227
68.092
1.00
18.16
6


3796
CE2
PHE
A
480
37.899
59.513
66.609
1.00
18.21
6


3797
CZ
PHE
A
480
36.770
60.255
66.848
1.00
19.62
6


3798
N
THR
A
481
41.459
58.476
69.565
1.00
15.04
7


3799
CA
THR
A
481
42.525
59.036
68.696
1.00
12.66
6


3800
C
THR
A
481
42.186
58.783
67.223
1.00
14.82
6


3801
O
THR
A
481
41.811
57.641
66.885
1.00
16.40
8


3802
CB
THR
A
481
43.859
58.332
69.002
1.00
19.94
6


3803
OG1
THR
A
481
44.253
58.543
70.360
1.00
21.84
8


3804
CG2
THR
A
481
44.953
58.894
68.091
1.00
20.55
6


3805
N
LEU
A
482
42.216
59.860
66.454
1.00
14.98
7


3806
CA
LEU
A
482
42.004
59.690
64.991
1.00
13.06
6


3807
C
LEU
A
482
43.383
59.527
64.394
1.00
14.32
6


3808
O
LEU
A
482
44.199
60.432
64.487
1.00
15.20
8


3809
CB
LEU
A
482
41.231
60.917
64.486
1.00
13.14
6


3810
CG
LEU
A
482
40.812
60.936
62.999
1.00
14.96
6


3811
CD1
LEU
A
482
39.938
59.717
62.720
1.00
16.24
6


3812
CD2
LEU
A
482
40.073
62.242
62.727
1.00
14.36
6


3813
N
ALA
A
483
43.621
58.414
63.680
1.00
12.65
7


3814
CA
ALA
A
483
44.961
58.090
63.175
1.00
13.54
6


3815
C
ALA
A
483
45.370
58.961
62.000
1.00
13.15
6


3816
O
ALA
A
483
44.562
59.723
61.387
1.00
13.10
8


3817
CB
ALA
A
483
44.892
56.581
62.782
1.00
12.82
6


3818
N
PRO
A
484
46.637
58.980
61.687
1.00
14.66
7


3819
CA
PRO
A
484
47.183
59.827
60.632
1.00
11.27
6


3820
C
PRO
A
484
46.509
59.496
59.301
1.00
12.98
6


3821
O
PRO
A
484
46.374
58.331
58.884
1.00
13.40
8


3822
CB
PRO
A
484
48.704
59.546
60.545
1.00
15.48
6


3823
CG
PRO
A
484
48.959
58.945
61.936
1.00
15.92
6


3824
CD
PRO
A
484
47.698
58.160
62.333
1.00
15.61
6


3825
N
GLY
A
485
45.977
60.548
58.671
1.00
14.03
7


3826
CA
GLY
A
485
45.399
60.352
57.309
1.00
13.19
6


3827
C
GLY
A
485
44.067
59.600
57.376
1.00
16.21
6


3828
O
GLY
A
485
43.561
59.235
56.271
1.00
13.21
8


3829
N
ALA
A
486
43.508
59.349
58.553
1.00
11.65
7


3830
CA
ALA
A
486
42.375
58.395
58.545
1.00
13.98
6


3831
C
ALA
A
486
41.058
58.969
58.068
1.00
15.41
6


3832
O
ALA
A
486
40.730
60.148
58.196
1.00
13.33
8


3833
CB
ALA
A
486
42.233
57.937
60.002
1.00
14.43
6


3834
N
VAL
A
487
40.213
58.008
57.647
1.00
12.17
7


3835
CA
VAL
A
487
38.776
58.220
57.403
1.00
9.79
6


3836
C
VAL
A
487
38.057
57.174
58.257
1.00
9.96
6


3837
O
VAL
A
487
38.406
55.970
58.179
1.00
12.30
8


3838
CB
VAL
A
487
38.428
58.022
55.919
1.00
10.95
6


3839
CG1
VAL
A
487
36.871
58.150
55.762
1.00
12.89
6


3840
CG2
VAL
A
487
39.127
58.990
54.964
1.00
15.13
6


3841
N
SER
A
488
37.112
57.635
59.078
1.00
11.84
7


3842
CA
SER
A
488
36.335
56.623
59.865
1.00
12.18
6


3843
C
SER
A
488
34.867
56.972
59.699
1.00
11.64
6


3844
O
SER
A
488
34.519
58.154
59.650
1.00
12.81
8


3845
CB
SER
A
488
36.850
56.705
61.336
1.00
15.82
6


3846
OG
SER
A
488
36.431
55.439
61.907
1.00
19.75
8


3847
N
VAL
A
489
33.950
55.975
59.626
1.00
11.85
7


3848
CA
VAL
A
489
32.567
56.313
59.340
1.00
11.74
6


3849
C
VAL
A
489
31.685
55.457
60.269
1.00
12.51
6


3850
O
VAL
A
489
31.910
54.276
60.410
1.00
13.59
8


3851
CB
VAL
A
489
32.231
55.903
57.882
1.00
12.50
6


3852
CG1
VAL
A
489
30.712
56.154
57.650
1.00
11.14
6


3853
CG2
VAL
A
489
32.978
56.812
56.882
1.00
13.14
6


3854
N
TRP
A
490
30.771
56.135
60.914
1.00
11.35
7


3855
CA
TRP
A
490
29.900
55.413
61.883
1.00
11.90
6


3856
C
TRP
A
490
28.446
55.715
61.508
1.00
13.16
6


3857
O
TRP
A
490
28.103
56.878
61.324
1.00
16.40
8


3858
CB
TRP
A
490
30.222
55.953
63.283
1.00
12.61
6


3859
CG
TRP
A
490
31.708
55.807
63.639
1.00
12.91
6


3860
CD1
TRP
A
490
32.381
54.628
63.904
1.00
14.71
6


3861
CD2
TRP
A
490
32.632
56.884
63.716
1.00
14.18
6


3862
NE1
TRP
A
490
33.717
54.969
64.166
1.00
13.76
7


3863
CE2
TRP
A
490
33.883
56.328
64.049
1.00
14.41
6


3864
CE3
TRP
A
490
32.509
58.271
63.546
1.00
16.82
6


3865
CZ2
TRP
A
490
35.020
57.117
64.216
1.00
13.91
6


3866
CZ3
TRP
A
490
33.641
59.052
63.701
1.00
14.61
6


3867
CH2
TRP
A
490
34.894
58.461
64.044
1.00
14.54
6


3868
N
GLN
A
491
27.680
54.618
61.394
1.00
11.75
7


3869
CA
GLN
A
491
26.332
54.869
60.903
1.00
12.20
6


3870
C
GLN
A
491
25.221
54.121
61.637
1.00
13.63
6


3871
O
GLN
A
491
25.472
53.092
62.207
1.00
13.45
8


3872
CB
GLN
A
491
26.259
54.452
59.410
1.00
12.17
6


3873
CG
GLN
A
491
26.541
52.972
59.117
1.00
12.78
6


3874
CD
GLN
A
491
25.208
52.219
58.993
1.00
19.79
6


3875
OE1
GLN
A
491
24.222
52.726
58.485
1.00
16.61
8


3876
NE2
GLN
A
491
25.214
50.952
59.455
1.00
19.28
7


3877
N
TYR
A
492
24.024
54.698
61.523
1.00
13.67
7


3878
CA
TYR
A
492
22.819
54.043
62.092
1.00
14.21
6


3879
C
TYR
A
492
21.665
54.203
61.102
1.00
17.30
6


3880
O
TYR
A
492
21.507
55.341
60.614
1.00
14.76
8


3881
CB
TYR
A
492
22.452
54.774
63.393
1.00
15.27
6


3882
CG
TYR
A
492
21.152
54.219
63.984
1.00
15.56
6


3883
CD1
TYR
A
492
21.146
53.010
64.638
1.00
20.95
6


3884
CD2
TYR
A
492
19.963
54.959
63.800
1.00
18.48
6


3885
CE1
TYR
A
492
19.956
52.511
65.176
1.00
21.55
6


3886
CE2
TYR
A
492
18.770
54.444
64.324
1.00
19.51
6


3887
CZ
TYR
A
492
18.817
53.254
65.003
1.00
22.52
6


3888
OH
TYR
A
492
17.596
52.781
65.511
1.00
24.89
8


3889
N
SER
A
493
20.879
53.151
60.925
1.00
15.17
7


3890
CA
SER
A
493
19.666
53.363
60.096
1.00
14.91
6


3891
C
SER
A
493
18.548
52.462
60.616
1.00
20.17
6


3892
O
SER
A
493
18.887
51.457
61.265
1.00
22.90
8


3893
CB
SER
A
493
19.867
53.083
58.619
1.00
23.97
6


3894
OG
SER
A
493
20.148
51.710
58.532
1.00
30.62
8


3895
N
THR
A
494
17.344
52.991
60.393
1.00
15.89
7


3896
CA
THR
A
494
16.243
52.127
60.906
1.00
18.40
6


3897
C
THR
A
494
14.999
52.406
60.060
1.00
20.14
6


3898
O
THR
A
494
14.967
53.429
59.367
1.00
20.45
8


3899
CB
THR
A
494
15.993
52.424
62.396
1.00
24.38
6


3900
OG1
THR
A
494
15.137
51.363
62.864
1.00
25.66
8


3901
CG2
THR
A
494
15.368
53.751
62.737
1.00
27.09
6


3902
N
SER
A
495
14.017
51.534
60.157
1.00
22.56
7


3903
CA
SER
A
495
12.772
51.870
59.422
1.00
19.72
6


3904
C
SER
A
495
12.082
53.049
60.021
1.00
19.50
6


3905
O
SER
A
495
12.132
53.418
61.188
1.00
21.11
8


3906
CB
ASER
A
495
11.766
50.698
59.444
0.60
26.59
6


3907
OG
ASER
A
495
12.447
49.487
59.259
0.60
31.40
8


3907
CB
BSER
A
495
11.888
50.603
59.441
0.40
20.10
6


3908
OG
BSER
A
495
11.922
50.184
60.798
0.40
20.04
8


3908
N
ALA
A
496
11.315
53.727
59.141
1.00
20.53
7


3909
CA
ALA
A
496
10.529
54.893
59.493
1.00
21.55
6


3910
C
ALA
A
496
9.094
54.492
59.960
1.00
24.11
6


3911
O
ALA
A
496
8.536
53.596
59.350
1.00
29.93
8


3912
CB
ALA
A
496
10.354
55.717
58.189
1.00
22.92
6


3913
N
SER
A
497
8.599
55.279
60.902
1.00
26.84
7


3914
CA
SER
A
497
7.226
54.967
61.354
1.00
32.64
6


3915
C
SER
A
497
6.242
56.009
60.853
1.00
31.20
6


3916
O
SER
A
497
5.049
55.788
61.090
1.00
33.40
8


3917
CB
SER
A
497
7.183
54.836
62.875
1.00
35.13
6


3918
OG
SER
A
497
7.578
56.030
63.515
1.00
39.06
8


3919
N
ALA
A
498
6.685
56.920
59.967
1.00
25.21
7


3920
CA
ALA
A
498
5.749
57.878
59.354
1.00
21.05
6


3921
C
ALA
A
498
6.350
58.189
57.975
1.00
22.00
6


3922
O
ALA
A
498
7.541
57.907
57.763
1.00
18.25
8


3923
CB
ALA
A
498
5.737
59.103
60.231
1.00
22.15
6


3924
N
PRO
A
499
5.633
58.771
57.054
1.00
18.84
7


3925
CA
PRO
A
499
6.176
59.058
55.718
1.00
19.31
6


3926
C
PRO
A
499
7.174
60.210
55.762
1.00
15.69
6


3927
O
PRO
A
499
6.934
61.242
56.370
1.00
16.96
8


3928
CB
PRO
A
499
4.930
59.294
54.823
1.00
20.07
6


3929
CG
PRO
A
499
3.927
59.790
55.829
1.00
23.72
6


3930
CD
PRO
A
499
4.205
59.113
57.173
1.00
23.70
6


3931
N
GLN
A
500
8.288
59.975
55.037
1.00
18.24
7


3932
CA
GLN
A
500
9.423
60.939
55.075
1.00
13.65
6


3933
C
GLN
A
500
9.921
61.084
53.596
1.00
12.93
6


3934
O
GLN
A
500
10.256
60.065
53.014
1.00
15.78
8


3935
CB
GLN
A
500
10.601
60.286
55.860
1.00
15.18
6


3936
CG
GLN
A
500
10.189
60.048
57.328
1.00
16.32
6


3937
CD
GLN
A
500
11.284
59.264
58.126
1.00
15.95
6


3938
OE1
GLN
A
500
12.239
58.781
57.571
1.00
17.99
8


3939
NE2
GLN
A
500
11.008
59.238
59.419
1.00
20.52
7


3940
N
ILE
A
501
9.662
62.283
53.054
1.00
12.81
7


3941
CA
ILE
A
501
10.101
62.501
51.667
1.00
12.56
6


3942
C
ILE
A
501
11.594
62.914
51.642
1.00
13.47
6


3943
O
ILE
A
501
11.899
63.905
52.301
1.00
14.35
8


3944
CB
ILE
A
501
9.262
63.635
51.032
1.00
12.51
6


3945
CG1
ILE
A
501
7.788
63.216
50.842
1.00
14.81
6


3946
CG2
ILE
A
501
9.888
63.939
49.629
1.00
12.71
6


3947
CD1
ILE
A
501
6.897
64.308
50.244
1.00
15.70
6


3948
N
GLY
A
502
12.383
62.169
50.872
1.00
12.33
7


3949
CA
GLY
A
502
13.793
62.673
50.746
1.00
12.41
6


3950
C
GLY
A
502
13.915
63.416
49.403
1.00
11.68
6


3951
O
GLY
A
502
14.806
64.300
49.332
1.00
12.18
8


3952
N
SER
A
503
13.120
63.068
48.395
1.00
12.99
7


3953
CA
SER
A
503
13.334
63.710
47.073
1.00
12.73
6


3954
C
SER
A
503
11.970
63.672
46.342
1.00
14.01
6


3955
O
SER
A
503
11.263
62.678
46.449
1.00
14.22
8


3956
CB
SER
A
503
14.364
62.853
46.296
1.00
12.66
6


3957
OG
SER
A
503
14.467
63.267
44.940
1.00
12.94
8


3958
N
VAL
A
504
11.736
64.763
45.625
1.00
12.13
7


3959
CA
VAL
A
504
10.738
64.716
44.521
1.00
11.27
6


3960
C
VAL
A
504
11.521
65.159
43.243
1.00
11.68
6


3961
O
VAL
A
504
12.287
66.121
43.321
1.00
11.43
8


3962
CB
VAL
A
504
9.614
65.700
44.790
1.00
12.52
6


3963
CG1
VAL
A
504
8.670
65.766
43.563
1.00
15.49
6


3964
CG2
VAL
A
504
8.740
65.263
46.021
1.00
12.38
6


3965
N
ALA
A
505
11.424
64.285
42.236
1.00
11.00
7


3966
CA
ALA
A
505
12.174
64.595
41.003
1.00
10.56
6


3967
C
ALA
A
505
11.447
64.174
39.798
1.00
12.28
6


3968
O
ALA
A
505
10.738
63.165
39.919
1.00
13.54
8


3969
CB
ALA
A
505
13.567
63.894
41.072
1.00
11.90
6


3970
N
PRO
A
506
11.674
64.766
38.661
1.00
12.95
7


3971
CA
PRO
A
506
12.353
66.020
38.410
1.00
11.12
6


3972
C
PRO
A
506
11.747
67.182
39.194
1.00
12.55
6


3973
O
PRO
A
506
10.711
67.015
39.862
1.00
12.33
8


3974
CB
PRO
A
506
12.227
66.313
36.887
1.00
13.30
6


3975
CG
PRO
A
506
11.545
65.090
36.310
1.00
15.76
6


3976
CD
PRO
A
506
11.007
64.329
37.471
1.00
14.19
6


3977
N
ASN
A
507
12.364
68.381
39.142
1.00
10.92
7


3978
CA
ASN
A
507
11.835
69.493
39.909
1.00
11.12
6


3979
C
ASN
A
507
10.940
70.447
39.087
1.00
10.54
6


3980
O
ASN
A
507
10.497
71.416
39.701
1.00
12.30
8


3981
CB
ASN
A
507
13.043
70.353
40.401
1.00
11.79
6


3982
CG
ASN
A
507
14.033
69.459
41.196
1.00
14.07
6


3983
OD1
ASN
A
507
15.192
69.361
40.778
1.00
13.37
8


3984
ND2
ASN
A
507
13.592
68.845
42.261
1.00
13.47
7


3985
N
MET
A
508
10.654
70.046
37.850
1.00
10.20
7


3986
CA
MET
A
508
9.823
70.957
37.021
1.00
11.04
6


3987
C
MET
A
508
9.102
70.087
36.027
1.00
11.63
6


3988
O
MET
A
508
9.633
69.029
35.633
1.00
12.66
8


3989
CB
MET
A
508
10.929
71.782
36.219
1.00
12.80
6


3990
CG
MET
A
508
10.270
72.808
35.305
1.00
15.57
6


3991
SD
MET
A
508
11.558
73.692
34.325
1.00
12.60
16


3992
CE
MET
A
508
11.921
72.582
33.003
1.00
11.82
6


3993
N
GLY
A
509
7.935
70.545
35.550
1.00
11.36
7


3994
CA
GLY
A
509
7.253
69.739
34.528
1.00
10.02
6


3995
C
GLY
A
509
5.851
70.331
34.276
1.00
13.18
6


3996
O
GLY
A
509
5.506
71.321
34.889
1.00
13.82
8


3997
N
ILE
A
510
5.070
69.599
33.480
1.00
11.23
7


3998
CA
ILE
A
510
3.674
70.061
33.192
1.00
12.19
6


3999
C
ILE
A
510
2.746
68.964
33.701
1.00
11.61
6


4000
O
ILE
A
510
3.156
67.806
33.903
1.00
13.58
8


4001
CB
ILE
A
510
3.456
70.272
31.683
1.00
12.75
6


4002
CG1
ILE
A
510
3.840
69.011
30.868
1.00
11.82
6


4003
CG2
ILE
A
510
4.241
71.485
31.163
1.00
14.82
6


4004
CD1
ILE
A
510
3.293
69.108
29.417
1.00
18.53
6


4005
N
PRO
A
511
1.462
69.267
33.824
1.00
13.51
7


4006
CA
PRO
A
511
0.442
68.291
34.164
1.00
14.15
6


4007
C
PRO
A
511
0.531
67.082
33.263
1.00
13.29
6


4008
O
PRO
A
511
0.780
67.180
32.026
1.00
13.86
8


4009
CB
PRO
A
511
−0.913
69.037
33.810
1.00
13.10
6


4010
CG
PRO
A
511
−0.528
70.435
34.265
1.00
15.94
6


4011
CD
PRO
A
511
0.925
70.625
33.729
1.00
16.03
6


4012
N
GLY
A
512
0.462
65.892
33.876
1.00
12.55
7


4013
CA
GLY
A
512
0.554
64.629
33.165
1.00
14.21
6


4014
C
GLY
A
512
1.950
63.971
33.170
1.00
13.76
6


4015
O
GLY
A
512
2.002
62.765
32.923
1.00
15.31
8


4016
N
ASN
A
513
2.994
64.789
33.454
1.00
12.18
7


4017
CA
ASN
A
513
4.306
64.154
33.561
1.00
10.79
6


4018
C
ASN
A
513
4.360
63.144
34.731
1.00
15.27
6


4019
O
ASN
A
513
3.699
63.392
35.738
1.00
13.64
8


4020
CB
ASN
A
513
5.408
65.230
33.833
1.00
11.43
6


4021
CG
ASN
A
513
5.762
66.023
32.583
1.00
11.94
6


4022
OD1
ASN
A
513
6.738
66.874
32.746
1.00
16.21
8


4023
ND2
ASN
A
513
5.078
65.931
31.505
1.00
8.90
7


4024
N
VAL
A
514
5.280
62.177
34.576
1.00
11.74
7


4025
CA
VAL
A
514
5.505
61.269
35.745
1.00
11.63
6


4026
C
VAL
A
514
6.594
61.894
36.612
1.00
13.73
6


4027
O
VAL
A
514
7.617
62.379
36.131
1.00
15.35
8


4028
CB
VAL
A
514
6.072
59.931
35.221
1.00
13.67
6


4029
CG1
VAL
A
514
6.529
59.036
36.390
1.00
14.35
6


4030
CG2
VAL
A
514
5.042
59.176
34.393
1.00
16.73
6


4031
N
VAL
A
515
6.335
61.959
37.923
1.00
10.41
7


4032
CA
VAL
A
515
7.256
62.496
38.927
1.00
12.67
6


4033
C
VAL
A
515
7.433
61.442
40.001
1.00
13.31
6


4034
O
VAL
A
515
6.495
60.711
40.306
1.00
14.78
8


4035
CB
VAL
A
515
6.563
63.772
39.511
1.00
14.30
6


4036
CG1
VAL
A
515
7.228
64.271
40.775
1.00
18.11
6


4037
CG2
VAL
A
515
6.678
64.883
38.435
1.00
16.90
6


4038
N
THR
A
516
8.669
61.321
40.514
1.00
11.19
7


4039
CA
THR
A
516
8.900
60.252
41.495
1.00
11.78
6


4040
C
THR
A
516
9.271
60.860
42.835
1.00
11.71
6


4041
O
THR
A
516
10.092
61.763
42.959
1.00
12.89
8


4042
CB
THR
A
516
10.107
59.384
41.001
1.00
14.88
6


4043
OG1
THR
A
516
9.696
58.789
39.742
1.00
14.59
8


4044
CG2
THR
A
516
10.446
58.275
42.004
1.00
14.18
6


4045
N
ILE
A
517
8.600
60.281
43.863
1.00
9.66
7


4046
CA
ILE
A
517
8.878
60.681
45.251
1.00
10.17
6


4047
C
ILE
A
517
9.670
59.586
45.920
1.00
13.57
6


4048
O
ILE
A
517
9.172
58.427
45.949
1.00
13.82
8


4049
CB
ILE
A
517
7.493
60.899
45.948
1.00
12.16
6


4050
CG1
ILE
A
517
6.659
61.984
45.278
1.00
15.38
6


4051
CG2
ILE
A
517
7.745
61.419
47.392
1.00
14.69
6


4052
CD1
ILE
A
517
5.200
61.951
45.779
1.00
22.16
6


4053
N
ASP
A
518
10.911
59.861
46.363
1.00
13.29
7


4054
CA
ASP
A
518
11.743
58.802
46.976
1.00
14.12
6


4055
C
ASP
A
518
11.868
59.161
48.435
1.00
13.11
6


4056
O
ASP
A
518
11.922
60.347
48.791
1.00
14.37
8


4057
CB
ASP
A
518
13.159
58.791
46.351
1.00
14.49
6


4058
CG
ASP
A
518
13.106
58.207
44.962
1.00
17.62
6


4059
OD1
ASP
A
518
12.858
56.963
44.888
1.00
17.47
8


4060
OD2
ASP
A
518
13.289
58.874
43.931
1.00
16.96
8


4061
N
GLY
A
519
11.769
58.138
49.315
1.00
13.39
7


4062
CA
GLY
A
519
11.872
58.484
50.757
1.00
14.21
6


4063
C
GLY
A
519
11.716
57.152
51.549
1.00
13.61
6


4064
O
GLY
A
519
12.278
56.130
51.134
1.00
15.70
8


4065
N
LYS
A
520
11.059
57.319
52.696
1.00
17.22
7


4066
CA
LYS
A
520
10.867
56.091
53.545
1.00
15.85
6


4067
C
LYS
A
520
9.539
56.230
54.256
1.00
16.54
6


4068
O
LYS
A
520
9.004
57.334
54.385
1.00
17.43
8


4069
CB
LYS
A
520
11.866
56.344
54.747
1.00
17.75
6


4070
CG
LYS
A
520
13.318
56.307
54.421
1.00
24.98
6


4071
CD
LYS
A
520
14.147
56.512
55.698
1.00
22.21
6


4072
CE
LYS
A
520
14.074
55.145
56.459
1.00
23.54
6


4073
NZ
LYS
A
520
15.426
54.879
57.005
1.00
27.08
7


4074
N
GLY
A
521
9.021
55.065
54.728
1.00
16.42
7


4075
CA
GLY
A
521
7.870
55.223
55.627
1.00
16.98
6


4076
C
GLY
A
521
6.540
55.347
54.874
1.00
19.49
6


4077
O
GLY
A
521
5.533
55.716
55.525
1.00
18.22
8


4078
N
PHE
A
522
6.569
55.053
53.560
1.00
19.15
7


4079
CA
PHE
A
522
5.299
55.230
52.839
1.00
17.53
6


4080
C
PHE
A
522
4.344
54.037
53.029
1.00
20.57
6


4081
O
PHE
A
522
3.173
54.222
52.638
1.00
20.45
8


4082
CB
PHE
A
522
5.587
55.448
51.342
1.00
17.55
6


4083
CG
PHE
A
522
6.513
56.605
51.009
1.00
15.40
6


4084
CD1
PHE
A
522
6.601
57.740
51.763
1.00
17.48
6


4085
CD2
PHE
A
522
7.262
56.452
49.824
1.00
17.80
6


4086
CE1
PHE
A
522
7.480
58.778
51.376
1.00
20.21
6


4087
CE2
PHE
A
522
8.142
57.475
49.422
1.00
16.35
6


4088
CZ
PHE
A
522
8.257
58.607
50.214
1.00
14.66
6


4089
N
GLY
A
523
4.826
52.902
53.488
1.00
23.38
7


4090
CA
GLY
A
523
3.947
51.721
53.586
1.00
26.21
6


4091
C
GLY
A
523
3.753
51.037
52.260
1.00
27.39
6


4092
O
GLY
A
523
4.082
51.536
51.167
1.00
21.64
8


4093
N
THR
A
524
3.204
49.785
52.316
1.00
26.00
7


4094
CA
THR
A
524
3.043
49.010
51.103
1.00
24.30
6


4095
C
THR
A
524
1.636
49.241
50.556
1.00
26.74
6


4096
O
THR
A
524
1.433
48.984
49.372
1.00
34.03
8


4097
CB
THR
A
524
3.314
47.505
51.308
1.00
36.63
6


4098
OG1
THR
A
524
2.403
47.020
52.315
1.00
34.71
8


4099
CG2
THR
A
524
4.711
47.251
51.862
1.00
34.40
6


4100
N
THR
A
525
0.748
49.673
51.432
1.00
27.38
7


4101
CA
THR
A
525
−0.646
49.948
51.027
1.00
29.73
6


4102
C
THR
A
525
−0.696
51.367
50.456
1.00
29.44
6


4103
O
THR
A
525
−0.315
52.313
51.159
1.00
28.46
8


4104
CB
THR
A
525
−1.558
49.835
52.265
1.00
31.59
6


4105
OG1
THR
A
525
−1.416
48.485
52.779
1.00
34.50
8


4106
CG2
THR
A
525
−3.020
50.076
51.920
1.00
33.53
6


4107
N
GLN
A
526
−1.341
51.530
49.304
1.00
26.38
7


4108
CA
GLN
A
526
−1.383
52.864
48.695
1.00
27.25
6


4109
C
GLN
A
526
−2.090
53.867
49.574
1.00
29.32
6


4110
O
GLN
A
526
−3.264
53.665
49.960
1.00
25.61
8


4111
CB
GLN
A
526
−2.101
52.757
47.340
1.00
28.17
6


4112
CG
GLN
A
526
−2.028
53.996
46.486
1.00
30.46
6


4113
CD
GLN
A
526
−2.542
53.744
45.055
1.00
28.73
6


4114
OE1
GLN
A
526
−3.419
54.518
44.679
1.00
33.21
8


4115
NE2
GLN
A
526
−1.951
52.750
44.438
1.00
31.17
7


4116
N
GLY
A
527
−1.476
55.032
49.820
1.00
22.05
7


4117
CA
GLY
A
527
−2.091
56.150
50.508
1.00
20.00
6


4118
C
GLY
A
527
−2.415
57.258
49.471
1.00
19.58
6


4119
O
GLY
A
527
−2.894
56.897
48.405
1.00
21.95
8


4120
N
THR
A
528
−2.136
58.506
49.804
1.00
21.30
7


4121
CA
THR
A
528
−2.428
59.597
48.884
1.00
18.42
6


4122
C
THR
A
528
−1.268
60.584
48.808
1.00
21.48
6


4123
O
THR
A
528
−0.375
60.642
49.647
1.00
20.31
8


4124
CB
THR
A
528
−3.685
60.387
49.320
1.00
24.98
6


4125
OG1
THR
A
528
−3.522
60.782
50.657
1.00
30.73
8


4126
CG2
THR
A
528
−4.933
59.511
49.240
1.00
26.25
6


4127
N
VAL
A
529
−1.209
61.255
47.667
1.00
16.67
7


4128
CA
VAL
A
529
−0.167
62.275
47.425
1.00
15.19
6


4129
C
VAL
A
529
−0.924
63.532
46.987
1.00
16.18
6


4130
O
VAL
A
529
−1.825
63.328
46.155
1.00
16.64
8


4131
CB
VAL
A
529
0.700
61.851
46.216
1.00
14.16
6


4132
CG1
VAL
A
529
1.664
62.995
45.841
1.00
17.46
6


4133
CG2
VAL
A
529
1.483
60.594
46.604
1.00
18.23
6


4134
N
THR
A
530
−0.533
64.669
47.531
1.00
14.50
7


4135
CA
THR
A
530
−1.148
65.900
47.016
1.00
14.78
6


4136
C
THR
A
530
−0.038
66.814
46.492
1.00
17.57
6


4137
O
THR
A
530
1.076
66.792
47.027
1.00
15.22
8


4138
CB
THR
A
530
−1.954
66.621
48.090
1.00
15.93
6


4139
OG1
THR
A
530
−1.209
66.722
49.308
1.00
17.69
8


4140
CG2
THR
A
530
−3.279
65.858
48.340
1.00
17.39
6


4141
N
PHE
A
531
−0.395
67.691
45.569
1.00
14.04
7


4142
CA
PHE
A
531
0.458
68.822
45.142
1.00
13.01
6


4143
C
PHE
A
531
−0.344
70.073
45.496
1.00
15.03
6


4144
O
PHE
A
531
−1.454
70.292
44.989
1.00
16.16
8


4145
CB
PHE
A
531
0.659
68.823
43.604
1.00
13.87
6


4146
CG
PHE
A
531
1.611
67.777
43.040
1.00
13.21
6


4147
CD1
PHE
A
531
1.438
66.431
43.191
1.00
14.34
6


4148
CD2
PHE
A
531
2.662
68.228
42.240
1.00
14.96
6


4149
CE1
PHE
A
531
2.288
65.515
42.629
1.00
16.70
6


4150
CE2
PHE
A
531
3.545
67.306
41.691
1.00
13.81
6


4151
CZ
PHE
A
531
3.385
65.943
41.836
1.00
16.70
6


4152
N
GLY
A
532
0.118
70.806
46.490
1.00
14.18
7


4153
CA
GLY
A
532
−0.569
72.077
46.884
1.00
15.57
6


4154
C
GLY
A
532
−1.992
71.702
47.378
1.00
19.88
6


4155
O
GLY
A
532
−2.928
72.482
47.068
1.00
18.91
8


4156
N
GLY
A
533
−2.193
70.510
47.921
1.00
17.41
7


4157
CA
GLY
A
533
−3.524
70.089
48.400
1.00
18.31
6


4158
C
GLY
A
533
−4.368
69.372
47.370
1.00
20.08
6


4159
O
GLY
A
533
−5.463
68.817
47.637
1.00
19.31
8


4160
N
VAL
A
534
−3.923
69.391
46.097
1.00
16.06
7


4161
CA
VAL
A
534
−4.592
68.721
44.999
1.00
15.11
6


4162
C
VAL
A
534
−4.197
67.275
44.894
1.00
15.67
6


4163
O
VAL
A
534
−3.019
66.888
44.712
1.00
17.94
8


4164
CB
VAL
A
534
−4.368
69.480
43.645
1.00
13.67
6


4165
CG1
VAL
A
534
−5.101
68.739
42.509
1.00
15.45
6


4166
CG2
VAL
A
534
−4.807
70.937
43.768
1.00
16.93
6


4167
N
THR
A
535
−5.185
66.334
44.967
1.00
13.93
7


4168
CA
THR
A
535
−4.827
64.927
44.890
1.00
16.87
6


4169
C
THR
A
535
−4.271
64.521
43.536
1.00
20.28
6


4170
O
THR
A
535
−4.796
64.893
42.462
1.00
17.64
8


4171
CB
THR
A
535
−6.065
64.042
45.192
1.00
20.23
6


4172
OG1
THR
A
535
−6.446
64.284
46.576
1.00
20.94
8


4173
CG2
THR
A
535
−5.787
62.565
45.026
1.00
24.73
6


4174
N
ALA
A
536
−3.162
63.773
43.562
1.00
15.87
7


4175
CA
ALA
A
536
−2.521
63.324
42.337
1.00
17.27
6


4176
C
ALA
A
536
−2.808
61.859
42.042
1.00
20.29
6


4177
O
ALA
A
536
−2.929
61.111
43.030
1.00
20.32
8


4178
CB
ALA
A
536
−0.976
63.441
42.384
1.00
17.03
6


4179
N
THR
A
537
−2.937
61.461
40.791
1.00
16.03
7


4180
CA
THR
A
537
−3.151
60.043
40.489
1.00
15.38
6


4181
C
THR
A
537
−1.865
59.242
40.679
1.00
19.21
6


4182
O
THR
A
537
−0.823
59.697
40.166
1.00
19.02
8


4183
CB
THR
A
537
−3.564
59.955
38.998
1.00
18.90
6


4184
OG1
THR
A
537
−4.828
60.651
38.950
1.00
19.30
8


4185
CG2
THR
A
537
−3.697
58.508
38.591
1.00
18.81
6


4186
N
VAL
A
538
−1.925
58.176
41.415
1.00
16.51
7


4187
CA
VAL
A
538
−0.704
57.394
41.746
1.00
16.38
6


4188
C
VAL
A
538
−0.516
56.415
40.613
1.00
18.34
6


4189
O
VAL
A
538
−1.390
55.599
40.252
1.00
20.80
8


4190
CB
VAL
A
538
−0.896
56.665
43.080
1.00
17.97
6


4191
CG1
VAL
A
538
0.219
55.621
43.337
1.00
16.03
6


4192
CG2
VAL
A
538
−1.016
57.646
44.226
1.00
19.59
6


4193
N
LYS
A
539
0.696
56.340
40.055
1.00
15.64
7


4194
CA
LYS
A
539
1.119
55.341
39.108
1.00
14.97
6


4195
C
LYS
A
539
1.626
54.044
39.732
1.00
17.57
6


4196
O
LYS
A
539
1.313
52.885
39.375
1.00
18.05
8


4197
CB
LYS
A
539
2.264
55.914
38.209
1.00
17.15
6


4198
CG
LYS
A
539
2.814
54.859
37.246
1.00
20.63
6


4199
CD
LYS
A
539
3.860
55.636
36.368
1.00
25.39
6


4200
CE
LYS
A
539
3.601
55.199
34.949
1.00
41.98
6


4201
NZ
LYS
A
539
4.369
53.976
34.672
1.00
30.47
7


4202
N
SER
A
540
2.424
54.212
40.787
1.00
15.53
7


4203
CA
SER
A
540
2.919
53.073
41.587
1.00
16.52
6


4204
C
SER
A
540
3.231
53.502
42.999
1.00
17.69
6


4205
O
SER
A
540
3.482
54.680
43.306
1.00
16.82
8


4206
CB
SER
A
540
4.136
52.424
40.903
1.00
20.58
6


4207
OG
SER
A
540
5.270
53.317
41.043
1.00
19.05
8


4208
N
TRP
A
541
3.206
52.536
43.953
1.00
16.64
7


4209
CA
TRP
A
541
3.361
52.905
45.378
1.00
15.40
6


4210
C
TRP
A
541
4.148
51.785
46.053
1.00
20.16
6


4211
O
TRP
A
541
3.682
50.647
46.008
1.00
21.11
8


4212
CB
TRP
A
541
2.034
53.084
46.101
1.00
17.49
6


4213
CG
TRP
A
541
2.124
53.605
47.502
1.00
15.27
6


4214
CD1
TRP
A
541
2.645
52.924
48.584
1.00
18.64
6


4215
CD2
TRP
A
541
1.689
54.854
48.006
1.00
15.30
6


4216
NE1
TRP
A
541
2.542
53.673
49.715
1.00
19.85
7


4217
CE2
TRP
A
541
1.976
54.894
49.381
1.00
17.27
6


4218
CE3
TRP
A
541
1.086
55.984
47.440
1.00
15.92
6


4219
CZ2
TRP
A
541
1.703
55.983
50.201
1.00
18.49
6


4220
CZ3
TRP
A
541
0.787
57.054
48.223
1.00
19.66
6


4221
CH2
TRP
A
541
1.076
57.063
49.619
1.00
21.41
6


4222
N
THR
A
542
5.297
52.107
46.615
1.00
18.77
7


4223
CA
THR
A
542
6.111
51.224
47.437
1.00
20.27
6


4224
C
THR
A
542
6.477
51.972
48.690
1.00
21.74
6


4225
O
THR
A
542
6.369
53.228
48.814
1.00
17.27
8


4226
CB
THR
A
542
7.356
50.641
46.743
1.00
24.92
6


4227
OG1
THR
A
542
8.305
51.745
46.576
1.00
21.04
8


4228
CG2
THR
A
542
7.091
49.930
45.442
1.00
26.69
6


4229
N
SER
A
543
7.123
51.252
49.648
1.00
18.34
7


4230
CA
SER
A
543
7.474
51.808
50.923
1.00
18.96
6


4231
C
SER
A
543
8.463
52.975
50.734
1.00
17.37
6


4232
O
SER
A
543
8.525
53.808
51.615
1.00
19.43
8


4233
CB
SER
A
543
8.201
50.711
51.743
1.00
24.79
6


4234
OG
SER
A
543
7.254
49.673
51.954
1.00
38.42
8


4235
N
ASN
A
544
9.313
52.865
49.721
1.00
17.78
7


4236
CA
ASN
A
544
10.349
53.917
49.575
1.00
14.67
6


4237
C
ASN
A
544
10.208
54.723
48.287
1.00
15.24
6


4238
O
ASN
A
544
11.018
55.668
48.072
1.00
16.63
8


4239
CB
AASN
A
544
11.734
53.252
49.583
0.50
18.64
6


4240
CG
AASN
A
544
12.145
52.868
51.005
0.50
24.93
6


4241
OD1
AASN
A
544
11.394
53.024
51.976
0.50
27.01
8


4242
ND2
AASN
A
544
13.359
52.364
51.118
0.50
19.54
7


4240
CB
BASN
A
544
11.746
53.263
49.523
0.50
15.95
6


4241
CG
BASN
A
544
11.998
52.552
50.860
0.50
20.57
6


4242
OD1
BASN
A
544
12.195
53.205
51.884
0.50
23.06
8


4243
ND2
BASN
A
544
11.914
51.250
50.767
0.50
19.16
7


4243
N
ARG
A
545
9.224
54.409
47.426
1.00
14.40
7


4244
CA
ARG
A
545
9.193
55.190
46.167
1.00
16.44
6


4245
C
ARG
A
545
7.727
55.246
45.682
1.00
19.39
6


4246
O
ARG
A
545
7.083
54.204
45.539
1.00
17.25
8


4247
CB
ARG
A
545
10.085
54.589
45.084
1.00
17.96
6


4248
CG
ARG
A
545
9.964
55.404
43.794
1.00
17.03
6


4249
CD
ARG
A
545
10.778
54.728
42.653
1.00
15.55
6


4250
NE
ARG
A
545
12.186
54.934
43.045
1.00
17.92
7


4251
CZ
ARG
A
545
13.164
54.094
42.735
1.00
27.70
6


4252
NH1
ARG
A
545
12.923
53.020
41.999
1.00
26.35
7


4253
NH2
ARG
A
545
14.392
54.343
43.179
1.00
26.80
7


4254
N
ILE
A
546
7.282
56.458
45.332
1.00
18.00
7


4255
CA
ILE
A
546
5.908
56.613
44.793
1.00
14.23
6


4256
C
ILE
A
546
6.077
57.267
43.406
1.00
17.86
6


4257
O
ILE
A
546
6.771
58.296
43.389
1.00
15.62
8


4258
CB
ILE
A
546
5.039
57.498
45.668
1.00
13.38
6


4259
CG1
ILE
A
546
4.895
56.781
47.045
1.00
15.14
6


4260
CG2
ILE
A
546
3.624
57.682
45.030
1.00
14.12
6


4261
CD1
ILE
A
546
4.473
57.773
48.119
1.00
13.44
6


4262
N
GLU
A
547
5.424
56.777
42.400
1.00
14.74
7


4263
CA
GLU
A
547
5.338
57.543
41.134
1.00
14.58
6


4264
C
GLU
A
547
3.943
58.116
40.945
1.00
15.30
6


4265
O
GLU
A
547
2.977
57.405
41.270
1.00
15.50
8


4266
CB
GLU
A
547
5.537
56.644
39.913
1.00
14.75
6


4267
CG
GLU
A
547
6.987
56.074
39.890
1.00
17.63
6


4268
CD
GLU
A
547
7.105
55.058
38.781
1.00
21.54
6


4269
OE1
GLU
A
547
6.335
54.046
38.730
1.00
18.28
8


4270
OE2
GLU
A
547
7.924
55.225
37.834
1.00
16.92
8


4271
N
VAL
A
548
3.865
59.377
40.603
1.00
12.67
7


4272
CA
VAL
A
548
2.565
60.033
40.428
1.00
13.16
6


4273
C
VAL
A
548
2.565
60.764
39.095
1.00
15.52
6


4274
O
VAL
A
548
3.587
61.028
38.477
1.00
14.55
8


4275
CB
VAL
A
548
2.266
61.100
41.499
1.00
15.22
6


4276
CG1
VAL
A
548
2.134
60.409
42.872
1.00
17.06
6


4277
CG2
VAL
A
548
3.376
62.179
41.584
1.00
16.26
6


4278
N
TYR
A
549
1.338
61.119
38.644
1.00
12.92
7


4279
CA
TYR
A
549
1.226
61.997
37.481
1.00
14.43
6


4280
C
TYR
A
549
0.902
63.397
37.975
1.00
13.16
6


4281
O
TYR
A
549
0.223
63.571
39.016
1.00
14.84
8


4282
CB
TYR
A
549
0.000
61.611
36.605
1.00
14.89
6


4283
CG
TYR
A
549
0.208
60.240
36.037
1.00
14.21
6


4284
CD1
TYR
A
549
1.049
60.058
34.934
1.00
17.04
6


4285
CD2
TYR
A
549
−0.398
59.160
36.628
1.00
14.96
6


4286
CE1
TYR
A
549
1.252
58.788
34.395
1.00
19.51
6


4287
CE2
TYR
A
549
−0.214
57.885
36.081
1.00
20.11
6


4288
CZ
TYR
A
549
0.577
57.730
34.984
1.00
20.28
6


4289
OH
TYR
A
549
0.789
56.436
34.508
1.00
21.51
8


4290
N
VAL
A
550
1.626
64.446
37.496
1.00
12.41
7


4291
CA
VAL
A
550
1.317
65.794
37.957
1.00
13.30
6


4292
C
VAL
A
550
−0.145
66.139
37.602
1.00
12.86
6


4293
O
VAL
A
550
−0.589
65.893
36.503
1.00
15.42
8


4294
CB
VAL
A
550
2.195
66.791
37.131
1.00
12.38
6


4295
CG1
VAL
A
550
1.968
68.236
37.581
1.00
13.91
6


4296
CG2
VAL
A
550
3.657
66.404
37.542
1.00
16.31
6


4297
N
PRO
A
551
−0.828
66.685
38.603
1.00
13.48
7


4298
CA
PRO
A
551
−2.272
66.942
38.387
1.00
16.42
6


4299
C
PRO
A
551
−2.447
68.081
37.424
1.00
16.09
6


4300
O
PRO
A
551
−1.599
68.955
37.236
1.00
16.43
8


4301
CB
PRO
A
551
−2.869
67.337
39.755
1.00
20.53
6


4302
CG
PRO
A
551
−1.772
66.991
40.707
1.00
20.55
6


4303
CD
PRO
A
551
−0.427
66.849
39.973
1.00
17.00
6


4304
N
ASN
A
552
−3.658
68.150
36.821
1.00
15.47
7


4305
CA
ASN
A
552
−4.017
69.248
35.941
1.00
15.18
6


4306
C
ASN
A
552
−4.401
70.475
36.748
1.00
19.54
6


4307
O
ASN
A
552
−5.630
70.744
36.917
1.00
19.65
8


4308
CB
ASN
A
552
−5.198
68.759
35.075
1.00
19.00
6


4309
CG
ASN
A
552
−5.522
69.706
33.925
1.00
23.61
6


4310
OD1
ASN
A
552
−4.763
70.583
33.553
1.00
29.14
8


4311
ND2
ASN
A
552
−6.635
69.481
33.239
1.00
23.65
7


4312
N
MET
A
553
−3.487
71.146
37.402
1.00
13.46
7


4313
CA
MET
A
553
−3.722
72.208
38.346
1.00
11.50
6


4314
C
MET
A
553
−3.003
73.456
37.901
1.00
15.54
6


4315
O
MET
A
553
−2.319
73.427
36.881
1.00
17.61
8


4316
CB
MET
A
553
−3.328
71.835
39.803
1.00
16.46
6


4317
CG
MET
A
553
−1.826
71.490
39.883
1.00
14.92
6


4318
SD
MET
A
553
−1.364
70.962
41.579
1.00
17.71
16


4319
CE
MET
A
553
−1.416
72.450
42.426
1.00
16.59
6


4320
N
ALA
A
554
−3.278
74.532
38.619
1.00
17.19
7


4321
CA
ALA
A
554
−2.711
75.834
38.289
1.00
21.10
6


4322
C
ALA
A
554
−1.169
75.788
38.321
1.00
17.79
6


4323
O
ALA
A
554
−0.631
75.032
39.141
1.00
17.24
8


4324
CB
ALA
A
554
−3.075
76.757
39.471
1.00
24.10
6


4325
N
ALA
A
555
−0.537
76.591
37.500
1.00
14.57
7


4326
CA
ALA
A
555
0.947
76.567
37.489
1.00
13.27
6


4327
C
ALA
A
555
1.568
77.356
38.600
1.00
13.78
6


4328
O
ALA
A
555
1.051
78.305
39.204
1.00
14.85
8


4329
CB
ALA
A
555
1.375
77.200
36.142
1.00
16.26
6


4330
N
GLY
A
556
2.874
76.966
38.857
1.00
12.02
7


4331
CA
GLY
A
556
3.602
77.675
39.947
1.00
14.17
6


4332
C
GLY
A
556
4.312
76.639
40.815
1.00
12.79
6


4333
O
GLY
A
556
4.121
75.415
40.670
1.00
12.92
8


4334
N
LEU
A
557
5.203
77.130
41.670
1.00
14.81
7


4335
CA
LEU
A
557
5.876
76.232
42.626
1.00
13.54
6


4336
C
LEU
A
557
4.918
75.806
43.737
1.00
12.41
6


4337
O
LEU
A
557
4.110
76.659
44.188
1.00
14.95
8


4338
CB
LEU
A
557
7.091
76.999
43.221
1.00
13.41
6


4339
CG
LEU
A
557
8.018
76.123
44.069
1.00
15.11
6


4340
CD1
LEU
A
557
8.847
75.220
43.141
1.00
13.33
6


4341
CD2
LEU
A
557
8.965
77.046
44.898
1.00
17.39
6


4342
N
THR
A
558
4.801
74.500
43.858
1.00
13.24
7


4343
CA
THR
A
558
3.807
73.941
44.818
1.00
13.26
6


4344
C
THR
A
558
4.469
72.927
45.741
1.00
16.19
6


4345
O
THR
A
558
5.520
72.402
45.379
1.00
16.82
8


4346
CB
THR
A
558
2.616
73.378
44.044
1.00
17.75
6


4347
OG1
THR
A
558
1.566
73.153
45.010
1.00
18.46
8


4348
CG2
THR
A
558
2.886
72.099
43.320
1.00
14.65
6


4349
N
ASP
A
559
3.750
72.559
46.821
1.00
13.53
7


4350
CA
ASP
A
559
4.351
71.569
47.739
1.00
13.26
6


4351
C
ASP
A
559
3.718
70.202
47.564
1.00
17.40
6


4352
O
ASP
A
559
2.469
70.015
47.579
1.00
17.26
8


4353
CB
ASP
A
559
4.129
72.027
49.195
1.00
13.77
6


4354
CG
ASP
A
559
4.998
73.219
49.580
1.00
25.94
6


4355
OD1
ASP
A
559
6.174
73.267
49.201
1.00
23.88
8


4356
OD2
ASP
A
559
4.468
74.127
50.251
1.00
28.55
8


4357
N
VAL
A
560
4.576
69.205
47.465
1.00
12.44
7


4358
CA
VAL
A
560
4.161
67.801
47.392
1.00
11.28
6


4359
C
VAL
A
560
4.193
67.207
48.826
1.00
14.98
6


4360
O
VAL
A
560
5.085
67.470
49.616
1.00
15.44
8


4361
CB
VAL
A
560
5.144
66.953
46.555
1.00
11.93
6


4362
CG1
VAL
A
560
4.738
65.496
46.488
1.00
16.58
6


4363
CG2
VAL
A
560
5.186
67.516
45.122
1.00
14.73
6


4364
N
LYS
A
561
3.136
66.439
49.097
1.00
15.49
7


4365
CA
LYS
A
561
2.989
65.835
50.443
1.00
14.90
6


4366
C
LYS
A
561
2.427
64.452
50.269
1.00
15.23
6


4367
O
LYS
A
561
1.502
64.157
49.522
1.00
16.90
8


4368
CB
LYS
A
561
1.960
66.720
51.206
1.00
18.50
6


4369
CG
LYS
A
561
1.847
66.177
52.656
1.00
22.42
6


4370
CD
LYS
A
561
1.025
67.110
53.523
1.00
25.69
6


4371
CE
LYS
A
561
−0.461
66.912
53.312
1.00
33.13
6


4372
NZ
LYS
A
561
−1.198
68.004
54.033
1.00
37.04
7


4373
N
VAL
A
562
2.947
63.489
51.047
1.00
16.07
7


4374
CA
VAL
A
562
2.525
62.108
51.051
1.00
14.01
6


4375
C
VAL
A
562
1.751
61.827
52.382
1.00
14.81
6


4376
O
VAL
A
562
2.150
62.324
53.398
1.00
17.73
8


4377
CB
VAL
A
562
3.735
61.158
51.036
1.00
16.60
6


4378
CG1
VAL
A
562
3.312
59.677
51.185
1.00
16.48
6


4379
CG2
VAL
A
562
4.473
61.228
49.672
1.00
17.80
6


4380
N
THR
A
563
0.603
61.156
52.140
1.00
17.67
7


4381
CA
THR
A
563
−0.181
60.806
53.380
1.00
18.18
6


4382
C
THR
A
563
−0.261
59.308
53.412
1.00
18.30
6


4383
O
THR
A
563
−0.679
58.642
52.456
1.00
19.93
8


4384
CB
THR
A
563
−1.542
61.496
53.361
1.00
18.11
6


4385
OG1
THR
A
563
−1.367
62.891
53.406
1.00
19.44
8


4386
CG2
THR
A
563
−2.281
61.112
54.705
1.00
20.36
6


4387
N
ALA
A
564
0.154
58.701
54.548
1.00
21.05
7


4388
CA
ALA
A
564
0.245
57.258
54.649
1.00
24.26
6


4389
C
ALA
A
564
−0.234
56.845
56.060
1.00
23.28
6


4390
O
ALA
A
564
0.104
57.536
57.008
1.00
21.58
8


4391
CB
ALA
A
564
1.658
56.711
54.437
1.00
25.03
6


4392
N
GLY
A
565
−1.218
55.968
56.140
1.00
30.08
7


4393
CA
GLY
A
565
−1.857
55.701
57.443
1.00
31.09
6


4394
C
GLY
A
565
−2.488
56.887
58.121
1.00
35.06
6


4395
O
GLY
A
565
−2.493
56.983
59.363
1.00
31.36
8


4396
N
GLY
A
566
−3.025
57.873
57.403
1.00
32.22
7


4397
CA
GLY
A
566
−3.549
59.083
58.011
1.00
31.70
6


4398
C
GLY
A
566
−2.523
60.107
58.438
1.00
31.07
6


4399
O
GLY
A
566
−2.936
61.213
58.829
1.00
32.69
8


4400
N
VAL
A
567
−1.202
59.887
58.271
1.00
26.17
7


4401
CA
VAL
A
567
−0.186
60.798
58.776
1.00
21.45
6


4402
C
VAL
A
567
0.537
61.488
57.557
1.00
17.95
6


4403
O
VAL
A
567
0.692
60.707
56.658
1.00
18.75
8


4404
CB
VAL
A
567
0.945
60.023
59.500
1.00
26.89
6


4405
CG1
VAL
A
567
1.981
60.946
60.096
1.00
30.00
6


4406
CG2
VAL
A
567
0.308
59.088
60.567
1.00
33.86
6


4407
N
SER
A
568
0.687
62.774
57.699
1.00
19.77
7


4408
CA
SER
A
568
1.267
63.410
56.486
1.00
19.16
6


4409
C
SER
A
568
2.770
63.585
56.688
1.00
19.28
6


4410
O
SER
A
568
3.351
63.752
57.763
1.00
21.35
8


4411
CB
SER
A
568
0.574
64.705
56.156
1.00
29.69
6


4412
OG
SER
A
568
0.595
65.549
57.266
1.00
41.18
8


4413
N
SER
A
569
3.399
63.581
55.503
1.00
19.22
7


4414
CA
SER
A
569
4.867
63.784
55.480
1.00
17.43
6


4415
C
SER
A
569
5.229
65.245
55.568
1.00
17.17
6


4416
O
SER
A
569
4.519
66.266
55.502
1.00
17.53
8


4417
CB
SER
A
569
5.381
63.220
54.137
1.00
17.58
6


4418
OG
SER
A
569
5.066
64.083
53.025
1.00
15.50
8


4419
N
ASN
A
570
6.572
65.473
55.538
1.00
14.77
7


4420
CA
ASN
A
570
7.143
66.776
55.253
1.00
13.84
6


4421
C
ASN
A
570
6.848
67.107
53.752
1.00
13.33
6


4422
O
ASN
A
570
6.527
66.217
52.996
1.00
16.50
8


4423
CB
ASN
A
570
8.670
66.723
55.435
1.00
17.22
6


4424
CG
ASN
A
570
9.363
65.581
54.758
1.00
16.95
6


4425
OD1
ASN
A
570
9.038
64.399
54.745
1.00
15.12
8


4426
ND2
ASN
A
570
10.455
65.853
54.023
1.00
16.51
7


4427
N
LEU
A
571
7.108
68.381
53.486
1.00
14.82
7


4428
CA
LEU
A
571
6.705
68.878
52.131
1.00
12.49
6


4429
C
LEU
A
571
7.959
69.019
51.828
1.00
16.79
8


4430
O
LEU
A
571
9.024
69.355
51.828
1.00
16.79
8


4431
CB
LEU
A
571
6.147
70.286
52.340
1.00
15.18
6


4432
CG
LEU
A
571
4.911
70.396
53.250
1.00
22.77
6


4433
CD1
LEU
A
571
4.368
71.807
53.300
1.00
22.26
6


4434
CD2
LEU
A
571
3.834
69.448
52.727
1.00
22.04
6


4435
N
TYR
A
572
7.747
68.878
49.946
1.00
13.65
7


4436
CA
TYR
A
572
8.930
69.100
49.067
1.00
12.87
6


4437
C
TYR
A
572
8.322
69.878
47.880
1.00
14.52
6


4438
O
TYR
A
572
7.347
69.399
47.262
1.00
14.71
8


4439
CB
TYR
A
572
9.480
67.704
48.701
1.00
12.62
6


4440
CG
TYR
A
572
10.887
67.679
48.121
1.00
13.61
6


4441
CD1
TYR
A
572
11.079
68.175
46.835
1.00
13.57
6


4442
CD2
TYR
A
572
11.946
67.161
48.845
1.00
15.40
6


4443
CE1
TYR
A
572
12.361
68.168
46.257
1.00
13.80
6


4444
CE2
TYR
A
572
13.221
67.135
48.283
1.00
12.70
6


4445
CZ
TYR
A
572
13.400
67.629
47.002
1.00
14.33
6


4446
OH
TYR
A
572
14.710
67.607
46.466
1.00
13.40
8


4447
N
SER
A
573
9.060
70.874
47.387
1.00
13.37
7


4448
CA
SER
A
573
8.571
71.734
46.294
1.00
12.21
6


4449
C
SER
A
573
8.665
71.055
44.920
1.00
12.75
6


4450
O
SER
A
573
9.520
70.234
44.703
1.00
12.64
8


4451
CB
ASER
A
573
9.436
72.999
46.162
0.60
17.33
6


4452
OG
ASER
A
573
9.459
73.767
47.331
0.60
22.77
8


4452
CB
BSER
A
573
9.408
73.025
46.276
0.40
15.40
6


4453
OG
BSER
A
573
10.793
72.728
46.149
0.40
16.17
8


4453
N
TYR
A
574
7.838
71.568
44.000
1.00
11.56
7


4454
CA
TYR
A
574
7.912
71.077
42.604
1.00
10.89
6


4455
C
TYR
A
574
7.374
72.249
41.771
1.00
13.28
6


4456
O
TYR
A
574
6.344
72.860
42.138
1.00
12.17
8


4457
CB
TYR
A
574
7.041
69.857
42.405
1.00
11.94
6


4458
CG
TYR
A
574
6.917
69.379
40.971
1.00
11.37
6


4459
CD1
TYR
A
574
7.921
68.521
40.467
1.00
12.69
6


4460
CD2
TYR
A
574
5.867
69.781
40.162
1.00
11.85
6


4461
CE1
TYR
A
574
7.863
68.052
39.154
1.00
13.23
6


4462
CE2
TYR
A
574
5.792
69.313
38.834
1.00
13.93
6


4463
CZ
TYR
A
574
6.796
68.466
38.366
1.00
11.32
6


4464
OH
TYR
A
574
6.679
68.006
37.078
1.00
12.54
8


4465
N
ASN
A
575
7.992
72.510
40.627
1.00
12.18
7


4466
CA
ASN
A
575
7.578
73.682
39.820
1.00
12.18
6


4467
C
ASN
A
575
6.738
73.306
38.608
1.00
12.59
6


4468
O
ASN
A
575
7.171
72.699
37.598
1.00
12.20
8


4469
CB
ASN
A
575
8.898
74.351
39.331
1.00
12.02
6


4470
CG
ASN
A
575
8.635
75.707
38.700
1.00
17.00
6


4471
OD1
ASN
A
575
7.562
76.292
38.872
1.00
14.54
8


4472
ND2
ASN
A
575
9.608
76.223
37.934
1.00
13.02
7


4473
N
ILE
A
576
5.400
73.515
38.739
1.00
10.95
7


4474
CA
ILE
A
576
4.506
73.221
37.604
1.00
10.36
6


4475
C
ILE
A
576
4.485
74.374
36.602
1.00
12.05
6


4476
O
ILE
A
576
4.145
75.497
36.930
1.00
13.39
8


4477
CB
ILE
A
576
3.036
73.061
38.127
1.00
12.95
6


4478
CG1
ILE
A
576
3.082
71.956
39.190
1.00
13.10
6


4479
CG2
ILE
A
576
2.079
72.677
36.966
1.00
14.18
6


4480
CD1
ILE
A
576
1.709
71.488
39.691
1.00
15.07
6


4481
N
LEU
A
577
4.883
74.054
35.368
1.00
10.51
7


4482
CA
LEU
A
577
4.908
75.052
34.303
1.00
12.74
6


4483
C
LEU
A
577
3.480
75.308
33.772
1.00
11.80
6


4484
O
LEU
A
577
2.572
74.474
34.021
1.00
13.37
8


4485
CB
LEU
A
577
5.757
74.463
33.137
1.00
11.48
6


4486
CG
LEU
A
577
7.226
74.238
33.569
1.00
12.21
6


4487
CD1
LEU
A
577
7.982
73.601
32.421
1.00
13.03
6


4488
CD2
LEU
A
577
7.897
75.576
33.989
1.00
13.85
6


4489
N
SER
A
578
3.398
76.385
33.006
1.00
11.76
7


4490
CA
SER
A
578
2.037
76.726
32.475
1.00
15.00
6


4491
C
SER
A
578
1.681
75.960
31.215
1.00
17.37
6


4492
O
SER
A
578
0.553
76.134
30.685
1.00
17.93
8


4493
CB
SER
A
578
2.081
78.230
32.132
1.00
13.25
6


4494
OG
SER
A
578
2.321
78.967
33.305
1.00
14.45
8


4495
N
GLY
A
579
2.538
75.095
30.688
1.00
15.28
7


4496
CA
GLY
A
579
2.266
74.270
29.497
1.00
14.88
6


4497
C
GLY
A
579
3.627
74.010
28.818
1.00
13.39
6


4498
O
GLY
A
579
4.670
74.450
29.318
1.00
14.78
8


4499
N
THR
A
580
3.518
73.227
27.740
1.00
11.35
7


4500
CA
THR
A
580
4.803
72.961
27.005
1.00
13.16
6


4501
C
THR
A
580
5.419
74.292
26.647
1.00
14.61
6


4502
O
THR
A
580
4.747
75.282
26.349
1.00
14.26
8


4503
CB
THR
A
580
4.517
72.009
25.835
1.00
13.57
6


4504
OG1
THR
A
580
5.753
71.676
25.176
1.00
16.06
8


4505
CG2
THR
A
580
3.688
72.715
24.732
1.00
20.75
6


4506
N
GLN
A
581
6.787
74.346
26.706
1.00
11.89
7


4507
CA
GLN
A
581
7.454
75.658
26.609
1.00
10.06
6


4508
C
GLN
A
581
8.012
75.905
25.148
1.00
10.19
6


4509
O
GLN
A
581
8.163
75.020
24.338
1.00
12.94
8


4510
CB
GLN
A
581
8.751
75.601
27.465
1.00
11.27
6


4511
CG
GLN
A
581
8.407
75.301
28.975
1.00
10.49
6


4512
CD
GLN
A
581
7.920
76.579
29.654
1.00
12.45
6


4513
OE1
GLN
A
581
8.545
77.588
29.921
1.00
13.44
8


4514
NE2
GLN
A
581
6.582
76.528
30.002
1.00
11.11
7


4515
N
THR
A
582
8.202
77.209
24.953
1.00
9.52
7


4516
CA
THR
A
582
8.978
77.646
23.772
1.00
10.13
6


4517
C
THR
A
582
10.049
78.609
24.293
1.00
10.70
6


4518
O
THR
A
582
9.921
79.235
25.313
1.00
12.73
8


4519
CB
THR
A
582
8.018
78.306
22.763
1.00
12.88
6


4520
OG1
THR
A
582
8.736
78.798
21.599
1.00
12.92
8


4521
CG2
THR
A
582
7.265
79.504
23.359
1.00
11.55
6


4522
N
SER
A
583
11.166
78.712
23.507
1.00
11.67
7


4523
CA
SER
A
583
12.321
79.527
23.931
1.00
12.58
6


4524
CA
SER
A
583
12.300
80.783
23.061
1.00
11.58
6


4525
O
SER
A
583
12.496
80.687
21.844
1.00
12.44
8


4526
CB
SER
A
583
13.612
78.697
23.747
1.00
12.53
6


4527
OG
SER
A
583
14.755
79.449
24.240
1.00
14.73
8


4528
N
VAL
A
584
12.118
81.899
23.781
1.00
10.19
7


4529
CA
VAL
A
584
11.741
83.141
23.016
1.00
9.76
6


4530
C
VAL
A
584
12.721
84.268
23.298
1.00
11.27
6


4531
O
VAL
A
584
13.066
84.570
24.440
1.00
11.87
8


4532
CB
VAL
A
584
10.358
83.645
23.506
1.00
12.33
6


4533
CG1
VAL
A
584
10.041
84.968
22.757
1.00
14.53
6


4534
CG2
VAL
A
584
9.279
82.604
23.220
1.00
12.71
6


4535
N
VAL
A
585
13.307
84.868
22.244
1.00
10.77
7


4536
CA
VAL
A
585
14.166
86.030
22.421
1.00
9.69
6


4537
C
VAL
A
585
13.244
87.219
22.693
1.00
12.06
6


4538
O
VAL
A
585
12.450
87.576
21.803
1.00
14.60
8


4539
CB
VAL
A
585
14.882
86.310
21.064
1.00
11.53
6


4540
CG1
VAL
A
585
15.712
87.605
21.158
1.00
15.03
6


4541
CG2
VAL
A
585
15.750
85.111
20.717
1.00
14.67
6


4542
N
PHE
A
586
13.361
87.762
23.908
1.00
12.32
7


4543
CA
PHE
A
586
12.622
88.986
24.243
1.00
12.19
6


4544
C
PHE
A
586
13.584
90.161
24.063
1.00
14.77
6


4545
O
PHE
A
586
14.668
90.209
24.709
1.00
12.38
8


4546
CB
PHE
A
586
12.174
88.944
25.704
1.00
12.57
6


4547
CG
PHE
A
586
10.886
88.184
25.987
1.00
11.39
6


4548
CD1
PHE
A
586
10.879
86.809
26.009
1.00
13.56
6


4549
CD2
PHE
A
586
9.694
88.868
26.231
1.00
13.70
6


4550
CE1
PHE
A
586
9.758
86.060
26.284
1.00
13.86
6


4551
CE2
PHE
A
586
8.543
88.102
26.520
1.00
12.32
6


4552
CZ
PHE
A
586
8.577
86.707
26.558
1.00
11.70
6


4553
N
THR
A
587
13.189
91.146
23.239
1.00
14.16
7


4554
CA
THR
A
587
14.016
92.324
23.066
1.00
12.96
6


4555
C
THR
A
587
13.247
93.561
23.468
1.00
13.58
6


4556
O
THR
A
587
12.072
93.651
23.058
1.00
15.22
8


4557
CB
THR
A
587
14.421
92.464
21.555
1.00
11.66
6


4558
OG1
THR
A
587
15.145
91.299
21.141
1.00
15.06
8


4559
CG2
THR
A
587
15.331
93.708
21.318
1.00
13.37
6


4560
N
VAL
A
588
13.829
94.487
24.195
1.00
14.03
7


4561
CA
VAL
A
588
13.156
95.779
24.469
1.00
14.79
6


4562
C
VAL
A
588
14.079
96.867
23.912
1.00
14.40
6


4563
O
VAL
A
588
15.258
97.015
24.225
1.00
15.56
8


4564
CB
VAL
A
588
12.863
95.933
25.971
1.00
14.24
6


4565
CG1
VAL
A
588
14.111
95.935
26.870
1.00
14.60
6


4566
CG2
VAL
A
588
12.079
97.255
26.232
1.00
13.38
6


4567
N
LYS
A
589
13.478
97.570
22.915
1.00
15.39
7


4568
CA
LYS
A
589
14.212
98.670
22.258
1.00
16.20
6


4569
C
LYS
A
589
14.180
100.009
22.953
1.00
18.01
6


4570
O
LYS
A
589
13.230
100.355
23.652
1.00
15.39
8


4571
CB
LYS
A
589
13.597
98.820
20.860
1.00
16.23
6


4572
CG
LYS
A
589
13.908
97.588
20.008
1.00
17.01
6


4573
CD
LYS
A
589
13.275
97.825
18.634
1.00
24.71
6


4574
CE
LYS
A
589
13.494
96.582
17.792
1.00
37.49
6


4575
NZ
LYS
A
589
13.368
96.852
16.321
1.00
51.36
7


4576
N
SER
A
590
15.302
100.747
22.828
1.00
16.34
7


4577
CA
SER
A
590
15.371
102.116
23.293
1.00
19.32
6


4578
C
SER
A
590
15.006
102.295
24.746
1.00
19.68
6


4579
O
SER
A
590
14.185
103.146
25.151
1.00
17.24
8


4580
CB
SER
A
590
14.448
103.009
22.421
1.00
20.32
6


4581
OG
SER
A
590
14.867
102.933
21.046
1.00
22.81
8


4582
N
ALA
A
591
15.698
101.514
25.612
1.00
17.08
7


4583
CA
ALA
A
591
15.458
101.617
27.048
1.00
16.02
6


4584
C
ALA
A
591
16.178
102.871
27.530
1.00
18.06
6


4585
O
ALA
A
591
17.152
103.325
26.878
1.00
15.85
8


4586
CB
ALA
A
591
16.045
100.326
27.695
1.00
15.17
6


4587
N
PRO
A
592
15.872
103.303
28.730
1.00
18.28
7


4588
CA
PRO
A
592
16.493
104.529
29.298
1.00
18.18
6


4589
C
PRO
A
592
17.967
104.319
29.512
1.00
22.69
6


4590
O
PRO
A
592
18.463
103.180
29.693
1.00
19.12
8


4591
CB
PRO
A
592
15.762
104.797
30.621
1.00
19.23
6


4592
CG
PRO
A
592
14.433
104.085
30.387
1.00
23.18
6


4593
CD
PRO
A
592
14.795
102.833
29.585
1.00
17.71
6


4594
N
PRO
A
593
18.778
105.367
29.550
1.00
21.02
7


4595
CA
PRO
A
593
20.204
105.252
29.779
1.00
20.83
6


4596
C
PRO
A
593
20.494
104.537
31.094
1.00
20.17
6


4597
O
PRO
A
593
19.811
104.784
32.102
1.00
21.50
8


4598
CB
PRO
A
593
20.715
106.727
29.941
1.00
22.70
6


4599
CG
PRO
A
593
19.643
107.491
29.165
1.00
24.71
6


4600
CD
PRO
A
593
18.337
106.774
29.432
1.00
23.44
6


4601
N
THR
A
594
21.530
103.723
31.165
1.00
19.91
7


4602
CA
THR
A
594
21.909
103.060
32.402
1.00
21.78
6


4603
C
THR
A
594
23.380
103.366
32.686
1.00
23.13
6


4604
O
THR
A
594
24.138
103.737
31.787
1.00
23.96
8


4605
CB
THR
A
594
21.729
101.521
32.292
1.00
23.27
6


4606
OG1
THR
A
594
22.466
101.094
31.140
1.00
20.06
8


4607
CG2
THR
A
594
20.245
101.183
32.157
1.00
21.33
6


4608
N
ASN
A
595
23.764
103.210
33.928
1.00
23.96
7


4609
CA
ASN
A
595
25.142
103.193
34.370
1.00
28.93
6


4610
C
ASN
A
595
25.614
101.791
34.716
1.00
31.88
6


4611
O
ASN
A
595
24.847
100.849
34.915
1.00
22.74
8


4612
CB
ASN
A
595
25.285
104.099
35.620
1.00
34.82
6


4613
CG
ASN
A
595
24.970
105.532
35.180
1.00
36.76
6


4614
CD1
ASN
A
595
24.047
106.190
35.647
1.00
42.57
8


4615
ND2
ASN
A
595
25.738
106.004
34.208
1.00
38.16
7


4616
N
LEU
A
596
26.939
101.654
34.839
1.00
34.83
7


4617
CA
LEU
A
596
27.559
100.380
35.212
1.00
37.55
6


4618
C
LEU
A
596
26.947
99.803
36.488
1.00
31.76
6


4619
O
LEU
A
596
26.589
100.502
37.435
1.00
35.49
8


4620
CB
LEU
A
596
29.051
100.642
35.407
1.00
48.79
6


4621
CG
LEU
A
596
30.042
99.528
35.681
1.00
52.60
6


4622
CD1
LEU
A
596
29.894
98.971
37.092
1.00
56.16
6


4623
CD2
LEU
A
596
29.934
98.433
34.628
1.00
56.63
6


4624
N
GLY
A
597
26.492
98.556
36.348
1.00
30.34
7


4625
CA
GLY
A
597
25.861
97.860
37.473
1.00
30.50
6


4626
C
GLY
A
597
24.337
97.822
37.288
1.00
25.20
6


4627
O
GLY
A
597
23.705
96.996
37.949
1.00
23.57
8


4628
N
ASP
A
598
23.780
98.803
36.544
1.00
21.92
7


4629
CA
ASP
A
598
22.315
98.799
36.399
1.00
18.64
6


4630
C
ASP
A
598
21.982
97.666
35.429
1.00
21.53
6


4631
O
ASP
A
598
22.702
97.563
34.399
1.00
20.69
8


4632
CB
ASP
A
598
21.814
100.096
35.763
1.00
17.61
6


4633
CG
ASP
A
598
22.046
101.382
36.536
1.00
20.17
6


4634
OD1
ASP
A
598
22.364
101.347
37.751
1.00
19.25
8


4635
OD2
ASP
A
598
21.858
102.432
35.868
1.00
22.20
8


4636
N
LYS
A
599
20.861
96.919
35.612
1.00
18.66
7


4637
CA
LYS
A
599
20.593
95.891
34.605
1.00
15.76
6


4638
C
LYS
A
599
19.056
95.824
34.461
1.00
11.90
6


4639
O
LYS
A
599
18.320
96.237
35.358
1.00
19.04
8


4640
CB
LYS
A
599
21.049
94.484
35.006
1.00
23.86
6


4641
CG
LYS
A
599
22.597
94.419
35.031
1.00
25.32
6


4642
CD
LYS
A
599
23.118
93.007
35.252
1.00
26.43
6


4643
CE
LYS
A
599
24.656
93.063
35.120
1.00
32.43
6


4644
NZ
LYS
A
599
25.179
91.656
35.106
1.00
35.89
7


4645
N
ILE
A
600
18.623
95.442
33.287
1.00
13.51
7


4646
CA
ILE
A
600
17.178
95.336
33.021
1.00
12.20
6


4647
C
ILE
A
600
16.746
93.886
33.130
1.00
13.74
6


4648
O
ILE
A
600
17.476
92.927
32.799
1.00
14.24
8


4649
CB
ILE
A
600
16.938
95.829
31.554
1.00
13.87
6


4650
CG1
ILE
A
600
17.249
97.335
31.566
1.00
21.52
6


4651
CG2
ILE
A
600
15.499
95.618
31.051
1.00
15.85
6


4652
CD1
ILE
A
600
16.798
98.104
30.313
1.00
23.52
6


4653
N
TYR
A
601
15.545
93.745
33.676
1.00
13.09
7


4654
CA
TYR
A
601
14.926
92.453
33.883
1.00
12.76
6


4655
C
TYR
A
601
13.531
92.475
33.288
1.00
13.27
6


4656
O
TYR
A
601
12.914
93.491
32.986
1.00
15.09
8


4657
CB
TYR
A
601
14.751
92.119
35.387
1.00
14.11
6


4658
CG
TYR
A
601
16.065
91.805
36.078
1.00
11.98
6


4659
CD1
TYR
A
601
16.902
92.834
36.502
1.00
12.52
6


4660
CD2
TYR
A
601
16.473
90.490
36.242
1.00
12.95
6


4661
CE1
TYR
A
601
18.138
92.544
37.097
1.00
13.54
6


4662
CE2
TYR
A
601
17.673
90.213
36.888
1.00
14.26
6


4663
CZ
TYR
A
601
18.499
91.239
37.276
1.00
15.84
6


4664
OH
TYR
A
601
19.691
90.903
37.935
1.00
16.92
8


4665
N
LEU
A
602
12.986
91.285
33.068
1.00
11.99
7


4666
CA
LEU
A
602
11.657
91.057
32.494
1.00
13.20
6


4667
C
LEU
A
602
10.762
90.434
33.580
1.00
14.26
6


4668
O
LEU
A
602
11.148
89.522
34.284
1.00
13.06
8


4669
CB
LEU
A
602
11.794
90.060
31.334
1.00
13.29
6


4670
CG
LEU
A
602
10.506
89.432
30.800
1.00
10.59
6


4671
CD1
LEU
A
602
9.579
90.481
30.155
1.00
14.08
6


4672
CD2
LEU
A
602
10.864
88.385
29.704
1.00
11.83
6


4673
N
THR
A
603
9.482
90.861
33.649
1.00
12.02
7


4674
CA
THR
A
603
8.570
90.233
34.635
1.00
12.81
6


4675
C
THR
A
603
7.158
90.267
34.066
1.00
12.50
6


4676
O
THR
A
603
6.876
91.096
33.183
1.00
14.59
8


4677
CB
THR
A
603
8.711
90.983
35.969
1.00
14.38
6


4678
OG1
THR
A
603
7.971
90.241
36.987
1.00
14.53
8


4679
CG2
THR
A
603
8.152
92.414
35.971
1.00
15.35
6


4680
N
GLY
A
604
6.310
89.331
34.489
1.00
11.51
7


4681
CA
GLY
A
604
4.995
89.274
33.787
1.00
11.82
6


4682
C
GLY
A
604
4.042
88.348
34.530
1.00
12.03
6


4683
O
GLY
A
604
4.358
87.909
35.636
1.00
13.68
8


4684
N
ASN
A
605
2.911
88.082
33.859
1.00
12.03
7


4685
CA
ASN
A
605
1.782
87.516
34.637
1.00
11.85
6


4686
C
ASN
A
605
1.680
86.017
34.575
1.00
12.50
6


4687
O
ASN
A
605
0.615
85.441
34.625
1.00
14.07
8


4688
CB
ASN
A
605
0.481
88.161
34.031
1.00
13.77
6


4689
CG
ASN
A
605
0.265
87.610
32.629
1.00
17.19
6


4690
CD1
ASN
A
605
1.080
87.101
31.828
1.00
13.63
8


4691
ND2
ASN
A
605
−1.025
87.681
32.165
1.00
16.36
7


4692
N
ILE
A
606
2.823
85.308
34.560
1.00
13.26
7


4693
CA
ILE
A
606
2.836
83.860
34.628
1.00
11.73
6


4694
C
ILE
A
606
4.099
83.493
35.448
1.00
13.02
6


4695
O
ILE
A
606
5.005
84.349
35.511
1.00
13.34
8


4696
CB
ILE
A
606
2.995
83.184
33.259
1.00
11.81
6


4697
CG1
ILE
A
606
4.029
83.874
32.346
1.00
12.94
6


4698
CC2
ILE
A
606
1.625
83.138
32.550
1.00
15.56
6


4699
CD1
ILE
A
606
4.300
82.981
31.113
1.00
15.13
6


4700
N
PRO
A
607
4.181
82.331
36.033
1.00
13.09
7


4701
CA
PRO
A
607
5.294
81.982
36.937
1.00
12.68
6


4702
C
PRO
A
607
6.616
81.880
36.189
1.00
10.98
6


4703
O
PRO
A
607
7.700
82.258
36.671
1.00
14.73
8


4704
CB
PRO
A
607
4.895
80.647
37.607
1.00
13.69
6


4705
CG
PRO
A
607
3.818
80.118
36.675
1.00
16.48
6


4706
CD
PRO
A
607
3.081
81.335
36.098
1.00
16.43
6


4707
N
GLU
A
608
6.531
81.525
34.880
1.00
11.74
7


4708
CA
GLU
A
608
7.747
81.559
34.031
1.00
10.58
6


4709
C
GLU
A
608
8.382
82.958
33.994
1.00
13.60
6


4710
O
GLU
A
608
9.606
83.060
33.731
1.00
11.79
8


4711
CB
GLU
A
608
7.437
81.056
32.616
1.00
11.09
6


4712
CG
GLU
A
608
7.145
79.550
32.522
1.00
10.94
6


4713
CD
GLU
A
608
5.674
79.163
32.699
1.00
14.31
6


4714
OE1
GLU
A
608
4.875
79.973
32.699
1.00
14.31
6


4715
OE2
GLU
A
608
5.344
78.040
32.280
1.00
13.22
8


4716
N
LEU
A
609
7.571
83.999
34.112
1.00
11.31
7


4717
CA
LEU
A
609
8.093
85.359
34.095
1.00
11.00
6


4718
C
LEU
A
609
7.944
86.002
35.453
1.00
12.01
6


4719
O
LEU
A
609
7.959
87.224
35.602
1.00
14.24
8


4720
CB
LEU
A
609
7.249
86.188
33.078
1.00
14.30
6


4721
CG
LEU
A
609
7.424
85.668
31.627
1.00
13.57
6


4722
CD1
LEU
A
609
6.672
86.643
30.695
1.00
18.28
6


4723
CD2
LEU
A
609
8.912
85.648
31.238
1.00
14.71
6


4724
N
GLY
A
610
7.854
85.194
36.525
1.00
10.78
7


4725
CA
GLY
A
610
7.950
85.729
37.864
1.00
10.94
6


4726
C
GLY
A
610
6.664
86.230
38.554
1.00
13.37
6


4727
O
GLY
A
610
6.767
86.832
39.647
1.00
13.90
8


4728
N
ASN
A
611
5.525
86.174
37.906
1.00
13.56
7


4729
CA
ASN
A
611
4.262
86.696
38.463
1.00
14.13
6


4730
C
ASN
A
611
4.462
88.079
39.072
1.00
13.68
6


4731
O
ASN
A
611
4.063
88.427
40.207
1.00
14.78
8


4732
CB
ASN
A
611
3.695
85.782
39.555
1.00
13.73
6


4733
CG
ASN
A
611
3.110
84.538
38.890
1.00
16.98
6


4734
OD1
ASN
A
611
2.353
84.585
37.897
1.00
17.26
8


4735
ND2
ASN
A
611
3.501
83.420
39.478
1.00
16.08
7


4736
N
TRP
A
612
5.010
88.962
38.242
1.00
13.00
7


4737
CA
TRP
A
612
5.298
90.339
38.534
1.00
13.35
6


4738
C
TRP
A
612
6.284
90.676
39.608
1.00
14.25
6


4739
O
TRP
A
612
6.420
91.775
40.107
1.00
15.26
8


4740
CB
TRP
A
612
3.915
91.044
38.832
1.00
13.65
6


4741
CG
TRP
A
612
2.965
91.036
37.664
1.00
13.25
6


4742
CD1
TRP
A
612
1.775
90.359
37.632
1.00
13.84
6


4743
CD2
TRP
A
612
3.138
91.564
36.359
1.00
14.07
6


4744
NE1
TRP
A
612
1.160
90.489
36.402
1.00
13.90
7


4745
CE2
TRP
A
612
1.983
91.288
35.617
1.00
16.64
6


4746
CE3
TRP
A
612
4.148
92.402
35.815
1.00
15.91
6


4747
CZ2
TRP
A
612
1.843
91.676
34.288
1.00
14.35
6


4748
CZ3
TRP
A
612
3.980
92.856
34.506
1.00
14.55
6


4749
CH2
TRP
A
612
2.844
92.490
33.747
1.00
14.05
6


4750
N
SER
A
613
7.114
89.674
40.049
1.00
14.59
7


4751
CA
SER
A
613
8.136
89.943
41.025
1.00
16.76
6


4752
C
SER
A
613
9.171
90.916
40.471
1.00
15.94
6


4753
O
SER
A
613
9.510
90.841
39.281
1.00
15.44
8


4754
CB
SER
A
613
8.804
88.572
41.315
1.00
14.15
6


4755
OG
SER
A
613
9.842
88.719
42.250
1.00
15.35
8


4756
N
THR
A
614
9.821
91.648
41.406
1.00
13.40
7


4757
CA
THR
A
614
11.021
92.394
41.037
1.00
13.18
6


4758
C
THR
A
614
12.238
91.869
41.796
1.00
12.85
6


4759
O
THR
A
614
13.311
92.464
41.777
1.00
15.88
8


4760
CB
THR
A
614
10.895
93.904
41.297
1.00
16.41
6


4761
OG1
THR
A
614
10.626
94.073
42.724
1.00
18.07
8


4762
CG2
THR
A
614
9.718
94.523
40.520
1.00
18.09
6


4763
N
ASP
A
615
12.033
90.680
42.425
1.00
13.65
7


4764
CA
ASP
A
615
13.138
90.024
43.143
1.00
15.24
6


4765
C
ASP
A
615
14.084
89.416
42.093
1.00
12.74
6


4766
O
ASP
A
615
13.582
88.794
41.143
1.00
13.71
8


4767
CB
ASP
A
615
12.511
88.981
44.075
1.00
14.77
6


4768
CG
ASP
A
615
13.634
88.423
44.970
1.00
21.15
6


4769
OD1
ASP
A
615
13.956
88.932
46.048
1.00
23.65
8


4770
OD2
ASP
A
615
14.204
87.431
44.586
1.00
18.42
8


4771
N
THR
A
616
15.390
89.536
42.350
1.00
12.77
7


4772
CA
THR
A
616
16.387
89.067
41.365
1.00
13.57
6


4773
C
THR
A
616
17.391
88.146
42.072
1.00
15.88
6


4774
O
THR
A
616
18.487
87.902
41.566
1.00
14.89
8


4775
CB
THR
A
616
17.144
90.224
40.674
1.00
14.32
6


4776
OG1
THR
A
616
17.752
91.045
41.713
1.00
15.99
8


4777
CG2
THR
A
616
16.189
91.128
39.884
1.00
16.33
6


4778
N
SER
A
617
16.981
87.590
43.216
1.00
13.15
7


4779
CA
SER
A
617
17.813
86.641
43.956
1.00
12.49
6


4780
C
SER
A
617
17.759
85.265
43.312
1.00
13.68
6


4781
O
SER
A
617
17.193
85.034
42.235
1.00
12.79
8


4782
CB
SER
A
617
17.271
86.583
45.396
1.00
14.38
6


4783
OG
SER
A
617
16.056
85.882
45.441
1.00
15.10
8


4784
N
GLY
A
618
18.327
84.268
44.080
1.00
15.05
7


4785
CA
GLY
A
618
18.300
82.869
43.621
1.00
13.01
6


4786
C
GLY
A
618
16.967
82.147
43.811
1.00
13.49
6


4787
O
GLY
A
618
16.835
80.938
43.552
1.00
15.47
8


4788
N
ALA
A
619
15.893
82.847
44.200
1.00
13.99
7


4789
CA
ALA
A
619
14.592
82.218
44.333
1.00
14.93
6


4790
C
ALA
A
619
14.033
81.691
43.015
1.00
15.28
6


4791
O
ALA
A
619
14.489
82.043
41.907
1.00
15.28
8


4792
CB
ALA
A
619
13.582
83.263
44.854
1.00
17.52
6


4793
N
VAL
A
620
13.043
80.805
43.172
1.00
11.74
7


4794
CA
VAL
A
620
12.419
80.230
41.967
1.00
12.25
6


4795
C
VAL
A
620
11.259
81.126
41.502
1.00
12.14
6


4796
O
VAL
A
620
10.533
81.679
42.344
1.00
14.38
8


4797
CB
VAL
A
620
11.796
78.892
42.436
1.00
15.46
6


4798
CG1
VAL
A
620
11.242
78.231
41.173
1.00
13.86
6


4799
CG2
VAL
A
620
12.924
77.941
42.923
1.00
15.04
6


4800
N
ASN
A
621
11.157
81.254
40.168
1.00
12.23
7


4801
CA
ASN
A
621
10.066
82.044
39.571
1.00
12.45
6


4802
C
ASN
A
621
9.968
83.484
40.032
1.00
12.62
6


4803
O
ASN
A
621
8.860
83.896
40.480
1.00
12.87
8


4804
CB
ASN
A
621
8.676
81.346
39.732
1.00
10.99
6


4805
CG
ASN
A
621
8.656
79.972
39.084
1.00
11.13
6


4806
OD1
ASN
A
621
9.398
79.689
38.141
1.00
13.90
8


4807
ND2
ASN
A
621
7.742
79.105
39.596
1.00
13.32
7


4808
N
ASN
A
622
11.106
84.199
40.048
1.00
13.97
7


4809
CA
ASN
A
622
11.116
85.623
40.322
1.00
11.35
6


4810
C
ASN
A
622
11.418
86.389
39.037
1.00
12.47
6


4811
O
ASN
A
622
11.090
85.862
37.960
1.00
12.66
8


4812
CB
ASN
A
622
12.073
85.956
41.471
1.00
12.54
6


4813
CG
ASN
A
622
13.543
85.545
41.151
1.00
12.82
6


4814
OD1
ASN
A
622
13.811
85.093
40.044
1.00
12.70
8


4815
ND2
ASN
A
622
14.377
85.753
42.196
1.00
13.72
7


4816
N
ALA
A
623
11.883
87.626
39.098
1.00
11.27
7


4817
CA
ALA
A
623
12.088
88.339
37.812
1.00
12.38
6


4818
C
ALA
A
623
13.107
87.592
36.947
1.00
13.25
6


4819
O
ALA
A
623
14.035
87.018
37.469
1.00
13.43
8


4820
CB
ALA
A
623
12.586
89.748
38.120
1.00
14.46
6


4821
N
GLN
A
624
12.905
87.740
35.631
1.00
12.11
7


4822
CA
GLN
A
624
13.742
87.034
34.660
1.00
11.87
6


4823
C
GLN
A
624
14.828
87.912
34.071
1.00
12.70
6


4824
O
GLN
A
624
14.646
89.092
33.762
1.00
13.14
8


4825
CB
GLN
A
624
12.880
86.477
33.521
1.00
14.55
6


4826
CG
GLN
A
624
11.779
85.492
34.084
1.00
13.33
6


4827
CD
GLN
A
624
12.451
84.323
34.754
1.00
14.35
6


4828
OE1
GLN
A
624
13.213
83.546
34.096
1.00
15.81
8


4829
NE2
GLN
A
624
12.268
84.078
36.040
1.00
14.08
7


4830
N
GLY
A
625
15.989
87.264
33.941
1.00
12.93
7


4831
CA
GLY
A
625
17.183
87.950
33.418
1.00
12.61
6


4832
C
GLY
A
625
18.392
87.917
34.310
1.00
12.24
6


4833
O
GLY
A
625
18.497
86.888
34.934
1.00
13.82
8


4834
N
PRO
A
626
19.296
88.815
34.131
1.00
12.81
7


4835
CA
PRO
A
626
19.237
90.097
33.510
1.00
15.64
6


4836
C
PRO
A
626
19.288
89.998
32.003
1.00
15.42
6


4837
O
PRO
A
626
19.675
88.992
31.364
1.00
15.65
8


4838
CB
PRO
A
626
20.374
91.012
34.019
1.00
15.71
6


4839
CG
PRO
A
626
21.401
89.927
34.320
1.00
14.63
6


4840
CD
PRO
A
626
20.565
88.780
34.858
1.00
13.83
6


4841
N
LEU
A
627
18.725
91.061
31.332
1.00
13.98
7


4842
CA
LEU
A
627
18.935
91.116
29.881
1.00
13.16
6


4843
C
LEU
A
627
20.364
91.609
29.649
1.00
14.14
6


4844
O
LEU
A
627
21.024
92.215
30.527
1.00
14.86
8


4845
CB
LEU
A
627
17.906
92.080
29.214
1.00
13.73
6


4846
CG
LEU
A
627
16.549
91.433
28.919
1.00
13.68
6


4847
CD1
LEU
A
627
15.771
91.075
30.200
1.00
16.08
6


4848
CD2
LEU
A
627
15.630
92.370
28.084
1.00
16.33
6


4849
N
LEU
A
628
20.804
91.374
28.421
1.00
12.55
7


4850
CA
LEU
A
628
22.139
91.805
27.919
1.00
12.76
6


4851
C
LEU
A
628
21.994
92.999
26.973
1.00
15.67
6


4852
O
LEU
A
628
20.910
93.197
26.394
1.00
14.76
8


4853
CB
LEU
A
628
22.746
90.663
27.111
1.00
14.06
6


4854
CG
LEU
A
628
22.848
89.332
27.886
1.00
14.72
6


4855
CD1
LEU
A
628
23.526
88.239
27.056
1.00
12.14
6


4856
CD2
LEU
A
628
23.659
89.508
29.185
1.00
20.12
6


4857
N
ALA
A
629
23.117
93.699
26.702
1.00
16.33
7


4858
CA
ALA
A
629
22.871
94.875
25.787
1.00
16.83
6


4859
C
ALA
A
629
23.983
95.083
24.795
1.00
15.77
6


4860
O
ALA
A
629
24.610
96.177
24.707
1.00
15.92
8


4861
CB
ALA
A
629
22.674
96.098
26.674
1.00
19.56
6


4862
N
PRO
A
630
24.278
94.136
23.970
1.00
16.96
7


4863
CA
PRO
A
630
25.237
94.281
22.873
1.00
19.28
6


4864
C
PRO
A
630
24.773
95.400
21.940
1.00
21.06
6


4865
O
PRO
A
630
25.633
96.015
21.314
1.00
23.58
8


4866
CB
PRO
A
630
25.314
92.944
22.123
1.00
17.59
6


4867
CG
PRO
A
630
23.928
92.367
22.442
1.00
18.42
6


4868
CD
PRO
A
630
23.644
92.807
23.877
1.00
18.05
6


4869
N
ASN
A
631
23.464
95.562
21.768
1.00
17.93
7


4870
CA
ASN
A
631
22.935
96.635
20.926
1.00
17.58
6


4871
C
ASN
A
631
22.382
97.779
21.748
1.00
17.45
6


4872
O
ASN
A
631
21.359
98.370
21.354
1.00
18.41
8


4873
CB
ASN
A
631
21.902
96.082
19.950
1.00
18.61
6


4874
CG
ASN
A
631
22.400
94.876
19.161
1.00
28.21
6


4875
OD1
ASN
A
631
21.838
93.764
19.168
1.00
27.73
8


4876
ND2
ASN
A
631
23.476
95.224
18.455
1.00
19.54
7


4877
N
TYR
A
632
22.980
98.110
22.883
1.00
16.27
7


4878
CA
TYR
A
632
22.570
99.229
23.700
1.00
17.84
6


4879
C
TYR
A
632
22.255
100.496
22.909
1.00
19.89
6


4880
O
TYR
A
632
23.030
100.672
21.982
1.00
19.89
8


4881
CB
TYR
A
632
23.749
99.537
24.643
1.00
18.23
6


4882
CG
TYR
A
632
23.520
100.604
25.654
1.00
20.78
6


4883
CD1
TYR
A
632
22.919
100.369
26.875
1.00
20.07
6


4884
CD2
TYR
A
632
23.839
101.933
25.333
1.00
22.98
6


4885
CE1
TYR
A
632
22.700
101.367
27.797
1.00
22.62
6


4886
CE2
TYR
A
632
23.578
102.953
26.223
1.00
23.64
6


4887
CZ
TYR
A
632
23.051
102.671
27.457
1.00
27.32
6


4888
OH
TYR
A
632
22.814
103.670
28.369
1.00
23.27
8


4889
N
PRO
A
633
21.113
101.067
23.157
1.00
19.06
7


4890
CA
PRO
A
633
20.194
101.103
24.225
1.00
16.58
6


4891
C
PRO
A
633
19.087
100.033
24.123
1.00
15.76
6


4892
O
PRO
A
633
18.188
100.153
24.954
1.00
16.24
8


4893
CB
PRO
A
633
19.474
102.498
24.311
1.00
19.94
6


4894
CG
PRO
A
633
19.449
102.810
22.846
1.00
24.00
6


4895
CD
PRO
A
633
20.772
102.271
22.369
1.00
24.76
6


4896
N
ASP
A
634
19.272
99.094
23.169
1.00
16.18
7


4897
CA
ASP
A
634
18.330
97.978
23.121
1.00
16.48
6


4898
C
ASP
A
634
18.923
96.792
23.937
1.00
15.97
6


4899
O
ASP
A
634
20.153
96.671
24.058
1.00
16.27
8


4900
CB
ASP
A
634
18.133
97.402
21.731
1.00
15.05
6


4901
CG
ASP
A
634
17.626
98.434
20.695
1.00
20.07
6


4902
OD1
ASP
A
634
17.138
99.519
21.100
1.00
17.34
8


4903
OD2
ASP
A
634
17.728
98.097
19.503
1.00
19.32
8


4904
N
TRP
A
635
18.009
96.147
24.656
1.00
14.45
7


4905
CA
TRP
A
635
18.413
95.017
25.510
1.00
16.15
6


4906
C
TRP
A
635
17.708
93.736
25.082
1.00
13.84
6


4907
O
TRP
A
635
16.590
93.820
24.606
1.00
13.90
8


4908
CB
TRP
A
635
18.024
95.299
26.962
1.00
15.52
6


4909
CG
TRP
A
635
18.818
96.421
27.587
1.00
14.07
6


4910
CD1
TRP
A
635
18.737
97.739
27.178
1.00
14.13
6


4911
CD2
TRP
A
635
19.713
96.407
28.694
1.00
16.17
6


4912
NE1
TRP
A
635
19.561
98.533
27.989
1.00
15.61
7


4913
CE2
TRP
A
635
20.179
97.706
28.908
1.00
17.77
6


4914
CE3
TRP
A
635
20.179
95.350
29.511
1.00
18.51
6


4915
CZ2
TRP
A
635
21.071
98.018
29.935
1.00
19.26
6


4916
CZ3
TRP
A
635
21.100
95.671
30.515
1.00
23.17
6


4917
CH2
TRP
A
635
21.514
96.992
30.735
1.00
20.92
6


4918
N
PHE
A
636
18.294
92.561
25.372
1.00
12.41
7


4919
CA
PHE
A
636
17.562
91.335
24.947
1.00
11.57
6


4920
C
PHE
A
636
18.071
90.194
25.855
1.00
12.41
6


4921
O
PHE
A
636
19.204
90.239
26.345
1.00
13.24
8


4922
CB
PHE
A
636
17.761
90.971
23.435
1.00
12.03
6


4923
CG
PHE
A
636
19.030
90.118
23.261
1.00
12.15
6


4924
CD1
PHE
A
636
20.287
90.667
23.292
1.00
17.38
6


4925
CD2
PHE
A
636
18.856
88.751
23.095
1.00
11.02
6


4926
CE1
PHE
A
636
21.417
89.860
23.207
1.00
19.56
6


4927
CE2
PHE
A
636
19.996
87.906
22.997
1.00
12.49
6


4928
CZ
PHE
A
636
21.250
88.466
23.034
1.00
17.21
6


4929
N
TYR
A
637
17.229
89.170
25.966
1.00
12.09
7


4930
CA
TYR
A
637
17.759
87.841
26.425
1.00
12.35
6


4931
C
TYR
A
637
16.714
86.848
25.989
1.00
12.24
6


4932
O
TYR
A
637
15.911
87.135
25.088
1.00
12.49
8


4933
CB
TYR
A
637
18.183
87.770
27.903
1.00
12.77
6


4934
CG
TYR
A
637
19.035
86.513
28.195
1.00
13.33
6


4935
CD1
TYR
A
637
20.253
86.244
27.548
1.00
12.60
6


4936
CD2
TYR
A
637
18.595
85.573
29.127
1.00
10.55
6


4937
CE1
TYR
A
637
21.022
85.134
27.792
1.00
11.85
6


4938
CE2
TYR
A
637
19.321
84.424
29.387
1.00
12.60
6


4939
CZ
TYR
A
637
20.521
84.221
28.728
1.00
11.69
6


4940
OH
TYR
A
637
21.255
83.073
29.016
1.00
11.85
8


4941
N
VAL
A
638
16.857
85.565
26.379
1.00
12.66
7


4942
CA
VAL
A
638
16.033
84.508
25.827
1.00
10.90
6


4943
C
VAL
A
638
15.492
83.693
27.023
1.00
11.04
6


4944
O
VAL
A
638
16.202
83.367
27.980
1.00
13.35
8


4945
CB
VAL
A
638
16.830
83.496
24.987
1.00
12.00
6


4946
CG1
VAL
A
638
15.922
82.650
24.118
1.00
12.74
6


4947
CG2
VAL
A
638
17.799
84.300
24.074
1.00
10.59
6


4948
N
PHE
A
639
14.137
83.517
26.957
1.00
12.77
7


4949
CA
PHE
A
639
13.441
82.960
28.082
1.00
9.34
6


4950
C
PHE
A
639
12.466
81.877
27.665
1.00
11.56
6


4951
O
PHE
A
639
11.814
81.982
26.632
1.00
12.26
8


4952
CB
PHE
A
639
12.612
84.072
28.807
1.00
11.50
6


4953
CG
PHE
A
639
13.498
85.209
29.322
1.00
12.29
6


4954
CD1
PHE
A
639
14.294
85.042
30.446
1.00
11.38
6


4955
CD2
PHE
A
639
13.567
86.380
28.563
1.00
13.67
6


4956
CE1
PHE
A
639
15.176
86.094
30.829
1.00
12.05
6


4957
CE2
PHE
A
639
14.416
87.425
28.965
1.00
13.84
6


4958
CZ
PHE
A
639
15.196
87.301
30.113
1.00
13.28
6


4959
N
SER
A
640
12.323
80.913
28.609
1.00
10.61
7


4960
CA
SER
A
640
11.376
79.833
28.360
1.00
11.72
6


4961
C
SER
A
640
10.005
80.223
28.872
1.00
11.19
6


4962
O
SER
A
640
9.878
80.649
30.026
1.00
12.90
8


4963
CB
SER
A
640
11.915
78.568
29.132
1.00
12.23
6


4964
OG
SER
A
640
11.028
77.448
28.846
1.00
12.04
8


4965
N
VAL
A
641
9.007
80.190
27.975
1.00
8.82
7


4966
CA
VAL
A
641
7.635
80.609
28.374
1.00
11.37
6


4967
C
VAL
A
641
6.697
79.601
27.775
1.00
11.35
6


4968
O
VAL
A
641
7.075
78.840
26.864
1.00
10.31
8


4969
CB
VAL
A
641
7.286
82.019
27.760
1.00
11.50
6


4970
CG1
VAL
A
641
8.061
83.038
28.624
1.00
13.20
6


4971
CG2
VAL
A
641
7.607
82.115
26.241
1.00
10.82
6


4972
N
PRO
A
642
5.470
79.384
28.254
1.00
10.92
7


4973
CA
PRO
A
642
4.582
78.438
27.626
1.00
11.56
6


4974
C
PRO
A
642
4.256
78.780
26.166
1.00
10.87
6


4975
O
PRO
A
642
4.048
79.994
25.888
1.00
12.26
8


4976
CB
PRO
A
642
3.295
78.524
28.529
1.00
11.37
6


4977
CG
PRO
A
642
3.352
79.948
29.064
1.00
11.52
6


4978
CD
PRO
A
642
4.866
80.234
29.308
1.00
14.12
6


4979
N
ALA
A
643
4.267
77.800
25.291
1.00
11.34
7


4980
CA
ALA
A
643
4.033
77.992
23.839
1.00
12.12
6


4981
C
ALA
A
643
2.531
78.215
23.567
1.00
13.78
6


4982
O
ALA
A
643
1.681
77.650
24.236
1.00
15.31
8


4983
CB
ALA
A
643
4.330
76.657
23.141
1.00
13.71
6


4984
N
GLY
A
644
2.317
79.106
22.623
1.00
14.27
7


4985
CA
GLY
A
644
0.952
79.377
22.150
1.00
14.42
6


4986
C
GLY
A
644
0.065
80.108
23.133
1.00
15.94
6


4987
O
GLY
A
644
−1.154
79.765
23.178
1.00
19.30
8


4988
N
LYS
A
645
0.597
80.884
24.030
1.00
14.60
7


4989
CA
LYS
A
645
−0.171
81.519
25.092
1.00
14.20
6


4990
C
LYS
A
645
−0.060
83.017
24.926
1.00
17.57
6


4991
O
LYS
A
645
1.002
83.579
24.623
1.00
17.47
8


4992
CB
LYS
A
645
0.376
81.126
26.483
1.00
14.57
6


4993
CG
LYS
A
645
0.313
79.611
26.725
1.00
17.45
6


4994
CD
LYS
A
645
−1.136
79.116
26.699
1.00
17.54
6


4995
CE
LYS
A
645
−1.184
77.572
26.837
1.00
21.69
6


4996
NZ
LYS
A
645
−0.587
77.121
28.112
1.00
31.91
7


4997
N
THR
A
646
−1.157
83.717
25.357
1.00
14.42
7


4998
CA
THR
A
646
−1.090
85.140
25.434
1.00
14.66
6


4999
C
THR
A
646
−0.662
85.594
26.824
1.00
13.55
6


5000
O
THR
A
646
−1.221
85.157
27.850
1.00
16.55
8


5001
CB
THR
A
646
−2.510
85.720
25.098
1.00
17.00
6


5002
OG1
THR
A
646
−2.824
85.361
23.738
1.00
16.76
8


5003
CG2
THR
A
646
−2.463
87.240
25.195
1.00
18.18
6


5004
N
ILE
A
647
0.360
86.434
26.913
1.00
11.81
7


5005
CA
ILE
A
647
1.001
86.816
28.152
1.00
11.47
6


5006
C
ILE
A
647
1.047
88.357
28.250
1.00
13.84
6


5007
O
ILE
A
647
0.991
89.054
27.201
1.00
14.89
8


5008
CB
ILE
A
647
2.476
86.353
28.278
1.00
13.09
6


5009
CG1
ILE
A
647
3.296
86.770
27.045
1.00
12.50
6


5010
CG2
ILE
A
647
2.410
84.817
28.343
1.00
14.24
6


5011
CD1
ILE
A
647
4.813
86.486
27.247
1.00
17.78
6


5012
N
GLN
A
648
1.150
88.776
29.495
1.00
12.61
7


5013
CA
GLN
A
648
1.402
90.212
29.726
1.00
11.91
6


5014
C
GLN
A
648
2.687
90.407
30.490
1.00
15.15
6


5015
O
GLN
A
648
3.041
89.586
31.338
1.00
15.89
8


5016
CB
GLN
A
648
0.298
90.835
30.611
1.00
13.04
6


5017
CG
GLN
A
648
−1.032
90.704
29.820
1.00
20.15
6


5018
CD
GLN
A
648
−2.040
91.727
30.260
1.00
27.13
6


5019
OE1
GLN
A
648
−1.797
92.691
30.982
1.00
23.22
8


5020
NE2
GLN
A
648
−3.309
91.503
29.847
1.00
28.35
7


5021
N
PHE
A
649
3.446
91.461
30.155
1.00
13.26
7


5022
CA
PHE
A
649
4.767
91.622
30.746
1.00
12.72
6


5023
C
PHE
A
649
5.219
93.094
30.663
1.00
14.64
6


5024
O
PHE
A
649
4.697
93.903
29.862
1.00
14.50
8


5025
CB
PHE
A
649
5.812
90.743
30.051
1.00
12.47
6


5026
CG
PHE
A
649
5.875
90.962
28.544
1.00
13.33
6


5027
CD1
PHE
A
649
4.996
90.400
27.682
1.00
14.84
6


5028
CD2
PHE
A
649
6.861
91.790
28.013
1.00
13.41
6


5029
CE1
PHE
A
649
5.031
90.678
26.303
1.00
15.17
6


5030
CE2
PHE
A
649
6.977
92.043
26.666
1.00
16.16
6


5031
CZ
PHE
A
649
6.057
91.493
25.807
1.00
13.88
6


5032
N
LYS
A
650
6.135
93.413
31.538
1.00
13.99
7


5033
CA
LYS
A
650
6.876
94.683
31.405
1.00
13.18
6


5034
C
LYS
A
650
8.349
94.411
31.797
1.00
15.87
6


5035
O
LYS
A
650
8.696
93.364
32.375
1.00
13.96
8


5036
CB
LYS
A
650
6.358
95.735
32.410
1.00
14.62
6


5037
CG
LYS
A
650
5.004
96.385
31.989
1.00
15.36
6


5038
CD
LYS
A
650
4.922
97.604
32.979
1.00
19.44
6


5039
CE
LYS
A
650
3.841
98.565
32.553
1.00
24.45
6


5040
NZ
LYS
A
650
3.898
99.741
33.515
1.00
18.41
7


5041
N
PHE
A
651
9.172
95.398
31.438
1.00
13.40
7


5042
CA
PHE
A
651
10.571
95.420
31.850
1.00
14.23
6


5043
C
PHE
A
651
10.800
96.474
32.926
1.00
16.48
6


5044
O
PHE
A
651
9.990
97.396
33.132
1.00
17.07
8


5045
CB
PHE
A
651
11.465
95.783
30.638
1.00
12.48
6


5046
CG
PHE
A
651
11.280
94.796
29.512
1.00
15.91
6


5047
CD1
PHE
A
651
10.277
94.943
28.564
1.00
13.76
6


5048
CD2
PHE
A
651
12.127
93.681
29.453
1.00
14.89
6


5049
CE1
PHE
A
651
10.114
94.016
27.568
1.00
12.48
6


5050
CE2
PHE
A
651
11.957
92.759
28.426
1.00
13.50
6


5051
CZ
PHE
A
651
10.944
92.884
27.461
1.00
16.56
6


5052
N
PHE
A
652
11.849
96.240
33.723
1.00
15.18
7


5053
CA
PHE
A
652
12.249
97.256
34.704
1.00
14.29
6


5054
C
PHE
A
652
13.756
97.339
34.785
1.00
17.92
6


5055
O
PHE
A
652
14.452
96.365
34.487
1.00
15.37
8


5056
CB
PHE
A
652
11.634
96.950
36.084
1.00
15.14
6


5057
CG
PHE
A
652
12.097
95.688
36.789
1.00
16.77
6


5058
CD1
PHE
A
652
13.251
95.685
37.565
1.00
15.74
6


5059
CD2
PHE
A
652
11.326
94.553
36.695
1.00
15.90
6


5060
CE1
PHE
A
652
13.633
94.518
38.231
1.00
14.76
6


5061
CE2
PHE
A
652
11.695
93.407
37.380
1.00
15.19
6


5062
CZ
PHE
A
652
12.866
93.343
38.139
1.00
14.25
6


5063
N
ILE
A
653
14.244
98.512
35.189
1.00
14.94
7


5064
CA
ILE
A
653
15.705
98.598
35.463
1.00
14.72
6


5065
C
ILE
A
653
15.906
98.394
36.962
1.00
18.67
6


5066
O
ILE
A
653
15.175
98.971
37.804
1.00
19.59
8


5067
CB
ILE
A
653
16.168
100.071
35.163
1.00
14.73
6


5068
CG1
ILE
A
653
16.000
100.337
33.693
1.00
18.74
6


5069
CG2
ILE
A
653
17.628
100.201
35.616
1.00
18.25
6


5070
CD1
ILE
A
653
16.191
101.838
33.353
1.00
20.43
6


5071
N
LYS
A
654
16.847
97.524
37.282
1.00
17.58
7


5072
CA
LYS
A
654
17.273
97.382
38.690
1.00
18.28
6


5073
C
LYS
A
654
18.623
98.139
38.780
1.00
15.87
6


5074
O
LYS
A
654
19.571
97.760
38.135
1.00
18.77
8


5075
CB
LYS
A
654
17.469
95.933
39.131
1.00
16.77
6


5076
CG
LYS
A
654
17.774
95.976
40.661
1.00
20.67
6


5077
CD
LYS
A
654
17.709
94.558
41.225
1.00
24.12
6


5078
CE
LYS
A
654
18.152
94.544
42.680
1.00
30.47
6


5079
NZ
LYS
A
654
17.967
93.152
43.221
1.00
39.55
7


5080
N
ARG
A
655
18.538
99.361
39.337
1.00
19.37
7


5081
CA
ARG
A
655
19.776
100.164
39.391
1.00
21.00
6


5082
C
ARG
A
655
20.820
99.478
40.256
1.00
24.58
6


5083
O
ARG
A
655
20.486
98.604
41.057
1.00
22.97
8


5084
CB
ARG
A
655
19.445
101.531
40.003
1.00
18.71
6


5085
CG
ARG
A
655
18.411
102.323
39.192
1.00
19.26
6


5086
CD
ARG
A
655
19.036
102.699
37.864
1.00
24.72
6


5087
NE
ARG
A
655
18.169
103.597
37.102
1.00
23.26
7


5088
CZ
ARG
A
655
18.428
104.073
35.883
1.00
23.74
6


5089
NH1
ARG
A
655
19.508
103.812
35.193
1.00
20.63
7


5090
NH2
ARG
A
655
17.509
104.882
35.343
1.00
24.30
7


5091
N
ALA
A
656
22.090
99.900
40.135
1.00
24.51
7


5092
CA
ALA
A
656
23.170
99.305
40.898
1.00
28.24
6


5093
C
ALA
A
656
22.865
99.430
42.401
1.00
27.25
6


5094
O
ALA
A
656
23.305
98.533
43.117
1.00
32.90
8


5095
CB
ALA
A
656
24.518
100.009
40.656
1.00
29.09
6


5096
N
ASP
A
657
22.145
100.427
42.856
1.00
31.34
7


5097
CA
ASP
A
657
21.850
100.561
44.282
1.00
32.95
6


5098
C
ASP
A
657
20.617
99.783
44.694
1.00
33.22
6


5099
O
ASP
A
657
20.202
99.906
45.852
1.00
30.17
8


5100
CB
ASP
A
657
21.725
102.050
44.643
1.00
27.78
6


5101
CG
ASP
A
657
20.499
102.712
44.087
1.00
34.66
6


5102
OD1
ASP
A
657
19.665
102.035
43.431
1.00
28.22
8


5103
OD2
ASP
A
657
20.239
103.920
44.267
1.00
33.52
8


5104
N
GLY
A
658
20.019
98.958
43.803
1.00
29.54
7


5105
CA
GLY
A
658
18.874
98.181
44.227
1.00
29.70
6


5106
C
GLY
A
658
17.543
98.837
43.931
1.00
26.81
6


5107
O
GLY
A
658
16.531
98.126
43.935
1.00
30.39
8


5108
N
THR
A
659
17.502
100.106
43.566
1.00
23.52
7


5109
CA
THR
A
659
16.313
100.826
43.215
1.00
25.61
6


5110
C
THR
A
659
15.641
100.184
41.985
1.00
23.40
6


5111
O
THR
A
659
16.419
99.778
41.118
1.00
27.85
8


5112
CB
THR
A
659
16.614
102.279
42.717
1.00
19.42
6


5113
OG1
THR
A
659
17.524
102.993
43.510
1.00
46.62
8


5114
CG2
THR
A
659
15.276
103.016
42.706
1.00
37.02
6


5115
N
ILE
A
660
14.319
100.215
41.909
1.00
20.34
7


5116
CA
ILE
A
660
13.596
99.691
40.758
1.00
25.29
6


5117
C
ILE
A
660
12.933
100.761
39.919
1.00
25.57
6


5118
O
ILE
A
660
12.186
101.612
40.465
1.00
27.02
8


5119
CB
ILE
A
660
12.458
98.722
41.207
1.00
26.69
6


5120
CG1
ILE
A
660
13.012
97.534
41.991
1.00
27.58
6


5121
CG2
ILE
A
660
11.704
98.273
39.972
1.00
21.18
6


5122
CD1
ILE
A
660
14.022
96.722
41.221
1.00
24.46
6


5123
N
GLN
A
661
13.169
100.849
38.624
1.00
20.86
7


5124
CA
GLN
A
661
12.479
101.793
37.743
1.00
19.49
6


5125
C
GLN
A
661
11.720
101.014
36.669
1.00
20.02
6


5126
O
GLN
A
661
12.266
100.405
35.730
1.00
19.24
8


5127
CB
GLN
A
661
13.410
102.775
37.023
1.00
20.06
6


5128
CG
GLN
A
661
12.611
103.688
36.077
1.00
21.00
6


5129
CD
GLN
A
661
13.541
104.665
35.350
1.00
21.47
6


5130
OE1
GLN
A
661
13.279
104.997
34.195
1.00
28.51
8


5131
NE2
GLN
A
661
14.578
105.095
36.040
1.00
22.67
7


5132
N
TRP
A
662
10.389
100.926
36.834
1.00
20.75
7


5133
CA
TRP
A
662
9.556
100.227
35.857
1.00
18.49
6


5134
C
TRP
A
662
9.441
100.967
34.536
1.00
21.67
6


5135
O
TRP
A
662
9.412
102.230
34.565
1.00
19.29
8


5136
CB
TRP
A
662
8.152
100.082
36.437
1.00
18.81
6


5137
CG
TRP
A
662
7.960
99.114
37.551
1.00
18.39
6


5138
CD1
TRP
A
662
8.083
99.359
38.889
1.00
19.35
6


5139
CD2
TRP
A
662
7.543
97.752
37.419
1.00
18.13
6


5140
NE1
TRP
A
662
7.781
98.218
39.608
1.00
21.46
7


5141
CE2
TRP
A
662
7.444
97.223
38.713
1.00
18.92
6


5142
CE3
TRP
A
662
7.213
96.960
36.295
1.00
18.78
6


5143
CZ2
TRP
A
662
6.994
95.923
38.966
1.00
16.39
6


5144
CZ3
TRP
A
662
6.798
95.661
36.537
1.00
18.67
6


5145
CH2
TRP
A
662
6.725
95.156
37.854
1.00
15.44
6


5146
N
GLU
A
663
9.170
100.250
33.453
1.00
18.24
7


5147
CA
GLU
A
663
8.551
100.857
32.292
1.00
17.79
6


5148
C
GLU
A
663
7.240
101.517
32.740
1.00
17.95
6


5149
O
GLU
A
663
6.519
100.973
33.574
1.00
18.49
8


5150
CB
GLU
A
663
8.001
99.880
31.232
1.00
22.54
6


5151
CG
GLU
A
663
9.065
99.526
30.195
1.00
23.03
6


5152
CD
GLU
A
663
8.380
98.560
29.223
1.00
19.52
6


5153
OE1
GLU
A
663
8.159
97.397
29.619
1.00
17.12
8


5154
OE2
GLU
A
663
8.063
98.990
28.102
1.00
18.01
8


5155
N
ASN
A
664
6.892
102.576
32.027
1.00
18.62
7


5156
CA
ASN
A
664
5.604
103.189
32.365
1.00
18.27
6


5157
C
ASN
A
664
4.522
102.581
31.484
1.00
20.85
6


5158
O
ASN
A
664
4.782
101.671
30.702
1.00
21.34
8


5159
CB
ASN
A
664
5.790
104.696
32.115
1.00
22.20
6


5160
CG
ASN
A
664
6.447
105.326
33.350
1.00
30.00
6


5161
OD1
ASN
A
664
6.281
104.932
34.519
1.00
35.11
8


5162
ND2
ASN
A
664
7.238
106.366
33.127
1.00
33.46
7


5163
N
GLY
A
665
3.295
103.085
31.667
1.00
22.07
7


5164
CA
GLY
A
665
2.187
102.708
30.786
1.00
23.10
6


5165
C
GLY
A
665
1.557
101.363
31.102
1.00
21.34
6


5166
O
GLY
A
665
1.827
100.710
32.119
1.00
22.70
8


5167
N
SER
A
666
0.832
100.839
30.093
1.00
18.43
7


5168
CA
SER
A
666
0.135
99.581
30.305
1.00
17.79
6


5169
C
SER
A
666
1.084
98.403
30.046
1.00
16.94
6


5170
O
SER
A
666
2.005
98.503
29.261
1.00
16.68
8


5171
CB
SER
A
666
−1.037
99.440
29.297
1.00
24.19
6


5172
OG
SER
A
666
−1.959
100.498
29.645
1.00
24.86
8


5173
N
ASN
A
667
0.642
97.227
30.470
1.00
14.27
7


5174
CA
ASN
A
667
1.491
96.058
30.168
1.00
16.75
6


5175
C
ASN
A
667
1.575
95.824
28.678
1.00
17.00
6


5176
O
ASN
A
667
0.616
96.050
27.899
1.00
15.91
8


5177
CB
ASN
A
667
0.795
94.804
30.736
1.00
16.66
6


5178
CG
ASN
A
667
0.703
94.817
32.248
1.00
19.33
6


5179
OD1
ASN
A
667
−0.178
94.105
32.855
1.00
20.96
8


5180
ND2
ASN
A
667
1.594
95.513
32.887
1.00
16.21
7


5181
N
HIS
A
668
2.720
95.243
28.272
1.00
13.63
7


5182
CA
HIS
A
668
2.882
94.747
26.930
1.00
15.66
6


5183
C
HIS
A
668
2.137
93.408
26.856
1.00
16.10
6


5184
O
HIS
A
668
2.048
92.666
27.847
1.00
16.87
8


5185
CB
HIS
A
668
4.327
94.431
26.491
1.00
15.51
6


5186
CG
HIS
A
668
5.208
95.653
26.519
1.00
14.13
6


5187
ND1
HIS
A
668
5.229
96.451
25.375
1.00
15.75
7


5188
CD2
HIS
A
668
6.066
96.158
27.410
1.00
17.00
6


5189
CE1
HIS
A
668
6.108
97.464
25.592
1.00
14.21
6


5190
NE2
HIS
A
668
6.581
97.305
26.830
1.00
15.51
7


5191
N
VAL
A
669
1.434
93.208
25.734
1.00
15.02
7


5192
CA
VAL
A
669
0.684
91.987
25.490
1.00
16.94
6


5193
C
VAL
A
669
1.205
91.294
24.260
1.00
14.25
6


5194
O
VAL
A
669
1.414
91.936
23.206
1.00
17.08
8


5195
CB
VAL
A
669
−0.852
92.295
25.322
1.00
17.60
6


5196
CG1
VAL
A
669
−1.624
90.970
25.253
1.00
20.63
6


5197
CG2
VAL
A
669
−1.341
93.078
26.547
1.00
17.53
6


5198
N
ALA
A
670
1.450
89.971
24.287
1.00
14.50
7


5199
CA
ALA
A
670
1.945
89.249
23.113
1.00
14.21
6


5200
C
ALA
A
670
1.437
87.798
23.234
1.00
15.38
6


5201
O
ALA
A
670
1.216
87.262
24.323
1.00
15.04
8


5202
CB
ALA
A
670
3.481
89.251
23.005
1.00
14.71
6


5203
N
THR
A
671
1.412
87.143
22.093
1.00
15.66
7


5204
CA
THR
A
671
1.145
85.704
22.056
1.00
15.06
6


5205
C
THR
A
671
2.463
85.017
21.737
1.00
15.13
6


5206
O
THR
A
671
3.141
85.293
20.734
1.00
16.78
8


5207
CB
THR
A
671
0.004
85.374
21.082
1.00
24.32
6


5208
OG1
THR
A
671
−1.181
86.041
21.584
1.00
19.33
8


5209
CG2
THR
A
671
−0.323
83.900
21.063
1.00
22.47
6


5210
N
THR
A
672
2.794
83.967
22.533
1.00
13.36
7


5211
CA
THR
A
672
4.035
83.264
22.249
1.00
14.54
6


5212
C
THR
A
672
3.911
82.312
21.096
1.00
14.80
6


5213
O
THR
A
672
2.831
81.798
20.772
1.00
13.92
8


5214
CB
THR
A
672
4.475
82.464
23.491
1.00
15.06
6


5215
OG1
THR
A
672
3.485
81.497
23.805
1.00
13.92
8


5216
CG2
THR
A
672
4.612
83.376
24.726
1.00
15.62
6


5217
N
PRO
A
673
5.068
81.983
20.499
1.00
16.20
7


5218
CA
PRO
A
673
5.116
81.063
19.381
1.00
21.02
6


5219
C
PRO
A
673
4.615
79.690
19.691
1.00
17.09
6


5220
O
PRO
A
673
4.691
79.290
20.893
1.00
16.99
8


5221
CB
PRO
A
673
6.606
80.975
18.937
1.00
22.47
6


5222
CG
PRO
A
673
7.309
81.859
19.872
1.00
22.50
6


5223
CD
PRO
A
673
6.355
82.558
20.857
1.00
20.76
6


5224
N
THR
A
674
4.164
78.885
18.724
1.00
16.36
7


5225
CA
THR
A
674
3.803
77.518
19.033
1.00
16.04
6


5226
C
THR
A
674
4.915
76.516
18.803
1.00
19.50
6


5227
O
THR
A
674
4.834
75.399
19.293
1.00
25.45
8


5228
CB
THR
A
674
2.613
77.053
18.117
1.00
26.38
6


5229
OG1
THR
A
674
2.997
77.353
16.786
1.00
31.27
8


5230
CG2
THR
A
674
1.409
77.936
18.521
1.00
27.63
6


5231
N
GLY
A
675
5.953
76.981
18.114
1.00
19.68
7


5232
CA
GLY
A
675
7.035
76.041
17.829
1.00
18.98
6


5233
C
GLY
A
675
8.164
76.145
18.885
1.00
21.20
6


5234
O
GLY
A
675
7.915
76.654
19.953
1.00
18.10
8


5235
N
ALA
A
676
9.349
75.612
18.560
1.00
14.92
7


5236
CA
ALA
A
676
10.419
75.562
19.578
1.00
12.67
6


5237
C
ALA
A
676
10.845
76.968
19.974
1.00
13.87
6


5238
O
ALA
A
676
11.505
77.096
21.031
1.00
12.93
8


5239
CB
ALA
A
676
11.611
74.771
19.006
1.00
12.85
6


5240
N
THR
A
677
10.860
77.884
19.014
1.00
13.69
7


5241
CA
THR
A
677
11.444
79.189
19.324
1.00
11.81
6


5242
C
THR
A
677
10.615
80.296
18.686
1.00
13.20
6


5243
O
THR
A
677
9.743
80.066
17.834
1.00
14.64
8


5244
CB
THR
A
677
12.847
79.366
18.681
1.00
14.32
6


5245
OG1
THR
A
677
12.712
79.294
17.249
1.00
16.35
8


5246
CG2
THR
A
677
13.851
78.287
19.079
1.00
14.03
6


5247
N
GLY
A
678
10.949
81.490
19.141
1.00
14.25
7


5248
CA
GLY
A
678
10.413
82.685
18.437
1.00
13.38
6


5249
C
GLY
A
678
10.969
83.958
19.066
1.00
13.68
6


5250
O
GLY
A
678
11.857
83.956
19.907
1.00
13.62
8


5251
N
ASN
A
679
10.374
85.094
18.654
1.00
13.18
7


5252
CA
ASN
A
679
10.858
86.398
19.082
1.00
11.86
6


5253
C
ASN
A
679
9.685
87.318
19.466
1.00
14.28
6


5254
O
ASN
A
679
8.718
87.315
18.699
1.00
15.54
8


5255
CB
ASN
A
679
11.485
87.180
17.892
1.00
16.45
6


5256
CG
ASN
A
679
12.952
86.818
17.758
1.00
25.76
6


5257
OD1
ASN
A
679
13.201
85.708
17.294
1.00
24.19
8


5258
ND2
ASN
A
679
13.881
87.684
18.146
1.00
26.44
7


5259
N
ILE
A
680
9.882
88.063
20.521
1.00
13.28
7


5260
CA
ILE
A
680
8.909
89.088
20.948
1.00
14.10
6


5261
C
ILE
A
680
9.758
90.331
21.083
1.00
16.54
6


5262
O
ILE
A
680
10.673
90.366
21.944
1.00
14.10
8


5263
CB
ILE
A
680
8.224
88.676
22.277
1.00
13.96
6


5264
CG1
ILE
A
680
7.245
87.519
21.978
1.00
16.92
6


5265
CG2
ILE
A
680
7.442
89.919
22.790
1.00
17.42
6


5266
CD1
ILE
A
680
6.611
86.867
23.218
1.00
15.15
6


5267
N
THR
A
681
9.363
91.378
20.334
1.00
13.57
7


5268
CA
THR
A
681
10.236
92.583
20.392
1.00
12.91
6


5269
C
THR
A
681
9.280
93.751
20.616
1.00
13.01
6


5270
O
THR
A
681
8.253
93.845
19.929
1.00
18.59
8


5271
CB
THR
A
681
10.904
92.718
18.990
1.00
16.97
6


5272
OG1
THR
A
681
11.807
91.633
18.765
1.00
17.30
8


5273
CG2
THR
A
681
11.642
94.052
18.964
1.00
19.53
6


5274
N
VAL
A
682
9.639
94.595
21.608
1.00
15.51
7


5275
CA
VAL
A
682
8.758
95.732
21.946
1.00
15.78
6


5276
C
VAL
A
682
9.635
96.952
22.186
1.00
17.87
6


5277
O
VAL
A
682
10.838
96.797
22.256
1.00
15.49
8


5278
CB
VAL
A
682
7.874
95.472
23.195
1.00
16.15
6


5279
CG1
VAL
A
682
6.968
94.243
23.002
1.00
16.76
6


5280
CG2
VAL
A
682
8.730
95.365
24.469
1.00
16.17
6


5281
N
THR
A
683
9.082
98.162
22.306
1.00
15.89
7


5282
CA
THR
A
683
9.863
99.346
22.623
1.00
15.51
6


5283
C
THR
A
683
9.529
99.798
24.046
1.00
16.36
6


5284
O
THR
A
683
8.371
99.703
24.462
1.00
17.59
8


5285
CB
THR
A
683
9.481
100.473
21.614
1.00
22.31
6


5286
OG1
THR
A
683
9.916
100.019
20.328
1.00
21.22
8


5287
CG2
THR
A
683
10.245
101.759
21.921
1.00
19.31
6


5288
N
TRP
A
684
10.586
100.168
24.759
1.00
14.24
7


5289
CA
TRP
A
684
10.411
100.587
26.154
1.00
14.76
6


5290
C
TRP
A
684
9.369
101.706
26.222
1.00
17.75
6


5291
O
TRP
A
684
9.556
102.695
25.469
1.00
18.74
8


5292
CB
TRP
A
684
11.745
101.086
26.705
1.00
14.95
6


5293
CG
TRP
A
684
11.696
101.465
28.146
1.00
14.49
6


5294
CD1
TRP
A
684
11.284
102.666
28.672
1.00
15.39
6


5295
CD2
TRP
A
684
12.163
100.683
29.271
1.00
17.84
6


5296
NE1
TRP
A
684
11.376
102.649
30.052
1.00
16.11
7


5297
CE2
TRP
A
684
11.921
101.440
30.423
1.00
20.66
6


5298
CE3
TRP
A
684
12.764
99.422
29.399
1.00
18.28
6


5299
CZ2
TRP
A
684
12.245
101.024
31.726
1.00
22.23
6


5300
CZ3
TRP
A
684
13.074
98.959
30.709
1.00
17.05
6


5301
CH2
TRP
A
684
12.791
99.766
31.796
1.00
17.97
6


5302
N
GLN
A
685
8.396
101.650
27.102
1.00
17.70
7


5303
CA
GLN
A
685
7.399
102.716
27.315
1.00
18.97
6


5304
C
GLN
A
685
7.850
103.719
28.333
1.00
19.08
6


5305
O
GLN
A
685
8.067
103.430
29.512
1.00
19.01
8


5306
CB
GLN
A
685
6.071
102.025
27.745
1.00
15.69
6


5307
CG
GLN
A
685
5.536
101.157
26.596
1.00
17.89
6


5308
CD
GLN
A
685
4.352
100.283
26.995
1.00
18.78
6


5309
OE1
GLN
A
685
3.797
99.604
26.110
1.00
20.58
8


5310
NE2
GLN
A
685
3.960
100.246
28.267
1.00
17.75
7


5311
N
ASN
A
686
8.037
105.011
27.906
1.00
21.27
7


5312
CA
ASN
A
686
8.547
106.008
28.836
1.00
20.38
6


5313
C
ASN
A
686
7.489
106.854
29.654
1.00
22.87
6


5314
O
ASN
A
686
6.387
106.692
29.016
1.00
22.87
8


5315
CB
ASN
A
686
9.300
107.060
27.975
1.00
24.12
6


5316
CG
ASN
A
686
10.434
106.404
27.176
1.00
23.38
6


5317
OD1
ASN
A
686
11.360
105.896
27.821
1.00
22.76
8


5318
ND2
ASN
A
686
10.376
106.412
25.832
1.00
25.47
7


5319
C11
HEX
A
690
38.644
78.012
38.228
1.00
27.46
6


5320
O11
HEX
A
690
39.147
78.243
39.503
1.00
37.24
8


5321
C12
HEX
A
690
37.596
79.172
38.058
1.00
23.95
6


5322
O12
HEX
A
690
36.681
78.887
39.109
1.00
20.96
8


5323
C13
HEX
A
690
36.915
78.887
36.685
1.00
17.64
6


5324
O13
HEX
A
690
35.915
79.908
36.442
1.00
18.04
8


5325
C14
HEX
A
690
38.048
79.023
35.670
1.00
17.74
6


5326
C15
HEX
A
690
39.141
77.967
35.956
1.00
19.52
6


5327
O15
HEX
A
690
39.679
78.312
37.276
1.00
26.20
8


5328
C16
HEX
A
690
40.338
77.919
35.016
1.00
23.71
6


5329
O16
HEX
A
690
40.867
79.240
34.817
1.00
28.38
8


5330
C21
HEX
A
690
37.609
79.324
33.250
1.00
19.03
6


5331
O21
HEX
A
690
37.414
78.562
34.414
1.00
18.39
8


5332
C22
HEX
A
690
36.237
79.756
32.692
1.00
18.97
6


5333
O22
HEX
A
690
35.419
80.404
33.669
1.00
17.96
8


5334
C23
HEX
A
690
35.514
78.516
32.153
1.00
16.72
6


5335
O23
HEX
A
690
34.355
79.014
31.406
1.00
16.31
8


5336
C24
HEX
A
690
36.415
77.760
31.174
1.00
12.77
6


5337
C25
HEX
A
690
37.690
77.301
31.955
1.00
17.32
6


5338
O25
HEX
A
690
38.321
78.596
32.286
1.00
20.72
8


5339
C26
HEX
A
690
38.704
76.681
30.979
1.00
18.94
6


5340
O26
HEX
A
690
39.852
76.182
31.780
1.00
21.07
8


5341
C31
HEX
A
690
35.507
76.403
29.409
1.00
11.28
6


5342
O31
HEX
A
690
35.723
76.501
30.811
1.00
12.85
8


5343
C32
HEX
A
690
34.026
76.118
29.118
1.00
13.04
6


5344
O32
HEX
A
690
33.259
77.030
29.933
1.00
14.06
8


5345
C33
HEX
A
690
33.654
74.698
29.626
1.00
13.59
6


5346
O33
HEX
A
690
32.285
74.486
29.158
1.00
12.48
8


5347
C34
HEX
A
690
34.578
73.670
28.936
1.00
11.83
6


5348
C35
HEX
A
690
36.004
74.036
29.487
1.00
14.01
6


5349
O35
HEX
A
690
36.301
75.341
28.930
1.00
12.70
8


5350
C36
HEX
A
690
37.084
73.167
28.829
1.00
13.71
6


5351
C41
HEX
A
690
33.322
71.601
28.292
1.00
9.18
6


5352
N41
HEX
A
690
34.214
72.300
29.267
1.00
10.73
7


5353
C42
HEX
A
690
33.682
70.074
28.156
1.00
11.48
6


5354
O42
HEX
A
690
33.732
69.433
29.448
1.00
10.30
8


5355
C43
HEX
A
690
35.023
69.963
27.455
1.00
10.39
6


5356
O43
HEX
A
690
35.686
68.699
27.591
1.00
11.44
8


5357
C44
HEX
A
690
34.791
70.257
25.986
1.00
11.02
6


5358
C45
HEX
A
690
33.925
71.520
25.899
1.00
10.58
6


5359
C40
HEX
A
690
33.262
72.097
26.944
1.00
9.08
6


5360
C46
HEX
A
690
33.519
71.887
24.466
1.00
12.28
6


5361
O46
HEX
A
690
32.492
71.022
24.020
1.00
12.58
8


5362
C51
HEX
A
690
36.288
69.864
24.116
1.00
10.88
6


5363
O51
HEX
A
690
36.061
70.541
25.327
1.00
12.10
8


5364
C52
HEX
A
690
37.495
68.906
24.274
1.00
11.69
6


5365
O52
HEX
A
690
37.227
67.917
25.285
1.00
12.57
8


5366
C53
HEX
A
690
38.717
69.698
24.774
1.00
10.51
6


5367
O53
HEX
A
690
39.832
68.756
24.609
1.00
11.97
8


5368
C54
HEX
A
690
39.025
70.807
23.714
1.00
12.82
6


5369
C55
HEX
A
690
37.748
71.660
23.566
1.00
12.56
6


5370
O55
HEX
A
690
36.680
70.820
23.133
1.00
11.57
8


5371
C56
HEX
A
690
37.890
72.687
22.436
1.00
12.61
6


5372
O56
HEX
A
690
38.082
72.074
21.134
1.00
19.74
8


5373
C61
HEX
A
690
40.720
72.590
24.188
1.00
22.95
6


5374
O61
HEX
A
690
39.890
71.572
24.637
1.00
20.26
8


5375
C62
HEX
A
690
42.050
72.500
24.991
1.00
23.13
6


5376
O62
HEX
A
690
42.582
71.189
24.918
1.00
23.06
8


5377
C63
HEX
A
690
41.937
73.006
26.411
1.00
24.03
6


5378
O63
HEX
A
690
43.280
72.994
26.932
1.00
28.78
8


5379
C64
HEX
A
690
41.310
74.405
26.428
1.00
25.79
6


5380
O64
HEX
A
690
41.035
74.789
27.809
1.00
29.96
8


5381
C65
HEX
A
690
39.918
74.255
25.759
1.00
22.19
6


5382
O65
HEX
A
690
40.146
73.866
24.404
1.00
22.47
8


5383
C66
HEX
A
690
39.177
75.555
25.611
1.00
26.12
6


5384
O66
HEX
A
690
39.936
76.644
25.149
1.00
24.41
8


5385
C11
MAL
A
691
38.534
71.299
69.464
1.00
19.75
6


5386
O11
MAL
A
691
38.776
72.581
69.883
1.00
20.21
8


5387
C12
MAL
A
691
37.973
71.384
68.024
1.00
17.66
6


5388
O12
MAL
A
691
38.798
72.262
67.225
1.00
18.71
8


5389
C13
MAL
A
691
36.555
71.949
68.006
1.00
16.03
6


5390
O13
MAL
A
691
35.969
71.754
66.689
1.00
17.47
8


5391
C14
MAL
A
691
35.642
71.104
68.925
1.00
15.64
6


5392
C15
MAL
A
691
36.269
71.291
70.364
1.00
14.01
6


5393
O15
MAL
A
691
37.561
70.667
70.312
1.00
16.48
8


5394
C16
MAL
A
691
35.519
70.221
71.238
1.00
19.77
6


5395
O16
MAL
A
691
36.004
70.431
72.581
1.00
18.54
8


5396
C21
MAL
A
691
33.285
70.813
68.523
1.00
18.83
6


5397
O21
MAL
A
691
34.336
71.683
68.968
1.00
17.92
8


5398
C22
MAL
A
691
32.403
71.638
67.561
1.00
17.24
6


5399
O22
MAL
A
691
33.177
72.083
66.433
1.00
17.89
8


5400
C23
MAL
A
691
31.765
72.820
68.304
1.00
18.41
6


5401
O23
MAL
A
691
30.812
73.419
67.431
1.00
18.30
8


5402
C24
MAL
A
691
30.951
72.194
69.478
1.00
18.57
6


5403
O24
MAL
A
691
30.444
73.291
70.263
1.00
19.15
8


5404
C25
MAL
A
691
31.923
71.424
70.383
1.00
19.32
6


5405
O25
MAL
A
691
32.521
70.374
69.608
1.00
18.98
8


5406
C26
MAL
A
691
31.067
70.708
71.468
1.00
15.38
6


5407
O26
MAL
A
691
31.944
70.075
72.412
1.00
18.74
8


5411
S
SUL
A
695
11.120
52.018
55.465
1.00
30.54
16


5412
O1
SUL
A
695
11.470
52.936
56.533
1.00
30.07
8


5413
O2
SUL
A
695
10.034
52.528
54.544
1.00
27.19
8


5414
O3
SUL
A
695
12.310
51.631
54.662
1.00
34.25
8


5415
O4
SUL
A
695
10.566
50.749
56.089
1.00
33.96
8


5451
CA
WAT
A
692
32.693
60.307
13.017
1.00
11.99
20


5452
CA
WAT
A
693
26.975
79.502
21.970
1.00
10.73
20


5453
CA
WAT
A
694
37.244
49.841
19.039
1.00
13.50
20


5454
OW0
WAT
V
1
24.447
79.971
21.858
1.00
9.43
8


5455
OW0
WAT
V
2
35.686
59.385
24.028
1.00
10.45
8


5456
OW0
WAT
V
3
33.934
60.773
18.648
1.00
10.63
8


5457
OW0
WAT
V
4
35.622
62.751
41.495
1.00
10.88
8


5458
OW0
WAT
V
5
25.780
77.914
20.486
1.00
10.75
8


5459
OW0
WAT
V
6
21.776
77.285
28.879
1.00
10.81
8


5460
OW0
WAT
V
7
29.415
69.145
19.400
1.00
10.86
8


5461
OW0
WAT
V
8
29.138
80.312
22.631
1.00
10.86
8


5462
OW0
WAT
V
9
27.613
72.037
24.448
1.00
10.77
8


5463
OW0
WAT
V
10
31.164
77.784
19.615
1.00
10.85
8


5464
OW0
WAT
V
11
32.790
66.917
36.378
1.00
10.94
8


5465
OW0
WAT
V
12
34.127
70.240
32.929
1.00
11.18
8


5466
OW0
WAT
V
13
33.080
60.581
23.767
1.00
11.11
8


5467
OW0
WAT
V
14
37.235
54.601
19.600
1.00
11.38
8


5468
OW0
WAT
V
15
26.119
65.542
21.574
1.00
11.07
8


5469
OW0
WAT
V
16
28.484
64.486
20.522
1.00
11.49
8


5470
OW0
WAT
V
17
28.194
73.536
36.853
1.00
11.53
8


5471
OW0
WAT
V
18
16.618
66.275
36.806
1.00
11.68
8


5472
OW0
WAT
V
19
26.088
62.658
22.854
1.00
11.54
8


5473
OW0
WAT
V
20
37.981
63.919
14.127
1.00
11.77
8


5474
OW0
WAT
V
21
34.932
60.656
13.769
1.00
11.70
8


5475
OW0
WAT
V
22
41.499
60.656
38.722
1.00
11.54
8


5476
OW0
WAT
V
23
40.945
66.711
20.205
1.00
11.65
8


5477
OW0
WAT
V
24
8.905
64.107
34.370
1.00
11.68
8


5478
OW0
WAT
V
25
19.426
72.356
40.893
1.00
11.74
8


5479
OW0
WAT
V
26
20.321
82.331
35.376
1.00
11.77
8


5480
OW0
WAT
V
27
14.993
64.250
37.502
1.00
11.91
8


5481
OW0
WAT
V
28
31.504
68.673
10.842
1.00
12.08
8


5482
OW0
WAT
V
29
37.606
61.402
40.167
1.00
11.91
8


5483
OW0
WAT
V
30
16.372
70.863
38.933
1.00
11.99
8


5484
OW0
WAT
V
31
7.950
69.079
31.258
1.00
12.08
8


5485
OW0
WAT
V
32
19.528
73.999
43.164
1.00
12.10
8


5486
OW0
WAT
V
33
16.210
66.954
39.606
1.00
12.02
8


5487
OW0
WAT
V
34
32.679
63.267
29.330
1.00
12.26
8


5488
OW0
WAT
V
35
13.649
74.479
39.683
1.00
12.21
8


5489
OW0
WAT
V
36
16.357
79.631
22.013
1.00
12.26
8


5490
OW0
WAT
V
37
21.471
63.888
43.225
1.00
12.25
8


5491
OW0
WAT
V
38
42.464
66.587
23.881
1.00
12.49
8


5492
OW0
WAT
V
39
31.355
60.893
19.838
1.00
12.31
8


5493
OW0
WAT
V
40
16.930
64.546
40.981
1.00
12.36
8


5494
OW0
WAT
V
41
10.918
81.011
32.425
1.00
12.42
8


5495
OW0
WAT
V
42
8.358
78.559
35.685
1.00
12.49
8


5496
OW0
WAT
V
43
22.052
71.621
41.190
1.00
12.24
8


5497
OW0
WAT
V
44
8.226
66.640
35.276
1.00
12.62
8


5498
OW0
WAT
V
45
6.031
77.562
36.868
1.00
12.35
8


5499
OW0
WAT
V
46
43.919
60.734
40.175
1.00
12.51
8


5500
OW0
WAT
V
48
11.578
73.478
41.191
1.00
12.62
8


5501
OW0
WAT
V
49
35.256
52.308
26.203
1.00
12.50
8


5502
OW0
WAT
V
50
22.628
81.739
22.782
1.00
12.52
8


5503
OW0
WAT
V
51
41.171
68.357
22.292
1.00
12.78
8


5504
OW0
WAT
V
52
34.554
71.110
10.783
1.00
12.58
8


5505
OW0
WAT
V
53
39.554
70.543
28.407
1.00
12.73
8


5506
OW0
WAT
V
54
14.970
66.671
43.779
1.00
12.94
8


5507
OW0
WAT
V
55
14.792
81.581
20.763
1.00
12.92
8


5508
OW0
WAT
V
56
30.205
75.643
31.109
1.00
12.90
8


5509
OW0
WAT
V
57
16.697
82.536
30.534
1.00
13.09
8


5510
OW0
WAT
V
58
38.776
53.289
57.732
1.00
13.10
8


5511
OW0
WAT
V
59
31.565
49.273
20.064
1.00
13.22
8


5512
OW0
WAT
V
60
20.200
85.147
36.037
1.00
13.29
8


5513
OW0
WAT
V
61
25.657
54.513
45.949
1.00
13.32
8


5514
OW0
WAT
V
62
37.048
52.273
18.284
1.00
13.46
8


5515
OW0
WAT
V
63
30.032
67.305
53.938
1.00
13.27
8


5516
OW0
WAT
V
64
32.331
68.357
33.829
1.00
13.58
8


5517
OW0
WAT
V
65
23.329
85.511
30.252
1.00
13.33
8


5518
OW0
WAT
V
66
20.246
61.387
18.981
1.00
13.61
8


5519
OW0
WAT
V
67
28.775
74.856
40.336
1.00
13.65
8


5520
OW0
WAT
V
68
32.567
68.924
43.607
1.00
13.35
8


5521
OW0
WAT
V
69
10.838
68.713
42.880
1.00
13.33
8


5522
OW0
WAT
V
70
12.859
61.518
43.606
1.00
13.90
8


5523
OW0
WAT
V
71
45.207
60.214
32.334
1.00
13.77
8


5524
OW0
WAT
V
72
27.427
66.987
53.108
1.00
13.75
8


5525
OW0
WAT
V
73
19.074
63.276
42.264
1.00
13.66
8


5526
OW0
WAT
V
74
36.934
75.592
8.270
1.00
13.53
8


5527
OW0
WAT
V
75
27.574
81.410
6.013
1.00
14.19
8


5528
OW0
WAT
V
76
30.621
83.670
31.215
1.00
14.28
8


5529
OW0
WAT
V
77
42.514
70.356
20.822
1.00
14.45
8


5530
OW0
WAT
V
78
12.529
75.168
22.815
1.00
14.52
8


5531
OW0
WAT
V
79
39.891
56.461
11.992
1.00
14.18
8


5532
OW0
WAT
V
80
30.677
68.114
68.620
1.00
14.47
8


5533
OW0
WAT
V
81
33.218
64.224
36.711
1.00
14.46
8


5534
OW0
WAT
V
82
12.035
74.811
37.533
1.00
14.63
8


5535
OW0
WAT
V
83
15.981
73.538
38.669
1.00
14.16
8


5536
OW0
WAT
V
84
10.686
81.113
35.947
1.00
14.90
8


5537
OW0
WAT
V
85
25.562
71.871
51.287
1.00
14.81
8


5538
OW0
WAT
V
86
29.447
83.564
16.644
1.00
14.86
8


5539
OW0
WAT
V
87
13.480
81.300
31.112
1.00
14.85
8


5540
OW0
WAT
V
88
5.774
80.076
41.775
1.00
14.92
8


5541
OW0
WAT
V
89
47.914
63.828
68.644
1.00
14.87
8


5542
OW0
WAT
V
90
34.743
77.662
45.101
1.00
15.02
8


5543
OW0
WAT
V
91
24.427
76.387
7.359
1.00
15.03
8


5544
OW0
WAT
V
92
−2.703
63.471
38.845
1.00
15.46
8


5545
OW0
WAT
V
93
14.681
69.092
37.625
1.00
15.14
8


5546
OW0
WAT
V
94
28.123
74.474
42.954
1.00
15.12
8


5547
OW0
WAT
V
95
23.589
80.407
29.737
1.00
15.19
8


5548
OW0
WAT
V
96
28.941
64.658
47.281
1.00
15.32
8


5549
OW0
WAT
V
97
33.848
82.923
7.441
1.00
15.09
8


5550
OW0
WAT
V
98
50.687
59.709
65.034
1.00
15.32
8


5551
OW0
WAT
V
99
29.977
80.264
14.804
1.00
15.36
8


5552
OW0
WAT
V
100
25.916
52.607
44.011
1.00
15.58
8


5553
OW0
WAT
V
101
6.765
62.176
32.083
1.00
15.56
8


5554
OW0
WAT
V
102
13.107
89.810
20.076
1.00
15.94
8


5555
OW0
WAT
V
103
11.601
78.292
36.745
1.00
15.75
8


5556
OW0
WAT
V
104
14.144
58.009
41.510
1.00
15.84
8


5557
OW0
WAT
V
105
44.010
71.623
35.990
1.00
15.89
8


5558
OW0
WAT
V
106
21.168
82.474
32.738
1.00
16.12
8


5559
OW0
WAT
V
107
28.667
48.688
46.155
1.00
16.35
8


5560
OW0
WAT
V
108
25.610
86.818
38.209
1.00
16.18
8


5561
OW0
WAT
V
109
29.070
89.992
31.492
1.00
16.47
8


5562
OW0
WAT
V
110
1.291
75.000
41.091
1.00
16.32
8


5563
OW0
WAT
V
111
34.624
56.600
71.328
1.00
16.34
8


5564
OW0
WAT
V
112
28.281
69.481
68.152
1.00
16.52
8


5565
OW0
WAT
V
113
26.135
87.038
35.304
1.00
16.58
8


5566
OW0
WAT
V
114
35.168
78.123
51.153
1.00
16.64
8


5567
OW0
WAT
V
115
19.827
81.281
46.203
1.00
16.48
8


5568
OW0
WAT
V
116
30.082
84.087
8.323
1.00
16.75
8


5569
OW0
WAT
V
117
45.164
71.238
15.992
1.00
16.58
8


5570
OW0
WAT
V
118
−2.555
86.829
29.585
1.00
16.73
8


5571
OW0
WAT
V
119
1.879
75.860
26.297
1.00
16.96
8


5572
OW0
WAT
V
120
20.960
94.415
22.713
1.00
16.87
8


5573
OW0
WAT
V
121
12.300
72.626
21.951
1.00
16.94
8


5574
OW0
WAT
V
122
21.720
86.954
37.648
1.00
17.08
8


5575
OW0
WAT
V
123
17.342
46.052
29.967
1.00
16.89
8


5576
OW0
WAT
V
124
15.847
84.337
34.562
1.00
16.74
8


5577
OW0
WAT
V
125
−3.241
60.294
45.682
1.00
16.67
8


5578
OW0
WAT
V
126
11.587
104.148
24.323
1.00
17.24
8


5579
OW0
WAT
V
127
28.501
56.852
51.441
1.00
17.40
8


5580
OW0
WAT
V
128
14.206
82.937
18.392
1.00
17.21
8


5581
OW0
WAT
V
129
41.516
56.407
63.525
1.00
17.22
8


5582
OW0
WAT
V
130
36.936
73.986
40.016
1.00
17.65
8


5583
OW0
WAT
V
131
20.790
40.115
27.752
1.00
17.53
8


5584
OW0
WAT
V
132
45.240
52.146
20.212
1.00
17.55
8


5585
OW0
WAT
V
133
41.799
49.726
28.892
1.00
17.29
8


5586
OW0
WAT
V
134
23.108
66.755
60.083
1.00
17.41
8


5587
OW0
WAT
V
135
26.863
48.805
41.435
1.00
17.67
8


5588
OW0
WAT
V
136
27.488
90.699
28.339
1.00
17.76
8


5589
OW0
WAT
V
137
0.191
69.111
49.096
1.00
17.78
8


5590
OW0
WAT
V
138
34.447
43.232
33.946
1.00
17.85
8


5591
OW0
WAT
V
139
22.589
64.044
49.415
1.00
18.18
8


5592
OW0
WAT
V
140
17.697
81.339
35.462
1.00
17.98
8


5593
OW0
WAT
V
141
2.444
96.838
37.934
1.00
18.09
8


5594
OW0
WAT
V
142
35.347
81.251
39.545
1.00
17.94
8


5595
OW0
WAT
V
143
14.511
56.297
49.652
1.00
18.35
8


5596
OW0
WAT
V
144
10.014
71.654
20.618
1.00
18.11
8


5597
OW0
WAT
V
145
47.629
63.815
18.991
1.00
18.25
8


5598
OW0
WAT
V
146
15.832
79.962
31.635
1.00
18.52
8


5599
OW0
WAT
V
147
35.482
76.428
39.594
1.00
18.64
8


5600
OW0
WAT
V
149
16.532
67.334
48.159
1.00
18.61
8


5601
OW0
WAT
V
150
32.280
83.173
33.550
1.00
18.44
8


5602
OW0
WAT
V
151
35.037
62.885
71.628
1.00
18.62
8


5603
OW0
WAT
V
152
14.756
56.448
28.743
1.00
18.87
8


5604
OW0
WAT
V
153
51.007
64.138
32.515
1.00
18.45
8


5605
OW0
WAT
V
154
44.683
55.406
52.749
1.00
18.86
8


5606
OW0
WAT
V
155
30.803
47.286
18.413
1.00
19.00
8


5607
OW0
WAT
V
156
21.419
87.008
31.586
1.00
18.86
8


5608
OW0
WAT
V
157
27.471
54.562
13.822
1.00
18.93
8


5609
OW0
WAT
V
158
19.938
85.031
32.888
1.00
18.77
8


5610
OW0
WAT
V
160
23.159
58.927
72.012
1.00
19.01
8


5611
OW0
WAT
V
161
20.470
84.773
18.243
1.00
19.09
8


5612
OW0
WAT
V
162
15.077
66.831
13.792
1.00
18.88
8


5613
OW0
WAT
V
164
34.016
76.548
58.886
1.00
19.18
8


5614
OW0
WAT
V
165
1.791
96.077
35.490
1.00
19.39
8


5615
OW0
WAT
V
168
16.921
65.681
50.173
1.00
19.74
8


5616
OW0
WAT
V
169
36.015
49.508
63.823
1.00
19.75
8


5617
OW0
WAT
V
170
19.146
93.639
20.716
1.00
19.72
8


5618
OW0
WAT
V
171
41.081
74.262
43.114
1.00
19.99
8


5619
OW0
WAT
V
172
27.356
86.834
41.150
1.00
19.86
8


5620
OW0
WAT
V
173
32.541
61.241
6.239
1.00
19.49
8


5621
OW0
WAT
V
174
51.971
65.011
17.317
1.00
20.07
8


5622
OW0
WAT
V
175
36.754
79.161
49.332
1.00
19.96
8


5623
OW0
WAT
V
176
21.529
68.516
52.600
1.00
19.88
8


5624
OW0
WAT
V
177
52.175
64.476
48.627
1.00
19.48
8


5625
OW0
WAT
V
178
47.687
55.894
28.556
1.00
19.85
8


5626
OW0
WAT
V
180
28.309
57.733
12.302
1.00
19.86
8


5627
OW0
WAT
V
181
19.852
88.585
39.017
1.00
20.03
8


5628
OW0
WAT
V
182
48.116
65.053
11.253
1.00
19.75
8


5629
OW0
WAT
V
183
45.728
49.401
46.755
1.00
20.07
8


5630
OW0
WAT
V
184
23.090
51.403
56.173
1.00
19.76
8


5631
OW0
WAT
V
185
23.972
69.604
53.226
1.00
20.10
8


5632
OW0
WAT
V
186
49.679
65.500
55.245
1.00
19.98
8


5633
OW0
WAT
V
187
50.720
57.388
48.688
1.00
20.39
8


5634
OW0
WAT
V
188
34.857
63.152
38.228
1.00
20.23
8


5635
OW0
WAT
V
189
37.511
43.029
19.233
1.00
20.32
8


5636
OW0
WAT
V
190
50.567
67.974
10.449
1.00
20.64
8


5637
OW0
WAT
V
191
29.875
92.014
24.922
1.00
20.34
8


5638
OW0
WAT
V
192
4.055
100.811
36.567
1.00
20.35
8


5639
OW0
WAT
V
194
23.592
87.859
32.780
1.00
20.02
8


5640
OW0
WAT
V
195
43.898
69.204
9.296
1.00
20.35
8


5641
OW0
WAT
V
196
17.503
91.553
19.944
1.00
20.36
8


5642
OW0
WAT
V
197
22.079
71.014
56.203
1.00
20.50
8


5643
OW0
WAT
V
198
24.611
90.278
32.659
1.00
20.71
8


5644
OW0
WAT
V
199
15.822
79.667
34.285
1.00
20.71
8


5645
OW0
WAT
V
200
41.507
64.519
35.769
1.00
20.47
8


5646
OW0
WAT
V
201
50.582
63.510
21.444
1.00
20.44
8


5647
OW0
WAT
V
202
−4.254
88.781
28.481
1.00
20.69
8


5648
OW0
WAT
V
203
41.289
48.120
25.349
1.00
20.50
8


5649
OW0
WAT
V
204
33.838
47.522
55.491
1.00
20.42
8


5650
OW0
WAT
V
205
28.696
42.611
30.481
1.00
21.10
8


5651
OW0
WAT
V
206
29.680
89.479
34.207
1.00
20.71
8


5652
OW0
WAT
V
207
13.375
82.989
38.528
1.00
20.79
8


5653
OW0
WAT
V
208
−0.381
94.652
35.925
1.00
20.71
8


5654
OW0
WAT
V
209
32.894
53.249
7.401
1.00
20.79
8


5655
OW0
WAT
V
210
47.202
71.009
63.961
1.00
20.83
8


5656
OW0
WAT
V
211
16.432
73.589
49.935
1.00
20.64
8


5657
OW0
WAT
V
212
36.761
42.123
23.718
1.00
20.49
8


5658
OW0
WAT
V
213
1.326
98.176
25.977
1.00
21.14
8


5659
OW0
WAT
V
215
32.369
84.143
13.694
1.00
21.27
8


5660
OW0
WAT
V
216
1.000
72.006
27.168
1.00
21.23
8


5661
OW0
WAT
V
217
21.907
50.669
62.000
1.00
21.19
8


5662
OW0
WAT
V
218
30.956
41.738
21.314
1.00
21.03
8


5663
OW0
WAT
V
219
36.121
71.463
4.684
1.00
21.46
8


5664
OW0
WAT
V
220
13.404
81.016
34.970
1.00
21.65
8


5665
OW0
WAT
V
221
22.957
65.844
62.604
1.00
21.35
8


5666
OW0
WAT
V
222
4.260
99.337
39.649
1.00
21.63
8


5667
OW0
WAT
V
223
17.535
84.263
32.555
1.00
20.98
8


5668
OW0
WAT
V
224
16.496
59.065
45.746
1.00
21.66
8


5669
OW0
WAT
V
225
16.576
52.574
34.164
1.00
21.65
8


5670
OW0
WAT
V
226
30.825
51.406
13.432
1.00
21.28
8


5671
OW0
WAT
V
227
39.177
82.848
23.121
1.00
21.63
8


5672
OW0
WAT
V
229
19.108
58.790
36.143
1.00
21.40
8


5673
OW0
WAT
V
230
19.087
75.378
50.063
1.00
21.22
8


5674
OW0
WAT
V
231
47.413
69.881
16.583
1.00
21.29
8


5675
OW0
WAT
V
232
26.686
91.040
31.058
1.00
21.61
8


5676
OW0
WAT
V
233
29.036
52.089
61.852
1.00
21.25
8


5677
OW0
WAT
V
234
36.187
79.293
46.671
1.00
21.45
8


5678
OW0
WAT
V
235
37.289
74.835
65.582
1.00
21.65
8


5679
OW0
WAT
V
236
−0.428
68.770
30.109
1.00
21.94
8


5680
OW0
WAT
V
237
50.762
57.829
44.061
1.00
22.15
8


5681
OW0
WAT
V
238
45.167
70.565
24.893
1.00
22.00
8


5682
OW0
WAT
V
239
28.609
48.609
51.930
1.00
22.03
8


5683
OW0
WAT
V
241
2.366
94.552
38.603
1.00
21.97
8


5684
OW0
WAT
V
242
9.365
68.970
20.742
1.00
22.04
8


5685
OW0
WAT
V
243
38.583
85.642
29.447
1.00
21.90
8


5686
OW0
WAT
V
244
24.639
49.542
55.081
1.00
22.42
8


5687
OW0
WAT
V
245
18.177
95.474
18.838
1.00
22.69
8


5688
OW0
WAT
V
246
37.307
43.276
33.862
1.00
22.90
8


5689
OW0
WAT
V
247
23.478
86.290
16.425
1.00
21.85
8


5690
OW0
WAT
V
248
43.569
60.466
72.156
1.00
23.10
8


5691
OW0
WAT
V
249
23.281
40.658
26.691
1.00
22.77
8


5692
OW0
WAT
V
250
8.761
65.837
24.376
1.00
23.00
8


5693
OW0
WAT
V
251
27.215
72.803
60.509
1.00
22.60
8


5694
OW0
WAT
V
252
16.174
91.014
44.772
1.00
22.53
8


5695
OW0
WAT
V
253
3.297
98.395
35.969
1.00
23.15
8


5696
OW0
WAT
V
254
10.918
68.974
53.447
1.00
23.22
8


5697
OW0
WAT
V
255
−5.802
66.167
37.375
1.00
23.15
8


5698
OW0
WAT
V
256
8.490
91.603
44.099
1.00
22.65
8


5699
OW0
WAT
V
257
9.234
73.507
16.552
1.00
22.92
8


5700
OW0
WAT
V
258
15.730
56.257
16.556
1.00
23.08
8


5701
OW0
WAT
V
259
19.989
82.268
13.713
1.00
22.90
8


5702
OW0
WAT
V
260
27.613
49.792
60.562
1.00
23.09
8


5703
OW0
WAT
V
261
26.408
61.061
10.006
1.00
23.11
8


5704
OW0
WAT
V
262
14.277
70.834
12.781
1.00
23.32
8


5705
OW0
WAT
V
263
−3.969
72.948
34.601
1.00
22.98
8


5706
OW0
WAT
V
264
−1.028
93.829
38.475
1.00
23.17
8


5707
OW0
WAT
V
265
19.230
101.476
27.805
1.00
22.95
8


5708
OW0
WAT
V
266
17.914
54.281
55.523
1.00
23.31
8


5709
OW0
WAT
V
267
−1.163
64.024
50.895
1.00
23.41
8


5710
OW0
WAT
V
268
16.209
48.607
29.481
1.00
23.45
8


5711
OW0
WAT
V
269
35.070
63.595
75.008
1.00
23.90
8


5712
OW0
WAT
V
270
38.343
43.626
21.918
1.00
23.33
8


5713
OW0
WAT
V
271
32.197
85.153
37.181
1.00
23.49
8


5714
OW0
WAT
V
272
28.789
71.419
66.331
1.00
22.79
8


5715
OW0
WAT
V
273
41.806
79.697
18.591
1.00
23.39
8


5716
OW0
WAT
V
274
38.127
43.105
36.443
1.00
23.39
8


5717
OW0
WAT
V
275
16.104
65.021
59.364
1.00
23.44
8


5718
OW0
WAT
V
276
−6.314
69.710
39.367
1.00
24.17
8


5719
OW0
WAT
V
277
25.476
86.458
13.742
1.00
23.04
8


5720
OW0
WAT
V
278
0.680
86.883
37.755
1.00
23.27
8


5721
OW0
WAT
V
279
33.015
81.157
29.976
1.00
23.30
8


5722
OW0
WAT
V
280
1.763
88.744
19.524
1.00
23.68
8


5723
OW0
WAT
V
281
13.574
55.293
46.773
1.00
23.63
8


5724
OW0
WAT
V
282
13.480
62.142
18.325
1.00
23.48
8


5725
OW0
WAT
V
283
19.332
56.925
43.429
1.00
23.84
8


5726
OW0
WAT
V
284
7.117
53.127
42.902
1.00
23.57
8


5727
OW0
WAT
V
285
27.829
78.220
46.852
1.00
24.20
8


5728
OW0
WAT
V
286
49.295
57.105
51.124
1.00
23.77
8


5729
OW0
WAT
V
287
13.680
105.356
27.022
1.00
24.03
8


5730
OW0
WAT
V
288
17.824
106.639
32.939
1.00
24.44
8


5731
OW0
WAT
V
289
15.542
66.715
53.507
1.00
24.42
8


5732
OW0
WAT
V
290
27.050
47.324
23.573
1.00
24.19
8


5733
OW0
WAT
V
291
39.482
73.577
31.816
1.00
24.19
8


5734
OW0
WAT
V
292
10.356
77.638
16.052
1.00
23.96
8


5735
OW0
WAT
V
293
24.405
50.730
63.252
1.00
24.31
8


5736
OW0
WAT
V
294
15.639
54.776
31.091
1.00
24.31
8


5737
OW0
WAT
V
295
−5.196
74.449
41.013
1.00
24.22
8


5738
OW0
WAT
V
296
40.985
72.335
29.872
1.00
24.55
8


5739
OW0
WAT
V
297
48.449
77.051
18.858
1.00
24.18
8


5740
OW0
WAT
V
298
25.992
92.521
26.784
1.00
24.84
8


5741
OW0
WAT
V
299
45.814
49.306
39.112
1.00
24.65
8


5742
OW0
WAT
V
300
44.725
55.968
11.440
1.00
24.94
8


5743
OW0
WAT
V
301
20.058
84.809
46.357
1.00
24.73
8


5744
OW0
WAT
V
302
18.079
50.984
17.334
1.00
24.58
8


5745
OW0
WAT
V
303
17.020
65.666
56.879
1.00
24.81
8


5746
OW0
WAT
V
304
44.682
72.661
22.319
1.00
24.66
8


5747
OW0
WAT
V
305
0.091
75.457
45.401
1.00
24.37
8


5748
OW0
WAT
V
306
50.222
58.393
53.380
1.00
24.90
8


5749
OW0
WAT
V
307
44.639
52.674
53.486
1.00
25.29
8


5750
OW0
WAT
V
308
49.725
64.827
52.493
1.00
24.60
8


5751
OW0
WAT
V
309
39.542
61.118
7.698
1.00
24.82
8


5752
OW0
WAT
V
310
41.190
79.148
23.073
1.00
25.15
8


5753
OW0
WAT
V
311
1.598
80.899
39.623
1.00
24.95
8


5754
OW0
WAT
V
312
25.053
45.139
19.817
1.00
24.92
8


5755
OW0
WAT
V
313
16.135
84.191
47.663
1.00
25.20
8


5756
OW0
WAT
V
314
11.381
71.857
49.110
1.00
25.29
8


5757
OW0
WAT
V
315
−4.512
57.278
42.326
1.00
25.43
8


5758
OW0
WAT
V
316
3.805
93.061
22.790
1.00
25.09
8


5759
OW0
WAT
V
317
34.832
82.782
37.221
1.00
25.16
8


5760
OW0
WAT
V
318
3.711
95.706
23.179
1.00
25.31
8


5761
OW0
WAT
V
319
20.209
70.499
54.469
1.00
25.69
8


5762
OW0
WAT
V
320
11.697
68.339
56.789
1.00
25.01
8


5763
OW0
WAT
V
321
7.254
91.019
18.448
1.00
25.40
8


5764
OW0
WAT
V
322
42.661
49.979
21.111
1.00
25.81
8


5765
OW0
WAT
V
323
17.078
70.892
50.293
1.00
25.51
8


5766
OW0
WAT
V
324
49.200
60.915
31.600
1.00
25.53
8


5767
OW0
WAT
V
325
31.661
71.214
4.552
1.00
25.64
8


5768
OW0
WAT
V
326
−2.062
96.310
27.990
1.00
25.87
8


5769
OW0
WAT
V
327
39.125
80.230
56.164
1.00
26.25
8


5770
OW0
WAT
V
328
48.433
70.294
57.525
1.00
25.87
8


5771
OW0
WAT
V
329
−2.772
64.990
34.941
1.00
25.71
8


5772
OW0
WAT
V
330
35.352
40.001
22.353
1.00
25.96
8


5773
OW0
WAT
V
331
34.557
81.627
46.792
1.00
26.23
8


5774
OW0
WAT
V
332
23.250
92.581
31.676
1.00
26.20
8


5775
OW0
WAT
V
333
23.167
53.251
13.715
1.00
25.74
8


5776
OW0
WAT
V
334
20.707
52.356
39.202
1.00
25.65
8


5777
OW0
WAT
V
335
4.870
93.727
41.264
1.00
26.54
8


5778
OW0
WAT
V
336
0.053
71.401
29.885
1.00
25.67
8


5779
OW0
WAT
V
337
20.015
56.517
72.324
1.00
25.86
8


5780
OW0
WAT
V
338
13.826
74.132
49.507
1.00
26.36
8


5781
OW0
WAT
V
339
44.958
71.632
28.685
1.00
26.80
8


5782
OW0
WAT
V
340
−0.093
73.784
33.119
1.00
26.07
8


5783
OW0
WAT
V
341
49.630
56.579
40.106
1.00
26.64
8


5784
OW0
WAT
V
342
15.628
79.186
45.524
1.00
26.42
8


5785
OW0
WAT
V
343
31.176
91.867
30.769
1.00
26.10
8


5786
OW0
WAT
V
344
15.626
67.643
55.543
1.00
26.46
8


5787
OW0
WAT
V
345
21.398
95.678
38.839
1.00
26.79
8


5788
OW0
WAT
V
346
41.099
41.982
39.915
1.00
26.66
8


5789
OW0
WAT
V
347
22.442
79.888
2.661
1.00
26.18
8


5790
OW0
WAT
V
348
44.448
72.532
39.099
1.00
27.08
8


5791
OW0
WAT
V
349
40.265
82.719
10.175
1.00
26.27
8


5792
OW0
WAT
V
350
40.934
43.657
30.662
1.00
27.04
8


5793
OW0
WAT
V
351
−1.666
97.213
32.163
1.00
27.31
8


5794
OW0
WAT
V
352
−8.111
67.221
45.293
1.00
27.12
8


5795
OW0
WAT
V
353
16.355
56.614
42.471
1.00
27.10
8


5796
OW0
WAT
V
354
11.346
65.531
19.934
1.00
27.40
8


5797
OW0
WAT
V
355
11.189
105.275
21.949
1.00
27.29
8


5798
OW0
WAT
V
356
23.545
83.502
8.615
1.00
27.06
8


5799
OW0
WAT
V
357
22.122
49.913
14.384
1.00
27.06
8


5800
OW0
WAT
V
358
6.833
52.668
34.000
1.00
27.79
8


5801
OW0
WAT
V
359
30.479
47.598
56.666
1.00
27.66
8


5802
OW0
WAT
V
360
33.166
42.826
19.802
1.00
27.33
8


5803
OW0
WAT
V
361
24.029
55.851
13.947
1.00
28.08
8


5804
OW0
WAT
V
362
39.488
85.709
20.632
1.00
27.01
8


5805
OW0
WAT
V
363
2.130
49.916
43.049
1.00
27.26
8


5806
OW0
WAT
V
364
35.616
41.373
27.626
1.00
27.13
8


5807
OW0
WAT
V
365
50.664
58.560
41.450
1.00
26.59
8


5808
OW0
WAT
V
366
30.943
49.068
15.778
1.00
26.98
8


5809
OW0
WAT
V
367
43.193
44.166
34.878
1.00
26.97
8


5810
OW0
WAT
V
368
6.994
74.430
21.876
1.00
27.26
8


5811
OW0
WAT
V
369
34.427
88.111
38.939
1.00
27.30
8


5812
OW0
WAT
V
370
1.636
93.582
40.791
1.00
27.54
8


5813
OW0
WAT
V
371
5.971
98.241
21.504
1.00
27.42
8


5814
OW0
WAT
V
372
29.223
75.038
60.445
1.00
26.93
8


5815
OW0
WAT
V
373
31.316
53.650
9.481
1.00
27.85
8


5816
OW0
WAT
V
374
43.939
56.548
55.050
1.00
27.63
8


5817
OW0
WAT
V
375
46.559
74.427
54.610
1.00
27.46
8


5818
OW0
WAT
V
376
26.961
70.400
70.205
1.00
28.10
8


5819
OW0
WAT
V
377
48.989
57.080
35.445
1.00
28.37
8


5820
OW0
WAT
V
378
14.950
47.050
27.899
1.00
27.90
8


5821
OW0
WAT
V
379
46.760
46.713
39.616
1.00
27.67
8


5822
OW0
WAT
V
380
−1.380
79.896
38.771
1.00
28.02
8


5823
OW0
WAT
V
381
12.690
81.625
15.826
1.00
28.03
8


5824
OW0
WAT
V
382
10.617
104.039
32.646
1.00
28.19
8


5825
OW0
WAT
V
383
13.859
80.594
13.625
1.00
27.99
8


5826
OW0
WAT
V
384
7.322
72.231
20.822
1.00
28.35
8


5827
OW0
WAT
V
385
29.284
46.632
44.658
1.00
28.26
8


5828
OW0
WAT
V
386
18.064
50.559
24.862
1.00
28.35
8


5829
OW0
WAT
V
387
35.054
45.412
46.835
1.00
28.58
8


5830
OW0
WAT
V
388
22.478
83.558
13.277
1.00
28.32
8


5831
OW0
WAT
V
389
10.928
67.510
14.236
1.00
28.65
8


5832
OW0
WAT
V
390
33.397
82.246
49.220
1.00
27.37
8


5833
OW0
WAT
V
391
23.434
88.556
18.508
1.00
28.95
8


5834
OW0
WAT
V
392
29.832
42.212
39.251
1.00
28.21
8


5835
OW0
WAT
V
393
15.076
70.102
51.758
1.00
27.91
8


5836
OW0
WAT
V
394
35.566
48.453
66.263
1.00
28.16
8


5837
OW0
WAT
V
395
34.691
46.594
49.301
1.00
28.85
8


5838
OW0
WAT
V
396
39.702
74.440
36.238
1.00
28.77
8


5839
OW0
WAT
V
397
50.176
56.086
14.851
1.00
28.75
8


5840
OW0
WAT
V
398
14.115
57.834
59.211
1.00
27.83
8


5841
OW0
WAT
V
399
38.189
49.702
11.383
1.00
29.29
8


5842
OW0
WAT
V
400
3.241
100.941
39.033
1.00
28.47
8


5843
OW0
WAT
V
401
44.298
73.510
63.099
1.00
28.91
8


5844
OW0
WAT
V
402
7.061
75.135
47.544
1.00
28.59
8


5845
OW0
WAT
V
403
5.477
86.910
42.452
1.00
29.56
8


5846
OW0
WAT
V
404
25.564
72.515
56.246
1.00
29.09
8


5847
OW0
WAT
V
405
25.075
41.160
32.189
1.00
29.20
8


5848
OW0
WAT
V
406
2.074
56.387
58.854
1.00
28.86
8


5849
OW0
WAT
V
407
47.163
58.038
33.355
1.00
28.76
8


5850
OW0
WAT
V
408
27.438
44.407
21.116
1.00
28.21
8


5851
OW0
WAT
V
409
32.690
89.765
34.445
1.00
29.13
8


5852
OW0
WAT
V
410
8.726
56.984
33.875
1.00
28.81
8


5853
OW0
WAT
V
411
−2.765
74.847
45.763
1.00
28.58
8


5854
OW0
WAT
V
412
9.880
76.028
48.593
1.00
29.43
8


5855
OW0
WAT
V
413
18.587
55.405
41.191
1.00
28.66
8


5856
OW0
WAT
V
414
0.831
95.595
23.928
1.00
28.90
8


5857
OW0
WAT
V
415
18.167
58.042
65.360
1.00
28.57
8


5858
OW0
WAT
V
416
42.814
47.661
27.620
1.00
29.34
8


5859
OW0
WAT
V
417
19.226
89.316
19.020
1.00
29.13
8


5860
OW0
WAT
V
418
17.933
82.283
11.952
1.00
28.48
8


5861
OW0
WAT
V
419
44.723
79.313
13.493
1.00
30.12
8


5862
OW0
WAT
V
420
34.399
78.316
0.819
1.00
29.81
8


5863
OW0
WAT
V
421
28.282
72.460
57.888
1.00
29.12
8


5864
OW0
WAT
V
422
50.448
63.547
18.793
1.00
29.31
8


5865
OW0
WAT
V
423
43.033
55.323
65.913
1.00
29.32
8


5866
OW0
WAT
V
424
45.865
51.168
51.498
1.00
29.29
8


5867
OW0
WAT
V
425
12.844
59.751
19.386
1.00
29.45
8


5868
OW0
WAT
V
426
−3.707
82.697
22.959
1.00
29.58
8


5869
OW0
WAT
V
427
28.989
45.171
18.941
1.00
29.97
8


5870
OW0
WAT
V
428
14.689
65.149
11.472
1.00
29.76
8


5871
OW0
WAT
V
429
49.962
74.061
53.225
1.00
29.59
8


5872
OW0
WAT
V
430
26.674
46.428
17.647
1.00
29.59
8


5873
OW0
WAT
V
431
32.017
64.281
73.846
1.00
29.67
8


5874
OW0
WAT
V
432
−1.685
89.735
36.396
1.00
29.42
8


5875
OW0
WAT
V
433
35.326
90.671
32.858
1.00
30.08
8


5876
OW0
WAT
V
434
−5.217
86.519
22.737
1.00
30.64
8


5877
OW0
WAT
V
435
22.655
40.619
31.468
1.00
30.18
8


5878
OW0
WAT
V
436
9.970
66.686
21.940
1.00
30.16
8


5879
OW0
WAT
V
437
22.156
103.267
41.579
1.00
28.97
8


5880
OW0
WAT
V
438
40.919
45.553
23.996
1.00
30.13
8


5881
OW0
WAT
V
439
24.378
42.994
18.498
1.00
30.29
8


5882
OW0
WAT
V
440
27.456
90.485
38.760
1.00
29.87
8


5883
OW0
WAT
V
441
41.628
78.372
57.406
1.00
30.24
8


5884
OW0
WAT
V
442
10.162
67.365
58.879
1.00
30.51
8


5885
OW0
WAT
V
443
7.899
70.258
55.642
1.00
29.98
8


5886
OW0
WAT
V
444
7.439
62.721
58.664
1.00
30.04
8


5887
OW0
WAT
V
445
30.182
60.296
5.170
1.00
30.62
8


5888
OW0
WAT
V
446
36.835
87.065
16.010
1.00
30.22
8


5889
OW0
WAT
V
447
48.154
58.076
55.789
1.00
30.39
8


5890
OW0
WAT
V
448
9.079
102.838
38.708
1.00
30.45
8


5891
OW0
WAT
V
449
31.488
67.009
5.903
1.00
30.35
8


5892
OW0
WAT
V
450
8.486
84.645
16.251
1.00
30.46
8


5893
OW0
WAT
V
451
17.712
70.200
52.856
1.00
31.30
8


5894
OW0
WAT
V
452
45.187
54.640
9.218
1.00
30.47
8


5895
OW0
WAT
V
453
23.220
65.098
2.001
1.00
30.15
8


5896
OW0
WAT
V
454
43.353
48.993
23.792
1.00
30.21
8


5897
OW0
WAT
V
455
0.241
76.716
42.809
1.00
30.43
8


5898
OW0
WAT
V
456
38.954
90.362
25.885
1.00
31.19
8


5899
OW0
WAT
V
457
8.998
51.618
42.193
1.00
30.65
8


5900
OW0
WAT
V
458
47.484
70.509
20.484
1.00
30.75
8


5901
OW0
WAT
V
459
26.632
83.732
7.006
1.00
30.86
8


5902
OW0
WAT
V
460
27.887
84.031
46.702
1.00
31.16
8


5903
OW0
WAT
V
461
10.456
52.659
39.931
1.00
31.37
8


5904
OW0
WAT
V
462
25.474
53.247
11.551
1.00
31.54
8


5905
OW0
WAT
V
463
21.666
48.674
41.178
1.00
31.71
8


5906
OW0
WAT
V
464
51.799
63.643
37.234
1.00
30.69
8


5907
OW0
WAT
V
465
17.686
48.668
36.134
1.00
31.38
8


5908
OW0
WAT
V
466
47.081
52.951
49.717
1.00
30.51
8


5909
OW0
WAT
V
467
15.593
93.203
42.768
1.00
30.90
8


5910
OW0
WAT
V
468
36.480
80.071
53.771
1.00
30.56
8


5911
OW0
WAT
V
469
42.137
47.781
14.882
1.00
31.85
8


5912
OW0
WAT
V
470
22.333
61.351
70.096
1.00
31.36
8


5913
OW0
WAT
V
471
40.228
72.527
72.095
1.00
31.17
8


5914
OW0
WAT
V
472
1.666
74.527
48.132
1.00
31.28
8


5915
OW0
WAT
V
473
14.531
66.936
59.718
1.00
31.26
8


5916
OW0
WAT
V
474
21.000
68.421
1.879
1.00
31.59
8


5917
OW0
WAT
V
475
37.163
82.170
41.385
1.00
31.32
8


5918
OW0
WAT
V
476
26.307
62.094
4.445
1.00
31.75
8


5919
OW0
WAT
V
477
51.579
61.409
40.641
1.00
31.25
8


5920
OW0
WAT
V
478
41.761
64.533
7.578
1.00
31.59
8


5921
OW0
WAT
V
479
−7.353
65.632
35.219
1.00
31.13
8


5922
OW0
WAT
V
480
16.514
82.720
36.237
1.00
31.25
8


5923
OW0
WAT
V
481
23.770
75.891
54.586
1.00
31.53
8


5924
OW0
WAT
V
482
50.377
68.458
56.245
1.00
31.72
8


5925
OW0
WAT
V
483
15.979
105.053
38.501
1.00
30.98
8


5926
OW0
WAT
V
484
27.194
93.867
31.829
1.00
31.85
8


5927
OW0
WAT
V
485
39.487
68.664
5.438
1.00
31.02
8


5928
OW0
WAT
V
486
30.446
58.438
75.573
1.00
31.49
8


5929
OW0
WAT
V
487
−2.258
85.349
34.418
1.00
31.74
8


5930
OW0
WAT
V
488
46.873
56.769
65.770
1.00
31.57
8


5931
OW0
WAT
V
489
18.407
47.617
19.229
1.00
31.61
8


5932
OW0
WAT
V
490
2.500
78.686
43.392
1.00
31.62
8


5933
OW0
WAT
V
491
7.727
97.913
42.497
1.00
32.36
8


5934
OW0
WAT
V
492
−5.430
71.658
30.991
1.00
32.45
8


5935
OW0
WAT
V
493
47.547
72.958
21.222
1.00
31.57
8


5936
OW0
WAT
V
494
9.955
91.961
24.393
1.00
32.43
8


5937
OW0
WAT
V
495
12.996
52.420
46.232
1.00
31.76
8


5938
OW0
WAT
V
496
7.952
65.594
58.841
1.00
32.02
8


5939
OW0
WAT
V
497
37.204
88.789
33.415
1.00
31.57
8


5940
OW0
WAT
V
498
36.857
41.938
29.865
1.00
32.38
8


5941
OW0
WAT
V
499
7.220
51.844
54.727
1.00
32.32
8


5942
OW0
WAT
V
500
16.110
76.377
49.777
1.00
32.31
8


5943
OW0
WAT
V
501
24.511
47.736
42.135
1.00
32.37
8


5944
OW0
WAT
V
502
22.783
46.357
48.051
1.00
32.64
8


5945
OW0
WAT
V
503
27.138
60.897
7.569
1.00
32.20
8


5946
OW0
WAT
V
504
47.227
50.290
36.850
1.00
32.13
8


5947
OW0
WAT
V
505
6.733
67.493
23.991
1.00
32.68
8


5948
OW0
WAT
V
506
16.514
70.176
56.941
1.00
32.03
8


5949
OW0
WAT
V
507
43.175
79.662
8.514
1.00
31.76
8


5950
OW0
WAT
V
508
−3.757
80.394
22.899
1.00
32.62
8


5951
OW0
WAT
V
509
10.932
85.936
45.262
1.00
32.65
8


5952
OW0
WAT
V
510
3.455
97.650
41.755
1.00
32.31
8


5953
OW0
WAT
V
511
33.419
50.551
69.455
1.00
32.14
8


5954
OW0
WAT
V
512
4.069
99.962
23.550
1.00
33.21
8


5955
OW0
WAT
V
513
−7.206
65.717
41.690
1.00
33.20
8


5956
OW0
WAT
V
514
53.785
60.262
61.406
1.00
33.37
8


5957
OW0
WAT
V
515
16.599
87.045
17.346
1.00
32.99
8


5958
OW0
WAT
V
516
47.349
54.074
30.752
1.00
32.14
8


5959
OW0
WAT
V
517
7.038
85.163
42.409
1.00
32.78
8


5960
OW0
WAT
V
518
16.879
50.503
27.538
1.00
32.69
8


5961
OW0
WAT
V
519
30.838
91.776
22.385
1.00
33.06
8


5962
OW0
WAT
V
520
33.882
41.296
32.218
1.00
34.59
8


5963
OW0
WAT
V
521
53.502
60.512
23.358
1.00
32.27
8


5964
OW0
WAT
V
522
41.841
73.003
34.316
1.00
33.63
8


5965
OW0
WAT
V
523
18.807
69.394
5.371
1.00
32.65
8


5966
OW0
WAT
V
524
0.567
102.365
27.670
1.00
32.87
8


5967
OW0
WAT
V
525
28.899
48.822
64.451
1.00
32.62
8


5968
OW0
WAT
V
526
42.766
46.627
21.339
1.00
33.04
8


5969
OW0
WAT
V
527
18.159
66.472
60.034
1.00
33.02
8


5970
OW0
WAT
V
528
22.385
49.518
59.427
1.00
33.48
8


5971
OW0
WAT
V
529
14.542
53.899
35.438
1.00
32.40
8


5972
OW0
WAT
V
530
0.923
81.260
18.821
1.00
33.19
8


5973
OW0
WAT
V
531
35.980
91.602
25.073
1.00
32.89
8


5974
OW0
WAT
V
532
40.667
67.024
71.313
1.00
32.79
8


5975
OW0
WAT
V
533
8.626
61.294
60.713
1.00
32.69
8


5976
OW0
WAT
V
534
35.615
48.266
53.410
1.00
33.74
8


5977
OW0
WAT
V
535
50.581
54.379
41.752
1.00
32.75
8


5978
OW0
WAT
V
536
34.738
50.213
7.372
1.00
33.68
8


5979
OW0
WAT
V
537
42.324
79.266
54.340
1.00
32.72
8


5980
OW0
WAT
V
538
16.132
78.441
8.864
1.00
33.64
8


5981
OW0
WAT
V
539
20.256
45.911
20.702
1.00
33.89
8


5982
OW0
WAT
V
540
37.253
43.882
46.170
1.00
33.73
8


5983
OW0
WAT
V
541
31.158
88.960
12.651
1.00
34.15
8


5984
OW0
WAT
V
542
2.885
65.252
30.182
1.00
33.66
8


5985
OW0
WAT
V
543
24.093
72.008
54.068
1.00
33.53
8


5986
OW0
WAT
V
544
−4.660
58.902
52.534
1.00
34.13
8


5987
OW0
WAT
V
545
20.523
52.571
71.335
1.00
34.29
8


5988
OW0
WAT
V
546
50.389
70.373
43.120
1.00
34.05
8


5989
OW0
WAT
V
547
−1.784
74.917
34.717
1.00
34.27
8


5990
OW0
WAT
V
548
25.051
100.468
31.517
1.00
33.73
8


5991
OW0
WAT
V
549
21.989
83.148
46.194
1.00
34.71
8


5992
OW0
WAT
V
550
47.521
62.364
11.718
1.00
34.05
8


5993
OW0
WAT
V
551
52.236
59.305
62.786
1.00
33.21
8


5994
OW0
WAT
V
552
40.232
80.510
16.448
1.00
34.62
8


5995
OW0
WAT
V
553
46.253
56.949
70.930
1.00
33.53
8


5996
OW0
WAT
V
554
47.895
53.053
37.454
1.00
33.41
8


5997
OW0
WAT
V
555
13.358
71.030
49.662
1.00
34.43
8


5998
OW0
WAT
V
556
−0.137
73.990
26.087
1.00
34.05
8


5999
OW0
WAT
V
557
43.973
74.382
6.399
1.00
34.44
8


6000
OW0
WAT
V
558
35.593
60.367
77.022
1.00
33.63
8


6001
OW0
WAT
V
559
6.112
83.592
41.192
1.00
34.97
8


6002
OW0
WAT
V
560
38.614
41.425
25.492
1.00
34.42
8


6003
OW0
WAT
V
561
34.074
88.144
12.960
1.00
34.41
8


6004
OW0
WAT
V
562
40.114
63.213
5.786
1.00
34.56
8


6005
OW0
WAT
V
563
−0.202
64.215
60.019
1.00
34.60
8


6006
OW0
WAT
V
564
4.614
92.264
20.329
1.00
33.82
8


6007
OW0
WAT
V
565
15.212
50.738
32.687
1.00
34.54
8


6008
OW0
WAT
V
566
13.018
70.753
53.378
1.00
35.00
8


6009
OW0
WAT
V
567
37.836
57.700
75.968
1.00
33.91
8


6010
OW0
WAT
V
568
18.054
71.354
7.047
1.00
34.28
8


6011
OW0
WAT
V
569
20.435
57.091
12.782
1.00
34.06
8


6012
OW0
WAT
V
570
−1.113
72.836
30.802
1.00
34.18
8


6013
OW0
WAT
V
571
45.394
47.985
15.576
1.00
34.25
8


6014
OW0
WAT
V
572
18.083
105.524
25.739
1.00
35.26
8


6015
OW0
WAT
V
573
42.363
51.035
61.868
1.00
34.64
8


6016
OW0
WAT
V
574
3.332
65.717
27.045
1.00
35.54
8


6017
OW0
WAT
V
575
0.099
70.672
51.291
1.00
34.72
8


6018
OW0
WAT
V
576
0.045
61.496
31.457
1.00
35.51
8


6019
OW0
WAT
V
577
46.395
53.881
61.040
1.00
34.53
8


6020
OW0
WAT
V
578
52.136
68.150
59.956
1.00
35.10
8


6021
OW0
WAT
V
579
19.009
41.546
26.130
1.00
33.65
8


6022
OW0
WAT
V
580
34.720
74.712
71.942
1.00
34.54
8


6023
OW0
WAT
V
581
37.259
73.783
73.743
1.00
35.82
8


6024
OW0
WAT
V
582
27.833
55.518
10.945
1.00
34.54
8


6025
OW0
WAT
V
583
46.309
60.566
10.060
1.00
35.04
8


6026
OW0
WAT
V
584
10.952
63.329
18.773
1.00
34.23
8


6027
OW0
WAT
V
585
−1.056
54.481
35.620
1.00
34.65
8


6028
OW0
WAT
V
586
−4.178
63.600
36.602
1.00
35.48
8


6029
OW0
WAT
V
587
4.690
96.750
20.660
1.00
34.69
8


6030
OW0
WAT
V
588
8.484
73.376
50.572
1.00
35.07
8


6031
OW0
WAT
V
589
44.017
50.506
11.023
1.00
35.68
8


6032
OW0
WAT
V
590
3.744
50.549
36.911
1.00
35.69
8


6033
OW0
WAT
V
591
49.672
55.539
26.394
1.00
35.74
8


6034
OW0
WAT
V
592
27.932
93.666
25.261
1.00
35.64
8


6035
OW0
WAT
V
593
22.451
73.996
54.266
1.00
35.51
8


6036
OW0
WAT
V
594
33.048
48.697
67.743
1.00
35.66
8


6037
OW0
WAT
V
595
12.820
101.046
44.339
1.00
36.16
8


6038
OW0
WAT
V
596
51.198
69.586
53.643
1.00
35.14
8


6039
OW0
WAT
V
597
29.662
79.574
54.942
1.00
35.66
8


6040
OW0
WAT
V
598
32.247
80.128
52.116
1.00
36.54
8


6041
OW0
WAT
V
599
6.142
51.551
37.685
1.00
35.34
8


6042
OW0
WAT
V
600
5.622
70.631
22.637
1.00
35.66
8


6043
OW0
WAT
V
601
22.365
48.081
48.242
1.00
36.08
8


6044
OW0
WAT
V
602
8.288
81.332
15.641
1.00
35.59
8


6045
OW0
WAT
V
603
10.941
74.805
15.117
1.00
35.60
8


6046
OW0
WAT
V
604
35.796
73.953
1.142
1.00
35.09
8


6047
OW0
WAT
V
605
38.777
85.286
9.309
1.00
36.46
8


6048
OW0
WAT
V
606
20.560
52.963
75.539
1.00
37.03
8


6049
OW0
WAT
V
607
−3.377
66.230
32.749
1.00
35.54
8


6050
OW0
WAT
V
608
40.087
44.107
14.031
1.00
36.33
8


6051
OW0
WAT
V
609
−1.635
86.958
36.864
1.00
35.23
8


6052
OW0
WAT
V
610
48.364
69.799
29.088
1.00
35.08
8


6053
OW0
WAT
V
611
18.383
50.939
35.706
1.00
36.23
8


6054
OW0
WAT
V
612
18.334
58.135
13.735
1.00
37.22
8


6055
OW0
WAT
V
613
16.341
55.369
50.997
1.00
35.78
8


6056
OW0
WAT
V
614
28.580
52.384
12.139
1.00
36.07
8


6057
OW0
WAT
V
615
23.108
103.615
38.927
1.00
36.81
8


6058
OW0
WAT
V
616
12.325
79.803
46.301
1.00
35.61
8


6059
OW0
WAT
V
617
21.280
67.375
64.153
1.00
36.55
8


6060
OW0
WAT
V
618
40.907
80.214
52.034
1.00
37.09
8


6061
OW0
WAT
V
619
47.006
72.793
58.223
1.00
36.47
8


6062
OW0
WAT
V
620
20.221
90.473
42.499
1.00
36.27
8


6063
OW0
WAT
V
621
4.100
73.674
21.447
1.00
36.94
8


6064
OW0
WAT
V
622
8.503
104.300
35.973
1.00
36.81
8


6065
OW0
WAT
V
623
30.691
78.729
57.692
1.00
35.94
8


6066
OW0
WAT
V
624
−3.070
94.866
30.332
1.00
36.58
8


6067
OW0
WAT
V
625
46.455
79.736
18.637
1.00
35.97
8


6068
OW0
WAT
V
626
46.537
55.701
59.420
1.00
37.10
8


6069
OW0
WAT
V
627
43.765
47.227
50.091
1.00
37.02
8


6070
OW0
WAT
V
628
−0.451
52.302
37.499
1.00
36.00
8


6071
OW0
WAT
V
629
47.301
50.088
41.392
1.00
37.12
8


6072
OW0
WAT
V
630
37.956
80.815
13.060
1.00
37.94
8


6073
OW0
WAT
V
631
17.138
62.973
7.515
1.00
37.42
8


6074
OW0
WAT
V
632
13.837
57.372
18.395
1.00
36.82
8


6075
OW0
WAT
V
633
41.756
55.821
70.896
1.00
36.92
8


6076
OW0
WAT
V
634
25.077
93.998
28.706
1.00
36.97
8


6077
OW0
WAT
V
635
47.608
54.704
64.130
1.00
37.13
8


6078
OW0
WAT
V
636
6.911
105.878
25.141
1.00
36.23
8


6079
OW0
WAT
V
637
42.682
67.557
69.041
1.00
36.92
8


6080
OW0
WAT
V
638
15.363
88.594
48.034
1.00
37.42
8


6081
OW0
WAT
V
639
33.890
42.321
17.015
1.00
37.23
8


6082
OW0
WAT
V
640
9.736
84.033
43.853
1.00
36.17
8


6083
OW0
WAT
V
641
10.886
51.035
46.103
1.00
37.66
8


6084
OW0
WAT
V
642
27.929
72.978
70.610
1.00
37.35
8


6085
OW0
WAT
V
643
1.233
69.664
25.786
1.00
37.56
8


6086
OW0
WAT
V
644
15.151
107.231
33.216
1.00
36.50
8


6087
OW0
WAT
V
645
25.823
98.361
30.305
1.00
36.65
8


6088
OW0
WAT
V
646
34.857
84.394
12.899
1.00
36.71
8


6089
OW0
WAT
V
647
20.425
52.936
41.877
1.00
36.99
8


6090
OW0
WAT
V
648
26.575
49.377
65.800
1.00
37.37
8


6091
OW0
WAT
V
649
31.193
44.914
15.071
1.00
36.96
8


6092
OW0
WAT
V
650
10.578
49.772
48.688
1.00
36.01
8


6093
OW0
WAT
V
651
18.128
51.717
38.409
1.00
37.57
8


6094
OW0
WAT
V
652
45.424
54.692
56.844
1.00
37.37
8


6095
OW0
WAT
V
653
28.011
90.646
18.192
1.00
37.91
8


6096
OW0
WAT
V
654
47.536
55.043
51.941
1.00
36.73
8


6097
OW0
WAT
V
655
24.853
98.451
32.915
1.00
37.70
8


6098
OW0
WAT
V
656
27.088
98.198
26.870
1.00
38.56
8


6099
OW0
WAT
V
657
33.663
49.796
11.597
1.00
37.19
8


6100
OW0
WAT
V
658
16.309
55.242
45.035
1.00
37.83
8


6101
OW0
WAT
V
659
20.804
43.210
25.195
1.00
37.72
8


6102
OW0
WAT
V
660
23.932
65.246
70.893
1.00
37.09
8


6103
OW0
WAT
V
661
0.664
53.286
53.271
1.00
38.36
8


6104
OW0
WAT
V
662
40.187
84.151
18.538
1.00
38.05
8


6105
OW0
WAT
V
663
44.129
77.826
7.095
1.00
38.36
8


6106
OW0
WAT
V
664
5.654
103.176
36.651
1.00
38.12
8


6107
OW0
WAT
V
665
−2.551
55.092
37.581
1.00
39.63
8


6108
OW0
WAT
V
666
48.102
56.702
13.267
1.00
37.64
8


6109
OW0
WAT
V
667
27.824
90.475
15.555
1.00
36.41
8


6110
OW0
WAT
V
668
38.699
49.812
63.112
1.00
37.80
8


6111
OW0
WAT
V
669
−2.199
54.401
53.588
1.00
39.21
8


6112
OW0
WAT
V
670
19.006
53.240
47.228
1.00
38.93
8


6113
OW0
WAT
V
671
46.897
48.817
19.829
1.00
39.11
8


6114
OW0
WAT
V
672
42.301
48.935
12.664
1.00
37.43
8


6115
OW0
WAT
V
673
16.098
53.972
53.322
1.00
38.55
8


6116
OW0
WAT
V
674
16.992
66.360
61.965
1.00
40.47
8


6117
OW0
WAT
V
675
17.396
84.259
14.592
1.00
37.45
8


6118
OW0
WAT
V
676
48.023
70.300
38.414
1.00
38.28
8


6119
OW0
WAT
V
677
21.061
60.355
72.008
1.00
38.68
8


6120
OW0
WAT
V
678
25.412
45.777
15.102
1.00
40.05
8


6121
OW0
WAT
V
679
43.705
73.272
1.624
1.00
38.78
8


6122
OW0
WAT
V
680
17.379
67.334
7.173
1.00
38.88
8


6123
OW0
WAT
V
681
19.500
72.583
5.113
1.00
41.12
8


6124
OW0
WAT
V
682
27.135
53.269
75.096
1.00
38.74
8


6125
OW0
WAT
V
683
43.871
76.670
2.397
1.00
38.42
8


6126
OW0
WAT
V
684
32.690
47.277
60.342
1.00
38.23
8


6127
OW0
WAT
V
685
38.889
50.643
67.387
1.00
38.05
8


6128
OW0
WAT
V
686
15.848
75.816
7.403
1.00
37.86
8


6129
OW0
WAT
V
687
25.036
96.149
30.003
1.00
38.02
8


6130
OW0
WAT
V
688
44.120
49.147
54.661
1.00
39.21
8


6131
OW0
WAT
V
689
31.793
51.208
10.937
1.00
39.53
8


6132
OW0
WAT
V
690
9.476
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43.783
1.00
37.31
8


6133
OW0
WAT
V
691
8.821
88.129
44.638
1.00
39.95
8


6134
OW0
WAT
V
692
8.003
80.636
43.644
1.00
37.70
8


6135
OW0
WAT
V
693
14.834
83.314
13.883
1.00
39.80
8


6136
OW0
WAT
V
694
21.370
44.389
41.265
1.00
39.75
8


6137
OW0
WAT
V
695
25.208
85.122
7.995
1.00
38.90
8


6138
OW0
WAT
V
696
34.431
64.498
5.882
1.00
37.43
8


6139
OW0
WAT
V
697
46.857
48.623
44.260
1.00
38.67
8


6140
OW0
WAT
V
698
48.394
49.074
31.806
1.00
38.40
8


6141
OW0
WAT
V
699
6.330
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18.323
1.00
39.24
8


6142
OW0
WAT
V
700
3.567
68.493
56.513
1.00
39.03
8


6143
OW0
WAT
V
701
19.531
67.580
61.273
1.00
38.68
8


6144
OW0
WAT
V
702
36.514
82.654
34.129
1.00
38.10
8


6145
OW0
WAT
V
703
43.559
50.161
59.718
1.00
39.15
8


6146
OW0
WAT
V
704
41.881
70.064
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1.00
39.49
8


6147
OW0
WAT
V
705
12.039
106.892
30.442
1.00
39.69
8


6148
OW0
WAT
V
706
25.673
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52.252
1.00
39.17
8


6149
OW0
WAT
V
707
46.855
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26.181
1.00
40.35
8


6150
OW0
WAT
V
708
21.077
93.052
39.231
1.00
39.44
8


6151
OW0
WAT
V
709
28.621
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1.00
38.56
8


6152
OW0
WAT
V
710
−3.607
57.742
54.506
1.00
38.82
8


6153
OW0
WAT
V
711
25.913
41.714
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1.00
38.94
8


6154
OW0
WAT
V
712
21.385
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1.00
39.85
8


6155
OW0
WAT
V
713
39.666
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56.093
1.00
40.16
8


6156
OW0
WAT
V
714
33.043
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1.00
38.56
8


6157
OW0
WAT
V
715
3.335
48.480
47.523
1.00
40.24
8


6158
OW0
WAT
V
716
−5.954
59.355
43.289
1.00
39.30
8


6159
OW0
WAT
V
717
−2.633
70.380
52.100
1.00
39.49
8


6160
OW0
WAT
V
718
14.943
51.881
28.927
1.00
41.17
8


6161
OW0
WAT
V
719
30.665
55.789
76.270
1.00
36.29
8


6162
OW0
WAT
V
720
38.153
41.243
44.336
1.00
39.61
8


6163
OW0
WAT
V
721
42.857
72.924
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1.00
39.33
8


6164
OW0
WAT
V
722
42.983
45.506
30.086
1.00
39.35
8


6165
OW0
WAT
V
723
8.541
68.671
15.477
1.00
40.10
8


6166
OW0
WAT
V
724
3.357
68.745
24.682
1.00
39.21
8


6167
OW0
WAT
V
725
32.096
74.899
2.155
1.00
38.68
8


6168
OW0
WAT
V
726
−3.316
99.677
31.930
1.00
40.29
8


6169
OW0
WAT
V
727
33.290
44.355
45.552
1.00
39.94
8


6170
OW0
WAT
V
728
50.677
69.314
25.213
1.00
38.89
8


6171
OW0
WAT
V
729
35.441
42.395
37.048
1.00
39.29
8


6172
OW0
WAT
V
730
8.363
53.922
35.516
1.00
38.32
8


6173
OW0
WAT
V
731
−1.713
91.588
39.071
1.00
40.09
8


6174
OW0
WAT
V
732
22.068
82.950
49.452
1.00
38.86
8


6175
OW0
WAT
V
733
−1.449
89.011
21.652
1.00
39.99
8


6176
OW0
WAT
V
734
37.354
59.035
5.289
1.00
40.90
8


6177
OW0
WAT
V
735
20.992
87.687
45.698
1.00
40.19
8


6178
OW0
WAT
V
736
46.650
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54.492
1.00
40.47
8


6179
OW0
WAT
V
737
7.370
47.777
49.173
1.00
41.37
8


6180
OW0
WAT
V
738
14.279
71.404
55.742
1.00
39.06
8


6181
OW0
WAT
V
739
13.276
62.067
63.468
1.00
38.95
8


6182
OW0
WAT
V
740
47.469
55.262
33.788
1.00
41.14
8


6183
OW0
WAT
V
741
35.182
72.963
73.409
1.00
38.69
8


6184
OW0
WAT
V
742
28.993
42.749
41.796
1.00
40.22
8


6185
OW0
WAT
V
743
12.430
51.804
37.400
1.00
39.68
8


6186
OW0
WAT
V
744
5.325
85.408
18.950
1.00
41.26
8


6187
OW0
WAT
V
745
41.721
66.169
73.677
1.00
39.43
8


6188
OW0
WAT
V
746
16.983
83.519
10.040
1.00
40.83
8


6189
OW0
WAT
V
747
−3.245
67.552
51.568
1.00
41.14
8


6190
OW0
WAT
V
748
18.547
72.699
54.390
1.00
40.80
8


6191
OW0
WAT
V
749
50.952
65.503
10.665
1.00
39.71
8


6192
OW0
WAT
V
750
6.873
59.618
31.097
1.00
40.61
8


6193
OW0
WAT
V
751
44.643
72.249
41.540
1.00
40.21
8


6194
OW0
WAT
V
752
10.333
59.620
21.158
1.00
40.03
8


6195
OW0
WAT
V
753
25.342
99.843
20.985
1.00
40.88
8


6196
OW0
WAT
V
754
13.886
67.341
51.913
1.00
41.40
8


6197
OW0
WAT
V
755
20.669
50.466
56.076
1.00
40.93
8


6198
OW0
WAT
V
756
16.062
51.352
42.439
0.00
41.08
8


6199
OW0
WAT
V
757
−2.323
91.095
34.519
1.00
40.69
8


6200
OW0
WAT
V
758
3.987
63.229
29.353
1.00
41.53
8


6201
OW0
WAT
V
759
20.694
99.900
18.786
1.00
39.84
8


6202
OW0
WAT
V
760
21.098
72.115
58.710
1.00
40.04
8


6203
OW0
WAT
V
761
39.451
41.349
13.513
1.00
40.57
8


6204
OW0
WAT
V
762
3.185
80.792
42.000
1.00
41.27
8


6205
OW0
WAT
V
763
15.866
68.494
52.407
1.00
40.90
8


6206
OW0
WAT
V
764
42.027
79.686
47.257
1.00
40.14
8


6207
OW0
WAT
V
765
41.063
55.022
68.081
1.00
42.98
8


6208
OW0
WAT
V
766
15.728
85.261
16.175
1.00
42.08
8


6209
OW0
WAT
V
767
−8.665
63.541
41.234
1.00
40.98
8


6210
OW0
WAT
V
768
28.828
85.580
44.440
1.00
40.75
8


6211
OW0
WAT
V
769
46.504
46.346
43.773
1.00
40.98
8


6212
OW0
WAT
V
770
52.964
61.429
54.373
1.00
41.49
8


6213
OW0
WAT
V
771
25.001
95.005
39.507
1.00
41.35
8


6214
OW0
WAT
V
772
4.818
62.633
59.449
1.00
41.54
8


6215
OW0
WAT
V
773
18.916
60.160
66.080
1.00
41.09
8


6216
OW0
WAT
V
774
27.033
88.841
12.019
1.00
41.39
8


6217
OW0
WAT
V
775
13.803
67.385
57.044
1.00
41.01
8


6218
OW0
WAT
V
776
11.356
101.651
18.715
1.00
42.40
8


6219
OW0
WAT
V
777
50.379
57.839
57.286
1.00
38.80
8


6220
OW0
WAT
V
778
9.739
81.288
44.991
1.00
38.14
8


6221
OW0
WAT
V
779
26.770
45.470
44.155
1.00
39.31
8


6222
OW0
WAT
V
780
51.219
61.900
12.424
1.00
42.17
8


6223
OW0
WAT
V
781
44.665
53.194
62.632
1.00
40.09
8


6224
OW0
WAT
V
782
−4.332
57.891
45.992
1.00
43.38
8


6225
OW0
WAT
V
783
54.313
63.995
27.513
1.00
40.34
8


6226
OW0
WAT
V
784
26.835
56.319
8.446
1.00
41.42
8


6227
OW0
WAT
V
785
53.198
59.584
25.852
1.00
42.12
8


6228
OW0
WAT
V
786
19.476
44.845
23.558
1.00
42.02
8


6229
OW0
WAT
V
787
21.294
88.109
18.755
1.00
42.02
8


6230
OW0
WAT
V
788
46.461
57.071
56.124
1.00
41.88
8


6231
OW0
WAT
V
789
52.975
62.124
50.393
1.00
41.59
8


6232
OW0
WAT
V
790
8.480
108.235
24.221
1.00
42.16
8


6233
OW0
WAT
V
791
18.517
78.200
51.474
1.00
42.31
8


6234
OW0
WAT
V
792
−5.150
51.726
49.471
1.00
40.85
8


6235
OW0
WAT
V
793
36.849
55.447
72.633
1.00
42.13
8


6236
OW0
WAT
V
794
37.563
79.694
42.494
1.00
41.67
8


6237
OW0
WAT
V
795
18.818
84.285
16.222
1.00
43.03
8


6238
OW0
WAT
V
796
36.451
82.759
13.933
1.00
41.71
8


6239
OW0
WAT
V
797
22.906
51.457
67.808
1.00
41.33
8


6240
OW0
WAT
V
798
1.528
102.171
36.053
1.00
41.41
8


6241
OW0
WAT
V
799
36.684
45.294
51.188
1.00
42.88
8


6242
OW0
WAT
V
800
14.017
67.414
9.706
1.00
41.87
8


6243
OW0
WAT
V
801
47.832
66.788
18.650
1.00
43.94
8


6244
OW0
WAT
V
802
34.436
88.324
36.102
1.00
43.03
8


6245
OW0
WAT
V
803
24.260
67.815
69.741
1.00
42.57
8


6246
OW0
WAT
V
804
13.129
74.685
52.293
1.00
42.14
8


6247
OW0
WAT
V
805
16.572
61.433
12.722
1.00
41.61
8


6248
OW0
WAT
V
806
46.827
51.429
47.524
1.00
42.73
8


6249
OW0
WAT
V
807
26.546
48.730
71.404
1.00
42.47
8


6250
OW0
WAT
V
808
33.308
76.572
61.813
1.00
42.82
8


6251
OW0
WAT
V
809
16.314
98.564
17.363
1.00
42.43
8


6252
OW0
WAT
V
810
47.038
73.620
61.642
1.00
43.62
8


6253
OW0
WAT
V
811
23.301
74.541
1.386
1.00
44.52
8


6254
OW0
WAT
V
812
23.719
88.481
37.683
1.00
40.46
8


6255
OW0
WAT
V
813
31.440
60.185
76.751
1.00
43.11
8


6256
OW0
WAT
V
814
16.573
101.550
19.316
1.00
43.14
8


6257
OW0
WAT
V
815
4.201
55.069
57.571
1.00
42.80
8


6258
OW0
WAT
V
816
−5.755
72.609
47.268
1.00
41.92
8


6259
OW0
WAT
V
817
23.802
106.033
28.040
1.00
42.13
8


6260
OW0
WAT
V
818
28.580
91.427
35.569
1.00
44.77
8


6261
OW0
WAT
V
819
−6.927
74.495
44.783
1.00
42.39
8


6262
OW0
WAT
V
820
42.898
80.745
21.282
1.00
42.72
8


6263
OW0
WAT
V
821
44.594
48.996
19.414
1.00
42.65
8


6264
OW0
WAT
V
822
22.357
66.608
68.417
1.00
43.63
8


6265
OW0
WAT
V
823
25.576
50.604
10.991
1.00
43.85
8


6266
OW0
WAT
V
824
47.220
77.741
25.726
1.00
44.91
8


6267
OW0
WAT
V
825
16.600
55.517
47.156
1.00
44.33
8


6268
OW0
WAT
V
826
1.892
50.074
39.116
1.00
42.83
8


6269
OW0
WAT
V
827
24.440
89.039
35.388
1.00
43.51
8


6270
OW0
WAT
V
828
21.480
53.418
43.918
1.00
43.38
8


6271
OW0
WAT
V
829
14.604
82.502
11.170
1.00
41.84
8


6272
OW0
WAT
V
830
14.875
62.765
14.779
1.00
42.12
8


6273
OW0
WAT
V
831
3.701
80.451
16.127
1.00
43.54
8


6274
OW0
WAT
V
832
48.724
69.957
34.245
1.00
43.72
8


6275
OW0
WAT
V
833
33.297
59.385
78.143
1.00
45.08
8


6276
OW0
WAT
V
834
17.544
53.593
51.513
1.00
46.32
8


6277
OW0
WAT
V
835
12.009
85.638
47.505
1.00
44.72
8


6278
OW0
WAT
V
836
12.936
54.854
19.146
1.00
42.89
8


6279
OW0
WAT
V
837
24.005
43.446
16.058
1.00
42.88
8


6280
OW0
WAT
V
838
2.563
57.015
61.406
1.00
42.80
8


6281
OW0
WAT
V
839
17.292
81.361
47.327
1.00
43.05
8


6282
OW0
WAT
V
840
26.973
97.353
24.292
1.00
42.44
8


6283
OW0
WAT
V
841
24.520
83.741
45.252
1.00
44.48
8


6284
OW0
WAT
V
842
40.943
89.452
22.148
1.00
43.11
8


6285
OW0
WAT
V
843
17.748
68.046
54.218
1.00
43.50
8


6286
OW0
WAT
V
844
53.072
63.513
23.413
1.00
44.03
8


6287
OW0
WAT
V
845
−1.018
97.468
34.805
1.00
44.47
8


6288
OW0
WAT
V
846
14.885
69.989
10.290
1.00
44.92
8


6289
OW0
WAT
V
847
15.800
50.802
20.677
1.00
46.01
8


6290
OW0
WAT
V
848
25.982
102.118
29.899
1.00
44.94
8


6291
OW0
WAT
V
849
0.247
52.205
55.531
1.00
45.62
8


6292
OW0
WAT
V
850
18.884
61.154
6.132
1.00
44.78
8


6293
OW0
WAT
V
851
11.959
71.909
12.344
1.00
44.89
8


6294
OW0
WAT
V
852
−1.246
74.512
28.721
1.00
43.38
8


6295
OW0
WAT
V
853
39.883
48.418
12.157
1.00
44.97
8


6296
OW0
WAT
V
854
25.484
65.082
75.271
1.00
40.98
8


6297
OW0
WAT
V
855
31.943
70.931
74.851
1.00
43.51
8


6298
OW0
WAT
V
856
35.277
49.445
9.697
1.00
45.37
8


6299
OW0
WAT
V
857
51.902
64.035
51.472
1.00
44.46
8


6300
OW0
WAT
V
858
5.381
94.650
19.292
1.00
45.20
8


6301
OW0
WAT
V
859
14.161
52.807
19.941
1.00
44.99
8


6302
OW0
WAT
V
860
0.976
49.582
46.683
1.00
45.54
8


6303
OW0
WAT
V
861
11.378
56.649
26.955
1.00
46.98
8


6304
OW0
WAT
V
862
23.725
48.499
52.657
1.00
43.58
8


6305
OW0
WAT
V
863
31.619
53.767
4.982
1.00
44.03
8


6306
OW0
WAT
V
864
21.564
85.158
16.121
1.00
46.34
8


6307
OW0
WAT
V
865
48.454
57.833
31.207
1.00
45.05
8


6308
OW0
WAT
V
866
13.820
78.070
11.134
1.00
47.52
8


6309
OW0
WAT
V
867
53.268
61.611
27.715
1.00
45.47
8


6310
OW0
WAT
V
868
40.661
42.455
21.732
1.00
43.57
8


6311
OW0
WAT
V
869
24.881
97.609
17.754
1.00
41.56
8


6312
OW0
WAT
V
870
46.779
45.863
33.183
1.00
38.06
8


6313
OW0
WAT
V
871
28.449
47.238
49.410
1.00
44.98
8


6314
OW0
WAT
V
872
31.691
90.618
16.034
1.00
45.59
8


6315
OW0
WAT
V
873
45.269
73.271
25.041
1.00
46.87
8


6316
OW0
WAT
V
874
18.096
50.245
53.261
1.00
45.09
8


6317
OW0
WAT
V
875
−5.062
64.679
39.520
1.00
44.00
8


6318
OW0
WAT
V
876
17.006
54.092
49.423
1.00
46.50
8


6319
OW0
WAT
V
877
39.580
64.107
77.580
1.00
45.16
8


6320
OW0
WAT
V
878
16.405
56.330
66.595
1.00
44.67
8


6321
OW0
WAT
V
879
28.253
74.829
0.308
1.00
44.14
8


6322
OW0
WAT
V
880
26.165
96.027
33.730
1.00
45.73
8


6323
OW0
WAT
V
881
25.024
94.673
31.684
1.00
45.30
8


6324
OW0
WAT
V
882
6.382
101.590
23.078
1.00
45.88
8


6325
OW0
WAT
V
883
20.784
106.032
25.469
1.00
44.92
8


6326
OW0
WAT
V
884
15.678
70.001
59.741
1.00
47.72
8


6327
OW0
WAT
V
885
43.426
78.175
61.043
1.00
46.23
8


6328
OW0
WAT
V
886
10.651
50.358
43.666
1.00
45.79
8


6329
OW0
WAT
V
887
0.918
49.811
54.685
1.00
45.38
8


6330
OW0
WAT
V
888
24.371
106.460
30.607
1.00
46.20
8


6331
OW0
WAT
V
889
7.425
93.590
16.782
1.00
45.79
8


6332
OW0
WAT
V
890
20.314
66.093
66.469
1.00
48.35
8


6333
OW0
WAT
V
891
12.244
93.829
44.935
1.00
47.03
8


6334
OW0
WAT
V
892
2.847
56.085
32.137
1.00
48.09
8


6335
OW0
WAT
V
893
15.592
72.473
53.588
1.00
46.24
8


6336
OW0
WAT
V
894
45.552
49.673
29.081
1.00
46.73
8


6337
OW0
WAT
V
895
48.867
72.566
56.249
1.00
45.76
8


6338
OW0
WAT
V
896
51.123
56.932
37.786
1.00
40.59
8


6339
OW0
WAT
V
897
30.394
49.733
9.142
1.00
48.10
8


6340
OW0
WAT
V
898
27.101
98.920
22.257
1.00
46.90
8


6341
OW0
WAT
V
899
14.712
51.617
24.308
1.00
47.17
8


6342
OW0
WAT
V
900
46.781
50.533
27.214
1.00
47.00
8


6343
OW0
WAT
W
1
−6.114
65.250
32.669
1.00
47.96
8


6344
OW0
WAT
W
2
47.645
71.480
60.598
1.00
45.49
8


6345
OW0
WAT
W
3
48.802
54.151
54.398
1.00
46.37
8


6346
OW0
WAT
W
4
4.605
105.268
26.990
1.00
46.92
8


6347
OW0
WAT
W
5
42.143
73.136
41.061
1.00
45.02
8


6348
OW0
WAT
W
6
26.105
89.154
41.563
1.00
47.90
8


6349
OW0
WAT
W
7
3.202
48.853
55.140
1.00
47.23
8


6350
OW0
WAT
W
8
−2.318
61.724
33.458
1.00
48.00
8


6351
OW0
WAT
W
9
38.569
50.803
7.204
1.00
46.95
8


6352
OW0
WAT
W
10
2.160
103.336
25.390
1.00
47.08
8


6353
OW0
WAT
W
11
27.464
41.903
36.189
1.00
42.96
8


6354
OW0
WAT
W
12
49.209
50.152
22.583
1.00
48.25
8


6355
OW0
WAT
W
13
10.266
57.487
62.131
1.00
43.39
8


6356
OW0
WAT
W
14
54.127
66.185
63.244
1.00
49.78
8


6357
OW0
WAT
W
15
19.083
49.330
63.179
1.00
49.30
8


6358
OW0
WAT
W
16
39.385
74.287
38.793
1.00
46.50
8


6359
OW0
WAT
W
17
−1.255
52.062
41.948
1.00
49.09
8


6360
OW0
WAT
W
18
16.630
69.708
8.569
1.00
48.63
8


6361
OW0
WAT
W
19
29.289
54.314
9.208
1.00
49.09
8


6362
OW0
WAT
W
20
38.590
83.950
31.916
1.00
48.14
8


6363
OW0
WAT
W
21
47.212
44.923
37.558
1.00
49.07
8


6364
OW0
WAT
W
22
2.016
104.557
33.998
1.00
50.31
8


6365
OW0
WAT
W
23
5.910
79.410
15.810
1.00
46.74
8


6366
OW0
WAT
W
24
18.824
46.920
16.693
1.00
44.54
8


6367
OW0
WAT
W
25
21.253
90.457
18.335
1.00
47.12
8


6368
OW0
WAT
W
26
46.674
72.576
34.746
1.00
48.69
8


6369
OW0
WAT
W
27
17.804
54.470
14.884
1.00
50.05
8


6370
OW0
WAT
W
28
−3.319
64.779
54.655
1.00
49.95
8


6371
OW0
WAT
W
29
20.035
59.810
69.328
1.00
47.36
8


6372
OW0
WAT
W
30
6.598
98.214
19.529
1.00
50.29
8


6373
OW0
WAT
W
31
29.388
57.634
5.275
1.00
49.23
8


6374
OW0
WAT
W
32
25.881
83.371
49.453
1.00
49.89
8


6375
OW0
WAT
W
33
46.828
48.534
13.616
1.00
48.17
8


6376
OW0
WAT
W
34
52.912
62.999
14.852
1.00
46.56
8


6377
OW0
WAT
W
35
2.107
83.103
18.070
1.00
48.10
8


6378
OW0
WAT
W
36
41.486
67.797
7.736
1.00
50.23
8


6379
OW0
WAT
W
37
9.492
94.962
15.817
1.00
48.00
8


6380
OW0
WAT
W
38
28.348
95.134
21.001
1.00
48.19
8


6381
OW0
WAT
W
39
32.401
92.434
25.439
1.00
50.58
8


6382
OW0
WAT
W
40
46.035
46.956
48.050
1.00
50.92
8


6383
OW0
WAT
W
41
34.909
51.572
71.159
1.00
49.38
8


6384
OW0
WAT
W
42
29.114
76.486
61.672
1.00
49.83
8


6385
OW0
WAT
W
43
−3.044
91.942
40.975
1.00
51.92
8


6386
OW0
WAT
W
44
−3.395
74.451
28.328
1.00
46.84
8


6387
OW0
WAT
W
45
20.187
89.421
44.602
1.00
49.88
8


6388
OW0
WAT
W
46
−4.080
54.699
41.545
1.00
50.13
8


6389
OW0
WAT
W
47
38.425
87.733
31.621
1.00
49.47
8


6390
OW0
WAT
W
48
4.305
62.413
62.323
1.00
49.60
8


6391
OW0
WAT
W
49
6.229
89.367
44.095
1.00
53.06
8


6392
OW0
WAT
W
50
49.747
66.902
23.155
0.00
51.47
8


6393
OW0
WAT
W
51
40.855
78.417
26.292
1.00
48.79
8


6394
OW0
WAT
W
52
17.489
50.714
66.895
1.00
52.19
8


6395
OW0
WAT
W
53
34.327
92.622
27.782
1.00
49.40
8


6396
OW0
WAT
W
54
49.464
48.219
14.354
1.00
55.58
8


6397
OW0
WAT
W
55
−2.823
49.394
48.028
1.00
50.11
8


6398
OW0
WAT
W
56
22.263
105.611
23.242
1.00
50.89
8


6399
OW0
WAT
W
57
16.395
51.479
56.998
1.00
54.48
8


6400
OW0
WAT
W
58
46.461
51.028
12.082
1.00
51.52
8


6401
OW0
WAT
W
59
35.996
61.651
5.602
1.00
53.96
8


6402
OW0
WAT
W
60
25.277
46.888
50.958
1.00
53.30
8


6403
OW0
WAT
W
61
15.763
94.604
17.487
1.00
49.77
8


6404
OW0
WAT
W
62
42.937
61.534
7.934
1.00
47.74
8


6405
OW0
WAT
W
63
24.840
46.516
44.072
1.00
51.69
8


6406
OW0
WAT
W
64
29.111
92.028
40.197
1.00
48.35
8


6407
OW0
WAT
W
65
4.689
89.221
19.393
1.00
50.44
8


6408
OW0
WAT
W
66
11.456
93.383
15.046
1.00
58.07
8


6409
OW0
WAT
W
67
15.227
108.500
35.816
1.00
52.43
8


6410
OW0
WAT
W
68
42.860
74.904
32.815
1.00
52.70
8


6411
OW0
WAT
W
69
48.829
69.006
23.605
1.00
55.19
8


6412
OW0
WAT
W
70
15.485
68.666
11.962
1.00
52.48
8


6413
OW0
WAT
W
71
−5.047
98.836
30.411
1.00
52.33
8


6414
OW0
WAT
W
72
38.899
69.928
3.024
1.00
53.43
8


6415
OW0
WAT
W
73
47.563
47.253
16.948
1.00
53.16
8


6416
OW0
WAT
W
74
8.621
51.721
57.810
1.00
51.63
8


6417
OW0
WAT
W
75
52.887
59.020
49.147
1.00
50.28
8


6418
OW0
WAT
W
76
4.037
61.529
30.846
1.00
54.62
8


6419
OW0
WAT
W
77
4.332
83.232
16.091
1.00
55.82
8


6420
OW0
WAT
W
78
36.037
53.977
74.978
1.00
55.15
8


6421
OW0
WAT
W
79
51.512
53.978
47.701
0.00
54.18
8


6422
OW0
WAT
W
80
14.797
91.920
17.273
1.00
51.87
8


6423
OW0
WAT
W
81
19.801
84.369
8.356
1.00
55.63
8


6424
OW0
WAT
W
82
31.496
46.252
52.107
1.00
55.15
8


6425
OW0
WAT
W
83
−1.823
79.829
19.762
1.00
53.76
8


6426
OW0
WAT
W
84
29.256
92.834
20.731
1.00
53.49
8


6427
OW0
WAT
W
85
−1.824
76.279
32.563
1.00
55.76
8


6428
OW0
WAT
W
86
32.061
46.088
49.588
1.00
55.95
8


6429
OW0
WAT
W
87
41.327
42.439
33.669
1.00
55.86
8


6430
OW0
WAT
W
88
43.153
80.324
3.532
1.00
52.67
8


6431
OW0
WAT
W
89
47.799
76.801
61.841
1.00
55.93
8


6432
OW0
WAT
W
90
35.708
85.333
37.348
1.00
54.64
8


6433
OW0
WAT
W
91
52.110
65.452
56.038
1.00
53.77
8


6434
OW0
WAT
W
92
16.996
79.167
47.458
1.00
56.65
8


6435
OW0
WAT
W
93
27.626
49.502
11.515
1.00
60.46
8


6436
OW0
WAT
W
94
29.317
47.547
14.906
1.00
61.23
8


6437
OW0
WAT
W
95
51.306
65.455
30.794
0.00
67.31
8


6438
OW0
WAT
W
96
21.436
52.799
12.475
1.00
60.39
8


6439
OW0
WAT
W
97
24.857
50.122
68.228
1.00
61.97
8


6440
OW0
WAT
W
98
53.436
60.942
47.809
1.00
59.88
8


6441
OW0
WAT
W
99
26.545
99.863
28.613
1.00
66.13
8


6442
OW0
WAT
W
100
28.187
94.100
34.809
1.00
47.55
8


6443
OW0
WAT
W
101
46.501
68.477
9.327
1.00
62.49
8


6444
OW0
WAT
W
102
41.335
80.622
32.546
1.00
56.46
8


6445
OW0
WAT
W
103
49.090
47.019
29.937
1.00
51.60
8


6446
OW0
WAT
W
104
29.677
70.505
75.480
1.00
55.52
8


6447
OW0
WAT
W
105
10.580
70.552
56.020
1.00
45.60
8


6448
OW0
WAT
W
106
−5.437
61.460
36.195
1.00
49.58
8


6449
OW0
WAT
W
107
41.636
42.378
28.372
1.00
47.73
8


6450
OW0
WAT
W
108
48.134
51.375
29.584
1.00
53.67
8


6451
OW0
WAT
W
109
20.029
46.534
41.141
1.00
45.69
8


6452
OW0
WAT
W
110
39.076
61.857
77.827
1.00
61.24
8


6453
OW0
WAT
W
111
40.140
79.602
28.296
1.00
58.08
8


6454
OW0
WAT
W
112
24.479
41.686
38.003
1.00
48.71
8


6455
OW0
WAT
W
113
18.748
86.522
18.736
1.00
54.95
8


6456
OW0
WAT
W
114
26.670
86.155
43.878
1.00
45.83
8


6457
OW0
WAT
W
115
34.014
44.101
58.947
1.00
55.80
8


6458
OW0
WAT
W
116
44.085
44.358
32.579
1.00
66.42
8


6459
OW0
WAT
W
117
2.549
102.526
41.260
1.00
56.37
8


6460
OW0
WAT
W
118
10.042
59.115
64.251
1.00
53.53
8


6461
OW0
WAT
W
119
52.498
59.271
37.676
1.00
46.44
8


6462
OW0
WAT
W
120
49.412
68.479
30.738
0.00
48.32
8


6463
OW0
WAT
W
121
39.604
81.174
29.899
1.00
40.72
8


6464
OW0
WAT
W
122
52.578
62.726
30.463
0.00
55.27
8


6465
OW0
WAT
W
123
32.284
38.992
32.423
1.00
44.19
8


6466
OW0
WAT
W
124
54.342
58.298
13.900
1.00
48.84
8


6467
OW0
WAT
W
125
53.831
60.018
17.609
1.00
53.12
8


6468
OW0
WAT
W
126
37.548
48.910
67.790
1.00
63.29
8


6469
OW0
WAT
W
127
16.364
67.201
64.210
1.00
54.77
8


6470
OW0
WAT
W
128
35.507
88.726
18.930
1.00
44.18
8


6471
OW0
WAT
W
129
49.585
56.011
59.240
1.00
44.54
8


6472
OW0
WAT
W
130
13.470
54.095
28.765
1.00
39.17
8


6473
OW0
WAT
W
131
11.141
90.680
16.198
1.00
49.46
8


6474
OW0
WAT
W
132
−9.184
65.150
46.616
1.00
52.99
8


6475
OW0
WAT
W
133
44.910
67.182
7.757
1.00
52.67
8


6476
OW0
WAT
W
134
38.968
68.370
71.252
1.00
37.18
8


6477
OW0
WAT
W
135
9.962
106.661
35.598
1.00
48.81
8


6478
OW0
WAT
W
136
−0.018
83.329
37.562
1.00
49.93
8


6479
OW0
WAT
W
137
6.077
95.625
42.890
1.00
41.31
8


6480
OW0
WAT
W
138
38.033
48.935
8.928
1.00
56.21
8


6481
OW0
WAT
W
139
22.720
48.167
43.406
1.00
43.05
8


6482
OW0
WAT
W
140
16.160
51.440
42.398
1.00
42.33
8


6483
OW0
WAT
W
141
51.286
65.520
30.747
0.00
58.93
8


6484
OW0
WAT
W
142
22.870
83.783
−0.279
1.00
39.91
8


6485
OW0
WAT
W
143
23.492
85.411
14.742
1.00
45.55
8


6486
OW0
WAT
W
144
30.609
38.135
34.869
1.00
53.23
8


6487
OW0
WAT
W
145
51.546
53.971
47.725
0.00
54.90
8


6488
OW0
WAT
W
146
37.344
40.493
33.234
1.00
46.02
8


6489
OW0
WAT
W
147
35.805
47.572
62.190
1.00
53.24
8


6490
OW0
WAT
W
148
32.439
62.293
76.111
1.00
52.51
8


6491
OW0
WAT
W
149
24.077
90.751
37.673
1.00
48.00
8


6492
OW0
WAT
W
150
20.655
50.869
68.464
1.00
51.34
8


6493
OW0
WAT
W
151
42.359
76.800
31.368
1.00
54.68
8


6494
OW0
WAT
W
152
40.991
84.869
28.522
1.00
51.94
8


6495
OW0
WAT
W
153
−3.448
59.486
34.298
1.00
60.14
8


6496
OW0
WAT
W
154
24.275
50.044
65.629
1.00
48.99
8


6497
OW0
WAT
W
155
24.898
47.635
57.042
1.00
50.00
8


6498
OW0
WAT
W
156
46.911
73.376
32.086
1.00
65.97
8


6499
OW0
WAT
W
157
12.448
63.643
14.806
1.00
50.68
8


6500
OW0
WAT
W
158
17.367
83.516
7.750
1.00
59.03
8


6501
OW0
WAT
W
159
38.537
87.429
19.244
1.00
48.05
8


6502
OW0
WAT
W
160
49.397
68.482
30.753
0.00
47.12
8


6503
OW0
WAT
W
161
52.562
62.737
30.460
0.00
55.04
8


6504
OW0
WAT
W
162
17.100
92.730
17.506
1.00
48.89
8


6505
OW0
WAT
W
163
54.143
65.666
53.272
1.00
49.78
8


6506
OW0
WAT
W
164
35.140
89.217
21.335
0.00
49.55
8


6507
OW0
WAT
W
165
40.864
85.144
25.201
1.00
51.96
8


6508
OW0
WAT
W
166
0.129
71.062
53.859
1.00
50.46
8


6509
OW0
WAT
W
167
19.749
95.732
16.395
1.00
54.02
8


6510
OW0
WAT
W
168
45.089
55.696
66.763
1.00
48.69
8


6511
OW0
WAT
W
169
29.920
93.952
27.969
1.00
57.82
8


6512
OW0
WAT
W
170
−1.140
103.281
29.038
1.00
59.68
8


6513
OW0
WAT
W
171
0.493
67.332
27.261
1.00
46.75
8


6514
OW0
WAT
W
172
11.663
49.273
52.961
1.00
47.65
8


6515
OW0
WAT
W
173
19.395
43.670
27.526
0.00
52.64
8


6516
OW0
WAT
W
174
12.558
73.429
10.221
1.00
52.09
8


6517
OW0
WAT
W
175
47.725
72.168
25.475
1.00
55.03
8


6518
OW0
WAT
W
176
37.354
46.525
53.992
1.00
62.86
8


6519
OW0
WAT
W
177
6.566
77.689
48.060
1.00
54.04
8


6520
OW0
WAT
W
178
27.239
80.756
54.362
1.00
54.49
8


6521
OW0
WAT
W
179
29.136
79.115
59.854
1.00
51.47
8


6522
OW0
WAT
W
180
51.301
65.512
30.778
1.00
58.87
8


6523
OW0
WAT
W
181
49.729
67.077
23.232
1.00
50.64
8


6524
OW0
WAT
W
182
15.428
63.127
65.725
1.00
53.21
8


6525
OW0
WAT
W
183
28.316
47.473
59.001
1.00
52.58
8


6526
OW0
WAT
W
184
11.167
50.777
21.789
1.00
55.21
8


6527
OW0
WAT
W
185
39.667
45.779
11.484
1.00
50.46
8


6528
OW0
WAT
W
186
9.302
78.481
48.408
1.00
50.14
8


6529
OW0
WAT
W
187
−2.511
95.777
25.082
1.00
50.26
8


6530
OW0
WAT
W
188
49.525
52.221
41.616
1.00
53.78
8


6531
OW0
WAT
W
189
33.219
90.787
32.195
1.00
53.22
8


6532
OW0
WAT
W
190
18.629
63.971
67.355
1.00
54.97
8


6533
OW0
WAT
W
191
6.996
55.402
34.790
1.00
49.49
8


6534
OW0
WAT
W
192
50.269
70.807
60.070
1.00
54.80
8


6535
OW0
WAT
W
193
−3.948
89.479
31.518
0.00
54.80
8


6536
OW0
WAT
W
194
4.036
51.795
57.529
1.00
56.49
8


6537
OW0
WAT
W
195
15.790
48.084
23.036
1.00
52.39
8


6538
OW0
WAT
W
196
22.577
105.708
45.361
1.00
51.14
8


6539
OW0
WAT
W
197
7.453
103.921
23.508
1.00
50.15
8


6540
OW0
WAT
W
198
37.899
80.588
45.384
1.00
52.20
8


6541
OW0
WAT
W
199
19.774
74.879
53.890
1.00
55.07
8


6542
OW0
WAT
W
200
50.055
68.873
30.956
1.00
30.00
8


6543
OW0
WAT
W
201
53.330
63.201
30.956
1.00
37.00
8


6544
OW0
WAT
W
202
35.086
89.130
21.284
1.00
49.00
8


6545
OW0
WAT
W
203
2.339
51.858
35.796
1.00
50.00
8


6546
OW0
WAT
W
204
19.180
43.755
27.572
1.00
50.00
8


6547
OW0
WAT
W
205
51.693
55.504
46.921
1.00
51.00
8


6548
OW0
WAT
W
206
31.811
80.217
54.661
1.00
51.00
8


6549
OW0
WAT
W
207
11.695
77.786
12.093
1.00
51.00
8


6550
OW0
WAT
W
208
29.940
46.996
53.693
1.00
52.00
8


6551
OW0
WAT
W
209
7.251
102.500
40.633
1.00
52.00
8


6552
OW0
WAT
W
210
23.858
91.561
17.414
1.00
52.00
8


6553
OW0
WAT
W
211
6.783
49.832
40.633
1.00
52.00
8


6554
OW0
WAT
W
212
44.910
47.806
22.735
1.00
52.00
8


6555
OW0
WAT
W
213
36.255
46.591
10.158
1.00
52.00
8


6556
OW0
WAT
W
214
27.601
61.581
77.880
1.00
52.00
8


6557
OW0
WAT
W
215
27.133
98.043
33.861
1.00
53.00
8


6558
OW0
WAT
W
216
18.479
55.504
45.470
1.00
53.00
8


6559
OW0
WAT
W
217
9.122
47.401
46.438
1.00
53.00
8


6560
OW0
WAT
W
218
9.590
66.037
16.447
1.00
53.00
8


6561
OW0
WAT
W
219
13.333
91.966
46.438
1.00
53.00
8

## Claims

1. A method of producing a variant of a parent maltogenic alpha-amylase, said method comprising
a) modeling the parent alpha-amylase on the three-dimensional structure of SEQ ID NO: depicted in the Appendix to produce a three-dimensional structure of the parent alpha-amylase;
b) identifying in the three-dimensional structure obtained in step (a) at least one structural part of the parent wherein an alteration in said structural part is predicted to result in said altered property;
c) modifying the sequence of a nucleic acid encoding the parent alpha-amylase to produce a nucleic acid encoding a deletion, insertion, or substitution of one or more amino acids at a position corresponding to said structural part; and
d) expressing the modified nucleic acid in a host cell to produce the variant alpha-amylase,
wherein the variant has alpha-amylase enzymatic activity and has at least one altered property relative to the parent.

2. The method of claim 1, wherein the altered property is pH dependent activity, thermostability, substrate cleavage pattern, specific activity of cleavage, transglycosylation, ability to reduce retrogradation of starch, ability to reduce staling of bread, substrate specificity, substrate binding or calcium binding.

3. A method of constructing a variant of a parent maltogenicalpha-amylase, which method comprises:
(a) identifying an internal cavity or crevice in the three-dimensional structure of said parent;
(b) substituting an amino acid residue in the neighborhood of the cavity or crevice with another amino acid residue which increases the hydrophobic interaction and/or fills out or reduces the size of the cavity or crevice;
(c) optionally repeating steps a) and b) recursively;
(d) optionally, making alterations each of which is an insertion, a deletion or a substitution of an amino acid residue at one or more positions other than b),
(e) preparing the variant resulting from steps a)-d);
(f) testing the thermostability of said variant; and
(g) optionally repeating steps a)-f) recursively; and
(h) selecting a variant having increased thermostability as compared to the parent amylase.

4. The method of claim 3, wherein the substitution of the amino acid residue results in increasing the hydrophobic interaction, substitution with proline, substitution of histidine with another amino acid, stabilization of calcium binding, introduction of an interdomain disulfide bond, removal of a deamidation site, altering a hydrogen bond contact, filling in an internal structural cavity with an amino acid with a bulkier side group, introduction of interdomain interactions, altering charge distribution, helix capping, or introduction of a salt bridge.

5. A method of constructing a variant of a parent maltogenic alpha-amylase, which method comprises:
(a) identifying an amino acid residue within 10 Å from a calcium binding site in the three dimensional structure of the amylase;
(b) substituting the amino acid residue with another amino acid residue so as to improve the interaction with the calcium ion;
(c) optionally repeating steps a) and b) recursively;
(d) optionally, making alterations each of which is an insertion, a deletion or a substitution of an amino acid residue at one or more positions other than b),
(e) preparing the variant resulting from steps a)-d);
(f) testing the thermostability of said variant; and
(g) optionally repeating steps a) f) recursively; and
(h) selecting a variant having increased thermostability as compared to the parent amylase.

6. A method of constructing a variant of a parent maltogenic alpha-amylase, which method comprises:
(a) identifying the substrate binding area in a model of the three-dimensional structure of the parent amylase;
(b) modifying the substrate binding area by an amino acid substitution, deletion or insertion;
(c) optionally repeating step b) recursively;
(d) optionally, making alterations each of which is an insertion, a deletion or a substitution of an amino acid residue at one or more positions other than b),
(e) preparing the variant resulting from steps a)-d);
(f) testing the substrate-cleavage pattern of the variant,
(g) optionally repeating steps a)-f) recursively; and
(h) selecting a variant having an altered substrate-cleavage pattern as compared to the parent amylase.