A METHOD OF DESIGNING ALPHA-AMYLASE MUTANTS WITH PREDETERMINED PROPERTIES

Abstract: A method of constructing a variant of a parent Termamyl-like alpha -amylase, which variant has alpha -amylase activity and at least one altered property as compared to the parent alpha -amylase, comprises i) analysing the structure of the parent Termamyl-like alpha -amylase to identify at least one amino acid residue or at least one structural part of the Termamyl-like alpha -amylase structure, which amino acid residue or structural part is believed to be of relevance for altering the property of the parent Termamyl-like alpha -amylase (as evaluated on the basis of structural or functional considerations), ii) constructing a Termamyl-like alpha -amylase variant, which as compared to the parent Termamyl-like alpha -amylase, has been modified in the amino acid residue or structural part identified in i) so as to alter the property, and iii) testing the resulting Termamyl-like alpha -amylase variant for the property in question.

Description: A METHOD OF DESIGNING ALPHA-AMYLASE MUTANTS WITH PREDETERMINED PROPERTIES FIELD OF THE INVENTION 5 The present invention relates to a novel method of designing α- amylase mutants with predetermined properties, which method is based on the hitherto unknown three-dimensional structure of bacterial α-amylases. 10 BACKGROUND OF THE INVENTION α-Amylases (α-1.4 glucan-4-glucanohydrolase, EC 3.2.1.1) constitute a group of enzymes which is capable of hydrolyzing starch and other linear and branched 1,4-glucosidic oligo- and is polysaccharides. Almost all α-amylases studied have a few conserved regions with approximately the same length and spacing. One of these regions resembles the Ca2+ binding site of cal odulin and the others are thought to be necessary for the active centre and/or binding of the substrate. 20 While the amino acid sequence and thus primary structure of a large number of α-amylases are known, it has proved very difficult to determine the three-dimensional structure of all α-amylases. The three-dimensional structure can be determined 25 by X-ray crystallographic analysis of α-amylase crystals, but it has proven difficult to obtain αr-amylase crystals suitable for actually solving the structure. Until now the three-dimensional structure of only a few 30 α-amylases have been determined at high resolution. These include the structure of the Aspergill us oryzae TAKA α-amylase (Swift et al. , 1991), the Aspergillus niger acid a ylase (Brady et al, 1991) , the structure of pig pancreatic α-amylase (Qian et al. , 1993), and the barley alpha-amylase (Kadziola et al. 35 1994, Journal of Molecular Biology 239: 104-121, A.Kadziola, Thesis, Dept of Chemistry, U. of Copenhagen, Denmark) . Furthermore, the three-dimensional structure of a Bacillus circulans cyclodextrin glycoεyltransferase (CGTase) is known (Klein et al., 1992) (Lawson et al. , 1994) . The CGT catalyzes the same type of reactions as α-amylases and exhib some structural resemblance with α-amylases. Furthermore, crystallization and preliminary X-ray studies B . subtilis α-amylases have been described (Chang et al. (19 and Mizuno et al. (1993)). No final B . subtilis structure been reported. Analogously, the preparation of B . lichenifor α-amylase crystals has been reported (Suzuki et al. (1990) , no subsequent report on X-ray crystallographic analysis three-dimensional structure are available. Several research teams have attempted to bui three-dimensional structures on the basis of the above kno α-amylase structures. For instance, Vihinen et al. (J. Bioche 107, 267-272, 1990), disclose the modelling (or comput simulation) of a three-dimensional structure of the Bacill stearothermophiluε α-amylase on the basis of the TAKA amyla structure. The model was used to investigate hypothetic structural consequences of various site-directed mutations the B . stearothermophilus α-amylase. E.A. MacGregor (198 predicts the presence of α-helices and β-barrels in α-amylas from different sources, including barley, pig pancreas a Bacillus amyloliquefaciens on the basis of the known structu of the A. oryzae TAKA α-amylase and secondary structu predicting algorithms. Furthermore, the possible loops a subsites which may be found to be present in, e.g., the amyloliquefaciens α-amylase are predicted (based on comparison with the A . oryzae sequence and structure) . A.E. MacGregor (Starch/Starke 45 (1993), No. 7, p. 232-23 presents a review of the relationship between the structure a activity of α-amylase related enzymes. Hitherto, no three-dimensional structure has been available f the industrially important Bacillus α-amylases (which in t oreser.t context are termed "Termamyl-like α-amylases") including the B. licheniformis, the B . amyloliquefaciens, and the B. stearothermophilus α-amylase. BRIEF DISCLOSURE OF THE INVENTION The three-dimensional structure of a Termamyl-like bacterial α-amylase has now been elucidated. On the basis of an analysis of said structure it is possible to identify structural parts or specific amino acid residues which from structural or functional considerations appear to be important for conferring the various properties to the Termamyl-like α-amylases. Furthermore, when comparing the Termamyl-like α-amylase structure with known structures of the fungal and mammalian α-amylases mentioned above, it has been found that some similarities exist between the structures, but also that some striking, and not previously predicted structural differences between the α-amylases exist. The present invention is based on these findings. Accordingly, in a first aspect the invention relates to a method of constructing a variant of a parent Termamyl-like α- amylase, which variant has α-amylase activity and at least one altered property as compared to said parent α-amylase, which method comprises i) analysing the structure of the Termamyl-like α-amylase with a view to identifying at least one amino acid residue or at least one structural part of the Termamyl-like α-amylase structure, which amino acid residue or structural part is believed to be of relevance for altering said property of the parent Termamyl-like α-amylase (as evaluated on the basis of structural or functional considerations) , ii) constructing a Termamyl-like α-amylase variant, which as compared to the parent Termamyl-like α-amylase, 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 Termamyl-like α-amylase variant said property. In a second aspect the present invention relates to a method constructing a variant of a parent Termamyl-like α-amyla which variant has α-amylase activity and one or more alte properties as compared to said parent α-amylase, which met comprises i) comparing the three-dimensional structure of the Termam like α-amylase with the structure of a non-Termamyl-like amylase, ii) identifying a part of the Termamyl-like α-amylase structu which is different from the non-Termamyl-like α-amyla structure, and iii) modifying the part of the Termamyl-like α-amyla identified in ii) whereby a Termamyl-like α-amylase variant obtained, one or more properties of which differ from the parent Termamyl-like α-amylase. In a third aspect the invention relates to a method constructing a variant of a parent non-Termamyl-like α-amylas which variant has α-amylase activity and one or more alter properties as compared to said parent α-amylase, which meth comprises i) comparing the three-dimensional structure of the no Termamyl-like α-amylase with the structure of a Termamyl-li α-amylase, ii) identifying a part of the non-Termamyl-like α-amyla structure which is different from the Termamyl-like α-amyla structure, and iii) modifying the part of the non-Termamyl-like α-amyla identified in ii) whereby a non-Termamyl-like α-amylase varia is obtained, one or more properties of which differ from t parent Termamyl-like α-amylase. The property which may be altered by the above methods of t present: invention may, e.g., be substrate specificit substrate binding, substrate cleavage pattern, temperature stability, pH dependent activity, pH dependent stability (especially increased stability at low (e.g. pH<6, in particular pH<5) or high (e.g. pH>9) pH values), stability towards oxidation, Ca 2* -dependency, specific activity, and other properties of interest. For instance, the alteration may result in a variant which, as compared to the parent Termamyl-like α- a ylase, has an increased specific activity at a given pH and/or an altered substrate specificity. 10 In still further aspects the invention relates to variants of a Termamyl-like α-amylase, DNA encoding such variants and methods of preparing the variants. Finally, the invention relates to the use of the variants for various industrial is purposes. DETAILED DISCLOSURE OF THE INVENTION The Termamyl-like α-amylase 20 It is well known that a number of alpha-amylases produced by Bacillus spp. are highly homologous on the amino acid level. For instance, the B . licheniformis α-amylase comprising the amino acid sequence shown in SEQ ID No. 2 (commercially 25 available as Termamyl ® ) has been found to be about 89% homologous with the B . amyloliquefaciens α-amylase comprising the amino acid sequence shown in SEQ ID No. 4 and about 79% homologous with the B. stearothermophilus α-amylase comprising the amino acid sequence shown in SEQ ID No. 6. Further 30 homologous α-amylases include an α-amylase derived from a strain of the Bacillus sp. NCIB 12289, NCIB 12512, NCIB 12513 or DSM 9375, all of which are described in detail in WO 95/26397, and the α-amylase described by Tsukamoto et al., 1988, Biochemical and Biophysical Research Communications, Vol. 35 151, No. 1. Still other homologous α-amylases include the α- amylase produced by the B . licheniformis described in EP 252 666 (ATCC 27811) , and the α-amylases identified in WO 91/00353 and WO 94/18314. Other commercial Termamyl-like £. licheniformis α-amylases are Optitherm ® and Takather (available from Solvay) , Maxamyl ® (available from Gis brocades/Genencor) , Spezym AA ® (available from Genencor) , a Keistase ® (available from Daiwa) . Because of the substantial homology found between these amylases, they are considered to belong to the same class of amylases, namely the class of "Termamyl-like α-amylases". Accordingly, in the present context, the term "Termamyl-like amylase" is intended to indicate an α-amylase which, on t amino acid level, exhibits a substantial homology to Termamyl ® i.e. the B. licheniformis α-amylase SEQ ID NO 2. In othe words, a Termamyl-like α-amylase is an α-amylase, which has th amino acid sequence shown in SEQ ID No. 2, 4 or 6 herein, o the amino acid sequence shown in SEQ ID NO 1 or 2 of W 95/26397 or in Tsukamoto et al., 1988, or i) which displays a least 60%, such as at least 70%, e.g. at least 75%, or at leas 80%, e.g. at least 85%, at least 90% or at least 95% homolog with at least one of said amino acid sequences and/or ii displays immunological cross-reactivity with an antibody raise against at least one of said α-amylases, and/or iii) is encode by a DNA sequence which hybridizes to the DNA sequence encoding the above specified α-amylases which are apparent fro SEQ ID Nos. 1, 3 and 5 of the present application, and SEQ I NO 4 and 5 of WO 95/26397, respectively. In connection with property i) the "homology" may be determine by use of any conventional algorithm, preferably by use of th GAP progamme from the GCG package version 7.3 (June 1993) usin default values for GAP penalties (Genetic Computer Group (1991 Programme Manual for the GCG Package, version 7, 575 Scienc Drive, Madison, Wisconsin, USA 53711) . Property ii) of the α-amylase, i.e. the immunological cros reactivity, may be assayed using an antibody raised against o reactive with at least one epitope of the relevant Termamyl like α-arnylase. The antibody, which may either be monoclonal c polyclonal, may be produced by methods known in the art, e.g. as described by Hudson et al., 1989. The immunological cross- reactivity may be determined using assays known in the art, examples of which are Western Blotting or radial immunodif- fusion assay, e.g. as described by Hudson et al. , 1989. In this respect, immunological cross-reactivity between the α-amylases having the amino acid sequences SEQ ID Nos. 2, 4 and 6, respectively, has been found. The oligonucleotide probe used in the characterization of the Termamyl-like α-amylase in accordance with property iii) above may suitably be prepared on the basis of the full or partial nucleotide or amino acid sequence of the α-amylase in question. Suitable conditions for testing hybridization involve presoaking in 5xSSC and prehybridizing for lh at -40°C in a solution of 20% formamide, 5xDenhardt's solution, 50mM sodium phosphate, pH 6.8, and 50μg of denatured sonicated calf thymus DNA, followed by hybridization in the same solution supplemented with lOOμM ATP for 18h at -40°C, or other methods described by e.g. Sambrook et al., 1989. In the present context, "derived from" is intended not only to indicate an α-amylase produced or producible by a strain of the organism in question, but also an α-amylase encoded by a DNA sequence isolated from such strain and produced in a host or¬ ganism transformed with said DNA sequence. Finally, the term is intended to indicate an α-amylase which is encoded by a DNA sequence of synthetic and/or cDNA origin and which has the identifying characteristics of the α-amylase in question. The term is also intended to indicate that the parent α-amylase may be a variant of a naturally occurring α-amylase, i.e. a variant which is the result of a modification (insertion, substitution, deletion) of one or more amino acid residues of the naturally occurring α-amylase. Parent hybrid α-amylases The parent α-amylase (being a Termamyl-like or non-Termamy like α-amylase) may be a hybrid α-amylase, i.e. an α-amyla which comprises a combination of partial amino acid sequenc derived from at least two α-amylases. The parent hybrid α-amylase may be one which on the basis amino acid homology and/or immunological cross-reactivit and/or DNA hybridization (as defined above) can be determine to belong to the Termamyl-like α-amylase family. In this case the hybrid α-amylase is typically composed of at least one par of a Termamyl-like α-amylase and part(s) of one or more othe α-amylases selected from Termamyl-like α-amylases or non Termamyl-like α-amylases of microbial (bacterial or fungal and/or mammalian origin. Thus, the parent hybrid α-amylase may comprise a combination o at least two Termamyl-like α-amylases, or of at least on Termamyl-like and at least one non-Termamyl-like bacterial α amylase, or of at least one Termamyl-like and at least on fungal α-amylase. For instance, the parent α-amylase comprise a C-terminal part of an α-amylase derived from a strain of B licheniformis and a N-terminal part of an α-amylase derive from a strain of B . amyloliquefaciens or from a strain of B stearothermophilus . For instance, the parent α-amylas comprises at least 430 amino acid residues of the C-termina part of the B . licheniformis α-amylase, and may, e.g. compris a) an amino acid segment corresponding to the 37 N-termina amino acid residues of the B . amyloliquefaciens α-amylas having the amino acid sequence shown in SEQ ID No. 4 and a amino acid segment corresponding to the 445 C-terminal amin acid residues of the B . licheniformis α-a ylase having th amino acid sequence shown in SEQ ID No. 2, or b) an amino aci segment corresponding to the 68 N-terminal amino acid residue of the B . s tearothermophilus α-amylase having the amino aci seσuence shown in SEQ ID No. 6 and an amino acid segmen corresponding to the 415 C-terminal amino acid residues of th B . licheniformis α-amylase having the amino acid sequence shown in SEQ ID No. 2. Analogously, the parent hybrid α-amylase may belong to a non- Termamyl-like α-amylase family, e.g. the Fungamyl-like α- a ylase family. In that case the hybrid may comprise at least one part of an α-amylase belonging to the non-Termamyl-like α- amylase family in combination with one or more parts derived from other α-amylases. The three-dimensional Termamyl-like α-amylase structure The Termamyl-like α-amylase which was used to elucidate the three-dimensional structure forming the basis for the present invention consists of the 300 N-terminal amino acids of the B . amyloliquefaciens α-amylase (with the amino acid sequence shown in SEQ ID No. 4) and amino acids 301-483 of the C-terminal end of the B . licheniformis α-amylase with the amino acid sequence SEQ ID No. 2. The bacterial α-amylase belongs to the "Termamyl- like α-amylase family" and the present structure is believed to be representative for the structure of any Termamyl-like α- amylase. The structure of the α-amylase was solved in accordance with the principle for X-ray crystallographic methods 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 the α-amylase at 2.2 A resolution using the isomorphous replacement method are given in a standard PDB format (Brookhaven Protein Data Base) in Appendix 1. It is to be understood that Appendix 1 forms part of the present application. Amino acid residues of the enzyme are identified by three- letter amino acid code (capitalized letters) . The α-amylase structure is made up of three globular domains ordered A, B, and C with respect to sequence, which lie approximately along a line in the order B, A, C. The doma can be defined as being residues 1-103 and 206-395 for dom A, residues 104-205 for domain B, and residues 396-483 domain C, the numbers referring to the B. licheniformis amylase. This gives rise to an elongated molecule, the long axis being about 85A. The widest point perpendicular to t axis is approximately 50A and spans the central A domain. active site residues of the B . licheniformis α-amylase (SEQ NO 2) are D323, D231 and E261. Domain A Domain A is the largest domain and contains the active s (comprised of a cluster of three amino acid residues placed the bottom of a deep cleft in the enzyme's surface) . Domai of all known α-amylase structures have the same overall fo viz. the (beta/alpha) 8 barrel with 8 central beta stra (number 1-8) and 8 flanking α-helices. The /3-barrel is defi by McGregor pp. cit. The C-terminal end of Beta strand 1 connected to helix 1 by a loop denoted loop l and an identi pattern is found for the other loops. These loops show s variation in size and some can be quite extensive. The 8 central Beta-strands in the (beta/alpha) 8 bar superimpose well between the various known α-amyl structures, and this part of the structure, including the clo surroundings of the active site located at the c-terminal e of the beta-strands, show high similarity between the differe amylases. The loops connecting beta-strands and alpha helices displ high variations between alpha amylases. These loops constitu the structural context of the active site and the majority the contacts to the substrate is found among residues locat in these loops. Such important characteristics as substra specificity, substrate binding, pH/activity profile, star cleavage pattern are determined by the amino acids and t positions of same in these loops. The substantial differences between the Fungamyl-like α-amylase structure and the structure of the Termamyl-like α-amylase disclosed herein which are found in loops 1, 2, 3, and 8 are visualized in the Figures. Domain B The Termamyl-like α-amylase structure has been found to comprise a special domain structure in the A domain's loop3, also called domain B. The structure of the Termamyl-like α- amylase B domain has never been seen before in any of the known α-amylase or (jS/alpha) 8-barrel proteins. The domain B structure is a very compact domain having a very high number of charged residues. The B domain arises as an extension of the loop between strand 3 and helix 3 of domain A (shown in Fig. 7) and contains a 5 stranded antiparallel β- sheet structure containing at least one long loop structure and having the connectivity -1, +3, -IX, +2 (Richardson, 1981, Adv. Protein Chem. 34, 167-339). The first four strands of the B domain form two hairpin loops which twist around each other like a pair of crossed fingers (right-hand twist) . The mainchain folds into a β-strand which connects two small β-sheet structures. After making one turn in one sheet it folds back and makes up a two stranded sheet in contact with domain A and an internal hole in the α-amylase structure. Then the mainchain folds up to a small sheet structure nearly perpendicular to the first two sheets. Before entering the helix 3 on top of the β-strand 3, the approximately 24 last amino acids in domain B form two calcium binding sites in the contact region to domain A. Domain B is connected with domain A by two peptide stretches, which divide the domain-domain contact areas into two. Domain B is in contact with Domain A by a calcium binding region and an internally buried hole containing waters. Many types of molecular contacts are present. Ionic interacting between acid and basic amino acids are possible, these interactions are ve important for the general stability at high pH and for keepin the Calcium binding sites intact. Domain C Domain C is the C-terminal part of the protein consisting o amino acids 394-483. Domain C is composed entirely of β-strand which forms a single 8-stranded sheet structure, which fold back on itself, and thus may be described as a β-sandwic structure. The connectivity is +1,+1, +5, -3, +1, +1, - although strands 6 and 7 are only loosely connected. One par of the β-sheet forms the interface to domain A. Ca -binding and Na-binding si tes The structure of the Termamyl-like α-amylase is remarkable i that it exhibits four calcium-binding sites and one sodium binding site. In other words four calcium ions and one sodiu ion are found to be present in the structure, although one o the calcium ions displays very weak coordination. Two of th calcium ions form part of a linear cluster of three ions, th central ion being attributed to sodium, which lie at th junction of the A and B domains. The coordinating residues for the calcium ions between the and B domain are as follows (using the Pdb file nomenclatur for amino acid residues and atoms in the Pdb file found i Appendix 1 herein) : For the calcium ion nearest to the activ site (IUM 502 in the pdb file), the backbone carbonyls fro His235 and Aspl94, the sidechain atom OD1 from residues Aspl94, Asnl02 and Asp200, and one water molecule WAT X3 (atom 0W7) . For the sodium ion (IUM 505) , the binding site includes ato 0D2 from Aspl94, Asp200, Aspl83 and Aspl59, and a backbon carbonyl from Val201. The coordinates for the other calcium io between domain A and B are (IUM 501) : atom 0D2 from Asp204 an A sp l 59, backbone carbonyl from Aspl83 and AlalBl, atom OD1 fro Asp202, and one water molecule WAT X7 (atom 0W7) . One calcium ion is located between the A and C domain, another is located in the C domain. The first mentioned calcium ion, which is also the one best coordinated (IUM 503) includes a carbonyl backbone from Gly300, Tyr302 and His406, atom OD2/OD1 from Asp430, atom ODl from Asp407, and one water molecule WAT X6 (atom OW7) . The other and very weakly coordinated calcium site (IUM 504) comprises 4 water molecules WAT X21 (atom OW8) , X6 (atom OW6) , X9 (atom OW0) and X28 (atom OW8) , OE1/OE2 from Glu4 7 and ODl from Asn444. Substrate-.binding site Without being limited to any theory it -is presently believed that favourable interactions between a substrate molecule and the enzyme (such as hydrogen bonds and/or strong electrostatic interaction) are found within a sphere of 4A of the substrate, when bound to the enzyme. The following residues of the B . licheniformis α-amylase having the amino acid sequence shown in SEQ ID No. 2 are contemplated to be within a distance of 4 A of the substrate and thus believed to be involved in interactions with the substrate: Trpl3, Tyrl4, Asnl7, Asplδ, Ser50, Gln51, Ala52, Asp53, Val54, Gly55, Tyr56, Lys70, Arg74, Lys76, Vall02, Hisl05, Glyl07, GlylOβ, Alal09, Trpl38, Thrl63, Aspl64, Trpl65, Asnl72, Glul89, Tyrl93, Leul96, Metl97, Tyrl98, Alal99, Arg229, Asp231, Ala232, Lys234, His235, Glu261, Trp263, His327, Asp328, Gln333, Ser334, and Leu335. The amino acid residues of another Termamyl-like α-amylase, which are contemplated to be within a distance of 4A of the substrate, may easily be identified by aligning the amino acid sequence SEQ ID NO 2 with that of the other Termamyl-like a- amylase and thereby identifying the positions equivalent to those identified above. Generality of structure Because of the high homology between the various Termamyl-li α-amylases, the solved structure defined by the coordinates Appendix 1 is believed to be representative for the structur of all Termamyl-like α-amylases. A model structure of othe Termamyl-like α-amylases may easily be built on the basis o the coordinates given in Appendix 1 adapted to the α-amylase i question by use of an alignment betweeen the respective amin acid sequences. The creation of a model structure i exemplified in Example 1. The above identified structurally characteristic parts of th Termamyl-like α-amylase structure (Ca-binding site, substrat binding site, loops, etc.) may easily be identified in othe Termamyl-like α-amylases on the basis of a model (or solved structure of the relevant Termamyl-like α-amylase or simply o the basis of an alignment between the amino acid sequence o the Termamyl-like α-amylase in question with that of the B lichenformis α-amylase used herein for identifying the amino acid residues of the respective structural elements. Furthermore, in connection with Termamyl-like variants of th invention, which are defined by modification of specific amin acid residues of a specific Termamyl-like α-amylase, it will b understood that variants of another Termamyl-like α-amylas modified in an equivalent position (as determined from the bes possible amino acid sequence alignment between the respectiv sequences) are intended to be covered as well. Thus, irrespective of whether an amino acid residue is identifie herein for the purpose of defining a structural part of a give α-amylase or used for identifying a variant of the α-amylase, this amino acid residue shall be considered as representing th equivalent amino acid residue of any other Termamyl-like α amylase. Methods of the invention for desiσn of novel α-amylase variants In the methods according to the first, second and third aspects of the invention the terms "structure of a Termamyl-like α- amylase" and "Termamyl-like α-amylase structure" are intended to indicate the solved structure defined by the coordinates presented in Appendix 1 or a model structure of a given Termamyl-like α-amylase (such as the B . licheniformis α- amylase) built on the basis of the solved structure. In most cases the parent Termamyl-like α-amylase to be modified in accordance with the present invention is different from the α-amylase which was actually used for solving the structure (Appendix 1) . This means that the amino acid residue(s) or structural part(s) identified in the solved structure (Appendix 1) in step i) of the method according to the first, second or third aspect of the invention must be translated into the corresponding amino acid residue(s) or structural part(s) of the parent Termamyl-like α-amylase in question. The "translation" is conveniently performed on the basis of an amino acid sequence alignment between the amino acid sequence of the Termamyl-like α-amylase used for solving the structure and the amino acid sequence of the parent Termamyl-like α- amylase in question. The analysis or comparison performed in step i) of the method according to the first, second and third aspect, respectively, of the invention may be performed by use of any suitable computer programme capable of analysing and/or comparing protein structures, e.g. the computer programme Insight, available from Biosym Technologies, Inc. For instance, the basic principle of structure comparison is that the three- dimensional structures to be compared are superimposed on the basis of an alignment of secondary structure elements (such as the central 8 /3-strands in the barrel) and the parts differing between the structures can subsequently easily be identified from the superimposed structure. The structural part which is identified in step i) of t methods of the first, second and third aspects of the inventi may be composed of one amino acid residue. However, normal the structural part comprises more than one amino acid residu typically constituting one of the above parts of the Termamy like α-amylase structure such as one of the A, B, or C domain an interface between any of these domains, a calcium bindi site, a loop structure, the substrate binding site, or t like. In the present context the term "structural or function considerations" is intended to indicate that modifications a made on the basis of an analysis of the relevant structure structural part and its contemplated impact on the function the enzyme. Thus, an analysis of the structures of the vario α-amylases, which until now has been elucidated, optionally combination with an analysis of the functional differenc between these α-amylases, may be used for assigning certa properties of the α-amylases to certain parts of the α-amyla structure or to contemplate such relationship. For instanc differences in the pattern or structure of loops surroundi the active site may result in differences in access to t active site of the substrate and thus differences in substra specificity and/or cleavage pattern. Furthermore, parts of Termamyl-like α-amylase involved in or contemplated to involved in substrate binding (and thus e. specificity/cleavage pattern) , calcium or sodium ion bindi (e.g. of importance for the Calcium-dependency of the enzyme) and the like has been identified ( vide infra) . The modification of an amino acid residue or structural part typically accomplished by suitable modifications of a D sequence encoding the parent enzyme in question. The te "modified" as used in step ii) in the method according to t first aspect of the invention is intended to have the followi meaning: When used in relation to an amino acid residue t t erm is intended to mean replacement of the amino acid resid in Question with another ammo acid residue. When used relation to a structural part, the term is intended to mean replacement of one or more amino acid residues of said structural part, addition of one or more amino acid residues to said part, or deletion of one or more amino acid residues of said structural part. 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. First aspect of the invention In a preferred embodiment of the method according to the first aspect of the invention the property of the parent enzyme to be modified is selected from calcium dependency, substrate binding, cleavage pattern, pH dependent activity and the like. Specific examples of how to change these properties of a parent Termamyl-like α-amylase are given further below. In another preferred embodiment the parent Termamyl-like α- amylase to be modified is a B . licheniformis α-amylase. Second and third aspects of the invention One important advantage of the methods according to the second and third aspects of the present invention is that it is possible to adapt the structure (or a structural part) of a Termamyl-like α-amylase to the structure (or structural part) of a non-Termamyl-like α-amylase and vide versa . For instance, having identified a loop structure of the non-Termamyl-like α- amylase which is believed to be responsible for or contributing to a particular property of the non-Termamyl-like α-amylase it is possible to replace the corresponding structure of the Termamyl-like α-amylase with said non-Termamyl-like α-amylase structure - or if no corresponding structure exists in the Termamyl-like α-amylase - to insert the structure into the Termamyl-like Q-amylase in such a manner that the resulting variant Termamyl-like α-amylase, as far as the relevant part concerned, resembles the corresponding part of the n Termamyl-like α-amylase. When two or more parts of structure of the parent Termamyl-like α-amylase are modified as to resemble the corresponding parts of the non-Termamyl-l α-amylase it is possible to increase the resemblance to t non-Termamyl-like α-amylase of the Termamyl-like α-amyl variant and thus to alter the properties of said variant in t direction of those of said non-Termamyl-like α-amylase. Lo modifications are discussed in much further detail furth below. Typically, the modification to be performed in step iii) of t method according to the second aspect of the invention accomplished by deleting one or more amino acid residues of t part of the Termamyl-like α-amylase to be modified so as adapt the structure of said part of the parent α-amylase to t corresponding part of the non-Termamyl-like α-amylase; replacing one or more amino acid residues of the part of t Termamyl-like α-amylase to be modified with the amino ac residues occupying corresponding positions in the non-Termamy like α-amylase; or by insertion of one or more amino ac residues present in the non-Termamyl-like α-amylase into corresponding position in the Termamyl-like α-amylase. For t method according to the third aspect the modification is to understood analogously, performed on the non-Termamyl-li parent α-amylase rather than the Termamyl-like α-amylase. In step ii) of the method according to the second or thi aspect of the invention the part of the structure to identified is preferably one which in the folded enzyme believed to be in contact with the substrate (cf the disclosu above in the section entitled "Substrate-binding site) involved in substrate specificity and/or cleavage patter and/or one which is in contact with one of the calcium sodium ions and/or one, which is contributing to the pH temperature profile of the enzyme, or one which otherwise, fr structural or functional considerations, is contemplated to responsible for differences in one or more properties of the Termamyl-like and non-Termamyl-like α-amylase. Non - Termamyl -like - amylase The non-Termamyl-like α-amylase with which the comparison is made in step i) of the method of the second aspect of the invention and which is the parent α-amylase in the method of the third aspect of the invention, may be any α-amylase, which does not belong to the family of Termamyl-like α-amylases (as defined above) and, which as a consequence thereof, has a different three-dimensional structure. Furthermore, the non- Termamyl-like α-amylase should be one which has, at the time that the method is performed, an elucidated or contemplated three-dimensional structure. The non-Termamyl-like α-amylase may, e.g., be a fungal α- amylase, a mammalian or a plant α-amylase or a bacterial α- amylase (different from a Termamyl-like α-amylase) . Specific examples of such α-amylases include the Aspergillus oryzae TAKA α-amylase, the A . niger acid α-amylase, the Bacillus subtilis α-amylase, the porcine pancreatic α-amylase and a barley α- amylase. All of these α-amylases have elucidated structures which are clearly different from the structure of the Termamyl- like α-amylase shown herein. The fungal α-amylases mentioned above, i.e. derived from A . niger and A. oryzae, are highly homologous on the amino acid level and generally considered to belong to the same family of α-amylases. In the present disclosure, this family is termed "Fungamyl-like α-amylase" and intends to indicate an α-amylase which exhibits a high homology, i.e. more than 70%, such as 80% homologous (as defined herein) to the fungal α-amylase derived from Aspergillus oryzae, commercially available as Fungamyl ® , and the A . niger α-amylase. From the enclosed illustrations of the α-amylase structure of a Termamyl-like α-amylase and a comparison of said structure with the structure of a Fungamyl-like α-amylase it is evident that major differences exist between the two structures. In t method of the invention it is of particular interest to modi parts of the parent Termamyl-like α-amylase, which belong to region with large differences to the Fungamyl-like α-amylas In particular, it is of interest to modify the parent Termamyl like α-amylase in one or more of the following loops: loop 1 loop 2, loop 3 and/or loop 8 of the parent α-amylase. In the method of the third aspect of the invention it is o particular interest to modify loop 1, loop 2, loop 3 and/o loop 8 of the parent non-Termamyl-like α-amylase to a close ressemblance to the similar loops of a Termamyl-like α-amylase such as Termamyl. In the following specific types of variants are described whic have been designed by use of the method of the invention. LOOP modifications In order to change the substrate specificity of the parent α amylase to be modified it is relevant to consider loo modifications. For instance changing one or more of the loo structures of the Termamyl-like α-amylase into a close ressemblance with the corresponding loop structure (s) of a non Termamyl-like α-amylase (such as a Fungamyl-like α-amylase) i is contemplated that it is possible to change the substrat specificity in the direction of that of the non-Termamyl α amylase. In the following different types of loop modification of interest are listed. It will be understood that the variant may have other changed properties in addition to the modifie substrate specificity. It will be understood that the followin modifications identified for a specific Termamyl-like α-amylas are intended to include corresponding modifications in othe equivalent positions of other Termamyl-like α-amylases Furthermore, it will be understood that, normally, the loo modification will comprise replacement of an entire loo s t ructure or a substantial part thereof in, e.g., the Termamyl like α-amylase, with the corresponding loop structure (or substantial part thereof) in a non-Termamyl-like α-amylase. Loop2 modifications In one embodiment the invention relates to a variant of a parent Termamyl-like α-amylase, in which variant at least one amino acid residue of the parent α-amylase, which is/are present in a fragment corresponding to the amino acid fragment 44-57 of the amino acid sequence of SEQ ID No. 4, i.e. loop 2, has been deleted or replaced with one or more amino acid residues which is/are present in a fragment corresponding to the amino acid fragment 66-84 of the amino acid sequence shown in SEQ ID No. 10, or in which one or more additional amino acid residues has been added using the relevant part of SEQ ID No. 10 or a corresponding part of another Fungamyl-like α-amylase as a template. The amino acid sequence shown in SEQ ID No. 10 is the amino acid sequence of the A. oryzae α-amylase, i.e. a Fungamyl-like α-amylase. It will be understood that amino acid residues or fragments found in corresponding positions in other α-amylases, in particular Fungamyl-like α-amylases, may be used as a template for the construction of the variant according to the invention. The corresponding part in other homologous α- amylases may easily be identified on the basis of a comparison of the amino acid sequences and/or three-dimensional structures of the respective α-amylases. For instance, the variant may be one, which, when the amino acid sequence of the variant is aligned most closely with the amino acid sequence of the said parent α-amylase, occupies the same position as the portion from residue X to residue Y of SEQ ID No 4, the said region having at least 80% such as at least 90% sequence homology with the part of SEQ ID No 10 extending from residue Z to residue V of SEQ ID No 10, wherein X is the amino acid residue occupying position 44, 45, 46, 47 or 48 of SEQ ID No. 4, Y is the amino acid residue occupying position 51, 52, 53, 54 55, 56 or 57 of SEQ ID No. 4, Z is the amino acid residue occupying position 66, 67, 68, 6 or 70 of SEQ ID No. 10, and V is the amino acid residue occupying position 78, 79, 80, 81 82, 83 or 84 of SEQ ID No. 10. In other words, the variant may be one in which an amino aci fragment X-Y of the parent α-amylase, which corresponds to o is within the amino acid fragment 44-57 of SEQ ID No. 4, ha been replaced with an amino acid fragment Z-V, whic corresponds to or is within the amino acid fragment 66-84 o the amino acid sequence shown in SEQ ID No. 10, in X, Y, Z an V have the meaning indicated above. A specific example of a variant according to this embodiment i a variant of a parent Termamyl-like α-amylase, in which th amino acid fragment of the parent α-amylase, which correspond to amino acid residues 48-51 of SEQ ID No. 4, has been replace with an amino acid fragment corresponding to amino aci residues 70-78 of the amino acid sequence shown in SEQ ID No 10. Loop 3 modifications - limited al teration In another embodiment the invention relates to a variant of parent Termamyl-like α-amylase, in which variant at least on of the amino acid residues of the parent α-amylase, whic is/are present in an amino acid fragment corresponding to th amino acid fragment 195-202 of the amino acid sequence of SE ID No. 4, has been deleted or replaced with one or more of th amino acid residues which is/are present in an amino aci fragment corresponding to the amino acid fragment 165-177 o the amino acid sequence shown in SEQ ID No. 10, or in which on or more additional amino acid residues has been added using th relevant part of SEQ ID No. 10 or a corresponding part o another Fungamyl-like α-amylase as a template. For instance, the variant may be one in which an amino acid fragment X-Y of the parent α-amylase which corresponds to or is within the amino acid fragment 195-202 of SEQ ID No. 4, has been replaced by an amino acid fragment Z-V, which corresponds to or is within the amino acid fragment 165-177 of the amino acid sequence shown in SEQ ID No. 10, in which X is an amino acid residue corresponding to the amino acid occupying position 195 or 196 of SEQ ID No. 4, Y is an amino acid residue corresponding to the amino acid occupying position 198, 199, 200, 201, or 202 of SEQ ID No. 4, Z is an amino acid residue corresponding to the amino acid occupying position 165 or 166 of SEQ ID No. 10, and V is an amino acid residue corresponding to the amino acid occupying position 173, 174, 175, 176 or 177 of SEQ ID No. 10. Expressed in another manner, the variant according to this aspect may be one, which, when the amino acid sequence of variant is aligned most closely with the amino acid sequence of the said parent Termamyl-like α-amylase, occupies the same position as the portion from residue X to residue Y of SEQ ID No 4, the said region having at least 80%, such as 90% sequence homology with the part of SEQ ID No 10 extending from residue Z to residue V of SEQ ID No 10, the meaning of X, Y, Z and V being as identified above. A specific example of a variant according to this embodiment is a variant of a parent Termamyl-like α-amylase, in which the amino acid fragment of the parent α-amylase, which corresponds to amino acid residues 196-198 of SEQ ID No. 4, has been replaced with the amino acid fragment corresponding to amino acid residues 166-173 of the amino acid sequence shown in SEQ ID No. 10. Loop 3 modifications - complete domain B In a further embodiment the invention relates to a variant a parent Termamyl-like α-amylase, in which variant at least o of the amino acid residues of the parent α-amylase, whi is/are present in a fragment corresponding to the amino ac fragment 117-185 of the amino acid sequence of SEQ ID No. has/have been deleted or replaced with one or more of the ami acid residues, which is/are present in an amino acid fragme corresponding to the amino acid fragment 98-210 of the ami acid sequence shown in SEQ ID No. 10, or in which one or mo additional amino acid residues has been added using t relevant part of SEQ ID No. 10 or a corresponding part another Fungamyl-like α-amylase as a template. For instance, the variant may be one, in which an amino ac fragment X-Y of the parent α-amylase, which corresponds to is within the amino acid fragment 117-185 of SEQ ID No. 4, h been replaced with an amino acid fragment Z-V, whi corresponds to or is within the amino acid fragment 98-210 the amino acid sequence shown in SEQ ID No. 10, in whi variant X is an amino acid residue corresponding to the amino ac occupying position 117, 118, 119, 120 or 121 of SEQ ID No. Y is an amino acid residue corresponding to the amino ac occupying position 181, 182, 183, 184 or 185 of SEQ ID No. 4, Z is an amino acid residue corresponding to the amino ac occupying position 98, 99, 100, 101, 102 of SEQ ID No. 10, a V is an amino acid residue corresponding to the amino ac occupying position 206, 207, 208, 209 or 210 of SEQ ID No. 1 A specific example of a variant according to this embodiment a variant of a parent α-amylase, in which an amino ac fragment of the parent α-amylase, which corresponds to ami acid residues 121-181 of SEQ ID No. 4, has been replaced wi the amino acid fragment corresponding to amino acid residues 102-206 of the amino acid sequence shown in SEQ ID No. 10. In another embodiment the invention relates to a variant of a parent Termamyl-like α-amylase, in which variant at least one of the amino acid residues of the parent α-amylase, which is/are present in a fragment corresponding to the amino acid fragment 117-181 of the amino acid sequence of SEQ ID No. 4, has/have been deleted or replaced with one or more of the amino acid residues, which is/are present in an amino acid fragment corresponding to the amino acid fragment to 98-206 of the amino acid sequence shown in SEQ ID No. 10, or in which one or more additional amino acid residues has been added using the relevant part of SEQ ID No. 10 or a corresponding part of another Fungamyl-like α-amylase as a template. For instance, the variant may be one, in which the amino acid fragment X-Y of the parent α-amylase, which corresponds to or is within the amino acid fragment 117-177 if SEQ ID No. 4, has/have been replaced with an amino acid fragment Z-V, which corresponds to or is within the amino acid fragment 98-202 of the amino acid sequence shown in SEQ ID No. 10, in which variant X is an amino acid residue corresponding to the amino acid occupying position 117, 118, 119, 120 or 121 of SEQ ID No. 4, Y is an amino acid residue corresponding to the amino acid occupying position 174, 175, 176 or 177 of SEQ ID No. 4, Z is an amino acid residue corresponding to the amino acid occupying position 98, 99, 100, 101, 102 of SEQ ID No. 10, and V is an amino acid residue corresponding to the amino acid occupying position 199, 200, 201 or 202 of SEQ ID No. 10. A specific example of a variant according to this embodiment of the invention is a variant, in which the amino acid fragment of the parent α-amylase, which corresponds to amino acid residu 121-174 of SEQ ID No. 4, has been replaced with the amino aci fragment corresponding to amino acid residues 102-199 of t amino acid sequence shown in SEQ ID No. 10. Loop 1 modifications - minimal addi tion In a further embodiment the present invention relates to variant of a parent Termamyl-like α-amylase, in which varian at least one of the amino acid residues of the parent α amylase, which is/are present in an amino acid fragmen corresponding to the amino acid fragment 12-19 of the amin acid sequence of SEQ ID No. 4, has/have been deleted o replaced with one or more of the amino acid residues, whic is/are present in an amino acid fragment which corresponds t the amino acid fragment 28-42 of SEQ ID No. 10, or in which on or more additional amino acid residues has/have been inserte using the relevant part of SEQ ID No. 10 or a correspondin part of another Fungamyl-like α-amylase as a template. For instance, the variant may be one, in which the amino aci fragment X-Y of the parent α-amylase, which corresponds to o is within the amino acid fragment 12-19 of SEQ ID No. 4 has/have been replaced with an amino acid fragment Z-V, whic corresponds to or is within the amino acid fragment 28-42 o the amino acid sequence shown in SEQ ID No. 10., in whic variant X is an amino acid residue corresponding to the amino aci occupying position 12, 13 or 14 of SEQ ID No. 4, Y is an amino acid residue corresponding to the amino aci occupying position 15, 16, 17, 18 or 19 of SEQ ID No. 4, Z is an amino acid residue corresponding to the amino aci occupying position 28, 29, 30 , 31 or 32 of SEQ ID No. 10, an V is an amino acid residue corresponding to the amino aci occupying position 38, 39, 40, 41 or 42 of SEQ ID No. 10. A specific example of a variant according to this aspect of the invention is a variant, in which the amino acid fragment of the parent α-amylase, which corresponds to amino acid residues 14- 15 of SEQ ID No. 4, has been replaced with the amino acid fragment corresponding to amino acid residues 32-38 of the amino acid sequence shown in SEQ ID No. 10. Loop 1 modifications - complete loop In a further embodiment the invention relates to a variant of a parent Termamyl-like α-amylase, in which variant at least one of the amino acid residues of the parent α-amylase, which is present in a fragment corresponding to amino acid residues 7-23 of the amino acid sequence of SEQ ID.No. 4, has/have been deleted or replaced with one or more amino acid residues, which is/are present in an amino acid fragment corresponding to amino acid residues 13-45 of the amino acid sequence shown in SEQ ID No. 10, or in which one or more additional amino acid residues has/have been inserted using the relevant part of SEQ ID No. 10 or a corresponding part of another Fungamyl-like α-amylase as a template. For instance, the variant may be one, in which the amino acid fragment X-Y of the parent α-amylase, which corresponds to or is within the amino acid fragment 7-23 of SEQ ID No. 4, has/have been replaced with an amino acid fragment Z-V, which corresponds to or is within the amino acid fragment 13-45 of the amino acid sequence shown in SEQ ID No. 10, in which variant X is an amino acid residue corresponding to the amino acid occupying position 7 or 8 of SEQ ID No. 4, Y is an amino acid residue corresponding to the amino acid occupying position 18, 19, 20, 21, 22 or 23 of SEQ ID No. 4, Z is an amino acid residue corresponding to the amino acid occupying position 13 or 14 of SEQ ID No. 10, and V is an amino acid residue corresponding to the amino ac occupying position 40, 41, 42, 43, 44 or 45 of SEQ ID No. 1 A specific variant according to this embodiment is one, which the amino acid fragment of the parent α-amylase, whi corresponds to amino acid residues 8-18 of SEQ ID No. 4, h been replaced with the amino acid fragment corresponding amino acid residues 14-40 of the amino acid sequence shown SEQ ID No. 10. Loop 8 modifications In a further embodiment the invention relates to a variant a parent Termamyl-like α-amylase, in which variant at least o of the amino acid residues of the parent α-amylase, which present in a fragment corresponding to amino acid residues 32 346 of the amino acid sequence of SEQ ID No. 2, has/have be deleted or replaced with one or more amino acid residues, whi is/are present in an amino acid fragment corresponding to ami acid residues 291-313 of the amino acid sequence shown in S ID No. 10, or in which one or more additional amino aci residues has/have been inserted using the relevant part of S ID No. 10 or a corresponding part of another Fungamyl-like amylase as a template. For instance, the variant may be one, in which the amino aci fragment X-Y of the parent α-amylase, which corresponds to o is within the amino acid fragment 322-346 of SEQ ID No. 2 has/have been replaced with an amino acid fragment Z-V, whic corresponds to or is within the amino acid fragment 291-313 o the amino acid sequence shown in SEQ ID No. 10, in whic variant X is an amino acid residue corresponding to the amino aci occupying position 322, 323, 324 or 325 of SEQ ID No. 2, Y is an amino acid residue corresponding to the amino aci occupying position 343, 344, 345 or 346 of SEQ ID Nc. 2, Z is an amino acid residue corresponding to the amino acid occupying position 291, 292, 293 or 294 of SEQ ID No. 10, and V is an amino acid residue corresponding to the amino acid occupying position 310, 311, 312 or 313 of SEQ ID No. 10. A specific variant according to this aspect of the invention is one, in which the amino acid fragment of the parent α-amylase, which corresponds to amino acid residues 325-345 of SEQ D No. 2, has been replaced with the amino acid fragment corresponding to amino acid residues 294-313 of the amino acid sequence shown in SEQ ID No. 10. Ca 2 * dependency It is highly desirable to be able to decrease the Ca 2 * dependency of a Termamyl-like α-amylase. Accordingly, in a further aspect the invention relates to a variant of a parent Termamyl-like α-amylase, which exhibits α-amylase activity and which has a decreased Ca + dependency as compared to the parent α-amylase. The decreased Ca 2 * dependency has the functional result that the variant exhibits a satisfactory amylolytic activity in the presence of a lower concentration of calcium ion in the extraneous medium than is necessary for the parent enzyme and, for example, therefore is less sensitive than the parent to calcium ion-depleting conditions such as those obtained in media containing calcium-complexing agents (such as certain detergent builders) . The decreased Ca 2+ dependency of the variant of the invention may advantageously be achieved by increasing the Ca 2* binding affinity of the parent Termamyl-like α-amylase, in other words the stronger the Ca 2* binding of the enzyme, the lower is the Ca 2* dependency. It is presently believed that amino acid residues located within 10A from a sodium or calcium ion are involved in or are of importance for the Ca 2* binding capability of the enzyme. Accordingly, the variant according to this aspect of t invention is preferably one, which has been modified in one more amino acid residues present within 10A from a calci and/or sodium ion identified in the three-dimensional Termamy like α-amylase structure in such a manner that the affinity the α-amylase for calcium is increased. The amino acid residues found within a distance of 10A from t Ca 2* binding sites of the B. licheniformis α-amylase with t amino acid sequence SEQ ID NO 2 were determined as described Example 2 and are as follows: V102, 1103, N104, H105, K106, R125, W155, W157, Y158, H15 F160, D161, G162, T163, Y175, K176, F177, G178, K180, A18 W182, D183, W184, E185, V186, S187, N192, Y193, D194, Y19 L196, M197, Y198, A199, D200, 1201, D202, Y203, D204, H20 P206, V208, A209, D231, A232, V233, K234, H235, 1236, K23 F238, F240, L241, A294, A295, S296, T297, Q298, G299, G30 G301, Y302, D303, M304, R305, K306, L307, W342, F343, L34 Q393, Y394, Y396, H405, H406, D407, 1408, V409, R413, E41 G415, D416, S417, V419, A420, N421, S422, G423, L424, 142 T429, D430, G431, P432, V440, G441, R442, Q443, N444, A44 G446, E447, T448, W449, 1462, G475, Y480, V481, Q482, R483. In order to construct a variant according to this aspect of t invention it is desirable to replace at least one of the abo mentioned amino acid residues (or an amino acid resid occupying an equivalent position in another Termamyl-like α amylase than that defined by SEQ ID NO 2) , which i contemplated to be involved in providing a non-optimal calciu binding, with any other amino acid residue which improves th Ca 2 * binding affinity of the variant enzyme. In practice, t identification and subsequent modification of the amino aci residue is performed by the following method: i) identifying an amino acid residue within 10A from a Ca binding site of a Termamyl-like α-amylase structure, which fro structural or functional considerations is believed to be responsible for a non-optimal calcium ion interaction, ii) constructing a variant in which said amino acid residue is replaced with another amino acid residue which from structural or functional considerations is believed to be important for establishing a higher Ca 2 * binding affinity, and testing the Ca 2 * dependency of the resulting Termamyl-like α-amylase variant. In the present context, the term "non-optimal calcium ion interaction" is intended to indicate that the amino acid residue in question is selected on the basis of a presumption that substituting said amino acid residue for another may improve 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 considerations: - to obtain an improved interaction between a calcium ion and an amino acid residue located near to the surface of the enzyme (as identified from the structure of the Termamyl-like α- 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 provide for a stronger interaction between said amino acid residue and a calcium ion. This can be achieved by replacing said residue (or an amino acid residue in the vicinity of said residue contributing to the shielding) by an amino acid residue which is more bulky or otherwise results in an improved shielding effect. - to stabilize a calcium binding site, for instance by stabilizing the structure of the Termamyl-like α-amylase (e.g. by stabilizing the contacts between the A, B and C domains or stabilizing one or more of the 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 replacing an N residue with a D residue and/or a Q residue with an E residue (e.g. N104D) , e.g. within 10A, and preferab within 3 or 4A, of a calcium binding site. - to protect the calcium binding site or to improve t s coordination between the calcium ion and the calcium bindi site, e.g. by providing a stronger interaction between the i and the binding site. Before actually constructing a Termamyl-like α-amylase varia 0 according to the above principles it may be convenient evaluate the contemplated amino acid modification by i accommodation into the Termamyl-like α-amylase structure, e. into a model structure of the parent Termamyl-like α-amylase. s Preferably, the amino acid residue to be modified is locate within 8A of a Ca 2 * binding site residue, such as within 5A o such residue. The amino acid residues within 8A and 5 respectively, may easily be identified by an analogous metho used for identifying amino acid residues within 10A (cf 0 Example 2) . The following mutation is contemplated to be of particula interest with respect to decreasing the Ca 2 * dependency of Termamyl-like α-amylase: 5 N104D (of the B . licheniformis α-amylase SEQ ID NO 2, or a equivalent (N to D) mutation of an equivalent position i another Termamyl-like α-amylase.) In connection with substitutions of relevance for Ca 0 dependency, some other substitutions appear to be of importanc in stabilizing the enzyme conformation (for instance th Domains A-B and/or Domains A-C interactions contributing to th overall stability of the enzyme) in that they may, e.g. enhance the strength of binding or retention of calcium ion o 5 sodium ion at or within a calcium or sodium binding site respectively, within the parent Termamyl-like α-amylase. It is desirable to stabilize the C-domain in order to increase the calcium stability and/or thermostability of the enzyme. In this connection the stabilization may result in a stabilization of the binding of calcium by the enzyme, and an improved contact between the C-domain and the A-domain (of importance for thermostability) . The latter may be achieved by introduction of cystein bridges, salt bridges or increase hydrogen, hydrophobic and/or electrostatic interactions. For instance, the C-domain of the B . licheniformis α-amylase having the amino acid sequence shown in SEQ ID No. 2 may be stabilized by introduction of a cystein bridge between domain A and domain C, e.g. by introducing of the following mutations: A349C+I479C and/or L346C+I430C. A salt bridge may be obtained by introduction of the following mutations: N457D,E N457D,E+K385R F350D,E+I430R,K F350D,E+I411R,K The calcium site of Domain C may be stabilized by replacing the amino acid residues H408 and/or G303 with any other amino acid residue. Of particular interest is the following mutations: H408Q,E,N,D and/or G303N,D,Q,E which are contemplated to provide a better calcium binding or protection from calcium depletion. Similar mutations may be introduced in equivalent positions of other Termamyl-like α-amylases. Other substitution mutations (relative to B . licheniformis α-amylase, SEQ ID No. 2) which appear to be of importance, inter alia , in the context of reducing calcium dependency include the following: R23K, H156Y, A181T, A209V and G310D (or equivalent mutations in equivalent positions in another Termamyl-like α-amylase) . Substitutions of R214 and P345 with other amino acids may also be of importancen in thi connection. Variants with altered activity at hiσher/lower pH It is contemplated that it is possible to change the pH optim of a Termamyl-like α-amylase or the enzymatic activity at given pH by changing the pKa of the active site residues. Thi may be achieved, e.g. by changing the electrostatic interactio or hydrophobic interaction between functional groups of amin acid side chains of the amino acid residue to be modified an of its close surroundings. This may, e.g., be accomplished b the following method: i) in a structure of the Termamyl-like α-amylase in question t identifying an amino acid residue within 15A from an activ site residue, in particulular 10A from an active site residue which amino acid residue is contemplated to be involved i electrostatic or hydrophobic interactions with an active sit residue, ii) replacing, in the structure, said amino acid residue wit an amino acid residue which changes the electrostatic and/o hydrophobic surroundings of an active site residue an evaluating the accomodation of the amino acid residue in th structure, iii) optionally repeating step i) and/or ii) until an amin acid replacement has been identified which is accomodated int the structure, iv) constructing a Termamyl-like α-amylase variant resultin from steps i) , ii) and optionally iii) and testing the p dependent enzymatic activity of interest of said variant. In the above method it may be of particular relevance to add positively charged residue within 5A of a glu a ate (thereb lowering the pKa of the glutamate from about 4.5 to 4), cr t add a negatively charged residue within 5 A of a glutamate (thereby increasing the pKa to about 5) , or to make similar modifications within a distance of about 5A of a Histidine. In a further aspect the invention relates to a variant of a Termamyl-like α-amylase which exhibits a higher activity at a lower pH (e.g. compared to the pH optimum) than the parent α- amylase. In particular, the variant comprises a mutation of an amino acid residue corresponding to at least one of the following positions of the B . licheniformis α-amylase (SEQ ID NO 2) : E336, Q333, P331, 1236, V102, A232, 1103, L196 The following mutations are of particular interest: E336R, K Q333R, K P331R, K V102R, K, A, T, S , G; I236K, R, N; I103K, R; L196K, R; A232T, S , G; or any combination of two or more of these variants or any combination of one or more of these variants with any of the other variants disclosed herein. In a still further aspect the invention relates to a variant of a Termamyl-like α-amylase which has a higher activity at a higher pH than the parent α-amylase. In particular, the variant comprises a mutation of an amino acid residue corresponding to at least one of the following positions of the B . licheniformis α-amylase (SEQ ID NO 2) : N236 , H281 , Y273 In particular, the variant comprises a mutation correspondi to at least one of the following mutations of the licheniformis α-amylase (SEQ ID NO 2) : N326I,Y,F,L,V H281F,I,L Y273F,W or any combination of two or more of these variants or a combination of one or more of these variants with any of the other variants disclosed herein. A mutation which appears to be importance in relation to t specific activity of variants of the invention is a mutati corresponding to the substitution S187D in B . licheniformis amylase (SEQ ID NO 2) . Variants with increased thermostability and/or alter temperature optimum In a further desired aspect the invention relates to a varia of a parent Termamyl-like α-amylase, which variant is t result of one or more amino acid residues having been delete from, replaced or added to the parent α-amylase so as to obtai an increased thermostability of the variant. The Termamyl-like α-amylase structure contains a number o unique internal holes, which may contain water, and a number o crevices. In order to increase the thermostability of the α amylase it may be desirable to reduce the number of holes an crevices (or reduce the size of the holes or crevices) , e.g. b introducing one or more hydrophobic contacts, preferabl achieved by introducing bulkier residues, in the vicinity o surroundings of the hole. For instance, the amino acid residue to be modified are those which are involved in the formation o the hole. Accordingly, in a further aspect the present invention relates to a method of increasing the thermostability and/or altering the temperature optimum of a parent Termamyl-like α-amylase, which method comprises i) identifying an internal hole or a crevice of the parent Termamyl-like α-amylase in the three-dimensional structure of said α-amylase, ii) replacing, in the structure, one or more amino acid residues in the neighbourhood of the hole or crevice identified in i) with another amino acid residue which from structural or functional considerations is believed to increase the hydrophobic interaction and to fill out or reduce the size of the hole or crevice, iii) constructing a Termamyl-like α-amylase variant resulting from step ii) and testing the thermostability and/or temperature optimum of the variant. The structure used for identifying the hole or crevice of the parent Termamyl-like α-amylase may be the structure identified in Appendix 1 or a model structure of the parent Termamyl-like α-amylase built thereon. It will be understood that the hole or crevice is identified by the amino acid residues surrounding the hole/crevice, and that modification of said amino acid residues are of importance for filling or reducing the size of the hole/crevice. The particular amino acid residues referred to below are those which in crystal structure have been found to flank the hole/crevice in question. In order to fill (completely or partly) a major hole located between domain A and B, mutation to any other amino acid residue of an amino acid residue corresponding to one or more of the following residues of the B . licheniformis α-amylase (SEQ ID NO 2) is contemplated: L61, Y62, F67, K106, G145, 1212, S151, R214, Y150, F143, R146 Of particular interest is a mutation to a more bulky amino ac residue than the amino acid residue of the parent enzyme. Of particular interest is a variant of a Termamyl-like amylase which comprises a mutation corresponding to t following mutations (using the numbering of B . licheniformis amylase (SEQ ID NO 2) : L61W,V,F; Y62W; F67W; K106R,F,W; G145F,W I212F,L,W,Y,R,K; S151 replaced with any other amino acid residue and i particular with F,W,I or L; R214W; Y150R,K; F143W; and/or R146W. In order to fill a hole in the vicinity of the active site mutation to any other amino acid residue of an amino aci residue corresponding to one or more of the following residue of the B . licheniformis α-amylase (SEQ ID NO 2) i contemplated: L241, 1236. Of interest is a mutation to a more bulky amino acid residue. Of particular interest is a variant of a Termamyl-like α- amylase which comprises a mutation corresponding to one or more of the following mutations in the B . licheniformis α-amylase: L241I,F,Y,W; and/or I236L,F,W,Y In order to fill a hole in the vicinity of the active site mutation to any other amino acid residue of an amino acid residue corresponding to one or more of the following residues of the B. licheniformis α-amylase (SEQ ID NO 2) is contemplated: L7, V259, F284 Of interest is a mutation to a more bulky amino acid residue. Of particular interest is a variant of a Termamyl-like α- amylase which comprises a mutation corresponding to one or more of the following mutations in the B. licheniformis α-amylase: L7F,I,W V259F,I,L F284W In order to fill a hole in the vicinity of the active site mutation to any other amino acid residue of an amino acid residue corresponding to one or more of the following residues of the B. licheniformis α-amylase (SEQ ID NO 2) is contemplated: F350, F343 Of interest is a mutation to a more bulky amino acid residue. Of particular interest is a variant of a Termamyl-like α- amylase which comprises a mutation corresponding to one or more of the following mutations in the B. licheniformis α-amylase: F350W F343W In order to fill a hole in the vicinity of the active sit mutation to any other amino acid residue of an amino ac residue corresponding to one or more of the following residu of the B . licheniformis α-amylase (SEQ ID NO 2) contemplated: L427, V481 Of interest is a mutation to a more bulky amino acid residue Of particular interest is a variant of a Termamyl-like α amylase which comprises a mutation corresponding to one or mor of the following mutations in the B . licheniformis α-amylase L427F,L,W V481,F,I,L,W Variants with an altered cleavaσe pattern In the starch liquefaction process it is desirable to use an α amylase which is capable of degrading the starch molecules int long branched oligo saccharides (like, e.g. the Fungamyl-lik α-amylases) rather than shorter branched oligo saccharide (like conventional Termamyl-like α-amylases) . The resultin very small branched oligosaccharides (panose precursors) canno be hydrolyzed properly by pullulanases, which in th liquefaction process are used after the α-amylases and befor the amyloglucosidases. Thus, in the presence of panos precursors the action of amylo-glucoamylase ends up with a hig degree of the small branched limiting-dextrin, th trisaccharide panose. The presence of panose lowers the sac charification yield significantly and is thus undesirable. Thus, one aim of the present invention is to change th degradation characteristics of a Termamyl-like α-amylase t that of a Fungamyl-like α-amylases without at the same tim reducing the thermostability cf the Termamyl-like α-amylase. Accordingly, in a further aspect the invention relates to a variant of a Termamyl-like α-amylase which has a reduced ability to cleave a substrate close to the branching point. The variant may suitably be constructed by a method which comprises i) identifying the substrate binding area of the parent Termamyl-like α-amylase in a model of the three-dimensional structure of said α-amylase, (e.g. within a sphere of 4A from the substrate binding site (as defined in the section above entitled "Substrate Binding Site"), ii) replacing, in the model, one or more amino acid residues of the substrate binding area of the cleft identified in i) , which is/are believed to be responsible for the cleavage pattern of the parent α-amylase, with another amino acid residue which from structural 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 favourable interactions to the substrate or adding one or more amino acid residues to the substrate binding area contemplated to introduce favourable interactions to the substrate, and iii) constructing a Termamyl-like α-amylase variant resulting from step ii) and testing the substrate cleavage pattern of the variant. Of particular interest is a variant which cleaves an amylopectin substrate, from the reducing end, more than one glucose unit from the branching point, preferably more than two or three glucose units from the branching point, i.e. at a further distance from the branching point than that obtained by use of a wild type B . licheniformis α-amylase. Residues of particular interest in connection with this aspect of the invention correspond to the following residues of the B . licheniformis α-amylase (SEQ ID NO 2) : V54, D53, Y56, Q333, G57, and the variants according to this aspect preferabl comprises a mutation in one or more of these residues. In particular, the variant comprises at least one of th following mutations, which are expected to prevent cleavag close to the branching point: V54L,I,F,Y,W,R,K,H,E,Q D53L,I,F,Y,W Y56W Q333W G57all possible amino acid residues A52amino acid residues larger than A, e.g. A52W,Y,L,F, I. Variants of a funσal α-amylase In a still further embodiment the invention relates to variant of a parent Fungamyl-like α-amylase, in which varian at least one of the amino acid residues of the parent α amylase, which is/are present in an amino acid fragmen corresponding to amino acid residues 291-313 of the amino aci sequence of SEQ ID No. 10, has/have been deleted or replace with one or more of the amino acid residues, which is/ar present in an amino acid fragment corresponding to amino aci residues 98-210 of the amino acid sequence shown in SEQ ID No. 4, or in which one or more additional amino acid residue has/have been inserted using the relevant part of SEQ ID No. or a corresponding part of another Termamyl-like α-amylase a a template. For instance, the variant may be one, in which the amino aci fragment X-Y of the parent α-amylase, which corresponds to o is within the amino acid fragment 117-185 of SEQ ID No. 10, has/have been replaced with an amino acid fragment Z-V, whic corresponds to or is within the amino acid fragment 98-210 of the amino acid sequence shown in SEQ ID No. 4, in which variant X is an amino acid residue corresponding to the amino acid occupying position 117, 118, 119, 120 or 121 of SEQ ID No. 10, Y is an amino acid residue corresponding to the amino acid occupying position 181, 182, 183, 184 or 185 of SEQ ID No. 10, Z is an amino acid residue corresponding to the amino acid occupying position 98, 99, 100, 101 or 102 of SEQ ID No. 4, and V is an amino acid residue corresponding to the amino acid occupying position 206, 207, 208, 209 or 210 of SEQ ID No. 4. A specific example of a variant according to this aspect of the invention is one, in which the amino acid fragment of the parent α-amylase, which corresponds to amino acid residues 121- 181 of SEQ ID No. 10, has been replaced with the amino acid fragment corresponding to amino acid residues 102-206 of the amino acid sequence shown in SEQ ID No. 4. Another example of a variant according to this aspect of the invention is one, in which the amino acid fragment of the parent α-amylase, which corresponds to amino acid residues 121- 174 of SEQ ID No. 10, has been replaced with the amino acid fragment corresponding to amino acid residues 102-199 of the amino acid sequence shown in SEQ ID No. 4. In a further embodiment the invention relates to a variant of a parent Fungamyl-like α-amylase, in which an amino acid fragment corresponding to amino acid residues 181-184 of the amino acid sequence shown in SEQ ID No. 10 has been deleted. General mutations in variants of the invention It may be preferred that the variant of the invention or prepared in accordance with the method of the invention comprises one or more modifications in addition to those outlined above. Thus, it may be advantageous that one or more proline residues present in the part of the α-amylase variant having been modified is/are replaced with a non-proline resid which may be any of the possible, naturally occurring no proline residues, and which preferably is an alanine, glycin serine, threonine, valine or leucine. Analogously, it may be preferred that one or more cystei residues present in the amino acid residues with which t parent α-amylase is modified are replaced with a non-cystei residues such as serine, alanine, threonine, glycine, valine leucine. Furthermore, the variant of the invention may either as t only modification or in combination with any of the abo outlined modifications be modified so that one or more A and/or Glu present in an amino acid fragment corresponding the amino acid fragment 185-209 of SEQ ID No. 8 is replaced an Asn and/or Gin, respectively. Also of interest is t modification of one or more of the Lys residues present in t Termamyl-like α-amylase is replaced by an Arg present in amino acid fragment corresponding to the amino acid fragme 185-209 of SEQ ID No. 8 is replaced by an Asn and/or Gi respectively. It will be understood that in accordance with the prese invention variants may be prepared which carry two or more o the above outlined modifications. For instance, variants may prepared which comprises a modification in the loop 1 and loo 2 region, a modification in loop 2 and limited loop 3, modification in loop 1, loop 2, loop 3 and loop 8, etc. Furthermore, it may be advantageous to introduce point mutations in any of the variants described herein. Methods of preparing α-amylase variants Several methods for introducing mutations into genes are know in the art. After a brief discussion of the cloning of α amylase-encoding DNA sequences, methods for generatin mutations at specific sites within the α-amylase-encoding sequence will be discussed. Cloning a DNA sequence encoding an α-amylase s The DNA sequence encoding a parent α-amylase may be isolated from any cell or microorganism producing the α-amylase in question, using various methods well known in the art. First, a genomic DNA and/or cDNA library should be constructed using chromosomal DNA or messenger RNA from the organism that pro- 0 duces the α-amylase to be studied. Then, if the amino acid sequence of the α-amylase is known, homologous, labelled oli¬ gonucleotide probes may be synthesized and used to identify α- amylase-encoding clones from a genomic library prepared from the organism in question. Alternatively, a labelled oligonu- 5 cleotide probe containing sequences homologous to a known α- amylase gene could be used as a probe to identify α-amylase-en¬ coding clones, using hybridization and washing conditions of lower stringency. 0 Yet another method for identifying α-amylase-encoding clones would involve inserting fragments of genomic DNA into an ex¬ pression 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 5 substrate for α-amylase, thereby allowing clones expressing the α-amylase to be identified. Alternatively, the DNA sequence encoding the enzyme may be prepared synthetically by established standard methods, e.g. 0 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. 5 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 iigating fragments of synthetic, genomic or cDNA origin (as appropriate, the fragmen corresponding to various parts of the entire DNA sequence) , accordance with standard techniques. The DNA sequence may al be prepared by polymerase chain reaction (PCR) using specif primers, for instance as described in US 4,683,202 or R. Saiki et al. (1988) . Site-directed mutagenesis Once an α-amylase-encoding DNA sequence has been isolated, a desirable sites for mutation identified, mutations may introduced using synthetic oligonucleotides. These oligonucle tides contain nucleotide sequences flanking the desired mut tion sites; mutant nucleotides are inserted during olig nucleotide synthesis. In a specific method, a single-strand gap of DNA, bridging the α-amylase-encoding sequence, is cr ated in a vector carrying the α-amylase gene. Then the sy thetic nucleotide, bearing the desired mutation, is annealed t a homologous portion of the single-stranded DNA. The remainin gap is then filled in with DNA polymerase I (Klenow fragment and the construct is ligated using T4 ligase. A specifi example of this method is described in Morinaga et al. (1984) US 4,760,025 discloses the introduction of oligonucleotide encoding multiple mutations by performing minor alterations o the cassette. However, an even greater variety of mutations ca be introduced at any one time by the Morinaga method, becaus a multitude of oligonucleotides, of various lengths, can b introduced. Another method of introducing mutations into α-amylase-encodin DNA sequences is described in Nelson and Long (1989) . I involves the 3-step generation of a PCR fragment containing th desired mutation introduced by using a chemically synthesize DNA strand as one of the primers in the PCR reactions. From th PCR-generated fragment, a DNA fragment carrying the mutatio may be isolated by cleavage with restriction endonucleases an reinserted into an expression plasmid. Random mi-. agenesis Random mutagenesis is suitably performed either as localized 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. For region-specific random mutagenesis with a view to improving the thermal stability of a parent Termamyl-like α-amylase, codon positions corresponding to the following amino acid residues of the B . licheniformis α-amylase (SEQ ID NO 2) may appropriately be targeted: To improve the stability of the calcium site between Domain A and C I428-A435 T297-L308 F403-V409 To improve the stability between domain A and B: D180-D204 H156-T163 A232-F238 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 Termamyl-like α-amylase variant, modified (e.g. higher) substrate specificity and/or modified (e.g. higher) specificity with respect to cleavage (hydrolysis) of substrate, it appears that the following codon positions for the amino acid sequence shown in SEQ ID NO 2 (or equivalent codon positions for another parent Termamyl-like α-amylase in the context of the invention) may particularly appropriately be targeted: 13-18 50-56 70-76 102-109 163-172 189-199 229-235 360-264 327-335 The random mutagenesis of a DNA sequence encoding a parent α amylase to be performed in accordance with step a) of th above-described method of the invention may conveniently b performed by use of any method known in the art. For instance, the random mutagenesis may be performed by use o 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 mutagene- sis may be performed by use of any combination of these mutage¬ nizing agents. The mutagenizing agent may, e.g., be one which induces tran¬ sitions, 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) , 0- methyl hydroxylamine, nitrous acid, ethyl methane sulphonate (EMS) , sodium bisulphite, formic acid, and nucleotide analo¬ gues. When such agents are used, the mutagenesis is typically per- formed 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 oligonucleo¬ tide, the oligonucleotide may be doped or spiked with the three non-parent nucieotides during tne synthesis of the oligonuoleo- tide 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 amylolytic enzyme by any published technique, using e.g. PCR, LCR or any DNA polymerase and ligase. When PCR-generated mutagenesis is used, either a chemically treated or non-treated gene encoding a parent α-amylase enzyme is subjected to PCR under conditions that increase the mis- incorporation of nucleotides (Deshler 1992; Leung et al. , Technique, Vol.l, 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 amylolytic enzyme 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 subsequently be transformed into the expression organism. The DNA sequence to be mutagenized may conveniently be present in a genomic or cDNA library prepared from an organism expres- sing the parent amylolytic enzyme. Alternatively, the DNA se¬ quence may be present on a suitable vector such as a plasmid or a bacteriophage, which as such may be incubated with or other¬ wise exposed to the mutagenizing agent. The DNA to be mutage¬ nized 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 harboured in the cell. Finally, the DNA to be mutage¬ nized may be in isolated form. It will be understood that the DNA sequence to be subjected to random mutagenesis is pre¬ ferably a cDNA or a genomic DNA sequence. In some cases it may be convenient to amplify the mutated DNA sequence prior to the expression step (b) or the screening step (c) being performed. Such amplification may be performed in accordance with methods known in the art, the presentl preferred method being PCR-generated amplification usin oligonucleotide primers prepared on the basis of the DNA o amino acid sequence of the parent enzyme. Subsequent to the incubation with or exposure to the mutage nizing agent, the mutated DNA is expressed by culturing suitable host cell carrying the DNA sequence under condition allowing expression to take place. The host cell used for thi purpose may be one which has been transformed with the mutate DNA sequence, optionally present on a vector, or one which wa carried the DNA sequence encoding the parent enzyme during th mutagenesis treatment. Examples of suitable host cells are th following: grampositive bacteria such as Bacillus subtilis Bacillus licheniformis, Bacillus lentus, Bacillus breviε Bacillus stearothermophilus, Bacillus alkalophilus, Bacillu amyloliquefaciens, Bacillus coagulanε, Bacillus circulans, Bacillus lautuε, Bacilluε megaterium, Bacilluε thuringienεiε , Streptomyces lividans or Strep tomyceε murinuε; and gramnegativ bacteria such as E. coli . The mutated DNA sequence may further comprise a DNA sequenc encoding functions permitting expression of the mutated DN sequence. Localized random mutagenesis: the random mutagenesis ma advantageously be localized to a part of the parent α-amylas in question. This may, e.g., be advantageous when certai regions of the enzyme have been identified to be of particula importance for a given property of the enzyme, and whe modified are expected to result in a variant having improve properties. Such regions may normally be identified when the tertiary structure of the parent enzyme has been elucidated an related to the function of the enzyme. The localized random mutagenesis is conveniently performed b 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 being inserted into a suitable vector, and said part may subsequently be sub¬ jected to mutagenesis by use of any of the mutagenesis methods discussed above. With respect to the screening step in the above-mentioned method of the invention, this may conveniently performed by use of aa filter assay based on the following principle: A microorganism capable of expressing the mutated amylolytic enzyme of interest is incubated on a suitable medium and under suitable conditions for the enzyme to be secreted, the medium being provided with a double filter comprising a first protein- binding filter and on top of that a second filter exhibiting a low protein binding capability. The microorganism is located on the second filter. Subsequent to the incubation, the first filter comprising enzymes secreted from the microorganisms is separated from the second filter comprising the microorganisms. The first filter is subjected to screening for the desired enzymatic activity and the corresponding microbial colonies present on the second filter are identified. The filter used for binding the enzymatic activity may be any protein binding filter e.g. nylon or nitrocellulose. The top- 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 Durapore™. The filter may be pretreated with any of the conditions to be used for screening or may be treated during the detection of enzymatic 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. α-Amylase activity is detected by Cibacron Red labell amylopectin, which is immobilized on agarose. For screening f variants with increased thermal and high-pH stability, t filter with bound α-amylase variants is incubated in a buff at pH 10.5 and 60° or 65°C for a specified time, rinsed brief in deionized water and placed on the amylopectin-agarose matr for activity detection. Residual activity is seen as lysis Cibacron Red by amylopectin degradation. The conditions a chosen to be such that activity due to the α-amylase having t amino acid sequence shown in SEQ ID No.l can barely detected. Stabilized variants show, under the same conditions increased colour intensity due to increased liberation o Cibacron Red. For screening for variants with an activity optimum at a lowe temperature and/or over a broader temperature range, the filte with bound variants is placed directly on the amylopectin Cibacron Red substrate plate and incubated at the desire temperature (e.g. 4°C, 10°C or 30°C) for a specified time After this time activity due to the α-amylase having the amin acid sequence shown in SEQ ID No.l can barely be detected whereas variants with optimum activity at a lower temperatur will show increase amylopectin lysis. Prior to incubation ont the amylopectin matrix, incubation in all kinds of desire media - e.g. solutions containing Ca 2* , detergents, EDTA o other relevant additives - can be carried out in order t screen for changed dependency or for reaction of the variant in question with such additives. Testing of variants of the invention The testing of variants of the invention may suitably b performed by determining the starch-degrading activity of th variant, for instance by growing host cells transformed with DN A sequence encoding a variant on a starch-containing agaros plate and identifying starch-degrading host cells. Furthe tes t ing as to altered properties (including specific activity substrate specificity, cleavage pattern, thermoactivation, pH optimum, pH dependency, temperature optimum, and any other parameter) may be performed in accordance with methods known in the art. Expression of α-amylase variants 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 enzyme form, using an expression vector which typically includes control sequences encoding a promoter, operator, riboso e binding site, translation initiation signal, and, optionally, a repressor gene or various activator genes. The recombinant expression vector carrying the DNA sequence encoding an α-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 an α-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 Bacilluε li cheniformis α- amylase gene (amyL) , the promoters of the Bacillu stearothermophiluε maltogenic amylase gene (amyM) , the promo ters of the Bacilluε amyloliquefaciens α-amylase (amyQ) , th promoters of the Bacilluε subtiliε xylA and xylB genes etc. Fo transcription in a fungal host, examples of useful promoter are those derived from the gene encoding A . oryzae TAK amylase, Rhizomucor miehei aspartic proteinase, A . niger neu¬ tral α-amylase, A. niger acid stable α-amylase, A . niger glu- coamylase, Rhizomucor miehei lipase, A . oryzae alkaline protease, A. oryzae triose phosphate isomerase or A . nidulan acetamidase. The expression vector of the invention may also comprise a suitable transcription terminator and, in eukaryotes, poly- adenylation sequences operably connected to the DNA sequence encoding the α-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, pUBHO, pE194, pAMBl 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. εubtilis or B . licheniformiε , or one which confers antibiotic resistance such as ampicillin, kanamycin, chloramphenicol or tetracyclin resistance. Fur- thermore, the vector may comprise Aεpergilluε 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 Bacill uε 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, conveni¬ ently accomplished by substitution of the DNA sequences encod- ing the respective preregions. The procedures used to ligate the DNA construct of the inven¬ tion encoding an α-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 produc¬ tion of an α-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 grampositive bacteria such as Bacillus subtilis, Bacilluε licheniformiε, Bacilluε lentuε, Bacilluε breviε, Bacilluε εtearothermophilu , Bacilluε alkalo- philuε, Bacilluε a yloliquefacienε, Bacillus coagulans, Bacilluε circulanε, Bacilluε lautu , Bacillus megaterium, Ba¬ cilluε thuringienεiε, or Streptomyceε lividanε or Streptomyces murinuε, or gramnegative bacteria such as E.coli. The trans¬ formation of the bacteria may, for instance, be effected b 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. Saccharomyceε cerevisiae . The filamentous fungus may advantageously belong to a species of Aspergilluε, e . g . Aspergillus oryzae or Aspergil - lus niger. Fungal cells may be transformed by a process involv¬ ing 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 Aεpergilluε host cells is described in EP 238 023. In a yet further aspect, the present invention relates to a method of producing an α-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 cul¬ ture 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 α-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 α-amylase variant secreted from the host cells may con¬ veniently 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 sulphate, followed by the use of chromatographic procedures such as ion exchange chromatography, affinity chromatography, or the like. Industrial Applications The α-amylase variants of this invention possesses valuable properties allowing for various industrial applications. In particular the enzyme variants finds potential applications as a component in washing, dishwashing and hard surface cleaning detergent compositions, but it may also be useful in the production of sweeteners and ethanol from starch and for textile desizing. Conditions for conventional starch converting processes and liquefaction and/or saccharification processes are described in for instance US Patent No. 3,912,590 and EP patent publications Nos. 252,730 and 63,909. Production of sweetners from starch: A "traditional" process for conversion of starch to fructose syrups normally consists of three consecutive enzymatic processes, viz. a liquefaction process followed by a saccharification process and an isomerization process. During the liquefaction process, starch is degraded to dextrins by an α-amylase (e.g. Termamyl 1 ") at pH values between 5.5 and 6.2 and at temperatures of 95-160°C for a period of approx. 2h. In order to ensure an optimal enzyme stability under these conditions, lmM of calcium is added (40 ppm free calcium ions) . After the liquefaction process the dextrins are converted into dextrose by addition of a glucoamylase (e.g. AMG™) and a debranching enzyme, such as an isoamylase or a pullulanase (e.g. Promozyme™) . Before this step the pH is reduced to a value below 4.5, maintaining the high temperature (above 95°C) , and the liquefying α-amylase activity is denatured. The tem- perature is lowered to 60°C, and glucoamylase and debranching enzyme are added. The saccharification process proceeds for 24-72 hours. After the saccharification process the pH is increased to a value in the range of 6-8, preferably pH 7.5, and the calcium is removed by ion exchange. The dextrose syrup is then con¬ verted into high fructose syrup using, e.g., an immmobilized glucoseisomerase (such as Sweetzyme 7 At least 3 enzymatic improvements of this process could be ob¬ tained. All three improvements could be seen as individual benefits, but any combination (e.g. 1+2, 1+3, 2+3 or 1+2+3) could be employed: Improvement 1. Reduction of the calcium dependency of the liquefying alpha-amylase. Addition of free calcium is required to ensure adequately high stability of the α-amylase, but free calcium strongly inhibits the activity of the glucoseisomerase and needs to be removed, by means of an expensive unit operation, to an extent which reduces the level of free calcium to below 3-5 ppm. Cost savings could be obtained if such an operation could be avoided and the liquefaction process could be performed without addition of free calcium ions. To achieve that, a less calcium-dependent Termamyl-like α-amylase which is stable and highly active at low concentrations of free calcium (< 40 ppm) is required. Such a Termamyl-like α-amylase should have a pH optimum at a pH in the range of 4.5-6.5, preferably in the range of 4.5-5.5. Improvement 2. Reduction of formation of unwanted Maillard products The extent of formation of unwanted Maillard products during the liquefaction process is dependent on the pH. Low pH favours reduced formation of Maillard products. It would thus be desirable to be able to lower the process pH from around pH 6.0 to a value around pH 4.5; unfortunately, all commonly known, thermostable Termamyl-like α-amylases are not very stable at low pH (i.e. pH < 6.0) and their specific activity is generally low. Achievement of the above-mentioned goal requires a Termamyl- like α-amylase which is stable at low pH in the range of 4.5-5.5 and at free calcium concentrations in the range of 0-40 ppm, and which maintains a high specific activity. Improvement 3. It has been reported previously (US patent 5,234,823) that when saccharifying with A. niger glucoamylase and B . acidopullu- lyticus pullulanase, the presence of residual α-amylase activi¬ ty from the liquefaction process can lead to lower yields of dextrose if the α-amylase is not inactivated before the saccharification stage. This inactivation can typically be carried out by adjusting the pH to below 4.3 at 95 β C, before lowering the temperature to 60°C for saccharification. The reason for this negative effect on dextrose yield is not fully understood, but it is assumed that the liquefying α-amy¬ lase (for example Termamyl™ 120 L from B . licheniformiε) generates "limit dextrins" (which are poor substrates for B . acidopullulyticuε pullulanase) by hydrolysing 1,4-alpha- glucosidic linkages close to and on both sides of the branching points in amylopectin. Hydrolysis of these limit dextrins by glucoamylase leads to a build-up of the trisaccharide panose, which is only slowly hydrolysed by glucoamylase. The development of a thermostable α-amylase which does not suffer from this disadvantage would be a significant process improvement, as no separate inactivation step would be re¬ quired. If a Termamyl-like, low-pH-stable α-amylase is developed, an alteration of the specificity could be an advantage needed in combination with increased stability at low pH. The methodology and principles of the present invention make it possible to design and produce variants according to the invention having the required properties as outlined above. Detergent Compositions According to the invention, the α-amylase may typically be component of a detergent composition. As such, it may included in the detergent composition in the form of a no dusting granulate, a stabilized liquid, or a protected enzyme Non-dusting granulates may be produced, e.g. as disclosed in 4,106,991 and 4,661,452 (both to Novo Industri A/S) and ma optionally be coated by methods known in the art. Examples o waxy coating materials are poly(ethylene oxide) product (polyethyleneglycol, PEG) with mean molar weights of 1000 t 20000, ethoxylated nonylphenols having from 16 to 50 ethylen oxide units; ethoxylated fatty alcohols in which the alcoho contains from 12 to 20 carbon atoms and in which there are 1 to 80 ethylene oxide units; fatty alcohols; fatty acids; an mono- and di- and triglycerides of fatty acids. Examples o film-forming coating materials suitable for application b fluid bed techniques are given in patent GB 1483591. Liqui enzyme preparations may, for instance, be stabilized by addin a polyol such as propylene glycol, a sugar or sugar alcohol lactic acid or boric acid according to established methods Other enzyme stabilizers are well known in the art. Protecte enzymes may be prepared according to the method disclosed in E 238,216. The detergent composition of the invention may be in an convenient form, e.g. as powder, granules, paste or liquid. liquid detergent may be aqueous, typically containing up to 70 of water and 0-30% of organic solvent, or nonaqueous. The detergent composition comprises one or more surfactants each of which may be anionic, nonionic, cationic, or zwitter ionic. The detergent will usually contain 0-50% of anioni surfactant such as linear alkylbenzenesulfonate (LAS) , alpha olefinsulfonate (AOS) , alkyl sulfate (fatty alcohol sulfate) (AS) , alcohol ethoxysulfate (AEOS or AES) , secondary alkane sulfonates (SAS) , alpha-sulfo fatty acid methyl esters, alkyl or alkenylsuccinic acid or soap. It may also contain 0-40% o nonionic surfactant such as alcohol ethoxylate (AEO or AE) , carboxylated alcohol ethoxylates, nonylphenci ethoxylate, aikylpolyglycoside, alkyldimethylamineoxide, ethoxylated fatt acid monoethanolamide, fatty acid monoethanolamide, or poly- hydroxy alkyl fatty acid amide (e.g. as described in WO 92/06154) . The detergent composition may additionally comprise one or more other enzymes, such as lipase, cutinase, protease, cellulase, peroxidase, e.g., laccase. The detergent may contain 1-65% of a detergent builder or complexing agent such as zeolite, diphosphate, triphosphate, phosphonate, citrate, nitrilotriacetic acid (NTA) , ethylene- diaminetetraacetic acid (EDTA) , diethylenetriaminepentaacetic acid (DTMPA) , alkyl- or alkenylsuccinic acid, soluble sili¬ cates or layered silicates (e.g. SKS-6 from Hoechst) . The detergent may also be unbuilt, i.e. essentially free of detergent builder. The detergent may comprise one or more polymers. Examples are carboxymethylcellulose (CMC), poly(vinylpyrrolidone) (PVP) , polyethyleneglycol (PEG), poly(vinyl alcohol) (PVA) , polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers. The detergent may contain a bleaching system which may comprise a H 2 0 2 source such as perborate or percarbonate which may be combined with a peracid-forming bleach activator such as tetraacetylethylenediamine (TAED) or nonanoyloxybenzene- sulfonate (NOBS) . Alternatively, the bleaching system may comprise peroxy acids of e.g. the amide, imide, or sulfone type. The enzymes of the detergent composition of the invention may be stabilized using conventional stabilizing agents, e.g. a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative as e.g. an aromatic borate ester, and the composition may be formulated as described in e.g. WO 92/19709 and WO 92/19708. The detergent may also contain other conventional detergen ingredients such as e.g. fabric conditioners including clays foam boosters, suds suppressors, anti-corrosion agents, soil suspending agents, anti-soil redeposition agents, dyes, bactericides, optical brighteners, or perfume. The pH (measured in aqueous solution at use concentration) wil usually be neutral or alkaline, e.g. 7-11. Particular forms of detergent compositions within the scope o the invention include: 1) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 2) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 3) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 4) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 5) An aqueous liquid detergent composition comprising 6) An aqueous structured liquid detergent composition compris* ing 7) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 8 ) A detergent composition formulated as a granulate comprising 9) A detergent composition formulated as a granulate comprising 11) An aqueous liquid detergent composition comprising 12 ) A detergent composition formulated as a granulate havin a bulk density of at least 600 g/1 comprising 13) Detergent formulations as described in 1) - 12) wherein all or part of the linear alkylbenzenesulfonate is replaced by (C 12 - C lβ ) alkyl sulfate. 14) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 15 ) A detergent composition formulated as a granulate having a bulk density of at least 600 g/1 comprising 10 15 16) Detergent formulations as described in 1) - 15) which contain a stabilized or encapsulated peracid, either as an additional component or as a substitute for already specified bleach systems. 20 17) Detergent compositions as described in 1) , 3) , 7] 9) and 12) wherein perborate is replaced by percarbonate. 18) Detergent compositions as described in 1), 3), 7), 9) , 12), 14) and 15) which additionally contain a manganese catalyst. 25 The manganese catalyst may, e.g., be one of the compounds described in "Efficient manganese catalysts for low-temperature bleaching", Nature 369. 1994, pp. 637-639. 19) Detergent composition formulated as a nonaqueous detergent 30 liquid comprising a liquid nonionic surfactant such as, e.g., linear alkoxylated primary alcohol, a builder system ( e.g. phosphate) , enzyme and alkali. The detergent may also comprise anionic surfactant and/or a bleach system. 35 The α-amylase variant of the invention may be incorporated in concentrations conventionally employed in detergents. It is at present contemplated that, in the detergent composition of the inven t ion, the α-amylase may be added in an amount correspon- ding to 0.00001-1 mg (calculated as pure enzyme protein) of α- amylase per liter of wash liquor. Dishwashing Composition The dishwashing detergent composition comprises a surfactant which may be anionic, non-ionic, cationic, amphoteric or a mixture of these types. The detergent will contain 0-90% of non-ionic surfactant such as low- to non-foaming ethoxylated propoxylated straight-chain alcohols. The detergent composition may contain detergent builder salts of inorganic and/or organic types. The detergent builders may be subdivided into phosphorus-containing and non-phosphorus- containing types. The detergent composition usually contains 1- 90% of detergent builders. Examples of phosphorus-containing inorganic alkaline detergent builders, when present, include the water-soluble salts especially alkali metal pyrophosphates, orthophosphates, and polyphosphates. An example of phosphorus-containing organic alkaline detergent builder, when present, includes the water- soluble salts of phosphonates. Examples of non-phosphorus- containing inorganic builders, when present, include water- soluble alkali metal carbonates, borates and silicates as well as the various types of water-insoluble crystalline or amor¬ phous alumino silicates of which zeolites are the best-known representatives. Examples of suitable organic builders include the alkali metal, ammonium and substituted ammonium, citrates, succinates, malonates, fatty acid sulphonates, carboxymetoxy succinates, ammonium polyacetates, carboxylates, polycarboxylates, amino- polycarboxylates, polyacetyl carboxylates and polyhy- droxsulphonates. Other suitable organic builders include the higher molecular weight polymers and co-polymers known to have builder prop¬ erties, for example appropriate polyacrylic acid, polymaleic and polyacrylic/polymaleic acid copolymers and their salts. The dishwashing detergent composition may contain bleachin agents of the chlorine/bromine-type or the oxygen-type. Examples of inorganic chlorine/bromine-type bleaches are li¬ thium, sodium or calcium hypochlorite and hypobromite as well as chlorinated trisodium phosphate. Examples of organic chlo¬ rine/bromine-type bleaches are heterocyclic N-bromo and N- chloro imides such as trichloroisocyanuric, tribromoiso- cyanuric, dibromoisocyanuric and dichloroisocyanuric acids, and salts thereof with water-solubilizing cations such as potassium and sodium. Hydantoin compounds are also suitable. The oxygen bleaches are preferred, for example in the form of an inorganic persalt, preferably with a bleach precursor or as a peroxy acid compound. Typical examples of suitable peroxy bleach compounds are alkali metal perborates, both tetra- hydrates and monohydrates, alkali metal percarbonates, per- silicates and perphosphates. Preferred activator materials are TAED and glycerol triacetate. The dishwashing detergent composition of the invention may be stabilized using conventional stabilizing agents for the enzyme(s), e.g. a polyol such as e.g.propylene glycol, a sugar or a sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g. an aromatic borate ester. The dishwashing detergent composition of the invention may also contain other conventional detergent ingredients, e.g. deflocculant material, filler material, foam depressors, anti- corrosion agents, soil-suspending agents, sequestering agents, anti-soil redeposition agents, dehydrating agents, dyes, bactericides, fluorescers, thickeners and perfumes. Finally, the α-amylase variant of the invention may be used in conventional dishwashing detergents, e.g. in any of the detergents described in any of the following patent publica¬ tions: EP 518 7 1 9, EP 518720, EP 518721, EP 516553, E? 516554, EP 516555, GB 2200132, DE 3741617, DE 3727911, DE 4212166, DE 4137470, DE 3833047, WO 93/17089, DE 4205071, WO 52/09680, WO 93/18129, WO 93/04153, WO 92/06157, WO 92/08777, EP 429124, WO 93/21299, US 5141664, EP 561452, EP 561446, GB 2234980, WO 93/03129, EP 481547, EP 530870, EP 533239, EP 554943, EP 346137, US 5112518, EP 318204, EP 318279, EP 271155, EP 271156, EP 346136, GB 2228945, CA 2006687, WO 93/25651, EP 530635, EP 414197, US 5240632. EXAMPLES EXAMPLE 1 Example on Homology building of TERM The overall homology of the B. licheniformis α-amylase (in the following referred to as TERM) to other Termamyl-like α- amylases is high and the percent similarity is extremely high. The similarity calculated for TERM to BSG (the B. stearothermophilus α-amylase with SEQ ID NO 6) , and BAN (the B. amyloliquefacienε α-amylase with SEQ ID NO 4) using the University of Wisconsin Genetics Computer Group's program GCG gave 89% and 78%, respectively. TERM has a deletion of 2 residues between residue G180 and K181 compared to BAN and BSG. BSG has a deletion of 3 residues between G371 and 1372 in comparison with BAN and TERM. Further BSG has a C-terminal extension of more than 20 residues compared to BAN and TERM. BAN has 2 residues less and TERM has one residue less in the N-terminal compared to BSG. The structure of the B. licheniformiε (TERM) and of the B . amyloliquefacienε α-amylase (BAN) , respectively, was model built on the structure disclosed in Appendix 1 herein. The structure of other Termamyl-like α-amylases (e.g. those dis¬ closed herein) may be built analogously. In comparison with the α-amylase used for elucidating the pr sent structure, TERM differs in that it lacks two residu around 178-182. In order to compensate for this in the mod structure, the HOMOLOGY program from BIOSYM was used substitute the residues in equivalent positions in t structure (not only structurally conserved regions) except f the deletion point. A peptide bond was established betwe G179(G177) and K180(K180) in TER (BAN) . The close structur relationship between the solved structure and the mod structure (and thus the validity of the latter) is indicated the presence of only very few atoms found to be too clo together in the model. To this very rough structure of TERM was then added all wate (605) and ions (4 Calcium and 1 Sodium) from the solv structure (Appendix 1) at the same coordinates as for sai solved structure using the INSIGHT program. This could be don with only few overlaps - in other words with a very nice fit This model structure were then minimized using 200 steps o Steepest descent and 600 steps of Conjugated gradient (se Brooks et al 1983, J. Computational Chemistry 4, p.187-217) The minimized structure was then subjected to molecula dynamics, 5ps heating followed by up to 200ps equilibration bu more than 35ps. The dynamics as run with the Verlet algorith and the equilibration temperature 300K were kept using the Beh rendsen coupling to a waterbath (Berendsen et. al., 1984, J Chemical Physics 81, p. 3684-3690) . Rotations and translation were removed every picosecond. The potential energy becam stable after appr. 35ps equilibration. A mean dynamics struc ture was extracted and can be used for further analysis. EXAMPLE 2 Determination of residues within 10A from the ions present i the solved structure The coordinates of Appendix 1 are read into the INSIGHT progra provided by BIOSYM tecnologies. The spatial coordinates ar presented showing the bonds between the atoms. The ions are presented as well as the water atoms. The program package part of creating subset are used to create a 10A subset around the Calcium and the Sodium ions in the structure using the command ZONE. All residues having an atom within the 10A are compiled and written out by the LIST MOLECULE command. By giving the ions the name ium in the coordinate file a lOA sphere around all atoms called ium is compiled. The specific residues identified in this manner are given further above in the section entitled "Ca 2 * dependency" . EXAMPLE 3 Determination of cavities in the solved structure (Appendix 1) The solved structure exhibits many internal holes and cavities. When analysing for such cavities the Connolly program is nor¬ mally 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 hole 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 were used. First 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 were calculated for all atoms and residues using a probe radius of 1.4A, and displayed on the graphics screen together with the model of the solved structure. The internal cavities where then seen as dot surfaces with no connections to external surface. Mutant suggestions for filling out the holes are given in the specification (in the section entitled "Variants with increased thermostability and/or altered temperature optimum") . By using the homology build structures or/and the sequence alignment mutations for the homologous structures of TERM and BSG and BAN can be made. EXAMPLE 4 Construction of Termamyl 1 " variants in accordance with the invention Termamyl (SEQ ID NO. 2) is expressed in B . subtiliε from a plasmid denoted pDN1528. This plasmid contains the complete gene encoding Termamyl, amyL, the expression of which is directed by its own promoter. Further, the plasmid contains the origin of replication, ori , from plasmid pUBHO and the cat gene from plasmid pC194 conferring resistance towards chloramphenicol. pDN1528 is shown in Fig. 9. A specific mutagenesis vector containing a major part of the coding region of SEQ ID NO 1 was prepared. The important features of this vector, denoted pJeENl, include an origin of replication derived from the pUC plasmids, the cat gene conferring resistance towards chloramphenicol, and a frameshift-containing version of the bla gene, the wild type of which normally confers resistance towards ampicillin (amp R phenotype) . This mutated version results in an amp s phenotype. The plasmid pJeENl is shown in Fig. 10, and the E. coli origin of replication, ori , bla, cat , the 5' -truncated version of the Termamyl amylase gene, and selected restriction sites are indicated on the plasmid. Mutations are introduced in amyL by the method described by Deng and Nickoloff (1992, Anal. Biochem. 200. pp. 81-88) except that plasmids with the "selection primer" (primer #6616; see below) incorporated are selected based on the amp R phenotype of transformed E. coli cells harboring a plasmid with a repaired Jbla gene, instead of employing the selection by restriction enzyme digestion outlined by Deng and Nickoloff. Chemicals and enzymes used for the mutagenesis were obtained from the Chameleon 1 " mutagenesis kit from Stratagene (catalogue number 200509) . After verification of the DNA sequence in variant plasmids, the truncated gene, containing the desired alteration, is subcloned into pDN1528 as a Pstl-EcoRI fragment and transformed into a protease- and amylase-depleted Bacilluε subtilis strain in order to express the variant enzyme. The Termamyl variant V54W was constructed by the use of the following mutagenesis primer (written 5' to 3', left to right) : PG GTC GTA GGC ACC GTA GCC CCA ATC CGC TTG The Termamyl variant A52W + V54W was constructed by the use of the following mutagenesis primer (written 5' to 3', left to right) : PG GTC GTA GGC ACC GTA GCC CCA ATC CCA TTG GCT CG Primer #6616 (written 5' to 3' , left to right; P denotes a 5' phosphate) : P CTG TGA CTG GTG AGT ACT CAA CCA AGT C EXAMPLE 5 Saccharification in the presence of "residual" α-amylase activity Two appropriate Termamyl variants with altered specificity were evaluated by saccharifying a DE 10 (DE = dextrose equivalent) maltodextrin substrate with A . niger glucoamylase and B . acidopullulyticus pullulanase under conditions where the variant amylase was active. Saccharification: Substrates for saccharification were prepared by dissolving 230 g DE 10 spray-dried maltodextrin, prepared from common corn starch, in 460 ml boiling deionized water an adjusting the dry substance (DS) content to approximately 30 w/w. The pH was adjusted to 4.7 (measured at 60°C) and aliquot of substrate corresponding to 15 g dry weight were transferre to 50 ml blue cap glass flasks. The flasks were then placed in a shaking water bat equilibrated at 60°C, and the enzymes added. The pH was readjusted to 4.7 where necessary. The following enzymes were used: Glucoamylase: AMG 1 " (Novo Nordisk A/S); dosage 0.18 AG/g DS Pullulanase: Promozyme 1 " (Novo Nordisk A/S) ; dosage 0.06 PUN/g DS α-Amylases: Termamyl 1 " (Novo Nordisk A/S) ; dosage 60 NU/g DS Termamyl variant V54W; dosage 60 NU/g DS Termamyl variant V5 W + A52W; dosage 60 NU/g DS 2 ml samples were taken periodically. The pH of each sample was adjusted to about 3.0, and the sample was then heated in a boiling water bath for 15 minutes to inactivate the enzymes. After cooling, the samples were treated with approximately 0.1 g mixed-bed ion exchange resin (BIO-Rad 501-X (D) ) for 30 minutes on a rotary mixer and then filtered. The carbohydrate composition of each sample was determined by HPLC. The following results were obtained after 72 hours [DP n denotes a dextrose (D-glucose) oligomer with n glucose units] : α-amylase %DP. %DP 2 %DP 3 %DP 4 1 . 0 0 . 8 0 . 8 0 . 8 It can be seen from the above results that compared with the control (no α-amylase activity present during liquefaction) , the presence of α-amylase activity from variants V54W and V54W + A52W did not lead to elevated panose (DP 3 ) levels. In contrast, Termamyl α-amylase activity resulted in higher levels of panose and a subsequent loss of D-glucose (DP- t ) yield. Thus, if α-amylase variants V54W or V54W + A52W are used for starch liquefaction, it will not be necessary to inactivate the residual α-amylase activity before the commencement of saccharification. EXAMPLE 6 Calcium-binding affinity of α-amylase variants of the invention Unfolding of amylases by exposure to heat or to denaturants such as guanidine hydrochloride is accompanied by a decrease in fluorescence. Loss of calcium ions leads to unfolding, and the affinity of α-amylases for calcium can be measured by fluorescence measurements before and after incubation of each α-amylase (e.g. at a concentration of 10 μg/ml) in a buffer (e.g. 50 mM HEPES, pH 7) with different concentrations of calcium (e.g. in the range of 1 /xM-100 mM) or of EGTA (e.g. in the range of 1-1000 μM) [EGTA = 1,2-di (2-aminoethoxy)ethane- N, N, N' , N' -tetraacetic acid] 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] / ( K dlss + [Ca] ) (α N - jB„log ( [Ca] ) ) + K ilss / ( K dlss + [Ca] ) ( a υ - jS„log ( [Ca] ) ) where α N is the fluorescence of the native (folded) form of the enzyme, β_. s the linear dependence of α N on the logarithm of the calcium concentration (as observed experimentally) , at υ is the fluorescence of the unfolded form and β v is the linear dependence of α σ on the logarithm of the calcium concentration, iζi^ s is the apparent calcium-binding constant for an equilibrium process as follows: N-Ca «-» U + Ca (N - native enzyme; U = unfolded enzyme) In fact, unfolding proceeds extremely slowly and is irreversible. The rate of unfolding is a dependent on calcium concentration, and the dependency for a given α-amylase provides a measure of the Ca-binding affinity of the enzyme. By defining a standard set of reaction conditions (e.g. 22 hours at 55°C) , a meaningful comparison of ^^ for different α- amylases can be made. The calcium dissociation curves for α-amylases in general can be fitted to the equation above, allowing determination of the corresponding values of Ka^ . The following values for J^ iee were obtained for a parent Termamyl-like α-amylase having the amino acid sequence shown in SEQ ID No. 1 of WO 95/26397 and for the indicated variant thereof according to the invent ion : α-Amylase (mol/1) L351C + M430C + T183* + G184* 1.7 (±0.5) x 10 "3 Parent 3.5 (±1.1) x 10 "1 It is apparent from the above that the calcium-binding affinity of the variant in question binds calcium significantly more strongly than the parent, and thereby has a correspondingly lower calcium dependency than the parent. 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 Cryεtallogr. 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.l, No. 5-6, p. B. Diderichsen and L. Christiansen, Cloning of a maltogenic α- amylase from Bacillus stearothermophiluε, FEMS Microbiol. let¬ ters: 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. 147-1 Hunkapiller et al., 1984, Nature 310:105-111 R. Higuchi, B. Krummel, and R.K. Saiki (1988) . A general meth of in vi tro preparation and specific mutagenesis of DNA fra ments: study of protein and DNA interactions. NucI . Acidε Re 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. Νatl. Acad. Sci. 74, pp. 1680-1682. Boel et al . , 1990 , Biochemistry 29 . pp . 6244 -6249 . SEQUENCE LISTING In the following SEQ ID Nos. 1, 3, 5 the 5', coding sequence and 3' sequence of the relevant α-amylase genes are illus- trated. The 5' sequence is the first separate part of the sequ¬ ence written with lower case letters, the coding sequence is the intermediate part of the sequence, where the signal sequen¬ ce is written with lower case letters and the sequence encoding the mature α-amylase is written with upper case letters, and the 3' sequence is the third separate part of the sequence written with lower case letters. SEQ ID No. 1 cggaagattggaagtacaaaaataagcaaaagattgtcaatcatgtcatgagccatgcgg- gagacggaaaaatcgtctta atgcacgatatttatgcaacgttcgcagatgctgctgaa- gagattattaaaaagctgaaagcaaaaggctatcaattggt aactgtatctcagcttga- agaagtgaagaagcagagaggctattgaataaatgagtagaagcgccatatcggcgcttttc ttttggaagaaaatatagggaaaatggtacttgttaaaaattcggaatatttatacaacatc- atatgtttcacattgaaa ggggaggagaatc atgaaacaacaaaaacggctttacgcccgattgctgacgctgttatttgcgctcatcttctt - gctgc ctcattctgcagcagcggcgGCAAATCTTAATGGGACGCTGATGCAGTATTTT- GAATGGTACATGCCCAATGACGGCCAA CATTGGAGGCGTTTGCAAAACGACTCGGCATAT- TTGGCTGAACACGGTATTACTGCCGTCTGGATTCCCCCGGCATATAA GGGAACGAGC - CAAGCGGATGTGGGCTACGGTGCTTACGACCTTTATGATTTAGGGGAGTTTCATCAAAAAG- GGACGGTTC GGACAAAGTACGGCACAAAAGGAGAGCTGCAATCTGCGATCAAAAGTCTTC - ATTCCCGCGACATTAACGTTTACGGGGAT GTGGTCATCAACCACAAAGGCGGCGCTGA - TGCGACCGAAGATGTAACCGCGGTTGAAGTCGATCCCGCTGACCGCAACCG CGTAATTT- CAGGAGAACACCTAATTAAAGCCTGGACACATTTTCATTTTCCGGGGCGCGGCAGCACATA- CAGCGATTTTA AATGGCATTGGTACCATTTTGACGGAACCGATTGGGACGAGTCCCGAAA- GCTGAACCGCATCTATAAGTTTCAAGGAAAG GCTTGGGATTGGGAAGTTTCCAATGAA- AACGGCAACTATGATTATTTGATGTATGCCGACATCGATTATGACCATCCTGA TGTCGCAG - CAGAAATTAAGAGATGGGGCACTTGGTATGCCAATGAACTGCAATTGGACGGTTTCCGTCTT - GATGCTGTCA AACACATTAAATTTTCTTTTTTGCGGGATTGGGTTAATCATGTCAGGG - AAAAA C G G G GAAG GAAAT GT T TA C GG TAG C T GAATAT T G G CA G AT - GACTTGGGCGCGCTGGAAAACTATTTGAACAAAACAAATTTTAATCATTCAGTGTTTGAC- GTGCC GCTTCATTATCAGTTCCATGCTGCATCGACACAGGGAGGCGGCTATGATATGAG GAAATTGCTGAACGGTACGGTCGTTT CCAAGCATCCGTTGAAATCGGTTACATTTGTCG ATAACCATGATACACAGCCGGGGCAATCGCTTGAGTCGACTGTCCAA ACATGGTTTAAG CCGCTTGCTTACGCTTTTATTCTCACAAGGGAATCTGGATACCCTCAGGTTTTCTACGGG GATATGTA CGGGACGAAAGGAGACTCCCAGCGCGAAATTCCTGCCTTGAAACACAAAAT TGAACCGATCTTAAAAGCGAGAAAACAGT ATGCGTACGGAGCACAGCATGATTATTTCGAC CACCATGACLATTGTCGGCrTGGACAAGGGAAGGCGACAGCTCGGTTGCA AATTCAGGTTTGG CGGCATTAATAACAGACGGACCCGGTGGGGCAAAGCGAATGTATGTCGGCCGGCA AAACGCCGGTGA GACATGGCATGACATTACCGGAAACCGTTCGGAGCCGGTTGTCATCA ATTCGGAAGGCTGGGGAGAGTTTCACGTAAACGGCGGGTCGGTTTCAATTTATGTTCAAA GATAG aagagcagagaggacggatttcctgaaggaaatccgtttttttatttt SEQ ID No. 2 ANLNGTLMQYFEWYMPNDGQHWRRLQNDSAYLAEHGITAV WIPPAYKGTSQADVGYGAYDLYDLGEFHQKGTVRTKYGTK GELQSAIKSLHSRDINVYGDWINHKGGADATEDVTAVEV DPADRNRVISGEHLIKAWTHFHFPGRGSTYSDFKWHWYHF DGTDWDESRKLNRIYKFQGKAWDWEVSNENGNYDYLMYAD IDYDHPDVAAEIKRWGTWYANELQLDGFRLDAVKHIKFSF LRDWVNHVREKTGKEMFTVAEYWQNDLGALENYLNKTNFN HSVFDVPLHYQFHAASTQGGGYDMRKLLNGTWSKHPLKS VTFVDNHDTQPGQSLESTVQTWFKPLAYAFILTRESGYPQ VFYGDMYGTKGDSQREIPALKHKIEPILKARKQYAYGAQH DYFDHHDIVGWTREGDSSVANSGLAALITDGPGGAKRMYV GRQNAGETWHDITGNRSEPWINSEGWGEFHVNGGSVSIY VQR SEQ ID No. 3 g cccc g cacatac g aaaagactggctgaaaacattgagcctttgatgactgatgatttgg- ctgaagaagtggatcgattg tttgagaaaagaagaagaccataaaaataccttgtctg - catcagacagggtattttttatgctgtccagactgtccgct gtgtaaaaataaggaata- aag gggggtt g tt a tt attttactgatatgtaaaatataatttgtataagaaaatgagaggg agaggaaac atgattcaaaaacgaaagcggacagtttcgttcagacttgtgcttatgtgcacgctgtt - atttgtcagttt gccgattacaaaaacatcagccGTAAATGGCACGCTGATGCAGTATT- TTGAATGGTATACGCCGAACGACGGCCAGCATT GGAAACGATTGCAGAATGATGCGGAA - CATTTATCGGATATCGGAATCACTGCCGTCTGGATTCCTCCCGCATACAAAGGA TTGAG - 5 CCAATCCGATAACGGATACGGACCTTATGATTTGTATGATTTAGGAGAATTCCAGCAAAA- AGGGACGGTCAGAAC GAAATACGGCACAAAATCAGAGCTTCAAGATGCGATCGGCTCAC - TGCATTCCCGGAACGTCCAAGTATACGGAGATGTGG TTTTGAATCATAAGGCTGGTGCT - GATGCAACAGAAGATGTAACTGCCGTCGAAGTCAATCCGGCCAATAGAAATCAGGAA ACTTCGGAGGAATATCAAATCAAAGCGTGGACGGATTTTCGTTTTCCGGGCCGTGGAAAC- 0 ACGTACAGTGATTTTAAATG GCATTGGTATCATTTCGACGGAGCGGACTGGGATGAATCCC- GGAAGATCAGCCGCATCTTTAAGTTTCGTGGGGAAGGAA AAGCGTGGGATTGGGAAGTAT - CAAGTGAAAACGGCAACTATGACTATTTAATGTATGCTGATGTTGACTACGACCACCCT GATGTCGTGGCAGAGA(_-AAAAAAATGGGGTATCTGGTATGCGAATGAACTGTCATTAGACGG- CTTCCGTATTGATGCCGC CAAACATATTAAATTTTCATTTCTGCGTGATTGGGTTCAGG - 5 CGGTCAGACAGGCGACGGGAAAAGAAATGTTTACGGTTG CGGAGTATTGGCAG- AATAATGCCGGGAAACTCGAAAACTACTTGAATAAAACAAGCTTTAATCAATCCGTGTTT- GATGTT CCGCTTCATTTCAATTTACAGGCGGCTTCCTCACAAGGAGGCGGATATGATAT - GAGGCGTTTGCTGGACGGTACCGTTGT GTCCAGGCATCCGGAAAAGGCGGTTACATTTGT - TGAAAATCATGACACACAGCCGGGACAGTCATTGGAATCGACAGTCC AAACTTGGTTTAA - o ACCGCTTGCATACGCCTTTATTTTGACAAGAGAATCCGGTTATCCTCAGGTGTTCTATGGG - GATATG TACGGGACAAAAGGGACATCGCCAAAGGAAATTCCCTCACTGAAAGATAATATA - GAGCCGATTTTAAAAGCGCGTAAGGA GTACGCATACGGGCCCCAGCACGATTATATTGAC - CACCCGGATGTGATCGGATGGACGAGGGAAGGTGACAGCTCCGCCG CCAA - ATCAGGTTTGGCCGCTTTAATCACGGACGGACCCGGCGGATCAAAGCGGATGTATGCCGG- 5 CCTGAAAAATGCCGGC GAGACATGGTATGACATAACGGGCAACCGTTCAGATACTGTAA- AAATCGGATCTGACGGCTGGGGAGAGTTTCATGTAAA CGATGGGTCCGTCTCCATTTAT - GTTCAGAAATAA ggtaataaaaaaacacctccaagctgagtgcgggtatcagcttgga ggtgcgtttattt - 0 tttcagccgtatgacaaggtcggcatcaggtgtgacaaatacggtatgctggctgtcata - ggtgaca aatccgggttttgcgccgtttggctttttcacatgtctgatttttgtataat - caacaggcacggagccggaatctttcgc cttggaaaaataagcggcgatcgtagctgct - tccaatatggattgttcatcgggatcgctgcttttaatcacaacgtggg atcc SEQ ID No . 4 VNGTLMQYFEWYTPNDGQHWKRLQNDAEHLSDIGITAVWI PPAYKGLSQSDNGYGPYDLYDLGEFQQKGTVRTKYGTKSE 5 LQDAIGSLHSRNVQVYGDWLNHKAGADATEDVTAVEVNP ANRNQETSEEYQIKAWTDFRFPGRGNTYSDFKWHWYHFDG ADWDESRKISRIFKFRGEGKAWDWEVSSENGNYDYLMYAD VDYDHPDWAETKKWGIWYANELSLDGFRIDAAKHIKFSF LRDWVQAVRQATGKEMFTVAEYWQNNAGKLENYLNKTSFN 0 QSVFDVPLHFNLQAASSQGGGYDMRRLLDGTWSRHPEKA VTFVENHDTQPGQSLESTVQTWFKPLAYAFILTRESGYPQ VFYGDMYGTKGTSPKEIPSLKDNIEPILKARKEYAYGPQH DYIDHPDVIGWTREGDSSAAKSGLAALITDGPGGSKRMYA GLKNAGETWYDITGNRSDTVKIGSDGWGEFHVNDGSVSIY SEQ ID No. 5 aaattcgatattgaaaacgattacaaataaaaattataatagacgtaaacgttcgagggt 0 ttgctccctttttactcttt ttatgcaatcgtttcccttaattttttggaagccaaacc- gtcgaatgtaacatttgattaagggggaagggcatt gtgct aacgtttcaccgcatcattcgaaaaggatggatgttcctgctcgcgtt- tttgctcactgtctcgctgttctgcccaacag gacagcccgccaaggctGCCGCACCGT- 5 TTAACGGCACCATGATGCAGTATTTTGAATGGTACTTGCCGGATGATGGCACG TTATGG- ACCAAAGTGGCCAATGAAGCCAACAACTTATCCAGCCTTGGCATCACCGCTCTTTGGCTG- CCGCCCGCTTACAA AGGAACAAGCCGCAGCGACGTAGGGTACGGAGTATACGACTTGTA- TGACCTCGGCGAATTCAATCAAAAAGGGACCGTCC GCACAAAATACGGAACAAAAGCTC- AATATCTTCAAGCCATTCAAGCCGCCCACGCCGCTGGAATGCAAGTGTACGCCGAT GTC- o GTGTTCGACCATAAAGGCGGCGCTGACGGCACGGAATGGGTGGACGCCGTCGAAGTCAAT- CCGTCCGACCGCAACCA AGAAATCTCGGGCACCTATCAAATCCAAGCATGGACGAAATT- TGATTTTCCCGGGCGGGGCAACACCTACTCCAGCTTTA AGTGGCGCTGGTACCATTTTG- ACGGCG TT GA TTGGG A CGAAAGCCGAAAATTGAGCCGCATTTACAAATTCCGCGGCATC GGC A AAG CG T GGGA TT GGGA AGTAGACACGGAAAACGGAAACTATGACTACTTAATGTAT- 5 GCCGACCTTGATATGGATCA TCCCGAAGTCGTGACCGAGCTGAAAAACTGGGGGAAATG- GTATGTCAACACAACGAACATTGATGGGTTCCGGCTTGATG CCGTCAAGCATATTAAGT- T C A G TTTTTTTCCTGATTGGTTGTCGTATGTGCGTTCTCAGACTG3CAAGCCGCTATTTACC GT CGGGG A A TATTGGAGCTATGACATCAACAAGTTGCACAATTA ATTAC3AAAACAGAC- GGAACGATGTCTTTGTTTGA TGCCCCGTTACACAACAAATTTTATACCG CTTCCAAATCAG - GGGGCGCATTTGATATGCGCACGTTAATGACCAATACTC TCATGAAAGATCAAC - CGACATTGGCCGTCACCTTCGTTGATAATCATGACACCGAACCCGGCCAAGCGC - TGCAGTCATGG GTCGACCCATGGTTCAAACCGTTGGCTTACGCCTTTATTCTAACTCGG - 5 CAGGAAGGATACCCGTGCGTCTTTTATGGTGA CTATTATGGCATTCCACAATATAACAT - TCCTTCGCTGAAAAGCAAAATCGATCCGCTCCTCATCGCGCGCAGGGATTATG CTTACG - GAACGCAACATGATTATCTTGATCΆCTCCGACATCATCGGGTGGACAAGGGAAGGGGGCA- CTGAAAAACCAGGA TCCGGACTGGCCGCACTGATCACCGATGGGCCGGGAGGAAGCAAA- TGGATGTACGTTGGCAAACAACACGCTGGAAAAGT GTTCTATGACCTTACCGGCAACCG - 0 GAGTGACACCGTCACC1AT<_^^ ( CAGTGATGGATGGGGGGAATTC_AAAGTC1AATGGCG GTT- CGGTTTCGGTTTGGGTTCCTAGAAAAACGACCGTTTCTACCATCGCTCGGCCGATCACAA- CCCGACCGTGGACTGGT GAATTCGTCCGTTGGACCGAACCACGGTTGGTGGCATGGCCTTGA tgcctgcga 5 SEQ ID No . 6 AAPFNGTMMQYFEWYLPDDGTLWTKVANEANNLSSLGITA o LWLPPAYKGTSRSDVGYGVYDLYDLGEFNQKGTVRTKYGT KAQYLQAI QAAHAAGMQVYADWFDHKGGADGTEWVDAVE VNPSDRNQE I SGTYQ I QAWTKFDFPGRGNTYSS FKWRWYH FDGVDWDESRKLSR I YKFRG I GKAWDWEVDTENGNYD YLM YADLDMDHPE WTELKNWGKWYVNTTN I DGFRLDAVKH I K 5 FSFFPDWLSYVRSQTGKPLFTVGEYWSYDINKLHNYITKT DGTMSLFDAPLHNKFYTASKSGGAFDMRTLMTNTLMKDQP TLAVTFVDNHDTEPGQALQSWVDPWFKPLAYAF I LTRQEG YPCVFYGDYYGI PQYNI PSLKSKIDPLLIARRDYAYGTQH DYLDHSD I I GWTREGGTEKPGSGLAAL I TDGPGGS KWMYV o GKQHAGKVFYDLTGNRSDTVTINSDGWGEFKVNGGSVSVW VPRKTTVSTIARPITTRPWTGEFVRWTEPRLVAW SEQ ID No . 10 5 1 ATPADWRSQS IYFLLTDRFA RTDGSTTATC 31 NTADQKYCGG TWQGIIDKLD YIQGMGFTAI 61 WITPVTAQLP QTTAYGDAYH GYWQQDIYSL SI NΞNYGTADDL KALSSALHER GMYLMVDWA 121 NHMGYDGAGS SVDYSVFKPF SSQDYFHPFC 151 FIQNYEDQTQ VEDCWLGDNT VSLPDLDTTK 181 DWKNEWYDW VGSLVSNYSI DGLRIDTVKH 211 VQKDFWPGYN KAAGVYCIGE VLDGDPAYTC 5 241 PYQNVMDGVL NYPIYYPLLN AFKSTSGSMD 271 DLYNMINTVK SDCPDSTLLG TFVENHDNPR 301 FASYTNDIAL AKNVAAFIIL NDGIPIIYAG 331 QEQHYAGGND PANREATWLS GYPTDSELYK 361 LIASANAIRN YAISKDTGFV TYKNWPIYKD 10 391 DITIAMRKGT DGSQIVTILS NKGASGDSYT 421 LSLSGAGYTA GQQLTEVIGC TTVTVGSDGN 451 VPVPMAGGLP RVLYPTEKLA GSKICSSS ATOM CB VAL 11.902 27.157 22.095 1.002386 ATOH 54 CB TYR 8 28.238 37.382 24.476 1.00 10.19 6 Al M CGI VAL 12.302 27.494 20.658 1.002408 ATOH 55 CG TYR 8 27.909 38.377 23.351 1.00 10.76 6 AIOH CG2 VAL 10.659 27.948 22.511 1.002637 ATOH 56 CD1 TYR 8 27.180 37.983 22.222 1.00 11.00 6 ATOM C VAL 13.030 25.096 22.743 1.0019.54 ATOH 57 CE1 TYR 8 26.891 38.842 21.190 1.00 11.22 6 ATOM 0 VAL 13.191 25.013 23.967 1.001986 ATOH 58 CD2 TYR 8 28.340 39.698 23.424 1.00 10.96 6 AIOH N VAL 10.702 25.241 23.415 1.0020.28 ATOH 59 CE2 TYR 8 28.080 40.620 22.423 1.00 11.25 6 AIOH CA VAL 11.659 25.658 22.335 1.0020.25 ATOH 60 CZ TYR 8 27.358 40.156 21.312 1.00 11.62 6 AIOH 8 H ASH 13.867 24.729 21.B02 1.001839 ATOH 61 OH TYR 8 27.114 41.063 20.294 1.00 11.87 8 AIIJH 9 CA ASH 15.168 24.197 22.212 1.001673 ATOH 62 C IYR 8 30.789 37.289 24.119 1.00 9.70 6 AIOH 10 CB ASH 15.836 23.657 20.945 1.0016.09 ATOH 63 0 TYR 8 30.918 38.427 24.563 1.00 9.67 8 Al .M 11 CG ASH 15.219 22.336 20.451 1.001533 ATOH 64 M PHE 9 31.890 36.710 23.639 1.00 9.16 7 AI'JH 12 001 ASH 14.707 21.549 21.252 1.001528 ATOH 65 CA PHE 9 33.191 37.307 23.588 1.00 9.15 6 Al W 13 ND2 ASH 15.283 22.082 19.151 1.0012.41 ATOH 66 CB PHE 9 33.805 37.750 24.941 1.00 8.08 6 _ ' JH 14 C ASH 15.969 25.334 22.767 1.0015.71 ATOH 67 CG PHE 9 33.968 36.659 25.978 1.00 9.21 6 AIJH 15 0 ASH 15.903 26.435 22.198 1.001602 ATOH 68 CD1 PHE 9 35.239 36.125 26.240 1.00 10.15 6 AJOH 16 H GLY 16.720 25.198 23.833 1.0014.56 ATOH 69 CD2 PHE 9 32.887 36.171 26.720 1.00 7.79 6 ■ fOH 17 CA GLY 17.541 26.305 24.331 1.001321 ATOH 70 CE1 PHE 9 35.440 35.161 27.245 1.00 10.23 6 0 AIOH 18 GLY 18.940 26.211 23.671 1.0012.14 ATOH 71 CE2 PHE 9 33.070 35.205 27.669 1.00 7.64 6 AIOH 19 GLY 19.498 25.153 23.302 1.0011.92 ATOH 72 CZ PHE 9 34.313 34.698 27.962 1.00 8.17 6 AIOH 20 1HR 19.503 27.368 23.499 1.0011.28 ATOH 73 C PHE 9 34.173 36.294 22.963 1.00 8.94 6 AIOH 21 CA 1IIR 20.829 27.555 22.912 1.0010.96 ATOH 74 0 PHE 9 33.903 35.102 22.918 1.00 8.65 8 AIOH 22 CB IHR 20.721 27.878 21.400 1.0011.09 ATOH 75 N GLU 10 35.284 36.856 22.536 1.00 9.09 7 AIOH 23 OG1 1HR 19.920 26.828 20.782 1.0012.31 ATOH 76 CA GLU 10 36.430 36.089 22.006 1.00 9.38 6 AIOH 24 CG2 IHR 22.048 27.933 20.693 1.00 8.99 ATOH 77 CB GLU 10 36.508 36.043 20.513 1.00 7.45 6 l AIOH 25 IHR 21.584 28.664 23.663 1.00 10.56 ATOH 78 CG GLU 10 36.604 37.345 19.740 1.00 7.55 6 AIOH 26 HR 21.080 29.743 23.866 1.00 9.98 ATOH 79 CD GLU 10 37.981 37.580 19.156 1.00 6.81 6 A10H 27 H LEU 22.809 28.376 24.092 1.00 1063 ATOH 80 OE1 GLU 10 38.145 38.544 18.397 1.00 8.43 8 AIOH 28 CA LEU 23.700 29.291 24.818 1.00 1069 ATOH 81 OE2 GLU 10 38.962 36.877 19.438 1.00 5.00 8 AIOH 29 CB LEU 24.515 28.477 25.789 1.00 9 ,31 ATOM 82 GLU 10 37.636 36.715 22.737 1.00 9.90 6 0 AIOH 30 CG LEU 25.429 28.946 26.864 1.00 10.96 ATOH 83 GLU 10 37.590 37.807 23.361 1.00 9.92 8 AIOH 31 CD1 LEU 24.887 30.150 27.608 1.00 .46 ATOH 84 N TRP 1 38.791 36.059 22.729 1.00 10.15 7 AIOH 32 C02 LEU 25.608 27.802 27.884 1.00 10.55 ATOH 85 CA TRP 1 39.980 36.551 23.407 1.00 10.35 6 AIOH 33 LEU 24.644 29.992 23.840 1.00 10.85 ATOH 86 CB TRP 1 41.182 35.619 23.186 1.00 9.98 6 AIOH 34 LEU 25.047 29.453 22.799 1.00 10.85 ATOH 87 CG TRP 1 42.271 35.940 24.181 1.00 11.61 6 AI H 35 H MET 25.031 31.217 24.123 1.00 10.88 ATOH 88 C02 TRP 1 42.292 35.583 25.565 1.00 12.44 6 AIOH 36 CA HEI 25.971 31.930 23.312 1.00 10.94 ATOH 89 CE2 TRP 1 43.516 36.063 26.103 1.00 12.84 6 AIOH 37 CB MET 25.455 33.143 22.507 1.00 12.97 ATOH 90 CE3 TRP 1 41.412 34.916 26.432 1.00 13.39 6 AIOH 38 CG HEI 26.629 33.643 21.638 1.00 15.17 ATOH 91 C01 TRP 1 43.446 36.606 23.915 1.00 11.78 6 AIOH 39 SD HET 26.027 34.480 20.185 1.00 19 .39 1 ATOH 92 NE1 TRP 1 44.188 36.673 25.083 1.00 12.99 7 AI H 40 CE HET 27.525 35.144 19.516 1.00 16 .94 ATOH 93 CZ2 TRP 1 43.831 35.890 27.441 1.00 13.37 6 AI H 41 HEI 27.089 32.485 24.223 1.00 10 .67 ATOH 94 CZ3 TRP 1 41.717 34.763 27.772 1.00 13.91 6 AIOH 42 MEI 26.774 33.206 25.170 1.00 10 .51 ATOH 95 CH2 TRP 1 42.946 35.256 28.280 1.00 14.23 6 AIOH 43 W GLH 28.325 32.133 23.911 1.00 10 .34 ATOH 96 C TRP 1 40.410 37.937 22.933 1.00 10.57 6 AIOH 44 CA GLH 29.440 32.727 24.681 1.00 10 .20 ATOH 97 0 TRP 1 40.843 38.709 23.797 1.00 10.47 8 AIOH 45 CB GLN 30.696 31.910 24.617 1.00 41 ATOH 98 N TYR 12 40.322 38.209 21.623 1.00 10.73 7 AIOH 46 CG GLH 31.967 32.632 25.053 1.00 10 .26 ATOH 99 CA TYR 12 40.766 39.508 21.126 1.00 11.11 6 AIOH 47 CD GLH 33.280 31.914 25.027 1.00 9 .15 ATOH 100 CB TYR 12 41.559 39.432 19.798 1.00 11.11 6 AIOH 48 0E1 GLH 34.327 32.470 25.449 1.00 12 .35 ATOH 101 CG TYR 12 42.765 38.515 20.029 1.00 11.60 6 AIOM 49 HE2 GLH 33.359 30.714 24.570 1.00 6 58 ATOH 102 CD1 TYR 12 42.605 37.158 19.704 1.00 11.95 6 AIOH 50 C GLH 29.578 34.125 24.015 1.00 .22 ATOH 103 CE1 TYR 12 43.666 36.268 19.892 1.00 12.43 6 AIOH 51 0 GLH 29.856 34.167 22.786 1.00 10 .30 ATOH 104 C02 TYR 12 43.985 38.951 20.540 1.00 11.48 6 AtOH 52 M IYR 29.394 35.236 24.691 1.00 9 97 ATOH 105 CE2 TYR 12 45.023 38.076 20.714 1.00 11.85 6 AIOH 53 CA IYR 29.467 36.526 24.022 1.00 9 95 ATOH 106 CZ TYR 12 44.870 36.749 20.388 1.00 12.61 6 AI OH 107 OH TYR A 12 45.854 35.787 20.560 1.00 13.18 8 ATOH 160 NE2 HIS 19 31.584 41.112 24.073 1 .00 9.42 7 AI OH 108 C TYR 12 39.687 40.574 20.991 1.00 11.38 6 ATOH 161 C HIS 19 30.007 45.489 25.132 1.00 9.04 6 A I OH 109 0 TYR 12 39.862 41.436 20.132 1.00 11.53 8 ATOH 162 0 HIS 19 29.153 44.838 24.493 1 .00 8.75 8 A I OH 110 N THR 13 38.630 40.547 21.783 1.00 11.49 7 ATOH 163 N TRP 20 29.650 46.184 26.217 1.00 9.17 7 AI OH 111 CA THR 13 37.651 41.656 21.700 1.00 11.50 6 ATOH 164 CA TRP 20 28.248 46.090 26.688 1 .00 9.56 6 A I OH 112 CB THR 13 36.604 41.321 22.761 1.00 13.32 6 ATOH 165 CB TRP 20 28.200 46.691 28.093 1.00 8.24 6 AI OH 113 OG1 THR 13 35.755 40.296 22.169 1.00 14.85 8 ATOH 166 CG TRP 20 29.112 46.119 29.122 1.00 7.50 6 A I H 114 CG2 THR 13 35.732 42.466 23.175 1.00 14.00 6 ATOH 167 C02 TRP 20 29.515 44.774 29.341 1.00 7.46 6 A I OH 115 C THR 13 38.489 42.880 22.036 1.00 11.41 6 ATOH 168 CE2 TRP 20 30.374 44.751 30.459 1.00 7.35 6 A I OH 116 O THR 13 39.429 42.805 22.840 1.00 11.13 8 ATOH 169 CE3 TRP 20 29.187 43.568 28.695 1.00 8.23 6 A I OH 117 H PRO 14 38.254 44.015 21.408 1.00 11.47 7 ATOH 170 C01 TRP 20 29.736 46.854 30.088 1.00 7.37 6 A I OH 118 CD PRO 14 37.184 44.144 20.397 1.00 11.68 6 ATOH 171 HE1 TRP 20 30.483 46.041 30.920 1.00 7.58 7 A IOH 119 CA PRO 14 38.979 45.243 21.611 1.00 11.44 6 ATOH 172 CZ2 TRP 20 30.926 43.591 31.006 1.00 6.78 6 <- I OM 120 CB PRO 14 38.477 46.296 20.569 1.00 11.60 6 ATOH 173 C23 TRP 20 29.750 42.407 29.223 1.00 9.26 6 - l oM 121 CG PRO 14 37.352 45.564 19.896 1.00 11.77 6 ATOH 174 CH2 TRP 20 30.608 42.427 30.366 1.00 7.69 6 M OH 122 C PRO 14 38.786 45.868 22.993 1.00 11.21 6 ATOH 175 C TRP 20 27.227 46.746 25.757 1.00 9.73 6 /» '. I OH 123 O PRO 14 37.703 45.785 23.618 1.00 11.15 8 ATOH 176 0 TRP 20 26.070 46.395 25.592 1.00 9.42 8 AI OH 124 H ASH 15 39.806 46.557 23.445 1.00 10.84 7 ATOH 177 H IYS 21 27.591 47.832 25.102 1.00 10.37 7 S A I OH 125 CA ASH 15 39.720 47.304 24.693 1.00 11.02 6 ATOH 178 CA LYS 21 26.731 48.544 24.144 1.00 11.41 6 /1 A I OH 126 CB ASN 15 41.073 47.318 25.411 1.00 11.27 6 AIOH 179 CB LYS 21 27.348 49.856 23.671 1.00 15.11 6 A IOH 127 CG ASH 15 41.055 48.247 26.614 1.00 11.89 6 ATOH 1B0 CG LYS 21 27.086 50.981 24.674 1.00 21.25 6 AIOH 128 001 ASH 15 40.008 48.358 27.277 1.00 12.57 8 ATOH 181 CD LYS 21 28.020 52.12B 24.411 1.00 25.92 6 A I OH 129 ND2 ASH 15 42.158 48.898 26.922 1.00 11.38 7 ATOH 182 CE LYS 21 27.600 53.426 25.067 1.00 30.86 6 A IOH 130 C ASH 15 39.240 48.737 24.377 1.00 11.05 6 ATOH 183 NZ LYS 21 27.119 54.448 24.030 1.00 34.41 7 o A I OH 131 O ASH 15 39.932 49.767 24.524 1.00 11.08 8 ATOH 184 C LYS 21 26.551 47.632 22.934 1.00 11.59 6 A I OH 132 N ASP 16 38.008 48.835 23.905 1.00 10.98 7 ATOH 185 0 LYS 21 25.474 47.562 22.400 1.00 11.80 8 A I OH 133 CA ASP 16 37.446 50.118 23.529 1.00 11.17 6 ATOH 186 N ARG 22 27.626 46.953 22.545 1.00 11.87 7 A I OH 134 CB ASP 16 36.924 50.059 22.068 1.00 11.99 6 ATOH 187 CA ARG 22 27.576 46.015 21.451 1.00 12.42 6 A I OH 135 CG ASP 16 35.761 49.101 21.873 1.00 12.89 6 ATOH 188 CB ARG 22 28.940 45.391 21.199 1 .00 12.84 6 __0 A I OH 136 ODl ASP 16 35.313 48.341 22.772 1.00 11.83 8 ATOH 189 CG ARG 22 29.804 46.215 20.240 1.00 13.26 6 C A I OH 137 002 ASP 16 35.244 49.114 20.732 1.00 14.31 8 ATOH 190 CD ARG 22 31.043 45.363 19.942 1.00 14.67 6 A I OH 138 C ASP 16 36.352 50.518 24.498 1.00 11.03 6 ATOH 191 NE ARG 22 32.084 45.253 20.955 1.00 14.04 7 A I OH 139 0 ASP 16 35.768 51.582 24.289 1.00 11.12 8 ATOH 192 CZ ARG 22 33.068 46.161 21.065 1.00 14.66 6 A I OH 140 H GLY 17 36.013 49.732 25.513 1.00 10.89 7 ATOH 193 NH1 ARG 22 33.913 45.855 22.063 1.00 13.42 7 o. AI OH 141 CA GLY 17 34.972 50.083 26.479 1.00 10.61 6 ATOH 194 HH2 ARG 22 33.206 47.242 20.261 1.00 12.34 7 A I OH 142 C GLY 17 33.545 50.032 25.938 1.00 10.65 6 ATOH 195 C ARG 22 26.586 44.921 21.812 1.00 12.77 6 AI OH 143 0 GLY 17 32.629 50.522 26.601 1.00 10.67 8 ATOH 196 0 ARG 22 25.682 44.543 21.038 1.00 13.11 8 A I OH 144 N GLH IB 33.287 49.436 24.766 1.00 10.50 7 ATOH 197 N LEU 23 26.678 44.342 23.002 1.00 12.84 7 A I OH 145 CA GLH 18 31.995 49.346 24.1S1 1.00 10.55 6 ATOH 198 CA LEU 23 25.698 43.292 23.370 1.00 12.86 6 A I OH 146 CB GLH 18 32.064 49.835 22.691 1.00 15.25 6 ATOH 199 CB LEU 23 26.092 42.716 24.721 1.00 10.68 6 A I ( 'H 147 CG GLH 18 32.718 51.182 22.436 1.0021.24 6 ATOH 200 CG LEU 23 25.126 41.739 25.361 1.00 10.16 6 A I OH K8 CD GLH IB 31.729 52.313 22.693 1.0025.84 6 ATOH 201 CD1 LEU 23 24.804 40.562 24.449 1.00 8.43 6 A I H 149 OE1 GLN 18 30.674 52.415 22.016 1.0029.22 8 ATOH 202 CD2 LEU 23 25.769 41.258 26.669 1.00 9.16 6 A I OH 150 NE2 GLH 18 32.104 53.124 23.668 1.0027.29 7 ATOH 203 C LEU 23 24.285 43.874 23.388 1.00 13.25 6 A IOH 151 C GLH IB 31.421 47.936 24.042 1.00 10.04 6 ATOH 204 0 LEU 23 23.302 43.247 22.969 1.00 12.84 8 A T CI . 152 0 GLH 18 30.467 47.808 23.281 1.00 9.96 8 ATOH 205 N GLH 24 24.144 45.123 23.873 1.00 13.66 7 A I OH 153 H HIS 19 31.986 46.944 24.702 1.00 9.66 7 ATOH 206 CA GLN 24 22.848 45.781 23.929 1.00 14.44 6 A I OH 154 CA HIS 19 31.440 45.572 24.582 1.00 9.29 6 ATOH 207 CB GLN 24 22.959 47.205 24.523 1.00 16.30 6 A I OH 155 CB HIS 19 32.412 44.535 25.162 1.00 6.70 6 ATOH 208 CG GLN 24 21.578 47.851 24.620 1.00 18.17 6 A im 156 CG HIS 19 32.091 43.173 24.563 1.00 8.79 6 ATOH 209 CO GLN 24 21.659 49.208 25.296 1.00 20.30 9 41.987 25.138 1.00 6 AIOH 157 CO2 HIS 19 31.74 7.93 6 ATOM 210 OE1 GLN 24 22.651 49.936 25.205 1.00 21.20 8 AI H 213 0 GLN 24 21.030 45.626 22.296 1.00 14 63 8 AI H 214 H ASN 25 23.034 46.369 21.594 1.00 14 90 7 AIOH 215 CA ASH 25 22.642 46.525 20.213 1.00 15 31 6 AIOH 216 CB ASH 25 23.645 47.256 19.304 1.00 18. 01 6 AIOH 217 CG ASN 25 23.711 48.719 19.680 1.00 22 28 6 AIOH 218 001 ASN 25 22.686 49.238 20.127 1.00 24 44 8 AIOH 219 HD2 ASH 25 24.B36 49.432 19.588 1.00 23 11 7 AIOH 220 C ASH 25 22.371 45.141 19.588 1.00 15 19 6 I H 221 0 ASN 25 21.542 45.198 18.637 1.00 15 31 8 AIOH 222 H ASP 26 22.954 44.059 20.051 1.00 14. 67 7 AIOH 223 CA ASP 26 22.647 42.765 19.394 1.00 14. 48 6 IOH 224 CB ASP 26 24.002 42.002 19.440 1.00 14. 63 6 AIOH 225 CG ASP 26 24.340 41.059 18.322 1.00 14. 74 6 <10H 226 001 ASP 26 23.651 41.073 17.292 1.00 14. 77 8 . IOH 227 002 ASP 26 25.294 40.238 18.363 1.00 14. 65 8 MOH 228 C ASP 26 21.497 41.933 19.949 1.00 14. 18 6 MOM 229 ASP 26 21.119 40.869 19.454 1.00 13. 76 8 AIOH 230 ALA 27 20.813 42.356 20.986 1.00 14. 32 7 0 AIOH 231 CA ALA 27 19.761 41.641 21.661 1.00 14. 78 6 1 AI H 232 CB ALA 27 19.276 42.463 22.849 1.00 12. 97 6 AI H 233 ALA 27 18.627 41.207 20.754 1.00 15. 34 6 AIOH 234 ALA 27 18.231 40.028 20.840 1.00 15. 56 8 AIOH 235 GLU 28 18.099 42.032 19.858 1.00 15. 76 7 AI H 236 CA GLU 28 17.010 41.598 18.984 1.00 16. 05 6 AIOH 237 CB GLU 28 16.526 42.815 18.170 1.00 23 00 6 AIOH 238 CG GLU 28 15.097 42.736 17.596 1.00 31 01 6 AIOH 239 CD GLU 28 14.001 42.258 18.547 1.0036 48 6 AIOH 240 OE1 GLU 28 13.644 41.013 18.587 1.00 40 .16 8 IOH 241 OE2 GLU 28 13.427 43.089 19.316 1.00 38 .33 8 AI H 242 C GLU 28 17.410 40.467 18.044 1.00 15 .55 6 AIOH 243 0 GLU 28 16.773 39.435 17.835 1.00 15 .27 8 AIOH 244 N HIS 29 18.577 40.712 17.415 1.00 15 .36 7 AIOH 245 CA HIS 29 19.158 39.769 16.461 1.00 15 .11 6 AIOH 246 CB HIS 29 20.492 40.422 16.008 1.00 16 .22 6 . AIOH 247 CG HIS 29 21.296 39.400 15.259 1.00 IB 29 6 AIOH 248 CD2 HIS 29 20.895 38.501 14.294 1.00 18 16 6 AIOH 249 HD1 HIS 29 22.639 39.155 15.496 1.00 18 52 7 AIOH 250 CE1 HIS 29 23.055 38.163 14.693 1.00 IB .61 6 AIOH 251 HE2 HIS 29 22.006 37.741 13.984 1.00 18 61 7 AIOH 252 C HIS 29 19.282 38.370 17.059 1.00 14 84 6 AI H 253 HIS 29 18.852 37.340 16.543 1.00 14 68 8 AIOH 254 LEU 30 19.913 3B.292 18.233 1.00 14 66 7 AI H 255 CA LEU 30 20.154 37.107 19.020 1.00 14 56 6 AIOH 256 CB LEU 30 20.913 37.409 20.319 1.00 13 60 6 ATOH 257 CG LEU 30 22.350 37.884 20.194 1.00 15 00 6 AI H 258 CD1 LEU 30 23.018 37.967 21.586 1.00 15 90 6 AIOH 259 CD2 LEU 30 23.229 37.049 19.292 1.00 14 94 6 AI H 260 C LEU 30 18.833 36.434 19.390 1.00 14 .68 6 ΛIOH 261 LEU 30 18.683 35.228 19.24B 1.00 14 21 8 ATOH 262 SER 31 17.877 37.240 19.879 1.00 15 37 7 AIOH 263 CA SER 31 16.596 36.559 20.204 1.00 16 15 6 AIOH 264 CB SER 31 15.603 37.378 21.005 1.00 17 .82 6 AIOH 265 OG SER 31 15.358 38.528 20.190 1.00 22 98 8 AIOH 319 C02 TRP 39 30.691 31.682 28.807 1.00 6.00 6 ATOH 72 CO LYS 45 39.093 48.021 37.024 1.00 5.00 6 IOH 320 CE2 TRP 39 31.875 32.074 29.473 1.00 5.58 6 ATOH 73 CE LYS 45 37.830 48.865 36.976 1.00 00 AIOH 321 CE3 TRP 39 30.708 30.585 27.908 1.00 5.00 6 ATOH 74 NZ LYS 45 37.599 49.990 37.908 1.00 00 α AIOH 322 CD1 TRP 39 30.201 33.372 30.190 1.00 5.74 6 ATOM 75 C LYS 45 39.029 44.010 37.657 1.00 87 AIOH 323 HE1 TRP 39 31.568 33.153 30.268 1.00 5.57 7 ATOH 76 LYS 45 39.207 43.306 38.636 1.00 70 ID D AIOH 324 CZ2 TRP 39 33.099 31.441 29.211 1.00 5.00 6 ATOH 77 GLY 46 39.847 43.978 36.608 1.00 09 7 0. AIOH 325 CZ3 TRP 39 31.955 29.964 27.701 1.00 5.00 6 ATOH 78 CA GLY 46 41.017 43.149 36.478 1.00 70 6 κ AIOH 326 CH2 TRP 39 33.115 30.400 28.307 1.00 5.00 6 ATOH 79 C GLY 46 42.246 43.917 36.957 1.00 7.41 6 AIOH 327 C TRP 39 28.317 35.078 28.452 1.00 8.53 6 ATOH 80 0 GLY 46 42.171 45.098 37.382 1.00 7.54 8 AIOH 328 TRP 39 28.856 35.399 27.384 1.00 8.32 8 ATOH 81 N LEU 47 43.420 43.291 36.970 1.00 7.77 7 AIOH 329 ILE 40 28.431 35.945 29.459 1.00 8.37 7 ATOH 82 CA LEU 47 44.681 43.889 37.385 1.00 8.34 6 AIOH 330 CA ILE 40 29.143 37.247 29.467 1.00 B.51 6 ATOH 83 CB LEU 47 45.838 42.922 37.455 1.00 9.18 6 IOH 331 CB ILE 40 28.091 38.113 30.259 1.00 9.85 6 ATOH 84 CG LEU 47 46.426 42.140 36.297 1.00 11.32 6 IOH 332 CG2 ILE 40 28.089 38.802 31.613 1.00 9.64 6 ATOH 85 CDl LEU 47 45.419 41.207 35.660 1.00 12.40 6 ■ IOH 333 CGI ILE 40 27.803 39.287 29.286 1.00 9.52 6 ATOH 86 CD2 LEU 47 46.897 42.995 35.137 1.00 12.34 6 AIOH 334 CD1 ILE 40 26.594 38.637 28.616 1.00 11.76 6 ATOH 87 C LEU 47 45.040 45.105 36.483 1.00 8.70 6 11OH 335 C ILE 40 30.524 37.121 30.063 1.00 8.39 6 ATOH 88 0 LEU 47 45.884 45.929 36.872 1.00 B.67 8 C AIOH 336 HE 40 30.680 36.373 31.033 1.00 8.04 8 ATOH 89 N SER 48 44.451 45.283 35.303 1.00 8.86 7 00 AIOH 337 PRO 41 31.571 37.800 29.564 1.00 8.30 7 ATOH 90 CA SER 48 44.667 46.453 34.457 1.00 9.11 6 H_Λ ATOH 338 CO PRO 41 31.469 38.773 28.451 1.00 8.06 6 ATOH 91 CB SER 48 45.870 46.312 33.492 1.00 9.17 6 339 CA PRO 41 32.887 37.771 30.151 1.00 8.14 6 ATOH 92 OG SER 48 45.546 45.387 32.490 1.00 8.88 8 H AIOH 340 CB PRO 41 33.802 38.683 29.246 1.00 8.13 6 ATOH 93 C SER 48 43.380 46.678 33.672 1.00 9.13 6 C AtOH AliH 341 CG PRO 41 32.756 39.565 28.595 1.00 8.01 6 ATOH 94 0 SER 48 42.533 45.777 33.610 1.00 9.05 8 Hm AIOH 342 PRO 41 32.846 38.312 31.590 1.00 7.87 6 ATOH 95 N GLN 49 43.225 47.807 33.003 1.00 9.23 7 AIOH 343 PRO 41 31.891 38.952 32.039 1.00 7.72 8 ATOH 96 CA GLN 49 42.076 48.113 32.174 1.00 9.17 6 IΛ X AIOH 344 PRO 42 33.909 38.044 32.341 1.00 7.64 7 ATOH 97 CB GLN 49 42.104 49.549 31.592 1.00 6.81 6 AIOH 345 CD PRO 42 35.113 37.297 31.B80 1.00 7.36 6 ATOH 98 CG GLN 49 40.813 49.921 30.864 1.00 5.86 6 AIOH 346 CA PRO 42 34.084 38.542 33.711 1.00 7.41 6 ATOH 99 CD GLN 49 41.078 51.178 30.041 1.00 7.48 6 AIOH 347 CB PRO 42 35.490 38.085 34.191 1.00 7.45 6 ATOH 00 OE1 GLN 49 41.898 51.153 29.103 1.00 7.62 8 AIOH 348 CG PRO 42 35.772 36.947 33.217 1.00 7.45 6 ATOH 01 NE2 GLN 49 40.489 52.278 30.467 1.00 5.00 7 30 AIOH 349 PRO 42 33.841 40.054 33.685 1.00 7.06 6 ATOH 02 GLN 49 41.929 47.121 31.006 1.00 9.30 6 C AIOH 350 PRO 42 34.481 40.819 32.931 1.00 6.95 8 ATOH 03 GLH 49 r- 40.774 46.745 30.647 1.00 9.52 8 m AIOH 351 ALA 43 32.875 40.536 34.452 1.00 6.53 7 ATOH 04 SER 50 43.038 46.690 30.424 1.00 9.20 7 AIOH 352 CA ALA 43 32.477 41.937 34.481 1.00 6.39 6 ATOH 05 CA SER 50 42.992 45.763 29.281 1.00 9.33 6 AIOH 353 CB ALA 43 30.968 41.991 34.756 1.00 5.00 6 ATOH 06 CB SER 50 44.173 46.116 28.346 1.00 11.13 6 AIOH 354 ALA 43 33.131 42.845 35.529 1.00 6.36 6 ATOH 07 OG SER 50 45.417 45.891 29.000 1.00 14.96 8 AIOH 355 ALA 43 32.847 44.042 35.582 1.00 6.42 8 ATOH 08 C SER 50 42.924 44.272 29.626 1.00 88 6 AIOH 356 TYR 44 33.995 42.333 36.394 1.00 6.22 7 ATOH 09 0 SER 50 42.810 43.409 28.736 1.00 96 8 AIOH 357 CA TYR 44 34.637 43.052 37.465 1.00 6.10 6 ATOH 10 N ASP 51 42.910 43.891 30.881 1.00 8.41 7 AIOH 358 CB TYR 44 34.455 42.266 38.819 1.00 6.31 6 ATOH 11 CA ASP 51 42.812 42.467 31.211 1.00 7.98 6 AI H 359 CG TYR 44 34.381 40.781 38.551 1.00 6.51 6 ATOH 12 CB ASP 51 43.030 42.303 32.724 1.00 7.44 6 AIOH 360 CD1 TYR 44 35.538 40.086 38.145 1.00 6.67 6 ATOH 13 CG ASP 51 43.044 40.822 33.120 1.00 8.58 6 AIOH 361 CE1 TYR 44 35.472 38.732 37.848 1.00 6.66 6 ATOH 14 ODl ASP 51 44.069 40.115 32.869 1.00 8.63 8 AIOH 362 CD2 TYR 44 33.200 40.071 38.613 1.00 6.52 6 ATOH 15 002 ASP 51 41.992 40.399 33.679 1.00 8.06 8 ATOM 363 CE2 TYR 44 33.108 38.722 38.301 1.00 6.55 6 ATOH ASP 51 41.460 41.932 30.766 1.00 7.80 6 AIOH 364 CZ TYR 44 34.276 38.073 37.917 1.00 6.98 6 ATOH ASP 51 40.441 42.613 30.990 1.00 7.70 8 AIOH 365 OH TYR 44 34.209 36.729 37.568 1.00 7.43 8 ATOH ASN 52 41.330 40.729 30.217 1.00 7.56 7 AIOH 366 C TYR 44 36.060 43.413 37.075 1.00 99 6 ATOH 19 CA ASN 52 40.040 40.182 29.867 1.00 7.47 6 AIOH 367 0 TYR 44 36.682 42.945 36.097 1.00 98 8 ATOH 20 CB ASN 52 40.175 38.887 29.057 1.00 9.45 6 AIOH 368 H LYS 45 36.556 44.410 37.815 1.00 93 7 ATOH 21 CG ASN 52 40.562 39.187 27.620 1.00 .003 12.85 6 AIOH 369 CA LYS 45 37.865 45 37.587 1.00 73 6 ATOH 22 001 ASN 52 40.516 40.341 27.167 1.00 15.76 .033 46.160 38.580 8 AII'M 370 CB LYS 45 38 1.00 00 6 ATOH 23 ND2 ASN 52 40.979 38.239 26.786 IOH 371 CG LYS 45 39.192 47.127 38.251 1.00 12.70 A 1.00 00 6 7 ATOH 24 C AS 0 Λ 0 - o . AIOH 531 C PHE 65 36.480 53.123 40.126 1.00 10.75 6 ATOM 584 CZ ARG A 72 38.053 51.266 28.054 1.00 5.00 6 AIOH 532 0 PHE 65 36.935 52.381 39.255 1.00 10.67 8 ATOH 585 NH1 ARG A 72 38.926 51.664 27.158 1.00 5.00 7 AIOH 533 N GLN 66 37.091 54.215 40.584 1.00 11.02 7 ATOH 586 NH2 ARG A 72 38.043 50.022 28.506 1.00 5.00 7 AK>H 534 CA GLN 66 38.370 54.590 39.964 1.00 11.57 6 ATOH 587 C ARG 72 36.316 49.984 33.347 1.00 8.29 6 > A IOH 535 CB GLN 66 38.512 56.102 40.168 1.00 15.18 6 ATOH 588 0 ARG 72 37.531 50.080 33.499 1.00 8.41 8 AIOH 536 CG GIN 66 39.855 56.661 39.832 1.00 20.59 6 ATOH 589 N THR 73 35.700 48.836 33.120 1.00 8.00 7 D GLH 66 40.150 56.793 38.363 1.00 24.82 6 ATOH 590 CA THR 73 36.539 47.632 32.967 1.00 8.12 6 - AIOH 537 C A IOH 538 OE1 GLN 66 39.958 57.812 37.688 1.00 28.38 8 ATOH 591 CB THR 73 35.820 46.301 33.270 1.00 6.10 6 AIOH 539 NE2 GLH 66 40.716 55.789 37.719 1.00 26.84 7 ATOH 592 OG1 THR 73 34.727 46.140 32.317 1.00 5.35 B I OH 540 C GLH 66 39.489 53.768 40.576 1.00 11.54 6 ATOH 593 CG2 THR 73 35.361 46.223 34.730 1.00 5.00 6 AIOH 541 0 GLH 66 39.989 54.089 41.699 1.00 11.29 8 ATOH 594 C THR 73 36.932 47.628 31.481 1.00 8.12 6 A IOH 542 H GLH 67 39.870 52.683 39.B95 1.00 11.31 7 ATOH 595 0 THR 73 36.630 48.581 30.739 1.00 8.16 8 IOH 543 CA GLH 67 40.915 51.786 40.411 1.00 11.24 6 ATOH 596 H LYS 74 37.514 46.575 30.939 1.00 8.08 7 I C H 544 CB GLH 67 40.390 50.591 41.201 1.00 9.56 6 ATOH 597 CA LYS 74 37.782 46.496 29.508 1.00 8.07 6 A;OH 545 CG GLN 67 39.353 50.740 42.242 1.00 7.94 6 ATOH 598 CB LYS 74 38.443 45.122 29.215 1.00 7.37 6 AIOH 546 CO GLH 67 38.970 49.695 43.240 1.00 6.97 6 ATOH 599 CG LYS 74 38.780 44.864 27.777 1.00 7.51 6 c ilOH 547 OE1 GLN 67 39.359 49.865 44.405 1.00 7.23 8 ATOH 600 CD LYS 74 39.173 43.465 27.359 1.00 6.71 6 AIOH 548 NE2 GLH 67 38.222 48.659 42.932 1.00 5.00 7 ATOH 601 CE LYS 74 39.463 43.461 25.867 1.00 7.86 6 00 AIOH 549 C GLH 67 41.738 51.246 39.242 1.00 11.63 6 ATOM 602 NZ LYS 74 40.043 42.121 25.465 1.00 7.32 7 AIOH 550 0 GLH 67 41.158 50.867 38.216 1.00 11.46 8 ATOH 603 C LYS 74 36.469 46.596 28.696 1.00 7.96 6 AIOH 551 H LYS 68 43.063 51.149 39.341 1.00 12.10 7 ATOH 604 0 LYS 74 36.376 47.163 27.598 1.00 7.92 B c AIOH 552 CA LYS 68 43.938 50.664 38.285 1.00 12.61 6 ATOH 605 N TYR 75 35.375 46.004 29.221 1.00 7.80 7 AIOH 553 CB LYS 68 43.621 49.280 37.709 1.00 13.06 6 ATOH 606 CA TYR 75 34.113 45.937 28.503 1.00 H 7.58 6 m AIOH 554 CG LYS 68 43.465 48.179 38.780 1.00 14.46 6 ATOH 607 CB TYR 75 33.400 44.620 29.024 1.00 7.14 6 IΛ AIOH 555 CD LYS 68 44.715 48.024 39.626 1.00 15.01 6 ATOM 608 CG TYR 75 34.311 43.409 28.864 1.00 6.68 6 X AIOH 556 CE LYS 68 44.683 47.225 40.918 1.00 14.26 6 ATOH 609 CD1 TYR 75 34.853 42.777 29.988 1.00 6.37 6 AIOH 557 NZ LYS 68 46.062 47.066 41.499 1.00 12.89 7 ATOM 610 CE1 TYR 75 35.716 41.696 29.857 1.00 6.28 6 AIOH 558 C LYS 68 43.908 51.710 37.17β 1.00 13.39 6 ATOH 611 CD2 TYR 75 34.677 42.916 27.589 1.00 6.45 6 AIOf! 559 0 LYS 68 43.978 51.422 35.955 1.00 14.41 8 ATOH 612 CE2 TYR 75 35.547 41.855 27.414 1 00 6.14 6 AIOH 560 N GLY 69 43.764 53.001 37.484 1.00 13.13 7 ATOH 613 CZ TYR 75 36.039 41.257 28.570 30 1 00 6.25 6 561 CA GLY 69 43.739 54.115 36.582 1.00 12.76 6 C AI H ATOH 614 OH TYR 75 36.913 40.195 28.479 1.00 6.33 8 AIOH 562 C GLY 69 42.535 54.177 35.674 1.00 12.59 6 ATOH 615 C TYR 75 33.188 47.141 28.576 1.00 7.81 6 AIOH 563 0 GLY 69 42.4B1 54.975 34.735 1.00 12.74 8 ATOH 616 0 TYR 75 32.274 47.302 27.713 1.00 7.79 8 AIOH 564 N THR 70 41.497 53.394 35.983 1.00 12.05 7 ATOH 617 N GLY 76 33.355 48.068 29.555 1.00 7.71 7 σ. IOH 565 CA THR 70 40.325 53.375 35.120 1.00 11.09 6 ATOH 618 CA GLY 76 32.468 49.243 29.681 1.00 7.27 6 AIOH 566 CB THR 70 40.536 52.215 34.122 1.00 9.79 6 ATOH 619 C GLY 76 32.204 49.486 31.152 1.00 7.13 6 AI H 567 OG1 THR 70 39.502 52.210 33.117 1.00 10.12 8 ATOH 620 0 GLY 76 32.841 48.904 32.048 1.00 6.91 8 AIOH 568 CG2 THR 70 40.547 50.831 34.773 1.00 9.26 6 ATOH 621 H THR 77 31.250 50.356 31.425 1.00 7.24 7 AIOH 569 C THR 70 39.087 53.169 35.950 1.00 10.63 6 ATOH 622 CA THR 77 30.855 50.694 32.813 1.00 7.52 6 AIOH 570 0 THR 70 39.115 52.524 36.977 1.00 10.42 8 ATOH 623 CB THR 77 30.386 52.172 32.914 1.00 7.84 6 AIOH 571 H VAL 71 37.978 53.737 35.484 1.00 10.18 7 ATOH 624 OG1 THR 77 29.223 52.337 32.073 1.00 8.21 8 AIOH 572 CA VAL 71 36.690 53.549 36.107 1.00 9.77 6 ATOH 625 CG2 THR 77 31.378 53.173 32.361 1.00 6.70 6 AIOH 573 CB VAL 71 35.802 54.788 35.985 1.00 10.20 6 ATOH 626 C THR 77 29.712 49.827 33.304 1.00 7.62 6 AIOH 574 CGI VAL 71 34.374 54.448 36.303 1.00 8.33 6 ATOH 627 0 THR 77 28.984 49.118 32.575 1.00 7.39 8 AIOH 575 CG2 VAL 71 36.393 55.860 36.919 1.00 9.35 6 ATOH 628 N LYS 78 29.460 49.853 34.611 1.00 7.89 7 AIOH 576 C VAL 71 36.093 52.313 35.404 1.00 9.37 6 ATOH 629 CA LYS 78 28.398 49.084 35.247 1.00 8.24 6 AIOH 577 0 VAL 71 35.766 51.299 36.050 1.00 9.39 8 ATOH 630 CB LYS 78 28.465 49.384 36.759 1.00 8.87 6 AIOH 578 N ARG 72 36.007 52.357 34.089 1.00 β.79 7 ATOH 631 CG LYS 78 27.449 48.604 37.551 1.00 11.52 6 AIOH 579 CA ARG 72 35.449 51.252 33.344 1.00 8.64 6 ATOH 632 CD LYS 78 27.592 49.117 39.004 1.00 13.82 6 AIOH 5SO CB ARG 72 35.205 51.645 31.846 1.00 7.09 6 ATOH 633 CE LYS 78 26.681 48.228 39.824 1.00 15.45 6 AIOH 581 CG ARG 72 36.443 51.798 30.962 1.00 6.38 6 ATOH 634 NZ LYS 78 26.132 49.000 40.954 1.00 18.28 7 AIOH 582 CD ARG 72 36.054 51.979 29.499 1.00 6.64 6 ATOM 635 C LYS 78 27.022 49.428 34.735 1.00 8.73 6 A10H 637 H SER 79 26.749 50.759 34.578 1.00 9.32 7 ATOH 638 CA SER 79 25.401 51.141 34.086 1.00 9.71 6 AIOH 639 CB SER 79 25.190 52.607 34.380 1.00 12.14 6 AIOH 640 OG SER 79 25.960 53.338 33.488 1.00 15.84 8 AIOH 641 C SER 79 25.262 50.703 32.644 1.00 9.79 6 AIOH 642 O SER 79 24.142 50.254 32.312 1.00 10.15 8 AIOH 643 N GLU BO 26.291 50.655 31.814 1.00 9.56 7 AIOH 644 CA GLU 80 26.160 50.128 30.452 1.00 9.39 6 AIOH 645 CB GLU 80 27.429 50.452 29.723 1.00 10.04 6 AIOH 646 CG GLU 80 27.546 51.928 29.378 1.00 11.54 6 AIOH 647 CD GLU 80 28.902 52.167 28.769 1.00 14.36 6 AIOH 648 OE1 GLU 80 29.881 51.408 28.913 1.00 15.28 8 A'OH 649 OE2 GLU 80 29.051 53.186 2B.075 1.00 18.22 8 _ OH 650 C GLU 80 25.853 48.629 30.476 1.00 9.05 6 AIOH 651 0 GLU 80 25.005 48.179 29.720 1.00 8.72 8 AIOH 652 H LEU 81 26.441 47.873 31.394 1.00 9.09 7 ♦.[OH 653 CA LEU 81 26.145 46.428 31.534 1.00 9.12 6 654 CB LEU 81 27.18B 45.716 32.385 1.00 8.24 6 0 AIOH AIOH 655 CG LEU 81 26.866 44.272 32.B43 1.00 68 6 AIOH 656 CD1 LEU 81 26.744 43.229 31.738 1.00 74 6 AIOH 657 CD2 LEU 81 27.983 43.841 33.771 1.00 60 6 AIOH 658 C LEU 81 24.710 46.226 32.053 1.00 19 6 AIOH 659 0 LEU 81 23.952 45.386 31.515 1.00 94 8 AIOH 660 H GLH B2 24.247 47.005 33.042 1.00 33 7 AIOH 661 CA GLH 82 22.853 46.834 33.479 1.00 81 6 AIOH 662 CB GLN 82 22.588 47.739 34.681 1.00 11.55 6 AIOH 663 CG GLH 82 23.288 47.105 35.901 1.00 14.03 6 AIOH 664 CD GLH 82 23.239 47.993 37.132 1.00 14.62 6 AIOH 665 0E1 GLH 82 23.497 49.180 36.990 1.00 15.76 a AIOH 666 NE2 GLH 82 22.947 47.380 0 38.266 1.00 14.70 7 AIOH 667 C GLH 82 21.878 47.108 32.358 1.00 10.18 6 AIOH 668 0 GLN 82 20.854 46.455 32.247 1.00 10.30 8 AIOH 669 H ASP 83 22.106 48.088 31.501 1.00 10.58 7 AIOH 670 CA ASP 83 21.281 48.355 30.317 1.00 11. OS 6 . AIOH 671 CB ASP 83 21.631 49.619 29.514 1.00 15.09 6 AIOH 672 CG ASP 83 21.228 50.893 30.246 1.00 18.79 6 AIOH 673 001 ASP 83 20.404 50.950 31.175 1.00 18.59 8 AIOH 674 002 ASP 83 21.B32 51.914 29.841 1.00 22.13 8 AIOH 675 C ASP 83 21.439 47.203 29.307 1.00 10.81 6 AIOH 676 0 ASP 83 20.391 46.942 28.751 1.00 11.02 8 IOH 677 N ALA 84 22.562 46.574 29.048 1.00 10.37 7 AIOH 678 CA ALA 84 22.630 45.461 28.120 1.00 10.32 6 AIOH 679 CB ALA 84 24.057 45.019 27.847 1.00 7.64 6 AIOH 680 C ALA 84 21.758 44.332 28.688 1.00 10.46 6 AIOH 681 0 ALA 84 20.988 43.692 27.939 1.00 10.32 8 AIOH 682 H ILE 85 21.828 44.045 29.995 1.00 10.47 7 AIOH 683 CA ILE 85 21.036 42.985 30.642 1.00 10.46 6 AIOH 684 CB ILE 85 21.501 42.710 32.116 1.00 9.71 6 AIOH 685 CG2 ILE 85 20.474 41.875 32.906 1.00 6.40 6 AIOH 686 CGI HE 85 22.921 42.132 32.080 1.00 9.01 6 AIOH 687 CD1 ILE B5 23.684 42.092 33.399 1.00 10.12 6 AIO. 688 C ILE 85 19.543 43.282 30.566 1.00 10.65 AIOH 689 0 ILE 85 18.768 42.340 30.313 1.00 10.41 AIOH 743 H VAL A 93 15.886 36.642 26.989 1.00 16.55 7 ATOH 796 0 VAL A 99 34.461 31.987 37.850 1.00 6.46 8 17.213 36.038 26.B33 1.00 15.28 6 ATOH 797 N VAL A 100 35.082 34.017 38.489 1.00 6.60 7 18.120 36.688 25.785 1.00 12.97 6 ATOH 798 CA VAL A 100 36.487 33.766 38.594 1.00 6.45 6 19.467 36.021 25.589 1.00 11.55 6 ATOH 799 CB VAL A 100 37.273 34.786 37.735 1.00 6.89 6 17.378 36.751 24.453 1.00 12.58 6 ATOH 800 CGI VAL A 100 38.728 34.308 37.697 1.00 6.74 6 17.771 36.161 28.256 1.00 14.60 6 ATOH 801 CG2 VAL A 100 36.761 34.893 36.314 1.00 6.94 6 17.736 37.228 28.829 1.00 14.36 8 ATOH 802 C VAL A 100 36.930 33.803 40.041 1.00 6.61 6 18.211 35.007 28.742 1.00 13.97 7 ATOH 803 0 VAL A 100 37.306 34.B66 40.566 1.00 6.72 8 18.792 34.812 30.045 1.00 13.10 6 ATOH 804 N LEU A 101 36.882 32.651 40.724 1.00 6.41 7 18.642 33.37S 30.542 1.00 13.62 6 ATOH 805 CA LEU A 101 37.189 32.537 42.133 1.00 6.10 6 17.165 33.203 30.919 1.00 16.17 6 ATOH 806 CB LEU A 101 36.017 31.716 42.731 1.00 7.20 6 17.047 31.82B 31.552 1.00 19.51 6 ATOH 807 CG LEU A 101 34.663 32.479 42.645 1.00 8.90 6 17.710 30.855 31.198 1.0021.76 B ATOH 808 CD1 LEU A 101 33.657 31.509 43.300 1.00 9.60 6 16.206 31.683 32.5S9 1.0021.21 7 ATOM 809 CD2 LEU A 101 34.726 33.873 43.244 1.00 7.63 6 20.275 35.223 30.003 1.00 12.28 6 ATOM 810 C LEU A 101 3B.456 31.843 42.579 1.00 5.96 6 20.882 35.311 28.935 1.00 12.02 8 ATOM 811 0 LEU 101 38.672 31.740 43.782 1.00 6.02 B 20.772 35.576 31.218 1.00 11.32 7 ATOM 812 N ASN 102 39.260 31.326 41.676 1.00 5.73 7 22.144 36.030 31.272 1.00 10.46 6 ATOM 813 CA ASN 102 40.471 30.629 42.025 1.00 5.58 6 22.215 37.553 31.568 1.00 11.92 6 ATOM 814 CB ASN A 102 40.963 29.889 40.727 1.00 5.00 6 23.646 38.014 31.735 1.00 12.03 6 ATOH B15 CG ASN A 102 42.327 29.247 40.912 1.00 5.00 6 21.591 38.367 30.411 1.00 12.21 6 ATOH 816 ODl ASN A 102 42.309 28.218 41.608 1.00 5.00 B 22.942 35.249 32.302 1.00 9.65 6 ATOH 817 ND2 ASN A 102 43.493 29.633 40.442 1.00 5.00 7 22.559 35.259 33.483 1.00 9.73 8 ATOH 818 C ASN A 102 41.580 31.490 42.620 1.00 5.69 6 24.034 34.613 31.857 1.00 8.90 7 ATOH 819 0 ASN A 102 42.261 31.045 43.593 1.00 6.11 8 24.920 33.882 32.786 1.00 B.34 6 AIOH 820 N HIS A 103 41.853 32.670 42.103 1.00 5.60 7 25.217 32.512 32.267 1.00 8.31 6 ATOH 821 CA HIS A 103 42.935 33.520 42.506 1.00 5.59 6 24.055 31.583 31.987 1.00 8.37 6 ATOH 822 CB HIS A 103 44.0B9 33.287 41.487 1.00 6.54 6 24.298 30.500 31.130 1.00 8.46 6 ATOH 823 CG HIS A 103 43.645 33.442 40.043 1.00 7.70 6 23.255 29.643 30.831 1.00 8.30 6 ATOM 824 CD2 HIS 103 43.560 34.512 39.230 1.00 6.52 6 22.797 31.752 32.491 1.00 8.19 6 ATOH 825 ND1 HIS 103 43.187 32.341 39.282 1.00 9.01 7 21.742 30.928 32.186 1.00 B.OS 6 ATOH 826 CE1 HIS 103 42.794 32.769 38.082 1.00 8.40 6 22.011 29.B54 31.363 1.00 7.94 6 ATOH 827 NE2 HIS 103 42.993 34.113 38.070 1.00 8.31 7 21.055 28.940 31.084 1.00 7.64 B ATOM 82B C HIS A 103 42.555 34.977 42.419 1.00 5.57 6 26.218 34.655 33.000 1.00 8.00 6 ATOM 829 0 HIS 103 41.470 35.229 41.899 1.00 5.20 8 26.855 35.017 32.005 1.00 7.99 8 ATOM 830 N LYS 104 43.438 35.861 42.914 1.00 5.83 7 26.624 34.919 34.243 1.00 7.85 7 AIOH B31 CA LYS 104 43.226 37.313 42.871 1.00 6.01 6 27.818 35.671 34.578 1.00 7.64 6 ATOH 832 CB LYS A 104 42.938 37.971 44.213 1.00 8.00 6 29.038 34.754 34.756 1.00 7.84 6 ATOH 833 CG LYS A 104 41.748 37.393 44.978 1.00 8.52 6 28.950 33.655 35.307 1.00 7.51 8 ATOM 834 CD LYS A 104 41 .373 38.324 46.133 1.00 9.80 6 30.194 35.231 34.285 1.00 7.87 7 ATOH 835 CE LYS A 104 40.973 39.748 45.746 1.00 8.97 6 31.455 34.489 34.4B2 1.00 8.04 6 ATOH 836 NZ LYS A 104 39.514 39.723 45.383 1.00 8.50 7 32.546 34.944 33.523 1.00 7.77 6 ATOH 837 C LYS A 104 44.489 37.894 42.278 1.00 6.11 6 33.452 33.B2B 33.077 1.00 7.80 6 ATOH 838 0 LYS A 104 45.526 37.321 42.649 1.00 6.50 8 33.916 33.045 33.920 1.00 8.28 8 ATOH 839 N ALA A 105 44.501 38.896 41.451 1.00 5.96 33.791 33.741 31.896 1.00 8.14 8 7 ATOH 840 CA ALA A 105 45.699 39.429 40.846 i .oo 6.18 6 31.868 34.668 35.953 1.00 7.80 6 ATOH 841 CB ALA A 105 45.660 39.063 39.341 1.00 5.88 6 31.644 35.739 36.518 1.00 7.83 8 ATOH 842 C ALA A 105 45.785 40.943 41.031 1.00 6.37 6 32.333 33.601 36.602 1.00 7.67 7 ATOH 843 0 ALA A 105 44.741 41.578 41.199 1.00 8.035 1.00 7.25 6 6.24 8 32.708 33.576 3 ATOH B44 N GLY A 106 46.958 41.S84 41.044 1.00 6.40 7 31.742 32.652 38.791 1.00 8.70 6 ATOH 845 CA GLY A 106 47.040 43.001 41.190 1.00 6.60 6 32.193 32.306 40.195 1.00 9.79 6 ATOH 846 C GLY A 106 47.006 43.611 42.573 1.00 7.01 6 30.366 33 62 3B.B85 00 ATOH 902 C THR 114 56.563 31.547 54.495 1.00 11.69 6 AIOH 903 0 IHR 114 55.355 31.265 54.457 1.00 11.32 8 ATOH 904 N ALA 115 57.429 31.042 53.643 1.00 11.64 7 ATOH 905 CA ALA 115 57.024 30.048 52.638 1.00 11.55 6 ATOH 906 CB ALA 115 56.825 30.894 51.357 1.00 10.80 6 ATOH 907 C ALA 115 58.039 28.947 52.343 1.00 11.45 6 ATOH 908 0 ALA 115 59.215 29.073 52.688 1.00 11.41 8 ATOH 909 N VAL 116 57.641 27.868 51.657 1.00 11.33 7 ATOH 910 CA VAL 116 58.513 26.814 51.184 1.00 11.10 6 ATOH 911 CB VAL 116 58.33B 25.436 51.815 1.00 12.01 6 ATOH 912 CGI VAL 116 58.978 25.449 53.208 1.00 12.23 6 ATOH 913 CG2 VAL 116 56.882 24.978 51.873 1.00 11.15 6 ATOH 914 C VAL 116 58.250 26.642 49.656 1.00 10.95 6 ATOH 915 0 VAL 116 57.100 26.960 49.240 1.00 11.03 8 ATOH 916 N GLU 117 59.187 26.205 48.856 1.00 10.29 7 ATOH 917 CA GLU 117 58.932 25.898 47.465 1.00 10.06 6 ATOH 918 CB GLU 117 60.201 25.861 46.625 1.00 11.90 6 ATOH 919 CG GLU 117 60.905 27.201 46.773 1.00 14.30 6 0 AIOH 920 CD GLU 117 62.245 27.143 46.070 1.00 16.13 6 AIOH 921 OE1 GLU 117 62.515 26.342 45.175 1.00 16.80 8 ATOH 922 OE2 GLU 117 63.067 28.004 46.366 1.00 17.32 8 ATOH 923 C GLU 117 58.354 24.480 47.369 1.00 9.67 6 ATOH 924 0 GLU 117 58.596 23.656 48.258 1.00 9.47 8 ATOH 925 H VAL 118 57.623 24.157 46.316 1.00 9.40 7 ATOH 926 CA VAL 118 56.987 22.802 46.152 1.00 9.25 6 ATOH 927 CB VAL 118 55.556 23.243 46.543 1.00 10.55 6 ATOH 928 CGI VAL 118 54.529 23.164 45.421 1.00 9.52 6 ATOH 929 CG2 VAL 118 55.061 22.664 47.855 1.00 10.49 6 AIOH 930 C VAL 118 57.360 22.305 44.765 1.00 9.31 6 ATOH 931 0 VAL 118 57.660 23.097 43.823 1.00 9.23 8 0 ATOH 932 N ASN 119 57.381 20.998 44.492 1.00 8.84 7 AIOH 933 CA ASN 119 57.701 20.403 43.206 1.00 8.20 6 ATOH 934 CB ASN 119 57.911 18.914 43.534 1.00 7.82 6 ATOH 935 CG ASN 119 58.248 18.097 42.289 1.00 8.10 6 _ ATOH 936 001 ASN 119 58.084 18.636 41.177 1.00 7.16 8 ATOH 937 ND2 ASN 119 58.706 16.848 42.386 1.00 6.98 7 ATOH 938 C ASH 119 56.553 20.692 42.242 1.00 7.98 6 ATOH 939 0 ASN 119 55.382 20.414 42.482 1.00 7.64 8 ATOH 940 N PRO 120 56.833 21.326 41.094 1.00 B.04 7 ATOH 941 CD PRO 120 58.207 21.735 40.728 1.00 β.00 6 ATOH 942 CA PRO 120 55.849 21.704 40.08B 1.00 a.27 6 ATOH 943 CB PRO 120 56.609 22.404 38.938 1.00 8.21 6 ATOH 944 CG PRO 120 57.980 22.618 39.530 1.00 8.16 6 ATOH 945 C PRO 120 55.032 20.526 39.601 1.00 8.65 6 ATOH 946 0 PRO 120 53.858 20.633 39.275 1.00 8.69 8 ATOH 947 N ALA 121 55.648 19.337 39.540 1.00 9.00 7 ATOH 948 CA ALA 121 54.977 18.104 39.122 1.00 9.39 6 ATOH 949 CB ALA 121 55.976 17.215 38.324 1.00 9.49 6 ATOH 950 C ALA 121 54.374 17.315 40.267 1.00 9.46 6 ATOH 951 0 ALA 121 53.644 16.327 40.066 1.00 9.60 8 ATOH 952 N ASN 122 54.624 17.656 41.537 1.00 9.45 7 ATOH 953 CA ASN 122 54.040 16.971 42.679 1.00 9.32 6 ATOH 954 CB ASN 122 54.881 15.802 43.207 1.00 10.30 6 ATOH 955 CG ASN 122 54.009 15.047 44.180 1.00 13.39 6 AIOH 956 001 ASN 122 53.085 15.591 44.786 13.50 8 AIOH 957 WD2 ASN 122 54.211 13.733 44.357 16.10 7 AIOH 958 ASH 122 53.936 18.050 43.742 1.00 9.22 6 AIOH 959 ASN 122 54.881 18.130 44.566 1.00 02 8 AIOH 960 ARG 123 52.869 18.855 43.722 1.00 27 7 AIOH 961 CA ARG 123 52.764 19.983 44.684 1.00 23 6 - AIOH 962 CB ARG 123 51.675 20.969 44.227 1.00 86 6 AIOH 963 CG ARG 123 52.067 21.746 42.991 1.00 .67 6 AIOH 964 CD ARG 123 51.511 21.080 41.764 1.00 .95 6 AIOH 965 NE ARG 123 51.759 21.959 40.604 1.00 .73 7 IOH 966 CZ ARG 123 50.906 22.937 40.275 1.00 10.25 6 AIOH 967 HH1 ARG 123 49.828 23.054 41.044 1.00 9.79 7 AIOH 968 NII2 ARG 123 51.000 23.793 39.273 1.00 10.20 7 A'OH 969 C ARG 123 52.593 19.557 46.158 1.00 9.23 6 AIOH 970 ARG 123 52.622 20.374 47.085 1.00 8.71 8 c IΛ 4.1OH 971 ASH 124 52.408 IB.256 46.379 1.00 9.56 7 AIOH 972 CA ASN 124 52.351 17.706 47.712 1.00 10.31 6 00 AIOH 973 CB ASN 124 51.742 16.299 47.800 1.00 11.34 6 HΛ AIOH 974 CG ASN 124 50.275 16.347 47.455 1.00 14.21 6 H AIOH 975 001 ASN 124 49.565 17.271 47.867 1.00 14.26 8 C AIOH 976 HD2 ASH 124 49.887 15.391 46.590 1.00 16.51 7 H ATOM 977 C ASH 124 53.796 17.564 4B.243 1.00 10.74 6 m AIOH 978 0 ASN 124 53.926 17.342 49.439 1.00 10.85 8 IΛ AIOH 979 H GLH 125 54.872 17.660 47.433 1.00 10.96 7 AIOH 980 CA GLN 125 56.223 17.549 47.925 1.00 11.21 6 AIOH 981 CB GLH 125 57.169 16.823 46.919 1.00 9.50 6 AI H 982 CG GLN 125 58.582 16.600 47.49B 1.00 β.17 6 AIOH 983 CD GLN 125 59.546 16.199 46.402 1.00 8.01 6 AIOH 984 0E1 GLH 125 59.184 16.310 45.207 1.00 6.56 8 30 C AIOH 985 NE2 GLN 125 60.762 15.784 46.73B 1.00 6.20 7 AIOH 986 C GLN 125 56.871 18.915 48.156 1.00 11.48 6 i— m AIOH 987 0 GLN 125 56.960 19.609 47.146 1.00 11.44 8 s» AIOH 988 H GLU 126 57.345 19.217 49.360 11.79 7 σ_ AIOH 989 CA GLU 126 58.053 20.468 49.610 12.46 6 AIOH 990 CB GLU 126 58.042 20.856 51.115 11.31 6 AIOH 991 CG GLU 126 56.589 20.799 51.582 1.00 12.45 6 AIOH 992 CD GLU 126 56.371 21.288 52.993 1.00 13.36 6 AIOH 993 0E1 GLU 126 57.329 21.471 53.748 1.00 13.22 8 AI H 994 0E2 GLU 126 55.214 21.519 53.374 1.00 14.72 8 AIOH 995 GLU 126 59.513 20.293 49.195 1.00 13.18 6 AIOH 996 GLU 126 60.198 19.292 49.513 1.00 12.98 8 AIOH 997 THR 127 60.045 21.216 48.430 1.00 14.11 7 AIOH 998 CA THR 127 61.407 21.048 47.954 1.00 15.19 6 AIOH 999 CB THR 127 61.487 21.193 46.420 1.00 14.68 6 AIOH 1000 0G1 THR 127 60.732 22.349 46.071 1.00 15.49 8 ATOH 1001 CG2 THR 127 60.902 19.957 45.774 1.00 13.94 6 AIOH 1002 THR 127 62.377 21.993 48.614 1.00 16.26 6 AI H 1003 THR 127 63.552 21.851 48.283 1.00 16.67 8 AIOH 1004 SER 128 62.015 22.892 49.503 1.00 16.75 7 AIOH 1005 CA SER 128 63.000 23.747 50.125 1.00 17.24 6 AIOH 1006 CB SER 128 63.016 25.141 49.511 1.00 15.04 6 AIOH 1061 CD LYS A 134 ATOH 1114 CG ARG A 140 45.059 48.594 50.380 1.00 22.69 6 AIOH 1062 CE LYS A 134 ATOH 1115 CO ARG A 140 45.796 48.583 51.753 1.00 27.78 6 AIOH 1063 HZ LYS A 134 ATOH 1116 NE ARG A 140 47.197 48.785 51.626 1.00 32.35 7 AIOH 1064 C LYS A 134 ATOH 1117 CZ ARG A 140 48.476 48.985 51.487 1.00 34.38 6 AIOH 1C65 0 LYS A 134 ATOH 1118 NH1 ARG A 140 48.873 49.714 50.421 1.00 34.62 7 AIOH 1066 N ALA A 135 ATOM 1119 NH2 ARG A 140 49.440 48.518 52.329 1.00 34.86 7 AIOH 1067 CA ALA A 135 ATOH 1120 C ARG A 140 41.766 48.037 49.205 1.00 11.28 6 ATOH 1068 CB ALA A 135 ATOH 1121 0 ARG A 140 40.965 48.699 49.916 1.00 11.54 8 AIOH 1069 C ALA A 135 ATOH 1122 N PHE A 141 41.672 47.993 47.908 1.00 10.83 7 AIOH 1070 0 ALA A 135 ATOH 1123 CA PHE A 141 40.554 48.658 47.231 1.00 10.94 6 ATOH 1071 N TRP A 136 ATOH 1124 CB PHE A 141 39.237 47.897 47.618 1.00 8.15 6 AIOH 1072 CA TRP A 136 ATOH 1125 CG PHE A 141 39.346 46.381 47.561 1.00 6.78 6 AIOH 1073 CB TRP A 136 ATOH 1126 C01 PHE A 141 39.041 45.616 48.673 1.00 5.88 6 AIOH 1074 CG TRP A 136 ATOH 1127 CD2 PHE A 141 39.793 45.725 46.453 1.00 5.72 6 IOH 1075 CD2 TRP A 136 ATOH 1128 CE1 PHE A 141 39.150 44.225 48.627 1.00 6.27 6 AIOH 1076 CE2 TRP A 136 ATOH 1129 CE2 PHE A 141 39.930 44.318 46.407 1.00 5.00 6 #10H 1077 CE3 TRP A 136 ATOH 1130 CZ PHE A 141 39.607 43.584 47.478 1.00 5.00 6 ATOM 1078 CD1 TRP A 136 ATOH 1131 C PHE A 141 40.372 50.134 47.543 1.00 11.05 6 σ AIOH 1079 HE1 TRP A 136 ATOH 1132 0 PHE A 141 39.377 50.553 4B.103 1.00 10.80 B AIOH 1080 CZ2 TRP A 136 ATOH 1133 N PRO A 142 41.402 50.934 47.254 1.00 11.32 7 ATOH 1081 CZ3 TRP A 136 ATOH 1134 CD PRO A 142 42.645 50.440 46.634 1.00 11.43 6 AIOH 1082 CH2 TRP A 136 ATOH 1135 CA PRO A 142 41.462 52.384 47.515 1.00 11.27 6 AIOH 1083 C TRP A 136 ATOM 1136 CB PRO A 142 42.900 52.829 47.190 1.00 11.50 6 AIOH 1084 0 TRP A 136 ATOH 1137 CG PRO A 142 43.300 51.728 46.191 1.00 11.68 6 AIOH 1085 H THR A 137 ATOH 1138 C PRO A 142 40.424 53.179 46.766 1.00 11.03 6 AIOH 1086 CA THR A 137 ATOH 1139 0 PRO A 142 39.933 54.100 47.431 1.00 11.24 a AIOH 1087 CB THR A 137 ATOM 1140 N GLY A 143 39.984 52.964 45.545 1.00 10.61 7 AIOH 1088 OG1 IHR A 137 ATOM 1141 CA GLY A 143 38.950 53.703 44.905 1.00 10.26 6 AIOH 1089 CG2 THR A 137 ATOH 1142 C GLY A 143 37.544 53.272 45.330 1.00 10.29 6 AIOH 1090 C THR A 137 ATOH 1143 0 GLY A 143 36.578 54.011 45.134 1.00 10.11 a 0 AIOH 1091 0 THR A 137 ATOH 1144 N ARG A 144 37.337 52.102 45.941 10.41 7 - AIOH 1092 H ASP A 138 ATOH 1145 CA ARG A 144 36.034 51.630 46.365 10.66 6 AIOH 1093 CA ASP A 138 ATOH 1146 CB ARG A 144 35.B55 50.122 46.066 6. .45 6 AIOH 1094 CB ASP A 138 ATOH 1147 CG ARG A 144 i 34.545 49.572 46.609 6..10 6 n AIOH 1095 CG ASP A 138 ATOH 1148 CD ARG A 144 34.074 48.222 46.139 6..59 6 AIOH 1096 ODl ASP A 138 ATOH 1149 NE ARG A 144 35.003 47.110 46.397 7..45 7 AIOH 1097 002 ASP A 138 ATOH 1150 CZ ARG A 144 35.062 46.377 47.500 7..53 6 AIOH 1098 C ASP A 138 ATOH 1151 NH1 ARG A 144 35.983 45.402 47.626 8..54 7 AIOH 1099 0 ASP A 138 ATOH 1152 NH2 ARG A 144 34.219 46.599 48.511 6..60 7 AIOH 1100 H PHE A 139 ATOH 1153 C ARG A 144 35. 36 51.908 47.869 1.00 11.31 6 A11iH 1101 CA PHE A 139 ATOH 1154 0 ARG A 144 34.643 52.176 4B.348 1.00 11. OS 8 AIOH 1102 CB PHE A 139 ATOH 1155 H GLY A 145 36.813 51.804 48.658 1.00 11.78 7 AIOH 1103 CG PHE A 139 ATOH 1156 CA GLY A 145 36.758 51.954 50.104 1.00 12.35 6 AIOH 1104 CD1 PHE A 139 ATOH 1157 C GLY A 145 35.922 50.757 50.584 1.00 12.97 6 AIOH 1105 CD2 PHE A 139 ATOH 1158 0 GLY A 145 36.169 49.601 50.164 1.00 13.33 8 AIOH 1106 CE1 PHE A 139 ATOH 1159 H ASN A 146 34.906 51.057 51.416 1.00 12.95 7 AIOH 1107 CE2 PHE A 139 ATOH 1160 CA ASN A 146 34.070 49.991 51.970 1.00 12.83 6 AIOH 110B CZ PHE A 139 ATOH 1161 CB ASN A 146 33.889 50.195 53.493 1.00 15.58 6 AIOH 1109 C PHE A 139 ATOH 1162 CG ASN A 146 35.151 49.936 54.288 1.00 19.40 6 AIOH 1110 0 PHE A 139 ATOH 1163 001 ASN A 146 36.065 49.159 53.989 1.00 20.79 8 AIOH 1111 H ARG A 140 ATOH 1164 ND2 ASN A 146 35.264 50.678 55.410 1.00 20.44 AIOH 1112 CA ARG A 140 7 ATOH 1165 C ASN A 146 32.689 49.855 SI.336 1.00 12.13 AIOH 1113 CB ARG A 140 6 ATOH 1166 0 ASN A 146 31.905 49.168 52.002 1.00 12.08 8 ATOM 220 N TRP 153 41.841 41.875 51.926 1.00 8.13 7 ATOM 221 CA TRP 153 42.585 40.644 51.805 1.00 7.85 6 ATOH 222 CB TRP 153 42.567 40.241 50.293 1.00 6.88 6 ATOH 223 CG TRP 153 41.174 39.851 49.872 1.00 6.70 6 ATOH 224 CO2 TRP 153 40.681 38.522 49.679 1.00 6.38 6 ATOH 225 CE2 TRP 153 39.330 38.637 49.270 1.00 7.85 6 ATOH 226 CE3 TRP 153 41.225 37.236 49.779 1.00 6.59 6 - ATOH 227 CD1 TRP 153 40.139 40.695 49.600 1.00 6.77 6 ATOH 228 NE1 TRP 153 39.018 39.986 49.233 1.00 6.86 7 ATOH 229 CZ2 TRP 153 38.542 37.504 48.986 1.00 7.93 6 ATOH 230 CZ3 TRP 153 40.477 36.113 49.452 1.00 7.12 6 ATOH 231 CH2 TRP 153 39.128 36.250 49.081 1.00 8.55 6 ATOH 232 TRP 153 44.014 40.738 52.256 i .oo 7.70 6 ATOH 233 TRP 153 44.633 41.770 52.009 1.00 7.54 8 ATOH 234 HIS 154 44.568 39.706 52.892 1.00 7.67 7 ATOH 235 CA HIS 154 45.937 39.586 53.334 1.00 7.24 6 IΛ ATOH 236 CB HIS 154 46.112 39.no 54.859 1.00 7.92 6 C ATOH 237 CG HIS 154 45.804 41.145 55.233 1.00 B.8B 6 09 ATOH 238 CD2 HIS 154 44.674 41.660 55.765 1.00 9.84 6 IΛ H ATOH 239 N01 HIS 154 46.672 42.197 55.006 1.00 10.11 7 ATOH 240 CE1 HIS 154 46.113 43.304 55.428 1.00 10.55 6 ATOH 241 NE2 HIS 154 44.890 43.016 55.840 1.00 10.76 7 ATOH 242 HIS 154 46.508 38.207 52.960 1.00 6.90 6 ATOH 243 HIS 154 45.778 37.294 52.603 1.00 6.75 8 ATOH 244 TRP 155 47.839 38.056 53.102 6.82 IΛ 1.00 7 ATOH 245 CA TRP 155 48.508 36.802 52.800 1.00 6.92 6 ATOM 246 CB TRP 155 49.994 36.800 53.254 1.00 6.54 6 ATOH 247 CG TRP 155 50.190 36.808 54.726 1.00 6.55 6 ATOH 248 CD2 TRP 155 50.282 35.636 55.575 1.00 7.16 6 ATOH 249 CE2 TRP 155 50.473 36.099 56.900 1.00 8.10 6 ATOM 250 CE3 TRP 155 50.261 34.254 55.319 1.00 7.58 6 ATOH 251 CD1 TRP 155 50.311 37.912 55.567 1 .00 7.09 6 rn ATOH 252 NE1 TRP 155 50.496 37.495 56.870 1.00 7.83 7 isj ATOH 253 CZ2 TRP 155 50.582 35.208 57.972 1 .00 9.47 6 on ATOH 254 CZ3 TRP 155 50.372 33.377 56.355 1.00 8.70 6 ATOH 255 CH2 IRP 155 50.556 33.847 57.685 1.00 9.74 6 ATOH 256 TRP 155 47.807 35.600 53.420 1.00 6.90 6 ATOH 257 TRP 155 47.749 34.576 52.755 1.00 6.82 8 ATOH 258 TYR 156 47.293 35.659 54.655 1.00 6.91 7 ATOM 259 CA TYR 156 46.692 34.492 55.283 1.00 6.91 6 ATOH 260 CB TYR 156 46.619 34.685 56.813 1.00 7.50 6 ATOH 261 CG TYR 156 46.056 36.003 57.270 1.00 8. 16 6 ATOH 262 CD1 TYR 156 44.665 36.114 57.420 1.00 8.64 6 ATOH 263 CE1 TYR 156 44.049 37.302 57.839 1.00 B.68 6 ATOH 264 CD2 TYR 156 46.829 37.094 57.597 1.00 8.54 6 ATOH 265 CE2 TYR 156 46.254 38.298 58.052 1.00 8.83 6 ATOH 266 CZ TYR 156 44.870 38.365 58.159 1.00 8.97 6 ATOH 267 OH TYR 156 44.271 39.510 58.597 1.00 9.48 8 ATOH 268 C TYR 156 45.351 34.041 54.691 1.00 6.48 6 ATOH 269 TYR 156 44.907 32.991 55.146 1.00 6.37 8 ATOH 270 HIS 157 44.751 34.691 53.719 1.00 5.96 7 ATOM 271 CA HIS 157 43.567 34.321 53.016 1.00 5.71 6 AirH 12/3 CG HIS A 157 42.236 36.398 53.732 1.00 5.00 6 ATOH 1326 CZ3 TRP 163 59.639 37.017 39.046 1.0014.61 6 AIOH 1274 C02 HIS A 157 41.620 36.018 54.866 1.00 5.00 6 AIOH 1327 CH2 TRP 163 60.210 38.279 39.139 1.0016.01 6 AIOH 1275 ND1 HIS A 157 42.426 37.765 53.793 1.00 5.10 7 ATOH 1328 C TRP 163 57.008 35.969 44.102 1.0012.82 6 AIOH 1276 CE1 HIS A 157 41.880 3B.216 54.935 1.00 6.49 6 ATOH 1329 0 TRP 163 56.225 36.180 45.012 1.0012.72 B AIOH 1277 HE2 HIS A 157 41.398 37.147 55.588 1.00 5.12 7 ATOH 1330 N ASP 164 58.298 36.130 44.243 1.0013.51 7 AIOH 1?78 C HIS A 157 43.896 33.473 51.753 1.00 5.75 6 ATOH 1331 CA ASP 164 58.961 36.679 45.420 14.00 6 ATOH 1279 0 HIS A 157 43.028 33.056 50.978 1.00 5.63 8 ATOH 1332 CB ASP 164 60.073 35.796 45.937 13.67 6 ATOH 1280 N PHE A 158 45.182 33.311 51.471 1.00 5.60 7 ATOH 1333 CG ASP 164 60.891 36.513 47.003 1.00 14.44 6 AIOH 1281 CA PHE A 158 45.722 32.597 50.312 1.00 5.84 6 ATOH 1334 001 ASP 164 60.392 37.464 47.682 1.00 14.14 8 AIOH 1282 CB PHE A 158 46.578 33.527 49.412 1.00 5.00 6 ATOM 1335 002 ASP A 164 62.070 36.096 47.155 1.00 15.41 8 AIOH 1283 CG PHE A 158 45.867 34.784 48.992 1.00 5.00 6 ATOH 1336 C ASP A 164 59.560 38.004 44.913 1.00 14.37 6 AIOH 1284 CD1 PHE A 158 46.099 35.994 49.658 1.00 5.00 6 ATOH 1337 ASP A 164 60.491 37.969 44.125 1.00 14.14 8 AIX 1285 CD2 PHE A 158 44.972 34.788 47.942 1.00 5.00 6 ATOH 1338 GLU A 165 59.024 39.109 45.390 1.00 14.96 7 UH 1286 CE1 PHE A 158 45.418 37.147 49.286 1.00 6.00 6 ATOH 1339 GLU A 165 59.449 40.429 44.953 1.00 15.64 6 AIOH 1287 CE2 PHE A 158 44.300 35.931 47.568 1.00 5.36 6 ATOH 1340 GLU A 165 58.453 41.456 45.446 1 .00 15.08 6 _ AIOH 1288 CZ PHE A 158 44.494 37.129 48.230 1.00 5.65 6 ATOH 1341 GLU A 165 58.724 42.887 45.070 1.00 16.95 6 ».OH 1289 C PHE A 158 46.580 31.365 50.692 1.00 5.86 6 ATOH 1342 GLU A 165 58.627 43.079 43.584 1.00 18.88 6 D AIOH 1290 0 PHE A 158 47.192 31.311 51.800 1.00 5.98 8 ATOH 1343 OE1 GLU A 165 59.126 44.095 43.075 1.00 22.59 8 ) AIOH 1291 H ASP A 159 46.638 30.354 49.804 1.00 5.59 7 ATOH 1344 OE2 GLU A 165 58.071 42.288 42.822 1.00 19.30 8 AIOH 1292 CA ASP A 159 47.461 29.211 50.022 1.00 5.30 6 ATOH 1345 C GLU A 165 60.843 40.736 45.498 1.00 16.33 6 _j AIOH 1293 CB ASP A 159 46.924 27.979 49.262 1.00 5.00 6 ATOH 1346 0 GLU A 165 61.504 41.590 44.951 1.00 16.30 8 ATOH 1294 CG ASP A 159 45.876 27.378 50.090 1.00 5.58 6 ATOH 1347 N SER A 166 61.227 40.104 46.593 1.00 16.71 7 AIOH 1295 001 ASP A 159 45.988 27.501 51.360 1.00 8.12 8 ATOH 1348 CA SER 166 62.499 40.241 47.255 1.00 17.23 6 ATOH 1296 002 ASP A 159 44.B52 26.B13 49.700 1.00 5.00 8 ATOH 1349 CB SER 166 62.471 39.215 48.415 1.00 17.88 6 ) AIOH 1297 C ASP A 159 48.876 29.377 49.47B 1.00 5.70 6 ATOH 1350 OG SER 166 63.157 39.838 49.443 1.00 21.31 8 AIOH 1298 0 ASP A 159 49.808 28.719 49.999 1.00 6.04 B ATOH 1351 C SER 166 63.694 39.857 46.363 1.00 17.59 6 AIOH 1299 H GLY A 160 49.083 30.164 48.444 1.00 5.67 7 ATOH 1352 0 SER 166 64.511 40.670 45.931 1.00 17.48 8 ~ AIOH 1300 CA GLY A 160 50.438 30.251 47.914 1.00 6.24 6 ATOH 1353 N ARG A 167 63.756 38.534 46.062 1.00 17.53 7 " ■■ AIOH 1301 C GLY A 160 50.472 31.296 46.79B 1.00 6.B2 6 ATOH 1354 CA ARG A 167 64.754 37.962 45.202 1.00 17.50 6 g AIOH 1302 0 GLY A 160 49.389 31.807 46.477 1.00 6.74 8 ATOH 1355 CB ARG A 167 64.972 36.483 45.538 1.00 18.49 6 AIOH 1303 H ALA A 161 51.622 31.520 46.224 1.00 7.20 7 ATOM 1356 CG ARG A 167 65.372 36.319 46.984 1.00 19.67 6 AIOH 1304 CA ALA A 161 51.756 32.488 45.174 1.00 8.08 6 ATOM 1357 CD ARG A 167 65.413 34.810 47.294 1.00 22.11 6 AIOH 1305 CB ALA A 161 52.023 33.869 45.775 1.00 B.B8 6 ATOH 1358 NE ARG A 167 65.554 34.699 48.736 1.00 24.69 7 AIOH 1306 C ALA A 161 52.933 32.083 44.297 1.00 9.05 6 ATOH 1359 CZ ARG A 167 64.638 35.047 49.658 1.00 27.34 6 . AIOH 1307 0 ALA A 161 53.582 31.055 44.591 1.00 8.86 8 ATOH 1360 NH1 ARG A 167 63.420 35.550 49.443 1.00 24.66 7 " AIOH 1308 N ASP A 162 53.158 32.846 43.215 1.0010.00 7 ATOH 1361 NH2 ARG A 167 65.027 34.B53 50.954 1.00 28.95 7 AIOH 1309 CA ASP A 162 54.278 32.418 42.372 1.0011.36 6 ATOH 1362 C ARG A 167 64.344 38.047 43.729 1.00 17.36 6 AIOH 1310 CB ASP A 162 53.786 32.031 40.983 1.00 15.10 6 ATOH 1363 ARG A 167 65.179 37.757 42.880 1.00 17.29 8 AIOH 1311 CG ASP A 162 53.111 33.242 40.352 1.0019.35 6 ATOH 1364 LYS A 168 63.124 38.406 43.386 1.00 17.25 7 AIOH 1312 001 ASP A 162 52.930 34.331 40.947 1.0019.47 B ATOH 1365 LYS A 168 62.636 38.491 42.048 1.00 17.27 6 IOH 1313 002 ASP A 162 52.725 32.956 39.169 1.0022.93 B ATOH 1366 LYS A 168 63.318 39.579 41.203 1.00 20.36 6 AIOH 1314 C ASP A 162 55.381 33.455 42.149 1.0011.95 6 ATOH 1367 LYS A 168 62.818 40.920 41.752 1.00 23.95 6 AIOH 1315 0 ASP A 162 56.107 33.336 41.131 1.0012.10 8 ATOH 1368 LYS A 168 63.605 42.120 41.269 1.00 26.67 6 AIOH 1316 N TRP A 163 55.489 34.435 43.048 1.0012.03 7 ATOH 1369 LYS A 168 62.855 43.415 41.686 1.00 28.90 6 ATOH 1317 CA TRP A 163 56.533 35.418 42.793 1.0012.34 6 ATOH 1370 LYS A 168 62.830 43.494 43.201 1.00 30.66 7 AIOH 1318 CB TRP A 163 55.954 36.485 41.881 1.0012.40 6 ATOH 1371 LYS A 168 62.766 37.148 41.332 1.00 17.23 6 AIOH 1319 CG TRP A 163 56.925 37.600 41.631 1.0013.20 6 ATOH 1372 LYS A 168 63.337 37.062 40.229 1.00 17.13 8 AIOH 1320 CD2 TRP A 163 58.014 37.602 40.715 1.0014.IB 6 AIOH 1373 ILE A 169 62.203 36.106 41.956 1.00 16.95 7 AIOH 1321 CE2 TRP A 163 58.646 38.869 40.826 1.0015.32 6 ATOM 1374 ILE A 169 62.199 34.766 41.380 1.00 16.59 6 AIOH 1322 CE3 TRP A 163 5B.520 36.667 39.803 1.00 14.71 6 ATOM 1375 ILE A 169 63.086 33.751 42.115 1.00 17. 17 6 AIOH 1323 CD1 TRP A 163 56.950 38.813 42.245 1.0013.62 6 ATOH 1376 CG2 ILE A 169 64.599 34.139 42.040 1 .00 16.91 6 AIOH 1324 HE1 IRP A 163 57.980 39.589 41.774 1.00 13.74 7 ATOH 1377 CGI ILE A 169 62.641 33.597 43.557 A IOH 1325 CZ2 IRP A 163 59.757 39.243 40.036 1.00 16.07 6 1 .00 17.77 6 AIOH 1378 C01 ILE A 169 63.595 32.811 44.434 1.00 18.17 6 ATOH 1379 C I LE A 169 60.748 34.265 41.354 1.00 16.43 6 AKΗ 1380 0 I LE A 169 S9.894 34.602 42.175 1.00 15.97 8 ATOM 1381 H SER A 170 60.458 33.469 40.342 1.00 16.39 7 AIOH 1382 CA SER A 170 59.209 32.808 40.120 1.00 16.32 6 ATOM 1383 CB SER A 170 58.830 32.767 38.642 1.00 18.20 6 AIOH 13B4 OG SER A 170 57.519 32.181 38.607 1.00 22.81 B AIOH 1385 C SER A 170 59.306 31.335 40.518 1.00 16.18 6 A IOH 1386 0 SER A 170 60.106 30.599 39.908 1.00 16.17 8 A I OH 1387 H ARG A 171 58.531 30.882 41.508 1.00 15.84 7 A I OH 1388 CA ARG A 171 58.504 29.492 41.954 1.00 15.28 6 A I OH 1389 CB ARG A 171 59.448 29.168 43.104 1.00 17.32 6 AI OH 1390 CG ARG A 171 60.894 29.497 43.152 1.00 19.88 6 A I OH 1391 CD ARG A 171 61.825 28.448 42.555 1.00 23.48 6 A l JH 1392 NE ARG A 171 63.204 28.981 42.466 1.00 27.05 7 I DH 1393 CZ ARG A 171 63.661 29.577 41.358 1.00 29.43 6 A I OH 1394 NH1 ARG A 171 62.909 29.718 40.256 1.00 30.87 7 « » AJ OH 1395 HH2 ARG A 171 64.884 30.070 41.191 1.00 30.59 7 C ATOH 1396 C ARG A 171 57.052 29.164 42.380 1.00 14.63 6 J5 AIOH 1397 0 ARG A 171 56.203 30.055 42.313 1.00 14.71 8 12 AIOH 1398 N ILE A 172 56.737 27.949 42.824 1.00 13. BO 7 3 ATOM 1399 CA ILE A 172 55.389 27.671 43.336 1.00 13.02 6 Zj AIOH 1400 CB ILE A 172 54.752 26.357 42.862 1.00 11.93 6 AIOH 1401 CG2 HE A 172 53.502 26.058 43.656 1.00 11.06 6 fri ATOH 1402 CGI HE A 172 54.360 26.386 41.354 1.00 11.59 6 AI OH 1403 CD1 ILE A 172 53.920 25.010 40.927 1.00 12.67 6 - AI OH 1404 C I LE A 172 55.639 27.730 44.867 1.00 12.55 6 ± ATOH 1405 0 I LE A 172 56.218 26.808 45.469 1.00 12.52 8 m AI OH 1406 N PHE A 173 55.290 28.812 45.529 1.00 11.95 7 H ATOM 1407 CA PHE A 173 55.464 28.982 46.956 1.00 11.52 6 5; A IOH 1408 CB PHE A 173 55.813 30.424 47.326 1.00 8.63 6 j2 AIOH 1409 CG PHE A 173 57.088 30.932 46.719 1.00 8.19 6 JΞ AIOH 1410 CD1 PHE A 173 57.085 31.845 45.697 1.00 6.97 6 i AIOH 1411 CD2 PHE A 173 58.313 30.470 47.211 1.00 8.07 6 _ A IOH 1412 CE 1 PHE A 173 58.277 32.307 45.123 1.00 8.69 6 S AIOH 1413 CE2 PHE A 173 59.512 30.949 46.686 1.00 8.72 6 _--_• AI OH 1414 CZ PHE A 173 59.484 31.844 45.607 1.00 7.75 6 A IOH 1415 C PHE A 173 54.1B9 28.583 47.688 1.00 11.50 6 ATOM 1416 0 PHE A 173 53.109 29.085 47.372 1.00 11.79 8 AIOH 1417 N LYS A 174 54.257 27.696 48.657 1.00 11.28 7 A IOH 1418 CA LYS A 174 53.185 27.303 49.524 1.00 11.02 6 A I OH 1419 CB LYS A 174 53.268 25.849 49.981 1.00 7.54 6 A IOH 1420 CG L YS A 174 52.045 25.443 50.770 1.00 6.03 6 AIOH 1421 CD LYS A 1 4 51.880 23.947 50.993 1.00 5.90 6 AI OH 1422 CE LYS A 174 53.109 23.439 51.713 1.00 6.00 6 AI OH 1423 HZ LYS A 174 52.991 22.034 52.176 1.00 5.20 7 AIOH 1424 C LYS A 174 53.313 28.195 50.787 1.00 11.19 6 AIOH 1425 0 LYS A 174 54.402 28.117 51.406 1.00 11.32 8 AIW 1426 H PHE A 175 52.357 28.950 51.264 1.00 11.10 7 A IOH 1427 CA PHE A 175 52.555 29.759 52.486 1.00 11.23 6 AIOH 1428 CB PHE A 175 51.440 30.845 52.516 1.00 9.58 6 AIOH 1429 CG PHE A 175 51.497 31.920 51.427 1.00 9.11 6 AIOH 1430 CD1 PHE A 175 50.410 32.806 51.283 1.00 8.73 6 A I OH 1431 CD2 PHE A 175 52.569 32.097 50.557 1.00 7.13 6 AKH 1485 CE3 TRP A 182 48.278 25.127 47.361 1.00 5.00 6 ATOH 1538 CA SER A 188 45.109 15.208 41.353 1.00 9.72 6 AHH 1486 CD1 TRP A 182 49.768 21.861 48.002 1.00 5.63 6 ATOM 1539 CB SER A 188 44.906 13.770 41.859 1.00 10.83 6 AIOH K87 HE1 TRP A 182 50.B60 22.616 47.616 1.00 5.04 7 ATOM 1540 OG SER A 188 44.547 12.983 40.714 1.00 12.11 8 All*. 1488 CZ2 IRP A 182 51.110 25.022 46.895 1.00 5.00 6 ATOH 1541 C SER A 188 46.215 15.213 40.288 1.00 9.72 6 AIOH 1489 CZ3 TRP A 182 48.966 26.236 46.927 1.00 5.00 6 ATOM 1542 0 SER A 188 47.239 14.540 40.529 1.00 9.62 8 AIOH 1490 CH2 TRP A 182 50.376 26.1B6 46.723 1.00 5.00 6 ATOH 1543 N GLU A 189 46.009 15.968 39.192 1.00 9.48 7 AIOH 1491 C IRP A 182 45.218 22.348 49.7B7 1.00 8.52 6 ATOH 1544 CA GLU A 189 47.091 16.143 38.252 1.00 9.58 6 AIOH 1492 0 TRP A 182 45.029 21.400 50.552 1.00 8.24 8 ATOH 1545 CB GLU A 189 46.761 17.025 37.029 1.00 12.65 6 AIOH 1493 U ASP A 183 44.187 22.939 49.183 1.00 β.61 7 ATOH 1546 CG GLU A 189 45.655 16.361 36.202 1.00 14.93 6 AloH 1494 CA ASP A 183 42.814 22.546 49.339 1.00 8.57 6 ATOH 1547 CD GLU A 189 44.958 17.419 35.359 1.00 16.59 6 AIOH 1495 CB ASP A 183 41.746 23.407 48.669 1.00 7.64 6 ATOM 1548 OE1 GLU A 189 44.060 18.118 35.868 1.00 16.06 8 AIOH 1496 CG ASP A 183 41.829 24.846 49.207 1.00 7.97 6 ATOH 1549 OE2 GLU A 1B9 45.364 17.496 34.187 1.00 19.90 8 AIOH 1497 001 ASP A 183 42.136 25.011 50.384 1.00 5.19 8 ATOH 1550 C GLU A 1B9 48.208 16.888 38.998 1.00 9.38 6 AIX 1498 002 ASP A 1B3 41.604 25.903 48.623 1.00 7.20 8 ATOM 1551 0 GLU A 189 47.948 17.852 39.783 1.00 9.35 8 Al: * M 1499 C ASP A 183 42.678 21.163 48.661 1.00 8.68 6 ATOH 1552 N ASN A 190 49.447 16.512 38.785 1.00 9.02 7 AIOH 1500 0 ASP A 183 43.392 20.764 47.757 1.00 8.29 8 ATOH 1553 CA ASN A 190 50.591 17.137 39.437 1.00 8.9B 6 /1 4;OH 1501 H TRP A 184 41.655 20.526 49.221 1.00 8.85 7 ATOH 1554 CB ASN A 190 50.708 18.629 39.139 1.00 11.63 6 AIOH 1502 CA TRP A 184 41.337 19.214 48.B16 1.00 9.31 6 ATOH 1555 CG ASN A 190 50.842 19.067 37.714 1.00 13.22 6 0 AIOH 1503 CB IRP A 184 42.068 18.015 49.485 1.00 9.16 6 ATOH 1556 ODl ASN 190 51.553 18.489 36.913 1.00 13.96 8 AIOH 1504 CG TRP A 184 41.B58 16.719 48.814 1.00 9.24 6 ATOH 1557 N02 ASN 190 50.145 20.093 37.234 1.00 14.84 7 2 AIOH 1505 CD2 IRP A 184 42.391 16.211 47.580 1.00 9.64 6 ATOM 1558 C ASN 190 50.548 16.928 40.959 1.00 8.84 6 \ AIOH 1506 CE2 TRP A 184 41.870 14.896 47.384 1.00 9.60 6 ATOH 1559 0 ASN 190 51.020 17.773 41.750 1.00 9.06 8 ~ AIOH 1507 CE3 IRP A 184 43.240 16.730 46.594 1.00 8.61 6 ATOM 1S60 N GLY A 191 49.949 15.854 41.439 1.00 8.36 7 2 ATOH 1508 C01 IRP A 1B4 41.009 15.713 49.300 1.0010.78 6 ATOM 1561 CA GLY 191 49.772 15.467 42.809 1.00 7.95 6 2 AIOH 1509 HE1 TRP A 184 41.019 14.620 48.426 1.00 9.86 7 ATOM 1562 C GLY 191 4B.597 16.148 43.430 1.00 7.74 6 l AIOH 1510 CZ2 TRP A 184 42.149 14.151 46.250 1.00 9.85 6 ATOM 1563 0 GLY 191 47.747 15.586 44.065 1.00 7.89 8 }: Ainu i5iι czs TRP A ιβ4 43.547 15.968 45.479 1.00 9.71 6 ATOH 1564 N ASN A 192 48.537 17.450 43.284 1.00 7.66 7 n AIOH 1512 CH2 TRP A 184 43.008 14.693 45.314 1.00 9.96 6 ATOH 1565 CA ASN A 192 47.472 18.353 43.732 1.00 7.21 6 AIOH 1513 C TRP A 184 39.766 18.960 48.936 1.00 9.70 6 ATOM 1566 CB ASN A 192 47.596 18.649 45.227 1.00 B.14 6 - ATOM 1514 0 TRP A 184 39.093 19.322 49.789 1.0010.01 8 ATOM 1567 CG ASH A 192 46.628 19.665 45.785 1.00 7.93 6 AIOH 1515 N GLU A 185 39.594 18.432 47.7B5 1.00 9.88 7 AIOH 1568 001 ASN A 192 46.584 20.794 45.287 1.00 8.55 β AIOH 1516 CA GLU A 185 39.263 17.724 46.655 1.00 9.32 6 ATOM 1569 ND2 ASH A 192 45.839 19.388 46.805 1.00 7.17 7 AIOH 1517 CB GLU A 185 38.201 16.707 46.321 1.0011.19 6 ATOM 1570 C ASN A 192 47.572 19.615 42.863 1.00 6.90 6 ~ AIOH 1518 CG GLU A 185 38.829 15.901 45.132 1.0011.41 6 ATOM 1571 0 ASN A 192 48.574 20.328 42.910 1.00 6.69 8 j AIOH 1519 CD GLU A 185 38.070 14.631 44.814 1.0013.77 6 ATOH 1572 N TYR A 193 46.517 19.881 42.099 1.00 6.77 7 AIOH 1520 0E1 GLU A 185 37.147 14.228 45.559 1.0014.04 8 ATOM 1573 CA TYR A 193 46.405 20.986 41.210 1.00 7.00 6 AIOH 1521 0E2 GLU A 185 38.349 14.001 43.76B 1.0014.41 8 ATOM 1574 CB TYR A 193 45.725 20.535 39.867 1.00 7.52 6 AIOH 1522 C GLU A 185 39.394 18.759 45.479 1.00 8. 8 6 ATOH 1575 CG TYR A 193 46.348 21.143 38.659 1.00 8.30 6 AIOH 1523 0 GLU A 185 38.591 19.636 45.294 1.00 8.92 8 ATOH 1576 C01 TYR A 193 46.218 20.596 37.385 1.00 8.97 6 AIOH 1524 N VAL A 186 40.502 18.566 44.792 1.00 8.34 7 ATOM 1577 CE1 TYR A 193 46.841 21.202 36.283 1.00 9.17 6 AIOH 1525 CA VAL A 186 40.810 19.326 43.583 1.00 8.33 6 ATOH 1578 C02 TYR A 193 47.096 22.301 38.738 1.00 8.68 6 AIOH 1526 CB VAL A 186 41.807 20.506 43.735 1.00 8.32 6 ATOH 1579 CE2 TYR A 193 47.695 22.928 37.673 1.00 9.08 6 ATOH 1527 CGI VAL A 186 41.196 21.617 44.616 1.00 7.05 6 ATOH 1580 CZ TYR A 193 47.564 22.343 36.424 1.00 9.29 6 ATOH 1528 CG2 VAL A 186 43.173 20.110 44.308 1.00 5.20 6 ATOM 1581 OH TYR A 193 48.177 22.966 35.361 1.00 9.62 AIOH 1529 C VAL A 186 41.364 18.291 42.578 1.00 8.42 6 8 ATOH 1582 C TYR A 193 45.646 22.201 41.776 1.00 6.92 AIOH 1530 0 VAL A 186 41.505 17.111 42.956 1.00 8.25 8 6 ATOH 1583 0 TYR A 193 45.034 22.979 41.061 1.00 AIOH 1531 N SER A 187 41.735 18.666 41.367 1.00 8.40 7 6.78 8 ATOH 1584 N ASP A 194 45.662 22.448 43.066 1.00 AIOH 1532 CA SER A 187 6.98 42.313 17.723 40.445 1.00 8.96 6 7 ATOH 1585 CA ASP A 194 45.102 23.587 43.773 AIOH 1533 CB SER A 187 1.00 42.664 18.422 39.113 1.00 8.95 6 6.81 6 ATOH 1586 CB ASP A 194 45.338 23.579 45.279 AIOH 1534 OG SER A 187 1.00 43.472 17.537 38.328 1.00 8.65 8 7.26 6 ATOH 1587 CG ASP A 194 44.586 24.609 AIOH 1535 C SER A 187 43.603 17.153 41.060 1.00 9.46 6 46.082 1.00 8.65 6 ATOH 1588 001 ASP A 194 43.590 AIOH 1536 0 SER A 187 25.127 44.375 17.887 41.684 1.00 9.28 8 45.523 1.00 9.18 8 ATOH 1589 002 ASP A 194 44.730 AIOH 1537 H SER A 188 43.908 15.846 40.823 1.00 9.77 7 24.922 47.280 1.00 8.87 8 ATOM 1590 C ASP A 194 45.815 24.809 43.156 1.00 6.63 6 AIOH 1697 N ASP 207 36.466 32.591 56.971 1.00 6.12 7 AIOH 1698 CA ASP 207 36.056 33.949 56.613 1.00 05 6 IOH 1699 CB ASP 207 36.954 35.059 57.168 1.00 37 6 AIOH 1700 CG ASP 207 36.964 35.075 58.705 1.00 87 6 AIOH 1701 001 ASP 207 36.208 34.392 59.396 1.00 00 B ATOH 1702 002 ASP 207 37.779 35.836 59.261 1.00 95 B AIOH 1703 C ASP 207 36.033 34.139 55.096 1.00 17 6 AIOH 1704 0 ASP 207 35.225 34.906 54.573 1.00 78 8 AIOH 1705 H VAL 208 36.985 33.441 54.427 1.00 47 7 AIOH 1706 CA VAL 208 37.054 33.472 52.973 1.00 6.SB 6 AIOH 1707 CB VAL 20B 38.353 32.859 52.465 1.00 .47 6 AIOH 1708 CGI VAL 208 38.292 32.594 50.949 1.00 06 6 A' H 1709 CG2 VAL 208 39.526 33.788 52.805 1.00 71 6 '■ ' OH 1710 C VAL 208 35.795 32.784 52.426 1.00 90 6 AIOH 1711 0 VAL 208 35.103 33.349 51.530 1.00 95 8 AI H 1712 H VAL 209 35.436 31.598 52.923 1.00 93 7 -*.IOH 1713 CA VAL 209 34.257 30.881 52.457 1.00 7.00 6 1714 209 34.140 29.527 53.170 1.00 5.34 6 O AIOH CB VAL ATOH 1715 CGI VAL 209 32.865 2B.784 52.814 1.00 5.00 6 AIOH 1716 CG2 VAL 209 35.346 28.638 52.878 1.00 5.00 6 AIOH 1717 C VAL 209 32.996 31.743 52.652 1.00 7.32 6 AIOH 1718 0 VAL 209 32.199 31.882 51.684 1.00 7.35 8 AIOH 1719 H ALA 210 32.798 32.341 53.838 1.00 7.34 7 AIOH 1720 CA ALA 210 31.623 33.165 54.102 1.00 7.52 6 AIOH 1721 CB ALA 210 31.558 33.591 55.584 1.00 7.62 6 ATOH 1722 ALA 210 31.490 34.416 53.261 1.00 7.58 6 ATOH 1723 ALA 210 30.401 34.806 52.803 1.00 7.48 8 AIOH 1724 GLU 211 32.614 35.095 53.060 1.00 7.67 7 AIOH 1725 CA GLU 211 32.662 36.296 52.216 1.00 7.90 6 0 ATOH 1726 CB GLU 211 34.061 36.946 52.363 1.00 9.96 6 AIOH 1727 CG GLU 211 34.267 38.168 51.517 1.00 13.B9 6 AIOH 1728 CD GLU 211 33.197 39.270 51.640 1.00 16.28 6 AI H 1729 OE1 GLU 211 32.845 39.772 50.515 1.00 18.47 8 AIOH 1730 OE2 GLU 211 32.747 39.610 52.771 1.00 13.34 B . AIOH 1731 C GLU 211 32.3B4 36.053 50.721 1.00 7.61 6 AIOH 1732 GLU 211 31.758 36.890 50.060 1.00 7.56 8 AI H 1733 THR 212 32.907 34.960 50.184 1.00 7.17 7 AIOH 1734 CA T HR 212 32.727 34.572 48.781 1.00 6.96 6 AIOH 1735 CB THR 212 33.705 33.464 48.413 1.00 8.17 6 AIOH 1736 OG1 THR 212 35.056 33.934 48.636 1.00 9.40 8 AIOH 1737 CG2 THR 212 33.660 33.139 46.939 1.00 7.69 6 AIOH 1738 T HR 212 31.276 34.155 48.564 1.00 6.87 6 AIOH 1739 T HR 212 30.724 34.456 47.522 1.00 6.69 8 AIOH 1740 L YS 213 30.604 33.516 49.527 1.00 6.92 7 AIOH 1741 CA LYS 213 29.168 33.214 49.424 1.00 7.14 6 AIOH 1742 CB LYS 213 28.634 32.331 50.553 1.00 6.97 6 AIOH 1743 CG LYS 213 29.076 30.863 50.321 1.00 9.06 6 AIOH 1744 CD LYS 213 28.605 30.065 51.592 1.00 9.86 6 AIOH 1745 CE LYS 213 29.312 28.701 51.442 1.00 10.33 6 AIOH 1746 NZ LYS 213 28.914 27.848 52.609 1.00 11.44 7 AIOH 1747 LYS 213 28.352 34.524 49.417 1.00 7.15 6 AIOH 1748 LYS 213 27.462 34.755 48.620 1.00 6.94 8 AIOH 1749 LYS 214 28.687 35.476 50.279 1.00 7.01 7 ATOH 1803 CE1 TYR 219 29.180 39.619 38.541 1.00 9.96 6 AIOH 18(14 C02 TYR 219 28.416 37.404 40.008 1.00 9.35 6 AIOH 1805 CE2 TYR 219 28.959 37.265 38.740 1.00 9.78 6 AIOH 1806 CZ TYR 219 29.346 38.361 38.021 1.00 10.19 6 AI H 1807 OH TYR 219 29.899 38.187 36.757 1.00 11.08 8 AIOH 1808 C TYR 219 25.279 39.259 41.447 1.00 8.69 6 ATOH 1809 O TYR 219 24.836 39.946 40.527 1.00 8.37 8 AIOH 1810 N ALA 220 24.676 38.131 41.869 1.00 9.13 7 AIOH 1811 CA ALA 220 23.427 37.644 41.267 1.00 9.77 6 AI H 1812 CB ALA 220 22.899 36.384 41.981 1.00 8.61 6 AIOH 1H13 ALA 220 22.315 38.685 41.321 1.00 10.07 6 AIOH 1814 ALA 220 21.536 38.887 40.377 1.00 10.05 8 AIOH 1815 ASH 221 22.192 39.338 42.473 1.00 10.39 7 IOH 1816 CA ASH 221 21.200 40.374 42.757 1.00 10.66 6 _ 'OH 1817 CB ASH 221 21.013 40.698 44.262 1.00 13.90 6 'OH 1818 CG ASH 221 20.192 39.543 44.855 1.00 18.18 6 Λ A'OH 1819 001 ASH 221 19.371 38.852 44.227 1.00 19.46 8 ON 1820 HD2 ASN 221 20.481 39.263 46.125 1.00 19.86 7 B ATL'H 1821 C ASH 221 21.524 41.717 42.136 1.00 10.51 6 Λ AIOH 1822 0 ASH 221 20.592 42.323 41.626 1.00 10.40 8 IOH 1823 N GLU 222 22.794 42.125 42.143 1.00 10.51 7 AIOH 1824 CA GLU 222 23.160 43.432 41..552 1.00 10.18 6 AI H 1825 CB GLU 222 24.621 43.807 41.,791 1.00 11.08 6 AIOH 1826 CG GLU 222 25.013 45.244 41.469 1.00 12.96 6 ATOH 1827 CD GLU 222 24.412 46.203 42.496 1.00 15.13 6 Λ ATOH 1828 0E1 GLU 222 23.947 45.777 43.576 1.00 15.79 8 ATOH 1829 0E2 GLU 222 24.381 47.432 42.254 1.00 16.17 8 AIOH 1830 GLU 222 22.903 43.428 40.052 1.00 9.82 6 AIOH 1831 GLU 222 22.470 44.444 39.507 1.00 9.72 8 AI H 1832 LEU 223 23.227 42.343 39.348 1.00 9.48 7 30 AIOH 1833 CA LEU 223 23.009 42.319 37.909 1.00 9.43 6 ATOM 1834 CB LEU 223 24.300 41.715 37.281 1.00 7.13 6 AIOH 1835 CG LEU 223 25.595 42.503 37.476 1.00 5.72 6 AIOH 1B36 CD1 LEU 223 26.752 41.715 36.835 1.00 5.00 6 AI H 1837 CD2 LEU 223 25.470 43.888 36.880 1.00 5.20 O- 6 AIOH 1U38 C LEU 223 21.794 41.550 37.456 1.00 9.44 6 AIOH 1839 LEU 223 21.561 41.335 36.280 1.00 9.57 8 AIOH 1840 SER 224 20.953 40.998 38.286 1.00 9.74 7 AIOH 1841 CA SER 224 19.B25 40.156 37.925 1.00 10.06 6 AIOH 1842 CB SER 224 18.660 40.832 37.156 1.00 14.91 6 AIOH 1843 OG SER 224 18.251 41.991 37.901 1.00 19.93 8 AIOH 1844 C SER 224 20.293 38.979 37.047 1.00 9.76 6 AI H 1845 SER 224 19.648 38.752 36.004 1.00 9.74 8 AIOH 1846 LEU 225 21.340 38.248 37.445 1.00 9.20 7 AIOH 1847 CA LEU 225 21.770 37.113 36.651 1.00 8.94 6 AIOH 1848 CB LEU 225 23.164 36.688 37.088 1.00 10.36 6 AIOH 1849 CG LEU 225 24.297 37.738 36.9S8 1.00 11.62 6 AIOH 1850 CD1 LEU 225 25.552 37.149 37.597 1.00 10.68 6 AIOH 1851 CD2 LEU 225 24.524 38.163 35.508 1.00 10.53 6 AIOH 1852 C LEU 225 20.793 35.945 36.827 1.00 8.77 6 AIOH 1853 0 LEU 225 20.084 35.785 37.796 1.00 8.44 8 AIOH 1854 H ASP 226 20.734 35.084 35.804 1.00 8.55 7 AI H 1855 CA ASP 226 19.950 33.911 35.674 1.00 7.98 6 ATOM 1962 CA SER 239 32.706 20.656 48.065 1.00 7.57 6 ATOH 1963 CB SER 239 32.940 19.984 49.417 1.00 7.79 6 ATOH 1964 OG SER 239 34.169 20.443 49.919 1.00 10.61 8 ATOH 1965 C SER 239 32.410 22.159 4B.249 1.00 7.33 6 ATOH 1966 0 SER 239 31.237 22.448 48.454 1.00 7.20 8 ATOM 1967 N PHE 240 33.380 23.066 48.168 1.00 7.19 7 ATOH 1968 CA PHE 240 33.073 24.471 48.275 1.00 7.28 6 ATOH 1969 CB PHE 240 34.332 25.325 48.382 1.00 7.42 6 ATOH 1970 CG PHE 240 34.049 26.801 48.123 1.00 7.00 6 ATOH 1971 CD1 PHE 240 33.390 27.560 49.085 1.00 6.31 6 ATOH 1972 CD2 PHE 240 34.413 27.352 46.911 1.00 6.51 6 ATOH 1973 CE1 PHE 240 33.091 28.B86 48.775 1.00 7.11 6 ATOH 1974 CE2 PHE 240 34.116 28.674 46.615 1.00 5.97 6 ATOH 1975 CZ PHE 240 33.479 29.440 47.555 1.00 5.18 6 ATOH 1976 C PHE 240 32.259 24.900 47.044 1.00 7.56 6 ATOH 1977 0 PHE 240 31.251 25.631 47.191 1.00 7.63 8 ATOH 1978 N LEU 241 32.639 24.464 4S.B38 1.00 7.46 7 ATOH 1979 CA LEU 241 31.880 24.877 44.661 1.00 7.91 6 0 ATOH 1980 CB LEU 241 32.528 24.553 43.318 1.00 5.00 6 ATOM 1981 CG LEU 241 33.B14 25.279 42.944 1.00 5.00 6 ATOM 1982 CD1 LEU 241 34.520 24.613 41.753 1.00 5.00 6 ATOH 1983 CD2 LEU 241 33.548 26.754 42.654 1.00 5.00 6 ATOH 1984 C LEU 241 30.418 24.377 44.720 1.00 8.46 6 ATOH 19B5 0 LEU 241 29.483 25.127 44.303 1.00 8.58 8 ATOH 1986 N ARG 242 30.184 23.164 45.219 1.00 8.61 7 ATOH 1987 CA ARG 242 28.777 22.774 45.286 1.00 8.92 6 ATOM 1988 CB ARG 242 28.716 21.286 45.431 1.00 10.58 6 ATOH 1989 CG ARG 242 28.819 20.546 46.608 1.00 12.57 6 ATOH 1990 CD ARG 242 27.687 19.642 47.094 1.00 13.52 6 0 ATOH 1991 NE ARG 242 28.192 19.629 48.476 1.00 15.26 7 ATOH 1992 CZ ARG 242 28.955 18.913 49.256 1.00 17.48 6 ATOH 1993 NH1 ARG 242 29.464 17.761 48.866 1.00 19.52 7 ATOH 1994 NH2 ARG 242 29.303 19.285 50.505 1.00 18.04 7 j ATOH 1995 C ARG 242 28.042 23.548 46.379 1.00 8.91 6 _ ATOH 1996 0 ARG 242 26.891 23.909 46.129 1.00 8.59 8 ATOM 1997 N ASP 243 28.653 23.828 47.526 1.00 9.00 7 ATOM 1998 CA ASP 243 27.964 24.591 48.533 1.00 9.47 6 ATOH 1999 CB ASP 243 28.812 24.581 49.811 1.00 11.98 6 ATOM 2000 CG ASP 243 28.766 23.183 50.417 1.00 15.20 6 ATOH 2001 001 ASP 243 29.580 22.982 51.372 1.00 19.21 8 ATOH 2002 002 ASP 243 28.049 22.251 50.036 1.00 13.33 8 ATOH 2003 C ASP 243 27.798 26.049 48.117 1.00 9.53 6 ATOM 2004 0 ASP 243 26.797 26.664 48.539 1.00 9.54 8 ATOM 2005 N TRP 244 28.755 26.581 47.303 1.00 9.34 7 ATOH 2006 CA TRP 244 28.622 28.005 46.908 1.00 9.20 6 ATOH 2007 CB TRP 244 29.862 28.511 46.195 1.00 7.34 6 ATOM 2008 CG TRP 244 29.831 29.924 45.719 1.00 8.91 6 ATOH 2009 CD2 TRP 244 29.442 30.367 44.411 1.00 9.51 6 ATOH 2010 CE2 TRP 244 29.589 31.773 44.384 1.00 10.54 6 ATOH 2011 CE3 TRP 244 29.020 29.698 43.243 1.00 10.38 6 ATOH 2012 CD1 TRP 244 30.168 31.065 46.419 1.00 9.07 6 ATOH 2013 NE1 TRP 244 30.036 32.191 45.638 1.00 9.59 7 ATOH 2014 CZ2 TRP 244 29.289 32.524 43.219 1.00 9.81 6 ATOH 2015 CZ3 TRP A 244 28.727 30.446 42.096 1.0010.45 6 AIOH 2016 CH2 TRP A 244 28.862 31.859 42.106 1.00 9.71 6 AIOH 2017 C TRP A 244 27.386 28.200 46.006 1.00 9.28 6 ATOH 2018 0 TRP A 244 26.651 29.168 46.164 1.00 8.82 8 ATOH 2019 N VAL A 245 27.217 27.284 45.056 1.00 9.64 7 ATOH 2020 CA VAL A 245 26.082 27.305 44.114 1.0010.52 6 ATOH 2021 CB VAL A 245 26.108 26.185 43.039 1.0012.05 6 ATOH 2022 CG1 VAL A 245 24.832 26.113 42.198 1.0013.84 6 ATOH 2023 CG2 VAL A 245 27.262 26.450 42.081 1.0013.35 6 AIOH 2024 C VAL A 245 24.722 27.203 44.853 1.0010.63 6 AIOH 2025 O VAL A 245 23.758 27.906 44.590 1.0010.02 8 ATI-. 2026 H GIN A 246 24.745 26.269 45.790 1.0011.30 7 AHΗ 2027 CA GLN A 246 23.552 26.022 46.634 1.0012.37 6 AT'H 2028 CB GLN A 246 23.878 24.727 47.381 1.0018.96 6 Al H 2029 CG GLN A 246 22.737 24.176 48.214 1.0027.47 6 VUH 2030 CD GLN A 246 23.367 23.366 49.350 1.0034.63 6 t/1 φH 20 1 OE1 GIN A 246 22.842 23.446 50.493 1.0037.91 8 C .OH 2032 NE2 GLN A 246 24.476 22.642 49.028 1.0036.61 7 00 ATOH 2033 C GLH A 246 23.153 27.225 47.485 1.0012.39 6 *J AIOH 2034 0 GIN A 246 21.970 27.561 47.531 1.0012.22 B 2 AIOH 2035 N ALA A 247 24.083 27.968 48.099 1.0012.46 7 H AIOH 2036 CA ALA A 247 23.852 29.144 48.893 1.0012.61 6 C AIOH 2037 CB ALA A 247 25.094 29.791 49.517 1.0012.47 6 H AIOH 2038 C ALA A 247 23.231 30.263 48.050 1.0012.74 6 m AIOH 2039 0 ALA A 247 22.308 30.857 48.561 1.0012.85 8 _ζ* AIOH 2040 N VAL A 248 23.710 30.49S 46.838 1.0012.75 7 •j AIOH 2041 CA VAL A 248 23.159 31.471 45.933 1.0012.69 6 IE AIOH 2042 CB VAL A 248 24.009 31.688 44.684 1.0011.87 6 _j AIOH 2043 CGI VAL A 248 23.357 32.721 43.754 1.0012.19 6 _____ ATOH 2044 CG2 VAL A 24B 25.400 32.171 45.014 1.0011.42 6 ~~ AIOH 2045 C VAL A 248 21.748 31.040 45.537 1.0012.91 6 C AIOH 2046 0 VAL A 248 20.866 31.889 45.506 1.0012.81 8 ζ~ AToH 2047 N ARG A 249 21.483 29.791 45.237 1.0013.31 7 m AIOH 2048 CA ARG A 249 20.124 29.352 44.897 1.0013.92 6 JjJ AIOH ?049 CB ARG A 249 20.066 27.906 44.404 1.0011.75 6 •2 AIOH 2050 CG ARG A 249 20.681 27.726 43.033 1.0012.59 6 AIOH 2051 CO ARG A 249 20.814 26.274 42.576 1.0012.82 6 AIOH 2052 HE ARG A 249 21.411 26.198 41.224 1.0013.02 7 AIOH 2053 CZ ARG A 249 22.045 25.141 40.739 1.0013.82 6 AIOH 2054 Hill ARG A 249 22.150 24.041 41.476 1.0011.68 7 AIOH 2055 NH2 ARG A 249 22.589 25.166 39.515 1.0015.22 7 ATOH 2056 C ARG A 249 19.215 29.503 46.125 1.0014.55 6 ATOH 2057 0 ARG A 249 18.082 30.00S 45.970 1.0014.34 8 AIOH 2058 N GLN A 250 19.685 29.106 47.329 1.0015.16 7 ATOH 2059 CA GIN A 250 18.794 29.252 48.498 1.0015.83 6 AIOH 2060 CB GLN A 250 19.437 28.816 49.790 1.0021.15 6 AIOH 2061 CG GLN A 250 18.902 27.566 50.460 1.0028.24 6 AIOH 2062 CO GLN A 250 20.067 26.619 50.807 1.0032.12 6 AIOH 2063 OE1 GLN A 250 21.116 27.047 51.333 1.0034.30 8 ATOH 2064 NE2 GLH A 250 19.907 25.331 50.478 1.0032.80 7 AIOH 2065 C GLN A 250 18.362 30.699 48.707 1.0015.86 6 A IOH 2066 0 GLH A 250 17.196 31.022 48.871 1.0015.83 8 ATOM 2067 H ALA A 251 19.316 31.621 48.689 1.0015.85 7 ATOM 2174 N GLN 264 39.758 18.950 31.301 1.00 10.57 7 ATOH 2175 CA GLN 264 40.441 17.687 31.185 1.00 10.92 6 ATOH 2176 CB GLN 264 40.619 16.999 32.536 1.00 14.66 6 ATOH 2177 CG GLN 264 41.796 16.043 32.600 1.00 18.65 6 ATOH 2178 CD GLN 264 41.972 15.344 33.934 1.00 22.60 6 ATOH 2179 0E1 GLN 264 41.214 15.481 34.907 1.00 24.23 8 ATOM 2180 NE2 GLN 264 42.996 14.478 34.047 1.00 23.90 7 ATOM 2181 C GLN 264 39.681 16.811 30.191 1.00 11.04 6 ATOM 2182 0 GLN 264 38.461 16.643 30.232 1.00 10.83 8 ATOH 2183 N ASN 265 40.454 16.216 29.289 1.00 11.25 7 ATOH 2184 CA ASN 265 40.151 15.322 28.209 1.00 11.87 6 ATOH 2185 CB ASN 265 41.223 15.365 27.078 1.00 11.52 6 ATOH 2186 CG ASH 265 40.655 14.637 25.854 1.00 12.03 6 ATOH 2187 001 ASN 265 39.485 14.278 25.764 1.00 11.79 8 ATOH 2188 ND2 ASN 265 41.445 14.294 24.857 1.00 11.74 7 AIOH 2189 C ASN 265 40.028 13.873 28.691 1.00 12.36 6 ATOH 2190 0 ASN 265 40.755 13.007 28.282 1.00 12.25 8 ATOM 2191 N ASN 266 39.116 13.676 29.634 1.00 13.06 7 0 ATOM 2192 CA ASN 266 38.844 12.428 30.337 1.00 13.75 6 ATOH 2193 CB ASN 266 39.910 12.362 31.416 1.00 18.58 6 ATOM 2194 CG ASN 266 40.150 11.016 32.031 1.00 22.56 6 ATOM 2195 001 ASN 266 41.311 10.519 31.969 1.00 26.43 8 ATOH 2196 N02 ASN 266 39.160 10.410 32.662 1.0021.13 7 ATOH 2197 C ASN 266 37.441 12.394 30.944 1.00 13.73 6 ATOH 2198 0 ASN 266 37.161 13.123 31.927 1.00 13.68 8 ATOH 2199 N ALA 267 36.552 11.545 30.362 1.00 13.47 7 ATOH 2200 CA ALA 267 35.178 11.440 30.83S 1.00 13.35 6 ATOM 2201 CB ALA 267 34.330 10.522 29.944 1.00 12.56 6 ATOH 2202 C ALA 267 35.076 10.997 32.287 1.00 13.08 6 AIOH 2203 0 ALA 267 34.19S 11.454 33.027 1.00 13.14 0 a ATOH 2204 N GLY 268 35.918 10.106 32.733 1.00 12.97 7 ATOH 220S CA GLY 268 35.973 9.564 34.083 1.00 12.93 6 ATOM 2206 C GLY 268 36.184 10.653 35.146 1.00 13.05 6 AIOH 2207 0 GLY 268 35.512 10.656 36.213 1.00 13.01 8 ATOH 2208 N LYS 269 37.109 11.575 34.879 1.00 12.90 7 ATOH 2209 CA LYS 269 37.425 12.681 35.786 1.00 13.04 6 ATOM 2210 CB LYS 269 38.790 13.296 35.417 1.00 17.83 6 ATOM 2211 CG LYS 269 39.840 12.506 36.217 1.00 22.85 6 ATOH 2212 CD LYS 269 40.869 12.034 35.211 1.00 27.74 6 ATOH 2213 CE LYS 269 41.722 10.BBS 35.785 1.0030.85 6 ATOM 2214 HZ LYS 269 42.663 10.356 34.698 1.00 32.23 7 ATOH 2215 C LYS 269 36.296 13.699 35.776 1.00 12.76 6 ATOH 2216 0 LYS 269 35.918 14.230 36.828 1.00 12.6S 8 ATOH 2217 N LEU 270 35.696 13.903 34.596 1.00 12.42 7 ATOH 2218 CA LEU 270 34.539 14.810 34.538 1.00 12.16 6 ATOH 2219 CB LEU 270 34.164 15.161 33.088 1.00 13.49 6 ATOH 2220 CG LEU 270 34.959 16.348 32.467 1.00 13.12 6 ATOH 2221 CD1 LEU 270 34.614 17.623 33.197 1.00 13.42 6 AIOH 2222 CD2 LEU 270 36.465 16.210 32.550 1.00 13.72 6 ATOH 2223 C LEU 270 33.412 14.169 35.315 1.00 11.76 6 ATOH 2224 0 LEU 270 32.700 14.934 35.981 1.00 11.63 8 ATOH 2225 N GLU 271 33.219 12.851 35.281 1.00 11.41 7 ATOH 2226 CA GLU 271 32.136 12.233 36.051 1.00 11.29 6 AIOH 2227 CB GLU A 271 32.024 10.817 35.510 1.00 16.08 6 ATOH 2280 CA THR A 277 29.173 18.187 43.406 1.0012.78 6 ATOH 2228 CG GLU A 271 31.015 10.010 36.333 1.00 23.09 6 ATOH 2281 CB THR A 277 29.520 19.264 42.357 1.00 12.02 6 ATOH 2229 CD GLU A 271 30.861 8.627 35.720 1.00 27.19 6 ATOH 2282 OG1 THR A 277 29.323 18.649 41.065 1.0012.30 8 AIOH 2230 OE1 GLU A 271 29.716 8.351 35.359 1.00 29.23 8 ATOH 2283 CG2 THR A 277 30.941 19.791 42.492 1.00 8.90 6 AIOH 2231 0E2 GLU A 271 31.830 7.845 35.526 1.00 30.01 8 ATOH 2284 C THR A 277 27.701 17.794 43.416 1.0012.70 6 AIOH 2232 C GLU A 271 32.339 12.279 37.554 1.00 10.89 6 ATOH 2285 0 THR A 277 26.812 18.613 43.190 1.0012.66 8 ATOH 2233 0 GLU A 271 31.458 12.370 38.404 1.00 10.58 8 ATOH 22B6 N SER A 278 27.426 16.518 43.673 1.0012.73 7 ATOH 2234 H ASN A 272 33.615 12.189 37.987 1.00 10.66 7 ATOH 2287 CA SER A 278 26.069 16.047 43.729 1.0012.83 6 AIOH 2235 CA ASN A 272 34.008 12.309 39.385 1.00 10.31 6 ATOH 2288 CB SER A 27B 25.280 16.804 44.854 1.0014.69 6 AK-H 2236 CB ASN A 272 35.520 12.089 39.643 1.00 11.32 6 ATOH 2289 OG SER A 278 25.963 16.531 46.061 1.0018.04 8 AIOH 2237 CG ASN A 272 35.969 12.380 41.064 1.00 11.99 6 ATOH 2290 C SER A 278 25.283 16.294 42.474 1.0012.85 6 Aim 2258 001 ASH A 272 35.616 11.603 41.966 1.00 11.66 8 ATOH 2291 0 SER A 278 24.049 16.483 42.663 1.00 13.07 8 AKH 2239 N02 ASN A 272 36.701 13.474 41.322 1.00 12.45 7 AIOH 2292 N PHE A 279 25.774 16.339 41.260 1.00 12.49 7 HI H 2240 C ASN A 272 33.588 13.709 39.873 1.00 9.78 6 ATOH 2293 CA PHE A 279 24.897 16.593 40.100 1.0012.16 6 .1 H 2241 0 ASH A 272 33.0B0 13.897 40.979 1.00 9.63 8 ATOH 2294 CB PHE A 279 23.976 15.344 39.973 1.0012.70 6 M.M 2242 H TYR A 273 33.777 14.748 39.063 1.00 9.45 7 ATOH 2295 CG PHE A 279 24.772 14.122 39.524 1.0012.B7 6 _ • *- . 2243 CA TYR A 273 33.349 16.104 39.486 1.00 9.06 6 ATOH 2296 CD1 PHE A 279 25.183 13.153 40.435 1.0013.85 6 ,NT0H 2244 CB TYR A 273 33.908 17.179 3B.558 1.00 8.65 6 ATOH 2297 CD2 PHE A 279 25.085 13.919 38.199 1.0013.30 6 ATOH 2245 CG TYR A 273 33.509 18.626 3B.903 1.00 8.44 6 ATOH 2298 CE1 PHE A 279 25.903 12.038 40.045 1.0013.14 6 J ATOH 2246 CD1 TYR A 273 34.242 19.333 39.838 1.00 8.51 6 ATOH 2299 CE2 PHE A 279 25.801 12.799 37.786 1.0013.99 6 AIOH 2247 CE1 IYR A 273 33.915 20.650 40.228 1.00 8.39 6 ATOH 2300 CZ PHE A 279 26.246 11.878 38.726 1.00 13.30 6 AIOH 2248 CD2 TYR A 273 32.391 19.231 38.364 1.00 B.33 6 ATOH 2301 C PHE A 279 24.170 17.912 40.149 1.00 12.03 6 AIOH 2249 CE2 TYR A 273 32.015 20.523 38.695 1.00 8.66 6 ATOH 2302 0 PHE A 279 23.18S 18.072 39.417 1.0012.27 8 ATOH 2250 CZ TYR A 273 32.827 21.214 39.625 1.00 B.60 6 ATOH 2303 N ASN A 280 24.646 18.942 40.882 1.0011.58 7 AIOH 2251 OH TYR A 273 32.452 22.481 39.938 1.00 8.94 8 ATOH 2304 CA ASN A 280 23.979 20.228 40.984 1.0011.30 6 AIOH 2252 C TYR A 273 31.837 16.135 39.662 1.00 9.06 6 ATOM 2305 CB ASN A 280 24.025 20.735 42.438 1.0011.18 6 AIOH 2253 0 TYR A 273 31.340 16.679 40.688 1.00 B.80 8 ATOH 2306 CG ASN A 280 25.222 21.558 42.868 1.0013.48 6 AIOH 2254 H LEU A 274 31.061 15.569 38.736 1.00 9.52 7 ATOH 2307 001 ASN A 2B0 26.142 21.809 42.087 1.0012.89 8 ATOH 2255 CA LEU A 274 29.590 15.550 38.849 1.00 10.16 6 ATOM 2308 N02 ASN A 280 25.289 22.094 44.111 1.0012.18 7 J AIOH 2256 CB LEU A 274 28.901 14.856 37.646 1.00 10.22 6 ATOM 2309 C ASN A 280 24.422 21.247 39.927 1.0010.94 6 AIOH 2257 CG LEU A 274 29.158 15.528 36.280 1.00 10.91 6 ATOH 2310 0 ASN A 280 23.910 22.353 39.820 1.0011.03 8 Z AIOH 2258 CD1 LEU A 274 28.719 14.634 35.107 1.00 11.67 6 ATOH 2311 N GLN A 281 25.325 20.890 39.032 1.0010.60 7 I AIOH 2259 CD2 LEU A 274 28.432 16.843 36.198 1.00 10.03 6 ATOH 2312 CA GLN A 281 25.784 21.736 37.949 1.0010.04 6 y j AIOH 2260 C LEU A 274 29.157 14.918 40.173 1.00 10.59 6 ATOH 2313 CB GLH A 281 26.930 22.636 38.400 1.00 9.98 6 ATOH 2261 0 LEU A 274 28.353 15.463 40.920 1.00 10.27 8 ATOM 2314 CG GIN A 281 28.117 21.977 39.038 1.00 9.72 6 ' ATOH 2262 N ASN A 275 29.706 13.730 40.471 1.00 11.45 7 ATOH 2315 CD GLN A 281 29.055 22.863 39.859 1.00 9.00 6 AIOH 2263 CA ASN A 275 29.463 13.009 41.709 1.00 12.37 6 ATOH 2316 OE1 GLH A 281 30.064 23.342 39.350 1.00 8.97 8 AIOH 2264 CB ASH A 275 30.287 11.694 41.835 1.00 19.11 6 ATOH 2317 NE2 GLN A 281 28.835 23.085 41.151 1.00 8.05 7 ATOH 2265 CG ASH A 275 29.761 10.565 40.962 1.00 24.07 6 ATOH 2318 C GLN A 2B1 26.239 20.871 36.771 1.00 9.46 6 AIOH 2266 ODl ASH A 275 28.743 9.915 41.314 1.00 27.53 8 AIOH 2319 0 GLN A 281 26.615 19.703 36.902 1.00 9.22 8 AIOH 2267 ND2 ASH A 275 30.352 10.254 39.805 1.00 25.40 7 ATOH 2320 N SER A 282 26.224 21.522 35.616 1.00 9.14 7 AIOH 2268 C ASH A 275 29.820 13.870 42.924 1.00 12.34 6 ATOM 2321 CA SER A 282 26.674 20.851 34.389 1.00 8.74 6 AIOH 2269 0 ASN A 275 28.964 14.072 43.761 1.00 12.19 8 ATOM 2322 CB SER A 282 25.985 21.419 33.131 1.00 7.22 6 ATOH 2270 N LYS A 276 31.008 14.435 43.005 1.00 12.51 7 ATOM 2323 OG SER A 282 24.607 21.123 33.102 1.00 6.53 8 AIOH 2271 CA LYS A 276 31.461 15.251 44.130 1.00 12.99 6 ATOH 2324 C SER A 282 28.170 21.077 34.201 1.00 8.54 6 AIOH 2272 CB LYS A 276 32.952 15.605 44.000 1.00 12.82 6 ATOH 2325 0 SER A 282 28.773 21.913 34.919 1.00 8.89 8 AIOH 2273 CG LYS A 276 33.825 14.346 44.050 1.00 13.95 6 ATOM 2326 N VAL A 283 28.777 20.420 33.240 1.00 8.11 7 AIOH 2274 CO LYS A 276 33.535 13.485 45.269 1.00 14.29 6 ATOH 2327 CA VAL A 283 30.154 20.596 32.841 1.00 7.98 6 AIOH 2275 CE LYS A 276 34.141 12.103 45.203 1.00 13.18 6 ATOM 2328 CB VAL A 283 31.137 19.443 33.210 1.00 8.54 6 AIOH 2276 HZ LYS A 276 35.602 12.070 44.906 1.00 13.50 7 ATOM 2329 CGI VAL A 283 31.457 19.441 34.708 1.00 9.20 6 AI O H 2277 C LYS A 276 30.651 16.533 44.311 1.00 13.24 6 ATOH 2330 CG2 VAL A 283 30.599 18.117 32.719 1.00 30.650 17.117 45.412 7.85 6 78 0 LYS A 276 1.00 13 7 3 ATOM 2439 OG SER A 297 42.921 18.303 13.176 1.00 20.24 8 ATOH 2492 CA ARG A 305 AIOH 2440 C SER A 297 42.921 16.146 10.50B 1.00 15.90 6 ATOH 2493 CB ARG A 305 AIOH 2441 0 SER A 297 44.076 16.216 10.160 1.00 15.87 8 ATOH 2494 CG ARG A 305 AIOH 2442 N GLN A 298 42.143 15.074 10.370 1.00 16.33 7 ATOH 2495 CD ARG A 305 AIOH 2443 CA GLN A 298 42.650 13.888 9.722 1.00 16.82 6 ATOH 2496 NE ARG A 305 AIOH 2444 CB GLN A 298 42.156 12.653 10.523 1.00 18.92 6 ATOH 2497 CZ ARG A 305 AIOH 2445 CG GLN A 298 43.084 12.447 11.693 1.0020.51 6 ATOH 2498 NHl ARG A 305 AIOH 2446 CO GLN A 298 42.613 11.548 12.798 1.0023.02 6 ATOM 2499 NH2 ARG A 305 ATOH 2447 0E1 GLN A 298 42.174 10.410 12.588 1.0024.09 8 ATOM 2500 C ARG A 305 AIOH 2448 NE2 GLN A 298 42.715 12.077 14.034 1.0023.74 7 ATOH 2501 0 ARG A 305 AIOH 2449 C GLN A 298 42.319 13.823 8.245 1.00 17.02 6 ATOH 2502 N LYS A 306 ATOH 2450 0 GLN A 298 42.486 12.719 7.679 1.00 17.29 8 ATOM 2503 CA LYS A 306 AIOH 2451 N GLY A 299 41.907 14.913 7.631 1.00 16.90 7 ATOM 2504 CB LYS A 306 ♦ OH 2452 CA GLY A 299 41.595 15.001 6.223 1.00 16.90 6 ATOH 2505 CG LYS A 306 - OH 2453 C GLY A 299 40.763 13.864 5.685 1.00 16.77 6 ATOH 2506 CD LYS A 306 AIOH 2454 0 GLY A 299 40.942 13.480 4.523 1.00 17.33 8 ATOH 2507 CE LYS A 306 Λ JIOH 2455 N GLY A 300 39.B55 13.274 6.435 1.00 16.11 7 ATOH 2508 NZ LYS A 306 c ATOH 2456 CA GLY A 300 39.068 12.163 5.983 1.00 15.25 6 ATOH 2509 C LYS A 306 00 AIOH 2457 C GLY A 300 39.483 10.868 6.650 1.00 14.82 6 ATOM 2510 0 LYS A 306 IΛ H ATOH 2458 0 GLY A 300 38.603 10.027 6.489 1.00 14.53 8 ATOM 2511 N LEU A 307 ATOH 2459 N GLY A 301 40.574 10.532 7.302 1.00 14.47 7 ATOH 2512 CA LEU A 307 ATOM 2460 CA GLY A 301 40.815 9.227 7.B60 1.00 14.37 6 ATOH 2513 CB LEU A 307 AIOH 2461 C GLY A 301 40.234 8.948 9.225 1.00 14.36 6 ATOH 2514 CG LEU A 307 AloH 2462 0 GLY A 301 40.318 7.830 9.696 1.00 14.17 8 ATOM 2515 C01 LEU A 307 AIOH 2463 N 1YR A 302 39.559 9.888 9.908 1.00 14.62 7 ATOH 2516 CD2 LEU A 307 IΛ X AIOH 2464 CA TYR A 302 38.973 9.650 11.220 1.00 14.57 6 ATOH 2517 C LEU A 307 ATOH 2465 CB TYR A 302 38.419 10.956 11.845 1.00 14.59 6 ATOH 2518 0 LEU A 307 AIOH 2466 CG TYR A 302 37.750 10.869 13.198 1.00 14.61 6 ATOH 2519 N LEU A 308 AIOH 2467 CD1 TYR A 302 38.559 10.860 14.355 1.00 14.96 6 ATOH 2520 CA LEU A 308 AIOH 2468 CE1 TYR A 302 37.990 10.754 15.630 1.00 14.98 6 ATOH 2521 CB LEU A 308 30 AIOH 2469 CD2 TYR A 302 36.380 10.751 13.400 1.00 14.40 6 c ATOH 2S22 CG LEU A 308 AIOH 2470 CE2 TYR A 302 35.820 10.629 14.663 1.00 14.56 6 ATOH 2523 CDl LEU A 308 AIOH 2471 CZ TYR A 302 36.622 10.655 15.778 1.00 14.83 6 ATOM 2524 CD2 LEU A 308 AIOH 2472 OH TYR A 302 36.157 10.564 17.049 1.00 15.01 8 ATOM 2525 C LEU A 308 σ. ATOH 2473 C TYR A 302 37.831 8.643 11.151 1.00 14.74 6 ATOM 2526 0 LEU A 308 AIOH 2474 0 TYR A 302 37.073 B.682 10.170 1.00 14.62 8 ATOH 2527 N ASN A 309 AK'H 2475 N ASP A 303 37.515 7.744 12.058 1.00 14.71 7 ATOH 2528 CA ASN A 309 ATOH 2476 CA ASP A 303 36.350 6.B73 11.910 1.00 14.90 6 ATOH 2529 CB ASN A 309 AIOH 2477 CB ASP A 303 36.617 5.550 12.620 1.00 16.31 6 ATOH 2530 CG ASN A 309 AK'H 2478 CG ASP A 303 35.526 4.517 12.403 1.00 17.88 6 ATOH 2531 001 ASN A 309 AIOH 2479 001 ASP A 303 34.383 4.796 12.005 1.00 17.07 8 ATOM 2532 ND2 ASN A 309 AIOH 2480 OD2 ASP A 303 35.893 3.348 12.637 1.00 19.55 8 ATOH 2533 C ASN A 309 AIOH 2481 C ASP A 303 35.165 7.627 12.500 1.00 14.85 6 ATOM 2534 0 ASN A 309 AIOH 2482 0 ASP A 303 35.013 7.729 13.714 1.00 14.59 8 ATOH 2535 N GLY A 310 AIOH 24B3 N MET A 304 34.315 8.199 11.658 1.00 14.94 7 ATOH 2536 CA GLY A 310 AIOH 2484 CA MET A 304 33.151 8.973 12.057 1.00 15.29 6 ATOH 2537 C GLY A 310 AIOH 2485 CB HET A 304 32.440 9.630 10.862 1.00 14.35 6 ATOH 2538 0 GLY A 310 AIOH 2486 CG HET A 304 33.307 10.718 10.201 1.00 13.91 6 ATOH 2539 N THR A 311 AIOH 2487 SD MET A 304 33.391 12.309 11.028 1.00 14.76 16 ATOH 2540 CA THR A 311 AloH 2488 CE HET A 304 31.941 13.156 10.378 1.00 11.94 6 ATOH 2541 CB THR A 311 AIOH 2489 C MET A 304 32.161 8.195 12.917 1.00 15.60 6 ATOH 2542 OG1 THR A 311 AIOH 2490 0 HET A 304 31.322 8.846 13.549 1.00 15.54 8 ATOH 2543 CG2 THR A 311 AloH 2491 M ARG A 305 32.251 6.872 13.019 1.00 15.77 7 ATOH 2544 C THR A 311 Λ Λ J Λ 0 - . ATOH 2651 001 ASP A 325 38.076 25.409 18.839 1.00 7.66 8 AIOH 2652 002 ASP A 325 37.027 25.682 16.964 1.00 9.34 8 ATOH 2653 C ASP A 325 35.117 27.261 21.116 1.00 8.18 6 ATOH 2654 0 ASP A 325 33.960 27.635 21.254 1.00 B.16 B AIOH 2655 N ASN A 326 36.108 27.788 21.826 1.00 8.35 7 AIOH 2656 CA ASN A 326 35.925 28.845 22.813 1.00 8.28 6 ATOH 2657 CB ASN A 326 35.487 28.329 24.160 1.00 9.54 6 ATOH 2658 CG ASN A 326 36.502 27.485 24.902 1.0011.91 6 AIOH 2659 001 ASN A 326 37.701 27.415 24.622 1.0012.52 B AIOH 2660 ND2 ASN A 326 36.121 26.782 25.965 1.0011.95 7 AIOH 2661 C ASN A 326 37.212 29.685 22.B71 1.00 8.44 6 AI'JH 2662 0 ASN A 326 3B.140 29.601 22.053 1.00 7.98 8 AIOH 2663 N HIS A 327 37.266 30.626 23.836 1.00 8.65 7 AIOH 2664 CA HIS A 327 38.367 31.562 23.994 1.00 9.17 6 AIOH 2665 CB HIS A 327 37.976 32.718 24.999 1.00 8.48 6 AIOH 2666 CG HIS A 327 37.800 32.154 26.392 1.00 7.81 6 IΛ *!0H 2667 CD2 HIS A 327 38.481 32.357 27.535 1.00 7.34 6 C AIOH 2668 ND1 HIS A 327 36.785 31.222 26.672 1.00 8.46 7 a AIOH 2669 CE1 HIS A 327 36.8B6 30.856 27.951 1.00 7.98 6 J3 AIOH 2670 NE2 HIS A 327 37.883 31.S38 28.493 1.00 8.30 7 Zj ATOH 2671 C HIS A 327 39.664 30.866 24.404 1.00 9.58 6 "3 AIOH 2672 0 HIS A 327 40.718 31.444 24.169 1.00 9.63 8 ~~ AIOH 2673 N ASP A 328 39.645 29.653 24.928 1.0010.01 7 m AIOH 2674 CA ASP A 328 40.783 28.869 25.312 1.0010.53 6 AIOH 2675 CB ASP A 328 40.422 27.735 26.312 1.0014.56 6 IΛ AIOH 2676 CG ASP A 328 39.676 27.936 27.629 1.0018.50 6 ±1 AIOH 2677 001 ASP A 328 40.162 28.843 28.385 1.0017.22 8 m AIOH 2678 002 ASP A 328 38.615 27.265 28.055 1.0018.97 8 H AIOH 2679 C ASP A 328 41.3B5 28.188 24.074 1.0010.65 6 ψ- • * AIOH 2680 0 ASP A 328 42.607 28.041 23.933 1.0010.58 8 ~~ AIOH 2681 H THR A 329 40.518 27.688 23.167 1.0010.47 7 C AIOH 26B2 CA THR A 329 40.946 26.880 22.028 1.0010.37 6 ~Z ATOH 2683 CB THR A 329 39.933 25.709 21.777 1.0010.26 6 m AIOH 2684 0G1 IHR A 329 38.709 26.293 21.286 1.00 9.63 8 gj AIOH 2685 CG2 THR A 329 39.596 24.873 23.020 1.00 9.29 6 AIOH 2686 C THR A 329 41.142 27.596 20.702 1.0010.36 6 AIOH 2687 0 THR A 329 41.563 26.999 19.704 1.00 9.94 8 AloH 2688 H GLN A 330 40.827 28.878 20.679 1.0010.77 7 AIOH 2689 CA GLH A 330 40.985 29.688 19.441 1.0011.30 6 AIOH 2690 CB GLH A 330 40.182 30.988 19.518 1.00 9.13 6 AIOH 2691 CG GLH A 330 40.749 31.987 20.543 1.00 8.40 6 AIOH 2692 CO GLH A 330 40.003 33.322 20.559 1.00 8.44 6 AIOH 2693 OE1 GLH A 330 39.089 33.499 21.393 1.00 7.21 8 ATOH 2694 NE2 GLN A 330 40.432 34.237 19.660 1.00 7.16 7 AIOH 2695 C GLN A 330 42.486 29.890 19.211 1.0011.99 6 ATOH 2696 0 GLH A 330 43.345 29.690 20.092 1.0011.70 8 AloH 2697 H PRO A 331 42.793 30.208 17.963 1.0012.80 7 AIOH 2698 CD PRO A 331 41.806 30.403 16.B73 1.0012.95 6 Aim. 2699 CA PRO A 331 44.119 30.424 17.447 1.0013.52 6 AIOH 2700 CB PRO A 331 43.974 30.918 15.966 1.00 13.53 6 AIOH 2701 CG PRO A 331 42.608 30.336 15.583 1.0013.10 6 36.745 21.811 16.483 1.00 9.86 6 ATOM 2810 N PRO A 345 30.989 23.886 10.213 1.00 9.37 7 38.513 23.484 13.385 1.0012.57 6 ATOM 2811 CO PRO A 345 31.697 24.236 8.991 1.00 9.33 6 3B.271 24.688 13.279 1.0012.26 8 ATOM 2812 CA PRO A 345 29.559 23.779 10.018 1.00 9.01 6 39.016 22.686 12.404 1.0012.55 7 ATOH 2813 CB PRO A 345 29.285 24.245 β.592 1.00 9.17 6 39.280 23.302 11.088 1.0012.55 6 ATOH 2814 CG PRO A 345 30.576 25.000 8.288 9.42 6 39.975 22.357 10.097 1.0011.11 6 ATOH 2815 C PRO A 345 29.077 22.331 10.309 8.68 6 41.372 21.974 10.559 1.0011.55 6 ATOH 2816 0 PRO A 345 27.992 22.162 10.862 8.28 8 42.073 21.105 9.513 1.0014.34 6 ATOH 2817 N LEU A 346 29.863 21.274 9.998 1.00 B.29 7 41.594 20.802 8.384 1.0015.11 8 ATOH 2818 CA LEU A 346 29.491 19.890 10.274 1.00 7.82 6 AIOH 2766 NE2 GLN A 340 43.272 20.743 9.959 1.0012.61 7 ATOH 2819 CB LEU A 346 30.443 18.876 9.664 1.00 71 6 AIOH 2767 C GLN A 340 38.009 23.900 10.468 1.0012.34 6 ATOH 2820 CG LEU A 346 30.608 18.730 β.147 1.00 48 6 AIOH 2768 0 GLN A 340 36.930 23.331 10.565 1.0012.28 8 ATOH 2821 CD1 LEU A 346 30.910 20.053 7.472 1.00 38 6 ATOH 2769 N THR A 341 38.147 25.042 9.779 1.0012.25 7 ATOH 2822 CD2 LEU A 346 31.710 17.710 7.794 1.00 58 6 AT )H 2770 CA IHR A 341 37.024 25.755 9.200 1.0012.38 6 ATOH 2823 C LEU A 346 29.426 19.714 11.796 1.00 55 6 A! x. 2771 CB THR A 341 37.514 26.993 B.393 1.0015.06 6 ATOH 2824 0 LEU A 346 28.510 19.084 12.262 100 43 B Al Η 2772 OG1 THR A 341 38.100 27.874 9.353 1.0016.92 8 ATOH 2825 N ALA A 347 30.320 20.297 12.583 1 00 30 7 il H 2773 CG2 IHR A 341 36.347 27.684 7.716 1.0014.77 6 ATOH 2826 CA ALA A 347 30.42S 20.274 14.019 100 11 6 ; AIOH 2774 C THR A 341 36.124 24.916 8.332 1.0012.08 6 ATOH 2827 CB ALA A 347 31.740 20.902 14.501 100 21 6 j ATOM 2775 0 THR A 341 34.910 25.018 8.411 1.0012.16 B ATOM 2828 C ALA A 347 29.264 21.031 14.671 1.00 06 6 j ATOH 2776 N TRP A 342 36.698 24.095 7.465 1.0011.85 7 ATOM 2829 0 ALA A 347 28.712 20.558 15.670 1.00 7.03 8 AIOH 2777 CA IRP A 342 35.902 23.225 6.585 1.0011.19 6 ATOH 2830 N TYR A 348 28.827 22.160 14.103 1.00 7.17 7 AIOH 2778 CB TRP A 342 36.871 22.438 5.673 1.0010.89 6 ATOH 2831 CA TYR A 348 27.673 22.854 14.693 1.00 7.17 6 AIOH 2779 CG TRP A 342 37.568 21.288 6.392 1.00 9.86 6 ATOH 2832 CB TYR A 348 27.650 24.299 14.175 1.00 7.45 6 AIOH 2780 CD2 TRP A 342 37.073 19.949 6.491 1.00 9.37 6 ATOH 2833 CG TYR A 348 28.510 25.236 15.008 1.00 7.77 6 AIOH 2781 CE2 TRP A 342 37.98B 19.219 7.276 1.00 9.97 6 ATOH 2834 CD1 TYR A 348 29.718 25.772 14.609 1.00 7.85 6 AIOH 2782 CE3 TRP A 342 35.916 19.290 5.991 1.0010.12 6 ATOH 2835 CE1 TYR 348 30.416 26.670 15.415 00 7.87 6 AIOH 2783 CD1 TRP A 342 3B.756 21.330 7.062 1.0010.06 6 ATOH 2836 CD2 TYR 34B 28.035 25.569 16.285 00 7.82 6 ATOH 2784 NE1 TRP A 342 39.027 20.080 7.592 1.0011.11 7 ATOH 2837 CE2 TYR 348 28.731 26.430 17.105 00 7.89 6 AIOH 2785 CZ2 IRP A 342 37.809 17.853 7.527 1.0010.50 6 ATOH 2838 CZ TYR 348 29.917 26.984 16.682 .00 7.94 6 ϊ ATOH 2786 C23 TRP A 342 35.700 17.950 6.293 1.00 9.23 6 ATOM 2839 OH TYR 348 30.609 27.789 17.576 1.00 7.87 8 . AIOH 2787 CH2 IRP A 342 36.654 17.222 7.050 1.0010.34 6 ATOH 2840 C TYR 348 26.404 22.081 14.387 .00 7.12 6 ATOH 2788 C IRP A 342 34.968 22.340 7.391 1.0010.76 6 ATOH 2841 0 TYR 348 25.461 22.029 IS.193 .00 7.05 8 AIOH 2789 0 TRP A 342 33.837 22.038 6.990 1.0010.60 8 ATOH 2842 N ALA 349 26.328 21.385 13.223 .00 6.87 7 AIOH 2790 N PHE A 343 35.375 21.846 8.577 1.0010.45 7 ATOH 2843 CA ALA 349 25.127 20.607 12.939 .00 6.67 6 AIOH 2791 CA PHE A 343 34.544 20.979 9.389 1.00 9.81 6 ATOH 2844 CB ALA 349 25.131 20.070 11.515 .00 6.51 6 * AIOH 2792 CB PHE A 343 35.520 20.08B 10.193 1.0010.59 6 ATOH 2845 C ALA 349 25.054 19.497 13.978 .00 6.62 6 ATOH 2793 CG PHE A 343 34.841 18.880 10.796 1.00 9.94 6 ATOH 2846 0 ALA 349 23.995 19.114 14.487 1.00 6.43 8 AIOH 2794 CD1 PHE A 343 34.561 17.786 9.989 1.00 9.97 6 ATOH 2847 N PHE 350 26.237 18.899 14.250 1.00 6.67 7 AIOH 2795 CD2 PHE A 343 34.466 18.875 12.117 1.00 9.30 6 ATOH 2848 CA PHE 350 26.268 17.814 15.220 1.00 6.81 6 ATOH 2796 CE1 PHE A 343 33.947 16.653 10.504 1.00 9.66 6 ATOH 2849 CB PHE 350 27.701 17.250 15.304 1.00 6.91 6 AIOH 2797 CE2 PHE A 343 33.842 17.747 12.659 1.0010.16 6 ATOH 2850 CG PHE 350 27.746 15.996 16.137 1.00 9.15 6 AIOH 2798 CZ PHE A 343 33.592 16.637 11.845 1.0010.55 6 ATOH 2851 CD1 PHE 350 27.494 14.763 15.559 1.00 8.95 6 AIOH 2799 C PHE A 343 33.621 21.720 10.332 1.00 9.65 6 ATOH 2852 CD2 PHE 3S0 28.009 16.069 17.510 1.0011.23 6 ATOH 2800 0 PHE A 343 32.649 21.140 10.826 1.00 9.50 β ATOM 2853 CE1 PHE 350 27.551 13.618 16.317 1.0010.89 6 AIOH 2801 N LYS A 344 33.897 23.010 10.569 1.00 9.52 7 ATOH 2854 CE2 PHE 350 28.044 14.894 18.273 1.0011.66 6 ATOH 2802 CA LYS A 344 33.084 23.775 11.536 1.00 9.73 6 ATOH 2855 CZ PHE 350 27.847 13.657 17.687 1.0010.74 6 AIOH 2803 CB LYS A 344 33.689 25.209 11.614 1.0011.03 6 ATOH 2856 C PHE 350 25.768 18.242 16.605 1.00 6.90 6 ATOH 2804 CG LYS A 344 33.193 25.978 12.846 1.0011.47 6 ATOH 2857 0 PHE 350 24.978 17.547 CD LYS A 344 17.275 1.00 6.86 34.235 26.954 13.366 1.0010.60 6 8 ATOH 2805 ATOH 285B N ILE 351 26.217 19.408 17.102 1.00 7.14 8 26.281 14.470 1.00 9.19 6 7 AIOH 2806 CE LYS A 344 35.06 ATOH 2859 CA ILE 351 25.736 19.797 ATOH 2807 NZ LYS A 344 36.09B 27.262 14.962 1.00 7.52 7 18.437 1.00 7.28 6 ATOH 2860 CB ILE 351 26.767 20.663 0 6.43 6 ATOH 2808 C LYS A 344 31.573 23.696 11.384 1.00 9.62 6 19.194 1.0 ATOH 2861 CG2 ILE 351 28.084 44 19.924 ATOH 2809 0 LYS A 3 30.838 23.428 12.371 1.00 9.63 8 19.275 1.00 6.52 6 ATOH 2862 CGI ILE 351 26.943 22.024 18.556 1.00 6.43 6 ATOH 2863 CD1 ILE A 351 ATOH 2916 CE1 TYR A 358 21.449 26.080 26.747 1.00 9.42 6 AIOH 2864 C HE A 351 ATOH 2917 CD2 TYR A 358 AIOH 2865 0 HE A 351 ATOH 2918 CE2 TYR A 358 AIOH 2866 N LEU A 352 ATOM 2919 CZ TYR A 358 AIOH 2867 CA LEU A 352 ATOH 2920 OH TYR A 358 AIOH 2868 CB LEU A 352 ATOH 2921 C TYR A 358 AIOH 2869 CG LEU A 352 ATOH 2922 0 TYR A 358 AIOH 2870 CD1 LEU A 352 ATOH 2923 N PRO A 359 AIOH 2871 CD2 LEU A 352 ATOH 2924 CD PRO A 359 AIOH 2B72 C LEU A 352 ATOH 292S CA PRO A 359 AIOH 2873 O LEU A 352 ATOM 2926 CB PRO A 359 AIOH 2874 N THR A 353 ATOH 2927 CG PRO A 359 AIOH 2875 CA THR A 353 ATOH 292B C PRO A 359 AIOH 2876 CB THR A 353 ATOH 2929 0 PRO A 359 I _H 2877 OG1 THR A 353 ATOH 2930 N GLN A 360 AIOH 2878 CG2 THR A 353 ATOH 2931 CA GLN A 360 »!3H 2879 C THR A 353 ATOH 2932 CB GLN A 360 *10H 2880 0 THR A 353 ATOH 2933 CG GLN A 360 AIOH 2881 N ARG A 354 ATOM 2934 CD GLN A 360 0 l ATOH 2882 CA ARG A 354 ATOH 2935 OE1 GLN A 360 AIOH 2883 CB ARG A 354 ATOH 2936 NE2 GLN A 360 ATOH 2884 CG ARG A 354 ATOH 2937 C GLN A 360 ATOH 2885 CD ARG A 354 ATOM 2938 0 GLN A 360 AIOH 2886 NE ARG A 354 ATOM 2939 N VAL A 361 AIOH 2887 CZ ARG A 354 ATOM 2940 CA VAL A 361 Λ AIOH 2888 NH1 ARG A 354 ATOH 2941 CB VAL A 361 AK'H 2889 NH2 ARG A 354 ATOM 2942 CGI VAL A 361 AIOH 2890 C ARG A 354 ATOH 2943 CG2 VAL A 361 AIOH 2891 0 ARG A 354 ATOH 2944 C VAL A 361 AIOH 2892 N GLU A 355 ATOH 2945 0 VAL A 361 jo ATOH 2893 CA GLU A 355 ATOH 2946 N PHE A 362 C ATOH 2894 CB GLU A 355 ATOM 2947 CA PHE A 362 ATOH 2895 CG GLU A 355 ATOM 2948 CB PHE A 362 AIOH 2B96 CD GLU A 355 ATOM 2949 CG PHE A 362 AIOH 2897 OE1 GLU A 355 ATOM 2950 C01 PHE A 362 AIOH 2898 OE2 GLU A 355 ATOM 2951 CD2 PHE A 362 AIOH 2899 C GLU A 355 ATOH 2952 CE1 PHE A 362 AIOH 2900 0 GLU A 355 ATOM 2953 CE2 PHE A 362 ATOH 2901 N SER A 356 ATOH 2954 CZ PHE A 362 ATOH 2902 CA SER A 356 ATOH 2955 C PHE A 362 ATOH 2903 CB SER A 356 ATOH 2956 0 PHE A 362 AIOH 2904 OG SER A 356 ATOH 2957 N TYR A 363 AIOH 2905 C SER A 356 ATOH 2958 CA TYR A 363 ATOH 2906 0 SER A 356 ATOM 2959 CB TYR A 363 AIOH 2907 N GLY A 357 ATOH 2960 CG TYR A 363 AIOH 290B CA GLY A 357 ATOH 2961 C01 TYR A 363 AIOH 2909 C GLY A 357 ATOM 2962 CE1 TYR A 363 AIOH 2910 0 GLY A 357 ATOM 2963 CD2 TYR A 363 ATOH 2911 N TYR A 358 ATOM 2964 CE2 TYR A 363 ATOM 2912 CA TYR A 358 ATOM 2965 CZ TYR A 363 ATOM 2913 CB TYR A 358 ATOH 2966 OH IYR A 363 AIOH 2914 CG TYR A 358 ATOH 2967 C TYR A 363 ATOH 3022 CA GLY A 371 43.889 37.991 16.742 1.00 22.15 6 ATOH 3023 C GLY A 371 44.817 38.443 15.581 1.00 23.36 6 ATOH 3024 0 GLY A 371 44.393 38.896 14.521 1.00 23.05 8 ATOH 3025 N ASP A 372 46.095 38.223 15.B77 1.00 24.83 7 ATOH 3026 CA ASP A 372 47.186 38.626 15.016 1.00 26.55 6 ATOH 3027 CB ASP A 372 48.323 39.306 15.B74 1.00 31.39 6 ATOH 3028 CG ASP A 372 47.962 40.791 15.968 1.00 34.93 6 ATOH 3029 001 ASP A 372 47.609 41.363 14.906 1.00 37.36 8 ATOH 3030 002 ASP 372 47.972 41.443 17.034 1.00 37.47 8 ATOH 3031 C ASP 372 47.796 37.520 14.189 1.00 27.31 6 ATOH 3032 0 ASP 372 48.870 37.818 13.613 1.00 27.65 8 ATOH 3033 N SER 373 47.162 36.353 14.146 1.00 27.64 7 ATOH 3034 CA SER 373 47.800 35.318 13.305 1.00 27.95 6 ATOH 3035 CB SER 373 47.678 33.936 13.932 1.00 26.91 6 ATOH 3036 OG SER 373 46.393 33.416 13.642 1.00 28.21 8 ATOH 3037 C SER 373 47.255 35.373 11.873 1.00 28.20 6 ATOM 3038 0 SER 373 46.480 36.189 11.366 1.00 28.10 8 ATOH 3039 N GLN 374 47.780 34.393 11.137 1.00 2B.61 7 ATOH 3040 CA GLN 374 47.348 34.201 9.729 1.00 28.86 6 ATOH 3041 CB GLN 374 48.525 34.112 8.767 1.00 34.24 6 ATOH 3042 CG GLN 374 49.400 35.309 8.530 1.00 40.44 6 ATOH 3043 CD GLN A 374 48.939 36.714 8.874 1.00 45.21 6 ATOH 3044 OE1 GLN A 374 48.111 37.342 8.149 1.00 47.86 8 ATOH 3045 NE2 GLN A 374 49.449 37.277 10.005 1.00 45.97 7 ATOH 3046 C GLN A 374 46.414 32.963 9.719 1.00 28.21 6 ATOH 3047 0 GLN A 374 46.105 32.340 8.674 1.00 28.76 8 ATOH 3048 N ARG A 375 45.952 32.517 10.873 1.00 26.96 7 ATOH 3049 CA ARG A 375 45.066 31.421 11.109 1.00 25.60 6 ATOH 3050 CB ARG A 375 45.641 30.394 12.115 1.00 29.84 6 ATOH 3051 CG ARG A 375 46.842 29.713 11.509 1.00 33.75 6 ATOH 3052 CD ARG A 375 48.088 30.386 12.067 1.00 36.33 6 ATOH 3053 NE ARG A 375 48.286 30.141 13.475 1.00 37.64 7 ATOH 3054 CZ ARG A 375 47.856 29.261 14.351 1.00 37.09 6 ATOM 3055 NH1 ARG A 375 47.016 28.308 13.998 1.00 37.77 7 ATOH 3056 NH2 ARG A 375 48.293 29.399 15.587 1.00 36.83 7 ATOM 3057 C ARG A 375 43.777 31.845 11.827 1.00 23.88 6 ATOH 3058 o ARG 375 43.218 30.942 12.450 1.00 23.81 8 ATOH 3059 H GLU 376 43.399 33.116 11.777 1.00 22.28 7 ATOH 3060 CA GLU A 376 42.196 33.558 12.450 1.00 20.37 6 ATOH 3061 CB GLU A 376 42.061 35.080 12.418 1.00 17.56 6 ATOM 3062 CG GLU A 376 43.203 3S.780 13.151 1.00 16.13 6 ATOH 3063 CO GLU A 376 43.361 35.421 14.595 1.00 14.90 6 ATOH 3064 OE1 GLU A 376 42.403 35.436 15.391 1.00 12.95 8 ATOM 3065 OE2 GLU A 376 44.510 35.188 15.051 1.00 16.10 8 ATOH 3066 C GLU A 376 40.955 32.886 11.869 1.00 19.17 6 ATOH 3067 0 GLU A 376 40.801 32.503 10.715 1.00 18.94 8 ATOH 3068 N ILE A 40.002 32.698 12.777 1.00 18.23 7 ATOH 3069 CA ILE A 38.726 32.102 12.410 1.00 17.23 6 ATOH 3070 CB ILE A 37.924 31.634 13.636 1.00 15.28 6 ATOH 3071 CG2 ILE A 36.616 30.961 13.205 1.00 15.23 6 ATOH 3072 CGI ILE A 38.720 30.715 14.564 1.00 14.23 6 ATOH 3073 CD1 ILE A 38.109 30.512 15.935 1.00 13.53 6 ATOH 3074 ILE A 37.957 33.184 11.660 1.00 16.78 6 ATOH 3075 0 ILE A 377 37.783 34.301 12.173 1.0016.90 8 ATOH 3128 CGI ILE A 384 28.029 28.790 12.411 1.00 13.70 6 AIOH 3076 H PRO A 378 37.461 32.927 10.461 1.0016.21 7 ATOH 3129 CD1 ILE A 384 28.902 29.649 13.343 1.00 15.12 6 ATOH 3077 CO PRO A 378 37.634 31.617 9.821 1.0016.04 6 ATOH 3130 C ILE A 384 24.335 29.241 11.430 1.00 12.61 6 ATOH 3U78 CA PRO A 37B 36.637 33.810 9.695 1.0015.87 6 ATOH 3131 0 ILE A 384 23.621 28.363 11.931 1.00 12.68 8 AIOH 3079 CB PRO A 378 36.555 33.232 8.263 1.0015.98 6 ATOM 3132 N GLU A 385 23.841 30.401 11.025 1.00 12.22 7 ATOH 3080 CG PRO A 378 37.023 31.835 8.456 1.0015.94 6 ATOM 3133 CA GLU A 385 22.459 30.804 11.178 1.00 12.09 6 AIOH 3081 C PRO A 378 35.214 33.860 10.247 1.0015.56 6 ATOM 3134 CB GLU A 385 22.249 32.252 10.671 1.00 13.25 6 AIOH 3082 O PRO A 378 34.741 32.94S 10.946 1.0015.55 8 ATOH 3135 CG GLU A 385 23.039 33.148 11.637 1.00 16.06 6 AIOH 3083 N ALA A 379 34.506 34.960 9.931 1.0015.19 7 ATOH 3136 CD GLU A 385 22.681 34.621 11.531 1.00 18.04 6 ATOH 3084 CA ALA A 379 33.095 35.063 10.370 1.0014.83 6 ATOH 3137 OE1 GLU A 385 22.082 35.050 10.531 1.00 18.27 8 AIOH 3085 CB ALA A 379 32.523 36.450 10.119 1.0013.37 6 ATOH 3138 OE2 GLU A 385 22.960 35.427 12.453 1.00 18.60 8 AKH 3086 C ALA A 379 32.246 33.979 9.679 1.0014.60 6 ATOM 3139 C GLU A 385 21.439 29.867 10.587 1.00 11.96 6 AKH 3087 0 ALA A 379 32.082 33.990 B.438 1.0014.6S 8 ATOM 3140 0 GLU A 385 20.439 29.608 11.273 1.00 12.04 8 Al ' H 3088 N LEU A 380 31.703 33.021 10.428 1.0014.2B 7 ATOM 3141 N PRO A 386 21.614 29.238 9.436 1.00 11.74 7 lΗ 3089 CA LEU A 3B0 30.925 31.960 9.792 1.0014.14 6 ATOH 3142 CD PRO A 386 22.735 29.467 8.528 1.00 11.74 6 AT *. 3090 CB LEU A 380 31.468 30.617 10.265 1.0015.00 6 ATOH 3143 CA PRO A 386 20.676 28.265 B.905 1.00 11.52 6 %/_ ll'iH 3091 CG LEU A 380 32.913 30.303 9.865 1.0016.56 6 ATOH 3144 CB PRO A 386 21.205 27.847 7.516 1.00 11.54 6 C '.OH 3092 CD1 LEU A 380 33.486 29.165 10.688 1.0016.26 6 ATOH 3145 CG PRO A 386 22.167 28.967 7.199 1.00 11.74 6 00 AIOH 3093 CD2 LEU A 380 32.975 30.004 8.350 1.0016.68 6 ATOH 3146 C PRO A 386 20.545 27.050 9.826 1.00 11.28 6 t ATOH 3094 C LEU A 380 29.448 32.123 10.017 1.0014.34 6 ATOH 3147 0 PRO A 386 19.493 26.419 9.963 1.00 11.21 8 __ AIOH 3095 0 LEU A 380 28.602 31.262 9.773 1.0014.38 8 ATOH 3148 N ILE 387 21.617 26.648 10.530 1.00 11 .05 7 H AIOH 3096 N LYS A 381 29.011 33.278 10.475 1.0014.36 7 ATOH 3149 CA ILE 387 21.619 25.492 11.424 1.00 10.84 6 C AIOH 3097 CA LYS A 381 27.615 33.579 10.719 1.0014.84 6 ATOH 3150 CB ILE 387 23.047 24.957 11.653 1.00 8.79 6 H AIOH 3098 CB LYS A 381 27.672 35.101 10.820 1.0018.02 6 ATOH 3151 CG2 ILE A 387 22.978 23.619 12.340 1.00 6.90 6 m ATOH 3099 CG LYS A 381 26.382 35.855 10.702 1.0021.47 6 ATOH 3152 CGI ILE A 387 23.799 24.850 10.310 1.00 8.27 6 *Λ ATOH 3100 CD LYS A 381 26.754 37.314 10.944 1.0025.20 6 ATOH 3153 CD1 ILE 387 25.231 24.430 10.511 1 .00 9.3B 6 -~ AIOH 3101 CE LYS A 381 25.912 38.275 10.104 1.0028.81 6 ATOH 3154 C ILE 387 20.917 25.808 12.754 1.00 11.01 6 JJJ AIOH 3102 NZ LYS A 381 24.564 38.411 10.770 1.0030.73 7 ATOH 3155 0 ILE 387 20.273 24.946 13.366 1.00 10.92 8 ~_\ ATOH 3103 C LYS A 381 26.667 33.106 9.634 1.0014.98 6 ATOH 3156 N LEU A 388 21.058 27.064 13.176 1 .00 11.09 7 ,____ AIOH 3104 0 LYS A 381 25.589 32.577 9.911 1.0014.84 8 ATOH 3157 CA LEU A 388 20.400 27.620 14.345 1.00 11.19 6 73 ATOH 3105 N HIS A 382 26.978 33.273 8.350 1.0014.98 7 ATOH 315B CB LEU A 388 20.902 29.010 14.682 1.00 10.46 6 C ATOH 3106 CA HIS A 382 26.079 32.889 7.268 1.0015.22 6 ATOH 3159 CG LEU A 388 22.084 29.061 15.638 1.00 11 .84 6 r~ AIOH 3107 CB HIS A 382 26.562 33.593 5.986 1.0021.24 6 ATOM 3160 C01 LEU A 388 22.502 30.545 15.745 1.00 11.69 6 m ATOH 3108 CG HIS A 382 28.036 33.424 5.842 1.0025.72 6 ATOM 3161 CD2 LEU A 388 21.636 28.377 16.916 1.00 10.70 6 W AIOH 3109 C02 HIS A 382 29.070 33.878 6.615 1.0027.36 6 ATOM 3162 C LEU A 388 18.887 27.688 14.042 1.00 11.21 6 ■2 AIOH 3110 N01 HIS A 382 28.569 32.671 4.810 1.0028.03 7 ATOM 3163 0 LEU A 388 18.017 27.443 14.899 1.00 11 .36 β AIOH 3111 CE1 HIS A 382 29.903 32.712 4.939 1.0028.96 6 ATOH 3164 N LYS A 389 18.551 28.015 12.792 1.00 11.22 7 AIOH 3112 NE2 HIS A 382 30.216 33.424 6.041 1.0028.60 7 ATOH 3165 CA LYS A 389 17.142 28.017 12.353 1.00 11.08 6 AIOH 3113 C HIS A 382 25.947 31.415 7.118 1.0015.05 6 ATOH 3166 CB LYS A 389 17.014 28.553 10.952 1.00 14.65 6 AIOH 3114 0 HIS A 382 24.948 30.932 6.602 1.0015.08 8 ATOM 3167 CG LYS A 389 15.591 28.665 10.402 1.00 20.09 6 AIOH 3115 N LYS A 383 26.887 30.595 7.622 1.0014.81 7 ATOM 3168 CD LYS A 389 1S.4S4 30.134 9.985 1.00 24.33 6 AIOH 3116 CA LYS A 383 26.802 29.161 7.615 1.0014.36 6 ATOM 3169 CE LYS A 389 14.860 30.232 8.592 1.00 27.30 6 AIOH 3117 CB LYS A 383 28.186 28.551 7.528 1.0016.14 6 ATOH 3170 NZ LYS A 389 13.649 29.337 8.568 1.00 30.42 7 AIOH 3118 CG LYS A 383 29.014 29.281 6.505 1.0020.51 6 ATOH 3171 C LYS A 389 16.620 26.566 12.377 1.00 10.52 6 AIOH 3119 CD LYS A 383 29.147 28.507 5.230 1.0023.48 6 ATOH 3172 0 LYS A 389 15.474 26.300 12.746 1.00 10.45 8 ATOH 3120 CE LYS A 383 30.673 2B.350 4.977 1.0026.30 6 ATOH 3173 N ALA A 390 17.445 25.613 11.937 1.00 10.03 7 ATOH 3121 MZ LYS A 383 31.046 29.207 3.792 1.0027.91 7 ATOH 3174 CA ALA A 390 17.007 24.226 12.020 1.00 9.88 6 ATOH 3122 C LYS A 383 26.207 28.595 8.926 1.0013.88 6 ATOH 3175 CB ALA A 390 17.970 23.263 11.375 1.00 7.86 6 ATOH 3123 0 LYS A 383 25.694 27.478 8.956 1.0013.80 8 ATOH 3176 C ALA A 390 16.848 23.832 13.506 1.00 9.86 6 ATOH 3124 M ILE A 384 26.351 29.374 10.004 1.0013.23 7 ATOH 3177 0 ALA A 390 15.876 23.103 13.761 1.00 AIOH 3125 CA ILE A 384 25.B14 28.889 11.252 1.0012.99 6 9.92 8 ATOH 3178 N ARG A 391 17.713 24.258 14.440 1.00 A IOH 3126 CB ILE A 384 26.609 29.381 12.486 1.00 13.25 6 9.66 7 ATOH 3179 CA ARG A 391 17.540 23.914 15.857 1.00 9.64 6 ATOH 3181 CG ARG A 391 18.295 24.255 18.295 1.00 6.17 6 ATOH 3234 C TYR 396 11.624 16.631 17.499 1.0010.90 6 AIOH 3182 CO ARG A 391 19.637 24.301 19.079 1.00 6.11 6 ATOH 3235 0 TYR 396 11.615 16.137 16.372 1.0010.58 β AIOH 3183 HE ARG A 391 19.415 23.9B2 20.476 1.00 6.39 7 ATOH 3236 N GLY 397 11.252 15.899 18.555 1.00 11.07 7 AIOH 3184 CZ ARG A 391 19.411 22.752 21.057 1.00 8.41 6 ATOH 3237 CA GLY 397 10.772 14.542 18.296 1.0011.32 6 AIOH 3185 NH1 ARG A 391 19.671 21.719 20.264 1.00 7.01 7 ATOH 3238 C GLY 397 11.808 13.450 18.353 1.00 11.58 6 AloH 3186 NII2 ARG A 391 19.147 22.533 22.359 1.00 6.75 7 ATOH 3239 0 GLY 397 13.001 13.761 18.466 1.0012.00 8 AIOH 3187 C ARG A 391 16.258 24.S18 16.434 1.00 9.84 6 ATOH 3240 N ALA 398 11.341 12.228 18.304 1.0011.57 7 ' ATOM 3188 0 ARG A 391 15.482 23.860 17.089 1.00 9.35 8 ATOM 3241 CA ALA 398 12.172 11.044 18.341 1.00 11.80 6 AIOH 3189 N LYS A 392 16.061 25.B11 16.184 1.0010.42 7 ATOH 3242 CB ALA 398 11.261 9.824 18.105 1.00 9.85 6 ATOH 3190 CA LYS A 392 14.904 26.555 16.666 1.0011.31 6 ATOH 3243 C ALA 398 13.348 11.115 17.365 1.0012.04 6 AIOH 3191 CB LYS A 392 15.137 28.036 16.253 1.0013.27 6 ATOH 3244 0 ALA 398 13.259 11.447 16.176 1.00 12.09 8 AT M 3192 CG LYS A 392 14.066 28.928 16.797 1.0016.07 6 ATOH 3245 N GLN 399 14.532 10.718 17.833 1.0012.00 7 AIOH 3193 CD LYS A 392 14.176 30.388 16.369 1.0020.09 6 ATOH 3246 CA GLN 399 15.761 10.691 17.058 1.00 12.04 6 IOH 3194 CE LYS A 392 12.806 31.069 16.665 1.0023.10 6 ATOH 3247 CB GLN 399 16.871 11.357 17.912 1.00 10.48 6 AIOH 3195 HZ LYS A 392 12.989 32.560 16.682 1.0026.05 7 ATOH 3248 CG GLN 399 18.261 11.287 17.346 1.00 9.54 6 AIOH 3196 C LYS A 392 13.536 26.046 16.200 1.0011.94 6 ATOH 3249 CD GLN 399 19.195 12.269 IB.066 1.00 9.97 6 J2 --.OH 3197 0 LYS A 392 12.590 25.903 17.011 1.0011.92 8 ATOH 3250 OE1 GLN 399 18.983 13.467 18.191 1.00 8.29 β ~ AIOH 3198 N GLN A 393 13.349 25.676 14.916 1.0012.38 7 ATOH 3251 NE2 GLN 399 20.306 11.751 18.528 1.00 9.30 7 J? ATOH 3199 CA GLH A 393 12.091 25.218 14.386 1.0012.80 6 ATOH 3252 C GLN 399 16.212 9.307 16.643 1.00 12.27 6 _| AIOH 3200 CB GLN A 393 11.736 25.947 13.069 1.0017.13 6 ATOM 32S3 0 GLN 399 16.138 B.327 17.361 1.00 12.29 8 3 ATOM 3201 CG GLN A 393 12.463 27.237 12.917 1.0024.67 6 ATOM 3254 N HIS 400 16.765 9.135 15.415 1.00 12.36 7 #2 ATOH 3202 CD GLN A 393 11.701 28.402 12.316 1.0029.33 6 ATOH 3255 CA HIS 400 17.270 7.893 14.903 1.00 12.28 6 Z3 ATOH 3203 0E1 GLH A 393 11.924 28.717 11.149 1.0030.64 8 ATOH 3256 CB HIS 400 16.419 7.243 13.800 1.00 12.34 6 AIOH 3204 NE2 GLN A 393 10.856 29.003 13.159 1.0031.70 7 ATOM 3257 CG HIS 400 15.001 6.998 14.252 1.00 13.76 6 Λ AIOH 3205 C GLH A 393 11.921 23.764 13.940 1.0012.57 6 ATOH 3258 C02 HIS 400 14.464 6.087 15.135 1.00 12.53 6 _ AIOH 3206 0 GLH A 393 10.718 23.422 13.839 1.0012.77 8 ATOH 3259 HOI HIS 400 13.959 7.856 13.831 1.00 13.34 7 m AIOH 3207 N TYR A 394 12.995 23.041 13.678 1.0011.99 7 ATOH 3260 CE1 HIS 400 12.B60 7.408 14.435 1.00 11.97 6 m ATOH 3208 CA TYR A 394 12.839 21.690 13.167 1.0011.56 6 ATOH 3261 NE2 HIS 400 13.095 6.378 15.194 1.00 11.69 7 H AIOH 3209 CB TYR A 394 13.577 21.661 11.798 1.0011.71 6 ATOH 3262 C HIS 400 18.710 8.179 14.411 1.00 12.21 6 "5 AIOH 3210 CG TYR A 394 12.942 22.687 10.852 1.0012.27 6 ATOH 3263 0 HIS 400 18.909 9.132 13.670 1.00 11.78 8 P. AIOH 3211 CD1 TYR A 394 13.444 23.941 10.588 1.0012.30 6 ATOH 3264 N ASP 401 19.651 7.332 14.89S 1.00 12.31 7 b= AIOH 3212 CE1 TYR A 394 12.811 24.826 9.747 1.0012.61 6 ATOM 3265 CA ASP 401 21.043 7.503 14.536 1.00 12.71 6 rπ AIOH 3213 CD2 TYR A 394 11.754 22.328 10.236 1.0012.73 6 ATOM 3266 CB ASP 401 21.964 7.308 15.758 1.00 15.32 6 w ATOH 3214 CE2 TYR A 394 11.066 23.192 9.378 1.0013.02 6 ATOH 3267 CG ASP 401 21.883 8.427 16.767 1.00 18.10 6 OI ATOH 3215 CZ TYR A 394 11.615 24.442 9.136 1.0013.05 6 ATOH 3268 001 ASP 401 21.438 9.578 16.520 1.00 20.24 8 "*-* AIOH 3216 OH TYR A 394 10.942 25.224 8.229 1.0013.25 8 ATOH 3269 002 ASP 401 22.299 8.187 17.921 1.00 19.29 8 AIOH 3217 C TYR A 394 13.360 20.552 14.017 1.0011.27 6 AIOH 3270 C ASP 401 21.556 6.515 13.484 1.00 12.57 6 AIOH 3218 0 TYR A 394 12.866 19.424 13.834 1.0010.94 8 ATOH 3271 0 ASP 401 21.145 5.360 13.483 1.00 12.31 8 ATOH 3219 N ALA A 395 14.338 20.794 14.908 1.0010.88 7 ATOH 3272 N TYR 402 22.385 6.972 12.5B4 1.00 12.55 7 ATOH 3220 CA ALA A 395 14.896 19.692 15.694 1.0010.74 6 ATOH 3273 CA TYR 402 22.977 6.173 11.524 1.00 12.83 6 ATOH 3221 CB ALA A 395 16.305 20.151 16.074 1.00 B.72 6 ATOM 3274 CB TYR 402 22.385 6.495 10.130 1.00 12.68 6 ATOH 3222 C ALA A 395 14.101 19.267 16.920 1.0010.85 6 ATOH 3275 CG TYR 402 20.891 6.179 10.105 1.00 12.98 6 AIOH 3223 0 ALA A 395 14.392 19.591 18.082 1.0010.94 8 ATOH 3276 CD1 TYR 402 19.990 186 10.470 1.00 13.23 6 ATOH 3224 M TYR A 396 12.986 1B.545 16.743 1.0010.85 7 ATOH 3277 CE1 TYR 402 18.631 9S2 10.544 1.00 13.64 6 ATOH 3225 CA TYR A 396 12.061 18.070 17.753 1.0010.83 6 ATOH 3278 CD2 TYR 402 20.378 927 9.801 1.00 13.10 6 AIOH 3226 CB TYR A 396 10.763 18.949 17.821 1.0010.80 6 ATOH 3279 CE2 TYR 402 19.018 654 9.819 1.00 13.39 6 ATOH 3227 CG TYR A 396 11.083 20.390 18.180 1.0010.52 6 ATOH 3280 C2 TYR 402 18.168 676 10.195 1.00 14.02 6 AIOH 3228 CD1 TYR A 396 11.333 21.365 17.195 1.0010.49 6 ATOM 3281 OH TYR 402 16.795 502 10.282 1.00 14.72 8 AIOH 3229 CE1 TYR A 396 11.683 22.665 17.546 1.0010.23 6 ATOM 3282 C TYR 402 24.478 371 11.592 1.00 13.30 6 AIOH 3230 CD2 TYR A 396 11.215 20.744 19.504 1.0010.24 6 AIOH 3283 0 TYR 402 25.019 7.054 AloH 3231 CE2 TYR A 396 10.747 1.00 13.17 11.536 22.043 19.B35 1.0010.IB 6 8 ATOH 3284 N PHE 403 25.162 818 12.581 1.00 14.08 AIOH 3232 CZ 1YR A 396 11.799 22.9B4 18.874 1.0010.23 6 7 ATOH 3285 CA PHE 403 26.591 861 12.792 AIOH 3233 OH TYR A 396 12.200 24.237 19.305 1.0010.59 8 1.00 14.73 6 ATOM 3286 CB PHE 403 26.978 6.035 14.266 1.00 16.26 6 AIOH 3287 CG PHE A 403 26.766 7.486 14.665 1.0019.71 6 ATOM 3340 CA VAL 409 27.012 9.436 9.309 1.00 11.68 6 AIOH 3288 CD1 PHE A 403 25.574 7.927 15.176 1.0020.07 6 ATOH 3341 CB VAL 409 27.735 9.616 10.63B 1.0013.02 6 AIOH 3289 CD2 PHE A 403 27.748 8.440 14.483 1.0021.01 6 ATOH 3342 CGI VAL 409 28.916 8.661 10.804 1.00 14.14 6 ATOH 3290 CE1 PHE A 403 25.379 9.241 15.534 1.0021.71 6 ATOH 3343 CG2 VAL 409 28.293 11.030 10.817 1.0011.59 6 AIOH 3291 CE2 PHE A 403 27.540 9.786 14.804 1.0022.26 6 ATOH 3344 C VAL 409 25.823 10.380 9.245 1.0011.38 6 AIOH 3292 CZ PHE A 403 26.338 10.216 15.345 1.0021.47 6 ATOH 3345 0 VAL 409 25.887 11.441 8.613 1.0011.38 8 ATOH 3293 C PHE A 403 27.113 4.537 12.220 1.0015.16 6 ATOH 3346 N GLY 410 24.747 10.000 9.898 1.00 10.96 7 AIOH 3294 O PHE A 403 27.616 3.625 12.902 1.0015.23 8 ATOH 3347 CA GLY 410 23.548 10.842 9.910 1.00 10.41 6 AIOH 3295 H ASP A 404 26.987 4.370 10.906 1.0015.33 7 ATOH 3348 C GLY 410 22.635 10.508 11.084 1.00 9.89 6 ATOH 3296 CA ASP A 404 27.398 3.103 10.294 1.0015.59 6 ATOM 3349 0 GLY 410 22.871 9.547 11.830 1.00 9.68 8 AIOH 3297 CB ASP A 404 26.115 2.428 9.754 1.0017.33 6 ATOH 3350 N TRP 411 21.623 11.347 11.201 1.00 9.60 7 AloH 3298 CG ASP A 404 25.433 3.431 8.838 1.0019.38 6 ATOM 3351 CA TRP 411 20.569 11.201 12.204 1.00 9.34 6 ATOH 3299 ODl ASP A 404 25.870 4.570 8.544 1.0019.96 8 ATOM 3352 CB TRP 411 20.994 11.750 13.S74 1.00 8.12 6 AI M 3300 002 ASP A 404 24.330 3.060 B.407 1.0021.24 8 ATOH 3353 CG TRP 411 21.417 13.213 13.561 1.00 8.50 6 AI IH 3301 C ASP A 404 28.346 3.116 9.119 1.0015.47 6 ATOH 3354 CD2 TRP 411 22.726 13.662 13.285 1.00 B.48 6 Aim 3302 O ASP A 404 28.339 2.154 8.320 1.0015.71 8 ATOH 3355 CE2 TRP 411 22.699 15.049 13.356 1.00 8.47 6 I ) »! )H 3303 N HIS A 405 29.168 4.144 8.997 1.0015.11 7 ATOH 3356 CE3 TRP 411 23.924 13.010 12.971 1.00 9.18 6 *'θH 3304 CA HIS A 405 30.098 4.238 7.885 1.0014.80 6 ATOH 3357 CD1 TRP 411 20.647 14.285 13.808 1.00 6.27 6 CD AIOH 3305 CB HIS A 405 29.332 4.915 6.719 1.0014.80 6 ATOH 3358 NE1 TRP 411 21.483 15.439 13.671 1.00 6.58 7 Λ AIOH 3306 CG HIS A 405 30.187 4.926 5.492 1.0015.21 6 ATOH 3359 CZ2 TRP 411 23.830 15.839 13.113 1.00 9.15 6 Zϊ AIOH 3307 C02 HIS A 405 30.385 3.954 4.561 1.0015.68 6 ATOH 3360 CZ3 TRP 411 25.054 13.814 12.732 1.00 9.35 6 H AIOH 3308 H01 HIS A 405 30.992 5.990 5.157 1.0015.84 7 ATOH 3361 CH2 TRP 411 25.007 15.163 12.799 1.00 9.69 6 ATOH 3309 CE1 HIS A 405 31.654 5.723 4.041 1.0016.58 6 ATOH 3362 C TRP 411 19.296 11.897 11.708 1.00 9.23 6 H ATOH 3310 NE2 HIS A 405 31.309 4.491 3.680 1.0017.15 7 ATOH 3363 0 TRP 411 19.372 12.824 10.901 1.00 8.76 m AIOH 3311 C HIS A 405 31.280 5.023 8.383 1.0014.46 6 ATOH 3364 N THR 412 IB.151 11.418 12.226 1.00 9.36 £ AIOH 3312 O HIS A 405 31.008 5.908 9.197 1.0014.63 8 ATOH 3365 CA THR 412 16.877 12.015 11.894 1.00 9.69 6 ~~ ATOH 3313 H HIS A 406 32.494 4.841 7.963 1.0014.11 7 ATOH 3366 CB THR 412 15.968 11.081 11.040 1.0010.82 6 !!! AIOH 3314 CA HIS A 406 33.630 5.587 8.495 1.0013.78 6 ATOH 3367 0G1 THR 412 15.687 9.914 11.826 1.0012.10 8 _J AIOH 3315 CB HIS A 406 35.000 4.932 8.189 1.0015.67 6 ATOM 3368 CG2 THR 412 16.614 10.613 9.743 1.00 9.28 6 ___, AIOH 3316 CG HIS A 406 34.9B1 4.416 6.777 1.0016.76 6 ATOH 3369 C THR 412 16.136 12.441 13.173 1.00 9.93 6 73 ATOH 3317 CD2 HIS A 406 34.450 3.285 6.232 1.0016.51 6 ATOH 3370 0 THR 412 16.399 12.027 14.318 1.00 9.78 8 C AIOH 331B ND1 HIS A 406 35.504 5.164 5.733 1.0018.12 7 ATOM 3371 N ARG 413 15.184 13.348 12.978 1.0010.07 7 P" AIOH 3319 CE1 HIS A 406 35.318 4.505 4.578 1.0016.95 6 ATOM 3372 CA ARG 413 14.332 13.843 14.055 1.0010.74 6 ~~ AIOH 3320 HE2 HIS A 406 34.666 3.388 4.8B0 1.0017.55 7 ATOM 3373 CB ARG 413 14.635 15.236 14.615 1.00 8.23 6 M AIOH 3321 C HIS A 406 33.580 7.002 8.026 1.0013.47 6 ATOH 3374 CG ARG 413 16.039 15.382 15.182 1.00 σ. 6.55 6 AIOH 3322 0 HIS A 406 34.298 7.753 B.672 1.0013.10 8 ATOH 3375 CD ARG 413 16.262 14.604 16.464 1.00 6.58 6 AIOH 3323 N ASP A 407 32.861 7.500 7.04B 1.0013.42 7 ATOH 3376 NE ARG 413 1S.3BB 14.982 17.577 1.00 5.58 7 AIOH 3324 CA ASP A 407 32.837 8.877 6.628 1.0013.27 6 ATOH 3377 CZ ARG 413 15.602 16.062 18.326 1.00 8.01 6 AIOH 3325 CB ASP A 407 33.163 9.063 5.138 1.0014.59 6 ATOH 3378 NH1 ARG 413 14.802 16.370 19.349 1.00 7.49 7 ATOH 3326 CG ASP A 407 34.556 8.665 4.654 1.0016.13 6 ATOM 3379 NH2 ARG 413 16.645 16.870 18.094 1.00 7.65 7 ATOH 3327 001 ASP A 407 35.474 8.360 5.486 1.0014.23 8 ATOH 3380 C ARG 413 12.946 13.767 13.403 1.00 11.41 6 ATOH 3328 002 ASP A 407 34.808 8.646 3.381 1.0018.38 8 ATOM 3381 0 ARG 413 12.678 14.374 12.355 1.00 11.24 a AIOH 3329 C ASP A 407 31.457 9.532 6.757 1.0012.98 6 ATOH 3382 N GLU 414 12.076 12.980 14.035 1.00 12.08 7 ATOH 3330 0 ASP A 407 31.310 10.601 7.360 1.0012.77 8 ATOH 3383 CA GLU 414 10.713 12.785 13.510 1.00 12.84 6 AIOH 3331 N ILE A 408 30.465 B.890 6.167 1.0012.85 7 ATOH 3384 CB GLU 414 9.957 11.626 14.195 1.00 11.98 6 AIOH 3332 CA ILE A 408 29.098 9.438 6.133 1.0012.79 6 ATOH 3385 CG GLU 414 10.578 10.270 13.880 1.00 12.67 6 AIOH 3333 CB ILE A 408 28.429 9.103 4.799 1.0014.07 6 ATOH 3386 CD GLU 414 9.722 9.123 14.401 1.00 14.64 6 AIOH 3534 CG2 ILE A 408 27.045 9.742 4.656 1.0012.86 6 ATOH 3387 OE1 GLU 414 8.485 9.240 14.504 1.00 14.73 8 AloH 3335 CGI ILE A 408 29.251 9.578 3.597 1.0013.69 6 ATOM 3388 OE2 GLU 414 10.249 8.041 14.723 1.00 15.78 8 ATOH 3336 CD1 ILE A 408 28.979 B.781 2.321 1.0014.63 6 ATOH 3389 C GLU 414 9.819 14.015 13.605 1.00 13.32 6 AIOH 3337 C ILE A 408 28.219 8.885 7.260 1.0012.60 6 ATOH 3390 0 GLU 414 8.855 14.006 12.864 1.00 13.17 a AIOH 3338 0 ILE A 408 27.838 7.712 7.271 1.0012.81 8 ATOH 3391 N GLY 415 10.096 15.006 14.389 1.00 14.06 AIOH 3339 M VAL A 409 27.910 9.762 8.195 1.0012.05 7 7 ATOH 3392 CA GLY 4 AIOH 3393 C GLY A 415 8.276 15.870 15.637 1.0017.18 6 ATOH 3394 0 GLY A 415 8.176 14.768 16.148 1.0017.23 8 ATOH 3395 N ASP A 416 7.581 16.904 16.048 1.0018.70 7 AIOH 3396 CA ASP A 416 6.606 16.860 17.118 1.0020.18 6 AIOH 3397 CB ASP A 416 7.228 17.531 18.307 1.0026.49 6 AIOH 3398 CG ASP A 416 6.358 17.615 19.535 1.0031.33 6 ATOH 3399 001 ASP A 416 6.791 18.402 20.413 1.0035.28 8 AIOH 3400 002 ASP A 416 5.301 16.975 19.696 1.0032.88 8 AIOH 3401 C ASP A 416 5.400 17.597 16.568 1.0021.08 6 AIOH 3402 O ASP A 416 5.423 18.631 15.908 1.0020.94 8 ATOM 3403 N SER A 417 4.234 17.031 16.824 1.0022.16 7 AloH 3404 CA SER A 417 2.928 17.484 16.380 1.0023.18 6 AlliH 3405 CB SER A 417 1.868 16.471 16.846 1.0027.52 6 A! >H 3406 OG SER A 417 1.734 16.874 18.237 1.0032.78 8 AlUM 3407 C SER A 417 2.585 18.852 16.929 1.0023.50 6 -: H 3408 0 SER A 417 1.821 19.541 16.258 1.0023.90 8 ) AIOH 3409 N SER A 418 3.145 19.217 18.073 1.0023.61 7 'lOM 3410 CA SER A 418 2.982 20.541 18.628 1.0023.56 6 0 ATOM 3411 CB SER A 418 3.247 20.523 20.135 1.0024.90 6 Λ AIOH 3412 OG SER A 418 4.660 20.195 20.198 1.0027.24 8 AIOH 3413 C SER A 418 3.988 21.525 18.023 1.0023.37 6 AIOH 3414 0 SER A 418 3.995 22.714 18.503 1.0023.96 8 AIOH 3415 N VAL A 419 4.894 21.195 17.094 1.0022.44 7 AIOH 3416 CA VAL A 419 5.793 22.233 16.490 1.0021.33 6 * AIOH 3417 CB VAL A 419 7.278 22.269 16.815 1.0019.53 6 Λ AIOH 3418 CGI VAL A 419 B.070 23.317 16.038 1.0015.95 6 ___ AIOH 3419 CG2 VAL A 419 7.558 22.527 18.315 1.0018.97 6 JJ AIOH 3420 C VAL A 419 5.477 21.951 14.988 1.0020.67 6 AIOH 3421 0 VAL A 419 5.911 20.939 14.404 1.0020.45 8 _- » AIOH 3422 N ALA A 420 4.616 22.803 14.400 1.0020.01 7 3 AIOH 3423 CA ALA A 420 4.174 22.558 13.017 1.0019.28 6 AIOH 3424 CB ALA A 420 3.189 23.619 12.527 1.0019.92 6 ~ AIOH 3425 C ALA A 420 5.329 22.464 12.050 1.0018.43 6 ~ AIOH 3426 0 ALA A 420 6.221 23.297 12.166 1.0018.43 8 AIOH 3427 N ASN A 421 5.312 21.471 11.161 1.0017.67 7 AIOH 3428 CA ASH A 421 6.356 21.242 10.168 1.0016.69 6 AIOH 3429 CB ASH A 421 6.537 22.436 9.204 1.0019.20 6 AIOH 3430 CG ASN A 421 5.312 22.617 8.330 1.0021.29 6 ATOH 3431 ODl ASN A 421 4.586 21.711 7.966 1.0022.05 8 AIOH 3432 ND2 ASN A 421 5.028 23.853 7.994 1.0023.75 7 AIOH 3433 C ASH A 421 7.760 20.891 10.703 1.0015.64 6 AIOH 3434 0 ASN A 421 8.711 20.946 9.931 1.0015.23 8 AIOH 3435 N SER A 422 7.882 20.479 11.947 1.0014.78 7 ATOH 3436 CA SER A 422 9.140 20.088 12.542 1.0014.31 6 ATOH 3437 CB SER A 422 9.064 20.137 14.071 1.0014.37 6 ATOH 3438 OG SER A 422 7.990 19.345 14.623 1.0013.80 8 AIOH 3439 C SER A 422 9.518 18.705 12.009 1.0013.67 6 ATOH 3440 0 SER A 422 8.713 17.932 11.459 1.0013.79 B AIOH 3441 N GLY A 423 10.797 18.389 12.161 1.0012.94 7 AIOH 3442 CA GLY A 423 11.329 17.086 11.679 1.0012.05 6 AIOH 3443 C GLY A 423 12.546 17.472 10.825 1.0011.56 6 AIOH 3444 0 GLY A 423 12.532 1B.566 10.232 1.0011.46 8 AIOH 3445 N LEU A 424 13.562 16.612 10.738 1.0010.94 7 AIOH 3499 CD PRO A 432 35.409 10.665 0.884 1.00 14.46 6 ATOM 3552 CD2 TYR A 439 11.815 5.768 11.397 1.00 16.76 6 33.653 11.935 -0.199 1.00 14.68 6 ATOH 3553 CE2 TYR A 439 10.514 5.667 11.875 1 .00 17.07 6 34.035 10.827 -1.190 1.00 14.46 6 ATOH 3554 CZ TYR 439 9.490 5.433 10.974 1 .00 17.36 6 35.224 10.168 -0.544 1.00 14.43 6 ATOH 3555 OH TYR 439 8.184 5.345 11.408 1.00 17.36 8 32.163 11.902 0.220 1.00 14.96 6 ATOM 3556 C TYR 439 13.404 B.144 9.357 1 .00 15.81 6 31.795 11.354 1.273 1.00 14.84 8 ATOH 3557 0 TYR 439 13.994 B.512 10.382 1.00 15.50 8 31.312 12.512 -0.641 1.00 15.15 7 ATOM 3558 N VAL 440 12.407 8.831 8.856 1.00 16.08 7 29.882 12.569 -0.450 1.00 15.39 6 ATOM 3559 CA VAL 440 11.897 10.144 9.350 1.00 16.61 6 29.192 11.254 -0.788 1.00 15.65 6 ATOM 3560 CB VAL 440 11 .999 10.905 7.980 1.00 16.77 6 29.814 10.259 -1.188 1.00 15.62 8 ATOH 3561 CGI VAL 440 10.764 11.601 7.561 1.00 17.08 6 27.885 11.213 -0.658 1.00 15.83 7 ATOH 3562 CG2 VAL 440 13.263 11.754 8.026 1.00 15.70 6 27.160 9.983 -0.950 1.00 15.94 6 ATOH 3563 C VAL 440 10.554 10.106 10.031 1.00 17.07 6 25.733 10.059 -0.444 1.00 15.96 6 ATOM 3564 O VAL 440 10.014 11.040 10.625 1.00 16.85 8 25.263 11.153 -0.176 1.00 16.25 8 ATOM 3565 N GLY 441 9.900 8.915 9.995 1.00 17.47 7 25.080 8.925 -0.297 1.00 15.72 7 ATOH 3566 CA GLY 441 8.607 8.729 10.597 1.00 18.13 6 23.722 8.872 0.128 1.00 15.72 6 ATOH 3567 C GLY 441 7.583 8.699 9.476 1.00 18.60 6 22.85B 8.337 -1.047 1.00 15.08 6 ATOH 3568 0 GLY 441 7.616 9.450 8.514 1.00 18.47 8 23.470 7.942 1.309 1.00 15.68 6 ATOM 3569 N ARG 442 6.636 7.793 9.673 1.00 19.21 7 24.260 7.007 1.516 1.00 15.51 8 ATOH 3570 CA ARG 442 5.540 7.559 8.739 1.00 19.79 6 22.366 8.252 2.019 1.00 15.52 7 ATOM 3571 CB ARG 442 4.804 6.264 9.145 1.00 27.13 6 21.990 7.383 3.119 1.00 15.58 6 ATOH 3572 CG ARG 442 3.910 5.788 8.008 1.00 34.25 6 22.566 7.682 4.490 1.00 15.09 6 ATOH 3573 CD ARG 442 3.727 4.252 7.911 1.00 40.05 6 22.500 6.476 5.442 1.00 14.85 6 ATOH 3574 NE ARG 442 3.027 • 3.980 6.634 1.00 44.01 7 23.071 6.769 6.810 1.00 13.83 6 ATOH 3575 CZ ARG 442 1.896 3.329 6.388 1.00 46.30 6 24.448 7.441 6.784 1.00 12.21 6 ATOH 3576 NH1 ARG 442 1.175 2.772 7.381 1.00 47.10 7 25.498 6.400 6.652 1.00 11.33 7 ATOH 3577 NH2 ARG 442 1.446 3.253 5.119 1.00 46.98 7 20.447 7.396 3.179 1.00 15.62 6 ATOM 3578 C ARG 442 .586 8.725 8.657 1.00 19.53 6 19.778 8.405 3.060 1.00 15.33 8 ATOM 3579 0 ARG 442 .955 9.003 7.621 1.00 19.67 8 19.931 6.177 3.314 1.00 15.95 7 ATOM 3580 N GLN 443 .479 9.544 9.684 1.00 19.05 7 18.502 5.972 3.422 1.00 16.36 6 ATOH 3581 CA GLN 443 .607 10.709 9.658 1.00 18.69 6 17.96S 4.624 2.977 1.0023.29 6 ATOH 3582 CB GLN 443 .431 11.246 11.093 1.00 21.29 6 17.573 4.499 1.510 1.0029.80 6 ATOH 3583 CG GLN 443 4.808 11.675 11.634 1.00 23.26 6 16.656 3.293 1.407 1.0035.68 6 ATOH 3S84 CD GLN 443 5.581 10.603 12.390 1.00 24.64 6 15.201 3.525 1.319 1.0040.60 7 ATOH 3585 OE1 GLN 443 5.631 9.402 12.134 1.00 24.10 8 14.309 2.734 1.964 1.0042.03 6 ATOH 3586 NE2 GLN 443 6.316 11.066 13.438 1.00 25.50 7 14.735 1.740 2.755 1.0042.08 7 ATOH 3587 C GLN 443 4.115 11.806 8.734 1.00 18.06 6 13.005 2.950 1.814 1.0042.49 7 ATOM 3588 0 GLN 443 3.414 12.798 8.501 1.00 17.90 8 IB.202 6.050 4.911 1.00 15.94 6 ATOM 3589 N ASN 444 5.307 11.714 8.193 1.00 17.51 7 18.833 5.318 5.678 1.00 15.62 8 ATOM 3590 CA ASN 444 5.897 12.636 7.253 1.00 16.84 6 17.303 6.932 5.265 1.00 15.86 7 ATOH 3591 CB ASN 444 7.400 12.828 7.563 1.00 14.89 6 17.019 7.059 6.722 1.00 15.87 6 ATOH 3592 CG ASN 444 7.497 13.458 8.951 1.00 15.66 6 17.846 8.236 7.242 1.00 16.35 6 ATOM 3593 001 ASN 444 6.765 14.374 9.269 1.00 13.70 8 19.360 8.200 7.266 1.00 15.99 6 ATOM 3594 HD2 ASN 444 8.368 12.974 9.818 1.00 15.53 7 20.172 9.634 7.987 1.00 16.66 16 ATOH 3595 C ASN 444 5.814 12.078 5.820 1.00 16.45 6 19.69B 10.9B9 6.970 1.00 14.67 6 ATOH 3596 0 ASN 444 6.396 12.716 4.943 1.00 16.24 8 15.525 7.205 6.983 1.00 15.63 6 ATOH 3597 N ALA 445 5.196 10.917 5.640 1.00 16.01 7 14.774 7.662 6.109 1.00 15.49 8 ATOH 3598 CA ALA 445 5.075 10.268 4.345 1.00 16.03 6 15.065 6.827 8.145 1.00 15.53 7 ATOH 3599 CB ALA 445 4.109 9.075 4.403 1.00 15.55 6 13.699 6.862 8.590 1.00 15.72 6 ATOH 3600 C ALA 445 4.572 11.159 3.208 1.00 15.90 6 13.484 5.632 9.498 1.00 15.96 6 ATOH 3601 0 ALA 445 3.624 11.896 3.441 1.00 15.97 8 12.110 5.576 10.071 1.00 16.56 6 ATOH 3602 N GLY 446 5.165 11.130 2.010 1.00 15.77 11.044 5.33B 9.188 1.00 17.21 6 7 ATOM 3603 CA GLY 446 4.752 11.944 0.885 1.00 15.36 9.728 5.283 9.611 1.00 17.34 6 6 ATOM 3604 C GLY 446 5.207 13.378 0.863 1.00 15.20 6 ATOH 3711 CG PRO 459 13.637 19.885 -4.393 1.00 18.37 6 IOH 3712 C PRO 459 14.504 16.723 -2.839 1.00 18.47 6 AIOH 3713 0 PRO 459 14.829 15.979 -3.780 1.00 18.68 8 AIOH 3714 N VAL 460 14.113 16.146 -1.728 1.00 18.24 7 AIOH 3715 CA VAL 460 13.987 14.691 -1.504 1.00 18.19 6 D 3 ATOH 3716 CB VAL 460 14.906 14.168 -0.379 1.00 17.56 6 AIOH 3717 CGI VAL 460 14.739 12.685 -0.076 1.00 17.48 6 y- x AIOH 3718 CG2 VAL 460 16.371 14.396 -0.750 1.00 17.31 6 ATOH 3719 C VAL 460 12.528 14.396 -1.209 1.00 18.23 6 AIOH 3720 O VAL 460 11.892 15.157 -0.428 1.00 18.51 8 ATOH 3721 N VAL 461 11.894 13.362 -1.798 1.00 18.03 7 AIOH 3722 CA VAL 461 10.468 13.105 -1.458 1.00 17.66 6 AIOH 3723 CB VAL 461 9.584 12.863 -2.709 1.00 17.06 6 AIOH 3724 CGI VAL 461 8.143 12.564 -2.256 1.00 16.42 6 MOM 3725 CG2 VAL 461 9.629 14.023 -3.678 1.00 15.12 6 MOH 3726 C VAL 461 10.418 11.943 • 0.456 1.00 17.45 6 MOM 3727 VAL 461 11.046 10.893 • 0.596 1.00 17.01 8 IΛ C ΛTOH 3728 ILE 462 9.707 12.111 0.647 1.00 17.69 7 00 AIOH 3729 CA ILE 462 9.596 11.050 1.642 1.00 18.12 6 I ) AI H 3730 CB HE 462 9.212 11.549 3.046 1.00 15.81 6 H AIOH 3731 CG2 ILE 462 9.222 10.334 3.984 1.00 15.11 6 H AIOH 3732 CGI ILE 462 10.089 12.691 3.597 1.00 13.00 6 AIOH 3733 CD1 HE 462 11.575 12.439 3.642 1.00 9.27 6 ATOH 3734 C ILE 462 8.554 10.036 1.116 1.00 18.85 6 ATOH 3735 0 ILE 462 7.432 10.390 0.717 1.00 18.67 8 ll AIOH 3736 N ASH 463 8.922 8.755 1.138 1.00 19.55 7 X AIOH 3737 CA ASN 463 8.090 7.650 0.672 1.0020.49 6 rπ AIOH 3738 CB ASN 463 8.960 6.443 0.342 1.00 20.20 6 m ATOH 3739 CG ASN 463 9.411 5.430 1.361 1.00 21.59 6 AIOH 3740 ODl ASN 463 9.117 5.376 2.570 1.00 22.11 8 73 AIOH 3741 ND2 ASN 463 10.221 4.455 0.904 1.00 19.99 7 C AT H 3742 C ASN 463 6.975 7.297 1.630 1.0021.45 6 A1"M 3743 ASH 463 6.884 7.742 2.770 1.0021.42 8 AIOH 3744 SER 464 6.070 6.390 1.173 1.0022.31 7 AT H 3745 CA SER 464 4.877 5.971 1.916 1.0022.97 6 σ ro. AIOH 3746 CB SER 464 3.915 5.159 1.024 1.0023.92 6 AIOH 3747 OG SER 464 4.365 3.841 0.731 1.0025.69 8 AT H 3748 C SER 464 5.187 5.303 3.248 1.00 23.29 6 ATOH 3749 SER 464 4.319 5.400 4.131 1.0023.52 8 ATOH 3750 GLU 465 6.344 4.722 3.486 1.0023.46 7 AIOH 3751 CA GLU 465 6.814 4.134 708 1.0023.73 6 AIOH 3752 CB GLU 465 7.931 3.164 313 1.0029.98 6 AIOH 3753 CG GLU 465 7.852 1.671 515 1.0035.99 6 AIOH 3754 CO GLU 465 6.542 1.117 976 1.0039.49 6 AIOH 3755 OE1 GLU 465 6.407 1.177 734 1.0041.43 8 AIOH 3756 OE2 GLU 465 5.709 0.684 812 1.0041.76 8 AIOH 3757 GLU 465 7.511 095 721 1.00 23.27 6 AIOH 3758 GLU 465 7.857 672 B4B 1.0023.24 8 ATOH 3759 GLY 466 7.744 345 5.324 1.00 22.53 7 AI H 3760 CA GLY 466 8.436 317 6.135 1.0021.95 6 AIOH 3761 C GLY 466 9.969 245 5.909 1.0021.47 6 AT H 3762 GLY 466 10.728 644 6.820 1.00 21.33 8 ATOH 3923 O 9 UAT 2 42.991 28.597 56.879 1.00 19.54 8 ATOH 3924 OUO WAT 3 42.416 33.909 17.726 1.00 10.85 8 AIOH 3925 OU1 UAT 3 48.842 22.953 44.340 1.00 7.46 8 AIOH 3926 OU2 UAT 3 36.038 55.628 43.083 1.00 10.34 8 AT H 3927 0U3 UAT 3 58.570 25.578 42.683 1.00 12.51 8 ATOH 3928 0W. UAT 3 35.732 43.524 49.882 1.00 5.95 8 AIOH 3929 0U5 UAT 3 26.190 18.692 1.154 1.00 12.57 8 - AIOH 3930 0U6 UAT 3 40.723 25.525 46.044 1.00 10.44 8 AIOH 3931 OW7 UAT 3 41.640 28.398 45.135 1.00 5.00 8 IOH 3932 OU8 UAT 3 36.546 42.416 33.352 1.00 5.00 8 AIOH 3933 OU9 UAT 3 40.987 21.110 52.091 1.00 20.54 8 AIOH 3934 OUO UAT 4 37.695 27.410 12.493 1.00 11.34 a ATOH 3935 OU1 UAT 4 22.844 23.707 36.872 1.00 9.B0 a AIOH 3936 OU2 UAT 4 36.012 18.648 48.284 1.00 17.35 8 > 0H 3937 OU3 UAT 4 31.899 45.870 33.523 1.00 10.56 B A'OH 3938 0U4 UAT 4 30.501 38.096 33.954 1.00 11.67 B » ι OH 3939 OU5 UAT 4 22.073 12.907 32.231 1.00 10.97 8 IOH 3940 0U6 UAT 4 40.488 14.451 42.396 1.00 12.74 8 ATOH 3941 OU7 UAT 4 53.405 37.236 44.839 1.00 12.00 8 ATOH 3942 OU8 UAT 4 43.396 20.817 52.968 1.00 25.21 8 AIOH 3943 OU9 UAT 4 45.712 34.753 17.330 1.00 22.47 8 AIOH 3944 OUO UAT 5 52.299 25.204 54.738 1.00 18. B5 8 ATOH 3945 OU1 UAT 5 10.464 19.211 8.671 1.00 8.04 8 AIOH 3946 OU2 UAT 5 23.407 21.100 30.729 1.00 15.19 8 AIOH 3947 OU3 UAT 5 34.672 39.007 47.914 1.00 25.93 8 Λ AIOH 3948 OU4 UAT 5 39.440 24.513 6.213 1.00 20.60 8 ATOH 3949 OU5 UAT 5 43.207 54.381 40.149 1.00 25.71 β AIOH 3950 OU6 UAT 5 29.887 49.393 26.775 1.00 10.08 8 AIOH 3951 OU7 UAT 5 18.296 28.320 27.646 1.00 17.61 8 AIOH 3952 OU8 UAT 5 42.657 37.701 31.679 1.00 16.67 8 73 AIOH 3953 OU9 UAT 5 43.242 40.411 24.206 1.00 19.05 8 AI H 3954 OUO UA1 6 27.361 IB.395 39.419 1.00 14.74 a AIOH 3955 OU1 UAT 6 28.339 52.900 35.976 1.00 18.51 8 AIOH 3956 OU2 UAT 6 37.756 14.989 39.100 1.00 17.01 8 OU3 UAT 6 22.B40 21.238 35.474 1.00 13.60 a σ M. AIOH 3957 AIOH 395B OU4 UAT 6 38.940 13.232 9.026 1.00 11.51 a AIOH 3959 OU5 UAT 6 25.342 16.185 20.356 1.00 18. B6 a AI H 3960 OW6 UAT 6 B.361 17.329 8.642 1.00 13.52 a AIOH 3961 OW7 UAT 6 37.794 6.917 7.269 1.00 20.73 8 AIOH 3962 OU8 UAT 6 45.060 49.979 33.793 1.00 12.44 a ATOH 3963 OU9 UAT 6 36.427 41.328 48.308 1.00 11.02 a ATI.. 3964 OUO AT 41.263 15.827 37.266 1.00 22.49 a ATOH 3965 OU1 UAT 25.131 39.394 49.866 1.00 10.30 B AIOH 3966 OU2 UAT 51.050 21.873 54.397 1.00 IB.11 8 ATOH 3967 OU3 UAT 43.851 40.827 26.978 1.00 38.82 8 ATOH 3968 OU4 UAT 48.952 26.479 52.035 1.00 17.95 8 AI H 3969 OU5 UAT 24.717 49.514 27.044 1.00 19.57 8 ATOH 3970 OU6 UAT 32.551 52.703 28.488 1.00 9.04 8 ATOH 3971 OW7 UAT 44.885 26.009 54.445 1.00 7.24 a AloH 3972 OUB UAT 38.325 36.644 45.393 1.00 19.65 8 AI H 3973 OU9 UAT 21 .609 12.965 20.907 1.00 9.32 8 AIOH 3974 OUO UAI 24.711 13.545 20.7B4 1.00 23.06 8 AloH 3975 OU1 UAT 42.374 43.789 25.824 1.00 2B.85 8 ATOH 4029 OU5 WAT 13 13.009 12.182 -4.047 1.002761 8 AIOH .082 OWβ UAT 18 30.748 53.658 S0.670 1.00 29.38 8 ATOH 4030 OU6 UAT 13 32.756 8.582 1.824 1.0029.04 8 ATOH 083 OU9 UAT 18 50.065 24.BOB 35.502 1.00 35.76 8 AIOH 4051 OU7 UAT 13 16.249 23.415 •2.919 1.0036.05 8 AIOH 084 OUO UAT 19 22.202 19.032 28.774 1.00 27.27 8 AIOH 4032 OW8 UAT 13 36.916 46.802 51.068 1.00 1392 8 AIOH 1085 OU1 UAT 19 54.614 46.941 48.285 1.00 29.46 8 ATOH 4033 OW9 UAT 13 51.456 45.867 53.043 1.002725 8 ATOH ,086 OW2 UAT 19 46.049 21.147 25.386 1.00 53.35 B AIOH 4034 OUO UAT 14 44.576 23.979 15.915 1.0039 18 8 ATOH 087 OW3 UAT 19 45.816 49.038 43.196 1.00 33.55 B AH>H 40J5 OU1 UAT 14 16.344 4.264 16.031 1.002200 8 ATOH ,088 OU4 UAT 19 22.659 43.614 47.560 1.00 46.32 a ATOH 4036 OW2 UAT 14 32.347 13.546 •3.049 1.003727 8 ATOH ,089 OW5 UAT 19 60.822 30.153 59.870 1.00 43.42 8 ATOH 4037 OU3 UAT 14 45.366 38.058 33.758 1.002090 8 ATOH ,090 OW6 UAT 19 53.393 13.840 38.545 1.00 34.26 8 AIOH 4038 OU4 UAT 14 4.549 18.600 13.099 1.002030 8 ATOH ,091 OU7 UAT 19 32.544 1.677 6.989 1.00 38.69 8 AIOH 4039 OU5 WAT 14 15.354 36.796 43.569 1.00 18 79 8 ATOH ,092 OWβ UAT 19 50.647 31.408 63.808 1.00 33.78 8 AIOH 4040 OU6 UAT 14 44.963 30.462 57.791 1.0033 45 a ATOH ,093 OU9 UAT 19 16.948 27.505 19.812 1.00 23.95 a A!OH 4041 OU7 UAT 14 53.136 23.195 37.475 1.0031 43 8 ATOH ,094 OUO UAT 20 6.330 5.129 -1.860 1.00 55.10 8 AIOH 4042 OU8 UAT 14 30.694 15.659 -3.842 1.002359 8 ATOH 095 OU1 UAT 20 32.149 29.484 1.396 1.00 29.24 8 *'OH 4043 OW9 WAT 14 39.010 7.257 14.525 1.0037.98 8 ATOH ,096 OU2 UAT 20 18.952 20.628 24.894 1.00 35.86 8 AIOH 4044 OUO WAT 15 37.498 55.360 32.899 1.0035.04 8 ATOH 1097 OU3 UAT 20 31.733 56.172 34.803 1.00 3B.99 8 Λ »:OH 4045 OW1 WAT 15 21.133 44.448 35.4B1 1.003584 8 ATOH ,098 OU4 UAT 20 54.293 14.452 50.415 1.00 35.67 a AIOH 4046 OW2 WAT 15 23.993 4.153 14.519 1.0020.07 a ATOH 099 OU5 UAT 20 44.169 20.632 26.756 1.00 27.57 8 0 Λ AIOH 4047 OW3 WAT 15 21.568 23.231 44.662 1.003460 a ATOH 100 OU6 UAT 20 25.114 53.998 30.655 1.00 43.33 8 . ATOH 4048 OW4 UAT 15 9.185 24.466 6.708 1.00 19.79 a AIOH 101 OU7 UAT 20 43.966 46.309 55.136 1.00 37.54 8 AIOH 4049 OU5 WAT 15 44.S86 35.812 31.349 1.0048..30 a ATOH 102 OU8 UAT 20 58.366 45.019 48.175 1.00 43.14 8 AIOH 4050 OW6 WAT 15 30.789 25.745 52.371 1.0038..63 a ATOH 103 OU9 UAT 20 44.205 21.201 13.125 1.00 51.53 a ATOH 4051 OU7 WAT 15 41.284 38.972 11.403 1.0029..22 8 ATOH 104 OUO UAT 21 61.128 25.016 42.919 1.00 34.86 a AIOH 4052 OW8 WAT 15 56.979 36.187 S8.016 1.0037..19 β ATOH 105 OU1 UAT 21 8.371 24.444 12.113 1.00 45.95 8 1 ATOH 4053 OW9 WAT 15 25.886 5.827 3.524 1.0021.64 a ATOH 106 OU2 UAT 21 18.370 31.505 12.739 1.00 27.20 8 AIOH 4054 OWO UAT 16 41.689 14.341 39.346 1.0028.91 a ATOH 107 OU3 UAT 21 33.430 25.045 51.739 1.00 31.92 a AIOH 4055 OU1 UAT 16 20.238 10.905 31.899 1.00 29.69 β ATOH 108 OU4 UAT 21 47.660 31.418 59.018 1.00 35.64 8 ATOH 4056 OW2 WAT 16 44.542 44.756 52.978 1.00 18.83 a AIOH 109 OW5 UAT 21 43.308 25.115 12.609 1.00 40.37 8 AIOH 4057 OW3 UAT 16 57.377 17.228 51.604 1.0020.62 8 ATOH 110 OU6 UAT 21 44.725 50.787 28.523 1.00 26.83 a AIOH 4058 OU4 UAT 16 53.851 33.580 56.957 1.0022.46 9 a ATOH 111 OU7 UAT 21 40.073 41.591 56.477 1.00 38.23 8 AIOH 4059 OU5 UAT 16 35.776 25.007 52.963 1.0030.96 a ATOH 112 OU8 UAT 21 3.706 15.718 9.641 1.00 23.55 8 AI H 4060 OU6 UAT 16 50.697 26.378 37.894 1.00 17.69 a ATOH 113 OW9 UAT 21 46.527 18.879 50.827 1.00 35.55 8 ATOH 4061 OU7 UAT 16 35.244 16.237 47.346 1.0035.92 a ATOH 114 OUO UAT 22 51.052 12.865 45.163 1.00 48.72 8 ATOH 4062 OWβ UAT 16 41.297 31.972 30.043 1.0023.15 a ATOH 115 OU1 UAT 22 54.191 42.505 55.913 1.00 22.39 8 . AIOH 4063 OU9 UAT 16 60.104 21.780 53.887 1.0024.69 a ATOH 116 OW2 UAT 22 65.480 31.263 47.436 1.00 36.62 a AIOH 4064 OUO UAT 17 33.930 36.911 56.317 1.00 28.54 8 ATOH 117 OU3 UAT 22 30.283 47.935 54.169 1.00 31.71 a AIOH 4065 OW1 UAT 17 27.783 49.620 50.985 1.0021.73 8 ATOH 118 OU4 UAT 22 35.283 36.318 46.899 1.00 68.71 a AIOH 4066 OU2 WAT 17 38.322 12.309 23.483 1.0042.93 β ATOH 119 OW5 UAT 22 47.B71 46.056 38.969 1.00 32.78 a AIOH 4067 OU3 UAT 17 19.759 16.587 26.896 1.0025.91 8 ATOH 120 OU6 UAT 22 37.896 8.826 3.495 1.00 35.54 a ATOH 4068 OW4 WAT 17 18.392 24.561 •0.866 1.0045.44 a ATOH 121 OU7 UAT 22 35.101 B.628 38.130 1.00 35.44 β ATOH 4069 OW5 WAT 17 43.370 16.553 29.268 1.0024.28 8 ATOH 122 OUβ UAT 22 38.308 4.945 9.263 1.00 39.44 8 AIOH 4070 OW6 WAT 17 12.508 25.520 4.810 1.0039.21 8 ATOH 123 OW9 UAT 22 29.192 42.186 18.601 1.00 35.54 β AIOH 4071 OW7 WAT 17 44.009 35.4B4 9.586 1.0024.72 8 ATOH 124 OUO UAT 23 43.449 25.207 33.605 1.00 42.65 8 AIOH 4072 OW8 UAT 17 38.155 15.958 4.049 1.0027.73 8 AIOH 125 OU1 UAT 23 42.056 26.583 57.914 1.00 44.04 8 AIOH 4073 0U9 UAT 17 32.659 22.367 51.695 1.0036.96 8 ATOH 126 OU2 UAT 23 15.436 32.096 27.975 1.00 29.94 a AIOH 4074 OUO WAT 18 8.655 11.822 1B.5S1 1.0022.83 8 AIOH 127 OU3 UAT 23 40.123 43.268 18.152 1.00 37.43 AIOH 4075 OW1 WAT IB 61.442 16.332 49.671 1.0035 a .09 8 AIOH 128 OU4 UAT 23 14.301 18.529 21.331 1.00 32.32 8 AIOH 4076 OW2 WAT 18 52.691 20.468 49.830 1.0027.27 8 ATOH 129 OU5 UAT 23 41.316 39.786 58.213 1.00 42.06 8 AIOH 4077 OW3 WAT 18 33.981 29.452 4.620 1.0046.70 8 ATOH 130 OU6 UAT 23 28.167 15.941 46.987 1.00 39.62 8 AIOH 407B OW4 WAT IB 22.398 9.094 32.744 1.0031.90 8 ATOH 131 OU7 UAT 23 62.463 32.861 38.118 1.00 33.05 4079 OW5 WAT IB 8 AIOH 24.654 27.519 4.442 1.002637 8 ATOH 132 OWβ UAT 23 50.420 44.042 41.952 1.00 24.23 8 AIOH 4080 OW6 WAT 18 24.112 52.226 27.595 1.003843 a ATOH 133 OW9 UAT 23 30.486 6.686 18.716 1.00 37.32 AIOH 4081 OW7 WAT 18 33.663 55.271 29.435 8 1.0043 20 a ATOH 134 OUO UAT 24 39.000 11.315 44.273 1.00 38.40 8 ATOH 4135 OU1 UAT X 24 26.342 44.842 18.030 1.0027.39 B ATOH 4188 OW4 UAT X 29 33.246 35.860 58.555 1.0024.66 8 AIOH 4136 OU2 UAT X 24 42.233 42.967 22.516 1.0028.16 8 AIOH 4137 OU3 WAT X 24 17.859 41.857 40.950 1.0044.87 8 AIOH 4UB OU4 UAT X 24 18.774 45.302 34.094 1.0036.85 8 ATOH 4139 OU5 UAT X 24 17.379 48.385 29.218 1.0036.40 8 ATOH 4140 OU6 UAT X 24 59.859 17.628 38.947 1.0024.00 B - ATOH 4141 OU7 UAT X 24 44.716 26.845 15.361 1.0031.66 8 AIOH 4142 OUB UAT X 24 16.B51 22.367 25.144 1.0038.33 8 AIOH 4143 OW9 WAT X 24 44.428 18.344 31.454 1.0028.87 8 AIOH 4144 OWO WAT X 25 53.824 36.690 57.769 1.0027.33 8 ATOH 4145 OW1 WAT X 25 53.68B 40.328 57.339 1.0034.91 8 ATOH 4146 OW2 UAT X 25 46.373 15.118 12.832 1.0038.80 8 ATOH 4147 OU3 UAT X 25 29.409 35.711 7.581 1.0030.09 8 AT >H 14B OU4 UAT X 25 26.515 13.237 -3.213 1.0030.52 β l ». 4149 OU5 UAT X 25 20.273 3.147 6.130 1.0029.22 8 At 3H 4150 OU6 WAT X 25 34.514 42.011 19.633 1.0023.60 8 IT. I DM 4151 OW7 WAT X 25 41.463 52.238 24.622 1.0033.B3 8 C NIOH 4152 OUB UAT X 25 18.346 37.804 42.302 1.0035.93 8 00 AIOH 4153 OU9 WAT X 25 35.262 54.671 32.179 1.0058.94 8 «Λ AH*. 4154 OWO WAT X 26 44.229 16. 73 16.585 1.0037.25 8 ZJ ATOH 4155 OU1 WAT X 26 44.766 14.121 14.699 1.0046.53 8 —I ATOH 4156 OU2 UAI X 26 31.390 33.920 59.134 1.0033.03 B C AIOH 4157 OU3 WAT X 26 12.971 21.397 23.449 1.0037.99 8 H AIOH 4158 OW4 WAT X 26 41.259 51.310 51.509 1.0040.81 8 m AIOH 4159 OW5 WAT X 26 41.929 11.622 42.697 1.0045.17 8 *Λ ATOH 4160 OW6 WAT X 26 42.707 44.751 57.570 1.0042.32 8 ~~ ATOH 4161 OU7 UAT X 26 56.463 43.749 51.681 1.0036.66 8 ATOH 4162 OUB WAT X 26 24.821 11.342 -3.728 1.0033.27 8 3 AIOH 4163 0W9 WAT X 26 60.493 39.175 53.713 1.0047.98 8 __-__ AIOH 4164 OWO WAT X 27 45.625 38.306 11.910 1.0037.28 8 73 AIOH 4165 OW1 UAT X 27 43.801 49.874 24.898 1.0075.50 8 C AIOH 4166 OU2 UAT X 27 11.684 17.068 21.179 1.0034.01 8 J~ AIOH 4167 OU3 UAT X 27 28.216 2.149 14.807 1.0042.07 B *" AIOH 416B OU4 UAT X 27 52.604 30.867 37.880 1.0033.10 8 JjJ AIOH 4169 OU5 WAT X 27 55.458 34.651 38.180 1.0047.45 8 -Hi ATOH 4170 OU6 WAT X 27 49.808 19.B47 34.1B9 1.0033.89 8 AIOH 4171 OW7 UAT X 27 1.703 6.632 4.199 1.0062.B8 B AIOH 4172 OWβ WAT X 27 4B.275 39.555 43.586 1.0028. B 8 AIOH 4173 OW9 WAT X 27 23.075 20.226 -6.003 1.0061.62 8 ATOH 4174 OWO WAT X 28 38.679 43.247 57.111 1.0053.07 8 AIOH 4175 OW1 WAT X 2B 21.533 51.639 33.545 1.0049.86 8 AIOH 4176 OW2 WAT X 28 . 1.544 11.851 5.024 1.0069.29 8 AIOH 4177 OW3 WAT X 28 22.566 43.229 15.525 1.0028.33 8 AIOH 4178 OW4 WAT X 28 44.851 57.241 34.B59 1.0042.49 8 ATOH 4179 OW5 WAT X 28 33.378 9.541 42.581 1.0051.22 8 ATOH 4180 OW6 WAT X 28 27.186 6.024 -0.021 1.0046.35 8 AIOH 4181 OW7 WAT X 28 56.162 41.254 59.120 1.0056.59 8 ATOH 4182 OWβ WAT X 28 5.756 19.201 7.132 1.0020.05 8 ATOH 4183 OW9 WAT X 28 14.700 29.886 48.605 1.0035.67 8 AIOH 4184 OWO WAI X 29 41.585 56.275 32.373 1.0042.13 8 AIOH 4185 OW1 WAT X 29 24.084 49.694 43.922 1.0040.12 8 ATOH 4186 OU2 WAT X 29 29.979 22.421 2.045 1.0042.88 8 AIOH 4187 OU3 UAT X 29 18.885 13.752 26.566 1.0049.31 8 ) 9 ~i Z JJ 3 — i J ATOH 4347 OU5 UAT X 45 15.297 36.178 30.314 1.0041.94 8 ATOH 4400 OUO UAT 51 43.751 9.508 10.207 1.00 72.09 8 AIOH 4348 OU6 UAT X 45 11.948 34.622 19.560 1.0083.16 8 ATOH 4401 OU1 UAT 51 21.156 18.175 -5.366 1.00 59.15 β AIOH 4349 OWβ WAT X 45 49.746 24.BB7 60.391 1.0066.28 8 ATOH 4402 OU2 UAT 51 20.822 20.591 30.625 1.00 53.15 8 AIOH 4350 OW9 WAT X 45 36.657 55.115 28.131 1.0037.69 8 AIOH 4403 OU3 UAT 51 25.847 41.728 50.223 1.00 53.16 8 AIOH 4351 OWO WAT X 46 55.074 25.248 36.950 1.0041.36 8 ATOH 4404 OU4 UAT 51 42.406 49.560 54.444 1.00 49.42 8 AIOH 4352 OWl UAI X 46 47.652 23.423 22.484 1.0042.59 8 ATOH 4405 OW5 UAT 51 11.152 -0.096 4.529 1.00 73.12 8 AIOH 4353 OW2 WAT X 46 44.015 15.772 24.447 1.0047.57 B ATOH 4406 OU6 UAT 51 41.064 10.519 39.198 1.00 76.33 8 AloH 4354 OW3 WAI X 46 7.635 2.279 10.B56 1.0061.51 8 ATOH 4407 OW7 UAT 51 11.838 45.652 24.174 1.00 52.20 8 AloH 4355 OW4 WAT X 46 55.490 45.238 53.756 1.0080.18 8 ATOH 4408 OWβ UAT 51 24.803 8.502 38.134 1.00 48.46 8 AloH 4356 OW5 WAT X 46 24.651 30.369 3.824 1.0053.51 8 ATOH 4409 OU9 UAT 51 28.241 55.029 32.933 1.00 S6.B1 8 AIOH 4357 0U6 UAT X 46 36.564 25.795 58.795 1.0043.24 8 ATOH 4410 OUO UAT 52 24.326 46.042 48.362 1.00 42.89 B All.. 4358 OW7 WAT X 46 37.878 24.510 56.673 1.0060.23 8 AIOH 4411 OWl UAT 52 60.372 23.243 57.581 1.00 51.46 8 AloH 4359 OWβ WAI X 46 9.767 27.253 17.228 1.0044.01 8 ATOH 4412 OU2 UAT 52 44.063 13.149 3.195 1.00 73.23 8 Al'-H 4360 OW9 WAT X 46 33.066 7.229 37.529 1.0048.47 8 ATOH 4413 OU3 UAT 52 29.959 38.273 7.993 1.00 74.96 8 AI*VH 4361 OWO UAT X 47 8.243 21.706 21.929 1.0061.56 8 ATOH 4414 OU4 UAT 52 17.959 47.341 32.823 1.00 52.58 8 AI--H 4362 OWl UAT X 47 46.978 13.274 45.175 1.0040.90 8 ATOH 4415 OW5 UAT 52 35.761 36.887 7.808 1.00 46.76 a ( I -l.X. 4363 OW2 UAT X 47 41.004 12.753 21.561 1.0073.88 β ATOH 4416 OU6 UAT 52 29.185 14.140 50.554 1.00100.00 8 "OH 4364 OU4 UAT X 47 3.035 8.918 -0.355 1.0050.88 8 ATOH 4417 OU7 UAT 52 46.852 47.409 54.235 1.00 47.47 8 00 AIOH 4365 0U5 UAT X 47 18.537 34.248 10.555 1.0079.91 8 ATOH 4418 OU8 UAT 52 46.124 18.871 10.000 1.00 74.45 8 IΛ AIOH 4366 OU6 UAT X 47 26.233 6.791 -2.079 1.004B.58 8 ATOH 4419 OW9 UAT 52 43.467 42.127 14.225 1.00 58.70 8 j ATOH 4367 OW7 WAT X 47 37.312 53.735 22.566 1.0063.31 8 ATOH 4420 OWl UAT 53 42.354 10.824 26.570 1.00 74.16 a H AIOH 4368 OWβ WAI X 47 17.940 29.638 6.277 1.0057.32 8 ATOH 4421 OU2 UAT 53 41.382 9.160 28.416 1.00 65.06 8 C ATOH 4369 0W9 WAT X 47 26.830 27.316 2.717 1.0062.15 8 ATOH 4422 OU3 UAT 53 32.249 16.276 51.085 1.00 66.53 8 H AIOH 4370 OWO WAT X 48 65.931 28.577 46.176 1.0069.51 8 ATOH 4423 OW4 UAT 53 43.754 20.935 55.297 1.00 89.21 8 m AIOH 4371 OWl WAT X 48 19.661 45.120 40.540 1.0040.74 8 ATOH 4424 OW5 UAT 53 46.525 22.435 61.833 1.00 64.40 8 *Λ AIOH 4372 OW2 WAT X 48 10.667 22.744 23.628 1.0036.22 8 ATOH 4425 OU6 UAT 53 36.689 9.501 46.403 1.00 43.78 a ~~ AIOH 4373 OU3 UAT X 48 8.702 24.434 20.838 1.0051.66 8 AIOH 4426 OU7 UAT 53 13.785 14.234 21.394 1.00 46.49 a "J ATOH 4374 OU4 WAT X 48 35.773 26.533 56.343 1.0038.96 8 ATOH 4427 OU8 UAT 53 44.108 8.30B 6.121 1.00 74.38 a ~2 AIOH 4375 OW5 WAT X 48 38.218 2.333 13.072 1.0037.60 8 ATOH 4428 OU9 UAT 53 37.095 13.297 47.553 1.00 92.89 a ____, AIOH 4376 OU6 WAT X 48 25.061 48.128 50.748 1.0069.43 8 ATOH 4429 OUO UAT 54 60.222 38.361 56.675 1.00 71.18 a 73 ATOH 4377 OW7 WAT X 48 24.333 37.538 52.402 1.0033.69 8 ATOH 4430 OWl UAT 54 43.676 52.104 52.067 1.00 52.01 a C AIOH 4378 OWβ WAT X 48 52.741 13.029 46.552 1.0046.94 8 ATOH 4431 OU2 UAT 54 13.472 23.519 26.526 1.00 85.06 a ~~ AIOH 4379 OW9 WAT X 48 30.393 18.085 52.715 1.0073.77 8 ATOH 4432 OU3 UAT 54 26.573 48.774 55.241 1.00 63.24 a m AIOH 4380 OWO WAI X 49 21.293 35.987 52.496 1.0056.71 8 ATOH 4433 OW4 UAT 54 38.373 54.655 25.877 1.00 61.51 β N» AIOH 4381 OU1 UAT X 49 26.704 53.743 20.826 1.0082.73 B ATOH 4434 OW5 UAT 54 40.109 29.004 7.323 1.00 50.80 a 2i ATOH 4382 OW2 WAT X 49 65.451 38.921 50.670 1.0050.91 8 ATOH 4435 OU6 UAT 54 40.897 28.228 33.474 1.00 55.10 8 AIOH 4383 OW3 WAT X 49 9.019 18.103 21.967 1.0057.54 8 ATOH 4436 OWβ UAT 54 26.359 57.407 32.671 1.00 74.31 8 AIOH 4384 OW4 WAT X 49 43.689 31.759 26.580 1.0033.20 8 ATOH 4437 OW9 UAT 54 15.383 36.694 13.336 1.00 63.49 β AIOH 4385 OU5 WAT X 49 65.973 31.154 38.950 1.0051.21 8 ATOH 4438 OUO UAT 55 25.637 23.526 51.791 1.00 62.36 β AIOH 4386 OW6 WAT X 49 50.668 41.968 57.102 1.0065.20 8 ATOH 4439 OWl UAT 55 47.868 37.197 21.724 1.00 98.01 8 AIOH 4387 OW7 WAT X 49 67.466 32.81B 48.733 1.0035.55 8 ATOH 4440 OU2 UAT 55 48.664 28.592 20.875 1.00 61.42 8 AIOH 4388 OWβ WAT X 49 12.540 31.451 14.136 1.0067.07 8 ATOH 4441 OW3 UAT 55 22.182 11.543 42.550 1.00 50.93 8 AIOH 4389 OW9 WAT X 49 24.089 6.493 18.874 1.0041.89 8 ATOH 4442 OU4 UAT 55 14.290 33.767 23.519 1.00 43.45 8 AIOH 4390 OWO WAT X 50 46.352 12.360 48.271 1.0078.91 8 ATOH 4443 OU5 UAT 55 49.2S4 21.261 57.3BB 1.00 74.77 8 AIOH 4391 OWl WAT X 50 26.960 36.851 6.038 1.0044.57 8 ATOH 4444 OW6 UAT 55 32.072 50.437 56.442 1.00 84.60 8 ATOH 4392 OW2 WAT X 50 37.082 59.754 36.774 1.0066.16 8 ATOH 4445 OU7 UAT 55 6.861 26.47B 7.012 1.00 69.24 8 AIOH 4393 OW3 WAT X 50 57.220 36.380 35.486 1.0060.08 8 ATOH 4446 OUB UAT 55 36.069 6.771 2.277 1.00 89.64 8 AIOH 4394 OW4 WAT X 50 47.460 48.140 35.950 1.0051.89 8 ATOH 4447 OU9 UAT 55 60.239 29.387 37.677 1.00 64.46 AIOH 4395 OW5 WAT X 50 32.642 7.671 29.024 1.0062.58 8 8 ATOH 4448 OWl WAT 56 46.693 15.300 46.504 1.00 37.40 ATOH 4396 OW6 WAT X 50 40.89B 5.278 12.690 1.0058.65 8 8 ATOH 4449 OU2 UAT 56 47.685 47.802 26.981 ATOH 4397 OU7 WAT X 50 43.951 11.795 23.BOB 1.0051.02 8 1.00 44.40 8 ATOH 4450 OU3 UAT 56 21.472 47.007 15.910 1.00 70.01 8 AT H 4453 OU6 UAT 56 53.874 20.460 35.843 1.006027 B AIOH 4454 OU7 UAT 56 34.043 6.968 31.691 1.0054.01 a AIOH 4455 OU8 WAT 56 20.830 41.B35 12.224 1.0010000 a AIOH 4456 OW9 UAT 56 16.599 30.946 13.916 1.003738 8 AIOH 4457 OUO AI 57 44.358 21.696 24.084 1.0064 44 8 A 'H 4458 OWl UAT 57 9.7B8 43.318 30.716 1.0090 76 8 ATOH 4459 OU2 UAT 57 65.207 28.476 57.1B9 1.0072 19 8 - ATOH 4460 OW3 WAT 57 20.871 4.547 -1.268 1.0064.52 a ATOH 4461 OW5 WAT 57 24.856 36.282 6.866 1.0055 25 a ATOH 4462 OW7 UAI 57 65.931 24.875 58.247 1.004206 a AIOH 4463 OUB UAT 57 41.604 10.565 45.137 1.008093 8 ATOH 4464 OU9 UAT 57 30.736 44.603 54.453 1.005839 8 AI'JH 4465 OUO WAT 58 22.167 48.706 40.870 1.0052 19 8 Al W 4466 OWl WAT 58 66.082 25.557 51.546 1.0048.90 8 Al JH 4467 OW2 WAT 58 25.692 34.825 52.948 1.005059 8 AI3H 4468 OW3 WAT 58 26.160 51.696 48.736 1.0044 75 B IΛ c »' H 4469 OU4 UAT 58 56.334 43.153 40.380 1.005334 a AIOH 4470 OU5 UAT 58 30.990 17.627 55.917 1.0084.28 8 CD Λ AIOH 4471 0U6 UAT 58 45.287 39.941 7.939 1.0057.03 8 H ATOH 4472 OU7 UAT 58 3.405 18.650 9.230 1.00 73.95 8 19.752 55.578 1.0050.99 8 ~λ ATOH 4473 OUB UAT 58 54.294 C AIOH 4474 OU9 WAT 58 44.732 52.287 54.381 1.0075.96 a H ATOH 4475 OWO WAT 59 47.776 51.035 36.798 1.0053.81 a AIOH 4476 OWl WAT 59 29.391 47.450 56.869 1.0086.62 8 IΛ ATOH 4477 OU2 UAI 59 38.808 50.946 52.782 1.0047.24 β X ATOH 4478 OU3 UAT 59 20.090 10.595 -7.477 1.0069.34 8 AIOH 4479 OU4 UAT 59 30.700 10.315 45.674 1.0063..75 8 AIOH 4480 OU5 UAT 59 60.01B 46.795 44.900 1.0057,35 8 AIOH 4481 OU6 UAT 59 46.214 52.834 49.312 1.0067,99 8 73 AIOH 4482 OW7 UAT 59 56.880 28.891 60.457 1.0085.53 8 C ATOH 4483 OUB UAT 59 36.201 48.379 58.178 1.0071.18 8 ATOH 4484 OW9 UAT 59 35.313 2.318 16.129 1.0066.51 8 AIOH 4485 OUO WAT 60 34.944 58.828 34.422 0069.27 8 i AIOH 4486 OWl WAT 60 47.891 40.270 60.882 0062.61 8 σ> AIOH 4487 OW2 UAI 60 20.100 54.046 30.414 0091.37 8 ATOH 4488 OU3 WAT 60 0.66B 22.084 15.126 0045.99 8 AIOH 4489 OW4 WAT 60 50.911 50.933 54.227 00 71.78 8 AIOH 4490 OW5 WAT 60 50.514 44.42B 38.574 1.0067.41 8 ATOH 4491 OW6 WAT 60 31.208 54.171 26.648 1.0065.99 8 AIOH 4492 OW7 WAT 60 49.541 38.319 60.498 1.0049.78 8 AIOH 4493 OUB UAI 60 23.270 55.339 31.653 1.0066.17 B ATOH 4494 OW9 WAI 60 46.551 15.109 50.163 1.0087.28 8 AIOH 4495 OWO UAT 61 65.999 24.860 47.686 1.0057.42 8 AIOH 4496 OU1 WAT 61 30.573 36.197 57.967 1.0051.73 8 AIOH 4497 OU2 UAT 61 3.779 13.380 -2.503 1.0065.73 8 AIOH 4498 OU3 WAT 61 46.944 12.221 41.061 1.0039.29 8 ATOH 4499 OU5 WAT 61 64.745 25.656 43.289 1.0052.05 8 AIOH 4500 OW6 WAI 61 51.657 40.026 13.448 1.006871 8 AI H 4501 OW7 WAT 61 27.718 47.942 52.615 1.005481 8 AIOH 4502 OWβ WAT 61 24.460 41.243 12.842 1.006585 8 ATOH 4503 OU9 WAT 61 2.848 14.406 12.411 1.0061 94 8 AIOH 4504 OWO WAI 62 23.747 48.9B9 47.991 1.005502 8 AIOH 4505 OWl WAI 62 63.167 23.291 45.B41 1.0064.42 8 AIOH 4559 0U3 UAT X 70 ATOH 4612 OU2 UAT X 81 13.341 34.872 38.349 1.0064.64 8 AIOH 4560 0W4 WAI X 70 ATOH 4613 OU3 UAT X 81 51.626 42.754 59.455 1.0087.45 8 AIOH 4561 OW5 WAI X 70 ATOH 4614 OUS UAT X 81 17.748 40.786 43.576 1.00 81.62 8 AIOH 4562 OW8 UAT X 70 ATOH 4615 OU6 UAT X 81 40.981 31.297 32.687 1.00 92.90 8 AIOH 4563 OU2 UAT X 71 ATOH 4616 OU7 UAT X 81 36.339 42.304 57.906 1.00 54.44 8 AIOH 4564 OU3 UAT X 71 ATOH 4617 OUO UAT X 82 52.ISO 44.557 55.907 1.00 81.29 8 AIOH 4565 OU4 UAT X 71 ATOH 4618 OU1 UAT X 82 44.696 27.699 29.BOO 1.00 66.84 8 - ATOH 4566 0U6 UAT X 71 ATOH 4619 OU2 UAT X 82 15.369 42.073 36.641 1.00 87.69 8 AIOH 4567 OWl WAT X 72 ATOH 4620 OU4 UAT X 82 44.262 38.613 61.725 1.00 74.79 8 AIOH 4568 OW2 UAT X 72 ATOH 4621 OUS UAT X 82 10.887 37.555 22.160 1.00 77.71 8 AIOH 4569 OU3 UAT X 72 ATOH 4622 OW6 UAT X 82 57.317 26.895 38.482 1.00 54.04 B AIOH 4570 OUS UAT X 72 ATOH 4623 OU1 UAT X 83 1.4B5 10.546 14.639 1.00 49.60 8 AIOH 4571 OU6 WAT X 72 ATOH 4624 OU2 UAT X 83 44.383 11.585 44.954 1.00 69.75 8 AIOH 4572 OW2 WAT X 73 ATOH 4625 OU4 UAT X 83 13.091 19.080 23.540 1.00 84.10 8 Al H 4573 0W3 WAT X 73 ATOH 4626 OUS UAT X 83 49.664 18.609 50.424 1.00 79.36 8 AT XH 4574 OW4 WAT X 73 ATOH 4627 OU6 UAT X 83 -0.411 -0.186 6.219 1.00 73.91 8 IΛ AT )H 4575 OW7 WAT X 73 ATOH 4628 OU1 UAT X 84 -0.060 12.467 10.762 1.00 74.36 8 !θH 4576 W9 WAT X 73 ATOH 4629 OU3 UAT X 84 4S.916 18.172 53.625 1.00 82.88 8 00 AIOH 4577 OWO WAT X 74 ATOH 4630 OU4 UAT X 84 42.886 23.516 61.123 1.00 71.70 8 IΛ AIOH 4578 OU2 UAT X 74 ATOH 4631 OUS UAT X 84 26.711 5.741 19.232 1.00 65.61 8 ATOH 4579 OU3 WAT X 74 ATOH 4632 OU6 UAT X 84 18.341 21.188 47.071 1.00 79.82 8 ATOH 4580 OW4 WAT X 74 ATOH 4633 OUB UAT X 84 30.324 37.244 55.283 1.00 63.21 8 c ATOH 4581 OW5 WAT X 74 ATOH 4634 OW9 UAT X 84 4S.383 21.54S 29.439 1.00 65.08 8 Hm ATOH 4582 OU6 UAT X 74 ATOH 4635 OU1 UAT X 85 47.617 21.423 28.329 1.00 72.90 8 ATOH 4583 OUB UAT X 74 ATOH 4636 OU2 UAT X 85 14.724 8.133 -4.054 1.00 80.41 8 IΛ AIOH 4584 OU2 UAT X 75 ATOH 4637 OU4 UAT X BS 14.404 3B.900 34.440 1.00 73.60 8 X AIOH 4585 OW5 WAI X 75 ATOH 4638 OU5 UAT X 85 30.311 39.411 S6.032 1.00 72.07 8 AIOH 4586 OW6 UAT X 75 ATOH 4639 OU1 UAT X 86 38.750 51.931 56.443 1.00 83.88 8 AIOH 45B7 OU2 WAT X 76 ATOH 4640 OU2 UAT X 86 28.737 50.755 56.620 T.00 78.91 8 AIOH 4588 OW3 WAT X 76 ATOH 4641 OU3 UAT X 86 38.447 9.203 1.111 1.00 60.02 8 73 AIOH 4589 OW5 WAT X 76 ATOH 4642 OU4 UAT X 86 63.955 18.750 55.290 1.00 75.30 B C AIOH 4590 OW9 WAT X 76 ATOH 4643 OUS UAT X 86 28.437 41.43S 56.329 1.00 77.99 a AIOH 4591 OW2 WAT X 77 ATOH 4644 OW6 UAT X 86 27.951 49.707 19.814 1.00 80.66 8 AIOH 4592 OU3 UAT X 77 ATOH 4645 OW7 UAT X 86 33.978 8.299 40.249 1.00 69.22 8 hi AIOH 4593 OU4 UAI X 77 σ. ATOH 4646 OW9 UAT X 86 17.498 1.498 10.616 1.00 71.37 8 AIOH 4594 OU5 UAT X 77 ATOH 4647 OWl UAT X B7 1.278 IS.798 6.438 1.00 70.87 8 AIOH 4595 OW6 WAT X 77 ATOH 4648 OU3 UAI X 87 37.174 55.549 52.513 1.00 69.91 a AIOH 4596 OU7 WAT X 77 ATOH 4649 OU4 UAT X 87 68.146 21.047 55.397 1.00 70.79 a ATOH 4597 OW2 WAT X 78 ATOH 4650 OUS UAT X 87 24.65S S2.S48 24.459 1.00 72.31 a AIOH 4598 OW3 WAT X 78 ATOH 4651 OW6 UAT X 87 46.009 24.086 33.287 1.00 79.02 a AIOH 4599 OU4 UAT X 78 ATOH 46S2 OW9 UAT X 87 S0.19S 14.529 36.835 1.00 6S.1S a ATOH 4600 OU6 UAT X 7B ATOH 46S3 OU2 UAT X 88 29.201 3.240 -2.272 1.00 78.74 8 ATOH 4601 OU2 WAT X 79 ATOH 4654 OU3 UAT X 88 13.357 32.036 24.857 1.00 62.05 8 AIOH 4602 OW3 WAT X 79 AIOH 465S OU4 UAT X 88 65.406 20.886 50.995 1.00 76.49 8 AIOH 4603 OU4 WAT X 79 ATOH 46S6 OUS UAT X ββ 20.515 8.228 19.759 1.00 73.9B 8 AIOH 4604 OW5 WAT X 79 ATOH 4657 OU6 UAT X 88 46.758 18.587 30.455 1.00 74.75 8 AIOH 4605 OW6 WAT X 79 ATOH 4658 OU2 UAT X 89 49.679 43.124 20.824 1.00 BO.84 8 AIOH 4606 OU2 WAT X 80 ATOH 4659 OU3 UAT X 89 60.303 44.435 40.737 1.00 70.62 AIOH 4607 OW3 WAI X 80 8 ATOH 4660 OU4 UAT X 89 13.240 -1.159 9.184 1.00 78.53 AIOH 4608 OW4 WAT X 80 8 ATOH 4661 OUS UAT X 89 61.700 19.538 53.061 ATOH 4609 OW6 WAT X 80 1.00 64.93 8 ATOH 4662 OU6 UAT X 89 24.291 28.301 0.472 AIOH 4610 OW8 WAT X 80 1.00 69.68 8 ATOH 4663 OUO UAT X 90 27.964 24.098 IOH 4611 OU1 WAT X 81 -2.600 1.00 64.61 8 ATO

Claims: CLAIMS 1. A method of constructing a variant of a parent Termamyl-lik α-amylase, which variant has α-amylase activity and at leas one altered property as compared to said parent α-amylase which method comprises i) analysing the structure of the parent Termamyl-like α a ylase to identify at least one amino acid residue or at leas one structural part of the Termamyl-like α-amylase structure which amino acid residue or structural part is believed to b of relevance for altering said property of the parent Termamyl like α-amylase (as evaluated on the basis of structural o functional considerations) , ii) constructing a Termamyl-like α-amylase variant, which a compared to the parent Termamyl-like α-amylase, has bee modified in the amino acid residue or structural par identified in i) so as to alter said property, and iii) testing the resulting Termamyl-like α-amylase variant fo said property. 2. The method according to claim 1, wherein the property to b altered is selected from the group consisting of substrat specificity, substrate binding, substrate cleavage pattern, temperature stability, pH dependent activity, pH dependent stability (especially increased stability at low (e.g. pH<6) o high (e.g. pH>9) pH values), stability towards oxidation, Ca 2* - dependency and specific activity. 3. The method according to claim 1 or 2, wherein the propert to be altered is the calcium ion dependency and the structural part to be modified is selected from the group consisting of the C domain, the interface between the A and B domain, the interface between the A and C domain, or the interaction to a calcium binding site of the Termamyl-like α-amylase. 4. The method according to claim 1 or 2, wherein the property to be altered is the substrate cleavage pattern and the structural part to be modified is located within 10A from an amino acid residue of the substrate binding site. 5. A method of constructing a variant of a parent Termamyl-like α-amylase, which variant has α-amylase activity and one or more altered properties as compared to said parent α-amylase, which method comprises i) comparing the three-dimensional structure of the Termamyl- like α-amylase with the structure of a non-Termamyl-like α- amylase, ii) identifying a part of the Termamyl-like α-amylase structure which is different from the non-Termamyl-like α-amylase structure and which from structural or functional considerations is contemplated to be responsible for differences in one or more properties of the Termamyl-like and non-Termamyl-like α-amylase, and iii) modifying the part of the Termamyl-like α-amylase identified in ii) whereby a Termamyl-like α-amylase variant is obtained, one or more properties of which differ from the parent Termamyl-like α-amylase. 6. The method according to claim 6, wherein, in step iii), the part of the Termamyl-like α-amylase is modified so as to ressemble the corresponding part of the non-Termamyl-like α- amylase. 7. The method according to claim 5 or 6, wherein, in step iii) , the modification is accomplished by deleting one or more amino acid residues of the part of the Termamyl-like α-amylase to be modified; by replacing one or more amino acid residues of the part of the Termamyl-like α-amylase to be modified with the amino acid residues occupying corresponding positions in the non-Termamyl-like α-amylase; or by insertion of one or more amino acid residues present in the non-Termamyl-like α-amylase into a corresponding position in the Termamyl-like α-amylase. 8. The method according to any of claims 5-7, wherein the no Termamyl-like α-amylase structure is the structure of a fung α-amylase or a mammalian α-amylase. s 9. The method according to claim 8, wherein the non-Termamy like α-amylase is the Aεpergilluε oryzae TAKA α-amylase, the niger acid α-amylase, the Bacilluε εubtiliε α-amylase or t pig pancreatic α-amylase. 10 10. The method according to any of claims 1-9, wherein t parent Termamyl-like α-amylase is derived from a strain Bacillus . 11. The method according to claim 10, wherein the parent 15 amylase is derived from a strain of a B. licheniformiε , B . am loliquefacienε, B . stearothermophilus or a strain from alkalophilic Bacillus sp. such as NCIB 12289, NCIB 12512 NCIB 12513. 20 12. The method according to any of claims 1-11, wherein t parent α-amylase is a hybrid α-amylase comprising a combinati of partial amino acid sequences derived from at least t α-amylases, of which one is a Termamyl-like α-amylase and t other(s) are, e.g., from a microbial and/or a mammalian 25 amylase. 13. The method according to any of claims 5-12, wherein t part of the parent Termamyl-like α-amylase to be modified a identified in step ii) is loop 1, loop 2, loop 3 and/or loop 30 of the parent α-amylase. 13. A method of constructing a variant of a parent Termamy like α-amylase, which has a decreased calcium ion dependency compared to said parent, which method comprises: 35 i) identifying an amino acid residue within lOA from a Ca bin d ing site of a Termamyl-like α-amylase in a model of t t hree-dimensional structure of said α-amylase, which fr structural or functional considerations is believed to be responsible for a non-optimal calcium ion interaction, ii) constructing a variant in which said amino acid residue is replaced with another amino acid residue which from structural 5 or functional considerations is believed to be important for establishing a higher Ca 2 * binding affinity, and iii) testing the Ca 2+ dependency of the resulting Termamyl-like α-amylase variant. 10 14. A method of constructing a variant of a parent Termamyl- like α-amylase which variant has α-amylase activity and an altered pH dependent activity, which method comprises i) in a three-dimensional structure of the Termamyl-like α- 15 amylase in question, identifying an amino acid residue within 15A from an active site residue, in particular 10A from an active site residue, which amino acid residue is contemplated to be involved in electrostatic or hydrophobic interactions with an active site residue, 20 ii) replacing, 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 accomodation of the amino acid residue in the 25 structure, iii) optionally repeating step i) and/or ii) until an amino acid replacement has been identified which is accomodated into the structure, 30 iv) constructing a Termamyl-like α-amylase variant resulting from steps i) , ii) and optionally iii) and testing the pH dependent activity of said variant. 35 15. A method of increasing the thermostability and/or altering the temperature optimum of a parent Termamyl-like α-amylase, which method comprises i) identifying an internal hole or a crevice of the paren Termamyl-like α-amylase in the three-dimensional structure o said α-amylase, ii) replacing, in the structure, one or more amino aci residues in the neighbourhood of the hole or crevice identifie in i) with another amino acid residue which from structural o functional considerations is believed to increase th hydrophobic interaction and to fill out or reduce the size o the hole or crevice, iii) constructing a Termamyl-like α-amylase variant resultin from step ii) and testing the thermostability and/o temperature optimum of the variant. 16. A method of constructing a variant of a Termamyl-like α amylase which has a reduced ability to cleave a substrate clos to the branching point, which method comprises i) identifying the substrate binding area of the paren Termamyl-like α-amylase in a model of the three-dimensiona structure of said α-amylase, ii) replacing, in the model, one or more amino acid residues o the substrate binding area of the cleft identified in i) , whic is/are believed to be responsible for the cleavage pattern o the parent α-amylase, with another amino acid residue whic from structural considerations is believed to result in a altered substrate cleavage pattern, or deleting one or mor amino acid residues of the substrate binding area contemplate to introduce favourable interactions to the substrate or addin one or more amino acid residues to the substrate binding area contemplated to introduce favourable interactions to the substrate, and iii) constructing a Termamyl-like α-amylase variant resultin from step ii) and testing the substrate cleavage pattern of the variant. 17. The method according to any of the preceeding claims, in which the α-amylase variant is obtained 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. 5 18. A variant of a parent Termamyl-like α-amylase, in which variant at least one amino acid residue of the parent α- amylase, which is/are present in a fragment corresponding to the amino acid fragment 44-57 of the amino acid sequence of SEQ 10 ID No. 4, has been deleted or replaced with one or more amino acid residues which is/are present in a fragment corresponding to the amino acid fragment 66-84 of the amino acid sequence shown in SEQ ID No. 10, or in which one or more additional amino acid residues has been added using the relevant part of is SEQ ID No. 10 or a corresponding part of another Fungamyl-like α-amylase as a template. 19. A variant of a parent Termamyl-like α-amylase, which variant has a region which, when the amino acid sequence of 20 variant is aligned most closely with the amino acid sequence of the said parent α-amylase, occupies the same position as the portion from residue X to residue Y of SEQ ID No 4, the said region having at least 80% sequence homology with the part of SEQ ID No 10 extending from residue Z to residue V of SEQ ID No 25 10, wherein X is the amino acid residue occupying position 44, 45, 46, 47 or 48 of SEQ ID No. 4, Y is the amino acid residue occupying position 51, 52, 53, 54, 55, 56 or 57 of SEQ ID No. 4, 30 Z is the amino acid residue occupying position 66, 67, 68, 69 or 70 of SEQ ID No. 10, and V is the amino acid residue occupying position 78, 79, 80, 81, 82, 83 or 84 of SEQ ID No. 10. 35 20. The variant according to claim 18 or 19, wherein X is the amino acid residue occupying position 48 and Y the amino acid residue occupying position 51 of SEQ ID NO 4 and Z is the amino acid residue occupying position 70 and V the amino acid residu occupying position 78 in SEQ ID No 10. 21. A variant of a parent Termamyl-like α-amylase, in whic 5 variant at least one of the amino acid residues of the paren α-amylase, which is/are present in an amino acid fragmen corresponding to the amino acid fragment 195-202 of the amin acid sequence of SEQ ID No. 4, has been deleted or replace with one or more of the amino acid residues which is/ar 0 present in an amino acid fragment corresponding to the amin acid fragment 165-177 of the amino acid sequence shown in SE ID No. 10, or in which one or more additional amino aci residues has been added using the relevant part of SEQ ID No. 10 or a corresponding part of another Fungamyl-like α-amylas s as a template. 22. A variant of a parent Termamyl-like α-amylase, which variant has a region which, when the amino acid sequence of variant is aligned most closely with the amino acid sequence of 0 the said parent α-amylase, occupies the same position as the portion from residue X to residue Y of SEQ ID No 4, the said region having at least 80%, such as 90% sequence homology with the part of SEQ ID No 10 extending from residue Z to residue V of SEQ ID No 10, wherein 25 X is the amino acid occupying position 195 or 196 of SEQ ID No. 4, Y is the amino acid residue occupying position 198, 199, 200, 201, or 202 of SEQ ID No. 4, 30 Z is the amino acid residue occupying position 165 or 166 of SEQ ID No. 10, and V is the amino acid residue occupying position 173, 174, 175, 35 176 or 177 of SEQ ID No. 10. 2 3 . The variant according to claim 21 or 22, in which the amino acid fragment ~- the parent α-amylase, which corresponds to amino acid residues 196-198 of SEQ ID No. 4, has been replaced with the amino acid fragment corresponding to amino acid residues 166-173 of the amino acid sequence shown in SEQ ID No. 10. 24. A variant of a parent Termamyl-like α-amylase, in which variant at least one of the amino acid residues of the parent α-amylase, which is/are present in a fragment corresponding to the amino acid fragment 117-185 of the amino acid sequence of SEQ ID No. 4, has/have been deleted or replaced with one or more of the amino acid residues, which is/are present in an amino acid fragment corresponding to the amino acid fragment 98-210 of the amino acid sequence shown in SEQ ID No. 10, or in which one or more additional amino acid residues has been added using the relevant part of SEQ ID No. 10 or a corresponding part of another Fungamyl-like α-amylase as a template. 25. A variant of a parent Termamyl-like α-amylase, which variant has a region which, when the amino acid sequence of variant is aligned most closely with the amino acid sequence of the said parent α-amylase, occupies the same position as the portion from residue X to residue Y of SEQ ID No 4, the said region having at least 80%, such as at least 90% sequence homology with the part of SEQ ID No 10 extending from residue Z to residue V of SEQ ID No 10, wherein X is the amino acid occupying position 117, 118, 119, 120 or 121 of SEQ ID No. 4, Y is the amino acid occupying position 181, 182, 183, 184 or 185 of SEQ ID No. 4, Z is the amino acid occupying position 98, 99, 100, 101, 102 of SEQ ID No. 10, and V is the amino acid occupying position 206, 207, 208, 209 or 210 of SEQ ID No. 10. 26. The variant according to claim 24 or 25, in which an ami acid fragment of the parent α-amylase, which corresponds amino acid residues 121-181 of SEQ ID No. 4, has been replac with the amino acid fragment corresponding to amino ac residues 102-206 of the amino acid sequence shown in SEQ ID N 10. 27. A variant of a parent Termamyl-like α-amylase, in whi variant at least one of the amino acid residues of the pare α-amylase, which is/are present in a fragment corresponding the amino acid fragment 117-181 of the amino acid sequence SEQ ID No. 4, has/have been deleted or replaced with one more of the amino acid residues, which is/are present in amino acid fragment corresponding to the amino acid fragme to 98-206 of the amino acid sequence shown in SEQ ID No. 1 or in which one or more additional amino acid residues has be added using the relevant part of SEQ ID No. 10 or corresponding part of another Fungamyl-like α-amylase as template. 28. A variant of a parent Termamyl-like α-amylase, whi variant has a region which, when the amino acid sequence variant is aligned most closely with the amino acid sequence the said parent α-amylase, occupies the same position as t portion from residue X to residue Y of SEQ ID No 4, the sai region having at least 80%, such as at least 90% sequenc homology with the part of SEQ ID No 10 extending from resid Z to residue V of SEQ ID No 10, wherein X is the amino acid occupying position 117, 118, 119, 120 121 of SEQ ID No. 4, Y is the amino acid occupying position 174, 175, 176 or 177 o SEQ ID No. 4, Z is the amino acid occupying position 98, 99, 100, 101, 102 o SEQ ID No. 10, and V is the amino acid occupying position 199, 200, 201 or 202 of SEQ ID No. 10. 29. The variant according to claim 27 or 28, in which the amino acid fragment of the parent α-amylase, which corresponds to amino acid residues 121-174 of SEQ ID No. 4, has been replaced with the amino acid fragment corresponding to amino acid residues 102-199 of the amino acid sequence shown in SEQ ID No. 10. 30. A variant of a parent Termamyl-like α-amylase, in which variant at least one of the amino acid residues of the parent α-amylase, which is/are present in an amino acid fragment corresponding to the amino acid fragment 12-19 of the amino acid sequence of SEQ ID No. 4, has/have been deleted or replaced with one or more of the amino acid residues, which is/are present in an amino acid fragment which corresponds to the amino acid fragment 28-42 of SEQ ID No. 10, or in which one or more additional amino acid residues has/have been inserted using the relevant part of SEQ ID No. 10 or a corresponding part of another Fungamyl-like α-amylase as a template. 31. A variant of a parent Termamyl-like α-amylase, which variant has a region which, when the amino acid sequence of variant is aligned most closely with the amino acid sequence of the said parent α-amylase, occupies the same position as the portion from residue X to residue Y of SEQ ID No 4, the said region having at least 80%, such as at least 90% sequence homology with the part of SEQ ID No 10 extending from residue Z to residue V of SEQ ID No 10, wherein X is the amino acid occupying position 12, 13 or 14 of SEQ ID No. 4, V is the amino acid occupying position 15, 16, 17, 18 or 19 of SEQ ID No. 4, Z is the amino acid occupying position 28, 29, 30, 31 or 32 of SEQ ID No. 10, and V is an amino acid residue corresponding to the amino acid occupying position 38, 39, 40, 41 or 42 of SEQ ID No. 10. 32. The variant according to claim 30 or 31, in which the ami acid fragment of the parent α-amylase, which corresponds amino acid residues 14-15 of SEQ ID No. 4, has been replac with the amino acid fragment corresponding to amino ac 5 residues 32-38 of the amino acid sequence shown in SEQ ID N 10. 33. A variant of a parent Termamyl-like α-amylase, in whic variant at least one of the amino acid residues of the paren 10 α-amylase, which is present in a fragment corresponding t amino acid residues 7-23 of the amino acid sequence of SEQ I No. 4, has/have been deleted or replaced with one or more amin acid residues, which is/are present in an amino acid fragmen corresponding to amino acid residues 13-45 of the amino aci is sequence shown in SEQ ID No. 10, or or in which one or mor additional amino acid residues has/have been inserted using th relevant part of SEQ ID No. 10 or a corresponding part o another Fungamyl-like α-amylase as a template. 20 34. A variant of a parent Termamyl-like α-amylase, whic variant has a region which, when the amino acid sequence o variant is aligned most closely with the amino acid sequence o the said parent α-amylase, occupies the same position as th portion from residue X to residue Y of SEQ ID No 4, the sai 25 region having at least 80%, such as at least 90% sequenc homology with the part of SEQ ID No 10 extending from residu Z to residue V of SEQ ID No 10, wherein X is the amino acid occupying position 7 or 8 of SEQ ID No. 4 30 Y is the amino acid occupying position 18, 19, 20, 21, 22 or 2 of SEQ ID No. 4, Z is the amino acid occupying position 13 or 14 of SEQ ID No 10, and 35 V is the amino acid occupying position 40, 41, 42, 43, 44 or 4 of SEQ ID No. 10. 35. The variant according to claim 33 or 34, in which the amino acid fragment of the parent α-amylase, which corresponds to amino acid residues 8-18 of SEQ ID No. 4, has been replaced with the amino acid fragment corresponding to amino acid 5 residues 14-40 of the amino acid sequence shown in SEQ ID No. 10. 36. A variant of a parent Termamyl-like α-amylase, in which variant at least one of the amino acid residues of the parent 10 α-amylase, which is present in a fragment corresponding to amino acid residues 322-346 of the amino acid sequence of SEQ ID No. 2, has/have been deleted or replaced with one or more amino acid residues, which is/are present in an amino acid fragment corresponding to amino acid residues 291-313 of the is amino acid sequence shown in SEQ ID No. 10, or or in which one or more additional amino acid residues has/have been inserted using the relevant part of SEQ ID No. 10 or a corresponding part of another Fungamyl-like α-amylase as a template. 20 37. A variant of a parent Termamyl-like α-amylase, which variant has a region which, when the amino acid sequence of variant is aligned most closely with the amino acid sequence of the said parent α-amylase, occupies the same position as the portion from residue X to residue Y of SEQ ID No 2, the said 25 region having at least 80% sequence homology with the part of SEQ ID No 10 extending from residue Z to residue V of SEQ ID No 10, wherein X is the amino acid occupying position 322, 323, 324 or 325 of SEQ ID No. 2, 30 Y is the amino acid occupying position 343, 344, 345 or 346 of SEQ ID No. 2, Z is the amino acid occupying position 291, 292, 293 or 294 of 35 SEQ ID No. 10, and V is the amino acid occupying position 310, 311, 312 or 313 of SEQ ID No. 10. 38. The variant according to claim 36 or 37, in which the ami acid fragment of the parent α-amylase, which corresponds amino acid residues 325-345 of SEQ D No. 2, has been replac with the amino acid fragment corresponding to amino ac residues 294-313 of the amino acid sequence shown in SEQ ID N 10. 39. A variant of a parent Fungamyl-like α-amylase, in whi variant at least one of the amino acid residues of the pare α-amylase, which is/are present in an amino acid fragme corresponding to amino acid residues 291-313 of the amino ac sequence of SEQ ID No. 10, has/have been deleted or replac with one or more of the amino acid residues, which is/a present in an amino acid fragment corresponding to amino ac residues 98-210 of the amino acid sequence shown in SEQ ID N 4, or in which one or more additional amino acid residu has/have been inserted using the relevant part of SEQ ID No. or a corresponding part of another Termamyl-like α-amylase a template. 40. A variant of a parent Fungamyl-like α-amylase, whi variant has a region which, when the amino acid sequence variant is aligned most closely with the amino acid sequence the said parent α-amylase, occupies the same position as t portion from residue X to residue Y of SEQ ID No 10, the sa region having at least 80%, such as at least 90% sequen homology with the part of SEQ ID No 10 extending from resid Z to residue V of SEQ ID No 4, wherein X is the amino acid occupying position 117, 118, 119, 120 121 of SEQ ID No. 10, Y is the amino acid occupying position 181, 182, 183, 184 185 of SEQ ID No. 10, Z is the amino acid occupying position 98, 99, 100, 101 or 10 of SEQ ID No. 4, and V is the amino acid occupying position 206, 207, 208, 209 or 210 of SEQ ID No. 4. 41. The variant according to claim 39 or 40, in which the amino 5 acid fragment of the parent α-amylase, which corresponds to amino acid residues 121-181 of SEQ ID No. 10, has been replaced with the amino acid fragment corresponding to amino acid residues 102-206 of the amino acid sequence shown in SEQ ID No. 4. 10 42. A variant according to any of claims 39-41, in which the the amino acid fragment of the parent α-amylase, which corresponds to amino acid residues 121-174 of SEQ ID No. 10, has been replaced with the amino acid fragment corresponding to is amino acid residues 102-199 of the amino acid sequence shown in SEQ ID No. 4. 43. A variant of a parent Fungamyl-like α-amylase, in which an amino acid fragment corresponding to amino acid residues 181- 20 184 of the amino acid sequence shown in SEQ ID No. 10 has been deleted. 45. A variant of a parent Termamyl-like α-amylase, which exhibits α-amylase activity and which has a decreased Ca 2* 25 dependency as compared to the parent α-amylase. 46. A variant according to claim 45, which comprises a mutation in a position corresponding to at least one of the following positions in SEQ ID NO 2: 30 N104, A349, 1479, L346, 1430, N457, K385, F350, 1411, H408 or G303, in particular a mutation corrsponding to N104D; A349C+I479C; L346C+I430C; 35 N457D,E; N457D,E+K385R; F350D,E+I430R,K; F350D,E+I411R,K; H408Q, E, N, D; and/or G303N, D , Q , E . 47. A variant of a parent Termamyl-like α-amylase which 5 exhibits a higher activity below the pH optimum than the parent α-amylase, which variant comprises a mutation of an amino acid residue corresponding to at least one of the following positions of the B. licheniformiε α-amylase (SEQ ID NO 2) : E336, Q333, P331, 1236, V102, A232, 1103, L196, in particular o at least one of the following mutations: E336R,K; Q333R,K; P331R,K; V102R,K,A,T,S,G; I236K,R,N; 5 I103K,R; L196K,R; and/or A232T,S,G. 48. A variant of a parent Termamyl-like α-amylase which 20 exhibits a higher activity above the pH optimum than the parent α-amylase, which variant comprises a mutation of an amino acid residue corresponding to at least one of the following positions of the B. licheniformiε α-amylase (SEQ ID NO 2) : N236, H281 and/or Y273, in particular one of the follwoing 25 mutations: N326I,Y,F,L,V; H281F,I,L; and/or Y273F,W. 30 49. A variant of a parent Termamyl-like α-amylase which exhibits α-amylase activity and which has an increased thermostability and/or altered temperature optimum as compared to the parent α-amylase, which variant comprises a mutation of an amino acid residue corresponding to at least one of the 35 following positions of the B . licheniformis α-amylase (SEQ ID NO 2) : L61, Y62, F67, K106, G145, 1212, S151, R214, Y150, F143, R146, L241, 1236, L7, V259, F284, F350, F343, L427 and/or V481, in particular at least one of the following mutations : L61W,V,F; Y62W; F67W; K106R,F,W; G145F,W I212F,L,W,Y,R,K; S151 replaced with any other amino acid residue and in particular with F,W,I or L; R214W; Y150R,K; F143W; R146W; L241I,F,Y,W; I236L,F,W,Y; L7F,I,W; V259F,I,L; F284W; F350W; F343W; L427F,L,W; and/or V481,F,I,L,W. 50. A variant of a parent Termamyl-like α-amylase, which exhibits α-amylase activity and which has a reduced capability of cleaving an oligo-saccharide substrate close to the branching point as compared to the parent α-amylase, which variant comprises a mutation of an amino acid residue corresponding to at least one of the following positions of the B . licheniformis α-amylase (SEQ ID NO 2) : V54, D53, Y56, Q333 and/or G57, in particular at least one of the following mutations: V54L,I,F,Y,W,R,K,H,E,Q; D53L,I,F,Y,W; Y,56 ; Q333W; and/or G57 to all possible amino acid residues. 51. The variant according to any of claims 17-50, wherein o 5 or more proline residues present in the amino acid residu with which the parent α-amylase is modified are replaced wi a non-proline residue such as alanine. 52. The variant according to any of claims 17-51, wherein o 10 or more cysteine residues present in the amino acid residu with which the parent α-amylase is modified are replaced wi a non-cysteine residue such as alanine. 53. A DNA construct comprising a DNA sequence encoding an α 15 amylase variant according to any of claims 17-52. 54. A recombinant expression vector which carries a DNA con struct according to Claim 53. 20 55. A cell which is transformed with a DNA construct accordin to Claim 53 or a vector according to Claim 54. 56. A cell according to Claim 55, which is a microorganism. 25 57. A cell according to Claim 56, which is a bacterium or fungus. 58. The cell according to Claim 57, which is a grampositiv bacterium such as Bacilluε εubtiliε, Bacilluε licheniformiε 30 Bacilluε lentuε, Bacilluε breviε, Bacilluε εtearothermophiluε Bacilluε alkalophiluε , Bacilluε amyloliquefacienε , Bacillu coagulans , Bacilluε circulanε, Bacilluε lautus or Bacillus thu ringiensis . 35 59. Use of an α-amylase variant according to any of claims 17 52 for washing and/or dishwashing. 60. Use of an α-amylase variant according to any of claims 17- 52 for desizing. 61. Use of an α-amylase variant according to any of claims 17- 5 52 for starch liquefaction. 62. A detergent additive comprising an α-amylase variant accor¬ ding to any of claims 17-52, optionally in the form of a non- dusting granulate, stabilised liquid or protected enzyme. 10 63. A detergent additive according to Claim 62 which contains 0.02-200 mg of enzyme protein/g of the additive. 64. A detergent additive according to Claim 62 or 63, which is additionally comprises another enzyme such as a protease, a lipase, a peroxidase, another amylolytic enzyme and/or a cellulase. 65. A detergent composition comprising an α-amylase variant ac- 20 cording to any of claims 17-52. 66. A detergent composition according to Claim 65 which addi¬ tionally comprises another enzyme such as a protease, a lipase, a peroxidase, another, amylolytic enzyme and/or a cellulase. 25 67. A manual or automatic dishwashing detergent composition comprising an α-amylase variant according to any of claims 17- 52. 30 68. A dishwashing detergent composition according to Claim 67 which additionally comprises another enzyme such as a protease, a lipase, a peroxidase, another amylolytic enzyme and/or a cellulase. 35 69. A manual or automatic laundry washing composition comprising an α-amylase variant according to any of claims 17- 52. 70. A laundry washing composition according to Claim 69, whic additionally comprises another enzyme such as a protease, lipase, a peroxidase, an amylolytic enzyme and/or a cellulase

Inventors: BISGAARD-FRANTZEN HENRIK, BORCHERT TORBEN VEDEL, SVENDSEN ALLAN, BISGAARD-FRANTZEN, HENRIK, BORCHERT, TORBEN, VEDEL, SVENDSEN, ALLAN
Applicants: BISGAARD FRANTZEN HENRIK, BORCHERT TORBEN VEDEL, NOVONORDISK AS, SVENDSEN ALLAN, BISGAARD-FRANTZEN, HENRIK, BORCHERT, TORBEN, VEDEL, NOVO NORDISK A/S, SVENDSEN, ALLAN
Application year: 1996
Main classification: C12N9
IPC codes: C11D3, C12N1, C12N9, C12N15, C12R1