EP1047785A1 - Modified deacetoxycephalosporin c synthase (daocs) and x-ray structure - Google Patents

Abstract

Three-dimensional crystal structure(s) of deacetoxycephalosporin C synthase (DAOCS) are described. The X-ray co-ordinates provide precise 3-dimensional information of amino acids within the structure of DAOCS. Some of these are in complexes with iron and/or substrates. Information from the structures is used to modify enzymes of the cephalosporin biosynthesis pathway including DAOCS, deacetylcephalosporin C synthase DAOC/DACS, such that they accept unnatural substrates (e.g. penicillins G, V) in order to improve the production of beta-lactam antibiotics. The structures may be used to predict the structures of other 2-oxoglutarate dependent enzymes, thereby allowing the design of inhibitors, and new catalysts for the production of e.g. oxidised amino acids/peptides. Specific modifications of amino acid residues are proposed and exemplified.

Description

MODIFIED DEACETOXYCEPHALOSPORIN C SYNTHASE (DAOCS) AND X-RAY STRUCTURE

Penicillin and cephalosporin antibiotics are produced either directly by fermentation or by modification of fermentation derived materials containing a beta-lactam ring. The biosynthetic pathway to the penicillins and cephalosporins has been extensively studied and reviewed (J. E. Baldwin and C. J. Schofield, in 'The Chemistry of β-lactams (Ed. M. I. Page), Chapter 1 , Blackie, London 1992; ingolia and Queener, Med. Res. Rev., 1989, 9, 245-264; Aharonowitz, Cohen and Martin, Ann. Rev. Microbiol., 1992, 46, 461-495; Schofield, Bycroft, Baldwin, Hadju, Roach, Current Opinion in Structural Biology, 1997, 7, 857-864) and includes the following steps (Figure 1): 1. Conversion of the tripeptide: L-δ-α-aminoadipoyl-L-cysteinyl-

D-valine (ACV) to isopenicillin N in a step catalysed by isopenicillin N synthase (IPNS). This step is common to both penicillin and cephalosporin biosynthesis.

2. In some organisms (e.g. Penicillium chrysogenum and Aspergillus nidulans) isopenicillin N is converted by exchange of its L-δ-α- aminoadipoyl side chain to penicillins with other side chains, which are normally more hydrophobic than the side chain of isopenicillin N. This conversion is catalysed by an amidohydrolase/ acyltransferase enzyme. Examples of penicillins produced by this biosynthetic process include penicillin G (which has a phenylacetyl side chain) and penicillin V (which has a phenoxyacetyl side chain). These hydrophobic penicillins may be commercially produced via fermentation under the appropriate conditions.

3. In other organisms (e.g. Streptomyces clavuligerus and Cephalosporium acremonium) isopenicillin N is epimerised to penicillin N. This reaction is catalysed by an epimerase enzyme. 4. In some organisms (e.g. S. clavuligerus and C. acremonium) penicillin N is converted to DAOC. This reaction is catalysed by deacetoxycephalosporin C synthase (DAOCS) in some organisms (e.g. Streptomyces clavuligerus) and by deacetoxy/deacetylcephalosporin C synthase (DAOC/DACS) in others (e.g. C. acremonium).

5. In some organisms (e.g. S. clavuligerus and C. acremonium) DAOC is converted to deacetylcephalosporin C (DAC). This reaction is catalysed by deacetylcephalosporin C synthase (DACS) in some organisms (e.g. S. clavuligerus) and by deacetoxy/deacetylcephalosporin C synthase (DAOC/DACS) in others (e.g. C. acremonium).

Further biosynthetic steps to give other cephalosporin derivatives may also occur, e.g. in C. acremonium DAC may be converted to cephalosporin C and in Streptomyces spp. DAC may be converted to cephamycin C. The genes encoding for each of the enzymes catalysing steps 1-6 above have been identified and sequenced.

Fermented penicillins, cephalosporins and their biosynthetic intermediates are useful as antibiotics or as intermediates in the production of antibiotics. Penicillins with hydrophobic side chains may be used for the preparation of cephalosporins or intermediates used in the preparation of cephalosporins, e.g. penicillins (including penicillin G and penicillin V) may be used to prepare C-3 exomethylene cephams which may be used as intermediates in the preparation of the commercial antibiotics, e.g. Cefachlor.

The enzymes IPNS, DAOCS, DACS and DAOC/DACS are members of an extended family of Fe(ll) utilising oxidase and oxygenase enzymes. Most of this family (including DAOCS, DACS and DAOC/DACS) utilise a 2-oxo acid (normally 2-oxoglutarate) as a cosubstrate in addition to dioxygen and the 'prime' substrate (e.g. penicillin N in the case of DAOCS). Since IPNS, does not use 2-oxoglutarate, it has a substantially different mechanism to the 2-oxoglutarate dependent oxygenases, and this gives rise to a significantly different active site.

The Invention

This invention is based on the determination of the three dimensional crystal structure of DAOCS and the information and developments which come from it. The X-ray co-ordinates provide very detailed 3-dimensional information on the relationships between amino acid residues in the structure of DAOCS and on the binding modes of the Fe-cofactor and the substrates to DAOCS. The structure allows the modification of DAOCS and related enzymes of penicillin and cephalosporin biosynthesis (including DACS and DAOC/DACS) in order to alter their substrate and product selectivities. Since the DAOCS structures are the first from the family of 2-oxoglutarate dependent dioxygenases they also allow for the design of new inhibitors of this family of enzymes. Previously partial overviews of the structures of IPNS complexed to manganese and IPNS complexed to iron and ACV were reported (Roach et al., Nature, 1995, 375, 700-704; Roach et al., Nature, 1997, 387, 827). The structures, as defined by their X-ray co-ordinates, of IPNS complexed to manganese and in complexes with iron, ACV and/or substrate analogues have been reported in Baldwin, Hajdu, Roach, Hensgens, Clifton, GB 9621486.1- (Oxygenase Enzymes and Method).

Procedures have been developed for the production of 7- aminodeacetoxycephaosporin C (7-ADCA) in which recombinant P. chrysogenum strains into which the DAOCS gene has been introduced are used for the production of cephalosporins. In particular if adipic acid is added to these recombinant strains adipoyl-6-APA is produced, which is converted by DAOCS into adipoyl-7-ADCA from which the adipoyi side chain can be removed (EPA-A-0532341 , Shibata et al., Bioorg. Med. Chem. Letts, 1996, 6, 1579-1584 ). The IPNS gene sequence (and therefore the amino acid sequence) is related but significantly different to those of DAOCS, DACS, DAOC/DACS. It is likely that gross elements of the fold (i.e. significant elements within the 3-dimensional structure) of these enzymes will be conserved but that the active site architecture will be very significantly different. Structural elements conserved are likely to include the beta- barrel 'jelly roll' core and certain alpha-helices (including alpha helix-10, as defined in Roach et al., Nature, 1995, 375, 700-704). The degree of similarity is insufficient to define the precise structure of DAOCS, DACS, or DAOC/DACS from the IPNS structures. To date no models of DAOCS, DACS, or DAOC/DACS based on the IPNS structure have been reported. Nor have any detailed studies on substrate binding of these enzymes been reported. One report (WO 97/20053) claims the use of products resulting from modification of certain residues in DAOCS for the improved conversion of penicillin G to phenyl acetyl (G)-7-aminocephalosporanic acid.

The three-dimensional structure of DAOCS is defined by the X-ray co-ordinates set out below (Structure A).

Also set out below is a high resolution crystal structure of a complex of prokaryotic DAOCS from S. clavuligerus with Fe(ll) and 2-oxoglutarate (Structure B).

In part the present invention relates to the use of the structures of DAOCS in order to make modifications to it or DACS or DAOC/DACS in order that the modified enzymes catalyse the conversion of unnatural penicillins (e.g. penicillin G and penicillin V) to cephalosporins more efficiently than the wild-type enzyme. Further aspects of the invention relate to the use of the DAOCS structure in order to produce unnatural products in micro-organisms. Such products include exomethylene cephalosporins, with or without alpha-aminoadipoyl or hydrophobic side chain (e.g. phenylacetyl or phenoxyacetyl). Thus one aspect of this invention refers to the use of the structure of DAOCS for modifying DAOCS (or the closely related enzymes DACS or DAOC/DACS) in order to: (i) permit the enzyme to accept (or accept more efficiently) unnatural penicillin substrates for the preparation of new or commercially valuable antibacterial materials. (ii) enable the modified enzyme to produce unnatural (e.g. exomethylene cephams) or optimise the production of minor products (e.g. 3-β-hydroxycephams) for use as antibacterials or as intermediates in the preparation of antibacterials or commercially valuable compounds.

In another aspect this invention provides modified enzymes that result from application of the aforementioned techniques. These are enzymes having significant (as defined below) sequence and thus structural similarity with DAOCS. Thus, structures of these enzymes may be predicted on the basis of the DAOCS structures. Preferably there will be sequence similarity/identity between most of the modified enzyme and a major part of DAOCS. Previous sequence comparisons (Roach et al., Nature, 1995, 375. 700), using pairwise comparisons of the sequences followed by single linkage cluster analysis show that IPNS, DAOCS, DACS and DAOC/DACS cluster with standard deviations scores of >5.0 (Barton and Stemberg, J. Mol. Biol., 1987, 198, 327). Scores over 5.0 and preferably over 6.0 indicate that the sequence alignments will be correct within all or most of the protein secondary structural elements (Barton, Methods in Enzymol., 1990, 183, 403); thus they have significantly similar sequences and hence structures. Note there are other criteria which may be used to ascertain significant sequence similarity for example % identity or % similarity of amino acids possessing side chains with similar physicochemical properties (Barton and Sternberg, J. Mol. Biol., 1987, 198, 327). Thus, on the basis of sequence comparisons it is possible to predict the structure of one enzyme (e.g. DACS or DAOC/DACS) from another closely related enzyme (e.g. DAOCS). Further, it is recognised that although two enzymes may have structures in which secondary structural elements are largely or wholly conserved, differences in the structures of the two enzymes may result from the side chains of the amino acids forming the secondary structural elements. The effect of these differences, which alter the substrate/product selectivities of the compared enzymes, is predictable once the three-dimensional structure of one of the enzymes is known.

In another aspect the invention provides an enzyme having significant (as herein defined) sequence similarity to DAOCS wherein the side chain binding site of penicillin N or DAOC is modified and at at least one of the following sites at least one amino acid residue is changed to another amino acid residue or is deleted: Thr72, Arg74, Arg75, Glu156, Leu158, Arg160, Arg162, Leu186, Ser187, Phe225, Phe264, Arg266, Asp301 , Tyr302, Val303, Asn304; and/or at least one additional amino acid residue is inserted within the region 300-311 ; provided that other residues interacting with the above may be changed in order to accommodate the change in one of the above.

Modifications of this kind will permit the expansion of penicillin V or penicillin G to the corresponding cephalosporins. To achieve this it is desirable to increase the kcat/Km for the mutant as compared to the wild type DAOCS. Kinetic results indicate that apparent kcat values for penicillin N and penicillin G are similar but that Km is much higher for penicillin G. Thus based on these analysis, a decrease in the binding constant of DAOCS for penicillin G should make it possible to increase kcat/Km for penicillin G.

The side chain binding pocket of DAOCS is made of residues from different parts of the peptide chain, so it is likely that more than one residue will have to be altered to make a better penicillin G/V expander. Nevertheless some residues are more important than others. Examination of the interactions between the last few C-terminal residues (Thr-308 to Ala-311) of one DAOCS molecule and the active site of another in the crystal structure, suggests a binding mode for the penicillin nucleus which is shown in Figure 2 of the accompanying drawings. The penam C-3 carboxylate group probably occupies an analogous position to that of Ala- 311 from a symmetry related molecule in the active site, forming electrostatic interactions with Arg-162 and Arg-160. The side chain of Arg-160 may also form a hydrogen bonding interaction with the β-lactam carbonyl.

It needs to be borne in mind that protein specificity is generally controlled by more than one amino acid. To alter the specificity of a protein in a major way is likely to require more than one of the mutational changes suggested below, although each of the mutations will contribute. With this in mind, preferred residues to modify for the expansion of a penicillin are as follows: a) Arg-266. This residue binds with the -aminoadipate side chain of the natural substrate and should be changed to a residue of more hydrophobic character, e.g. Phe, Ala, Val, Leu, He. b) Thr-72. This should be changed to a hydrophobic residue e.g. Val, Leu, He, Phe, Ala, to help bind the hydrophobic side chain of penicillin G. It should be effective in combination with other mutants. c) Arg-74 may be usefully changed to a neutral or hydrophobic residue (Phe, Tyr, Val, Leu, He, Ala). Modification of Arg-75 may be necessary in addition because it forms a hydrogen-bonding network with Arg-74. d) Glu-156. This residue binds with the α-aminoadipate side chain. It should be changed to one of Ala, Val, Leu, He, Phe, Tyr, Trp, Asn, Gin, Ser. e) The side chains of Leu-158, Asn-301 and Tyr-302 form part of the binding pocket for the penicillin side chain and can be usefully modified to more hydrophobic character. f) Asn-304. This residue binds the amide linking the side chain to the penam nucleus. Modification is effected to expand penicillins with shortened or no side chains (e.g. to Asp or Glu for 6-Apa). Note that other changes may be used to construct part or all of a side chain binding pocket via hydrogen bonding or other interactions.

The insertion or deletion of residues into the DAOCS sequence may also be of use in constructing a hydrophobic binding pocket for the penicillin side chain. Insertion of hydrophobic residues into the

C-terminal region (residue 300-31 1 and in particular 301-303) may assist in the construction of a hydrophobic binding pocket for penicillin side chains. In another aspect the invention provides an enzyme having significant (as herein defined) sequence similarity to DAOCS wherein the penicillin/cephalosporin binding site of penicillin N or DAOC is modified and at at least one of the following amino acid residues is changed or deleted: Ile88, Arg160, Arg162, Phe164, Met180, Thr190, Ile192, Phe225, Pro241 , Val245, Val262, Phe264, Asn304, Ile305, Arg306, Arg307; and/or at least one additional amino acid residue is inserted within the region 300-31 1 ; provided that other residues interacting with the above may be changed in order to accommodate the change in one of the above.

Further discussion of this aspect may be found in Nature Volume 394, pages 805-809 published on 20 August 1998 and incorporated by reference herein. Another aspect of the invention refers to the use of the structure of DAOCS in order to modify its active site (or that of a structurally related 2-oxoglutarate dependent dioxygenase) in order that the modified enzyme accepts non beta lactam substrates in order to produce oxidised compounds of value. Oxidised amino acids (e.g. 4-hydroxyprolines, hydroxylysines, hydroxyaspartic acids and others) are useful as synthetic intermediates in the production of valuable materials. Using the structure of DAOCS specific residues can be targeted for modification in order that the modified enzyme can be used to produce oxidised amino acids or peptides. The process may include modification of the following residues: Arg74, Glu156, Leu158, Arg160, Arg162, Leu186, Ser187, Phe225, Phe264, Arg266, Asp301 , Tyr302, Val303, Asn304, Ile88, Arg162, Phe164, Met180, Thr190, Ile192, Pro241 , Val245, Val262, Ile305, Arg306, Arg307. Another aspect of the invention refers to the use of the

DAOCS structure for the design of selective inhibitors of 2-oxoglutarate dependent dioxygenases. The 2-oxoglutarate dependent dioxygenase prolyl 4-hydroxylase has been the target of inhibition in order to provide a therapeutic treatment for fibrotic diseases (e.g. liver cirrhosis, arthritis). However, no inhibitors are in clinical use, probably because it is difficult to achieve selective inhibition of the target enzyme for inhibition over other enzymes (including 2-oxoglutarate dependent enzymes). The structure of DAOCS provides a template for the design of inhibitors of 2-oxoglutarate dependent dioxygenases. Set out below are two high resolution crystal structures for

DAOCS from S. clavuligerus: the structure of the iron-free apoenzyme (Structure A) and the structure of the complex with Fe(ll) and 2-oxoglutarate (Structure B). The results imply a mechanism by which the enzyme-Fe(ll) complex reacts with 2-oxoglutarate and dioxygen to give the reactive ferryl species, a process common to many non-haem oxygenases. Other notable 2-oxoacid-dependent ferrous enzymes are prolyl hydroxylase, involved in collagen biosynthesis, gibberellin 3β-hydroxylase, a mutation of which influences stem length in plants, and clavaminic acid synthase, involved in the biosynthesis of the β-lactamase inhibitor, clavulanic acid. Within the family of 2-oxoacid-dependent enzymes, DAOCS belongs to a sub-family, the members of which show sequence similarity with IPNS and 1-aminocyclopropane-1-carboxylate oxidase (the ethylene forming enzyme), enzymes that do not use a 2-oxoacid in catalysis. The iron-free form of DAOCS crystallises in space group R3 as a crystallographic trimer. The main chain of the protein folds into a conserved jelly roll core with flanking helices.

Co-ordinates and structure factors have been deposited with the Protein Data Bank (entries 1 rxg, and r1 rxgsf for the Fe(ll)-2-oxoglutarate complex).

LEGENDS TO FIGURES.

Figure 1 : the biosynthetic pathway to the penicillins and cephalosporins. Figure 2 is a view of the active site of DAOCS showing

2-oxoglutarate binding to the iron and proposed penicillin N binding. Interactions with the side chains of certain amino acid residues are indicated by arrows.

Structure A is a three-dimensional structure of DAOCS. Structure B is a high resolution crystal structure for prokaryotic DAOCS from S. clavuligerus as a complex with Fe(ll) and 2- oxoglutarate.

The peptide sequence of DAOCS (with the numbering used herein) is set out below:

Met Asp Thr Thr Val Pro Thr Phe Ser Leu 10

Ala Glu Leu Gin Gin Gly Leu His Gin Asp 20

Glu Phe Arg Arg Cys Leu Arg Asp Lys Gly 30

Leu Phe Tyr Leu Thr Asp Cys Gly Leu Thr 40 Asp Thr Glu Leu Lys Ser Ala Lys Asp Leu 50

Val He Asp Phe Phe Glu His Gly Ser Glu 60

Ala Glu Lys Arg Ala Val Thr Ser Pro Val 70

Pro Thr Met Arg Arg Gly Phe Thr Gly Leu 80 Glu Ser Glu Ser Thr Ala Gin He Thr Asn 90 Thr Gly Ser Tyr Ser Asp Tyr Ser Met Cys 100

Tyr Ser Met Gly Thr Ala Asp Asn Leu Phe 110

Pro Ser Gly Asp Phe Gly Arg He Trp Thr 120

Gin Tyr Phe Asp Arg Gin Tyr Thr Ala Ser 130

Arg Ala Val Ala Arg Glu Val Leu Arg Ala 140 Thr Gly Thr Glu Pro Asp Gly Gly Val Glu 150

Ala Phe Leu Asp Cys Glu Pro Leu Leu Arg 160

Phe Arg Tyr Phe Pro Gin Val Pro Glu His 170

Arg Ser Ala Glu Glu Gin Pro Leu Arg Met 180

Ala Pro His Tyr Asp Leu Ser Met Val Thr 190 Leu He Gin Gin Thr Pro Cys Ala Asn Gly 200

Phe Val Ser Leu Gin Ala Glu Val Gly Gly 210

Ala Phe Thr Asp Leu Pro Tyr Arg Pro Asp 220

Ala Val Leu Val Phe Cys Gly Ala He Ala 230

Thr Leu Val Thr Gly Gly Gin Val Lys Ala 240 Pro Arg His His Val Ala Ala Pro Arg Arg 250

Asp Gin He Ala Gly Ser Ser Arg Thr Ser 260

Ser Val Phe Phe Leu Arg Pro Asn Ala Asp 270

Phe Thr Phe Ser Val Pro Leu Ala Arg Glu 280

Cys Gly Phe Asp Val Ser Leu Asp Gly Glu 290 Thr Ala Thr Phe Gin Asp Trp He Gly Gly 300

Asn Tyr Val Asn He Arg Arg Thr Ser Lys 310

Ala 311 STRUCTURE A

CRYST1 106.400 106.400 71.100 90.00 90.00 120.00

SCALE1 0.009398 0.005426 0.000000 0.000000

SCALE2 0.000000 0.010852 0.000000 0.000000

SCALE3 0.000000 0.000000 0.014065 0.000000

ATOM N AMET 1 31.434 10.641 59.873 0.542 44.31

ANISOU N AMET 1 8315 2319 6203 -614 -3454 791

ATOM CA AMET 1 30.985 11.769 59.065 0.542 39.90

ANISOU CA AMET 1 9037 3006 3117 -786 -1026 -296

ATOM C AMET 1 30.472 12.900 59.956 0.542 28.97

ANISOU C AMET 1 4807 3113 3086 -421 -2189 119

ATOM O AMET 1 29.961 12.670 61.055 0.542 28.12

ANISOU O O AMET 1 3925 2381 4377 -402 -1097 7 4

ATOM C CBB AMET 1 29.970 11.328 58.023 0.542 34. 5

ANISOU C CBB AMET 1 7877 3692 1672 30 -91 - 73

ATOM C CGG AMET 1 28.626 12.015 57.903 0.542 3 S 19

ANISOU C CGG AMET 1 7367 4873 2270 133 912 - 17 65

ATOM S SDD AMET 1 27.564 11.232 56.654 0.542 47. 19

ANISOU S SDD AMET 1 6146 7957 3827 -2344 1050 1326

ATOM C CEE AMET 1 28.129 11.973 55.135 0.542 27.10

ANISOU C CEE AMET 1 5030 2111 3155 2345 -1467 - 9

ATOM 9 N N AASP 2 30.592 14.105 59.425 0.268 30.20

ANISOU 9 N N AASP 2 4674 3022 3777 -1210 -782 - 383

ATOM 10 C CAA AASP 2 29.993 15.322 59.963 0.268 34.22

ANISOU 10 C C AASP 2 5567 2803 4633 -1106 -964 525

ATOM 11 C C AASP 2 28.494 15.268 59.655 0.268 33.34

ANISOU 11 C C AASP 2 5665 1997 5006 -314 -1457 7 7

ATOM 12 O O AASP 2 28.099 15.650 58.551 0.268 44.76

ANISOU 12 O O AASP 2 6859 5248 4901 -1023 -1582 1631

ATOM 13 C CBB AASP 2 30.629 16.528 59.281 0.268 25.9.

ANISOU 13 C CBB AASP 2 4424 3085 2361 322 -1794 582

ATOM 14 C CGG AASP 2 29.978 17.862 59.553 0.268 38.05

ANISOU 14 C CGG AASP 2 6456 2611 5389 -501 -608 -1114

ATOM 15 OD1 AASP 2 28.995 17.937 60.318 0.268 42.35

ANISOU 15 OD1 AASP 2 6406 504 9179 873 920 1 91

ATOM 16 OD2 AASP 2 30.449 18.885 58.997 0.268 28.59

ANISOU 16 OD2 AASP 2 1619 2901 6341 790 -1022 253

ATOM 17 N BMET 1 32.709 12.640 58.544 0.458 29.49

ANISOU 17 N BMET 1 4552 2218 4435 -105 1580 4 77

ATOM 18 CA BMET 1 31.874 13.050 57.425 0.458 40.62

ANISOU 18 CA BMET 1 4228 4809 6395 580 210 1 03

ATOM 19 C BMET 1 30.884 14.113 57.894 0.458 38 .21

ANISOU 19 C BMET 1 5082 3637 5797 282 -909 - 915

ATOM 20 O BMET 1 30.075 14.599 57.110 0.458 44.81

ANISOU 20 O BMET 1 8292 3208 5525 2071 -656 - 12

ATOM 21 CB BMET 1 31.131 11.857 56.829 0.458 33 .14

ANISOU 21 CB BMET 1 4866 2613 5114 2013 -122 8

ATOM 22 CG BMET 1 29.625 11.840 56.968 0.458 40.28

ANISOU 22 CG BMET 1 4795 5740 4768 230 -751 5

ATOM 23 SD BMET 1 28.761 11.495 55.422 0.458 34.23

ANISOU 23 SD BMET 1 5619 3819 3566 2050 -215 2

ATOM 24 CE BMET 1 29.953 12.079 54.222 0.458 54.24

ANISOU 24 CE BMET 1 10672 4519 5420 1149 4083 -2-4 63

ATOM 25 N BASP 2 30.914 14.381 59.194 0.732 37.72

ANISOU 25 N BASP 2 4433 3914 5984 -1323 -1208 -1385

ATOM 26 CA BASP 2 29.979 15.308 59.811 0.732 35.78

ANISOU 26 CA BASP 2 5412 3387 4794 -1064 -1050 - 795

ATOM 27 C BASP 2 28.536 14.886 59.567 0.732 29.66

ANISOU 27 C BASP 2 4876 1624 4771 27 -1561 121

ATOM 28 O BASP 2 28.181 14.602 58.414 0.732 34 .65

ANISOU 28 O BASP 2 4375 3689 5100 65 -1485 2 47

ATOM 29 CB BASP 2 30.195 16.696 59.181 0.732 37 .39

ANISOU 29 CB BASP 2 6632 3351 4222 -1850 869 - 1 518

ATOM 30 CG BASP 2 29.562 17.730 60.104 0.732 30.38

ANISOU 30 CG BASP 2 3243 3791 4510 -500 -606 -1 191

ATOM 31 OD1 BASP 2 28.866 17.247 61.030 0.732 48.88

SUBSTΓΓUTE SHEET (RULE 26) ANISOU 31 OD1 BASP 2 6276 4203 8095 -1203 3147 - 1901

ATOM 32 OD2 BASP 2 29.760 18.945 59.875 0.732 34.85

ANISOU 32 OD2 BASP 2 2852 3708 6680 -491 444 - 1450

ATOM 33 N THR 3 27.717 14.789 60.606 1.000 35.58

ANISOU 33 N THR 3 4586 4123 4811 601 -1628 1516

ATOM 34 C THR 3 26.303 14.433 60.495 1.000 40.48

ANISOU 34 CA THR 3 4650 4555 6175 371 -911 - 385

ATOM 35 C THR 3 25.382 15.647 60.611 1.000 39.82

ANISOU 35 C THR 3 4376 4155 6598 320 -3864 - 586

ATOM 36 O THR 3 24.150 15.556 60.751 1.000 33 .55

ANISOU 36 O THR 3 4668 3107 4972 357 -2748 - 588

ATOM 37 CB THR 3 25.905 13.450 61.613 1.000 39.95

ANISOU 37 CB THR 3 3787 4004 7387 160 -1209 6 2

ATOM 38 OG1 THR 3 26.591 13.851 62.817 1.000 61.83

ANISOU 38 OG1 THR 3 10134 5882 7476 -4164 -3020 2051

ATOM 39 CG2 THR 3 26.399 12.052 61.278 1.000 59.32

ANISOU 39 CG2 THR 3 4613 3971 13955 1114 -3135 - 198

ATOM 40 N THR 4 26.036 16.780 60.456 1.000 32.55

ANISOU 40 N THR 4 4306 4611 3450 377 -2166 - 217

ATOM 41 CA THR 4 25.439 18.092 60.393 1.000 31.22

ANISOU 41 CA THR 4 4275 4229 3358 -81 -1179 9 5

ATOM 42 C THR 4 24.672 18.272 59.090 1.000 30.06

ANISOU 42 C THR 4 4876 3341 3207 773 -1156 - 204

ATOM 43 O THR 4 25.195 17.935 58.017 1.000 31.64

ANISOU 43 O THR 4 4877 3780 3363 1935 -1255 - 52

ATOM 44 CB THR 4 26.510 19.208 60.407 1.000 32.31

ANISOU 44 CB THR 4 2320 4762 5194 475 -547 593

ATOM 45 OG1 THR 4 27.324 19.091 61.578 1.000 32 .36

ANISOU 45 OG1 THR 4 3705 3955 4635 -79 -797 - 389

ATOM 46 CG2 THR 4 25.852 20.582 60.458 1.000 27.22

ANISOU 46 CG2 THR 4 3728 4174 2443 71 304 - 151

ATOM 47 N VAL 5 23.464 18.796 59.211 1.000 21.69

ANISOU 47 N VAL 5 4041 1985 2215 -543 -657 15 8

ATOM 48 CA VAL 5 22.690 19.140 58.024 1.000 20.42

ANISOU 48 CA VAL 5 3675 1964 2120 -622 -517 1 03

ATOM 49 C VAL 5 23.199 20.489 57.499 1.000 17.01

ANISOU 49 C VAL 5 2263 1803 2396 -279 -622 8 9

ATOM 50 O VAL 5 23.156 21.449 58.252 1.000 21.10

ANISOU 50 O VAL 5 3662 1885 2472 -389 -656 1 6

ATOM 51 CB VAL 5 21.204 19.216 58.402 1.000 24.22

ANISOU 51 CB VAL 5 3551 2155 3495 -1045 -396 7 83

ATOM 52 CGI VAL 5 20.434 19.700 57.166 1.000 20.14

ANISOU 52 CGI VAL 5 3202 1779 2672 -453 10 - 226

ATOM 53 CG2 VAL 5 20.701 17.867 58.860 1.000 28.58

ANISOU 53 CG2 VAL 5 5258 2086 3516 -1226 431 5 10

ATOM 54 N PRO 6 23.750 20.542 56.300 1.000 16.95

ANISOU 54 N PRO 6 2378 1629 2434 29 -594 3 0 1

ATOM 55 CA PRO 6 24.354 21.793 55.857 1.000 16.90

ANISOU 55 CA PRO 6 1645 1775 3000 6 -445 3 03

ATOM 56 C PRO 6 23.298 22.800 55.383 1.000 15.61

ANISOU 56 C PRO 6 1477 1766 2687 -192 -437 5 4 5

ATOM 57 O PRO 6 22.133 22.432 55.201 1.000 15.75

ANISOU 57 O PRO 6 1578 1761 2647 -260 -579 5 5

ATOM 58 CB PRO 6 25.216 21.375 54.682 1.000 19.85

ANISOU 58 CB PRO 6 2320 1752 3468 50 70 182

ATOM 59 CG PRO 6 24.632 20.095 54.187 1.000 24.76

ANISOU 59 CG PRO 6 3550 2953 2904 -1186 300 - 286

ATOM 60 CD PRO 6 23.926 19.428 55.357 1.000 17.91

ANISOU 60 CD PRO 6 1960 1962 2882 -168 -138 - 44

ATOM 61 N THR 7 23.723 24.031 55.156 1.000 14.38

ANISOU 61 N THR 7 1518 1567 2378 -158 -616 1 00 ATOM 62 CA THR 7 22.907 25.103 54.610 1.000 14.09

ANISOU 62 CA THR 7 1625 1554 2174 -255 -581 2 2 8

ATOM 63 C THR 7 23.605 25.684 53.374 1.000 14.74

ANISOU 63 C THR 7 1683 1849 2067 -193 -468 12 1

ATOM 64 O THR 7 24.828 25.894 53.423 1.000 15.95

ANISOU 64 O THR 7 1752 2137 2171 -378 -457 1 8 5

ATOM 65 CB THR 7 22.795 26.248 55.637 1.000 15.25

ANISOU 65 CB THR 7 1548 1846 2401 56 -124 5 2

ATOM 66 OG1 THR 7 22.208 25.717 56.829 1.000 16.91

ANISOU 66 OG1 THR 7 1818 2149 2458 -402 -183 4 7

ATOM 67 CG2 THR 7 21.952 27.387 55.040 1.000 16.09

ANISOU 67 CG2 THR 7 1651 1613 2848 -138 -263 - 2 5

ATOM 68 N PHE 8 22.830 25.892 52.325 1.000 15.06

ANISOU 68 N PHE 8 1966 1618 2137 -411 -558 2 3 0

ATOM 69 CA PHE 8 23.317 26.545 51.136 1.000 14.76

ANISOU 69 CA PHE 8 1857 1558 2192 -213 -411 2 8 1

ATOM 70 C PHE 8 22.421 27.728 50.810 1.000 14.94

ANISOU 70 c PHE 8 1907 1421 2347 -275 -357 181

ATOM 71 0 PHE 8 21.198 27.678 50.995 1.000 16.40

ANISOU 71 0 PHE 8 1782 1642 2808 -197 -550 3 4

ATOM 72 CB PHE 8 23.242 25.562 49.948 1.000 16.49

ANISOU 72 CB PHE 8 2123 1854 2287 49 -371 - 1

ATOM 73 CG PHE 8 24.225 24.432 50.027 1.000 14.92

ANISOU 73 CG PHE 8 1710 1824 2135 -197 -365 1 63

ATOM 74 CD1 PHE 8 23.822 23.227 50.600 1.000 16.78

ANISOU 74 CD1 PHE 8 1808 1726 2842 -300 -358 184

ATOM 75 CD2 PHE 8 25.539 24.558 49.602 1.000 16.67

ANISOU 75 CD2 PHE 8 1705 2130 2500 -310 -361 3 2 1

ATOM 76 CE1 PHE 8 24.702 22.183 50.742 1.000 16.74

ANISOU 76 CE1 PHE 8 2035 1966 2359 -4 -99 2 95

ATOM 77 CE2 PHE 8 26.420 23.525 49.773 1.000 19.18

ANISOU 77 CE2 PHE 8 1398 2153 3736 -408 -631 1 87

ATOM 78 CZ PHE 8 26.026 22.336 50.351 1.000 17.90

ANISOU 78 CZ PHE 8 1849 2003 2948 -119 -376 2 0

ATOM 79 N SER 9 23.023 28.776 50.314 1.000 14.82

ANISOU 79 N SER 9 2134 1488 2008 -351 -528 3 10

ATOM 80 CA SER 9 22.338 29.902 49.715 1.000 15.12

ANISOU 80 CA SER 9 2037 1259 2449 -357 -571 13 4

ATOM 81 C SER 9 21.977 29.607 48.270 1.000 16.19

ANISOU 81 C SER 9 2138 1791 2224 -374 -535 5 47

ATOM 82 O SER 9 22.877 29.312 47.473 1.000 17.04

ANISOU 82 O SER 9 2191 1892 2393 -423 -544 2 3 2

ATOM 83 CB SER 9 23.306 31.113 49.696 1.000 18.74

ANISOU 83 CB SER 9 2891 1712 2519 -1012 -478 717

ATOM 84 OG SER 9 22.738 32.131 48.853 1.000 20.82

ANISOU 84 OG SER 9 2866 1569 3477 -662 -854 607

ATOM 85 N LEU 10 20.697 29.674 47.924 1.000 16.46

ANISOU 85 N LEU 10 2215 1495 2542 -228 -740 - 48

ATOM 86 CA LEU 10 20.345 29.401 46.529 1.000 17.55

ANISOU 86 CA LEU 10 2263 1856 2551 -582 -694 3 6

ATOM 87 C LEU 10 21.079 30.373 45.591 1.000 18.84

ANISOU 87 C LEU 10 2506 1870 2784 -596 -830 3 57

ATOM 88 O LEU 10 21.573 30.025 44.520 1.000 20.19

ANISOU 88 O LEU 10 2705 2263 2704 -524 -663 5 08

ATOM 89 CB LEU 10 18.844 29.559 46.327 1.000 18.87

ANISOU 89 CB LEU 10 2302 2516 2354 -288 -715 2 8 0

ATOM 90 CG LEU 10 18.355 29.333 44.895 1.000 18.28

ANISOU 90 CG LEU 10 2182 2172 2591 -668 -677 - 301

ATOM 91 CD1 . LEU 10 18.708 27.955 44.397 1.000 22.45

ANISOU 91 CD1 . LEU 10 3418 2024 3089 -308 -537 1 7

ATOM 92 CD2 : LEU 10 16.852 29.603 44.869 1.000 21.93

SUBSTΓΓUTE SHEET (RULE 26) ANISOU 92 CD2 LEU 10 2250 2658 3424 -504 -1139 7 5

ATOM 93 N ALA 11 21.154 31.638 46.037 1.000 20.05

ANISOU 93 N ALA 11 2862 1780 2977 -595 -1279 4 72

ATOM 94 CA ALA 11 21.810 32.647 45.202 1.000 24.24

ANISOU 94 CA ALA 11 3160 1670 4380 -455 -979 8 9 1

ATOM 95 C ALA 11 23.285 32.309 44.946 1.000 21.06

ANISOU 95 C ALA 11 3128 1937 2937 -644 -1016 43 1

ATOM 96 O ALA 11 23.819 32.447 43.829 1.000 26.29

ANISOU 96 O ALA 11 3569 3261 3158 -1628 -923 1137

ATOM 97 CB ALA 11 21.752 33.989 45.953 1.000 24.29

ANISOU 97 CB ALA 11 3740 1692 3797 -461 -216 9 9 6

ATOM 98 N GLU 12 23.953 31.844 46.005 1.000 20.65

ANISOU 98 N GLU 12 2829 1975 3044 -828 -930 674

ATOM 99 CA GLU 12 25.354 31.463 45.862 1.000 21.19

ANISOU 99 CA GLU 12 3036 2400 2615 -506 -715 5 9 8

ATOM 100 C GLU 12 25.483 30.277 44.920 1.000 21.56

ANISOU 100 C GLU 12 3894 2179 2117 -702 -206 9 88

ATOM 101 O GLU 12 26.375 30.215 44.069 1.000 21.98

ANISOU 101 O GLU 12 3463 2917 1971 -1144 -488 618

ATOM 102 CB GLU 12 26.032 31.170 47.204 1.000 20.27

ANISOU 102 CB GLU 12 2874 2192 2636 -221 -624 5 0 1

ATOM 103 CG GLU 12 26.156 32.451 48.032 1.000 20.54

ANISOU 103 CG GLU 12 2889 2316 2598 -344 -516 4 0 6

ATOM 104 CD GLU 12 26.787 32.279 49.389 1.000 21.86

ANISOU 104 CD GLU 12 3146 2542 2619 -1297 -612 7 9 9

ATOM 105 OEl GLU 12 27.068 31.149 49.803 1.000 24.98

ANISOU 105 OEl GLU 12 3642 2681 3169 -1348 -1088 1134

ATOM 106 OE2 GLU 12 26.819 33.305 50.092 1.000 33.52

ANISOU 106 OE2 GLU 12 5881 2966 3888 -1119 -2251 4 6

ATOM 107 N LEU 13 24.600 29.295 45.060 1.000 18.91

ANISOU 107 N LEU 13 2567 2345 2275 -351 -390 3 82

ATOM 108 CA LEU 13 24.645 28.117 44.174 1.000 18.61

ANISOU 108 CA LEU 13 2575 2347 2149 -209 270 4 0 6

ATOM 109 C LEU 13 24.432 28.566 42.738 1.000 21.40

ANISOU 109 C LEU 13 3558 2367 2206 -709 -41 52 6

ATOM 110 O LEU 13 25.102 28.095 41.824 1.000 23 .75

ANISOU 110 O LEU 13 3827 3216 1981 -823 -117 1 9 0

ATOM 111 CB LEU 13 23.541 27.137 44.562 1.000 18.97

ANISOU 111 CB LEU 13 2982 2243 1984 -462 -145 44 0

ATOM 112 CG LEU 13 23.773 26.344 45.860 1.000 18.57

ANISOU 112 CG LEU 13 2313 2322 2422 -467 -362 745

ATOM 113 CD1 LEU 13 22.526 25.480 46.070 1.000 20.74

ANISOU 113 CD1 LEU 13 2769 2266 2845 -789 -142 5 94

ATOM 114 CD2 LEU 13 25.023 25.473 45.858 1.000 19.80

ANISOU 114 CD2 LEU 13 2709 2229 2585 -244 -509 - 107

ATOM 115 N GLN 14 23.544 29.508 42.478 1.000 22.03

ANISOU 115 N GLN 14 3596 2139 2635 -960 -903 3 79

ATOM 116 CA GLN 14 23.284 29.978 41.104 1.000 23 .79

ANISOU 116 CA GLN 14 3010 3335 2694 -992 -816 64 8

ATOM 117 C GLN 14 24.481 30.712 40.509 1.000 25.44

ANISOU 117 C GLN 14 3360 3427 2881 -1070 -382 4 87

ATOM 118 O GLN 14 24.655 30.829 39.288 1.000 30.04

ANISOU 118 O GLN 14 3836 4657 2922 -1208 -427 8 98

ATOM 119 CB GLN 14 22.064 30.906 41.131 1.000 26.28

ANISOU 119 CB GLN 14 3133 3630 3222 -760 -863 9 3 8

ATOM 120 CG GLN 14 20.772 30.111 41.355 1.000 23.26

ANISOU 120 CG GLN 14 3106 2319 3413 -299 -577 5 14

ATOM 121 CD GLN 14 19.586 31.020 41.631 1.000 23.69

ANISOU 121 CD GLN 14 3384 2462 3155 -317 -393 - 196

ATOM 122 OEl GLN 14 19.734 32.104 42.160 1.000 28.34

ANISOU 122 OEl GLN 14 4973 2619 3175 -183 -732 - 408 -17-

ATOM 123 NE2 GLN 14 18.398 30.513 41.349 1.000 23.60

ANISOU 123 NE2 GLN 14 3058 2969 2941 -383 54 245

ATOM 124 N GLN 15 25.309 31.243 41.395 1.000 25.00

ANISOU 124 N GLN 15 3078 3281 3140 -1159 -394 57;

ATOM 125 CA GLN 15 26.530 31.936 40.945 1.000 24.05

ANISOU 125 CA GLN 15 2947 3560 2631 -866 -98 65 :

ATOM 126 C GLN 15 27.650 30.920 40.707 1.000 26.06

ANISOU 126 C GLN 15 3810 3951 2139 -345 406 66 i

ATOM 127 O GLN 15 28.756 31.284 40.302 1.000 35.85

ANISOU 127 O GLN 15 4294 4851 4476 102 1871 11 S

ATOM 128 CB GLN 15 27.018 32.918 42.009 1.000 25.90

ANISOU 128 CB GLN 15 3055 3037 3748 -1092 -109 36 -

ATOM 129 CG GLN 15 26.103 34.092 42.219 1.000 31.24

ANISOU 129 CG GLN 15 4562 2577 4731 -806 962 10 E

ATOM 130 CD GLN 15 26.503 35.022 43.348 1.000 59.75

ANISOU 130 CD GLN 15 9927 2475 10301 -1855 -14 - 19 0 4

ATOM 131 OEl GLN 15 27.634 35.031 43.840 1.000 81.81

ANISOU 131 OEl GLN 15 15059 3931 12094 -944 -6272 - -:1 8 0 3

ATOM 132 NE2 GLN 15 25.539 35.841 43.767 1.000 91.46

ANISOU 132 NE2 GLN 15 14070 4846 15833 -923 3672 - 48 5 0

ATOM 133 N GLY 16 27.379 29.643 40.969 1.000 29.90

ANISOU 133 N GLY 16 4634 3820 2907 -239 22 787

ATOM 134 CA GLY 16 28.410 28.649 40.699 1.000 28.76

ANISOU 134 CA GLY 16 4466 3629 2833 -709 461 25

ATOM 135 C GLY 16 29.339 28.473 41.878 1.000 27.60

ANISOU 135 C GLY 16 3816 3779 2891 -616 914 14 i 8 5

ATOM 136 O GLY 16 30.398 27.867 41.725 1.000 31.47

ANISOU 136 O GLY 16 3386 4758 3814 -899 1243 10 ; 2 3

ATOM 137 N LEU 17 28.960 28.898 43.083 1.000 26.01

ANISOU 137 N LEU 17 3295 3636 2950 -721 162 74

ATOM 138 CA LEU 17 29.776 28.666 44.257 1.000 23.96

ANISOU 138 CA LEU 17 2700 3032 3372 -601 100 67

ATOM 139 C LEU 17 29.462 27.338 44.932 1.000 20.31

ANISOU 139 C LEU 17 2222 2763 2733 -252 611 26

ATOM 140 O LEU 17 28.389 26.780 44.789 1.000 23.13

ANISOU 140 O LEU 17 2347 3134 3308 -443 263 85

ATOM 141 CB LEU 17 29.645 29.806 45.286 1.000 25.94

ANISOU 141 CB LEU 17 2886 2933 4035 -1318 -405 25

ATOM 142 CG LEU 17 29.962 31.209 44.716 1.000 31.57

ANISOU 142 CG LEU 17 3741 2948 5308 -523 1150 72

ATOM 143 CD1 LEU 17 29.550 32.358 45.615 1.000 32.04

ANISOU 143 CD1 LEU 17 5221 2887 4066 -1269 278 50

ATOM 144 CD2 LEU 17 31.458 31.278 44.416 1.000 38.11

ANISOU 144 CD2 LEU 17 3828 5491 5160 -2315 954 23

ATOM 145 N HIS 18 30.441 26.822 45.681 1.000 22.49

ANISOU 145 N HIS 18 2600 3067 2877 -662 42 449

ATOM 146 CA HIS 18 30.289 25.644 46.537 1.000 21.54

ANISOU 146 CA HIS 18 2378 2809 2996 -432 201 31

ATOM 147 C HIS 18 29.908 24.376 45.790 1.000 22.76

ANISOU 147 C HIS 18 2256 3245 3148 -1009 282 11

ATOM 148 O HIS 18 29.147 23.565 46.331 1.000 22.60

ANISOU 148 O HIS 18 2008 3064 3516 -629 -166 88

ATOM 149 CB HIS 18 29.224 25.872 47.618 1.000 22.81

ANISOU 149 CB HIS 18 2514 2879 3272 -526 450 42

ATOM 150 CG HIS 18 29.320 27.248 48.217 1.000 21.70

ANISOU 150 CG HIS 18 2797 3038 2411 -149 39 503

ATOM 151 ND] . HIS 18 30.438 27.773 48.807 1.000 25.01

ANISOU 151 NDl HIS 18 3714 3505 2284 -207 -629 14

ATOM 152 CD; - HIS 18 28.370 28.216 48.269 1.000 24.95

ANISOU 152 CD2 HIS 18 3244 3278 2957 87 544 275

ATOM 153 CE1 HIS 18 30.197 28.982 49.223 1.000 29.26 ANISOU 153 CE1 HIS 18 4603 3396 3118 -388 -335 2 7

ATOM 154 NE2 HIS 18 28.937 29.271 48.919 1.000 27.24

ANISOU 154 NΞ2 HIS 18 4582 3137 2632 2 224 3 6 5

ATOM 155 N GLN 19 30.269 24.270 44.521 1.000 22 .74

ANISOU 155 N GLN 19 2724 3094 2822 -511 -123 423

ATOM 156 CA GLN 19 29.806 23.113 43.730 1.000 23 .85

ANISOU 156 CA GLN 19 3129 2668 3263 148 63 8 9

ATOM 157 C GLN 19 30.271 21.760 44.221 1.000 22.77

ANISOU 157 C GLN 19 2532 3026 3095 -502 -574 7 78

ATOM 158 O GLN 19 29.480 20.801 44.259 1.000 21.99

ANISOU 158 O GLN 19 1869 2911 3574 -187 0 5 5 8

ATOM 159 CB GLN 19 30.227 23.322 42.276 1.000 27.66

ANISOU 159 CB GLN 19 5043 2519 2947 29 -339 4 5 8

ATOM 160 CG GLN 19 29.397 24.333 41.523 1.000 26.21

ANISOU 160 CG GLN 19 3289 3163 3508 299 171 4 3 7

ATOM 161 CD GLN 19 27.917 24.368 41.862 1.000 32.47

ANISOU 161 CD GLN 19 3403 4411 4521 -986 535 654

ATOM 162 OEl GLN 19 27.154 23.604 41.277 1.000 39.69

ANISOU 162 OEl GLN 19 3996 4238 6845 -262 -2770 1829

ATOM 163 NE2 GLN 19 27.511 25.212 42.811 1.000 42.55

ANISOU 163 NE2 GLN 19 3803 6153 6212 81 1944 1 1

ATOM 164 N ASP 20 31.526 21.572 44.631 1.000 22.63

ANISOU 164 N ASP 20 2073 3400 3123 -414 95 7 08

ATOM 165 CA ASP 20 31.926 20.292 45.225 1.000 23.10

ANISOU 165 CA ASP 20 1869 3674 3235 83 236 704

ATOM 166 C ASP 20 31.190 20.042 46.546 1.000 20.03

ANISOU 166 c ASP 20 1775 2963 2873 -280 -143 49 3

ATOM 167 0 ASP 20 30.772 18.899 46.768 1.000 21.48

ANISOU 167 0 ASP 20 1429 2884 3848 -311 225 224

ATOM 168 CB ASP 20 33.414 20.268 45.521 1.000 27.66

ANISOU 168 CB ASP 20 1835 4546 4130 -16 207 8 8 1

ATOM 169 CG ASP 20 34.298 20.206 44.291 1.000 39.35

ANISOU 169 CG ASP 20 2355 6893 5705 -654 1323 -1915

ATOM 170 OD1 ASP 20 33.870 19.914 43.153 1.000 35.78

ANISOU 170 OD1 ASP 20 3152 5452 4992 -741 1508 - 797

ATOM 171 OD2 ASP 20 35.508 20.433 44.467 1.000 45.22

ANISOU 171 OD2 ASP 20 2201 8705 6277 -589 1088 - 87

ATOM 172 N GLU 21 31.046 21.053 47.404 1.000 20.01

ANISOU 172 N GLU 21 1574 2935 3093 -412 -241 3 67

ATOM 173 CA GLU 21 30.323 20.811 48.665 1.000 18.97

ANISOU 173 CA GLU 21 1412 2956 2838 -481 -464 118

ATOM 174 C GLU 21 28.858 20.448 48.402 1.000 17.84

ANISOU 174 C GLU 21 1386 2342 3050 -307 -395 234

ATOM 175 O GLU 21 28.290 19.602 49.054 1.000 18.46

ANISOU 175 O GLU 21 1671 2286 3057 -419 -351 116

ATOM 176 CB GLU 21 30.415 22.058 49.563 1.000 20.10

ANISOU 176 CB GLU 21 1646 2821 3170 -514 -499 127

ATOM 177 CG GLU 21 31.893 22.322 49.918 1.000 24.11

ANISOU 177 CG GLU 21 1682 3568 3912 -766 -326 - 711

ATOM 178 CD GLU 21 32.574 23.380 49.081 1.000 29.70

ANISOU 178 CD GLU 21 1330 4241 5713 -752 -666 5 2 1

ATOM 179 OEl . GLU 21 32.249 23.594 47.887 1.000 35.14

ANISOU 179 OEl . GLU 21 2623 4054 6677 -1336 -1741 1977

ATOM 180 OE2 ! GLU 21 33.483 24.007 49.678 1.000 39.39

ANISOU 180 OE2 ! GLU 21 3681 4425 6860 -2089 -1618 647

ATOM 181 N PHE 22 28.231 21.048 47.395 1.000 17.30

ANISOU 181 N PHE 22 1540 2352 2680 -243 -446 - 7 9

ATOM 182 CA PHE 22 26.851 20.761 47.071 1.000 17.13

ANISOU 182 CA PHE 22 1534 2166 2807 -235 -396 3 74

ATOM 183 C PHE 22 26.733 19.329 46.552 1.000 17.41

ANISOU 183 C PHE 22 1688 2500 2427 -502 -334 1 04 ATOM 184 O PHE 22 25.867 18.574 46.995 1.000 15.87

ANISOU 184 0 PHE 22 1570 2118 2343 -249 -361 13 1

ATOM 185 CB PHE 22 26.305 21.840 46.149 1.000 18.00

ANISOU 185 CB PHE 22 1747 2754 2337 70 -178 445

ATOM 186 CG PHE 22 24.802 21.729 45.930 1.000 16.38

ANISOU 186 CG PHE 22 1763 1748 2714 -90 -326 2 2 3

ATOM 187 CD1 PHE 22 23.934 21.723 47.003 1.000 18.29

ANISOU 187 CD1 PHE 22 1812 2091 3045 -197 -88 5 7 6

ATOM 188 CD2 PHE 22 24.290 21.720 44.641 1.000 18.62

ANISOU 188 CD2 PHE 22 2106 2079 2890 -143 -623 3 94

ATOM 189 CE1 PHE 22 22.569 21.727 46.771 1.000 18.90

ANISOU 189 CE1 PHE 22 1826 2086 3271 -198 -133 3 02

ATOM 190 CE2 PHE 22 22.911 21.660 44.379 1.000 19.28

ANISOU 190 CE2 PHE 22 2189 2023 3114 -242 -754 - 144

ATOM 191 CZ PHE 22 22.059 21.645 45.473 1.000 19.42

ANISOU 191 CZ PHE 22 2048 1723 3607 90 -483 - 376

ATOM 192 N ARG 23 27.580 18.971 45.583 1.000 17.88

ANISOU 192 N ARG 23 1647 2437 2709 -168 -218 3 17

ATOM 193 CA ARG 23 27.520 17.594 45.079 1.000 19.18

ANISOU 193 CA ARG 23 1724 2539 3022 -166 36 15 8

ATOM 194 C ARG 23 27.767 16.595 46.211 1.000 19.11

ANISOU 194 C ARG 23 1279 2461 3518 -173 -113 4 5 5

ATOM 195 0 ARG 23 27.107 15.547 46.229 1.000 18.82

ANISOU 195 0 ARG 23 1614 2156 3381 -33 181 - 128

ATOM 196 CB ARG 23 28.605 17.351 44.030 1.000 22.81

ANISOU 196 CB ARG 23 1934 4099 2633 -34 -105 - 354

ATOM 197 CG ARG 23 28.248 17.790 42.617 1.000 24.82

ANISOU 197 CG ARG 23 2601 4078 2752 191 -122 - 204

ATOM 198 CD ARG 23 29.376 17.272 41.685 1.000 29.71

ANISOU 198 CD ARG 23 2503 5619 3168 -285 908 7 04

ATOM 199 NE ARG 23 30.479 18.206 41.800 1.000 30.96

ANISOU 199 NE ARG 23 2877 5034 3851 -43 286 2 97

ATOM 200 CZ ARG 23 30.549 19.360 41.148 1.000 29.49

ANISOU 200 CZ ARG 23 2612 5063 3529 -225 606 177

ATOM 201 NHl ARG 23 29.536 19.665 40.328 1.000 29.26

ANISOU 201 NHl ARG 23 3242 4951 2923 -960 331 52 5

ATOM 202 NH2 ARG 23 31.629 20.092 41.345 1.000 32.61

ANISOU 202 NH2 ARG 23 2320 5347 4722 -134 519 179

ATOM 203 N ARG 24 28.708 16.851 47.125 1.000 17.80

ANISOU 203 N ARG 24 1262 2168 3332 183 38 9 8

ATOM 204 CA ARG 24 28.930 15.899 48.222 1.000 18.85

ANISOU 204 CA ARG 24 1368 2509 3287 69 -162 105

ATOM 205 C ARG 24 27.701 15.811 49.114 1.000 17.51

ANISOU 205 C ARG 24 1456 2015 3181 132 -177 2 43

ATOM 206 O ARG 24 27.333 14.733 49.544 1.000 17.93

ANISOU 206 0 ARG 24 1851 1965 2997 -16 -402 2 5 3

ATOM 207 CB ARG 24 30.203 16.321 48.991 1.000 19.88

ANISOU 207 CB ARG 24 1685 2700 3169 -398 -218 4 4

ATOM 208 CG ARG 24 31.459 16.053 48.135 1.000 29.07

ANISOU 208 CG ARG 24 1467 4625 4954 269 203 7 0 9

ATOM 209 CD ARG 24 32.700 16.206 49.016 1.000 41.84

ANISOU 209 CD ARG 24 1745 7021 7130 -451 -494 - 922

ATOM 210 NE ARG 24 33.690 17.103 48.464 1.000 57.06

ANISOU 210 NE ARG 24 4362 9316 8003 -3326 -669 - 1141

ATOM 211 CZ ARG 24 34.032 18.327 48.810 1.000 60.67

ANISOU 211 CZ ARG 24 5961 10369 6723 -4627 -1324 - 1586

ATOM 212 NHl . ARG 24 33.430 18.980 49.799 1.000 49.70

ANISOU 212 NHl . ARG 24 7748 6565 4569 -951 -2185 2226

ATOM 213 NH- ^> ARG 24 34.997 18.971 48.159 1.000 54.12

ANISOU 213 NHl - ARG 24 8696 8490 3378 -3780 -2352 1607

ATOM 214 N CYS 25 27.092 16.963 49.370 1.000 15.74 ANISOU 214 N CYS 25 1435 1969 2574 -16 -393 - 3 3

ATOM 215 CA CYS 25 25.884 16.921 50.223 1.000 16.39

ANISOU 215 CA CYS 25 1518 1954 2756 -95 -317 - 300

ATOM 216 C CYS 25 24.826 16.068 49.547 1.000 15.73

ANISOU 216 C CYS 25 1629 1699 2648 -114 -432 6 6

ATOM 217 O CYS 25 24.124 15.262 50.155 1.000 15.89

ANISOU 217 O CYS 25 1453 1801 2783 -88 -469 2 5 2

ATOM 218 CB CYS 25 25.367 18.362 50.424 1.000 15.93

ANISOU 218 CB CYS 25 1644 1779 2629 -49 -261 - 3 0

ATOM 219 SG CYS 25 23.700 18.417 51.184 1.000 17.82

ANISOU 219 SG CYS 25 1742 1825 3202 -122 -33 - 55

ATOM 220 N LEU 26 24.623 16.308 48.250 1.000 15.25

ANISOU 220 N LEU 26 1449 1843 2504 -54 -263 - 142

ATOM 221 CA LEU 26 23.560 15.590 47.534 1.000 15.62

ANISOU 221 CA LEU 26 1616 1739 2580 -86 -453 4 8

ATOM 222 C LEU 26 23.763 14.085 47.621 1.000 15.18

ANISOU 222 C LEU 26 1697 1764 2306 -113 -479 6

ATOM 223 O LEU 26 22.819 13.345 47.771 1.000 16.96

ANISOU 223 O LEU 26 1797 1725 2920 -234 -664 - 300

ATOM 224 CB LEU 26 23.526 16.068 46.066 1.000 16.02

ANISOU 224 CB LEU 26 1811 1645 2633 -191 -483 12 2

ATOM 225 CG LEU 26 23.057 17.510 45.864 1.000 15.69

ANISOU 225 CG LEU 26 1762 1716 2485 -6 -15 7 9

ATOM 226 CD1 LEU 26 23.252 17.880 44.405 1.000 17.48

ANISOU 226 CD1 LEU 26 1750 2360 2532 -17 -130 4 65

ATOM 227 CD2 LEU 26 21.584 17.680 46.290 1.000 17.11

ANISOU 227 CD2 LEU 26 1655 2188 2660 -29 -75 1 68

ATOM 228 N ARG 27 25.027 13.648 47.494 1.000 17.26

ANISOU 228 N ARG 27 1870 1818 2871 155 -326 140

ATOM 229 CA ARG 27 25.295 12.205 47.372 1.000 18.75

ANISOU 229 CA ARG 27 2108 1845 3170 270 -955 102

ATOM 230 C ARG 27 25.240 11.599 48.744 1.000 17.95

ANISOU 230 C ARG 27 1667 1801 3351 159 -897 219

ATOM 231 O ARG 27 24.777 10.454 48.913 1.000 20.99

ANISOU 231 O ARG 27 2158 1793 4026 -43 -360 168

ATOM 232 CB ARG 27 26.641 12.008 46.670 1.000 21.35

ANISOU 232 CB ARG 27 2815 2034 3264 622 -377 - 129

ATOM 233 N ASP 28 25.827 12.293 49.723 1.000 16.71

ANISOU 233 N ASP 28 1487 2004 2856 178 -328 6 7

ATOM 234 CA ASP 28 26.034 11.672 51.026 1.000 17.47

ANISOU 234 CA ASP 28 1613 2095 2931 107 -301 12 7

ATOM 235 C ASP 28 24.872 11.866 51.990 1.000 17.22

ANISOU 235 C ASP 28 1414 2264 2863 223 -447 47 1

ATOM 236 O ASP 28 24.816 11.081 52.937 1.000 17.62

ANISOU 236 O ASP 28 1932 2139 2624 150 -565 3 2 7

ATOM 237 CB ASP 28 27.306 12.237 51.657 1.000 22.17

ANISOU 237 CB ASP 28 1581 3894 2948 -272 -467 5 5 9

ATOM 238 CG ASP 28 28.590 11.906 50.941 1.000 24.72

ANISOU 238 CG ASP 28 1596 3323 4472 236 -288 648

ATOM 239 ODl . ASP 28 28.572 10.905 50.199 1.000 27.56

ANISOU 239 ODl . ASP 28 2317 3071 5084 808 -284 572

ATOM 240 OD2 ! ASP 28 29.573 12.617 51.251 1.000 32.08

ANISOU 240 OD2 ! ASP 28 1584 4343 6261 -144 -470 4 16

ATOM 241 N LYS 29 24.098 12.942 51.821 1.000 15.57

ANISOU 241 N LYS 29 1475 1814 2627 5 -303 178

ATOM 242 CA LYS 29 23.048 13.305 52.778 1.000 15.13

ANISOU 242 CA LYS 29 1584 1999 2165 -68 -500 - 9 6

ATOM 243 C LYS 29 21.686 13.500 52.118 1.000 14.56

ANISOU 243 C LYS 29 1496 1352 2686 77 -452 1 0 6

ATOM 244 O LYS 29 20.688 12.985 52.635 1.000 16.21

ANISOU 244 O LYS 29 1627 1876 2657 -177 -315 - 5 ATOM 245 CB LYS 29 23.431 14.563 53.574 1.000 16.09

ANISOU 245 CB LYS 29 1666 1672 2777 3 -642 - 2 5

ATOM 246 CG LYS 29 24.776 14.421 54.292 1.000 17.68

ANISOU 246 CG LYS 29 2192 1918 2606 7 -1144 141

ATOM 247 CD LYS 29 25.161 15.647 55.096 1.000 20.71

ANISOU 247 CD LYS 29 2675 2044 3151 -35 -1518 4 1

ATOM 248 CE LYS 29 26.498 15.331 55.844 1.000 22.24

ANISOU 248 CE LYS 29 2203 2714 3535 142 -1369 - 685

ATOM 249 NZ LYS 29 26.955 16.594 56.492 1.000 32.67

ANISOU 249 NZ LYS 29 3199 3381 5831 -502 -2085 - 1260

ATOM 250 N GLY 30 21.604 14.198 50.993 1.000 14.09

ANISOU 250 N GLY 30 1552 1461 2340 135 -455 - 100

ATOM 251 CA GLY 30 20.358 14.373 50.250 1.000 14.09

ANISOU 251 CA GLY 30 1428 1561 2365 92 -342 - 97

ATOM 252 C GLY 30 19.372 15.284 50.955 1.000 12.30

ANISOU 252 C GLY 30 1423 1192 2059 -95 -275 9 4

ATOM 253 O GLY 30 18.168 15.223 50.696 1.000 14.58

ANISOU 253 0 GLY 30 1435 1689 2415 52 -476 - 121

ATOM 254 N LEU 31 19.884 16.146 51.823 1.000 13.93

ANISOU 254 N LEU 31 1472 1479 2343 -182 -248 - 181

ATOM 255 CA LEU 31 19.012 17.114 52.511 1.000 14.44

ANISOU 255 CA LEU 31 1534 1457 2495 -235 -55 -246

ATOM 256 C LEU 31 19.894 18.286 52.942 1.000 15.08

ANISOU 256 c LEU 31 1411 1535 2784 -177 -326 - 314

ATOM 257 0 LEU 31 21.113 18.136 53.140 1.000 15.64

ANISOU 257 0 LEU 31 1468 1664 2812 -169 -328 - 67

ATOM 258 CB LEU 31 18.222 16.560 53.694 1.000 16.76

ANISOU 258 CB LEU 31 2192 1664 2511 -367 128 -213

ATOM 259 CG LEU 31 18.883 16.517 55.039 1.000 20.16

ANISOU 259 CG LEU 31 2435 2485 2739 -289 -141 44 5

ATOM 260 CD1 LEU 31 17.977 16.145 56.202 1.000 26.49

ANISOU 260 CD1 LEU 31 2253 5076 2738 -508 -341 9 69

ATOM 261 CD2 LEU 31 20.052 15.526 55.032 1.000 24.73

ANISOU 261 CD2 LEU 31 4192 2967 2237 1001 153 610

ATOM 262 N PHE 32 19.289 19.462 53.052 1.000 14.11

ANISOU 262 N PHE 32 1569 1457 2335 -231 -179 -207

ATOM 263 CA PHE 32 20.020 20.697 53.417 1.000 13.56

ANISOU 263 CA PHE 32 1447 1389 2317 -225 -137 1 4

ATOM 264 C PHE 32 18.976 21.777 53.687 1.000 13.72

ANISOU 264 C PHE 32 1411 1439 2365 -218 -421 - 142

ATOM 265 O PHE 32 17.889 21.711 53.118 1.000 15.50

ANISOU 265 O PHE 32 1392 1862 2634 -175 -436 - 389

ATOM 266 CB PHE 32 20.958 21.157 52.308 1.000 15.01

ANISOU 266 CB PHE 32 1379 2201 2125 -305 -342 2 3 1

ATOM 267 CG PHE 32 20.381 21.156 50.920 1.000 14.60

ANISOU 267 CG PHE 32 1649 1662 2237 -193 -429 1 18

ATOM 268 CD1 PHE 32 20.326 19.986 50.148 1.000 14.53

ANISOU 268 CD1 PHE 32 1328 1688 2504 -156 -507 1 5

ATOM 269 CD2 PHE 32 19.831 22.345 50.396 1.000 13.66

ANISOU 269 CD2 PHE 32 1320 1678 2191 -179 -309 1 6 6

ATOM 270 CE1 . PHE 32 19.742 20.033 48.892 1.000 14.26

ANISOU 270 CE1 . PHE 32 1507 1655 2256 -346 -271 1 9 9

ATOM 271 CE2 : PHE 32 19.267 22.348 49.138 1.000 15.49

ANISOU 271 CE2 : PHE 32 1681 1932 2272 72 -504 - 126

ATOM 272 CZ PHE 32 19.177 21.184 48.385 1.000 15.25

ANISOU 272 CZ PHE 32 1979 1700 2117 -185 -295 1 68

ATOM 273 N TYR 33 19.376 22.785 54.442 1.000 14.44

ANISOU 273 N TYR 33 1813 1302 2372 -237 -496 - 5 0

ATOM 274 CA TYR 33 18.616 24.023 54.519 1.000 14.32

ANISOU 274 CA TYR 33 1764 1415 2261 -143 -295 - 111

ATOM 275 C TYR 33 19.039 24.929 53.364 1.000 13.70 ANISOU 275 C TYR 33 1479 1565 2161 -79 -459 - 5

ATOM 276 O TYR 33 20.158 24.871 52.859 1.000 15.28

ANISOU 276 0 TYR 33 1370 1524 2912 -190 -420 2 63

ATOM 277 CB TYR 33 18.874 24.734 55.853 1.000 14.47

ANISOU 277 CB TYR 33 1648 1717 2133 -197 -309 - 131

ATOM 278 CG TYR 33 18.231 24.046 57.049 1.000 15.71

ANISOU 278 CG TYR 33 2131 1537 2302 -339 -109 - 136

ATOM 279 CD1 TYR 33 16.938 24.390 57.453 1.000 17.41

ANISOU 279 CD1 TYR 33 2478 1967 2172 -154 246 - 249

ATOM 280 CD2 TYR 33 18.912 23.116 57.799 1.000 19.58

ANISOU 280 CD2 TYR 33 2901 2070 2468 144 115 1 92

ATOM 281 CE1 TYR 33 16.354 23.758 58.542 1.000 20.18

ANISOU 281 CE1 TYR 33 3138 1948 2581 26 740 - 102

ATOM 282 CE2 TYR 33 18.368 22.475 58.900 1.000 21.50

ANISOU 282 CE2 TYR 33 3571 2480 2118 340 196 12 2

ATOM 283 CZ TYR 33 17.081 22.821 59.263 1.000 22 .02

ANISOU 283 CZ TYR 33 4140 1772 2454 471 1035 - 105

ATOM 284 OH TYR 33 16.541 22.194 60.355 1.000 29.55

ANISOU 284 OH TYR 33 5088 2809 3329 377 1512 72 8

ATOM 285 N LEU 34 18.076 25.709 52.878 1.000 14.28

ANISOU 285 N LEU 34 1496 1533 2396 -80 -517 - 17

ATOM 286 CA LEU 34 18.278 26.620 51.756 1.000 15.02

ANISOU 286 CA LEU 34 1830 1452 2425 -126 -580 2 0

ATOM 287 C LEU 34 17.871 28.039 52.151 1.000 14.46

ANISOU 287 c LEU 34 1703 1575 2217 -146 -241 - 7

ATOM 288 0 LEU 34 16.716 28.289 52.492 1.000 16.95

ANISOU 288 0 LEU 34 1663 1852 2923 -75 -186 - 64

ATOM 289 CB LEU 34 17.389 26.127 50.598 1.000 16.54

ANISOU 289 CB LEU 34 2355 1485 2444 -212 -749 2 5

ATOM 290 CG LEU 34 17.633 26.800 49.249 1.000 15.65

ANISOU 290 CG LEU 34 2010 1567 2371 -7 -633 - 63

ATOM 291 CD1 LEU 34 18.977 26.422 48.664 1.000 20.14

ANISOU 291 CD1 LEU 34 1919 2018 3717 -225 -171 2 60

ATOM 292 CD2 LEU 34 16.490 26.535 48.291 1.000 17.29

ANISOU 292 CD2 LEU 34 2152 1824 2592 -425 -819 2 14

ATOM 293 N THR 35 18.842 28.944 52.065 1.000 15.48

ANISOU 293 N THR 35 1817 1532 2534 -230 -200 1 3

ATOM 294 CA THR 35 18.587 30.362 52.324 1.000 17.02

ANISOU 294 CA THR 35 2149 1537 2781 -206 -827 - 196

ATOM 295 C THR 35 18.491 31.127 51.010 1.000 17.04

ANISOU 295 C THR 35 1895 1693 2887 -149 -882 - 44

ATOM 296 O THR ^' 35 18.765 30.572 49.938 1.000 17.01

ANISOU 296 O THR 35 1880 1692 2893 -262 -458 144

ATOM 297 CB THR 35 19.772 30.917 53.180 1.000 17.79

ANISOU 297 CB THR 35 2018 1942 2800 -87 -854 - 200

ATOM 298 OG1 THR 35 20.986 30.673 52.474 1.000 21.10

ANISOU 298 OG1 . THR 35 2110 2035 3873 -253 -364 - 402

ATOM 299 CG2 THR 35 19.847 30.331 54.567 1.000 20.44

ANISOU 299 CG2 THR 35 2600 2194 2971 228 -1113 5 9

ATOM 300 N ASP 36 18.186 32.407 51.059 1.000 18.62

ANISOU 300 N ASP 36 2287 1747 3040 -187 -316 149

ATOM 301 CA ASP 36 18.240 33.300 49.884 1.000 20.75

ANISOU 301 CA ASP 36 2678 1722 3483 -632 -508 3 74

ATOM 302 C ASP 36 17.474 32.711 48.703 1.000 20.05

ANISOU 302 C ASP 36 2104 1929 3586 198 -928 4 8 9

ATOM 303 O ASP 36 17.929 32.685 47.540 1.000 21.06

ANISOU 303 O ASP 36 2593 1749 3662 -496 -756 13 1

ATOM 304 CB ASP 36 19.703 33.561 49.500 1.000 22.21

ANISOU 304 CB ASP 36 2666 2366 3406 -876 -755 8 07

ATOM 305 CG ASP 36 20.588 34.192 50.551 1.000 23 .05

ANISOU 305 CG ASP 36 2537 1818 4402 -175 -833 - 208 ATOM 306 ODl ASP 36 20.061 34.886 51.457 1.000 26.16

ANISOU 306 ODl ASP 36 2981 2100 4860 378 -777 - 381

ATOM 307 OD2 ASP 36 21.824 33.982 50.528 1.000 24.87

ANISOU 307 OD2 ASP 36 2532 1994 4924 -49 -950 - 628

ATOM 308 N CYS 37 16.282 32.196 48.971 1.000 20.25

ANISOU 308 N CYS 37 2135 1711 3849 118 -638 - 263

ATOM 309 CA CYS 37 15.463 31.587 47.902 1.000 20.28

ANISOU 309 CA CYS 37 2390 1478 3839 136 -799 - 138

ATOM 310 C CYS 37 14.078 32.183 47.818 1.000 19.90

ANISOU 310 C CYS 37 2374 1724 3463 214 -711 - 74

ATOM 311 O CYS 37 13.176 31.629 47.156 1.000 22 .75

ANISOU 311 O CYS 37 2569 1984 4091 -12 -1108 1 5

ATOM 312 CB CYS 37 15.359 30.061 48.083 1.000 22 .21

ANISOU 312 CB CYS 37 2739 1454 4247 194 -477 - 115

ATOM 313 SG CYS 37 14.500 29.595 49.596 1.000 22 .84

ANISOU 313 SG CYS 37 2854 1884 3942 -203 -922 141

ATOM 314 N GLY 38 13.855 33.390 48.314 1.000 20.85

ANISOU 314 N GLY 38 2353 1638 3933 217 -375 - 42

ATOM 315 CA GLY 38 12.570 34.044 48.194 1.000 23 .42

ANISOU 315 CA GLY 38 2233 1874 4790 255 -292 1 65

ATOM 316 C GLY 38 11.534 33.619 49.217 1.000 23 .29

ANISOU 316 C GLY 38 2577 2045 4228 113 -136 - 601

ATOM 317 O GLY 38 10.400 34.091 49.129 1.000 25.58

ANISOU 317 O GLY 38 2529 3424 3765 214 -96 - 264

ATOM 318 N LEU 39 11.894 32.836 50.237 1.000 24.55

ANISOU 318 N LEU 39 2310 2980 4037 119 -46 - 364

ATOM 319 CA LEU 39 10.938 32.331 51.195 1.000 24.44

ANISOU 319 CA LEU 39 2637 2964 3684 -105 175 - 946

ATOM 320 C LEU 39 11.107 32.885 52.593 1.000 35.41

ANISOU 320 C LEU 39 5341 4215 3898 -796 165 -1435

ATOM 321 O LEU 39 11.784 32.313 53.441 1.000 43 .41

ANISOU 321 O LEU 39 7338 4986 4171 -2639 -1333 - 303

ATOM 322 CB LEU 39 10.850 30.810 51.206 1.000 26.48

ANISOU 322 CB LEU 39 4244 2940 2879 49 -70 - 261

ATOM 323 CG LEU 39 10.404 30.097 49.921 1.000 30.21

ANISOU 323 CG LEU 39 4834 2452 4195 258 -1618 -474

ATOM 324 CD1 LEU 39 10.683 28.595 49.972 1.000 24.78

ANISOU 324 CD1 LEU 39 3351 2597 3468 424 -707 - 118

ATOM 325 CD2 LEU 39 8.940 30.407 49.640 1.000 27.50

ANISOU 325 CD2 LEU 39 4828 2118 3503 860 -860 - 323

ATOM 326 N THR 40 10.365 33.957 52.882 1.000 45.58

ANISOU 326 N THR 40 7392 4849 5077 -520 2852 -1993

ATOM 327 CA THR 40 10.610 34.661 54.136 1.000 32.50

ANISOU 327 CA THR 40 4224 3732 4393 999 961 - 558

ATOM 328 C THR 40 9.700 34.177 55.248 1.000 29.68

ANISOU 328 C THR 40 3175 4204 3898 -116 294 -1630

ATOM 329 O THR 40 8.653 33.556 55.031 1.000 39.75

ANISOU 329 O THR 40 3930 5847 5326 -1079 -301 - 1653

ATOM 330 CB THR 40 10.641 36.183 53.997 1.000 56.31

ANISOU 330 CB THR 40 10586 3758 7052 -1417 1006 - 992

ATOM 331 OGl . THR 40 11.545 36.606 52.946 1.000 68.39

ANISOU 331 OGl . THR 40 7379 3900 14707 -1978 3617 - 246

ATOM 332 CG2 ! THR 40 11.214 36.837 55.256 1.000 70.22

ANISOU 332 CG2 ! THR 40 8265 5228 13188 1389 -4422 -3241

ATOM 333 N ASP 41 10.191 34.302 56.486 1.000 33 .20

ANISOU 333 N ASP 41 3580 5223 3810 -203 307 -1779

ATOM 334 CA ASP 41 9.329 33.943 57.613 1.000 27.51

ANISOU 334 CA ASP 41 2705 3858 3891 91 -253 - 1061

ATOM 335 C ASP 41 8.107 34.861 57.660 1.000 33 .43

ANISOU 335 C ASP 41 3131 3064 6508 32 547 -1307

ATOM 336 O ASP 41 7.034 34.469 58.101 1.000 30.76 ANISOU 336 O ASP 41 2690 3223 5774 141 -149 - 969

ATOM 337 CB ASP 41 10.113 34.135 58.915 1.000 33 .51

ANISOU 337 CB ASP 41 4853 4026 3852 -1222 -698 - 938

ATOM 338 CG ASP 41 9.453 33.351 60.039 1.000 33 .37

ANISOU 338 CG ASP 41 3324 5291 4065 -739 -501 - 571

ATOM 339 ODl ASP 41 9.152 32.164 59.780 1.000 34 .95

ANISOU 339 ODl ASP 41 4040 4681 4557 -380 824 - 9 2

ATOM 340 OD2 ASP 41 9.395 33.904 61.161 1.000 86.76

ANISOU 340 OD2 ASP 41 18972 10427 3567 -10425 588 - 1858

ATOM 341 N THR 42 8.272 36.089 57.205 1.000 32 .71

ANISOU 341 N THR 42 3217 3695 5516 9 -58 - 586

ATOM 342 CA THR 42 7.198 37.074 57.221 1.000 38.48

ANISOU 342 CA THR 42 4747 4161 5711 1067 -861 - 630

ATOM 343 C THR 42 6.005 36.640 56.375 1.000 35.83

ANISOU 343 c THR 42 3333 4044 6237 1136 157 -1162

ATOM 344 0 THR 42 4.877 36.606 56.900 1.000 38.90

ANISOU 344 0 THR 42 4048 3603 7128 1186 1059 1224

ATOM 345 CB THR 42 7.751 38.449 56.815 1.000 37.05

ANISOU 345 CB THR 42 4526 3763 5788 1021 -677 - 1532

ATOM 346 OGl THR 42 8.831 38.301 55.889 1.000 98.08

ANISOU 346 OGl THR 42 16381 13757 7127 -3208 7500 -2318

ATOM 347 CG2 THR 42 8.358 39.113 58.047 1.000 36.08

ANISOU 347 CG2 THR 42 6097 3613 3997 886 -1119 2 69

ATOM 348 N GLU 43 6.259 36.184 55.173 1.000 34.64

ANISOU 348 N GLU 43 4208 3312 5642 656 -275 - 698

ATOM 349 CA GLU 43 5.391 35.557 54.192 1.000 32 .98

ANISOU 349 CA GLU 43 3527 2886 6120 1199 -883 - 152

ATOM 350 C GLU 43 4.701 34.300 54.713 1.000 41.67

ANISOU 350 C GLU 43 3454 4151 8229 225 -1743 953

ATOM 351 O GLU 43 3.484 34.124 54.605 1.000 38.53

ANISOU 351 O GLU 43 3375 4041 7222 589 -1417 - 578

ATOM 352 CB GLU 43 6.278 35.074 53.026 1.000 44.72

ANISOU 352 CB GLU 43 5991 4098 6901 28 137 -2137

ATOM 353 CG GLU 43 6.658 36.125 52.003 1.000 53.42

ANISOU 353 CG GLU 43 5931 6417 7949 -993 1540 -1338

ATOM 354 CD GLU 43 7.838 36.976 52.429 1.000 50.41

ANISOU 354 CD GLU 43 4087 7601 7467 -439 2486 -1725

ATOM 355 OEl GLU 43 8.024 37.112 53.661 1.000 59.44

ANISOU 355 OEl GLU 43 7237 7592 7757 -1284 1632 -2146

ATOM 356 OE2 GLU 43 8.555 37.476 51.531 1.000 71.33

ANISOU 356 OE2 GLU 43 11550 6344 9207 -4131 6267 -4645

ATOM 357 N LEU 44 5.511 33.373 55.224 1.000 27.80

ANISOU 357 N LEU 44 2837 2924 4802 -55 -626 - 227

ATOM 358 CA LEU 44 4.926 32.222 55.902 1.000 27.88

ANISOU 358 CA LEU 44 2207 3379 5009 241 813 - 382

ATOM 359 C LEU 44 3.886 32.670 56.934 1.000 34.30

ANISOU 359 C LEU 44 1930 4771 6333 -537 776 -2629

ATOM 360 O LEU 44 2.781 32.159 56.924 1.000 33 .35

ANISOU 360 O LEU 44 2046 5235 5390 -840 705 -2397

ATOM 361 CB LEU 44 5.999 31.394 56.587 1.000 24.59

ANISOU 361 CB LEU 44 2781 3494 3070 81 940 - 74

ATOM 362 CG LEU 44 5.592 30.147 57.343 1.000 31.76

ANISOU 362 CG LEU 44 2414 5135 4517 -845 792 1217

ATOM 363 CD1 . LEU 44 4.563 29.328 56.575 1.000 47.71

ANISOU 363 CD1 . LEU 44 5860 7081 5188 -3576 3333 -2541

ATOM 364 CD2 : LEU 44 6.793 29.259 57.653 1.000 51.56

ANISOU 364 CD2 ! LEU 44 6294 3688 9608 1956 2240 1382

ATOM 365 N LYS 45 4.212 33.712 57.694 1.000 41.91

ANISOU 365 N LYS 45 2865 6802 6256 -1455 381 -3^'537

ATOM 366 CA LYS 45 3.369 34.195 58.773 1.000 44.31

ANISOU 366 CA LYS 45 4768 5427 6639 74 837 -2985 ATOM 367 C LYS 45 1.981 34.582 58.278 1.000 38.58

ANISOU 367 C LYS 45 4535 3445 6681 -245 1221 - 2820

ATOM 368 O LYS 45 0.984 34.238 58.902 1.000 39.93

ANISOU 368 O LYS 45 4857 3594 6720 262 1634 - 2337

ATOM 369 CB LYS 45 4.038 35.400 59.447 1.000 50.20

ANISOU 369 CB LYS 45 4944 5561 8569 1081 -447 - 3980

ATOM 370 CG LYS 45 3.082 36.546 59.706 1.000 53 .07

ANISOU 370 CG LYS 45 3548 6321 10296 1148 -2094 -4809

ATOM 371 CD LYS 45 3.714 37.922 59.622 1.000 58.29

ANISOU 371 CD LYS 45 4723 5694 11730 1422 -3745 -5024

ATOM 372 CE LYS 45 3.199 38.793 60.761 1.000 65.33

ANISOU 372 CE LYS 45 6294 6898 11629 1072 -3430 -5603

ATOM 373 NZ LYS 45 1.713 38.779 60.852 1.000 73 .75

ANISOU 373 NZ LYS 45 6392 9216 12412 -718 -1071 - 7436

ATOM 374 N SER 46 1.973 35.341 57.193 1.000 36.94

ANISOU 374 N SER 46 4074 3478 6484 -956 1068 - 2939

ATOM 375 CA SER 46 0.743 35.856 56.607 1.000 37.61

ANISOU 375 CA SER 46 3983 3417 6892 -1335 988 -2335

ATOM 376 C SER 46 -0.137 34.702 56.137 1.000 34.45

ANISOU 376 c SER 46 3430 3057 6602 -1104 1656 -2394

ATOM 377 0 SER 46 -1.337 34.625 56.449 1.000 29.50

ANISOU 377 0 SER 46 3195 2789 5224 -587 1093 -1206

ATOM 378 CB SER 46 1.160 36.726 55.419 1.000 40.36

ANISOU 378 CB SER 46 4102 3809 7425 -2099 617 - 1930

ATOM 379 OG SER 46 0.018 37.017 54.630 1.000 43 .38

ANISOU 379 OG SER 46 5005 3431 8048 -1261 53 - 1863

ATOM 380 N ALA 47 0.493 33.808 55.361 1.000 29.82

ANISOU 380 N ALA 47 3246 2173 5910 -18 809 - 1228

ATOM 381 CA ALA 47 -0.208 32.623 54.879 1.000 25.84

ANISOU 381 CA ALA 47 3566 2106 4148 7 630 - 891

ATOM 382 C ALA 47 -0.722 31.792 56.058 1.000 25.02

ANISOU 382 C ALA 47 2591 2344 4572 481 280 - 280

ATOM 383 O ALA 47 -1.888 31.381 56.063 1.000 23.19

ANISOU 383 O ALA 47 2850 2366 3597 129 318 -1119

ATOM 384 CB ALA 47 0.615 31.791 53.912 1.000 26.76

ANISOU 384 CB ALA 47 2892 2764 4511 270 351 -1134

ATOM 385 N LYS 48 0.132 31.529 57.041 1.000 24.64

ANISOU 385 N LYS 48 3107 2076 4178 130 -57 -1085

ATOM 386 CA LYS 48 -0.186 30.712 58.202 1.000 25.83

ANISOU 386 CA LYS 48 3545 2979 3291 -16 30 -1416

ATOM 387 C LYS 48 -1.337 31.339 59.003 1.000 28.58

ANISOU 387 c LYS 48 3373 3344 4144 -354 129 -2041

ATOM 388 0 LYS 48 -2.310 30.694 59.396 1.000 27.04

ANISOU 388 0 LYS 48 3849 2793 3633 312 419 - 634

ATOM 389 CB LYS 48 1.035 30.654 59.149 1.000 28.95

ANISOU 389 CB LYS 48 3507 3294 4200 -274 -257 - 738

ATOM 390 CG LYS 48 0.775 29.694 60.313 1.000 32.96

ANISOU 390 CG LYS 48 4412 3214 4897 113 -543 - 156

ATOM 391 CD LYS 48 1.418 30.222 61.570 1.000 39.92

ANISOU 391 CD LYS 48 5828 4616 4724 705 -1278 - 3 9

ATOM 392 CE LYS 48 1.217 29.320 62.769 1.000 33 .67

ANISOU 392 CE LYS 48 3973 4020 4799 1402 -205 - 356

ATOM 393 NZ LYS 48 0.731 30.100 63.946 1.000 38.33

ANISOU 393 NZ LYS 48 4516 5230 4816 916 -1039 -1555

ATOM 394 N ASP 49 -1.253 32.656 59.255 1.000 23 .78

ANISOU 394 N ASP 49 2796 3136 3104 79 -459 -1588

ATOM 395 CA ASP 49 -2.298 33.326 60.006 1.000 24.05

ANISOU 395 CA ASP 49 2826 2913 3398 -291 366 -1043

ATOM 396 C ASP 49 -3.679 33.181 59.366 1.000 24.45

ANISOU 396 C ASP 49 2721 3270 3300 -220 555 -1454

ATOM 397 O ASP 49 -4.637 32.951 60.082 1.000 27.10 ANISOU 397 O ASP 49 2863 3177 4257 -368 1004 - 1544

ATOM 398 CB ASP 49 -2.034 34.824 60.167 1.000 30.34

ANISOU 398 C3 ASP 49 3695 3210 4623 -559 713 - 2178

ATOM 399 CG ASP 49 -0.924 35.181 61.128 1.000 37.18

ANISOU 399 CG ASP 49 5259 4057 4810 -1109 -211 -2007

ATOM 400 ODl ASP 49 -0.556 34.266 61.904 1.000 33 .36

ANISOU 400 ODl ASP 49 3717 4549 4408 -737 888 -1727

ATOM 401 OD2 ASP 49 -0.525 36.375 61.087 1.000 48.45

ANISOU 401 OD2 ASP 49 7960 3575 6875 -927 -2887 -2409

ATOM 402 N LEU 50 -3.788 33.402 58.059 1.000 24.46

ANISOU 402 N LEU 50 3114 2668 3513 374 200 - 1298

ATOM 403 CA LEU 50 -5.123 33.344 57.471 1.000 22.92

ANISOU 403 CA LEU 50 2949 2145 3614 161 397 - 562

ATOM 404 C LEU 50 -5.679 31.937 57.328 1.000 21.79

ANISOU 404 C LEU 50 3345 2197 2737 33 417 - 556

ATOM 405 O LEU 50 -6.878 31.741 57.475 1.000 24.96

ANISOU 405 O LEU 50 3463 2502 3517 -276 766 - 1181

ATOM 406 CB LEU 50 -5.254 34.137 56.194 1.000 22.13

ANISOU 406 CB LEU 50 3127 2016 3266 -103 524 - 757

ATOM 407 CG LEU 50 -6.661 34.578 55.807 1.000 28.87

ANISOU 407 CG LEU 50 3549 3538 3881 961 825 2 08

ATOM 408 CD1 LEU 50 -7.389 35.082 57.049 1.000 52.72

ANISOU 408 CD1 LEU 50 4567 8556 6907 940 2929 - 1936

ATOM 409 CD2 LEU 50 -6.644 35.642 54.723 1.000 41.07

ANISOU 409 CD2 LEU 50 6971 3395 5240 -1005 -2258 8 57

ATOM 410 N VAL 51 -4.801 30.956 57.138 1.000 21.78

ANISOU 410 N VAL 51 3345 2052 2877 -160 216 - 860

ATOM 411 CA VAL 51 -5.293 29.580 57.118 1.000 19.40

ANISOU 411 CA VAL 51 2631 2056 2683 -12 173 - 303

ATOM 412 C VAL 51 -5.631 29.135 58.533 1.000 25.25

ANISOU 412 C VAL 51 4453 2656 2485 -753 587 - 955

ATOM 413 O VAL 51 -6.652 28.454 58.725 1.000 25.07

ANISOU 413 O VAL 51 4555 2176 2795 -484 1185 - 827

ATOM 414 CB VAL 51 -4.377 28.589 56.396 1.000 18.78

ANISOU 414 CB VAL 51 2729 1786 2620 -72 171 - 313

ATOM 415 CGI VAL 51 -3.152 28.238 57.231 1.000 20.42

ANISOU 415 CGI VAL 51 3002 1841 2918 295 -13 -480

ATOM 416 CG2 VAL 51 -5.147 27.306 56.021 1.000 24.10

ANISOU 416 CG2 VAL 51 3112 2337 3708 -511 355 - 846

ATOM 417 N ILE 52 -4.836 29.500 59.534 1.000 25.23

ANISOU 417 N ILE 52 4514 2471 2603 388 76 - 874

ATOM 418 CA ILE 52 -5.205 29.114 60.921 1.000 24.38

ANISOU 418 CA ILE 52 3488 3010 2765 248 19 - 509

ATOM 419 C ILE 52 -6.498 29.771 61.355 1.000 24.20

ANISOU 419 C ILE 52 3026 2482 3687 -354 114 - 648

ATOM 420 O ILE 52 -7.328 29.182 62.071 1.000 27.73

ANISOU 420 O ILE 52 3735 2812 3989 -198 614 - 334

ATOM 421 CB ILE 52 -4.016 29.427 61.829 1.000 27.59

ANISOU 421 CB ILE 52 3321 4347 2815 590 0 - 785

ATOM 422 CGI ILE 52 -2.853 28.439 61.510 1.000 31.45

ANISOU 422 CGI ILE 52 3278 5248 3425 741 363 -1288

ATOM 423 CG2 ILE 52 -4.293 29.312 63.317 1.000 33 .62

ANISOU 423 CG2 ILE 52 3827 6199 2750 881 150 -1454

ATOM 424 CD1 . ILE 52 -1.930 28.351 62.710 1.000 36.22

ANISOU 424 CD1 . ILE 52 3956 5082 4722 979 -601 - 234

ATOM 425 N ASP 53 -6.771 30.992 60.913 1.000 24.56

ANISOU 425 N ASP 53 3479 2878 2974 165 609 -426

ATOM 426 CA ASP 53 -8.051 31.646 61.278 1.000 23 .50

ANISOU 426 CA ASP 53 3242 2942 2745 -5 355 - 677

ATOM 427 C ASP 53 -9.201 30.929 60.594 1.000 26.34

ANISOU 427 C ASP 53 3462 2986 3561 -435 612 -1064 ATOM 428 O ASP 53 -10.342 30.836 61.051 1.000 29.73

ANISOU 428 O ASP 53 3468 3085 4743 -436 937 -1142

ATOM 429 CB ASP 53 -7.964 33.084 60.772 1.000 33.83

ANISOU 429 CB ASP 53 3800 2322 6730 -92 1806 - 933

ATOM 430 CG ASP 53 -9.308 33.758 60.583 1.000 32 .05

ANISOU 430 CG ASP 53 4652 2412 5113 172 -302 - 1138

ATOM 431 ODl ASP 53 -9.653 34.524 61.486 1.000 43 .68

ANISOU 431 ODl ASP 53 3661 4686 8248 150 1379 - 3120

ATOM 432 OD2 ASP 53 -9.950 33.556 59.532 1.000 51.30

ANISOU 432 OD2 ASP 53 8386 6074 5033 -2062 -1738 922

ATOM 433 N PHE 54 -8.933 30.376 59.413 1.000 25.39

ANISOU 433 N PHE 54 3372 2640 3637 72 71 -1176

ATOM 434 CA PHE 54 -9.917 29.557 58.704 1.000 24.10

ANISOU 434 CA PHE 54 3015 3264 2876 -366 263 - 539

ATOM 435 C PHE 54 -10.180 28.259 59.456 1.000 24.00

ANISOU 435 C PHE 54 3264 3174 2680 -365 459 - 688

ATOM 436 O PHE 54 -11.333 27.893 59.686 1.000 28.19

ANISOU 436 O PHE 54 3551 3246 3914 -549 1305 - 1130

ATOM 437 CB PHE 54 -9.465 29.273 57.263 1.000 23.62

ANISOU 437 CB PHE 54 3241 2955 2779 -249 218 - 434

ATOM 438 CG PHE 54 -10.522 28.499 56.461 1.000 27.62

ANISOU 438 CG PHE 54 4712 2945 2838 -694 -636 1 4

ATOM 439 CD1 PHE 54 -11.729 29.078 56.087 1.000 31.38

ANISOU 439 CD1 PHE 54 3613 4658 3654 -951 -262 - 621

ATOM 440 CD2 PHE 54 -10.283 27.210 56.033 1.000 30.92

ANISOU 440 CD2 PHE 54 5782 3589 2377 -831 293 - 844

ATOM 441 CE1 PHE 54 -12.653 28.406 55.307 1.000 44.29

ANISOU 441 CE1 PHE 54 5504 5404 5919 -3066 -2057 1178

ATOM 442 CE2 PHE 54 -11.228 26.503 55.306 1.000 38.69

ANISOU 442 CE2 PHE 54 7997 4412 2289 -2803 155 - 387

ATOM 443 CZ PHE 54 -12.424 27.092 54.927 1.000 42.33

ANISOU 443 CZ PHE 54 5992 6305 3787 -4256 54 - 446

ATOM 444 N PHE 55 -9.126 27.558 59.870 1.000 25.87

ANISOU 444 N PHE 55 3787 2768 3276 -85 431 - 839

ATOM 445 CA PHE 55 -9.195 26.310 60.625 1.000 25.69

ANISOU 445 CA PHE 55 3567 3042 3151 68 763 - 711

ATOM 446 C PHE 55 -9.929 26.484 61.944 1.000 27.69

ANISOU 446 C PHE 55 3357 3961 3205 181 703 - 719

ATOM 447 O PHE 55 -10.745 25.670 62.373 1.000 30.08

ANISOU 447 O PHE 55 4046 4165 3217 142 878 - 127

ATOM 448 CB PHE 55 -7.759 25.873 60.932 1.000 25.48

ANISOU 448 CB PHE 55 3556 3159 2964 117 835 - 638

ATOM 449 CG PHE 55 -7.019 25.242 59.762 1.000 26.31

ANISOU 449 CG PHE 55 3437 3039 3522 -468 1068 - 1156

ATOM 450 CD1 PHE 55 -7.611 24.820 58.590 1.000 27.09

ANISOU 450 CD1 PHE 55 3553 3895 2845 -1018 1404 - 658

ATOM 451 CD2 PHE 55 -5.651 25.031 59.935 1.000 31.68

ANISOU 451 CD2 PHE 55 3244 4185 4609 -726 1123 -2221

ATOM 452 CE1 PHE 55 -6.878 24.150 57.621 1.000 23.8

ANISOU 452 CE1 PHE 55 3472 2525 3079 -58 551 - 547

ATOM 453 CE2 PHE 55 -4.904 24.433 58.950 1.000 31.74

ANISOU 453 CE2 PHE 55 3487 4387 4186 226 337 -2304

ATOM 454 CZ PHE 55 -5.514 24.004 57.770 1.000 24.23

ANISOU 454 CZ PHE 55 3706 2187 3312 414 -22 -416

ATOM 455 N GLU 56 -9.633 27.581 62.629 1.000 30.39

ANISOU 455 N GLU 56 3961 5033 2553 -308 520 - 1110

ATOM 456 CA GLU 56 -10.22- > 27.875 63.925 1.000 30.18

ANISOU 456 CA GLU 56 4160 4504 2805 -734 1221 - 637

ATOM 457 C GLU 56 -11.65028.401 63.820 1.000 33.50

ANISOU 457 C GLU 56 4324 4124 4280 -535 1489 - 892

ATOM 458 O GLU 56 -12.47028.149 64.708 1.000 44.44 ANISOU 458 O GLU 56 3864 8872 4150 93 1013 1011

ATOM 459 CB GLU 56 -9.403 28.978 64.615 1.000 35 .85

ANISOU 459 CB GLU 56 5037 5109 3475 -221 574 - 1821

ATOM 460 CG GLU 56 -8.192 28.508 65.401 1.000 38 .63

ANISOU 460 CG GLU 56 4804 7152 2721 -337 763 - 1692

ATOM 461 CD GLU 56 -7.395 29.699 65.916 1.000 45.55

ANISOU 461 CD GLU 56 5576 7183 4546 -24 -295 - 2330

ATOM 462 OEl GLU 56 -7.935 30.828 65.888 1.000 55.54

ANISOU 462 OEl GLU 56 7344 7247 6512 586 2570 - 3059

ATOM 463 OE2 GLU 56 -6.246 29.492 66.350 1.000 50.41

ANISOU 463 OE2 GLU 56 4050 10497 4606 -1066 1163 - 2063

ATOM 464 N HIS 57 -11.890 29.289 62.866 1.000 32 .20

ANISOU 464 N HIS 57 3273 4700 4261 -549 1540 - 670

ATOM 465 CA HIS 57 -13.101 30.078 62.909 1.000 33 .38

ANISOU 465 CA HIS 57 3795 4885 4002 -110 1553 - 1239

ATOM 466 C HIS 57 -13.981 29.873 61.697 1.000 32 .85

ANISOU 466 C HIS 57 3380 4736 4367 278 1506 - 1797

ATOM 467 O HIS 57 -15.012 30.533 61.571 1.000 37.09

ANISOU 467 O HIS 57 3362 4733 5998 276 1087 - 2205

ATOM 468 CB HIS 57 -12.802 31.573 62.976 1.000 37.39

ANISOU 468 CB HIS 57 4327 4959 4922 -193 1402 - 1970

ATOM 469 CG HIS 57 -11.981 31.949 64.162 1.000 36.99

ANISOU 469 CG HIS 57 4111 5046 4896 680 1344 - 2319

ATOM 470 NDl HIS 57 -12.465 31.917 65.453 1.000 38.84

ANISOU 470 NDl HIS 57 5090 4844 4823 -171 1362 -1598

ATOM 471 CD2 HIS 57 -10.707 32.387 64.232 1.000 37.91

ANISOU 471 CD2 HIS 57 5259 4197 4947 -891 1544 -2828

ATOM 472 CE1 HIS 57 -11.510 32.305 66.275 1.000 40.37

ANISOU 472 CE1 HIS 57 5481 5191 4668 -243 1087 - 1361

ATOM 473 NE2 HIS 57 -10.441 32.592 65.552 1.000 35.63

ANISOU 473 NE2 HIS 57 4420 4376 4743 980 799 -1492

ATOM 474 N GLY 58 -13.464 29.068 60.786 1.000 32.06

ANISOU 474 N GLY 58 4402 3186 4594 5 1572 -1525

ATOM 475 CA GLY 58 -14.290 28.731 59.627 1.000 35.74

ANISOU 475 CA GLY 58 4508 4402 4669 -1129 1877 - 1893

ATOM 476 C GLY 58 -15.449 27.859 60.099 1.000 31.52

ANISOU 476 C GLY 58 3317 3688 4969 308 1657 - 593

ATOM 477 O GLY 58 -15.245 26.952 60.922 1.000 32.66

ANISOU 477 O GLY 58 4561 4176 3674 -204 624 -1012

ATOM 478 N SER 59 -16.632 28.152 59.574 1.000 31.03

ANISOU 478 N SER 59 3786 3623 4379 519 1142 -1442

ATOM 479 CA SER 59 -17.823 27.359 59.859 1.000 32.03

ANISOU 479 CA SER 59 3305 3925 4939 757 850 -1188

ATOM 480 C SER 59 -17.763 26.034 59.117 1.000 37.27

ANISOU 480 C SER 59 3654 4001 6507 0 2065 - 1682

ATOM 481 O SER 59 -16.987 25.858 58.181 1.000 31.23

ANISOU 481 O SER 59 3027 3655 5184 613 1003 - 1174

ATOM 482 CB SER 59 -19.077 28.136 59.444 1.000 39 .80

ANISOU 482 CB SER 59 3930 5925 5266 1707 -545 -2846

ATOM 483 OG SER 59 -19.252 28.159 58.029 1.000 35.38

ANISOU 483 OG SER 59 3505 4800 5137 355 119 -1624

ATOM 484 N GLU 60 -18.589 25.065 59.507 1.000 46.32

ANISOU 484 N GLU 60 5438 6083 6078 -2395 2115 -2700

ATOM 485 CA GLU 60 -18.573 23.801 58.754 1.000 34.21

ANISOU 485 CA GLU 60 3381 4798 4818 -960 716 - 1238

ATOM 486 C GLU 60 -19.033 24.055 57.330 1.000 34.22

ANISOU 486 C GLU 60 4659 3711 4632 455 1378 - 847

ATOM 487 O GLU 60 -18.616 123.437 56.361 1.000 29.91

ANISOU 487 O GLU 60 3708 3040 4615 -679 2037 - 604

ATOM 488 CB GLU 60 -19.39C ) 22.742 59.488 1.000 38 .26

ANISOU 488 CB GLU 60 5012 5567 3958 -1599 748 - 1000 ATOM 489 CG GLU 60 -18.625 22.182 60.678 1.000 42 .01

ANISOU 489 CG GLU 60 5470 5439 5055 503 950 - 782

ATOM 490 CD GLU 60 -17.307 21.528 60.312 1.000 45.34

ANISOU 490 CD GLU 60 4036 7496 5695 -885 1094 -2276

ATOM 491 OEl GLU 60 -17.21920.867 59.264 1.000 49.69

ANISOU 491 OEl GLU 60 5383 6689 6809 -864 1730 - 2838

ATOM 492 OE2 GLU 60 -16.323 21.659 61.084 1.000 43 .62

ANISOU 492 OE2 GLU 60 4677 4974 6924 -1984 109 - 12

ATOM 493 N ALA 61 -19.92825.028 57.167 1.000 34.26

ANISOU 493 N ALA 61 3091 3912 6014 -81 1209 - 1122

ATOM 494 CA ALA 61 -20.408 25.324 55.823 1.000 33 .07

ANISOU 494 CA ALA 61 1647 4409 6508 -228 657 -1105

ATOM 495 C ALA 61 -19.31425.876 54.938 1.000 30.69

ANISOU 495 C ALA 61 2053 3742 5866 -59 640 - 1066

ATOM 496 O ALA 61 -19.138 25.482 53.790 1.000 31.15

ANISOU 496 O ALA 61 2754 2893 6189 31 793 - 1285

ATOM 497 CB ALA 61 -21.543 26.336 55.932 1.000 34.43

ANISOU 497 CB ALA 61 2783 4403 5897 288 1210 - 1650

ATOM 498 N GLU 62 -18.568 26.824 55.498 1.000 28.80

ANISOU 498 N GLU 62 2168 3404 5371 -9 915 - 964

ATOM 499 CA GLU 62 -17.478 27.395 54.704 1.000 26.78

ANISOU 499 CA GLU 62 2339 2374 5461 423 871 - 413

ATOM 500 C GLU 62 -16.43226.330 54.389 1.000 22.61

ANISOU 500 C GLU 62 2569 1621 4402 84 1049 - 376

ATOM 501 O GLU 62 -15.85126.316 53.289 1.000 24.41

ANISOU 501 O GLU 62 2399 2669 4209 -132 801 -548

ATOM 502 CB GLU 62 -16.86128.591 55.429 1.000 32.86

ANISOU 502 CB GLU 62 3129 2117 7239 251 2039 - 1358

ATOM 503 CG GLU 62 -17.73929.834 55.554 1.000 34.69

ANISOU 503 CG GLU 62 2824 2859 7499 916 -95 -1430

ATOM 504 CD GLU 62 -17.27430.810 56.616 1.000 38.93

ANISOU 504 CD GLU 62 4998 2780 7014 1622 224 -1820

ATOM 505 OEl GLU 62 -16.86130.391 57.717 1.000 40.92

ANISOU 505 OEl GLU 62 4844 3636 7068 1268 34 -1673

ATOM 506 OE2 GLU 62 -17.32432.041 56.385 1.000 45.13

ANISOU 506 OE2 GLU 62 7600 2889 6658 -525 1698 - 1099

ATOM 507 N LYS 63 -16.193 25.431 55.345 1.000 25.20

ANISOU 507 N LYS 63 2470 2380 4723 312 1050 8

ATOM 508 CA LYS 63 -15.21424.369 55.207 1.000 21.62

ANISOU 508 CA LYS 63 2608 2894 2712 688 349 - 446

ATOM 509 C LYS 63 -15.70823.397 54.147 1.000 22.42

ANISOU 509 C LYS 63 2930 3038 2549 84 433 - 217

ATOM 510 O LYS 63 -14.913 23.038 53.289 1.000 24.17

ANISOU 510 O LYS 63 3340 2354 3491 239 782 - 790

ATOM 511 CB LYS 63 -14.94023.650 56.534 1.000 24.50

ANISOU 511 CB LYS 63 3411 3057 2842 42 -105 - 299

ATOM 512 CG LYS 63 -13.963 24.465 57.381 1.000 27.58

ANISOU 512 CG LYS 63 4640 2792 3045 -302 -465 - 306

ATOM 513 CD LYS 63 -13.86623.937 58.811 1.000 26.09

ANISOU 513 CD LYS 63 3132 3570 3211 305 -575 - 12

ATOM 514 CE LYS 63 -12.76124.695 59.560 1.000 28.96

ANISOU 514 CE LYS 63 4342 3579 3083 -317 -286 - 792

ATOM 515 NZ LYS 63 -12.92724.614 61.030 1.000 35.00

ANISOU 515 NZ LYS 63 4884 5356 3057 64 -298 - 817

ATOM 516 N ARG 64 -17.00723.112 54.143 1.000 29.82

ANISOU 516 N ARG 64 3238 2676 5418 -533 1111 - 1259

ATOM 517 CA ARG 64 -17.52122.169 53.118 1.000 25.56

ANISOU 517 CA ARG 64 2396 2474 4841 -170 1252 - 962

ATOM 518 C ARG 64 -17.41722.735 51.708 1.000 28.45

ANISOU 518 C ARG 64 3022 2681 5106 153 1369 - 562

ATOM 519 O ARG 64 -17.149 21.981 50.759 1.000 22.57 ANISOU 519 O ARG 64 1672 2466 4436 -71 148 - 395

ATOM 520 CB ARG 64 -18.937 21.809 53.537 1.000 32.48

ANISOU 520 CB ARG 64 2669 4144 5526 -809 1483 - 1029

ATOM 521 CG ARG 64 -19.094 20.442 54.189 1.000 45.55

ANISOU 521 CG ARG 64 4444 4749 8116 -2443 1343 - 153

ATOM 522 CD ARG 64 -20.557 19.985 54.080 1.000 59.48

ANISOU 522 CD ARG 64 5723 6760 10116 -3977 -2863 2461

ATOM 523 NE ARG 64 -20.759 19.485 52.714 1.000 77.63

ANISOU 523 NE ARG 64 10254 9303 9938 -4031 -4193 2666

ATOM 524 CZ ARG 64 -21.166 20.236 51.696 1.000 60.23

ANISOU 524 CZ ARG 64 5289 6952 10644 -1128 -4334 5 0 1

ATOM 525 NHl ARG 64 -21.424 21.528 51.892 1.000 91.64

ANISOU 525 NHl ARG 64 18286 5072 11461 -5082 -3134 - 7 5

ATOM 526 NH2 ARG 64 -21.286 19.711 50.489 1.000 43 .67

ANISOU 526 NH2 ARG 64 3318 4095 9178 -183 -1521 2085

ATOM 527 N ALA 65 -17.624 24.041 51.515 1.000 26.71

ANISOU 527 N ALA 65 1907 2770 5472 189 936 - 556

ATOM 528 CA ALA 65 -17.522 24.661 50.199 1.000 24.91

ANISOU 528 CA ALA 65 1798 2379 5288 280 417 - 754

ATOM 529 C ALA 65 -16.109 24.575 49.595 1.000 21.81

ANISOU 529 C ALA 65 1808 2408 4071 597 155 - 626

ATOM 530 O ALA 65 -15.935 24.724 48.381 1.000 24.13

ANISOU 530 O ALA 65 2127 3076 3964 224 -220 - 485

ATOM 531 CB ALA 65 -18.023 26.096 50.221 1.000 31.78

ANISOU 531 CB ALA 65 3096 2984 5993 1337 1401 - 453

ATOM 532 N VAL 66 -15.098 24.306 50.426 1.000 19.29

ANISOU 532 N VAL 66 1836 1880 3614 466 360 - 541

ATOM 533 CA VAL 66 -13.723 24.167 49.953 1.000 18.17

ANISOU 533 CA VAL 66 1636 1653 3616 204 79 - 487

ATOM 534 C VAL 66 -13.166 22.767 50.248 1.000 15.18

ANISOU 534 C VAL 66 1516 1638 2613 120 126 - 571

ATOM 535 O VAL 66 -11.959 22.623 50.353 1.000 17.63

ANISOU 535 O VAL 66 1567 2071 3060 217 -106 - 317

ATOM 536 CB VAL 66 -12.784 25.277 50.437 1.000 18.91

ANISOU 536 CB VAL 66 2175 1576 3433 183 -135 - 598

ATOM 537 CGI VAL 66 -13.139 26.627 49.805 1.000 20.60

ANISOU 537 CGI VAL 66 2067 1751 4010 219 593 - 83

ATOM 538 CG2 VAL 66 -12.736 25.373 51.945 1.000 21.61

ANISOU 538 CG2 VAL 66 2689 2066 3455 102 22 - 603

ATOM 539 N THR 67 -14.048 21.792 50.343 1.000 18.30

ANISOU 539 N THR 67 1761 1614 3577 -20 -6 - 514

ATOM 540 CA THR 67 -13.673 20.403 50.563 1.000 17.18

ANISOU 540 CA THR 67 1927 1656 2946 -32 50 - 556

ATOM 541 C THR 67 -13.979 19.566 49.332 1.000 16.52

ANISOU 541 C THR 67 1763 1742 2773 21 27 - 467

ATOM 542 O THR 67 -15.107 19.613 48.811 1.000 18.13

ANISOU 542 O THR 67 1750 2211 2929 73 -86 - 383

ATOM 543 CB THR 67 -14.373 19.791 51.782 1.000 18.54

ANISOU 543 CB THR 67 2202 2014 2827 192 224 - 492

ATOM 544 OGl . THR 67 -14.060 20.554 52.961 1.000 20.14

ANISOU 544 OGl . THR 67 2481 2251 2920 -108 155 - 468

ATOM 545 CG2 1 THR 67 -13.912 18.364 52.017 1.000 20.04

ANISOU 545 CG2 : THR 67 2393 2016 3203 29 -86 - 235

ATOM 546 N SER 68 -13.030 18.818 48.821 1.000 16.71

ANISOU 546 N SER 68 1612 1720 3018 -135 154 - 498

ATOM 547 CA SER 68 -13.281 .17.947 47.688 1.000 16.33

ANISOU 547 CA SER 68 1508 1631 3065 -184 365 - 561

ATOM 548 C SER 68 -14.223 16.795 48.057 1.000 14.85

ANISOU 548 C SER 68 1194 1775 2672 -81 197 - 448

ATOM 549 O SER 68 -14.303 I 16.431 49.233 1.000 16.36

ANISOU 549 O SER 68 1783 1775 2659 -145 192 - 481 ATOM 550 CB SER 68 -11.958 17.303 47.257 1.000 17 .84

ANISOU 550 CB SER 68 1459 2139 3182 -87 647 - 313

ATOM 551 OG SER 68 -10.998 18.259 46.904 1.000 17.21

ANISOU 551 OG SER 68 1659 1987 2893 -75 364 - 4 9

ATOM 552 N PRO 69 -14.929 16.284 47.054 1.000 15.8

ANISOU 552 N PRO 69 1574 1661 2803 -201 -103 - 280

ATOM 553 CA PRO 69 -15.877 15.182 47.339 1.000 16.42

ANISOU 553 CA PRO 69 1428 1903 2908 -251 -148 - 218

ATOM 554 C PRO 69 -15.168 13.889 47.684 1.000 17.22

ANISOU 554 C PRO 69 1633 1578 3331 -199 266 - 424

ATOM 555 O PRO 69 -15.794 12.997 48.287 1.000 18.35

ANISOU 555 O PRO 69 1815 1760 3399 -365 232 - 376

ATOM 556 CB PRO 69 -16.712 15.057 46.060 1.000 16.75

ANISOU 556 CB PRO 69 1354 2279 2733 -360 155 - 729

ATOM 557 CG PRO 69 -15.799 15.637 45.008 1.000 16.72

ANISOU 557 CG PRO 69 1553 1971 2827 -359 38 - 452

ATOM 558 CD PRO 69 -15.059 16.797 45.681 1.000 17.10

ANISOU 558 CD PRO 69 1918 1804 2776 -344 -119 - 313

ATOM 559 N VAL 70 -13.884 13.746 47.366 1.000 18 .07

ANISOU 559 N VAL 70 1716 1764 3384 -89 292 - 215

ATOM 560 CA VAL 70 -13.100 12.594 47.824 1.000 17.3

ANISOU 560 CA VAL 70 1763 1851 2974 -20 260 - 196

ATOM 561 C VAL 70 -11.995 13.142 48.720 1.000 17.59

ANISOU 561 C VAL 70 2207 1686 2788 -180 159 - 142

ATOM 562 O VAL 70 -11.431 14.186 48.389 1.000 18.5

ANISOU 562 O VAL 70 1794 1688 3581 -4 9 152

ATOM 563 CB VAL 70 -12.429 11.757 46.724 1.000 18.10

ANISOU 563 CB VAL 70 1922 1756 3199 -353 560 - 446

ATOM 564 CGI VAL 70 -13.441 10.754 46.213 1.000 20.54

ANISOU 564 CGI VAL 70 1927 2611 3268 -369 76 - 663

ATOM 565 CG2 VAL 70 -11.760 12.608 45.642 1.000 17.65

ANISOU 565 CG2 VAL 70 2379 1806 2520 145 9 1 0

ATOM 566 N PRO 71 -11.697 12.466 49.815 1.000 16.21

ANISOU 566 N PRO 71 1653 1810 2695 -34 464 - 156

ATOM 567 CA PRO 71 -10.839 13.091 50.833 1.000 17.32

ANISOU 567 CA PRO 71 1795 1931 2854 -121 184 - 12

ATOM 568 C PRO 71 -9.356 12.804 50.590 1.000 17.67

ANISOU 568 C PRO 71 1865 1927 2921 46 -57 156

ATOM 569 O PRO 71 -8.585 12.223 51.350 1.000 20.57

ANISOU 569 O PRO 71 2218 2247 3350 424 28 474

ATOM 570 CB PRO 71 -11.362 12.458 52.117 1.000 19.76

ANISOU 570 CB PRO 71 2976 1862 2668 -347 479 - 304

ATOM 571 CG PRO 71 -11.721 11.056 51.670 1.000 19.08

ANISOU 571 CG PRO 71 2838 1805 2608 -267 259 -234

ATOM 572 CD PRO 71 -12.323 11.220 50.286 1.000 17.97

ANISOU 572 CD PRO 71 2314 1974 2538 -390 451 - 167

ATOM 573 N THR 72 -8.894 13.338 49.446 1.000 17.15

ANISOU 573 N THR 72 1677 2231 2610 -215 -17 - 165

ATOM 574 CA THR 72 -7.573 13.012 48.935 1.000 16.83

ANISOU 574 CA THR 72 1721 1863 2810 -60 -134 - 472

ATOM 575 C THR 72 -6.490 14.000 49.358 1.000 15.20

ANISOU 575 C THR 72 1791 1623 2362 -304 163 - 73

ATOM 576 O THR 72 -5.320 13.729 49.104 1.000 17.49

ANISOU 576 O THR 72 1776 1961 2908 -61 -31 -225

ATOM 577 CB THR 72 -7.533 12.971 47.399 1.000 16.18

ANISOU 577 CB THR 72 1552 1848 2748 -146 -86 -261

ATOM 578 OGl THR 72 -8.091 14.238 47.005 1.000 17.81

ANISOU 578 OGl THR 72 1856 1880 3031 -34 115 -191

ATOM 579 CG2 THR 72 -8.338 11.816 46.825 1.000 17.49

ANISOU 579 CG2 THR 72 1953 2087 2605 -550 181 - 329

ATOM 580 N MET 73 -6.877 15.098 49.987 1.000 17.78 ANISOU 580 N MET 73 2057 1748 2951 -58 -254 - 426

ATOM 581 CA MET 73 -5.867 16.117 50.394 1.000 16.58

ANISOU 581 CA MET 73 1796 1708 2797 88 -302 - 340

ATOM 582 C MET 73 -5.073 16.618 49.198 1.000 16.65

ANISOU 582 C MET 73 1514 1787 3027 241 -162 - 420

ATOM 583 O MET 73 -3.911 17.039 49.292 1.000 19.39

ANISOU 583 O MET 73 1705 2313 3348 -112 -240 - 540

ATOM 584 CB MET 73 -4.925 15.531 51.469 1.000 20.56

ANISOU 584 CB MET 73 2099 2629 3083 345 -507 - 286

ATOM 585 CG MET 73 -5.703 15.154 52.715 1.000 30.33

ANISOU 585 CG MET 73 3008 5133 3384 -69 -609 1027

ATOM 586 SD MET 73 -4.692 14.263 53.891 1.000 36.13

ANISOU 586 SD MET 73 4121 5050 4558 336 -918 1596

ATOM 587 CE MET 73 -3.165 13.987 53.082 1.000 58 .07

ANISOU 587 CE MET 73 2810 8820 10435 975 -1592 -313

ATOM 588 N ARG 74 -5.687 16.632 48.025 1.000 16.83

ANISOU 588 N ARG 74 1699 1714 2982 -6 -211 13 1

ATOM 589 CA ARG 74 -5.099 17.215 46.817 1.000 15.87

ANISOU 589 CA ARG 74 1365 1618 3046 -17 52 - 325

ATOM 590 C ARG 74 -5.359 18.714 46.761 1.000 14.22

ANISOU 590 C ARG 74 1484 1651 2269 141 -32 - 42

ATOM 591 O ARG 74 -4.472 19.488 46.353 1.000 15 .45

ANISOU 591 0 ARG 74 1525 1758 2586 -12 -46 - 7 3

ATOM 592 CB ARG 74 -5.675 16.530 45.566 1.000 15.68

ANISOU 592 CB ARG 74 1330 1667 2959 160 -14 - 311

ATOM 593 CG ARG 74 -4.890 16.941 44.299 1.000 16.46

ANISOU 593 CG ARG 74 1325 1870 3059 -175 55 - 395

ATOM 594 CD ARG 74 -5.655 16.396 43.072 1.000 16.37

ANISOU 594 CD ARG 74 1789 1533 2899 -181 -8 - 177

ATOM 595 NE ARG 74 -4.840 16.601 41.857 1.000 19.21

ANISOU 595 NE ARG 74 2289 1990 3020 -142 241 - 156

ATOM 596 CZ ARG 74 -4.944 17.626 41.039 1.000 17.00

ANISOU 596 CZ ARG 74 1545 2351 2562 -67 26 - 147

ATOM 597 NHl ARG 74 -5.878 18.573 41.213 1.000 18.00

ANISOU 597 NHl ARG 74 1818 2383 2638 51 -66 - 220

ATOM 598 NH2 ARG 74 -4.144 17.703 39.987 1.000 20.50

ANISOU 598 NH2 ARG 74 2285 2972 2532 -110 310 - 387

ATOM 599 N ARG 75 -6.579 19.151 47.101 1.000 15.28

ANISOU 599 N ARG 75 1755 1544 2507 137 340 - 173

ATOM 600 CA ARG 75 -6.999 20.550 46.980 1.000 14.68

ANISOU 600 CA ARG 75 1679 1627 2272 236 98 - 150

ATOM 601 C ARG 75 -7.956 20.869 48.122 1.000 14.75

ANISOU 601 C ARG 75 1445 1747 2414 124 133 - 233

ATOM 602 O ARG 75 -8.760 19.989 48.460 1.000 18.12

ANISOU 602 O ARG 75 1677 2109 3101 -156 458 - 433

ATOM 603 CB ARG 75 -7.747 20.804 45.668 1.000 15.59

ANISOU 603 CB ARG 75 1577 2030 2317 I 46 - 106

ATOM 604 CG ARG 75 -6.848 20.634 44.441 1.000 15.63

ANISOU 604 CG ARG 75 1495 2110 2334 9 147 2 2 0

ATOM 605 CD ARG 75 -5.712 21.618 44.334 1.000 15.59

ANISOU 605 CD ARG 75 1658 1792 2475 II 130 - 10

ATOM 606 NE ARG 75 -5.061 21.601 43.011 1.000 15.25

ANISOU 606 NE ARG 75 1421 1779 2596 122 227 144

ATOM 607 CZ ARG 75 -3.957 20.865 42.732 1.000 14.90

ANISOU 607 CZ ARG 75 1079 2361 2221 71 -86 2 42

ATOM 608 NHl ARG 75 -3.405 20.091 43.664 1.000 16.18

ANISOU 608 NHl ARG 75 1804 1722 2623 -134 -387 3 3 7

ATOM 609 NH2 ARG 75 -3.418 20.940 41.518 1.000 15.83

ANISOU 609 NH2 ARG 75 1677 2107 2232 -193 221 0

ATOM 610 N GLY 76 -7.895 22.086 48.651 1.000 16.06

ANISOU 610 N GLY 76 1686 1904 2513 109 220 - 464 ATOM 611 CA GLY 76 -8.858 22.532 49.637 1.000 16.67

ANISOU 611 CA GLY 76 1650 2260 2425 -70 199 - 612

ATOM 612 C GLY 76 -8.602 22.002 51.036 1.000 16.32

ANISOU 612 C GLY 76 1584 2014 2602 -126 268 - 347

ATOM 613 0 GLY 76 -7.469 21.651 51.370 1.000 16.87

ANISOU 613 0 GLY 76 1638 1998 2773 -45 308 - 218

ATOM 614 N PHE 77 -9.643 22.025 51.863 1.000 16.88

ANISOU 614 N PHE 77 1597 2141 2675 -7 283 - 191

ATOM 615 CA PHE 77 -9.584 21.646 53.274 1.000 17.61

ANISOU 615 C PHE 77 1838 2196 2656 109 328 - 114

ATOM 616 C PHE 77 -9.776 20.154 53.512 1.000 17.64

ANISOU 616 C PHE 77 1855 2248 2600 -68 243 - 185

ATOM 617 O PHE 77 -10.589 19.528 52.831 1.000 18.23

ANISOU 617 0 PHE 77 1844 2488 2594 -183 357 - 240

ATOM 618 CB PHE 77 -10.698 22.383 53.998 1.000 17.70

ANISOU 618 CB PHE 77 1730 2515 2480 162 65 - 344

ATOM 619 CG PHE 77 -10.877 22.081 55.473 1.000 19.61

ANISOU 619 CG PHE 77 2405 2530 2515 195 261 - 516

ATOM 620 CD1 PHE 77 -9.966 22.594 56.395 1.000 22.27

ANISOU 620 CD1 PHE 77 2514 3523 2426 431 -23 - 527

ATOM 621 CD2 PHE 77 -11.917 21.285 55.941 1.000 21.31

ANISOU 621 CD2 PHE 77 3282 2070 2743 36 615 - 288

ATOM 622 CE1 PHE 77 -10.116 22.294 57.742 1.000 21.05

ANISOU 622 CE1 PHE 77 2719 2768 2510 171 221 - 339

ATOM 623 CE2 PHE 77 -12.079 20.991 57.300 1.000 25.09

ANISOU 623 CE2 PHE 77 2967 4120 2447 -501 625 - 826

ATOM 624 CZ PHE 77 -11.175 21.523 58.207 1.000 23.79

ANISOU 624 CZ PHE 77 2263 3681 3095 -1 376 - 756

ATOM 625 N THR 78 -9.022 19.631 54.490 1.000 17.64

ANISOU 625 N THR 78 1616 2161 2925 37 336 1

ATOM 626 CA THR 78 -9.296 18.279 54.983 1.000 18.12

ANISOU 626 CA THR 78 1926 2243 2717 -157 624 - 2 8

ATOM 627 C THR 78 -9.291 18.316 56.505 1.000 18.66

ANISOU 627 C THR 78 2120 2308 2663 -367 519 -288

ATOM 628 O THR 78 -8.335 18.821 57.095 1.000 21.42

ANISOU 628 O THR 78 2158 2883 3098 -432 90 177

ATOM 629 CB THR 78 -8.252 17.242 54.521 1.000 21.00

ANISOU 629 CB THR 78 2973 2067 2939 113 428 - 574

ATOM 630 OGl THR 78 -8.027 17.392 53.104 1.000 21.18

ANISOU 630 OGl THR 78 2544 2671 2833 160 317 - 773

ATOM 631 CG2 THR 78 -8.735 15.832 54.800 1.000 26.65

ANISOU 631 CG2 THR 78 3759 2227 4141 -275 853 - 618

ATOM 632 N GLY 79 -10.311 17.804 57.181 1.000 20.36

ANISOU 632 N GLY 79 2669 2379 2690 -670 630 - 144

ATOM 633 CA GLY 79 -10.344 : 17.679 58.623 1.000 25.96

ANISOU 633 CA GLY 79 3871 3249 2745 -790 576 3 75

ATOM 634 C GLY 79 -10.029 ' 16.238 59.039 1.000 39.70

ANISOU 634 C GLY 79 6407 3542 5135 -1658 -1944 1511

ATOM 635 O GLY 79 -10.623 15.303 58.491 1.000 31.02

ANISOU 635 O GLY 79 4327 3187 4272 -404 419 - 7 5

ATOM 636 N LEU 80 -9.069 16.055 59.936 1.000 36.07

ANISOU 636 N LEU 80 4380 4536 4788 1381 -564 - 835

ATOM 637 CA LEU 80 -8.634 14.713 60.340 1.000 32.52

ANISOU 637 CA LEU 80 3640 4083 4632 611 -502 - 898

ATOM 638 C LEU 80 -9.131 14.311 61.716 1.000 39.82

ANISOU 638 C LEU 80 5051 4652 5428 -128 418 - 538

ATOM 639 O LEU 80 -9.998 14.963 62.305 1.000 37.05

ANISOU 639 O LEU 80 5057 3807 5213 -292 666 8 7

ATOM 640 CB LEU 80 -7.122 14.580 60.265 1.000 38.36

ANISOU 640 CB LEU 80 3821 5456 5299 1568 -33 -1406

ATOM 641 CG LEU 80 -6.488 14.753 58.883 1.000 38.27 -34-

ANISOU 641 CG LEU 80 3714 5900 4926 725 -288 - 258

ATOM 642 CDI LEU 80 -5.007 14.359 58.948 1.000 45.41

ANISOU 642 CDI LEU 80 2579 8505 6170 -1092 -76 3 7

ATOM 643 CD2 LEU 80 -7.170 13.856 57.854 1.000 40.75

ANISOU 643 CD2 LEU 80 4296 5601 5587 872 -1965 -1^' 9 3

ATOM 644 N SER 98 -6.459 17.442 63.930 1.000 36.72

ANISOU 644 N SER 98 3404 6429 4118 -2114 -698 194,

ATOM 645 C SER 98 -5.629 17.877 62.824 1.000 39.59

ANISOU 645 CA SER 98 6031 5376 3635 -449 383 217^'

ATOM 646 C SER 98 -6.402 18.372 61.610 1.000 29.89

ANISOU 646 C SER 98 3806 3509 4040 141 640 120.

ATOM 647 O SER 98 -7.474 17.856 61.304 1.000 38.27

ANISOU 647 O SER 98 4936 4300 5303 -1107 395 885

ATOM 648 CB SER 98 -4.694 16.739 62.358 1.000 44.06

ANISOU 648 CB SER 98 3175 7425 6141 633 -753 270'

ATOM 649 OG SER 98 -3.672 17.368 61.583 1.000 46.84

ANISOU 649 OG SER 98 3497 6502 7797 95 -408 2418

ATOM 650 N MET 99 -5.829 19.317 60.869 1.000 28.56

ANISOU 650 N MET 99 5029 3458 2365 -1080 -550 546

ATOM 651 CA MET 99 -6.426 19.941 59.700 1.000 21.44

ANISOU 651 CA MET 99 2284 3549 2315 -182 157 132

ATOM 652 C MET 99 -5.376 20.229 58.624 1.000 19.16

ANISOU 652 C MET 99 2306 2592 2382 -433 60 137

ATOM 653 O MET 99 -4.232 20.575 58.930 1.000 23.34

ANISOU 653 O MET 99 2489 3920 2460 -773 225 -411

ATOM 654 CB MET 99 -7.164 21.209 60.105 1.000 25.20

ANISOU 654 CB MET 99 3172 3375 3028 -572 661 -54'

ATOM 655 CG MET 99 -8.481 20.965 60.872 1.000 25.85

ANISOU 655 CG MET 99 3172 3862 2787 -275 739 -78:

ATOM 656 SD MET 99 -9.251 22.517 61.389 1.000 32.21

ANISOU 656 SD MET 99 4405 3750 4083 -133 1580 -56:

ATOM 657 CE MET 99 -8.884 22.461 63.145 1.000 76.12

ANISOU 657 CE MET 99 14782 11538 2603 -3321 3478 - 32 4. 1

ATOM 658 N CYS 100 -5.778 20.094 57.361 1.000 18.85

ANISOU 658 N CYS 100 2434 2443 2285 -160 93 194

ATOM 659 CA CYS 100 -4.868 20.333 56.234 1.000 18.55

ANISOU 659 CA CYS 100 2251 2380 2418 92 127 2 3 6

ATOM 660 C CYS 100 -5.496 21.312 55.228 1.000 16.26

ANISOU 660 C CYS 100 1826 2031 2321 110 329 2

ATOM 661 O CYS 100 -6.728 21.308 55.071 1.000 17.69

ANISOU 661 O CYS 100 1741 2395 2586 -69 154 - 10

ATOM 662 CB CYS 100 -4.604 18.982 55.545 1.000 18.46

ANISOU 662 CB CYS 100 2822 2081 2111 98 118 5 11

ATOM 663 SG CYS 100 -3.243 18.974 54.329 1.000 22.76

ANISOU 663 SG CYS 100 2622 2968 3058 307 391 1 0

ATOM 664 N TYR 101 -4.697 22.069 54.498 1.000 17.49

ANISOU 664 N TYR 101 1839 2473 2332 46 291 2 2 4

ATOM 665 CA TYR 101 -5.117 22.874 53.373 1.000 15.38

ANISOU 665 CA TYR 101 1946 1939 1960 -50 90 - 262

ATOM 666 C TYR 101 -4.102 22.594 52.245 1.000 13.65

ANISOU 666 C TYR 101 1676 1543 1967 -2 -123 - 151

ATOM 667 O TYR 101 -2.896 22.629 52.475 1.000 15.95

ANISOU 667 O TYR 101 1611 2231 2217 -43 -232 -21

ATOM 668 CB TYR 101 -5.122 24.382 53.739 1.000 19.02

ANISOU 668 CB TYR 101 2816 2082 2328 234 48 - 519

ATOM 669 CG TYR 101 -5.617 25.109 52.498 1.000 17.85

ANISOU 669 CG TYR 101 2084 1895 2804 18 -26 - 231

ATOM 670 CDI TYR 101 -6.964 25.134 52.171 1.000 18.25

ANISOU 670 CDI TYR 101 2042 1596 3298 29 28 -496

ATOM 671 CD2 TYR 101 -4.730 25.778 51.658 1.000ι 1 1 . 1 1

ANISOU 671 CD2 TYR 101 2037 1611 3106 -46 -125 - 12 ATOM 672 CE1 TYR 101 -7.406 25.796 51.036 1.000 1 .63

ANISOU 672 CE1 TYR 101 1977 1776 3704 88 -241 - 221

ATOM 673 CE2 TYR 101 -5.147 26.386 50.478 1.000 20.46

ANISOU 673 CE2 TYR 101 2060 2608 3108 239 40 1 8 2

ATOM 674 CZ TYR 101 -6.504 26.392 50.166 1.000 20.29

ANISOU 674 CZ TYR 101 2187 2397 3127 -73 -353 - 260

ATOM 675 OH TYR 101 -6.932 26.995 49.000 1.000 23 .34

ANISOU 675 OH TYR 101 2790 2555 3523 -3 -641 5 2

ATOM 676 N SER 102 -4.648 22.210 51.097 1.000 14.60

ANISOU 676 N SER 102 1618 1890 2041 -61 -109 - 477

ATOM 677 CA SER 102 -3.797 21.792 49.980 1.000 14.52

ANISOU 677 CA SER 102 1684 1802 2030 -108 62 - 276

ATOM 678 C SER 102 -4.011 22.670 48.747 1.000 14.9

ANISOU 678 C SER 102 1545 1790 2361 -296 -41 2 1

ATOM 679 O SER 102 -5.167 23.105 48.477 1.000 16.73

ANISOU 679 O SER 102 1589 2342 2425 2 128 - 3

ATOM 680 CB SER 102 -4.163 20.340 49.593 1.000 13 .82

ANISOU 680 CB SER 102 1692 1548 2013 174 9 - 138

ATOM 681 OG SER 102 -3.996 19.476 50.720 1.000 16.06

ANISOU 681 OG SER 102 1886 2066 2153 97 -121 6 3

ATOM 682 N MET 103 -2.978 22.775 47.920 1.000 14.47

ANISOU 682 N MET 103 1568 1724 2206 51 -59 1 52

ATOM 683 CA MET 103 -3.102 23.552 46.687 1.000 16.58

ANISOU 683 CA MET 103 2194 1933 2173 331 -74 253

ATOM 684 C MET 103 -2.150 23.013 45.608 1.000 14.41

ANISOU 684 C MET 103 1598 1793 2083 -202 -210 6 3

ATOM 685 O MET 103 -1.157 22.347 45.920 1.000 16.24

ANISOU 685 O MET 103 1527 2384 2259 -61 -23 468

ATOM 686 CB MET 103 -2.716 25.004 46.835 1.000 28.78

ANISOU 686 CB MET 103 6537 1318 3081 859 -207 3 66

ATOM 687 CG MET 103 -3.258 25.986 47.801 1.000 22 .60

ANISOU 687 CG MET 103 2531 2157 3900 -161 -57 - 291

ATOM 688 SD MET 103 -2.338 27.505 47.506 1.000 20.60

ANISOU 688 SD MET 103 2499 1927 3400 -4 -164 - 226

ATOM 689 CE MET 103 -2.587 27.945 45.804 1.000 21.63

ANISOU 689 CE MET 103 2319 2601 3300 308 209 - 236

ATOM 690 N GLY 104 -2.439 23.430 44.378 1.000 15.44

ANISOU 690 N GLY 104 1468 2228 2169 -68 -120 1 64

ATOM 691 CA GLY 104 -1.511 23.199 43.276 1.000 16.13

ANISOU 691 CA GLY 104 1688 2202 2241 42 65 4 6 9

ATOM 692 C GLY 104 -1.583 24.355 42.294 1.000 15.76

ANISOU 692 c GLY 104 1706 1997 2286 -32 -194 3 8 8

ATOM 693 0 GLY 104 -1.987 25.478 42.653 1.000 19.06

ANISOU 693 0 GLY 104 1953 2032 3256 -71 144 3 3 3

ATOM 694 N THR 105 -1.151 24.092 41.054 1.000 16.73

ANISOU 694 N THR 105 1685 2385 2287 -375 -55 5 15

ATOM 695 CA THR 105 -1.115 25.205 40.094 1.000 17.06

ANISOU 695 CA THR 105 1725 2390 2369 -231 -148 5 77

ATOM 696 C THR 105 -2.513 25.631 39.635 1.000 19.55

ANISOU 696 C THR 105 1768 1817 3842 -160 -346 52 5

ATOM 697 O THR 105 -2.680 26.703 39.059 1.000 22.41

ANISOU 697 O THR 105 2262 2116 4136 -119 -520 8 42

ATOM 698 CB THR 105 -0.301 24.857 38.840 1.000 17.57

ANISOU 698 CB THR 105 1759 2877 2038 -394 -343 3 77

ATOM 699 OGl THR 105 -0.865 23.675 38.217 1.000 18 .66

ANISOU 699 OGl THR 105 2035 2449 2607 -140 -458 4 1 6

ATOM 700 CG2 THR 105 1.155 24.590 39.178 1.000 18.95

ANISOU 700 CG2 THR 105 1748 2853 2601 -105 -248 2 9 6

ATOM 701 N ALA 106 -3.507 24.751 39.741 1.000 16.52

ANISOU 701 N ALA 106 1596 2293 2389 -180 -1 2 9 8

ATOM 702 C ALA 106 -4.846 25.035 39.218 1.000 16.59

SUBSTΓΓUTE SHEET (RULE 26) ANISOU 702 CA ALA 106 1692 1952 2660 -214 -209 2 43

ATOM 703 C ALA 106 -5.848 24.142 39.923 1.000 17.52

ANISOU 703 C ALA 106 1651 1821 3186 26 -66 5 5 5

ATOM 704 O ALA 106 -5.479 23.323 40.805 1.000 17.88

ANISOU 704 O ALA 106 2038 2087 2668 59 -51 3 8 8

ATOM 705 CB ALA 106 -4.862 24.838 37.713 1.000 20.31

ANISOU 705 CB ALA 106 2331 2764 2620 -197 -403 4 4 0

ATOM 706 N ASP 107 -7.149 24.329 39.717 1.000 18.00

ANISOU 706 N ASP 107 1576 2208 3057 -77 -120 4 9

ATOM 707 C ASP 107 -8.217 23.535 40.344 1.000 17 .46

ANISOU 707 CA ASP 107 1563 2191 2881 -83 -472 3 63

ATOM 708 C ASP 107 -8.173 23.753 41.859 1.000 17.74

ANISOU 708 C ASP 107 1825 2044 2869 447 -269 3 62

ATOM 709 O ASP 107 -8.458 22.854 42.650 1.000 18 .95

ANISOU 709 O ASP 107 1994 2230 2974 167 -133 4 02

ATOM 710 CB ASP 107 -8.089 22.044 39.990 1.000 1 .62

ANISOU 710 CB ASP 107 2213 2300 2942 -394 -727 173

ATOM 711 CG ASP 107 -8.370 21.842 38.508 1.000 20.81

ANISOU 711 CG ASP 107 1952 3093 2862 -138 -532 - 14

ATOM 712 ODl ASP 107 -9.369 22.369 37.976 1.000 25.84

ANISOU 712 ODl ASP 107 2524 3967 3327 222 -1149 - 240

ATOM 713 OD2 ASP 107 -7.544 21.168 37.844 1.000 25.86

ANISOU 713 OD2 ASP 107 3314 2989 3523 391 -91 - 89

ATOM 714 N ASN 108 -7.893 24.962 42.298 1.000 18.18

ANISOU 714 N ASN 108 2049 2075 2786 509 189 1 53

ATOM 715 CA ASN 108 -7.831 25.263 43.740 1.000 17.10

ANISOU 715 CA ASN 108 1804 1977 2715 266 291 3 2 7

ATOM 716 C ASN 108 -9.158 25.716 44.314 1.000 17.11

ANISOU 716 C ASN 108 1705 2061 2734 367 44 14 9

ATOM 717 0 ASN 108 -10.103 26.086 43.604 1.000 20.72

ANISOU 717 0 ASN 108 2066 2377 3430 759 -248 2 45

ATOM 718 CB ASN 108 -6.799 26.379 43.969 1.000 19.90

ANISOU 718 CB ASN 108 1770 2308 3483 186 298 - 171

ATOM 719 CG ASN 108 -5.400 25.862 43.717 1.000 17.24

ANISOU 719 CG ASN 108 1709 2212 2628 200 68 184

ATOM 720 ODl ASN 108 -4.986 24.850 44.277 1.000 17.42

ANISOU 720 ODl ASN 108 2003 1984 2631 109 11 - 62

ATOM 721 ND2 ASN 108 -4.644 26.487 42.834 1.000 18.41

ANISOU 721 ND2 ASN 108 2083 2326 2587 -82 300 - 18

ATOM 722 N LEU 109 -9.308 25.509 45.607 1.000 18.09

ANISOU 722 N LEU 109 1795 2294 2786 349 344 1 0

ATOM 723 CA LEU 109 -10.532 25.803 46.369 1.000 19.11

ANISOU 723 CA LEU 109 1763 2200 3296 14 476 - 598

ATOM 724 C LEU 109 -10.169 26.790 47.457 1.000 17.40

ANISOU 724 C LEU 109 1682 1937 2990 251 129 - 207

ATOM 725 O LEU 109 -9.443 26.423 48.395 1.000 21.18

ANISOU 725 O LEU 109 2443 1922 3684 174 -520 2

ATOM 726 CB LEU 109 -11.10C ) 24.504 46.940 1.000 17 .10

ANISOU 726 CB LEU 109 1888 2142 2469 199 426 - 630

ATOM 727 CG LEU 109 -11.52C ) 23.425 45.944 1.000 18.07

ANISOU 727 CG LEU 109 2515 1943 2409 190 -198 - 363

ATOM 728 CDI . LEU 109 -11.89E > 22.124 46.654 1.000 20.06

ANISOU 728 CDI . LEU 109 2842 2406 2375 -331 -175 - 200

ATOM 729 CD2 ! LEU 109 -12.63C ) 23.908 45.035 1.000 25.24

ANISOU 729 CD-: ! LEU 109 3481 2892 3217 306 -992 - 111

ATOM 730 N PHE 110 -10.609 28.036 47.313 1.000 17.25

ANISOU 730 N PHE 110 1584 1926 3045 272 184 - 132

ATOM 731 CA PHE 110 -10.235 29.071 48.277 1.000 18.20

ANISOU 731 CA PHE 110 1751 1816 3346 169 221 - 160

ATOM 732 C PHE 110 -11.409 29.567 49.106 1.000 19.93

ANISOU 732 C PHE 110 2077 1609 3886 71 650 - 335 ATOM 733 O PHE 110 -12.433 29.948 48.494 1.000 24.64

ANISOU 733 O PHE 110 2051 2461 4851 612 328 - 779

ATOM 734 CB PHE 110 -9.607 30.243 47.520 1.000 19.92

ANISOU 734 CB PHE 110 2367 1876 3324 224 619 - 9 3

ATOM 735 CG PHE 110 -8.380 29.986 46.688 1.000 19 .47

ANISOU 735 CG PHE 110 2009 2209 3179 -321 327 - 791

ATOM 736 CDI PHE 110 -7.177 29.680 47.287 1.000 20.59

ANISOU 736 CDI PHE 110 2071 2080 3674 -274 236 - 331

ATOM 737 CD2 PHE 110 -8.437 30.035 45.299 1.000 20.19

ANISOU 737 CD2 PHE 110 2557 1914 3200 112 543 - 289

ATOM 738 CE1 PHE 110 -6.034 29.454 46.559 1.000 21.06

ANISOU 738 CE1 PHE 110 2020 2309 3673 -386 165 - 622

ATOM 739 CE2 PHE 110 -7.277 29.811 44.547 1.000 20.77

ANISOU 739 CE2 PHE 110 2495 2138 3257 197 504 - 398

ATOM 740 CZ PHE 110 -6.081 29.518 45.175 1.000 22 .42

ANISOU 740 CZ PHE 110 2747 2092 3678 531 339 - 357

ATOM 741 N PRO 111 -11.238 29.718 50.416 1.000 22.11

ANISOU 741 N PRO 111 2250 2153 3996 -72 871 - 620

ATOM 742 CA PRO 111 -12.287 30.389 51.195 1.000 28.23

ANISOU 742 CA PRO 111 3895 2210 4621 698 1514 - 671

ATOM 743 C PRO 111 -12.333 31.866 50.784 1.000 30.57

ANISOU 743 C PRO 111 4528 2026 5061 410 410 -1041

ATOM 744 O PRO 111 -11.390 32.340 50.115 1.000 31.71

ANISOU 744 O PRO 111 4040 2236 5774 -179 -597 - 12

ATOM 745 CB PRO 111 -11.799 30.250 52.627 1.000 33 .20

ANISOU 745 CB PRO 111 5609 2702 4303 671 1671 - 790

ATOM 746 CG PRO 111 -10.646 29.326 52.647 1.000 26.04

ANISOU 746 CG PRO 111 2742 3316 3835 -931 1324 - 192

ATOM 747 CD PRO 111 -10.161 29.149 51.230 1.000 22.15

ANISOU 747 CD PRO 111 2587 2307 3522 -471 541 - 623

ATOM 748 N SER 112 -13.337 32.641 51.150 1.000 42.13

ANISOU 748 N SER 112 7176 2716 6115 2074 1731 - 526

ATOM 749 CA SER 112 -13.368 34.026 50.672 1.000 44.05

ANISOU 749 CA SER 112 6799 2255 7684 1107 -485 - 826

ATOM 750 C SER 112 -13.262 34.157 49.149 1.000 68.28

ANISOU 750 C SER 112 13632 4498 7812 -1855 -2077 1301

ATOM 751 O SER 112 -12.347 34.825 48.646 1.000 95.18

ANISOU 751 O SER 112 15991 11425 8747 -4337 -70 1985

ATOM 752 CB SER 112 -12.493 35.069 51.349 1.000 39.31

ANISOU 752 CB SER 112 2247 4535 8153 580 1662 -1437

ATOM 753 OG SER 112 -11.474 34.624 52.213 1.000 37.49

ANISOU 753 OG SER 112 7213 2453 4579 806 747 -1152

ATOM 754 N ASP 114 -9.515 37.322 49.945 1.000 36.40

ANISOU 754 N ASP 114 3476 2118 8237 1254 403 1484

ATOM 755 CA ASP 114 -8.205 37.586 50.600 1.000 30.79

ANISOU 755 CA ASP 114 3503 2856 5340 1229 1240 9 9 6

ATOM 756 C ASP 114 -7.242 36.402 50.648 1.000 26.16

ANISOU 756 C ASP 114 2581 2404 4955 601 1114 8 04

ATOM 757 O ASP 114 -6.031 36.458 50.338 1.000 25.45

ANISOU 757 O ASP 114 2302 2503 4866 -43 602 13 1

ATOM 758 CB ASP 114 -8.595 37.874 52.075 1.000 43 .68

ANISOU 758 CB ASP 114 7509 2783 6304 1157 2727 - 210

ATOM 759 CG ASP 114 -7.391 38.386 52.835 1.000 46.96

ANISOU 759 CG ASP 114 9259 3225 5359 2517 519 1 07

ATOM 760 ODl . ASP 114 -6.487 38.959 52.189 1.000 83 .49

ANISOU 760 ODl . ASP 114 13724 9866 8132 -6354 650 -3056

ATOM 761 OD2 ! ASP 114 -7.370 38.262 54.071 1.000113.59

ANISOU 761 OD2i ASP 114 27880 10550 4730 -6984 -159 -2575

ATOM 762 N PHE 115 -7.831 35.323 51.153 1.000 22.32

ANISOU 762 N PHE 115 2620 2062 3799 204 954 - 114

ATOM 763 CA PHE 115 -7.115 34.026 51.183 1.000 22 .69 ANISOU 763 CA PHE 115 2765 1909 3947 118 1093 - 187

ATOM 764 C PHE 115 -6.502 33.754 49.816 1.000 21.49

ANISOU 764 C PHE 115 2146 2316 3702 305 559 - 255

ATOM 765 O PHE 115 -5.328 33.362 49.758 1.000 20.51

ANISOU 765 O PHE 115 2153 2011 3627 323 488 - 158

ATOM 766 CB PHE 115 -8.096 32.928 51.638 1.000 20.76

ANISOU 766 CB PHE 115 2369 1946 3574 -3 563 1 -473

ATOM 767 CG PHE 115 -7.496 31.590 51.998 1.000 20.23

ANISOU 767 CG PHE 115 2369 1854 3463 -155 629 - 377

ATOM 768 CDI PHE 115 -6.915 30.756 51.041 1.000 20.35

ANISOU 768 CDI PHE 115 2572 1786 3372 -195 112 - 756

ATOM 769 CD2 PHE 115 -7.474 31.152 53.309 1.000 21.11

ANISOU 769 CD2 PHE 115 2802 1932 3287 -113 17 - 689

ATOM 770 CΞ1 PHE 115 -6.351 29.538 51.325 1.000 21.09

ANISOU 770 CE1 PHE 115 2502 1728 3784 -295 471 - 538

ATOM 771 CE2 PHE 115 -6.938 29.901 53.623 1.000 27.40

ANISOU 771 CE2 PHE 115 5012 1955 3445 444 43 - 572

ATOM 772 CZ PHE 115 -6.332 29.110 52.655 1.000 24.92

ANISOU 772 CZ PHE 115 3356 1889 4222 50 1519 221

ATOM 773 N GLU 116 -7.301 33.768 48.757 1.000 21.64

ANISOU 773 N GLU 116 2396 1835 3990 338 261 - 13

ATOM 774 CA GLU 116 -6.750 33.424 47.444 1.000 20.90

ANISOU 774 CA GLU 116 2235 1965 3742 224 74 116

ATOM 775 C GLU 116 -5.550 34.262 47.054 1.000 20.32

ANISOU 775 C GLU 116 1978 1899 3845 439 -108 448

ATOM 776 O GLU 116 -4.544 33.679 46.604 1.000 20.18

ANISOU 776 O GLU 116 2209 2147 3312 424 73 139

ATOM 777 CB GLU 116 -7.851 33.561 46.385 1.000 24.22

ANISOU 777 CB GLU 116 2425 2638 4139 -467 -237 519

ATOM 778 CG GLU 116 -7.339 33.331 44.980 1.000 23.27

ANISOU 778 CG GLU 116 2425 2465 3952 -7 -494 75 0

ATOM 779 CD GLU 116 -8.401 33.273 43.910 1.000 25.02

ANISOU 779 CD GLU 116 2695 2703 4107 -510 -739 1509

ATOM 780 OEl GLU 116 -9.617 33.306 44.207 1.000 34.83

ANISOU 780 OEl GLU 116 2466 4606 6161 -203 -928 1566

ATOM 781 OE2 GLU 116 -8.001 33.030 42.763 1.000 40.92

ANISOU 781 OE2 GLU 116 4389 7172 3988 -24 -968 693

ATOM 782 N ARG 117 -5.549 35.571 47.300 1.000 20.60

ANISOU 782 N ARG 117 2299 1811 3718 382 -10 469

ATOM 783 CA ARG 117 -4.374 36.374 46.866 1.000 22.65

ANISOU 783 CA ARG 117 2230 1791 4586 351 107 153

ATOM 784 C ARG 117 -3.163 35.911 47.648 1.000 21.87

ANISOU 784 C ARG 117 2269 1865 4178 252 179 9 7

ATOM 785 O ARG 117 -2.060 35.789 47.102 1.000 22.10

ANISOU 785 O ARG 117 2197 2270 3931 216 41 205

ATOM 786 CB ARG 117 -4.682 37.861 47.105 1.000 29.47

ANISOU 786 CB ARG 117 2849 1691 6658 259 -555 - 1

ATOM 787 CG ARG 117 -3.485 38.815 47.046 1.000 40.24

ANISOU 787 CG ARG 117 3905 2567 8818 -819 -1330 -476

ATOM 788 CD ARG 117 -3.745 40.160 47.716 1.000 52.75

ANISOU 788 CD ARG 117 4698 2848 12496 -595 -1653 -166

ATOM 789 NE ARG 117 -3.934 39.987 49.155 1.000 68.00

ANISOU 789 NE ARG 117 8247 4719 12872 422 1842 -3441

ATOM 790 CZ ARG 117 -3.166 40.448 50.126 1.000 78.38

ANISOU 790 CZ ARG 117 13026 5658 11097 283 448 - 2498

ATOM 791 NHl . ARG 117 -2.097 41.186 49.849 1.000 89.01

ANISOU 791 NHl . ARG 117 14218 11488 8115 -3550 -6761 357:

ATOM 792 NH2 : ARG 117 -3.479 40.189 51.391 1.000 82.58

ANISOU 792 NH2 1 ARG 117 16575 2856 11947 2617 2551 -2095

ATOM 793 N ILE 118 -3.334 35.759 48.954 1.000 21.70

ANISOU 793 N ILE 118 2319 1797 4127 311 271 - 314 -39-

ATOM 794 CA ILE 118 -2.206 35.425 49.810 1.000 20.99

ANISOU 794 CA ILE 118 2546 1624 3805 408 294 - 470

ATOM 795 C ILE 118 -1.596 34.073 49.475 1.000 18 .79

ANISOU 795 C ILE 118 2222 1534 3384 218 573 - 201

ATOM 796 O ILE 118 -0.409 33.858 49.323 1.000 17.27

ANISOU 796 O ILE 118 2194 1663 2707 283 351 - 136

ATOM 797 CB ILE 118 -2.588 35.542 51.293 1.000 22 .62

ANISOU 797 CB ILE 118 2702 1997 3895 276 416 - 856

ATOM 798 CGI ILE 118 -2.916 36.995 51.700 1.000 27.54

ANISOU 798 CGI ILE 118 5077 1801 3587 503 768 - 401

ATOM 799 CG2 ILE 118 -1.552 34.940 52.206 1.000 23 .59

ANISOU 799 CG2 ILE 118 3084 2274 3606 183 254 - 818

ATOM 800 CDI ILE 118 -3.493 37.115 53.096 1.000 29.35

ANISOU 800 CDI ILE 118 5212 2054 3885 558 1114 - 645

ATOM 801 N TRP 119 -2.454 33.069 49.341 1.000 17.93

ANISOU 801 N TRP 119 2378 1605 2828 147 -80 -2^'69

ATOM 802 CA TRP 119 -2.035 31.688 49.103 1.000 16.57

ANISOU 802 CA TRP 119 2126 1538 2630 152 -25 - 1 6

ATOM 803 C TRP 119 -1.575 31.476 47.676 1.000 16.98

ANISOU 803 C TRP 119 2126 1723 2604 269 -91 - 5 1

ATOM 804 O TRP 119 -0.700 30.640 47.455 1.000 17.58

ANISOU 804 O TRP 119 1892 1674 3113 135 181 6 3

ATOM 805 CB TRP 119 -3.127 30.690 49.591 1.000 18.32

ANISOU 805 CB TRP 119 2156 1789 3014 -34 5 - 7

ATOM 806 CG TRP 119 -2.934 30.457 51.082 1.000 18.27

ANISOU 806 CG TRP 119 2208 1711 3025 86 349 5 6

ATOM 807 CDI TRP 119 -3.354 31.273 52.103 1.000 20.36

ANISOU 807 CDI TRP 119 2624 2029 3083 156 276 - 153

ATOM 808 CD2 TRP 119 -2.213 29.383 51.683 1.000 18.61

ANISOU 808 CD2 TRP 119 2049 2055 2967 134 263 110

ATOM 809 NE1 TRP 119 -2.955 30.773 53.323 1.000 20.55

ANISOU 809 NE1 TRP 119 2471 2229 3109 92 266 - 106

ATOM 810 CE2 TRP 119 -2.260 29.603 53.073 1.000 20.21

ANISOU 810 CE2 TRP 119 2529 2258 2893 180 754 2 97

ATOM 811 CE3 TRP 119 -1.576 28.258 51.147 1.000 18.29

ANISOU 811 CE3 TRP 119 2258 1714 2977 42 -70 - 2 0

ATOM 812 CZ2 TRP 119 -1.636 28.728 53.981 1.000 21.97

ANISOU 812 CZ2 TRP 119 2876 2526 2945 384 51 - 106

ATOM 813 CZ3 TRP 119 -0.968 27.375 52.045 1.000 19.35

ANISOU 813 CZ3 TRP 119 2576 2028 2750 187 415 2 9 9

ATOM 814 CH2 TRP 119 -1.026 27.618 53.442 1.000 21.67

ANISOU 814 CH2 TRP 119 3033 2379 2823 350 250 9 7

ATOM 815 N THR 120 -2.129 32.192 46.701 1.000 16.93

ANISOU 815 N THR 120 2023 1833 2577 122 -112 1 8

ATOM 816 CA THR 120 -1.598 32.086 45.342 1.000 17.85

ANISOU 816 CA THR 120 1915 2469 2398 222 -371 - 324

ATOM 817 C THR 120 -0.169 32.587 45.288 1.000 17.15

ANISOU 817 C THR 120 2031 1855 2629 241 -155 1 92

ATOM 818 O THR 120 0.700 31.960 44.674 1.000 18.67

ANISOU 818 O THR 120 1996 1887 3212 389 -131 177

ATOM 819 CB THR 120 -2.487 32.865 44.344 1.000 18.10

ANISOU 819 CB THR 120 1951 2204 2720 28 -93 3 45

ATOM 820 OGl . THR 120 -3.773 32.238 44.284 1.000 20.49

ANISOU 820 OGl . THR 120 1807 2801 3179 59 -363 558

ATOM 821 CG2 : THR 120 -1.919 32.803 42.933 1.000 22.46

ANISOU 821 CG2 : THR 120 2438 3266 2830 475 US' 705

ATOM 822 N GLN 121 0.094 33.708 45.956 1.000 18.62

ANISOU 822 N GLN 121 2180 1657 3237 123 -94 2 13

ATOM 823 CA GLN 121 1.466 34.232 45.993 1.000 ι 18.15

ANISOU 823 CA GLN 121 2077 1698 3119 77 96 i 52 0

ATOM 824 C GLN 121 2.412 33.284 46.718 ! 1.00C ι 17.04 ANISOU 824 C GLN 121 2022 1431 3019 192 234 2 2 3

ATOM 825 O GLN 121 3.510 33.047 46.270 1.000 19.32

ANISOU 825 O GLN 121 1894 1800 3645 93 246 12 9

ATOM 826 CB GLN 121 1.490 35.579 46.756 1.000 22 .90

ANISOU 826 CB GLN 121 2520 1479 4702 327 -812 2 7 1

ATOM 827 CG GLN 121 2.888 36.159 46.871 1.000 27.04

ANISOU 827 CG GLN 121 2949 2062 5262 -346 -400 132

ATOM 828 CD GLN 121 3.530 36.511 45.535 1.000 31.94

ANISOU 828 CD GLN 121 3307 2733 6097 983 1031 9 9

ATOM 829 OEl GLN 121 4.660 36.085 45.247 1.000 62 .76

ANISOU 829 OEl GLN 121 3009 9570 11267 1758 2366 2029

ATOM 830 NE2 GLN 121 2.859 37.306 44.716 1.000 55.89

ANISOU 830 NE2 GLN 121 6516 7728 6993 2815 1745 3249

ATOM 831 N TYR 122 1.997 32.791 47.871 1.000 16.87

ANISOU 831 N TYR 122 2389 1518 2501 71 -161 - 54

ATOM 832 CA TYR 122 2.795 31.881 48.683 1.000 17.97

ANISOU 832 CA TYR 122 2564 1600 2666 176 -224 - 5 6

ATOM 833 C TYR 122 3.080 30.600 47.909 1.000 16.83

ANISOU 833 C TYR 122 1870 1460 3065 -31 -57 - 98

ATOM 834 O TYR 122 4.224 30.129 47.823 1.000 17.67

ANISOU 834 O TYR 122 1891 1952 2872 189> -220 12 6

ATOM 835 CB TYR 122 2.018 31.522 49.960 1.000 18.01

ANISOU 835 CB TYR 122 2526 1821 2495 2 -325 - 5 5

ATOM 836 CG TYR 122 2.753 30.619 50.898 1.000 17.89

ANISOU 836 CG TYR 122 2332 1695 2769 255 -147 - 51

ATOM 837 CDI TYR 122 4.058 30.901 51.323 1.000 21.71

ANISOU 837 CDI TYR 122 2883 2101 3267 -257 -913 3 4

ATOM 838 CD2 TYR 122 2.107 29.496 51.415 1.000 21.2

ANISOU 838 CD2 TYR 122 2428 2026 3634 128 -267 468

ATOM 839 CE1 TYR 122 4.680 30.037 52.212 1.000 21.27

ANISOU 839 CE1 TYR 122 2681 2045 3356 140 -725 - 210

ATOM 840 CE2 TYR 122 2.746 28.637 52.290 1.000 24.50

ANISOU 840 CE2 TYR 122 3376 1876 4057 -292 -1163 5 0 6

ATOM 841 CZ TYR 122 4.043 28.914 52.675 1.000 22.16

ANISOU 841 CZ TYR 122 3161 1881 3379 95 -909 - 128

ATOM 842 OH TYR 122 4.699 28.079 53.566 1.000 23.72

ANISOU 842 OH TYR 122 3471 2398 3142 52 -1005 - 5 6

ATOM 843 N PHE 123 2.074 30.023 47.253 1.000 16.21

ANISOU 843 N PHE 123 1794 1571 2793 49 -66 - 54

ATOM 844 CA PHE 123 2.347 28.843 46.397 1.000 15.71

ANISOU 844 CA PHE 123 1622 1800 2548 34 -142 - 103

ATOM 845 C PHE 123 3.378 29.188 45.337 1.000 15.96

ANISOU 845 C PHE 123 1681 1304 3078 42 90 3

ATOM 846 O PHE 123 4.276 28.375 45.037 1.000 15.47

ANISOU 846 O PHE 123 1703 1437 2739 54 14 - 24

ATOM 847 CB PHE 123 1.036 28.309 45.779 1.000 15.07

ANISOU 847 CB PHE 123 1460 1364 2904 209 -148 1

ATOM 848 CG PHE 123 1.241 27.104 44.879 1.000 17.41

ANISOU 848 CG PHE 123 2090 1620 2906 -39 -179 - 238

ATOM 849 CDI . PHE 123 1.170 25.831 45.452 1.000 17.41

ANISOU 849 CDI . PHE 123 1680 1439 3494 72 -119 - 255

ATOM 850 CD2 : PHE 123 1.490 27.259 43.513 1.000 18.22

ANISOU 850 CD2 : PHE 123 1723 2331 2870 -96 -216 - 372

ATOM 851 CE1 . PHE 123 1.419 24.740 44.636 1.000 19.15

ANISOU 851 CE1 . PHE 123 2112 1766 3397 212 -540 - 536

ATOM 852 CE2 ! PHE 123 1.722 26.144 42.717 1.000 19.63

ANISOU 852 CE2 ! PHE 123 1901 2476 3083 -134 -261 - 632

ATOM 853 CZ PHE 123 1.635 24.868 43.274 1.000 19.40

ANISOU 853 CZ PHE 123 1525 2424 3421 385 -529 - 490

ATOM 854 N ASP 124 3.164 30.304 44.636 1.000 16.86

ANISOU 854 N ASP 124 1947 1466 2992 -23 -110 124 -41 -

ATOM 855 CA ASP 124 4.060 30.640 43.544 1.000 17.82

ANISOU 855 C ASP 124 2103 1747 2921 405 -24 3 14

ATOM 856 C ASP 124 5.490 30.733 44.024 1.000 17 .52

ANISOU 856 C ASP 124 1999 1439 3219 181 94 8 9

ATOM 857 O ASP 124 6.402 30.324 43.317 1.000 17.18

ANISOU 857 O ASP 124 2086 1427 3015 34 181 . 177

ATOM 858 C3 AASP 124 3.639 31.997 42.942 0.534 21.77

ANISOU 858 CB AASP 124 3475 2089 2706 642 -372 5 9 7

ATOM 859 CG AASP 124 4.381 32.304 41.659 0.534 19 .28

ANISOU 859 CG AASP 124 2376 1982 2967 173 -553 495

ATOM 860 ODl AASP 124 4.223 31.538 40.678 0.534 21.03

ANISOU 860 ODl AASP 124 2189 2636 3164 -28 76 2 1

ATOM 861 OD2 AASP 124 5.068 33.348 41.639 0.534 24.96

ANISOU 861 OD2 AASP 124 3681 2052 3752 -296 -1067 88 9

ATOM 862 C3 BASP 124 3.632 31.975 42.908 0.466 19.67

ANISOU 862 CB BASP 124 2559 1993 2923 1003 673 4 4 6

ATOM 863 CG BASP 124 2.368 31.849 42.089 0.466 22.78

ANISOU 863 CG BASP 124 3552 3217 1889 872 177 1175

ATOM 864 ODl BASP 124 2.021 30.781 41.545 0.466 27.78

ANISOU 864 ODl BASP 124 2138 3932 4483 100 503 3 47

ATOM 865 OD2 BASP 124 1.703 32.893 41.902 0.466 29.73

ANISOU 865 OD2 BASP 124 3845 3804 3646 1239 -312 1644

ATOM 866 N ARG 125 5.669 31.416 45.153 1.000 16.65

ANISOU 866 N ARG 125 1942 1350 3032 276 139 276

ATOM 867 CA ARG 125 7.038 31.528 45.646 1.000 17.58

ANISOU 867 CA ARG 125 1918 1819 2944 98 177 241

ATOM 868 C ARG 125 7.662 30.188 45.992 1.000 17.38

ANISOU 868 C ARG 125 1544 1777 3282 -42 40 2 73

ATOM 869 O ARG 125 8.841 29.942 45.754 1.000 18.26

ANISOU 869 O ARG 125 1639 1669 3631 -97 91 - 233

ATOM 870 CB ARG 125 7.062 32.468 46.851 1.000 20.45

ANISOU 870 CB ARG 125 2219 2162 3387 -244 450 - 274

ATOM 871 CG ARG 125 6.860 33.916 46.344 1.000 28.23

ANISOU 871 CG ARG 125 3178 2007 5542 147 666 - 222

ATOM 872 CD ARG 125 6.693 34.891 47.477 1.000 31.76

ANISOU 872 CD ARG 125 3065 2279 6725 -628 1455 - 993

ATOM 873 NE ARG 125 6.496 36.221 46.932 1.000 40.81

ANISOU 873 NE ARG 125 3332 2095 10080 -169 1790 - 694

ATOM 874 CZ ARG 125 5.970 37.229 47.628 1.000 43 .42

ANISOU 874 CZ ARG 125 4531 2891 9076 839 2072 - 188

ATOM 875 NHl ARG 125 5.551 37.025 48.866 1.000 38.62

ANISOU 875 NHl ARG 125 3999 2858 7816 -858 61 - 700

ATOM 876 NH2 ARG 125 5.858 38.382 47.006 1.000 42.11

ANISOU 876 NH2 ARG 125 5319 2652 8030 908 1627 - 681

ATOM 877 N GLN 126 6.884 29.282 46.557 1.000 15.28

ANISOU 877 N GLN 126 1876 1527 2404 -70 13 - 60

ATOM 878 CA GLN 126 7.376 27.929 46.853 1.000 15.37

ANISOU 878 CA GLN 126 1726 1625 2488 -54 -312 2 0

ATOM 879 C GLN 126 7.649 27.150 45.578 1.000 14.21

ANISOU 879 C GLN 126 1643 1268 2488 -75 -398 7 1

ATOM 880 O GLN 126 8.682 26.462 45.496 1.000 15.36

ANISOU 880 O GLN 126 1531 1554 2753 -37 -316 5 3

ATOM 881 CB GLN 126 6.356 27.158 47.702 1.000 17.40

ANISOU 881 CB GLN 126 2034 1313 3264 158 293 4 3

ATOM 882 CG GLN 126 6.336 27.634 49.150 1.000 26.14

ANISOU 882 CG GLN 126 4503 1690 3739 431 1908 - 732

ATOM 883 CD GLN 126 5.208 26.998 49.891 1.000 21.95

ANISOU 883 CD GLN 126 2957 2670 2713 0 -123 102

ATOM 884 OEl GLN 126 4.051 27.372 49.730 1.000 42.52

ANISOU 884 OEl GLN 126 2994 5747 7416 -62 -1272 3147

ATOM 885 NE2 GLN 126 5.524 26.003 50.691 . 1.000 ι 28.32 -42-

ANISOU 885 NE2 GLN 126 2867 3971 3922 -184 -780 131

ATOM 886 N TYR 127 6.797 27.287 44.574 1.000 14.52

ANISOU 886 N TYR 127 1629 1438 2448 -41 -373 - 3 6

ATOM 887 CA TYR 127 7.039 26.554 43.317 1.000 13 .93

ANISOU 887 CA TYR 127 1563 1455 2277 -136 -234 15 0

ATOM 888 C TYR 127 8.289 27.091 42.624 1.000 14.54

ANISOU 888 C TYR 127 1461 1318 2745 24 -195 19 0

ATOM 889 O TYR 127 9.133 26.345 42.140 1.000 14.39

ANISOU 889 O TYR 127 1611 1580 2277 34 -252 9

ATOM 890 CB TYR 127 5.801 26.676 42.435 1.000 14.00

ANISOU 890 CB TYR 127 1510 1549 2258 29 -180 - 7 0

ATOM 891 CG TYR 127 5.752 25.795 41.202 1.000 12.33

ANISOU 891 CG TYR 127 1315 1037 2334 -34 -187 4 5

ATOM 892 CDI TYR 127 6.483 24.626 41.024 1.000 14.05

ANISOU 892 CDI TYR 127 1810 1158 2371 7 -84 - 8

ATOM 893 CD2 TYR 127 4.837 26.086 40.206 1.000 15.71

ANISOU 893 CD2 TYR 127 1936 1548 2484 55 -513 2 1

ATOM 894 CE1 TYR 127 6.382 23.829 39.899 1.000 13 .10

ANISOU 894 CE1 TYR 127 1450 999 2529 -101 -227 - 62

ATOM 895 CE2 TYR 127 4.661 25.322 39.071 1.000 15.07

ANISOU 895 CE2 TYR 127 1928 1620 2177 158 -342 1 9 7

ATOM 896 CZ TYR 127 5.440 24.179 38.934 1.000 13.71

ANISOU 896 CZ TYR 127 1617 1348 2245 -146 -106 246

ATOM 897 OH TYR 127 5.337 23.386 37.811 1.000 15.04

ANISOU 897 OH TYR 127 1682 1755 2279 -87 -60 5 3

ATOM 898 N THR 128 8.467 28.412 42.616 1.000 14.69

ANISOU 898 N THR 128 1813 1324 2446 -154 -217 2 6 £

ATOM 899 CA THR 128 9.673 28.984 42.011 1.000 14.67

ANISOU 899 CA THR 128 1867 1469 2238 -98 -32 19 E

ATOM 900 C THR 128 10.921 28.552 42.736 1.000 14.68

ANISOU 900 c THR 128 1794 1318 2466 59 -123 - 285

ATOM 901 0 THR 128 11.900 28.166 42.062 1.000 15.45

ANISOU 901 0 THR 128 1715 1487 2667 -259 153 7 1

ATOM 902 CB THR 128 9.572 30.544 42.069 1.000 16.02

ANISOU 902 CB THR 128 2043 1348 2695 -79 59 479

ATOM 903 OGl THR 128 8.519 30.849 41.162 1.000 19.14

ANISOU 903 OGl THR 128 2226 2038 3008 195 -23 54 -

ATOM 904 CG2 THR 128 10.835 31.187 41.582 1.000 19.03

ANISOU 904 CG2 THR 128 2107 1329 3793 125 311 6 1 i

ATOM 905 N ALA 129 10.933 28.564 44.085 1.000 14.21

ANISOU 905 N ALA 129 1708 1266 2424 -137 -256 - 18

ATOM 906 CA ALA 129 12.108 28.110 44.836 1.000 15.08

ANISOU 906 CA ALA 129 1670 1435 2624 -118 -210 - 22

ATOM 907 C ALA 129 12.389 26.643 44.562 1.000 14.37

ANISOU 907 C ALA 129 1706 1299 2457 -159 -203 15 ^'

ATOM 908 O ALA 129 13.552 26.238 44.445 1.000 14.10

ANISOU 908 O ALA 129 1758 1464 2137 -5 -244 - 148

ATOM 909 CB ALA 129 11.887 28.313 46.313 1.000 17.08

ANISOU 909 CB ALA 129 2132 1851 2506 -183 -514 - 2 Ξ

ATOM 910 N SER 130 11.343 25.819 44.553 1.000 14.18

ANISOU 910 N SER 130 1884 1237 2267 -224 -257 17 :

ATOM 911 CA SER 130 11.487 24.375 44.351 1.000 15.44

ANISOU 911 CA SER 130 1840 1219 2807 -115 -135 - 7

ATOM 912 C SER 130 12.072 24.114 42.965 1.000 14.45

ANISOU 912 c SER 130 1345 1481 2665 78 -796 - 209

ATOM 913 0 SER 130 13.037 23.329 42.807 1.000 14.43

ANISOU 913 0 SER 130 1327 1382 2773 -74 -246 17

ATOM 914 CB SER 130 10.120 23.677 44.663 1.000 17.54

ANISOU 914 CB SER 130 1555 1225 3884 -379 -647 12

ATOM 915 OG SER 130 9.268 23.888 43.558 1.000 27.32

ANISOU 915 OG SER 130 2321 3168 4893 11 -1207 8 65 ATOM 916 N ARG 131 11.555 24.772 41.909 1.000 14.47

ANISOU 916 N ARG 131 1421 1448 2628 161 -384 - 166

ATOM 917 CA ARG 131 12.163 24.598 40.592 1.000 14.91

ANISOU 917 CA ARG 131 1689 1452 2525 -4 -526 - 341

ATOM 918 C ARG 131 13.605 25.079 40.566 1.000 14.05

ANISOU 918 c ARG 131 1772 1435 2132 -72 -381 - 173

ATOM 919 0 ARG 131 14.448 24.438 39.912 1.000 15.14

ANISOU 919 0 ARG 131 1829 1658 2267 -109 -170 - 230

ATOM 920 CB ARG 131 11.349 25.316 39.514 1.000 15.77

ANISOU 920 CB ARG 131 1720 1613 2660 -54 -493 - 94

ATOM 921 CG ARG 131 9.970 24.737 39.251 1.000 16.08

ANISOU 921 CG ARG 131 1703 1695 2711 -13 -647 - 141

ATOM 922 CD ARG 131 9.326 25.390 38.017 1.000 26.56

ANISOU 922 CD ARG 131 3589 2689 3813 -1037 -2156 745

ATOM 923 NE ARG 131 9.327 26.831 37.918 1.000 25.91

ANISOU 923 NE ARG 131 2856 2814 4174 -979 -1682 1413

ATOM 924 CZ ARG 131 8.472 27.716 38.413 1.000 31.86

ANISOU 924 CZ ARG 131 3546 2861 5697 -254 -1094 2201

ATOM 925 NHl ARG 131 7.467 27.244 39.138 1.000 31.34

ANISOU 925 NHl ARG 131 5127 3636 3144 -1474 -458 - 115

ATOM 926 NH2 ARG 131 8.633 29.032 38.235 1.000 40.12

ANISOU 926 NH2 ARG 131 3500 2831 8912 -582 -1620 1802

ATOM 927 N ALA 132 13.893 26.186 41.236 1.000 13 .42

ANISOU 927 N ALA 132 1683 1385 2033 -85 -652 - 24

ATOM 928 CA ALA 132 15.246 26.751 41.128 1.000 13.38

ANISOU 928 CA ALA 132 1617 1443 2022 -16 -499 - 79

ATOM 929 C ALA 132 16.225 25.808 41.837 1.000 13.37

ANISOU 929 C ALA 132 1398 1365 2316 -93 -253 154

ATOM 930 O ALA 132 17.306 25.586 41.328 1.000 14.43

ANISOU 930 O ALA 132 1459 1772 2251 -91 -240 1 06

ATOM 931 CB ALA 132 15.275 28.084 41.859 1.000 16.52

ANISOU 931 CB ALA 132 2019 1243 3014 -199 -366 - 236

ATOM 932 N VAL 133 15.893 25.248 42.996 1.000 13.62

ANISOU 932 N VAL 133 1522 1515 2139 -63 -362 8 6

ATOM 933 CA VAL 133 16.839 24.363 43.689 1.000 14.86

ANISOU 933 CA VAL 133 1902 1566 2179 120 -491 - 27

ATOM 934 C VAL 133 16.923 23.073 42.890 1.000 15.04

ANISOU 934 C VAL 133 1390 1633 2690 -9 -220 - 218

ATOM 935 O VAL 133 18.036 22.538 42.773 1.000 15.49

ANISOU 935 O VAL 133 1442 1814 2630 63 -193 - 99

ATOM 936 CB VAL 133 16.545 24.170 45.187 1.000 14.61

ANISOU 936 CB VAL 133 1528 1789 2234 -45 -391 2 10

ATOM 937 CGI . VAL 133 15.362 23.267 45.453 1.000 16.78

ANISOU 937 CGI . VAL 133 1544 2123 2708 -249 -437 - 81

ATOM 938 CG2 : AL 133 17.766 23.650 45.950 1.000 16.51

ANISOU 938 CG2 : VAL 133 1769 1942 2561 -61 -831 6 4

ATOM 939 N ALA 134 15.840 22.583 42.270 1.000 13.73

ANISOU 939 N ALA 134 1605 1451 2160 -75 -397 18 5

ATOM 940 CA ALA 134 15.951 21.369 41.451 1.000 14.21

ANISOU 940 CA ALA 134 1505 1796 2100 116 -570 - 3 3

ATOM 941 C ALA 134 16.838 21.618 40.246 1.000 15.07

ANISOU 941 C ALA 134 1766 1511 2450 43 -292 1 7

ATOM 942 O ALA 134 17.600 20.750 39.800 1.000 14.36

ANISOU 942 O ALA 134 1555 1567 2333 -60 -286 5 2

ATOM 943 CB ALA 134 14.535 20.925 41.032 1.000 16.97

ANISOU 943 CB ALA 134 1472 1943 3031 12 -470 - 299

ATOM 944 N ARG 135 16.752 22.808 39.631 1.000 15.48

ANISOU 944 N ARG 135 1848 1600 2433 14 -341 - 2

ATOM 945 CA ARG 135 17.618 23.153 38.508 1.000 16.07

ANISOU 945 CA ARG 135 2139 1230 2735 -138 -189 3 5

ATOM 946 C ARG 135 19.082 23.057 38.955 1.000 15.70 ANISOU 946 C ARG 135 2059 1370 2535 -134 27 12 1

ATOM 947 O ARG 135 19.928 22.604 38.176 1.000 18 .07

ANISOU 947 0 ARG 135 2317 2014 2534 108 256 2 7 6

ATOM 948 CB ARG 135 17.277 24.586 38.096 1.000 21.96

ANISOU 948 CB ARG 135 3936 1640 2767 -4 -1480 614

ATOM 949 CG ARG 135 17.571 24.989 36.689 1.000 27.53

ANISOU 949 CG ARG 135 5112 2482 2866 816 -610 5 9 5

ATOM 950 CD ARG 135 16.930 26.332 36.393 1.000 23 .27

ANISOU 950 CD ARG 135 3548 2428 2865 148 61 1371

ATOM 951 NE ARG 135 15.551 26.309 35.928 1.000 22 .68

ANISOU 951 NE ARG 135 3488 1575 3556 -116 167 2 9 7

ATOM 952 CZ ARG 135 14.520 26.858 36.562 1.000 25.90

ANISOU 952 CZ ARG 135 3801 2165 3874 921 -506 - 179

ATOM 953 NHl ARG 135 14.708 27.515 37.702 1.000 23.50

ANISOU 953 NHl ARG 135 3582 2378 2969 94 137 5 3 2

ATOM 954 NH2 ARG 135 13.287 26.758 36.035 1.000 24.30

ANISOU 954 NH2 ARG 135 3520 2441 3272 -101 72 5 8 2

ATOM 955 N GLU 136 19.403 23.533 40.149 1.000 15.76

ANISOU 955 N GLU 136 1897 1696 2396 -178 17 3 1 8

ATOM 956 CA GLU 136 20.752 23.431 40.694 1.000 15.16

ANISOU 956 CA GLU 136 1687 1770 2302 -97 279 14 0

ATOM 957 C GLU 136 21.186 22.001 40.978 1.000 16.74

ANISOU 957 C GLU 136 1535 1704 3122 -148 -172 - 72

ATOM 958 O GLU 136 22.350 21.637 40.701 1.000 17.42

ANISOU 958 O GLU 136 1710 1908 2999 7 30 9 2

ATOM 959 CB GLU 136 20.957 24.284 41.962 1.000 16.64

ANISOU 959 CB GLU 136 2048 1785 2487 53 11 - 16

ATOM 960 CG GLU 136 20.762 25.772 41.718 1.000 17.80

ANISOU 960 CG GLU 136 2036 1714 3014 -286 -169 110

ATOM 961 CD GLU 136 21.534 26.269 40.513 1.000 20.92

ANISOU 961 CD GLU 136 2174 2273 3503 -343 70 469

ATOM 962 OEl GLU 136 22.742 25.987 40.454 1.000 24.97

ANISOU 962 OEl GLU 136 2116 2434 4938 -494 531 2 19

ATOM 963 OE2 GLU 136 21.022 27.037 39.672 1.000 24.77

ANISOU 963 OE2 GLU 136 2975 2618 3817 -708 -133 1029

ATOM^' 964 N VAL 137 20.262 21.172 41.450 1.000 15.34

ANISOU 964 N VAL 137 1681 1696 2453 -108 -287 113

ATOM 965 CA VAL 137 20.568 19.750 41.647 1.000 15.92

ANISOU 965 CA VAL 137 1755 1802 2493 83 -4 2 1 0

ATOM 966 C VAL 137 20.926 19.086 40.326 1.000 15.86

ANISOU 966 C VAL 137 1604 1869 2555 -38 -35 6 6

ATOM 967 O VAL 137 21.905 18.308 40.174 1.000 16.70

ANISOU 967 O VAL 137 1617 2118 2609 72 -151 - 9 0

ATOM 968 CB VAL 137 19.358 18.990 42.283 1.000 15.35

ANISOU 968 CB VAL 137 1729 1663 2440 8 -29 5

ATOM 969 CGI . VAL 137 19.607 17.478 42.176 1.000 16.93

ANISOU 969 CGI . VAL 137 1521 1689 3223 160 -345 9 6

ATOM 970 CG2 ! VAL 137 19.144 19.420 43.724 1.000 15.43

ANISOU 970 CG2 ! VAL 137 1529 2090 2245 -53 -277 185

ATOM 971 N LEU 138 20.149 19.407 39.284 1.000 15.52

ANISOU 971 N LEU 138 1625 1735 2535 -105 -61 109

ATOM 972 CA LEU 138 20.378 18.881 37.936 1.000 15.74

ANISOU 972 CA LEU 138 1576 1862 2543 -71 15 5 1

ATOM 973 C LEU 138 21.721 19.396 37.406 1.000 17.42

ANISOU 973 C LEU 138 1588 2119 2912 -87 162 - 4 5

ATOM 974 O LEU 138 22.503 18.609 36.846 1.000 19.13

ANISOU 974 O LEU 138 1878 2406 2985 186 317 6 2

ATOM 975 CB LEU 138 19.211 19.248 36.996 1.000 14.70

ANISOU 975 CB LEU 138 1592 1642 2349 -50 141 1 9 0

ATOM 976 CG LEU 138 17.883 18.541 37.375 1.000 14.38

ANISOU 976 CG LEU 138 1657 1409 2399 -44 -4 2 8 8 ATOM 977 CDI LEU 138 16.774 19.122 36.491 1.000 16. — J

ANISOU 977 CDI LEU 138 1743 1848 2539 128 -218 1 6

ATOM 978 CD2 LEU 138 17.975 17.027 37.156 1.000 17. 48

ANISOU 978 CD2 LEU 138 2185 1435 3021 -107 -48C : 2 8

ATOM 979 N ARG 139 21.963 20.708 37.548 1.000 17. s ά

ANISOU 979 N ARG 139 1797 2157 2674 -319 238 1 S

ATOM 980 CA ARG 139 23.189 21.319 36.996 1.000 19. 06

ANISOU 980 CA ARG 139 2043 2462 2735 -366 482 3 7

ATOM 981 C ARG 139 24.419 20.734 37.685 1.000 19. 72

ANISOU 981 C ARG 139 1797 2600 3097 -518 482 3 1

ATOM 982 O ARG 139 25.461 20.432 37.094 1.000 20. 70

ANISOU 982 O ARG 139 2046 2469 3350 -288 607 1 S

ATOM 983 CB ARG 139 23.152 22.850 37.101 1.000 24. 54

ANISOU 983 CB ARG 139 2525 2403 4396 -402 951 6 -

ATOM 984 CG ARG 139 23.886 23.665 36.073 1.000 36. 05

ANISOU 984 CG ARG 139 6517 2967 4212 -2176 160S ⁾ 1 .

ATOM 985 CD ARG 139 23.852 25.148 36.443 1.000 4 444..9 955

ANISOU 985 CD ARG 139 7459 1902 7716 -242 - -113322 >44 1I 9 3 0

ATOM 986 NE ARG 139 22.525 25.727 36.547 1.000 4 433..2 277

ANISOU 986 NE ARG 139 6637 3846 5959 -828 - -22117: '33 -- 6 9 8

ATOM 987 CZ ARG 139 21.821 26.330 35.605 1.000 4411 .. 3344

ANISOU 987 CZ ARG 139 5939 4102 5666 497 6 64455 1 1114 0

ATOM 988 NHl ARG 139 22.308 26.436 34.376 1.000 4444 .. 0011

ANISOU 988 NHl ARG 139 6564 4146 6011 550 1 133993: . 33 3 : 6

ATOM 989 NH2 ARG 139 20.614 26.837 35.833 1.000 4 455..7 755

ANISOU 989 NH2 ARG 139 6162 4618 6602 537 1 199338, . 2244 0 5

ATOM 990 N ALA 140 24.357 20.566 39.009 1.000 1 188..7 1 71

ANISOU 990 N ALA 140 1742 2387 3003 -255 114455 66 9

ATOM 991 CA ALA 140 25.532 20.169 39.773 1.000 19. 53

ANISOU 991 CA ALA 140 1583 2641 3197 -28 38 - - 66

ATOM 992 C ALA 140 25.932 18.732 39.490 1.000 18. 96

ANISOU 992 C ALA 140 2018 2342 2843 -67 76 - - 10

ATOM 993 O ALA 140 27.109 18.335 39.626 1.000 21. 36

ANISOU 993 O ALA 140 1900 2436 3778 -2 472 - 8 0

ATOM 994 CB ALA 140 25.273 20.345 41.275 1.000 19. 74

ANISOU 994 CB ALA 140 1824 2592 3084 35 0 - 360

ATOM 995 N THR 141 24.958 17.943 39.062 1.000 20. 32

ANISOU 995 N THR 141 2014 2209 3498 -115 305 _ 1 1 3

ATOM 996 CA THR 141 25.151 16.530 38.717 1.000 17. 15

ANISOU 996 CA THR 141 1870 2039 2609 61 51 21 : 3

ATOM 997 C THR 141 25.269 16.278 37.208 1.000 17. 44

ANISOU 997 C THR 141 1492 2443 2693 21 278 1 ' 9

ATOM 998 O THR 141 25.343 15.106 36.792 1.000 19. 24

ANISOU 998 O THR 141 1871 2623 2814 63 579 - 6 ; 3

ATOM 999 CB THR 141 24.048 15.629 39.290 1.000 16. 79

ANISOU 999 CB THR 141 1708 2261 2410 83 164 3 1

ATOM 1000 OGl . THR 141 22.788 16.012 38.710 1.000 17. 18

ANISOU 1000 OGl . THR 141 1894 2235 2399 -101 -53 5

ATOM 1001 CG2 : THR 141 23.982 15.734 40.807 1.000 17. .83

ANISOU 1001 CG2 : THR 141 1521 2878 2377 164 -43 2

ATOM 1002 N GLY 142 25.361 17.301 36.381 1.000 19. .69

ANISOU 1002 N GLY 142 2091 2789 2603 -708 302 2 9 7

ATOM 1003 CA GLY 142 25.517 17.123 34.923 1.000 19. .08

ANISOU 1003 CA GLY 142 1878 2819 2551 128 -163 2 5 5

ATOM 1004 C GLY 142 24.284 16.441 34.313 1.000 18 .75

ANISOU 1004 C GLY 142 1972 2410 2744 0 252 - 117

ATOM 1005 O GLY 142 24.443 15.755 33.315 1.000 22 .41

ANISOU 1005 O GLY 142 2432 2681 3403 -161 571 - 6 8 0

ATOM 1006ι N THR 143 23.093 16.650 34.854 1.000 17 .28

ANISOU 1006i N THR 143 1895 2002 2667 67 300 2 • 44

ATOM 1007 ' CA THR 143 21.909 15.932 34.393 1.000 1 16 .88 ANISOU 1007 C THR 143 1953 2006 2456 164 332 6 ,

ATOM 1008 C THR 143 20.998 16.660 33.432 1.000 17.02

ANISOU 1008 C THR 143 2149 1795 2521 82 196 117

ATOM 1009 O THR 143 20.457 17.713 33.764 1.000 20.30

ANISOU 1009 O THR 143 2795 1815 3103 344 12 - 28

ATOM 1010 CB THR 143 21.085 15.490 35.623 1.000 16.40

ANISOU 1010 CB THR 143 1755 2329 2148 -37 95 - 44

ATOM 1011 OGl THR 143 21.922 14.692 36.479 1.000 17.82

ANISOU 1011 OGl THR 143 2009 2075 2688 -109 39 3 3 7

ATOM 1012 CG2 THR 143 19.887 14.621 35.270 1.000 19.51

ANISOU 1012 CG2 THR 143 1957 2290 3167 -192 -94 10

ATOM 1013 N GLU 144 20.742 16.070 32.248 1.000 18 .79

ANISOU 1013 N GLU 144 2138 2203 2800 47 12 - 121

ATOM 1014 CA GLU 144 19.729 16.573 31.334 1.000 20.13

ANISOU 1014 CA GLU 144 2202 2696 2750 -292 -41 3 1

ATOM 1015 C GLU 144 18.637 15.506 31.254 1.000 19.18

ANISOU 1015 C GLU 144 2255 2614 2418 -292 230 - 1 31

ATOM 1016 O GLU 144 18.827 14.438 30.665 1.000 21.46

ANISOU 1016 O GLU 144 2268 2442 3446 19 649 - 88

ATOM 1017 CB AGLU 144 20.250 17.061 30.006 0.753 29.50

ANISOU 1017 CB AGLU 144 3376 4266 3566 -855 206 15 01

ATOM 1018 CG AGLU 144 20.195 18.567 29.741 0.753 36.54

ANISOU 1018 CG AGLU 144 6059 3913 3913 -1728 1769 7 9

ATOM 1019 CD AGLU 144 21.242 19.411 30.426 0.753 33 .13

ANISOU 1019 CD AGLU 144 4189 3432 4966 104 744 88

ATOM 1020 OE1AGLU 144 21.079 19.690 31.641 0.753 51.91

ANISOU 1020 OE1AGLU 144 3684 11101 4940 -868 -202 - 5 90

ATOM 1021 OE2AGLU 144 22.207 19.910 29.807 0.753 50.79

ANISOU 1021 OE2AGLU 144 7949 3695 7653 -3071 3099 -1 249

ATOM 1022 CB BGLU 144 20.372 16.724 29.951 0.247 18.36

ANISOU 1022 CB BGLU 144 868 3091 3016 334 16 262

ATOM 1023 CG BGLU 144 21.214 17.988 29.779 0.247 23 .54

ANISOU 1023 CG BGLU 144 1301 3586 4056 -38 595 55

ATOM 1024 CD BGLU 144 21.150 18.468 28.336 0.247 33.24

ANISOU 1024 CD BGLU 144 3589 3975 5064 438 -20 20 31

ATOM 1025 OE1BGLU 144 20.417 17.818 27.557 0.247 28.68

ANISOU 1025 OE1BGLU 144 3222 4813 2861 389 1729 12

ATOM 1026 OE2BGLU 144 21.814 19.464 27.990 0.247 35.35

ANISOU 1026 OE2BGLU 144 3176 5148 5108 35 1752 151

ATOM 1027 N PRO 145 17.508 15.724 31.911 1.000 17.11

ANISOU 1027 N PRO 145 2132 1825 2543 68 62 15 8

ATOM 1028 CA PRO 145 16.396 14.781 31.846 1.000 17.41

ANISOU 1028 CA PRO 145 2290 1942 2384 -73 400 1

ATOM 1029 C PRO 145 15.966 14.546 30.406 1.000 17.94

ANISOU 1029 C PRO 145 2386 1955 2475 -116 292 - 1 04

ATOM 1030 O PRO 145 16.068 15.439 29.557 1.000 18.26

ANISOU 1030 O PRO 145 2271 2196 2472 -272 170 4

ATOM 1031 CB PRO 145 15.250 15.493 32.594 1.000 17.07

ANISOU 1031 CB PRO 145 2181 1771 2534 35 133 - 143

ATOM 1032 CG PRO 145 15.950 16.504 33.464 1.000 17.11

ANISOU 1032 CG PRO 145 2341 1841 2319 23 -49 - 24

ATOM 1033 CD PRO 145 17.131 16.977 32.649 1.000 17.54

ANISOU 1033 CD PRO 145 2178 1601 2884 178 -88 3 0 3

ATOM 1034 N ASP 146 15.490 13.346 30.104 1.000 18.15

ANISOU 1034 N ASP 146 2140 1965 2790 -60 321 - 1 - 52

ATOM 1035 CA ASP 146 14.909 13.121 28.775 1.000 18.43

ANISOU 1035 CA ASP 146 2487 1664 2853 -329 310 - : 156

ATOM 1036 C ASP 146 13.809 14.154 28.566 1.000 18.07

ANISOU 1036 C ASP 146 2824 1979 2064 -31 208 - - :309

ATOM 1037 O ASP 146 12.959 14.333 29.422 1.000 18.29

ANISOU 1037 O ASP 146 2491 2173 2287 -168 203 - 230 ATOM 1038 CB ASP 146 14.221 11.735 28.717 1.000 23.50

ANISOU 1038 CB ASP 146 3489 1671 3769 -653 908 - 665

ATOM 1039 CG ASP 146 13.636 11.508 27.334 1.000 34.15

ANISOU 1039 CG ASP 146 4070 4205 4700 -1004 361 -2386

ATOM 1040 ODl ASP 146 12.393 11.521 27.138 1.000 44.73

ANISOU 1040 ODl ASP 146 3971 9175 3849 -2156 683 3 7 8

ATOM 1041 OD2 ASP 146 14.421 11.229 26.397 1.000 44.78

ANISOU 1041 OD2 ASP 146 4342 8626 4046 -813 289 -2326

ATOM 1042 N GLY 147 13.901 14.854 27.450 1.000 19.28

ANISOU 1042 N GLY 147 2622 2331 2374 -635 -72 1 13

ATOM 1043 CA GLY 147 12.916 15.878 27.171 1.000 18.58

ANISOU 1043 CA GLY 147 2463 2607 1991 -550 -234 - 3 6

ATOM 1044 C GLY 147 13.355 17.262 27.590 1.000 18.25

ANISOU 1044 C GLY 147 2511 2432 1993 -335 -138 6 4

ATOM 1045 O GLY 147 12.586 18.183 27.289 1.000 20.74

ANISOU 1045 O GLY 147 2469 2739 2673 -182 -144 2 05

ATOM 1046 N GLY 148 14.494 17.357 28.286 1.000 17.38

ANISOU 1046 N GLY 148 2237 2174 2191 -462 -42 - 9 0

ATOM 1047 CA GLY 148 15.027 18.658 28.672 1.000 16.72

ANISOU 1047 CA GLY 148 2308 1789 2255 39 -82 - 77

ATOM 1048 C GLY 148 14.653 19.076 30.085 1.000 13.94

ANISOU 1048 C GLY 148 1517 1645 2135 77 -201 117

ATOM 1049 O GLY 148 13.637 18.634 30.694 1.000 16.29

ANISOU 1049 O GLY 148 1839 1863 2487 -151 -77 2 8 5

ATOM 1050 N VAL 149 15.431 20.003 30.641 1.000 14.93

ANISOU 1050 N VAL 149 1624 1780 2269 1 -193 - 14

ATOM 1051 CA VAL 149 15.275 20.509 32.017 1.000 14.16

ANISOU 1051 CA VAL 149 1647 1511 2222 92 -195 8 6

ATOM 1052 C VAL 149 13.958 21.218 32.235 1.000 14.37

ANISOU 1052 C VAL 149 1735 1044 2682 -39 83 188

ATOM 1053 O VAL 149 13.203 20.970 33.163 1.000 14.63

ANISOU 1053 O VAL 149 1653 1517 2390 -160 -40 107

ATOM 1054 CB VAL 149 16.439 21.410 32.417 1.000 14.02

ANISOU 1054 CB VAL 149 1745 1530 2052 -112 -57 2 7 0

ATOM 1055 CGI VAL 149 16.228 22.101 33.752 1.000 16.48

ANISOU 1055 CGI VAL 149 2360 1709 2193 -153 -305 8 7

ATOM 1056 CG2 VAL 149 17.733 20.614 32.482 1.000 17.85

ANISOU 1056 CG2 VAL 149 1618 1937 3226 -59 -52 441

ATOM 1057 N GLU 150 13.634 22.199 31.371 1.000 15.26

ANISOU 1057 N GLU 150 1759 1328 2711 186 36 2 67

ATOM 1058 CA GLU 150 12.471 23.028 31.687 1.000 14.91

ANISOU 1058 CA GLU 150 1591 1434 2640 93 13 415

ATOM 1059 C GLU 150 11.182 22.237 31.553 1.000 16.66

ANISOU 1059 C GLU 150 1680 1980 2670 -197 113 19 9

ATOM 1060 O GLU 150 10.259 22.408 32.379 1.000 15.89

ANISOU 1060 O GLU 150 1697 1761 2578 29 79 580

ATOM 1061 CB GLU 150 12.531 24.305 30.874 1.000 17.07

ANISOU 1061 CB GLU 150 1925 1337 3223 254 189 5 13

ATOM 1062 CG GLU 150 13.761 25.167 31.220 1.000 19.00

ANISOU 1062 CG GLU 150 2483 1212 3523 -65 -95 4 65

ATOM 1063 CD GLU 150 13.810 25.624 32.658 1.000 20.32

ANISOU 1063 CD GLU 150 2444 1746 3532 -130 -24 4 54

ATOM 1064 OEl . GLU 150 12.781 25.749 33.377 1.000 20.88

ANISOU 1064 OEl . GLU 150 2558 1728 3648 29 58 396

ATOM 1065 OE2 ! GLU 150 14.913 25.946 33.161 1.000 21.77

ANISOU 1065 OE2 ! GLU 150 2549 2030 3693 -165 -202 2 7 3

ATOM 1066 N ALA 151 11.050 21.288 30.603 1.000 14.98

ANISOU 1066 N ALA 151 1649 1710 2334 37 -307 5 5 1

ATOM 1067 CA ALA 151 9.834 20.475 30.543 1.000 15.79

ANISOU 1067 CA ALA 151 1820 2045 2136 -173 -198 408

ATOM 1068 C ALA 151 9.748 19.531 31.724 1.000 15.38 ANISOU 1068 C ALA 151 1674 1953 2216 165 181 4 42

ATOM 1069 0 ALA 151 8.642 19.186 32.184 1.000 16.51

ANISOU 1069 0 ALA 151 1778 1852 2643 -152 110 3 3 C

ATOM 1070 CB ALA 151 9.823 19.663 29.236 1.000 18.05

ANISOU 1070 CB ALA 151 1910 2811 2139 -275 -316 1 6 c

ATOM 1071 N PHE 152 10.893 19.135 32.306 1.000 14.25

ANISOU 1071 N PHE 152 1858 1132 2423 10 -107 2 63

ATOM 1072 CA PHE 152 10.893 18.285 33.493 1.000 13 .42

ANISOU 1072 CA PHE 152 1457 1291 2353 -102 -34 3 04

ATOM 1073 C PHE 152 10.406 19.056 34.695 1.000 13 .93

ANISOU 1073 C PHE 152 1481 1400 2412 -43 -165 1 9 .

ATOM 1074 O PHE 152 9.679 18.495 35.558 1.000 14.50

ANISOU 1074 O PHE 152 1590 1482 2438 -85 25 2 6

ATOM 1075 CB PHE 152 12.309 17.744 33.728 1.000 13 .95

ANISOU 1075 CB PHE 152 1504 1547 2248 -29 111 4 63

ATOM 1076 CG PHE 152 12.475 16.966 35.011 1.000 14.04

ANISOU 1076 CG PHE 152 1747 1386 2200 88 -58 2 47

ATOM 1077 CDI PHE 152 12.032 15.653 35.076 1.000 13 .90

ANISOU 1077 CDI PHE 152 1906 1306 2069 165 -36 2 8 1

ATOM 1078 CD2 PHE 152 13.094 17.499 36.127 1.000 15.67

ANISOU 1078 CD2 PHE 152 1927 1770 2259 -155 -115 2 3 :

ATOM 1079 CE1 PHE 152 12.213 14.949 36.263 1.000 14.06

ANISOU 1079 CE1 PHE 152 1669 1507 2165 182 -282 3 4 ^'

ATOM 1080 CE2 PHE 152 13.323 16.799 37.276 1.000 14.83

ANISOU 1080 CE2 PHE 152 1724 1671 2240 35 -112 165

ATOM 1081 CZ PHE 152 12.861 15.522 37.361 1.000 14.86

ANISOU 1081 CZ PHE 152 1994 1734 1916 -162 99 .113

ATOM 1082 N LEU 153 10.789 20.324 34.789 1.000 15.25

ANISOU 1082 N LEU 153 1742 1355 2696 58 110 154

ATOM 1083 CA LEU 153 10.454 21.151 35.939 1.000 14.65

ANISOU 1083 CA LEU 153 1783 1429 2354 -66 16 2 03

ATOM 1084 C LEU 153 9.082 21.791 35.877 1.000 14.47

ANISOU 1084 C LEU 153 1732 1402 2362 -80 76 1 1

ATOM 1085 O LEU 153 8.581 22.216 36.953 1.000 15.82

ANISOU 1085 O LEU 153 1940 1454 2616 -313 312 -IE

ATOM 1086 CB LEU 153 11.537 22.224 36.165 1.000 16.53

ANISOU 1086 CB LEU 153 1626 1451 3205 -23 269 - 8 :

ATOM 1087 CG LEU 153 12.914 21.685 36.514 1.000 15.90

ANISOU 1087 CG LEU 153 1893 2013 2135 -33 -186 - 3

ATOM 1088 CDI LEU 153 13.922 22.829 36.614 1.000 18.41

ANISOU 1088 CDI LEU 153 1732 2473 2791 -156 80 - 876

ATOM 1089 CD2 LEU 153 12.863 20.883 37.794 1.000 21.76

ANISOU 1089 CD2 LEU 153 3083 3182 2005 365 261 19

ATOM 1090 N ASP 154 8.473 21.866 34.708 1.000 14.41

ANISOU 1090 N ASP 154 1768 1181 2525 -25 -8 2 93

ATOM 1091 CA ASP 154 7.092 22.373 34.553 1.000 15.90

ANISOU 1091 CA ASP 154 1665 1615 2760 -195 27 7 69

ATOM 1092 C ASP 154 6.216 21.161 34.814 1.000 14.66

ANISOU 1092 C ASP 154 1859 1304 2409 -92 143 5 1

ATOM 1093 O ASP 154 5.995 20.368 33.889 1.000 17.30

ANISOU 1093 O ASP 154 2561 1455 2557 -29 314 2 3

ATOM 1094 CB ASP 154 6.923 22.909 33.125 1.000 18.59

ANISOU 1094 CB ASP 154 1905 2077 3081 124 269 13 : 17

ATOM 1095 CG ASP 154 5.461 23.157 32.768 1.000 19.87

ANISOU 1095 CG ASP 154 2029 2531 2990 226 129 14 : 36

ATOM 1096 ODl . ASP 154 4.561 23.253 33.639 1.000 19.68

ANISOU 1096 ODl . ASP 154 1949 2209 3318 92 221 4 9 6

ATOM 1097 OD2 ! ASP 154 5.207 23.189 31.554 1.000 23 .73

ANISOU 1097 OD2 ! ASP 154 2512 3475 3029 246 -137 6 5

ATOM 1098 N CYS 155 5.831 20.904 36.070 1.000 14.25

ANISOU 1098 N CYS 155 1708 1365 2342 -101 -62 54 ---- -..

-49-

ATOM 1099 CA CYS 155 5.418 19.569 36.468 1.000 13 .45

ANISOU 1099 CA CYS 155 1608 1346 2158 -191 4 45 8

ATOM 1100 C CYS 155 4.157 19.574 37.302 1.000 12 . 9

ANISOU 1100 C CYS 155 1644 1331 1772 -200 -148 6 2

ATOM 1101 O CYS 155 3.224 20.303 36.941 1.000 14.55

ANISOU 1101 O CYS 155 1633 1492 2402 -122 -111 44 :

ATOM 1102 CB CYS 155 6.664 18.872 37.098 1.000 14.37

ANISOU 1102 CB CYS 155 1907 1366 2186 122 -137 2 l :

ATOM 1103 SG CYS 155 7.265 19.595 38.641 1.000 14.99

ANISOU 1103 SG CYS 155 1561 1821 2315 -74 -98 1 8 :

ATOM 1104 N GLU 156 4.060 18.706 38.316 1.000 12 .89

ANISOU 1104 N GLU 156 1575 1379 1945 -130 29 1 9 4

ATOM 1105 CA GLU 156 2.788 18.447 39.029 1.000 12.98

ANISOU 1105 CA GLU 156 1508 1311 2114 -210 21 14 0

ATOM 1106 C GLU 156 2.987 18.676 40.510 1.000 12.34

ANISOU 1106 C GLU 156 1414 1198 2078 102 24 2 04

ATOM 1107 O GLU 156 2.828 17.757 41.289 1.000 14.89

ANISOU 1107 O GLU 156 1875 1425 2359 -15 -54 44 :

ATOM 1108 CB GLU 156 2.278 17.047 38.678 1.000 14.48

ANISOU 1108 CB GLU 156 1968 1323 2213 -279 120 8 7

ATOM 1109 CG GLU 156 1.855 17.038 37.227 1.000 14.86

ANISOU 1109 CG GLU 156 1894 1526 2227 -120 95 - 152

ATOM 1110 CD GLU 156 0.523 17.687 36.932 1.000 17.10

ANISOU 1110 CD GLU 156 2091 1976 2431 44 -4 144

ATOM 1111 OEl GLU 156 -0.204 17.967 37.886 1.000 17.98

ANISOU 1111 OEl GLU 156 1811 2155 2866 -35 10 - 355

ATOM 1112 OE2 GLU 156 0.214 17.990 35.759 1.000 20.99

ANISOU 1112 OE2 GLU 156 2854 2419 2704 -386 -516 5 6

ATOM 1113 N PRO 157 3.292 19.893 40.958 1.000 12.09

ANISOU 1113 N PRO 157 1314 1347 1934 12 -48 249

ATOM 1114 CA PRO 157 3.576 20.121 42.391 1.000 13.28

ANISOU 1114 CA PRO 157 1425 1696 1924 -68 117 14

ATOM 1115 C PRO 157 2.330 19.996 43.248 1.000 12.87

ANISOU 1115 C PRO 157 1236 1737 1916 -214 -47 12

ATOM 1116 O PRO 157 1.192 20.190 42.744 1.000 13.73

ANISOU 1116 O PRO 157 1286 1717 2214 -190 -17 14

ATOM 1117 CB PRO 157 4.061 21.580 42.407 1.000 13 .94

ANISOU 1117 CB PRO 157 1518 1729 2047 -289 -166 2 4

ATOM 1118 CG PRO 157 3.363 22.184 41.226 1.000 13.06

ANISOU 1118 CG PRO 157 1558 1518 1887 -32 -158 - 8

ATOM 1119 CD PRO 157 3.494 21.128 40.167 1.000 12.03

ANISOU 1119 CD PRO 157 1521 1081 1968 -2 -7 121

ATOM 1120 N LEU 158 2.542 19.738 44.526 1.000 13.02

ANISOU 1120 N LEU 158 1554 1493 1899 -124 148 7 3

ATOM 1121 CA LEU 158 1.438 19.699 45.496 1.000 12.72

ANISOU 1121 CA LEU 158 1465 1552 1815 -126 -14 3 6

ATOM 1122 C LEU 158 1.927 20.389 46.772 1.000 12.90

ANISOU 1122 C LEU 158 1230 1715 1957 -27 -29 - 8

ATOM 1123 O LEU 158 2.975 19.977 47.289 1.000 14.06

ANISOU 1123 O LEU 158 1374 1666 2304 59 -257 - 23 .

ATOM 1124 CB LEU 158 1.046 18.244 45.815 1.000 13.58

ANISOU 1124 CB LEU 158 1673 1590 1896 -213 57 17 1

ATOM 1125 CG LEU 158 0.044 18.030 46.945 1.000 14.84

ANISOU 1125 CG LEU 158 1471 1774 2396 -16 262 2 4

ATOM 1126 CDI LEU 158 -1.333 18.635 46.671 1.000 16.96

ANISOU 1126 CDI LEU 158 1485 2196 2764 5 -148 - 40 :

ATOM 1127 CD2 LEU 158 -0.142 16.539 47.161 1.000 ι 14.98

ANISOU 1127 CD2 LEU 158 1976 1820 1897 -390 171 7 -

ATOM 1128 N LEU 159 1.139 21.306 47.283 1.00C 1 13.44

ANISOU 1128 N LEU 159 1509 1434 2165 43 -87 - 119

ATOM 1129 CA LEU 159 1.443 21.963 48.571 . 1.00C ) 13.39 ANISOU 1129 CA LEU 159 1438 1555 2095 -36 -80 - 9 1

ATOM 1130 C LEU 159 0.419 21.494 49.602 1.000 14.49

ANISOU 1130 C LEU 159 1336 2034 2135 -152 -208 - 3 8

ATOM 1131 0 LEU 159 -0.790 21.596 49.419 1.000 15.09

ANISOU 1131 0 LEU 159 1414 1999 2319 90 -131 9 0

ATOM 1132 CB LEU 159 1.390 23.466 48.394 1.000 15.28

ANISOU 1132 CB LEU 159 1720 1447 2639 55 -325 - 197

ATOM 1133 CG LEU 159 1.484 24.320 49.669 1.000 17.11

ANISOU 1133 CG LEU 159 2146 1689 2665 363 -332 - 343

ATOM 1134 CDI LEU 159 2.775 24.114 50.453 1.000 18 .70

ANISOU 1134 CDI LEU 159 2276 1759 3070 379 -687 - 540

ATOM 1135 CD2 LEU 159 1.312 25.801 49.291 1.000 21.00

ANISOU 1135 CD2 LEU 159 2918 1535 3526 439 -692 - 382

ATOM 1136 N ARG 160 0.916 21.107 50.774 1.000 14.37

ANISOU 1136 N ARG 160 1688 1709 2063 -101 -186 4 7

ATOM 1137 CA ARG 160 0.055 20.747 51.901 1.000 15.61

ANISOU 1137 CA ARG 160 1726 1990 2217 -64 90 - 118

ATOM 1138 C ARG 160 0.480 21.501 53.155 1.000 15.40

ANISOU 1138 C ARG 160 1557 2158 2135 -34 -46 - 3 8

ATOM 1139 0 ARG 160 1.639 21.401 53.576 1.000 16.32

ANISOU 1139 0 ARG 160 1528 2508 2164 63 41 - 104

ATOM 1140 CB ARG 160 0.048 19.263 52.227 1.000 16.13

ANISOU 1140 CB ARG 160 2134 2084 1912 -127 -30 12 9

ATOM 1141 CG ARG 160 -0.594 18.410 51.155 1.000 17.17

ANISOU 1141 CG ARG 160 1963 1934 2628 -140 -212 - 60

ATOM 1142 CD ARG 160 -0.672 16.959 51.627 1.000 18.16

ANISOU 1142 CD ARG 160 2767 1965 2166 125 -330 - 3 5

ATOM 1143 NE ARG 160 -1.382 16.102 50.682 1.000 18.11

ANISOU 1143 NE ARG 160 2408 1775 2699 -56 -308 2 0

ATOM 1144 CZ ARG 160 -1.221 14.789 50.581 1.000 16.76

ANISOU 1144 CZ ARG 160 2191 1748 2428 -97 55 17 4

ATOM 1145 NHl ARG 160 -0.326 14.192 51.374 1.000 20.55

ANISOU 1145 NHl ARG 160 2306 2012 3491 -26 -457 3 05

ATOM 1146 NH2 ARG 160 -1.908 14.095 49.689 1.000 19.23

ANISOU 1146 NH2 ARG 160 2502 2031 2774 181 -147 - 338

ATOM 1147 N PHE 161 -0.469 22.257 53.755 1.000 15.36

ANISOU 1147 N PHE 161 1604 2120 2111 -37 -63 - 128

ATOM 1148 CA PHE 161 -0.209 22.975 54.999 1.000 16.25

ANISOU 1148 CA PHE 161 2173 1774 2227 -71 -187 - 89

ATOM 1149 C PHE 161 -1.030 22.236 56.069 1.000 16.98

ANISOU 1149 C PHE 161 1980 2432 2041 -217 -161 - 162

ATOM 1150 O PHE 161 -2.248 22.113 55.948 1.000 20.38

ANISOU 1150 O PHE 161 1981 3291 2473 -190 -191 - 72

ATOM 1151 CB PHE 161 -0.683 24.431 54.862 1.000 19.76

ANISOU 1151 CB PHE 161 2065 1903 3540 167 355 - 198

ATOM 1152 CG PHE 161 -0.379 25.259 56.109 1.000 23.61

ANISOU 1152 CG PHE 161 3026 1905 4041 836 -59 - 591

ATOM 1153 CDI PHE 161 -1.194 25.304 57.228 1.000 28.25

ANISOU 1153 CDI PHE 161 3992 2474 4268 1077 369 -1253

ATOM 1154 CD2 PHE 161 0.807 25.978 56.141 1.000 26.62

ANISOU 1154 CD2 PHE 161 4015 2483 3616 -130 -927 - 106

ATOM 1155 CE1 . PHE 161 -0.850 25.992 58.383 1.000 35.29

ANISOU 1155 CE1 . PHE 161 6873 2097 4437 1538 -135 -1399

ATOM 1156 CE2 : PHE 161 1.153 26.723 57.258 1.000 33 .63

ANISOU 1156 CE2 : PHE 161 4643 3240 4894 1263 -2085 -1268

ATOM 1157 CZ PHE 161 0.320 26.726 58.363 1.000 36.44

ANISOU 1157 CZ PHE 161 6071 4282 3493 1455 -2477 -1044

ATOM 1158 N ARG 162 -0.358 21.767 57.130 1.000 17.59

ANISOU 1158 N ARG 162 2095 2487 2103 -118 -135 - 69

ATOM 1159 CA ARG 162 -1.072 21.078 58.199 1.000 18.27

ANISOU 1159 CA ARG 162 2769 2414 1758 6 178 - 378 ATOM 1160 C ARG 162 -0.880 21.758 59.553 1.000 20.16

ANISOU 1160 C ARG 162 2110 3341 2210 -36 41 - 960

ATOM 1161 0 ARG 162 0.217 22.160 59.893 1.000 19.61

ANISOU 1161 0 ARG 162 2257 2993 2201 -194 -73 - 359

ATOM 1162 CB ARG 162 -0.580 19.640 58.356 1.000 20.81

ANISOU 1162 CB ARG 162 2958 2275 2675 -129 6 - 169

ATOM 1163 CG ARG 162 -0.843 18.724 57.166 1.000 19.90

ANISOU 1163 CG ARG 162 3044 2073 2443 -112 254 - 3 8

ATOM 1164 CD ARG 162 -0.182 17.383 57.393 1.000 28.02

ANISOU 1164 CD ARG 162 5599 2038 3010 381 -14 1 14

ATOM 1165 NE ARG 162 -0.369 16.420 56.326 1.000 27.74

ANISOU 1165 NE ARG 162 4151 2294 4097 555 -687 - 434

ATOM 1166 CZ ARG 162 -1.278 15.445 56.370 1.000 31.11

ANISOU 1166 CZ ARG 162 2560 3729 5531 470 -350 - 1152

ATOM 1167 NHl ARG 162 -2.092 15.324 57.403 1.000 42.97

ANISOU 1167 NHl ARG 162 3475 5906 6946 -579 1019 - 2492

ATOM 1168 NH2 ARG 162 -1.329 14.603 55.353 1.000 29.64

ANISOU 1168 NH2 ARG 162 3066 2738 5458 120 -143 - 708

ATOM 1169 N TYR 163 -1.956 21.780 60.311 1.000 19.52

ANISOU 1169 N TYR 163 2394 2901 2120 147 263 - 763

ATOM 1170 CA TYR 163 -1.943 22.102 61.732 1.000 22.74

ANISOU 1170 CA TYR 163 3312 3107 2219 369 302 - 878

ATOM 1171 C TYR 163 -2.037 20.800 62.536 1.000 24.20

ANISOU 1171 C TYR 163 2802 3901 2492 -222 253 - 189

ATOM 1172 0 TYR 163 -2.992 20.049 62.274 1.000 28.02

ANISOU 1172 0 TYR 163 2305 4409 3934 -202 -126 3 99

ATOM 1173 CB TYR 163 -3.198 22.912 62.114 1.000 28.98

ANISOU 1173 CB TYR 163 3861 3231 3920 267 1196 -1783

ATOM 1174 CG TYR 163 -3.342 22.997 63.623 1.000 25.58

ANISOU 1174 CG TYR 163 2572 3382 3767 543 749 -1204

ATOM 1175 CDI TYR 163 -2.458 23.826 64.319 1.000 37.32

ANISOU 1175 CDI TYR 163 3654 6112 4413 -759 884 -2373

ATOM 1176 CD2 TYR 163 -4.315 22.333 64.345 1.000 29.13

ANISOU 1176 CD2 TYR 163 2622 3994 4452 749 1084 - 769

ATOM 1177 CE1 TYR 163 -2.546 23.966 65.702 1.000 38.28

ANISOU 1177 CE1 TYR 163 2905 7138 4503 -454 987 -2740

ATOM 1178 CE2 TYR 163 -4.396 22.431 65.726 1.000 37.36

ANISOU 1178 CE2 TYR 163 3220 6336 4640 -273 1997 - 1618

ATOM 1179 CZ TYR 163 -3.500 23.250 66.393 1.000 49.85

ANISOU 1179 CZ TYR 163 5272 8795 4872 -1810 1593 -2223

ATOM 1180 OH TYR 163 -3.595 23.365 67.768 1.000 44.81

ANISOU 1180 OH TYR 163 5246 7368 4413 -222 270 - 496

ATOM 1181 N PHE 164 -1.098 20.651 63.448 1.000 24.84

ANISOU 1181 N PHE 164 2905 3368 3164 -89 -125 - 361

ATOM 1182 CA PHE 164 -1.045 19.532 64.370 1.000 28.14

ANISOU 1182 CA PHE 164 3538 3957 3195 223 -163 - 3 0

ATOM 1183 C PHE 164 -1.360 20.003 65.787 1.000 26.67

ANISOU 1183 C PHE 164 2964 3937 3234 -473 -194 - 257

ATOM 1184 O PHE 164 -0.540 20.730 66.342 1.000 31.26

ANISOU 1184 O PHE 164 3119 4888 3869 -959 -260 - 519

ATOM 1185 CB PHE 164 0.347 18.881 64.396 1.000 27.86

ANISOU 1185 CB PHE 164 3423 3725 3436 76 -199 - 3 2

ATOM 1186 CG PHE 164 0.744 18.301 63.052 1.000 26.77

ANISOU 1186 CG PHE 164 2914 ^'3474 3785 -598 74 - 275

ATOM 1187 CDI . PHE 164 1.435 19.093 62.143 1.000 26.16

ANISOU 1187 CDI . PHE 164 2827 3836 3278 135 -615 7 1 1

ATOM 1188 CDI ! PHE 164 0.414 16.996 62.717 1.000 31.24

ANISOU 1188 CΌ: ! PHE 164 4365 2808 4698 349 -298 - 9 6

ATOM 1189 CE1 PHE 164 1.787 18.609 60.894 1.000 30.09

ANISOU 1189 CE1 PHE 164 3609 5052 2771 -148 -1030 641

ATOM 1190 CE2 PHE 164 0.786 16.501 61.475 1.000 38.25 ANISOU 1190 CE2 PHE 164 6659 4077 3797 -740 -1363 - 612

ATOM 1191 CZ PHE 164 1.494 17.298 60.588 1.000 32.74

ANISOU 1191 CZ PHE 164 3189 5078 4172 712 -944 - 385

ATOM 1192 N PRO 165 -2.469 19.609 66.379 1.000 30.62

ANISOU 1192 N PRO 165 3876 4009 3751 -1371 344 - 508

ATOM 1193 CA PRO 165 -2.670 19.813 67.809 1.000 33 .09

ANISOU 1193 CA PRO 165 3299 5764 3510 -190 80 2 3 6

ATOM 1194 C PRO 165 -1.459 19.408 68.638 1.000 36.32

ANISOU 1194 C PRO 165 3538 5745 4518 664 -191 - 234

ATOM 1195 0 PRO 165 -0.776 18.428 68.371 1.000 32 .94

ANISOU 1195 0 PRO 165 4268 4761 3487 220 501 3 8 7

ATOM 1196 CB PRO 165 -3.882 18.929 68.123 1.000 38.44

ANISOU 1196 CB PRO 165 3807 6924 3873 -765 271 82 7

ATOM 1197 CG PRO 165 -4.635 18.842 66.845 1.000 35.82

ANISOU 1197 CG PRO 165 2595 7020 3995 5 688 - 828

ATOM 1198 CD PRO 165 -3.690 19.130 65.710 1.000 33 .90

ANISOU 1198 CD PRO 165 3192 5919 3770 -1149 194 169

ATOM 1199 N LEU 178 7.727 7.453 68.180 1.000 64.52

ANISOU 1199 N LEU 178 12297 5376 6843 278 -218 3721

ATOM 1200 CA LEU 178 7.629 8.260 66.973 1.000 43 .31

ANISOU 1200 CA LEU 178 10557 2730 3168 -984 -2821 - 135

ATOM 1201 C LEU 178 6.159 8.539 66.662 1.000 47.36

ANISOU 1201 C LEU 178 9239 3530 5225 -2598 -1186 1204

ATOM 1202 O LEU 178 5.314 7.659 66.796 1.000 56.53

ANISOU 1202 O LEU 178 11777 5626 4076 -4835 1265 - 602

ATOM 1203 CB LEU 178 8.222 7.582 65.746 1.000 55.55

ANISOU 1203 CB LEU 178 11470 3734 5902 -1314 -1197 - 1822

ATOM 1204 CG LEU 178 9.662 7.092 65.774 1.000 62.34

ANISOU 1204 CG LEU 178 10812 5116 7760 -1971 194 - 443

ATOM 1205 CDI LEU 178 9.916 6.185 64.579 1.000 54.23

ANISOU 1205 CDI LEU 178 9626 4989 5988 1878 -3799 5 11

ATOM 1206 CD2 LEU 178 10.633 8.264 65.773 1.000 66.44

ANISOU 1206 CD2 LEU 178 11265 3454 10526 -1170 4090 - 516

ATOM 1207 N ARG 179 5.879 9.751 66.192 1.000 52.90

ANISOU 1207 N ARG 179 7853 3826 8421 102 1230 1031

ATOM 1208 CA ARG 179 4.495 10.033 65.807 1.000 51.26

ANISOU 1208 CA ARG 179 7235 4820 7421 -229 1890 - 383

ATOM 1209 C ARG 179 4.242 9.563 64.383 1.000 55.25

ANISOU 1209 C ARG 179 7178 6083 7731 -946 2260 -1134

ATOM 1210 O ARG 179 3.120 9.211 64.021 1.000 58.51

ANISOU 1210 O ARG 179 7036 7628 7565 -1820 3675 -2851

ATOM 1211 CB ARG 179 4.180 11.512 66.040 1.000 41.49

ANISOU 1211 CB ARG 179 6600 4448 4716 -155 1916 1137

ATOM 1212 CG ARG 179 3.293 11.700 67.277 1.000 43 .15

ANISOU 1212 CG ARG 179 6120 5908 4367 90 1338 53 0

ATOM 1213 CD ARG 179 1.888 12.059 66.833 1.000 47.63

ANISOU 1213 CD ARG 179 6180 7453 4463 195 860 - 531

ATOM 1214 NE ARG 179 1.459 13.367 67.269 1.000 52.00

ANISOU 1214 NE ARG 179 7384 7834 4539 1669 -1168 - 538

ATOM 1215 CZ ARG 179 1.322 14.470 66.556 1.000 64.81

ANISOU 1215 CZ ARG 179 10838 8000 5788 1457 -1107 6 3

ATOM 1216 NHl . ARG 179 1.637 14.518 65.268 1.000 59.74

ANISOU 1216 NHl . ARG 179 9535 8090 5074 3628 -2691 44 5

ATOM 1217 NH2 : RG 179 0.907 15.606 67.117 1.000 65.83

ANISOU 1217 NH2 ! ARG 179 10451 9083 5478 4171 -776 1200

ATOM 1218 N . MET 180 5.304 9.501 63.589 1.000 43 .96

ANISOU 1218 N MET 180 5383 3769 7550 705 852 -1245

ATOM 1219 CA MET 180 5.264 9.035 62.210 1.000 40.44

ANISOU 1219 CA MET 180 2356 5467 7543 -398 574 -1482

ATOM 1220 C MET 180 6.552 8.258 61.920 1.000 43.91

ANISOU 1220 C MET 180 2731 6220 7733 18 320 -2324 ATOM 1221 0 MET 180 7.629 8.679 62.327 1.000 39.46

ANISOU 1221 0 MET 180 2377 5064 7554 -395 906 - 912

ATOM 1222 CB MET 180 5.129 10.189 61.219 1.000 49.84

ANISOU 1222 CB MET 180 2749 7966 8223 -452 -1114 7 2

ATOM 1223 CG MET 180 5.339 9.818 59.757 1.000 62.58

ANISOU 1223 CG MET 180 7280 8911 7587 -2331 -3353 - 505

ATOM 1224 SD MET 180 4.622 11.015 58.608 1.000 74.24

ANISOU 1224 SD MET 180 7480 13510 7216 4918 -262 - 905

ATOM 1225 CE MET 180 4.501 10.037 57.110 1.000 79.59

ANISOU 1225 CE MET 180 6119 20000 4120 -1978 1874 - 912

ATOM 1226 N ALA 181 6.376 7.112 61.275 1.000 37.44

ANISOU 1226 N ALA 181 3523 5646 5055 -271 882 - 1132

ATOM 1227 CA ALA 181 7.407 6.140 60.986 1.000 37.40

ANISOU 1227 CA ALA 181 3980 3980 6250 -625 2048 4 6 1

ATOM 1228 C ALA 181 8.287 6.591 59.837 1.000 31.49

ANISOU 1228 C ALA 181 2975 3842 5149 -32 920 9 5 6

ATOM 1229 0 ALA 181 7.834 7.393 58.997 1.000 30.77

ANISOU 1229 0 ALA 181 2903 4021 4765 197 -98 1 64

ATOM 1230 CB ALA 181 6.727 4.817 60.620 1.000 42.66

ANISOU 1230 CB ALA 181 4105 4284 7820 -1023 1629 557

ATOM 1231 N PRO 182 9.541 6.137 59.840 1.000 24.52

ANISOU 1231 N PRO 182 2782 4237 2296 -240 -76 3 2 0

ATOM 1232 CA PRO 182 10.442 6.667 58.820 1.000 20.55

ANISOU 1232 CA PRO 182 2612 2870 2326 -335 -117 - 65

ATOM 1233 C PRO 182 9.958 6.402 57.408 1.000 19.31

ANISOU 1233 C PRO 182 2609 2491 2236 -391 48 - 8 6

ATOM 1234 0 PRO 182 9.448 5.326 57.080 1.000 21.68

ANISOU 1234 0 PRO 182 2991 2486 2759 -440 -340 - 55

ATOM 1235 CB PRO 182 11.768 5.939 59.047 1.000 24.98

ANISOU 1235 CB PRO 182 2589 3860 3042 -170 -286 153

ATOM 1236 CG PRO 182 11.681 5.351 60.393 1.000 28.42

ANISOU 1236 CG PRO 182 3352 3582 3863 656 321 1038

ATOM 1237 CD PRO 182 10.215 5.210 60.747 1.000 32.21

ANISOU 1237 CD PRO 182 3333 4905 4000 -826 -390 1785

ATOM 1238 N HIS 183 10.111 7.414 56.561 1.000 19.27

ANISOU 1238 N HIS 183 2131 2658 2533 -274 -204 17 6

ATOM 1239 CA HIS 183 9.757 7.306 55.144 1.000 18.01

ANISOU 1239 CA HIS 183 1882 2311 2652 -341 -455 34 6

ATOM 1240 C HIS 183 10.749 8.124 54.337 1.000 15.74

ANISOU 1240 C HIS 183 1964 1560 2456 -75 -352 12 8

ATOM 1241 0 HIS 183 11.355 9.061 54.868 1.000 18.14

ANISOU 12410 HIS 183 2297 2093 2504 -509 -127 - 135

ATOM 1242 CB HIS 183 8.338 7.781 54.835 1.000 18.66

ANISOU 1242 CB HIS 183 1970 2173 2945 -136 -243 3 71

ATOM 1243 CG HIS 183 8.089 9.120 55.447 1.000 26.67

ANISOU 1243 CG HIS 183 3100 2751 4281 262 222 - 306

ATOM 1244 NDl . HIS 183 7.884 9.362 56.800 1.000 35.36

ANISOU 1244 NDl . HIS 183 4432 4078 4926 -1190 1466 -1454

ATOM 1245 CD2 : HIS 183 8.051 10.311 54.821 1.000 33 .00

ANISOU 1245 CD2 : HIS 183 4117 2522 5898 1687 -677 - 173

ATOM 1246 CE1 . HIS 183 7.739 10.658 56.980 1.000 35.91

ANISOU 1246 CE1 . HIS 183 2611 4468 6565 -472 -625 - 2616

ATOM 1247 NE2 ! HIS 183 7.829 11.251 55.798 1.000 40.55

ANISOU 1247 NE2 ! HIS 183 4375 3417 7614 1821 -1013 -1590

ATOM 1248 N TYR 184 10.890 7.778 53.061 1.000 15.68

ANISOU 1248 N TYR 184 1973 1551 2434 -124 -470 1 07

ATOM 1249 CA TYR 184 11.605 8.685 52.152 1.000 14.81

ANISOU 1249 CA TYR 184 1798 1392 2438 147 -312 14 5

ATOM 1250 C TYR 184 10.572 9.239 51.169 1.000 14.53

ANISOU 1250 C TYR 184 1656 1449 2416 -70 -399 9 8

ATOM 1251 O TYR 184 9.468 8.728 51.045 1.000 15.83

SUBSTΓΓUTE SHEET (RULE 26) ANISOU 1251 0 TYR 184 1717 1383 2916 -103 -443 1 5 0

ATOM 1252 CB TYR 184 12.699 8.004 51.360 1.000 15.66

ANISOU 1252 CB TYR 184 1686 1323 2943 69 -366 - 168

ATOM 1253 CG TYR 184 12.383 6.785 50.562 1.000 14.85

ANISOU 1253 CG TYR 184 1743 1313 2586 109 -567 4 3

ATOM 1254 CDI TYR 184 12.200 5.540 51.185 1.000 15.49

ANISOU 1254 CDI TYR 184 1549 1315 3021 -29 -575 19 0

ATOM 1255 CD2 TYR 184 12.329 6.836 49.165 1.000 15.89

ANISOU 1255 CD2 TYR 184 1724 1763 2552 55 -27 - 64

ATOM 1256 CE1 TYR 184 11.962 4.396 50.442 1.000 15.61

ANISOU 1256 CE1 TYR 184 1695 1244 2992 229 -137 1 13

ATOM 1257 CE2 TYR 184 12.130 5.661 48.447 1.000 17.52

ANISOU 1257 CE2 TYR 184 2340 1776 2540 4 83 - 9 0

ATOM 1258 CZ TYR 184 11.915 4.449 49.083 1.000 16.96

ANISOU 1258 CZ TYR 184 1695 1736 3014 -156 -480 3 4

ATOM 1259 OH TYR 184 11.682 3.325 48.310 1.000 18.81

ANISOU 1259 OH TYR 184 2020 1775 3352 260 -277 - 312

ATOM 1260 N ASP 185 10.924 10.330 50.502 1.000 14.36

ANISOU 1260 N ASP 185 1518 1599 2338 87 -225 27 6

ATOM 1261 CA ASP 185 10.026 11.005 49.574 1.000 13 .88

ANISOU 1261 CA ASP 185 1875 1322 2078 141 -364 - 42

ATOM 1262 C ASP 185 10.240 10.490 48.152 1.000 12.57

ANISOU 1262 C ASP 185 1182 1385 2211 -160 -77 - 130

ATOM 1263 0 ASP 185 11.357 10.135 47.824 1.000 14.14

ANISOU 1263 0 ASP 185 1177 1637 2559 -135 146 140

ATOM 1264 CB ASP 185 10.294 12.521 49.580 1.000 14.97

ANISOU 1264 CB ASP 185 1879 1293 2517 121 -186 - 159

ATOM 1265 CG ASP 185 9.702 13.155 50.830 1.000 17.61

ANISOU 1265 CG ASP 185 2680 1659 2351 232 -13 - 172

ATOM 1266 ODl ASP 185 9.507 12.466 51.856 1.000 23.69

ANISOU 1266 ODl ASP 185 3553 3133 2314 443 -302 52 1

ATOM 1267 OD2 ASP 185 9.174 14.257 50.742 1.000 24.32

ANISOU 1267 OD2 ASP 185 4063 1730 3449 644 1140 - 1 6

ATOM 1268 N LEU 186 9.141 10.465 47.382 1.000 12.57

ANISOU 1268 N LEU 186 1271 1378 2126 -117 -117 - 117

ATOM 1269 CA LEU 186 9.169 10.091 45.986 1.000 12.92

ANISOU 1269 CA LEU 186 1533 1225 2150 -331 -84 - 175

ATOM 1270 C LEU 186 9.134 11.292 45.052 1.000 14.12

ANISOU 1270 C LEU 186 1730 1307 2330 -93 -165 5 5

ATOM 1271 0 LEU 186 8.971 11.173 43.849 1.000 20.12

ANISOU 1271 0 LEU 186 3721 1643 2280 -423 99 9 2

ATOM 1272 CB LEU 186 8.040 9.106 45.609 1.000 13.72

ANISOU 1272 CB LEU 186 1509 1310 2393 -270 -375 - 6

ATOM 1273 CG LEU 186 8.020 7.811 46.438 1.000 15.92

ANISOU 1273 CG LEU 186 1549 1141 3361 -145 -307 1 68

ATOM 1274 CDI . LEU 186 6.929 6.908 45.866 1.000 19.36

ANISOU 1274 CDI . LEU 186 1686 1845 3825 -700 -209 3 9 6

ATOM 1275 CD2 : LEU 186 9.369 7.115 46.341 1.000 18.32

ANISOU 1275 CD2 ! LEU 186 1689 1742 3528 200 -432 17 9

ATOM 1276 N SER 187 9.286 12.494 45.618 1.000 13 .60

ANISOU 1276 N SER 187 1326 1234 2608 -26 -95 1 3 7

ATOM 1277 CA SER 187 9.388 13.734 44.826 1.000 13.22

ANISOU 1277 CA SER 187 1489 1197 2338 -54 -68 2 9

ATOM 1278 C SER 187 10.736 13.853 44.134 1.000 12.79

ANISOU 1278 C SER 187 1482 1186 2192 -17 -114 - 9 0

ATOM 1279 0 SER 187 11.683 13.076 44.356 1.000 14.50

ANISOU 1279 0 SER 187 1532 1257 2720 76 -224 - 113

ATOM 1280 CB SER 187 9.201 14.915 45.811 1.000 12.87

ANISOU 1280 CB SER 187 1463 1282 2147 164 -154 9 8

ATOM 1281 OG SER 187 10.296 14.873 46.716 1.000 13 .22

ANISOU 1281 OG SER 187 1589 1420 2015 -34 -143 2 2 4 ATOM 1282 N MET 188 10.898 14.844 43.292 1.000 13 .44

ANISOU 1282 N MET 188 1552 1334 2221 -64 -34 - 2 6

ATOM 1283 CA MET 188 12.215 15.380 42.878 1.000 12 .11

ANISOU 1283 CA MET 188 1508 1261 1833 29 -60 - 61

ATOM 1284 C MET 188 12.853 16.022 44.104 1.000 12 .78

ANISOU 1284 C MET 188 1563 1156 2136 167 -311 - 42

ATOM 1285 0 MET 188 13.896 15.550 44.600 1.000 13 .40

ANISOU 1285 0 MET 188 1408 1390 2294 116 -264 - 2 6

ATOM 1286 CB MET 188 12.038 16.300 41.667 1.000 13 .66

ANISOU 1286 CB MET 188 1565 1501 2123 44 -161 2 07

ATOM 1287 CG MET 188 13.296 17.095 41.315 1.000 14.05

ANISOU 1287 CG MET 188 1697 1595 2046 66 150 13 3

ATOM 1288 SD MET 188 14.600 15.971 40.752 1.000 14.96

ANISOU 1288 SD MET 188 1565 1591 2529 109 -81 110

ATOM 1289 CE MET 188 16.005 17.102 40.686 1.000 17.74

ANISOU 1289 CE MET 188 1852 2032 2855 -242 505 12 1

ATOM 1290 N VAL 189 12.244 17.112 44.616 1.000 12 .62

ANISOU 1290 N VAL 189 1586 1203 2007 103 -147 - 134

ATOM 1291 CA VAL 189 12.565 17.671 45.918 1.000 12.60

ANISOU 1291 CA VAL 189 1412 1438 1937 -228 -11 - 44

ATOM 1292 C VAL 189 11.285 17.968 46.679 1.000 11.71

ANISOU 1292 C VAL 189 1328 1294 1825 -170 -171 - 49

ATOM 1293 0 VAL 189 10.227 18.099 46.050 1.000 12.56

ANISOU 1293 0 VAL 189 1446 1291 2036 21 -320 - 49

ATOM 1294 CB VAL 189 13.440 18.955 45.856 1.000 12.95

ANISOU 1294 CB VAL 189 1150 1517 2252 -174 -205 9 4

ATOM 1295 CGI VAL 189 14.778 18.637 45.167 1.000 15.54

ANISOU 1295 CGI VAL 189 1376 2094 2437 -140 161 9 1

ATOM 1296 CG2 VAL 189 12.730 20.056 45.082 1.000 15.00

ANISOU 1296 CG2 VAL 189 1763 1391 2547 -130 -483 8 1

ATOM 1297 N THR 190 11.425 18.067 47.984 1.000 12.18

ANISOU 1297 N THR 190 1445 1422 1760 -109 -130 1 0

ATOM 1298 CA THR 190 10.353 18.454 48.897 1.000 11.98

ANISOU 1298 CA THR 190 1292 1356 1903 -57 -221 - 151

ATOM 1299 C THR 190 10.879 19.630 49.710 1.000 12 .47

ANISOU 1299 C THR 190 1178 1436 2124 -32 -297 - 232

ATOM 1300 0 THR 190 11.959 19.523 50.320 1.000 15.06

ANISOU 1300 O THR 190 1424 1767 2531 46 -571 - 446

ATOM 1301 CB THR 190 9.913 17.297 49.808 1.000 13.16

ANISOU 1301 CB THR 190 1509 1605 1886 -168 80 - 121

ATOM 1302 OGl THR 190 9.481 16.201 48.993 1.000 14.47

ANISOU 1302 OGl THR 190 1693 1469 2334 -100 -25 - 194

ATOM 1303 CG2 THR 190 8.778 17.723 50.734 1.000 14.79

ANISOU 1303 CG2 THR 190 1696 1510 2415 73 258 - 89

ATOM 1304 N LEU 191 10.148 20.724 49.732 1.000 12.97

ANISOU 1304 N LEU 191 1329 1449 2149 23 -21 - 286

ATOM 1305 CA LEU 191 10.511 21.908 50.526 1.000 13 .75

ANISOU 1305 CA LEU 191 1543 1442 2238 78 -206 - 301

ATOM 1306 C LEU 191 9.603 21.964 51.763 1.000 14.47

ANISOU 1306 C LEU 191 1543 1689 2265 83 -179 - 412

ATOM 1307 O LEU 191 8.370 21.868 51.645 1.000 16.58

ANISOU 1307 O LEU 191 1517 2486 2297 219 -176 - 725

ATOM 1308 CB LEU 191 10.398 23.212 49.722 1.000 15 .37

ANISOU 1308 CB LEU 191 1717 1444 2680 58 -106 - 189

ATOM 1309 CG LEU 191 11.705 ^■23.578 48.973 1.000 16.10

^'ANISOU 1309 CG LEU 191 1747 1688 2680 -128 -113 - 135

ATOM 1310 CDI LEU 191 12.069 22.565 47.906 1.000 16.67

ANISOU 1310 CDI LEU 191 2034 2093 2209 -23 -64 1 9

ATOM 1311 CD2 LEU 191 11.570 24.959 48.350 1.000 18.53

ANISOU 1311 CD2 LEU 191 2297 1906 2837 -345 -437 148

ATOM 1312 N ILE 192 10.199 22.148 52.946 1.000 15.36 ANISOU 1312 N ILE 192 1479 2152 2204 -47 -165 - 164

ATOM 1313 CA ILE 192 9.417 22.162 54.194 1.000 15.13

ANISOU 1313 CA ILE 192 1456 2043 2251 -304 -173 - 280

ATOM 1314 C ILE 192 9.692 23.423 55.010 1.000 15 .58

ANISOU 1314 C ILE 192 1696 1973 2251 -199 -254 - 226

ATOM 1315 0 ILE 192 10.836 23.691 55.381 1.000 17 .20

ANISOU 1315 0 ILE 192 1856 2449 2229 -307 -341 - 574

ATOM 1316 CB ILE 192 9.722 20.920 55.040 1.000 17.03

ANISOU 1316 CB ILE 192 2246 1958 2266 -52 325 - 303

ATOM 1317 CGI ILE 192 9.454 19.596 54.317 1.000 19.80

ANISOU 1317 CGI ILE 192 3040 2010 2473 -71 128 - 382

ATOM 1318 CG2 ILE 192 8.995 20.967 56.403 1.000 18.14

ANISOU 1318 CG2 ILE 192 2278 2354 2262 229 290 - 258

ATOM 1319 CDI ILE 192 9.420 18.387 55.235 1.000 31.57

ANISOU 1319 CDI ILE 192 4658 2114 5222 -398 -1094 7 65

ATOM 1320 N GLN 193 8.625 24.172 55.249 1.000 17.04

ANISOU 1320 N GLN 193 2042 2185 2248 112 -388 - 301

ATOM 1321 CA GLN 193 8.680 25.291 56.201 1.000 17.70

ANISOU 1321 CA GLN 193 1737 2167 2824 -204 -186 - 559

ATOM 1322 C GLN 193 7.898 24.869 57.443 1.000 19.67

ANISOU 1322 C GLN 193 1882 2624 2969 -232 211 - 840

ATOM 1323 0 GLN 193 7.082 23.942 57.426 1.000 26.60

ANISOU 1323 0 GLN 193 2066 3843 4197 -965 -110 6 2

ATOM 1324 CB GLN 193 8.129 26.598 55.643 1.000 23 .74

ANISOU 1324 CB GLN 193 3070 2388 3561 500 -98 - 514

ATOM 1325 CG GLN 193 8.913 27.304 54.559 1.000 28.26

ANISOU 1325 CG GLN 193 4664 2384 3689 656 209 0

ATOM 1326 CD GLN 193 8.338 28.665 54.156 1.000 26.30

ANISOU 1326 CD GLN 193 2868 2943 4181 791 3 111

ATOM 1327 OEl GLN 193 7.193 28.695 53.688 1.000 45.31

ANISOU 1327 OEl GLN 193 2826 7147 7241 -51 -616 3173

ATOM 1328 NE2 GLN 193 9.080 29.748 54.345 1.000 30.44

ANISOU 1328 NE2 GLN 193 3609 2588 5368 418 1259 692

ATOM 1329 N GLN 194 8.241 25.259 58.645 1.000 22.04

ANISOU 1329 N GLN 194 2926 2758 2690 303 -368 - 83

ATOM 1330 CA GLN 194 7.569 24.793 59.847 1.000 22.68

ANISOU 1330 CA GLN 194 3144 2617 2855 82 -230 - 150

ATOM 1331 C GLN 194 7.275 26.054 60.663 1.000 22.19

ANISOU 1331 C GLN 194 2809 2768 2856 117 -396 - 320

ATOM 1332 0 GLN 194 7.889 27.100 60.418 1.000 25.26

ANISOU 1332 0 GLN 194 4041 2877 2679 -313 -21 - 411

ATOM 1333 CB GLN 194 8.467 23.943 60.739 1.000 29.21

ANISOU 1333 CB GLN 194 4493 2707 3899 477 -50 93 9

ATOM 1334 CG GLN 194 9.105 22.735 60.083 1.000 28.80

ANISOU 1334 CG GLN 194 3108 3530 4305 576 -121 494

ATOM 1335 CD GLN 194 10.296 22.332 60.962 1.000 31.97

ANISOU 1335 CD GLN 194 2961 5384 3800 824 359 1075

ATOM 1336 OEl . GLN 194 11.421 22.325 60.474 1.000 27.28

ANISOU 1336 OEl . GLN 194 2781 4189 3397 118 133 - 249

ATOM 1337 NE2 : GLN 194 9.998 22.100 62.232 1.000 29.82

ANISOU 1337 NE2 : GLN 194 3540 3958 3832 989 645 8 0 0

ATOM 1338 N THR 195 6.419 25.891 61.658 1.000 23 .30

ANISOU 1338 N THR 195 2407 3058 3387 -211 -235 - 720

ATOM 1339 CA THR 195 6.476 26.833 62.768 1.000 27.14

ANISOU 1339 CA THR 195 3459 3544 3308 25 -50 - 890

ATOM 1340 C THR 195 6.933 25.997 63.958 1.000 26.11

ANISOU 1340 C THR 195 3825 2829 3268 558 19 -1247

ATOM 1341 O THR 195 6.639 24.815 63.994 1.000 28.17

ANISOU 1341 O THR 195 2973 2916 4815 481 171 - 1030

ATOM 1342 CB THR 195 5.149 27.534 63.069 1.000 25.87

ANISOU 1342 CB THR 195 3428 2849 3551 -16 -592 - 1137

SUBSTΓΓUTE SHEET (RULE 26) ATOM 1343 OGl THR 195 4.111 26.550 63.196 1.000 25.45

ANISOU 1343 OGl THR 195 3427 3101 3141 -9 -117 - 750

ATOM 1344 CG2 THR 195 4.788 28.396 61.847 1.000 31.31

ANISOU 1344 CG2 THR 195 4965 2552 4380 274 -70 - 409

ATOM 1345 N PRO 196 7.604 26.587 64.923 1.000 30.84

ANISOU 1345 N PRO 196 5225 3191 3300 785 -517 - 1542

ATOM 1346 CA PRO 196 8.101 25.823 66.065 1.000 28.50

ANISOU 1346 CA PRO 196 3113 3700 4016 -279 -441 - 646

ATOM 1347 C PRO 196 7.018 25.534 67.096 1.000 28.97

ANISOU 1347 C PRO 196 3581 3326 4102 42 113 - 1381

ATOM 1348 0 PRO 196 6.002 26.229 67.192 1.000 32.32

ANISOU 1348 0 PRO 196 4146 4649 3485 901 -180 - 1658

ATOM 1349 CB PRO 196 9.094 26.816 66.694 1.000 29.72

ANISOU 1349 CB PRO 196 3888 3292 4111 -285 -353 - 1072

ATOM 1350 CG PRO 196 8.533 28.174 66.364 1.000 34.87

ANISOU 1350 CG PRO 196 6285 3575 3390 421 -1326 -1332

ATOM 1351 CD PRO 196 7.897 28.035 65.012 1.000 33.20

ANISOU 1351 CD PRO 196 6407 3606 2600 -598 -494 - 1031

ATOM 1352 N CYS 197 7.289 24.533 67.919 1.000 26.96

ANISOU 1352 N CYS 197 2739 4038 3465 -113 85 - 1227

ATOM 1353 CA CYS 197 6.519 24.289 69.126 1.000 31.73

ANISOU 1353 CA CYS 197 3979 4543 3533 -39 721 -1726

ATOM 1354 C CYS 197 6.803 25.412 70.124 1.000 35.58

ANISOU 1354 C CYS 197 4213 4819 4486 -480 1126 -2282

ATOM 1355 0 CYS 197 7.917 25.939 70.175 1.000 31.34

ANISOU 1355 0 CYS 197 3817 4845 3246 36 -383 - 992

ATOM 1356 CB CYS 197 6.940 22.962 69.767 1.000 35.79

ANISOU 1356 CB CYS 197 5913 4705 2980 284 1566 -1423

ATOM 1357 SG CYS 197 6.553 21.535 68.741 1.000 28.53

ANISOU 1357 SG CYS 197 3605 4224 3009 50 -5 - 452

ATOM 1358 N ALA 198 5.771 25.791 70.866 1.000 37.27

ANISOU 1358 N ALA 198 5038 4984 4139 -421 1647 -2070

ATOM 1359 CA ALA 198 5.983 26.811 71.888 1.000 35.91

ANISOU 1359 CA ALA 198 6273 4144 3230 910 522 -1230

ATOM 1360 C ALA 198 6.993 26.328 72.921 1.000 44.30

ANISOU 1360 C ALA 198 5998 6138 4696 -193 -199 3 3

ATOM 1361 0 ALA 198 7.759 27.127 73.457 1.000 42.85

ANISOU 1361 0 ALA 198 5209 6328 4742 7 490 - 555

ATOM 1362 CB ALA 198 4.671 27.231 72.532 1.000 41.70

ANISOU 1362 CB ALA 198 7588 5697 2557 2355 1068 - 721

ATOM 1363 N ASN 199 7.036 25.036 73.225 1.000 34.93

ANISOU 1363 N ASN 199 4027 5975 3270 805 167 - 621

ATOM 1364 CA ASN 199 7.969 24.578 74.264 1.000 33 .58

ANISOU 1364 CA ASN 199 3643 6167 2950 -670 -265 - 808

ATOM 1365 C ASN 199 9.352 24.262 73.718 1.000 31.53

ANISOU 1365 C ASN 199 4077 5048 2853 384 -420 - 855

ATOM 1366 0 ASN 199 10.153 23.667 74.467 1.000 36.33

ANISOU 1366 0 ASN 199 4223 5624 3957 -403 -1305 - 126

ATOM 1367 CB ASN 199 7.441 23.308 74.929 1.000 36.38

ANISOU 1367 CB ASN 199 4533 5029 4262 859 584 - 522

ATOM 1368 CG ASN 199 7.198 22.180 73.952 1.000 31.28

ANISOU 1368 CG ASN 199 4030 4863 2993 882 202 17 8

ATOM 1369 ODl ASN 199 7.743 22.151 72.853 1.000 37.62

ANISOU 1369 ODl ASN 199 4693 6272 3330 122 728 - 5 6

ATOM 1370 ND2 ASN 199 6.393 21.190 74.314 1.000 36.42

ANISOU 1370 ND2 ASN 199 3508 6251 4078 -13 1132 - 958

ATOM 1371 N GLY 200 9.616 24.569 72.449 1.000 30.93

ANISOU 1371 N GLY 200 4342 4232 3179 436 144 - 692

ATOM 1372 CA GLY 200 10.920 24.304 71.866 1.000 35.26

ANISOU 1372 CA GLY 200 4430 4905 4060 -317 480 -2400

ATOM 1373 C GLY 200 11.184 22.886 71.429 1.000 36.83 ANISOL- 1373 C GLY 200 4683 4375 4936 -360 1601 - 1460

ATOM 1374 0 GLY 200 12.257 22.566 70.897 1.000 32 .71

ANISOU 1374 0 GLY 200 3921 4072 4436 -377 752 - 1400

ATOM 1375 N PHE 201 10.264 21.939 71.588 1.000 28 .66

ANISOU 1375 N PHE 201 3813 4229 2847 145 463 - 326

ATOM 1376 CA PHE 201 10.491 20.575 71.106 1.000 27.55

ANISOU 1376 CA PHE 201 3190 4337 2943 -233 219 - 672

ATOM 1377 C PHE 201 10.752 20.553 69.600 1.000 24.89

ANISOU 1377 C PHE 201 2943 3682 2832 190 -268 - 379

ATOM 1378 0 PHE 201 9.994 21.255 68.910 1.000 28 .22

ANISOU 1378 0 PHE 201 3583 3184 3957 10 -421 277

ATOM 1379 CB PHE 201 9.250 19.729 71.413 1.000 30.46

ANISOU 1379 CB PHE 201 3153 4862 3560 -371 -40 - 73

ATOM 1380 CG PHE 201 9.425 18.262 71.027 1.000 34.89

ANISOU 1380 CG PHE 201 4015 4609 4632 -772 162 8 9

ATOM 1381 CDI PHE 201 10.395 17.472 71.605 1.000 31.18

ANISOU 1381 CDI PHE 201 3436 4103 4310 -875 -93 - 1105

ATOM 1382 CD2 PHE 201 8.613 17.681 70.078 1.000 28 .84

ANISOU 1382 CD2 PHE 201 2979 4019 3960 329 612 - 107

ATOM 1383 CE1 PHE 201 10.564 16.160 71.240 1.000 37 .73

ANISOU 1383 CE1 PHE 201 6489 3608 4239 -1078 -1475 - 500

ATOM 1384 CE2 PHE 201 8.761 16.363 69.679 1.000 31.78

ANISOU 1384 CE2 PHE 201 4327 3911 3838 652 250 119

ATOM 1385 CZ PHE 201 9.755 15.606 70.265 1.000 29.78

ANISOU 1385 CZ PHE 201 3705 3397 4211 6 -638 - 849

ATOM 1386 N VAL 202 11.706 19.751 69.144 1.000 23 .51

ANISOU 1386 N VAL 202 2671 3392 2868 -292 -1 - 578

ATOM 1387 CA VAL 202 11.969 19.626 67.706 1.000 26.37

ANISOU 1387 CA VAL 202 3025 4050 2946 -667 57 - 724

ATOM 1388 C VAL 202 11.423 18.283 67.198 1.000 22 .75

ANISOU 1388 C VAL 202 2729 3348 2567 96 -120 - 435

ATOM 1389 0 VAL 202 11.880 17.190 67.541 1.000 28.71

ANISOU 1389 0 VAL 202 3249 3799 3859 119 31 66 1

ATOM 1390 CB VAL 202 13.476 19.721 67.415 1.000 24.99

ANISOU 1390 CB VAL 202 3060 3427 3008 -278 283 1 52

ATOM 1391 CGI VAL 202 13.715 19.464 65.938 1.000 27.70

ANISOU 1391 CGI VAL 202 4642 2577 3307 87 1014 - 3

ATOM 1392 CG2 VAL 202 14.050 21.071 67.823 1.000 26.80

ANISOU 1392 CG2 VAL 202 2826 3868 3487 -490 474 - 398

ATOM 1393 N SER 203 10.405 18.402 66.333 1.000 24.10

ANISOU 1393 N SER 203 2194 3607 3356 -31 -179 - 528

ATOM 1394 CA SER 203 9.634 17.231 65.940 1.000 23.70

ANISOU 1394 CA SER 203 2373 3584 3046 -290 308 - 533

ATOM 1395 C SER 203 10.168 16.511 64.710 1.000 21.28

ANISOU 1395 C SER 203 2173 3041 2871 46 227 - 42

ATOM 1396 0 SER 203 10.159 15.285 64.640 1.000 27.60

ANISOU 1396 0 SER 203 4105 3097 3284 -482 1010 - 249

ATOM 1397 CB SER 203 8.148 17.571 65.685 1.000 29.06

ANISOU 1397 CB SER 203 2251 3790 5001 -180 203 -2064

ATOM 1398 OG SER 203 7.584 18.175 66.843 1.000 32.55

ANISOU 1398 OG SER 203 3840 4298 4231 920 1099 - 382

ATOM 1399 N LEU 204 10.688 17.233 63.724 1.000 22 .46

ANISOU 1399 N LEU 204 2476 3013 3043 79 450 - 4 6

ATOM 1400 CA LEU 204 11.166 16.530 62.544 1.000 20.26

ANISOU 1400 CA LEU 204 2200 2831 2667 45 -18 - 15

ATOM 1401 C LEU 204 12.595 16.038 62.747 1.000 18.83

ANISOU 1401 C LEU 204 2151 2528 2477 -75 60 - 1

ATOM 1402 O LEU 204 13.443 16.783 63.251 1.000 20.47

ANISOU 1402 O LEU 204 2333 2386 3059 -303 -195 4 04

ATOM 1403 CB LEU 204 11.103 17.486 61.362 1.000 21.42

ANISOU 1403 CB LEU 204 2718 2548 2871 311 -16 - 8 ATOM 1404 CG LEU 204 9.769 18.188 61.079 1.000 33 .57

ANISOU 1404 CG LEU 204 2820 4319 5617 177 -1316 1172

ATOM 1405 CDI LEU 204 9.797 18.747 59.660 1.000 36.19

ANISOU 1405 CDI LEU 204 4402 3807 5540 1276 -1167 9 8 7

ATOM 1406 CD2 LEU 204 8.581 17.234 61.219 1.000 37 .76

ANISOU 1406 CD2 LEU 204 3058 5328 5960 -526 -1896 6 8 6

ATOM 1407 N GLN 205 12.864 14.836 62.284 1.000 20.33

ANISOU 1407 N GLN 205 2518 2644 2563 104 -31 - 129

ATOM 1408 CA GLN 205 14.209 14.247 62.335 1.000 18.88

ANISOU 1408 CA GLN 205 2522 2225 2425 -6 -181 3 6

ATOM 1409 C GLN 205 14.512 13.504 61.036 1.000 18.19

ANISOU 1409 C GLN 205 1986 2383 2543 -143 -188 - 8 0

ATOM 1410 O GLN 205 13.577 13.033 60.408 1.000 19.87

ANISOU 1410 O GLN 205 1974 3063 2514 -125 -212 - 237

ATOM 1411 CB GLN 205 14.296 13.267 63.493 1.000 24.25

ANISOU 1411 CB GLN 205 3948 2716 2548 202 -343 2 9 6

ATOM 1412 CG GLN 205 14.164 13.948 64.856 1.000 30.64

ANISOU 1412 CG GLN 205 4099 5159 2382 850 -327 - 8 9

ATOM 1413 CD GLN 205 14.744 13.078 65.948 1.000 28.28

ANISOU 1413 CD GLN 205 4473 3633 2640 -161 -1015 - 390

ATOM 1414 OEl GLN 205 14.307 11.921 66.041 1.000 37.69

ANISOU 1414 OEl GLN 205 5733 5073 3515 -2145 -699 4 7 8

ATOM 1415 NE2 GLN 205 15.710 13.553 66.711 1.000 40.53

ANISOU 1415 NE2 GLN 205 6798 4417 4185 -1341 -2865 3 23

ATOM 1416 N ALA 206 15.752 13.471 60.576 1.000 18.52

ANISOU 1416 N ALA 206 2070 2199 2769 -240 -13 4

ATOM 1417 CA ALA 206 16.152 12.700 59.405 1.000 18.42

ANISOU 1417 CA ALA 206 2074 2351 2575 -100 -158 2 3

ATOM 1418 C ALA 206 17.343 11.802 59.738 1.000 17.41

ANISOU 1418 C ALA 206 2107 2158 2350 -185 -254 - 17

ATOM 1419 O ALA 206 18.123 12.203 60.613 1.000 20.67

ANISOU 1419 O ALA 206 2469 2410 2973 -48 -711 - 396

ATOM 1420 CB ALA 206 16.637 13.599 58.270 1.000 18.77

ANISOU 1420 CB ALA 206 2119 2310 2703 156 -65 147

ATOM 1421 N GLU 207 17.492 10.764 58.931 1.000 18.09

ANISOU 1421 N GLU 207 2092 2101 2680 -249 -496 - 162

ATOM 1422 CA GLU 207 18.710 9.944 58.966 1.000 19.48

ANISOU 1422 CA GLU 207 2210 2091 3100 -73 -432 - 44

ATOM 1423 C GLU 207 19.851 10.730 58.320 1.000 19.98

ANISOU 1423 C GLU 207 2018 2233 3342 220 -560 544

ATOM 1424 O GLU 207 19.732 11.068 57.143 1.000 20.33

ANISOU 1424 O GLU 207 2000 2753 2970 5 -471 8 9

ATOM 1425 CB GLU 207 18.566 8.623 58.214 1.000 24.03

ANISOU 1425 CB GLU 207 3401 1784 3946 316 -1226 6 1

ATOM 1426 CG GLU 207 19.757 7.674 58.295 1.000 24.35

ANISOU 1426 CG GLU 207 3223 1907 4121 354 93 467

ATOM 1427 CD GLU 207 20.730 7.791 57.129 1.000 31.69

ANISOU 1427 CD GLU 207 2729 5178 4134 -1218 -175 122

ATOM 1428 OEl . GLU 207 20.376 7.611 55.943 1.000 26.97

ANISOU 1428 OEl . GLU 207 2849 3404 3993 31 -256 3 09

ATOM 1429 OE2 ! GLU 207 21.908 8.121 57.407 1.000 30.70

ANISOU 1429 OE2 : GLU 207 2484 3416 5764 -233 -342 - 1168

ATOM 1430 N VAL 208 20.919 10.936 59.078 1.000 18.53

ANISOU 1430 N VAL 208 2020 2112 2907 130 -362 3 2 0

ATOM 1431 CA VAL 208 22.150 11.547 58.541 1.000 19.53

ANISOU 1431 CA VAL 208 2044 2238 3137 39 -476 63 0

ATOM 1432 C VAL 208 23.341 10.755 59.088 1.000 21.95

ANISOU 1432 C VAL 208 2040 2792 3507 225 -461 7 97

ATOM 1433 O VAL 208 23.460 10.663 60.314 1.000 23 .82

ANISOU 1433 O VAL 208 2262 3240 3547 -40 -858 82 5

ATOM 1434 CB VAL 208 22.271 13.027 58.905 1.000 19.72 AMISOL- 1434 CB VAL 208 1918 2429 3145 -47 -308 3 11

ATOM 1435 CGI VAL 208 23.524 13.626 58.281 1.000 23 .14

ANISOL- 1435 CGI VAL 208 2524 2374 3895 -202 284 3 4 9

ATOM 1436 CG2 VAL 208 21.030 13.812 58.469 1.000 19.47

ANISOU 1436 CG2 VAL 208 2462 2279 2658 232 -667 - 8 7

ATOM 1437 N GLY 209 24.180 10.169 58.246 1.000 23 .88

ANISOU 1437 N GLY 209 2500 2449 4123 465 -711 3 6

ATOM 1438 CA GLY 209 25.306 9.374 58.773 1.000 26.42

ANISOU 1438 CA GLY 209 1987 3599 4450'. 460 -487 5 1 6

ATOM 1439 C GLY 209 24.905 8.250 59.695 1.000 30.01

ANISOU 1439 C GLY 209 3469 3240 4693 238 -1422 73 2

ATOM 1440 0 GLY 209 25.609 7.835 60.629 1.000 31.45

ANISOU 1440 0 GLY 209 4053 4458 3438 1225 -897 8 3

ATOM 1441 N GLY 210 23.691 7.702 59.523 1.000 26.64

ANISOU 1441 N GLY 210 3165 3214 3744 259 -86 3 5 0

ATOM 1442 CA GLY 210 23.263 6.585 60.360 1.000 29.78

ANISOU 1442 CA GLY 210 4603 3091 3619 -55 -997 5 8 4

ATOM 1443 C GLY 210 22.622 6.993 61.663 1.000 38.28

ANISOU 1443 C GLY 210 5827 4212 4507 -2536 732 5 0

ATOM 1444 0 GLY 210 22.160 6.187 62.481 1.000 41.45

ANISOU 1444 0 GLY 210 4152 6516 5082 -1874 -567 2346

ATOM 1445 N ALA 211 22.512 8.274 61.976 1.000 32.81

ANISOU 1445 N ALA 211 4803 4625 3037 1372 -1177 63 2

ATOM 1446 CA ALA 211 21.828 8.603 63.235 1.000 35.62

ANISOU 1446 CA ALA 211 3993 5958 3584 1061 -610 9 7 0

ATOM 1447 C ALA 211 20.663 9.543 62.940 1.000 31.43

ANISOU 1447 C ALA 211 3508 4737 3699 302 69 1854

ATOM 1448 0 ALA 211 20.652 10.097 61.858 1.000 28.28

ANISOU 1448 0 ALA 211 3661 4062 3020 -571 -551 1010

ATOM 1449 CB ALA 211 22.812 9.278 64.170 1.000 41.36

ANISOU 1449 CB ALA 211 3644 8904 3169 1372 -18 - 791

ATOM 1450 N PHE 212 19.682 9.676 63.825 1.000 36.68

ANISOU 1450 N PHE 212 5211 4237 4489 1166 1265 2171

ATOM 1451 CA PHE 212 18.620 10.654 63.641 1.000 28.82

ANISOU 1451 CA PHE 212 4490 3167 3293 263 504 1037

ATOM 1452 C PHE 212 19.100 12.023 64.124 1.000 34.72

ANISOU 1452 C PHE 212 6746 3760 2685 -248 -539 77 6

ATOM 1453 0 PHE 212 19.667 12.191 65.210 1.000 39.12

ANISOU 1453 0 PHE 212 6144 5384 3335 -549 -1129 1220

ATOM 1454 CB PHE 212 17.358 10.219 64.388 1.000 45.35

ANISOU 1454 CB PHE 212 6376 2569 8288 1348 3748 2314

ATOM 1455 N THR 213 18.906 13.008 63.271 1.000 26.30

ANISOU 1455 N THR 213 4134 2738 3122 662 -581 1 0 0

ATOM 1456 CA THR 213 19.424 14.359 63.433 1.000 25.08

ANISOU 1456 CA THR 213 3587 2852 3089 767 -810 - 323

ATOM 1457 C THR 213 18.190 15.283 63.400 1.000 23 .81

ANISOU 1457 C THR 213 2835 2652 3560 215 -855 - 643

ATOM 1458 0 THR 213 17.329 15.137 62.517 1.000 21.40

ANISOU 1458 0 THR 213 2640 2269 3223 -328 -580 - 179

ATOM 1459 CB THR 213 20.398 14.759 62.308 1.000 27.60

ANISOU 1459 CB THR 213 3155 3220 4113 189 -356 - 798

ATOM 1460 OGl THR 213 21.673 14.084 62.374 1.000 32 .00

ANISOU 1460 OGl THR 213 3582 4220 4356 746 -410 52 0

ATOM 1461 CG2 THR 213 20.735 16.254 62.355 1.000 29.45

ANISOU 1461 CG2 THR 213 4422 3320 3448 -106 -1265 - 204

ATOM 1462 N ASP 214 18.119 16.177 64.371 1.000 21.05

ANISOU 1462 N ASP 214 2790 2236 2972 -82 -380 - 142

ATOM 1463 CA ASP 214 17.001 17.110 64.462 1.000 20.61

ANISOU 1463 CA ASP 214 2742 2095 2993 -117 -898 - 379

ATOM 1464 C ASP 214 16.994 18.030 63.226 1.000 20.58

ANISOU 1464 C ASP 214 2373 2525 2923 182 -169 - 237 ATOM 1465 0 ASP 214 18.018 18.430 62.678 1.000 23 .02

ANISOU 1465 0 ASP 214 2461 2883 3404 -167 -52 - 572

ATOM 1466 CB ASP 214 17.205 18.058 65.637 1.000 23 .54

ANISOU 1466 CB ASP 214 3304 2607 3032 -92 -748 - 668

ATOM 1467 CG ASP 214 16.915 17.506 67.004 1.000 24.93

ANISOL- 1467 CG ASP 214 3545 2850 3079 450 -417 - 614

ATOM 1468 ODl ASP 214 16.357 16.395 67.113 1.000 29.17

ANISOU 1468 ODl ASP 214 4134 3070 3878 202 -705 2 6 2

ATOM 1469 OD2 ASP 214 17.276 18.191 67.990 1.000 34.38

ANISOL- 1469 OD2 ASP 214 6917 3040 3107 1017 -1413 - 736

ATOM 1470 N LEU 215 15.802 18.452 62.859 1.000 20.74

ANISOU 1470 N LEU 215 2426 2372 3081 86 -60 3 06

ATOM 1471 CA LEU 215 15.568 19.401 61.796 1.000 20.55

ANISOU 1471 CA LEU 215 2895 2013 2899 -202 -178 141

ATOM 1472 C LEU 215 14.724 20.552 62.332 1.000 19.02

ANISOU 1472 C LEU 215 2482 2240 2504 -142 -34 3 2 1

ATOM 1473 0 LEU 215 13.510 20.613 62.142 1.000 22 .39

ANISOU 1473 0 LEU 215 2635 2483 3389 -160 -475 5 7 3

ATOM 1474 CB LEU 215 14.826 18.722 60.650 1.000 22 .04

ANISOU 1474 CB LEU 215 2778 2510 3086 -140 -261 - 6 5

ATOM 1475 CG LEU 215 15.598 17.502 60.128 1.000 25.25

ANISOU 1475 CG LEU 215 3680 2829 3085 85 -166 - 402

ATOM 1476 CDI LEU 215 14.680 16.736 59.174 1.000 27.12

ANISOU 1476 CDI LEU 215 4886 2934 2482 419 -1128 - 65

ATOM 1477 CD2 LEU 215 16.881 18.046 59.510 1.000 30.76

ANISOU 1477 CD2 LEU 215 3434 3089 5165 1003 524 5 61

ATOM 1478 N PRO 216 15.383 21.433 63.078 1.000 19.68

ANISOU 1478 N PRO 216 2407 2191 2879 -157 148 1 03

ATOM 1479 CA PRO 216 14.665 22.534 63.708 1.000 22.42

ANISOU 1479 CA PRO 216 2869 2812 2836 272 10 - 228

ATOM 1480 C PRO 216 14.201 23.576 62.698 1.000 25.36

ANISOU 1480 C PRO 216 4118 2433 3086 566 -131 - 315

ATOM 1481 0 PRO 216 14.700 23.759 61.586 1.000 24.67

ANISOU 1481 0 PRO 216 3682 2406 3284 187 -176 - 2 6

ATOM 1482 CB PRO 216 15.693 23.092 64.676 1.000 23 .88

ANISOU 1482 CB PRO 216 3108 3049 2917 -216 116 -318

ATOM 1483 CG PRO 216 17.033 22.701 64.146 1.000 28.31

ANISOU 1483 CG PRO 216 2994 2996 4766 -88 -117 - 1454

ATOM 1484 CD PRO 216 16.807 21.405 63.436 1.000 24.55

ANISOU 1484 CD PRO 216 2353 1777 5197 -436 -83 - 348

ATOM 1485 N TYR 217 13.154 24.287 63.102 1.000 24.13

ANISOU 1485 N TYR 217 3237 2704 3229 244 -631 - 511

ATOM 1486 CA TYR 217 12.676 25.510 62.462 1.000 26.08

ANISOU 1486 CA TYR 217 2514 2899 4498 104 -592 3 9

ATOM 1487 C TYR 217 13.824 26.516 62.369 1.000 25.24

ANISOU 1487 C TYR 217 3049 2948 3592 -257 -506 - 538

ATOM 1488 0 TYR 217 14.570 26.675 63.340 1.000 31.78

ANISOU 1488 0 TYR 217 4114 2863 5096 -352 -2151 5 64

ATOM 1489 CB TYR 217 11.559 26.103 63.315 1.000 25.97

ANISOU 1489 CB TYR 217 2747 2773 4346 86 -615 - 167

ATOM 1490 CG TYR 217 11.189 27.543 63.125 1.000 31.64

ANISOU 1490 CG TYR 217 3080 2803 6139 338 -1473 - 644

ATOM 1491 CDI . TYR 217 10.430 27.928 62.022 1.000 27 .85

ANISOU 1491 CDI . TYR 217 2238 3029 5314 511 -175 9 3

ATOM 1492 CD2 : TYR 217 11.512 28.522 64.069 1.000 38.49

ANISOU 1492 CD2 ! TYR 217 4721 2813 7093 -686 -1682 - 749

ATOM 1493 CE1 . TYR 217 10.021 29.219 61.772 1.000 26.53

ANISOU 1493 CE1 . TYR 217 1908 2675 5496 -41 107 6 9

ATOM 1494 CE2 > TYR 217 11.113 29.835 63.827 1.000 42.90

ANISOU 1494 CE; > TYR 217 7112 2347 6842 -1415 -1949 - 218

ATOM 1495 CZ TYR 217 10.373 30.168 62.712 1.000 34.93 ANISOU 1495 CZ TYR 217 4042 2747 6483 -1462 -545 1 6 6

ATOM 1496 OH TYR 217 9.996 31.486 62.473 1.000 36.41

ANISOU 1496 OH TYR 217 5499 2895 5439 -753 -250 - 289

ATOM 1497 N ARG 218 14.022 27.110 61.218 1.000 25 .58

ANISOU 1497 N ARG 218 3461 2406 3852 -227 -533 - 476

ATOM 1498 CA ARG 218 14.923 28.243 61.049 1.000 29 .26

ANISOU 1498 CA ARG 218 3630 3270 4219 -784 -1349 2 68

ATOM 1499 C ARG 218 14.113 29.336 60.366 1.000 24.81

ANISOU 1499 C ARG 218 4063 2949 2415 -382 -228 - 5 6

ATOM 1500 0 ARG 218 13.746 29.174 59.212 1.000 29 .56

ANISOU 1500 0 ARG 218 6298 2267 2666 -890 -994 1 6 5

ATOM 1501 CB ARG 218 16.162 27.823 60.256 1.000 35 .90

ANISOU 1501 CB ARG 218 3223 3685 6732 -624 -703 8 9 6

ATOM 1502 CG ARG 218 17.369 28.665 60.661 1.000 51.38

ANISOU 1502 CG ARG 218 4740 6768 8015 -3031 430 - 183

ATOM 1503 CD ARG 218 18.539 28.606 59.701 1.000 38.84

ANISOU 1503 CD ARG 218 4968 6308 3482 -3596 -1165 1647

ATOM 1504 NE ARG 218 19.343 27.395 59.905 1.000 45 .09

ANISOU 1504 NE ARG 218 4655 7495 4982 -2325 -962 - 94

ATOM 1505 CZ ARG 218 20.272 27.208 58.959 1.000 55 .53

ANISOU 1505 CZ ARG 218 5299 11458 4340 -2701 -1188 - 194 I

ATOM 1506 NHl ARG 218 20.289 28.158 58.031 1.000 60.85

ANISOU 1506 NHl ARG 218 2399 16648 4071 -1943 -1333 548

ATOM 1507 NH2 ARG 218 21.060 26.165 59.001 1.000 60.37

ANISOU 1507 NH2 ARG 218 8580 10111 4247 -2152 639 -4241

ATOM 1508 N PRO 219 13.871 30.496 60.972 1.000 25.89

ANISOU 1508 N PRO 219 2625 4126 3086 35 296 - 1014

ATOM 1509 CA PRO 219 13.065 31.548 60.326 1.000 28 .10

ANISOU 1509 CA PRO 219 2828 3120 4730 -410 379 - 696

ATOM 1510 C PRO 219 13.636 31.959 58.981 1.000 28.43

ANISOU 1510 C PRO 219 3141 3010 4653 -190 116 - 328

ATOM 1511 O PRO 219 12.904 32.393 58.081 1.000 34.17

ANISOU 1511 O PRO 219 4734 3500 4750 302 -798 - 893

ATOM 1512 CB PRO 219 13.115 32.717 61.316 1.000 39 .70

ANISOU 1512 CB PRO 219 5621 3612 5852 -500 1615 - 1527

ATOM 1513 CG PRO 219 13.368 32.033 62.628 1.000 42 .38

ANISOU 1513 CG PRO 219 6139 5277 4688 -257 2084 - 2086

ATOM 1514 CD PRO 219 14.370 30.943 62.289 1.000 32.77

ANISOU 1514 CD PRO 219 3901 5719 2831 -602 828 -1603

ATOM 1515 N ASP 220 14.950 31.824 58.811 1.000 25.65

ANISOU 1515 N ASP 220 3328 1582 4837 -276 801 - 878

ATOM 1516 CA ASP 220 15.590 32.280 57.587 1.000 26.45

ANISOU 1516 CA ASP 220 3594 2115 4341 -782 248 - 861

ATOM 1517 C ASP 220 15.781 31.305 56.451 1.000 28.46

ANISOU 1517 C ASP 220 3549 1843 5423 -111 1638 - 943

ATOM 1518 O ASP 220 16.432 31.620 55.433 1.000 25.80

ANISOU 1518 O ASP 220 3249 2021 4533 -140 623 - 412

ATOM 1519 CB ASP 220 16.911 32.962 57.998 1.000 33 .76

ANISOU 1519 CB ASP 220 2351 3539 6938 -445 1187 - 1724

ATOM 1520 CG ASP 220 17.882 31.913 58.502 1.000 42 .36

ANISOU 1520 CG ASP 220 2653 3531 9912 -812 230 - 957

ATOM 1521 ODl . ASP 220 17.484 31.170 59.423 1.000 37.00

ANISOU 1521 ODl . ASP 220 3154 4148 6757 -104 -410 - 2001

ATOM 1522 OD_ > ASP 220 18.981 31.787 57.957 1.000 37.34

ANISOU 1522 OD- ^> ASP 220 2520 4700 6969 93 -824 - 1266

ATOM 1523 N ALA 221 15.292 30.072 56.537 1.000 24.79

ANISOU 1523 N ALA 221 4148 1872 3398 -252 671 - 659

ATOM 1524 CA ALA 221 15.695 29.016 55.596 1.000 19.17

ANISOU 1524 CA ALA 221 2165 1868 3251 -52 -92 - 610

ATOM 1525 C ALA 221 14.551 27.996 55.479 1.000 18.60

ANISOU 1525 C ALA 221 1920 2238 2908 -82 -207 - 362 ATOM 1526 0 ALA 221 13.763 27.852 56.415 1.000 26.47

ANISOU 1526 0 ALA 221 4127 2641 3289 -1307 894 - 904

ATOM 1527 CB ALA 221 16.939 28.316 56.104 1.000 19.36

ANISOU 1527 CB ALA 221 2054 2333 2969 -537 -316 6 6

ATOM 1528 N VAL 222 14.490 27.385 54.313 1.000 17.35

ANISOU 1528 N VAL 222 2089 1841 2661 -101 -323 - 154

ATOM 1529 CA VAL 222 13.556 26.276 54.083 1.000 17 .45

ANISOU 1529 CA VAL 222 1620 2004 3004 -66 -417 1 9

ATOM 1530 C VAL 222 14.333 24.965 54.077 1.000 15.69

ANISOU 1530 C VAL 222 1616 1876 2471 -269 -349 - 324

ATOM 1531 0 VAL 222 15.512 24.934 53.716 1.000 17.84

ANISOU 1531 0 VAL 222 1658 1730 3390 -108 -194 4 8

ATOM 1532 CB VAL 222 12.822 26.433 52.747 1.000 19.60

ANISOU 1532 CB VAL 222 2267 2202 2979 91 -666 - 304

ATOM 1533 CGI VAL 222 13.781 26.363 51.563 1.000 21.96

ANISOU 1533 CGI VAL 222 2252 3113 2977 250 -645 - 182

ATOM 1534 CG2 VAL 222 11.730 25.411 52.490 1.000 22.44

ANISOU 1534 CG2 VAL 222 2923 2537 3067 -497 -898 4 4

ATOM 1535 N LEU 223 13.789 23.892 54.621 1.000 16.30

ANISOU 1535 N LEU 223 1792 1694 2706 -239 -93 -532

ATOM 1536 CA LEU 223 14.407 22.575 54.579 1.000 15.91

ANISOU 1536 CA LEU 223 1679 1864 2503 -93 -297 - 333

ATOM 1537 C LEU 223 14.114 21.908 53.243 1.000 14.86

ANISOU 1537 C LEU 223 1337 1537 2773 -141 -322 - 458

ATOM 1538 0 LEU 223 12.969 21.888 52.766 1.000 16.23

ANISOU 1538 0 LEU 223 1317 2132 2719 70 -391 - 281

ATOM 1539 CB LEU 223 13.829 21.779 55.761 1.000 19.97

ANISOU 1539 CB LEU 223 2740 1945 2901 -121 205 -212

ATOM 1540 CG LEU 223 14.298 20.348 55.882 1.000 23.01

ANISOU 1540 CG LEU 223 2668 1871 4205 -375 -170 9 1

ATOM 1541 CDI LEU 223 15.797 20.322 56.143 1.000 23.73

ANISOU 1541 CDI LEU 223 2570 3067 3378 69 135 3 16

ATOM 1542 CD2 LEU 223 13.492 19.668 56.979 1.000 35.71

ANISOU 1542 CD2 LEU 223 2813 3296 7459 525 1116 2333

ATOM 1543 N VAL 224 15.115 21.370 52.570 1.000 14.18

ANISOU 1543 N VAL 224 1383 1446 2560 -28 -320 - 205

ATOM 1544 CA VAL 224 14.956 20.627 51.330 1.000 14.52

ANISOU 1544 CA VAL 224 1585 1501 2431 -23 -323 - 127

ATOM 1545 C VAL 224 15.320 19.160 51.561 1.000 13 .59

ANISOU 1545 C VAL 224 1464 1522 2178 23 -290 - 251

ATOM 1546 0 VAL 224 16.442 18.861 51.981 1.000 15.38

ANISOU 1546 0 VAL 224 1464 1558 2822 0 -505 - 374

ATOM 1547 CB VAL 224 15.832 21.209 50.222 1.000 14.25

ANISOU 1547 CB VAL 224 1402 1606 2407 -60 -461 - 108

ATOM 1548 CGI . VAL 224 15.685 20.443 48.906 1.000 16.63

ANISOU 1548 CGI . VAL 224 1682 2164 2474 -159 -408 - 421

ATOM 1549 CG2 VAL 224 15.575 22.687 50.040 1.000 16.40

ANISOU 1549 CG2 : VAL 224 1807 1562 2863 6 -509 8 7

ATOM 1550 N PHE 225 14.340 18.299 51.299 1.000 13 .49

ANISOU 1550 N PHE 225 1494 1526 2106 -66 -353 - 130

ATOM 1551 CA PHE 225 14.647 16.882 51.162 1.000 14.67

ANISOU 1551 CA PHE 225 1639 1505 2431 -115 -61 -283

ATOM 1552 C PHE 225 14.756 16.533 49.675 1.000 14.27

ANISOU 1552 C PHE 225 1536 1533 2352 100 -260 - 194

ATOM 1553 O PHE 225 13.858 16.876 48.893 1.000 16.25

ANISOU 1553 O PHE 225 1604 2000 2569 296 -311 - 8 8

ATOM 1554 CB PHE 225 13.537 15.999 51.749 1.000 15.57

ANISOU 1554 CB PHE 225 1613 1563 2740 -25 -46 2 4

ATOM 1555 CG PHE 225 13.387 15.996 53.257 1.000 17.95

ANISOU 1555 CG PHE 225 1888 2267 2666 -650 -302 2 03

ATOM 1556 CDI PHE 225 14.409 15.809 54.157 1.000 27.39 ANISOU 1556 CDI PHE 225 2740 4234 3431 -910 -1094 9 0 C

ATOM 1557 CD2 PHE 225 12.125 15.863 53.820 1.000 21.09

ANISOU 1557 CD2 PHE 225 2333 2765 2917 -166 399 - 527

ATOM 1558 CE1 PHE 225 14.211 15.673 55.521 1.000 26.82

ANISOU 1558 CE1 PHE 225 3108 3657 3424 -1044 -1241 1128

ATOM 1559 CE2 PHE 225 11.910 15.910 55.186 1.000 21.65

ANISOU 1559 CE2 PHE 225 2994 2414 2817 623 239 - 3 9

ATOM 1560 CZ PHE 225 12.958 15.787 56.078 1.000 28.82

ANISOU 1560 CZ PHE 225 3705 3716 3531 -832 -663 3 40

ATOM 1561 N CYS 226 15.795 15.817 49.266 1.000 12 .77

ANISOU 1561 N CYS 226 1428 1292 2131 -60 -370 - 239

ATOM 1562 CA CYS 226 15.810 15.180 47.956 1.000 12.99

ANISOU 1562 CA CYS 226 1360 1440 2135 12 -355 - 207

ATOM 1563 C CYS 226 14.903 13.956 47.985 1.000 12 .37

ANISOU 1563 C CYS 226 1533 1212 1955 8 -283 - 311

ATOM 1564 0 CYS 226 14.961 13.217 48.974 1.000 15.68

ANISOU 1564 0 CYS 226 1885 1651 2424 -140 -611 1 5 8

ATOM 1565 CB CYS 226 17.228 14.855 47.527 1.000 13 .77

ANISOU 1565 CB CYS 226 1410 1627 2193 19 -203 - 7 5

ATOM 1566 SG CYS 226 18.224 16.367 47.314 1.000 16.37

ANISOU 1566 SG CYS 226 1744 1740 2735 -222 -236 - 12

ATOM 1567 N GLY 227 14.150 13.722 46.928 1.000 13.20

ANISOU 1567 N GLY 227 1388 1513 2113 -28 -293 - 290

ATOM 1568 CA GLY 227 13.352 12.496 46.899 1.000 12.58

ANISOU 1568 CA GLY 227 1279 1631 1872 -83 -438 - 255

ATOM 1569 C GLY 227 13.903 11.541 45.849 1.000 12.54

ANISOU 1569 C GLY 227 1518 1279 1965 15 -288 - 7 9

ATOM 1570 0 GLY 227 14.917 11.732 45.152 1.000 13.58

ANISOU 1570 0 GLY 227 1630 1523 2008 51 -155 8 2

ATOM 1571 N ALA 228 13.212 10.400 45.712 1.000 13.02

ANISOU 1571 N ALA 228 1490 1306 2151 59 -204 - 161

ATOM 1572 CA ALA 228 13.663 9.321 44.860 1.000 12.41

ANISOU 1572 CA ALA 228 1649 1155 1912 -68 -119 - 63

ATOM 1573 C ALA 228 13.706 9.727 43.404 1.000 12.82

ANISOU 1573 C ALA 228 1566 1288 2016 97 -223 - 5

ATOM 1574 0 ALA 228 14.482 9.132 42.651 1.000 13.64

ANISOU 1574 0 ALA 228 1717 1462 2004 26 -6 - 131

ATOM 1575 CB ALA 228 12.714 8.121 45.058 1.000 14.56

ANISOU 1575 CB ALA 228 1808 1366 2356 -219 358 - 243

ATOM 1576 N ILE 229 12.909 10.695 42.952 1.000 13.61

ANISOU 1576 N ILE 229 1340 1391 2441 -43 -289 2 73

ATOM 1577 CA ILE 229 13.024 11.131 41.566 1.000 12.93

ANISOU 1577 CA ILE 229 1325 1243 2344 -42 -306 173

ATOM 1578 C ILE 229 14.342 11.864 41.358 1.000 13.17

ANISOU 1578 C ILE 229 1327 1364 2311 -47 -191 13 0

ATOM 1579 0 ILE 229 14.938 11.746 40.262 1.000 14.41

ANISOU 1579 0 ILE 229 1587 1596 2293 -37 -167 1 83

ATOM 1580 CB ILE 229 11.768 11.888 41.103 1.000 13 .46

ANISOU 1580 CB ILE 229 1470 1631 2015 171 -354 - 42

ATOM 1581 CGI . ILE 229 10.599 10.920 40.973 1.000 15.72

ANISOU 1581 CGI . ILE 229 1218 1936 2817 85 31 118

ATOM 1582 CG2i ILE 229 12.040 12.674 39.808 1.000 14.19

ANISOU 1582 CG2 ! ILE 229 1670 1425 2298 76 -364 174

ATOM 1583 CDI . ILE 229 10.745 9.924 39.836 1.000 20.03

ANISOU 1583 CDI ILE 229 2129 1814 3667 -208 -385 - 488

ATOM 1584 N ALA 230 14.877 12.575 42.353 1.000 13 .38

ANISOU 1584 N ALA 230 1252 1378 2454 -97 -176 7 4

ATOM 1585 CA ALA 230 16.209 13.185 42.130 1.000 12.30

ANISOU 1585 CA ALA 230 1156 1444 2074 66 -97 - 108

ATOM 1586 C ALA 230 17.223 12.033 41.976 1.000 12.89

ANISOU 1586 C ALA 230 1491 1327 2079 128 30 - 2 0 ATOM 1587 0 ALA 230 18.100 12.091 41.146 1.000 13 .65

ANISOU 1587 0 ALA 230 1240 1530 2418 108 4 4 6

ATOM 1588 CB ALA 230 16.588 14.000 43.345 1.000 13 .66

ANISOU 1588 CB ALA 230 1559 1415 2215 -186 -21 - 229

ATOM 1589 N THR 231 17.143 10.978 42.805 1.000 13 .31

ANISOU 1589 N THR 231 1526 1318 2214 58 -261 - 1

ATOM 1590 CA THR 231 18.022 9.815 42.659 1.000 13 .32

ANISOU 1590 CA THR 231 1660 1307 2093 78 -302 3 2

ATOM 1591 C THR 231 17.906 9.224 41.251 1.000 13 .27

ANISOU 1591 C THR 231 1300 1631 2111 205 -211 3

ATOM 1592 0 THR 231 18.932 8.974 40.620 1.000 15 .51

ANISOU 1592 0 THR 231 1468 1759 2667 245 58 - 170

ATOM 1593 CB THR 231 17.656 8.751 43.688 1.000 13 .03

ANISOU 1593 CB THR 231 1500 1302 2151 46 -166 1 2

ATOM 1594 OGl THR 231 17.530 9.313 44.995 1.000 14.70

ANI SOU- 1594 OGl THR 231 1742 1614 2230 -99 32 - 14

ATOM 1595 CG2 THR 231 18.698 7.621 43.697 1.000 13 .69

ANISOU 1595 CG2 THR 231 1449 1419 2335 113 -211 1 9 7

ATOM 1596 N LEU 232 16.665 9.049 40.796 1.000 13 .43

ANISOU 1596 N LEU 232 1447 1384 2271 75 -404 - 27

ATOM 1597 CA LEU 232 16.446 8.396 39.527 1.000 14.11

ANISOU 1597 CA LEU 232 1809 1226 2326 80 -468 4 9

ATOM 1598 C LEU 232 16.975 9.248 38.381 1.000 15.53

ANISOU 1598 C LEU 232 1968 1557 2376 209 -3 9 0

ATOM 1599 0 LEU 232 17.749 8.808 37.504 1.000 17.16

ANISOU 1599 0 LEU 232 2024 1949 2546 107 -116 - 519

ATOM 1600 CB LEU 232 14.940 8.135 39.368 1.000 14.47

ANISOU 1600 CB LEU 232 1692 1630 2175 72 -396 - 161

ATOM 1601 CG LEU 232 14.525 7.307 38.155 1.000 15.89

ANISOU 1601 CG LEU 232 1941 1768 2329 120 -470 - 303

ATOM 1602 CDI LEU 232 15.118 5.920 38.202 1.000 23.19

ANISOU 1602 CDI LEU 232 3565 2020 3228 743 -1110 - 851

ATOM 1603 CD2 LEU 232 13.003 7.190 38.126 1.000 19.46

ANISOU 1603 CD2 LEU 232 2006 2262 3126 -470 -523 - 6 6

ATOM 1604 N VAL 233 16.539 10.514 38.299 1.000 13.73

ANISOU 1604 N VAL 233 1736 1454 2025 -7 -263 193

ATOM 1605 CA VAL 233 16.893 11.317 37.117 1.000 13 .84

ANISOU 1605 CA VAL 233 1674 1658 1926 141 -73 107

ATOM 1606 C VAL 233 18.407 11.510 37.025 1.000 14.08

ANISOU 1606 C VAL 233 1716 1674 1958 72 -46 113

ATOM 1607 O VAL 233 18.940 11.587 35.910 1.000 16.65

ANISOU 1607 O VAL 233 1923 2325 2079 38 109 4 01

ATOM 1608 CB VAL 233 16.098 12.626 37.062 1.000 14.69

ANISOU 1608 CB VAL 233 1680 1696 2206 141 -165 33 3

ATOM 1609 CGI VAL 233 16.529 13.650 38.113 1.000 15.70

ANISOU 1609 CGI VAL 233 1615 1654 2698 34 156 - 2 8

ATOM 1610 CG2 VAL 233 16.117 13.206 35.647 1.000 16.43

ANISOU 1610 CG2 VAL 233 1740 2041 2459 251 117 5 9 6

ATOM 1611 N THR 234 19.100 11.594 38.175 1.000 14.23

ANISOU 1611 N THR 234 1599 1724 2083 146 -110 2 3 5

ATOM 1612 CA THR 234 20.524 11.908 38.148 1.000 16.14

ANISOU 1612 CA THR 234 1664 1868 2602 63 -171 - 4 9

ATOM 1613 C THR 234 21.346 10.621 38.006 1.000 17.09

ANISOU 1613 C THR 234 1717 1865 2912 146 211 - 5 1

ATOM 1614 O THR 234 22.558 10.644 38.139 1.000 17.25

ANISOU 1614 O THR 234 1776 1951 2828 108 200 2 2 9

ATOM 1615 CB THR 234 21.030 12.681 39.373 1.000 15.29

ANISOU 1615 CB THR 234 1667 1502 2642 -46 -149 1 63

ATOM 1616 OGl THR 234 20.849 11.819 40.522 1.000 15.45

ANISOU 1616 OGl THR 234 1659 1708 2502 -80 59 4 4

ATOM 1617 CG2 THR 234 20.291 13.978 39.597 1.000 16.61 -

-66-

ANISOU 1617 CG2 THR 234 1564 1672 3077 3 -34 - 42

ATOM 1618 N GLY 235 20.712 9.441 37.833 1.000 15.80

ANI SOL- 1618 N GLY 235 1905 1914 2564 193 29 - 219

ATOM 1619 C GLY 235 21.484 8.209 37.792 1.000 17.10

ANISOU 1619 CA GLY 235 2049 1861 2586 133 223 - 488

ATOM 1620 C GLY 235 22.225 7.931 39.083 1.000 18.06

ANI SOL- 1620 C GLY 235 2046 2049 2768 419 499 3 03

ATOM 1621 0 GLY 235 23.285 7.289 39.010 1.000 21.26

ANISOU 1621 0 GLY 235 2167 2606 3303 679 343 - 7 4

ATOM 1622 N GLY 236 21.602 8.149 40.237 1.000 16.17

ANISOU 1622 N GLY 236 1663 1901 2582 36 291 3 05

ATOM 1623 CA GLY 236 22.080 7.673 41.520 1.000 17.27

ANISOU 1623 CA GLY 236 2135 1671 2754 225 2S 22 9

ATOM 1624 C GLY 236 23.033 8.639 42.194 1.000 16.88

ANI SOL- 1624 C GLY 236 1880 1890 2644 204 100 2 22

ATOM 1625 0 GLY 236 23.692 8.272 43.193 1.000 19.42

ANISOU 1625 0 GLY 236 2165 2399 2814 314 -90 4 1 9

ATOM 1626 N GLN 237 23.134 9.890 41.746 1.000 16.99

ANISOU 1626 N GLN 237 1647 1851 2957 213 -213 1 67

ATOM 1627 CA GLN 237 24.074 10.849 42.298 1.000 15.75

ANISOU 1627 CA GLN 237 1608 2004 2752 72 177 9 8

ATOM 1628 C GLN 237 23.481 11.604 43.483 1.000 15.64

ANISOU 1628 C GLN 237 1404 2136 2402 231 -146 2 00

ATOM 1629 0 GLN 237 24.183 12.382 44.164 1.000 18.17

ANISOU 1629 0 GLN 237 1581 2508 2817 -227 -6 - 4 6

ATOM 1630 CB GLN 237 24.456 11.855 41.217 1.000 17.17

ANISOU 1630 CB GLN 237 1912 2080 2532 71 141 - 7

ATOM 1631 CG GLN 237 25.304 11.221 40.115 1.000 17.64

ANISOU 1631 CG GLN 237 1850 2410 2441 226 95 - 3 0

ATOM 1632 CD GLN 237 25.721 12.302 39.137 1.000 19.72

ANISOU 1632 CD GLN 237 1680 2833 2979 104 317 3 07

ATOM 1633 OEl GLN 237 26.602 13.110 39.436 1.000 24.27

ANISOU 1633 OEl GLN 237 1841 3145 4234 -213 -187 809

ATOM 1634 NE2 GLN 237 24.986 12.399 38.027 1.000 18.53

ANISOU 1634 NE2 GLN 237 2007 2298 2735 432 374 202

ATOM 1635 N VAL 238 22.221 11.359 43.807 1.000 14.75

ANISOU 1635 N VAL 238 1563 1804 2237 -32 -54 4 3

ATOM 1636 CA VAL 238 21.533 12.075 44.862 1.000 14.41

ANISOU 1636 CA VAL 238 1535 1553 2388 0 -44 3 2

ATOM 1637 C VAL 238 20.861 11.060 45.781 1.000 13.56

ANISOU 1637 C VAL 238 1414 1392 2346 82 55 - 149

ATOM 1638 0 VAL 238 20.136 10.174 45.302 1.000 15.87

ANISOU 1638 0 VAL 238 1655 1639 2737 -218 -285 - 22

ATOM 1639 CB VAL 238 20.467 13.061 44.309 1.000 14.73

ANISOU 1639 CB VAL 238 1817 1626 2152 35 -437 - 95

ATOM 1640 CGI . VAL 238 19.805 13.764 45.489 1.000 15.70

ANISOU 1640 CGI . VAL 238 1965 1490 2510 174 -524 - 423

ATOM 1641 CG2 : VAL 238 21.064 13.994 43.280 1.000 16.82

ANISOU 1641 CG2 ! VAL 238 1862 1718 2812 -60 -378 222

ATOM 1642 N LYS 239 21.119 11.153 47.071 1.000 14.47

ANISOU 1642 N LYS 239 1704 1474 2318 14 -40 1 2

ATOM 1643 CA LYS 239 20.470 10.360 48.104 1.000 14.43

ANISOU 1643 CA LYS 239 1460 1617 2406 106 -168 17 9

ATOM 1644 C LYS 239 19.048 10.852 48.409 1.000 14.82

ANISOU 1644 C LYS 239 1533 1456 2642 102 -53 2 3 2

ATOM 1645 O LYS 239 18.839 12.067 48.457 1.000 14.74

ANI SOL- 1645 O LYS 239 1841 1442 2318 158 -275 190

ATOM 1646 CB LYS 239 21.320 10.435 49.385 . 1.000 16.40

ANISOU 1646 CB LYS 239 1995 1712 2527 243 -543 252

ATOM 1647 CG LYS 239 20.767 9.549 50.498 ! 1.000 16.65

ANISOU 1647 CG LYS 239 1954 1759 2614 -58 -781 2 44 ATOM 1648 CD LYS 239 21.738 9.511 51.683 1.000 19.76

ANISOU 1648 CD LYS 239 2954 1820 2732 -123 -1234 3 6 3

ATOM 1649 CE LYS 239 21.107 8.835 52.896 1.000 22.58

ANISOU 1649 CE LYS 239 3331 2164 3086 -652 -1502 8 63

ATOM 1650 NZ LYS 239 21.904 8.883 54.145 1.000 23 .13

ANISOU 1650 NZ LYS 239 2817 3360 2612 -471 -943 2 87

ATOM 1651 N ALA 240 18.140 9.892 48.659 1.000 14.35

ANISOU 1651 N ALA 240 1429 1607 2418 -156 -334 - 6 1

ATOM 1652 CA ALA 240 16.791 10.192 49.145 1.000 13 .98

ANISOU 1652 C ALA 240 1468 1635 2210 -151 -335 - 1 0

ATOM 1653 C ALA 240 16.728 9.776 50.605 1.000 13 .44

ANISOU 1653 C ALA 240 1439 1388 2279 77 -450 2 2

ATOM 1654 0 ALA 240 16.514 8.592 50.913 1.000 16.32

ANISOU 1654 0 ALA 240 1932 1567 2699 -215 -673 3 14

ATOM 1655 CB ALA 240 15.712 9.565 48.268 1.000 15.21

ANISOU 1655 CB ALA 240 1510 1962 2306 -104 -387 - 307

ATOM 1656 N PRO 241 16.907 10.701 51.546 1.000 14.23

ANISOU 1656 N PRO 241 1634 1551 2221 -87 -292 7 1

ATOM 1657 CA PRO 241 17.035 10.251 52.940 1.000 14.68

ANISOU 1657 CA PRO 241 1718 1681 2180 -350 -174 - 3 0

ATOM 1658 C PRO 241 15.693 9.961 53.579 1.000 13.89

ANISOU 1658 C PRO 241 1659 1581 2039 -107 -207 - 74

ATOM 1659 0 PRO 241 14.629 10.527 53.261 1.000 17.06

ANISOU 1659 0 PRO 241 1698 1946 2838 17 -254 14 6

ATOM 1660 CB PRO 241 17.689 11.462 53.619 1.000 16.63

ANISOU 1660 CB PRO 241 2162 1657 2501 -460 -487 5 5

ATOM 1661 CG PRO 241 17.138 12.651 52.826 1.000 16.56

ANISOU 1661 CG PRO 241 2433 1601 2258 -367 -274 3 1

ATOM 1662 CD PRO 241 17.164 12.140 51.409 1.000 14.92

ANISOU 1662 CD PRO 241 1841 1490 2339 -215 -186 - 66

ATOM 1663 N ARG 242 15.740 9.049 54.544 1.000 15.74

ANISOU 1663 N ARG 242 1914 1853 2212 -381 -308 2 04

ATOM 1664 CA ARG 242 14.574 8.772 55.376 1.000 15.50

ANISOU 1664 CA ARG 242 1955 1863 2073 -236 -291 1 8 0

ATOM 1665 C ARG 242 14.406 9.841 56.437 1.000 16.60

ANISOU 1665 C ARG 242 1889 2011 2407 -120 -411 - 51

ATOM 1666 0 ARG 242 15.372 10.416 56.994 1.000 18.31

ANISOU 1666 0 ARG 242 2041 2186 2732 -216 -559 - 180

ATOM 1667 CB ARG 242 14.728 7.419 56.085 1.000 18.38

ANISOU 1667 CB ARG 242 2920 1810 2253 -486 -391 2 69

ATOM 1668 CG ARG 242 14.564 6.273 55.094 1.000 18.42

ANISOU 1668 CG ARG 242 2372 1873 2755 -88 162 - 155

ATOM 1669 CD ARG 242 14.854 4.935 55.796 1.000 23 .07

ANISOU 1669 CD ARG 242 3380 2022 3366 470 -483 - 217

ATOM 1670 NE ARG 242 16.334 4.954 55.991 1.000 26.69

ANISOU 1670 NE ARG 242 3498 2727 3916 444 -829 4 7

ATOM 1671 CZ ARG 242 16.941 3.921 56.584 1.000 27.19

ANISOU 1671 CZ ARG 242 3166 2879 4284 -297 -1143 8 02

ATOM 1672 NHl ARG 242 16.157 2.913 56.989 1.000 33.14

ANISOU 1672 NHl ARG 242 3810 3235 5546 -316 528 72 6

ATOM 1673 NH - ARG 242 18.241 3.889 56.779 1.000 31.13

ANISOU 1673 NH2 ARG 242 3043 2925 5859 227 -769 4 84

ATOM 1674 N HIS 243 13.188 10.057 56.872 1.000 17.55

ANISOU 1674 N HIS 243 1979 2233 2457 -165 -173 - 7 4

ATOM 1675 CA HIS 243 12.913 11.050 57.914 1.000 17.84

ANISOU 1675 CA HIS 243 2186 2139 2452 -260 -123 - 7 5

ATOM 1676 C HIS 243 11.644 10.627 58.643 1.000 17.52

ANISOU 1676 C HIS 243 2102 2084 2470 -248 -164 - 325

ATOM 1677 O HIS 243 10.870 9.803 58.132 1.000 20.23

ANISOU 1677 O HIS 243 2226 2593 2868 -551 -323 - 392

ATOM 1678 CB HIS 243 12.865 12.456 57.324 1.000 19.74 ANISOU 1678 CB HIS 243 2770 2248 2432 -188 -106 8 3

ATOM 1679 CG HIS 243 11.922 12.630 56.187 1.000 22 .60

ANISOU 1679 CG HIS 243 3449 2513 2624 164 -382 0

ATOM 1680 NDl HIS 243 12.209 12.299 54.879 1.000 25.87

ANISOU 1680 NDl HIS 243 4780 2575 2473 -609 -403 5 3

ATOM 1681 CD2 HIS 243 10.633 13.034 56.172 1.000 29.11

ANISOU 1681 CD2 HIS 243 3220 4490 3348 121 -421 1630

ATOM 1682 CE1 HIS 243 11.182 12.573 54.109 1.000 32 .92

ANISOU 1682 CE1 HIS 243 5835 3672 3001 -1102 -1367 6 8 9

ATOM 1683 NE2 HIS 243 10.214 13.012 54.875 1.000 36.95

ANISOU 1683 NE2 HIS 243 5719 4201 4119 1019 -2016 9 87

ATOM 1684 N HIS 244 11.437 11.194 59.831 1.000 18.87

ANISOU 1684 N HIS 244 2523 2477 2171 -88 -141 - 117

ATOM 1685 CA HIS 244 10.302 10.801 60.649 1.000 20.83

ANISOU 1685 CA HIS 244 2802 2485 2628 171 251 2 72

ATOM 1686 C HIS 244 9.927 11.968 61.551 1.000 20.33

ANISOU 1686 C HIS 244 1803 2969 2953 -31 -78 - 273

ATOM 1687 0 HIS 244 10.482 13.073 61.510 1.000 21.71

ANISOU 1687 0 HIS 244 2057 3418 2774 -535 145 - 853

ATOM 1688 CB HIS 244 10.714 9.557 61.468 1.000 24.38

ANISOU 1688 CB HIS 244 4066 2644 2553 -76 -390 441

ATOM 1689 CG HIS 244 11.859 9.725 62.423 1.000 28.34

ANISOU 1689 CG HIS 244 4158 3498 3113 696 -727 - 8 9

ATOM 1690 NDl HIS 244 13.132 9.205 62.268 1.000 32 .35

ANISOU 1690 NDl HIS 244 4012 4471 3808 548 -485 - 850

ATOM 1691 CD2 HIS 244 11.928 10.391 63.609 1.000 25.21

ANISOU 1691 CD2 HIS 244 2937 4137 2505 -373 45 2 19

ATOM 1692 CE1 HIS 244 13.887 9.531 63.312 1.000 31.71

ANISOU 1692 CE1 HIS 244 4157 4277 3613 1224 -749 - 518

ATOM 1693 NE2 HIS 244 13.146 10.263 64.150 1.000 24.52

ANISOU 1693 NE2 HIS 244 3165 3517 2633 94 -82 492

ATOM 1694 N VAL 245 8.890 11.687 62.349 1.000 23 .87

ANISOU 1694 N VAL 245 2627 3119 3322 -251 531 - 310

ATOM 1695 CA VAL 245 8.473 12.691 63.349 1.000 24.85

ANISOU 1695 CA VAL 245 2785 3770 2888 481 149 -293

ATOM 1696 C VAL 245 8.624 12.079 64.735 1.000 26.03

ANISOU 1696 C VAL 245 3220 3558 3112 -289 179 8 9

ATOM 1697 0 VAL 245 8.023 11.025 64.969 1.000 27.98

ANISOU 1697 0 VAL 245 3120 3085 4428 42 295 - 59

ATOM 1698 CB VAL 245 7.020 13.114 63.099 1.000 26.02

ANISOU 1698 CB VAL 245 2621 3489 3777 94 -103 - 569

ATOM 1699 CGI VAL 245 6.586 14.114 64.161 1.000 28.06

ANISOU 1699 CGI VAL 245 2717 3330 4614 159 746 - 485

ATOM 1700 CG2 VAL 245 6.927 13.705 61.680 1.000 30.51

ANISOU 1700 CG2 VAL 245 3564 3809 4220 1264 -305 - 3 3

ATOM 1701 N ALA 246 9.399 12.696 65.603 1.000 28.08

ANISOU 1701 N ALA 246 4338 3787 2543 -850 250 2 54

ATOM 1702 CA ALA 246 9.567 12.316 67.003 1.000 27.45

ANISOU 1702 CA ALA 246 4363 3360 2707 292 275 3 73

ATOM 1703 C ALA 246 8.356 12.740 67.833 1.000 32.68

ANISOU 1703 C ALA 246 4915 4473 3031 98 880 1 97

ATOM 1704 O ALA 246 7.774 13.791 67.563 1.000 29.54

ANISOU 1704 O ALA 246 3522 4283 3417 -224 875 - 329

ATOM 1705 CB ALA 246 10.819 13.010 67.542 1.000 30.33

ANISOU 1705 CB ALA 246 4564 3949 3011 615 -221 - 422

ATOM 1706 N ALA 247 8.048 11.958 68.849 1.000 34.09

ANISOU 1706 N ALA 247 4483 5156 3311 -1190 466 3 9 3

ATOM 1707 CA ALA 247 7.036 12.190 69.859 1.000 34.23

ANISOU 1707 CA ALA 247 4188 5627 3189 -1215 315 5 15

ATOM 1708 C ALA 247 7.609 12.910 71.081 1.000 33 .31

ANISOU 1708 C ALA 247 5419 4684 2555 249 -506 1147 -.--- -.

-69-

ATOM 1709 0 ALA 247 8.733 12.708 71.523 1.000 38.23

ANISOU 1709 0 ALA 247 5787 4478 4259 -378 -1519 1230

ATOM 1710 CB ALA 247 6.383 10.881 70.314 1.000 47.11

ANISOU 1710 CB ALA 247 8374 6726 2801 -2800 1464 686

ATOM 1711 N PRO 248 6.817 13.851 71.577 1.000 42.28

ANISOU 1711 N PRO 248 5771 5458 4836 -300 933 - 97

ATOM 1712 CA PRO 248 7.256 14.581 72.773 1.000 44.85

ANISOU 1712 CA PRO 248 7568 5478 3996 -645 1413 214

ATOM 1713 C PRO 248 7.161 13.618 73.948 1.000 49.25

ANISOU 1713 C PRO 248 7978 5660 5075 -1446 552 985

ATOM 1714 0 PRO 248 6.251 12.794 74.014 1.000 45.48

ANISOU 1714 0 PRO 248 7651 5391 4237 -1127 2573 - 796

ATOM 1715 CB PRO 248 6.196 15.674 72.897 1.000 49.75

ANISOU 1715 CB PRO 248 8563 4816 5523 -513 1238 - 138

ATOM 1716 CG PRO 248 4.973 15.053 72.299 1.000 50.89

ANISOU 1716 CG PRO 248 7228 5564 6545 -108 2210 - 1064

ATOM 1717 CD PRO 248 5.489 14.272 71.114 1.000 44.69

ANISOU 1717 CD PRO 248 6395 4579 6006 937 953 - 577

ATOM 1718 N ARG 249 8.109 13.683 74.883 1.000 48.76

ANISOU 1718 N ARG 249 9141 6341 3045 -1317 1069 - 477

ATOM 1719 CA ARG 249 7.865 12.783 76.024 1.000 55.51

ANISOU 1719 CA ARG 249 10023 6914 4156 -1098 895 566

ATOM 1720 C ARG 249 6.844 13.466 76.916 1.000 46.09

ANISOU 1720 C ARG 249 5561 8382 3568 -2484 -7 1237

ATOM 1721 O ARG 249 6.244 12.915 77.831 1.000 56.25

ANISOU 1721 O ARG 249 7572 6368 7433 -377 1799 3995

ATOM 1722 CB ARG 249 9.177 12.459 76.721 1.000 55.24

ANISOU 1722 CB ARG 249 8950 7715 4326 705 2864 1270

ATOM 1723 CG ARG 249 9.915 11.278 76.110 1.000 71.04

ANISOU 1723 CG ARG 249 12881 7330 6779 1135 3707 622

ATOM 1724 CD ARG 249 10.403 10.303 77.165 1.000 72.89

ANISOU 1724 CD ARG 249 11721 7991 7984 2171 2723 409

ATOM 1725 NE ARG 249 11.124 9.162 76.580 1.000 70.73

ANISOU 1725 NE ARG 249 8627 9977 8271 2362 2650 - 266

ATOM 1726 CZ ARG 249 12.039 8.493 77.282 1.000 72.71

ANISOU 1726 CZ ARG 249 10269 9417 7942 2304 2153 133

ATOM 1727 NHl ARG 249 12.297 8.893 78.521 1.000 89.50

ANISOU 1727 NHl . ARG 249 22286 6161 5559 2015 1622 3874

ATOM 1728 NH2 ARG 249 12.682 7.462 76.761 1.000 67.68

ANISOU 1728 NH2 ARG 249 5358 10062 10295 1004 3886 221

ATOM 1729 N ALA 254 1.981 18.918 75.430 1.000 85.24

ANISOU 1729 N ALA 254 15501 7922 8964 -4581 -1437 2347

ATOM 1730 CA ALA 254 2.287 20.081 76.257 1.000 76.08

ANISOU 1730 CA ALA 254 12510 8110 8286 -3993 1617 1592

ATOM 1731 C ALA 254 2.943 21.216 75.489 1.000 60.91

ANISOU 1731 C ALA 254 8383 5719 9040 -506 2886 1312

ATOM 1732 O ALA 254 4.174 21.309 75.487 1.000 72.37

ANISOU 1732 O ALA 254 8056 8109 11332 1602 4553 3381

ATOM 1733 CB ALA 254 3.264 19.667 77.351 1.000 60.48

ANISOU 1733 CB ALA 254 12589 7262 3131 -866 4570 - 1112

ATOM 1734 N GLY 255 2.200 22.108 74.846 1.000 54.40

ANISOU 1734 N GLY 255 8029 5451 7190 594 2922 - 940

ATOM 1735 CA GLY 255 2.880 23.171 74.098 1.000 40.05

ANISOU 1735 CA GLY 255 5181 4570 5465 1424 836 - 921

ATOM 1736 C GLY 255 3.640 22.565 72.921 1.000 38.82

ANISOU 1736 C GLY 255 4227 4772 5749 557 702 -1561

ATOM 1737 O GLY 255 4.580 23.163 72.398 1.000 39.96

ANISOU 1737 O GLY 255 2978 6491 5715 -128 -136 - 2226

ATOM 1738 N SER 256 3.164 21.387 72.509 1.00Cι 37.29

ANISOU 1738 N SER 256 5047 4594 4527 389 11 - 853

ATOM 1739 CA SER 256 3.738 20.606 71.429 1.00Cl 35.71 -70-

ANISOU 1739 CA SER 256 4737 4533 4299 560 -5C1 - 919

ATOM 1740 C SER 256 2.983 20.742 70.118 1.000 34.93

ANISOU 1740 C SER 256 4584 4669 4019 -98 -85 9 1

ATOM 17410 SER 256 3.251 20.000 69.162 1.000 33.92

ANISOU 1741 0 SER 256 3575 6107 3207 503 304 377

ATOM 1742 CB SER 256 3.845 19.136 71.853 1.000 30.17

ANISOU 1742 CB SER 256 3125 4830 3509 624 212 - 492

ATOM 1743 OG SER 256 2.688 18.752 72.601 1.000 61.15

ANISOU 1743 OG SER 256 2987 8497 11750 451 1943 2630

ATOM 1744 N SER 257 2.065 21.700 70.030 1.000 35.54

ANISOU 1744 N SER 257 4037 5989 3479 347 242 - 86

ATOM 1745 CA SER 257 1.379 21.993 68.767 1.000 30.95

ANISOU 1745 CA SER 257 2824 5827 3109 170 672 - 509

ATOM 1746 C SER 257 2.378 22.538 67.760 1.000 30.63

ANISOU 1746 C SER 257 3181 5524 2934 -476 765 - 1297

ATOM 1747 0 SER 257 3.359 23.159 68.199 1.000 34.70

ANISOU 1747 0 SER 257 3500 6070 3616 -829 603 - 1516

ATOM 1748 CB SER 257 0.331 23.088 69.036 1.000 38.70

ANISOU 1748 CB SER 257 3085 6518 5103 796 1381 435

ATOM 1749 OG SER 257 0.801 24.361 68.601 1.000 65.12

ANISOU 1749 OG SER 257 8002 5175 11565 -999 -3375 383

ATOM 1750 N ARG 258 2.119 22.384 66.471 1.000 30.51

ANISOU 1750 N ARG 258 3668 5068 2855 -332 677 - 995

ATOM 1751 CA ARG 258 2.997 22.819 65.396 1.000 28.15

ANISOU 1751 CA ARG 258 3100 4620 2976 -106 358 - 544

ATOM 1752 C ARG 258 2.198 22.913 64.096 1.000 25.64

ANISOU 1752 C ARG 258 3488 3381 2872 -676 273 - 904

ATOM 1753 0 ARG 258 1.132 22.294 63.981 1.000 24.93

ANISOU 1753 0 ARG 258 3162 3240 3070 -441 478 - 560

ATOM 1754 CB ARG 258 4.175 21.873 65.154 1.000 27.21

ANISOU 1754 CB ARG 258 3158 4041 3141 -446 313 - 1352

ATOM 1755 CG ARG 258 3.861 20.508 64.570 1.000 30.90

ANISOU 1755 CG ARG 258 4782 3429 3531 -737 -738 - 389

ATOM 1756 CD ARG 258 5.039 19.537 64.769 1.000 36.65

ANISOU 1756 CD ARG 258 5937 3466 4523 106 477 306

ATOM 1757 NE ARG 258 4.597 18.176 64.411 1.000 32.42

ANISOU 1757 NE ARG 258 3372 3858 5089 -85 -274 528

ATOM 1758 CZ ARG 258 4.633 17.777 63.143 1.000 37.32

ANISOU 1758 CZ ARG 258 5670 2958 5553 155 680 4 3

ATOM 1759 NHl ARG 258 5.075 18.622 62.217 1.000 29.98

ANISOU 1759 NHl ARG 258 3077 3435 4881 -150 -211 - 103

ATOM 1760 NH2 ARG 258 4.210 16.566 62.824 1.000 38.66

ANISOU 1760 NH2 ARG 258 5812 3151 5724 -190 -1632 865

ATOM 1761 N THR 259 2.806 23.572 63.120 1.000 23.62

ANISOU 1761 N THR 259 2625 3578 2771 -519 315 - 1037

ATOM 1762 CA THR 259 2.337 23.482 61.730 1.000 21.97

ANISOU 1762 CA THR 259 2614 2934 2800 -36 247 - 1041

ATOM 1763 C THR 259 3.528 23.197 60.808 1.000 19.76

ANISOU 1763 C THR 259 2257 2663 2587 -38 21 - 699

ATOM 1764 O THR 259 4.698 23.411 61.159 1.000 21.13

ANISOU 1764 O THR 259 2464 3096 2468 -495 -10 - 286

ATOM 1765 CB THR 259 1.682 24.793 61.278 1.000 24.04

ANISOU 1765 CB THR 259 2125 3084 3927 70 -157 - 1229

ATOM 1766 OGl THR 259 2.697 25.790 61.041 1.000 23.14

ANISOU 1766 OGl THR 259 2297 2848 3648 196 -142 - 829

ATOM 1767 CGI ^> THR 259 0.760 25.408 62.331 1.000 25.17

ANISOU 1767 CG2 THR 259 2941 3229 3393 726 264 - 136

ATOM 1768 N SER 260 3.234 22.706 59.600 1.000ι 20.41

ANISOU 1768 N SER 260 2386 2762 2609 -61 74 - 806

ATOM 1769 CA SER 260 4.225 22.515 58.551 . 1.00Cι 19.33

ANISOU 1769 CA SER 260 2488 2459 2399 192 8 - 344 -

-71 -

ATOM 1770 C SER 260 3.587 22.871 57.210 1.000 18 .78

ANISOU 1770 C SER 260 1996 2544 2595 -379 -264 - 311

ATOM 1771 0 SER 260 2.375 22.758 56.988 1.000 21.20

ANISOU 1771 0 SER 260 1917 2448 3689 -75 -269 - 573

ATOM 1772 CB SER 260 4.738 21.076 58.480 1.000 20.28

ANISOU 1772 CB SER 260 2491 2458 2755 160 -101 - 495

ATOM 1773 OG SER 260 3.656 20.197 58.227 1.000 22.70

ANISOU 1773 OG SER 260 2758 2574 3294 -113 -284 - 169

ATOM 1774 N SER 261 4.474 23.329 56.330 1.000 18.79

ANISOU 1774 N SER 261 2189 2215 2737 -55 -92 3 5

ATOM 1775 CA SER 261 4.148 23.585 54.929 1.000 16.88

ANISOU 1775 CA SER 261 2074 1718 2622 22 -117 - 404

ATOM 1776 C SER 261 5.066 22.672 54.106 1.000 17.25

ANISOU 1776 C SER 261 1720 1833 3000 101 -350 - 491

ATOM 1777 0 SER 261 6.272 22.876 54.173 1.000 19.96

ANISOU 1777 0 SER 261 1712 2417 3456 50 -483 - 781

ATOM 1778 CB SER 261 4.471 25.028 54.503 1.000 19.95

ANISOU 1778 CB SER 261 2903 1675 3002 164 -113 - 135

ATOM 1779 OG SER 261 4.404 25.127 53.107 1.000 35.64

ANISOU 1779 OG SER 261 5435 4814 3293 -1089 -766 1263

ATOM 1780 N VAL 262 4.467 21.722 53.435 1.000 15.56

ANISOU 1780 N VAL 262 1751 2021 2140 -75 -40 - 436

ATOM 1781 CA VAL 262 5.247 20.713 52.711 1.000 15.41

ANISOU 1781 CA VAL 262 1871 1938 2048 43 21 - 196

ATOM 1782 C VAL 262 4.914 20.874 51.242 1.000 14.05

ANISOU 1782 C VAL 262 1460 1784 2095 -13 29 - 144

ATOM 1783 0 VAL 262 3.759 20.712 50.844 1.000 15.45

ANISOU 1783 0 VAL 262 1488 1900 2481 -175 -94 - 191

ATOM 1784 CB VAL 262 4.902 19.307 53.253 1.000 16.87

ANISOU 1784 CB VAL 262 2144 2005 2260 165 -164 2 3

ATOM 1785 CGI VAL 262 5.567 18.275 52.364 1.000 20.01

ANISOU 1785 CGI VAL 262 2433 2006 3165 4 -191 - 637

ATOM 1786 CG2 VAL 262 5.335 19.200 54.715 1.000 18.63

ANISOU 1786 CG2 VAL 262 2390 2242 2446 147 -397 175

ATOM 1787 N PHE 263 5.894 21.163 50.412 1.000 13.73

ANISOU 1787 N PHE 263 1497 1573 2148 5 -64 186

ATOM 1788 CA PHE 263 5.762 21.411 48.994 1.000 13.04

ANISOU 1788 CA PHE 263 1654 1196 2105 -12 -193 1 13

ATOM 1789 C PHE 263 6.479 20.253 48.284 1.000 13.56

ANISOU 1789 C PHE 263 1432 1351 2370 -175 -98 - 87

ATOM 1790 O PHE 263 7.732 20.177 48.281 1.000 13.83

ANISOU 1790 O PHE 263 1415 1437 2403 -82 -299 - 104

ATOM 1791 CB PHE 263 6.364 22.770 48.594 1.000 13.50

ANISOU 1791 CB PHE 263 1658 1374 2098 -295 -97 3 4

ATOM 1792 CG PHE 263 6.062 23.148 47.135 1.000 13.34

ANISOU 1792 CG PHE 263 1616 1358 2096 -159 -111 8 2

ATOM 1793 CDI PHE 263 6.750 22.635 46.051 1.000 14.95

ANISOU 1793 CDI . PHE 263 1977 1547 2156 -354 -131 - 384

ATOM 1794 CD2 PHE 263 5.005 24.048 46.883 1.000 15.37

ANISOU 1794 CD2 PHE 263 1549 1557 2735 -139 -264 303

ATOM 1795 CEl . PHE 263 6.468 22.945 44.720 1.000 14.58

ANISOU 1795 CEl . PHE 263 1721 1621 2196 -242 71 - 144

ATOM 1796 CE2 : PHE 263 4.703 24.366 45.566 1.000 14.71

ANISOU 1796 CE2 : PHE 263 1482 1428 2680 -20 -261 13 7

ATOM 1797 CZ PHE 263 5.383 23.809 44.479 1.000 16.55

ANISOU 1797 CZ PHE 263 1935 1492 2862 -152 29 1 4

ATOM 1798 N PHE 264 5.721 19.405 47.588 1.000 12.07

ANISOU 1798 N PHE 264 1277 1343 1967 -66 -49 1 9

ATOM 1799 CA PHE 264 6.267 18.328 46.769 1.000 11.90

ANISOU 1799 CA PHE 264 1177 1289 2058 -129 34 - 2 1

ATOM 1800 C PHE 264 6.440 18.775 45.314 : 1.000 11.76 -72-

ANISOL- 1800 C PHE 264 1206 1258 2004 -121 -42 8

ATOM 1801 0 PHE 264 5.418 19.097 44.683 1.000 12. 55

ANISOL- 1801 0 PHE 264 1165 1473 2133 -77 -120 4 6

ATOM 1802 CB PHE 264 5.346 17.099 46.773 1.000 12. 39

ANISOU 1802 CB PHE 264 1101 1498 2110 -304 -42 6 3

ATOM 1803 CG PHE 264 5.022 16.558 48.150 1.000 13. 97

ANISOU 1803 CG PHE 264 1647 1465 2197 -290 13 : L 2 1

ATOM 1804 CDI PHE 264 5.960 15.848 48.852 1.000 17. 07

ANISOU 1804 CDI PHE 264 2039 1976 2471 -422 -41049

ATOM 1805 CD2 PHE 264 3.747 16.679 48.668 1.000 17. 41

ANISOL- 1805 CD2 PHE 264 1835 2359 2419 -440 433 1 1

ATOM 1806 CEl PHE 264 5.661 15.247 50.053 1.000 20. 59

ANISOU 1806 CEl PHE 264 2616 2710 2496 -556 -425 72

ATOM 1807 CE2 PHE 264 3.458 16.133 49.906 1.000 22. 51

ANISOU 1807 CE2 PHE 264 2151 4047 2355 -787 106 55

ATOM 1808 CZ PHE 264 4.386 15.350 50.562 1.000 20. 88

ANISOU 1808 CZ PHE 264 2889 2376 2669 -936 -22 3 0

ATOM 1809 N LEU 265 7.676 18.756 44.811 1.000 11. 81

ANISOU 1809 N LEU 265 1192 1248 2047 -37 47 : 1 9

ATOM 1810 CA LEU 265 7.900 19.000 43.374 1.000 12. 01

ANISOU 1810 CA LEU 265 1264 1269 2028 -223 16 -63

ATOM 1811 C LEU 265 7.915 17.617 42.703 1.000 12. 10

ANISOU 1811 C LEU 265 1266 1298 2033 -117 -81 3

ATOM 1812 O LEU 265 8.842 16.834 42.915 1.000 12. 93

ANISOU 1812 O LEU 265 1367 1283 2260 -107 -152 4 4

ATOM 1813 CB LEU 265 9.246 19.730 43.156 1.000 12. 59

ANISOU 1813 CB LEU 265 1399 1364 2019 -257 57 - 9

ATOM 1814 CG LEU 265 9.500 20.124 41.709 1.000 12. 19

ANISOU 1814 CG LEU 265 1168 1399 2066 -292 -248 30

ATOM 1815 CDI LEU 265 8.620 21.314 41.318 1.000 13. 29

ANISOU 1815 CDI LEU 265 1518 1546 1984 84 36 1 9

ATOM 1816 CD2 LEU 265 10.971 20.458 41.449 1.000 13. .14

ANISOU 1816 CD2 LEU 265 1204 1593 2197 -234 41 -20

ATOM 1817 N ARG 266 6.842 17.249 41.996 1.000 12. .06

ANISOU 1817 N ARG 266 1412 1127 2043 -220 -190 4 5

ATOM 1818 CA ARG 266 6.586 15.913 41.488 1.000 12. .07

ANISOU 1818 CA ARG 266 1372 1201 2012 -258 0 8 0

ATOM 1819 C ARG 266 6.619 15.965 39.972 1.000 11. .75

ANISOU 1819 C ARG 266 1203 1315 1948 29 -267 142

ATOM 1820 O ARG 266 6.032 16.860 39.396 1.000 13 .06

ANISOU 1820 O ARG 266 1430 1318 2214 5 -173 2 81

ATOM 1821 CB ARG 266 5.243 15.370 41.994 1.000 12 .95

ANISOU 1821 CB ARG 266 1142 1477 2302 -189 43 -33

ATOM 1822 CG ARG 266 5.036 15.606 43.488 1.000 13 .80

ANISOU 1822 CG ARG 266 1351 1686 2207 -159 66 -11!

ATOM 1823 CD ARG 266 3.723 15.041 43.993 1.000 12 .70

ANISOU 1823 CD ARG 266 1369 1362 2094 66 -22 8 4

ATOM 1824 NE ARG 266 2.581 15.648 43.281 1.000 12 .97

ANISOU 1824 NE ARG 266 1343 1155 2428 52 -165 -13^'

ATOM 1825 CZ ARG 266 1.304 15.281 43.500 1.000 11 .34

ANISOU 1825 CZ ARG 266 1432 1009 1869 45 -149 - 1 o :

ATOM 1826 NHl . ARG 266 0.995 14.414 44.476 1.000 13 .39

ANISOU 1826 NHl . ARG 266 1802 1165 2119 -11 -36 ! 7 :

ATOM 1827 NH2 ! ARG 266 0.305 15.821 42.826 1.000 12 .55

ANISOU 1827 NH2 ! ARG 266 1490 1067 2210 125 -357 - 1 5 9

ATOM 1828 N PRO 267 7.237 14.951 39.357 1.000 12 .74

ANISOU 1828 N PRO 267 1418 1394 2030 16 -146 108

ATOM 1829 CA PRO 267 7.298 14.947 37.887 1.000 13 .88

ANISOU 1829 CA PRO 267 1442 1786 2047 167 -125 - 8

ATOM 1830 C PRO 267 5.957 14.722 37.222 1.000 ' 12 .61

ANISOU 1830 C PRO 267 1413 1508 1868 -6 44 : 2 7 -73-

ATOM 1831 0 PRO 267 4.998 14.155 37.772 1.000 13 .60

ANISOU 1831 0 PRO 267 1648 1355 2164 -160 118 9 3

ATOM 1832 CB PRO 267 8.238 13.761 37.599 1.000 15.30

ANISOU 1832 CB PRO 267 1435 1740 2637 115 -28 - 169

ATOM 1833 CG PRO 267 8.033 12.846 38.764 1.000 15.82

ANI SOL- 1833 CG PRO 267 1885 1804 2324 381 -270 - 197

ATOM 1834 CD PRO 267 7.872 13.746 39.965 1.000 14.73

ANISOU 1834 CD PRO 267 1803 1356 2438 311 -666 - 205

ATOM 1835 N ASN 268 5.933 15.051 35.939 1.000 13.27

ANI SOL- 1835 N ASN 268 1601 1665 1777 -126 -43 - 127

ATOM 1836 CA ASN 268 4.800 14.709 35.073 1.000 13 .72

ANI SOL- 1836 CA ASN 268 1793 1401 2018 -214 -236 - 71

ATOM 1837 C ASN 268 4.723 13.192 34.875 1.000 13 .14

ANI SOL- 1837 C ASN 268 1485 1350 2156 -213 104 5 4

ATOM 1838 0 ASN 268 5.702 12.467 34.934 1.000 13.90

ANISOU 1838 0 ASN 268 1698 1416 2167 -91 123 - 3 6

ATOM 1839 CB ASN 268 4.997 15.338 33.690 1.000 15.74

ANISOU 1839 CB ASN 268 2597 1369 2016 -66 -437 13 5

ATOM 1840 CG ASN 268 5.011 16.862 33.811 1.000 15.41

ANISOU 1840 CG ASN 268 2255 1439 2162 -17 -184 4 7

ATOM 1841 ODl ASN 268 4.069 17.454 34.352 1.000 17.75

ANISOU 1841 ODl ASN 268 2573 1686 2487 42 91 - 98

ATOM 1842 ND2 ASN 268 6.066 17.503 33.319 1.000 16.61

ANISOU 1842 ND2 ASN 268 2408 1355 2546 -50 -57 142

ATOM 1843 N ALA 269 3.531 12.712 34.594 1.000 13 .99

ANISOU 1843 N ALA 269 1677 1467 2172 -356 -65 170

ATOM 1844 CA ALA 269 3.278 11.286 34.353 1.000 13 .42

ANISOU 1844 CA ALA 269 1459 1405 2234 -208 -118 1 07

ATOM 1845 C ALA 269 4.182 10.729 33.252 1.000 13.93

ANISOU 1845 C ALA 269 1289 1538 2466 -168 -5 153

ATOM 1846 0 ALA 269 4.581 9.550 33.318 1.000 14.97

ANISOU 1846 0 ALA 269 1718 1476 2494 -143 112 8 6

ATOM 1847 CB ALA 269 1.806 11.051 34.008 1.000 13.76

ANISOU 1847 CB ALA 269 1300 1474 2454 -60 -61 12 3

ATOM 1848 N ASP 270 4.482 11.541 32.251 1.000 14.38

ANISOU 1848 N ASP 270 1688 1476 2300 -151 30 - 5

ATOM 1849 CA ASP 270 5.247 11.079 31.098 1.000 14.83

ANISOU 1849 CA ASP 270 1747 1693 2194 -99 -42 6 8

ATOM 1850 C ASP 270 6.749 11.287 31.227 1.000 15.68

ANISOU 1850 C ASP 270 1714 1886 2357 -224 143 8 6

ATOM 1851 0 ASP 270 7.483 11.008 30.255 1.000 17.12

ANISOU 1851 0 ASP 270 1952 2354 2200 -80 139 2 2 6

ATOM 1852 CB ASP 270 4.718 11.681 29.800 1.000 17.67

ANISOU 1852 CB ASP 270 2461 1966 2288 -75 -319 12 6

ATOM 1853 CG ASP 270 4.968 13.168 29.649 1.000 18.22

ANISOU 1853 CG ASP 270 2284 2024 2613 -88 -80 474

ATOM 1854 ODl . ASP 270 5.386 13.826 30.607 1.000 20.55

ANISOU 1854 ODl . ASP 270 3424 1541 2844 -47 -287 42 5

ATOM 1855 OD2 : ASP 270 4.646 13.698 28.552 1.000 23.06

ANISOU 1855 OD2 : ASP 270 3317 2727 2719 -49 -136 8 12

ATOM 1856 N PHE 271 7.221 11.668 32.413 1.000 13 .93

ANISOU 1856 N PHE 271 1556 1318 2417 97 31 4 1

ATOM 1857 CA PHE 271 8.671 11.723 32.644 1.000 14.41

ANISOU 1857 CA PHE 271 1624 1430 2423 110 29 2 63

ATOM 1858 C PHE 271 9.275 10.349 32.325 1.000 13 .31

ANISOU 1858 C PHE 271 1402 1430 2225 -30 28 218

ATOM 1859 0 PHE 271 8.790 9.340 32.870 1.000 14.91

ANISOU 1859 0 PHE 271 1900 1374 2392 -26 240 1 92

ATOM 1860 CB PHE 271 8.942 12.146 34.098 1.000 15.57

ANISOU 1860 CB PHE 271 1700 1721 2495 -66 -36 9

ATOM 1861 CG PHE 271 10.386 11.791 34.516 1.000 14.56 ANISOU 1861 CG PHE 271 1729 1320 2485 -152 34 - 124

ATOM 1862 CDI PHE 271 11.460 12.369 33.814 1.000 17. 76

ANISOU 1862 CDI PHE 271 1714 1581 3452 -235 393 - 2 < 4 9

ATOM 1863 CD2 PHE 271 10.698 10.972 35.570 1.000 18. 04

ANISOU 1863 CD2 PHE 271 2182 1543 3130 -95 -54Cι 17

ATOM 1864 CEl PHE 271 12.786 12.092 34.166 1.000 17. 54

ANISOU 1864 CEl PHE 271 1838 1700 3128 -291 114 - 5

ATOM 1865 CE2 PHE 271 11.997 10.609 35.899 1.000 18. 84

ANISOU 1865 CE2 PHE 271 1935 1646 3578 -392 -396i 42

ATOM 1866 CZ PHE 271 13.039 11.154 35.162 1.000 17. 25

ANISOU 1866 CZ PHE 271 2444 1697 2415 -486 -19 - 31 9 4

ATOM 1867 N THR 272 10.278 10.298 31.453 1.000 13. 78

ANISOU 1867 N THR 272 1514 1641 2083 30 19 154

ATOM 1868 CA THR 272 10.811 9.046 30.938 1.000 13. 99

ANISOU 1868 CA THR 272 1551 1660 2105 -99 83 6 ; 7

ATOM 1869 C THR 272 12.246 8.841 31.410 1.000 14. 71

ANISOU 1869 C THR 272 1598 1549 2441 -3 10, . 35 7

ATOM 1870 0 THR 272 13.046 9.808 31.424 1.000 16. 23

ANISOU 1870 0 THR 272 1646 1742 2780 -246 5 1 .8 5

ATOM 1871 CB THR 272 10.751 9.117 29.388 1.000 16. 27

ANISOU 1871 CB THR 272 1856 2205 2119 191 125 8

ATOM 1872 OGl THR 272 9.341 9.221 29.032 1.000 17. 99

ANISOU 1872 OGl THR 272 1996 2473 2368 64 -190 I > 64

ATOM 1873 CG2 THR 272 11.249 7.856 28.723 1.000 17. 94

ANISOU 1873 CG2 THR 272 2423 2167 2227 173 177 - 9

ATOM 1874 N PHE 273 12.567 7.600 31.743 1.000 14. 91

ANISOU 1874 N PHE 273 1644 1521 2499 92 238 21 8

ATOM 1875 CA PHE 273 13.894 7.253 32.254 1.000 15. 16

ANISOU 1875 CA PHE 273 1602 1813 2345 296 277 5 5

ATOM 1876 C PHE 273 14.350 5.899 31.724 1.000 14. 69

ANISOU 1876 C PHE 273 1408 1647 2528 24 479 17 8

ATOM 1877 0 PHE 273 13.541 5.086 31.262 1.000 15. 91

ANISOU 1877 0 PHE 273 1738 1767 2541 -115 450 11

ATOM 1878 CB PHE 273 13.899 7.301 33.769 1.000 15. 77

ANISOU 1878 CB PHE 273 1758 1921 2314 -344 286 12

ATOM 1879 CG PHE 273 12.931 6.336 34.424 1.000 14. 54

ANISOU 1879 CG PHE 273 1390 1726 2410 -95 -11 19

ATOM 1880 CDI PHE 273 11.601 6.743 34.655 1.000 16. 64

ANISOU 1880 CDI PHE 273 1457 2343 2521 -24 308 3 6

ATOM 1881 CD2 PHE 273 13.295 5.038 34.721 1.000 15. 23

ANISOU 1881 CD2 PHE 273 1863 1624 2300 -110 91 : 13 6

ATOM 1882 CEl PHE 273 10.719 5.848 35.259 1.000 16. 10

ANISOU 1882 CEl PHE 273 1593 2158 2365 -162 292 12

ATOM 1883 CΞ2 PHE 273 12.419 4.148 35.354 1.000 16. 01

ANISOU 1883 CE2 PHE 273 1904 1980 2198 -139 285 18

ATOM 1884 CZ PHE 273 11.109 4.559 35.548 1.000 15. 18

ANISOU 1884 CZ PHE 273 1843 2001 1925 -141 73 -22'

ATOM 1885 N SER 274 15.634 5.612 31.926 1.000 15. 31

ANISOU 1885 N SER 274 1559 1940 2317 361 383 2 4

ATOM 1886 CA SER 274 16.221 4.318 31.518 1.000 15. , 37

ANISOU 1886 CA SER 274 1476 1723 2642 32 557 1 E 5 6

ATOM 1887 C SER 274 15.953 3.284 32.588 1.000 14. .67

ANISOU 1887 C SER 274 973 1877 2726 -113 265 302

ATOM 1888 0 SER 274 16.310 3.476 33.770 1.000 15 , .98

ANISOU 18880 SER 274 1668 1677 2728 126 143 19

ATOM 1889 CB SER 274 17.742 4.556 31.356 1.000 17 .41

ANISOU 1889 CB SER 274 1487 2019 3112 235 945 72

ATOM 1890 OG SER 274 18.362 3.280 31.334 1.000 18 .03

ANISOU 1890 OG SER 274 1839 1961 3052 293 840 l ε

ATOM 1891 N VAL 275 15.395 2.133 32.182 1.000 15 .58

ANISOU 1891 N VAL 275 1646 1857 2417 -182 461 2 i 6 1 ATOM 1892 CA VAL 275 15.158 1.033 33.137 1.000 15.65

ANISOU 1892 CA VAL 275 1681 1800 2466 -180 261 2 6 S

ATOM 1893 C VAL 275 16.454 0.445 33.659 1.000 15. 33

ANISOU 1893 C VAL 275 1805 1881 2139 116 392 4 D

ATOM 1894 O VAL 275 16.623 0.280 34.871 1.000 15. 68

ANISOU 1894 O VAL 275 2037 1655 2267 6 297 19 6

ATOM 1895 CB VAL 275 14.227 -0.004 32.483 1.000 16. 05

ANISOU 1895 CB VAL 275 1635 1708 2755 -76 405 2

ATOM 1896 CGI VAL 275 14.080 -1.186 33.426 1.000 17.04

ANISOU 1896 CGI VAL 275 2045 1688 2740 -211 230 1

ATOM 1897 CG2 VAL 275 12.847 0.608 32.203 1.000 18.45

ANISOU 1897 CG2 VAL 275 1650 2432 2928 -57 135 2 69

ATOM 1898 N PRO 276 17.437 0.093 32.844 1.000 16.21

ANISOU 1898 N PRO 276 1927 1700 2532 97 589 3 .

ATOM 1899 CA PRO 276 18.707 -0.434 33.399 1.000 1 8.10

ANISOU 1899 CA PRO 276 1736 2115 3025 147 616 9 3

ATOM 1900 C PRO 276 19.382 0.541 34.321 1.000 17. 52

ANISOU 1900 C PRO 276 1998 1961 2697 97 469 239

ATOM 1901 O PRO 276 19.963 0.171 35.348 1.000 19.66

ANISOU 1901 O PRO 276 2015 2409 3047 24 280 46

ATOM 1902 CB PRO 276 19.590 -0.796 32.214 1.000 20. 80

ANISOU 1902 CB PRO 276 2094 2687 3121 306 771 249

ATOM 1903 CG PRO 276 18.852 -0.390 30.999 1.000 21 57

ANISOU 1903 CG PRO 276 2051 3098 3046 340 802 288

ATOM 1904 CD PRO 276 17.446 -0.021 31.368 1.000 1 8.17

ANISOU 1904 CD PRO 276 2053 2306 2546 179 832 31

ATOM 1905 N LEU 277 19.325 1.845 34.027 1.000 17. 09

ANISOU 1905 N LEU 277 1571 1898 3025 230 511 1 07

ATOM 1906 CA LEU 277 19.962 2.802 34.940 1.000 19. 34

ANISOU 1906 CA LEU 277 2035 2141 3171 -219 218 2 62

ATOM 1907 C LEU 277 19.214 2.858 36.249 1.000 18. 34

ANISOU 1907 C LEU 277 1963 1958 3049 -33 -3 ^• 3

ATOM 1908 O LEU 277 19.815 2.957 37.319 1.000 19. 29

ANISOU 1908 O LEU 277 2466 1710 3154 -271 -18

ATOM 1909 CB LEU 277 20.094 4.178 34.291 1.000 21 41

ANISOU 1909 CB LEU 277 2739 2011 3383 14 12 2 87

ATOM 1910 CG LEU 277 20.910 5.192 35.111 1.000 26.34

ANISOU 1910 CG LEU 277 3662 2367 3978 -980 -547 9 44

ATOM 1911 CDI LEU 277 22.396 4.839 35.069 1.000 38.04

ANISOU 1911 CDI LEU 277 3764 3171 7518 -487 -2057 53

ATOM 1912 CD2 LEU 277 20.708 6.607 34.631 1.000 31. 98

ANISOU 1912 CD2 LEU 277 4023 2018 6109 -366 508 7 3 2

ATOM 1913 N ALA 278 17.875 2.711 36.202 1.000 17.30

ANISOU 1913 N ALA 278 2015 1766 2793 74 218 115

ATOM 1914 CA ALA 278 17.124 2.712 37.464 1.000 16.75

ANISOU 1914 CA ALA 278 2200 1566 2600 216 146

ATOM 1915 C ALA 278 17.575 1.523 38.313 1.000 16. 31

ANISOU 1915 C ALA 278 1849 1553 2794 -337 196 1 07

ATOM 1916 O ALA 278 17.718 1.635 39.523 1.000 17. 26

ANISOU 1916 O ALA 278 1963 1839 2754 -62 -53 2 0 5

ATOM 1917 CB ALA 278 15.642 2.622 37.177 1.000 17. 55

ANISOU 1917 CB ALA 278 2109 1880 2679 295 195 - 1 1

ATOM 1918 N ARG 279 17.724 0.362 37.696 1.000 17 .07

ANISOU 1918 N ARG 279 2322 1399 2766 -178 26 308

ATOM 1919 CA ARG 279 18.099 -0.829 38.473 1.000 16.93

ANISOU 1919 CA ARG 279 2377 1734 2323 15 -241 203

ATOM 1920 C ARG 279 19.477 -0.587 39.098 1.000 19.87

ANISOU 1920 C ARG 279 2491 2292 2766 -487 -384 54

ATOM 1921 O ARG 279 19.687 -0.974 40.234 1.000 33.04

ANISOU 1921 O ARG 279 3615 4823 4115 -1726 -1700 2 603

ATOM 1922 CB ARG 279 18.164 -2.042 37.517 1.000 20.04 ANISOU 1922 CB ARG 279 2042 1609 3964 108 -221 - 305

ATOM 1923 CG ARG 279 16.742 -2.491 37.179 1.000 20.73

ANISOU 1923 CG ARG 279 2152 2728 2997 -93 -401 - 351

ATOM 1924 CD ARG 279 16.601 -3.422 35.990 1.000 24.81

ANISOL- 1924 CD ARG 279 3213 2982 3231 -1 -507 - 609

ATOM 1925 NE ARG 279 17.575 -4.484 36.195 1.000 27.50

ANISOU 1925 NE ARG 279 4331 2656 3463 355 -146 - 181

ATOM 1926 CZ ARG 279 17.301 -5.725 36.620 1.000 41.33

ANISOL- 1926 CZ ARG 279 7720 2466 5519 -186 -454 - 142

ATOM 1927 NHl ARG 279 16.024 -6.012 36.866 1.000 40.58

ANISOU 1927 NHl ARG 279 8821 3012 3585 -1564 507 4 5 2

ATOM 1928 NH2 ARG 279 18.200 -6.688 36.807 1.000 53.27

ANISOU 1928 NH2 ARG 279 9516 2227 8496 -127 -4607 - 463

ATOM 1929 N GLU 280 20.390 0.119 38.424 1.000 19.68

ANISOU 1929 N GLU 280 2172 2276 3028 84 324 13 6

ATOM 1930 CA GLU 280 21.748 0.334 38.948 1.000 20.28

ANISOU 1930 CA GLU 280 2046 2274 3385 25 581 115

ATOM 1931 C GLU 280 21.705 1.257 40.182 1.000 20.67

ANISOU 1931 C GLU 280 2334 1968 3552 -281 285 2 0

ATOM 1932 0 GLU 280 22.723 1.079 40.908 1.000 26.81

ANISOU 1932 0 GLU 280 2659 3419 4107 -37 -183 - 8 7

ATOM 1933 CB GLU 280 22.651 1.029 37.926 1.000 24.69

ANISOU 1933 CB GLU 280 2778 2558 4044 -351 1022 3 03

ATOM 1934 CG GLU 280 22.997 0.342 36.634 1.000 27.13

ANISOU 1934 CG GLU 280 2605 4888 2816 596 116 62 3

ATOM 1935 CD GLU 280 23.815 1.298 35.760 1.000 43 .10

ANISOU 1935 CD GLU 280 4693 7780 3903 -1328 1206 83 4

ATOM 1936 OEl GLU 280 24.541 2.171 36.296 1.000 41.36

ANISOU 1936 OEl GLU 280 2666 6033 7015 27 1099 69 0

ATOM 1937 OE2 GLU 280 23.727 1.219 34.520 1.000 64.81

ANISOU 1937 OE2 GLU 280 10844 10028 3751 -2356 1104 2134

ATOM 1938 N CYS 281 20.777 2.156 40.313 1.000 21.61

ANISOU 1938 N CYS 281 2372 2240 3599 -211 532 - 238

ATOM 1939 CA CYS 281 20.481 3.164 41.337 1.000 24.33

ANISOU 1939 CA CYS 281 2114 2911 4219 -526 1121 - 817

ATOM 1940 C CYS 281 19.858 2.568 42.585 1.000 27.11

ANISOU 1940 C CYS 281 2492 3261 4546 -1608 1457 -1343

ATOM 1941 0 CYS 281 19.789 3.161 43.685 1.000 19.19

ANISOU 1941 0 CYS 281 1997 2012 3282 -250 -326 13 5

ATOM 1942 CB CYS 281 19.632 4.438 40.795 1.000 22.02

ANISOU 1942 CB CYS 281 1214 3088 4063 -286 100 -2108

ATOM 1943 SG CYS 281 20.639 5.092 39.444 1.000 53.41

ANISOU 1943 SG CYS 281 10822 4742 4730 -3261 1316 4 5

ATOM 1944 N GLY 282 19.370 1.317 42.565 1.000 18.81

ANISOU 1944 N GLY 282 1230 2224 3695 3 -149 - 206

ATOM 1945 CA GLY 282 18.675 0.750 43.744 1.000 17.07

ANISOU 1945 CA GLY 282 1544 1771 3171 31 -552 - 168

ATOM 1946 C GLY 282 17.194 0.496 43.538 1.000 14.91

ANISOU 1946 C GLY 282 1601 1645 2417 -135 -453 3 7 8

ATOM 1947 0 GLY 282 16.480 -0.062 44.380 1.000 16.38

ANISOU 1947 0 GLY 282 1998 1921 2306 -211 -399 3 6 0

ATOM 1948 N PHE 283 16.625 0.919 42.404 1.000 13 .44

ANISOU 1948 N PHE 283 1563 1539 2006 -189 -336 - 115

ATOM 1949 CA PHE 283 15.173 0.829 42.203 1.000 14.52

ANISOU 1949 CA PHE 283 1677 1410 2428 -187 -670 4 6

ATOM 1950 C PHE 283 14.810 -0.604 41.809 1.000 13.08

ANISOU 1950 C PHE 283 1519 1314 2137 -121 -338 17 4

ATOM 1951 O PHE 283 15.311 -1.184 40.837 1.000 14.11

ANISOU 1951 O PHE 283 1366 1418 2578 -142 -78 1 7

ATOM 1952 CB PHE 283 14.749 1.800 41.078 1.000 13 .76

ANISOU 1952 CB PHE 283 1814 1288 2125 -39 -268 0 ATOM 1953 CG PHE 283 14.842 3.269 41.512 1.000 14.75

ANISOU 1953 CG PHE 283 1985 1363 2255 12 -317 - 3

ATOM 1954 CDI PHE 283 13.814 3.904 42.142 1.000 21.50

ANISOU 1954 CDI PHE 283 2318 1759 4091 303 -23 - 626

ATOM 1955 CD2 PHE 283 15.994 3.999 41.298 1.000 17.72

ANISOU 1955 CD2 PHE 283 2526 1244 2963 -307 -89 2 72

ATOM 1956 CEl PHE 283 13.909 5.177 42.655 1.000 20.78

ANISOU 1956 CEl PHE 283 2056 1802 4036 92 66 - 647

ATOM 1957 CE2 PHE 283 16.115 5.290 41.814 1.000 15.06

ANISOU 1957 CE2 PHE 283 2101 1257 2364 -5 -255 3 77

ATOM 1958 CZ PHE 283 15.084 5.891 42.506 1.000 18.04

ANISOU 1958 CZ PHE 283 1881 1995 2979 192 -432 2 0

ATOM 1959 N ASP 284 13.883 -1.178 42.579 1.000 13.07

ANISOU 1959 N ASP 284 1549 1366 2049 -73 -331 1 17

ATOM 1960 CA ASP 284 13.502 -2.584 42.395 1.000 12.80

ANISOU 1960 CA ASP 284 1481 1460 1924 -231 -207 1 5 7

ATOM 1961 C ASP 284 12.335 -2.654 41.421 1.000 12 .88

ANISOU 1961 C ASP 284 1493 1508 1891 -19 -180 - 5 5

ATOM 1962 0 ASP 284 11.231 -3.147 41.741 1.000 13 .69

ANISOU 1962 0 ASP 284 1407 1351 2442 -93 -281 9 2

ATOM 1963 CB ASP 284 13.141 -3.203 43.744 1.000 14.10

ANISOU 1963 CB ASP 284 1966 1534 1858 -40 -11 145

ATOM 1964 CG ASP 284 13.165 -4.730 43.717 1.000 14.49

ANISOU 1964 CG ASP 284 1906 1520 2079 47 -424 2 9 0

ATOM 1965 ODl ASP 284 13.732 -5.305 42.758 1.000 14.81

ANISOU 1965 ODl ASP 284 2036 1343 2250 -152 -166 2 3 1

ATOM 1966 OD2 ASP 284 12.652 -5.310 44.696 1.000 15.32

ANISOU 1966 OD2 ASP 284 1979 1557 2286 -79 -109 15 3

ATOM 1967 N VAL 285 12.644 -2.191 40.217 1.000 12.40

ANISOU 1967 N VAL 285 1582 1260 1870 79 -185 - 131

ATOM 1968 CA VAL 285 11.599 -2.064 39.216 1.000 12.31

ANISOU 1968 CA VAL 285 1442 1469 1767 -161 -59 - 1

ATOM 1969 C VAL 285 11.229 -3.419 38.589 1.000 12.09

ANISOU 1969 C VAL 285 1220 1407 1967 -1 -100 - 79

ATOM 1970 0 VAL 285 12.085 -4.311 38.433 1.000 13.68

ANISOU 19700 VAL 285 1237 1514 2446 67 56 4 0

ATOM 1971 CB VAL 285 12.009 -1.066 38.098 1.000 14.68

ANISOU 1971 CB VAL 285 1943 1621 2014 -163 -50 2 5 9

ATOM 1972 CGI VAL 285 12.131 0.332 38.672 1.000 17.08

ANISOU 1972 CGI VAL 285 2429 1402 2658 18 -465 42 5

ATOM 1973 CG2 VAL 285 13.309 -1.499 37.433 1.000 15.69

ANISOU 1973 CG2 VAL 285 2131 2180 1649 -316 161 3 0 6

ATOM 1974 N SER 286 9.952 -3.541 38.241 1.000 12.24

ANISOU 1974 N SER 286 1263 1440 1946 -12 -148 - 117

ATOM 1975 CA SER 286 9.398 -4.669 37.495 1.000 12 .84

ANISOU 1975 CA SER 286 1571 1463 1845 -356 -30 1 4

ATOM 1976 C SER 286 8.861 -4.118 36.172 1.000 11.99

ANISOU 1976 C SER 286 1516 1374 1666 -28 60 - 198

ATOM 1977 0 SER 286 7.654 -4.110 35.917 1.000 15.68

ANISOU 1977 0 SER 286 1514 2384 2059 2 18 - 2 0

ATOM 1978 CB SER 286 8.301 -5.327 38.300 1.000 12.54

ANISOU 1978 CB SER 286 1407 1442 1915 -59 170 - 55

ATOM 1979 OG SER 286 7.415 -4.380 38.890 1.000 13 .15

ANISOU 1979 OG SER 286 1531 1430 2034 105 -73 - 5 9

ATOM 1980 N LEU 287 9.769 -3.649 35.333 1.000 13 .56

ANISOU 1980 N LEU 287 1574 1521 2058 41 133 177

ATOM 1981 CA LEU 287 9.451 -2.932 34.101 1.000 13 .48

ANISOU 1981 CA LEU 287 1812 1418 1891 -84 116 1 7

ATOM 1982 C LEU 287 10.075 -3.654 32.908 1.000 15.12

ANISOU 1982 C LEU 287 1945 1714 2086 32 233 - 3 1

ATOM 1983 O LEU 287 11.277 -3.883 32.927 1.000 17.91 -.

-78-

ANISOU 1983 0 LEU 287 1885 2275 2645 109 300 - 27

ATOM 1984 CB LEU 287 9.954 -1.480 34.118 1.000 14.37

ANISOU 1984 CB LEU 287 1773 1380 2306 -34 24S 10 .

ATOM 1985 CG LEU 287 9.362 -0.603 35.231 1.000 14.32

ANISOU 1985 CG LEU 287 1421 1496 2523 62 52 -158

ATOM 1986 CDI LEU 287 10.143 0.705 35.413 1.000 14.53

ANISOU 1986 CDI LEU 287 1672 1444 2403 0 -146 143

ATOM 1987 CD2 LEU 287 7.921 -0.197 34.820 1.000 16.03

ANISOU 1987 CD2 LEU 287 1476 2035 2579 166 -100 - 7

ATOM 1988 N ASP 288 9.256 -4.060 31.958 1.000 15.09

ANISOU 1988 N ASP 288 2041 1611 2081 73 17Ei -216

ATOM 1989 CA ASP 288 9.764 -4.722 30.757 1.000 16.55

ANISOU 1989 CA ASP 288 1992 2028 2268 29 33Ei -314

ATOM 1990 C ASP 288 10.437 -3.682 29.874 1.000 18.74

ANISOU 1990 C ASP 288 2484 2597 2040 -231 97 8 1

ATOM 1991 0 ASP 288 9.998 -2.526 29.849 1.000 25.48

ANISOU 1991 0 ASP 288 3382 2433 3865 -322 639 34 f

ATOM 1992 CB ASP 288 8.659 -5.490 30.060 1.000 19.23

ANISOL- 1992 CB ASP 288 2431 2414 2460 -209 258 - 72

ATOM 1993 CG ASP 288 9.139 -6.468 29.000 1.000 19.50

ANISOU 1993 CG ASP 288 2688 2223 2499 -49 393 - 5 E

ATOM 1994 ODl ASP 288 10.173 -7.145 29.185 1.000 27.03

ANISOU 1994 ODl ASP 288 3134 3038 4100 624 427 - 71

ATOM 1995 OD2 ASP 288 8.458 -6.566 27.955 1.000 31.00

ANISOU 1995 OD2 ASP 288 3596 4859 3325 307 -361 -21 0 0

ATOM 1996 N GLY 289 11.489 -4.035 29.137 1.000 22.68

ANISOU 1996 N GLY 289 2960 2893 2765 -531 778 11

ATOM 1997 CA GLY 289 12.008 -3.083 28.169 1.000 25.60

ANISOU 1997 CA GLY 289 3678 3562 2486 -1469 558 1 1

ATOM 1998 C GLY 289 12.988 -2.078 28.725 1.000 21.08

ANISOU 1998 C GLY 289 2567 2916 2528 -485 353 15

ATOM 1999 0 GLY 289 13.411 -2.097 29.891 1.000 23.72

ANISOU 1999 0 GLY 289 3428 3219 2364 -1104 440 11

ATOM 2000 N GLU 290 13.402 -1.168 27.818 1.000 18.32

ANISOU 2000 N GLU 290 2246 2396 2319 -145 616 - 1 f 1 5

ATOM 2001 CA GLU 290 14.538 -0.301 28.074 1.000 17.75

ANISOU 2001 CA GLU 290 1912 2419 2412 97 770 - 367

ATOM 2002 C GLU 290 14.261 1.058 28.696 1.000 17.90

ANISOU 2002 C GLU 290 2180 2308 2313 50 711 - 297

ATOM 2003 O GLU 290 15.143 1.619 29.353 1.000 17.58

ANISOU 2003 O GLU 290 2525 2050 2104 -35 380 16

ATOM 2004 CB GLU 290 15.341 -0.161 26.785 1.000 23.21

ANISOU 2004 CB GLU 290 3184 2508 3126 -273 1753 - 4 ⁽ 6 7

ATOM 2005 CG GLU 290 15.833 -1.492 26.226 1.000 24.55

ANISOU 2005 CG GLU 290 3609 2992 2725 348 1232 - 7 - 4 3

ATOM 2006 CD GLU 290 16.676 -2.280 27.221 1.000 30.03

ANISOU 2006 CD GLU 290 3365 3708 4337 476 753 - 2 : 1 1

ATOM 2007 OEl . GLU 290 17.492 -1.684 27.947 1.000 40.04

ANISOU 2007 OEl . GLU 290 5043 6674 3498 525 36 -122

ATOM 2008 OE2 : GLU 290 16.622 -3.527 27.237 1.000 51.76

ANISOU 2008 OE2 ! GLU 290 8785 3812 7070 -12 -483 15 8 3

ATOM 2009 N THR 291 13.064 1.578 28.486 1.000 18.14

ANISOU 2009 N THR 291 2305 2486 2103 224 711 - 3 2 1

ATOM 2010 CA THR 291 12.697 2.896 29.049 1.000 18.72

ANISOU 2010 CA THR 291 2521 2080 2511 105 1131 6 6

ATOM 2011 C THR 291 11.278 2.744 29.593 1.000 15.79

ANISOU 2011 C THR 291 2178 1758 2064 134 538 - 5

ATOM 2012 O THR 291 10.517 1.834 29.217 1.000 18.62

ANISOU 2012 O THR 291 2764 1966 2344 -248 664 - 3 1 1

ATOM 2013 CB THR 291 12.722 4.031 28.044 ; 1.000 21.54

ANISOU 2013 CB THR 291 3043 2625 2516 -164 891 36

SUBSTΓΓUTE SHEET (RULE 26) ATOM 2014 OGl THR 291 11.695 3.862 27.077 1.000 25.98

ANISOU 2014 OGl THR 291 3160 4072 2641 -86 703 5 0

ATOM 2015 CG2 THR 291 14.048 4.115 27.292 1.000 24. 20

ANISOU 2015 CG2 THR 291 3199 3832 2164 -445 930 5 3

ATOM 2016 N ALA 292 10.959 3.658 30.492 1.000 14. 84

ANISOU 2016 N ALA 292 1637 1656 2347 200 429 - 1 : 5 3

ATOM 2017 CA ALA 292 9.675 3.657 31.179 1.000 13. 84

ANISOU 2017 C ALA 292 1488 1477 2294 170 299 7 8

ATOM 2018 C ALA 292 9.356 5.065 31.619 1.000 12. 65

ANISOU 2018 C ALA 292 1334 1564 1908 60 144 - 139

ATOM 2019 O ALA 292 10.228 5.939 31.710 1.000 14. 27

ANISOU 2019 O ALA 292 1529 1596 2295 -35 109 1 1

ATOM 2020 CB ALA 292 9.670 2.754 32.414 1.000 14. 02

ANISOU 2020 CB ALA 292 1693 1580 2053 37 22 - 27

ATOM 2021 N THR 293 8.054 5.258 31.916 1.000 13. 54

ANISOU 2021 N THR 293 1468 1617 2058 117 373 - i :

ATOM 2022 CA THR 293 7.605 6.546 32.424 1.000 13. 40

ANISOU 2022 CA THR 293 1565 1647 1877 152 209 - 2 : 3 2

ATOM 2023 C THR 293 7.407 6.482 33.952 1.000 12. 09

ANISOU 2023 C THR 293 1345 1322 1927 -62 326 - 1

ATOM 2024 O THR 293 7.214 5.441 34.555 1.000 12. 93

ANISOU 2024 O THR 293 1385 1356 2170 -190 194 9 0

ATOM 2025 CB THR 293 6.295 7.058 31.788 1.000 13. 45

ANISOU 2025 CB THR 293 1598 1579 1935 95 345 34 5

ATOM 2026 OGl THR 293 5.273 6.112 32.117 1.000 13. 75

ANISOU 2026 OGl THR 293 1672 1570 1981 -12 314 13

ATOM 2027 CG2 THR 293 6.476 7.139 30.272 1.000 15. 93

ANISOU 2027 CG2 THR 293 2121 2022 1911 255 434 3 3

ATOM 2028 N PHE 294 7.241 7.661 34.544 1.000 12. 81

ANISOU 2028 N PHE 294 1607 1440 1822 -83 149 - 1 5 1

ATOM 2029 CA PHE 294 6.857 7.773 35.935 1.000 12. 37

ANISOU 2029 CA PHE 294 1332 1469 1899 -267 166 - - 22 8 9

ATOM 2030 C PHE 294 5.556 7.022 36.184 1.000 12. 36

ANISOU 2030 C PHE 294 1336 1361 1999 -151 30 ^■ - 3 6

ATOM 2031 O PHE 294 5.403 6.253 37.143 1.000 13. 27

ANISOU 2031 O PHE 294 1556 1410 2076 -191 183 4 6

ATOM 2032 CB PHE 294 6.698 9.271 36.267 1.000 13. 83

ANISOU 2032 CB PHE 294 2039 1351 1866 -192 -29 - 1 7 7

ATOM 2033 CG PHE 294 6.306 9.488 37.711 1.000 13. 10

ANISOU 2033 CG PHE 294 1786 1216 1974 -125 -63 - 2 4 4

ATOM 2034 CDI PHE 294 7.207 9.411 38.749 1.000 17. 41

ANISOU 2034 CDI PHE 294 2132 2533 1952 -1012 -287 7 .

ATOM 2035 CD2 PHE 294 4.964 9.739 38.026 1.000 18. 41

ANISOU 2035 CD2 PHE 294 2156 2263 2575 565 332 5

ATOM 2036 CEl PHE 294 6.810 9.608 40.054 1.000 17. , 72

ANISOU 2036 CEl PHE 294 2348 2296 2086 -308 -362 - 1 3 6

ATOM 2037 CE2 PHE 294 4.591 10.010 39.324 1.000 19. .37

ANISOU 2037 CE2 PHE 294 2078 2541 2740 330 232 - 6 3 0

ATOM 2038 CZ PHE 294 5.507 9.956 40.355 1.000 18. .36

ANISOU 2038 CZ PHE 294 2443 1678 2855 -394 -55 - 2 4 5

ATOM 2039 N GLN 295 4.588 7.205 35.246 1.000 12 .59

ANISOU 2039 N GLN 295 1248 1429 2106 -62 38 -16

ATOM 2040 CA GLN 295 3.320 6.484 35.408 1.000 12 .76

ANISOU 2040 CA GLN 295 1266 1215 2365 7 -157 -11

ATOM 2041 C GLN 295 3.512 4.984 35.318 1.000 12 .24

ANISOU 2041 C GLN 295 1449 1256 1944 10 1 - 7 3

ATOM 2042 O GLN 295 2.922 4.238 36.101 1.000 13 .61

ANISOU 2042 O GLN 295 1323 1427 2424 7 85 15 5

ATOM 2043 CB GLN 295 2.375 6.975 34.317 1.000 14 .31

ANISOU 2043 CB GLN 295 1227 1594 2616 81 -133 192

ATOM 2044 CG GLN 295 1.062 6.256 34.249 1.000 14 .03 ANISOU 2044 CG GLN 295 1391 1509 2430 -59 -300 4 7

ATOM 2045 CD GLN 295 0.157 5.687 33.115 1.000 13 .56

ANISOU 2045 CD GLN 295 1305 1486 2361 133 -117 1 65

ATOM 2046 OEl GLN 295 0.459 7.693 32.419 1.000 15.35

ANISOU 2046 OEl GLN 295 1811 1651 2371 161 206 2 2 0

ATOM 2047 NE2 GLN 295 -0.982 6.026 32.943 1.000 15.04

ANISOU 2047 NE2 GLN 295 1225 1995 2493 75 -139 - 9 9

ATOM 2048 N ASP 296 4.363 4.463 34.423 1.000 12 .66

ANISOU 2048 N ASP 296 1425 1396 1990 181 -112 - 110

ATOM 2049 CA ASP 296 4.653 3.016 34.439 1.000 12 .26

ANISOU 2049 CA ASP 296 1628 1274 1755 53 -51 - 151

ATOM 2050 C ASP 296 5.167 2.569 35.792 1.000 11.57

ANISOU 2050 C ASP 296 1199 1300 1895 -82 30 - 2 2

ATOM 2051 O ASP 296 4.854 1.460 36.224 1.000 13 .08

ANI SOL- 2051 O ASP 296 1534 1368 2070 -107 38 13 9

ATOM 2052 CB ASP 296 5.709 2.634 33.399 1.000 14.18

ANISOU 2052 CB ASP 296 1870 1700 1819 141 30 - 378

ATOM 2053 CG ASP 296 5.295 2.848 31.952 1.000 13.32

ANISOU 2053 CG ASP 296 1655 1557 1848 -58 67 2

ATOM 2054 ODl ASP 296 4.110 2.725 31.601 1.000 15.83

ANISOU 2054 ODl ASP 296 1680 1935 2402 -68 -126 - 189

ATOM 2055 OD2 ASP 296 6.212 3.098 31.114 1.000 15.27

ANISOU 2055 OD2 ASP 296 1757 1937 2106 -229 137 17 7

ATOM 2056 N TRP 297 6.038 3.352 36.416 1.000 12 .26

ANISOU 2056 N TRP 297 1325 1403 1931 -34 -123 - 118

ATOM 2057 CA TRP 297 6.683 2.960 37.656 1.000 12.82

ANISOU 2057 CA TRP 297 1328 1599 1943 -104 -49 151

ATOM 2058 C TRP 297 5.746 3.007 38.858 1.000 13.13

ANISOU 2058 C TRP 297 1418 1580 1992 24 -23 18 5

ATOM 2059 O TRP 297 5.565 2.030 39.584 1.000 14.03

ANISOU 2059 O TRP 297 1554 1619 2159 102 137 3 2 0

ATOM 2060 CB TRP 297 7.908 3.847 37.928 1.000 13.68

ANISOU 2060 CB TRP 297 1130 1692 2376 -19 -169 151

ATOM 2061 CG TRP 297 8.646 3.455 39.166 1.000 13.28

ANISOU 2061 CG TRP 297 1143 1646 2255 91 -96 2 2

ATOM 2062 CDI TRP 297 8.932 2.179 39.622 1.000 15.58

ANISOU 2062 CDI TRP 297 1615 1689 2618 275 -544 - 77

ATOM 2063 CD2 TRP 297 9.144 4.353 40.189 1.000 14.69

ANISOU 2063 CD2 TRP 297 1327 1693 2562 -117 -219 5

ATOM 2064 NE1 TRP 297 9.583 2.265 40.840 1.000 15.34

ANISOU 2064 NE1 TRP 297 1378 1853 2598 70 -494 7 5

ATOM 2065 CE2 TRP 297 9.724 3.597 41.203 1.000 16.13

ANISOU 2065 CE2 TRP 297 1241 2009 2880 182 -676 - 196

ATOM 2066 CE3 TRP 297 9.094 5.756 40.284 1.000 22.13

ANISOU 2066 CE3 TRP 297 3040 1658 3712 -665 -1408 12 9

ATOM 2067 CZ2 TRP 297 10.318 4.180 42.316 1.000 18.45

ANISOU 2067 CZ2 TRP 297 2204 2387 2418 44 -326 - 331

ATOM 2068 CZ3 TRP 297 9.670 6.353 41.399 1.000 21.55

ANISOU 2068 CZ3 TRP 297 2916 2104 3167 -55 -752 - 458

ATOM 2069 CH2 TRP 297 10.258 5.546 42.397 1.000 23.53

ANISOU 2069 CH2 TRP 297 3298 2356 3285 -320 -1146 - 344

ATOM 2070 N ILE 298 5.106 4.167 39.044 1.000 13 .58

ANISOU 2070 N ILE 298 1324 1726 2108 241 -167 127

ATOM 2071 CA ILE 298 4.299 4.440 40.229 1.000 14.68

ANISOU 2071 CA ILE 298 1413 2177 1986 -13 -161 - 208

ATOM 2072 C ILE 298 2.841 4.054 40.121 1.000 12 .02

ANISOU 2072 C ILE 298 1455 1300 1813 56 -239 4 02

ATOM 2073 O ILE 298 2.182 3.782 41.147 1.000 13 .67

ANISOU 2073 O ILE 298 1732 1582 1881 -23 -4 193

ATOM 2074 CB ILE 298 4.428 5.914 40.673 1.000 19.45

ANISOU 2074 CB ILE 298 2261 2446 2683 -699 237 - 835 ATOM 2075 CGI ILE 298 5.907 6.245 41.001 1.000 27.83

ANISOU 2075 CGI ILE 298 2776 4275 3525 -1314 -556 - 1030

ATOM 2076 CG2 ILE 298 3.679 6.319 41.929 1.000 25.05

ANISOU 2076 CG2 ILE 298 3770 3344 2405 -57 255 - 983

ATOM 2077 CDI ILE 298 6.368 5.628 42.306 1.000 43 .32

ANISOU 2077 CDI ILE 298 4561 7224 4674 -652 -1890 - 117

ATOM 2078 N GLY 299 2.317 3.980 38.893 1.000 12 .16

ANISOU 2078 N GLY 299 1432 1308 1879 78 -304 1 0 6

ATOM 2079 CA GLY 299 0.918 3.741 38.670 1.000 12.98

ANISOU 2079 CA GLY 299 1276 1279 2379 106 -188 - 154

ATOM 2080 C GLY 299 0.135 5.017 38.378 1.000 13 .09

ANISOU 2080 C GLY 299 1421 1403 2151 113 -231 1 1 8

ATOM 2081 O GLY 299 0.738 6.025 38.017 1.000 14.00

ANISOU 2081 O GLY 299 1713 1353 2252 122 289 - 13

ATOM 2082 N GLY 300 -1.183 4.917 38.447 1.000 13 .08

ANISOU 2082 N GLY 300 1325 1545 2099 146 -267 - 145

ATOM 2083 CA GLY 300 -2.075 5.966 37.992 1.000 13 .45

ANISOU 2083 CA GLY 300 1447 1521 2143 116 -415 - 143

ATOM 2084 C GLY 300 -2.519 6.972 39.042 1.000 12.94

ANISOU 2084 C GLY 300 1098 1365 2456 -52 -407 - 192

ATOM 2085 O GLY 300 -3.262 7.875 38.672 1.000 13 .39

ANISOU 2085 O GLY 300 1321 1342 2423 -19 -217 - 45

ATOM 2086 N ASN 301 -1.973 6.845 40.254 1.000 13 .35

ANISOU 2086 N ASN 301 1494 1429 2151 -225 -232 - 104

ATOM 2087 CA ASN 301 -2.162 7.842 41.313 1.000 13.83

ANISOU 2087 CA ASN 301 1590 1435 2230 -194 -38 - 61

ATOM 2088 C ASN 301 -0.837 8.254 41.885 1.000 12 .46

ANISOU 2088 C ASN 301 1676 1268 1791 -35 -142 - 2 0

ATOM 2089 O ASN 301 -0.007 7.405 42.169 1.000 13.89

ANISOU 2089 O ASN 301 1831 1355 2093 73 -144 - 13

ATOM 2090 CB ASN 301 -3.075 7.238 42.360 1.000 16.01

ANISOU 2090 CB ASN 301 1632 1909 2542 77 224 3 15

ATOM 2091 CG ASN 301 -3.942 8.199 43.106 1.000 18.23

ANISOU 2091 CG ASN 301 1986 2508 2435 190 152 - 9 0

ATOM 2092 ODl ASN 301 -4.973 8.690 42.614 1.000 17.44

ANISOU 2092 ODl ASN 301 1606 1626 3394 -21 144 -190

ATOM 2093 ND2 ASN 301 -3.518 8.454 44.338 1.000 33.30

ANISOU 2093 ND2 ASN 301 2804 6923 2928 1012 -230 - 1523

ATOM 2094 N TYR 302 -0.595 9.564 42.073 1.000 12.96

ANISOU 2094 N TYR 302 1662 1278 1985 -69 -21 - 135

ATOM 2095 CA TYR 302 0.674 9.948 42.702 1.000 13 .48

ANISOU 2095 CA TYR 302 1673 1259 2192 -130 -132 3 4

ATOM 2096 C TYR 302 0.768 9.269 44.078 1.000 12.63

ANISOU 2096 C TYR 302 1413 1293 2092 53 44 1 9

ATOM 2097 O TYR 302 -0.218 9.151 44.806 1.000 14.15

ANISOU 2097 O TYR 302 1332 1737 2305 -65 48 - 27

ATOM 2098 CB TYR 302 0.764 11.472 42.916 1.000 13.30

ANISOU 2098 CB TYR 302 1635 1192 2226 -81 33 4 1

ATOM 2099 CG TYR 302 1.159 12.143 41.619 1.000 12 .02

ANISOU 2099 CG TYR 302 1586 1103 1880 -59 -25 - 271

ATOM 2100 CDI . TYR 302 2.501 12.233 41.275 1.000 13 .11

ANISOU 2100 CDI . TYR 302 1633 1284 2066 -80 11 - 18

ATOM 2101 CD2 : TYR 302 0.235 12.709 40.739 1.000 12.52

ANISOU 2101 CD2 : TYR 302 1576 1132 2049 -44 13 - 127

ATOM 2102 CEl . TYR 302 2.933 12.822 40.119 1.000 12.29

ANISOU 2102 CEl . TYR 302 1581 1043 2045 -185 -84 - 77

ATOM 2103 CE2 ! TYR 302 0.637 13.273 39.535 1.000 14.12

ANISOU 2103 CE2 ! TYR 302 1462 1443 2458 -241 15 3 2 5

ATOM 2104 CZ TYR 302 1.983 13.347 39.241 1.000 12.69

ANISOU 2104 CZ TYR 302 1483 1224 2113 -287 -91 1 0

ATOM 2105 OH TYR 302 2.376 13.866 38.013 1.000 13 .42

SUBSTΓΓUTE SHEET (RULE 26) ANISOU 2105 OH TYR 302 1505 1469 2124 -93 33 14 6

ATOM 2106 N VAL 303 1.956 8.855 44.450 1.000 13.92

ANISOU 2106 N VAL 303 1406 1637 2246 153 88 9 9

ATOM 2107 CA VAL 303 2.355 8.336 45.746 1.000 14.51

ANISOU 2107 CA VAL 303 1838 1320 2355 -137 -391 - 74

ATOM 2108 C VAL 303 3.498 9.244 46.239 1.000 15.23

ANISOU 2108 C VAL 303 1404 1507 2876 -102 -105 - 348

ATOM 2109 O VAL 303 4.471 9.386 45.512 1.000 18.70

ANISOU 2109 O VAL 303 1859 1861 3386 -239 326 - 504

ATOM 2110 CB VAL 303 2.856 6.880 45.632 1.000 16.75

ANISOU 2110 CB VAL 303 2140 1319 2905 16 -759 - 123

ATOM 2111 CGI VAL 303 3.279 6.401 47.017 1.000 19.53

ANISOU 2111 CGI VAL 303 2185 1951 3284 232 -1054 14 8

ATOM 2112 CG2 VAL 303 1.723 5.956 45.125 1.000 17.82

ANISOU 2112 CG2 VAL 303 2476 1442 2852 -213 -558 - 406

ATOM 2113 N ASN 304 3.349 9.900 47.378 1.000 14.07

ANISOU 2113 N ASN 304 1409 1369 2566 -39 -407 - 8 6

ATOM 2114 CA ASN 304 4.317 10.928 47.772 1.000 14.31

ANISOU 2114 CA ASN 304 1474 1387 2578 -102 -424 - 5 5

ATOM 2115 C ASN 304 5.450 10.397 48.637 1.000 13 .75

ANISOU 2115 C ASN 304 1360 1487 2378 34 -274 - 8 7

ATOM 2116 O ASN 304 6.539 10.962 48.584 1.000 14.60

ANISOU 2116 O ASN 304 1314 1795 2438 -34 -55 - 320

ATOM 2117 CB ASN 304 3.589 12.035 48.551 1.000 14.26

ANISOU 2117 CB ASN 304 1710 1214 2494 6 -303 176

ATOM 2118 CG ASN 304 2.535 12.661 47.642 1.000 14.81

ANISOU 2118 CG ASN 304 1551 1627 2449 23 -114 402

ATOM 2119 ODl ASN 304 2.866 13.255 46.622 1.000 16.52

ANISOU 2119 ODl ASN 304 1896 1746 2636 80 19 589

ATOM 2120 ND2 ASN 304 1.290 12.595 48.102 1.000 18.43

ANISOU 2120 ND2 ASN 304 1560 2980 2463 127 -10 1 9 9

ATOM 2121 N ILE 305 5.175 9.413 49.463 1.000 16.36

ANISOU 2121 N ILE 305 1546 1553 3117 -78 -503 2 66

ATOM 2122 CA ILE 305 6.173 8.890 50.407 1.000 14.85

ANISOU 2122 CA ILE 305 1670 1537 2436 165 -277 - 40

ATOM 2123 C ILE 305 6.183 7.372 50.352 1.000 15.78

ANISOU 2123 C ILE 305 1527 1555 2914 95 -438 - 5 1

ATOM 2124 O ILE 305 5.231 6.736 49.886 1.000 17.54

ANISOU 2124 O ILE 305 1463 1789 3412 -131 -404 5

ATOM 2125 CB ILE 305 5.949 9.430 51.818 1.000 17.80

ANISOU 2125 CB ILE 305 2167 1962 2634 -23 265 - 209

ATOM 2126 CGI ILE 305 4.578 9.091 52.416 1.000 18.93

ANISOU 2126 CGI ILE 305 1716 2948 2526 1 -218 - 163

ATOM 2127 CG2 ILE 305 6.171 10.944 51.823 1.000 19.17

ANISOU 2127 CG2 ILE 305 2685 1863 2737 70 -534 - 405

ATOM 2128 CDI . ILE 305 4.415 9.459 53.863 1.000 21.28

ANISOU 2128 CDI . ILE 305 2521 2902 2662 19 452 - 7 1

ATOM 2129 N ARG 306 7.246 6.806 50.908 1.000 14.59

ANISOU 2129 N ARG 306 1738 1641 2165 52 -356 27 1

ATOM 2130 CA ARG 306 7.424 5.360 50.828 1.000 15.25

ANISOU 2130 CA ARG 306 1509 1663 2622 139 -302 7 7

ATOM 2131 C ARG 306 8.234 4.903 52.024 1.000 15.02

ANISOU 2131 C ARG 306 1588 1464 2656 133 -332 - 2 1

ATOM 2132 O ARG 306 9.141 5.614 52.433 1.000 16.63

ANISOU 2132 O ARG 306 1682 2101 2536 -219 -294 - 168

ATOM 2133 CB ARG 306 8.135 4.943 49.532 1.000 16.31

ANISOU 2133 CB ARG 306 1820 1681 2697 -100 -270 - 150

ATOM 2134 CG ARG 306 8.226 3.414 49.377 1.000 18.43

ANISOU 2134 CG ARG 306 2476 1700 2828 40 -194 - 156

ATOM 2135 CD ARG 306 8.401 3.068 47.900 1.000 18.26

ANISOU 2135 CD ARG 306 2087 1971 2880 -120 -145 - 330 ATOM 2136 NE ARG 306 7.136 3.228 47.188 1.000 20.53

ANISOU 2136 NE ARG 306 2442 2013 3345 -577 -66S - 234

ATOM 2137 CZ ARG 306 6.980 3.178 45.873 1.000 20.27

ANISOU 2137 CZ ARG 306 2330 2057 3316 373 -522 2 0

ATOM 2138 NHl ARG 306 8.086 3.000 45.107 1.000 22.13

ANISOU 2138 NHl ARG 306 2136 2580 3695 274 -589 - 723

ATOM 2139 NH2 ARG 306 5.759 3.250 45.341 1.000 18.44

ANISOU 2139 NH2 ARG 306 2107 1838 3062 259 -285 8 4

ATOM 2140 N ARG 307 7.898 3.775 52.612 1.000 19.10

ANISOU 2140 N ARG 307 2716 1872 2671 -294 -607 3 2 7

ATOM 2141 CA ARG 307 8.576 3.212 53.768 1.000 21.13

ANISOU 2141 CA ARG 307 3321 2201 2504 -48 -845 1 3 9

ATOM 2142 C ARG 307 9.536 2.138 53.277 1.000 23 .30

ANISOU 2142 C ARG 307 3417 2170 3267 181 -1046 3 9

ATOM 2143 0 ARG 307 9.385 1.601 52.187 1.000 21.01

ANISOU 2143 0 ARG 307 2574 2355 3052 174 -728 1 12

ATOM 2144 CB ARG 307 7.557 2.522 54.694 1.000 27.30

ANISOU 2144 CB ARG 307 4545 3184 2645 -13 -247 7 0 5

ATOM 2145 CG ARG 307 6.839 3.488 55.629 1.000 46.30

ANISOU 2145 CG ARG 307 6310 6374 4907 215 1655 - 970

ATOM 2146 CD ARG 307 7.054 3.085 57.085 1.000 66.50

ANISOU 2146 CD ARG 307 11107 10355 3806 -2980 2792 - 1145

ATOM 2147 NE ARG 307 5.989 2.203 57.531 1.000 78.91

ANISOU 2147 NE ARG 307 11821 12833 5330 -4530 1969 - 5

ATOM 2148 CZ ARG 307 5.987 1.285 58.479 1.000 73.67

ANISOU 2148 CZ ARG 307 7704 14382 5907 -4724 1249 1051

ATOM 2149 NHl ARG 307 7.063 1.038 59.214 1.000 80.32

ANISOU 2149 NHl ARG 307 6613 17949 5955 -3290 2179 1 05

ATOM 2150 NH2 ARG 307 4.872 0.597 58.707 1.000 73.74

ANISOU 2150 NH2 ARG 307 9116 15919 2983 -6954 438 - 917

ATOM 2151 N THR 308 10.551 1.861 54.113 1.000 25.61

ANISOU 2151 N THR 308 4234 2212 3285 536 -1421 -232

ATOM 2152 CA THR 308 11.308 0.640 53.822 1.000 30.02

ANISOU 2152 CA THR 308 3468 1939 5998 225 -1629 - 194

ATOM 2153 C THR 308 10.468 -0.611 54.030 1.000 25.42

ANISOU 2153 C THR 308 2915 2190 4552 453 -626 - 321

ATOM 2154 0 THR 308 9.523 -0.768 54.787 1.000 30.10

ANISOU 2154 0 THR 308 4042 3482 3912 614 -217 - 125

ATOM 2155 CB THR 308 12.581 0.531 54.688 1.000 26.09

ANISOU 2155 CB THR 308 2701 3586 3626 242 -361 - 456

ATOM 2156 OGl THR 308 12.140 0.751 56.028 1.000 32.90

ANISOU 2156 OGl THR 308 4146 4188 4167 504 745 - 495

ATOM 2157 CG2 THR 308 13.577 1.594 54.256 1.000 31.43

ANISOU 2157 CG2 THR 308 3193 4702 4047 -577 -132 - 538

ATOM 2158 N SER 309 10.850 -1.591 53.217 1.000 24.73

ANISOU 2158 N SER 309 2934 2092 4370 94 -574 - 391

ATOM 2159 CA SER 309 10.199 -2.897 53.230 1.000 25.1

ANISOU 2159 CA SER 309 3793 2464 3316 -485 451 - 230

ATOM 2160 C SER 309 10.466 -3.691 54.512 1.000 24.06

ANISOU 2160 C SER 309 2360 2888 3893 302 107 3 5

ATOM 2161 O SER 309 11.565 -3.621 55.084 1.000 34.54

ANISOU 2161 O SER 309 3626 2131 7366 -76 -1944 - 3 4

ATOM 2162 CB SER 309 10.639 -3.700 52.012 1.000 26.52

ANISOU 2162 CB SER 309 3970 2159 3948 167 580 - 366

ATOM 2163 OG SER 309 10.217 -5.039 52.148 1.000 26.34

ANISOU 2163 OG SER 309 3198 2207 4604 156 -844 - 260

ATOM 2164 N LYS 310 9.494 -4.458 54.961 1.000 24.99

ANISOU 2164 N LYS 310 3172 2459 3864 160 262 3 6 6

ATOM 2165 CA LYS 310 9.651 -5.339 56.125 1.000 28.38

ANISOU 2165 CA LYS 310 4191 3167 3427 764 278 2 81

ATOM 2166 C LYS 310 9.941 -6.768 55.711 1.000 26.07

-84-

ANISOU 2166 C LYS 310 3371 2687 3846 168 -29C ) 5 7

ATOM 2167 0 LYS 310 10.150 -7.684 56.515 1.000 33. 48

ANISOU 2167 0 LYS 310 5267 3056 4400 -66 -450 10 7 3

ATOM 2168 CB LYS 310 8.299 -5.367 56.858 1.000 37. 77

ANISOU 2168 CB LYS 310 5736 4695 3921 299 1818 1

ATOM 2169 CG LYS 310 8.014 -4.214 57.806 1.000 40. 55

ANISOU 2169 CG LYS 310 6395 4716 4295 1525 1524 1 C

ATOM 2170 CD LYS 310 6.798 -4.587 58.649 1.000 44. 24

ANISOU 2170 CD LYS 310 9091 4224 3495 1053 2816 5 8. 4

ATOM 2171 CE LYS 310 6.722 -6.109 58.818 1.000 59. 12

ANISOU 2171 CE LYS 310 9281 4577 8606 766 -82 24 7 8

ATOM 2172 NZ LYS 310 6.088 -6.563 60.089 1.000 55. 80

ANISOU 2172 NZ LYS 310 4884 5742 10577 287 -947 47 9 6

ATOM 2173 N ALA 311 9.896 -7.030 54.410 1.000 22. 45

ANISOU 2173 N ALA 311 2190 2402 3939 10 52 26! .

ATOM 2174 CA ALA 311 10.360 -8.369 53.972 1.000 31. 89

ANISOU 2174 CA ALA 311 3771 2594 5753 434 -516 - 4 2 1

ATOM 2175 C ALA 311 11.909 -8.459 53.833 1.000 23. 30

ANISOU 2175 C ALA 311 3907 2328 2616 1393 -593 1 : 1 2

ATOM 2176 CB ALA 311 9.619 -8.665 52.674 1.000 27. 94

ANISOU 2176 CB ALA 311 2407 2878 5329 -355 542 - 6 6 7 2

ATOM 2177 OW HOH 501 -6.477 10.237 44.256 1.000 15. 66

ATOM 2178 OW HOH 502 -9.349 16.189 51.010 1.000 19. 26

ATOM 2179 OW HOH 503 -1.489 3.653 34.560 1.000 15. 78

ATOM 2180 OW HOH 504 -10.499 18.731 50.182 1.000 16. 19

ATOM 2181 OW HOH 505 -8.612 16.958 47.640 1.000 17. 30

ATOM 2182 OW HOH 506 -10.255 20.839 42.881 1.000 19. 05

ATOM 2183 OW HOH 507 2.096 1.076 32.810 1.000 29. 32

ATOM 2184 OW HOH 508 -0.284 4.743 41.885 1.000 13. 93

ATOM 2185 OW HOH 509 -8.525 18.553 42.416 1.000 21. 33

ATOM 2186 OW HOH 5103.165 2.604 43.488 1.000 24. 59

ATOM 2187 OW HOH 511 -6.282 19.386 52.341 1.000 18. 98

ATOM 2188 OW HOH 512 -6.826 24.638 46.833 1.000 21. 77

ATOM 2189 OW HOH 513 10.510 -4.344 46.092 1.000 25. 88

ATOM 2190 OW HOH 514 -0.806 16.964 40.372 1.000 16. 54

ATOM 2191 OW HOH 515 -1.269 18.855 42.411 1.000 15. 76

ATOM 2192 OW HOH 516 14.277 -5.146 40.175 1.000 15. 53

ATOM 2193 OW HOH 517 -0.123 21.538 40.640 1.000 17. 22

ATOM 2194 OW HOH 518 13.131 -0.967 51.791 1.000 31. 17

ATOM 2195 OW HOH 519 11.009 2.875 45.599 1.000 20. 20

ATOM 2196 OW HOH 520 5.789 13.543 45.996 1.000 17. , 36

ATOM 2197 OW HOH 521 2.168 19.767 55.925 1.000 20. .41

ATOM 2198 OW HOH 522 8.487 15.960 34.949 1.000 15. .40

ATOM 2199 OW HOH 523 10.794 12.697 29.921 1.000 19. .99

ATOM 2200 OW HOH 524 -11.722 19.112 44.516 1.000 19 , .82

ATOM 2201 OW HOH 525 1.672 -2.081 35.124 1.000 16 .29

ATOM 2202 OW HOH 526 9.651 15.283 32.342 1.000 20 .37

ATOM 2203 OW HOH 527 28.749 31.187 52.019 1.000 18 .53

ATOM 2204 OW HOH 528 15.326 11.252 32.041 1.000 19 .60

ATOM 2205 OW HOH 529 26.897 26.984 52.035 1.000 19 .86

ATOM 2206 OW HOH 530 13.528 11.592 50.915 1.000 16 .17

ATOM 2207 OW HOH 531 25.631 32.409 52.682 1.000 19 .20

ATOM 2208 OW HOH 532 18.287 6.835 52.185 1.000 18 .49

ATOM 2209 OW HOH 533 12.635 29.035 39.395 1.000 18 .09

ATOM 2210 OW HOH 534 10.797 31.968 45.659 1.000 20 .66

ATOM 2211 OW HOH 535 10.167 24.890 33.567 1.000 19 .12

ATOM 2212 OW HOH 536 23.530 24.122 58.531 1.000 20 .39

ATOM 2213 OW HOH 537 23.358 12.639 35.292 1.000 22 .61

ATOM 2214 OW HOH 538 25.879 28.699 50.264 1.000 19 .44

ATOM 2215 OW HOH 539 11.674 16.559 30.502 1.000 18 .57

ATOM 2216 OW HOH 540 18.515 27.775 40.042 1.000 22 .23 ATOM 2217 OW HOH 541 21.233 20.367 33.996 1.000 21.45

ATOM 2218 OW HOH 542 22.826 32.643 53. 094 1. 000 19. 38

ATOM 2219 OW HOH 543 19.670 22.387 35. 310 1. 000 20. 05

ATOM 2220 OW HOH 544 -13.591 21.996 61. 494 1. 000 49. 93

ATOM 2221 OW HOH 545 21.295 11.783 55. 080 1. 000 20. 04

ATOM 2222 OW HOH 546 5.431 2.533 51. 677 1. 000 28. 11

ATOM 2223 OW HOH 547 17.311 25.489 32. 148 1. 000 24. 38

ATOM 2224 OW HOH 548 17.427 7.744 33. 008 1. 000 20. 78

ATOM 2225 OW HOH 549 11.656 23.874 58. 194 1. 000 23. 39

ATOM 2226 OW HOH 550 8.037 14.987 53. 326 1. 000 33. 52

ATOM 2227 OW HOH 551 1.354 14.574 33. 889 1. 000 21. 05

ATOM 2228 OW HOH 552 11.203 20.116 63. 686 1. 000 24. 59

ATOM 2229 OW HOH 553 2.671 21.240 34. 245 1. 000 34. 51

ATOM 2230 OW HOH 554 6.339 19.832 30. 751 1. 000 26. 36

ATOM 2231 OW HOH 555 26.611 24.519 55. 570 1. 000 21. 22

ATOM 2232 OW HOH 556 27.669 17.156 53. 039 1. 000 25. 86

ATOM 2233 OW HOH 557 -14.392 19.977 44. 154 1. 000 25. 03

ATOM 2234 OW HOH 558 14.828 32.652 51. 443 1. 000 25. 23

ATOM 2235 OW HOH 559 17.937 7.207 54. 915 1. 000 20. 59

ATOM 2236 OW HOH 560 10.729 -8.875 31. 499 1. 000 24. 65

ATOM 2237 OW HOH 561 6.455 2.298 42. 613 1. 000 22. 74

ATOM 2238 OW HOH 562 13.784 31.245 44. 166 1. 000 27. 75

ATOM 2239 OW HOH 563 17.292 33.470 53. 556 1. 000 25. 28

ATOM 2240 OW HOH 564 11.210 1.109 49. 697 1. 000 23. 33

ATOM 2241 OW HOH 565 -11.339 25.246 41. 370 1. .000 26. 08

ATOM 2242 OW HOH 566 20.363 -8.375 38. 242 1. ,000 30. 07

ATOM 2243 OW HOH 567 3.890 24.604 35. ,837 1. 000 25. 86

ATOM 2244 OW HOH 568 5.334 11.875 43. .937 1. ,000 25. 45

ATOM 2245 OW HOH 569 7.861 22.385 64. .046 1. .000 28. , 98

ATOM 2246 OW HOH 570 7.754 -1.508 30. .848 1. .000 24. .72

ATOM 2247 OW HOH 571 6.297 3.583 28. .471 1. .000 33. .06

ATOM 2248 OW HOH 572 -15.790 28.800 51. .855 1. .000 30. .09

ATOM 2249 OW HOH 573 -5.388 20.310 38, .883 1, .000 23 , .64

ATOM 2250 OW HOH 574 17.657 21.059 29. .053 1, .000 24. .31

ATOM 2251 OW HOH 575 8.763 20.920 66. .102 1. .000 24 , .81

ATOM 2252 OW HOH 576 10.135 27.617 58 .357 1 .000 25 .12

ATOM 2253 OW HOH 577 7.795 1.060 29 .730 1 .000 29 .00

ATOM 2254 OW HOH 578 22.601 19.580 61 .946 1 .000 28 .66

ATOM 2255 OW HOH 579 8.859 4.744 27 .898 1 .000 26 .12

ATOM 2256 OW HOH 580 4.937 3.932 48 .882 1 .000 26 .29

ATOM 2257 OW HOH 581 17.096 5.891 35 .057 1 .000 23 .31

ATOM 2258 OW HOH 582 -16.337 ¹ 31.047 64 .719 1 .000 54 .01

ATOM 2259 OW HOH 583 7.652 24.826 52 .106 1 .000 27 .23

ATOM 2260 OW HOH 584 7.174 24.915 29 .292 1 .000 26 .60

ATOM 2261 OW HOH 585 23.452 10.614 55 .439 1 .000 26 .42

ATOM 2262 OW HOH 586 12.640 26.413 58 .676 1 .000 27 .15

ATOM 2263 OW HOH 587 6.204 21.166 62 .094 1 .000 24 .65

ATOM 2264 OW HOH 588 2.385 0.810 37 .616 1 .000 19 .92

ATOM 2265 OW HOH 589 32.930 28.236 45 .738 1 .000 38 .29

ATOM 2266 OW HOH 590 -12.04Ei 28.716 45 .065 1 .000 30 .46

ATOM 2267 OW HOH 591 0.219 13.612 36 .120 1 .000 27 .12

ATOM 2268 OW HOH 592 -2.525 3.881 43 .344 1 .000 26 .67

ATOM 2269 OW HOH 593 7.533 13.297 48 .055 1 .000 19 .59

ATOM 2270 OW HOH 594 -1.575 28.355 42 .057 1 .000 25 .53

ATOM 2271 OW HOH 595 11.209 -1.188 46 .425 1 .000 22 .12

ATOM 2272 OW HOH 596 5.684 -7.000 28 .451 1 .000 27 .97

ATOM 2273 OW HOH 597 28.868 19.406 51 .825 1 .000 27 .72

ATOM 2274 OW HOH 598 13.432 2.493 57 .904 1 .000 31 .12

ATOM 2275 OW HOH 599 8.196 7.483 27 .148 1 .000 29 .99

ATOM 2276 OW HOH 600 20.809 19.088 63 .369 1 .000 36 .86

ATOM 2277 OW HOH 601 21.352 10.656 34 .614 1 .000 30 .60 ATOM 2278 OW HOH 602 2.891 7.196 30.899 1.000 25.41

ATOM 2279 OW HOH 603 8.260 26.496 34. 561 1. 000 35. 71

ATOM 2280 OW HOH 604 22.300 13.959 31. 378 1. 000 32. 53

ATOM 2281 OW HOH 605 15.689 35.750 48. 870 1. 000 31. 17

ATOM 2282 OW HOH 606 7.219 15.638 30. 914 1. 000 27. 80

ATOM 2283 OW HOH 607 -3.237 14.604 47. 092 1. 000 20. 96

ATOM 2284 OW HOH 608 17.543 10.581 33. 561 1. 000 23. 51

ATOM 2285 OW HOH 609 -1.899 36.370 44. 261 1. 000 32. 64

ATOM 2286 OW HOH 610 26.095 14.431 43. 803 1. 000 19. 19

ATOM 2287 OW HOH 611 27.664 13.183 41. 954 1. 000 26. 48

ATOM 2288 OW HOH 612 4.302 34.604 49. 981 1. 000 24. 70

ATOM 2289 OW HOH 613 -15.580 27.012 46. 728 1. 000 42. 45

ATOM 2290 OW HOH 614 1.615 35.544 50. 347 1. 000 23. 78

ATOM 2291 OW HOH 615 -10.137 34.259 49. 033 1. 000 23. 94

ATOM 2292 OW HOH 616 26.084 6.502 57. 657 1. 000 39. 32

ATOM 2293 OW HOH 617 -15.962 20.656 46. 340 1. 000 25. 94

ATOM 2294 OW HOH 618 6.113 29.517 40. 143 1. 000 29. 43

ATOM 2295 OW HOH 619 19.797 4.627 51. 313 1. 000 27. 15

ATOM 2296 OW HOH 620 -1.748 11.315 48. 716 1. 000 21. 83

ATOM 2297 OW HOH 621 11.099 34.289 44. 259 1. 000 27. 15

ATOM 2298 OW HOH 622 28.352 14.351 37. 877 1. 000 41. 48

ATOM 2299 OW HOH 623 -2.826 36.968 57. 149 1. 000 32. 75

ATOM 2300 OW HOH 624 16.983 9.258 29. 962 1. 000 32. 82

ATOM 2301 OW HOH 625 16.780 29.213 38. 384 1. 000 27. 96

ATOM 2302 OW HOH 626 1.632 17.213 33. 689 1. 000 23. 17

ATOM 2303 OW HOH 627 33.536 23.640 45. ,028 1. 000 41. 91

ATOM 2304 OW HOH 628 23.821 6.059 50. ,174 1. 000 34. 22

ATOM 2305 OW HOH 629 3.482 2.785 46. ,751 1. 000 39. 07

ATOM 2306 OW HOH 630 20.218 24.803 60. .918 1. ,000 50. , 12

ATOM 2307 OW HOH 631 3.366 16.272 30. .698 1. ,000 31. , 50

ATOM 2308 OW HOH 632 18.871 11.791 31. .384 1. ,000 30. , 78

ATOM 2309 OW HOH 633 4.455 25.782 58. .823 1. .000 32. .14

ATOM 2310 OW HOH 634 24.721 5.202 40. .319 1. .000 40. .13

ATOM 2311 OW HOH 635 19.623 35.238 43. .466 1. ,000 50. .48

ATOM 2312 OW HOH 636 22.789 26.242 60. .797 1, ,000 26. .58

ATOM 2313 OW HOH 637 7.008 -4.809 54 .039 1, .000 33 , .89

ATOM 2314 OW HOH 638 -15.821 18.362 42 .559 1, .000 29 , .61

ATOM 2315 OW HOH 639 -11.847 15.711 52 .841 1. .000 25 .21

ATOM 2316 OW HOH 640 -1.948 13.411 35 .401 1 .000 30 .41

ATOM 2317 OW HOH 641 -14.293 21.937 42 .145 1 .000 27 .58

ATOM 2318 OW HOH 642 18.216 20.839 66 .863 1 .000 31 .23

ATOM 2319 OW HOH 643 9.836 36.288 48 .178 1 .000 44 .21

ATOM 2320 OW HOH 644 3.510 16.168 66 .253 1 .000 33 .82

ATOM 2321 OW HOH 645 7.571 33.398 41 .687 1 .000 37 .96

ATOM 2322 OW HOH 646 0.780 21.844 36 .729 1 .000 31 .71

ATOM 2323 OW HOH 647 21.244 -2.321 35 .579 1 .000 32 .40

ATOM 2324 OW HOH 648 3.027 25.244 69 .907 1 .000 36 .84

ATOM 2325 OW HOH 649 1.129 25.273 66 .516 1 .000 35 .42

ATOM 2326 OW HOH 650 14.646 7.560 60 .327 1 .000 46 .42

ATOM 2327 OW HOH 651 -8.287 26.381 37 .998 1 .000 29 .17

ATOM 2328 OW HOH 652 10.153 23.548 67 .703 1 .000 31 .50

ATOM 2329 OW HOH 653 28.906 22.258 38 .969 1 .000 32 .66

ATOM 2330 OW HOH 654 13.568 -4.482 31 .517 1 .000 26 .94

ATOM 2331 OW HOH 655 -12.63E . 17.106 55 .637 1 .000 26 .85

ATOM 2332 OW HOH . 656 2.698 5.770 50 .702 1 .000 29 .05

ATOM 2333 OW HOH 657 -1.384 7.487 46 .512 1 .000 36 .52

ATOM 2334 OW HOH 658 3.880 19.246 31 .498 1 .000 31 .50

ATOM 2335 OW HOH 659 -1.400 31.406 64 .001 1 .000 56 .62

ATOM 2336 OW HOH 660 11.416 23.260 65 .229 1 .000 32 .69

ATOM 2337 OW HOH 661 15.994 14.673 25 .680 1 .000 36 .46

ATOM 2338 OW HOH 662 28.572 21.242 53 .423 1 .000 39 .06 ATOM 2339 OW HOH 663 19.354 0.465 27.273 1.000 44.56

ATOM 2340 OW HOH 664 24.969 27.026 38. 838 1. 000 35. 41

ATOM 2341 OW HOH 665 24.294 7.488 55. 914 1. 000 32. 97

ATOM 2342 OW HOH 666 19.540 7.882 31. 178 1. 000 30. 04

ATOM 2343 OW HOH 667 -9.236 32.988 57. 241 1. 000 39. 20

ATOM 2344 OW HOH 668 2.098 18.351 67. 496 1. 000 38. 88

ATOM 2345 OW HOH 669 11.390 3.245 56. 270 1. 000 37. 56

ATOM 2346 OW HOH 670 -21.413 24.449 52. 026 1. 000 44. 66

ATOM 2347 OW HOH 671 -14.575 19.220 55. 240 1. 000 30. 91

ATOM 2348 OW HOH 672 32.112 25.958 43. 051 1. 000 33. 34

ATOM 2349 OW HOH 673 -15.050 31.151 53. 232 1. 000 34. 71

ATOM 2350 OW HOH 674 2.941 -1.607 30. 245 1. 000 34. 63

ATOM 2351 OW HOH 675 26.951 14.544 34. 757 1. 000 49. 17

ATOM 2352 OW HOH 676 14.707 30.669 39. 386 1. 000 30. 55

ATOM 2353 OW HOH 677 5.203 18.009 68. 080 1. 000 43. 41

ATOM 2354 OW HOH 678 14.151 7.965 26. 591 1. 000 38. 80

ATOM 2355 OW HOH 679 24.470 24.261 41. 443 1. 000 31. 28

ATOM 2356 OW HOH 680 17.540 2.410 28. 478 1. 000 34. 31

ATOM 2357 OW HOH 681 25.992 20.593 34. 326 1. 000 39. 66

ATOM 2358 OW HOH 682 13.802 35.357 44. 421 1. 000 34. 06

ATOM 2359 OW HOH 683 1.087 2.355 45. 456 1. 000 35. 39

ATOM 2360 OW HOH 684 22.443 34.538 42. 053 1. 000 33. 55

ATOM 2361 OW HOH 685 4.419 4.720 27. 356 1. 000 48. 02

ATOM 2362 OW HOH 686 -15.830 34.507 51. 877 1. ,000 50. 63

ATOM 2363 OW HOH 687 -15.217 29.490 48. 887 1. ,000 33. 54

ATOM 2364 OW HOH 688 36.808 21.183 46. 206 1. ,000 44. 97

ATOM 2365 OW HOH 689 3.756 1.312 29. ,272 1. .000 35. , 16

ATOM 2366 OW HOH 690 18.802 13.646 27. ,901 1. .000 30. , 08

ATOM 2367 OW HOH 691 6.997 17.521 29. .313 1. .000 47. , 70

ATOM 2368 OW HOH 692 13.725 16.327 69. .105 1. .000 36. .97

ATOM 2369 OW HOH 693 22.369 22.161 60. .503 1. .000 44. .09

ATOM 2370 OW HOH 694 -5.429 31.620 42. .219 1. .000 33. .40

ATOM 2371 OW HOH 695 19.351 23.082 30, .744 1, .000 34. .21

ATOM 2372 OW HOH 696 6.897 22.414 29, .376 1, .000 36. .59

ATOM 2373 OW HOH 697 28.700 7.809 57, .304 1, .000 38. .35

ATOM 2374 OW HOH 698 3.224 0.679 39 .819 1 .000 24 .13

ATOM 2375 OW HOH 699 -4.634 33.717 62 .593 1 .000 32 .26

ATOM 2376 OW HOH 700 32.423 17.018 43 .200 1 .000 43 .20

ATOM 2377 OW HOH 701 12.119 25.228 68 .342 1 .000 39 .95

ATOM 2378 OW HOH 702 9.307 16.477 28 .976 1 .000 31 .75

ATOM 2379 OW HOH 703 -11.313 34.067 46 .117 1 .000 49 .40

ATOM 2380 OW HOH 704 7.774 31.390 65 .371 1 .000 39 .12

ATOM 2381 OW HOH 705 24.764 7.530 36 .802 1 .000 38 .55

ATOM 2382 OW HOH 706 -22.095 25.669 59 .047 1 .000 36 .71

ATOM 2383 OW HOH 707 14.509 9.840 68 .854 1 .000 50 .38

ATOM 2384 OW HOH 708 -10.129 ' 28.722 42 .036 1 .000 38 .92

ATOM 2385 OW HOH 709 29.011 34.910 48 .390 1 .000 35 .29

ATOM 2386 OW HOH 710 15.822 31.612 42 .021 1 .000 33 .61

ATOM 2387 OW HOH 711 -1.996 17.676 33 .645 1 .000 49 .57

ATOM 2388 OW HOH 712 10.216 17.748 26 .015 1 .000 41 .04

ATOM 2389 OW HOH 713 23.535 29.642 37 .371 1 .000 43 .47

ATOM 2390 OW HOH 714 20.488 -7.214 35 .599 1 .000 45 .99

ATOM 2391 OW HOH 715 11.411 10.149 25 .081 1 .000 41 .63

ATOM 2392 OW HOH 716 19.329 -4.258 34 .139 1 .000 42 .50

ATOM 2393 OW HOH 717 13.688 26.799 66 .321 1 .000 43 .74

ATOM 2394 OW HOH 718 -10.75133.064 54 .747 1 .000 40 .47

ATOM 2395 OW HOH 719 13.800 18.258 70 .756 1 .000 34 .54

ATOM 2396 OW HOH 720 17.151 5.815 28 .003 1 .000 40 .80

ATOM 2397 OW HOH 721 0.000 0.000 36 .691 0 .330 27 .42

ATOM 2398 OW HOH 722 0.000 0.000 41 .559 0 .330 37 .77

ATOM 2399 OW HOH 723 15.314 7.549 28 .791 1 .000 36 .24 ATOM 2400 OW HOH 724 -1.663 19.944 39..196 1.,000 33..87

ATOM 2401 OW HOH 725 19.289 24.195 33. .321 1. ,000 32. .28

ATOM 2402 OW HOH 726 0.000 0.000 31. .798 0. ,330 50. .38

ATOM 2403 OW HOH 727 -1.223 38.165 59. .229 1. ,000 31. .24

ATOM 2404 OW HOH 728 22.035 38.254 45. .742 1. 000 48. .21

ATOM 2405 OW HOH 729 28.388 16.248 63. .044 1. 000 31. ,59

ATOM 2406 OW HOH 730 0.000 0.000 45. .995 0. 330 36. ,14

ATOM 2407 OW HOH 731 2.984 29.007 40. ,091 1. 000 36. 08

ATOM 2408 OW HOH 732 5.297 15.835 27. ,318 1. 000 41. ,53

ATOM 2409 OW HOH 733 17.347 10.778 27. .373 1. 000 35. ,27

ATOM 2410 OW HOH 734 29.417 14.607 53. .127 1. 000 40. ,12

ATOM 2411 OW HOH 735 4.222 -8.636 27. .012 1. 000 35. ,22

ATOM 2412 OW HOH 736 -9.949 17.712 62. .813 1. ,000 34. .43

ATOM 2413 OW HOH 737 13.960 -10.203 55. .259 1. ,000 31. .79

ATOM 2414 OW HOH 738 11.831 -1.522 49, .308 1. ,000 25. .22

ATOM 2415 OW HOH 739 2.896 4.247 29, .596 1. .000 38. .64

ATOM 2416 OW HOH 740 10.959 13.759 25. .528 1. .000 61. .86

ATOM 2417 OW HOH 741 0.864 17.227 30, .557 1. .000 50. .71

ATOM 2418 OW HOH 742 31.755 18.949 52, .065 1. .000 40. .48

ATOM 2419 OW HOH 743 21.678 -0.485 28, .218 1. .000 43. .23

ATOM 2420 OW HOH 744 10.583 16.397 75, .211 1. .000 45. .04

ATOM 2421 OW HOH 745 7.480 7.996 78, .287 1. .000 57. .64

ATOM 2422 OW HOH 746 24.067 35.122 40, .297 1. .000 41, .95

ATOM 2423 OW HOH 747 7.804 10.269 78 .332 1. .000 49, .63

ATOM 2424 OW HOH 748 22.131 40.645 45. .806 1. .000 49, .69

ATOM 2425 OW HOH 749 14.850 -4.647 33, .872 1. .000 42, .88

ATOM 2426 OW HOH 750 -12.930 32.504 55, .211 1. .000 37, .15

ATOM 2427 OW HOH 751 -4.832 35.986 43, .333 1. .000 44, .39

ATOM 2428 OW HOH 752 19.834 33.566 56, .449 1. .000 31, .56

ATOM 2429 OW HOH 753 3.363 22.310 29, .844 1. .000 42, .02

ATOM 2430 OW HOH 754 25.594 4.030 34, .174 1. .000 51, .90

ATOM 2431 OW HOH 755 28.036 35.859 46, .448 1. .000 39, .50

ATOM 2432 OW HOH 756 -12.951 16.294 61, .787 1. .000 40, .94

ATOM 2433 OW HOH 757 -10.870 26.452 38, .737 1. .000 44, .85

ATOM 2434 OW HOH 758 13.216 12.896 70, .729 1. .000 63, .42

ATOM 2435 OW HOH 759 -0.403 21.161 74, .990 1. .000 38, .96

ATOM 2436 OW HOH 760 -7.025 32.526 64 .316 1. .000 39, .64

ATOM 2437 OW HOH 761 -15.459 19.739 58. .090 1. .000 40, .84

ATOM 2438 OW HOH 762 -4.964 36.577 59 .068 1. .000 48, .64

ATOM 2439 OW HOH 763 26.807 35.717 50 .036 1, .000 43. .54

ATOM 2440 OW HOH 764 19.542 7.083 65 .538 1, .000 41, .41

ATOM 2441 OW HOH 765 3.709 35.837 42, .709 1, .000 33 .78

ATOM 2442 OW HOH 766 0.431 33.688 40 .172 1. .000 36 .91

ATOM 2443 OW HOH 767 18.620 5.064 64 .617 1, .000 45 .76

ATOM 2444 OW HOH 768 35.526 19.792 41 .322 1. .000 52 .54

ATOM 2445 OW HOH 769 19.671 7.789 67 .717 1 .000 43 .44

ATOM 2446 OW HOH 770 3.562 12.048 26 .149 1 .000 40 .08

ATOM 2447 OW HOH 771 20.245 35.637 53 .927 1, .000 52 .16

ATOM 2448 OW HOH 772 -20.588 25.640 61 .573 1 .000 58 .60

ATOM 2449 OW HOH 773 1.556 37.342 52 .171 1 .000 36 .23

ATOM 2450 OW HOH 774 8.340 0.668 49 .382 1 .000107. .24

ATOM 2451 OW HOH 775 27.160 2.372 34 .466 1 .000 59 .84

ATOM 2452 OW HOH 776 6.575 19.271 25 .545 1 .000 36 .68 ATOM 2453 OW HOH 777 -17.605 29.205 62..661 1..000 56..83

ATOM 2454 OW HOH 778 7.616 6.902 24. .722 1. .000 61. .34

ATOM 2455 OW HOH 779 19.749 10.700 68. .006 1. ,000 65. .22

ATOM 2456 W HOH 780 7.281 -5.270 50, .090 1. .000 50. .00

ATOM 2457 W HOH 781 -6.809 28.483 40. .515 1. .000 50. .00

ATOM 2458 W HOH 782 9.990 17.263 38. .636 1. .000 50. .00

ATOM 2459 W HOH 783 5.767 -2.331 28. .939 1. ,000 50. ,00

ATOM 2460 W HOH 784 11.694 -0.118 24. ,984 1. ,000 50. ,00

ATOM 2461 W HOH 785 24.442 7.952 47. ,994 1. 000 50. ,00

ATOM 2462 W HOH 786 14.251 36.889 46. .491 1. ,000 50. , 00

ATOM 2463 w HOH 787 5.759 26.477 33. .851 1. ,000 50. ,00

ATOM 2464 w HOH 788 -11.816 22.606 40. .795 1. ,000 50. ,00

ATOM 2465 w HOH 789 -2.531 5.579 45. .829 1. ,000 50. ,00

ATOM 2466 w HOH 790 -13.002 32.034 46. ,612 1. ,000 50. ,00

ATOM 2467 w HOH 791 2.230 3.555 48. ,985 1. ,000 50. ,00

ATOM 2468 w HOH 792 9.397 13.464 28. .121 1. .000 50. .00

ATOM 2469 w HOH 793 28.257 10.442 42. .781 1. ,000 50. .00

ATOM 2470 w HOH 794 4.652 17.944 59. .241 1. .000 50. .00

ATOM 2471 w HOH 795 5.977 15.287 79. .554 1. .000 50. .00

ATOM 2472 w HOH 796 30.501 11.852 47. .616 1. .000 50. .00

ATOM 2473 w HOH 797 5.625 14.258 54. .367 1. .000 50. .00

ATOM 2474 w HOH 798 23.942 20.228 33. .277 1. .000 50, .00

ATOM 2475 w HOH 799 10.164 14.642 58, .997 1. .000 50, .00

ATOM 2476 w HOH 800 7.807 31.943 52, .999 1. .000 50, .00

ATOM 2477 w HOH 801 23.377 9.361 34, .817 1. .000 50, .00

ATOM 2478 w HOH 802 21.193 9.722 32. .004 1. .000 50. .00

ATOM 2479 w HOH 803 34.928 14.644 46. ,038 1. .000 50. .00

ATOM 2480 w HOH 804 29.073 16.684 34. .445 1. .000 50 .00

ATOM 2481 w HOH 805 7.008 -2.049 51, .872 1. .000 50 .00

ATOM 2482 w HOH 806 25.363 7.860 45, .531 1. .000 50, .00

ATOM 2483 w HOH 807 30.704 8.207 55, .971 1. .000 50, .00

ATOM 2484 w HOH 808 33.072 24.900 40, .599 1. .000 50, .00

ATOM 2485 w HOH 809 -15.577 19.225 63 , .152 1. .000 50, .00

ATOM 2486 w HOH 810 6.072 18.137 23 .603 1, .000 50 .00

ATOM 2487 w HOH 811 -7.214 39.940 55, .639 1. .000 50 .00

ATOM 2488 w HOH 812 5.509 18.517 74, .919 1. .000 50 .00

ATOM 2489 w HOH 813 33.845 9.908 56 .672 1, .000 50 .00

ATOM 2490 w HOH 814 0.421 35.779 42, .931 1, .000 50 .00

ATOM 2491 w HOH 815 35.282 21.705 48, .656 1, .000 50 .00

ATOM 2492 w HOH 816 39.344 22.173 46 .871 1 .000 50 .00

ATOM 2493 w HOH 817 -5.192 39.820 60 .056 1. .000 50 .00

ATOM 2494 w HOH 818 30.199 13.039 33 .383 1 .000 50 .00

ATOM 2495 w HOH 819 -4.860 36.454 61 .731 1 .000 50 .00

ATOM 2496 w HOH 820 -14.599 17.407 58 .382 1 .000 50 .00

ATOM 2497 w HOH 821 1.340 -0.111 41 .711 0 .500 50 .00

ATOM 2498 w HOH 822 34.512 23.218 52 .108 1 .000 50 .00

ATOM 2499 w HOH 823 32.136 12.571 52 .190 1 .000 50 .00

ATOM 2500 w HOH 824 13.525 -6.549 29 .838 1 .000 50 .00

ATOM 2501 w HOH 825 6.072 -4.141 27 .534 1 .000 50 .00 STRUCTURE B

ATOM 1 CB MET 1 31.030 11.882 57.066 1.000 50.96

ANISOU 1 CB MET 1 5663 3892 9809 1113 -2217 - 554

ATOM 2 CG MET 1 30.206 12.690 56.086 1.000 51.63

ANISOU 2 CG MET 1 6595 3775 9246 691 -1891 1 6 9

ATOM 3 SD MET 1 28.694 11.848 55.559 1.000 40.50

ANISOU 3 SD MET 1 7003 3962 4424 833 -1535 - 460

ATOM 4 CE MET 1 27.852 11.584 57.120 1.000 45.32

ANISOU 4 CE MET 1 8632 3912 4677 -239 -653 - 1702

ATOM 5 C MET 1 31.587 13.367 58.999 1.000 52.14

ANISOU 5 C MET 1 6204 4752 8854 287 -2128 - 63

ATOM 6 0 MET 1 31.239 12.847 60.058 1.000 52.92

ANISOU 6 0 MET 1 7381 5242 7483 1417 -4224 5 1 9

ATOM 7 N MET 1 33.170 11.646 58.275 1.000 57.78

ANISOU 7 N MET 1 4533 6034 11388 34 -1912 - 811

ATOM 8 ' CA MET 1 32.156 12.587 57.819 1.000 54.62

ANISOU 8 CA MET 1 6441 4752 9560 137 -2012 - 617

ATOM 9 N ASP 2 31.485 14.679 58.792 1.000 43 .52

ANISOU 9 N ASP 2 3460 4866 8210 474 -2350 4 7

ATOM 10 CA ASP 2 30.759 15.471 59.796 1.000 41.69

ANISOU 10 CA ASP 2 4439 4678 6722 -309 -2603 - 3 1

ATOM 11 CB ASP 2 31.206 16.912 59.644 1.000 37.89

ANISOU 11 CB ASP 2 3805 4768 5822 -304 -3473 2 6 6

ATOM 12 CG ASP 2 30.219 17.958 60.121 1.000 39.59

ANISOU 12 CG ASP 2 4511 4616 5916 15 -3218 5 8 9

ATOM 13 ODl ASP 2 29.325 17.637 60.933 1.000 45.10

ANISOU 13 ODl ASP 2 5866 4689 6581 -553 -1950 - 625

ATOM 14 OD2 ASP 2 30.363 19.121 59.663 1.000 42.05

ANISOU 14 OD2 ASP 2 5994 4341 5643 -465 -3788 1 45

ATOM 15 C ASP 2 29.275 15.213 59.556 1.000 33.84

ANISOU 15 C ASP 2 4131 3634 5094 -59 -1682 - 122

ATOM 16 O ASP 2 28.901 15.176 58.379 1.000 29.25

ANISOU 16 O ASP 2 2232 4393 4489 658 -390 - 615

ATOM 17 N THR 3 28.467 15.029 60.597 1.000 29.41

ANISOU 17 N THR 3 4731 2636 3807 907 -2076 - 284

ATOM 18 CA THR 3 27.046 14.764 60.421 1.000 28.55

ANISOU 18 CA THR 3 4602 2494 3753 597 -1006 - 390

ATOM 19 CB THR 3 26.447 13.762 61.414 1.000 36.51

ANISOU 19 CB THR 3 7170 2209 4495 -791 -1996 5 2

ATOM 20 OGl THR 3 26.629 14.220 62.758 1.000 42.45

ANISOU 20 OGl THR 3 9519 2620 3989 -920 -1251 3 83

ATOM 21 CG2 THR 3 27.153 12.412 61.315 1.000 50.26

ANISOU 21 CG2 THR 3 9604 1863 7630 -602 -733 - 333

ATOM 22 C THR 3 26.240 16.061 60.553 1.000 29.01

ANISOU 22 C THR 3 4535 2548 3939 738 -1079 9 9

ATOM 23 O THR 3 25.041 16.044 60.827 1.000 35.82

ANISOU 23 O THR 3 5149 2485 5976 390 524 - 1246

ATOM 24 N THR 4 26.928 17.181 60.332 1.000 24.98

ANISOU 24 N THR 4 3874 2456 3162 542 -2040 - 986

ATOM 25 CA THR 4 26.214 18.465 60.327 1.000 23.97

ANISOU 25 CA THR 4 3437 2426 3244 344 -1563 - 375

ATOM 26 CB THR 4 27.183 19.650 60.408 1.000 26.77

ANISOU 26 CB THR 4 2636 2429 5105 651 -988 - 923

ATOM 27 OGl THR 4 28.050 19.484 61.551 1.000 32.62

ANISOU 27 OGl THR 4 3398 2812 6184 195 -2081 - 1134

ATOM 28 CG2 THR 4 26.429 20.942 60.663 1.000 26.40

ANISOU 28 CG2 THR 4 2373 2692 4967 533 -573 - 1570

ATOM 29 C THR 4 25.325 18.577 59.097 1.000 21.64

ANISOU 29 C THR 4 3090 2760 2374 368 -750 - 2 0

ATOM 30 O THR 4 25.738 18.264 57.980 1.000 21.58

ANISOU 30 O THR 4 2668 2629 2902 246 -560 - 659

ATOM 31 N VAL 5 24.104 19.049 59.340 1.000 15.88 ANISOU 31 N VAL 5 2505 2021 1508 -613 -630 - 162

ATOM 32 CA VAL 5 23.211 19.385 58.211 1.000 14.80

ANISOU 32 CA VAL 5 2463 1893 1266 -594 -473 - 8 7

ATOM 33 CB VAL 5 21.742 19.402 58.606 1.000 16.09

ANISOU 33 CB VAL 5 2476 1881 1757 -412 -406 5 02

ATOM 34 CGI VAL 5 20.855 19.846 57.447 1.000 14.91

ANISOU 34 CGI VAL 5 2468 1859 1337 9 -102 197

ATOM 35 CG2 VAL 5 21.310 17.994 59.074 1.000 21.15

ANISOU 35 CG2 VAL 5 3015 2345 2677 -700 -418 1198

ATOM 36 C VAL 5 23.639 20.762 57.694 1.000 17.70

ANISOU 36 C VAL 5 2893 2085 1749 -1137 -713 1 0 3

ATOM 37 O VAL 5 23.532 21.759 58.419 1.000 17.35

ANISOU 37 O VAL 5 2566 1978 2050 -698 -650 1 0 5

ATOM 38 N PRO 6 24.150 20.845 56.479 1.000 13.23

ANISOU 38 N PRO 6 1334 1597 2097 -162 -668 409

ATOM 39 CD PRO 6 24.302 19.770 55.484 1.000 15.56

ANISOU 39 CD PRO 6 1887 1850 2176 -309 -383 2 7 7

ATOM 40 CA PRO 6 24.667 22.137 56.005 1.000 14.49

ANISOU 40 CA PRO 6 1332 1740 2432 -218 -536 5 2 2

ATOM 41 CB PRO 6 25.571 21.722 54.847 1.000 18.21

ANISOU 41 CB PRO 6 2294 1740 2886 -224 130 434

ATOM 42 CG PRO 6 25.132 20.378 54.409 1.000 20.37

ANISOU 42 CG PRO 6 2708 2632 2399 -1078 38 - 6 1

ATOM 43 C PRO 6 23.576 23.091 55.510 1.000 14.59

ANISOU 43 C PRO 6 1388 1712 2443 -406 -786 6 9 8

ATOM 44 O PRO 6 22.408 22.743 55.295 1.000 13 .06

ANISOU 44 O PRO 6 1298 1547 2118 -283 -596 1 5

ATOM 45 N THR 7 24.048 24.326 55.313 1.000 14.56

ANISOU 45 N THR 7 1393 1678 2463 -380 -565 5 8 7

ATOM 46 CA THR 7 23.288 25.428 54.771 1.000 13.28

ANISOU 46 CA THR 7 1463 1584 1998 -469 -734 44 0

ATOM 47 CB THR 7 23.121 26.572 55.799 1.000 14.44

ANISOU 47 CB THR 7 1927 1652 1905 -348 -1257 3 2 9

ATOM 48 OGl THR 7 22.454 26.102 56.998 1.000 18.44

ANISOU 48 OGl THR 7 3136 2013 1858 -333 -829 17 6

ATOM 49 CG2 THR 7 22.290 27.719 55.261 1.000 14.98

ANISOU 49 CG2 THR 7 1390 1788 2513 -213 -727 4 12

ATOM 50 C THR 7 23.973 26.005 53.539 1.000 14.62

ANISOU 50 C THR 7 1144 2200 2212 -355 -693 7 04

ATOM 51 O THR 7 25.192 26.257 53.600 1.000 17.21

ANISOU 51 O THR 7 1284 2515 2738 -641 -840 975

ATOM 52 N PHE 8 23.211 26.222 52.472 1.000 12.32

ANISOU 52 N PHE 8 1165 1596 1919 -314 -534 3 7 0

ATOM 53 CA PHE 8 23.692 26.869 51.283 1.000 13.31

ANISOU 53 CA PHE 8 1554 1531 1971 -60 -295 3 43

ATOM 54 CB PHE 8 23.724 25.933 50.067 1.000 13.71

ANISOU 54 CB PHE 8 1479 1705 2025 -136 -232 234

ATOM 55 CG PHE 8 24.635 24.746 50.258 1.000 13 .68

ANISOU 55 CG PHE 8 1225 1716 2257 -185 8 15 5

ATOM 56 CDI PHE 8 24.147 23.503 50.628 1.000 14.10

ANISOU 56 CDI PHE 8 1317 1710 2329 -93 231 2 2 1

ATOM 57 CD2 PHE 8 26.006 24.882 50.079 1.000 17.52

ANISOU 57 CD2 PHE 8 1239 2282 3134 -234 -56 917

ATOM 58 CEl PHE 8 24.984 22.420 50.812 1.000 15.39

ANISOU 58 CEl PHE 8 1473 1878 2497 -11 242 4 8 1

ATOM 59 CE2 PHE 8 26.840 23.807 50.271 1.000 17.73

ANISOU 59 CE2 PHE 8 1179 2259 3301 -157 -143 4 2 3

ATOM 60 CZ PHE 8 26.348 22.567 50.654 1.000 17.12

ANISOU 60 CZ PHE 8 1310 2437 2757 24 -382 9 7 8

ATOM 61 C PHE 8 22.821 28.073 50.909 1.000 12.76

ANISOU 61 C PHE 8 1401 1513 1935 -164 -145 442 ATOM 62 0 PHE 8 21.602 28.033 51.079 1.000 13 .18

ANISOU 62 0 PHE 8 1392 1295 2322 -256 -400 3 64

ATOM 63 N SER 9 23.478 29.096 50.394 1.000 13 .03

ANISOU 63 N SER 9 1722 1636 1593 -565 -601 4 9 0

ATOM 64 CA SER 9 22.861 30.224 49.718 1.000 12.55

ANISOU 64 CA SER 9 1591 1468 1708 -392 -438 3 15

ATOM 65 CB SER 9 23.743 31.472 49.761 1.000 15.41

ANISOU 65 CB SER 9 2385 1833 1637 -915 -1057 7 8 3

ATOM 66 OG SER 9 23.138 32.539 49.007 1.000 17.99

ANISOU 66 OG SER 9 2504 1721 2611 -718 -999 9 2 4

ATOM 67 C SER 9 22.520 29.868 48.276 1.000 12.72

ANISOU 67 C SER 9 2040 1187 1606 -411 -576 47 6

ATOM 68 0 SER 9 23.397 29.495 47.478 1.000 16.18

ANISOU 68 0 SER 9 2265 2053 1830 -465 -381 7 3

ATOM 69 N LEU 10 21.229 29.982 47.968 1.000 14.19

ANISOU 69 N LEU 10 2154 1488 1750 -301 -699 17 4

ATOM 70 CA LEU 10 20.798 29.714 46.596 1.000 14.62

ANISOU 70 CA LEU 10 2243 1579 1734 -184 -784 22 4

ATOM 71 CB LEU 10 19.291 29.883 46.436 1.000 14.72

ANISOU 71 CB LEU 10 2222 1714 1657 -142 -657 - 168

ATOM 72 CG LEU 10 18.693 29.633 45.050 1.000 14.10

ANISOU 72 CG LEU 10 2087 1557 1713 -702 -695 14 5

ATOM 73 CDI LEU 10 18.986 28.214 44.582 1.000 16.23

ANISOU 73 CDI LEU 10 2994 1578 1595 -554 -1132 8 7

ATOM 74 CD2 LEU 10 17.198 29.913 44.997 1.000 21.82

ANISOU 74 CD2 LEU 10 2180 2904 3206 -421 -1151 -51E

ATOM 75 C LEU 10 21.531 30.639 45.626 1.000 15.87

ANISOU 75 C LEU 10 2449 1785 1796 -491 -844 3 14

ATOM 76 0 LEU 10 21.962 30.199 44.553 1.000 16.33

ANISOU 76 0 LEU 10 2607 1816 1780 -601 -829 2 7 6

ATOM 77 N ALA 11 21.669 31.917 45.986 1.000 17.17

ANISOU 77 N ALA 11 2521 1889 2115 -607 -548 139

ATOM 78 CA ALA 11 22.335 32.912 45.129 1.000 16.56

ANISOU 78 CA ALA 11 2377 1884 2029 -732 -1033 3 02

ATOM 79 CB ALA 11 22.199 34.259 45.805 1.000 20.05

ANISOU 79 CB ALA 11 3210 1877 2529 -670 -674 2 5 9

ATOM 80 C ALA 11 23.786 32.535 44.831 1.000 16.33

ANISOU 80 C ALA 11 2319 2255 1629 -754 -988 434

ATOM 81 0 ALA 11 24.260 32.587 43.677 1.000 19.66

ANISOU 81 0 ALA 11 3115 2559 1795 -947 -560 6 19

ATOM 82 N GLU 12 24.558 32.085 45.810 1.000 17.28

ANISOU 82 N GLU 12 2686 1994 1884 -454 -1087 3 9 0

ATOM 83 CA GLU 12 25.931 31.654 45.752 1.000 16.34

ANISOU 83 CA GLU 12 2703 1674 1831 -474 -889 1033

ATOM 84 CB GLU 12 26.527 31.477 47.158 1.000 16.09

ANISOU 84 CB GLU 12 2440 1867 1808 -770 -820 1058

ATOM 85 CG GLU 12 26.633 32.802 47.915 1.000 18.90

ANISOU 85 CG GLU 12 2717 2127 2335 -1216 -1090 7 88

ATOM 86 CD GLU 12 27.115 32.657 49.342 1.000 21.17

ANISOU 86 CD GLU 12 3300 2547 2198 -1182 -1053 724

ATOM 87 OEl . GLU 12 27.538 31.558 49.756 1.000 22.07

ANISOU 87 OEl . GLU 12 2722 3014 2650 -720 -1365 7 97

ATOM 88 OE2 : GLU 12 27.068 33.679 50.059 1.000 29.26

ANISOU 88 OE2 : GLU 12 5764 2634 2722 -1279 -1848 47 6

ATOM 89 C GLU 12 25.997 30.402 44.882 1.000 17.16

ANISOU 89 C GLU 12 2044 2319 2158 -624 -715 4 8 1

ATOM 90 0 GLU 12 26.879 30.317 44.032 1.000 18.88

ANISOU 90 0 GLU 12 3200 2388 1583 -1004 -306 8 9 9

ATOM 91 N LEU 13 25.083 29.441 45.049 1.000 17.32

ANISOU 91 N LEU 13 2176 2300 2104 -659 -386 9 4

ATOM 92 CA LEU 13 25.082 28.252 44.189 1.000 14.00

SUBSTΠΓUTE SHEET (RULE 26) -93-

ANISOU 92 CA LEU 13 1734 1873 1713 -140 -170 498

ATOM 93 CB LEU 13 24.003 27.248 44.620 1.000 15.37

ANISOU 93 CB LEU 13 2205 1838 1795 -375 -149 465

ATOM 94 CG LEU 13 24.154 26.554 45.967 1.000 14.52

ANISOU 94 CG LEU 13 1913 1803 1799 -280 -204442

ATOM 95 CDI LEU 13 22.934 25.680 46.193 1.000 15.15

ANISOU 95 CDI LEU 13 2174 1817 1766 -433 185 175

ATOM 96 CD2 LEU 13 25.411 25.690 46.067 1.000 17.54

ANISOU 96 CD2 LEU 13 2119 2043 2502 -38 -419 270

ATOM 97 C LEU 13 24.876 28.626 42.725 1.000 16.54

ANISOU 97 C LEU 13 2510 2062 1710 -222 -93 565

ATOM 98 O LEU 13 25.548 28.122 41.821 1.000 18.28

ANISOU 98 O LEU 13 2685 2514 1748 -687 75 259

ATOM 99 N GLN 14 23.945 29.534 42.472 1.000 16.86

ANISOU 99 N GLN 14 1970 2337 2100 -557 -683 838

ATOM 100 CA GLN 14 23.657 30.015 41.132 1.000 18.63

ANISOU 100 CA GLN 14 2761 2404 1915 -610 -802 568

ATOM 101 CB GLN 14 22.421 30.923 41.130 1.000 19.39

ANISOU 101 CB GLN 14 3166 2176 2025 -392 -918 977

ATOM 102 CG GLN 14 21.108 30.250 41.460 1.000 19.00

ANISOU 102 CG GLN 14 2879 2383 1957 -209 -725 460

ATOM 103 CD GLN 14 19.974 31.227 41.766 1.000 18.83

ANISOU 103 CD GLN 14 3139 2118 1897 -6 -1229 494

ATOM 104 OEl GLN 14 20.177 32.317 42.314 1.000 26.10

ANISOU 104 OEl GLN 14 3928 2407 3582 -98 -1172 -241

ATOM 105 NE2 GLN 14 18.745 30.823 41.411 1.000 20.94

ANISOU 105 NE2 GLN 14 2900 2716 2340 -149 -840454

ATOM 106 C GLN 14 24.804 30.812 40.525 1.000 20.40

ANISOU 106 C GLN 14 3226 2458 2065 -795 -712 937

ATOM 107 O GLN 14 24.812 30.951 39.311 1.000 30.48

ANISOU 107 O GLN 14 5089 4340 2152 -2337 -898 1211

ATOM 108 N GLN 15 25.734 31.309 41.329 1.000 20.35

ANISOU 108 N GLN 15 3252 2452 2030 -1067 -240 497

ATOM 109 CA GLN 15 26.909 32.041 40.884 1.000 21.88

ANISOU 109 CA GLN 15 3184 3230 1901 -1152 -299788

ATOM 110 CB GLN 15 27.288 33.100 41.920 1.000 22.20

ANISOU 110 CB GLN 15 2720 3162 2551 -1131 -770 691

ATOM 111 CG GLN 15 26.450 34.358 41.954 1.000 25.73

ANISOU 111 CG GLN 15 4496 2735 2545 -821 -233 1269

ATOM 112 CD GLN 15 26.325 35.021 43.306 1.000 35.76

ANISOU 112 CD GLN 15 6010 3945 3631 -643 -229 - 135

ATOM 113 OEl GLN 15 27.145 34.884 44.225 1.000 49.13

ANISOU 113 OEl GLN 15 8425 5866 4378 -2857 -2197 - 564

ATOM 114 NE2 GLN 15 25.255 35.812 43.489 1.000 51.85

ANISOU 114 NE2 GLN 15 7190 5567 6945 62 3066 107

ATOM 115 C GLN 15 28.069 31.079 40.625 1.000 23.93

ANISOU 115 C GLN 15 3451 3513 2127 -990 145 884

ATOM 116 O GLN 15 29.177 31.448 40.213 1.000 28.95

ANISOU 116 O GLN 15 3535 4619 2845 -899 510 1225

ATOM 117 N GLY 16 27.828 29.794 40.891 1.000 25.86

ANISOU 117 N GLY 16 4089 3282 2457 -889 -36 469

ATOM 118 CA GLY 16 28.812 28.763 40.649 1.000 29.00

ANISOU 118 CA GLY 16 4785 3562 2671 -677 765 255

ATOM 119 C GLY 16 29.741 28.546 41.814 1.000 25.45

ANISOU 119 c GLY 16 3427 3490 2754 -264 1422 673

ATOM 120 0 GLY 16 30.805 27.955 41.625 1.000 29.63

ANISOU 120 0 GLY 16 3925 3267 4068 -66 1997 523

ATOM 121 N LEU 17 29.387 28.979 43.015 1.000 22.50

ANISOU 121 N LEU 17 3266 2713 2569 -39 923 733

ATOM 122 CA LEU 17 30.234 28.727 44.172 1.000 21.73

ANISOU 122 CA LEU 17 2299 2931 3025 -282 867 748 . -.

-94-

ATOM 123 CB LEU 17 30.124 29.921 45.132 1.000 21.23

ANISOU 123 CB LEU 17 2137 2858 3071 -620 669 71 :

ATOM 124 CG LEU 17 30.354 31.274 44.431 1.00026.12

ANISOU 124 CG LEU 17 2708 2965 4253 -889 1342 93 :

ATOM 125 CDI LEU 17 29.962 32.444 45.305 1.00029.81

ANISOU 125 CDI LEU 17 2515 2924 5885 -396 464 30 :

ATOM 126 CD2 LEU 17 31.808 31.350 43.974 1.00032.84

ANISOU 126 CD2 LEU 17 2845 3703 5930 -281 1871 211

ATOM 127 C LEU 17 29.886 27.456 44.936 1.000 19.36

ANISOU 127 C LEU 17 2081 2819 2455 -239 545 581

ATOM 128 O LEU 17 28.773 26.920 44.848 1.00021.11

ANISOU 128 O LEU 17 2284 3004 2734 -444 107 105

ATOM 129 N HIS 18 30.838 26.952 45.706 1.00021.02

ANISOU 129 N HIS 18 2124 2752 3109 -314 193 49 :

ATOM 130 CA HIS 18 30.678 25.814 46.615 1.000 18.11

ANISOU 130 CA HIS 18 1569 2996 2315 -460 -28 3 6

ATOM 131 CB HIS 18 29.655 26.149 47.702 1.00021.25

ANISOU 131 CB HIS 18 1731 3332 3010 -45 282 35

ATOM 132 CG HIS 18 29.796 27.515 48.283 1.00023.28

ANISOU 132 CG HIS 18 2234 3612 2999 211 -46 - 2

ATOM 133 CD2 HIS 18 28.898 28.535 48.344 1.000 24.53

ANISOU 133 CD2 HIS 18 3112 3479 2728 532 41 440

ATOM 134 NDl HIS 18 30.940 27.977 48.895 1.00026.72

ANISOU 134 NDl HIS 18 2938 4039 3173 -151 -569 3 8

ATOM 135 CEl HIS 18 30.756 29.218 49.307 1.00029.80

ANISOU 135 CEl HIS 18 4476 3775 3071 -542 -562 23

ATOM 136 NE2 HIS 18 29.524 29.581 48.985 1.00030.03

ANISOU 136 NE2 HIS 18 4752 3282 3377 216 -148 33

ATOM 137 C HIS 18 30.266 24.528 45.917 1.000 18.57

ANISOU 137 C HIS 18 1943 3084 2028 -951 30 590

ATOM 138 O HIS 18 29.594 23.682 46.532 1.000 19.92

ANISOU 138 O HIS 18 1949 3125 2493 -777 -87 99

ATOM 139 N GLN 19 30.647 24.340 44.658 1.000 19.24

ANISOU 139 N GLN 19 2329 2700 2282 -256 298 49

ATOM 140 CA GLN 19 30.119 23.206 43.908 1.00021.51

ANISOU 140 CA GLN 19 3249 2431 2492 -228 597 31

ATOM 141 CB GLN 19 30.446 23.307 42.406 1.00022.8

ANISOU 141 CB GLN 19 3231 3058 2408 -148 463 24

ATOM 142 CG GLN 19 29.738 24.453 41.698 1.00025.83

ANISOU 142 CG GLN 19 3445 3712 2658 -384 -40756

ATOM 143 CD GLN 19 28.223 24.470 41.747 1.00031.56

ANISOU 143 CD GLN 19 3439 4722 3832 -252 -98835

ATOM 144 OEl GLN 19 27.521 23.640 41.153 1.00038.51

ANISOU 144 OEl GLN 19 3869 3649 7115 377 -3045 6 8 6

ATOM 145 NE2 GLN 19 27.621 25.433 42.475 1.00033.32

ANISOU 145 NE2 GLN 19 3303 5695 3663 647 -1109 4 4 9

ATOM 146 C GLN 19 30.578 21.873 44.485 1.00020.32

ANISOU 146 C GLN 19 2224 2710 2785 -60 514 39

ATOM 147 O GLN 19 29.806 20.900 44.473 1.000 19.08

ANISOU 147 O GLN 19 1888 2451 2910 221 257 74

ATOM 148 N ASP 20 31.800 21.761 44.999 1.00024.09

ANISOU 148 N ASP 20 3001 3507 2645 -773 -507 41

ATOM 149 CA ASP 20 32.268 20.498 45.553 1.00021.82

ANISOU 149 CA ASP 20 1707 3811 2774 -327 -58 35

ATOM 150 CB ASP 20 33.780 20.527 45.779 1.00026.34

ANISOU ^' 150 CB ASP 20 1594 4552 3863 -962 236 49

ATOM 151 CG ASP 20 34.596 20.517 44.503 1.00034.45

ANISOU ' 151 CG ASP 20 2531 5859 4701 -1208 1213 - 2

ATOM 152 ODl ASP 20 34.177 19.982 43.457 1.00033.11

ANISOUr 152 ODl ASP 20 3768 4173 4640 -311 1233 - 3 7 5

ATOM 153 OD2 ASP 20 35.725 21.056 44.532 1.00049.71 ANISOU 153 OD2 ASP 20 3445 9922 5519 -3116 1710 5 3

ATOM 154 C ASP 20 31.538 20.179 46.862 1.000 21.03

ANISOU 154 C ASP 20 1876 2702 3412 -231 616 3 8 8

ATOM 155 O ASP 20 31.118 19.038 47.075 1.000 20.80

ANISOU 155 O ASP 20 1162 2583 4157 -72 -139 55 0

ATOM 156 N GLU 21 31.359 21.177 47.729 1.000 17.88

ANISOU 156 N GLU 21 1218 2751 2824 -263 -148 5 1 1

ATOM 157 CA GLU 21 30.599 20.999 48.965 1.000 16.80

ANISOU 157 CA GLU 21 1128 2173 3083 -96 46 3 9 4

ATOM 158 CB GLU 21 30.654 22.304 49.781 1.000 20.23

ANISOU 158 CB GLU 21 1366 2620 3701 5 -262 - 210

ATOM 159 CG GLU 21 32.040 22.669 50.307 1.000 24.60

ANISOU 159 CG GLU 21 1660 3325 4359 -221 -654 - 301

ATOM 160 CD GLU 21 32.860 23.565 49.402 1.000 28.46

ANISOU 160 CD GLU 21 1191 4348 5275 -498 -1597 1125

ATOM 161 OEl GLU 21 33.751 24.294 49.919 1.000 31.17

ANISOU 161 OEl GLU 21 2360 4428 5057 -1039 -1094 3 4 9

ATOM 162 OE2 GLU 21 32.664 23.590 48.171 1.000 31.16

ANISOU 162 OE2 GLU 21 2734 3901 5203 -1519 -1565 1123

ATOM 163 C GLU 21 29.159 20.594 48.689 1.000 16.44

ANISOU 163 C GLU 21 1271 2295 2679 -165 -53 4 3 0

ATOM 164 O GLU 21 28.599 19.700 49.329 1.000 14.30

ANISOU 164 O GLU 21 1271 2257 1907 -417 -301 3 6

ATOM 165 N PHE 22 28.548 21.257 47.708 1.000 16.14

ANISOU 165 N PHE 22 1440 2441 2253 -316 -28 3 2 8

ATOM 166 CA PHE 22 27.155 20.947 47.327 1.000 15.36

ANISOU 166 CA PHE 22 1530 2012 2294 -262 -173 2 8 1

ATOM 167 CB PHE 22 26.612 21.967 46.343 1.000 15.43

ANISOU 167 CB PHE 22 1863 2056 1944 -316 -247 184

ATOM 168 CG PHE 22 25.119 21.932 46.077 1.000 15.59

ANISOU 168 CG PHE 22 1822 2141 1962 -299 -170 5 6 1

ATOM 169 CDI PHE 22 24.218 21.987 47.129 1.000 17.03

ANISOU 169 CDI PHE 22 1923 2605 1943 -410 -162 - 40

ATOM 170 CD2 PHE 22 24.606 21.856 44.797 1.000 14.84

ANISOU 170 CD2 PHE 22 1541 2083 2013 51 -94 - 155

ATOM 171 CEl PHE 22 22.861 21.938 46.906 1.000 15.96

ANISOU 171 CEl PHE 22 1844 1805 2414 -159 -64 17 6

ATOM 172 CE2 PHE 22 23.243 21.797 44.551 1.000 15.81

ANISOU 172 CE2 PHE 22 1600 1993 2416 -261 -190 - 176

ATOM 173 CZ PHE 22 22.360 21.853 45.612 1.000 14.18

ANISOU 173 CZ PHE 22 1427 1430 2531 -105 -164 3 2 5

ATOM 174 C PHE 22 27.049 19.515 46.792 1.000 16.23

ANISOU 174 C PHE 22 1325 2042 2797 -110 164 1 02

ATOM 175 O PHE 22 26.183 18.751 47.229 1.000 13 .24

ANISOU 175 O PHE 22 1411 1743 1876 105 -194 3 9 1

ATOM 176 N ARG 23 27.888 19.097 45.853 1.000 15.45

ANISOU 176 N ARG 23 1585 2313 1971 -167 -80 2 8 9

ATOM 177 CA ARG 23 27.865 17.746 45.325 1.000 15.49

ANISOU 177 CA ARG 23 8092443 2634 50 -41 - 22

ATOM 178 CB ARG 23 28.928 17.539 44.248 1.000 17.81

ANISOU 178 CB ARG 23 9663142 2658 -1 28 43 - 167

ATOM 179 CG ARG 23 28.470 17.928 42.860 1.000 25.86

ANISOU 179 CG ARG 23 2719 4636 2470 -758 -176 - 4 9

ATOM 180 CD ARG 23 29.485 17.370 41.867 1.000 34.68

ANISOU 180 CD ARG 23 5148 4847 3183 -1532 1634 - 548

ATOM 181 NE ARG 23 30.660 18.253 41.877 1.000 31.13

ANISOU 181 NE ARG 23 2799 4194 4836 305 747 6 6

ATOM 182 CZ ARG 23 30.703 19.424 41.244 1.000 34.24

ANISOU 182 CZ ARG 23 2749 4844 5418 -757 239 7 64

ATOM 183 NHl . ARG 23 29.647 19.856 40.551 1.000 28.06

ANISOU ^■ 183 NHl . ARG 23 2714 3685 4263 -721 555 1 8 1 -96-

ATOM 184 NH2 ARG 23 31.830 20.114 41.340 1.000 36.08

ANISOU 184 NH2 ARG 23 2261 5328 6121 -562 776 - 8 ι

ATOM 185 C ARG 23 28.045 16.713 46.420 1.000 15.06

ANISOU 185 C ARG 23 1071 2061 2589 167 -32 - 23

ATOM 186 O ARG 23 27.335 15.687 46.410 1.000 16.28

ANISOU 186 O ARG 23 1443 2244 2497 -118 -71 - 21 77

ATOM 187 N ARG 24 28.952 16.988 47.353 1.000 15.27

ANISOU 187 N ARG 24 1024 2156 2623 -52 -21 2 9

ATOM 188 C ARG 24 29.193 16.003 48.430 1.000 17.70

ANISOU 188 CA ARG 24 1443 2589 2693 275 -2 2 1 5

ATOM 189 CB ARG 24 30.466 16.422 49.148 1.000 21.11

ANISOU 189 CB ARG 24 1244 3486 3289 484 -257 3 8 ■

ATOM 190 CG ARG 24 31.787 16.217 48.429 1.000 30.46

ANISOU 190 CG ARG 24 1438 5078 5057 426 441 3 0

ATOM 191 CD ARG 24 32.979 16.537 49.330 1.000 33 .50

ANISOU 191 CD ARG 24 1163 5831 5736 208 370 4 5

ATOM 192 NE ARG 24 33.636 17.804 49.071 1.000 51.46

ANISOU 192 NE ARG 24 5800 7316 6437 -2596 -1688 ι : 165

ATOM 193 CZ ARG 24 33.973 18.776 49.903 1.000 46.72

ANISOU 193 CZ ARG 24 4738 6888 6124 -1719 -1822 ι: 316

ATOM 194 NHl ARG 24 33.731 18.728 51.213 1.000 44.24

ANISOU 194 NHl ARG 24 2650 6998 7160 -392 1001 8 4

ATOM 195 NH2 ARG 24 34.579 19.871 49.448 1.000 42.82

ANISOU 195 NH2 ARG 24 5339 4428 6503 513 -991 12 : 16

ATOM 196 C ARG 24 27.972 15.887 49.334 1.000 17.16

ANISOU 196 C ARG 24 1549 2071 2900 129 140 2 9

ATOM 197 O ARG 24 27.536 14.779 49.713 1.000 15.38

ANISOU 197 O ARG 24 1706 1890 2247 72 -388 104

ATOM 198 N CYS 25 27.355 17.011 49.696 1.000 12.91

ANISOU 198 N CYS 25 907 1824 2176 -254 -386 151

ATOM 199 CA CYS 25 26.105 17.040 50.454 1.000 12.45

ANISOU 199 CA CYS 25 942 1838 1949 -178 -480 8 1

ATOM 200 CB CYS 25 25.660 18.491 50.697 1.000 11.67

ANISOU 200 CB CYS 25 1150 1759 1527 -136 -604 18

ATOM 201 SG CYS 25 23.973 18.580 51.425 1.000 14.90

ANISOU 201 SG CYS 25 1465 1593 2602 -164 -26 - 1

ATOM 202 C CYS 25 25.001 16.225 49.769 1.000 11.67

ANISOU 202 C CYS 25 893 1897 1645 -283 -64 - 8 6

ATOM 203 O CYS 25 24.360 15.377 50.390 1.000 12.73

ANISOU 203 O CYS 25 1347 1426 2064 -233 -196 12

ATOM 204 N LEU 26 24.798 16.461 48.470 1.000 11.70

ANISOU 204 N LEU 26 1102 1530 1814 -128 -390 1

ATOM 205 CA LEU 26 23.766 15.716 47.735 1.000 11.11

ANISOU 205 CA LEU 26 1190 1476 1556 -238 -79 - 1 94

ATOM 206 CB LEU 26 23.674 16.198 46.285 1.000 11.54

ANISOU 206 CB LEU 26 1345 1522 1518 -75 -84 - 2 02

ATOM 207 CG LEU 26 23.242 17.638 46.019 1.000 12.42

ANISOU 207 CG LEU 26 1199 1542 1978 -153 -167 - 4

ATOM 208 CDI , LEU 26 23.414 17.993 44.539 1.000 14.77

ANISOU 208 CDI , LEU 26 1428 1916 2270 43 131 4 01

ATOM 209 CD2 , LEU 26 21.814 17.885 46.466 1.000 14.45

ANISOU 209 CD2 : LEU 26 1384 2061 2047 264 -32 3 2

ATOM 210 C LEU 26 23.979 14.209 47.780 1.000 12.93

ANISOU 210 C LEU 26 1360 1542 2011 -121 -486 - 1 07

ATOM 211 O LEU 26 23.011 13.461 48.008 1.000 13 .78

ANISOU 211 O LEU 26 1660 1450 2125 -305 -426 - 5

ATOM 212 N ARG 27 25.196 13.721 47.576 1.000 14.09

ANISOU 212 N ARG 27 1518 1729 2108 151 -530 - 1 05

ATOM 213 CA ARG 27 25.491 12.283 47.574 1.00C ι 15.39

ANISOU 213 CA ARG 27 2260 1690 1897 186 141 - 3 54

ATOM 214 CB ARG 27 26.846 12.122 46.900 1.00C ) 17.04 -97-

ANISOU 214 C3 ARG 27 2259 2356 1861 517 49 - 248

ATOM 215 CG ARG 27 27.502 10.780 46.801 1.000 25.08

ANISOU 215 CG ARG 27 3110 2837 3583 1105 606 - 399

ATOM 216 CD ARG 27 28.995 10.992 46.457 1.000 30.32

ANISOU 216 CD ARG 27 2976 3836 4710 1190 720 - 1381

ATOM 217 NE ARG 27 29.818 11.407 47.581 1.000 36.51

ANISOU 217 NΞ ARG 27 3633 4937 5301 121 391 - 1429

ATOM 218 CZ ARG 27 30.988 12.019 47.560 1.000 38.07

ANISOU 218 CZ ARG 27 3334 5192 5941 364 661 - 1776

ATOM 219 NHl ARG 27 31.565 12.340 46.401 1.000 48.56

ANISOU 219 NHl ARG 27 44-82 7688 6280 -1305 736 - 1326

ATOM 220 NH2 ARG 27 31.606 12.328 48.701 1.000 40.23

ANISOU 220 NH2 ARG 27 2891 6127 6266 457 717 - 2463

ATOM 221 C ARG 27 25.479 11.630 48.949 1.000 14.66

ANISOU 221 c ARG 27 1720 1617 2233 135 -33 - 42

ATOM 222 0 ARG 27 24.968 10.499 49.072 1.000 17.44

ANISOU 222 0 ARG 27 1981 1533 3114 98 -394 15 5

ATOM 223 N ASP 28 26.031 12.308 49.973 1.000 13.72

ANISOU 223 N ASP 28 1703 1366 2146 317 -327 3 1 9

ATOM 224 CA ASP 28 26.227 11.701 51.277 1.000 15.33

ANISOU 224 C ASP 28 1886 1704 2234 538 -247 3 9 1

ATOM 225 CB ASP 28 27.541 12.280 51.842 1.000 18.31

ANISOU 225 CB ASP 28 2092 2709 2155 186 -465 544

ATOM 226 CG ASP 28 28.785 11.875 51.083 1.000 23 .06

ANISOU 226 CG ASP 28 2002 3583 3176 -96 -50 47 8

ATOM 227 ODl ASP 28 28.741 10.904 50.290 1.000 25.09

ANISOU 227 ODl ASP 28 2515 2855 4163 830 406 440

ATOM 228 OD2 ASP 28 29.831 12.528 51.283 1.000 30.05

ANISOU 228 OD2 ASP 28 1919 4262 5236 -216 -695 1058

ATOM 229 C ASP 28 25.092 11.910 52.267 1.000 14.90

ANISOU 229 C ASP 28 2071 1435 2154 411 -203 2 17

ATOM 230 O ASP 28 24.967 11.093 53.200 1.000 14.50

ANISOU 230 O ASP 28 1878 1501 2132 444 -265 179

ATOM 231 N LYS 29 24.317 12.975 52.096 1.000 12.90

ANISOU 231 N LYS 29 1487 1290 2126 77 -276 13 6

ATOM 232 CA LYS 29 23.265 13.368 53.029 1.000 12.95

ANISOU 232 CA LYS 29 1369 1649 1904 8 -390 1 4

ATOM 233 CB LYS 29 23.699 14.653 53.763 1.000 12.71

ANISOU 233 CB LYS 29 1105 1581 2145 209 -359 - 3 0

ATOM 234 CG LYS 29 25.016 14.504 54.518 1.000 16.11

ANISOU 234 CG LYS 29 1413 1998 2711 , 21 -818 - 161

ATOM 235 CD LYS 29 25.449 15.727 55.309 1.000 18.24

ANISOU 235 CD LYS 29 2500 1989 2442 -47 -1140 - 14

ATOM 236 CE LYS 29 26.789 15.445 56.002 1.000 19.36

ANISOU 236 CE LYS 29 2038 3171 2148 -90 -822 - 725

ATOM 237 NZ LYS 29 27.515 16.696 56.351 1.000 26.61

ANISOU 237 NZ LYS 29 2592 3146 4373 -309 -1571 - 353

ATOM 238 C LYS 29 21.888 13.550 52.386 1.000 11.62

ANISOU 238 C LYS 29 1432 1153 1831 52 -290 2 4

ATOM 239 O LYS 29 20.877 13.028 52.880 1.000 12.57

ANISOU 239 O LYS 29 1426 1556 1792 -97 -282 1 00

ATOM 240 N GLY 30 21.779 14.280 51.284 1.000 11.98

ANISOU 240 N GLY 30 1359 1454 1741 -5 -310 7 8

ATOM 241 CA GLY 30 20.510 14.478 50.562 1.000 ι 10.93

ANISOU 241 CA GLY 30 1192 1497 1465 -158 -116 - 18

ATOM 242 C GLY 30 19.544 15.433 51.242 1.00C 1 11.15

ANISOU 242 C GLY 30 1137 1143 1955 -260 -154 - 131

ATOM 243 O GLY 30 18.337 15.374 50.963 1.00C ) 11.26

ANISOU 243 O GLY 30 1247 1082 1949 -56 -419 1 04

ATOM 244 N LEU 31 20.064 16.278 52.129 1.00C ) 10.54

ANISOU 244 N LEU 31 1292 894 1821 -98 -367 8 9 ATOM 245 C LEU 31 19.272 17.324 52.803 1.000 11.07

ANISOU 245 CA LEU 31 1345 1111 1752 46 -520 - 3 3

ATOM 246 CB LEU 31 18.465 16.777 53.975 1.000 14.44

ANISOU 246 CB LEU 31 1753 1671 2062 -284 -80 - 178

ATOM 247 CG LEU 31 19.113 16.629 55.333 1.000 17.74

ANISOU 247 CG LEU 31 2456 2220 2064 -172 -115 4 9 9

ATOM 248 CDI LEU 31 18.220 15.978 56.371 1.000 26.19

ANISOU 248 CDI LEU 31 2716 4691 2543 -1224 -213 1016

ATOM 249 CD2 LEU 31 20.388 15.821 55.182 1.000 22.77

ANISOU 249 CD2 LEU 31 3121 2633 2899 650 -18 1487

ATOM 250 C LEU 31 20.176 18.498 53.195 1.000 10.95

ANISOU 250 C LEU 31 1041 1129 1989 180 -318 - 223

ATOM 251 O LEU 31 21.376 18.314 53.424 1.000 10.89

ANISOU 251 O LEU 31 1015 1171 1952 69 -160 2 04

ATOM 252 N PHE 32 19.570 19.688 53.219 1.000 11.42

ANISOU 252 N PHE 32 1134 995 2211 75 -273 6 5

ATOM 253 CA PHE 32 20.280 20.916 53.545 1.000 10.33

ANISOU 253 CA PHE 32 1071 1152 1703 -57 -288 - 3 3

ATOM 254 CB PHE 32 21.244 21.307 52.422 1.000 12.25

ANISOU 254 CB PHE 32 1054 1729 1872 -113 -173 - 5

ATOM 255 CG PHE 32 20.624 21.346 51.041 1.000 11.94

ANISOU 255 CG PHE 32 1158 1572 1809 -281 -148 12 2

ATOM 256 CDI PHE 32 20.522 20.188 50.270 1.000 11.12

ANISOU 256 CDI PHE 32 1070 1308 1846 -182 -458 3 18

ATOM 257 CD2 PHE 32 20.145 22.528 50.513 1.000 12.14

ANISOU 257 CD2 PHE 32 1618 1353 1639 -300 -185 - 47

ATOM 258 CEl PHE 32 19.943 20.212 49.015 1.000 12.00

ANISOU 258 CEl PHE 32 1342 1377 1840 -301 -468 3 3 2

ATOM 259 CE2 PHE 32 19.553 22.534 49.266 1.000 12.79

ANISOU 259 CE2 PHE 32 1858 1543 1457 -86 -34 2 8

ATOM 260 CZ PHE 32 19.416 21.376 48.503 1.000 11.50

ANISOU 260 CZ PHE 32 1623 1414 1331 -76 -272 2 17

ATOM 261 C PHE 32 19.310 22.071 53.762 1.000 9 .82

ANISOU 261 C PHE 32 1015 1042 1674 -120 -367 - 77

ATOM 262 O PHE 32 18.165 21.990 53.285 1.000 11.29

ANISOU 262 O PHE 32 1097 1286 1906 -95 -495 - 77

ATOM 263 N TYR 33 19.736 23.099 54.493 1.000 12.68

ANISOU 263 N TYR 33 1606 1053 2158 -57 -766 - 159

ATOM 264 CA TYR 33 18.945 24.335 54.607 1.000 10.64

ANISOU 264 CA TYR 33 1491 1173 1380 -77 -97 - 132

ATOM 265 CB TYR 33 19.141 25.022 55.955 1.000 10.85

ANISOU 265 CB TYR 33 1019 1725 1379 -260 -224 - 164

ATOM 266 CG TYR 33 18.545 24.331 57.156 1.000 10.71

ANISOU 266 CG TYR 33 1173 1552 1342 -45 -230 - 117

ATOM 267 CDI TYR 33 17.266 24.643 57.619 1.000 11.64

ANISOU 267 CDI TYR 33 1385 1441 1596 -68 83 - 94

ATOM 268 CEl TYR 33 16.694 24.023 58.719 1.000 13.60

ANISOU 268 CEl TYR 33 1879 1483 1804 -147 339 - 2 6

ATOM 269 CD2 TYR 33 19.273 23.364 57.853 1.000 14.04

ANISOU 269 CD2 TYR 33 1604 2040 1689 132 -509 12 7

ATOM 270 CE2 TYR 33 18.711 22.752 58.964 1.000 15.75

ANISOU 270 CE2 TYR 33 1872 2227 1886 -187 -701 43 3

ATOM 271 CZ TYR 33 17.438 23.078 59.387 1.000 16.02

ANISOU 271 CZ TYR 33 2205 1939 1942 -332 -154 3 0 0

ATOM 272 OH TYR 33 16.919 22.454 60.504 1.000 19.95

ANISOU 272 OH TYR 33 3412 2154 2015 -60 278 4 0 0

ATOM 273 C TYR 33 19.357 25.253 53.452 1.000 10.92

ANISOU 273 C TYR 33 1249 1448 1453 -125 -271 1 49

ATOM 274 O TYR 33 20.514 25.192 53.006 1.000 11.50

ANISOU 274 O TYR 33 1204 1375 1791 -98 -270 2 8 1

ATOM 275 N LEU 34 18.399 26.049 53.000 1.000 11.28 ANISOU 275 N LEU 34 1159 1265 1862 -210 -149 12 1

ATOM 276 CA LEU 34 18.577 26.942 51.864 1.000 12.99

ANISOU 276 CA LEU 34 1565 1444 1926 81 -478 2 74

ATOM 277 CB LEU 34 17.757 26.420 50.682 1.000 13.96

ANISOU 277 CB LEU 34 2007 1301 1995 -430 -459 3 2 1

ATOM 278 CG LEU 34 17.990 27.112 49.334 1.000 13 .81

ANISOU 278 CG LEU 34 2085 1322 1839 -331 -365 1 9 8

ATOM 279 CDI LEU 34 19.308 26.691 48.704 1.000 15.94

ANISOU 279 CDI LEU 34 2123 1793 2140 -10 -313 607

ATOM 280 CD2 LEU 34 16.818 26.799 48.411 1.000 16.36

ANISOU 280 CD2 LEU 34 2186 1837 2193 122 -721 13 4

ATOM 281 C LEU 34 18.195 28.361 52.241 1.000 13 .03

ANISOU 281 C LEU 34 1676 1418 1857 31 -643 2 1 8

ATOM 282 O LEU 34 17.055 28.647 52.595 1.000 13 .99

ANISOU 282 O LEU 34 1690 1281 2344 140 -714 8 5

ATOM 283 N THR 35 19.148 29.283 52.175 1.000 15.03

ANISOU 283 N THR 35 1837 1584 2288 -118 -625 - 3

ATOM 284 CA THR 35 18.918 30.704 52.369 1.000 14.80

ANISOU 284 CA THR 35 1866 1560 2196 -169 -175 - 144

ATOM 285 CB THR 35 20.013 31.366 53.232 1.000 15.65

ANISOU 285 CB THR 35 2025 1719 2202 -149 -204 - 281

ATOM 286 OGl THR 35 21.276 31.115 52.601 1.000 18.81

ANISOU 286 OGl THR 35 1885 2679 2583 -279 -229 - 728

ATOM 287 CG2 THR 35 20.138 30.811 54.622 1.000 18.84

ANISOU 287 CG2 THR 35 2523 2207 2427 -850 -510 1 5 5

ATOM 288 C THR 35 18.915 31.456 51.043 1.000 15.07

ANISOU 288 C THR 35 1904 1473 2348 -57 -283 - 7 0

ATOM 289 O THR 35 19.209 30.909 49.973 1.000 15.00

ANISOU 289 O THR 35 2034 1520 2145 -215 -372 8 9

ATOM 290 N ASP 36 18.564 32.739 51.086 1.000 17.46

ANISOU 290 N ASP 36 2302 1366 2968 -209 -766 - 120

ATOM 291 CA ASP 36 18.618 33.606 49.924 1.000 17.91

ANISOU 291 CA ASP 36 2150 1592 3063 112 -660 8 6

ATOM 292 CB ASP 36 20.063 33.845 49.471 1.000 17.91

ANISOU 292 CB ASP 36 2153 1584 3067 84 -587 - 42

ATOM 293 CG ASP 36 20.948 34.545 50.469 1.000 19.23

ANISOU 293 CG ASP 36 2575 2160 2571 -642 -324 1 8 1

ATOM 294 ODl ASP 36 20.426 35.304 51.325 1.000 24.17

ANISOU 294 ODl ASP 36 2843 3055 3284 152 -1013 - 652

ATOM 295 OD2 ASP 36 22.199 34.355 50.412 1.000 21.00

ANISOU 295 OD2 ASP 36 2637 2571 2772 -382 -834 - 393

ATOM 296 C ASP 36 17.783 33.038 48.784 1.000 18.20

ANISOU 296 C ASP 36 2402 1736 2779 -446 -390 1 9 1

ATOM 297 O ASP 36 18.222 33.063 47.629 1.000 18.98

ANISOU 297 O ASP 36 2127 2022 3062 -464 -60 - 252

ATOM 298 N CYS 37 16.593 32.547 49.077 1.000 17.22

ANISOU 298 N CYS 37 1873 2190 2479 63 -350 - 1

ATOM 299 CA CYS 37 15.730 31.945 48.043 1.000 15.98

ANISOU 299 CA CYS 37 1997 1590 2485 -81 -65 - 184

ATOM 300 CB CYS 37 15.621 30.423 48.252 1.000 18.87

ANISOU 300 CB CYS 37 2112 1790 3268 -114 -405 5 7 0

ATOM 301 SG CYS 37 14.753 29.917 49.759 1.000 19.42

ANISOU 301 SG CYS 37 2532 1683 3164 -74 -230 3 2 2

ATOM 302 C CYS 37 14.349 32.580 47.958 1.000 16.12

ANISOU 302 C CYS 37 1992 1669 2465 -175 -504 1 6

ATOM 303 O CYS 37 13.483 32.032 47.253 1.000 20.60

ANISOU 303 O CYS 37 2761 1769 3296 -241 -1333 5 1

ATOM 304 N GLY 38 14.125 33.714 48.617 1.000 17.89

ANISOU 304 N GLY 38 1847 1572 3381 209 -898 - 111

ATOM 305 CA GLY 38 12.850 34.404 48.587 1.00C ι 18.16

ANISOU 305 CA GLY 38 1608 2126 3164 141 -999 - 6 ATOM 306 C GLY 38 11.843 33.864 49.589 1.000 21.98

ANISOU 306 C GLY 38 2598 2574 3180 262 -97 - 455

ATOM 307 0 GLY 38 10.677 34.273 49.499 1.000 22 .75

ANISOU 307 0 GLY 38 2542 3027 3073 241 79 - 9 7

ATOM 308 N LEU 39 12.241 32.982 50.501 1.000 21.93

ANISOU 308 N LEU 39 2112 3318 2903 -65 -102 - 154

ATOM 309 CA LEU 39 11.443 32.357 51.545 1.000 26.16

ANISOU 309 CA LEU 39 3141 3610 3188 -1071 162 - 400

ATOM 310 CB LEU 39 11.220 30.868 51.277 1.000 28 .13

ANISOU 310 CB LEU 39 2980 3192 4516 -352 -848 2 5 8

ATOM 311 CG LEU 39 10.296 30.434 50.157 1.000 27.39

ANISOU 311 CG LEU 39 3352 2591 4463 541 -637 - 1052

ATOM 312 CDI LEU 39 10.472 28.940 49.910 1.000 28.66

ANISOU 312 CDI LEU 39 3375 2293 5221 581 -150 - 190

ATOM 313 CD2 LEU 39 8.838 30.768 50.478 1.000 30.62

ANISOU 313 CD2 LEU 39 3155 2985 5496 1275 -1485 - 208

ATOM 314 C LEU 39 12.060 32.430 52.949 1.000 26.26

ANISOU 314 C LEU 39 2868 3969 3143 -796 170 3 3 5

ATOM 315 O LEU 39 13.105 31.861 53.266 1.000 35.57

ANISOU 315 O LEU 39 4990 4057 4470 804 -630 3 2 0

ATOM 316 N THR 40 11.388 33.136 53.827 1.000 26.61

ANISOU 316 N THR 40 3425 3883 2803 -703 -191 102

ATOM 317 CA THR 40 11.676 33.329 55.228 1.000 22 .95

ANISOU 317 CA THR 40 1972 3864 2886 4 -608 51 8

ATOM 318 C THR 40 10.380 33.424 56.031 1.000 27.03

ANISOU 318 C THR 40 2331 4900 3040 -690 -220 - 3

ATOM 319 O THR 40 9.254 33.316 55.537 1.000 25.98

ANISOU 319 O THR 40 2148 4860 2864 -546 36 - 720

ATOM 320 CB THR 40 12.476 34.624 55.456 1.000 27.16

ANISOU 320 CB THR 40 2646 4799 2874 -932 -391 148

ATOM 321 OGl THR 40 11.639 35.687 54.986 1.000 36.24

ANISOU 321 OGl THR 40 5158 3872 4740 -472 -136 6 6 0

ATOM 322 CG2 THR 40 13.771 34.669 54.659 1.000 34.29

ANISOU 322 CG2 THR 40 5268 3289 4470 -1303 2206 42 9

ATOM 323 N ASP 41 10.524 33.635 57.346 1.000 28.20

ANISOU 323 N ASP 41 2270 5223 3223 -711 -317 - 479

ATOM 324 CA ASP 41 9.324 33.604 58.191 1.000 25.10

ANISOU 324 CA ASP 41 1935 4633 2968 13 -551 - 505

ATOM 325 C ASP 41 8.418 34.785 57.896 1.000 24.69

ANISOU 325 C ASP 41 2686 3839 2855 -446 -749 - 241

ATOM 326 O ASP 41 7.219 34.846 58.163 1.000 24.79

ANISOU 326 O ASP 41 2757 2721 3941 174 -584 - 141

ATOM 327 CB ASP 41 9.728 33.549 59.678 1.000 28.21

ANISOU 327 CB ASP 41 2221 5503 2995 892 -594 - 555

ATOM 328 CG ASP 41 9.892 32.129 60.180 1.000 42.46

ANISOU 328 CG ASP 41 6437 5911 3784 -1196 -1257 82 6

ATOM 329 ODl ASP 41 9.705 31.161 59.401 1.000 55.96

ANISOU 329 ODl ASP 41 12184 5138 3940 -2654 -82 1249

ATOM 330 OD2 ASP 41 10.214 31.951 61.383 1.000 61.55

ANISOU 330 OD2 ASP 41 10370 7470 5548 -4396 -4720 2309

ATOM 331 N THR 42 8.991 35.807 57.305 1.000 29.30

ANISOU 331 N THR 42 3761 4531 2839 -1404 -1089 - 72

ATOM 332 CA THR 42 8.255 36.976 56.863 1.000 33 .69

ANISOU 332 CA THR 42 4852 3472 4475 -1524 -819 - 127

ATOM 333 C THR 42 7.199 36.598 55.834 1.000 29.14

ANISOU 333 C THR 42 3354 3051 4667 204 -648 - 277

ATOM 334 O THR 42 6.026 36.969 55.844 1.000 36.90

ANISOU 334 O THR 42 3578 2980 7462 603 -176 643

ATOM 335 CB THR 42 9.282 37.967 56.281 1.000 40.80

ANISOU 335 CB THR 42 5831 4318 5354 -2254 -450 3 7

ATOM 336 OGl . THR 42 10.288 38.317 57.263 1.000 46.30 ANISOU 336 OGl THR 42 6998 3682 6912 ^■3163 '8 1 7 7

ATOM 337 CG2 THR 42 8.582 39.253 55.872 1.000 45.59

ANISOU 337 CG2 THR 42 9083 3877 4363 -2166 -1048 2 3 8

ATOM 338 N GLU 43 7.573 35.773 54.862 1.000 31.74

ANISOU 338 N GLU 43 3380 4360 4319 -673 -223 - 782

ATOM 339 CA GLU 43 6.647 35.355 53.810 1.000 35.40

ANISOU 339 CA GLU 43 4856 4683 3913 -1510 -860 3 2 9

ATOM 340 C GLU 43 5.643 34.324 54.330 1.000 28.03

ANISOU 340 C GLU 43 2988 3297 4363 -41 -919 1 6 8

ATOM 341 O GLU 43 4.560 34.138 53.764 1.000 38.18

ANISOU 341 O GLU 43 3818 2970 7717 -66 -2774 1469

ATOM 342 CB GLU 43 7.423 34.811 52.608 1.000 38.89

ANISOU 342 CB GLU 43 4464 6532 3779 -2546 -860 - 393

ATOM 343 CG GLU 43 8.462 35.745 52.010 1.000 46.47

ANISOU 343 CG GLU 43 5175 7105 5377 -2936 -92 - 289

ATOM 344 CD GLU 43 9.750 35.764 52.826 1.000 46.40

ANISOU 344 CD GLU 43 4506 7977 5145 -3155 548 - 1210

ATOM 345 OEl GLU 43 9.775 36.447 53.880 1.000 55.20

ANISOU 345 OEl GLU 43 8741 7607 4627 -2062 -1002 - 669

ATOM 346 OE2 GLU 43 10.706 35.080 52.433 1.000 56.77

ANISOU 346 OE2 GLU 43 4592 8930 8050 -2652 939 - 1258

ATOM 347 N LEU 44 5.980 33.645 55.426 1.000 22.72

ANISOU 347 N LEU 44 2508 2161 3964 464 -476 - 450

ATOM 348 CA LEU 44 5.117 32.592 55.959 1.000 26.76

ANISOU 348 CA LEU 44 4009 1973 4187 140 570 - 986

ATOM 349 CB LEU 44 5.978 31.585 56.727 1.000 28.25

ANISOU 349 CB LEU 44 5094 2194 3448 -153 277 - 562

ATOM 350 CG LEU 44 5.284 30.494 57.533 1.000 32.03

ANISOU 350 CG LEU 44 5971 2801 3398 -279 1192 - 627

ATOM 351 CDI LEU 44 4.485 29.535 56.656 1.000 37.95

ANISOU 351 CDI LEU 44 7665 2239 4514 -1148 2039 - 1403

ATOM 352 CD2 LEU 44 6.302 29.703 58.361 1.000 36.97

ANISOU 352 CD2 LEU 44 7096 2869 4080 1150 2171 1 8 6

ATOM 353 C LEU 44 4.000 33.145 56.841 1.000 31.10

ANISOU 353 C LEU 44 3835 3182 4800 -700 837 -2205

ATOM 354 O LEU 44 2.913 32.543 56.867 1.000 30.19

ANISOU 354 O LEU 44 4402 3299 3768 -1248 870 -2165

ATOM 355 N ALA 45 4.238 34.247 57.547 1.000 28.74

ANISOU 355 N ALA 45 2897 2938 5083 -562 710 -2061

ATOM 356 CA ALA 45 3.382 34.751 58.623 1.000 27.09

ANISOU 356 CA ALA 45 2716 2817 4761 -751 467 -2140

ATOM 357 C ALA 45 1.943 35.014 58.195 1.000 24.95

ANISOU 357 C ALA 45 2697 3110 3673 -784 709 -1257

ATOM 358 O ALA 45 1.021 34.515 58.875 1.000 22.50

ANISOU 358 O ALA 45 2762 2585 3201 -565 560 -1146

ATOM 359 CB ALA 45 3.975 36.005 59.248 1.000 36.30

ANISOU 359 CB ALA 45 3259 4219 6315 -1912 1332 - 3404

ATOM 360 N SER 46 1.729 35.779 57.128 1.000 26.85

ANISOU 360 N SER 46 3258 3756 3187 -1732 618 - 1184

ATOM 361 CA SER 46 0.380 36.052 56.642 1.000 24.97

ANISOU 361 CA SER 46 3686 3189 2611 -1223 511 - 1105

ATOM 362 CB SER 46 0.422 36.950 55.392 1.000 32.35

ANISOU 362 CB SER 46 5428 3467 3395 -2232 70 - 458

ATOM 363 OG SER 46 0.630 38.289 55.772 1.000 45.77

ANISOU 363 OG SER 46 7730 3349 6313 -2746 2499 - 807

ATOM 364 C SER 46 -0.408 34.787 56.307 1.000 20.63

ANISOU 364 C SER 46 2797 2469 2572 -423 -151 - 542

ATOM 365 O SER 46 -1.578 34.672 56.698 1.000 21.93

ANISOU 365 O SER 46 3120 2486 2725 -559 305 -403

ATOM 366 N ALA 47 0.211 33.855 55.590 1.000 22.39

ANISOU 366 N ALA 47 3096 2167 3244 -488 394 - 368 ATOM 367 CA ALA 47 -0.397 32.596 55.176 1.000 19.54

ANISOU 367 CA ALA 47 2746 1863 2814 -289 362 - 18

ATOM 368 CB ALA 47 0.548 31.900 54.191 1.000 23 .54

ANISOU 368 CB ALA 47 3524 1717 3705 -617 1237 - 159

ATOM 369 C ALA 47 -0.715 31.714 56.381 1.000 19.95

ANISOU 369 C ALA 47 2282 2546 2752 -327 19 2 5 7

ATOM 370 O ALA 47 -1.836 31.199 56.518 1.000 19.66

ANISOU 370 O ALA 47 2489 2589 2393 -614 211 - 165

ATOM 371 N LYS 48 0.270 31.558 57.268 1.000 18.24

ANISOU 371 N LYS 48 2713 1966 2253 -210 -139 - 912

ATOM 372 CA LYS 48 0.042 30.782 58.486 1.000 19.33

ANISOU 372 CA LYS 48 2398 2625 2321 43 -312 - 563

ATOM 373 C LYS 48 -1.110 31.329 59.322 1.000 20.57

ANISOU 373 C LYS 48 2476 2556 2785 -326 83 - 566

ATOM 374 O LYS 48 -2.022 30.613 59.771 1.000 20.34

ANISOU 374 O LYS 48 3207 2598 1923 -521 139 - 340

ATOM 375 CB LYS 48 1.352 30.758 59.294 1.000 24.61

ANISOU 375 CB LYS 48 2400 3792 3158 -258 -556 - 8 0

ATOM 376 CG LYS 48 1.237 29.873 60.531 1.000 30.84

ANISOU 376 CG LYS 48 4306 4044 3366 -291 -1504 2 77

ATOM 377 CD LYS 48 1.837 30.575 61.736 1.000 41.45

ANISOU 377 CD LYS 48 6742 5755 3251 -1067 -1382 - 356

ATOM 378 CE LYS 48 1.625 29.717 62.966 1.000 41.63

ANISOU 378 CE LYS 48 6620 6124 3073 -466 -1047 - 353

ATOM 379 NZ LYS 48 1.074 30.497 64.112 1.000 42.62

ANISOU 379 NZ LYS 48 5883 6866 3444 460 -1193 - 425

ATOM 380 N ASP 49 -1.110 32.625 59.607 1.000 19.18

ANISOU 380 N ASP 49 2348 2602 2337 -464 100 - 806

ATOM 381 CA ASP 49 -2.127 33.243 60.433 1.000 21.95

ANISOU 381 CA ASP 49 2555 2986 2801 -791 617 -1035

ATOM 382 CB ASP 49 -1.868 34.756 60.611 1.000 23.97

ANISOU 382 CB ASP 49 2827 2872 3409 -250 -79 -1325

ATOM 383 CG ASP 49 -0.681 35.078 61.492 1.000 25.41

ANISOU 383 CG ASP 49 2787 3405 3464 -365 113 -1866

ATOM 384 ODl ASP 49 -0.153 34.153 62.143 1.000 30.75

ANISOU 384 ODl ASP 49 3572 4181 3932 -254 -967 -1667

ATOM 385 OD2 ASP 49 -0.235 36.256 61.563 1.000 30.78

ANISOU 385 OD2 ASP 49 3303 3649 4742 -710 344 -2413

ATOM 386 C ASP 49 -3.543 33.061 59.904 1.000 21.44

ANISOU 386 C ASP 49 2465 2651 3030 -388 540 - 900

ATOM 387 O ASP 49 -4.476 32.770 60.654 1.000 20.72

ANISOU 387 O ASP 49 2346 2181 3347 -279 550 - 726

ATOM 388 N LEU 50 -3.731 33.269 58.596 1.000 23.28

ANISOU 388 N LEU 50 2942 2712 3191 -1251 216 - 644

ATOM 389 CA LEU 50 -5.086 33.185 58.068 1.000 22.94

ANISOU 389 CA LEU 50 3104 1796 3815 -575 -205 - 1079

ATOM 390 CB LEU 50 -5.204 33.861 56.696 1.000 28.78

ANISOU 390 CB LEU 50 3948 2453 4535 -852 -755 - 254

ATOM 391 CG LEU 50 -6.620 34.246 56.260 1.000 25.30

ANISOU 391 CG LEU 50 3800 2294 3520 30 325 - 531

ATOM 392 CDI . LEU 50 -7.552 34.478 57.441 1.000 44.77

ANISOU 392 CDI . LEU 50 6382 4432 6196 -475 3026 - 1060

ATOM 393 CD2 : LEU 50 -6.625 35.485 55.385 1.000 32.52

ANISOU 393 CD2 : LEU 50 5861 1962 4533 752 354 - 433

ATOM 394 C LEU 50 -5.566 31.737 57.982 1.000 21.12

ANISOU 394 C LEU 50 2559 1870 3595 -643 742 -1270

ATOM 395 O LEU 50 -6.772 31.494 58.175 1.000 21.13

ANISOU ^' 395 O LEU 50 2491 2457 3083 -543 579 -1097

ATOM 396 N VAL 51 -4.681 30.769 57.715 1.000 16.27

ANISOU ^• 396 N VAL 51 2517 1843 1823 -302 -3 - 646

ATOM 397 CA VAL 51 -5.186 29.370 57.701 1.000 18.07 ANISOU 397 CA VAL 51 3154 1763 1947 -401 -15 - 427

ATOM 398 CB VAL 51 -4.281 28.415 56.889 1.000 16.07

ANISOU 398 CB VAL 51 2981 1629 1496 -621 -255 - 501

ATOM 399 CGI VAL 51 -3.002 28.114 57.668 1.000 18 .99

ANISOU 399 CGI VAL 51 2959 2382 1875 -383 -100 3 02

ATOM 400 CG2 VAL 51 -5.006 27.119 56.497 1.000 22.16

ANISOU 400 CG2 VAL 51 4569 2121 1728 -1393 64 - 869

ATOM 401 C VAL 51 -5.446 28.899 59.114 1.000 17.74

ANISOU 401 C VAL 51 2508 2223 2009 -435 142 - 445

ATOM 402 O VAL 51 -6.430 28.187 59.346 1.000 19.76

ANISOU 402 O VAL 51 3005 2160 2345 -692 726 - 1021

ATOM 403 N ILE 52 -4.671 29.263 60.125 1.000 20.23

ANISOU 403 N ILE 52 2980 2945 1760 -649 364 - 902

ATOM 404 CA ILE 52 -4.990 28.875 61.507 1.000 20.17

ANISOU 404 CA ILE 52 3200 2665 1800 -758 627 - 1134

ATOM 405 CB ILE 52 -3.847 29.230 62.469 1.000 21.31

ANISOU 405 CB ILE 52 3294 3151 1652 -449 462 -1043

ATOM 406 CG2 ILE 52 -4.238 29.178 63.931 1.000 21.29

ANISOU 406 CG2 ILE 52 3543 2826 1719 -362 529 - 689

ATOM 407 CGI ILE 52 -2.619 28.346 62.217 1.000 25.37

ANISOU 407 CGI ILE 52 3213 3819 2608 -307 727 - 1090

ATOM 408 CDI ILE 52 -2.871 26.872 62.470 1.000 28.56

ANISOU 408 CDI ILE 52 3474 3578 3798 106 178 - 1110

ATOM 409 C ILE 52 -6.284 29.514 61.950 1.000 22.44

ANISOU 409 C ILE 52 3119 3216 2190 -710 645 -1228

ATOM 410 O ILE 52 -7.072 28.856 62.647 1.000 23.23

ANISOU 410 O ILE 52 3390 3654 1781 -766 758 -1246

ATOM 411 N ASP 53 -6.519 30.754 61.530 1.000 23.33

ANISOU 411 N ASP 53 2897 3064 2903 -626 700 -1361

ATOM 412 CA ASP 53 -7.826 31.335 61.897 1.000 24.49

ANISOU 412 CA ASP 53 2818 3347 3141 -759 781 -1545

ATOM 413 CB ASP 53 -7.942 32.781 61.411 1.000 27.43

ANISOU 413 CB ASP 53 2854 3335 4235 -434 819 -1446

ATOM 414 CG ASP 53 -9.309 33.397 61.570 1.000 30.99

ANISOU 414 CG ASP 53 3166 4281 4326 36 1242 -1214

ATOM 415 ODl ASP 53 -9.657 33.779 62.705 1.000 37.26

ANISOU 415 ODl ASP 53 4369 4569 5220 153 1263 -2733

ATOM 416 OD2 ASP 53 -10.050 33.491 60.553 1.000 38.45

ANISOU 416 OD2 ASP 53 3393 6043 5173 810 557 -1648

ATOM 417 C ASP 53 -8.953 30.495 61.316 1.000 24.64

ANISOU 417 C ASP 53 3028 3701 2634 -919 372 -1031

ATOM 418 O ASP 53 -10.011 30.327 61.915 1.000 28.52

ANISOU 418 O ASP 53 3399 3835 3603 -1519 962 -2151

ATOM 419 N PHE 54 -8.744 29.978 60.108 1.000 22.04

ANISOU 419 N PHE 54 2921 2974 2479 -573 174 - 704

ATOM 420 CA PHE 54 -9.772 29.187 59.432 1.000 19.99

ANISOU 420 CA PHE 54 2253 2879 2463 -421 771 - 978

ATOM 421 CB PHE 54 -9.423 29.030 57.942 1.000 18.45

ANISOU 421 CB PHE 54 2856 1983 2171 -65 426 - 518

ATOM 422 CG PHE 54 -10.492 ; 28.292 57.145 1.000 21.36

ANISOU 422 CG PHE 54 3063 2735 2318 -646 599 - 627

ATOM 423 CDI PHE 54 -11.714 = 28.906 56.933 1.000 23.18

ANISOU 423 CDI PHE 54 3199 2783 2826 -703 -29 - 624

ATOM 424 CD2 PHE 54 -10.29] 1 27.035 56.619 1.000 23.32

ANISOU 424 CD2 PHE 54 3482 2802 2577 -689 212 - 858

ATOM 425 CEl PHE 54 -12.71Σ ⁾ 28.291 56.241 1.000 26.45

ANISOU 425 CEl , PHE 54 3345 3696 3008 -1418 129 - 554

ATOM 426 CE2 PHE 54 -11.301 5 26.375 55.921 1.000 25.65

ANISOU 426 CE2 PHE 54 3750 3815 2182 -1404 607 - 1005

ATOM 427 CZ PHE 54 -12.522 27.013 55.725 1.000 26.17

ANISOU ^■ 427 CZ PHE 54 3433 3830 2679 -1829 298 - 813 ATOM 428 C PHE 54 -9.959 27.854 60.132 1.000 19 .44

ANISOU 428 C PHE 54 2340 3430 1617 -834 319 - 759

ATOM 429 O PHE 54 -11.087 27.450 60.386 1.000 22.11

ANISOU 429 O PHE 54 2601 3066 2734 -948 1018 - 1466

ATOM 430 N PHE 55 -8.882 27.166 60.448 1.000 20.59

ANISOU 430 N PHE 55 2728 3375 1720 -666 180 - 611

ATOM 431 CA PHE 55 -8.966 25.927 61.212 1.000 22.59

ANISOU 431 CA PHE 55 3092 3671 1820 -728 381 - 372

ATOM 432 CB PHE 55 -7.579 25.360 61.478 1.000 21.93

ANISOU 432 CB PHE 55 3163 3622 1549 -692 287 - 158

ATOM 433 CG PHE 55 -6.790 24.833 60.284 1.000 20.60

ANISOU 433 CG PHE 55 3034 2998 1793 -1004 365 - 375

ATOM 434 CDI PHE 55 -7.352 24.526 59.057 1.000 18.72

ANISOU 434 CDI PHE 55 2300 3095 1717 -1078 586 - 271

ATOM 435 CD2 PHE 55 -5.430 24.615 60.385 1.000 18.06

ANISOU 435 CD2 PHE 55 3132 2490 1241 -926 128 - 497

ATOM 436 CEl PHE 55 -6.609 24.037 58.014 1.000 18.92

ANISOU 436 CEl PHE 55 2455 2761 1971 -844 436 - 542

ATOM 437 CE2 PHE 55 -4.672 24.124 59.352 1.000 18.58

ANISOU 437 CE2 PHE 55 3291 2606 1163 -478 63 - 299

ATOM 438 CZ PHE 55 -5.256 23.814 58.134 1.000 17.68

ANISOU 438 CZ PHE 55 2660 2567 1490 -380 129 - 806

ATOM 439 C PHE 55 -9.684 26.111 62.546 1.000 24.99

ANISOU 439 C PHE 55 3310 4138 2046 -830 647 - 415

ATOM 440 O PHE 55 -10.532 25.281 62.872 1.000 30.29

ANISOU 440 O PHE 55 3802 4943 2763 -1527 1314 - 1102

ATOM 441 N GLU 56 -9.330 27.144 63.311 1.000 23 .65

ANISOU 441 N GLU 56 2864 4109 2013 -634 937 - 525

ATOM 442 CA GLU 56 -9.868 27.355 64.636 1.000 30.01

ANISOU 442 CA GLU 56 3632 5378 2394 -1050 1465 - 994

ATOM 443 CB GLU 56 -8.998 28.333 65.436 1.000 36.40

ANISOU 443 CB GLU 56 4531 6933 2367 -1606 1318 - 1623

ATOM 444 CG GLU 56 -7.666 27.827 65.916 1.000 41.89

ANISOU 444 CG GLU 56 5006 8196 2713 -1457 404 - 1900

ATOM 445 CD GLU 56 -6.787 28.880 66.575 1.000 48.94

ANISOU 445 CD GLU 56 6081 9310 3202 -2278 -73 - 2062

ATOM 446 OEl GLU 56 -5.694 28.515 67.078 1.000 60.73

ANISOU 446 OEl GLU 56 8034 12274 2769 -3208 -2335 2 66

ATOM 447 OE2 GLU 56 -7.145 30.084 66.614 1.000 58.51

ANISOU 447 OE2 GLU 56 8742 9338 4151 -2088 1096 - 3951

ATOM 448 C GLU 56 -11.289 27.920 64.617 1.000 30.60

ANISOU 448 C GLU 56 3764 4923 2941 -977 1967 - 1271

ATOM 449 O GLU 56 -12.058 : 27.542 65.504 1.000 35.21

ANISOU 449 O GLU 56 4384 5304 3690 -1136 2652 - 1235

ATOM 450 N HIS 57 -11.603 . 28.805 63.673 1.000 30.00

ANISOU 450 N HIS 57 3730 4846 2823 -654 1684 - 1582

ATOM 451 CA HIS 57 -12.854 .29.559 63.759 1.000 33 .51

ANISOU 451 CA HIS 57 3853 5101 3778 -519 1673 - 1911

ATOM 452 CB HIS 57 -12.536 J 31.046 63.991 1.000 33 .40

ANISOU 452 CB HIS 57 3844 5183 3664 -411 1546 -2250

ATOM 453 CG HIS 57 -11.57^' ' 31.344 65.095 1.000 35.13

ANISOU 453 CG HIS 57 4497 5409 3444 -505 1340 - 1992

ATOM 454 CD2 HIS 57 -10.361 31.946 65.071 1.000 35.26

ANISOU 454 CD2 HIS 57 4837 5214 3345 -834 637 - 1456

ATOM 455 NDl , HIS 57 -11.819 31.021 66.411 1.000 40.52

ANISOU 455 NDl . HIS 57 6021 5885 3490 -1360 1474 - 2002

ATOM 456 CEl . HIS 57 -10.798 31.410 67.151 1.000 42.28

ANISOU 456 CEl . HIS 57 6680 6066 3320 -1632 1099 - 1772

ATOM 457 NE2 ! HIS 57 -9.902 31.970 66.362 1.000 41.69

ANISOU 457 NE2 ! HIS 57 6377 6133 3329 -1817 407 - 1148

ATOM 458 C HIS 57 -13.769 29.466 62.547 1.000 32 .58 ANISOU 458 C HIS 57 3083 5097 4199 -729 1723 -2066

ATOM 459 0 HIS 57 -14.902 29.965 62.578 1.000 33 .80

ANISOU 459 0 HIS 57 3121 5097 4625 -731 1865 -2565

ATOM 460 N GLY 58 -13.370 28.866 61.432 1.000 28 .78

ANISOU 460 N GLY 58 2841 4353 3742 -253 1341 - 1506

ATOM 461 CA GLY 58 -14.326 28.685 60.332 1.000 26.99

ANISOU 461 CA GLY 58 2471 3916 3869 24 1298 -1173

ATOM 462 C GLY 58 -15.447 27.737 60.738 1.000 29.94

ANISOU 462 C GLY 58 2665 4357 4353 -261 1323 -1058

ATOM 463 O GLY 58 -15.241 26.805 61.534 1.000 29.23

ANISOU 463 O GLY 58 2976 4044 4087 -571 1192 -1297

ATOM 464 N SER 59 -16.635 27.958 60.193 1.000 27.61

ANISOU 464 N SER 59 2556 3905 4029 -108 1461 -1767

ATOM 465 CA SER 59 -17.812 27.153 60.497 1.000 28.42

ANISOU 465 CA SER 59 2675 4074 4049 -189 1294 -1325

ATOM 466 CB SER 59 -19.121 27.889 60.162 1.000 28.29

ANISOU 466 CB SER 59 2556 4574 3618 -339 1198 - 928

ATOM 467 OG SER 59 -19.229 27.978 58.739 1.000 28.66

ANISOU 467 OG SER 59 3598 3742 3547 166 1729 - 867

ATOM 468 C SER 59 -17.795 25.843 59.724 1.000 29.57

ANISOU 468 C SER 59 3467 3990 3779 -646 1463 -1206

ATOM 469 O SER 59 -16.990 25.651 58.810 1.000 22.72

ANISOU 469 O SER 59 3054 3042 2537 -144 648 - 369

ATOM 470 N GLU 60 -18.698 24.939 60.103 1.000 26.90

ANISOU 470 N GLU 60 2413 3900 3907 -69 1079 - 853

ATOM 471 CA GLU 60 -18.699 23.684 59.359 1.000 26.98

ANISOU 471 CA GLU 60 2699 3515 4037 -98 709 - 537

ATOM 472 CB GLU 60 -19.646 22.681 60.001 1.000 39.11

ANISOU 472 CB GLU 60 5393 4393 5075 -1361 908 3 64

ATOM 473 CG GLU 60 -19.011 21.665 60.917 1.000 44.63

ANISOU 473 CG GLU 60 5606 5473 5878 -977 1079 1219

ATOM 474 CD GLU 60 -17.507 21.543 60.797 1.000 48.52

ANISOU 474 CD GLU 60 5714 6217 6503 -390 1207 877

ATOM 475 OEl GLU 60 -17.030 21.223 59.684 1.000 48.11

ANISOU 475 OEl GLU 60 5349 7545 5384 709 366 1951

ATOM 476 OE2 GLU 60 -16.828 21.763 61.829 1.000 46.50

ANISOU 476 OE2 GLU 60 4926 5742 7000 1158 1550 -1504

ATOM 477 C GLU 60 -19.091 23.960 57.915 1.000 25.30

ANISOU 477 C GLU 60 2829 2728 4055 86 725 - 656

ATOM 478 O GLU 60 -18.529 23.346 57.027 1.000 24.18

ANISOU 478 O GLU 60 2119 2980 4091 -202 741 - 752

ATOM 479 N ALA 61 -20.032 24.890 57.716 1.000 25.58

ANISOU 479 N ALA 61 2083 3206 4432 -34 612 - 774

ATOM 480 CA ALA 61 -20.495 25.212 56.368 1.000 24.05

ANISOU 480 CA ALA 61 1838 2999 4301 228 720 -1055

ATOM 481 CB ALA 61 -21.670 26.176 56.459 1.000 27.53

ANISOU 481 CB ALA 61 2807 1857 5797 394 704 - 606

ATOM 482 C ALA 61 -19.385 25.790 55.500 1.000 27.31

ANISOU 482 C ALA 61 3170 2572 4633 -377 1178 - 1026

ATOM 483 O ALA 61 -19.247 25.467 54.311 1.000 22.29

ANISOU 483 O ALA 61 2363 1876 4232 42 661 - 319

ATOM 484 N GLU 62 -18.580 26.642 56.118 1.000 22.18

ANISOU 484 N GLU 62 2075 2258 4094 396 569 - 394

ATOM 485 CA GLU 62 -17.455 27.258 55.416 1.000 24.19

ANISOU 485 CA GLU 62 2401 2603 4188 150 852 - 590

ATOM 486 CB GLU . 62 -16.806 28.354 56.277 1.000 24.68

ANISOU 486 CB GLU 62 2401 2490 4485 91 1273 - 828

ATOM 487 CG GLU 62 -17.641 29.636 56.356 1.000 25.19

ANISOU 487 CG GLU 62 2542 2620 4409 353 421 - 685

ATOM 488 CD GLU 62 -17.288 30.581 57.480 1.000 29.27

ANISOU 488 CD GLU 62 3284 2991 4845 621 515 -1290 ATOM 489 OEl GLU 62 -16.527 30.241 58.410 1.000 30.11

ANISOU 489 OEl GLU 62 3231 3067 5143 318 56 - 1639

ATOM 490 OE2 GLU 62 -17.796 31.739 57.436 1.000 35.30

ANISOU 490 OE2 GLU 62 4832 2994 5584 863 109 - 1327

ATOM 491 C GLU 62 -16.409 26.226 55.025 1.000 21.70

ANISOU 491 C GLU 62 2394 2421 3430 30 784 - 579

ATOM 492 O GLU 62 -15.818 26.218 53.940 1.000 19.44

ANISOU 492 O GLU 62 2095 2140 3153 -301 467 - 604

ATOM 493 N LYS 63 -16.184 25.308 55.972 1.000 20.08

ANISOU 493 N LYS 63 2472 2266 2893 -74 761 - 902

ATOM 494 CA LYS 63 -15.246 24.227 55.678 1.000 19.73

ANISOU 494 C LYS 63 2322 2559 2614 133 429 - 903

ATOM 495 CB LYS 63 -14.93423.497 56.988 1.000 18.48

ANISOU 495 CB LYS 63 1803 2743 2476 -218 587 - 836

ATOM 496 CG LYS 63 -13.94624.240 57.881 1.000 19.17

ANISOU 496 CG LYS 63 2115 2332 2836 -296 325 - 674

ATOM 497 CD LYS 63 -13.83923.651 59.290 1.000 26.23

ANISOU 497 CD LYS 63 2978 4084 2902 -888 -177 - 287

ATOM 498 CE LYS 63 -12.753 24.383 60.068 1.000 27.75

ANISOU 498 CE LYS 63 3074 5008 2461 -1239 500 - 1082

ATOM 499 NZ LYS 63 -12.929 24.378 61.530 1.000 34.95

ANISOU 499 NZ LYS 63 3177 7579 2524 -2594 840 - 894

ATOM 500 C LYS 63 -15.78923.304 54.586 1.000 17.52

ANISOU 500 C LYS 63 2014 2191 2453 51 529 - 691

ATOM 501 O LYS 63 -15.025 22.953 53.654 1.000 17.58

ANISOU 501 O LYS 63 2266 1709 2704 158 707 - 653

ATOM 502 N ARG 64 -17.069 22.912 54.641 1.000 19.63

ANISOU 502 N ARG 64 2081 2452 2926 -14 614 - 592

ATOM 503 CA ARG 64 -17.61822.041 53.595 1.000 19.00

ANISOU 503 CA ARG 64 1509 2526 3185 -3 620 - 652

ATOM 504 C ARG 64 -17.47122.634 52.194 1.000 20.42

ANISOU 504 C ARG 64 2165 2436 3157 -390 -22 - 536

ATOM 505 O ARG 64 -17.20421.934 51.195 1.000 18.83

ANISOU 505 O ARG 64 1854 2184 3115 -434 575 - 201

ATOM 506 CB ARG 64 -19.08021.670 53.871 1.000 24.70

ANISOU 506 CB ARG 64 1470 3652 4263 -51 841 - 909

ATOM 507 CG ARG 64 -19.838 20.933 52.795 1.000 36.49

ANISOU 507 CG ARG 64 2961 5284 5621 -2020 138 - 882

ATOM 508 CD ARG 64 -21.31520.645 53.095 1.000 46.32

ANISOU 508 CD ARG 64 3034 6962 7603 -2438 327 - 1187

ATOM 509 NE ARG 64 -21.77621.216 54.331 1.000 55.81

ANISOU 509 NE ARG 64 3917 8636 8652 -3960 2222 -1870

ATOM 510 CZ ARG 64 -22.81421.840 54.811 1.000 58.82

ANISOU 510 CZ ARG 64 4438 8939 8972 -3479 1988 -2480

ATOM 511 NHl ARG 64 -23.88422.106 54.071 1.000 76.83

ANISOU 511 NHl ARG 64 6024 9527 13641 -1787 -165 -1872

ATOM 512 NH2 ARG 64 -22.79722.213 56.093 1.000 69.53

ANISOU 512 NH2 ARG 64 7792 9201 9424 -5884 3891 -3304

ATOM 513 N ALA 65 -17.62123.947 52.066 1.000 20.43

ANISOU 513 N ALA 65 1689 2554 3519 24 612 - 525

ATOM 514 CA ALA 65 -17.50524.656 50.782 1.000 19.45

ANISOU 514 CA ALA 65 1649 2216 3523 409 184 - 553

ATOM 515 CB ALA 65 -17.912 26.108 50.984 1.000 23.73

ANISOU 515 CB ALA 65 1420 2019 5579 126 -373 - 742

ATOM 516 C ALA 65 -16.118 24.549 50.168 1.000 17.89

ANISOU 516 C ALA 65 1524 2099 3173 -47 108 - 101

ATOM 517 O ALA 65 -15.983 24.732 48.954 1.000 18.77

ANISOU 517 O ALA 65 1830 2178 3123 122 -8 - 229

ATOM 518 N VAL 66 -15.10024.248 50.973 1.000 17.99

ANISOU 518 N VAL 66 1547 2151 3137 -86 36 - 196

ATOM 519 CA VAL 66 -13.74624.066 50.430 1.000 16.74 ANISOU 519 C VAL 66 1553 1859 2948 -62 -56 - 254

ATOM 520 CB VAL 66 -12.775 25.151 50.951 1.000 17.29

ANISOU 520 CB VAL 66 1805 1804 2963 -330 338 - 185

ATOM 521 CGI VAL 66 -13.238 26.532 50.455 1.000 16.70

ANISOU 521 CGI VAL 66 1547 1800 2997 111 545 - 553

ATOM 522 CG2 VAL 66 -12.652 25.180 52.462 1.000 18.65

ANISOU 522 CG2 VAL 66 2053 1996 3036 -193 17 - 538

ATOM 523 C VAL 66 -13.201 22.680 50.724 1.000 15.66

ANISOU 523 C VAL 66 1775 1813 2362 -70 -250 - 457

ATOM 524 O VAL 66 -11.972 22.493 50.808 1.000 14.19

ANISOU 524 O VAL 66 1747 1576 2069 -122 -56 - 347

ATOM 525 N THR 67 -14.071 21.695 50.873 1.000 14.46

ANISOU 525 N THR 67 1550 1602 2343 126 -48 - 722

ATOM 526 CA THR 67 -13.723 20.279 51.000 1.000 14.06

ANISOU 526 CA THR 67 1461 1698 2185 234 5 - 740

ATOM 527 CB THR 67 -14.419 19.647 52.225 1.000 15.08

ANISOU 527 CB THR 67 1721 1955 2053 -51 -426 - 444

ATOM 528 OGl THR 67 -14.089 20.337 53.453 1.000 17. 1

ANISOU 528 OGl THR 67 2538 1949 2128 -39 70 - 716

ATOM 529 CG2 THR 67 -13.915 18.215 52.420 1.000 16.63

ANISOU 529 CG2 THR 67 2182 1888 2248 148 293 - 658

ATOM 530 C THR 67 -14.067 19.518 49.728 1.000 12.37

ANISOU 530 C THR 67 1144 1422 2132 209 -95 - 517

ATOM 531 O THR 67 -15.208 19.567 49.229 1.000 14.82

ANISOU 531 O THR 67 1197 2086 2350 208 -168 - 362

ATOM 532 N SER 68 -13.092 18.790 49.180 1.000 11.61

ANISOU 532 N SER 68 1109 1421 1881 37 -58 - 534

ATOM 533 CA SER 68 -13.306 17.955 48.003 1.000 11.45

ANISOU 533 CA SER 68 1274 1444 1631 -49 -30 - 374

ATOM 534 CB SER 68 -12.027 17.317 47.480 1.000 11.88

ANISOU 534 CB SER 68 1446 1523 1544 79 252 - 157

ATOM 535 OG SER 68 -11.026 18.292 47.239 1.000 16.95

ANISOU 535 OG SER 68 1557 2314 2569 -336 389 - 218

ATOM 536 C SER 68 -14.269 16.815 48.319 1.000 11.56

ANISOU 536 c SER 68 1287 1375 1732 -61 53 - 406

ATOM 537 0 SER 68 -14.308 16.384 49.476 1.000 14.62

ANISOU 537 0 SER 68 1998 1860 1697 -538 153 - 430

ATOM 538 N PRO 69 -15.026 16.324 47.344 1.000 12.78

ANISOU 538 N PRO 69 1476 1473 1905 -243 -88 - 194

ATOM 539 CD PRO 69 -15.130 16.801 45.953 1.000 12.47

ANISOU 539 CD PRO 69 1022 1808 1909 -199 -203 - 144

ATOM 540 CA PRO 69 -15.941 15.214 47.639 1.000 12.21

ANISOU 540 CA PRO 69 1358 1369 1913 -178 148 - 437

ATOM 541 CB PRO 69 -16.825 15.193 46.355 1.000 13 .94

ANISOU 541 CB PRO 69 1362 1591 2343 -251 -178 - 14

ATOM 542 CG PRO 69 -15.924 15.715 45.290 1.000 14.38

ANISOU 542 CG PRO 69 1396 1947 2122 -554 -511 17 8

ATOM 543 C PRO 69 -15.270 13.882 47.912 1.000 13.25

ANISOU 543 C PRO 69 1206 1526 2303 -217 -115 - 100

ATOM 544 O PRO 69 -15.932 12.985 48.481 1.000 14.01

ANISOU 544 O PRO 69 1753 1450 2122 -373 99 - 301

ATOM 545 N VAL 70 -14.015 13.692 47.554 1.000 13.46

ANISOU 545 N VAL 70 1288 1479 2348 -174 -108 - 265

ATOM 546 CA VAL 70 -13.184 12.548 47.898 1.000 13.49

ANISOU 546 CA VAL 70 1404 1692 2030 37 138 - 195

ATOM 547 CB VAL 70 -12.587 11.720 46.737 1.000 16.39

ANISOU 547 CB VAL 70 2142 1648 2439 -225 614 - 452

ATOM 548 CGI . VAL 70 -13.615ι 10.756 46.208 1.000 33 .50

ANISOU 548 CG . VAL 70 6470 2984 3274 -2702 41 - 867

ATOM 549 CG: ^> VAL 70 -11.995ι 12.613 45.640 1.000 16.46

ANISOU ^■ 549 CG: - VAL 70 1749 2234 2273 269 444 2 3 ATOM 550 C VAL 70 -12.042 13.057 48.782 1.000 13 .59

ANISOU 550 C VAL 70 1618 1382 2163 -38 -114 127

ATOM 551 0 VAL 70 -11.426 14.105 48.493 1.000 14.20

ANISOU 551 0 VAL 70 1748 1685 1964 -265 26 1 8 2

ATOM 552 N PRO 71 -11.786 12.365 49.898 1.000 14.21

ANISOU 552 N PRO 71 1607 1507 2285 -115 -62 3 1 0

ATOM 553 CD PRO 71 -12.432 11.125 50.378 1.000 14.70

ANISOU 553 CD PRO 71 1920 1590 2076 -201 646 4

ATOM 554 CA PRO 71 -10.830 12.919 50.878 1.000 17.41

ANISOU 554 CA PRO 71 2429 2008 2178 -522 -342 4 18

ATOM 555 CB PRO 71 -11.338 12.304 52.193 1.000 20.87

ANISOU 555 CB PRO 71 3768 2082 2081 -743 190 1 4

ATOM 556 CG PRO 71 -11.908 10.989 51.775 1.000 18.28

ANISOU 556 CG PRO 71 3534 1665 1746 -338 781 - 5 4

ATOM 557 C PRO 71 -9.384 12.543 50.619 1.000 17.14

ANISOU 557 C PRO 71 2183 2304 2026 -684 -815 4 4

ATOM 558 O PRO 71 -8.730 11.796 51.330 1.000 20.54

ANISOU 558 O PRO 71 2745 2610 2448 -87 -404 4 14

ATOM 559 N THR 72 -8.834 13.111 49.556 1.000 16.59

ANISOU 559 N THR 72 2156 2046 2103 -235 -508 - 17

ATOM 560 CA THR 72 -7.496 12.818 49.090 1.000 17.43

ANISOU 560 CA THR 72 2113 1884 2626 -254 -510 - 288

ATOM 561 CB THR 72 -7.477 12.829 47.545 1.000 15.98

ANISOU 561 CB THR 72 1700 1761 2611 211 -458 - 421

ATOM 562 OGl THR 72 -8.027 14.094 47.128 1.000 17.28

ANISOU 562 OGl THR 72 2146 1553 2868 27 -355 - 271

ATOM 563 CG2 THR 72 -8.348 11.764 46.929 1.000 12.63

ANISOU 563 CG2 THR 72 1296 1581 1923 -46 328 - 127

ATOM 564 C THR 72 -6.418 13.805 49.549 1.000 17.83

ANISOU 564 C THR 72 2153 1773 2847 -155 -1228 2 3 2

ATOM 565 O THR 72 -5.216 13.536 49.329 1.000 20.17

ANISOU 565 O THR 72 2142 2265 3257 -225 -1049 48 0

ATOM 566 N MET 73 -6.785 14.920 50.169 1.000 19.43

ANISOU 566 N MET 73 2876 2052 2455 -782 -451 - 144

ATOM 567 CA MET 73 -5.799 15.944 50.521 1.000 18.75

ANISOU 567 CA MET 73 2117 2326 2682 -538 -466 - 280

ATOM 568 CB MET 73 -4.758 15.338 51.480 1.000 22.03

ANISOU 568 CB MET 73 1826 2825 3718 -377 -306 5 9 5

ATOM 569 CG MET 73 -5.374 15.059 52.843 1.000 27.01

ANISOU 569 CG MET 73 3545 2853 3864 -84 -87 1526

ATOM 570 SD MET 73 -4.107 14.850 54.107 1.000 32.23

ANISOU 570 SD MET 73 4364 4245 3637 469 -400 583

ATOM 571 CE MET 73 -3.179 13.492 53.374 1.000 26.74

ANISOU 571 CE MET 73 2885 4895 2381 326 425 1348

ATOM 572 C MET 73 -5.066 16.582 49.355 1.000 17.20

ANISOU 572 C MET 73 1338 2129 3067 -20 -269 - 175

ATOM 573 O MET 73 -3.945 17.110 49.498 1.000 21.20

ANISOU 573 O MET 73 1713 2512 3832 -541 51 - 1024

ATOM 574 N ARG 74 -5.630 16.600 48.175 1.000 18.64

ANISOU 574 N ARG 74 1881 2051 3150 84 -461 54 3

ATOM 575 CA ARG 74 -5.091 17.180 46.967 1.000 15.73

ANISOU 575 CA ARG 74 9371986 3053 169 27 - 174

ATOM 576 CB ARG 74 -5.655 16.537 45.704 1.000 16.53

ANISOU 576 CB ARG 74 1711 1434 3137 -263 142 - 160

ATOM 577 CG ARG 74 -4.911 16.934 44.440 1.000 15.01

ANISOU 577 CG ARG 74 1270 1288 3144 -156 279 - 554

ATOM 578 CD ARG 74 -5.683 16.543 43.185 1.000 16.10

ANISOU 578 CD ARG 74 1967 1031 3120 268 -92 - 407

ATOM 579 NE ARG 74 -4.902 16.816 41.966 1.000 18.81

ANISOU 579 NE ARG 74 2259 1813 3075 -432 -252 - 296

ATOM 580 CZ ARG 74 -5.033 17.824 41.130 1.000 16.64 ANISOU 580 CZ ARG 74 1968 1646 2709 -141 -190 - 59 f

ATOM 581 NHl ARG 74 -5.951 18.775 41.293 1.000 20.09

ANISOU 581 NHl ARG 74 1899 2075 3660 54 -35 3 - 788

ATOM 582 NH2 ARG 74 -4.220 17.896 40.068 1.000 20.12

ANISOU 582 NH2 ARG 74 2366 2844 2437 153 -196 - 40 ⁽

ATOM 583 C ARG 74 -5.373 18.681 46.966 1.000 12 .70

ANISOU 583 C ARG 74 1187 1880 1758 6 -22 - 136

ATOM 584 O ARG 74 -4.501 19.465 46.582 1.000 14.07

ANISOU 584 O ARG 74 1049 2048 2247 -221 -170 - 481

ATOM 585 N ARG 75 -6.567 19.099 47.387 1.000 12 .72

ANISOU 585 N ARG 75 1402 1702 1728 95 182 - 103

ATOM 586 CA ARG 75 -7.006 20.471 47.308 1.000 13.40

ANISOU 586 CA ARG 75 1924 1618 1548 87 275 - 193

ATOM 587 CB ARG 75 -7.737 20.784 45.995 1.000 13.45

ANISOU 587 CB ARG 75 1972 1387 1751 -179 51 - 9

ATOM 588 CG ARG 75 -6.908 20.637 44.721 1.000 13 .38

ANISOU 588 CG ARG 75 1638 1851 1594 78 -217 10 1

ATOM 589 CD ARG 75 -5.849 21.708 44.582 1.000 12.85

ANISOU 589 CD ARG 75 1537 1602 1741 237 62 - 15

ATOM 590 NE ARG 75 -5.087 21.685 43.347 1.000 13.71

ANISOU 590 NE ARG 75 1708 1797 1705 188 90 - 9 1

ATOM 591 CZ ARG 75 -3.984 21.036 43.013 1.000 12.46

ANISOU 591 CZ ARG 75 1348 1656 1731 -89 86 117

ATOM 592 NHl ARG 75 -3.418 20.241 43.894 1.000 14.64

ANISOU 592 NHl ARG 75 1933 1794 1834 186 -91 6 5

ATOM 593 NH2 ARG 75 -3.444 21.167 41.794 1.000 13.72

ANISOU 593 NH2 ARG 75 1510 2037 1667 -136 84 - 8 3

ATOM 594 C ARG 75 -7.948 20.787 48.475 1.000 12.74

ANISOU 594 C ARG 75 1400 1656 1784 -209 214 - 46

ATOM 595 O ARG 75 -8.780 19.944 48.818 1.000 14.60

ANISOU 595 O ARG 75 1348 1926 2273 -427 156 - 48

ATOM 596 N GLY 76 -7.830 21.955 49.078 1.000 11.92

ANISOU 596 N GLY 76 1268 1537 1724 -22 34 - 389

ATOM 597 CA GLY 76 -8.801 22.395 50.070 1.000 12.44

ANISOU 597 CA GLY 76 1439 1493 1796^' -315 263 - 41

ATOM 598 C GLY 76 -8.536 21.857 51.469 1.000 12.50

ANISOU 598 C GLY 76 1324 1527 1900 5 326 - 273

ATOM 599 O GLY 76 -7.388 21.517 51.769 1.000 14.25

ANISOU 599 O GLY 76 1100 2099 2218 -277 239 - 22

ATOM 600 N PHE 77 -9.574 21.840 52.287 1.000 12.65

ANISOU 600 N PHE 77 1191 1806 1809 -162 231 - 35

ATOM 601 CA PHE 77 -9.526 21.474 53.694 1.000 14.00

ANISOU 601 CA PHE 77 1295 2110 1914 -260 276 - 13

ATOM 602 CB PHE 77 -10.644 : 22.226 54.451 1.000 14.73

ANISOU 602 CB PHE 77 1554 2169 1874 -402 485 - 31

ATOM 603 CG PHE 77 -10.773 21.824 55.912 1.000 17.13

ANISOU 603 CG PHE 77 1927 2730 1849 -374 378 - 24

ATOM 604 CDI PHE 77 -9.949 22.369 56.886 1.000 19.49

ANISOU 604 CDI PHE 77 2744 2700 1962 -119 219 - 78

ATOM 605 CD2 PHE 77 -11.73C ) 20.902 56.309 1.000 19.13

ANISOU 605 CD2 PHE 77 2348 3068 1852 -501 864 - 16

ATOM 606 CEl PHE 77 -10.06 1 21.973 58.217 1.000 19.75

ANISOU 606 CEl PHE 77 2956 2381 2168 -174 -313 - 30

ATOM 607 CE2 PHE 77 -11.82S . 20.479 57.627 1.000 18.73

ANISOU 607 CE2 PHE 77 2565 2711 1841 -382 310 - 7 ^'

ATOM 608 CZ PHE 77 -10.986 21.013 58.584 1.000 19.22

ANISOU 608 CZ PHE 77 2378 2542 2382 98 13 - 364

ATOM 609 C PHE 77 -9.668 19.976 53.924 1.000 13.73

ANISOU 609 C PHE 77 1306 2096 1813 -368 21 - 204

ATOM 610 O PHE 77 -10.520 19.313 53.291 1.000 ι 16.02

ANISOU 610 O PHE 77 1386 2508 2194 -470 -128 - 42 ATOM 611 N THR 78 -8.869 19.439 54.852 1.000 14.33

ANISOU 611 N THR 78 1543 2270 1629 -472 35 - 4 9

ATOM 612 CA THR 78 -9.034 18.053 55.276 1.000 15.80

ANISOU 612 CA THR 78 1813 2310 1880 -508 -23 8 2

ATOM 613 CB THR 78 -8.001 17.081 54.666 1.000 18.26

ANISOU 613 C3 THR 78 1583 2199 3158 -599 334 1 3 1

ATOM 614 OGl THR 78 -7.924 17.323 53.266 1.000 21.81

ANISOU 614 OGl THR 78 3351 1877 3057 -88 943 - 370

ATOM 615 CG2 THR 78 -8.419 15.634 54.888 1.000 20.35

ANISOU 615 CG2 THR 78 2855 2254 2622 -1119 1108 - 707

ATOM 616 C THR 78 -8.832 17.881 56.777 1.000 19.14

ANISOU 616 C THR 78 2845 2479 1948 -1747 -471 1 6 9

ATOM 617 O THR 78 -7.801 18.311 57.290 1.000 22.04

ANISOU 617 O THR 78 2781 2889 2704 -1718 -985 7 63

ATOM 618 N GLY 79 -9.730 17.203 57.484 1.000 19.20

ANISOU 618 N GLY 79 2629 2823 1844 -1352 19 4 5

ATOM 619 CA GLY 79 -9.429 16.695 58.819 1.000 16.69

ANISOU 619 CA GLY 79 1800 2770 1771 -518 196 - 9 5

ATOM 620 C GLY 79 -8.672 15.376 58.720 1.000 22.98

ANISOU 620 C GLY 79 2381 2874 3477 -272 -289 - 545

ATOM 621 O GLY 79 -9.227 14.504 58.044 1.000 25.57

ANISOU 621 O GLY 79 3683 2520 3514 -456 -974 - 141

ATOM 622 N LEU 80 -7.494 15.236 59.319 1.000 22.91

ANISOU 622 N LEU 80 2412 2900 3392 30 -206 - 606

ATOM 623 CA LEU 80 -6.644 14.081 59.072 1.000 25.08

ANISOU 623 CA LEU 80 2848 2777 3904 206 621 3 6 1

ATOM 624 C LEU 80 -6.372 13.294 60.370 1.000 24.30

ANISOU 624 C LEU 80 2834 2762 3637 -300 480 2 00

ATOM 625 0 LEU 80 -5.729 13.812 61.291 1.000 25.14

ANISOU 625 0 LEU 80 2253 3017 4283 27 145 - 5

ATOM 626 CB LEU 80 -5.318 14.480 58.415 1.000 27.16

ANISOU 626 CB LEU 80 3057 3326 3937 379 918 641

ATOM 627 CG LEU 80 -4.411 13.338 57.933 1.000 29.43

ANISOU 627 CG LEU 80 3474 3505 4204 287 1260 173

ATOM 628 CDI LEU 80 -5.145 12.438 56.956 1.000 38.31

ANISOU 628 CDI LEU 80 5673 3891 4993 -1554 1987 - 287

ATOM 629 CD2 LEU 80 -3.137 13.884 57.306 1.000 29.85

ANISOU 629 CD2 LEU 80 3502 3919 3920 125 1307 - 264

ATOM 630 N GLU 81 -6.853 12.055 60.396 1.000 25.58

ANISOU 630 N GLU 81 2469 2759 4490 -196 -82 5 1 0

ATOM 631 CA GLU 81 -6.739 11.038 61.415 1.000 25.98

ANISOU 631 CA GLU 81 2739 2692 4441 -258 -55 424

ATOM 632 C GLU 81 -5.299 10.536 61.562 1.000 26.28

ANISOU 632 C GLU 81 2870 3268 3848 187 407 8 41

ATOM 633 O GLU 81 -4.489 10.655 60.655 1.000 28.19

ANISOU 633 O GLU 81 3709 3520 3483 253 799 - 544

ATOM 634 CB GLU 81 -7.685 9.861 61.123 1.000 29.83

ANISOU 634 CB GLU 81 3533 2894 4906 -770 270 1 8 1

ATOM 635 CG GLU 81 -7.241 8.832 60.098 1.000 25.34

ANISOU 635 CG GLU 81 1737 2915 4976 284 -1220 158

ATOM 636 CD GLU 81 -7.568 9.156 58.649 1.000 27.00

ANISOU 636 CD GLU 81 1841 3405 5012 475 -1887 - 456

ATOM 637 OEl GLU 81 -8.120 10.240 58.324 1.000 28.81

ANISOU 637 OEl GLU 81 3444 3091 4413 322 -155 7 9 1

ATOM 638 OE2 GLU 81 -7.240 8.273 57.814 1.000 31.31

ANISOU 638 OE2 GLU 81 3514 3384 4999 162 352 1 0 0

ATOM 639 N SER 82 -4.988 9.974 62.720 1.000 31.00

ANISOU 639 N SER 82 3568 3780 4430 -65 -30 1484

ATOM 640 CA SER 82 -3.653 9.422 62.959 1.000 30.2

ANISOU 640 CA SER 82 3692 3278 4540 -157 -515 1011

ATOM 641 C SER 82 -3.421 8.150 62.150 1.000 31.76 ANISOU 641 C SER 82 3995 3241 4831 -102 -1104 8 4 7

ATOM 642 O SER 82 -4.313 7.728 61.397 1.000 34.01

ANISOU 642 0 SER 82 3193 3794 5935 458 -1188 1 3 4

ATOM 643 CB SER 82 -3.463 9.167 64.452 1.000 34.74

ANISOU 643 CB SER 82 4687 3907 4606 -232 -979 9 7 1

ATOM 644 OG SER 82 -2.360 8.305 64.681 1.000 41.53

ANISOU 644 OG SER 82 4922 5366 5490 236 -1958 9 7 0

ATOM 645 N GLY 91 -17.230 9.498 70.136 1.000 42 .64

ANISOU 645 N GLY 91 4516 7599 4086 -2166 2340 - 427

ATOM 646 CA GLY 91 -17.485 10.892 69.789 1.000 44.91

ANISOU 646 CA GLY 91 6666 7702 2697 -4311 -1561 5 65

ATOM 647 C GLY 91 -16.227 11.662 69.452 1.000 38.67

ANISOU 647 C GLY 91 5455 7587 1652 -2821 -274 - 159

ATOM 648 O GLY 91 -15.164 11.480 70.040 1.000 32.45

ANISOU 648 O GLY 91 4241 4474 3616 -183 1152 - 439

ATOM 649 N GLY 92 -16.332 12.558 68.474 1.000 31.97

ANISOU 649 N GLY 92 3881 5904 2363 -1382 735 - 571

ATOM 650 CA GLY 92 -15.232 13.412 68.075 1.000 33 .02

ANISOU 650 CA GLY 92 4121 6150 2274 -1716 851 - 956

ATOM 651 C GLY 92 -15.223 13.696 66.572 1.000 26.22

ANISOU 651 C GLY 92 2603 5046 2314 -885 741 - 947

ATOM 652 O GLY 92 -16.289 13.666 65.939 1.000 23 .91

ANISOU 652 O GLY 92 2490 3396 3198 -680 548 - 567

ATOM 653 N SER 93 -14.010 13.956 66.088 1.000 23 .77

ANISOU 653 N SER 93 2405 3917 2708 -372 736 - 560

ATOM 654 CA SER 93 -13.801 14.287 64.690 1.000 23.41

ANISOU 654 CA SER 93 2700 3292 2901 -386 970 - 399

ATOM 655 C SER 93 -12.410 13.852 64.240 1.000 24.26

ANISOU 655 C SER 93 2547 3908 2763 -286 833 -224

ATOM 656 O SER 93 -11.497 13.831 65.089 1.000 27.06

ANISOU 656 O SER 93 3401 3536 3346 630 92 - 386

ATOM 657 CB SER 93 -13.966 15.795 64.467 1.000 25.71

ANISOU 657 CB SER 93 2811 3225 3735 -576 271 - 506

ATOM 658 OG SER 93 -13.558 16.158 63.150 1.000 28.14

ANISOU 658 OG SER 93 2694 3713 4284 -373 290 5 17

ATOM 659 N TYR 94 -12.254 13.533 62.949 1.000 24.24

ANISOU 659 N TYR 94 2786 3320 3104 -204 791 - 817

ATOM 660 CA TYR 94 -10.878 13.262 62.498 1.000 23.94

ANISOU 660 CA TYR 94 3089 2502 3505 95 1112 - 683

ATOM 661 C TYR 94 -10.017 14.531 62.584 1.000 25.19

ANISOU 661 C TYR 94 2601 2657 4312 147 737 - 625

ATOM 662 O TYR 94 -8.786 14.421 62.694 1.000 30.11

ANISOU 662 O TYR 94 2617 3095 5726 307 760 3 6

ATOM 663 CB TYR 94 -10.800 12.659 61.098 1.000 25.64

ANISOU 663 CB TYR 94 3566 2910 3267 -293 1331 - 525

ATOM 664 CG TYR 94 -11.600 11.410 60.876 1.000 23.22

ANISOU 664 CG TYR 94 3359 2768 2697 -69 784 - 274

ATOM 665 CDI TYR 94 -12.451 11.455 59.777 1.000 26.01

ANISOU 665 CDI TYR 94 4410 2730 2741 499 353 - 543

ATOM 666 CD2 TYR 94 -11.564 10.252 61.635 1.000 24.42

ANISOU 666 CD2 TYR 94 3117 2866 3297 73 458 - 14

ATOM 667 CEl TYR 94 -13.243 10.407 59.443 1.000 28.75

ANISOU 667 CEl TYR 94 4559 3328 3037 434 140 - 1370

ATOM 668 CE2 TYR 94 -12.375 9.159 61.305 1.000 26.47

ANISOU 668 CE2 TYR 94 4707 2585 2764 -220 1227 - 718

ATOM 669 CZ TYR 94 -13.209 9.247 60.212 1.000 29.70

ANISOU 669 CZ TYR 94 5641 3518 2125 -1172 1103 - 1447

ATOM 670 OH TYR 94 -14.05Sι 8.281 59.730 1.000 34.02

ANISOU 670 OH TYR 94 3079 3962 5886 -423 1593 -2638

ATOM 671 N SER 95 -10.628 ! 15.714 62.561 1.000 22.61

ANISOU 671 N SER 95 2460 2497 3632 -54 59 - 338 ATOM 672 C SER 95 -9.924 16.975 62.750 1.000 22 .54

ANISOU 672 C SER 95 2257 2603 3706 -120 -301 4 6

ATOM 673 C SER 95 -9.370 17.106 64.163 1.000 23.58

ANISOU 673 C SER 95 1811 3478 3671 -521 -88 - 8 5

ATOM 674 O SER 95 -8.623 18.034 64.481 1.000 26.53

ANISOU 674 0 SER 95 2592 3242 4247 -469 -167 - 64

ATOM 675 C3 SER 95 -10.838 18.177 62.478 1.000 27.58

ANISOU 675 CB SER 95 3657 2556 4264 365 -379 2 8

ATOM 676 OG SER 95 -11.506 18.093 61.242 1.000 39.40

ANISOU 676 OG SER 95 6336 4214 4421 900 -1445 14 442

ATOM 677 N ASP 96 -9.712 16.194 65.060 1.000 25.04

ANISOU 677 N ASP 96 2579 3688 3248 -399 277 - 23

ATOM 678 CA ASP 96 -9.228 16.317 66.422 1.000 24.42

ANISOU 678 CA ASP 96 2603 3347 3330 -470 257 - 52

ATOM 679 C ASP 96 -7.735 16.050 66.501 1.000 24.45

ANISOU 679 C ASP 96 2597 3228 3466 -471 162 - 38

ATOM 680 O ASP 96 -7.073 16.589 67.404 1.000 26.51

ANISOU 680 O ASP 96 2656 4047 3370 -170 160 - 79

ATOM 681 CB ASP 96 -9.952 15.334 67.334 1.000 24.97

ANISOU 681 CB ASP 96 2310 3806 3371 -423 -228 7 7

ATOM 682 CG ASP 96 -11.411 15.605 67.606 1.000 26.77

ANISOU 682 CG ASP 96 2272 4334 3566 -362 -240 716

ATOM 683 ODl ASP 96 -11.935 16.723 67.388 1.000 33.94

ANISOU 683 ODl ASP 96 3267 4894 4733 647 204 5 6 9

ATOM 684 OD2 ASP 96 -12.058 14.646 68.083 1.000 32.65

ANISOU 684 OD2 ASP 96 3624 4709 4072 -1032 1446 - 20

ATOM 685 N TYR 97 -7.254 15.226 65.581 1.000 22.21

ANISOU 685 N TYR 97 2292 3389 2760 -376 -77 - 10

ATOM 686 CA TYR 97 -5.835 14.852 65.583 1.000 23 .71

ANISOU 686 CA TYR 97 2480 3542 2987 -27 106 644

ATOM 687 C TYR 97 -5.026 15.828 64.743 1.000 23.06

ANISOU 687 C TYR 97 2363 3754 2647 -410 -78 3 5 C

ATOM 688 O TYR 97 -3.992 16.327 65.230 1.000 24.29

ANISOU 688 O TYR 97 2205 3845 3178 -133 -230 7 4

ATOM 689 CB TYR 97 -5.585 13.451 65.035 1.000 28.38

ANISOU 689 CB TYR 97 3230 3324 4229 540 -450 8 3.

ATOM 690 CG TYR 97 -4.132 13.025 65.082 1.000 30.37

ANISOU 690 CG TYR 97 3278 4101 4161 766 -191 67 ]

ATOM 691 CDI TYR 97 -3.511 12.691 66.285 1.000 30.19

ANISOU 691 CDI TYR 97 2878 4475 4119 1106 151 9 5 .

ATOM 692 CD2 TYR 97 -3.370 12.945 63.922 1.000 29.79

ANISOU 692 CD2 TYR 97 3317 4005 3997 53 -253 544

ATOM 693 CEl TYR 97 -2.178 12.294 66.324 1.000 32.77

ANISOU 693 CEl TYR 97 2554 4771 5126 574 -68 76 !

ATOM 694 CE2 TYR 97 -2.043 12.553 63.955 1.000 32.68

ANISOU 694 CE2 TYR 97 3536 3793 5087 403 353 32 :

ATOM 695 CZ TYR 97 -1.445 12.228 65.157 1.000 33 .00

ANISOU 695 CZ TYR 97 2633 4284 5622 1066 264 4 5 I

ATOM 696 OH TYR 97 -0.121 11.845 65.156 1.000 42.66

ANISOU 696 OH TYR 97 2572 5373 8264 1161 764 127

ATOM 697 CB SER 98 -3.465 16.575 62.134 1.000 23 .20

ANISOU 697 CB SER 98 2461 2766 3587 105 2 - 544

ATOM 698 OG SER 98 -3.632 15.649 61.078 1.000 26.49

ANISOU 698 OG SER 98 3824 3059 3180 -154 238 - 4 - 57

ATOM 699 C SER 98 -5.694 17.744 61.701 1.000 18.66

ANISOU 699 c SER 98 2301 2150 2637 -295 66 1 3

ATOM 700 0 SER 98 -6.768 17.212 61.413 1.000 > 20.88

ANISOU 700 0 SER 98 3042 2245 2646 -945 -249 1 8

ATOM 701 N SER 98 -5.457 16.110 63.511 1.00C 1 23 .62

ANISOU 701 N SER 98 2816 3227 2931 -441 -395 60

ATOM 702 CA SER 98 -4.748 17.143 62.741 1.00C ) 21.31 - 113 -

ANISOU 702 CA SER 98 2430 2687 2982 133 153 2 9

ATOM 703 N MET 99 -5.307 18.891 61.148 1.000 18.68

ANISOU 703 N MET 99 2392 2722 1984 -978 -366 1 0

ATOM 704 CA MET 99 -6.047 19.560 60.075 1.000 17.84

ANISOU 704 CA MET 99 2431 2620 1726 -945 -212 - 1

ATOM 705 CB MET 99 -6.819 20.779 60.585 1.000 19.71

ANISOU 705 CB MET 99 2348 2968 2173 -679 25 6 4

ATOM 706 CG MET 99 -8.052 20.392 61.374 1.000 23.68

ANISOU 706 CG MET 99 2360 3055 3582 -504 393 48

ATOM 707 SD MET 99 -9.031 21.821 61.911 1.000 22.33

ANISOU 707 SD MET 99 2569 3383 2534 -522 170 - 1 - 20

ATOM 708 CE MET 99 -8.148 22.225 63.419 1.000 36.98

ANISOU 708 CE MET 99 6485 4165 3401 -225 -1904 - : 2 3

ATOM 709 C MET 99 -5.070 19.954 58.973 1.000 17.19

ANISOU 709 C MET 99 2269 2488 1776 -960 -194 - 2 C 01

ATOM 710 O MET 99 -3.964 20.341 59.324 1.000 16.93

ANISOU 710 O MET 99 1932 2583 1919 -367 -208 - 2 4. 1

ATOM 711 N CYS 100 -5.486 19.864 57.715 1.000 20.00

ANISOU 711 N CYS 100 3178 2683 1739 -1753 -358 16

ATOM 712 CA CYS 100 -4.645 20.181 56.554 1.000 16.64

ANISOU 712 CA CYS 100 2213 2294 1817 -924 -563 4 6

ATOM 713 CB CYS 100 -4.291 18.893 55.813 1.000 17.74

ANISOU 713 CB CYS 100 2161 2174 2407 560 -765 10 ! 53

ATOM 714 SG CYS 100 -3.035 18.928 54.552 1.000 33.56

ANISOU 714 SG CYS 100 5244 3511 3997 414 1509 60

ATOM 715 C CYS 100 -5.347 21.121 55.590 1.000 13.48

ANISOU 715 C CYS 100 1879 1415 1829 -68 240 - 9

ATOM 716 O CYS 100 -6.585 21.127 55.496 1.000 14.49

ANISOU 716 O CYS 100 1880 1952 1673 -497 -57 1 4

ATOM 717 N TYR 101 -4.589 21.921 54.852 1.000 13.35

ANISOU 717 N TYR 101 1721 1677 1673 -254 -78 4 9

ATOM 718 CA TYR 101 -5.016 22.753 53.755 1.000 10.27

ANISOU 718 CA TYR 101 926 1498 1477 -15 -141 -231

ATOM 719 CB TYR 101 -5.102 24.265 54.124 1.000 13.60

ANISOU 719 CB TYR 101 1626 1513 2027 -48 322 - 2 36

ATOM 720 CG TYR 101 -5.498 25.025 52.863 1.000 17.31

ANISOU 720 CG TYR 101 2373 1509 2694 -158 -103 19

ATOM 721 CDI TYR 101 -6.815 25.068 52.519 1.000 16.38

ANISOU 721 CDI TYR 101 2464 752 3006 190 -227 5 5

ATOM 722 CEl TYR 101 -7.307 25.715 51.412 1.000 17.01

ANISOU 722 CEl TYR 101 2755 714 2993 -86 -416 122

ATOM 723 CD2 TYR 101 -4.616 25.679 52.012 1.000 19.51

ANISOU 723 CD2 TYR 101 3032 1533 2847 -1143 -594 47

ATOM 724 CE2 TYR 101 -5.065 26.321 50.872 1.000 20.96

ANISOU 724 CE2 TYR 101 2802 1949 3211 238 112 7 6

ATOM 725 CZ TYR 101 -6.414 26.334 50.568 1.000 22.78

ANISOU 725 CZ TYR 101 3238 2291 3126 -1228 -919 62

ATOM 726 OH TYR 101 -6.875 26.986 49.442 1.000 23.10

ANISOU 726 OH TYR 101 3141 3112 2522 -14 -129 42

ATOM 727 C TYR 101 -4.041 22.518 52.596 1.000 11.25

ANISOU 727 C TYR 101 1223 1398 1654 -323 103 - 2 52

ATOM 728 O TYR 101 -2.823 22.677 52.787 1.000 12.23

ANISOU 728 O TYR 101 1114 1750 1784 -87 130 - 2

ATOM 729 N SER 102 -4.542 22.190 51.405 1.000 11.17

ANISOU 729 N SER 102 1355 1279 1611 -220 145 - 2 63

ATOM 730 CA SER 102 -3.752 21.802 50.235 1.000 10.46

ANISOU 730 CA SER 102 1144 1263 1568 62 -1 - 125

ATOM 731 CB SER 102 -4.027 20.343 49.908 1.00C ι 13.46

ANISOU 731 CB SER 102 1668 1212 2234 324 105 - 3 01

ATOM 732 OG SER 102 -3.723 19.487 51.025 1.00C ) 16.42

ANISOU 732 OG SER 102 2291 1313 2637 -122 -43 9 ATOM 733 C SER 102 -4.046 22.668 49.008 1.000 11.74

ANISOU 733 C SER 102 1346 1500 1614 18 -39 - 1 0

ATOM 734 O SER 102 -5.148 23.148 48.784 1.000 12 .84

ANISOU 734 O SER 102 1480 1410 1988 90 -66 2 49

ATOM 735 N MET 103 -3.004 22.871 48.187 1.000 12 .33

ANISOU 735 N MET 103 1554 1722 1409 -262 -10 - 246

ATOM 736 CA MET 103 -3.188 23.603 46.938 1.000 12.92

ANISOU 736 CA MET 103 1663 1681 1565 22 47 - 7 0

ATOM 737 CB MET 103 -3.215 25.122 47.179 1.000 17.51

ANISOU- 737 CB MET 103 2439 1634 2579 -363 812 - 44

ATOM 738 CG MET 103 -1.929 25.808 47.549 1.000 20.07

ANISOU- 738 CG MET 103 2509 1470 3646 -538 688 3 7 6

ATOM 739 SD MET 103 -2.136 27.614 47.689 1.000 18.10

ANISOU 739 SD MET 103 2235 1665 2975 -3 -334 - 352

ATOM 740 CE MET 103 -2.365 28.068 45.991 1.000 18.09

ANISOU 740 CE MET 103 2319 1457 3098 -187 -718 - 214

ATOM 741 C MET 103 -2.152 23.221 45.892 1.000 12.57

ANISOU 741 C MET 103 1420 1837 1519 119 -53 2 3 8

ATOM 742 O MET 103 -1.120 22.573 46.175 1.000 12 .57

ANISOU 742 O MET 103 1094 1891 1792 -155 -165 27 6

ATOM 743 N GLY 104 -2.418 23.650 44.655 1.000 12.83

ANISOU 743 N GLY 104 1493 1958 1422 237 -124 - 3 4

ATOM 744 CA GLY 104 -1.533 23.459 43.513 1.000 12 .65

ANISOU 744 CA GLY 104 1075 2188 1544 -93 -37 2 42

ATOM 745 C GLY 104 -1.624 24.622 42.542 1.000 14.36

ANISOU 745 c GLY 104 1909 1985 1561 -265 -294 142

ATOM 746 0 GLY 104 -2.033 25.700 42.967 1.000 15.69

ANISOU 746 0 GLY 104 1628 2273 2060 163 -197 2 13

ATOM 747 N THR 105 -1.242 24.397 41.276 1.000 14.52

ANISOU 747 N THR 105 1829 2182 1504 -59 -375 3 19

ATOM 748 CA THR 105 -1.218 25.452 40.279 1.000 15.27

ANISOU 748 CA THR 105 1977 2223 1603 -105 -363 3 65

ATOM 749 CB THR 105 -0.359 25.083 39.039 1.000 15.61

ANISOU 749 CB THR 105 1936 2122 1873 -37 -106 554

ATOM 750 OGl THR 105 -0.884 23.876 38.446 1.000 16.16

ANISOU 750 OGl THR 105 1738 2260 2140 217 -285 151

ATOM 751 CG2 THR 105 1.092 24.882 39.369 1.000 17.47

ANISOU 751 CG2 THR 105 1918 2871 1847 -293 -227 52 7

ATOM 752 C THR 105 -2.603 25.828 39.755 1.000 14.73

ANISOU 752 C THR 105 1989 1694 1913 122 -340 1 9 9

ATOM 753 O THR 105 -2.730 26.921 39.174 1.000 19.91

ANISOU 753 O THR 105 2579 2355 2632 23 -437 1004

ATOM 754 N ALA 106 -3.587 24.960 39.913 1.000 16.57

ANISOU 754 N ALA 106 1836 2413 2047 2 -260 661

ATOM 755 CA ALA 106 -4.975 25.167 39.465 1.000 14.94

ANISOU 755 CA ALA 106 1975 1904 1798 105 -456 3 65

ATOM 756 CB ALA 106 -5.054 24.945 37.965 1.000 17.75

ANISOU 756 CB ALA 106 2006 2862 1876 140 -201 - 3 2

ATOM 757 C ALA 106 -5.942 24.251 40.222 1.000 16.26

ANISOU 757 C ALA 106 1710 2174 2293 327 -127 49 1

ATOM 758 O ALA 106 -5.498 23.398 41.013 1.000 14.57

ANISOU 758 O ALA 106 1622 1971 1945 213 -21 3 3 7

ATOM 759 N ASP 107 -7.253 24.410 40.008 1.000 16.71

ANISOU 759 N ASP 107 1768 2096 2485 540 -22 3 04

ATOM 760 CA ASP 107 -8.310 23.638 40.633 1.000 16.10

ANISOU 760 CA ASP 107 1696 2175 2246 51 -485 - 14

ATOM 761 CB ASP 107 -8.231 22.171 40.211 1.000 17.09

ANISOU 761 CB ASP 107 1299 2385 2808 144 -203 - 399

ATOM 762 CG ASP 107 -8.418 21.966 38.720 1.000 21.54

ANISOU ^• 762 CG ASP 107 2385 2894 2906 84 -317 - 722

ATOM 763 ODl ASP 107 -9.452 22.445 38.189 1.000 23 .92 ANISOU 763 ODl ASP 107 3447 2970 2672 698 -753 - 772

ATOM 764 OD2 ASP 107 -7.563 21.311 38.080 1.000 24.88

ANISOU 764 OD2 ASP 107 2496 4004 2954 105 244 - 679

ATOM 765 C ASP 107 -8.285 23.785 42.160 1.000 14.16

ANISOU 765 C ASP 107 1261 1918 2201 237 -447 1 5 3

ATOM 766 O ASP 107 -8.507 22.850 42.936 1.000 16.67

ANISOU 766 O ASP 107 2017 1927 2390 -189 -193 9 7

ATOM 767 N ASN 108 -8.027 25.020 42.598 1.000 15.34

ANISOU 767 N ASN 108 2093 1866 1870 82 51 23 9

ATOM 768 C ASN 108 -7.967 25.314 44.031 1.000 13 .68

ANISOU 768 CA ASN 108 1479 1823 1898 153 107 2 5 7

ATOM 769 CB ASN 108 -6.925 26.420 44.272 1.000 15.60

ANISOU 769 CB ASN 108 1593 2026 2309 16 267 - 98

ATOM 770 CG ASN 108 -5.516 25.942 43.963 1.000 15.23

ANISOU 770 CG ASN 108 1505 2141 2142 5 -53 2

ATOM 771 ODl ASN 108 -5.086 24.932 44.505 1.000 15.40

ANISOU 771 ODl ASN 108 1412 2442 1998 -5 -239 1 8 8

ATOM 772 ND2 ASN 108 -4.823 26.678 43.094 1.000 16.96

ANISOU 772 ND2 ASN 108 1593 2198 2652 339 393 2 2 2

ATOM 773 C ASN 108 -9.310 25.708 44.642 1.000 14.55

ANISOU 773 C ASN 108 1471 1937 2120 261 191 52 6

ATOM 774 O ASN 108 -10.222 26.170 43.958 1.000 16.89

ANISOU 774 O ASN 108 1861 2336 2219 716 -109 1 4

ATOM 775 N LEU 109 -9.412 25.512 45.954 1.000 13 .42

ANISOU 775 N LEU 109 1458 1648 1994 179 130 9

ATOM 776 CA LEU 109 -10.602 25.796 46.769 1.000 13 .53

ANISOU 776 CA LEU 109 1094 2122 1923 -52 -86 - 256

ATOM 777 CB LEU 109 -11.187 24.499 47.331 1.000 14.50

ANISOU 777 CB LEU 109 1382 1959 2169 119 455 - 468

ATOM 778 CG LEU 109 -11.580 23.383 46.370 1.000 15.21

ANISOU 778 CG LEU 109 1593 1785 2403 235 63 - 342

ATOM 779 CDI LEU 109 -11.931 22.083 47.089 1.000 18.26

ANISOU 779 CDI LEU 109 2460 1674 2806 382 -414 - 94

ATOM 780 CD2 LEU 109 -12.780 23.783 45.529 1.000 22.36

ANISOU 780 CD2 LEU 109 3055 2391 3052 44 -1155 2 8 8

ATOM 781 C LEU 109 -10.203 26.794 47.840 1.000 13.54

ANISOU 781 C LEU 109 1179 1989 1979 76 -116 - 259

ATOM 782 O LEU 109 -9.416 26.428 48.717 1.000 16.15

ANISOU 782 O LEU 109 2196 2210 1730 -52 -366 3 2

ATOM 783 N PHE 110 -10.706 28.025 47.786 1.000 16.11

ANISOU 783 N PHE 110 1369 2042 2709 105 -118 - 288

ATOM 784 CA PHE 110 -10.298 29.079 48.732 1.000 17.05

ANISOU 784 CA PHE 110 1626 1801 3050 -116 259 - 362

ATOM 785 CB PHE 110 -9.660 30.259 47.991 1.000 17.94

ANISOU 785 CB PHE 110 1423 2366 3027 -290 228 - 129

ATOM 786 CG PHE 110 -8.425 29.972 47.165 1.000 20.32

ANISOU 786 CG PHE 110 1702 2650 3368 -176 459 - 385

ATOM 787 CDI PHE 110 -7.257 29.598 47.793 1.000 20.35

ANISOU 787 CDI PHE 110 1885 2462 3387 461 573 - 707

ATOM 788 CD2 PHE 110 -8.405 30.110 45.789 1.000 20.31

ANISOU 788 CD2 PHE 110 2073 2226 3419 512 712 - 264

ATOM 789 CEl PHE 110 -6.102 29.347 47.065 1.000 19.49

ANISOU 789 CEl PHE 110 1958 2116 3332 176 749 - 631

ATOM 790 CE2 PHE 110 -7.288 29.846 45.050 1.000 20.65

ANISOU 790 CE2 PHE 110 2158 2094 3596 758 724 - 321

ATOM 791 CZ PHE 110 -6.118 29.496 45.694 1.000 19.43

ANISOU 791 CZ PHE 110 1925 2131 3327 219 542 - 780

ATOM 792 C PHE 110 -11.49: . 29.556 49.538 1.000 17.08

ANISOU 792 c PHE 110 1774 1806 2911 -74 414 - 111

ATOM 793 0 PHE 110 -12.56229.792 48.929 1.000 21.26

ANISOU 793 0 PHE 110 1849 2577 3650 405 178 - 448 ATOM 794 N PRO 111 -11.40629.717 50.851 1.000 19. 1

ANISOU 794 N PRO 111 2279 2110 2985 -386 519 - 314

ATOM 795 CD PRO 111 -10.278 29.322 51.705 1.000 19.20

ANISOU 795 CD PRO 111 2773 1880 2640 -417 255 - 514

ATOM 796 CA PRO 111 -12.549 30.252 51.604 1.000 21.47

ANISOU 796 CA PRO 111 3026 1924 3206 -50 728 - 635

ATOM 797 CB PRO 111 -12.167 30.007 53.055 1.000 23 .63

ANISOU 797 CB PRO 111 3789 2054 3137 334 776 - 575

ATOM 798 CG PRO 111 -10.775 29.535 53.100 1.000 22 .33

ANISOU 798 CG PRO 111 2767 2908 2809 -1006 623 - 414

ATOM 799 C PRO 111 -12.828 31.739 51.433 1.000 23.88

ANISOU 799 C PRO 111 3139 2049 3887 79 -142 - 479

ATOM 800 O PRO 111 -13.919 32.194 51.834 1.000 26.77

ANISOU 800 O PRO 111 3800 2818 3555 992 -91 - 397

ATOM 801 N SER 112 -11.906 32.517 50.872 1.000 25.19

ANISOU 801 N SER 112 3514 2269 3788 -247 -856 2 82

ATOM 802 CA SER 112 -12.300 33.919 50.631 1.000 26.43

ANISOU 802 CA SER 112 2654 2655 4734 496 1364 4 5 6

ATOM 803 CB SER 112 -12.506 34.712 51.912 1.000 33.37

ANISOU 803 CB SER 112 3122 3663 5895 172 2582 - 510

ATOM 804 OG SER 112 -11.322 34.719 52.688 1.000 36.94

ANISOU 804 OG SER 112 6530 2154 5351 1399 206 - 415

ATOM 805 C SER 112 -11.262 34.587 49.723 1.000 26.62

ANISOU 805 C SER 112 2613 2546 4956 1021 1668 65 1

ATOM 806 O SER 112 -10.219 34.029 49.414 1.000 22.81

ANISOU 806 O SER 112 2241 2782 3645 800 837 - 400

ATOM 807 N GLY 113 -11.570 35.802 49.279 1.000 28.93

ANISOU 807 N GLY 113 2937 2947 5108 1008 1175 1198

ATOM 808 CA GLY 113 -10.659 36.478 48.365 1.000 30.79

ANISOU 808 CA GLY 113 2992 3606 5102 381 798 1400

ATOM 809 C GLY 113 -9.362 36.829 49.070 1.000 31.83

ANISOU 809 C GLY 113 3297 3919 4878 262 897 52 8

ATOM 810 O GLY 113 -8.294 36.790 48.459 1.000 25.85

ANISOU 810 O GLY 113 2920 2317 4585 857 450 - 203

ATOM 811 N ASP 114 -9.479 37.145 50.365 1.000 29.56

ANISOU 811 N ASP 114 3487 2877 4868 866 1104 760

ATOM 812 CA ASP 114 -8.257 37.463 51.122 1.000 26.15

ANISOU 812 CA ASP 114 3189 2680 4066 1028 1584 542

ATOM 813 CB ASP 114 -8.628 37.937 52.526 1.000 33 .81

ANISOU 813 CB ASP 114 5580 2697 4569 1774 1691 - 240

ATOM 814 CG ASP 114 -7.904 39.232 52.840 1.000 40.77

ANISOU 814 CG ASP 114 6798 3734 4960 719 693 -248

ATOM 815 ODl ASP 114 -8.330 40.277 52.295 1.000 48.61

ANISOU 815 ODl ASP 114 6014 2534 9920 1703 931 - 913

ATOM 816 OD2 ASP 114 -6.932 39.178 53.622 1.000 54.35

ANISOU 816 OD2 ASP 114 5258 7609 7783 -868 495 1602

ATOM 817 C ASP 114 -7.310 36.281 51.231 1.000 23.05

ANISOU 817 C ASP 114 2621 2102 4033 444 1874 340

ATOM 818 O ASP 114 -6.111 36.371 50.955 1.000 22.05

ANISOU 818 O ASP 114 2423 2277 3677 131 1411 - 461

ATOM 819 N PHE 115 -7.854 35.160 51.637 1.000 23.21

ANISOU 819 N PHE 115 2945 1890 3984 -130 1293 - 228

ATOM 820 CA PHE 115 -7.120 33.896 51.690 1.000 19.93

ANISOU 820 CA PHE 115 2562 1908 3102 -198 655 - 294

ATOM 821 CB PHE 115 -8.085 32.792 52.157 1.000-19.49

ANISOU 821 CB PHE 115 2378 1754 3275 64 881 - 314

ATOM 822 CG PHE 115 -7.523 31.445 52.540 1.000 17.25

ANISOU 822 CG PHE 115 2053 1589 2912 -56 348 - 695

ATOM 823 CDI . PHE 115 -7.637 30.951 53.833 1.000 19.00

ANISOU 823 CDI . PHE 115 2728 1539 2950 73 496 - 683

ATOM 824 CD2 ! PHE 115 -6.868 30.634 51.615 1.000 17.88 ANISOU 824 CD2 PHE 115 1933 1931 2927 7 298 - 810

ATOM 825 CEl PHE 115 -7.100 29.711 54.163 1.00020.25

ANISOU 825 CEl PHE 115 2825 1825 3042 317 341 - 51

ATOM 826 CE2 PHE 115 -6.338 29.412 51.955 1.000 19.11

ANISOU 826 CE2 PHE 115 1865 2158 3237 336 351 - 8 £

ATOM 827 CZ PHE 115 -6.452 28.936 53.233 1.000 19.39

ANISOU- 827 CZ PHE 115 2068 1910 3390 320 248 - 6 6, 9

ATOM 828 C PHE 115 -6.506 33.624 50.327 1.000 17.86

ANISOU- 828 C PHE 115 1964 1945 2878 61 344 1 6

ATOM 829 O PHE 115 -5.324 33.315 50.271 1.000 17.34

ANISOU 829 O PHE 115 1868 2107 2613 -132 179 15

ATOM 830 N GLU 116 -7.310 33.683 49.263 1.00018.21

ANISOU 830 N GLU 116 1921 1934 3065 547 281 6 2

ATOM 831 CA GLU 116 -6.848 33.387 47.907 1.000 19.99

ANISOU 831 CA GLU 116 2128 2618 2851 81231 222

ATOM 832 CB GLU 116 -7.968 33.605 46.884 1.000 18.61

ANISOU 832 CB GLU 116 2058 1952 3060 231 244 27

ATOM 833 CG GLU 116 -7.398 33.378 45.482 1.00018.61

ANISOU 833 CG GLU 116 1813 2288 2971 295 -32 - 3

ATOM 834 CD GLU 116 -8.442 33.230 44.412 1.00022.40

ANISOU 834 CD GLU 116 1908 3193 3410 -122 -278 - 9

ATOM 835 OEl GLU 116 -9.654 33.272 44.678 1.00030.82

ANISOU 835 OEl GLU 116 1793 4465 5452 273 -414 - 2

ATOM 836 OE2 GLU 116 -8.085 33.063 43.225 1.00030.24

ANISOU 836 OE2 GLU 116 3333 5132 3026 382 -658 32

ATOM 837 C GLU 116 -5.620 34.211 47.535 1.00018.82

ANISOU 837 C GLU 116 2090 2069 2990 294 119 48

ATOM 838 O GLU 116 -4.605 33.701 47.049 1.000 17.41

ANISOU 838 O GLU 116 2228 1780 2606 45 259 282

ATOM 839 N ARG 117 -5.660 35.508 47.777 1.00021.02

ANISOU 839 N ARG 117 2313 2185 3487 408 220 9 0

ATOM 840 CA ARG 117 -4.560 36.420 47.431 1.00021.35

ANISOU 840 CA ARG 117 2337 1800 3976 466 147 - 3

ATOM 841 C ARG 117 -3.291 36.054 48.192 1.00020.52

ANISOU 841 C ARG 117 2292 2124 3380 353 288 - 1

ATOM 842 O ARG 117 -2.186 35.969 47.636 1.00018.96

ANISOU 842 O ARG 117 2223 1664 3316 138 318 23

ATOM 843 CB ARG 117 -4.971 37.885 47.693 1.00025.59

ANISOU 843 CB ARG 117 3237 1900 4587 929 1882 63

ATOM 844 CG ARG 117 -3.881 38.908 47.478 1.000 32.57

ANISOU 844 CG ARG 117 5212 1925 5237 -281 1083 62

ATOM 845 CD ARG 117 -4.325 40.323 47.859 1.00036.56

ANISOU 845 CD ARG 117 6009 2157 5724 149 1774 66

ATOM 846 NE ARG 117 -5.162 40.335 49.056 1.00044.43

ANISOU 846 NE ARG 117 7200 3742 5940 -96 2344 - 1

ATOM 847 CZ ARG 117 -4.763 40.501 50.306 1.00045.48

ANISOU 847 CZ ARG 117 6422 4804 6054 -370 2388 - 2

ATOM 848 NHl ARG 117 -3.484 40.683 50.619 1.000 53.21

ANISOU 848 NHl ARG 117 6867 6451 6900 -2543 2487 35

ATOM 849 NH2 ARG 117 -5.647 40.487 51.301 1.00050.00

ANISOU 849 NH2 ARG 117 6265 6511 6220 224 2433 - 1 5 3 4

ATOM 850 N ILE 118 -3.439 35.832 49.493 1.000 19.30

ANISOU 850 N ILE 118 2275 1838 3221 128 407 -6 4 5

ATOM 851 CA ILE 118 -2.275 35.527 50.331 1.000 18.25

ANISOU 851 CA ILE 118 2376 1745 2811 78 530 - 449

ATOM 852 CB ILE 118 -2.665 35.597 51.820 1.00018.24

ANISOU 852 CB ILE 118 2201 1726 3003 346 906 -3 0 6

ATOM 853 CG2 ! ILE 118 -1.712 34.851 52.732 1.000 18.49

ANISOU 853 CG2 ! ILE 118 2077 2158 2792 -202 308 -5 3 0

ATOM 854 CGI . ILE 118 -2.877 37.031 52.368 1.00024.69

ANISOU ^■ 854 CG . ILE 118 4436 1808 3136 284 1382 - 4 1 4 ATOM 855 CDI ILE 118 -3.786 37.025 53.582 1.000 29.63

ANISOU 855 CDI ILE 118 6169 3096 1994 189 1258 - 1 C 068

ATOM 856 C ILE 118 -1.692 34.172 49.959 1.000 15.65

ANISOU 856 C ILE 118 2316 1549 2082 -89 573 - 1 : 17

ATOM 857 O ILE 118 -0.463 34.035 49.802 1.000 14.59

ANISOU 857 O ILE 118 2240 1255 2051 16 286 2 14

ATOM 858 N TRP 119 -2.523 33.139 49.784 1.000 14.44

ANISOU 858 N TRP 119 2125 1592 1771 47 128 - 71

ATOM 859 CA TRP 119 -2.010 31.795 49.518 1.000 13 .68

ANISOU 859 CA TRP 119 1712 1529 1957 -61 220 4 0

ATOM 860 C3 TRP 119 -3.089 30.755 49.932 1.000 14.93

ANISOU 860 CB TRP 119 1819 1729 2123 -234 295 - 3

ATOM 861 CG TRP 119 -2.864 30.482 51.420 1.000 16.19

ANISOU 861 CG TRP 119 1640 2364 2146 -168 582 1 6

ATOM 862 CD2 TRP 119 -2.116 29.430 51.993 1.000 20.41

ANISOU 862 CD2 TRP 119 3189 2414 2151 202 523 4 0

ATOM 863 CE2 TRP 119 -2.177 29.580 53.392 1.000 19.84

ANISOU 863 CE2 TRP 119 3536 1818 2184 -439 234 13

ATOM 864 CE3 TRP 119 -1.390 28.357 51.456 1.000 23 .94

ANISOU 864 CE3 TRP 119 5382 1647 2068 561 126 4 0

ATOM 865 CDI TRP 119 -3.340 31.223 52.460 1.000 20.05

ANISOU 865 CDI TRP 119 3207 2343 2069 -9 189 - 139

ATOM 866 NE1 TRP 119 -2.938 30.689 53.649 1.000 20.32

ANISOU 866 NE1 TRP 119 2806 2726 2188 -96 -68 - 1

ATOM 867 CZ2 TRP 119 -1.547 28.714 54.281 1.000 22.12

ANISOU 867 CZ2 TRP 119 4071 2256 2078 -17 105 2 2

ATOM 868 CZ3 TRP 119 -0.761 27.490 52.332 1.000 21.52

ANISOU 868 CZ3 TRP 119 4214 2168 1794 311 -193 19

ATOM 869 CH2 TRP 119 -0.847 27.674 53.715 1.000 24.34

ANISOU 869 CH2 TRP 119 5349 2047 1850 329 148 18

ATOM 870 C TRP 119 -1.521 31.634 48.095 1.000 14.27

ANISOU 870 C TRP 119 2180 1259 1985 -187 334 - 6

ATOM 871 O TRP 119 -0.569 30.865 47.855 1.000 14.73

ANISOU 871 O TRP 119 1996 1653 1946 -67 362 10

ATOM 872 N THR 120 -2.109 32.325 47.116 1.000 13 .99

ANISOU 872 N THR 120 2231 1237 1848 106 627 - 1 37

ATOM 873 CA THR 120 -1.541 32.275 45.762 1.000 15.19

ANISOU 873 CA THR 120 1903 2093 1774 9 435 - 242

ATOM 874 CB THR 120 -2.492 32.983 44.787 1.000 16.41

ANISOU 874 CB THR 120 1934 2304 1995 -331 152 6 ,

ATOM 875 OGl THR 120 -3.738 32.297 44.766 1.000 18.53

ANISOU 875 OGl THR 120 1891 2288 2863 -236 195 40

ATOM 876 CG2 THR 120 -1.974 32.906 43.358 1.000 18.02

ANISOU 876 CG2 THR 120 2135 2602 2108 324 322 3 1

ATOM 877 C THR 120 -0.145 32.870 45.727 1.000 14.19

ANISOU 877 C THR 120 1868 2050 1475 87 285 - 167

ATOM 878 O THR 120 0.756 32.299 45.078 1.000 13 .62

ANISOU 878 O THR 120 1864 1692 1620 301 354 2 1

ATOM 879 N GLN 121 0.114 33.962 46.429 1.000 14.55

ANISOU 879 N GLN 121 1721 1672 2136 304 175 - 6

ATOM 880 CA GLN 121 1.459 34.548 46.483 1.000 15.80

ANISOU 880 CA GLN 121 2067 1666 2271 -18 -119 3 6

ATOM 881 C GLN 121 2.465 33.642 47.176 1.000 13 .73

ANISOU 881 C GLN 121 1747 1665 1806 -30 18 114

ATOM 882 Q GLN 121 3.603 33.452 46.685 1.000 15.36

ANISOU 882 O GLN 121 2063 1688 2084 48 360 - 44

ATOM 883 CB GLN 121 1.315 35.918 47.154 1.000 18.85

ANISOU 883 CB GLN 121 2537 1426 3200 -73 -5 3 5 6

ATOM 884 CG GLN 121 2.639 36.558 47.543 1.000 18.88

ANISOU 884 CG GLN 121 2507 1788 2878 59 9 - 248

ATOM 885 CD GLN 121 3.468 36.936 46.337 1.000 20.70 ANISOU 885 CD GLN 121 2584 2138 3142 -373 -85 2 3 1

ATOM 886 OEl GLN 121 2.935 37.088 45.224 1.000 22.47

ANISOU 886 OEl GLN 121 2695 2822 3019 -245 0 12 1

ATOM 887 NE2 GLN 121 4.779 37.101 46.522 1.000 25.22

ANISOU 887 NE2 GLN 121 2426 3344 3811 127 -131 1385

ATOM 888 N TYR 122 2.081 33.054 48.299 1.000 12.26

ANISOU 888 N TYR 122 1747 1514 1399 99 -55 - 258

ATOM 889 CA TYR 122 2.896 32.102 49.050 1.000 13.18

ANISOU 889 C TYR 122 1901 1643 1464 -20 -253 - 160

ATOM 890 CB TYR 122 2.211 31.724 50.364 1.000 13 .78

ANISOU 890 CB TYR 122 2045 1435 1756 116 48 - 2 8

ATOM 891 CG TYR 122 2.994 30.808 51.282 1.000 14.22

ANISOU 891 CG TYR 122 1966 1681 1758 101 68 10 1

ATOM 892 CDI TYR 122 4.271 31.120 51.722 1.000 17.48

ANISOU 892 CDI TYR 122 1788 1972 2882 149 -5 42 0

ATOM 893 CEl TYR 122 5.003 30.284 52.576 1.000 18.55

ANISOU 893 CEl TYR 122 2131 2050 2868 102 -404 2 5 1

ATOM 894 CD2 TYR 122 2.445 29.619 51.731 1.000 20.72

ANISOU 894 CD2 TYR 122 3308 1366 3197 -519 -1524 3 23

ATOM 895 CE2 TYR 122 3.140 28.773 52.574 1.000 25.40

ANISOU 895 CE2 TYR 122 3772 1812 4067 -782 -2084 873

ATOM 896 CZ TYR 122 4.413 29.101 52.992 1.000 20.93

ANISOU 896 CZ TYR 122 2985 1742 3224 -96 -1145 3 13

ATOM 897 OH TYR 122 5.068 28.230 53.826 1.000 29.87

ANISOU 897 OH TYR 122 4830 1998 4522 -680 -3078 62 1

ATOM 898 C TYR 122 3.218 30.876 48.209 1.000 12.33

ANISOU 898 C TYR 122 1833 1412 1439 89 -218 8 8

ATOM 899 O TYR 122 4.395 30.507 48.117 1.000 14.25

ANISOU 899 O TYR 122 1896 1861 1656 339 -242 2 16

ATOM 900 N PHE 123 2.224 30.269 47.573 1.000 11.28

ANISOU 900 N PHE 123 1950 1297 1041 6 -151 18 5

ATOM 901 CA PHE 123 2.482 29.151 46.665 1.000 12.08

ANISOU 901 CA PHE 123 1731 1219 1640 64 -60 2 6

ATOM 902 CB PHE 123 1.139 28.719 46.024 1.000 13.86

ANISOU 902 CB PHE 123 2048 1550 1666 -104 -276 - 82

ATOM 903 CG PHE 123 1.311 27.516 45.099 1.000 14.44

ANISOU 903 CG PHE 123 2173 1677 1637 142 -475 - 9 4

ATOM 904 CDI PHE 123 1.281 26.234 45.614 1.000 13.64

ANISOU 904 CDI PHE 123 1857 1563 1764 -42 -702 - 236

ATOM 905 CD2 PHE 123 1.511 27.664 43.729 1.000 13.81

ANISOU 905 CD2 PHE 123 1450 2164 1634 -420 -295 - 248

ATOM 906 CEl PHE 123 1.468 25.141 44.795 1.000 17.16

ANISOU 906 CEl PHE 123 2282 1819 2418 130 -855 - 644

ATOM 907 CE2 PHE 123 1.715 26.559 42.916 1.000 18.31

ANISOU 907 CE2 PHE 123 2098 2657 2201 -1053 172 - 845

ATOM 908 CZ PHE 123 1.706 25.295 43.445 1.000 16.71

ANISOU 908 CZ PHE 123 1442 2382 2526 -36 -306 - 1077

ATOM 909 C PHE 123 3.489 29.511 45.581 1.000 13.48

ANISOU 909 C PHE 123 2004 1472 1645 236 157 1 8

ATOM 910 O PHE 123 4.424 28.768 45.242 1.000 13.07

ANISOU 910 O PHE 123 1591 1498 1876 42 -78 - 172

ATOM 911 N ASP 124 3.294 30.684 44.948 1.000 13.83

ANISOU 911 N ASP 124 1490 1575 2189 51 207 288

ATOM 912 CA ASP 124 4.207 31.036 43.861 1.000 13 .75

ANISOU 912 CA ASP 124 1505 1330 2389 458 398 3 44

ATOM 913 CB ASP 124 3.708 32.352 43.242 1.000 18.95

ANISOU ^' 913 CB ASP 124 2650 1970 2580 656 -63 92 6

ATOM 914 CG ASP 124 4.470 32.708 41.989 1.000 27.54

ANISOU ' 914 CG ASP 124 5327 2099 3036 -123 939 8 8 0

ATOM 915 ODl . ASP 124 4.541 31.904 41.023 1.000 37.04

ANISOUr 915 ODl ASP 124 6362 3225 4485 108 2616 - 331 ATOM 916 OD2 ASP 124 4.985 33.843 42.011 1.000 32 .60

ANISOU 916 OD2 ASP 124 4724 3509 4151 -1539 234 8 5 1

ATOM 917 C ASP 124 5.645 31.164 44.328 1.000 14.49

ANISOU 917 C ASP 124 1493 1721 2293 327 485 482

ATOM 918 O ASP 124 6.591 30.721 43.674 1.000 14.52

ANISOU 918 O ASP 124 1477 1363 2679 289 497 3 07

ATOM 919 N ARG 125 5.866 31.777 45.499 1.000 14.03

ANISOU 919 N ARG 125 1501 1271 2558 353 398 4 14

ATOM 920 CA ARG 125 7.214 31.863 46.044 1.000 16.40

ANISOU 920 CA ARG 125 1642 1625 2963 194 178 2 2 6

ATOM 921 C ARG 125 7.828 30.494 46.346 1.000 14.69

ANISOU 921 C ARG 125 1396 1688 2496 232 -25 1 5 3

ATOM 922 O ARG 125 8.999 30.245 46.034 1.000 14.10

ANISOU 922 O ARG 125 1279 1656 2424 7 -205 - 201

ATOM 923 CB ARG 125 7.213 32.705 47.318 1.000 18.13

ANISOU 923 CB ARG 125 1950 1902 3035 787 -81 4 6

ATOM 924 CG ARG 125 7.045 34.193 47.041 1.000 23 .51

ANISOU 924 CG ARG 125 2232 1780 4919 883 -36 - 225

ATOM 925 CD ARG 125 8.391 34.815 46.694 1.000 29.33

ANISOU 925 CD ARG 125 3596 2824 4724 -667 237 - 187

ATOM 926 NE ARG 125 8.194 36.262 46.803 1.000 32.99

ANISOU 926 NE ARG 125 4350 2766 5418 -678 -1642 15 6

ATOM 927 CZ ARG 125 8.868 37.153 47.495 1.000 27.38

ANISOU 927 CZ ARG 125 2292 2758 5353 -276 -580 - 246

ATOM 928 NHl ARG 125 9.916 36.821 48.235 1.000 38.55

ANISOU 928 NHl ARG 125 4611 3604 6433 449 -2476 - 669

ATOM 929 NH2 ARG 125 8.491 38.423 47.442 1.000 30.26

ANISOU 929 NH2 ARG 125 4062 2570 4865 -369 -835 3 63

ATOM 930 N GLN 126 7.065 29.573 46.920 1.000 12.36

ANISOU 930 N GLN 126 1316 1376 2002 248 -63 - 264

ATOM 931 CA GLN 126 7.524 28.201 47.153 1.000 13 .39

ANISOU 931 CA GLN 126 1765 1323 1999 219 -355 - 377

ATOM 932 CB AGLN 126 6.363 27.455 47.828 0.500 16.24

ANISOU 932 CB AGLN 126 2422 1391 2357 188 202 - 192

ATOM 933 CG AGLN 126 6.149 27.758 49.284 0.500 18.83

ANISOU 933 CG AGLN 126 2761 2021 2371 68 233 - 210

ATOM 934 CD AGLN 126 7.077 27.146 50.298 0.500 23 .94

ANISOU 934 CD AGLN 126 3578 2745 2774 -604 -757 3 3

ATOM 935 OEl AGLN 126 7.181 27.683 51.419 0.500 35.94

ANISOU 935 OEl AGLN 126 6788 3731 3136 -578 -1567 - 478

ATOM 936 NE2 AGLN 126 7.774 26.055 50.008 0.500 24.63

ANISOU 936 NE2 AGLN 126 4491 1118 3751 -881 -2407 4 62

ATOM 937 CB BGLN 126 6.525 27.417 48.018 0.500 13 .36

ANISOU 937 CB BGLN 126 1695 1137 2245 602 -114 - 255

ATOM 938 CG BGLN 126 6.604 27.750 49.497 0.500 18.28

ANISOU 938 CG BGLN 126 2537 2257 2153 -68 -176 - 105

ATOM 939 CD BGLN 126 5.442 27.237 50.319 0.500 18.42

ANISOU 939 CD BGLN 126 2227 2573 2198 344 -159 1 06

ATOM 940 OEl BGLN 126 5.605 26.442 51.242 0.500 25.36

ANISOU 940 OEl . BGLN 126 3289 3517 2828 -100 -223 9 53

ATOM 941 NE2 BGLN 126 4.231 27.685 50.003 0.500 25.02

ANISOU 941 NE2 , BGLN ^' 126 2427 2669 4413 1004 -83 - 298

ATOM 942 C GLN 126 7.860 27.448 45.861 1.000 12.95

ANISOU 942 C GLN 126 1506 1434 1979 307 -372 - 366

ATOM 943 O GLN 126 8.859 26.721 45.748 1.000 11.66

ANISOU 943 O GLN 126 1461 1142 1827 182 -85 1 5 9

ATOM 944 N TYR 127 6.960 27.578 44.868 1.000 11.61

ANISOU ^• 944 N TYR 127 1400 1276 1735 146 -168 - 10

ATOM 945 CA TYR 127 7.152 26.869 43.585 1.000 11.21

ANISOUr 945 CA TYR 127 1469 1242 1550 -92 -40 1 92

ATOM 946 CB TYR 127 5.901 26.940 42.724 1.000 11.82 -121 -

ANISOU 946 CB TYR 127 1346 1655 1491 -13 82 4 7

ATOM 947 CG TYR 127 5.791 26.069 41.496 1.000 11.49

ANISOU 947 CG TYR 127 1278 1428 1660 -4 -4 1 0

ATOM 948 CDI TYR 127 6.550 24.928 41.270 1.000 11.28

ANISOU 948 CDI TYR 127 1030 1334 1921 -87 -100 3 3

ATOM 949 CEl TYR 127 6.406 24.153 40.115 1.000 11.47

ANISOU 949 CEl TYR 127 1164 1167 2027 -51 -53 2 1

ATOM 950 CD2 TYR 127 4.871 26.410 40.500 1.000 11.98

ANISOU 950 CD2 TYR 127 1677 1093 1784 204 -219 - 1 ( 00

ATOM 951 CE2 TYR 127 4.715 25.655 39.357 1.000 11.37

ANISOU 951 CE2 TYR 127 1539 1118 1665 140 -68 - 7

ATOM 952 CZ TYR 127 5.494 24.508 39.163 1.000 11.02

ANISOU 952 CZ TYR 127 1202 1226 1760 91 48 - 125

ATOM 953 OH TYR 127 5.379 23.720 38.030 1.000 11.57

ANISOU 953 OH TYR 127 1547 1138 1712 94 177 - 3 4

ATOM 954 C TYR 127 8.386 27.392 42.882 1.000 10.83

ANISOU 954 C TYR 127 1296 989 1830 230 -43 3 7 8

ATOM 955 O TYR 127 9.185 26.605 42.375 1.000 10.86

ANISOU 955 O TYR 127 1292 1232 1603 164 -237 - 4

ATOM 956 N THR 128 8.565 28.716 42.865 1.000 10.98

ANISOU 956 N THR 128 1554 976 1642 212 -9 557

ATOM 957 CA THR 128 9.766 29.305 42.295 1.000 11.80

ANISOU 957 CA THR 128 1686 1125 1673 -47 -169 3 8

ATOM 958 CB THR 128 9.605 30.849 42.378 1.000 12.66

ANISOU 958 CB THR 128 1873 1074 1864 -52 -233 52

ATOM 959 OGl THR 128 8.530 31.286 41.517 1.000 16.74

ANISOU 959 OGl THR 128 2223 1597 2542 124 -457 9 9

ATOM 960 CG2 THR 128 10.878 31.510 41.893 1.000 16.54

ANISOU 960 CG2 THR 128 1871 778 3635 262 655 13 8

ATOM 961 C THR 128 11.040 28.828 42.964 1.000 11.26

ANISOU 961 C THR 128 1562 980 1738 -71 -162 148

ATOM 962 O THR 128 11.995 28.458 42.258 1.000 12.16

ANISOU 962 O THR 128 1769 1092 1758 17 26 279

ATOM 963 N ALA 129 11.083 28.802 44.300 1.000 10.39

ANISOU 963 N ALA 129 1183 1001 1763 70 -118 147

ATOM 964 CA ALA 129 12.273 28.386 45.037 1.000 10.59

ANISOU 964 CA ALA 129 1206 945 1873 -69 -170 281

ATOM 965 CB ALA 129 12.113 28.603 46.536 1.000 12.46

ANISOU 965 CB ALA 129 2113 851 1769 82 -218 577

ATOM 966 C ALA 129 12.575 26.906 44.802 1.000 11.35

ANISOU 966 C ALA 129 1258 883 2170 -16 -141 410

ATOM 967 O ALA 129 13.738 26.485 44.641 1.000 10.93

ANISOU 967 O ALA 129 1202 1157 1796 -36 -213 12

ATOM 968 N SER 130 11.519 26.086 44.750 1.000 12.27

ANISOU 968 N SER 130 1280 984 2398 -65 -1 - 24

ATOM 969 CA SER 130 11.682 24.650 44.512 1.000 10.89

ANISOU 969 CA SER 130 1623 876 1638 -85 44 37 0

ATOM 970 CB ASEP . 130 10.342 23.940 44.716 0.500 10.08

ANISOU 970 CB ASEP - 130 1432 603 1793 213 247 413

ATOM 971 OG ASEP - 130 9.771 24.063 46.006 0.500 9 .12

ANISOU 971 OG ASEP - 130 1021 651 1792 91 1 - 143

ATOM 972 CB BSER 130 10.364 23.919 44.765 0.500 10.60

ANISOU 972 CB BSEF - 130 1687 822 1521 -45 318 15 8

ATOM 973 OG BSER 130 9.418 24.098 43.734 0.500 16.22

ANISOU 973 OG BSER 130 1717 1289 3156 137 -525 3 4

ATOM 974 C SER 130 12.214 24.373 43.110 1.000 10.53

ANISOU 974 C SER 130 1586 733 1684 -166 210 484

ATOM 975 O SER 130 13.137 23.532 42.942 1.000 11.17

ANISOU ^' 975 O SER 130 1385 1012 1849 -151 -95 14

ATOM 976 N ARG 131 11.680 25.044 42.079 1.000 10.46

ANISOU ^' 976 N ARG 131 1578 861 1534 -87 -66 9 9 ATOM 977 CA ARG 131 12.260 24.839 40.742 1.000 10.60

ANISOU 977 CA ARG 131 1480 1110 1438 61 -288 8 2

ATOM 978 CB ARG 131 11.426 25.553 39.679 1.000 12 .99

ANISOU- 978 CB ARG 131 1893 1369 1673 63 -525 27 6

ATOM 979 CG ARG 131 10.003 25.065 39.431 1.000 13 .64

ANISOU 979 CG ARG 131 1707 1735 1742 335 -559 - 8 6

ATOM 980 CD ARG 131 9.349 25.669 38.206 1.000 17.71

ANISOU 980 CD ARG 131 2078 1973 2677 81 -983 7 0 1

ATOM 981 NE ARG 131 9.453 27.113 38.015 1.000 19.76

ANISOU 981 NE ARG 131 2716 2034 2757 -25 -525 7 13

ATOM 982 CZ ARG 131 8.629 28.004 38.568 1.000 21.24

ANISOU 982 CZ ARG 131 3688 1878 2503 -8 -128 647

ATOM 983 NHl ARG 131 7.631 27.634 39.366 1.000 21.32

ANISOU 983 NHl ARG 131 2792 3142 2166 -486 -667 5 7

ATOM 984 NH2 ARG 131 8.771 29.310 38.361 1.000 27.83

ANISOU 984 NH2 ARG 131 4649 1822 4103 -90 -422 5 6 1

ATOM 985 C ARG 131 13.714 25.323 40.688 1.000 10.42

ANISOU 985 C ARG 131 1542 1078 1339 50 -103 1

ATOM 986 O ARG 131 14.568 24.683 40.080 1.000 10.94

ANISOU 986 O ARG 131 1544 1105 1506 177 -134 4 2

ATOM 987 N ALA 132 14.028 26.438 41.343 1.000 10.97

ANISOU 987 N ALA 132 1477 1129 1563 74 -364 - 45

ATOM 988 CA ALA 132 15.379 26.983 41.343 1.000 11.10

ANISOU 988 CA ALA 132 1539 944 1735 9 -102 9 7

ATOM 989 CB ALA 132 15.429 28.344 42.048 1.000 12.82

ANISOU 989 CB ALA 132 1711 1171 1987 -48 -248 - 198

ATOM 990 C ALA 132 16.393 26.045 41.995 1.000 11.55

ANISOU 990 C ALA 132 1085 1107 2197 -197 305 745

ATOM 991 O ALA 132 17.481 25.832 41.432 1.000 11.81

ANISOU 991 O ALA 132 1081 1809 1599 -204 17 - 9

ATOM 992 N VAL 133 16.061 25.490 43.175 1.000 11.16

ANISOU 992 N VAL 133 1260 1356 1623 -148 51 350

ATOM 993 CA VAL 133 17.011 24.587 43.840 1.000 11.62

ANISOU 993 CA VAL 133 1505 1529 1380 -69 -297 8 9

ATOM 994 CB VAL 133 16.738 24.418 45.344 1.000 12.14

ANISOU 994 CB VAL 133 1376 1674 1564 -74 -25 3 64

ATOM 995 CGI VAL 133 15.550 23.501 45.608 1.000 14.96

ANISOU 995 CGI VAL 133 1705 2316 1662 -706 8 - 357

ATOM 996 CG2 VAL 133 17.981 23.864 46.033 1.000 15.63

ANISOU 996 CG2 VAL 133 1755 2340 1845 -341 -677 5 5 1

ATOM 997 C VAL 133 17.079 23.268 43.065 1.000 11.71

ANISOU 997 C VAL 133 1376 1363 1711 -24 -425 169

ATOM 998 O VAL 133 18.198 22.733 42.925 1.000 11.55

ANISOU 998 O VAL 133 1391 1453 1545 -4 -116 3 9 8

ATOM 999 N ALA 134 15.982 22.758 42.480 1.000 12.87

ANISOU 999 N ALA 134 1399 1517 1973 28 -334 - 228

ATOM 1000 CA ALA 134 16.084 21.557 41.621 1.000 10.57

ANISOU 1000 CA ALA 134 1106 1220 1691 153 -298 9 6

ATOM 1001 CB ALA 134 14.699 21.096 41.186 1.000 12.20

ANISOU 1001 CB ALA 134 1254 1589 1794 35 -303 - 127

ATOM 1002 C ALA 134 16.968 21.797 40.399 1.000 12.58

ANISOU 1002 C ALA 134 1393 1399 1987 272 -4 277

ATOM 1003 O ALA 134 17.712 20.924 39.970 1.000 11.01

ANISOU 1003 O ALA 134 1254 1358 1574 83 -268 2 6

ATOM 1004 N ARG 135 16.908 22.995 39.809 1.000 12.03

ANISOU 1004 N ARG 135 1517 1230 1824 -62 -327 8 7

ATOM 1005 CA ARG 135 17.773 23.353 38.676 1.000 13.23

ANISOU 1005 CA ARG 135 1854 1158 2015 -270 -209 1 6 1

ATOM 1006 CB ARG 135 17.393 24.734 38.170 1.000 14.57

ANISOU 1006 CB ARG 135 2203 1339 1994 -45 -541 222

ATOM 1007 CG ARG 135 17.753 25.160 36.797 1.000 19.22 ANISOU 1007 CG ARG 135 4204 1120 1980 -490 -433 15 0

ATOM 1008 CD ARG 135 17.237 26.563 36.471 1.000 22 .14

ANISOU 1008 CD ARG 135 4046 1500 2868 -159 315 82 2

ATOM 1009 NE ARG 135 15.831 26.607 36.077 1.000 22 .66

ANISOU 1009 NE ARG 135 4239 1404 2965 -94 47 2 5 7

ATOM 1010 CZ ARG 135 14.802 27.184 36.684 1.000 21.69

ANISOU 1010 CZ ARG 135 4004 1906 2333 92 -506 6 4

ATOM 1011 NHl ARG 135 14.917 27.843 37.833 1.000 22.26

ANISOU 1011 NHl ARG 135 4114 2532 1812 460 -833 3 4 1

ATOM 1012 NH2 ARG 135 13.582 27.113 36.149 1.000 22 .31

ANISOU 1012 NH2 ARG 135 4000 2243 2234 -544 -419 8

ATOM 1013 C ARG 135 19.251 23.275 39.057 1.000 12 .70

ANISOU 1013 C ARG 135 1742 1264 1821 -119 -16 43 0

ATOM 1014 O ARG 135 20.069 22.818 38.238 1.000 14.67

ANISOU 1014 O ARG 135 2133 1529 1910 19 169 3 91

ATOM 1015 N GLU 136 19.572 23.712 40.266 1.000 12 .15

ANISOU 1015 N GLU 136 1423 1372 1820 -36 70 43 0

ATOM 1016 CA GLU 136 20.960 23.630 40.763 1.000 14.52

ANISOU 1016 CA GLU 136 1622 1701 2194 -90 -197 3 7 1

ATOM 1017 CB GLU 136 21.212 24.513 41.981 1.000 15.59

ANISOU 1017 CB GLU 136 1502 1781 2642 14 -231 1 1

ATOM 1018 CG GLU 136 21.064 26.020 41.783 1.000 18.01

ANISOU 1018 CG GLU 136 2010 1762 3071 -232 -153 12 6

ATOM 1019 CD GLU 136 21.798 26.484 40.537 1.000 20.18

ANISOU 1019 CD GLU 136 2071 2079 3519 -308 89 3 69

ATOM 1020 OEl GLU 136 22.987 26.148 40.394 1.000 24.64

ANISOU 1020 OEl GLU 136 2060 2937 4364 -262 338 615

ATOM 1021 OE2 GLU 136 21.195 27.150 39.670 1.000 24.19

ANISOU 1021 OE2 GLU 136 2479 2327 4385 -381 317 1426

ATOM 1022 C GLU 136 21.364 22.186 41.076 1.000 14.00

ANISOU 1022 C GLU 136 1338 1619 2361 -112 -442 22 3

ATOM 1023 O GLU 136 22.508 21.781 40.833 1.000 13.86

ANISOU 1023 O GLU 136 1366 1890 2009 -100 -287 3 2 9

ATOM 1024 N VAL 137 20.472 21.338 41.580 1.000 11.78

ANISOU 1024 N VAL 137 1309 1451 1715 148 -223 8 5

ATOM 1025 CA VAL 137 20.753 19.896 41.771 1.000 12.49

ANISOU 1025 CA VAL 137 1369 1522 1853 240 -69 2 89

ATOM 1026 CB VAL 137 19.560 19.165 42.429 1.000 12.41

ANISOU 1026 CB VAL 137 1422 1424 1869 -67 -85 - 204

ATOM 1027 CGI VAL 137 19.728 17.634 42.401 1.000 12.55

ANISOU 1027 CGI VAL 137 1371 1508 1892 182 185 111

ATOM 1028 CG2 VAL 137 19.355 19.607 43.852 1.000 11.35

ANISOU 1028 CG2 VAL 137 1461 1281 1572 182 -254 288

ATOM 1029 C VAL 137 21.100 19.241 40.435 1.000 12.48

ANISOU 1029 C VAL 137 1202 1428 2113 150 -16 8 5

ATOM 1030 O VAL 137 22.057 18.462 40.287 1.000 13.03

ANISOU 1030 O VAL 137 1021 1683 2249 149 1 14 6

ATOM 1031 N LEU 138 20.309 19.562 39.401 1.000 10.28

ANISOU 1031 N LEU 138 1198 881 1829 -1 5 158 2 2 6

ATOM 1032 CA LEU 138 20.571 19.029 38.066 1.000 12.48

ANISOU 1032 CA LEU 138 1312 1408 2024 110 273 - 52

ATOM 1033 CB LEU 138 19.398 19.358 37.130 1.000 11.81

ANISOU 1033 CB LEU 138 1260 1586 1642 -20 383 4 3

ATOM 1034 CG LEU 138 18.036 18.726 37.457 1.000 10.77

ANISOU 1034 CG LEU 138 1391 1397 1304 -83 219 2 13

ATOM 1035 CDI . LEU 138 16.916 19.324 36.596 1.000 12 .72

ANISOU ^• 1035 CDI . LEU 138 1416 1587 1829 -59 -25 17 3

ATOM 1036 CD2 ^> LEU 138 18.052 17.207 37.320 1.000 14.32

ANISOU >^■ 1036 CD: ^> LEU 138 1986 1390 2065 -79 296 3 70

ATOM 1037 c LEU 138 21.903 19.525 37.505 1.000 13 .61

ANISOUr 1037 c LEU 138 1305 2026 1840 -65 174 5 ATOM 1038 O LEU 138 22.695 18.760 36.920 1.000 14.97

ANISOU 1038 0 LEU 138 1125 2247 2313 105 234 1 7 :

ATOM 1039 N ARG 139 22.184 20.816 37.614 1.000 13 . 26

ANISOU 1039 N ARG 139 1432 2046 1561 -155 219 3 1 ^'

ATOM 1040 CA ARG 139 23.397 21.372 37.085 1.000 14. 71

ANISOU 1040 CA ARG 139 1648 1941 2000 -27 502 44 4 ^' 7

ATOM 1041 C ARG 139 24.636 20.815 37.775 1.000 15. 16

ANISOU 1041 C ARG 139 1425 2101 2235 -158 324 11 ι

ATOM 1042 O ARG 139 25.650 20.495 37.166 1.000 18. 15

ANISOU 1042 O ARG 139 1628 2581 2688 18 612 33 9

ATOM 1043 CB ARG 139 23.394 22.926 37.206 1.000 19. 67

ANISOU 1043 CB ARG 139 1749 1923 3803 -196 186 2 5 :

ATOM 1044 CG ARG 139 24.418 23.487 36.237 1.000 28 . 66

ANISOU 1044 CG ARG 139 3924 2584 4383 -2305 882 - 5 6. 3

ATOM 1045 CD ARG 139 24.245 24.997 36.111 1.000 39. 58

ANISOU 1045 CD ARG 139 6801 2389 5849 -3273 119 - 3 C 0 6

ATOM 1046 NE ARG 139 24.910 25.660 37.210 1.000 47. 91

ANISOU 1046 NE ARG 139 9548 2435 6222 -2157 -1331 - : 7 0 8

ATOM 1047 CZ ARG 139 24.493 26.682 37.928 1.000 45. 42

ANISOU 1047 CZ ARG 139 6941 4516 5802 -882 -2118 -1 1 2 3 8

ATOM 1048 NHl ARG 139 23.316 27.273 37.722 1.000 64. 33

ANISOU 1048 NHl ARG 139 7248 8153 9039 93 -2965 - -980

ATOM 1049 NH2 ARG 139 25.309 27.109 38.888 1.000 32. 62

ANISOU 1049 NH2 ARG 139 5020 4758 2616 -2746 590 1 6

ATOM 1050 N ALA 140 24.562 20.684 39.096 1.000 14. 85

ANISOU 1050 N ALA 140 1287 2204 2151 -517 -26 - 4

ATOM 1051 CA ALA 140 25.730 20.257 39.856 1.000 15. 80

ANISOU 1051 CA ALA 140 989 2649 2366 -309 -9 -401

ATOM 1052 CB ALA 140 25.444 20.442 41.330 1.000 19. 36

ANISOU 1052 CB ALA 140 2685 2447 2222 243 -435 - 4 I 8 0

ATOM 1053 C ALA 140 26.111 18.806 39.584 1.000 16. 86

ANISOU 1053 C ALA 140 1555 2795 2054 12 -186 - -458

ATOM 1054 O ALA 140 27.258 18.403 39.796 1.000 18. 90

ANISOU 1054 O ALA 140 1538 2686 2958 -21 60 : L 45

ATOM 1055 N THR 141 25.147 18.025 39.098 1.000 17. 53

ANISOU 1055 N THR 141 1779 2532 2350 -528 218 - 1 ( 0 8

ATOM 1056 CA THR 141 25.340 16.625 38.765 1.000 15. 59

ANISOU 1056 CA THR 141 1256 2401 2268 -192 -95 2 9

ATOM 1057 CB THR 141 24.207 15.735 39.343 1.000 14. 77

ANISOU 1057 CB THR 141 1238 2200 2172 155 282 30

ATOM 1058 OGl THR 141 22.946 16.168 38.849 1.000 12. 47

ANISOU 1058 OGl THR 141 1249 1565 1926 -31 295 47

ATOM 1059 CG2 THR 141 24.167 15.818 40.859 1.000 14. 82

ANISOU 1059 CG2 THR 141 1394 2077 2160 135 -47 17

ATOM 1060 C THR 141 25.423 16.374 37.257 1.000 16. .11

ANISOU 1060 C THR 141 1732 2046 2343 303 583 32

ATOM 1061 O THR 141 25.432 15.235 36.778 1.000 17. , 55

ANISOU 1061 O THR 141 1991 2104 2573 237 555 24

ATOM 1062 N GLY 142 25.474 17.416 36.446 1.000 17. .74

ANISOU 1062 N GLY 142 2127 2197 2416 303 260 5 0

ATOM 1063 CA GLY 142 25.611 17.263 34.987 1.000 17. .32

ANISOU 1063 CA GLY 142 1642 2494 2447 -160 453 51

ATOM 1064 C GLY 142 24.426 16.556 34.358 1.000 16 .37

ANISOU 1064 C GLY 142 1619 1893 2710 261 472 4 2

ATOM 1065 O GLY 142 24.654 15.824 33.379 1.000 18 .43

ANISOU 1065 O GLY 142 2243 2558 2201 57798 1 f 53

ATOM 1066 N THR 143 23.232 16.738 34.907 1.000 13 .99

ANISOU 1066 N THR 143 1531 1429 2356 83 430 3 ! 5 0

ATOM 1067 CA THR 143 22.049 16.003 34.472 1.000 14 .69

ANISOU 1067 CA THR 143 1768 1591 2223 8 342 9 3

ATOM 1068 CB THR 143 21.208 15.584 35.700 1.000 > 15 .52 -125-

ANISOU 1068 CB THR 143 1457 1653 2785 55 419 52 9

ATOM 1069 OGl THR 143 22.037 14.784 36.573 1.000 14.63

ANISOU 1069 OGl THR 143 1296 1792 2471 52 434 3 69

ATOM 1070 CG2 THR 143 20.044 14.738 35.231 1.000 14.24

ANISOU 1070 CG2 THR 143 1761 1981 1669 3 379 1 92

ATOM 1071 C THR 143 21.135 16.785 33.532 1.000 13 .96

ANISOU 1071 C THR 143 1553 1708 2044 128 479 - 131

ATOM 1072 O THR 143 20.642 17.828 33.923 1.000 15.65

ANISOU 1072 O THR 143 2374 1580 1995 315 486 5 5

ATOM 1073 N GLU 144 20.928 16.279 32.322 1.000 15.32

ANISOU 1073 N GLU 144 1734 1904 2184 -156 260 - 271

ATOM 1074 CA GLU 144 19.917 16.693 31.362 1.000 17.30

ANISOU 1074 CA GLU 144 1686 2470 2417 -377 152 10 6

ATOM 1075 C GLU 144 18.774 15.693 31.292 1.000 16.84

ANISOU 1075 C GLU 144 1633 2380 2386 -298 313 - 242

ATOM 1076 O GLU 144 18.922 14.631 30.680 1.000 16.71

ANISOU 1076 O GLU 144 1470 2057 2821 -43 610 5 8

ATOM 1077 CB GLU 144 20.539 16.856 29.970 1.000 21.91

ANISOU 1077 CB GLU 144 2747 3417 2162 -1508 31 - 8

ATOM 1078 CG GLU 144 19.568 17.063 28.825 1.000 37.93

ANISOU 1078 CG GLU 144 6652 4374 3385 -2057 -2082 176 ^'

ATOM 1079 CD GLU 144 19.293 18.507 28.466 1.000 43.55

ANISOU 1079 CD GLU 144 7869 4258 4419 -2497 -2259 212

ATOM 1080 OEl GLU 144 19.602 19.365 29.326 1.000 51.81

ANISOU 1080 OEl GLU 144 9843 4613 5230 -3180 -832 1126

ATOM 1081 OE2 GLU 144 18.766 18.798 27.367 1.000 40.12

ANISOU 1081 OE2 GLU 144 5551 6029 3662 -285 -115 2660

ATOM 1082 N PRO 145 17.620 15.959 31.908 1.000 14.29

ANISOU 1082 N PRO 145 1634 1364 2432 -420- ! 265

ATOM 1083 CD PRO 145 17.256 17.136 32.718 1.000 14.14

ANISOU 1083 CD PRO 145 1735 1778 1859 -55 32 167

ATOM 1084 CA PRO 145 16.507 15.000 31.807 1.000 13.72

ANISOU 1084 CA PRO 145 1484 1391 2337 66 17: i 466

ATOM 1085 CB PRO 145 15.406 15.701 32.606 1.000 14.20

ANISOU 1085 CB PRO 145 1459 1636 2302 161 -41 2 8 9

ATOM 1086 CG PRO 145 16.132 16.608 33.561 1.000 14.43

ANISOU 1086 CG PRO 145 1796 2007 1679 -23 -42 449

ATOM 1087 C PRO 145 16.076 14.794 30.372 1.000 15.18

ANISOU 1087 C PRO 145 1745 1665 2359 -192 231 2 87

ATOM 1088 O PRO 145 16.178 15.685 29.509 1.000 15.40

ANISOU 1088 O PRO 145 2430 1511 1910 -85 613 - 15

ATOM 1089 N ASP 146 15.544 13.613 30.070 1.000 15.79

ANISOU 1089 N ASP 146 2019 1611 2367 -191 666 8 1

ATOM 1090 CA ASP 146 14.918 13.366 28.773 1.000 16.74

ANISOU 1090 CA ASP 146 2095 1759 2506 -348 575 - 77

ATOM 1091 CB ASP 146 14.300 11.966 28.727 1.000 18.99

ANISOU 1091 CB ASP 146 2508 1729 2977 -323 780 - 439

ATOM 1092 CG ASP 146 13.504 11.784 27.444 1.000 27.04

ANISOU 1092 CG ASP 146 4012 2450 3813 -720 -229 - 805

ATOM 1093 ODl ASP 146 12.295 12.121 27.409 1.000 38.65

ANISOU 1093 ODl , ASP 146 3943 4889 5852 -595 -1282 - 32

ATOM 1094 OD2 ASP 146 14.091 11.311 26.466 1.000 39.95

ANISOU 1094 OD2 ; ASP 146 6913 5052 3214 16 0 -1182

ATOM 1095 C ASP 146 13.860 14.441 28.552 1.000 16.65

ANISOU 1095 C ASP 146 2461 1904 1961 -128 580 - 4 0

ATOM 1096 O ASP 146 13.041 14.605 29.457 1.000 15.67

ANISOU 1096 O ASP 146 2110 1935 1908 -334 381 - 420

ATOM 1097 N GLY 147 13.871 15.149 27.429 1.000 20.60

ANISOU 1097 N GLY 147 3484 2416 1927 -26 419 12 9

ATOM 1098 CA GLY 147 12.903 16.212 27.155 1.000 ι 18.06

ANISOU 1098 CA GLY 147 2771 2451 1638 -382 98 9 3 ATOM 1099 C GLY 147 13.361 17.574 27.609 1.000 18 .73

ANISOU 1099 c GLY 147 2836 2195 2085 -524 143 52 '

ATOM 1100 0 GLY 147 12.676 18.570 27.282 1.000 18.34

ANISOU 1100 0 GLY 147 2865 2416 1687 -413 -72 3 8 !

ATOM 1101 N GLY 148 14.498 17.634 28.316 1.000 16.35

ANISOU 1101 N GLY 148 2936 1506 1772 -157 142 8 8

ATOM 1102 CA GLY 148 15.116 18.889 28.747 1.000 15.34

ANISOU 1102 CA GLY 148 2723 1279 1829 55 450 - 2 6

ATOM 1103 C GLY 148 14.768 19.339 30.144 1.000 12.97

ANISOU 1103 C GLY 148 2231 1416 1280 -93 -62 40 ^'

ATOM 1104 O GLY 148 13.769 18.930 30.771 1.000 13 .79

ANISOU 1104 O GLY 148 2301 1376 1561 -164 88 3 2 3

ATOM 1105 N VAL 149 15.604 20.224 30.718 1.000 12.81

ANISOU 1105 N VAL 149 1815 1366 1686 155 -31 2 3

ATOM 1106 CA VAL 149 15.388 20.724 32.079 1.000 11.81

ANISOU 1106 CA VAL 149 1333 1390 1765 54 -92 129

ATOM 1107 CB VAL 149 16.594 21.636 32.480 1.000 11.97

ANISOU 1107 CB VAL 149 1136 1696 1717 -100 246 12

ATOM 1108 CGI VAL 149 16.358 22.336 33.802 1.000 15.26

ANISOU 1108 CGI VAL 149 1941 1922 1936 -195 55 - 223

ATOM 1109 CG2 VAL 149 17.868 20.794 32.538 1.000 17.21

ANISOU 1109 CG2 VAL 149 1231 2045 3265 45 102 - 103

ATOM 1110 C VAL 149 14.101 21.482 32.280 1.000 11.32

ANISOU 1110 C VAL 149 1186 1303 1813 -78 131 47

ATOM 1111 O VAL 149 13.378 21.218 33.253 1.000 12.35

ANISOU 1111 O VAL 149 1664 1423 1608 -71 229 16

ATOM 1112 N GLU 150 13.752 22.463 31.460 1.000 11.96

ANISOU 1112 N GLU 150 1347 1453 1746 29 -36 420

ATOM 1113 CA GLU 150 12.592 23.286 31.815 1.000 10.90

ANISOU 1113 CA GLU 150 1623 1359 1159 118 0 4 05

ATOM 1114 CB GLU 150 12.608 24.601 30.999 1.000 17.60

ANISOU 1114 CB GLU 150 2530 1470 2687 181 -161 9 0

ATOM 1115 CG GLU 150 13.811 25.488 31.314 1.000 17.86

ANISOU 1115 CG GLU 150 2744 797 3246 246 434 2 02

ATOM 1116 CD GLU 150 13.956 25.929 32.738 1.000 19.47

ANISOU 1116 CD GLU 150 3018 1353 3027 -97 -84 66

ATOM 1117 OEl GLU 150 12.951 26.005 33.475 1.000 18.21

ANISOU 1117 OEl GLU 150 3035 1512 2373 -178 -321 5 3

ATOM 1118 OE2 GLU 150 15.109 26.237 33.122 1.000 22.59

ANISOU 1118 OE2 GLU 150 2993 1664 3927 -38 -150 2 8

ATOM 1119 C GLU 150 11.277 22.533 31.705 1.000 12.22

ANISOU 1119 C GLU 150 1429 1540 1676 235 147 - 5

ATOM 1120 O GLU 150 10.341 22.757 32.530 1.000 13.44

ANISOU 1120 O GLU 150 1739 1474 1894 315 470 2 8

ATOM 1121 N ALA 151 11.118 21.625 30.742 1.000 11.88

ANISOU 1121 N ALA 151 1783 1255 1477 9445 253

ATOM 1122 CA ALA 151 9.881 20.844 30.698 1.000 13 .82

ANISOU 1122 CA ALA 151 1744 2054 1454 -100 -413 3 9

ATOM 1123 CB ALA 151 9.739 20.094 29.390 1.000 14.89

ANISOU 1123 CB ALA 151 1489 2318 1851 22 -269 - 3 5

ATOM 1124 C ALA 151 9.792 19.864 31.867 1.000 12.71

ANISOU 1124 C ALA 151 1448 1463 1920 93 41 424

ATOM 1125 O ALA 151 8.655 19.580 32.280 1.000 14.69

ANISOU 1125 O ALA 151 1535 2114 1932 -242 204 - 1 08

ATOM 1126 N PHE 152 10.925 19.401 32.410 1.000 11.73

ANISOU 1126 N PHE 152 1598 1259 1598 120 9 271

ATOM 1127 CA PHE 152 10.890 18.554 33.602 1.000 10.61

ANISOU 1127 CA PHE 152 1444 1061 1526 -33 34 1 6 0

ATOM 1128 CB PHE 152 12.293 17.981 33.820 1.000 10.23

ANISOU 1128 CB PHE 152 1317 1132 1437 -144 207 4 1

ATOM 1129 CG PHE 152 12.517 17.187 35.095 1.000 10.36

SUBSTΓΓUTE SHEET (RULE 26) -127-

ANISOU 1129 CG PHE 152 1388 1149 1399 -34 147 2 7 ι

ATOM 1130 CDI PHE 152 12.036 15.896 35.229 1.000 11.24

ANISOU 1130 CDI PHE 152 1479 1047 1743 114 -103 5 6 ι

ATOM 1131 CD2 PHE 152 13.229 17.701 36.154 1.000 11.21

ANISOU 1131 CD2 PHE 152 1489 1449 1319 85 174 15 1

ATOM 1132 CEl PHE 152 12.252 15.163 36.380 1.000 10.80

ANISOU 1132 CEl PHE 152 1400 1234 1467 249 -111 3 7 :

ATOM 1133 CE2 PHE 152 13.431 16.992 37.341 1.000 11.82

ANISOU 1133 CE2 PHE 152 1709 1622 1160 -276 414 25 ι

ATOM 1134 CZ PHE 152 12.932 15.717 37.457 1.000 11.97

ANISOU 1134 CZ PHE 152 1651 1604 1293 -255 296 17 ι

ATOM 1135 C PHE 152 10.430 19.292 34.858 1.000 12.24

ANISOU 1135 C PHE 152 1754 1168 1730 -10 339 8 4

ATOM 1136 0 PHE 152 9.728 18.729 35.726 1.000 11.49

ANISOU 1136 0 PHE 152 1672 1142 1550 200 109 2 7

ATOM 1137 N LEU 153 10.809 20.575 34.997 1.000 11.86

ANISOU 1137 N LEU 153 2030 1236 1240 -6 73 15 6

ATOM 1138 CA LEU 153 10.532 21.386 36.155 1.000 11.99

ANISOU 1138 CA LEU 153 1890 1229 1437 -165 307 8 5

ATOM 1139 CB LEU 153 11.654 22.420 36.353 1.000 12.81

ANISOU 1139 CB LEU 153 1691 1381 1794 -72 97 - 4 0

ATOM 1140 CG LEU 153 13.059 21.910 36.592 1.000 12.87

ANISOU 1140 CG LEU 153 1762 1645 1483 146 269 6 4

ATOM 1141 CDI LEU 153 14.027 23.081 36.611 1.000 15.99

ANISOU 1141 CDI LEU 153 1609 2006 2462 -49 450 - 4 : 31

ATOM 1142 CD2 LEU 153 13.185 21.158 37.914 1.000 19.37

ANISOU 1142 CD2 LEU 153 3091 2462 1806 809 275 54

ATOM 1143 C LEU 153 9.179 22.084 36.123 1.000 12.96

ANISOU 1143 C LEU 153 1728 1253 1943 -336 360 - 4

ATOM 1144 0 LEU 153 8.709 22.506 37.193 1.000 13.24

ANISOU 1144 0 LEU 153 1617 1302 2109 -443 481 - 1 ! 82

ATOM 1145 N ASP 154 8.568 22.203 34.955 1.000 13.29

ANISOU 1145 N ASP 154 1643 1457 1951 60 517 280

ATOM 1146 CA ASP 154 7.195 22.671 34.764 1.000 14.21

ANISOU 1146 CA ASP 154 1862 1255 2280 313 631 68

ATOM 1147 CB ASP 154 6.995 23.269 33.373 1.000 18.38

ANISOU 1147 CB ASP 154 2091 2156 2738 328 728 14 75

ATOM 1148 CG ASP 154 5.534 23.367 32.929 1.000 22.95

ANISOU 1148 CG ASP 154 2323 3543 2855 676 430 15 01

ATOM 1149 ODl ASP 154 4.685 23.607 33.820 1.000 20.85

ANISOU 1149 ODl ASP 154 2164 2368 3389 895 478 11 44

ATOM 1150 OD2 ASP 154 5.168 23.254 31.702 1.000 24.33

ANISOU 1150 OD2 ASP 154 2989 3146 3110 228 48 112 ε

ATOM 1151 C ASP 154 6.294 21.455 34.985 1.000 11.22

ANISOU 1151 C ASP 154 1594 1403 1265 123 147 41

ATOM 1152 O ASP 154 6.043 20.729 34.015 1.000 13.31

ANISOU 1152 O ASP 154 2143 1728 1186 427 219 17

ATOM 1153 N CYS 155 5.891 21.220 36.233 1.000 9 .91

ANISOU 1153 N CYS 155 1425 1098 1243 -76 186 2 ^'

ATOM 1154 CA CYS 155 5.446 19.881 36.627 1.000 9 .41

ANISOU 1154 CA CYS 155 1294 1168 1115 -13 154 17

ATOM 1155 CB CYS 155 6.635 19.171 37.269 1.000 10.64

ANISOU 1155 CB CYS 155 1276 1015 1753 28 -51 - 122

ATOM 1156 SG CYS 155 7.316 19.819 38.797 1.000 12.01

ANISOU 1156 SG CYS 155 1376 1554 1633 -195 -199 9 .

ATOM 1157 C CYS 155 4.138 19.885 37.423 1.00C 1 9 .66

ANISOU 1157 C CYS 155 1301 1355 1013 115 146 2 1

ATOM 1158 O CYS 155 3.215 20.645 37.064 1.00C > 11.61

ANISOU ^' 1158 O CYS 155 1349 1386 1676 130 116 2 9

ATOM 1159 N GLU 156 4.021 19.033 38.442 1.00C ) 10.26

ANISOU r 1159 N GLU 156 1263 1495 1139 -29 168 2 9 ATOM 1160 CA GLU 156 2.778 18.787 39.173 1.000 9 . 04

ANISOU 1160 CA GLU 156 998 1160 1278 -76 -37 2 3 6

ATOM 1161 CB GLU 156 2.300 17.391 38.772 1.000 11.63

ANISOU 1161 CB GLU 156 1187 1348 1885 -67 -135 - 190

ATOM 1162 CG GLU 156 1.841 17.282 37.326 1.000 14.29

ANISOU 1162 CG GLU 156 1741 1640 2049 -628 -507 5 0

ATOM 1163 CD GLU 156 0.502 17.949 37.039 1.000 17.90

ANISOU 1163 CD GLU 156 1772 2692 2336 -365 -686 13 7

ATOM 1164 OEl GLU 156 -0.220 18.241 38.024 1.000 19.17

ANISOU 1164 OEl GLU 156 1429 2973 2884 -632 -270 2 53

ATOM 1165 OE2 GLU 156 0.136 18.198 35.858 1.000 22.03

ANISOU 1165 OE2 GLU 156 2449 3269 ^' 2653 -243 -721 924

ATOM 1166 C GLU 156 2.961 18.942 40.677 1.000 9 .21

ANISOU 1166 C GLU 156 1166 1135 1197 -26 239 1 8 3

ATOM 1167 O GLU 156 2.828 17.997 41.476 1.000 11.22

ANISOU 1167 O GLU 156 1631 1199 1434 103 162 43 1

ATOM 1168 N PRO 157 3.337 20.158 41.118 1.000 10.29

ANISOU 1168 N PRO 157 1329 1201 1381 -109 21 12 3

ATOM 1169 CD PRO 157 3.527 21.407 40.359 1.000 10.17

ANISOU 1169 CD PRO 157 1381 1093 1391 -40 -30 2 1

ATOM 1170 CA PRO 157 3.618 20.363 42.553 1.000 10.28

ANISOU 1170 CA PRO 157 1160 1354 1391 -12 -61 6 4

ATOM 1171 CB PRO 157 4.173 21.805 42.590 1.000 12.44

ANISOU 1171 CB PRO 157 1832 1567 1330 -397 20 5 8

ATOM 1172 CG PRO 157 3.475 22.471 41.429 1.000 10.44

ANISOU 1172 CG PRO 157 1469 1259 1237 -388 166 - 15

ATOM 1173 C PRO 157 2.387 20.269 43.450 1.000 10.83

ANISOU 1173 C PRO 157 1206 1554 1357 -89 -61 7 6

ATOM 1174 O PRO 157 1.247 20.422 42.992 1.000 11.38

ANISOU 1174 O PRO 157 1157 1742 1426 -93 -64 3 3

ATOM 1175 N LEU 158 2.561 19.988 44.742 1.000 9 .91

ANISOU 1175 N LEU 158 1011 1308 1447 -86 -53 15 1

ATOM 1176 CA LEU 158 1.524 19.940 45.764 1.000 10.85

ANISOU 1176 CA LEU 158 1319 1461 1344 -387 -2 - 3

ATOM 1177 CB LEU 158 1.152 18.482 46.078 1.000 11.03

ANISOU 1177 CB LEU 158 1280 1447 1464 -251 99 9 3

ATOM 1178 CG LEU 158 0.111 18.239 47.155 1.000 12.01

ANISOU 1178 CG LEU 158 1271 1497 1795 -303 241 12 8

ATOM 1179 CDI LEU 158 -1.212 18.826 46.736 1.000 16.21

ANISOU 1179 CDI LEU 158 1224 2249 2685 -111 41 - 239

ATOM 1180 CD2 LEU 158 -0.086 16.736 47.397 1.000 17.17

ANISOU 1180 CD2 LEU 158 2656 1542 2325 -254 1273 174

ATOM 1181 C LEU 158 1.997 20.626 47.048 1.000 11.22

ANISOU 1181 C LEU 158 1496 1366 1402 110 -304 5

ATOM 1182 O LEU 158 3.056 20.201 47.539 1.000 11.28

ANISOU 1182 O LEU 158 1283 1368 1635 20 -262 7 5

ATOM 1183 N LEU 159 1.234 21.599 47.548 1.000 10.86

ANISOU 1183 N LEU 159 1103 1744 1278 68 -180 - 7 0

ATOM 1184 CA LEU 159 1.540 22.278 48.797 1.000 11.62

ANISOU 1184 CA LEU 159 1247 1761 1407 -59 -68 - 180

ATOM 1185 CB LEU 159 1.494 23.802 48.640 1.000 12.44

ANISOU 1185 CB LEU 159 1624 1747 1354 -209 -73 - 3 3

ATOM 1186 CG LEU 159 1.633 24.635 49.934 1.000 12.83

ANISOU 1186 CG LEU 159 1600 1698 1576 246 -54 - 215

ATOM 1187 CD . LEU 159 2.947 24.435 50.651 1.000 14.28

ANISOU 1187 CDI . LEU 159 2019 2250 1158 177 -292 1 04

ATOM 1188 CΌ: ^> LEU 159 1.442 26.134 49.640 1.000 13 .33

ANISOU ^' 1188 CΌ: - LEU 159 1802 1721 1543 87 -87 - 2 0

ATOM 1189 c LEU 159 0.537 21.846 49.868 1.000 11.24

ANISOUf 1189 c LEU 159 1393 1474 1404 -174 -9 - 271

ATOM 1190 0 LEU 159 -0.665 21.940 49.620 1.000 13 .70 ANISOU 1190 O LEU 159 1354 2395 1457 -328 34 - 269

ATOM 1191 N ARG 160 1.013 21.385 51.010 1.000 14.59

ANISOU 1191 N ARG 160 1737 2569 1239 -390 -128 - 224

ATOM 1192 CA ARG 160 0.158 21.030 52.153 1.000 13 .94

ANISOU 1192 CA ARG 160 1265 2631 1402 157 -137 9 2

ATOM 1193 CB ARG 160 0.161 19.528 52.343 1.000 18.20

ANISOU 1193 CB ARG 160 1932 2645 2338 -301 32 1 93

ATOM 1194 CG ARG 160 -0.423 18.661 51.252 1.000 25.12

ANISOU 1194 CG ARG 160 3451 2902 3191 -653 -787 2 3

ATOM 1195 CD ARG 160 -0.765 17.301 51.831 1.000 31.98

ANISOU 1195 CD ARG 160 4825 3598 3729 -1994 -905 3 2 1

ATOM 1196 NE ARG 160 -1.284 16.322 50.896 1.000 26.15

ANISOU 1196 NE ARG 160 3392 2957 3587 -739 -1056 3 10

ATOM 1197 CZ ARG 160 -0.970 15.044 50.779 1.000 25.30

ANISOU 1197 CZ ARG 160 3195 3390 3028 94 -785 2 9 5

ATOM 1198 NHl ARG 160 -0.063 14.433 51.552 1.000 31.26

ANISOU 1198 NHl ARG 160 3654 4142 4080 -629 -1089 2054

ATOM 1199 NH2 ARG 160 -1.572 14.308 49.850 1.000 28.82

ANISOU 1199 NH2 ARG 160 4020 3122 3807 -13 -966 - 9 0

ATOM 1200 C ARG 160 0.649 21.669 53.447 1.000 15.12

ANISOU 1200 C ARG 160 1649 2863 1232 104 -66 12 5

ATOM 1201 O ARG 160 1.804 21.556 53.863 1.000 17.09

ANISOU 1201 O ARG 160 1291 3411 1791 -400 74 - 812

ATOM 1202 N PHE 161 -0.258 22.369 54.114 1.000 14.95

ANISOU 1202 N PHE 161 1512 2506 1660 -253 -8 - 146

ATOM 1203 CA PHE 161 -0.036 22.949 55.427 1.000 13 .27

ANISOU 1203 CA PHE 161 1600 1681 1760 -9 -249 - 41

ATOM 1204 CB PHE 161 -0.587 24.381 55.472 1.000 16.82

ANISOU 1204 CB PHE 161 1594 1947 2851 384 58 6 4

ATOM 1205 CG PHE 161 -0.317 25.109 56.771 1.000 22.56

ANISOU 1205 CG PHE 161 2464 2424 3684 -39 790 -1067

ATOM 1206 CDI PHE 161 -1.175 25.010 57.849 1.000 26.03

ANISOU 1206 CDI PHE 161 3353 2919 3620 267 1106 - 702

ATOM 1207 CD2 PHE 161 0.822 25.901 56.885 1.000 25.34

ANISOU 1207 CD2 PHE 161 2353 3265 4011 -179 -161 - 738

ATOM 1208 CEl PHE 161 -0.943 25.660 59.051 1.000 30.50

ANISOU 1208 CEl PHE 161 4784 3324 3481 -972 1456 - 620

ATOM 1209 CE2 PHE 161 1.061 26.553 58.080 1.000 26.10

ANISOU 1209 CE2 PHE 161 2546 3067 4302 -129 281 -1127

ATOM 1210 CZ PHE 161 0.199 26.438 59.164 1.000 30.06

ANISOU 1210 CZ PHE 161 3839 3197 4386 -152 774 - 677

ATOM 1211 C PHE 161 -0.737 22.073 56.447 1.000 13.93

ANISOU 1211 C PHE 161 1842 1946 1503 -334 -277 - 240

ATOM 1212 O PHE 161 -1.916 21.843 56.270 1.000 18.26

ANISOU 1212 O PHE 161 2000 3277 1662 -744 -399 475

ATOM 1213 N ARG 162 -0.090 21.631 57.503 1.000 16.29

ANISOU 1213 N ARG 162 2063 2516 1610 -937 -523 7 7

ATOM 1214 CA ARG 162 -0.635 20.719 58.483 1.000 15.62

ANISOU 1214 CA ARG 162 1772 2512 1650 -519 -266 7 6

ATOM 1215 C ARG 162 -0.476 21.312 59.890 1.000 17.48

ANISOU 1215 C ARG 162 1855 3131 1656 -603 -186 - 7 6

ATOM 1216 O ARG 162 0.609 21.734 60.251 1.000 17.23

ANISOU 1216 O ARG 162 1928 3063 1557 -771 -42 - 160

ATOM 1217 CB ARG 162 0.081 19.374 58.458 1.000 21.99

ANISOU 1217 CB ARG 162 3309 2318 2727 -272 -737 - 22

ATOM 1218 CG ARG 162 -0.573 18.322 59.348 1.000 26.07

ANISOU 1218 CG ARG 162 3488 2375 4041 489 655 2 8 0

ATOM 1219 CD ARG 162 -0.231 16.896 58.886 1.000 25.85

ANISOU ^' 1219 CD ARG 162 3106 2221 4495 418 -2 2 3 9

ATOM 1220 NE ARG 162 -0.943 15.916 59.698 1.000 28.83

ANISOU ^• 1220 NE ARG 162 4379 2437 4139 -181 332 - 177 ATOM 1221 CZ ARG 162 -0.642 14.638 59.879 1.000 27.99

ANISOU 1221 CZ ARG 162 4271 2497 3868 -179 962 8 4

ATOM 1222 NHl ARG 162 0.429 14.119 59.273 1.000 26.61

ANISOU 1222 NHl ARG 162 3200 3167 3742 -91 -126 - 268

ATOM 1223 NH2 ARG 162 -1.408 13.883 60.658 1.000 34.20

ANISOU 1223 NH2 ARG 162 3807 3522 5663 -986 702 78 0

ATOM 1224 N TYR 163 -1.570 21.296 60.622 1.000 16.77

ANISOU 1224 N TYR 163 1803 2865 1705 -484 -194 8 4

ATOM 1225 CA TYR 163 -1.627 21.749 61.997 1.000 16.73

ANISOU 1225 CA TYR 163 1819 2770 1766 -692 -51 4 0

ATOM 1226 CB TYR 163 -2.712 22.804 62.116 1.000 18.99

ANISOU 1226 CB TYR 163 2479 2560 2175 -427 -303 - 214

ATOM 1227 CG TYR 163 -3.173 23.206 63.488 1.000 23 .52

ANISOU 1227 CG TYR 163 2573 3821 2544 -16 -335 - 868

ATOM 1228 CDI TYR 163 -2.316 23.848 64.367 1.000 31.80

ANISOU 1228 CDI TYR 163 3613 5005 3466 -1151 304 - 2338

ATOM 1229 CEl TYR 163 -2.731 24.222 65.625 1.000 40.74

ANISOU 1229 CEl TYR 163 5855 5676 3950 -1906 976 - 3116

ATOM 1230 CD2 TYR 163 -4.459 22.965 63.931 1.000 32.55

ANISOU 1230 CD2 TYR 163 3307 5654 3408 -1066 639 -2340

ATOM 1231 CE2 TYR 163 -4.902 23.332 65.189 1.000 42.99

ANISOU 1231 CE2 TYR 163 5626 6630 4080 -2352 1989 -2949

ATOM 1232 CZ TYR 163 -4.017 23.960 66.025 1.000 42.52

ANISOU 1232 CZ TYR 163 6281 5799 4075 -1721 1943 - 3714

ATOM 1233 OH TYR 163 -4.380 24.351 67.274 1.000 48.87

ANISOU 1233 OH TYR 163 8167 6831 3569 -269 1801 - 3052

ATOM 1234 C TYR 163 -1.935 20.551 62.896 1.000 17.90

ANISOU 1234 C TYR 163 2872 2353 1575 -894 -465 - 173

ATOM 1235 O TYR 163 -2.933 19.858 62.653 1.000 18.12

ANISOU 1235 O TYR 163 2694 2130 2060 -732 -615 6 7

ATOM 1236 N PHE 164 -1.112 20.326 63.898 1.000 18.32

ANISOU 1236 N PHE 164 2516 2621 1826 -614 -402 - 9 0

ATOM 1237 CA PHE 164 -1.340 19.381 64.984 1.000 23.44

ANISOU 1237 CA PHE 164 4176 2692 2038 -727 -669 2 19 ATOM 1238 CB PHE 164 -0.073 18.617 65.327 1.000 26.02

ANISOU 1238 CB PHE 164 4594 2824 2470 -459 -822 3 7 9

ATOM 1239 CG PHE 164 0.407 17.669 64.231 1.000 29.00

ANISOU 1239 CG PHE 164 4118 3639 3263 -518 -427 - 254

ATOM 1240 CDI PHE 164 1.224 18.118 63.205 1.000 27.11

ANISOU 1240 CDI PHE 164 3040 4013 3249 -198 -821 4

ATOM 1241 CD2 PHE 164 0.051 16.332 64.240 1.000 28.37

ANISOU 1241 CD2 PHE 164 3935 3139 3704 472 30 - 64

ATOM 1242 CEl PHE 164 1.657 17.248 62.223 1.000 28.13

ANISOU 1242 CEl PHE 164 2730 3926 4034 -43 -229 6

ATOM 1243 CE2 PHE 164 0.459 15.464 63.250 1.000 31.71

ANISOU 1243 CE2 PHE 164 4719 3694 3635 -293 657 - 383

ATOM 1244 CZ PHE 164 1.276 15.924 62.234 1.000 30.26

ANISOU 1244 CZ PHE 164 3827 3808 3862 0 300 12 6

ATOM 1245 C PHE 164 -1.775 20.160 66.228 1.000 24.65

ANISOU 1245 C PHE 164 3541 4049 1777 -1025 -455 3 7

ATOM 1246 O PHE 164 -0.889 20.713 66.885 1.000 25.54

ANISOU 1246 O PHE 164 3520 4167 2019 -921 -440 - 257

ATOM 1247 N PRO 165 -3.058 20.293 66.527 1.000 32 .24

ANISOU 1247 N PRO 165 3641 5095 3513 -1894 266 - 680

ATOM 1248 CA PRO 165 -3.486 21.012 67.720 1.000 32.98

ANISOU 1248 CA PRO 165 3570 5737 3225 -1271 397 - 322

ATOM 1249 C PRO 165 -2.854 20.429 68.986 1.000 38.48

ANISOU 1249 C PRO 165 4355 6808 3457 -1872 40 3 4 3

ATOM 1250 O PRO 165 -2.551 19.230 69.034 1.000 53 .87

ANISOU ^' 1250 O PRO 165 9948 7012 3507 -959 692 1750

ATOM 1251 CB PRO 165 -5.001 20.820 67.769 1.000 37.76 ANISOU 1251 CB PRO 165 3640 6479 4227 -1488 380 - 717

ATOM 1252 CG PRO 165 -5.417 20.048 66.569 1.000 36.16

ANISOU 1252 CG PRO 165 3341 6449 3948 -518 -349 - 398

ATOM 1253 CD PRO 165 -4.197 19.816 65.734 1.000 35.70

ANISOU 1253 CD PRO 165 3440 6296 3828 -1656 -5 - 604

ATOM 1254 N LEU 178 4.459 8.087 66.987 1.000 36.23

ANISOU 1254 N LEU 178 4509 3338 5918 -26 1216 1175

ATOM 1255 CA LEU 178 4.994 9.117 66.116 1.000 28.63

ANISOU 1255 CA LEU 178 3397 3170 4312 377 1344 4 0 1

ATOM 1256 CB LEU 178 5.882 8.534 65.027 1.000 30.08

ANISOU 1256 CB LEU 178 3497 3245 4688 760 752 - 620

ATOM 1257 CG LEU 178 7.245 7.948 65.348 1.000 29.43

ANISOU 1257 CG LEU 178 3557 2950 4674 667 371 - 979

ATOM 1258 CDI LEU 178 7.859 7.367 64.073 1.000 32.13

ANISOU 1258 CDI LEU 178 2972 4524 4713 586 810 - 790

ATOM 1259 CD2 LEU 178 8.208 8.964 65.937 1.000 41.71

ANISOU 1259 CD2 LEU 178 5303 3695 6850 356 -1656 - 1154

ATOM 1260 C LEU 178 3.885 9.909 65.420 1.000 27.18

ANISOU 1260 C LEU 178 2107 3534 4686 -175 1776 83 3

ATOM 1261 O LEU 178 2.845 9.351 65.086 1.000 39.60

ANISOU 1261 O LEU 178 2407 4624 8016 -1253 1290 2183

ATOM 1262 N ARG 179 4.128 11.200 65.160 1.000 25.65

ANISOU 1262 N ARG 179 2220 3437 4089 -216 878 74 1

ATOM 1263 CA ARG 179 3.231 11.973 64.321 1.000 25.04

ANISOU 1263 CA ARG 179 1860 3289 4365 69 641 1 5

ATOM 1264 C ARG 179 3.297 11.572 62.852 1.000 24.51

ANISOU 1264 C ARG 179 2158 2721 4434 39 99 - 89

ATOM 1265 O ARG 179 2.295 11.687 62.139 1.000 28.60

ANISOU 1265 O ARG 179 2545 3242 5079 441 -332 - 256

ATOM 1266 CB ARG 179 3.517 13.480 64.451 1.000 28.58

ANISOU 1266 CB ARG 179 3980 3317 3561 -110 -843 5 7

ATOM 1267 CG ARG 179 2.936 14.092 65.724 1.000 30.01

ANISOU 1267 CG ARG 179 3817 3725 3862 57 -957 - 372

ATOM 1268 CD ARG 179 3.307 15.570 65.757 1.000 31.51

ANISOU 1268 CD ARG 179 4457 3675 3840 90 -1514 - 338

ATOM 1269 NE ARG 179 2.925 16.126 67.058 1.000 37.82

ANISOU 1269 NE ARG 179 7035 3190 4144 153 -310 - 15

ATOM 1270 CZ ARG 179 2.897 17.425 67.292 1.000 39.43

ANISOU 1270 CZ ARG 179 8420 3029 3532 -479 580 400

ATOM 1271 NHl ARG 179 3.213 18.286 66.331 1.000 59.73

ANISOU 1271 NHl ARG 179 11745 4676 6273 -1045 3177 1722

ATOM 1272 NH2 ARG 179 2.548 17.896 68.457 1.000 33.13

ANISOU 1272 NH2 ARG 179 5661 3832 3094 275 -1463 - 173

ATOM 1273 N MET 180 4.455 11.099 62.424 1.000 21.43

ANISOU 1273 N MET 180 2013 2457 3674 -395 108 - 222

ATOM 1274 CA MET 180 4.695 10.539 61.108 1.000 20.07

ANISOU 1274 CA MET 180 2346 1965 3315 -349 -300 1 5 1

ATOM 1275 C MET 180 5.802 9.482 61.182 1.000 17.33

ANISOU 1275 C MET 180 2251 2080 2254 -332 -86 3 3 7

ATOM 1276 O MET 180 6.894 9.757 61.677 1.000 18.52

ANISOU 1276 O MET 180 2237 2019 2781 -398 -79 5 2

ATOM 1277 CB MET 180 5.041 11.646 60.136 1.000 22.64

ANISOU 1277 CB MET 180 2571 2321 3709 -197 -549 6 8 3

ATOM 1278 CG MET 180 5.065 11.367 58.678 1.000 27.90

ANISOU 1278 CG MET 180 3918 3095 3588 -453 -654 9 13

ATOM 1279 SD MET 180 4.945 12.838 57.629 1.000 25.01

ANISOU 1279 SD MET 180 2936 2942 3626 -399 124 8 5 1

ATOM 1280 CE MET 180 4.385 12.010 56.147 1.000 37.00

ANISOU 1280 CE MET 180 5917 3450 4690 -258 -2680 1204

ATOM 1281 N ALA 181 5.467 8.295 60.680 1.000 16.99

ANISOU 1281 N ALA 181 2144 2139 2174 -90 -558 2 9 9 ATOM 1282 CA ALA 181 6.396 7.168 60.676 1.000 16.12

ANISOU 1282 CA ALA 181 2275 1958 1890 -171 -343 6 02

ATOM 1283 CB ALA 181 5.668 5.891 60.279 1.000 20.24

ANISOU 1283 CB ALA 181 2857 2158 2673 -648 694 1 0 6

ATOM 1284 C ALA 181 7.576 7.409 59.738 1.000 15.43

ANISOU 1284 C ALA 181 2223 1717 1925 -315 -369 4 3 2

ATOM 1285 0 ALA 181 7.458 8.198 58.783 1.000 15.49

ANISOU 1285 0 ALA 181 2268 1761 1858 -173 -296 43 4

ATOM 1286 N PRO 182 8.698 6.733 59.986 1.000 16.03

ANISOU 1286 N PRO 182 2517 1745 1829 32 -78 5 3 1

ATOM 1287 CD PRO 182 8.983 5.802 61.101 1.000 19.61

ANISOU 1287 CD PRO 182 2321 2908 2221 -210 -306 1240

ATOM 1288 CA PRO 182 9.865 6.907 59.076 1.000 14.78

ANISOU 1288 CA PRO 182 2573 1336 1706 -101 -86 2 9 9

ATOM 1289 CB PRO 182 10.914 5.948 59.649 1.000 16.20

ANISOU 1289 CB PRO 182 2570 1978 1607 170 -251 7 7

ATOM 1290 CG PRO 182 10.479 5.713 61.066 1.000 19.28

ANISOU 1290 CG PRO 182 2301 3071 1952 -199 -245 1001

ATOM 1291 C PRO 182 9.541 6.571 57.627 1.000 14.90

ANISOU 1291 C PRO 182 2230 1658 1772 -421 -262 3 40

ATOM 1292 0 PRO 182 8.920 5.573 57.249 1.000 15.38

ANISOU 1292 0 PRO 182 2301 1587 1957 -467 -482 53 9

ATOM 1293 N HIS 183 9.969 7.460 56.730 1.000 12 .28

ANISOU 1293 N HIS 183 1737 1312 1617 -154 -284 15 6

ATOM 1294 CA HIS 183 9.733 7.354 55.300 1.000 11.90

ANISOU 1294 CA HIS 183 1413 1495 1614 -254 -351 3 5

ATOM 1295 CB HIS 183 8.300 7.824 54.922 1.000 12 .43

ANISOU 1295 CB HIS 183 1399 1368 1957 -128 -241 112

ATOM 1296 CG HIS 183 8.168 9.314 55.089 1.000 11.36

ANISOU 1296 CG HIS 183 1349 1369 1600 -367 -296 5 6

ATOM 1297 CD2 HIS 183 8.259 10.374 54.249 1.000 12.03

ANISOU 1297 CD2 HIS 183 1684 1296 1589 -43 157 - 1 0

ATOM 1298 NDl HIS 183 7.989 9.858 56.339 1.000 13 .27

ANISOU 1298 NDl HIS 183 1901 1439 1700 -65 267 193

ATOM 1299 CEl HIS 183 7.943 11.187 56.244 1.000 12.43

ANISOU 1299 CEl HIS 183 1939 1490 1296 77 -244 15 0

ATOM 1300 NE2 HIS 183 8.101 11.515 54.992 1.000 11.04

ANISOU 1300 NE2 HIS 183 1560 1437 1199 215 -232 4 8

ATOM 1301 C HIS 183 10.749 8.176 54.515 1.000 12.27

ANISOU 1301 C HIS 183 1446 1639 1577 -303 -282 - 67

ATOM 1302 O HIS 183 11.433 9.032 55.064 1.000 12.94

ANISOU 1302 O HIS 183 1496 1915 1505 -558 -292 1 5

ATOM 1303 N TYR 184 10.849 7.907 53.215 1.000 10.61

ANISOU 1303 N TYR 184 1453 1027 1552 -41 -380 110

ATOM 1304 CA TYR 184 11.483 8.800 52.256 1.000 11.36

ANISOU 1304 CA TYR 184 1475 1104 1738 -71 -264 17 8

ATOM 1305 CB TYR 184 12.628 8.151 51.481 1.000 11.79

ANISOU 1305 CB TYR 184 1631 1114 1734 -62 -197 3 4

ATOM 1306 CG TYR 184 12.368 6.907 50.677 1.000 11.29

ANISOU 1306 CG TYR 184 1680 921 1688 225 -893 174

ATOM 1307 CDI TYR 184 12.156 5.659 51.268 1.000 11.76

ANISOU 1307 CDI TYR 184 1663 927 1879 388 -487 19 0

ATOM 1308 CEl . TYR 184 11.911 4.526 50.492 1.000 12.64

ANISOU 1308 CEl , TYR 184 1960 878 1964 173 -40 182

ATOM 1309 CD2 TYR 184 12.333 6.949 49.279 1.000 11.13

ANISOU 1309 CD2 : TYR 184 1252 1302 1674 109 -283 9 3

ATOM 1310 CE2 : TYR 184 12.102 5.834 48.502 1.000 12.93

ANISOU ^' 1310 CE2 ! TYR 184 1944 1422 1546 49 -384 7 3

ATOM 1311 CZ TYR 184 11.898 4.611 49.121 1.000 13 .14

ANISOUf 1311 CZ TYR 184 1717 1304 1972 30 -611 6 7

ATOM 1312 OH TYR 184 11.663 3.490 48.343 1.000 15.45 ANISOU 1312 OH TYR 184 2028 1471 2373 42 -476 - 247

ATOM 1313 C TYR 184 10.447 9.390 51.314 1.000 11.50

ANISOU 1313 C TYR 184 1445 1215 1709 -187 -201 3 4

ATOM 1314 0 TYR 184 9.362 8.797 51.089 1.000 11.75

ANISOU 1314 0 TYR 184 1305 1308 1853 -106 -171 42

ATOM 1315 N ASP 185 10.784 10.557 50.743 1.000 10.79

ANISOU 1315 N ASP 185 1581 1069 1449 -141 -132 11

ATOM 1316 CA ASP 185 9.861 11.218 49.815 1.000 9 . 10

ANISOU 1316 CA ASP 185 1089 1093 1277 -326 23 2 0 6

ATOM 1317 CB ASP 185 9.934 12.743 49.886 1.000 10.13

ANISOU 1317 CB ASP 185 1427 1095 1327 -298 -178 17

ATOM 1318 CG ASP 185 9.540 13.388 51.185 1.000 11.79

ANISOU 1318 CG ASP 185 1797 1350 1333 -250 -149 1 1

ATOM 1319 ODl ASP 185 9.681 14.638 51.278 1.000 13 .79

ANISOU 1319 ODl ASP 185 2050 1316 1875 135 -52 - 2

ATOM 1320 OD2 ASP 185 9.114 12.755 52.189 1.000 13 .31

ANISOU 1320 OD2 ASP 185 1805 1848 1405 -411 -63 1 0

ATOM 1321 C ASP 185 10.098 10.759 48.371 1.000 9 .44

ANISOU 1321 C ASP 185 1036 1150 1401 -309 -26 1 0

ATOM 1322 O ASP 185 11.234 10.469 48.005 1.000 10.64

ANISOU 1322 O ASP 185 1167 1376 1500 -127 -35 - 2 06

ATOM 1323 N LEU 186 9.038 10.684 47.568 1.000 10.09

ANISOU 1323 N LEU 186 1211 1186 1437 -272 -177 - 5

ATOM 1324 CA LEU 186 9.124 10.312 46.161 1.000 10.60

ANISOU 1324 CA LEU 186 1641 986 1401 -239 -52 , - 44

ATOM 1325 CB LEU 186 8.030 9.295 45.798 1.000 11.32

ANISOU 1325 CB LEU 186 1652 929 1721 -111 17 - 479

ATOM 1326 CG LEU 186 7.989 7.977 46.602 1.000 12.60

ANISOU 1326 CG LEU 186 1408 1039 2340 -263 -200 - 1 66

ATOM 1327 CDI LEU 186 6.896 7.064 46.028 1.000 16.64

ANISOU 1327 CDI LEU 186 1900 1373 3049 -634 -398 - 1 35

ATOM 1328 CD2 LEU 186 9.356 7.332 46.629 1.000 13 .84

ANISOU 1328 CD2 LEU 186 1438 1245 2575 -155 443 2 8

ATOM 1329 C LEU 186 9.024 11.521 45.223 1.000 10.90

ANISOU 1329 C LEU 186 1327 1211 1603 -3 -451 164

ATOM 1330 O LEU 186 8.768 11.406 44.031 1.000 13 .60

ANISOU 1330 O LEU 186 2067 1608 1494 -211 -321 1 0

ATOM 1331 N SER 187 9.264 12.705 45.734 1.000 10.71

ANISOU 1331 N SER 187 1546 1129 1393 -76 -282 3 1

ATOM 1332 CA SER 187 9.401 13.943 44.998 1.000 10.49

ANISOU 1332 CA SER 187 1427 1191 1370 195 -107 4 8

ATOM 1333 CB SER 187 9.221 15.103 46.002 1.000 10.56

ANISOU 1333 CB SER 187 1105 1048 1857 298 161 5 3

ATOM 1334 OG SER 187 10.430 14.918 46.726 1.000 13 .01

ANISOU 1334 OG SER 187 1343 1432 2169 -132 -295 2 0

ATOM 1335 C SER 187 10.774 14.062 44.336 1.000 10.47

ANISOU 1335 C SER 187 1447 862 1669 135 -3 145

ATOM 1336 O SER 187 11.684 13.246 44.513 1.000 10.54

ANISOU 1336 O SER 187 1577 799 1629 183 -91 - 7 7

ATOM 1337 N MET 188 10.962 15.095 43.502 1.000 9 .78

ANISOU 1337 N MET 188 1419 978 1318 147 44 7 4

ATOM 1338 CA MET 188 12.267 15.584 43.065 1.000 9 . 94

ANISOU 1338 CA MET 188 1394 942 1441 182 58 3 7

ATOM 1339 CB MET 188 12.128 16.543 41.891 1.000 10.89

ANISOU 1339 CB MET 188 1523 840 1774 98 48 2 2 : 7

ATOM 1340 CG MET 188 13.385 17.258 41.470 1.000 11.40

ANISOU 1340 CG MET 188 1403 1172 1756 46 -51 2 14

ATOM 1341 SD MET 188 14.687 16.134 40.891 1.000 12.71

ANISOU 1341 SD MET 188 1619 1272 1940 139 137 1 £

ATOM 1342 CE MET 188 16.061 17.267 40.790 1.000 ' 13.86

ANISOU ^' 1342 CE MET 188 1862 1399 2003 -2 911 - 9 0 ATOM 1343 C MET 188 12.946 16.217 44.291 1.000 12.13

ANISOU 1343 c MET 188 1325 1586 1698 169 -18 - 285

ATOM 1344 0 MET 188 13.971 15.727 44.804 1.000 11.52

ANISOU- 1344 0 MET 188 1288 1553 1535 144 132 8 7

ATOM 1345 N VAL 189 12.362 17.290 44.838 1.000 10.00

ANISOU 1345 N VAL 189 1290 1217 1292 53 -175 6

ATOM 1346 CA VAL 189 12.745 17.894 46.099 1.000 9 . 70

ANISOU 1346 CA VAL 189 1209 1057 1420 -212 -45 - 1 9

ATOM 1347 CB VAL 189 13.618 19.154 45.979 1.000 9 . 97

ANISOU 1347 CB VAL 189 1288 1103 1398 -238 129 1 8 9

ATOM 1348 CGI VAL 189 14.953 18.837 45.266 1.000 13 .45

ANISOU 1348 CGI VAL 189 1334 1410 2368 -236 390 143

ATOM 1349 CG2 VAL 189 12.899 20.289 45.264 1.000 12 .24

ANISOU 1349 CG2 VAL 189 1715 1242 1693 -25 150 2 9 5

ATOM 1350 C VAL 189 11.469 18.245 46.871 1.000 10.10

ANISOU 1350 C VAL 189 1089 1600 1149 -456 -156 - 7 3

ATOM 1351 O VAL 189 10.405 18.399 46.250 1.000 9 . 53

ANISOU 1351 O VAL 189 1153 1249 1217 -222 -190 8

ATOM 1352 N THR 190 11.609 18.327 48.187 1.000 8 . 66

ANISOU 1352 N THR 190 1273 894 1123 15 -202 12 7

ATOM 1353 CA THR 190 10.565 18.771 49.091 1.000 9.64

ANISOU 1353 CA THR 190 1350 1167 1147 -11 -228 - 9 9

ATOM 1354 CB THR 190 10.194 17.699 50.132 1.000 10.69

ANISOU 1354 CB THR 190 1231 1196 1635 -300 121 - 54

ATOM 1355 OGl THR 190 9.662 16.586 49.501 1.000 12.45

ANISOU 1355 OGl THR 190 1333 1341 2055 -140 -258 - 48

ATOM 1356 CG2 THR 190 9.038 18.131 51.019 1.000 13.59

ANISOU 1356 CG2 THR 190 1121 2222 1821 -272 151 - 195

ATOM 1357 C THR 190 11.058 19.976 49.891 1.000 9 .23

ANISOU 1357 C THR 190 1257 1096 1152 -102 -336 - 49

ATOM 1358 O THR 190 12.149 19.867 50.447 1.000 10.54

ANISOU 1358 O THR 190 1322 1292 1390 -5 -359 - 122

ATOM 1359 N LEU 191 10.313 21.064 49.978 1.000 10.23

ANISOU 1359 N LEU 191 1319 1167 1401 -71 -177 - 133

ATOM 1360 CA LEU 191 10.691 22.241 50.770 1.000 10.19

ANISOU 1360 CA LEU 191 1259 1176 1438 0 -294 - 142

ATOM 1361 CB LEU 191 10.604 23.511 49.910 1.000 11.52

ANISOU 1361 CB LEU 191 1203 1185 1990 -118 -601 3 2

ATOM 1362 CG LEU 191 11.897 23.898 49.167 1.000 13.23

ANISOU 1362 CG LEU 191 1898 1710 1419 -391 -358 9 7

ATOM 1363 CDI LEU 191 12.333 22.794 48.218 1.000 15.25

ANISOU 1363 CDI LEU 191 1685 2018 2091 -476 -214 - 305

ATOM 1364 CD2 LEU 191 11.717 25.231 48.448 1.000 17.46

ANISOU 1364 CD2 LEU 191 2310 2044 2281 -14 17 604

ATOM 1365 C LEU 191 9.798 22.328 52.006 1.000 11.93

ANISOU 1365 C LEU 191 1275 1677 1579 56 -190 - 372

ATOM 1366 O LEU 191 8.560 22.262 51.868 1.000 13 .49

ANISOU 1366 O LEU 191 1276 2173 1676 1 -192 - 601

ATOM 1367 N ILE 192 10.394 22.483 53.190 1.000 11.06

ANISOU 1367 N ILE 192 1115 1603 1487 -111 -92 - 108

ATOM 1368 CA ILE 192 9.671 22.539 54.443 1.000 11.13

ANISOU 1368 CA ILE 192 1071 1638 1521 11 -173 - 149

ATOM 1369 CB ILE 192 9.927 21.304 55.330 1.000 12.94

ANISOU 1369 CB ILE 192 2099 1586 1232 -65 -9 - 233

ATOM 1370 CG2 ILE 192 9.221 21.428 56.673 1.000 16.06

ANISOU 1370 CG2 ILE 192 2479 1983 1641 -206 426 -215

ATOM 1371 CGI , ILE 192 9.512 20.028 54.590 1.000 15.51

ANISOU 1371 CGI . ILE 192 2633 1658 1601 -400 -48 - 175

ATOM 1372 CDI . ILE 192 9.845 18.765 55.339 1.000 25.71

ANISOU ^' 1372 CDI . ILE 192 5869 1608 2290 -175 -1566 - 301

ATOM 1373 C ILE 192 9.966 23.809 55.253 1.000 11.47

SUBSTΓΓUTE SHEET (RULE 26) ANISOU 1373 C ILE 192 1330 1603 1427 -4 -222 - 122

ATOM 1374 0 ILE 192 11.123 24.106 55.567 1.000 13 .33

ANISOU 1374 0 ILE 192 1344 1738 1981 -96 -289 - 219

ATOM 1375 N GLN 193 8.904 24.525 55.602 1.000 15.78

ANISOU 1375 N GLN 193 1316 2462 2219 -64 -5 - 975

ATOM 1376 CA GLN 193 8.987 25.653 56.533 1.000 14.56

ANISOU 1376 CA GLN 193 1582 1858 2091 212 -304 - 529

ATOM 1377 CB GLN 193 8.449 26.975 56.020 1.000 20.03

ANISOU 1377 CB GLN 193 2226 2203 3180 318 -329 142

ATOM 1378 CG GLN 193 9.203 27.684 54.914 1.000 23 .86

ANISOU 1378 CG GLN 193 3399 2492 3174 313 45 2 8 0

ATOM 1379 CD GLN 193 8.665 ^' 29.079 54.675 1.000 22.92

ANISOU 1379 CD GLN 193 3250 2363 3097 78 -477 2 0 5

ATOM 1380 OEl GLN 193 7.603 29.292 54.099 1.000 27.68

ANISOU 1380 OEl GLN 193 4175 3310 3031 552 -1214 2 9

ATOM 1381 NE2 GLN 193 9.411 30.075 55.134 1.000 27.01

ANISOU 1381 NE2 GLN 193 3187 2667 4408 -440 124 1 7

ATOM 1382 C GLN 193 8.216 25.265 57.804 1.000 15.14

ANISOU 1382 C GLN 193 1945 1827 1982 136 -174 - 722

ATOM 1383 O GLN 193 7.147 24.662 57.714 1.000 27.80

ANISOU 1383 O GLN 193 2523 6225 1817 -1586 -592 2 3 5

ATOM 1384 N GLN 194 8.714 25.552 58.978 1.000 19.80

ANISOU 1384 N GLN 194 2994 2502 2025 -632 -752 3 3

ATOM 1385 CA GLN 194 8.100 25.080 60.213 1.000 22.89

ANISOU 1385 CA GLN 194 3961 2626 2110 493 -20 5 2

ATOM 1386 C GLN 194 7.763 26.236 61.141 1.000 27.79

ANISOU 1386 C GLN 194 4886 2757 2916 823 25 - 262

ATOM 1387 O GLN 194 8.424 27.258 60.983 1.000 30.03

ANISOU 1387 O GLN 194 4727 3168 3516 368 -259 - 910

ATOM 1388 CB GLN 194 9.086 24.170 60.950 1.000 23 .97

ANISOU 1388 CB GLN 194 3952 3133 2021 846 483 3 52

ATOM 1389 CG GLN 194 9.398 22.835 60.314 1.000 21.94

ANISOU 1389 CG GLN 194 2740 3238 2358 683 -182 - 10

ATOM 1390 CD GLN 194 10.546 22.148 61.052 1.000 20.51

ANISOU 1390 CD GLN 194 2450 3433 1911 509 -321 - 429

ATOM 1391 OEl GLN 194 11.707 22.142 60.627 1.000 20.80

ANISOU 1391 OEl GLN 194 2245 2996 2662 -171 -382 - 681

ATOM 1392 NE2 GLN 194 10.223 21.585 62.197 1.000 24.91

ANISOU 1392 NE2 GLN 194 2539 3902 3023 210 -365 7 60

ATOM 1393 N THR 195 6.817 26.035 62.030 1.000 32.47

ANISOU 1393 N THR 195 5716 2729 3891 1095 1056 - 616

ATOM 1394 CA THR 195 6.588 26.708 63.282 1.000 35.83

ANISOU 1394 CA THR 195 6329 3539 3748 1011 999 - 722

ATOM 1395 CB THR 195 5.263 27.492 63.357 1.000 37.96

ANISOU 1395 CB THR 195 5756 4304 4365 647 2095 - 1151

ATOM 1396 OGl THR 195 4.191 26.576 63.604 1.000 48.36

ANISOU 1396 OGl THR 195 6874 6076 5423 -806 2581 - 1842

ATOM 1397 CG2 THR 195 4.958 28.175 62.033 1.000 44.54

ANISOU 1397 CG2 THR 195 2944 7471 6510 -872 -963 621

ATOM 1398 C THR 195 6.590 25.684 64.429 1.000 48.86

ANISOU 1398 C THR 195 10133 4924 3508 -321 -1356 - 221

ATOM 1399 0 THR 195 6.122 24.544 64.293 1.000 64.12

ANISOU 1399 0 THR 195 13267 4150 6945 -264 -4541 1682

ATOM 1400 N PHE 201 12.035 21.374 72.205 1.000 71.12

ANISOU 1400 N PHE 201 13961 9034 4028 -5932 -1658 - 1741

ATOM 1401 CA PHE 201 11.775 20.053 71.629 1.000 49.44

ANISOU 1401 CA PHE 201 7918 7543 3326 -3128 1317 - 1488

ATOM 1402 CB PHE 201 10.469 19.464 72.181 1.000 47.85

ANISOU 1402 CB PHE 2017119 6892 4168 -1869 1937 - 1899

ATOM 1403 CG PHE 201 10.130 18.113 71.545 1.000 46.41

ANISOU ^■ 1403 CG PHE 201 6643 6596 4396 -2038 1879 - 1497 ATOM 1404 CDI PHE 201 10.738 16.954 71.991 1.000 50.03

ANISOU 1404 CDI PHE 201 7982 6634 4393 -2326 1092 - 991

ATOM 1405 CD2 PHE 201 9.220 18.001 70.513 1.000 42 .63

ANISOU 1405 CD2 PHE 201 5458 6427 4313 -1097 2449 - 2268

ATOM 1406 CEl PHE 201 10.434 15.739 71.417 1.000 49.95

ANISOU 1406 CEl PHE 201 8275 6464 4240 -2047 227 - 716

ATOM 1407 CΞ2 PHE 201 8.901 16.783 69.934 1.000 41.38

ANISOU 1407 CE2 PHE 201 6016 5946 3762 -578 2006 - 1844

ATOM 1408 CZ PHE 201 9.515 15.636 70.392 1.000 44.74

ANISOU 1408 CZ PHE 201 7075 6261 3663 -1063 1020 - 975

ATOM 1409 C PHE 201 11.722 20.110 70.107 1.000 42.42

ANISOU 1409 C PHE 201 6324 6442 3351 -1964 717 - 1441

ATOM 1410 O PHE 201 11.007 20.941 69.536 1.000 47.79

ANISOU 1410 O PHE 201 9668 4400 4090 -762 691 - 2416

ATOM 1411 N VAL 202 12.477 19.232 69.449 1.000 34.04

ANISOU 1411 N VAL 202 4525 5852 2558 -1948 7 - 425

ATOM 1412 CA VAL 202 12.535 19.245 67.993 1.000 25.09

ANISOU 1412 CA VAL 202 3221 3752 2558 -1041 -182 9 9

ATOM 1413 CB VAL 202 13.988 19.286 67.489 1.000 22.88

ANISOU 1413 CB VAL 202 2832 3430 2432 -577 -691 - 198

ATOM 1414 CGI VAL 202 14.053 19.387 65.965 1.000 26.02

ANISOU 1414 CGI VAL 202 3821 3594 2470 -958 35 - 277

ATOM 1415 CG2 VAL 202 14.771 20.443 68.078 1.000 24.69

ANISOU 1415 CG2 VAL 202 3043 3473 2867 -786 -410 - 320

ATOM 1416 C VAL 202 11.798 18.035 67.421 1.000 20.69

ANISOU 1416 C VAL 202 3027 2810 2023 -648 58 6 15

ATOM 1417 O VAL 202 12.288 16.914 67.581 1.000 26.08

ANISOU 1417 O VAL 202 3294 3219 3396 -136 452 8 84

ATOM 1418 N SER 203 10.662 18.234 66.766 1.000 20.21

ANISOU 1418 N SER 203 3100 2794 1787 -414 25 - 152

ATOM 1419 CA SER 203 9.820 17.192 66.218 1.000 20.37

ANISOU 1419 CA SER 203 3149 2709 1884 -355 129 -256

ATOM 1420 CB SER 203 8.437 17.779 65.896 1.000 24.72

ANISOU 1420 CB SER 203 2726 4106 2558 -178 369 -1015

ATOM 1421 OG SER 203 7.841 18.239 67.097 1.000 31.80

ANISOU 1421 OG SER 203 3328 5782 2974 -457 1175 -1104

ATOM 1422 C SER 203 10.367 16.524 64.958 1.000 19.13

ANISOU 1422 C SER 203 2580 2647 2040 -339 170 -244

ATOM 1423 O SER 203 10.279 15.302 64.832 1.000 17.01

ANISOU 1423 O SER 203 2311 2625 1527 -414 206 - 18

ATOM 1424 N LEU 204 10.902 17.259 63.998 1.000 16.16

ANISOU 1424 N LEU 204 2142 1976 2024 71 77 - 292

ATOM 1425 CA LEU 204 11.403 16.679 62.740 1.000 14.07

ANISOU 1425 CA LEU 204 1670 1626 2049 -22 -24 - 283

ATOM 1426 CB LEU 204 11.269 17.704 61.618 1.000 13.80

ANISOU 1426 CB LEU 204 1549 1763 1931 -249 -340 - 277

ATOM 1427 CG LEU 204 11.647 17.272 60.212 1.000 14.13

ANISOU 1427 CG LEU 204 1726 1722 1919 -253 -482 - 412

ATOM 1428 CDI LEU 204 10.770 16.134 59.680 1.000 18.76

ANISOU 1428 CDI LEU 204 2579 2895 1654 -1297 -927 - 106

ATOM 1429 CD2 LEU 204 11.609 18.478 59.255 1.000 16.20

ANISOU 1429 CD2 LEU 204 1987 2095 2074 65 75 - 123

ATOM 1430 C LEU 204 12.832 16.140 62.885 1.000 14.81

ANISOU 1430 C LEU 204 1734 1748 2144 9 -199 - 250

ATOM 1431 O LEU 204 13.699 16.853 63.397 1.000 15.52

ANISOU 1431 O LEU 204 1833 1789 2274 -59 -435 - 42

ATOM 1432 N GLN 205 13.065 14.900 62.469 1.000 14.42

ANISOU 1432 N GLN 205 1847 1804 1827 189 -120 - 153

ATOM 1433 CA GLN 205 14.288 14.143 62.574 1.000 12.76

ANISOU ^' 1433 CA GLN 205 1777 1655 1419 43 -347 - 113

ATOM 1434 C GLN 205 14.622 13.434 61.260 1.000 11.12 ANISOU 1434 C GLN 205 1412 1474 1338 49 -468 - 2 1

ATOM 1435 O GLN 205 13.707 12.927 60.606 1.000 13 .97

ANISOU 1435 O GLN 205 1622 2235 1449 -293 -449 - 147

ATOM 1436 CB GLN 205 14.164 13.062 63.662 1.000 15.57

ANISOU 1436 CB GLN 205 2421 1925 1568 341 151 8 3

ATOM 1437 CG GLN 205 13.863 13.635 65.032 1.000 18.58

ANISOU 1437 CG GLN 205 3321 2286 1451 689 -129 8 2

ATOM 1438 CD GLN 205 15.086 14.243 65.680 1.000 24.33

ANISOU 1438 CD GLN 205 3687 3465 2091 520 -499 - 570

ATOM 1439 OEl GLN 205 16.206 13.717 65.549 1.000 29.12

ANISOU 1439 OEl GLN 205 3350 3464 4251 14 -270 - 1800

ATOM 1440 NE2 GLN 205 14.840 15.356 66.378 1.000 23.01

ANISOU 1440 NE2 GLN 205 3055 2465 3225 335 -592 - 140

ATOM 1441 N ALA 206 15.893 13.401 60.893 1.000 12.63

ANISOU 1441 N ALA 206 1523 1770 1506 -251 -234 - 6

ATOM 1442 CA ALA 206 16.335 12.649 59.731 1.000 13 .77

ANISOU 1442 CA ALA 206 1392 2099 1742 -522 -72 - 295

ATOM 1443 CB ALA 206 16.693 13.519 58.528 1.000 16.34

ANISOU 1443 CB ALA 206 2034 2494 1682 -603 123 - 277

ATOM 1444 C ALA 206 17.567 11.813 60.046 1.000 15.92

ANISOU 1444 C ALA 206 1489 2331 2230 -290 179 - 341

ATOM 1445 O ALA 206 18.368 12.182 60.908 1.000 15.86

ANISOU 1445 O ALA 206 1877 1772 2377 150 -356 3 0

ATOM 1446 N GLU 207 17.707 10.712 59.305 1.000 16.98

ANISOU 1446 N GLU 207 1981 2086 2383 -335 348 - 186

ATOM 1447 CA GLU 207 18.938 9.942 59.364 1.000 20.58

ANISOU 1447 CA GLU 207 2198 1938 3684 -164 490 - 10

ATOM 1448 C GLU 207 20.082 10.688 58.681 1.000 18.75

ANISOU 1448 C GLU 207 1828 2037 3260 272 185 55 8

ATOM 1449 O GLU 207 19.948 10.953 57.503 1.000 18.23

ANISOU 1449 O GLU 207 1746 2145 3034 52 8 - 45

ATOM 1450 CB GLU 207 18.665 8.612 58.676 1.000 25.81

ANISOU 1450 CB GLU 207 3289 1794 4724 -19 83 - 135

ATOM 1451 CG GLU 207 19.879 7.737 58.429 1.000 30.08

ANISOU 1451 CG GLU 207 4102 2221 5105 907 -948 - 546

ATOM 1452 CD GLU 207 19.429 6.356 57.959 1.000 29.93

ANISOU 1452 CD GLU 207 5549 2024 3798 1179 -2099 - 123

ATOM 1453 OEl GLU 207 19.491 5.471 58.839 1.000 35.14

ANISOU 1453 OEl GLU 207 5782 2692 4879 938 -931 8 85

ATOM 1454 OE2 GLU 207 19.037 6.251 56.762 1.000 38.62

ANISOU 1454 OE2 GLU 207 4955 5608 4109 135 -2494 - 366

ATOM 1455 N VAL 208 21.146 10.997 59.414 1.000 16.97

ANISOU 1455 N VAL 208 1926 1974 2549 120 337 8 07

ATOM 1456 CA VAL 208 22.376 11.593 58.902 1.000 17.77

ANISOU 1456 CA VAL 208 1894 2109 2748 93 500 411

ATOM 1457 CB VAL 208 22.455 13.111 59.155 1.000 16.89

ANISOU 1457 CB VAL 208 2774 2148 1494 -372 -149 5 69

ATOM 1458 CGI , VAL 208 23.652 13.688 58.409 1.000 20.76

ANISOU 1458 CGI , VAL 208 3214 2150 2526 -423 647 148

ATOM 1459 CG2 : VAL 208 21.172 13.815 58.720 1.000 16.36

ANISOU 1459 CG2 : VAL 208 3146 1640 1431 25 98 3 5 3

ATOM 1460 C VAL 208 23.585 10.877 59.507 1.000 20.29

ANISOU 1460 C VAL 208 1936 2555 3217 11 -58 13 2

ATOM 1461 O VAL 208 23.726 10.829 60.741 1.000 20.74

ANISOU 1461 O VAL 208 2436 2256 3187 460 206 544

ATOM 1462 N GLY 209 24.457 10.295 58.672 1.000 18.94

ANISOU 1462 N GLY 209 1764 2445 2989 211 -494 1 5

ATOM 1463 CA GLY 209 25.558 9.508 59.194 1.000 24.01

ANISOU ^■ 1463 CA GLY 209 2171 3040 3910 549 -396 7 09

ATOM 1464 C GLY 209 25.123 8.364 60.082 1.000 25.00

ANISOUf 1464 C GLY 209 2874 3156 3470 1406 772 64 9 ATOM 1465 O GLY 209 25.850 7.934 60.991 1.000 35.98

ANISOU 1465 O GLY 209 4448 3946 5279 1425 -426 1769

ATOM 1466 N GLY 210 23.951 7.786 59.869 1.000 25.89

ANISOU 1466 N GLY 210 3802 2756 3278 523 899 7 4 9

ATOM 1467 CA GLY 210 23.477 6.678 60.671 1.000 26.43

ANISOU 1467 CA GLY 210 4479 2136 3427 1228 742 9 12

ATOM 1468 C GLY 210 22.885 7.025 62.016 1.000 28.45

ANISOU 1468 C GLY 210 5472 2099 3237 831 1029 1175

ATOM 1469 O GLY 210 22.634 6.098 62.789 1.000 40.26

ANISOU 1469 O GLY 210 7322 2719 5256 1881 2759 2360

ATOM 1470 N ALA 211 22.651 8.281 62.338 1.000 25 .78

ANISOU 1470 N ALA 211 4671 2359 2763 1370 724 1197

ATOM 1471 CA ALA 211 22.048 8.671 63.613 1.000 23 .74

ANISOU 1471 CA ALA 211 2966 3156 2896 727 339 6 63

ATOM 1472 CB ALA 211 23.093 9.333 64.496 1.000 29.57

ANISOU 1472 CB ALA 211 2957 4372 3906 834 -96 6 9

ATOM 1473 C ALA 211 20.900 9.626 63.360 1.000 21.19

ANISOU 1473 C ALA 211 3090 2611 2350 484 178 7 4 1

ATOM 1474 O ALA 211 20.936 10.381 62.399 1.000 23 .91

ANISOU 1474 O ALA 211 3771 2659 2653 -30 -66 9 3 0

ATOM 1475 N PHE 212 19.889 9.629 64.204 1.000 19.88

ANISOU 1475 N PHE 212 2603 2577 2375 398 -128 3 74

ATOM 1476 CA PHE 212 IS .814 10.613 64.130 1.000 19.13

ANISOU 1476 CA PHE 212 2581 2257 2432 284 -565 3 17

ATOM 1477 C PHE 212 19.320 12.006 64.489 1.000 20.00

ANISOU 1477 C PHE 212 3004 2480 2115 133 -640 6 8

ATOM 1478 O PHE 212 19.893 12.230 65.569 1.000 21.10

ANISOU 1478 O PHE 212 2497 3558 1964 -391 -406 22 2

ATOM 1479 CB PHE 212 17.688 10.290 65.096 1.000 21.37

ANISOU 1479 CB PHE 212 2553 2616 2952 293 -197 - 184

ATOM 1480 CG PHE 212 17.010 8.950 64.912 1.000 23 .45

ANISOU 1480 CG PHE 212 2161 3496 3253 -376 -282 - 558

ATOM 1481 CDI PHE 212 16.369 8.377 65.990 1.000 23 .33

ANISOU 1481 CDI PHE 212 2545 3115 3206 -382 -350 - 508

ATOM 1482 CD2 PHE 212 17.029 8.302 63.687 1.000 25.83

ANISOU 1482 CD2 PHE 212 2554 3962 3299 -622 -217 - 787

ATOM 1483 CEl PHE 212 15.730 7.149 65.872 1.000 28.13

ANISOU 1483 CEl PHE 212 3784 3544 3362 -1119 96 - 973

ATOM 1484 CE2 PHE 212 16.419 7.072 63.569 1.000 23.04

ANISOU 1484 CE2 PHE 212 2504 2960 3289 382 -232 - 558

ATOM 1485 CZ PHE 212 15.781 6.486 64.651 1.000 27.88

ANISOU 1485 CZ PHE 212 3658 3977 2957 -1072 -501 - 760

ATOM 1486 N THR 213 19.076 12.936 63.578 1.000 18.30

ANISOU 1486 N THR 213 2690 2083 2181 149 -583 - 9 3

ATOM 1487 CA THR 213 19.566 14.310 63.681 1.000 17.99

ANISOU 1487 CA THR 213 1976 2139 2721 230 -686 - 287

ATOM 1488 CB THR 213 20.515 14.586 62.498 1.000 20.43

ANISOU 1488 CB THR 213 1798 2280 3683 140 -119 - 423

ATOM 1489 OGl THR 213 21.638 13.695 62.629 1.000 25.33

ANISOU 1489 OGl THR 213 2571 3378 3676 925 71 5 2 8

ATOM 1490 CG2 THR 213 21.087 15.985 62.485 1.000 21.11

ANISOU 1490 CG2 THR 213 1935 2667 3420 -310 -289 - 747

ATOM 1491 C THR 213 18.391 15.277 63.641 1.000 15.53

ANISOU 1491 C THR 213 1732 2135 2032 111 -557 - 167

ATOM 1492 O THR 213 17.533 15.195 62.761 1.000 16.11

ANISOU 1492 O THR 213 1742 2197 2180 -327 -669 5 6

ATOM 1493 N ASP 214 18.362 16.199 64.590 1.000 15.60

ANISOU 1493 N ASP 214 2025 2046 1857 64 -405 2

ATOM 1494 CA ASP 214 17.380 17.256 64.672 1.000 15.59

ANISOU ^' 1494 CA ASP 214 2130 1722 2072 2 -1010 - 242

ATOM 1495 CB ASP 214 17.744 18.200 65.822 1.000 17.13 ANISOU 1495 CB ASP 214 2528 1893 2086 -226 -1022 - 247

ATOM 1496 CG ASP 214 17.612 17.672 67.219 1.000 20.21

ANISOU 1496 CG ASP 214 3138 2495 2045 -451 -1276 - 148

ATOM 1497 ODl ASP 214 17.079 16.571 67.460 1.000 20.87

ANISOU 1497 ODl ASP 214 2778 2632 2518 -247 -505 15 1

ATOM 1498 OD2 ASP 214 18.076 18.401 68.127 1.000 28 .05

ANISOU 1498 OD2 ASP 214 5110 3118 2429 -257 -1997 - 619

ATOM 1499 C ASP 214 17.314 18.146 63.441 1.000 15.14

ANISOU 1499 C ASP 214 2029 1822 1901 182 -574 - 319

ATOM 1500 O ASP 214 18.349 18.552 62.897 1.000 17 .63

ANISOU 1500 O ASP 214 1956 2032 2710 -214 -810 - 15

ATOM 1501 N LEU 215 16.105 18.493 63.027 1.000 14.69

ANISOU 1501 N LEU 215 1936 1758 1887 38 -334 2 42

ATOM 1502 CA LEU 215 15.915 19.504 61.979 1.000 13 .35

ANISOU 1502 CA LEU 215 1820 1753 1498 89 -22 5 9

ATOM 1503 CB LEU 215 15.352 18.819 60.734 1.000 14.24

ANISOU 1503 CB LEU 215 1735 2167 1506 -98 75 - 3

ATOM 1504 CG LEU 215 16.291 17.813 60.056 1.000 16.39

ANISOU 1504 CG LEU 215 2031 2285 1911 -340 320 - 424

ATOM 1505 CDI LEU 215 15.517 16.999 59.031 1.000 22.61

ANISOU 1505 CDI LEU 215 3139 2024 3427 -10 -801 - 877

ATOM 1506 CD2 LEU 215 17.482 18.543 59.434 1.000 26.93

ANISOU 1506 CD2 LEU 215 1998 5409 2827 -1083 909 - 542

ATOM 1507 C LEU 215 15.002 20.622 62.500 1.000 14.65

ANISOU 1507 C LEU 215 1770 1607 2190 86 -165 - 95

ATOM 1508 O LEU 215 13.822 20.662 62.151 1.000 19.45

ANISOU 1508 O LEU 215 1748 2165 3476 116 -303 - 203

ATOM 1509 N PRO 216 15.552 21.523 63.314 1.000 15.99

ANISOU 1509 N PRO 216 2390 1970 1715 -164 21 - 175

ATOM 1510 CD PRO 216 16.955 21.601 63.757 1.000 19.37

ANISOU 1510 CD PRO 216 2900 2306 2155 -83 -790 - 548

ATOM 1511 CA PRO 216 14.760 22.620 63.846 1.000 18.68

ANISOU 1511 CA PRO 216 3104 2017 1976 12 -74 - 420

ATOM 1512 CB PRO 216 15.649 23.227 64.949 1.000 18.63

ANISOU 1512 CB PRO 216 3592 1517 1971 -120 -421 9

ATOM 1513 CG PRO 216 17.030 22.847 64.581 1.000 22.35

ANISOU 1513 CG PRO 216 3401 2426 2666 -419 -427 - 783

ATOM 1514 C PRO 216 14.461 23.700 62.819 1.000 18.50

ANISOU 1514 C PRO 216 2921 2083 2026 58 -465 - 473

ATOM 1515 O PRO 216 15.024 23.854 61.731 1.000 19.82

ANISOU 1515 O PRO 216 2752 2453 2325 -32 -375 1 9

ATOM 1516 N TYR 217 13.487 24.536 63.194 1.000 20.05

ANISOU 1516 N TYR 217 3213 1981 2422 90 -482 - 718

ATOM 1517 CA TYR 217 13.178 25.662 62.308 1.000 22.97

ANISOU 1517 CA TYR 217 2849 2652 3227 211 -1467 - 313

ATOM 1518 C TYR 217 14.347 26.647 62.283 1.000 23.92

ANISOU 1518 C TYR 217 4139 2131 2819 -337 -1776 - 165

ATOM 1519 O TYR 217 15.149 26.726 63.213 1.000 30.46

ANISOU 1519 O TYR 217 4321 3440 3812 -1118 -2477 72 8

ATOM 1520 CB TYR 217 11.891 26.314 62.768 1.000 32.68

ANISOU 1520 CB TYR 217 3958 3294 5164 1148 -874 - 783

ATOM 1521 CG TYR 217 12.064 27.462 63.718 1.000 44.77

ANISOU 1521 CG TYR 217 6829 4326 5854 895 38 - 1870

ATOM 1522 CDI , TYR 217 11.853 28.763 63.285 1.000 54.26

ANISOU 1522 CDI . TYR 217 10311 3688 6615 -323 132 -1945

ATOM 1523 CD2 TYR 217 12.428 27.243 65.043 1.000 57.77

ANISOU 1523 CD2 : TYR 217 10635 5155 6158 -1027 -1446 - 1931

ATOM 1524 CEl . TYR 217 12.011 29.816 64.174 1.000 60.33

ANISOU ^' 1524 CEl . TYR 217 11807 4345 6772 -1101 -132 -2259

ATOM 1525 CE2 ! TYR 217 12.585 28.296 65.926 1.000 64.51

ANISOU ^■ 1525 CE2 ! TYR 217 12481 5199 6832 -1936 -1520 - 2074 ATOM 1526 CZ TYR 217 12.378 29.586 65.481 1.000 64.11

ANISOU 1526 CZ TYR 217 12047 5183 7129 -1460 -817 - 2160

ATOM 1527 OH TYR 217 12.536 30.639 66.358 1.000 63.69

ANISOU 1527 OH TYR 217 11840 5206 7153 -1832 -1191 - 2064

ATOM 1528 N ARG 218 14.418 27.374 61.188 1.000 24.08

ANISOU 1528 N ARG 218 4482 1611 3055 507 -1471 - 145

ATOM 1529 CA ARG 218 15.335 28.465 60.948 1.000 30.71

ANISOU 1529 C ARG 218 5932 2490 3245 -504 -1565 3 8 2

ATOM 1530 C3 ARG 218 16.326 28.135 59.840 1.000 35.08

ANISOU 1530 C3 ARG 218 5969 2797 4562 -1397 -779 - 348

ATOM 1531 CG ARG 218 17.401 27.114 60.073 1.000 35.77

ANISOU 1531 CG ARG 218 6009 3087 4497 -1107 -733 - 773

ATOM 1532 CD ARG 218 18.658 27.775 60.626 1.000 34.46

ANISOU 1532 CD ARG 218 5680 3264 4152 -1242 -244 - 619

ATOM 1533 NΞ ARG 218 19.223 28.746 59.709 1.000 29.51

ANISOU 1533 NE ARG 218 4707 2579 3926 78 81 - 629

ATOM 1534 CZ ARG 218 20.218 28.620 58.830 1.000 33 .18

ANISOU 1534 CZ ARG 218 5269 3166 4170 60 452 - 1075

ATOM 1535 NHl ARG 218 20.839 27.452 58.709 1.000 27.44

ANISOU 1535 NHl ARG 218 4202 2881 3341 -503 -373 - 1585

ATOM 1536 NH2 ARG 218 20.583 29.675 58.077 1.000 22.96

ANISOU 1536 NH2 ARG 218 2327 3579 2817 233 -1117 - 872

ATOM 1537 C ARG 218 14.513 29.655 60.464 1.000 31.05

ANISOU 1537 C ARG 218 7353 1949 2496 -448 -1823 197

ATOM 1538 O ARG 218 14.114 29.533 59.295 1.000 40.40

ANISOU 1538 O ARG 218 9873 2241 3235 531 -3168 - 627

ATOM 1539 N PRO 219 14.246 30.747 61.157 1.000 30.01

ANISOU 1539 N PRO 219 6290 2559 2555 -499 -1839 - 284

ATOM 1540 CD PRO 219 14.597 31.043 62.543 1.000 36.79

ANISOU 1540 CD PRO 219 8147 2878 2954 -1848 -2548 - 374

ATOM 1541 CA PRO 219 13.464 31.841 60.549 1.000 26.34

ANISOU 1541 CA PRO 219 4421 2564 3025 -573 -988 - 340

ATOM 1542 CB PRO 219 13.523 32.993 61.563 1.000 32.44

ANISOU 1542 CB PRO 219 5361 2891 4073 -691 -417 - 989

ATOM 1543 CG PRO 219 13.947 32.372 62.825 1.000 38.75

ANISOU 1543 CG PRO 219 7916 3462 3344 -1981 -958 - 1235

ATOM 1544 C PRO 219 14.005 32.329 59.220 1.000 23.64

ANISOU 1544 C PRO 219 3472 2066 3443 -161 -1028 109

ATOM 1545 O PRO 219 13.300 32.950 58.412 1.000 30.61

ANISOU 1545 O PRO 219 4358 2934 4339 -347 -1712 87 6

ATOM 1546 N ASP 220 15.269 32.087 58.906 1.000 25.98

ANISOU 1546 N ASP 220 3611 1756 4506 -389 -644 - 815

ATOM 1547 CA ASP 220 15.847 32.660 57.705 1.000 27.96

ANISOU 1547 CA ASP 220 3951 1603 5071 -364 30 - 824

ATOM 1548 CB ASP 220 17.212 33.238 58.155 1.000 29.61

ANISOU 1548 CB ASP 220 3549 3142 4558 -176 -326 17 6

ATOM 1549 CG ASP 220 18.091 32.158 58.780 1.000 32.09

ANISOU 1549 CG ASP 220 3706 3527 4961 625 978 6 15

ATOM 1550 ODl . ASP 220 17.697 31.434 59.719 1.000 26.12

ANISOU 1550 ODl . ASP 220 3013 3522 3390 -158 -289 - 97

ATOM 1551 OD2 ; ASP 220 19.241 32.088 58.281 1.000 29.09

ANISOU 1551 OD2 : ASP 220 3714 3756 3581 304 677 - 712

ATOM 1552 C ASP 220 16.037 31.726 56.525 1.000 25.26

ANISOU 1552 C ASP 220 2508 1291 5800 354 1110 - 822

ATOM 1553 O ASP 220 16.641 32.095 55.515 1.000 28.28

ANISOU 1553 O ASP 220 4088 1665 4994 -855 298 - 434

ATOM 1554 N ALA 221 15.500 30.510 56.631 1.000 21.58

ANISOU 1554 N ALA 221 2748 1770 3681 -288 178 - 651

ATOM 1555 CA ALA 221 15.840 29.484 55.658 1.000 19.81

ANISOU 1555 CA ALA 221 2986 1452 3090 -342 -224 - 315

ATOM 1556 CB ALA 221 17.130 28.800 56.109 1.000 19.51 ANISOU 1556 CB ALA 221 2267 1497 3647 -648 45 - 746

ATOM 1557 C ALA 221 14.718 28.469 55.489 1.000 17.71

ANISOU 1557 c ALA 221 2304 1912 2512 -251 -75 - 30

ATOM 1558 0 ALA 221 13.866 28.356 56.380 1.000 20.97

ANISOU 1558 0 ALA 221 3596 2029 2344 -503 406 - 28

ATOM 1559 N VAL 222 14.728 27.756 54.378 1.000 14.22

ANISOU 1559 N VAL 222 1560 1582 2262 -76 -92 - 1 1

ATOM 1560 CA VAL 222 13.823 26.617 54.160 1.000 14.89

ANISOU 1560 CA VAL 222 1326 1608 2723 98 -216 - 205

ATOM 1561 CB VAL 222 13.079 26.779 52.830 1.000 17.28

ANISOU 1561 CB VAL 222 1680 1754 3133 90 -657 - 144

ATOM 1562 CGI VAL 222 13.995 26.685 51.620 1.000 19.17

ANISOU 1562 CGI VAL 222 1974 2625 2686 -446 -775 150

ATOM 1563 CG2 VAL 222 11.996 25.747 52.641 1.000 17 .36

ANISOU 1563 CG2 VAL 222 2185 1879 2533 -254 -362 - 38

ATOM 1564 C VAL 222 14.653 25.339 54.263 1.000 12.66

ANISOU 1564 C VAL 222 1136 1564 2112 -50 -225 - 37

ATOM 1565 O VAL 222 15.828 25.320 53.893 1.000 13 .12

ANISOU 1565 O VAL 222 1280 1825 1881 104 -13 - 19

ATOM 1566 N LEU 223 14.049 24.267 54.775 1.000 12.98

ANISOU 1566 N LEU 223 1123 1538 2270 -163 -370 - 41

ATOM 1567 CA LEU 223 14.681 22.952 54.749 1.000 10.70

ANISOU 1567 CA LEU 223 891 1704 1472 -26 -98 - 7

ATOM 1568 CB LEU 223 14.276 22.130 55.961 1.000 13 .02

ANISOU 1568 CB LEU 223 1387 1968 1593 -419 289 - 10

ATOM 1569 CG LEU 223 14.739 20.683 56.106 1.000 17.41

ANISOU 1569 CG LEU 223 2434 2132 2050 -290 -476 5 6 6

ATOM 1570 CDI LEU 223 16.247 20.614 56.204 1.000 17.20

ANISOU 1570 CDI LEU 223 2576 1518 2441 26 -989 - 249

ATOM 1571 CD2 LEU 223 13.983 20.076 57.282 1.000 33.63

ANISOU 1571 CD2 LEU 223 3981 4721 4077 -341 134 294

ATOM 1572 C LEU 223 14.362 22.211 53.456 1.000 10.02

ANISOU 1572 C LEU 223 1000 1265 1543 58 -319 8 8

ATOM 1573 O LEU 223 13.206 22.160 53.088 1.000 12.86

ANISOU 1573 O LEU 223 949 1945 1992 -97 -174 - 372

ATOM 1574 N VAL 224 15.406 21.675 52.798 1.000 10.55

ANISOU 1574 N VAL 224 978 1070 1962 -76 -418 - 382

ATOM 1575 CA VAL 224 15.227 20.932 51.553 1.000 11.98

ANISOU 1575 CA VAL 224 1376 1288 1887 -249 -278 - 37

ATOM 1576 CB VAL 224 16.095 21.461 50.391 1.000 11.23

ANISOU 1576 CB VAL 224 901 1541 1824 -279 -622 - 9 9

ATOM 1577 CGI VAL 224 15.833 20.690 49.102 1.000 13 .16

ANISOU 1577 CGI VAL 224 1899 1485 1615 -462 -516 8 4

ATOM 1578 CG2 VAL 224 15.837 22.941 50.156 1.000 13.86

ANISOU 1578 CG2 VAL 224 1480 1520 2266 -135 -354 - 6 .

ATOM 1579 C VAL 224 15.539 19.450 51.786 1.000 10.87

ANISOU 1579 C VAL 224 953 1275 1901 -13 342 -484

ATOM 1580 O VAL 224 16.646 19.148 52.201 1.000 12.57

ANISOU 1580 O VAL 224 1283 1363 2132 -175 -154 - 27

ATOM 1581 N PHE 225 14.585 18.553 51.533 1.000 11.86

ANISOU 1581 N PHE 225 1241 1128 2137 -15 -303 - 6 :

ATOM 1582 CA PHE 225 14.811 17.130 51.412 1.000 11.38

ANISOU 1582 CA PHE 225 1260 1157 1909 -22 -67 - 5 ι

ATOM 1583 CB PHE 225 13.707 16.280 52.044 1.000 11.34

ANISOU 1583 CB PHE 225 1117 1176 2015 205 -213 3 3 !

ATOM 1584 CG PHE 225 13.654 16.172 53.544 1.000 11.38

ANISOU 1584 CG PHE 225 964 1369 1991 -251 -333 181

ATOM 1585 CDI . PHE 225 14.685 15.653 54.291 1.000 15.28

ANISOU 1585 CDI . PHE 225 1771 1777 2256 -98 -853 2 9

ATOM 1586 CD2 ! PHE 225 12.532 16.576 54.254 1.000 17.91

ANISOU ^' 1586 CD2 ! PHE 225 1904 2748 2153 341 106 0 ATOM 1587 CEl PHE 225 14.619 15.535 55.661 1.000 17.46

ANISOU 1587 CEl PHE 225 2449 1862 2321 -249 -795 6 6 i

ATOM 1588 CE2 PHE 225 12.447 16.474 55.612 1.000 19.35

ANISOU 1588 CE2 PHE 225 2563 2678 2111 121 129 - 11

ATOM 1589 CZ PHE 225 13.499 15.945 56.341 1.000 18.20

ANISOU 1589 CZ PHE 225 2952 1641 2324 -501 -470 3 6

ATOM 1590 C PHE 225 14.907 16.774 49.927 1.000 12.03

ANISOU 1590 C PHE 225 1480 1285 1804 130 -201 4 2

ATOM 1591 0 PHE 225 14.019 17.160 49.163 1.000 12 .77

ANISOU 1591 0 PHE 225 1473 1466 1912 341 -118 3 8

ATOM 1592 N CYS 226 15.940 16.032 49.521 1.000 9 . 62

ANISOU 1592 N CYS 226 954 1403 1296 -204 -407 2 9

ATOM 1593 CA CYS 226 15.917 15.400 48.197 1.000 10.80

ANISOU 1593 CA CYS 226 1432 1204 1468 -258 -310 - 5 !

ATOM 1594 CB CYS 226 17.337 15.029 47.744 1.000 12 .02

ANISOU 1594 CB CYS 226 1539 1362 1666 -357 16 - 125

ATOM 1595 SG CYS 226 18.426 16.490 47.554 1.000 13 .74

ANISOU 1595 SG CYS 226 1627 1400 2192 -341 18 13 9

ATOM 1596 C CYS 226 14.998 14.178 48.256 1.000 9 . 86

ANISOU 1596 C CYS 226 1190 1061 1495 -20 -293 - 1 ι

ATOM 1597 0 CYS 226 15.015 13.431 49.252 1.000 11.17

ANISOU 1597 0 CYS 226 1181 1280 1781 -129 -435 2 7 :

ATOM 1598 N GLY 227 14.217 13.963 47.205 1.000 10.17

ANISOU 1598 N GLY 227 1428 1010 1427 -258 -271 - 3

ATOM 1599 CA GLY 227 13.370 12.806 47.053 1.000 9 .73

ANISOU 1599 CA GLY 227 1231 860 1604 -178 -74 - 3 7

ATOM 1600 C GLY 227 13.908 11.769 46.074 1.000 9 .48

ANISOU 1600 C GLY 227 1438 717 1445 16 -35 1 69

ATOM 1601 O GLY 227 14.935 11.961 45.402 1.000 9 . 86

ANISOU 1601 O GLY 227 1321 1137 1290 -104 -179 7 8

ATOM 1602 N ALA 228 13.217 10.631 45.971 1.000 9 . 17

ANISOU 1602 N ALA 228 1279 729 1477 109 -135 5 8

ATOM 1603 CA ALA 228 13.650 9.529 45.108 1.000 9 .41

ANISOU 1603 CA ALA 228 1315 887 1371 9 -74 - 52

ATOM 1604 CB ALA 228 12.727 8.296 45.256 1.000 10.50

ANISOU 1604 CB ALA 228 2011 824 1155 -143 124 101

ATOM 1605 C ALA 228 13.712 9.918 43.637 1.000 9 .25

ANISOU 1605 C ALA 228 1343 666 1507 -108 90 13 9

ATOM 1606 O ALA 228 14.493 9.305 42.895 1.000 9 .48

ANISOU 1606 O ALA 228 1171 1026 1405 -88 -50 9 0

ATOM 1607 N ILE 229 12.970 10.907 43.143 1.000 10.30

ANISOU 1607 N ILE 229 1402 1004 1509 18 25 177

ATOM 1608 CA ILE 229 13.074 11.311 41.727 1.000 10.87

ANISOU 1608 CA ILE 229 1197 1446 1487 -2 -159 2 5 1

ATOM 1609 CB ILE 229 11.802 12.078 41.295 1.000 11.52

ANISOU 1609 CB ILE 229 1257 1473 1647 34 -57 3 62

ATOM 1610 CG2 ILE 229 11.997 12.852 39.999 1.000 11.30

ANISOU 1610 CG2 ILE 229 1655 1211 1426 83 -189 15 6

ATOM 1611 CGI , ILE 229 10.575 11.131 41.237 1.000 14.39

ANISOU 1611 CGI , ILE 229 1031 2034 2402 -40 210 3 1

ATOM 1612 CDI . ILE 229 10.676 10.093 40.138 1.000 19.20

ANISOU 1612 CDI . ILE 229 2085 1723 3489 -610 93 - 13.

ATOM 1613 C ILE 229 14.389 12.034 41.477 1.000 10.38

ANISOU 1613 C ILE 229 1293 1405 1247 -62 -169 32

ATOM 1614 O ILE 229 14.952 11.947 40.369 1.000 11.66

ANISOU 1614 O ILE 229 1805 1257 1368 -13 145 3 2

ATOM 1615 N ALA 230 14.965 12.692 42.490 1.000 10.66

ANISOU ^■ 1615 N ALA 230 1476 1274 1300 -104 -151 3 5

ATOM 1616 CA ALA 230 16.312 13.259 42.338 1.000 11.21

ANISOU r 1616 CA ALA 230 1473 975 1813 -57 -308 9 0

ATOM 1617 CB ALA 230 16.681 14.148 43.509 1.000 10.58 -143-

ANISOU 1617 CB ALA 230 1350 1295 1375 62 -106 12 6

ATOM 1618 C ALA 230 17.336 12.136 42.132 1.000 11.28

ANISOU 1618 C ALA 230 1640 1037 1610 1 55 242

ATOM 1619 O ALA 230 18.220 12.185 41.273 1.000 11.29

ANISOU 1619 O ALA 230 1510 1240 1539 -189 -40 2 8 .

ATOM 1620 N THR 231 17.173 11.097 42.946 1.000 10.55

ANISOU 1620 N THR 231 1328 894 1787 -262 -70 2 14

ATOM 1621 CA THR 231 18.064 9.939 42.819 1.000 11.98

ANISOU 1621 CA THR 231 1929 1018 1605 0 -164 15 9

ATOM 1622 CB THR 231 17.717 8.865 43.878 1.000 10.76

ANISOU 1622 CB THR 231 1381 1070 1636 -86 -453 2 4 .

ATOM 1623 OGl THR 231 17.658 9.437 45.198 1.000 11.82

ANISOU 1623 OGl THR 231 1615 1236 1641 35 -115 277

ATOM 1624 CG2 THR 231 18.765 7.752 43.880 1.000 12.57

ANISOU 1624 CG2 THR 231 1621 1314 1840 160 -89 3 5 :

ATOM 1625 C THR 231 17.958 9.352 41.415 1.000 12 .52

ANISOU 1625 C THR 231 1632 1500 1624 -145 42 1 1

ATOM 1626 O THR 231 18.939 9.050 40.732 1.000 12.15

ANISOU 1626 O THR 231 1636 1233 1747 -17 86 2 2 4

ATOM 1627 N LEU 232 16.717 9.154 40.959 1.000 11.14

ANISOU 1627 N LEU 232 1608 1005 1620 90 -68 141

ATOM 1628 CA LEU 232 16.446 8.522 39.675 1.000 12 .47

ANISOU 1628 CA LEU 232 1880 1203 1657 109 -169 4 5

ATOM 1629 CB LEU 232 14.950 8.214 39.552 1.000 12.81

ANISOU 1629 CB LEU 232 1989 1225 1654 -78 -209 1 9

ATOM 1630 CG LEU 232 14.452 7.464 38.314 1.000 14.85

ANISOU 1630 CG LEU 232 2171 1753 1719 -5 -410 - 9 6

ATOM 1631 CDI LEU 232 15.020 6.055 38.240 1.000 16.78

ANISOU 1631 CDI LEU 232 2693 1749 1932 72 -431 - 487

ATOM 1632 CD2 LEU 232 12.914 7.411 38.291 1.000 15.70

ANISOU 1632 CD2 LEU 232 2180 1866 1920 -278 -589 49

ATOM 1633 C LEU 232 16.964 9.354 38.511 1.000 11.58

ANISOU 1633 C LEU 232 1452 1390 1559 309 -301 13

ATOM 1634 O LEU 232 17.752 8.837 37.686 1.000 13.45

ANISOU 1634 O LEU 232 1808 1436 1867 320 -17 3 0

ATOM 1635 N VAL 233 16.565 10.617 38.414 1.000 10.95

ANISOU 1635 N VAL 233 1428 1210 1522 -14 -210 0

ATOM 1636 CA VAL 233 16.948 11.421 37.242 1.000 11.70

ANISOU 1636 CA VAL 233 1703 1345 1397 97 5 1 3

ATOM 1637 CB VAL 233 16.156 12.743 37.215 1.000 11.14

ANISOU 1637 CB VAL 233 1672 1272 1287 -26 276 7 3

ATOM 1638 CGI VAL 233 16.661 13.774 38.249 1.000 13.34

ANISOU 1638 CGI VAL 233 1834 1562 1673 -205 653 -3 ι 68

ATOM 1639 CG2 VAL 233 16.106 13.412 35.827 1.000 14.66

ANISOU 1639 CG2 VAL 233 1992 1873 1704 -4 -45 5 8 6

ATOM 1640 C VAL 233 18.459 11.586 37.132 1.000 13.41

ANISOU 1640 C VAL 233 1712 1573 1811 91 151 125

ATOM 1641 O VAL 233 19.012 11.627 36.021 1.000 13.45

ANISOU 1641 O VAL 233 1844 1402 1866 46 192 43 8

ATOM 1642 N THR 234 19.188 11.665 38.250 1.000 13.13

ANISOU 1642 N THR 234 1457 1639 1893 -139 223 12

ATOM 1643 CA THR 234 20.613 11.930 38.244 1.000 13 .00

ANISOU 1643 CA THR 234 1483 1600 1855 -188 428 14

ATOM 1644 CB THR 234 21.069 12.726 39.465 1.000 12.46

ANISOU 1644 CB THR 234 1300 1632 1803 -32 200 2 5

ATOM 1645 OGl . THR 234 20.825 11.941 40.639 1.000 13.71

ANISOU 1645 OGl , THR 234 1660 1662 1888 192 202 2 9

ATOM 1646 CG2 THR 234 20.301 14.027 39.643 1.000 11.37

ANISOU 1646 CG2 : THR 234 1097 1565 1657 -153 -87 16

ATOM 1647 C THR 234 21.424 10.643 38.178 1.000 14.44

ANISOU 1647 C THR 234 1550 1823 2114 6 -73 - 53 -144-

ATOM 1648 O THR 234 22.659 10.710 38.233 1.000 15.81

ANISOU 1648 O THR 234 1546 2169 2293 61 27 217

ATOM 1649 N GLY 235 20.767 9.477 38.070 1.000 14.76

ANISOU 1649 N GLY 235 1776 1576 2254 77 81 4 1 0

ATOM 1650 CA GLY 235 21.530 8.249 37.994 1.000 16.69

ANISOU 1650 CA GLY 235 2053 1803 2486 304 35 18 9

ATOM 1651 C GLY 235 22.243 7.862 39.275 1.000 16.83

ANISOU 1651 C GLY 235 1854 2031 2512 765 244 1 9

ATOM 1652 O GLY 235 23.305 7.237 39.194 1.000 19 .67

ANISOU 1652 O GLY 235 2074 2172 3225 1035 383 3 7

ATOM 1653 N GLY 236 21.665 8.227 40.425 1.000 14.46

ANISOU 1653 N GLY 236 1732 1327 2433 154 198 7 5

ATOM 1654 CA GLY 236 22.187 7.768 41.692 1.000 15 .73

ANISOU 1654 CA GLY 236 2060 1381 2536 41 186 3 12

ATOM 1655 C GLY 236 23.166 8.691 42.388 1.000 14.76

ANISOU 1655 C GLY 236 1931 1332 2346 252 73 2 8 8

ATOM 1656 O GLY 236 23.778 8.244 43.373 1.000 18.32

ANISOU 1656 O GLY 236 1983 2197 2782 106 -105 84

ATOM 1657 N GLN 237 23.318 9.938 41.953 1.000 13 .99

ANISOU 1657 N GLN 237 1831 1349 2137 158 165 17

ATOM 1658 CA GLN 237 24.209 10.956 42.485 1.000 13.13

ANISOU 1658 CA GLN 237 1474 1304 2210 367 -31 2 7

ATOM 1659 CB GLN 237 24.629 11.948 41.383 1.000 13 .38

ANISOU 1659 CB GLN 237 1367 1566 2151 99 72 159

ATOM 1660 CG GLN 237 25.390 11.335 40.219 1.000 14.74

ANISOU 1660 CG GLN 237 1404 1529 2666 518 410 3 3

ATOM 1661 CD GLN 237 25.816 12.428 39.257 1.000 17.22

ANISOU 1661 CD GLN 237 2039 2018 2486 -64 426 3 6

ATOM 1662 OEl GLN 237 26.754 13.208 39.522 1.000 20.60

ANISOU 1662 OEl GLN 237 1566 2334 3928 -10 -29 9 6

ATOM 1663 NE2 GLN 237 25.116 12.470 38.127 1.000 17.47

ANISOU 1663 NE2 GLN 237 2014 2093 2533 208 438 4 0

ATOM 1664 C GLN 237 23.627 11.739 43.663 1.000 12.90

ANISOU 1664 C GLN 237 1474 1324 2104 72 -10 2 5 5

ATOM 1665 O GLN 237 24.332 12.549 44.282 1.000 15.90

ANISOU 1665 O GLN 237 1739 1888 2413 -291 74 - 84

ATOM 1666 N VAL 238 22.365 11.481 44.013 1.000 12.13

ANISOU 1666 N VAL 238 1372 962 2276 212 -33 2 0 0

ATOM 1667 CA VAL 238 21.664 12.182 45.082 1.000 11.91

ANISOU 1667 CA VAL 238 1169 1436 1920 -121 -276 - 1

ATOM 1668 CB VAL 238 20.622 13.158 44.510 1.000 12.00

ANISOU 1668 CB VAL 238 1024 1179 2357 -6 199 - 3 1

ATOM 1669 CGI VAL 238 19.978 13.999 45.601 1.000 13.07

ANISOU 1669 CGI VAL 238 1530 1668 1767 63 -232 - 22

ATOM 1670 CG2 VAL 238 21.207 14.088 43.463 1.000 14.00

ANISOU 1670 CG2 VAL 238 1795 1470 2053 -40 -2 181

ATOM 1671 C VAL 238 20.990 11.156 46.000 1.000 13 .62

ANISOU 1671 C VAL 238 1707 1415 2054 -103 -40 - 2

ATOM 1672 O VAL 238 20.252 10.288 45.492 1.000 12.64

ANISOU 1672 O VAL 238 1702 977 2123 60 -318 2 57

ATOM 1673 N LYS 239 21.247 11.246 47.300 1.000 11.99

ANISOU 1673 N LYS 239 1075 1404 2076 127 -1017

ATOM 1674 CA LYS 239 20.568 10.444 48.322 1.000 12.77

ANISOU 1674 CA LYS 239 1224 1541 2088 -12 -124 8

ATOM 1675 CB LYS 239 21.382 10.463 49.622 1.000 - 12.23

ANISOU 1675 CB LYS 239 1333 1155 2158 183 -234 - 2 8

ATOM 1676 CG LYS 239 20.953 9.626 50.793 1.00C i 13.85

ANISOU 1676 CG LYS 239 1643 1689 1931 187 -52 - - 8. 9

ATOM 1677 CD LYS 239 21.927 9.579 51.957 1.00C ) 20.13

ANISOU ^' 1677 CD LYS 239 2893 1795 2961 10 -1185 5 8 8

ATOM 1678 CE LYS 239 21.364 8.745 53.098 1.00C ) 24.73 ANISOU 1678 CE LYS 239 4065 2250 3030 -348 -1466 1064

ATOM 1679 NZ LYS 239 22.019 8.841 54.420 1.000 32.28

ANISOU 1679 NZ LYS 239 5658 4315 2293 1610 -930 - 304

ATOM 1680 C LYS 239 19.169 10.949 48.661 1.000 11.59

ANISOU 1680 C LYS 239 1207 1332 1866 -35 -82 6 4

ATOM 1681 0 LYS 239 18.976 12.191 48.708 1.000 12.32

ANISOU 1681 0 LYS 239 1638 1294 1749 -2 -25 2 3 6

ATOM 1682 N ALA 240 18.222 10.047 48.863 1.000 10.65

ANISOU 1682 N ALA 240 1248 1266 1534 -52 -185 - 8 8

ATOM 1683 C ALA 240 16.884 10.368 49.354 1.000 10.21

ANISOU 1683 CA ALA 240 1292 1057 1531 -195 -37 - 109

ATOM 1684 CB ALA 240 15.784 9.782 48.466 1.000 13 .46

ANISOU 1684 CB ALA 240 1195 2378 1543 -232 20 - 403

ATOM 1685 C ALA 240 16.784 9.881 50.807 1.000 10.97

ANISOU 1685 C ALA 240 1308 1249 1611 -127 -142 4 9

ATOM 1686 O ALA 240 16.595 8.664 51.059 1.000 13 .02

ANISOU 1686 O ALA 240 2136 1242 1568 -243 28 - 7

ATOM 1687 N PRO 241 16.967 10.783 51.782 1.000 11.13

ANISOU 1687 N PRO 241 1723 1041 1466 160 -49 13 8

ATOM 1688 CD PRO 241 17.172 12.237 51.654 1.000 11.17

ANISOU 1688 CD PRO 241 1419 1204 1618 -180 -128 7 6

ATOM 1689 CA PRO 241 17.043 10.340 53.166 1.000 11.96

ANISOU 1689 CA PRO 241 1597 1447 1499 -172 -32 193

ATOM 1690 CB PRO 241 17.712 11.545 53.891 1.000 14.25

ANISOU 1690 CB PRO 241 1875 1837 1701 -531 -383 242

ATOM 1691 CG PRO 241 17.286 12.724 53.069 1.000 13.61

ANISOU 1691 CG PRO 241 2015 1446 1709 -596 -465 - 22

ATOM 1692 C PRO 241 15.708 10.072 53.861 1.000 12.35

ANISOU 1692 C PRO 241 1417 1610 1665 -175 -187 418

ATOM 1693 O PRO 241 14.759 10.829 53.655 1.000 12.28

ANISOU 1693 O PRO 241 1359 1582 1723 -232 -468 8 1

ATOM 1694 N ARG 242 15.700 9.033 54.711 1.000 12.75

ANISOU 1694 N ARG 242 1775 1407 1664 -170 76 2 5 0

ATOM 1695 CA ARG 242 14.563 8.804 55.576 1.000 10.76

ANISOU 1695 CA ARG 242 1292 1417 1380 -207 -281 211

ATOM 1696 CB ARG 242 14.614 7.405 56.223 1.000 15.02

ANISOU 1696 CB ARG 242 2419 1368 1918 -357 117 2 94

ATOM 1697 CG ARG 242 14.115 6.342 55.230 1.000 17.85

ANISOU 1697 CG ARG 242 3373 1274 2135 9 -560 251

ATOM 1698 CD ARG 242 14.254 4.934 55.763 1.000 19.42

ANISOU 1698 CD ARG 242 3148 1111 3120 506 503 1 1 6

ATOM 1699 NE ARG 242 15.667 4.552 55.849 1.000 20.71

ANISOU 1699 NE ARG 242 3225 2107 2538 938 638 2 12

ATOM 1700 CZ ARG 242 16.107 3.444 56.416 1.000 23.22

ANISOU 1700 CZ ARG 242 3198 2206 3417 307 -544 589

ATOM 1701 NHl ARG 242 15.285 2.567 56.980 1.000 24.46

ANISOU 1701 NHl ARG 242 4097 2112 3083 307 387 19 5

ATOM 1702 NH2 ARG 242 17.416 3.184 56.438 1.000 25.41

ANISOU 1702 NH2 ARG 242 3402 2332 3921 819 -267 4 03

ATOM 1703 C ARG 242 14.477 9.834 56.704 1.000 11.95

ANISOU 1703 C ARG 242 1571 1463 1506 -248 -214 107

ATOM 1704 O ARG 242 15.469 10.377 57.213 1.000 13.65

ANISOU 1704 O ARG 242 1708 1439 2040 -322 -401 - 3 8

ATOM 1705 N HIS 243 13.252 10.085 57.118 1.000 11.60

ANISOU 1705 N HIS 243 1657 1410 1342 -311 -206 5

ATOM 1706 CA HIS 243 12.942 11.056 58.158 1.000 11.49

ANISOU 1706 CA HIS 243 1855 1571 938 -306 -183 14 0

ATOM 1707 CB HIS 243 12.968 12.462 57.546 1.000 11.22

ANISOU 1707 CB HIS 243 1432 1379 1453 -231 -221 3 9

ATOM 1708 CG HIS 243 12.133 12.694 56.341 1.000 11.80

ANISOU 1708 CG HIS 243 1937 1171 1378 -31 -268 7 9 ATOM 1709 CD2 HIS 243 10.885 13.236 56.181 1.000 11.15

ANISOU 1709 CD2 HIS 243 1990 1106 1142 35 -344 14 1

ATOM 1710 NDl HIS 243 12.538 12.345 55.086 1.000 12.29

ANISOU 1710 NDl HIS 243 1670 1606 1395 -394 -91 8

ATOM 1711 CEl HIS 243 11.599 12.653 54.209 1.000 12 .59

ANISOU 1711 CEl HIS 243 1686 1740 1357 -522 -202 - 253

ATOM 1712 NE2 HIS 243 10.585 13.204 54.841 1.000 10.77

ANISOU 1712 NE2 HIS 243 1612 1307 1172 -616 -268 - 3 6

ATOM 1713 C HIS 243 11.605 10.737 58.812 1.000 12.49

ANISOU 1713 C HIS 243 1869 1570 1308 -321 -53 7 3

ATOM 1714 0 HIS 243 10.807 9.949 58.271 1.000 12 .26

ANISOU 1714 0 HIS 243 1756 1404 1497 -188 -115 4 7

ATOM 1715 N HIS 244 11.352 11.319 59.983 1.000 12 .16

ANISOU 1715 N HIS 244 1464 1715 1442 -230 -112 - 3 2

ATOM 1716 CA HIS 244 10.138 11.043 60.758 1.000 12.02

ANISOU 1716 CA HIS 244 1606 1809 1152 -599 -167 - 2 4

ATOM 1717 CB HIS 244 10.255 9.778 61.615 1.000 12.51

ANISOU 1717 CB HIS 244 1655 1763 1334 -19 101 - 47

ATOM 1718 CG HIS 244 11.270 9.810 62.698 1.000 15 .04

ANISOU 1718 CG HIS 244 2025 1723 1965 -178 -433 1 54

ATOM 1719 CD2 HIS 244 11.276 10.380 63.923 1.000 18.19

ANISOU 1719 CD2 HIS 244 2946 2339 1627 36 -732 2 9 7

ATOM 1720 NDl HIS 244 12.504 9.203 62.662 1.000 19.30

ANISOU 1720 NDl HIS 244 2303 2232 2800 229 -708 2 6 6

ATOM 1721 CEl HIS 244 13.226 9.387 63.731 1.000 22.48

ANISOU 1721 CEl HIS 244 2649 2734 3159 11 -1206 6 5 0

ATOM 1722 NE2 HIS 244 12.476 10.120 64.531 1.000 22.33

ANISOU 1722 NE2 HIS 244 3088 2895 2500 -272 -1236 3 84

ATOM 1723 C HIS 244 9.780 12.246 61.613 1.000 13 .47

ANISOU 1723 C HIS 244 1897 1673 1549 -362 254 6 7

ATOM 1724 O HIS 244 10.603 13.165 61.798 1.000 13.48

ANISOU 1724 O HIS 244 1800 1726 1595 -283 139 - 161

ATOM 1725 N VAL 245 8.551 12.245 62.130 1.000 15.26

ANISOU 1725 N VAL 245 1852 1964 1983 -417 232 - 5 5

ATOM 1726 CA VAL 245 8.090 13.352 62.970 1.000 17.31

ANISOU 1726 CA VAL 245 2108 2442 2026 -125 476 - 161

ATOM 1727 CB VAL 245 6.939 14.169 62.360 1.000 17.33

ANISOU 1727 CB VAL 245 2094 2473 2019 -80 340 - 477

ATOM 1728 CGI VAL 245 6.551 15.334 63.286 1.000 25.25

ANISOU 1728 CGI VAL 245 2217 2966 4410 -137 1939 -124:

ATOM 1729 CG2 VAL 245 7.252 14.713 60.966 1.000 21.49

ANISOU 1729 CG2 VAL 245 3070 2538 2556 -180 313 27 1

ATOM 1730 C VAL 245 7.682 12.768 64.327 1.000 18.29

ANISOU 1730 C VAL 245 2123 2689 2137 -443 508 - 7 1

ATOM 1731 O VAL 245 6.765 11.945 64.429 1.000 18.62

ANISOU 1731 O VAL 245 1810 2174 3089 -15 451 2 54

ATOM 1732 N ALA 246 8.385 13.202 65.369 1.000 21.54

ANISOU 1732 N ALA 246 2813 3045 2327 -591 -407 9 07

ATOM 1733 CA ALA 246 8.133 12.701 66.719 1.000 25.10

ANISOU 1733 CA ALA 246 4596 2562 2379 94 -225 9 9 7

ATOM 1734 CB ALA 246 9.424 12.723 67.537 1.000 29.82

ANISOU 1734 CB ALA 246 5381 3408 2540 402 -889 1325

ATOM 1735 C ALA 246 7.080 13.545 67.412 1.000 31.20

ANISOU 1735 C ALA 246 5079 4143 2632 314 280 42 8

ATOM 1736 O ALA 246 6.876 14.714 67.052 1.000 32.39

ANISOU 1736 O ALA 246 4706 3748 3853 567 1247 - 6 6

ATOM 1737 N ALA 247 6.429 12.973 68.413 1.00C 1 37.30

ANISOU ^' 1737 N ALA 247 5548 5498 3126 92 640 83 5

ATOM 1738 CA ALA 247 5.585 13.794 69.271 1.00C ) 4Q .42

ANISOU J 1738 CA ALA 247 5434 6048 3878 15 1313 8 5 0

ATOM 1739 C ALA 247 6.289 14.132 70.578 1.00C ) 42.17 _

-147-

ANISOU- 1739 C ALA 247 6495 5891 3636 -823 1720 341

ATOM 1740 O ALA 247 7.048 13.338 71.136 1.000 41.63

ANISOU 1740 0 ALA 247 5811 6371 3637 -1631 804 425

ATOM 1741 CB ALA 247 4.280 13.067 69.525 1.000 47.17

ANISOU 1741 CB ALA 247 5186 9059 3676 -520 523 2683

ATOM 1742 N SER 257 1.781 21.848 70.382 1.000 31.02

ANISOU 1742 N SER 257 4109 5558 2119 137 -235 - 810

ATOM 1743 CA SER 257 1.214 21.932 69.052 1.000 27.01

ANISOU 1743 CA SER 257 2792 5165 2304 109 -143 - 707

ATOM 1744 CB SER 257 0.039 22.914 68.992 1.000 28.16

ANISOU- 1744 CB SER 257 2655 4473 3572 -238 -90 - 1071

ATOM 1745 OG SER 257 0.491 24.251 69.074 1.000 51.32

ANISOU 1745 OG SER 257 8516 4131 6853 -616 -2734 - 807

ATOM 1746 C SER 257 2.259 22.389 68.034 1.000 26.19

ANISOU- 1746 C SER 257 2537 5064 235.0 -132 -413 - 527

ATOM 1747 0 SER 257 3.286 22.988 68.352 1.000 31.47

ANISOU 1747 0 SER 257 2740 5886 3330 -435 -689 - 639

ATOM 1748 N ARG 258 2.022 22.123 66.763 1.000 26.04

ANISOU 1748 N ARG 258 3257 4477 2161 -238 -441 - 19

ATOM 1749 CA ARG 258 2.982 22.541 65.747 1.000 25.81

ANISOU 1749 CA ARG 258 2606 4735 2466 73 -338 - 197

ATOM 1750 C ARG 258 2.321 22.609 64.383 1.000 18.26

ANISOU 1750 C ARG 258 2374 2541 2021 39 83 - 854

ATOM 1751 O ARG 258 1.288 21.967 64.131 1.000 19.23

ANISOU 1751 O ARG 258 2600 2819 1888 -389 311 - 420

ATOM 1752 CB ARG 258 4.188 21.592 65.664 1.000 29.78

ANISOU 1752 CB ARG 258 3403 5052 2861 695 -552 - 57

ATOM 1753 CG ARG 258 4.246 20.784 64.384 1.000 32.64

ANISOU 1753 CG ARG 258 4358 4148 3896 146 97 - 561

ATOM 1754 CD ARG 258 5.325 19.746 64.499 1.000 30.38

ANISOU 1754 CD ARG 258 3812 4423 3309 -57 341 - 16

ATOM 1755 NE ARG 258 6.433 19.909 63.581 1.000 29.43

ANISOU 1755 NE ARG 258 3990 4604 2588 -22 70 542

ATOM 1756 CZ ARG 258 6.453 19.389 62.359 1.000 25.02

ANISOU 1756 CZ ARG 258 2540 3893 3074 304 -243 104

ATOM 1757 NHl ARG 258 5.456 18.677 61.835 1.000 22.88

ANISOU 1757 NHl ARG 258 2105 2607 3982 359 315 289

ATOM 1758 NH2 ARG 258 7.523 19.593 61.617 1.000 22.03

ANISOU 1758 NH2 ARG 258 2477 2775 3120 -430 -287 - 964

ATOM 1759 N THR 259 2.927 23.415 63.527 1.000 20.17

ANISOU 1759 N THR 259 2010 3640 2013 -743 91 -1001

ATOM 1760 CA THR 259 2.485 23.505 62.138 1.000 18.33

ANISOU 1760 CA THR 259 1801 3043 2121 -533 43 - 685

ATOM 1761 CB THR 259 1.821 24.821 61.713 1.000 23.23

ANISOU 1761 CB THR 259 2082 3169 3576 -384 -164 - 580

ATOM 1762 OGl THR 259 2.839 25.830 61.681 1.000 34.27

ANISOU 1762 OGl THR 259 2181 2562 8277 -137 -996 - 794

ATOM 1763 CG2 THR 259 0.738 25.198 62.704 1.000 25.49

ANISOU 1763 CG2 THR 259 4466 2233 2987 325 396 - 948

ATOM 1764 C THR 259 3.702 23.352 61.222 1.000 18.44

ANISOU 1764 C THR 259 2035 2822 2150 -753 274 - 583

ATOM 1765 O THR 259 4.835 23.698 61.603 1.000 24.74

ANISOU 1765 O THR 259 1961 5370 2069 -964 231 - 714

ATOM 1766 N SER 260 3.420 22.867 60.026 1.000 16.29

ANISOU 1766 N SER 260 1971 2352 1864 -224 2 - 75

ATOM 1767 CA SER 260 4.447 22.832 58.989 1.000ι 17.43

ANISOU 1767 CA SER 260 1783 2961 1879 321 -95 - 72

ATOM 1768 CB SER 260 5.224 21.514 58.956 1.00C 120.17

ANISOU ^' 1768 CB SER 260 2306 3257 2100 762 -127 388

ATOM 1769 OG SER 260 4.416 20.392 58.698 1.00C ) 27.09

ANISOU ^• 1769 OG SER 260 3651 2803 3839 426 217 554 ATOM 1770 C SER 260 3.832 23.062 57.614 1.000 14.52

ANISOU 1770 C SER 260 1463 2165 1889 83 -100 - 1

ATOM 1771 O SER 260 2.686 22.681 57.402 1.000 15.92

ANISOU 1771 O SER 260 1513 2489 2049 -93 -1 2 5 7

ATOM 1772 N SER 261 4.617 23.660 56.742 1.000 13 .45

ANISOU 1772 N SER 261 1489 1832 1788 -190 -120 - 500

ATOM 1773 CA SER 261 4.294 23.864 55.334 1.000 13 .52

ANISOU 1773 CA SER 261 1599 1726 1812 -204 30 - 315

ATOM 1774 C SER 261 5.209 22.943 54.545 1.000 12.45

ANISOU 1774 C SER 261 1332 18! 7 1513 -42 -240 - 161

ATOM 1775 O SER 261 6.438 23 072 54.662 1.000 15.07

ANISOU 1775 O SER 261 1344 18! 5 2497 -68 -331 - 343

ATOM 1776 CB SER 261 4.446 25 330 54.943 1.000 17.76

ANISOU 1776 CB SER 261 2718 1625 2404 -399 -485 - 318

ATOM 1777 OG SER 261 4.428 25.554 53.570 1.000 27.54

ANISOU 1777 OG SER 261 4342 3308 2814 -719 -821 9 5 5

ATOM 1778 N VAL 262 4.623 22.045 53.782 1.000 10.90

ANISOU 1778 N VAL 262 1215 1630 1299 41 -135 1 9

ATOM 1779 CA VAL 262 5.393 21.031 53.026 1.000 11.61

ANISOU 1779 CA VAL 262 1334 1634 1442 156 -103 1 7

ATOM 1780 CB VAL 262 5.026 19.639 53.55! 1.000 11.87

ANISOU 1780 CB VAL 262 1262 1636 1614 9 -187 - 7 4

ATOM 1781 CGI VAL 262 5.778 18.577 52.779 1.000 13 .12

ANISOU 1781 CGI VAL 262 1462 1527 1997 -2 185 5 1

ATOM 1782 CG2 VAL 262 5.262 19.564 55.062 1.000 17.08

ANISOU 1782 CG2 VAL 262 3390 1494 1604 -374 -245 3 9

ATOM 1783 C VAL 262 5.096 21.149 51.543 1.000 11.18

ANISOU 1783 C VAL 262 1026 1790 1431 1 -111 - 138

ATOM 1784 O VAL 262 3.939 20.969 51.127 1.000 12.76

ANISOU 1784 O VAL 262 1064 2137 1648 -251 -84 -271

ATOM 1785 N PHE 263 6.090 21.438 50.714 1.000 9 .50

ANISOU 1785 N PHE 263 995 1297 1316 -6 -210 - 181

ATOM 1786 CA PHE 263 5.933 21.637 49.288 1.000 9 . 61

ANISOU 1786 CA PHE 263 1310 1017 1324 -6 -284 - 42

ATOM 1787 CB PHE 263 6.486 23.002 48.848 1.000 10.94

ANISOU 1787 CB PHE 263 1282 1055 1821 -50 -253 4

ATOM 1788 CG PHE 263 6.150 23.399 47.418 1.000 10.35

ANISOU 1788 CG PHE 263 779 1231 1921 -58 32 34 0

ATOM 1789 CDI PHE 263 6.858 22.915 46.326 1.000 9 . 98

ANISOU 1789 CDI PHE 263 766 1181 1841 -26 -101 2 4 0

ATOM 1790 CD2 PHE 263 5.106 24.277 47.148 1.000 11.95

ANISOU 1790 CD2 PHE 263 1229 1261 2052 245 -29 2 61

ATOM 1791 CEl PHE 263 6.530 23.229 45.019 1.000 12.49

ANISOU 1791 CEl PHE 263 1718 1173 1857 31 -370 13 6

ATOM 1792 CE2 PHE 263 4.769 24.601 45.836 1.000 13 .12

ANISOU 1792 CE2 PHE 263 1451 1382 2151 43 -292 3 53

ATOM 1793 CZ PHE 263 5.491 24.112 44.762 1.000 12.42

ANISOU 1793 CZ PHE 263 1318 1453 1948 -138 -187 649

ATOM 1794 C PHE 263 6.636 20.505 48.530 1.000 8 . 91

ANISOU 1794 c PHE 263 1076 1085 1223 -39 -142 2 4

ATOM 1795 0 PHE 263 7.868 20.406 48.538 1.000 10.98

ANISOU 1795 0 PHE 263 1098 1233 1842 -120 -224 - 145

ATOM 1796 N PHE 264 5.856 19.691 47.812 1.000 9 .19

ANISOU 1796 N PHE 264 1089 1266 1136 -86 -105 - 82

ATOM 1797 CA PHE 264 6.386 18.602 46.991 1.000 9 . 64

ANISOU 1797 CA PHE 264 1009 1238 1417 -56 -60 - 126

ATOM 1798 CB PHE 264 5.483 17.358 47.005 1.000 9 . 92

ANISOU 1798 CB PHE 264 1209 1201 1359 -78 17 9

ATOM 1799 CG PHE 264 5.265 16.673 48.336 1.000 11.22

ANISOU 1799 CG PHE 264 1241 1647 1374 -121 38 7 7

ATOM 1800 CDI PHE 264 6.292 16.236 49.139 1.000 15 .38 -149-

ANISOU 1800 CDI PHE 264 1467 2641 1734 -225 -8 873

ATOM 1801 CD2 PHE 264 3.988 16.433 48.808 1.000 16.96

ANISOU 1801 CD2 PHE 264 1425 3252 1769 -610 -79 9 5 8

ATOM 1802 CEl PHE 264 6.090 15.596 50.336 1.000 14.52

ANISOU 1802 CEl PHE 264 1745 2417 1354 162 334 4 52

ATOM 1803 CE2 PHE 264 3.755 15.796 50.019 1.000 18.04

ANISOU 1803 CE2 PHE 264 1747 3405 1704 -590 -109 100

ATOM 1804 CZ PHE 264 4.817 15.354 50.779 1.000 12.52

ANISOU 1804 CZ PHE 264 1772 1536 1449 -57 227 3 3 4

ATOM 1805 C PHE 264 6.535 19.038 45.533 1.000 8 . 98

ANISOU 1805 C PHE 264 1103 919 1392 143 ι 81 - 92

ATOM 1806 O PHE 264 5.497 19.368 44.930 1.000 9 .79

ANISOU 1806 O PHE 264 991 1190 1540 28 105 1 03

ATOM 1807 N LEU 265 7.758 19.031 44.999 1.000 8 .43

ANISOU 1807 N LEU 265 992 884 1325 173 -180 1 5 8

ATOM 1808 CA LEU 265 7.984 19.224 43.566 1.000 8 . 66

ANISOU 1808 CA LEU 265 883 1066 1339 63 -33 - 7 6

ATOM 1809 CB LEU 265 9.309 19.964 43.328 1.000 10.10

ANISOU 1809 CB LEU 265 1179 1188 1469 -225 -220 248

ATOM 1810 CG LEU 265 9.570 20.351 41.871 1.000 9 .37

ANISOU 1810 CG LEU 265 1072 1009 1478 242 25 129

ATOM 1811 CDI LEU 265 8.725 21.522 41.408 1.000 10.80

ANISOU 1811 CDI LEU 265 1291 1004 1811 181 -114 29 6

ATOM 1812 CD2 LEU 265 11.048 20.684 41.678 1.000 10.87

ANISOU 1812 CD2 LEU 265 1129 1483 1519 134 43 14 6

ATOM 1813 C LEU 265 7.933 17.849 42.875 1.000 10.21

ANISOU 1813 C LEU 265 932 1188 1760 -6 -38 - 302

ATOM 1814 O LEU 265 8.858 17.043 43.042 1.000 10.45

ANISOU 1814 O LEU 265 1388 969 1612 84 -217 1 07

ATOM 1815 N ARG 266 6.853 17.530 42.135 1.000 10.00

ANISOU 1815 N ARG 266 1325 1069 1404 -120 -222 1 5

ATOM 1816 CA ARG 266 6.572 16.198 41.628 1.000 10.50

ANISOU 1816 CA ARG 266 1219 1217 1554 -294 110 -21

ATOM 1817 CB ARG 266 5.208 15.675 42.124 1.000 10.56

ANISOU 1817 CB ARG 266 978 1460 1574 -168 -103 - 105

ATOM 1818 CG ARG 266 4.965 15.894 43.609 1.000 11.24

ANISOU 1818 CG ARG 266 1337 1373 1563 -40 119 2 0 f

ATOM 1819 CD ARG 266 3.668 15.318 44.146 1.000 11.17

ANISOU 1819 CD ARG 266 1113 1567 1564 -17 -49 - 1 :

ATOM 1820 NE ARG 266 2.508 15.879 43.447 1.000 9 .43

ANISOU 1820 NE ARG 266 1341 1157 1086 24 -100 - 145

ATOM 1821 CZ ARG 266 1.236 15.509 43.657 1.000 9 .83

ANISOU 1821 CZ ARG 266 1245 1194 1294 132 -159 - 1

ATOM 1822 NHl ARG 266 0.961 14.567 44.572 1.000 11.20

ANISOU 1822 NHl ARG 266 1208 1240 1806 -144 -454 27 :

ATOM 1823 NH2 ARG 266 0.225 16.048 42.975 1.000 11.08

ANISOU 1823 NH2 ARG 266 1460 1265 1484 191 -283 7 3

ATOM 1824 C ARG 266 6.601 16.190 40.099 1.000 10.28

ANISOU 1824 C ARG 266 1273 1089 1545 -200 -5 - 167

ATOM 1825 O ARG 266 6.027 17.109 39.519 1.000 11.05

ANISOU 1825 O ARG 266 1254 1153 1793 -132 47 - 64

ATOM 1826 N PRO 267 7.215 15.162 39.496 1.000 10.27

ANISOU 1826 N PRO 267 1194 1239 1468 -33 130 3 2

ATOM 1827 CD PRO 267 7.828 13.963 40.109 1.000 ι 12.36

ANISOU 1827 CD PRO 267 1865 1132 1697 -26 -529 - 1 ! 92

ATOM 1828 CA PRO 267 7.304 15.157 38.036 1.00C I 10.12

ANISOU 1828 CA PRO 267 1278 1095 1472 -129 38 - 185

ATOM 1829 CB PRO 267 8.250 13.986 37.767 1.00C ) 11.83

ANISOU 1829 CB PRO 267 1489 1088 1919 -72 90 - 322

ATOM 1830 CG PRO 267 8.017 13.053 38.913 1. OOC ) 10.72

ANISOU 1830 CG PRO 267 960 1356 1755 95 ι -257 - 187 ATOM 1831 C PRO 267 5.977 14.929 37.344 1.000 10.86

ANISOU 1831 C PRO 267 1330 1226 1570 -252 47 - 161

ATOM 1832 0 PRO 267 5.030 14.421 37.934 1.000 12.03

ANISOU 1832 0 PRO 267 1316 1174 2080 -258 17 7 7

ATOM 1 33 N ASN 268 5.931 15.288 36.065 1.000 10.61

ANISOU 1833 N ASN 268 1216 1146 1670 -70 -86 - 129

ATOM 1834 CA ASN 268 4.810 14.949 35.198 1.000 11.20

ANISOU 1834 CA ASN 268 1285 1349 1622 -167 -43 - 229

ATOM 1835 CB ASN 268 4.954 15.664 33.846 1.000 14.02

ANISOU 1835 CB ASN 268 2160 1410 1756 132 -316 2 3

ATOM 1836 CG ASN 268 4.992 17.175 33.992 1.000 13.03

ANISOU 1836 CG ASN 268 1811 1393 1747 189 -355 - 8 8

ATOM 1837 ODl ASN 268 4.046 17.748 34.566 1.000 16.65

ANISOU 1837 ODl ASN 268 1910 1744 2673 292 -1 - 159

ATOM 1838 ND2 ASN 268 6.037 17.818 33.495 1.000 14.19

ANISOU 1838 ND2 ASN 268 2505 1372 1516 161 264 - 172

ATOM 1839 C ASN 268 4.705 13.446 34.968 1.000 10.88

ANISOU 1839 C ASN 268 1294 1314 1526 -75 -226 - 164

ATOM 1840 0 ASN 268 5.715 12.732 34.979 1.000 11.68

ANISOU 1840 0 ASN 268 1534 1439 1464 87 -458 - 121

ATOM 1841 N ALA 269 3.484 12.980 34.688 1.000 12.22

ANISOU 1841 N ALA 269 1484 1428 1732 -108 -397 - 427

ATOM 1842 CA ALA 269 3.277 11.547 34.417 1.000 12.12

ANISOU 1842 CA ALA 269 1432 1356 1819 -238 -29 - 282

ATOM 1843 CB ALA 269 1.817 11.310 34.058 1.000 12 .38

ANISOU 1843 CB ALA 269 1439 1278 1985 -228 -183 2 9

ATOM 1844 C ALA 269 4.125 10.981 33.283 1.000 11.26

ANISOU 1844 C ALA 269 1445 1240 1592 25 -280 - 141

ATOM 1845 0 ALA 269 4.493 9.800 33.263 1.000 12.53

ANISOU 1845 0 ALA 269 1428 1249 2085 -110 108 - 188

ATOM 1846 N ASP 270 4.438 11.799 32.276 1.000 11.47

ANISOU 1846 N ASP 270 1701 1280 1378 -261 -341 - 300

ATOM 1847 CA ASP 270 5.214 11.378 31.113 1.000 11.92

ANISOU 1847 CA ASP 270 1826 1106 1595 19 -183 - 156

ATOM 1848 CB ASP 270 4.760 12.096 29.850 1.000 14.13

ANISOU 18 48 CB ASP 270 1733 2038 1597 84 111 2 12

ATOM 49 CG ASP 270 5.050 13.568 29.777 1.000 15.98

ANISOU 49 CG ASP 270 2309 1939 1823 418 -418 5 64

ATOM 50 ODl ASP 270 5.432 14.186 30.762 1.000 21.61

ANISOU 50 ODl ASP 270 4101 1797 2312 176 -515 1 63

ATOM 51 OD2 ASP 270 4.880 14.152 28.674 1.000 24.64

ANISOU 51 OD2 ASP 270 3995 3221 2145 -62 -169 1395

ATOM 52 C ASP 270 6.721 11.542 31.264 1.000 12.86

ANISOU 52 C ASP 270 1840 1392 1654 -398 -61 3 15

ATOM 53 0 ASP 270 7.443 11.290 30.292 1.000 14.83

ANISOU 53 0 ASP 270 1813 2114 1709 -346 -141 4 9

ATOM 54 N PHE 271 7.230 11.911 32.439 1.000 11.85

ANISOU 54 N PHE 271 1360 1316 1824 59 -25 7 0

ATOM 55 CA PHE 271 8.665 11.927 32.715 1.000 11.14

ANISOU 55 CA PHE 271 1242 1349 1641 10 230 162

ATOM 56 CB PHE 271 8.972 12.378 34.143 1.000 12.19

ANISOU 856 CB PHE 271 1467 1444 1722 -96 -3 1 8 2

ATOM 57 CG PHE 271 10.385 11.992 34.597 1.000 12.77

ANISOU 857 CG PHE 271 1411 1640 1800 42 31 5 6

ATOM 858 CDI PHE 271 11.475 12.488 33.904 1.000 13 .22

ANISOU 858 CDI PHE 271 1513 1516 1993 168 220 4 9

ATOM 859 CD2 PHE 271 10.624 11.155 35.666 1.000 13.55

ANISOU 859 CD2 PHE 271 1343 1674 2131 139 84 2 5 5

ATOM 860 CEl PHE 271 12.779 12.178 34.249 1.000 14.26

ANISOU 860 CEl PHE 271 1432 1760 2225 -39 46 - 416

ATOM 861 CE2 PHE 271 11.925 10.806 36.019 1.000 15.88 ANISOU 1, 61 CE2 PHE 271 1537 1818 2679 -263 -675 2 6 0 ATOM 1, 62 CZ PHE 271 13.006 11.288 35.304 1.000 14.15 ANISOU 1. 62 CZ PHE 271 1166 1736 2475 7 -531 - 467 ATOM IE 63 C PHE 271 9.259 10.550 32.410 1.000 11.27 ANISOU 1. 63 C PHE 271 1359 1338 1585 75 271 3 48 ATOM IE 64 0 PHE 271 8.785 9.531 32.920 1.000 12 . 97 ANISOU- IE 64 0 PHE 271 2011 1320 1596 -85 473 2 7 ATOM IE 65 N THR 272 10.261 10.498 31.541 1.000 11.95 ANISOU IE 65 N THR 272 1018 1503 2020 -214 300 - 1 15 ATOM IE 66 CA THR 272 10.823 9.254 30.992 1.000 12.70 ANISOU IE 66 CA THR 272 1615 1557 1652 132 341 1 4 ATOM IE 67 CB THR 272 10.679 9.281 29.450 1.000 16.79 ANISOU IE 67 CB THR 272 1814 2829 1737 -595 157 - 4 06 ATOM IS 68 OGl THR 272 9.301 9.471 29.090 1.000 18 .02 ANISOU 1! 68 OGl THR 272 1912 2921 2013 -497 -73 9 1 ATOM 1! 69 CG2 THR 272 11.200 7.976 28.856 1.000 17.02 ANISOU 1! 69 CG2 THR 272 2144 2857 1467 -475 538 - 1 94 ATOM 1! 70 C THR 272 12.272 9.057 31.423 1.000 12 .02 ANISOU 1! 70 C THR 272 1436 1573 1559 92 603 13 7 ATOM 1! 71 0 THR 272 13.055 10.031 31.437 1.000 14.17 ANISOU 1! 71 0 THR 272 1451 1583 2351 125 602 4 12 ATOM 1 72 N PHE 273 12.625 7.837 31.828 1.000 12 .34 ANISOU 1 72 N PHE 273 1402 1585 1703 17 378 15 ATOM 1 73 CA PHE 273 13.953 7.492 32.312 1.000 12 . 20 ANISOU 1 73 CA PHE 273 1362 1364 1909 -126 336 1 47 ATOM 1 ;74 CB PHE 273 13.951 7.514 33.861 1.000 12 . 37 ANISOU 1 :74 CB PHE 273 1362 1447 1890 -102 211 ATOM 1 :75 CG PHE 273 12.988 6.528 34.491 1.000 11. 65 ANISOU 1 175 CG PHE 273 1398 1631 1396 -367 42 - 215 ATOM 1 176 CDI PHE 273 11.684 6.889 34.773 1.000 14.11 ANISOU 1 !76 CDI PHE 273 1531 2214 1614 -336 293 - 62 ATOM 1 !77 CD2 PHE 273 13.409 5.245 34.803 1.000 13.20 ANISOU 1 !77 CD2 PHE 273 2024 1639 1352 -358 339 - 9 ATOM 1 !78 CEl PHE 273 10.793 5.993 35.323 1.000 13. 25 ANISOU 1 178 CEl PHE 273 1536 2081 1418 -98 447 4 2 ATOM 1 !79 CE2 PHE 273 12.530 4.329 35.327 1.000 13 . 39 ANISOU 1 .79 CE2 PHE 273 1529 1905 1654 -224 140 2 83 ATOM 1 .80 CZ PHE 273 11.227 4.706 35.604 1.000 14.75 ANISOU 1 -80 CZ PHE 273 1444 2260 1902 -90 -186 2 1 5 ATOM 1 81 PHE 273 14.423 6.135 31.795 1.000 12.45 ANISOU 1 ;8l PHE 273 1278 1526 1927 -120 317 - 3 1 ATOM 1 882 0 PHE 273 13.645 5.311 31.291 1.000 11. 95 ANISOU 1 882 0 PHE 273 1590 1580 1370 -137 226 13 ATOM 1 883 N SER 274 15.717 5.854 31.952 1.000 12 , 07 ANISOU 1 883 N SER 274 1270 1640 1677 -29 558 3 53 ATOM 1 884 CA SER 274 16.335 4.586 31.604 1.000 14 39 ANISOU 1 884 CA SER 274 1583 1534 2349 43 707 3 i 4 ATOM 1 885 CB SER 274 17.845 4.771 31.438 1.000 14. 49 ANISOU 1 885 CB SER 274 1578 1727 2202 213 695 3 2 9 ATOM 1 886 OG SER 274 18.564 3.558 31.424 1.000 14. 97 ANISOU 1 886 OG SER 274 1763 1848 2078 349 348 13 ATOM 1 887 C SER 274 16.100 3.505 32.666 1.000 13 . 12 ANISOU 1 887 C SER 274 1670 1481 1833 8 461 13 7 ATOM 1 888 0 SER 274 16.438 3.700 33.834 1.000 13.50 ANISOU 1 888 0 SER 274 1493 1518 2116 -65 119 1 ATOM 1 889 N VAL 275 15.533 2.359 32.271 1.000 11.90 ANISOU 1 889 N VAL 275 1476 1618 1427 -110 490 1 9 5 ATOM 1 890 CA VAL 275 15.283 1.254 33.180 1.000 11.41 ANISOU 1 890 CA VAL 275 1708 1424 1204 -8 286 7 > ATOM 1 891 CB VAL 275 14.346 0.198 32.543 1.000 12 .74 ANISOU 1891 CB VAL 275 1732 1300 1809 62 164 - 1 6 ATOM 1892 CGI VAL 275 14.157 -1.020 33.437 1.000 16.10 ANISOU 1892 CGI VAL 275 2352 1803 1962 -614 -663 3 7 0 ATOM 1893 CG2 VAL 275 12.961 0.763 32.261 1.000 13 81 ANISOU 1893 CG2 VAL 275 1535 1786 1924 16 363 1 6 ATOM 1894 C VAL 275 16.577 0.622 33.692 1.000 12 62 ANISOU 1894 C VAL 275 1574 1628 1594 14 375 1 6 ATOM 1895 O VAL 275 16.729 0.405 34.926 1. 000 13 01 ANISOU 1895 O VAL 275 1667 1643 1634 9 118 1 0 ATOM 1896 N PRO 276 17.569 0.286 32.889 1. 000 14 64 ANISOU 1896 N PRO 276 1583 2066 1914 2 454 - 2 ATOM 1897 CD PRO 276 17.583 0.285 31.415 1. 000 15 84 ANISOU 1897 CD PRO 276 1565 2536 1916 89 755 3 5 ATOM 1898 CA PRO 276 18.827 -0.250 33.453 1.000 16.76 ANISOU- 1898 CA PRO 276 1667 2403 2296 261 393 - 1 63 ATOM 1899 CB PRO 276 19.732 -0.503 32.236 1.000 18.27 ANISOU 1899 CB PRO 276 1804 2568 2571 411 574 - 1 42 ATOM 1900 CG PRO 276 18.868 -0.385 31.029 1.000 18. 96 ANISOU 1900 CG PRO 276 2147 2763 2293 725 694 3 7 ATOM 1901 C PRO 276 19.500 0.710 34.420 1.000 16. 32 ANISOU 1901 C PRO 276 1521 2342 2336 115 237 6 7 ATOM 1902 O PRO 276 20.035 0.277 35.456 1.000 16. 78 ANISOU 1902 O PRO 276 1411 2689 2275 93 376 2 5 3 ATOM 1903 N LEU 277 19.475 2.019 34.155 1.000 16.58 ANISOU 1903 N LEU 277 1835 2412 2052 -15 483 14 8 ATOM 1904 CA LEU 277 20.142 2.919 35.099 1.000 17.70 ANISOU 1904 CA LEU 277 1990 2226 2511 -21 362 118 ATOM 1905 CB LEU 277 20.298 4.277 34.425 1.000 20.20 ANISOU 1905 CB LEU 277 2952 2292 2432 -1 -14 271 ATOM 1906 CG LEU 277 21.048 5.359 35.186 1.000 20.86 ANISOU 1906 CG LEU 277 2213 2221 3490 -32 -355 482 ATOM 1907 CDI LEU 277 22.446 4.888 35.531 1.000 34.24 ANISOU 1907 CDI LEU 277 2157 2303 8552 69 -842 2 5 8 ATOM 1908 CD2 LEU 277 21.062 6.620 34.334 1.000 31.91 ANISOU 1908 CD2 LEU 277 4745 2460 4918 -474 -572 1150 ATOM 1909 C LEU 277 19.411 2.989 36.430 1.000 16.55 ANISOU 1909 C LEU 277 1975 1885 2430 -218 211 -243 ATOM 1910 O LEU 277 19.997 3.116 37.517 1.000 19.19 ANISOU 1910 O LEU 277 2179 2636 2476 -617 50 122 ATOM 1911 N ALA 278 18.080 2.905 36.386 1.000 15.48 ANISOU 1911 N ALA 278 2008 1904 1969 -358 279 112 ATOM 1912 CA ALA 278 17.308 2.896 37.636 1.000 14.51 ANISOU 1912 CA ALA 278 2109 1763 1641 -309 74 1 67 ATOM 1913 CB ALA 278 15.814 2.896 37.347 1.000 15.41 ANISOU 1913 CB ALA 278 2017 1773 2064 66 301 62 6 ATOM 1914 C ALA 278 17.710 1.684 38.479 1.000 14.55 ANISOU 1914 C ALA 278 1972 1869 1689 -195 -255 7 ATOM 1915 O ALA 278 17.894 1.770 39.683 1.00013.80 ANISOU 1915 O ALA 278 1444 2144 1655 -250 -166 8 9 ATOM 1916 N ARG 279 17.841 0.530 37.842 1.000 13 .86 ANISOU 1916 N ARG 279 1795 1728 1742 -432 -128 1 69 ATOM 1917 CA ARG 279 18.242 -0.679 38.560 1.00015.88 ANISOU 1917 CA ARG 279 1995 1973 2064 59 355 411 ATOM 1918 CB ARG 279 18.204 -1.922 37.648 1.000 16. 83 ANISOU 1918 CB ARG 279 1889 1897 2609 84 544 2 5 0 ATOM 1919 CG ARG 279 16.790 -2.323 37.291 1.000 19. 63 ANISOU 1919 CG ARG 279 2123 2196 3139 -63 233 9 1 ATOM 1920 CD ARG 279 16.656 -3.288 36.131 1.000 27. 03 ANISOU 1920 CD ARG 279 3924 3198 3150 -603 -275 - 198 ATOM 1921 NE ARG 279 17.236 -4.578 36.364 1.000 27.45 ANISOU 1921 NE ARG 279 4659 2854 2915 -359 751 - 7 89 ATOM 1922 CZ ARG 279 16.714 -5.717 36.779 1.000 32.85 -

-153-

ANISOU 1922 CZ ARG 279 4486 3045 4948 -475 448 - 22 :

ATOM 1923 NHl ARG 279 15.424 -5.874 37.089 1.000 29.96

ANISOU 1923 NHl ARG 279 4653 2168 4562 -103 967 - 67

ATOM 1924 NH2 ARG 279 17.551 -6.750 36.890 1.000 37.87

ANISOU 1924 NH2 ARG 279 4879 2436 7074 -276 3278 - 82 '

ATOM 1925 C ARG 279 19.628 -0.519 39.150 1.000 17.48

ANISOU 1925 C ARG 279 2118 1653 2871 75 -8 7 0 5

ATOM 1926 0 ARG 279 19.916 -1.064 40.212 1.000 26.82

ANISOU 1926 0 ARG 279 3764 3102 3325 -1987 -1467 13 83

ATOM 1927 N GLU 280 20.538 0.189 38.505 1.000 17.73

ANISOU 1927 N GLU 280 1983 2293 2459 109 609 3 7

ATOM 1928 CA GLU 280 21.899 0.317 39.026 1.000 19.66

ANISOU 1928 CA GLU 280 2049 2023 3396 125 215 7 3 7

ATOM 1929 CB GLU 280 22.836 0.886 37.936 1.000 20.17

ANISOU 1929 CB GLU 280 1648 2457 3560 464 138 109

ATOM 1930 CG GLU 280 22.964 -0.149 36.818 1.000 31.79

ANISOU 1930 CG GLU 280 3477 4175 4427 801 1187 - 4

ATOM 1931 CD GLU 280 23.698 0.341 35.590 1.000 39.66

ANISOU 1931 CD GLU 280 5144 5703 4221 -64 1339 - 6

ATOM 1932 OEl GLU 280 24.466 1.327 35.685 1.000 39.65

ANISOU 1932 OEl GLU 280 3464 5891 5710 334 574 163

ATOM 1933 OE2 GLU 280 23.489 -0.294 34.519 1.000 41.55

ANISOU 1933 OE2 GLU 280 5257 6747 3781 2245 -184 1 02

ATOM 1934 C GLU 280 21.984 1.188 40.266 1.000 19.68

ANISOU 1934 C GLU 280 1488 2350 3640 -566 162 490

ATOM 1935 0 GLU 280 23.031 1.142 40.958 1.000 25.69

ANISOU 1935 0 GLU 280 1871 3766 4123 231 -245 180

ATOM 1936 N CYS 281 20.943 1.980 40.565 1.000 18.57

ANISOU 1936 N CYS 281 1560 2609 2887 -406 -211 17 6

ATOM 1937 CA CYS 281 21.098 2.762 41.806 1.00023.83

ANISOU 1937 CA CYS 281 3222 2647 3184 -1189 176 - 12

ATOM 1938 CB CYS 281 21.079 4.264 41.523 1.000 25.40

ANISOU 1938 CB CYS 281 3278 2655 3718 -426 368 - 46

ATOM 1939 SG CYS 281 19.587 4.904 40.763 1.000 27.05

ANISOU 1939 SG CYS 281 3069 2914 4295 -522 -37 - 79

ATOM 1940 C CYS 281 20.098 2.406 42.907 1.000 16.99

ANISOU 1940 C CYS 281 1377 1604 3475 109 -6 - 546

ATOM 1941 0 CYS 281 19.971 3.173 43.889 1.000 17.04

ANISOU 1941 0 CYS 281 2294 1277 2902 -204 -484 - 12

ATOM 1942 N GLY 282 19.447 1.245 42.794 1.000 15.23

ANISOU 1942 N GLY 282 1617 1597 2572 3 -58 - 436

ATOM 1943 CA GLY 282 18.731 0.674 43.914 1.000 15.61

ANISOU 1943 CA GLY 282 1565 1973 2394 6 -331 - 266

ATOM 1944 C GLY 282 17.246 0.519 43.727 1.000 13.75

ANISOU 1944 C GLY 282 1635 1562 2029 -270 -446 - 7 E

ATOM 1945 0 GLY 282 16.585 0.012 44.639 1.000 14.99

ANISOU 1945 0 GLY 282 1751 1630 2313 207 -242 45 -

ATOM 1946 N PHE 283 16.744 1.009 42.582 1.000 12.65

ANISOU 1946 N PHE 283 1434 1803 1570 -200 18 - 252

ATOM 1947 CA PHE 283 15.292 0.886 42.374 1.000 11.80

ANISOU 1947 CA PHE 283 1477 1032 1974 -15 -264 4 6

ATOM 1948 CB PHE 283 14.839 1.890 41.295 1.000 14.13

ANISOU 1948 CB PHE 283 2262 972 2136 109 -187 1 5 9

ATOM 1949 CG PHE 283 14.906 3.351 41.757 1.000 12.63

ANISOU 1949 CG PHE 283 1711 1033 2055 47 -86 9

ATOM 1950 CDI . PHE 283 13.851 3.928 42.409 1.000 13 .45

ANISOU 1950 CDI . PHE 283 1697 1399 2013 -166 24 - 229

ATOM 1951 CD » PHE 283 16.037 4.111 41.519 1.000 13.15

ANISOU ^■ 1951 CD^ > PHE 283 1567 1135 2295 142 -41 - 9 !

ATOM 1952 CEl PHE 283 13.903 5.248 42.839 1.000 15.61

ANISOU ^' 1952 CEl PHE 283 2111 1649 2171 -202 484 - 61 17 ATOM 1953 CE2 PHE 283 16.112 5.432 41.963 1.000 12 .60

ANISOU 1953 CE2 PHE 283 1783 937 2068 32 -18 2 64

ATOM 1954 CZ PHE 283 15.040 5.993 42.641 1.000 13 .37

ANISOU 1954 CZ PHE 283 1863 865 2352 187 -149 1 3

ATOM 1955 C PHE 283 14.915 -0.534 41.972 1.000 11.23

ANISOU 1955 C PHE 283 1527 974 1765 63 -172 6 5

ATOM 1956 O PHE 283 15.471 -1.071 40.990 1.000 13 .24

ANISOU 1956 O PHE 283 1249 1428 2355 175 -120 - 361

ATOM 1957 N ASP 284 13.998 -1.130 42.712 1.000 12.31

ANISOU 1957 N ASP 284 1607 1333 1736 -268 -312 8 7

ATOM 1958 CA ASP 284 13.589 -2.528 42.527 1.000 12 .48

ANISOU 1958 CA ASP 284 1725 1202 1814 -148 -543 3 5 0

ATOM 1959 CB ASP 284 13.159 -3.156 43.876 1.000 12 .67

ANISOU 1959 CB ASP 284 2014 1145 1656 -50 -406 13 5

ATOM 1960 CG ASP 284 13.261 -4.667 43.909 1.000 13 .40

ANISOU 1960 CG ASP 284 2077 1171 1843 110 -419 3 6 3

ATOM 1961 ODl ASP 284 13.861 -5.246 42.974 1.000 14.98

ANISOU 1961 ODl ASP 284 1956 1094 2640 -87 11 6 0

ATOM 1962 OD2 ASP 284 12.762 -5.306 44.883 1.000 15.79

ANISOU 1962 OD2 ASP 284 2494 1539 1966 -330 -446 43 8

ATOM 1963 C ASP 284 12.478 -2.641 41.510 1.000 10.82

ANISOU 1963 C ASP 284 1238 1387 1487 -205 -99 12 3

ATOM 1964 O ASP 284 11.373 -3.100 41.777 1.000 12.28

ANISOU 1964 O ASP 284 1331 1175 2159 -209 48 19 1

ATOM 1965 N VAL 285 12.751 -2.154 40.308 1.000 11.32

ANISOU 1965 N VAL 285 1204 1671 1426 -93 -48 6 1

ATOM 1966 CA VAL 285 11.748 -2.062 39.260 1.000 11.45

ANISOU 1966 CA VAL 285 1468 1384 1500 39 -219 - 15

ATOM 1967 CB VAL 285 12.153 -1.072 38.157 1.000 11.58

ANISOU 1967 CB VAL 285 1412 1523 1465 -388 -428 - 8

ATOM 1968 CGI VAL 285 12.278 0.362 38.679 1.000 15.02

ANISOU 1968 CGI VAL 285 2209 1458 2040 -264 -442 - 32

ATOM 1969 CG2 VAL 285 13.467 -1.482 37.495 1.000 15.70

ANISOU 1969 CG2 VAL 285 1909 1443 2615 -159 309 447

ATOM 1970 C VAL 285 11.424 -3.431 38.642 1.000 10.83

ANISOU 1970 C VAL 285 1232 1281 1602 93 -221 108

ATOM 1971 O VAL 285 12.267 -4.301 38.520 1.000 12.13

ANISOU 1971 O VAL 285 1214 1192 2202 -28 300 1 62

ATOM 1972 N SER 286 10.168 -3.523 38.248 1.000 11.09

ANISOU 1972 N SER 286 1116 1608 1489 -76 96 7

ATOM 1973 CA SER 286 9.558 -4.622 37.510 1.000 11.32

ANISOU 1973 CA SER 286 1104 1479 1718 -41 -274 2 52

ATOM 1974 CB SER 286 8.483 -5.292 38.344 1.000 9 . 88

ANISOU 1974 CB SER 286 1328 1141 1285 72 -207 7 0

ATOM 1975 OG SER 286 7.570 -4.361 38.905 1.000 11.34

ANISOU 1975 OG SER 286 1391 1188 1729 147 -153 7 5

ATOM 1976 C SER 286 9.019 -4.106 36.175 1.000 10.34

ANISOU 1976 C SER 286 1127 1227 1575 28 -87 2 4 5

ATOM 1977 O SER 286 7.829 -4.112 35.869 1.000 12.62

ANISOU 1977 O SER 286 1223 2219 1353 0 -178 2 2 8

ATOM 1978 N LEU 287 9.926 -3.622 35.335 1.000 12.45

ANISOU 1978 N LEU 287 1414 1664 1653 -212 3 1 6 1

ATOM 1979 CA LEU 287 9.654 -2.900 34.099 1.000 12.59

ANISOU 1979 CA LEU 287 1622 1558 1605 -366 94 1 8 4

ATOM 1980 CB LEU 287 10.145 -1.452 34.210 1.000 12.91

ANISOU 1980 CB LEU 287 1716 1591 1597 -373 -95 2 7

ATOM 1981 CG LEU 287 9.452 -0.590 35.264 1.000 12.96

ANISOU 1981 CG LEU 287 1182 1848 1895 -407 -51 - 170

ATOM 1982 CDI . LEU 287 10.229 0.708 35.484 1.-000 13 .34

ANISOU ^' 1982 CD! . LEU 287 1644 1108 2318 -38 -124 2 2 3

ATOM 1983 CD: > LEU 287 8.006 -0.248 34.914 1.000 14.56 ANI SOL- 1983 CD2 LEU 287 1716 1548 2267 36 -550 3 18

ATOM 1984 C LEU 287 10.319 -3.610 32.928 1.000 12.63

ANISOU 1984 C LEU 287 1837 1244 1719 -233 248 35 <

ATOM 1985 O LEU 287 11.529 -3.805 32.916 1.000 16.68

ANISOU 1985 O LEU 287 1779 1998 2560 -292 390 - 1

ATOM 1986 N ASP 288 9.531 -4.045 31.950 1.000 13. 1

ANISOU- 1986 N ASP 288 2080 1751 1455 4 223 227

ATOM 1987 CA ASP 288 10.079 -4.688 30.759 1.000 15.50

ANI SOU- 1987 CA ASP 288 2029 2269 1593 -122 605 15 :

ATOM 1988 CB ASP 288 8.979 -5.478 30.043 1.000 17.00

ANISOU- 1988 CB ASP 288 2722 2125 1613 -250 362 - 2

ATOM 1989 CG ASP 288 9.480 -6.452 29.014 1.000 19.30

ANISOU- 1989 CG ASP 288 2467 2980 1885 173 243 - 31 7 7

ATOM 1990 ODl ASP 288 10.447 -7.183 29.292 1.000 25.95

ANISOU 1990 ODl ASP 288 2812 3190 3856 501 -239 - 7 £

ATOM 1991 OD2 ASP 288 8.911 -6.508 27.907 1.000 31.76

ANISOU 1991 OD2 ASP 288 5375 4430 2260 1266 -849 -11 5 4

ATOM 1992 C ASP 288 10.654 -3.652 29.811 1.000 17.08

ANISOU- 1992 C ASP 288 2259 2631 1602 -263 248 53

ATOM 1993 O ASP 288 10.197 -2.502 29.708 1.000 23.31

ANISOU 1993 O ASP 288 4276 2268 2313 -244 -13 29

ATOM 1994 N GLY 289 11.702 -3.966 29.049 1.000 21.26

ANISOU 1994 N GLY 289 2748 3699 1632 -610 752 51

ATOM 1995 CA GLY 289 12.116 -2.880 28.152 1.000 21.65

ANISOU 1995 CA GLY 289 2842 3988 1396 -1163 71 626

ATOM 1996 C GLY 289 13.084 -1.859 28.736 1.000 22.09

ANISOU 1996 C GLY 289 2888 3509 1996 -738 -23 24

ATOM 1997 O GLY 289 13.414 -1.836 29.924 1.000 20.34

ANISOU 1997 O GLY 289 3230 2606 1891 -918 124 14

ATOM 1998 N GLU 290 13.562 -0.952 27.869 1.000 16.48

ANISOU 1998 N GLU 290 2665 2099 1496 5 22: » -445

ATOM 1999 CA GLU 290 14.716 -0.117 28.182 1.000 16.94

ANISOU 1999 CA GLU 290 2470 2161 1806 81 411 - 484

ATOM 2000 CB GLU 290 15.579 0.012 26.912 1.000 20.26

ANISOU 2000 CB GLU 290 2670 2740 2287 414 863 - 2 : 3 9

ATOM 2001 CG GLU 290 16.071 -1.333 26.386 1.000 24.53

ANISOU 2001 CG GLU 290 3251 3153 2916 664 1218 - 6 : 1 2

ATOM 2002 CD GLU 290 16.812 -2.170 27.411 1.000 27.91

ANISOU 2002 CD GLU 290 3019 3161 4424 989 940 - 2 5 1

ATOM 2003 OEl GLU 290 17.874 -1.747 27.917 1.000 35.13

ANISOU 2003 OEl GLU 290 3913 4458 4975 963 -85 - 8 7 7

ATOM 2004 OE2 GLU 290 16.336 -3.280 27.734 1.000 43.76

ANISOU 2004 OE2 GLU 290 6893 3257 6478 -30 -748 59

ATOM 2005 C GLU 290 14.406 1.271 28.716 1.000 14.67

ANISOU 2005 C GLU 290 2512 1756 1308 95142 1 0

ATOM 2006 O GLU 290 15.260 1.840 29.412 1.000 15.25

ANISOU 2006 O GLU 290 2074 1969 1750 50 418 - 262

ATOM 2007 N THR 291 13.232 1.814 28.437 1.000 15.72

ANISOU 2007 N THR 291 2173 2393 1406 78 346 - 519

ATOM 2008 CA THR 291 12.792 3.087 28.991 1.000 15.16

ANISOU 2008 CA THR 291 2080 1845 1833 -88 631 - 1

ATOM 2009 CB THR 291 12.766 4.226 27.956 1.000 18.67

ANISOU 2009 CB THR 291 2724 2529 1842 -361 769 33

ATOM 2010 OGl . THR 291 11.756 4.009 26.976 1.000 22.93

ANISOU 2010 OGl . THR 291 3313 3135 2265 445 78 146

ATOM 2011 CG2 : THR 291 14.096 4.306 27.213 1.000 21.82

ANISOU 2011 CG2 : THR 291 3035 2126 3130 357 145090

ATOM 2012 C THR 291 11.402 2.920 29.622 1.000 1 12.86

ANISOU 2012 C THR 291 1863 1604 1421 47305 219

ATOM 2013 O THR 291 10.625 2.024 29.270 1.00c 116.13

ANISOU ^' 2013 O THR 291 2344 1983 1804 -303 750 - 4 3 1 ATOM 2014 N ALA 292 11.037 3.791 30.542 1.000 12 .41

ANISOU 2014 N ALA 292 1495 1363 1859 -2 256 7 /

ATOM 2015 CA ALA 292 9.746 3.839 31.202 1.000 11. 57

ANISOU 2015 CA ALA 292 1362 1257 1779 -213 153 3 7

ATOM 2016 CB ALA 292 9.718 2.954 32.439 1.000 12. 62

ANISOU 2016 CB ALA 292 1768 1245 1784 100 357 4

ATOM 2017 C ALA 292 9.385 5.255 31.614 1.000 10. 32

ANISOU 2017 C ALA 292 1317 1335 1270 -181 99 E > 4

ATOM 2018 O ALA 292 10.266 6.134 31.701 1.000 10. 97

ANISOU 2018 O ALA 292 1389 1138 1641 -146 279 1 04

ATOM 2019 N THR 293 8.091 5.445 31.882 1.000 12 . 32

ANISOU 2019 N THR 293 1486 1547 1647 -314 563 - 28

ATOM 2020 CA THR 293 7.626 6.715 32.421 1.000 12 . 28

ANISOU 2020 CA THR 293 1717 1460 1489 -168 337 - 20

ATOM 2021 CB THR 293 6.352 7.215 31.733 1.000 13 . 27

ANISOU 2021 CB THR 293 2128 1182 1730 -258 -159 - 28

ATOM 2022 OGl THR 293 5.317 6.237 31.911 1.000 13 . 85

ANISOU 2022 OGl THR 293 1831 1217 2216 8 -131 ^' ' 4

ATOM 2023 CG2 THR 293 6.474 7.303 30.212 1.000 13 . 72

ANISOU 2023 CG2 THR 293 1791 1683 1738 -252 -56 -40

ATOM 2024 C THR 293 7.363 6.635 33.937 1.000 10. 58

ANISOU 2024 C THR 293 1439 1050 1533 12 447 ' 9

ATOM 2025 O THR 293 7.211 5.576 34.553 1.000 10. 29

ANISOU 2025 O THR 293 1049 1102 1758 -56 93 118

ATOM 2026 N PHE 294 7.243 7.810 34.569 1.000 11. 53

ANISOU 2026 N PHE 294 1794 1093 1494 -307 306 - 66

ATOM 2027 CA PHE 294 6.806 7.939 35.950 1.000 10. 41

ANISOU 2027 CA PHE 294 1432 1061 1463 -174 125 - 16

ATOM 2028 CB PHE 294 6.709 9.426 36.336 1.000 12. 25

ANISOU 2028 CB PHE 294 1930 1030 1694 -164 292 - 64

ATOM 2029 CG PHE 294 6.270 9.658 37.770 1.000 12. 77

ANISOU 2029 CG PHE 294 1880 1136 1837 -103 178 - 42

ATOM 2030 CDI PHE 294 7.123 9.462 38.839 1.000 14. 73

ANISOU 2030 CDI PHE 294 1976 1893 1727 -539 161 - 13

ATOM 2031 CD2 PHE 294 4.989 10.068 38.056 1.000 16. 59

ANISOU 2031 CD2 PHE 294 2180 1923 2199 348 386 -49

ATOM 2032 CEl PHE 294 6.726 9.673 40.144 1.000 14. 36

ANISOU 2032 CEl PHE 294 1598 2028 1830 -505 280 -11

ATOM 2033 CE2 PHE 294 4.575 10.275 39.345 1.000 16. 75

ANISOU 2033 CE2 PHE 294 2214 2062 2087 692 144 -60

ATOM 2034 CZ PHE 294 5.426 10.065 40.413 1.000 15. , 17

ANISOU 2034 CZ PHE 294 2040 1426 2296 327 97 -135

ATOM 2035 C PHE 294 5.484 7.195 36.172 1.000 10. , 89

ANISOU 2035 C PHE 294 1401 1200 1536 -155 78 137

ATOM 2036 O PHE 294 5.325 6.425 37.125 1.000 10. .67

ANISOU 2036 O PHE 294 1396 1297 1360 90337 105

ATOM 2037 N GLN 295 4.487 7.355 35.299 1.000 10. .62

ANISOU 2037 N GLN 295 1399 1187 1450 -18 88 -24

ATOM 2038 CA GLN 295 3.217 6.612 35.393 1.000 11 , .31

ANISOU 2038 CA GLN 295 1433 1205 1660 -96 120 - 32

ATOM 2039 CB GLN 295 2.284 7.053 34.254 1.000 11 .66

ANISOU 2039 CB GLN 295 1425 1053 1953 -25 63 -141

ATOM 2040 CG GLN 295 0.951 6.360 34.200 1.000 11 .05

ANISOU 2040 CG GLN 295 1573 1011 1614 -93 -118 1 8

ATOM 2041 CD GLN 295 0.052 6.843 33.087 1.000 11 .35

ANISOU 2041 CD GLN 295 1592 1326 1395 173 57 - 13

ATOM 2042 OEl GLN 295 0.349 7.823 32.378 1.000 15 .06

ANISOU 2042 OEl GLN 295 2306 1589 182,5 -^• 110 7 3 7 9

ATOM 2043 NE2 GLN 295 -1.053 6.153 32.914 1.000 13 .90

ANISOU 2043 NE2 GLN 295 1511 1757 2015 156 -282 2 0 I

ATOM 2044 C GLN 295 3.412 5.107 35.389 1.000ι 10 .12 ANISOU 2044 C GLN 295 1154 1203 1486 21 160 - 191

ATOM 2045 O GLN 295 2.827 4.309 36.128 1.000 11.82

ANISOU 2045 O GLN 295 1264 1542 1686 -107 41 13 7

ATOM 2046 N ASP 296 4.267 4.558 34.538 1.000 9 .35

ANISOU 2046 N ASP 296 1076 1056 1422 -118 -76 - 275

ATOM 2047 CA ASP 296 4.655 3.172 34.416 1.000 9 . 1

ANISOU 2047 CA ASP 296 1241 1139 1387 56 60 - 243

ATOM 2048 CB ASP 296 5.699 2.852 33.347 1.000 10.26

ANISOU 2048 CB ASP 296 1315 1156 1429 113 132 - 3 6

ATOM 2049 CG ASP 296 5.343 2.981 31.885 1.000 11.42

ANISOU 2049 CG ASP 296 1357 1578 1405 358 121 - 199

ATOM 2050 ODl ASP 296 4.143 2.904 31.531 1.000 13 .82

ANISOU 2050 ODl ASP 296 1511 1744 1997 149 -209 - 62

ATOM 2051 OD2 ASP 296 6.282 3.151 31.047 1.000 13 .48

ANISOU 2051 OD2 ASP 296 1802 1758 1564 228 364 7 3

ATOM 2052 C ASP 296 5.175 2.682 35.770 1.000 10.31

ANISOU 2052 C ASP 296 1416 1141 1361 16 91 - 198

ATOM 2053 0 ASP 296 4.852 1.551 36.197 1.000 11.40

ANISOU 2053 0 ASP 296 1428 1452 1453 -288 32 3 5

ATOM 2054 N TRP 297 6.004 3.484 36.441 1.000 10.88

ANISOU 2054 N TRP 297 1752 1144 1238 -161 11 5 5

ATOM 2055 CA TRP 297 6.646 3.104 37.685 1.000 11.26

ANISOU 2055 CA TRP 297 1768 1215 1294 -217 -57 4 5

ATOM 2056 CB TRP 297 7.899 3.999 37.890 1.000 10.31

ANISOU 2056 CB TRP 297 1387 1417 1112 -87 213 12 0

ATOM 2057 CG TRP 297 8.621 3.651 39.172 1.000 10.98

ANISOU 2057 CG TRP 297 1456 1394 1324 164 -29 - 43

ATOM 2058 CD2 TRP 297 9.082 4.534 40.202 1.000 12.49

ANISOU 2058 CD2 TRP 297 1255 1729 1761 75 -298 - 197

ATOM 2059 CE2 TRP 297 9.692 3.755 41.201 1.000 16.08

ANISOU 2059 CE2 TRP 297 1860 2049 2202 -294 -977 4 9

ATOM 2060 CE3 TRP 297 9.040 5.910 40.379 1.000 17.41

ANISOU 2060 CE3 TRP 297 2778 1740 2096 -388 -916 - 234

ATOM 2061 CDI TRP 297 8.969 2.400 39.589 1.000 13.58

ANISOU 2061 CDI TRP 297 1617 1518 2025 0 -664 114

ATOM 2062 NE1 TRP 297 9.614 2.444 40.808 1.000 16.12

ANISOU 2062 NE1 TRP 297 2165 1909 2051 -22 -873 22 0

ATOM 2063 CZ2 TRP 297 10.243 4.320 42.341 1.000 19.85

ANISOU 2063 CZ2 TRP 297 2756 2383 2404 -951 -1337 2 67

ATOM 2064 CZ3 TRP 297 9.586 6.466 41.515 1.000 23.40

ANISOU 2064 CZ3 TRP 297 4215 2030 2645 -1001 -1757 - 77

ATOM 2065 CH2 TRP 297 10.181 5.670 42.486 1.000 21.51

ANISOU 2065 CH2 TRP 297 3178 2457 2537 -910 -1473 - 5 1

ATOM 2066 C TRP 297 5.700 3.138 38.882 1.000 10.39

ANISOU 2066 C TRP 297 1172 1448 1329 -280 -237 3 9 1

ATOM 2067 O TRP 297 5.574 2.159 39.639 1.000 13.52

ANISOU 2067 O TRP 297 1748 1830 1557 32 -91 7 03

ATOM 2068 N ILE 298 5.033 4.272 39.079 1.000 12.08

ANISOU 2068 N ILE 298 1400 1710 1480 -49 83 451

ATOM 2069 CA ILE 298 4.223 4.521 40.272 1.000 13.43

ANISOU 2069 CA ILE 298 1301 2484 1317 -199 -158 - 3 3

ATOM 2070 CB ILE 298 4.370 5.988 40.689 1.000 16.97

ANISOU 2070 CB ILE 298 1877 2908 1661 -1000 214 - 630

ATOM 2071 CG2 ILE 298 3.538 6.423 41.876 1.000 22 .01

ANISOU 2071 CG2 ILE 298 3980 3121 1263 -233 546 - 339

ATOM 2072 CGI ILE 298 5.847 6.253 41.037 1.000 27.10

ANISOU ^' 2072 CGI ILE 298 2588 5151 2557 -2140 -708 9 7

ATOM 2073 CDI . ILE 298 6.365 5.522 42.266 1.000 43 .13

ANISOU ^' 2073 CDI . ILE 298 5185 8299 2904 -3717 -3055 7 08

ATOM 2074 C ILE 298 2.772 4.116 40.131 1.000 10.94

ANISOU ^• 2074 C ILE 298 1350 1652 1156 -165 -79 9 6 o

t^ r "^ σι cs . -n - rH r rH CD o

- -3* • CM ro

α) -_. N ιrl ι-) o cri ^ oo ffl • n - co -

o o o o

S L7_ S w S

HOHO

ANISOU 2105 CA VAL 303 1434 1609 1471 -368 -197 2 2 3

ATOM 2106 CB VAL 303 2.755 6.967 45.736 1.000 14.57

ANISOU 2106 CB VAL 303 1395 1682 2459 -217 -918 3 12

ATOM 2107 CGI VAL 303 3.131 6.462 47.132 1.000 17.33

ANISOU 2107 CGI VAL 303 2644 1608 2331 -48 -1114 6 1

ATOM 2108 CG2 VAL 303 1.703 6.041 45.122 1.000 14.80

ANISOU 2108 CG2 VAL 303 1876 1676 2069 -592 -639 3 2 2

ATOM 2109 C VAL 303 3.467 9.328 46.303 1.000 13 .88

ANISOU 2109 C VAL 303 8701791 2613 75 -286 - 375

ATOM 2110 O VAL 303 4.526 9.417 45.681 1.000 19.70

ANISOU 2110 O VAL 303 1064 2307 4114 -61 323 - 999

ATOM 2111 N ASN 304 3.271 10.046 47.393 1.000 13 .77

ANISOU 2111 N ASN 304 1681 1815 1737 -479 -388 140

ATOM 2112 CA ASN 304 4.205 11.077 47.828 1.000 13 .37

ANISOU 2112 CA ASN 304 1626 1240 2212 -213 -533 2 7 9

ATOM 2113 CB ASN 304 3.460 12.223 48.566 1.000 13 .24

ANISOU 2113 CB ASN 304 1206 1454 2370 -243 -344 2 9 6

ATOM 2114 CG ASN 304 2.457 12.922 47.667 1.000 14.16

ANISOU 2114 CG ASN 304 1142 2326 1910 146 -88 23 0

ATOM 2115 ODl ASN 304 2.776 13.283 46.540 1.000 16.65

ANISOU 2115 ODl ASN 304 1408 2456 2464 107 185 9 1 6

ATOM 2116 ND2 ASN 304 1.263 13.126 48.209 1.000 17.45

ANISOU 2116 ND2 ASN 304 1414 2961 2257 545 181 3 15

ATOM 2117 C ASN 304 5.325 10.588 48.728 1.000 11.18

ANISOU 2117 C ASN 304 1382 1299 1566 -183 -163 112

ATOM 2118 O ASN 304 6.396 11.232 48.699 1.000 12.07

ANISOU 2118 O ASN 304 1325 1382 1879 -167 -66 - 5 9

ATOM 2119 N ILE 305 5.092 9.541 49.516 1.000 12.56

ANISOU 2119 N ILE 305 1791 1296 1685 -152 -232 2 02

ATOM 2120 CA ILE 305 6.063 9.011 50.463 1.000 14.01

ANISOU 2120 CA ILE 305 2314 1393 1614 -55 -479 7 9

ATOM 2121 CB ILE 305 5.781 9.493 51.906 1.000 14.44

ANISOU 2121 CB ILE 305 2223 1604 1659 -29 -217 15 7

ATOM 2122 CG2 ILE 305 5.725 11.017 51.956 1.000 15.31

ANISOU 2122 CG2 ILE 305 1768 1608 2441 43 -479 - 314

ATOM 2123 CGI ILE 305 4.543 8.853 52.498 1.000 14.83

ANISOU 2123 CGI ILE 305 1779 1694 2163 27 -307 - 153

ATOM 2124 CDI ILE 305 4.163 9.252 53.900 1.000 28.68

ANISOU 2124 CDI ILE 305 3788 5324 1786 -1491 381 9 2

ATOM 2125 C ILE 305 6.059 7.487 50.389 1.000 12.79

ANISOU 2125 C ILE 305 1703 1355 1800 -260 -586 2 3 1

ATOM 2126 O ILE 305 5.111 6.864 49.897 1.000 15.63

ANISOU 2126 O ILE 305 1779 1564 2597 -185 -1008 2 77

ATOM 2127 N ARG 306 7.170 6.896 50.829 1.000 13 .04

ANISOU 2127 N ARG 306 1618 1389 1946 -368 -598 3 83

ATOM 2128 CA ARG 306 7.340 5.435 50.868 1.000 11.82

ANISOU 2128 CA ARG 306 1352 1366 1773 -375 -154 444

ATOM 2129 CB ARG 306 8.111 4.965 49.640 1.000 15.28

ANISOU 2129 CB ARG 306 1976 1941 1886 -368 -19 1 1 1

ATOM 2130 CG ARG 306 8.203 3.472 49.395 1.000 17.16

ANISOU 2130 CG ARG 306 2566 1953 2001 -68 -68 7 6

ATOM 2131 CD ARG 306 8.344 3.075 47.937 1.000 19.51

ANISOU 2131 CD ARG 306 2921 2361 2130 -397 -396 - 302

ATOM 2132 NE ARG 306 7.078 3.198 47.212 1.000 20.65

ANISOU 2132 NE ARG 306 2693 2844 2309 -1056 -310 2 1 4

ATOM 2133 CZ ARG 306 6.948 3.186 45.893 1.000 17.11

ANISOU ^' 2133 CZ ARG 306 2006 2225 2268 45 -91 596

ATOM 2134 NHl . ARG 306 8.013 3.065 45.083 1.000 21.58

ANISOU ^' 2134 NHl . ARG 306 2405 2677 3116 -232 381 - 669

ATOM 2135 NH2 ! ARG 306 5.734 3.301 45.365 1.000 17.51

ANISOUr 2135 NH2 ! ARG 306 2235 1550 2868 150 -484 - 162 -160-

ATOM 2136 C ARG 306 8.035 5.027 52.155 1.000 13.45

ANISOU 2136 C ARG 306 2254 1018 1837 -246 -481 9 8

ATOM 2137 O ARG 306 9.006 5.682 52.556 1.000 12.15

ANISOU 2137 O ARG 306 1902 1099 1615 -18 -362 - 80

ATOM 2138 N ARG 307 7.571 3.968 52.811 1.000 18.19

ANISOU- 2138 N ARG 307 3073 1620 2218 -734 -938792

ATOM 2139 CA ARG 307 8.197 3.380 53.989 1.000 19.20

ANISOU 2139 CA ARG 307 3053 1963 2277 -675 -1236 643

ATOM 2140 C ARG 307 9.086 2.191 53.611 1.00023.08

ANISOU 2140 C ARG 307 4018 1905 2847 -270 -1885 329

ATOM 2141 O ARG 307 8.636 1.292 52.895 1.000 35.93

ANISOU 2141 O ARG 307 6003 2403 5244 38 -3227 - 791

ATOM 2142 CB ARG 307 7.131 2.918 54.997 1.00028.25

ANISOU 2142 CB ARG 307 5557 3297 1882 -1503 -277 509

ATOM 2143 CG ARG 307 6.032 3.921 55.275 1.000 33.39

ANISOU 2143 CG ARG 307 4564 4859 3261 -1613 731 208

ATOM 2144 CD ARG 307 5.022 3.523 56.317 1.00040.42

ANISOU 2144 CD ARG 307 6335 5701 3322 -1900 1263 971

ATOM 2145 NE ARG 307 5.605 2.952 57.529 1.000 50.83

ANISOU 2145 NE ARG 307 8119 7287 3908 -2786 105 1624

ATOM 2146 CZ ARG 307 4.894 2.441 58.530 1.000 51.36

ANISOU 2146 CZ ARG 307 7424 8064 4025 -3650 -9662451

ATOM 2147 NHl ARG 307 3.567 2.422 58.485 1.00069.51

ANISOU 2147 NHl ARG 307 7586 10951 7874 -6970 -2008 3245

ATOM 2148 NH2 ARG 307 5.489 1.937 59.600 1.000 59.99

ANISOU 2148 NH2 ARG 307 10714 8150 3930 -5986 -3291 2028

ATOM 2149 N THR 308 10.347 2.147 54.048 1.00022.92

ANISOU 2149 N THR 308 2759 2587 3364 -589 -200 170

ATOM 2150 CA THR 308 11.215 1.009 53.794 1.00024.47

ANISOU 2150 CA THR 308 3382 2649 3268 -360 52 150

ATOM 2151 C THR 308 10.602 -0.252 54.382 1.00031.10

ANISOU 2151 C THR 308 5251 2520 4044 -768 16 279

ATOM 2152 O THR 308 10.610 -1.292 53.718 1.00031.44

ANISOU 2152 O THR 308 4573 2676 4696 -457 -1745 - 40

ATOM 2153 CB THR 308 12.615 1.279 54.378 1.00023.51

ANISOU 2153 CB THR 308 3718 2086 3131 413 -694542

ATOM 2154 OGl THR 308 13.195 2.410 53.705 1.00023.61

ANISOU 2154 OGl THR 308 2711 2503 3754 153 437 - 9

ATOM 2155 CG2 THR 308 13.573 0.141 54.117 1.00026.37

ANISOU 2155 CG2 THR 308 4427 2796 2796 927 -329 - 18

ATOM 2156 N SER 309 10.066 -0.156 55.596 1.00028.39

ANISOU 2156 N SER 309 3759 2774 4252 -19 2 1300

ATOM 2157 CA SER 309 9.488 -1.335 56.238 1.00034.69

ANISOU 2157 CA SER 309 6110 3146 3925 -1066 -1089 1626

ATOM 2158 C SER 309 8.109 -1.737 55.724 1.00041.41

ANISOU 2158 C SER 309 6442 3910 5383 -2171 -1170 2144

ATOM 2159 O SER 309 7.672 -2.884 55.952 1.000 57.05

ANISOU 2159 O SER 309 11389 5141 5146 -4907 -2077 2027

ATOM 2160 CB SER 309 9.450 -1.104 57.755 1.00031.61

ANISOU 2160 CB SER 309 4863 2958 4188 -483 368 962

ATOM 2161 OG SER 309 8.485 -0.135 58.107 1.000 38.99

ANISOU 2161 OG SER 309 4731 3477 6604 313 -2249 - 496

ATOM 2162 N LYS 310 7.391 -0.868 55.032 1.00047.69

ANISOU 2162 N LYS 310 5502 5577 7040 -539 -1369 1583

ATOM 2163 FE IUM 312 8.574 13.466 54.055 1.000 11.05

ANISOU 2163 FE IUM 312 1690 1156 1351 -101 -2377 1

ATOM 2164 CI AKG 313 5.987 14.815 54.612 1.000 19.65

ANISOU ^' 2164 CI AKG 313 2777 2119 2572 258 -117 556

ATOM 2165 01 AKG 313 4.799 15.240 54.659 1.00020.82

ANISOU ^■ 2165 01 AKG 313 2957 2293 2659 514 -234 264

ATOM 2166 02 AKG 313 6.643 14.144 53.787 1.000 17.79 ANISOU 2166 02 AKG 313 2407 1765 2587 74 -377 4 2 9

ATOM 2167 C2 AKG 313 6.867 15.178 55.844 1.00020. 08

ANISOU 2167 C2 AKG 313 1997 2566 3068 -528 419 - 3 9 9

ATOM 2168 05 AKG 313 7.982 14.661 55.821 1.000 17. 60

ANISOU 2168 05 AKG 313 2289 2066 2334 -314 226 - 2 5 2

ATOM 2169 C3 AKG 313 6.272 16.080 56.872 1.000 21. 69

ANISOU 2169 C3 AKG 313 2751 1910 3581 240 62 - - 32

ATOM 2170 C4 AKG 313 7.318 16.741 57.716 1.00021. 50

ANISOU 2170 C4 AKG 313 3246 1761 3160 199 -143 - 1

ATOM 2171 C5 AKG 313 6.923 17.816 58.672 1.00022. 58

ANISOU 2171 C5 AKG 313 3122 1840 3618 755 -49: 5 - 3 1 3

ATOM 2172 03 AKG 313 7.754 18.591 59.124 1.00027. 48

ANISOU 2172 03 AKG 313 3581 2470 4389 -34 602 - 1 2 6 6

ATOM 2173 04 AKG 313 5.660 17.889 58.999 1.00028. 55

ANISOU 2173 04 AKG 313 3191 2809 4846 612 -246 - 1 1 4

ATOM 2174 S S04 401 11.676 0.439 24.942 1.000 40. 14

ATOM 2175 01 S04 401 11.293 0.826 26.321 1.000 33. 12

ATOM 2176 02 S04 401 12.501 -0.829 25.014 1.000 35. 79

ATOM 2177 03 S04 401 10.430 0.189 24.129 1.00054. 89

ATOM 2178 04 S04 401 12.500 1.520 24.329 1.00044. 80

ATOM 2179 OW HOH 501 -6.455 10.219 44.319 1.000 14. 29

ATOM 2180 OW HOH 502 -10.520 18.612 50.560 1.00012. 86

ATOM 2181 OW HOH 503 -8.644 16.907 47.858 1.000 16. 83

ATOM 2182 OW HOH 504 -10.313 20.800 43.074 1.00016. 10

ATOM 2183 OW HOH 505 -6.051 19.199 52.602 1.00016. 38

ATOM 2184 OW HOH 506 -6.873 24.642 47.100 1.00020. 55

ATOM 2185 OW HOH 507 10.676 -4.179 46.406 1.00027. 41

ATOM 2186 OW HOH 508 -0.077 21.786 40.872 1.00015. 22

ATOM 2187 OW HOH 509 5.761 13.656 46.041 1.00017. 40

ATOM 2188 OW HOH 510 29.135 31.449 51.982 1.00018. 40

ATOM 2189 OW HOH 511 26.032 32.724 52.741 1.00017. 03

ATOM 2190 OW HOH 512 10.965 32.371 46.000 1.00016. 70

ATOM 2191 OW HOH 513 23.871 24.457 58.649 1.00018. 71

ATOM 2192 OW HOH 514 26.353 29.063 50.326 1.00018. 96

ATOM 2193 OW HOH 515 23.191 33.106 53.153 1.00020. 41

ATOM 2194 OW HOH 516 21.429 11.721 55.329 1.00018. , 39

ATOM 2195 OW HOH 517 9.122 15.567 53.585 1.00024. .87

ATOM 2196 OW HOH 518 27.843 17.352 53.437 1.00027. , 76

ATOM 2197 OW HOH 519 -14.415 20.029 44.444 1.00023. .47

ATOM 2198 OW HOH 520 15.253 33.050 51.771 1.00027. .20

ATOM 2199 OW HOH 521 14.080 31.486 44.302 1.00021 , .58

ATOM 2200 OW HOH 522 17.770 33.842 53.596 1.00023. .56

ATOM 2201 OW HOH 523 3.671 24.673 36.173 1.00020. .95

ATOM 2202 OW HOH 524 -15.683ι 28.618 52.535 1.00024 .05

ATOM 2203 OW HOH 525 -5.386 20.413 39.013 1.00026 .85

ATOM 2204 OW HOH 526 10.417 27.949 58.778 1.00028 .33

ATOM 2205 OW HOH 527 23.165 19.592 62.202 1.00029 .36

ATOM 2206 OW HOH 528 23.736 10.550 55.737 1.00024 .02

ATOM 2207 OW HOH 529 -1.662 28.650 42.485 1.00021 .62

ATOM 2208 OW HOH 530 -4.689 10.177 46.511 1.00031 .65

ATOM 2209 OW HOH 531 1.545 35.657 50.866 1.00019 .59

ATOM 2210 OW HOH 532 0.980 22.687 36.818 1.00030 .57

ATOM 2211 OW HOH 533 -12.450 16.848 56.071 1.00028 .42

ATOM 2212 OW HOH 534 -9.418 16.139 51.364 1.00022 .60

ATOM 2213 OW HOH 535 32.711 25.816 43.116 1.00031 .44

ATOM 2214 OW HOH 536 27.068 24.587 55.468 1.00023 .32

ATOM 2215 OW HOH 537 13.523 11.832 51.199 1.00010 .73

ATOM 2216 OW HOH 538 8.513 16.158 35.074 1.00012 .26

ATOM 2217 OW HOH 539 0.922 2.590 35.058 1.000 14 .79

ATOM 2218 OW HOH 540 -1.548 3.709 34.484 1.00014 .25

ATOM 2219 OW HOH 541 11.711 16.898 30.416 1.000 17 .84 ATOM 2220 OW HOH 542 15.389 11.536 32.065 -. 000 17 .88

ATOM 2221 OW HOH 543 18.496 6.995 52. 191 1. 000 17. 47

ATOM 2222 OW HOH 544 19.848 22.580 35. 334 1. 000 17. 28

ATOM 2223 OW HOH 545 -0.387 4.787 41. 967 1. 000 13 . 22

ATOM 2224 OW HOH 546 23.502 12.662 35. 308 1. 000 18. 14

ATOM 2225 OW HOH 547 10.332 25.236 33. 926 1. 000 19. 05

ATOM 2226 OW HOH 548 21.447 20.605 34. 090 1. 000 17. 24

ATOM 2227 O HOH 549 8.164 7.685 27. 077 1. 000 25. 40

ATOM 2228 O HOH 550 14.393 -5.127 40. 321 1. 000 15. 88

ATOM 2229 OW HOH 551 12.873 29.356 39. 662 000 16. 45

ATOM 2230 O HOH 552 11.974 24.144 58. 426 1. 000 19 . 71

ATOM 2231 OW HOH 553 17.521 7.949 33. 182 1. 000 17. 90

ATOM 2232 OW HOH 554 3.401 2.691 43. 340 1. 000 23 . 76

ATOM 2233 OW HOH 555 18.669 28.057 40. 079 1. 000 18 . 44

ATOM 2234 OW HOH 556 10.827 12.928 30. 017 1. 000 19 . 57

ATOM 2235 OW HOH 557 20.630 16.270 66. 466 1. 000 20. 84

ATOM 2236 OW HOH 558 11.315 20.266 64. 044 1. 000 21. 62

ATOM 2237 OW HOH 559 26.277 14.516 43. 946 1. 000 16. 22

ATOM 2238 OW HOH 560 9.616 15.488 32. 365 1. 000 19. 40

ATOM 2239 O HOH 561 8.888 4.903 27. 857 1. 000 22. 74

ATOM 2240 OW HOH 562 20.496 -1.851 42. 511 1. 000 22. 98

ATOM 2241 OW HOH 563 17.033 29.415 38. 332 1. 000 26. 36

ATOM 2242 O HOH 564 18.595 6.141 37. 697 1. 000 25. 10

ATOM 2243 OW HOH 565 22.446 13.893 31. 420 1. 000 29. 00

ATOM 2244 OW HOH 566 6.586 3.577 28. 350 1. 000 27. 82

ATOM 2245 OW HOH 567 6.250 20.077 30. ,961 1. 000 23. 27

ATOM 2246 OW HOH 568 7.341 16.113 31. ,186 1. 000 28. 59

ATOM 2247 OW HOH 569 16.090 32.070 42. .552 1. ,000 33. , 08

ATOM 2248 OW HOH 570 11.500 28.806 37. .258 1. ,000 25. , 17

ATOM 2249 OW HOH 571 12.901 26.768 58. .591 1. .000 28. , 58

ATOM 2250 OW HOH 572 -17.071 17.043 50. .450 1. .000 28. , 82

ATOM 2251 OW HOH 573 25.262 7.705 37. .199 1. .000 39. .05

ATOM 2252 OW HOH 574 32.884 26.440 51. .734 1. .000 29. .03

ATOM 2253 OW HOH 575 -1.199 19.088 42. .527 1. .000 14. .86

ATOM 2254 OW HOH 576 -4.389 33.026 63 , .392 1. .000 29. .56

ATOM 2255 OW HOH 577 17.569 25.732 32 .249 1. .000 20 .62

ATOM 2256 OW HOH 578 -19.107 12.822 67 .516 1. .000 22. .35

ATOM 2257 OW HOH 579 29.333 19.198 51 .975 1 .000 22 .51

ATOM 2258 OW HOH 580 27.950 27.635 51 .903 1 .000 25 .40

ATOM 2259 OW HOH 581 -21.085 14.501 68 .535 1 .000 21 .19

ATOM 2260 OW HOH 582 1.529 17.378 33 .953 1 .000 25 .29

ATOM 2261 OW HOH 583 9.138 20.887 66 .894 1 .000 33 .92

ATOM 2262 OW HOH 584 -11.896 i 19.091 44 .780 1 .000 17 .48

ATOM 2263 OW HOH 585 6.382 12.597 43 .347 1 .000 22 .09

ATOM 2264 OW HOH 586 17.762 21.268 29 .046 1 .000 20 .79

ATOM 2265 OW HOH 587 -11.50C I 25.438 41 .729 1 .00029 .68

ATOM 2266 OW HOH 588 7.877 1.046 29 .689 1 .000 27 .70

ATOM 2267 OW HOH 589 27.985 13.540 42 .235 1 .000 25 .91

ATOM 2268 OW HOH 590 1.276 14.852 34 .021 1 .000 20 .41

ATOM 2269 OW HOH 591 24.622 24.179 41 .242 1 .000 26 .77

ATOM 2270 OW HOH 592 0.404 14.096 36 .006 1 .000 27 .92

ATOM 2271 OW HOH 593 -2.835 36.981 57 .827 1 .000 31 .86

ATOM 2272 OW HOH 594 3.276 0.788 39 .940 1 .000 32 .07

ATOM 2273 OW HOH 595 11.025 -8.794 31 .468 1 .000 27 .18

ATOM 2274 OW HOH 596 6.301 2.276 42 .639 1 .000 29 .74

ATOM 2275 OW HOH 597 29.302 16.146 62 .924 1 .000 43 .75

ATOM 2276 _. OW HOH 598 19.039 20.964 67 .011 1 .000 30 .85

ATOM 2277 OW HOH 599 8.380 22.088 64 .518 1 .000 42 .62

ATOM 2278 OW HOH 600 21.480 10.826 34 .742 1 .000 25 .74

ATOM 2279 OW HOH 601 -2.907 21.956 38 .566 1 .000 30 .92

ATOM 2280 OW HOH 602 -3.928 29.841 43 .352 1 .000 43 .96 . -

- 163-

ATOM 2281 O HOH 603 2.885 21.563 34. 437 1. 00033. 10

ATOM 2282 O HOH 604 11.801 6.043 25. 270 1. 000 38. 18

ATOM 2283 O HOH 605 -1.019 17.197 40. 472 1. 00018. 48

ATOM 2284 OW HOH 606 18.382 23.349 68. 110 1. 00022. 54

ATOM 2285 OW HOH 607 -8.141 8.137 45. 609 1. 00017. 64

ATOM 2286 OW HOH 608 5.022 2.667 51. 700 1. 00024. 29

ATOM 2287 O HOH 609 17.557 10.755 33. 490 1. 00021. 94

ATOM 2288 O HOH 610 11.222 1.201 49. 675 1. 00020. 61

ATOM 2289 O HOH 611 4.243 35.047 50. 509 1. 000 22. 18

ATOM 2290 O HOH 612 11.103 4.031 56. 082 1. 00022. 08

ATOM 2291 O HOH 613 11.366 31.522 36. 791 1. 000 32. 32

ATOM 2292 OW HOH 614 -21.189 24.787 52. 739 1. 00031. 83

ATOM 2293 OW HOH 615 7.847 -1.491 30. 674 1. 00024. 77

ATOM 2294 O HOH 616 19.041 11.937 31. 445 1. 00025. 97

ATOM 2295 OW HOH 617 6.221 29.879 40. 410 1. 00029. 24

ATOM 2296 O HOH 618 17.266 5.933 35. 280 1. 00023. 72

ATOM 2297 OW HOH 619 5.983 -7.215 28. 510 1. 000 28. 19

ATOM 2298 OW HOH 620 22.574 8.129 57. 639 1. 00030. 97

ATOM 2299 OW HOH 621 2.553 7.806 60. 287 1. 00028. 77

ATOM 2300 OW HOH 622 29.939 25.812 51. 234 1. 00034. 00

ATOM 2301 OW HOH 623 2.205 34.823 53. 632 1. 00025. 88

ATOM 2302 OW HOH 624 18.091 13.838 67. 343 1. 00028. 46

ATOM 2303 OW HOH 625 8.342 3.195 58. 475 1. 00026. 84

ATOM 2304 OW HOH 626 -16.086 18.427 42. 790 1. 00031. 11

ATOM 2305 OW HOH 627 -2.098 13.445 35. ,620 1. 00027. , 48

ATOM 2306 OW HOH 628 0.481 30.471 42. 834 1. 00032. 55

ATOM 2307 OW HOH 629 13.368 33.845 42. ,899 1. 00028. 70

ATOM 2308 OW HOH 630 -13.792 14.642 51. .533 1. .00025. , 58

ATOM 2309 OW HOH 631 3.299 1.461 29. .242 1. ,00039. , 62

ATOM 2310 OW HOH 632 -16.012 20.690 46. .705 1. ,00027. .75

ATOM 2311 OW HOH 633 19.606 8.142 31. .259 1. ,00027. .02

ATOM 2312 OW HOH 634 5.077 7.954 57. .205 1. .00030. .59

ATOM 2313 OW HOH 635 -1.502 6.963 45. .877 1. .00035. .68

ATOM 2314 OW HOH 636 9.974 17.449 38, .804 1. .00021. .84

ATOM 2315 OW HOH 637 -22.829 12.836 67. .228 1. .00025. .04

ATOM 2316 OW HOH 638 6.275 34.333 39. .722 1. .00025. .88

ATOM 2317 OW HOH 639 2.248 19.798 56, .051 1. .00026. .67

ATOM 2318 OW HOH 640 -20.552 17.013 67 .454 1. .00031 .34

ATOM 2319 OW HOH 641 9.298 16.570 28 .911 1, .00029 .96

ATOM 2320 OW HOH 642 -1.732 11.113 60 .074 1 .00028 .13

ATOM 2321 OW HOH 643 34.157 23.604 44 .657 1 .00036 .36

ATOM 2322 OW HOH 644 24.298 20.199 33 .576 1 .00034 .90

ATOM 2323 OW HOH 645 13.803 -4.667 31 .570 1 .00032 .66

ATOM 2324 OW HOH 646 6.295 -2.594 29 .009 1 .00034 .61

ATOM 2325 OW HOH 647 5.623 37.039 49 .318 1 .00028 .08

ATOM 2326 OW HOH 648 -18.805 19.286 46 .868 1 .00038 .32

ATOM 2327 OW HOH 649 16.026 35.829 49 .382 1 .00034 .45

ATOM 2328 OW HOH 650 -12.187 ^' 28.769 45 .330 1 .00027 .36

ATOM 2329 OW HOH 651 21.344 5.778 55 .101 1 .00027 .43

ATOM 2330 OW HOH 652 -1.848 2.125 32 .240 1 .000 32 .02

ATOM 2331 OW HOH 653 -14.568 ! 18.811 55 .775 1 .00029 .95

ATOM 2332 OW HOH 654 -8.655 26.254 38 .301 1 .00032 .07

ATOM 2333 OW HOH 655 18.836 13.542 28 .102 1 .00032 .24

ATOM 2334 OW HOH 656 16.217 14.669 25 .619 1 .00033 .35

ATOM 2335 OW HOH 657 28.678 14.477 38 .043 1 .00030 .94

ATOM 2336 OW HOH 658 -11.83. - 15.408 53 .330 1 .00033 .25

ATOM 2337 OW HOH 659 -1.317 38.273 59 .599 1 .00034 .45

ATOM 2338 OW HOH 660 8.784 13.918 28 .681 1 .00033 .62

ATOM 2339 OW HOH 661 -3.058 14.508 47 .405 1 .00028 .79

ATOM 2340 OW HOH 662 10.968 33.651 38 .533 1 .00036 .21

ATOM 2341 OW HOH 663 28.960 21.602 53 .665 1 .00029 .25 ATOM 2342 O HOH 664 -10.709 26.808 39 175 000 7 1 ATOM 2343 O HOH 665 17.790 7.093 55 023 000 2 9 ATOM 2344 OW HOH 666 6.404 24.865 29 848 000 5 5 ATOM 2345 OW HOH 667 -15.418 19.777 341 000 8 2 ATOM 2346 OW HOH 668 0.000 0.000 37 259 330 9 0 ATOM 2347 OW HOH 669 19.652 24.610 33 660 000 7 7 ATOM 2348 OW HOH 670 17.188 9.619 29 950 000 9 4 ATOM 2349 OW HOH 671 17.708 2.958 28 338 000 . 9 4 ATOM 2350 OW HOH 672 -0.059 3.652 30 079 000 . 2 3 ATOM 2351 OW HOH 673 29.037 20.923 56 153 000 . 5 2 ATOM 2352 OW HOH 674 -15.435 31 .088 53 795 000 . 6 1 ATOM 2353 OW HOH 675 -12.84621.220 61 856 000 . 7 9 ATOM 2354 O HOH 676 10.299 39.666 49 554 000 . 3 0 ATOM 2355 OW HOH 677 -5.921 28.822 41 521 000 . 0 1 ATOM 2356 OW HOH 678 6.029 39.991 46 094 000 . 6 9 ATOM 2357 O HOH 679 35.052 23.156 52 356 000 . 1 7 ATOM 2358 OW HOH 680 -12.008 38.355 51 601 000 . 1 8 ATOM 2359 OW HOH 681 3.061 13.047 53 152 000 . 1 7 ATOM 2360 OW HOH 682 1.379 2.075 27 532 000 . 3 8 ATOM 2361 OW HOH 683 -0.516 -2.480 37 686 .000 . 7 7 ATOM 2362 OW HOH 684 4.567 10.310 43 503 .000 . 8 6 ATOM 2363 OW HOH 685 19.443 5.558 61 133 000 0 6 ATOM 2364 OW HOH 686 3.205 29.499 40 656 000 9 9 ATOM 2365 OW HOH 687 32.498 16.774 43 447 000 1 8 ATOM 2366 OW HOH 28.166 23.113 57 593 000 5 6 ATOM 2367 OW HOH 689 -17.023 23.220 46 759 000 0 5 ATOM 2368 OW HOH 690 15.567 7.782 28 910 000 5 1 ATOM 2369 OW HOH 691 11.780 30.287 57 203 000 3 4 ATOM 2370 OW HOH 692 24.449 12.699 32 400 000 9 9 ATOM 2371 OW HOH 693 26.200 25.005 57 918 000 3

Claims

1. Deacetoxycephalosporin C synthase (DAOCS) having a structure designated by the X-ray co-ordinates of structure A or structure B herein.

2. DAOCS in the form of a complex with a metal, e.g. iron or lead, and optionally in the presence of a substrate and/or a substrate analogue or inhibitor, having a structure designated by the X-ray co-ordinates herein.

3. DAOCS as claimed in claim 2, wherein the substrate is penicillin N, penicillin G, 2-oxoglutarate or dioxygen, and the inhibitor is selected from N-oxalylamino acids, pyridine-carboxylates and nitrous oxide.

4. Use of the three-dimensional structure of DAOCS for the modification of DAOCS or other related 2-oxoglutarate dependent enzyme.

5. Use as claimed in claim 4, wherein the related 2-oxoglutarate dependent enzyme is DACS, DAOC/DACS or the oxygenase enzyme involved in the introduction of the 7╬▒-methoxy group into cephamycin C.

6. Use as claimed in claim 5 for the modification of DAOCS,

DACS or DAOC/DACS such that they accept unnatural substrates more efficiently than the wild type enzymes.

7. Use as claimed in claim 5 for the modification of DAOCS, DACS, DAOC/DACS such that they convert natural substrates to pharmaceuticals or useful intermediates in the preparation of pharmaceuticals.

8. Use as claimed in claim 6 wherein the unnatural substrates are penicillins including penicillin G, penicillin V, 6-aminopenicillanic acid, amoxycillin, or penicillins with a phenyl glycine or p-hydroxyphenyl glycine side chain.

9. Use as claimed in claim 6 wherein the unnatural substrate is a cephalosporin.

10. Use as claimed in claim 6 wherein the unnatural substrate is an amino acid, including the proteinogenic amino acids, or a peptide.

11. Use as claimed in any one of claims 6-8, wherein penicillin G, penicillin V, another unnatural substrate or penicillin N is converted to a cephalosporin or exomethylene cephalosporin.

12. An enzyme having significant (as herein defined) sequence similarity to DAOCS wherein the side chain binding site of penicillin N or DAOC is modified and at at least one of the following sites at least one amino acid residue is changed to another amino acid residue or is deleted: Thr72, Arg74, Arg75, Glu156, Leu158, Arg160, Arg162, Leu186, Ser187, Phe225, Phe264, Arg266, Asp301 , Tyr302, Val303, Asn304; and/or at least one additional amino acid residue is inserted within the region 300-311 ; provided that other residues interacting with the above may be changed in order to accommodate the change in one of the above.

13. An enzyme having significant (as herein defined) sequence similarity to DAOCS wherein the penicillin/cephalosporin binding site of penicillin N or DAOC is modified and at at least one of the following amino acid residues is changed or deleted: Ile88, Arg160, Arg162, Phe164, Met180, Thr190, Ile192, Phe225, Pro241 , Val245, Val262, Phe264, Ile305, Arg306, Arg307; and/or at least one additional amino acid residue is inserted within the region 300-311 ; provided that other residues interacting with the above may be changed in order to accommodate the change in one of the above.

14. An enzyme according to claim 12 or claim 13 which is a mutant of DAOCS or DACS or DAOC/DACS.

15. An enzyme as claimed in any one of claims 12-14, wherein both the side chain and the penicillin/cephalosporin binding sites of penicillin N or DAOC are modified and at least one of the residues specified in claims 12 and 13 is changed or deleted.

16. An enzyme as claimed in any one of claims 12-15, wherein two or more complementary mutations are introduced to create or delete a binding interaction, including H-bonds, electrostatic, or hydrophobic interactions.

17. A gene encoding for the enzyme of any one of claims 12-16.

18. A micro-organism capable of expressing the gene of claim 17 under fermentation conditions.

19. Use of micro-organisms of claim 18 for the production of beta-lactams of the penicillin or cephalosporin (including cepham) families.

20. Use as claimed in claim 19 wherein the micro-organism contains another modified enzyme of the penicillin and cephalosporin biosynthesis pathway including isopenicillin N synthase, amidohydrolase/acetyltransferase, or L-delta-(aminoadipoyl)-L-cysteine-D- valine (ACV) synthetase.

21. A method which comprises using the three-dimensional structure of DAOCS for determining or predicting the structure of another related 2-oxoglutarate dependent enzyme or related enzyme not from the penicillin and cephalosporin biosynthesis pathway, and using the structural information so obtained for modifying the other enzyme or for designing an inhibitor for the other enzyme.

22. A method as claimed in claim 21 wherein the said other related 2-oxoglutarate dependent enzyme or related enzyme is

1-aminocylopropane-1-carboxylate oxidase, gibberellin C-20 oxidase, flavone synthase, flavanone 3╬▓-hydroxylase, hyoscyamine 6╬▓-hydroxylase, prolyl 4-hydroxylase, prolyl 3-hydroxylase, aspartyl hydroxyiase, lysyl hydroxylase, proline hydroxylases, ╬│-butyrobetaine hydroxyiase, enzymes in herbicide resistance mechanisms, ciavaminate synthase, an oxygenase enzyme involved in the biosynthesis of carbapenems, the so called ethylene forming enzyme from Pseudomonas syringe, p-hydroxyphenylpyruvate dioxygenase, and an oxygenase enzyme involved in the oxidation of phytol in human liver peroxisomes.

23. A method as claimed in claim 21 or 22, wherein the said other enzyme is modified, by deletion or addition or alteration; at one or more of the sites defined in claim 12 or claim 13; or using the following information for the design or an inhibitor: Asp185, His183 and His243 act as ligands to the iron; Arg258 and Ser260 and the Fe bind the 2-oxoglutarate; Met180, Phe225, Leu31 and Val245 are close to the iron binding site; Tyr33, Arg160, Arg162, Phe164, Ile192, Gln194, Leu204, Leu223, Leu215 are important for the construction of the part of the active site binding 2-oxoglutarate; and Arg160 and Arg162 are important for binding an amino acid or peptide derived substrate.

24. A method as claimed in any one of claims 21-23, wherein the said other enzyme is prolyl 4-hydroxylase, prolyl 3-hydroxylase, aspartyl hydroxyiase, or lysyl hydroxyiase and the inhibitor is to be used for the treatment of human diseases including fibrotic diseases including liver cirrhosis and arthritis.

25. A method as claimed in any one of claims 21-23, wherein the said other enzyme is p-hydroxyphenylpyruvate dioxygenase and the inhibitor is to be used in the treatment of certain genetic disorders.

26. A method as claimed in any one of claims 21-23, wherein the said other enzyme is involved in herbicide resistance and the information is to be used to design new herbicides to overcome the problem of resistance.