WO2001019971A1 - Novel imp-1 metallo beta-lactamase enzyme - Google Patents

Novel imp-1 metallo beta-lactamase enzyme Download PDF

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WO2001019971A1
WO2001019971A1 PCT/US2000/025340 US0025340W WO0119971A1 WO 2001019971 A1 WO2001019971 A1 WO 2001019971A1 US 0025340 W US0025340 W US 0025340W WO 0119971 A1 WO0119971 A1 WO 0119971A1
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atom
lys
leu
beta
val
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Sherin S. Abdel-Meguid
Nestor O. Concha
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Smithkline Beecham Corporation
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    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
    • C12N9/86—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in cyclic amides, e.g. penicillinase (3.5.2)

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Abstract

A novel Pseudomonas aeruginosa IMP-1 metallo beta-lactamase native crystalline structure and a novel Pseudomonas aeruginosa IMP-1 metallo beta-lactamase complex with the inhibitor SB-252619 crystalline structure are identified.

Description

NOVEL IMP-1 METALLO BETA-LACTAMASE ENZYME Technical Field of the Invention
The invention relates to the identification of a novel enzyme active site, its mode of binding with an inhibitor, and methods enabling further design and selection of inhibitors of that active site. Background of the Invention
The proliferation of antibiotic-resistant bacteria are an increasing public health threat [Tenover, F. C, and Hughes, J. M. (1996) J. Am. Med. Assoc. 275, 300-304]. Of the mechanisms by which bacteria becomes resistant to antibiotics, the production of enzymes that catalyze reactions by which the antibiotic molecules are rendered inactive is the most important. Beta-lactamases, enzymes that hydrolyze beta-lactam antibiotics such as penicillin(s) and cephalosporin(s), were discovered in the early 1940's [Abraham, E. P., and Chain, E. (1940) Nature (London) 146, 837-837]. Based on their amino acid sequences they are divided into four structural classes [Ambler, R. P. (1980) Philos. Trans. R. Soc. London B289, 321-331 ; Jaurin, B., and Grundstrom, T. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 4897-4901; Houvinen, P., Houvinen, S., and Jacoby, G. A. (1988) Antimicrob. Agents Chemother. 32, 134- 136]. Classes A, C, and D are known as serine beta-lactamases because they have an active site serine residue important for catalysis. Effective inhibitors of class A enzymes, the most prevalent form, such as clavulanic acid, are already in the market in the form of Augmentin® (co-amoxyclav). Class B or metallo beta-lactamases activate a solvent molecule using an active site metal that is required for catalysis [Concha, N. O., Rasmussen, B. A., Bush, K., and Herzberg, O. (1996) Structure 4, 823-836]. The different catalytic mechanism makes the class A enzyme inhibitor clavulanate ineffective against the metallo beta-lactamases. The increase in antibiotic resistance due to metallo beta-lactamases present in bacterial strains not previously known to carry this form of resistance such as Klebsiella pneumoniae, Aeromonas hydrophyla, Bacteroides fragilis, Stenotrophomonas maltophilia, Bacillus cereus, and Pseudomonas aeruginosa, and the lack of commercially available inhibitors against metallo beta-lactamases for use in the treatment of bacterial infections makes these metallo beta-lactamase enzymes a suitable target for antibacterial agents.
There is a need for novel metallo beta-lactamase enzyme active sites in complex with both inhibitors and reaction intermediates to enable identification and structure-based design of metallo beta-lactamase inhibitors useful in the treatment or prophylaxis of infectious diseases resistant to beta-lactam antibiotics due to the production of metallo beta-lactamases.
Summary of the Invention In one aspect, the present invention relates to an IMP-1 metallo beta-lactamase which is derived from Pseudomonas aeruginosa and comprising a protein having the crystalline coordinates of Table la, and interatomic distances and angles of active site residues listed in Table IV in an essentially pure native form or a homolog thereof. In another aspect, the present invention provides a novel crystalline form of the metallo beta-lactamase enzyme active site in complex with a putative inhibitor 2-[5-(l- tetrazolylmethyl)thien-3-yl]-N-[2-(mercaptomethyl)-4-phenylbutyrylglycine)] identified herein as SB-252619.
In yet another aspect, the invention provides direct information on the specific role of the residues in the active site responsible for the binding of inhibitors, substrates and substrate analogs.
In yet another aspect, the invention provides the structural basis for the role of active site amino acid residues and metals bound in the active site responsible for the catalytic activity of these enzymes. This provides a method for identifying inhibitors of the metallo beta- lactamase, which methods involve the steps of: providing the coordinates of the metallo beta- lactamase structure of the invention to a computerized modeling system; identifying compounds which will bind to the active site; and screening the compounds identified for metallo beta-lactamase inhibitory bio-activity.
Another aspect of this invention includes machine-readable media encoded with data representing the coordinates of the three-dimensional structure of the metallo beta-lactamase crystal structure alone or in complex with the inhibitor SB-252619.
Other aspects and advantages of the present invention are described further in the following detailed description of the preferred embodiments thereof. Brief Description of the Drawings Fig. 1 provides a representation of the secondary structure elements of the native IMP-
1 metallo beta-lactamase.
Fig. 2A and 2B provides a representation of the secondary structure elements of the IMP-1 metallo beta-lactamase from two different views.
Fig. 3A and 3B provide a stereoview of a schematic drawing of the active site of the IMP-1 metallo beta-lactamase enzyme from Pseudomonas aeruginosa in complex with the inhibitor SB-252619.
Fig. 4A and 4B provide a stereoview of a schematic drawing of the comparison between the active sites of the native IMP- 1 metallo beta-lactamase from Pseudomonas aeruginosa and the active site of the its complex with the inhibitor SB-252619. The structures are shown superimposed to highlight the conformational changes. Detailed Description of the Invention The present invention provides a novel IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa crystalline structure of the native enzyme. In addition, it provides a novel metallo beta-lactamase active site of the crystalline structure of the IMP-1 metallo beta- lactamase in complex with the inhibitor SB-252619 and methods to use these crystalline forms and their active sites to identify and improve metallo beta-lactamase inhibitor compounds (peptide, peptidomimetic or synthetic compositions). These compounds are characterized by the ability to competitively inhibit binding of substrates or other like-molecules to the active site of metallo beta-lactamases.
The IMP-1 Metallo Beta-Lactamase From Pseudomonas aeruginosa Crystalline Three- Dimensional Structure And Its Complex With The Inhibitor SB252619.
The crystal structures of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa in its native form and in complex with the inhibitor SB-252619 have been determined and refined to 3.lA and 2.0A resolution, respectively.
The novel IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa crystalline structure, like other metallo beta-lactamases, has the alpha+beta fold characterized by four layers: alpha/beta/beta/alpha. The beta strands form a beta sandwich with a seven, mixed-strand beta-sheet on the N-terminal side and a five, mixed-strand beta-sheet on the C-terminal side of the molecule. Two alpha helices pack against the faces on either side of the sandwich and a third alpha helix is located at the edge of the beta-sandwich. The metallo beta-lactamases from B.fragilis, B. cereus and the IMP-1 from P. aeruginosa share a 34-37% sequence identity.
Superposition of the Cα atoms of their crystal structures results in an overall root mean square, rms, deviation of 0.6A for the superposition of the B. fragilis and the IMP- 1 enzymes, and a overall rms deviation of 0.6A for the superposition of the B. cereus and the IMP-1 enzymes. Residues 42-48 (this numbering scheme includes the 18 residues comprising the signal sequence at the N-terminus) are disordered in the native IMP- 1 structure. Residues 40-42 and 48-50, at the base of a hairpin loop form one side of the active site groove with Trp46 located above the active site dinuclear metal center, and although the precise position of Trp46 in this and other metallo beta-lactamase native structures could not be determined due to the disorder of that portion of the polypeptide chain, it has been proposed that the hairpin loop acts as a flap that closes to cover the active site bound substrate during catalysis. This prediction has been confirmed by the crystal structure of the IMP- 1 metallo beta-lactamase with the inhibitor SB- 252619 as described below.
The position of the Zn+2 ions, the metal ligand amino acid side chains and the conserved active site amino acid residues presumed to be involved in catalysis are similarly positioned in IMP-1 as in all other known crystal structures of metallo beta-lactamases. The exception is Lys 179, a conserved residue suspected to be involved in substrate binding, whose NZ atom is 2.3-2.5A closer to the dinuclear center in the IMP-1 native structure compared to the B. fragilis and the B. cereus enzymes. The position of the lysine is different in IMP-1 because the loop immediately following this residue, between beta strand #1 1 and alpha helix #4, has a three-residue deletion in the IMP- 1 and therefore is shorter than in the B. fragilis or the B. cereus enzymes.
The active site of the IMP- 1 metallo beta-lactamase is formed by a dinuclear Zn+ center, Znl and Zn2, located at one edge of the central beta-sandwich. Side chain atoms from residues His95, His97 and Hisl57 are ligands to Zn l , and Asp99, Cysl76 and His215 are ligands to Zn2. The tetrahedral coordination geometry of Znl completed by a water molecule that bridges both metals could not be identified in the native IMP-1 crystal structure due to the low resolution of the data. This water molecule is likely to be in a deprotonated state, or hydroxide, and act as the nucleophile to attack the carbonyl carbon of the substrate's beta- lactam ring. The pentagonal bipyramid coordination of Zn2 completed by a second water molecule could not be identified either due to the low resolution experimental data of the native IMP-1 crystal structure. It is believed to be present based on the similarity of the active site architecture with the B. fragilis crystal structure. The zinc ions are located in the floor of a wide active site groove open to bulk solvent at both ends. The groove is bound on one side by residues 40 to 50 from the C-terminal end of beta2, the N-terminal end of beta3 and the hairpin loop connecting them. It is in this connecting loop, or flap, with the sequence Gly45-Trp46- Gly47 that is disordered in the native metallo beta-lactamase structures, but not in the complex with the inhibitor SB-252619.
The present invention also provides a novel metallo beta-lactamase crystalline structure based on the IMP-1 Pseudomonas aeruginosa metallo beta-lactamase in complex with the inhibitor SB-252619. The major structural change between the native and the inhibitor complex crystal structures is the closing of the active site groove by the flap, a hairpin loop formed by residues 42-48 that brings Trp46 to interact with the active-site bound inhibitor. The interactions between the inhibitor and the enzyme are summarized as follows:
1. The phenyl ring of the inhibitor is bound to a hydrophobic pocket formed by the side chain of residues Glu41 , Val43, Val49, Lys51 and Phe69. 2. The thiol group of the inhibitor is positioned between the two zinc ions in place of the shared water. The second (apical) water molecule is also absent in the complex displaced by the inhibitor's carboxyl oxygen which lies 1.4A from the metal-coordinated water position and 4.0A from the Zn2.
3. A carboxyl oxygen of the inhibitor forms an ion pair with Lysl79NZ, while the second carboxyl oxygen forms a hydrogen bond with main chain amide nitrogen of Asnl85. 4. The thiophene ring of the inhibitor and the flap's Trp46 indole ring make an edge-to- face interaction.
5. Although not making direct contacts, the carbonyl oxygen of the inhibitor is correctly oriented to interact in the oxyanion hole with the side chain of Asnl85 (4.2 A) and Znl (5.0A).
Table I provides the atomic coordinates of the native (Table la) IMP- 1 metallo beta- lactamase from P. aeruginosa, and its complex with SB-252619 (Table lb). The model of the complex includes residues 20 to 239 for both molecules, A and B, in the crystallographic asymmetric unit. The amino acid sequence of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa is provided in SEQ ID No. 1.
Variation in the atomic coordinates shown in Tables I - IV will occur such as upon refinement of a crystal structure from a different crystal form, which will result in a new set of coordinates. The deviation on Coc atoms from the present coordinate set is not expected to substantially exceed a rms of 1.0-1.5A. Similarly, bond angles and bond lengths will usually vary within a small range [Engh, R. A., and Huber, R. (1991) Ada Crystallogr. A47, 392-400.], however, the inter-atomic interactions in Tables I - IV will remain constant, within the experimental error, as will the relative conformation and orientation or positioning of residues in the active site. The atomic coordinates of the active site residues including the inhibitor (residue name "SB2") are provided in Table I. TABLE I
Table IA. Atomic coordinates of the native IMP-1 structure
CRYST150.300 105.800 112.30090.0093.9090.00 P21 ORIGX1 1.0000000.0000000.000000 0.00000
ORIGX2 0.000000 1.0000000.000000 0.00000
ORIGX3 0.0000000.000000 1.000000 0.00000
SCALE 1 0.019881 0.0000000.001355 0.00000
SCALE2 0.0000000.009452 0.000000 0.00000
SCALE3 0.0000000.0000000.008925 0.00000
ATOM 1 CB GLU 20 -10.377 7.466 58.754 1.00 58.41
ATOM 2 CG GLU 20 -9.080 8.094 59.285 1.00 59.56
ATOM 3 CD GLU 20 -7.982 7.078 59.574 1.00 60.99
ATOM 4 OE1 GLU 20 -7.341 6.602 58.611 1.00 61.27
ATOM 5 OE2 GLU 20 -7.757 6.762 60.764 1.00 60.72
ATOM 6 C GLU 20 9.208 7.037 56.547 1.00 57.06
ATOM 7 O GLU 20 ■8.660 6.277 55.744 1.00 56.41
ATOM 10 N GLU 20 -9.875 5.144 58.034 1.00 57.48 ATOM 12 CA GLU 20 -10.235 6.506 57.552 1.00 58.25
ATOM 13 N SER 21 -8.969 8.345 56.590 1.00 56.58
ATOM 15 CA SER 21 -8.012 9.006 55.709 1.00 55.84
ATOM 16 CB SER 21 -7.876 10.481 56.103 1.00 58.30
ATOM 17 OG SER 21 -8.727 10.801 57.195 1.00 60.59
ATOM 19 C SER 21 -6.627 8.361 55.702 1.00 53.54
ATOM 20 O SER 21 -5.913 8.357 56.707 1.00 52.79
ATOM 21 N LEU 22 -6.259 7.826 54.544 1.0049.53
ATOM 23 CA LEU 22 -4.969 7.184 54.338 1.00 44.22
AATTOOMM 2244 CCBB LLEEUU 2222 -4.970 5.781 54.937 1.0045.62
ATOM 25 CG LEU 22 -3.599 5.153 55.177 1.0045.44
ATOM 26 CD1 LEU 22 -3.062 5.575 56.542 1.00 43.35
ATOM 27 CD2 LEU 22 -3.723 3.634 55.076 1.00 45.50
ATOM 28 C LEU 22 -4.815 7.106 52.830 1.00 39.73
AATTOOMM 2299 OO LLEEUU 2222 -5.518 6.342 52.168 1.0040.84
ATOM 30 N PRO 23 -3.896 7.902 52.265 1.00 35.08
ATOM 31 CD PRO 23 -2.965 8.813 52.946 1.00 34.23
ATOM 32 CA PRO 23 -3.692 7.895 50.817 1.00 32.16
ATOM 33 CB PRO 23 -2.418 8.704 50.626 1.00 31.25
AATTOOMM 3344 CCGG PPRROO 2233 -2.346 9.574 51.81 1 1.00 32.74
ATOM 35 C PRO 23 -3.545 6.476 50.320 1.00 32.95
ATOM 36 O PRO 23 -3.223 5.573 51.092 1.00 35.49
ATOM 37 N ASP 24 -3.793 6.271 49.035 1.00 31.16
ATOM 39 CA ASP 24 -3.681 4.939 48.482 1.00 30.10
AATTOOMM 4400 CCBB AASSPP 2244 -4.926 4.587 47.668 1.00 37.70
ATOM 41 CG ASP 24 -5.794 5.793 47.378 1.0042.70
ATOM 42 OD1 ASP 24 -5.734 6.300 46.234 1.00 46.59
ATOM 43 OD2 ASP 24 -6.535 6.230 48.292 1.00 44.50
ATOM 44 C ASP 24 -2.448 4.813 47.615 1.00 25.90
AATTOOMM 4455 OO AASSPP 2244 -1.860 5.807 47.186 1.00 22.29
ATOM 46 N LEU 25 -2.059 3.567 47.384 1.00 22.84
ATOM 48 CA LEU 25 -0.904 3.246 46.571 1.00 18.14
ATOM 49 CB LEU 25 -1.006 1.803 46.095 1.00 14.07
ATOM 50 CG LEU 25 0.294 1.268 45.524 1.00 12.68
AATTOOMM 5511 CCDD11 LLEEUU 2255 1.126 0.703 46.668 1.00 12.70
ATOM 52 CD2 LEU 25 0.004 0.218 44.463 1.00 11.92
ATOM 53 C LEU 25 -0.837 4.166 45.362 1.00 19.01
ATOM 54 O LEU 25 -1.866 4.465 44.741 1.00 17.87 ATOM 55 N LYS 26 0.375 4.617 45.044 1.00 17.46
ATOM 57 CA LYS 26 0.61 1 5.483 43.894 1.00 15.58
ATOM 58 CB LYS 26 1.063 6.853 44.357 1.00 15.59
ATOM 59 CG LYS 26 0.182 7.466 45.422 1.00 21.72
ATOM 60 CD LYS 26 0.239 8.983 45.374 1.00 22.21
ATOM 61 CE LYS 26 1.686 9.470 45.305 1.00 24.28
ATOM 62 NZ LYS 26 2.214 9.508 43.901 1.00 20.02
ATOM 66 C LYS 26 1.714 4.829 43.084 1.00 14.60
ATOM 67 O LYS 26 2.728 4.428 43.646 1.00 15.44
AATTOOMM 6688 NN Π IL_EE : 2 277 1.538 4.720 41.774 1.00 13.57
ATOM 70 CA ILE 27 2.551 4.071 40.965 1.00 15.83
ATOM 71 CB ILE 27 1.995 2.785 40.341 1.00 14.51
ATOM 72 CG2 ILE 27 3.109 2.003 39.664 1.00 17.67
ATOM 73 CGI ILE 27 1.351 1.924 41.424 1.00 14.72
AATTOOMM 7744 CCDDI1 IILLEE 2277 0.928 0.560 40.937 1.00 12.04
ATOM 75 C ILE : 27 3.141 4.932 39.861 1.00 18.78
ATOM 76 O ILE : 27 2.955 4.647 38.684 1.00 20.79
ATOM 77 N GLU 28 3.881 5.969 40.236 1.00 22.55
ATOM 79 CA GLU 28 4.495 6.853 39.250 1.00 24.42
AATTOOMM 8800 CCBB GGLLUU 2288 4.927 8.152 39.918 1.00 25.05
ATOM 81 CG GLU 28 3.844 9.21 1 39.942 1.00 33.22
ATOM 82 CD GLU 28 4.073 10.268 41.013 1.00 37.05
ATOM 83 OE1 GLU 28 5.029 10.1 13 41.814 1.00 38.13
ATOM 84 OE2 GLU 28 3.292 11.252 41.049 1.00 37.15
AATTOOMM 8855 CC GGLLUU 2288 5.703 6.235 38.555 1.00 24.10
ATOM 86 O GLU 28 6.502 5.555 39.191 1.00 24.43
ATOM 87 N LYS 29 5.832 6.479 37.252 1.00 24.58
ATOM 89 CA LYS 29 6.967 5.983 36.465 1.00 23.51
ATOM 90 CB LYS 29 6.668 6.1 12 34.971 1.0020.81
AATTOOMM 9911 CCGG LLYYSS 2299 7.741 5.526 34.070 1.00 22.17
ATOM 92 CD LYS 29 7.188 5.223 32.684 1.00 29.64
ATOM 93 CE LYS 29 8.266 4.717 31.740 1.00 33.10
ATOM 94 NZ LYS 29 9.021 5.839 31.097 1.00 38.16
ATOM 98 C LYS 29 8.237 6.793 36.789 1.00 24.78
AATTOOMM 9999 OO LLYYSS 2299 8.158 7.963 37.173 1.00 25.19
ATOM 100 N LEU 30 9.407 6.181 36.632 1.00 24.64
ATOM 102 CA LEU 30 10.653 6.888 36.917 1.00 23.10
ATOM 103 CB LEU 30 11.390 6.232 38.077 1.00 21.80 ATOM 104 CG LEU 30 12.530 7.106 38.602 1.00 22.08
ATOM 105 CD1 LEU 30 1 1.983 8.124 39.605 1.00 18.94
ATOM 106 CD2 LEU 30 13.604 6.231 39.232 1.00 19.61
ATOM 107 C LEU 30 11.591 6.969 35.723 1.00 22.34
ATOM 108 O LEU 30 12.194 8.01 1 35.466 1.00 21.41
ATOM 109 N ASP 31 11.708 5.869 34.992 1.00 22.73
ATOM 1 1 1 CA ASP 31 12.582 5.830 33.831 1.00 25.61
ATOM 1 12 CB ASP 31 14.046 5.803 34.279 1.00 27.66
ATOM 1 13 CG ASP 31 14.980 6.441 33.272 1.00 28.50
AATTOOMM 11 1144 O0DD11 AASSPP 3311 15.124 7.678 33.341 1.00 32.51
ATOM 1 15 OD2 ASP 31 15.565 5.722 32.421 1.00 26.62
ATOM 1 16 C ASP 31 12.305 4.614 32.960 1.00 27.35
ATOM 1 17 O ASP 31 11.473 3.779 33.296 1.00 26.20
ATOM 118 N GLU 32 13.029 4.535 31.848 1.00 31.20
AATTOOMM 112200 CCAA GGLLUU 3322 12.929 3.449 30.878 1.00 37.1 1
ATOM 121 CB GLU 32 14.334 2.993 30.481 1.0045.22
ATOM 122 CG GLU 32 14.851 3.576 29.168 1.0055.37
ATOM 123 CD GLU 32 15.622 2.550 28.346 1.00 60.84
ATOM 124 OE1 GLU 32 16.696 2.903 27.797 1.00 61.55
AATTOOMM 112255 OOEE22 GGLLUU 3322 15.144 1.391 28.258 1.00 62.76
ATOM 126 C GLU 32 12.111 2.232 31.315 1.00 35.09
ATOM 127 O GLU 32 1 1.200 1.806 30.599 1.0040.02
ATOM 128 N GLY 33 12.432 1.662 32.471 1.00 29.53
ATOM 130 CA GLY 33 11.678 0.507 32.932 1.00 23.70
AATTOOMM 113311 CC GGLLYY 3333 11.576 0.455 34.441 1.00 21.62
ATOM 132 O GLY 33 11.306 -0.601 35.023 1.00 21.32
ATOM 133 N VAL 34 11.792 1.600 35.081 1.00 17.10
ATOM 135 CA VAL 34 11.749 1.668 36.535 1.00 15.86
ATOM 136 CB VAL 34 13.131 2.161 37.106 1.00 16.78
AATTOOMM 113377 CCGGII VVAALL 3344 13.941 2.822 36.014 1.00 16.22
ATOM 138 CG2 VAL 34 12.934 3.1 14 38.270 1.00 18.31
ATOM 139 C VAL 34 10.598 2.535 37.057 1.00 15.22
ATOM 140 O VAL 34 10.375 3.659 36.600 1.00 12.26
ATOM 141 N TYR 35 9.877 1.999 38.035 1.00 14.26
AATTOOMM 114433 CCAA TTYYRR 3355 8.746 2.697 38.607 1.00 11.58
ATOM 144 CB TYR 35 7.484 1.874 38.371 1.00 11.60
ATOM 145 CG TYR 35 6.957 1.928 36.956 1.00 9.68
ATOM 146 CD1 TYR 35 7.486 1.096 35.962 1.00 8.64 ATOM 147 CE1 TYR 35 7.004 1.141 34.644 1.00 10.22
ATOM 148 CD2 TYR 35 5.926 2.806 36.608 1.00 6.92
ATOM 149 CE2 TYR 35 5.437 2.859 35.299 1.00 9.42
ATOM 150 CZ TYR 35 5.981 2.029 34.318 1.00 9.59 ATOM 151 OH TYR 35 5.541 2.1 19 33.015 1.00 4.78
ATOM 153 C TYR 35 8.884 2.979 40.100 1.00 12.36
ATOM 154 0 TYR 35 9.539 2.243 40.836 1.00 12.37
ATOM 155 N VAL 36 8.244 4.051 40.539 1.00 11.38
ATOM 157 CA VAL 36 8.252 4.435 41.939 1.00 12.15 ATOM 158 CB VAL 36 8.467 5.963 42.084 1.00 11.03
ATOM 159 CGI VAL 36 9.063 6.295 43.455 1.00 5.43
ATOM 160 CG2 VAL 36 9.349 6.463 40.955 1.00 6.14
ATOM 161 C VAL 36 6.894 4.076 42.550 1.00 13.54
ATOM 162 0 VAL 36 5.865 4.619 42.139 1.00 13.52 ATOM 163 N HIS 37 6.877 3.170 43.523 1.00 12.07
ATOM 165 CA HIS 37 5.61 1 2.810 44.153 1.00 10.83
ATOM 166 CB HIS 37 5.367 1.298 44.039 1.00 10.79
ATOM 167 CG HIS 37 6.204 0.465 44.956 1.00 11.37
ATOM 168 CD2 HIS 37 7.197 -0.419 44.698 1.00 9.96 ATOM 169 ND1 HIS 37 6.029 0.457 46.326 1.00 14.18
ATOM 171 CE1 HIS 37 6.879 -0.394 46.872 1.00 13.27
ATOM 172 NE2 HIS 37 7.599 -0.939 45.905 1.00 12.97
ATOM 174 C HIS 37 5.513 3.274 45.612 1.00 9.86
ATOM 175 O HIS 37 6.243 2.801 46.482 1.00 11.84 ATOM 176 N THR 38 4.604 4.209 45.882 1.00 6.46
ATOM 178 CA THR 38 4.462 4.729 47.236 1.00 3.87
ATOM 179 CB THR 38 4.400 6.266 47.241 1.00 2.46
ATOM 180 OG1 THR 38 5.1 19 6.780 46.1 12 1.00 2.46
ATOM 182 CG2 THR 38 5.015 6.808 48.513 1.00 2.46 ATOM 183 C THR 38 3.260 4.194 47.998 1.00 4.06
ATOM 184 O THR 38 2.171 4.018 47.436 1.00 4.17
ATOM 185 N SER 39 3.481 3.926 49.283 1.00 5.84
ATOM 187 CA SER 39 2.442 3.422 50.172 1.00 7.90
ATOM 188 CB SER 39 2.718 1.965 50.566 1.00 13.12 ATOM 189 OG SER 39 3.862 1.855 51.388 1.00 19.00
ATOM 191 C SER 39 2.473 4.323 51.395 1.00 7.18
ATOM 192 O SER 39 3.462 5.018 51.625 1.00 8.52
ATOM 193 N PHE 40 1.402 4.323 52.179 1.00 6.84 ATOM 195 CA PHE 40 1.343 5.209 53.334 1.00 6.23
ATOM 196 CB PHE 40 0.310 6.317 53.100 1.00 2.46
ATOM 197 CG PHE 40 0.530 7.093 51.829 1.00 3.29
ATOM 198 CD1 PHE 40 0.191 6.544 50.598 1.00 2.46
ATOM 199 CD2 PHE 40 1.1 1 1 8.355 51.863 1.00 4.97
ATOM 200 CE1 PHE 40 0.431 7.235 49.418 1.00 5.07
ATOM 201 CE2 PHE 40 1.356 9.057 50.689 1.00 6.82
ATOM 202 CZ PHE 40 1.016 8.493 49.462 1.00 8.45
ATOM 203 C PHE 40 0.963 4.476 54.571 1.00 8.69 ATOM 204 O PHE 40 0.176 3.550 54.511 1.00 15.31
ATOM 205 N GLU 41 1.505 4.891 55.704 1.00 10.24
ATOM 207 CA GLU 41 1.158 4.241 56.951 1.00 15.19
ATOM 208 CB GLU 41 2.076 3.062 57.231 0.00 11.57
ATOM 209 CG GLU 41 1.630 2.270 58.434 1.00 19.28 ATOM 210 CD GLU 41 0.343 1.527 58.184 1.00 22.36
ATOM 211 OE1 GLU 41 0.384 0.286 58.106 1.00 27.25
ATOM 212 OE2 GLU 41 -0.713 2.173 58.063 1.00 24.17
ATOM 213 C GLU 41 1.230 5.206 58.109 1.0021.90
ATOM 214 O GLU 41 2.082 6.093 58.140 1.00 24.37 ATOM 215 N GLU 42 0.323 5.036 59.062 1.00 26.27
ATOM 217 CA GLU 42 0.314 5.893 60.221 1.00 32.14
ATOM 218 CB GLU 42 -1.102 6.031 60.784 1.00 36.05
ATOM 219 CG GLU 42 -1.185 7.018 61.963 1.00 44.52
ATOM 220 CD GLU 42 -2.618 7.358 62.409 1.0048.75 ATOM 221 OE1 GLU 42 -3.452 7.771 61.559 1.0049.09
ATOM 222 OE2 GLU 42 -2.901 7.220 63.625 1.0049.93
ATOM 223 C GLU 42 1.229 5.301 61.276 1.00 36.47
ATOM 224 O GLU 42 1.1 16 4.125 61.615 1.00 38.10
ATOM 225 N VAL 43 2.160 6.1 13 61.763 1.0041.76 ATOM 227 CA VAL 43 3.077 5.706 62.826 1.0045.81
ATOM 228 CB VAL 43 4.519 5.461 62.315 1.0043.27
ATOM 229 CGI VAL 43 4.499 4.496 61.144 1.0040.03
ATOM 230 CG2 VAL 43 5.172 6.778 61.923 1.0042.70
ATOM 231 C VAL 43 3.070 6.890 63.787 1.00 50.35 ATOM 232 O VAL 43 2.501 7.940 63.468 1.0052.43
ATOM 233 N ASN 44 3.685 6.741 64.953 1.00 55.63
ATOM 235 CA ASN 44 3.710 7.833 65.924 1.00 59.44
ATOM 236 CB ASN 44 3.968 7.266 67.325 1.00 62.13 ATOM 237 CG ASN 44 2.747 6.545 67.904 1.00 65.07
ATOM 238 OD1 ASN 44 2.576 6.472 69.124 1.00 67.06
ATOM 239 ND2 ASN 44 1.895 6.013 67.027 1.00 64.76
ATOM 242 C ASN 44 4.704 8.963 65.607 1.00 60.93 ATOM 243 O ASN 44 5.700 9.152 66.309 1.00 60.49
ATOM 244 N GLY 45 4.412 9.705 64.539 1.00 62.68
ATOM 246 CA GLY 45 5.231 10.833 64.122 1.00 65.62
ATOM 247 C GLY 45 4.248 1 1.984 63.990 1.00 68.99
ATOM 248 O GLY 45 3.146 11.866 64.526 1.00 69.89 ATOM 249 N TRP 46 4.586 13.084 63.310 1.00 69.69
ATOM 251 CA TRP 46 3.591 14.157 63.184 1.00 68.87
ATOM 252 CB TRP 46 4.212 15.528 62.807 1.00 73.19
ATOM 253 CG TRP 46 4.987 15.647 61.501 1.00 79.18
ATOM 254 CD2 TRP 46 4.640 16.457 60.354 1.00 81.91 ATOM 255 CE2 TRP 46 5.715 16.368 59.438 1.00 82.77
ATOM 256 CE3 TRP 46 3.534 17.248 60.017 1.00 82.07
ATOM 257 CD1 TRP 46 6.215 15.1 14 61.227 1.00 80.39
ATOM 258 NE1 TRP 46 6.659 15.544 59.996 1.00 82.16
ATOM 260 CZ2 TRP 46 5.713 17.042 58.203 1.00 82.40 ATOM 261 CZ3 TRP 46 3.534 17.920 58.787 1.00 80.70
ATOM 262 CH2 TRP 46 4.618 17.809 57.900 1.00 79.95
ATOM 263 C TRP 46 2.506 13.742 62.186 1.00 63.62
ATOM 264 O TRP 46 1.855 14.584 61.555 1.00 64.59
ATOM 265 N GLY 47 2.323 12.423 62.062 1.00 56.81 ATOM 267 CA GLY 47 1.299 11.886 61.190 1.0045.08
ATOM 268 C GLY 47 1.570 10.595 60.435 1.00 34.25
ATOM 269 O GLY 47 2.125 9.624 60.954 1.00 30.61
ATOM 270 N VAL 48 1.1 17 10.622 59.187 1.00 27.25
ATOM 272 CA VAL 48 1.230 9.544 58.226 1.00 21.86 ATOM 273 CB VAL 48 0.1 18 9.688 57.167 1.00 22.63
ATOM 274 CGI VAL 48 0.561 9.114 55.812 1.00 23.06
ATOM 275 CG2 VAL 48 -1.134 9.025 57.671 1.00 21.02
ATOM 276 C VAL 48 2.580 9.659 57.544 1.00 19.51
ATOM 277 O VAL 48 3.105 10.761 57.384 1.00 23.03 ATOM 278 N VAL 49 3.147 8.531 57.138 1.00 14.29
ATOM 280 CA VAL 49 4.430 8.582 56.471 1.00 12.34
ATOM 281 CB VAL 49 5.592 8.113 57.412 1.00 14.75
ATOM 282 CGI VAL 49 5.216 8.384 58.870 1.00 13.82 ATOM 283 CG2 VAL 49 5.936 6.629 57.185 1.00 12.04
ATOM 284 C VAL 49 4.453 7.794 55.177 1.00 1 1.00
ATOM 285 O VAL 49 4.123 6.610 55.137 1.00 12.87
ATOM 286 N PRO 50 4.815 8.466 54.085 1.00 7.83 ATOM 287 CD PRO 50 5.145 9.899 54.094 1.00 5.1 1
ATOM 288 CA PRO 50 4.908 7.887 52.741 1.00 8.54
ATOM 289 CB PRO 50 4.937 9.108 51.842 1.00 7.96
ATOM 290 CG PRO 50 5.585 10.145 52.692 1.00 9.16
ATOM 291 C PRO 50 6.185 7.034 52.607 1.00 10.97 ATOM 292 O PRO 50 7.207 7.322 53.248 1.00 10.81
ATOM 293 N LYS 51 6.129 5.993 51.778 1.00 8.12
ATOM 295 CA LYS 51 7.276 5.1 10 51.597 1.00 3.41
ATOM 296 CB LYS 51 7.105 3.854 52.434 1.00 2.46
ATOM 297 CG LYS 51 8.412 3.231 52.839 1.00 5.99 ATOM 298 CD LYS 51 8.975 2.371 51.730 1.00 7.64
ATOM 299 CE LYS 51 10.295 1.752 52.136 1.00 5.14
ATOM 300 NZ LYS 51 1 1.212 1.692 50.963 1.00 7.48
ATOM 304 C LYS 51 7.481 4.713 50.146 1.00 4.30
ATOM 305 O LYS 51 6.627 4.068 49.532 1.00 3.95 ATOM 306 N HIS 52 8.637 5.090 49.610 1.00 5.87
ATOM 308 CA HIS 52 8.974 4.804 48.227 1.00 3.70
ATOM 309 CB HIS 52 9.901 5.896 47.696 1.00 2.46
ATOM 310 CG HIS 52 9.264 7.250 47.660 1.00 2.48
ATOM 311 CD2 HIS 52 8.550 7.873 46.691 1.00 3.86 ATOM 312 ND1 HIS 52 9.268 8.105 48.741 1.00 2.60
ATOM 314 CE1 HIS 52 8.586 9.196 48.441 1.00 2.46
ATOM 315 NE2 HIS 52 8.139 9.079 47.204 1.00 2.63
ATOM 317 C HIS 52 9.617 3.441 48.046 1.00 5.98
ATOM 318 O HIS 52 10.422 2.992 48.864 1.00 7.00 ATOM 319 N GLY 53 9.236 2.788 46.961 1.00 5.16
ATOM 321 CA GLY 53 9.765 1.482 46.630 1.00 2.46
ATOM 322 C GLY 53 9.869 1.524 45.123 1.00 4.47
ATOM 323 O GLY 53 9.611 2.574 44.504 1.00 3.38
ATOM 324 N LEU 54 10.234 0.410 44.506 1.00 4.22 ATOM 326 CA LEU 54 10.348 0.420 43.058 1.00 6.91
ATOM 327 CB LEU 54 11.789 0.732 42.626 1.00 9.65
ATOM 328 CG LEU 54 12.536 2.004 43.046 1.00 8.39
ATOM 329 CD1 LEU 54 13.956 1.914 42.504 1.00 2.46 ATOM 330 CD2 LEU 54 1 1.828 3.265 42.523 1.00 8.23
ATOM 331 C LEU 54 9.947 -0.883 42.408 1.00 7.1 1
ATOM 332 O LEU 54 9.880 -1.930 43.059 1.00 4.62
ATOM 333 N VAL 55 9.675 -0.787 41.1 10 1.00 7.22 ATOM 335 CA VAL 55 9.339 -1.940 40.295 1.00 8.06
ATOM 336 CB VAL 55 7.828 -2.025 39.918 1.00 7.11
ATOM 337 CGI VAL 55 7.548 -3.342 39.215 1.00 2.46
ATOM 338 CG2 VAL 55 6.973 -1.909 41.148 1.00 2.55
ATOM 339 C VAL 55 10.154 -1.714 39.032 1.00 10.26 ATOM 340 O VAL 55 9.971 -0.728 38.313 1.00 7.95
ATOM 341 N VAL 56 11.092 -2.611 38.795 1.00 11.01
ATOM 343 CA VAL 56 11.924 -2.514 37.622 1.00 11.73
ATOM 344 CB VAL 56 13.394 -2.859 37.938 1.00 11.14
ATOM 345 CGI VAL 56 14.276 -2.346 36.827 1.00 8.66 ATOM 346 CG2 VAL 56 13.802 -2.271 39.272 1.00 2.46
ATOM 347 C VAL 56 1 1.384 -3.551 36.662 1.00 14.99
ATOM 348 O VAL 56 10.932 -4.622 37.085 1.00 16.35
ATOM 349 N LEU 57 11.418 -3.243 35.374 1.00 15.60
ATOM 351 CA LEU 57 10.929 -4.194 34.401 1.00 15.31 ATOM 352 CB LEU 57 9.720 -3.652 33.620 1.00 15.99
ATOM 353 CG LEU 57 8.800 -2.553 34.169 1.00 17.20
ATOM 354 CD1 LEU 57 7.732 -2.264 33.141 1.00 18.91
ATOM 355 CD2 LEU 57 8.147 -2.973 35.474 1.00 21.47
ATOM 356 C LEU 57 12.041 -4.495 33.437 1.00 17.58 ATOM 357 O LEU 57 12.646 -3.591 32.868 1.00 18.26
ATOM 358 N VAL 58 12.335 -5.776 33.296 1.00 20.90
ATOM 360 CA VAL 58 13.339 -6.232 32.360 1.00 24.34
ATOM 361 CB VAL 58 14.458 -7.026 33.071 1.00 23.21
ATOM 362 CGI VAL 58 14.752 -6.385 34.405 1.00 23.46 ATOM 363 CG2 VAL 58 14.066 -8.480 33.263 1.0025.90
ATOM 364 C VAL 58 12.504 -7.117 31.449 1.00 27.46
ATOM 365 O VAL 58 11.913 -8.108 31.895 1.00 28.22
ATOM 366 N ASN 59 12.41 1 -6.730 30.184 1.00 30.99
ATOM 368 CA ASN 59 11.606 -7.484 29.240 1.00 36.66 ATOM 369 CB ASN 59 12.095 -8.933 29.147 1.00 44.10
ATOM 370 CG ASN 59 13.597 -9.033 28.907 1.0049.92
ATOM 371 OD1 ASN 59 14.172 -8.244 28.150 1.00 53.63
ATOM 372 ND2 ASN 59 14.241 -10.009 29.554 1.00 50.97 ATOM 375 C ASN 59 10.171 -7.440 29.764 1.00 37.33
ATOM 376 O ASN 59 9.615 -6.354 29.964 1.00 37.88
ATOM 377 N ALA 60 9.580 -8.610 30.005 1.00 37.00
ATOM 379 CA ALA 60 8.21 1 -8.678 30.507 1.00 36.69 ATOM 380 CB ALA 60 7.376 -9.590 29.621 1.00 36.30
ATOM 381 C ALA 60 8.151 -9.164 31.954 1.00 35.96
ATOM 382 O ALA 60 7.167 -9.777 32.378 1.00 35.76
ATOM 383 N GLU 61 9.204 -8.883 32.714 1.00 34.21
ATOM 385 CA GLU 61 9.258 -9.301 34.102 1.00 31.69 ATOM 386 CB GLU 61 10.369 -10.317 34.300 1.00 32.14
ATOM 387 CG GLU 61 10.470 -11.360 33.220 1.00 33.36
ATOM 388 CD GLU 61 1 1.542 -12.382 33.539 1.00 37.09
ATOM 389 OE1 GLU 61 1 1.327 -13.584 33.269 1.0040.24
ATOM 390 OE2 GLU 61 12.604 -11.978 34.070 1.00 37.49 ATOM 391 C GLU 61 9.500 -8.136 35.040 1.00 30.18
ATOM 392 O GLU 61 10.459 -7.380 34.868 1.00 32.10
ATOM 393 N ALA 62 8.630 -7.999 36.036 1.00 25.78
ATOM 395 CA ALA 62 8.762 -6.935 37.019 1.00 19.57
ATOM 396 CB ALA 62 7.400 -6.375 37.380 1.00 14.26 ATOM 397 C ALA 62 9.457 -7.477 38.264 1.00 17.99
ATOM 398 O ALA 62 9.400 -8.680 38.569 1.00 17.39
ATOM 399 N TYR 63 10.128 -6.579 38.974 1.00 15.73
ATOM 401 CA TYR 63 10.840 -6.957 40.179 1.00 12.88
ATOM 402 CB TYR 63 12.343 -6.946 39.919 1.00 12.90 ATOM 403 CG TYR 63 12.790 -8.161 39.136 1.00 12.44
ATOM 404 CD1 TYR 63 12.716 -8.178 37.736 1.00 10.50
ATOM 405 CE1 TYR 63 13.057 -9.324 37.009 1.00 8.16
ATOM 406 CD2 TYR 63 13.227 -9.318 39.791 1.00 6.75
ATOM 407 CE2 TYR 63 13.572 -10.467 39.072 1.00 5.04 ATOM 408 CZ TYR 63 13.478 -10.464 37.684 1.00 5.91
ATOM 409 OH TYR 63 13.741 -11.61 1 36.975 1.00 4.38
ATOM 411 C TYR 63 10.453 -5.962 41.244 1.00 9.71
ATOM 412 O TYR 63 10.444 -4.752 41.008 1.00 9.84
ATOM 413 N LEU 64 10.1 12 -6.474 42.414 1.00 4.33 ATOM 415 CA LEU 64 9.679 -5.602 43.467 1.00 2.48
ATOM 416 CB LEU 64 8.524 -6.237 44.234 1.00 2.92
ATOM 417 CG LEU 64 7.171 -6.187 43.522 1.00 2.46
ATOM 418 CD1 LEU 64 6.079 -6.582 44.492 1.00 3.16 ATOM 419 CD2 LEU 64 6.921 -4.794 42.984 1.00 2.46
ATOM 420 C LEU 64 10.776 -5.258 44.412 1.00 2.46
ATOM 421 O LEU 64 11.194 -6.099 45.21 1 1.00 2.96
ATOM 422 N ILE 65 11.249 -4.018 44.318 1.00 2.46 ATOM 424 CA ILE 65 12.292 -3.543 45.223 1.00 2.46
ATOM 425 CB ILE 65 13.157 -2.434 44.61 1 1.00 2.46
ATOM 426 CG2 ILE 65 14.366 -2.213 45.501 1.00 2.46
ATOM 427 CGI ILE 65 13.587 -2.808 43.190 1.00 2.46
ATOM 428 CD1 ILE 65 14.029 -4.250 43.040 1.00 2.88 ATOM 429 C ILE 65 1 1.580 -2.974 46.436 1.00 2.46
ATOM 430 O ILE 65 1 1.171 -1.805 46.448 1.00 2.46
ATOM 431 N ASP 66 11.434 -3.827 47.446 1.00 2.46
ATOM 433 CA ASP 66 10.746 -3.492 48.688 1.00 2.46
ATOM 434 CB ASP 66 11.048 -2.045 49.107 1.00 2.46 ATOM 435 CG ASP 66 12.173 -1.957 50.121 1.00 2.46
ATOM 436 OD1 ASP 66 13.011 -2.881 50.179 1.00 2.46
ATOM 437 OD2 ASP 66 12.217 -0.962 50.863 1.00 2.46
ATOM 438 C ASP 66 9.261 -3.672 48.412 1.00 2.46
ATOM 439 O ASP 66 8.842 -3.640 47.255 1.00 2.46 ATOM 440 N THR 67 8.466 -3.894 49.451 1.00 2.46
ATOM 442 CA THR 67 7.028 -4.054 49.257 1.00 2.46
ATOM 443 CB THR 67 6.575 -5.500 49.547 1.00 2.46
ATOM 444 OG1 THR 67 6.888 -5.846 50.902 1.00 6.96
ATOM 446 CG2 THR 67 7.275 -6.468 48.611 1.00 2.46 ATOM 447 C THR 67 6.270 -3.088 50.168 1.00 5.44
ATOM 448 O THR 67 6.806 -2.642 51.180 1.00 3.61
ATOM 449 N PRO 68 5.036 -2.706 49.795 1.00 5.98
ATOM 450 CD PRO 68 4.255 -3.000 48.579 1.00 2.46
ATOM 451 CA PRO 68 4.332 -1.782 50.693 1.00 2.46 ATOM 452 CB PRO 68 3.030 -1.476 49.949 1.00 4.24
ATOM 453 CG PRO 68 3.353 -1.804 48.482 1.00 3.34
ATOM 454 C PRO 68 4.1 19 -2.393 52.082 1.00 3.60
ATOM 455 O PRO 68 4.526 -3.529 52.330 1.00 2.46
ATOM 456 N PHE 69 3.505 -1.636 52.988 1.00 6.72 ATOM 458 CA PHE 69 3.271 -2.1 16 54.363 1.00 10.44
ATOM 459 CB PHE 69 2.752 -0.992 55.272 1.00 8.42
ATOM 460 CG PHE 69 3.575 0.257 55.253 1.00 4.32
ATOM 461 CD 1 PHE 69 3.654 1.036 54.11 1 1.00 2.46 ATOM 462 CD2 PHE 69 4.218 0.686 56.406 1.00 2.46
ATOM 463 CE1 PHE 69 4.357 2.227 54.125 1.00 2.46
ATOM 464 CE2 PHE 69 4.921 1.872 56.430 1.00 2.46
ATOM 465 CZ PHE 69 4.992 2.648 55.292 1.00 2.66 ATOM 466 C PHE 69 2.254 -3.249 54.473 1.00 12.74
ATOM 467 O PHE 69 2.394 -4.163 55.287 1.00 12.75
ATOM 468 N THR 70 1.219 -3.162 53.653 1.00 11.90
ATOM 470 CA THR 70 0.144 -4.123 53.692 1.00 12.1 1
ATOM 471 CB THR 70 -1.150 -3.393 53.769 1.00 17.15 ATOM 472 OG1 THR 70 -1.102 -2.309 52.831 1.00 18.75
ATOM 474 CG2 THR 70 -1.372 -2.858 55.181 1.00 21.18
ATOM 475 C THR 70 0.055 -5.033 52.496 1.00 1 1.19
ATOM 476 O THR 70 0.740 -4.825 51.486 1.00 13.29
ATOM 477 N ALA 71 -0.827 -6.025 52.621 1.00 6.28 ATOM 479 CA ALA 71 -1.066 -6.990 51.564 1.00 5.18
ATOM 480 CB ALA 71 -1.788 -8.182 52.108 1.00 3.93
ATOM 481 C ALA 71 -1.929 -6.291 50.540 1.00 7.92
ATOM 482 O ALA 71 -1.713 -6.424 49.333 1.00 7.37
ATOM 483 N LYS 72 -2.905 -5.535 51.041 1.00 10.84 ATOM 485 CA LYS 72 -3.826 -4.789 50.189 1.00 12.50
ATOM 486 CB LYS 72 -4.639 -3.796 51.031 1.00 15.99
ATOM 487 CG LYS 72 -5.138 -2.564 50.280 1.00 21.35
ATOM 488 CD LYS 72 -5.631 -1.488 51.251 1.00 26.52
ATOM 489 CE LYS 72 -6.796 -0.681 50.671 1.00 30.37 ATOM 490 NZ LYS 72 -8.102 -1.429 50.695 1.00 32.66
ATOM 494 C LYS 72 -3.038 -4.043 49.124 1.00 13.48
ATOM 495 O LYS 72 -3.271 -4.219 47.928 1.00 14.93
ATOM 496 N ASP 73 -2.091 -3.220 49.564 1.00 10.83
ATOM 498 CA ASP 73 -1.280 -2.446 48.639 1.00 7.27 ATOM 499 CB ASP 73 -0.505 -1.380 49.408 1.00 9.87
ATOM 500 CG ASP 73 -1.392 -0.209 49.848 1.00 15.34
ATOM 501 OD1 ASP 73 -1.258 0.240 51.010 1.00 17.89
ATOM 502 OD2 ASP 73 -2.221 0.267 49.033 1.00 18.29
ATOM 503 C ASP 73 -0.339 -3.340 47.835 1.00 5.46 ATOM 504 O ASP 73 -0.119 -3.099 46.649 1.00 2.46
ATOM 505 N THR 74 0.205 -4.378 48.466 1.00 4.34
ATOM 507 CA THR 74 1.105 -5.302 47.769 1.00 2.46
ATOM 508 CB THR 74 1.700 -6.346 48.752 1.00 2.46 ATOM 509 OG1 THR 74 2.573 -5.681 49.673 1.00 2.46
ATOM 511 CG2 THR 74 2.493 -7.424 48.003 1.00 2.46
ATOM 512 C THR 74 0.363 -6.036 46.641 1.00 2.46
ATOM 513 O THR 74 0.895 -6.263 45.553 1.00 2.46 ATOM 514 N GLU 75 -0.883 -6.390 46.906 1.00 2.63
ATOM 516 CA GLU 75 -1.696 -7.092 45.927 1.00 6.19
ATOM 517 CB GLU 75 -2.907 -7.697 46.645 1.00 12.20
ATOM 518 CG GLU 75 -4.245 -7.388 46.033 1.00 18.61
ATOM 519 CD GLU 75 -4.652 -8.456 45.057 1.00 23.22 ATOM 520 OE1 GLU 75 -5.1 18 -9.527 45.514 1.00 27.63
ATOM 521 OE2 GLU 75 -4.497 -8.224 43.835 1.00 25.80
ATOM 522 C GLU 75 -2.1 16 -6.090 44.850 1.00 6.00
ATOM 523 O GLU 75 -2.036 -6.363 43.655 1.00 2.46
ATOM 524 N LYS 76 -2.543 -4.915 45.305 1.00 8.18 ATOM 526 CA LYS 76 -2.973 -3.830 44.433 1.00 8.99
ATOM 527 CB LYS 76 -3.321 -2.600 45.278 1.00 11.28
ATOM 528 CG LYS 76 -4.208 -1.581 44.584 1.00 16.74
ATOM 529 CD LYS 76 -5.031 -0.795 45.594 1.00 21.41
ATOM 530 CE LYS 76 -4.476 0.622 45.789 1.00 27.48 ATOM 531 NZ LYS 76 -4.832 1.228 47.1 19 1.00 25.63
ATOM 535 C LYS 76 -1.852 -3.487 43.460 1.00 7.58
ATOM 536 O LYS 76 -2.086 -3.240 42.282 1.00 5.12
ATOM 537 N LEU 77 -0.630 -3.486 43.978 1.00 8.40
ATOM 539 CA LEU 77 0.564 -3.181 43.200 1.00 7.16 ATOM 540 CB LEU 77 1.740 -2.992 44.163 1.00 5.71
ATOM 541 CG LEU 77 3.180 -2.910 43.652 1.00 2.72
ATOM 542 CD1 LEU 77 3.262 -1.933 42.487 1.00 3.77
ATOM 543 CD2 LEU 77 4.093 -2.469 44.807 1.00 2.46
ATOM 544 C LEU 77 0.867 -4.292 42.186 1.00 6.09 ATOM 545 O LEU 77 1.150 -4.015 41.017 1.00 2.46
ATOM 546 N VAL 78 0.795 -5.544 42.636 1.00 6.11
ATOM 548 CA VAL 78 1.064 -6.678 41.761 1.00 8.26
ATOM 549 CB VAL 78 0.903 -8.027 42.483 1.00 7.11
ATOM 550 CGI VAL 78 0.988 -9.148 41.479 1.00 4.37 ATOM 551 CG2 VAL 78 1.967 -8.193 43.544 1.00 7.47
ATOM 552 C VAL 78 0.125 -6.698 40.568 1.00 12.17
ATOM 553 O VAL 78 0.572 -6.783 39.426 1.00 13.19
ATOM 554 N THR 79 - 1.177 -6.616 40.831 1.00 14.74 ATOM 556 CA THR 79 -2.174 -6.654 39.759 1.00 12.53
ATOM 557 CB THR 79 -3.603 -6.682 40.306 1.00 9.09
ATOM 558 0G1 THR 79 -3.727 -5.697 41.330 1.00 6.52
ATOM 560 CG2 THR 79 -3.934 -8.068 40.868 1.00 8.36 ATOM 561 C THR 79 -2.074 -5.488 38.796 1.00 1 1.61
ATOM 562 O THR 79 -2.238 -5.675 37.595 1.00 9.35
ATOM 563 N TRP 80 -1.813 -4.291 39.311 1.00 1 1.27
ATOM 565 CA TRP 80 -1.696 -3.125 38.445 1.00 13.67
ATOM 566 CB TRP 80 -1.248 -1.910 39.246 1.00 20.70 ATOM 567 CG TRP 80 -1.245 -0.622 38.467 1.00 27.36
ATOM 568 CD2 TRP 80 -0.243 -0.179 37.540 1.00 29.87
ATOM 569 CE2 TRP 80 -0.650 1.087 37.058 1.00 31.26
ATOM 570 CE3 TRP 80 0.956 -0.729 37.069 1.00 29.38
ATOM 571 CD1 TRP 80 -2.190 0.368 38.510 1.00 29.40 ATOM 572 NE1 TRP 80 -1.839 1.396 37.667 1.00 31.65
ATOM 574 CZ2 TRP 80 0.100 1.811 36.127 1.00 31.35
ATOM 575 CZ3 TRP 80 1.702 -0.009 36.144 1.00 30.77
ATOM 576 CH2 TRP 80 1.268 1.250 35.684 1.00 31.34
ATOM 577 C TRP 80 -0.680 -3.419 37.349 1.00 14.96 ATOM 578 O TRP 80 -0.789 -2.903 36.229 1.00 17.33
ATOM 579 N PHE 81 0.301 -4.259 37.674 1.00 15.43
ATOM 581 CA PHE 81 1.339 -4.633 36.718 1.00 13.50
ATOM 582 CB PHE 81 2.675 -4.852 37.444 1.00 12.11
ATOM 583 CG PHE 81 3.535 -3.612 37.510 1.00 10.82 ATOM 584 CD1 PHE 81 3.577 -2.833 38.671 1.00 8.61
ATOM 585 CD2 PHE 81 4.280 -3.206 36.403 1.00 8.83
ATOM 586 CE1 PHE 81 4.345 -1.671 38.726 1.00 4.05
ATOM 587 CE2 PHE 81 5.048 -2.047 36.449 1.00 3.64
ATOM 588 CZ PHE 81 5.078 -1.282 37.610 1.00 5.70 ATOM 589 C PHE 81 0.960 -5.880 35.913 1.00 13.39
ATOM 590 O PHE 81 1.144 -5.912 34.692 1.00 1 1.74
ATOM 591 N VAL 82 0.437 -6.899 36.590 1.00 1 1.86
ATOM 593 CA VAL 82 0.018 -8.130 35.922 1.00 11.91
ATOM 594 CB VAL 82 -0.531 -9.1 17 36.940 1.00 11.45 ATOM 595 CGI VAL 82 -0.996 -10.392 36.252 1.00 12.26
ATOM 596 CG2 VAL 82 0.538 -9.410 37.958 1.00 11.00
ATOM 597 C VAL 82 -1.073 -7.807 34.905 1.00 13.63
ATOM 598 O VAL 82 -1.203 -8.462 33.866 1.00 8.62 ATOM 599 N GLU 83 -1.851 -6.778 35.233 1.00 17.12
ATOM 601 CA GLU 83 -2.928 -6.286 34.385 1.00 18.66
ATOM 602 CB GLU 83 -3.630 -5.105 35.060 1.00 21.00
ATOM 603 CG GLU 83 -5.134 -5.085 34.875 1.00 28.49
ATOM 604 CD GLU 83 -5.874 -5.802 36.001 1.00 37.35
ATOM 605 OE1 GLU 83 -6.109 -5.158 37.051 1.00 40.57
ATOM 606 OE2 GLU 83 -6.222 -7.003 35.839 1.00 37.37
ATOM 607 C GLU 83 -2.286 -5.812 33.093 1.00 17.65
ATOM 608 O GLU 83 -2.657 -6.249 32.004 1.00 17.50
AATTOOMM 660099 NN AARRGG 8844 -1.313 -4.914 33.232 1.00 17.44
ATOM 611 CA ARG 84 -0.593 -4.372 32.090 1.00 17.50
ATOM 612 CB ARG 84 0.167 -3.104 32.501 1.00 13.27
ATOM 613 CG ARG 84 -0.725 -1.987 33.038 0.00 2.46
ATOM 614 CD ARG 84 -1.692 -1.472 31.976 0.00 2.46
AATTOOMM 661155 NNEE AARRGG 8844 -2.639 -0.499 32.518 0.00 2.46
ATOM 617 CZ ARG 84 -3.656 0.019 31.835 0.00 2.46 ATOM 618 NH1 ARG 84 -3.868 -0.339 30.575 0.00 2.46 ATOM 621 NH2 ARG 84 -4.465 0.898 32.411 0.00 2.46 ATOM 624 C ARG 84 0.356 -5.409 31.468 1.00 19.99 ATOM 625 O ARG 84 1.305 -5.060 30.774 1.00 19.07 ATOM 626 N GLY 85 0.096 -6.686 31.746 1.00 22.83 ATOM 628 CA GLY 85 0.870 -7.772 31.162 1.00 24.10 ATOM 629 C GLY 85 2.316 -8.068 31.526 1.00 27.07 ATOM 630 O GLY 85 3.138 -8.309 30.630 1.00 26.84 ATOM 631 N TYR 86 2.630 -8.070 32.821 1.00 27.55 ATOM 633 CA TYR 86 3.984 -8.375 33.290 1.00 28.54 ATOM 634 CB TYR 86 4.677 -7.139 33.863 1.00 27.19 ATOM 635 CG TYR 86 4.955 -6.059 32.858 1.00 27.90 ATOM 636 CD1 TYR 86 5.810 -6.289 31.785' 1.00 28.46 ATOM 637 CE1 TYR 86 6.048 -5.301 30.843 1.00 28.67 ATOM 638 CD2 TYR 86 4.343 -4.805 32.967 1.00 26.53 ATOM 639 CE2 TYR 86 4.575 -3.815 32.030 1.00 24.57 ATOM 640 CZ TYR 86 5.425 -4.073 30.973 1.00 26.05 ATOM 641 OH TYR 86 5.647 -3.1 12 30.030 1.00 30.81 ATOM 643 C TYR 86 3.892 -9.399 34.400 1.00 30.50 ATOM 644 O TYR 86 3.064 -9.265 35.306 1.00 33.72 ATOM 645 N LYS 87 4.746 -10.413 34.340 1.00 28.43 ATOM 647 CA LYS 87 4.759 -11.444 35.368 1.00 26.34 ATOM 648 CB LYS 87 5.210-12.79034.786 1.0032.15
ATOM 649 CG LYS 87 5.950-12.69033.448 1.0035.82
ATOM 650 CD LYS 87 5.003-12.35632.284 1.0036.47
ATOM 651 CE LYS 87 5.698-12.51930.938 1.0034.41 ATOM 652 NZ LYS 87 4.751-12.48029.795 1.0031.87
ATOM 656 C LYS 87 5.734-10.99036.437 1.0020.66
ATOM 6570 LYS 87 6.879-10.68036.138 1.0019.58
ATOM 658 N ILE 88 5.267-10.93237.675 1.0017.24
ATOM 660 CA ILE 88 6.096-10.52038.803 1.0015.47 ATOM 661 CB ILE 88 5.225-10.34640.039 1.0015.74
ATOM 662 CG2ILE 88 6.081-10.38741.288 1.0019.38
ATOM 663 CGI ILE 88 4.443 -9.03939.935 1.0017.13
ATOM 664 CD 1 ILE 88 3.759 -8.83638.605 1.0019.87
ATOM 665 C ILE 88 7.143-11.59939.086 1.0016.38 ATOM 6660 ILE 88 6.810-12.65939.607 1.0016.01
ATOM 667 N LYS 89 8.404 -11.34238.762 1.0015.75
ATOM 669 CA LYS 89 9.423-12.36238.979 1.0016.51
ATOM 670 CB LYS 89 10.653-12.07638.128 1.0015.28
ATOM 671 CG LYS 89 10.948-13.161 37.134 1.0019.51 ATOM 672 CD LYS 89 9.868-13.181 36.075 1.0027.30
ATOM 673 CE LYS 89 9.557-14.59335.626 1.0032.75
ATOM 674 NZ LYS 89 8.207-14.661 34.988 1.0037.24
ATOM 678 C LYS 89 9.847-12.53740.430 1.0017.49
ATOM 679 O LYS 89 10.320-13.60540.826 1.0019.66 ATOM 680 N GLY 90 9.688-11.49541.228 1.0013.39
ATOM 682 CA GLY 90 10.077-11.62442.612 1.008.27
ATOM 683 C GLY 90 10.203-10.281 43.284 1.009.34
ATOM 684 O GLY 90 9.910 -9.23542.694 1.009.40
ATOM 685 N SER 91 10.643-10.31844.532 1.009.45 ATOM 687 CA SER 91 10.809 -9.111 45.313 1.0012.38
ATOM 688 CB SER 91 9.635 -8.95946.278 1.0012.95
ATOM 689 OG SER 91 9.842 -9.78447.425 1.0015.65
ATOM 691 C SER 91 12.091 -9.22246.121 1.0012.74
ATOM 6920 SER 91 12.613-10.31846.333 1.0013.68 ATOM 693 N ILE 92 12.596 -8.081 46.574 1.008.40
ATOM 695 CA ILE 92 13.787 -8.05747.403 1.002.94
ATOM 696 CB ILE 92 15.052 -7.78946.581 1.004.17
ATOM 697 CG2ILE 92 14.835 -6.58045.665 1.002.46 ATOM 698 CGI ILE 92 16.240 -7.652 47.538 1.00 2.46
ATOM 699 CD 1 ILE 92 17.252 -6.604 47.150 1.00 2.46
ATOM 700 C ILE 92 13.570 -6.921 48.382 1.00 2.46
ATOM 701 O ILE 92 13.339 -5.787 47.972 1.00 2.46 ATOM 702 N SER 93 13.603 -7.233 49.672 1.00 2.46
ATOM 704 CA SER 93 13.406 -6.215 50.692 1.00 2.46
ATOM 705 CB SER 93 12.725 -6.815 51.928 1.00 2.46
ATOM 706 OG SER 93 11.333 -6.983 51.728 1.00 2.46
ATOM 708 C SER 93 14.773 -5.674 51.079 1.00 3.99 ATOM 709 O SER 93 15.711 -6.462 51.274 1.00 9.05
ATOM 710 N SER 94 14.885 -4.350 51.194 1.00 2.46
ATOM 712 CA SER 94 16.145 -3.718 51.546 1.00 2.46
ATOM 713 CB SER 94 16.118 -2.234 51.167 1.00 2.46
ATOM 714 OG SER 94 15.337 -1.435 52.051 1.00 9.44 ATOM 716 C SER 94 16.479 -3.896 53.018 1.00 2.46
ATOM 717 O SER 94 17.645 -3.868 53.381 1.00 2.46
ATOM 718 N HIS 95 15.459 -4.064 53.865 1.00 2.46
ATOM 720 CA HIS 95 15.656 -4.304 55.308 1.00 2.46
ATOM 721 C HIS 95 14.434 -4.935 56.013 1.00 2.46 ATOM 722 O HIS 95 13.340 -4.995 55.453 1.00 2.46
ATOM 723 CB HIS 95 16.184 -3.043 56.031 1.00 2.46
ATOM 724 CG HIS 95 15.134 -2.064 56.471 1.00 2.46
ATOM 725 ND1 HIS 95 14.465 -1.205 55.624 1.00 7.22
ATOM 727 CD2 HIS 95 14.736 -1.717 57.724 1.00 2.84 ATOM 728 NE2 HIS 95 13.840 -0.656 57.667 1.00 2.46
ATOM 729 CE1 HIS 95 13.706 -0.382 56.382 1.00 6.47
ATOM 730 N PHE 96 14.645 -5.440 57.228 1.00 2.46
ATOM 732 CA PHE 96 13.609 -6.151 57.971 1.00 2.46
ATOM 733 CB PHE 96 14.244 -6.957 59.113 1.00 2.46 ATOM 734 CG PHE 96 14.494 -6.163 60.358 1.00 2.46
ATOM 735 CD1 PHE 96 15.556 -5.272 60.425 1.00 2.46
ATOM 736 CD2 PHE 96 13.671 -6.315 61.472 1.00 2.46
ATOM 737 CE1 PHE 96 15.799 -4.543 61.581 1.00 2.46
ATOM 738 CE2 PHE 96 13.896 -5.596 62.634 1.00 2.46 ATOM 739 CZ PHE 96 14.964 -4.707 62.690 1.00 2.46
ATOM 740 C PHE 96 12.432 -5.372 58.508 1.00 2.46
ATOM 741 O PHE 96 1 1.556 -5.941 59.140 1.00 4.40
ATOM 742 N HIS 97 12.383 -4.076 58.264 1.00 2.46 ATOM 744 CA HIS 97 1 1.257 -3.316 58.762 1.00 3.68
ATOM 745 C HIS 97 10.080 -3.473 57.810 1.00 9.16
ATOM 746 O HIS 97 10.253 -3.903 56.661 1.00 9.21
ATOM 747 CB HIS 97 1 1.651 -1.865 58.935 1.00 2.46 ATOM 748 CG HIS 97 12.542 -1.634 60.1 12 1.00 2.46
ATOM 749 ND1 HIS 97 13.325 -0.509 60.215 1.00 2.46
ATOM 750 CE1 HIS 97 13.953 -0.617 61.371 1.00 3.53
ATOM 751 CD2 HIS 97 12.716 -2.410 61.214 1.00 2.46
ATOM 752 NE2 HIS 97 13.620 -1.754 62.016 1.00 2.46 ATOM 754 N SER 98 8.888 -3.139 58.303 1.00 12.50
ATOM 756 CA SER 98 7.634 -3.270 57.554 1.00 12.71
ATOM 757 CB SER 98 6.466 -2.952 58.472 1.00 1 1.40
ATOM 758 OG SER 98 6.740 -3.441 59.769 1.00 16.65
ATOM 760 C SER 98 7.492 -2.464 56.276 1.00 12.38 ATOM 761 O SER 98 6.988 -2.976 55.276 1.00 14.47
ATOM 762 N ASP 99 7.914 -1.209 56.292 1.00 10.04
ATOM 764 CA ASP 99 7.800 -0.397 55.089 1.00 12.17
ATOM 765 CB ASP 99 8.424 0.985 55.294 1.00 17.84
ATOM 766 CG ASP 99 9.542 0.975 56.312 1.0023.25 ATOM 767 OD1 ASP 99 9.306 0.494 57.439 1.00 24.60
ATOM 768 OD2 ASP 99 10.655 1.450 55.989 1.00 28.50
ATOM 769 C ASP 99 8.502 -1.104 53.941 1.00 12.02
ATOM 770 O ASP 99 8.419 -0.668 52.783 1.00 12.47
ATOM 771 N SER 100 9.191 -2.197 54.263 1.00 8.14 ATOM 773 CA SER 100 9.905 -2.958 53.252 1.00 6.64
ATOM 774 CB SER 100 1 1.417 -2.892 53.520 1.00 5.10
ATOM 775 OG SER 100 12.017 -1.743 52.951 1.00 2.46
ATOM 777 C SER 100 9.475 -4.423 53.167 1.00 7.44
ATOM 778 O SER 100 9.469 -5.014 52.086 1.00 9.76 ATOM 779 N THR 101 9.089 -5.000 54.296 1.00 6.76
ATOM 781 CA THR 101 8.734 -6.416 54.330 1.00 6.66
ATOM 782 CB THR 101 9.598 -7.1 17 55.401 1.00 3.38
ATOM 783 0G1 THR 101 9.458 -6.438 56.659 1.00 2.46
ATOM 785 CG2 THR 101 1 1.065 -7.080 54.980 1.00 2.46 ATOM 786 C THR 101 7.267 -6.805 54.546 1.00 9.05
ATOM 787 O THR 101 6.941 -7.996 54.589 1.00 9.68
ATOM 788 N GLY 102 6.391 -5.810 54.676 1.00 10.09
ATOM 790 CA GLY 102 4.975 -6.069 54.907 1.00 9.79 ATOM 791 C GLY 102 4.276 -7.001 53.931 1.0012.36
ATOM 792 O GLY 102 3.625 -7.96854.335 1.0013.95
ATOM 793 N GLY 103 4.415 -6.71052.642 1.0013.20
ATOM 795 CA GLY 103 3.777 -7.52251.621 1.0010.82 ATOM 796 C GLY 103 4.408 -8.86551.287 1.009.45
ATOM 797 O GLY 103 4.033 -9.50050.293 1.008.27
ATOM 798 N ILE 104 5.360 -9.31252.099 1.008.37
ATOM 800 CA ILE 104 5.999-10.59551.827 1.007.07
ATOM 801 CB ILE 104 7.208-10.87452.773 1.006.08 ATOM 802 CG2ILE 104 7.511-12.36252.802 1.0010.47
ATOM 803 CGI ILE 104 8.462-10.16052.276 1.002.46
ATOM 804 CD 1 ILE 104 9.657-10.40653.151 1.002.46
ATOM 805 C ILE 104 4.960-11.69052.023 1.004.13
ATOM 806 O ILE 104 4.667-12.43751.085 1.004.68 ATOM 807 N GLU 105 4.407 -11.77353.238 1.002.86
ATOM 809 CA GLU 105 3.396-12.77853.557 1.002.46
ATOM 810 CB GLU 105 2.511-12.30754.699 1.003.61
ATOM 811 CG GLU 105 2.153-13.39055.680 1.008.76
ATOM 812 CD GLU 105 1.801-12.81957.039 1.0015.30 ATOM 8130E1GLU 105 2.728-12.521 57.827 1.0011.11
ATOM 814 OE2GLU 105 0.589-12.65857.314 1.0018.47
ATOM 815 C GLU 105 2.538-13.01652.338 1.002.90
ATOM 816 O GLU 105 2.600-14.08251.742 1.002.74
ATOM 817 N TRP 106 1.750-12.01351.961 1.002.46 ATOM 819 CA TRP 106 0.902-12.13950.787 1.003.29
ATOM 820 CB TRP 106 0.429 -10.76850.295 1.005.24
ATOM 821 CG TRP 106 -0.618-10.84949.181 1.005.66
ATOM 822 CD2TRP 106 -0.400-10.771 47.760 1.004.92
ATOM 823 CE2TRP 106 -1.666-10.86547.136 1.007.38 ATOM 824 CE3TRP 106 0.736-10.63046.958 1.008.55
ATOM 825 CD 1 TRP 106 -1.965-10.98749.346 1.007.99
ATOM 826 NE1TRP 106 -2.599-10.99748.127 1.009.68
ATOM 828 CZ2TRP 106 -1.832-10.82345.740 1.008.72
ATOM 829 CZ3TRP 106 0.572-10.58645.559 1.0012.99 ATOM 830 CH2TRP 106 -0.707-10.68344.971 1.009.87
ATOM 831 C TRP 106 1.659-12.79349.644 1.004.98
ATOM 8320 TRP 106 1.243-13.82049.105 1.006.80
ATOM 833 N LEU 107 2.770-12.17449.268 1.005.41 ATOM 835 CA LEU 107 3.561 -12.66948.160 1.005.42
ATOM 836 CB LEU 107 4.818-11.80447.988 1.003.37
ATOM 837 CG LEU 107 4.566-10.39647.411 1.002.46
ATOM 838 CD1LEU 107 5.797 -9.54847.598 1.002.46 ATOM 839 CD2LEU 107 4.227-10.47245.928 1.002.78
ATOM 840 C LEU 107 3.912-14.14848.279 1.005.74
ATOM 841 O LEU 107 3.885-14.86447.288 1.005.26
ATOM 842 N ASN 108 4.210-14.62349.482 1.005.99
ATOM 844 CA ASN 108 4.556-16.03549.653 1.008.73 ATOM 845 CB ASN 108 5.148-16.28651.039 1.008.68
ATOM 846 CG ASN 108 6.552-15.74351.174 1.007.33
ATOM 8470D1ASN 108 7.008-15.44452.278 1.008.44
ATOM 848 ND2ASN 108 7.247-15.60550.046 1.005.42
ATOM 851 C ASN 108 3.372-16.96449.455 1.0010.40 ATOM 8520 ASN 108 3.524-18.05948.910 1.0012.41
ATOM 853 N SER 109 2.203-16.51949.919 1.0013.49
ATOM 855 CA SER 109 0.949-17.27249.825 1.0011.11
ATOM 856 CB SER 109 -0.171-16.54250.587 1.008.67
ATOM 857 OG SER 109 -0.589-15.36549.912 1.002.46 ATOM 859 C SER 109 0.568-17.42548.366 1.0013.11
ATOM 860 O SER 109 -0.033-18.43547.975 1.0013.78
ATOM 861 N ARG 110 0.921-16.40547.578 1.0011.97
ATOM 863 CA ARG 110 0.672-16.38646.137 1.0012.48
ATOM 864 CB ARG 110 0.502-14.94345.642 1.0015.18 ATOM 865 CG ARG 110 -0.921-14.38645.744 1.0023.20
ATOM 866 CD ARG 110 -1.871-15.01244.716 1.0030.16
ATOM 867 NE ARG 110 -3.260-15.06345.186 1.0039.60
ATOM 869 CZ ARG 110 -3.682-15.751 46.2521.0044.54
ATOM 870 NH1 ARG 110 -2.837-16.46346.987 1.0045.63 ATOM 873 NH2 ARG 110 -4.964-15.731 46.592 1.0047.38
ATOM 876 C ARG 110 1.893-17.02545.468 1.0011.16
ATOM 877 O ARG 110 1.999-17.08544.244 1.009.00
ATOM 878 N SER 111 2.811-17.48646.312 1.008.44
ATOM 880 CA SER 111 4.055-18.13045.915 1.007.31 ATOM 881 CB SER 111 3.790 -19.591 45.548 1.007.82
ATOM 882 OG SER 111 3.385-19.72644.207 1.0011.76
ATOM 884 C SER 111 4.902-17.44044.833 1.006.80
ATOM 885 O SER 111 5.311-18.061 43.849 1.005.99 ATOM 886 N ILE 112 5.162-16.14945.042 1.007.37
ATOM 888 CA ILE 112 6.017-15.34644.173 1.005.95
ATOM 889 CB ILE 112 5.507-13.91944.041 1.006.17
ATOM 890 CG2ILE 112 6.523-13.08643.254 1.006.05 ATOM 891 CGI ILE 112 4.119-13.90643.393 1.006.15
ATOM 892 CD 1 ILE 112 3.487-12.50343.331 1.007.50
ATOM 893 C ILE 112 7.363-15.28044.922 1.009.37
ATOM 8940 ILE 112 7.408-14.95746.112 1.0010.19
ATOM 895 N PRO 113 8.476-15.54844.230 1.009.01 ATOM 896 CD PRO 113 8.523-15.83542.787 1.0010.58
ATOM 897 CA PRO 113 9.815-15.52944.841 1.009.99
ATOM 898 CB PRO 113 10.747-15.75743.655 1.0013.24
ATOM 899 CG PRO 113 9.884-16.38542.592 1.0012.57
ATOM 900 C PRO 113 10.210-14.26645.631 1.0010.13 ATOM 901 O PRO 113 10.351-13.18645.052 1.0012.22
ATOM 902 N THR 114 10.399-14.40446.946 1.008.28
ATOM 904 CA THR 114 10.805-13.27047.782 1.005.14
ATOM 905 CB THR 114 9.902-13.09349.024 1.006.15
ATOM 906 OG1 THR 114 10.014-14.23949.873 1.004.05 ATOM 908 CG2THR 114 8.463-12.90348.616 1.008.44
ATOM 909 C THR 114 12.258-13.41248.261 1.005.95
ATOM 910 O THR 114 12.704-14.48248.681 1.002.46
ATOM 911 N TYR 115 12.968-12.28948.212 1.0010.17
ATOM 913 CA TYR 115 14.375-12.19948.575 1.008.50 ATOM 914 CB TYR 115 15.129-11.63247.386 1.007.20
ATOM 915 CG TYR 115 15.158-12.60246.241 1.007.63
ATOM 916 CD1TYR 115 14.237-12.52045.197 1.003.83
ATOM 917 CE1TYR 115 14.264-13.43444.149 1.008.09
ATOM 918 CD2TYR 115 16.106-13.62046.212 1.0010.53 ATOM 919 CE2TYR 115 16.144-14.53545.179 1.0013.90
ATOM 920 CZ TYR 115 15.225-14.44244.151 1.0013.33
ATOM 921 OH TYR 115 15.283-15.37643.143 1.0017.63
ATOM 923 C TYR 115 14.670-11.35349.804 1.008.02
ATOM 924 O TYR 115 13.959-10.38650.084 1.0012.01 ATOM 925 N ALA 116 15.735-11.71050.518 1.005.56
ATOM 927 CA ALA 116 16.138-10.99351.718 1.003.86
ATOM 928 CB ALA 116 15.157-11.22952.835 1.005.31
ATOM 929 C ALA 116 17.498-11.46452.147 1.004.49 ATOM 930 O ALA 116 17.775-12.65252.177 1.005.15
ATOM 931 N SER 117 18.358-10.521 52.483 1.007.97
ATOM 933 CA SER 117 19.690-10.87252.928 1.005.56
ATOM 934 CB SER 117 20.458 -9.61653.318 1.003.88 ATOM 935 OG SER 117 20.822 -9.66754.682 1.004.08
ATOM 937 C SER 117 19.542-11.79654.132 1.003.84
ATOM 938 O SER 117 18.532-11.75954.845 1.002.46
ATOM 939 N GLU 118 20.557-12.62554.340 1.003.66
ATOM 941 CA GLU 118 20.575-13.58555.438 1.005.80 ATOM 942 CB GLU 118 21.835-14.46355.289 1.0010.28
ATOM 943 CG GLU 118 22.633-14.76556.560 1.0020.28
ATOM 944 CD GLU 118 23.299-16.14656.523 1.0022.87
ATOM 945 OE1 GLU 118 23.728-16.63657.598 1.0025.77
ATOM 946 OE2GLU 118 23.389-16.74055.419 1.0025.22 ATOM 947 C GLU 118 20.505-12.89256.809 1.003.06
ATOM 948 O GLU 118 20.218-13.51557.834 1.002.46
ATOM 949 N LEU 119 20.744-11.58856.813 1.003.06
ATOM 951 CA LEU 119 20.705-10.831 58.054 1.005.30
ATOM 952 CB LEU 119 21.764 -9.71558.050 1.005.09 ATOM 953 CG LEU 119 23.273-10.02858.052 1.006.85
ATOM 954 CD 1 LEU 119 24.006 -8.83258.651 1.005.83
ATOM 955 CD2LEU 119 23.593-11.311 58.842 1.006.68
ATOM 956 C LEU 119 19.313-10.23458.271 1.007.08
ATOM 957 O LEU 119 18.814-10.21459.400 1.008.36 ATOM 958 N THR 120 18.684 -9.74657.200 1.005.91
ATOM 960 CA THR 120 17.350 -9.171 57.332 1.002.93
ATOM 961 CB THR 120 16.873 -8.40856.055 1.002.46
ATOM 9620G1THR 120 15.947 -9.23255.336 1.006.55
ATOM 964 CG2THR 120 18.038 -8.01855.144 1.002.46 ATOM 965 C THR 120 16.386-10.32557.592 1.005.30
ATOM 966 O THR 120 15.386-10.17358.305 1.007.17
ATOM 967 N ASN 121 16.701-11.48957.029 1.002.46
ATOM 969 CA ASN 121 15.839-12.64457.206 1.002.46
ATOM 970 CB ASN 121 16.165 -13.72356.202 1.002.46 ATOM 971 CG ASN 121 14.967-14.09555.393 1.002.46
ATOM 972 OD1 ASN 121 13.848-13.72055.743 1.002.46
ATOM 973 ND2ASN 121 15.177-14.82254.300 1.003.24
ATOM 976 C ASN 121 15.903-13.22358.590 1.002.46 ATOM 977 O ASN 121 14.912-13.72759.113 1.002.46
ATOM 978 N GLU 122 17.074-13.16259.190 1.002.46
ATOM 980 CA GLU 122 17.200-13.67660.523 1.002.46
ATOM 981 CB GLU 122 18.671 -13.91460.843 1.002.46 ATOM 982 CG GLU 122 18.984-15.361 61.214 1.0011.39
ATOM 983 CD GLU 122 18.615-15.68962.660 1.0022.31
ATOM 9840E1GLU 122 17.951-16.73562.888 1.0027.81
ATOM 985 OE2GLU 122 18.986-14.89863.568 1.0024.77
ATOM 986 C GLU 122 16.570-12.67761.495 1.002.46 ATOM 987 O GLU 122 16.068-13.071 62.546 1.002.46
ATOM 988 N LEU 123 16.584-11.39261.120 1.002.46
ATOM 990 CA LEU 123 16.030-10.30861.936 1.002.46
ATOM 991 CB LEU 123 16.509 -8.96561.405 1.002.46
ATOM 992 CG LEU 123 17.749 -8.42562.134 1.002.46 ATOM 993 CD 1 LEU 123 18.044 -7.01261.657 1.002.46
ATOM 994 CD2LEU 123 17.539 -8.43063.648 1.002.46
ATOM 995 C LEU 123 14.508-10.36761.954 1.002.46
ATOM 996 O LEU 123 13.886-10.18362.998 1.002.46
ATOM 997 N LEU 124 13.910-10.61460.790 1.002.46 ATOM 999 CA LEU 124 12.458-10.781 60.707 1.002.46
ATOM 1000 CB LEU 124 12.023-11.25859.322 1.002.46
ATOM 1001 CG LEU 124 12.281-10.37558.110 1.002.46
ATOM 1002 CD1 LEU 124 12.064-11.21956.863 1.003.14
ATOM 1003 CD2LEU 124 11.351 -9.17458.112 1.002.46 ATOM 1004 C LEU 124 12.153-11.90261.689 1.002.46
ATOM 1005 O LEU 124 11.509-11.67862.700 1.002.46
ATOM 1006 N LYS 125 12.637-13.10861.366 1.005.04
ATOM 1008 CA LYS 125 12.459-14.29462.206 1.007.05
ATOM 1009 CB LYS 125 13.631-15.24962.024 1.005.92 ATOM 1010 CG LYS 125 13.685-16.38863.046 1.0014.42
ATOM 1011 CD LYS 125 14.939-17.26962.865 1.0020.52
ATOM 1012 CE LYS 125 14.668-18.74363.164 1.0027.79
ATOM 1013 NZ LYS 125 13.766-19.41262.158 1.0028.68
ATOM 1017 C LYS 125 12.376-13.89063.668 1.0012.73 ATOM 1018 O LYS 125 11.345-14.071 64.319 1.0016.99
ATOM 1019 N LYS 126 13.476-13.341 64.171 1.0015.72
ATOM 1021 CA LYS 126 13.554-12.88265.554 1.0019.45
ATOM 1022 CB LYS 126 14.777-11.96665.742 1.0022.28 ATOM 1023 CG LYS 126 15.884 -12.506 66.667 1.00 28.87
ATOM 1024 CD LYS 126 15.730 -13.997 66.994 1.00 33.08
ATOM 1025 CE LYS 126 16.407 -14.888 65.953 1.00 34.84
ATOM 1026 NZ LYS 126 16.072 -16.343 66.120 1.00 34.79 ATOM 1030 C LYS 126 12.281 -12.114 65.902 1.00 19.02
ATOM 1031 O LYS 126 11.588 -12.443 66.862 1.00 19.61
ATOM 1032 N ASP 127 11.985 -1 1.095 65.102 1.00 18.52
ATOM 1034 CA ASP 127 10.805 -10.253 65.288 1.00 17.69
ATOM 1035 CB ASP 127 10.822 -9.126 64.266 1.00 20.81 ATOM 1036 CG ASP 127 10.531 -7.791 64.880 1.00 22.21
ATOM 1037 OD1 ASP 127 11.233 -7.444 65.847 1.00 27.07
ATOM 1038 OD2 ASP 127 9.608 -7.092 64.402 1.00 22.58
ATOM 1039 C ASP 127 9.489 -1 1.018 65.150 1.00 16.63
ATOM 1040 O ASP 127 8.412 -10.412 65.106 1.00 16.15 ATOM 1041 N GLY 128 9.583 -12.342 65.073 1.00 15.78
ATOM 1043 CA GLY 128 8.398 -13.163 64.935 1.00 13.93
ATOM 1044 C GLY 128 7.602 -12.781 63.710 1.00 13.52
ATOM 1045 O GLY 128 6.412 -12.482 63.807 1.00 16.01
ATOM 1046 N LYS 129 8.257 -12.781 62.553 1.00 12.91 ATOM 1048 C A LYS 129 7.595 -12.434 61.299 1.00 14.86
ATOM 1049 CB LYS 129 7.979 -1 1.024 60.851 1.00 15.67
ATOM 1050 CG LYS 129 7.691 -9.943 61.870 1.00 19.87
ATOM 1051 CD LYS 129 7.978 -8.556 61.289 1.00 26.01
ATOM 1052 CE LYS 129 6.741 -7.662 61.312 1.00 29.79 ATOM 1053 NZ LYS 129 5.525 -8.356 61.861 1.00 34.06
ATOM 1057 C LYS 129 7.989 -13.424 60.215 1.00 15.02
ATOM 1058 O LYS 129 9.039 -14.050 60.307 1.00 17.45
ATOM 1059 N VAL 130 7.142 -13.554 59.195 1.00 13.45
ATOM 1061 CA VAL 130 7.382 -14.459 58.075 1.00 8.46 ATOM 1062 CB VAL 130 6.208 -14.434 57.108 1.00 4.12
ATOM 1063 CGI VAL 130 6.520 -15.300 55.900 1.00 2.46
ATOM 1064 CG2 VAL 130 4.945 -14.883 57.823 1.00 2.46
ATOM 1065 C VAL 130 8.647 -14.064 57.306 1.00 11.47
ATOM 1066 O VAL 130 8.854 -12.876 57.011 1.00 1 1.42 ATOM 1067 N GLN 131 9.474 -15.058 56.970 1.00 7.85
ATOM 1069 CA GLN 131 10.727 -14.803 56.265 1.00 7.40
ATOM 1070 CB GLN 131 11.784 -15.813 56.682 1.00 7.09
ATOM 1071 CG GLN 131 12.444 -15.526 58.008 1.00 11.63 ATOM 1072 CD GLN 131 13.001-16.78858.651 1.0016.02
ATOM 1073 OE1 GLN 131 13.715-16.72059.645 1.0019.13
ATOM 1074 NE2 GLN 131 12.674-17.95258.082 1.0016.19
ATOM 1077 C GLN 131 10.582-14.87354.766 1.004.20 ATOM 1078 O GLN 131 9.588-15.37754.271 1.005.14
ATOM 1079 N ALA 132 11.580-14.35654.050 1.005.17
ATOM 1081 CA ALA 132 11.588-14.39552.588 1.004.25
ATOM 1082 CB ALA 132 12.665-13.46652.020 1.002.46
ATOM 1083 C ALA 132 11.921-15.83752.263 1.004.28 ATOM 1084 O ALA 132 12.345-16.58353.136 1.003.26
ATOM 1085 N THR 133 11.733-16.23551.014 1.007.96
ATOM 1087 CA THR 133 12.011-17.60650.619 1.009.96
ATOM 1088 CB THR 133 10.922-18.12049.658 1.007.65
ATOM 1089 OG1THR 133 10.793-17.22348.552 1.004.15 ATOM 1091 CG2 THR 133 9.596-18.20050.372 1.004.03
ATOM 1092 C THR 133 13.387-17.73749.968 1.0011.43
ATOM 1093 O THR 133 13.804-18.82649.565 1.0014.33
ATOM 1094 N ASN 134 14.094-16.62249.864 1.0012.23
ATOM 1096 CA ASN 134 15.426-16.63949.285 1.0013.92 ATOM 1097 CB ASN 134 15.353-16.26047.818 1.0018.11
ATOM 1098 CG ASN 134 14.297-17.04547.079 1.0023.80
ATOM 1099 OD1 ASN 134 14.327-18.27947.048 1.0026.91
ATOM 1100 ND2 ASN 134 13.347-16.33546.485 1.0028.34
ATOM 1103 C ASN 134 16.336-15.69450.050 1.0011.93 ATOM 1104 O ASN 134 15.913-14.63350.496 1.0011.70
ATOM 1105 N SER 135 17.588-16.10350.208 1.0013.42
ATOM 1107 CA SER 135 18.567-15.32550.950 1.0014.53
ATOM 1108 CB SER 135 18.850-15.99252.302 1.0015.21
ATOM 1109 OG SER 135 17.862-15.68653.265 1.0017.79 ATOM 1111 C SER 135 19.873-15.231 50.178 1.0015.95
ATOM 11120 SER 135 20.110-16.00349.245 1.0017.09
ATOM 1113 N PHE 136 20.715-14.28350.582 1.0015.49
ATOM 1115 CA PHE 136 22.025-14.08349.974 1.0012.53
ATOM 1116 CB PHE 136 21.916-13.21448.716 1.0012.36 ATOM 1117 CG PHE 136 21.243-11.89748.948 1.0017.92
ATOM 1118 CD1 PHE 136 21.947-10.82449.477 1.0019.00
ATOM 1119 CD2 PHE 136 19.899-11.72948.656 1.0019.89
ATOM 1120 CE1 PHE 136 21.319 -9.60549.712 1.0018.26 ATOM 1121 CE2 PHE 136 19.265-10.51248.889 1.0020.80
ATOM 1122 CZ PHE 136 19.979 -9.44949.418 1.0020.09
ATOM 1123 C PHE 136 22.863-13.38451.030 1.0010.83
ATOM 1124 O PHE 136 22.314-12.72251.913 1.009.18 ATOM 1125 N SER 137 24.180-13.54850.959 1.0010.17
ATOM 1127 CA SER 137 25.080-12.91651.917 1.0010.04
ATOM 1128 CB SER 137 25.758-13.97352.786 1.0013.43
ATOM 1129 OG SER 137 25.827-13.54954.145 1.0023.34
ATOM 1131 C SER 137 26.127-12.14551.153 1.009.53 ATOM 11320 SER 137 25.943-11.84149.984 1.0011.76
ATOM 1133 N GLY 138 27.226-11.811 51.803 1.0010.43
ATOM 1135 CA GLY 138 28.271-11.111 51.086 1.0016.40
ATOM 1136 C GLY 138 28.072 -9.61951.061 1.0019.02
ATOM 1137 O GLY 138 27.190 -9.09851.742 1.0023.05 ATOM 1138 N VAL 139 28.894 -8.93550.273 1.0019.93
ATOM 1140 CA VAL 139 28.830 -7.48750.176 1.0021.53
ATOM 1141 CB VAL 139 30.243 -6.86050.238 1.0021.47
ATOM 1142 CGI VAL 139 30.291 -5.78551.325 1.0019.64
ATOM 1143 CG2VAL 139 31.278 -7.93550.534 1.0022.76 ATOM 1144 C VAL 139 28.121 -7.04848.906 1.0022.95
ATOM 1145 O VAL 139 27.897 -5.85548.686 1.0027.68
ATOM 1146 N ASN 140 27.781 -8.01648.065 1.0021.86
ATOM 1148 CA ASN 140 27.045 -7.74346.838 1.0022.83
ATOM 1149 CB ASN 140 27.864 -6.93545.827 1.0027.56 ATOM 1150 CG ASN 140 29.243 -7.47545.628 1.0033.08
ATOM 1151 OD1 ASN 140 29.438 -8.68445.480 1.0037.25
ATOM 1152 ND2 ASN 140 30.224 -6.581 45.614 1.0037.95
ATOM 1155 C ASN 140 26.522 -9.01346.195 1.0024.65
ATOM 1156 O ASN 140 27.171-10.06546.189 1.0024.02 ATOM 1157 N TYR 141 25.317 -8.88345.663 1.0025.31
ATOM 1159 CA TYR 141 24.590 -9.96245.039 1.0024.32
ATOM 1160 CB TYR 141 23.472-10.36445.996 1.0021.75
ATOM 1161 CG TYR 141 22.553-11.44845.526 1.0022.74
ATOM 1162 CD1TYR 141 21.236-11.15845.195 1.0024.66 ATOM 1163 CE1 TYR 141 20.360-12.16344.814 1.0026.45
ATOM 1164 CD2 TYR 141 22.975-12.77445.464 1.0021.38
ATOM 1165 CE2 TYR 141 22.111-13.78345.086 1.0018.12
ATOM 1166 CZ TYR 141 20.806-13.471 44.763 1.0023.95 ATOM 1167 OH TYR 141 19.932-14.45344.380 1.0028.31
ATOM 1169 C TYR 141 24.026 -9.41243.735 1.0026.65
ATOM 1170 O TYR 141 23.863 -8.20543.586 1.0029.73
ATOM 1171 N TRP 142 23.757-10.28842.780 1.0027.12 ATOM 1173 CA TRP 142 23.189 -9.85441.522 1.0027.16
ATOM 1174 CB TRP 142 24.069-10.27940.357 1.0028.51
ATOM 1175 CG TRP 142 25.181 -9.34540.091 1.0031.97
ATOM 1176 CD2 TRP 142 25.093 -8.04639.489 1.0034.91
ATOM 1177 CE2TRP 142 26.397 -7.51239.456 1.0034.24 ATOM 1178 CE3 TRP 142 24.038 -7.28038.975 1.0034.76
ATOM 1179 CD1 TRP 142 26.490 -9.54040.386 1.0034.44
ATOM 1180 NE1 TRP 142 27.230 -8.44640.011 1.0036.13
ATOM 1182 CZ2TRP 142 26.679 -6.24838.931 1.0032.67
ATOM 1183 CZ3TRP 142 24.323 -6.01438.450 1.0031.35 ATOM 1184 CH2 TRP 142 25.634 -5.51838.434 1.0030.25
ATOM 1185 C TRP 142 21.845-10.52941.404 1.0029.01
ATOM 1186 O TRP 142 21.767-11.68340.985 1.0028.33
ATOM 1187 N LEU 143 20.790 -9.82741.804 1.0031.08
ATOM 1189 CA LEU 143 19.449-10.38341.705 1.0034.36 ATOM 1190 CB LEU 143 18.398 -9.34442.096 1.0033.36
ATOM 1191 CG LEU 143 16.981 -9.86242.361 1.0026.97
ATOM 1192 CD1 LEU 143 17.042-11.13943.152 1.0026.04
ATOM 1193 CD2LEU 143 16.191 -8.831 43.127 1.0025.82
ATOM 1194 C LEU 143 19.291-10.74440.242 1.0037.05 ATOM 1195 O LEU 143 18.729-11.78039.893 1.0039.06
ATOM 1196 N VAL 144 19.805 -9.86539.393 1.0038.80
ATOM 1198 CA VAL 144 19.772-10.06737.960 1.0041.65
ATOM 1199 CB VAL 144 18.609 -9.33037.305 1.0042.75
ATOM 1200 CGI VAL 144 18.654 -9.53435.802 1.0040.78 ATOM 1201 CG2VAL 144 17.296 -9.83637.870 1.0043.68
ATOM 1202 C VAL 144 21.068 -9.51237.419 1.0043.33
ATOM 1203 O VAL 144 21.334 -8.31637.516 1.0041.76
ATOM 1204 N LYS 145 21.875-10.39936.861 1.0045.82
ATOM 1206 CA LYS 145 23.161-10.02736.310 1.0046.88 ATOM 1207 CB LYS 145 23.772-11.22835.579 1.0053.24
ATOM 1208 CG LYS 145 25.289-11.14635.373 1.0059.14
ATOM 1209 CD LYS 145 25.933-12.531 35.216 1.0063.60
ATOM 1210 CE LYS 145 25.755-13.09833.801 1.0067.93 ATOM 121 1 NZ LYS 145 24.519 -13.944 33.658 1.00 70.68
ATOM 1215 C LYS 145 23.092 -8.831 35.369 1.0045.60
ATOM 1216 O LYS 145 22.333 -8.827 34.402 1.0046.14
ATOM 1217 N ASN 146 23.891 -7.816 35.677 1.00 43.29 ATOM 1219 CA ASN 146 23.989 -6.608 34.866 1.0042.57
ATOM 1220 CB ASN 146 24.291 -6.990 33.418 1.00 44.45
ATOM 1221 CG ASN 146 25.641 -7.663 33.265 1.0045.78
ATOM 1222 OD1 ASN 146 26.464 -7.638 34.176 1.00 48.49
ATOM 1223 ND2 ASN 146 25.875 -8.266 32.108 1.00 47.95 ATOM 1226 C ASN 146 22.812 -5.643 34.889 1.00 40.36
ATOM 1227 O ASN 146 22.782 -4.693 34.112 1.00 42.72
ATOM 1228 N LYS 147 21.842 -5.866 35.765 1.00 35.37
ATOM 1230 CA LYS 147 20.705 -4.965 35.826 1.00 27.88
ATOM 1231 CB LYS 147 19.51 1 -5.602 35.120 1.00 26.24 ATOM 1232 CG LYS 147 19.864 -6.150 33.747 1.00 26.13
ATOM 1233 CD LYS 147 18.694 -6.057 32.788 1.00 28.68
ATOM 1234 CE LYS 147 19.153 -5.988 31.344 1.00 30.46
ATOM 1235 NZ LYS 147 20.439 -6.703 31.138 1.00 36.08
ATOM 1239 C LYS 147 20.360 -4.583 37.263 1.00 25.92 ATOM 1240 O LYS 147 20.191 -3.397 37.563 1.00 26.37
ATOM 1241 N ILE 148 20.265 -5.568 38.153 1.00 21.25
ATOM 1243 CA ILE 148 19.944 -5.269 39.545 1.00 17.84
ATOM 1244 CB ILE 148 18.569 -5.800 39.958 1.00 17.45
ATOM 1245 CG2 ILE 148 18.254 -5.348 41.376 1.00 15.02 ATOM 1246 CGI ILE 148 17.501 -5.303 38.991 1.00 15.65
ATOM 1247 CD 1 ILE 148 16.788 -6.418 38.273 1.00 14.47
ATOM 1248 C ILE 148 20.943 -5.834 40.529 1.00 15.81
ATOM 1249 O ILE 148 20.974 -7.034 40.796 1.00 18.19
ATOM 1250 N GLU 149 21.751 -4.949 41.083 1.00 12.54 ATOM 1252 CA GLU 149 22.744 -5.353 42.044 1.00 9.10
ATOM 1253 CB GLU 149 24.098 -4.740 41.684 1.00 16.20
ATOM 1254 CG GLU 149 25.311 -5.509 42.204 1.00 22.43
ATOM 1255 CD GLU 149 26.468 -4.595 42.588 1.00 25.21
ATOM 1256 OE1 GLU 149 27.415 -5.089 43.247 1.00 28.93 ATOM 1257 OE2 GLU 149 26.430 -3.389 42.234 1.00 24.50
ATOM 1258 C GLU 149 22.295 -4.861 43.401 1.00 6.77
ATOM 1259 O GLU 149 21.705 -3.795 43.525 1.00 5.49
ATOM 1260 N VAL 150 22.573 -5.660 44.414 1.00 6.47 ATOM 1262 CA VAL 150 22.222 -5.346 45.785 1.00 9.60
ATOM 1263 CB VAL 150 21.479 -6.538 46.428 1.00 9.53
ATOM 1264 CGI VAL 150 21.016 -6.178 47.829 1.00 8.44
ATOM 1265 CG2 VAL 150 20.300 -6.962 45.544 1.00 8.46 ATOM 1266 C VAL 150 23.569 -5.174 46.476 1.00 1 1.63
ATOM 1267 O VAL 150 24.406 -6.066 46.410 1.00 19.12
ATOM 1268 N PHE 151 23.803 -4.045 47.127 1.00 10.62
ATOM 1270 CA PHE 151 25.082 -3.846 47.789 1.00 8.81
ATOM 1271 CB PHE 151 25.765 -2.593 47.227 1.00 12.46 ATOM 1272 CG PHE 151 27.009 -2.192 47.972 1.00 19.23
ATOM 1273 CD1 PHE 151 28.157 -2.991 47.919 1.00 18.26
ATOM 1274 CD2 PHE 151 27.031 -1.025 48.740 1.00 20.30
ATOM 1275 CE1 PHE 151 29.305 -2.638 48.619 1.00 19.29
ATOM 1276 CE2 PHE 151 28.180 -0.661 49.448 1.00 19.67 ATOM 1277 CZ PHE 151 29.318 -1.469 49.386 1.00 20.41
ATOM 1278 C PHE 151 24.886 -3.696 49.289 1.00 5.39
ATOM 1279 O PHE 151 23.953 -3.032 49.727 1.00 8.55
ATOM 1280 N TYR 152 25.756 -4.310 50.079 1.00 2.46
ATOM 1282 CA TYR 152 25.651 -4.186 51.520 1.00 2.46 ATOM 1283 CB TYR 152 25.663 -5.548 52.203 1.00 2.46
ATOM 1284 CG TYR 152 25.800 -5.510 53.726 1.00 2.46
ATOM 1285 CD1 TYR 152 24.838 -4.891 54.537 1.00 2.46
ATOM 1286 CE1 TYR 152 24.926 -4.940 55.937 1.00 2.46
ATOM 1287 CD2 TYR 152 26.857 -6.169 54.364 1.00 4.65 ATOM 1288 CE2 TYR 152 26.947 -6.220 55.766 1.00 2.46
ATOM 1289 CZ TYR 152 25.982 -5.61 1 56.534 1.00 2.46
ATOM 1290 OH TYR 152 26.087 -5.702 57.898 1.00 2.46
ATOM 1292 C TYR 152 26.842 -3.393 51.994 1.00 3.19
ATOM 1293 O TYR 152 27.948 -3.927 52.109 1.00 9.83 ATOM 1294 N PRO 153 26.639 -2.098 52.273 1.00 2.78
ATOM 1295 CD PRO 153 25.364 -1.362 52.141 1.00 3.23
ATOM 1296 CA PRO 153 27.724 -1.239 52.747 1.00 2.46
ATOM 1297 CB PRO 153 27.162 0.167 52.550 1.00 4.58
ATOM 1298 CG PRO 153 25.674 -0.006 52.726 1.00 2.46 ATOM 1299 C PRO 153 28.143 -1.499 54.204 1.00 2.46
ATOM 1300 O PRO 153 29.302 -1.313 54.540 1.00 5.40
ATOM 1301 N GLY 154 27.205 -1.914 55.058 1.00 2.46
ATOM 1303 CA GLY 154 27.496 -2.174 56.467 1.00 2.46 ATOM 1304 C GLY 154 26.385 -1.729 57.409 1.00 2.46
ATOM 1305 O GLY 154 25.522 -0.970 56.993 1.00 2.46
ATOM 1306 N PRO 155 26.351 -2.166 58.677 1.00 2.46
ATOM 1307 CD PRO 155 27.251 -3.082 59.389 1.00 2.46 ATOM 1308 CA PRO 155 25.259 -1.704 59.550 1.00 2.46
ATOM 1309 CB PRO 155 25.661 -2.215 60.944 1.00 2.46
ATOM 1310 CG PRO 155 27.057 -2.693 60.823 1.00 2.46
ATOM 131 1 C PRO 155 25.040 -0.173 59.534 1.00 5.51
ATOM 1312 O PRO 155 25.992 0.603 59.526 1.00 6.49 ATOM 1313 N GLY 156 23.779 0.259 59.525 1.00 9.55
ATOM 1315 CA GLY 156 23.475 1.690 59.503 1.00 10.49
ATOM 1316 C GLY 156 22.091 2.005 60.057 1.00 1 1.37
ATOM 1317 O GLY 156 21.904 2.050 61.279 1.00 8.79
ATOM 1318 N HIS 157 21.117 2.234 59.175 1.00 9.88 ATOM 1320 CA HIS 157 19.766 2.515 59.642 1.00 7.72
ATOM 1321 CB HIS 157 18.768 2.571 58.491 1.00 6.68
ATOM 1322 CG HIS 157 17.353 2.638 58.961 1.00 8.50
ATOM 1323 CD2 HIS 157 16.239 1.976 58.565 1.00 8.26
ATOM 1324 ND1 HIS 157 16.975 3.416 60.035 1.00 8.49 ATOM 1326 CE1 HIS 157 15.692 3.226 60.283 1.00 1 1.58
ATOM 1327 NE2 HIS 157 15.222 2.358 59.404 1.00 9.45
ATOM 1329 C HIS 157 19.418 1.341 60.543 1.00 5.44
ATOM 1330 O HIS 157 18.947 1.504 61.665 1.00 6.58
ATOM 1331 N THR 158 19.665 0.151 60.014 1.00 6.39 ATOM 1333 CA THR 158 19.459 -1.103 60.723 1.00 2.46
ATOM 1334 CB THR 158 18.251 -1.886 60.182 1.00 2.46
ATOM 1335 OG1 THR 158 18.299 -1.941 58.749 1.00 2.46
ATOM 1337 CG2 THR 158 16.983 -1.225 60.612 1.00 2.46
ATOM 1338 C THR 158 20.722 -1.906 60.444 1.00 2.46 ATOM 1339 O THR 158 21.462 -1.624 59.502 1.00 3.67
ATOM 1340 N PRO 159 20.996 -2.912 61.261 1.00 2.46
ATOM 1341 CD PRO 159 20.242 -3.344 62.445 1.00 2.46
ATOM 1342 CA PRO 159 22.196 -3.723 61.041 1.00 2.94
ATOM 1343 CB PRO 159 22.295 -4.562 62.31 1 1.00 5.62 ATOM 1344 CG PRO 159 20.876 -4.679 62.769 1.00 8.61
ATOM 1345 C PRO 159 22.168 -4.609 59.791 1.00 3.55
ATOM 1346 O PRO 159 23.114 -5.365 59.548 1.00 6.07
ATOM 1347 N ASP 160 21.11 1 -4.516 58.991 1.00 3.10 ATOM 1349 CA ASP 160 21.014 -5.360 57.805 1.00 3.63
ATOM 1350 CB ASP 160 19.926 -6.395 58.018 1.00 2.46
ATOM 1351 CG ASP 160 18.574 -5.760 58.188 1.00 2.46
ATOM 1352 OD1 ASP 160 17.678 -6.032 57.366 1.00 2.46 ATOM 1353 OD2 ASP 160 18.416 -4.972 59.138 1.00 2.46
ATOM 1354 C ASP 160 20.714 -4.611 56.514 1.00 5.25
ATOM 1355 O ASP 160 20.817 -5.188 55.430 1.00 5.12
ATOM 1356 N ASN 161 20.342 -3.338 56.622 1.00 5.81
ATOM 1358 CA ASN 161 19.994 -2.556 55.437 1.00 6.48 ATOM 1359 CB ASN 161 20.048 -1.042 55.722 1.00 9.86
ATOM 1360 CG ASN 161 21.312 -0.615 56.469 1.00 10.45
ATOM 1361 OD1 ASN 161 21.258 0.227 57.371 1.00 9.50
ATOM 1362 ND2 ASN 161 22.450 -1.187 56.095 1.00 11.64
ATOM 1365 C ASN 161 20.874 -2.858 54.250 1.00 4.49 ATOM 1366 O ASN 161 22.045 -3.178 54.411 1.00 10.09
ATOM 1367 N VAL 162 20.303 -2.785 53.057 1.00 2.46
ATOM 1369 CA VAL 162 21.076 -2.993 51.837 1.00 2.46
ATOM 1370 CB VAL 162 20.899 -4.410 51.21 1 1.00 2.46
ATOM 1371 CGI VAL 162 21.350 -5.478 52.191 1.00 2.46 ATOM 1372 CG2 VAL 162 19.467 -4.623 50.794 1.00 2.46
ATOM 1373 C VAL 162 20.563 -1.938 50.885 1.00 2.46
ATOM 1374 O VAL 162 19.544 -1.299 51.154 1.00 2.46
ATOM 1375 N VAL 163 21.283 -1.737 49.793 1.00 2.46
ATOM 1377 CA VAL 163 20.914 -0.736 48.808 1.00 4.38 ATOM 1378 CB VAL 163 22.002 0.376 48.734 1.00 2.46
ATOM 1379 CGI VAL 163 23.267 -0.167 48.085 0.00 9.76
ATOM 1380 CG2 VAL 163 21.474 1.569 47.967 0.00 2.46
ATOM 1381 C VAL 163 20.807 -1.465 47.476 1.00 4.18
ATOM 1382 O VAL 163 21.492 -2.475 47.282 1.00 7.43 ATOM 1383 N VAL 164 19.956 -0.993 46.563 1.00 3.14
ATOM 1385 CA VAL 164 19.846 -1.687 45.280 1.00 2.48
ATOM 1386 CB VAL 164 18.398 -2.236 45.021 1.00 2.46
ATOM 1387 CGI VAL 164 18.322 -2.900 43.663 1.00 2.46
ATOM 1388 CG2 VAL 164 18.036 -3.269 46.073 1.00 2.46 ATOM 1389 C VAL 164 20.304 -0.812 44.125 1.00 2.46
ATOM 1390 O VAL 164 19.718 0.231 43.843 1.00 2.46
ATOM 1391 N TRP 165 21.381 -1.264 43.481 1.00 4.37
ATOM 1393 CA TRP 165 21.994 -0.584 42.355 1.00 6.45 ATOM 1394 CB TRP 165 23.506 -0.858 42.323 1.00 8.55
ATOM 1395 CG TRP 165 24.233 -0.102 41.224 1.00 13.63
ATOM 1396 CD2 TRP 165 24.160 1.31 1 40.953 1.00 15.34
ATOM 1397 CE2 TRP 165 24.975 1.563 39.824 1.00 12.31 ATOM 1398 CE3 TRP 165 23.482 2.388 41.557 1.00 17.27
ATOM 1399 CD1 TRP 165 25.069 -0.626 40.273 1.00 13.02
ATOM 1400 NE1 TRP 165 25.515 0.367 39.431 1.00 10.50
ATOM 1402 CZ2 TRP 165 25.133 2.850 39.283 1.00 13.16
ATOM 1403 CZ3 TRP 165 23.638 3.668 41.020 1.00 15.50 ATOM 1404 CH2 TRP 165 24.461 3.885 39.891 1.00 14.19
ATOM 1405 C TRP 165 21.382 -1.018 41.039 1.00 5.21
ATOM 1406 O TRP 165 21.153 -2.202 40.815 1.00 2.46
ATOM 1407 N LEU 166 21.141 -0.036 40.175 1.00 9.82
ATOM 1409 CA LEU 166 20.557 -0.240 38.854 1.00 16.73 ATOM 1410 CB LEU 166 19.292 0.598 38.729 1.00 15.90
ATOM 1411 CG LEU 166 18.084 0.028 39.457 1.00 14.46
ATOM 1412 CD1 LEU 166 16.916 0.964 39.276 1.00 11.67
ATOM 1413 CD2 LEU 166 17.765 -1.353 38.906 1.00 12.58
ATOM 1414 C LEU 166 21.524 0.154 37.733 1.00 20.58 ATOM 1415 O LEU 166 21.460 1.275 37.209 1.00 20.60
ATOM 1416 N PRO 167 22.435 -0.761 37.355 1.00 22.40
ATOM 1417 CD PRO 167 22.572 -2.092 37.971 1.00 23.39
ATOM 1418 CA PRO 167 23.438 -0.567 36.305 1.00 24.25
ATOM 1419 CB PRO 167 23.710 -1.984 35.806 1.00 21.25 ATOM 1420 CG PRO 167 23.491 -2.843 37.003 1.00 21.54
ATOM 1421 C PRO 167 23.077 0.371 35.162 1.00 24.36
ATOM 1422 O PRO 167 23.410 1.550 35.195 1.00 23.90
ATOM 1423 N GLU 168 22.390 -0.154 34.154 1.00 26.71
ATOM 1425 CA GLU 168 22.045 0.643 32.981 1.00 31.91 ATOM 1426 CB GLU 168 21.391 -0.229 31.908 1.00 33.25
ATOM 1427 CG GLU 168 20.463 -1.299 32.407 1.0041.38
ATOM 1428 CD GLU 168 20.271 -2.376 31.361 1.0048.71
ATOM 1429 OE1 GLU 168 21.274 -2.738 30.709 1.00 50.32
ATOM 1430 OE2 GLU 168 19.128 -2.854 31.182 1.00 52.59 ATOM 1431 C GLU 168 21.191 1.881 33.180 1.00 32.43
ATOM 1432 O GLU 168 20.722 2.467 32.212 1.00 34.03
ATOM 1433 N ARG 169 20.990 2.304 34.414 1.00 31.03
ATOM 1435 C A ARG 169 20.177 3.482 34.61 1 1.00 32.03 ATOM 1436 CB ARG 169 18.759 3.055 34.979 1.00 33.64
ATOM 1437 CG ARG 169 17.694 3.607 34.043 1.00 39.65
ATOM 1438 CD ARG 169 18.006 3.321 32.586 1.0045.33
ATOM 1439 NE ARG 169 18.1 12 1.887 32.344 1.00 53.61 ATOM 1441 CZ ARG 169 17.071 1.058 32.299 1.00 57.67
ATOM 1442 NH1 ARG 169 15.839 1.521 32.480 1.00 59.50
ATOM 1445 NH2 ARG 169 17.261 -0.239 32.082 1.00 59.21
ATOM 1448 C ARG 169 20.763 4.413 35.664 1.00 32.27
ATOM 1449 O ARG 169 20.235 5.498 35.915 1.00 32.33 ATOM 1450 N LYS 170 21.870 3.985 36.265 1.00 31.62
ATOM 1452 CA LYS 170 22.545 4.774 37.285 1.00 29.64
ATOM 1453 CB LYS 170 23.197 6.007 36.652 1.00 31.11
ATOM 1454 CG LYS 170 24.376 5.682 35.737 1.00 33.51
ATOM 1455 CD LYS 170 23.942 5.632 34.276 1.00 36.10 ATOM 1456 CE LYS 170 24.339 4.322 33.597 1.00 38.31
ATOM 1457 NZ LYS 170 23.943 4.301 32.149 1.0040.03
ATOM 1461 C LYS 170 21.574 5.198 38.383 1.00 27.32
ATOM 1462 O LYS 170 21.652 6.31 1 38.923 1.00 27.14
ATOM 1463 N ILE 171 20.652 4.305 38.714 1.00 23.65 ATOM 1465 CA ILE 171 19.703 4.610 39.759 1.00 20.25
ATOM 1466 CB ILE 171 18.273 4.319 39.325 1.00 20.41
ATOM 1467 CG2 ILE 171 17.397 4.1 16 40.550 1.00 16.97
ATOM 1468 CGI ILE 171 17.744 5.493 38.499 1.00 21.62
ATOM 1469 CD 1 ILE 171 16.750 5.094 37.426 1.00 20.85 ATOM 1470 C ILE 171 20.030 3.769 40.967 1.00 14.59
ATOM 1471 O ILE 171 20.315 2.577 40.853 1.00 13.73
ATOM 1472 N LEU 172 19.994 4.401 42.129 1.00 8.39
ATOM 1474 CA LEU 172 20.281 3.700 43.363 1.00 4.93
ATOM 1475 CB LEU 172 21.527 4.293 44.031 1.00 2.46 ATOM 1476 CG LEU 172 21.861 3.646 45.373 1.00 2.46
ATOM 1477 CD 1 LEU 172 22.847 2.527 45.143 1.00 2.46
ATOM 1478 CD2 LEU 172 22.416 4.669 46.337 1.00 2.46
ATOM 1479 C LEU 172 19.086 3.791 44.309 1.00 3.41
ATOM 1480 O LEU 172 18.565 4.874 44.566 1.00 4.52 ATOM 1481 N PHE 173 18.626 2.645 44.795 1.00 3.53
ATOM 1483 CA PHE 173 17.523 2.639 45.737 1.00 2.86
ATOM 1484 CB PHE 173 16.587 1.440 45.520 1.00 4.29
ATOM 1485 CG PHE 173 15.461 1.379 46.524 1.00 3.56 ATOM 1486 CD1 PHE 173 14.332 2.172 46.365 1.00 2.46
ATOM 1487 CD2 PHE 173 15.583 0.621 47.681 1.00 4.87
ATOM 1488 CE1 PHE 173 13.353 2.224 47.347 1.00 2.46
ATOM 1489 CE2 PHE 173 14.606 0.664 48.674 1.00 7.38 ATOM 1490 CZ PHE 173 13.489 1.472 48.506 1.00 5.93
ATOM 1491 C PHE 173 18.189 2.518 47.095 1.00 2.46
ATOM 1492 O PHE 173 18.595 1.432 47.490 1.00 2.96
ATOM 1493 N GLY 174 18.314 3.630 47.802 1.00 2.46
ATOM 1495 CA GLY 174 18.964 3.587 49.092 1.00 2.46 ATOM 1496 C GLY 174 18.037 3.363 50.270 1.00 5.72
ATOM 1497 O GLY 174 18.496 3.292 51.419 1.00 8.56
ATOM 1498 N GLY 175 16.736 3.264 49.996 1.00 4.56
ATOM 1500 CA GLY 175 15.763 3.047 51.060 1.00 3.21
ATOM 1501 C GLY 175 15.940 3.875 52.324 1.00 2.46 ATOM 1502 O GLY 175 16.352 5.021 52.274 1.00 2.46
ATOM 1503 N CYS 176 15.635 3.286 53.470 1.00 2.46
ATOM 1505 CA CYS 176 15.741 4.000 54.740 1.00 2.46
ATOM 1506 CB CYS 176 14.930 3.267 55.825 1.00 5.45
ATOM 1507 SG CYS 176 13.163 3.026 55.461 1.00 2.46 ATOM 1508 C CYS 176 17.173 4.216 55.237 1.00 2.46
ATOM 1509 O CYS 176 17.387 4.529 56.418 1.00 2.46
ATOM 1510 N PHE 177 18.144 4.043 54.342 1.00 2.94
ATOM 1512 CA PHE 177 19.559 4.221 54.690 1.00 3.04
ATOM 1513 CB PHE 177 20.438 3.216 53.923 1.00 5.49 ATOM 1514 CG PHE 177 21.910 3.337 54.223 1.00 4.41
ATOM 1515 CD1 PHE 177 22.679 4.323 53.616 1.00 2.71
ATOM 1516 CD2 PHE 177 22.517 2.493 55.144 1.00 5.51
ATOM 1517 CE1 PHE 177 24.027 4.475 53.927 1.00 2.46
ATOM 1518 CE2 PHE 177 23.875 2.639 55.462 1.00 3.41 ATOM 1519 CZ PHE 177 24.626 3.635 54.852 1.00 2.46
ATOM 1520 C PHE 177 19.934 5.630 54.292 1.00 2.46
ATOM 1521 O PHE 177 20.695 6.311 54.974 1.00 2.46
ATOM 1522 N ILE 178 19.382 6.046 53.164 1.00 2.46
ATOM 1524 CA ILE 178 19.621 7.376 52.635 1.00 2.46 ATOM 1525 CB ILE 178 19.400 7.403 51.128 1.00 2.46
ATOM 1526 CG2 ILE 178 19.875 8.715 50.574 1.00 3.89
ATOM 1527 CGI ILE 178 20.127 6.235 50.484 1.00 2.46
ATOM 1528 CD1 ILE 178 21.582 6.481 50.308 1.00 2.46 ATOM 1529 C ILE 178 18.694 8.420 53.262 1.00 2.46
ATOM 1530 O ILE 178 17.620 8.678 52.745 1.00 3.29
ATOM 1531 N LYS 179 19.127 9.027 54.361 1.00 2.96
ATOM 1533 CA LYS 179 18.335 10.034 55.057 1.00 8.36 ATOM 1534 CB LYS 179 18.002 9.510 56.455 1.00 9.12
ATOM 1535 CG LYS 179 17.396 8.117 56.483 1.00 6.36
ATOM 1536 CD LYS 179 16.072 8.129 57.244 1.00 2.76
ATOM 1537 CE LYS 179 15.421 6.751 57.233 1.00 5.98
ATOM 1538 NZ LYS 179 14.239 6.676 58.151 1.00 9.09 ATOM 1542 C LYS 179 19.088 11.373 55.169 1.00 9.32
ATOM 1543 O LYS 179 19.704 11.643 56.192 1.00 14.93
ATOM 1544 N PRO 180 19.009 12.243 54.144 1.00 6.30
ATOM 1545 CD PRO 180 18.222 12.064 52.914 1.00 4.16
ATOM 1546 CA PRO 180 19.717 13.537 54.173 1.00 5.28 ATOM 1547 CB PRO 180 19.434 14.134 52.801 1.00 2.46
ATOM 1548 CG PRO 180 18.183 13.432 52.334 1.00 4.19
ATOM 1549 C PRO 180 19.379 14.530 55.288 1.00 7.34
ATOM 1550 O PRO 180 20.266 14.966 56.039 1.00 7.43
ATOM 1551 N TYR 181 18.092 14.873 55.379 1.00 8.78 ATOM 1553 CA TYR 181 17.534 15.837 56.343 1.00 3.09
ATOM 1554 CB TYR 181 16.161 16.285 55.850 1.00 2.46
ATOM 1555 CG TYR 181 16.051 16.332 54.346 1.00 2.46
ATOM 1556 CD1 TYR 181 14.866 16.016 53.708 1.00 2.46
ATOM 1557 CE1 TYR 181 14.740 16.130 52.324 1.00 3.34 ATOM 1558 CD2 TYR 181 17.124 16.756 53.563 1.00 3.24
ATOM 1559 CE2 TYR 181 17.014 16.874 52.181 1.00 5.46
ATOM 1560 CZ TYR 181 15.816 16.565 51.570 1.00 4.21
ATOM 1561 OH TYR 181 15.685 16.739 50.212 1.00 6.32
ATOM 1563 C TYR 181 17.401 15.349 57.778 1.00 2.59 ATOM 1564 O TYR 181 17.259 16.136 58.704 1.00 2.46
ATOM 1565 N GLY 182 17.438 14.042 57.968 1.00 6.11
ATOM 1567 CA GLY 182 17.316 13.522 59.314 1.00 8.42
ATOM 1568 C GLY 182 17.525 12.042 59.222 1.00 9.40
ATOM 1569 O GLY 182 17.218 1 1.453 58.189 1.00 10.75 ATOM 1570 N LEU 183 18.057 11.447 60.281 1.00 10.02
ATOM 1572 CA LEU 183 18.307 10.012 60.283 1.00 12.54
ATOM 1573 CB LEU 183 19.381 9.654 61.313 1.00 12.09
ATOM 1574 CG LEU 183 20.807 10.051 60.930 1.00 1 1.54 ATOM 1575 CD1 LEU 183 21.785 9.484 61.938 1.00 9.22
ATOM 1576 CD2 LEU 183 21.1 19 9.558 59.517 1.00 7.96
ATOM 1577 C LEU 183 17.019 9.306 60.630 1.00 15.37
ATOM 1578 0 LEU 183 16.831 8.127 60.291 1.00 15.91 ATOM 1579 N GLY 184 16.138 10.038 61.313 1.00 14.89
ATOM 1581 CA GLY 184 14.863 9.480 61.712 1.00 13.53
ATOM 1582 C GLY 184 14.938 8.405 62.783 1.00 12.11
ATOM 1583 O GLY 184 15.734 8.493 63.714 1.00 11.67
ATOM 1584 N ASN 185 14.103 7.382 62.635 1.00 10.80 ATOM 1586 CA ASN 185 14.025 6.289 63.588 1.00 10.40
ATOM 1587 CB ASN 185 13.135 5.196 63.015 1.00 11.33
ATOM 1588 CG ASN 185 13.019 4.004 63.935 1.00 16.46
ATOM 1589 OD1 ASN 185 12.968 4.159 65.161 1.00 20.56
ATOM 1590 ND2 ASN 185 12.975 2.800 63.354 1.00 16.04 ATOM 1593 C ASN 185 15.372 5.698 64.001 1.00 12.78
ATOM 1594 0 ASN 185 15.984 4.904 63.262 1.00 13.32
ATOM 1595 N LEU 186 15.829 6.061 65.195 1.00 9.06
ATOM 1597 CA LEU 186 17.106 5.548 65.669 1.00 8.27
ATOM 1598 CB LEU 186 17.763 6.579 66.585 1.00 5.09 ATOM 1599 CG LEU 186 18.261 7.855 65.894 1.00 3.37
ATOM 1600 CD1 LEU 186 18.999 8.710 66.907 1.00 2.46
ATOM 1601 CD2 LEU 186 19.165 7.505 64.709 1.00 2.46
ATOM 1602 C LEU 186 16.982 4.198 66.389 1.00 8.40
ATOM 1603 O LEU 186 17.966 3.667 66.909 1.00 7.53 ATOM 1604 N GLY 187 15.766 3.650 66.391 1.00 7.66
ATOM 1606 C A GLY 187 15.472 2.379 67.039 1.00 10.41
ATOM 1607 C GLY 187 16.507 1.271 66.969 1.00 11.90
ATOM 1608 O GLY 187 17.195 1.015 67.950 1.00 12.55
ATOM 1609 N ASP 188 16.603 0.586 65.834 1.00 13.54 ATOM 1611 CA ASP 188 17.583 -0.482 65.697 1.00 14.13
ATOM 1612 CB ASP 188 16.932 -1.761 65.163 1.00 19.23
ATOM 1613 CG ASP 188 15.485 -1.913 65.588 1.00 22.52
ATOM 1614 OD1 ASP 188 15.222 -1.956 66.810 1.00 24.79
ATOM 1615 OD2 ASP 188 14.613 -1.998 64.691 1.00 22.45 ATOM 1616 C ASP 188 18.674 -0.040 64.732 1.00 13.26
ATOM 1617 O ASP 188 18.840 -0.628 63.662 1.00 14.00
ATOM 1618 N ALA 189 19.418 0.994 65.107 1.00 15.74
ATOM 1620 CA ALA 189 20.478 1.508 64.250 1.00 17.84 ATOM 1621 CB ALA 189 20.283 2.990 64.032 1.00 14.78
ATOM 1622 C ALA 189 21.864 1.242 64.829 1.00 22.24
ATOM 1623 O ALA 189 21.997 0.715 65.935 1.00 27.27
ATOM 1624 N ASN 190 22.893 1.612 64.068 1.00 22.31 ATOM 1626 CA ASN 190 24.289 1.429 64.469 1.00 22.37
ATOM 1627 CB ASN 190 24.956 0.377 63.584 1.00 25.53
ATOM 1628 CG ASN 190 26.332 -0.004 64.072 1.00 30.94
ATOM 1629 OD1 ASN 190 27.148 0.871 64.394 1.00 35.40
ATOM 1630 ND2 ASN 190 26.608 -1.317 64.132 1.00 30.32 ATOM 1633 C ASN 190 24.986 2.762 64.285 1.00 20.52
ATOM 1634 O ASN 190 25.859 2.909 63.435 1.00 20.17
ATOM 1635 N ILE 191 24.571 3.725 65.096 1.00 20.37
ATOM 1637 CA ILE 191 25.081 5.084 65.057 1.00 20.33
ATOM 1638 CB ILE 191 24.726 5.816 66.358 1.00 22.97 ATOM 1639 CG2 ILE 191 25.720 5.447 67.466 1.00 23.79
ATOM 1640 CGI ILE 191 24.682 7.316 66.096 1.00 22.12
ATOM 1641 CD 1 ILE 191 23.285 7.841 65.863 1.00 16.42
ATOM 1642 C ILE 191 26.575 5.210 64.823 1.00 19.86
ATOM 1643 O ILE 191 27.025 6.152 64.161 1.00 16.83 ATOM 1644 N GLU 192 27.339 4.263 65.363 1.00 19.73
ATOM 1646 C A GLU 192 28.791 4.292 65.227 1.00 16.96
ATOM 1647 CB GLU 192 29.442 3.387 66.260 1.00 20.72
ATOM 1648 CG GLU 192 30.039 4.135 67.430 1.00 28.02
ATOM 1649 CD GLU 192 29.183 4.023 68.678 1.00 34.74 ATOM 1650 OE1 GLU 192 29.583 4.582 69.723 1.00 37.36
ATOM 1651 OE2 GLU 192 28.111 3.373 68.609 1.00 37.61
ATOM 1652 C GLU 192 29.293 3.894 63.863 1.00 13.94
ATOM 1653 O GLU 192 30.299 4.425 63.402 1.00 17.34
ATOM 1654 N ALA 193 28.603 2.966 63.213 1.00 7.88 ATOM 1656 CA ALA 193 29.033 2.511 61.903 1.00 6.86
ATOM 1657 CB ALA 193 28.854 1.013 61.805 1.00 3.18
ATOM 1658 C ALA 193 28.367 3.197 60.709 1.00 6.93
ATOM 1659 O ALA 193 28.888 3.158 59.596 1.00 6.75
ATOM 1660 N TRP 194 27.222 3.827 60.922 1.00 9.95 ATOM 1662 CA TRP 194 26.538 4.489 59.818 1.00 1 1.18
ATOM 1663 CB TRP 194 25.357 5.285 60.343 1.00 12.43
ATOM 1664 CG TRP 194 24.263 5.497 59.339 1.00 14.91
ATOM 1665 CD2 TRP 194 22.877 5.719 59.632 1.00 12.77 ATOM 1666 CE2 TRP 194 22.215 5.906 58.402 1.00 1 1.37
ATOM 1667 CE3 TRP 194 22.131 5.780 60.821 1.00 4.59
ATOM 1668 CD 1 TRP 194 24.382 5.555 57.973 1.00 13.42
ATOM 1669 NE1 TRP 194 23.153 5.803 57.407 1.00 13.21 ATOM 1671 CZ2 TRP 194 20.850 6.146 58.331 1.00 10.30
ATOM 1672 CZ3 TRP 194 20.793 6.015 60.751 1.00 2.46
ATOM 1673 CH2 TRP 194 20.156 6.195 59.518 1.00 10.87
ATOM 1674 C TRP 194 27.465 5.414 59.030 1.00 11.41
ATOM 1675 O TRP 194 27.397 5.474 57.797 1.00 11.06 ATOM 1676 N PRO 195 28.336 6.162 59.731 1.00 12.28
ATOM 1677 CD PRO 195 28.527 6.241 61.193 1.00 11.72
ATOM 1678 CA PRO 195 29.245 7.062 59.004 1.00 1 1.76
ATOM 1679 CB PRO 195 29.927 7.878 60.116 1.00 9.99
ATOM 1680 CG PRO 195 29.164 7.584 61.386 1.00 10.00 ATOM 1681 C PRO 195 30.262 6.309 58.124 1.00 11.90
ATOM 1682 O PRO 195 30.624 6.758 57.031 1.00 7.31
ATOM 1683 N LYS 196 30.724 5.162 58.613 1.00 1 1.88
ATOM 1685 CA LYS 196 31.684 4.363 57.871 1.00 11.18
ATOM 1686 CB LYS 196 32.247 3.251 58.759 1.00 15.44 ATOM 1687 CG LYS 196 32.826 3.753 60.078 1.00 21.54
ATOM 1688 CD LYS 196 33.966 2.866 60.577 1.00 27.53
ATOM 1689 CE LYS 196 34.271 3.140 62.057 1.00 32.20
ATOM 1690 NZ LYS 196 35.672 2.790 62.458 1.00 32.74
ATOM 1694 C LYS 196 31.030 3.784 56.623 1.00 10.06 ATOM 1695 O LYS 196 31.650 3.758 55.563 1.00 9.13
ATOM 1696 N SER 197 29.780 3.333 56.743 1.00 10.66
ATOM 1698 CA SER 197 29.045 2.767 55.605 1.00 6.36
ATOM 1699 CB SER 197 27.862 1.943 56.093 1.00 2.46
ATOM 1700 OG SER 197 28.031 1.633 57.460 1.00 3.74 ATOM 1702 C SER 197 28.542 3.891 54.712 1.00 5.43
ATOM 1703 O SER 197 28.442 3.741 53.491 1.00 2.61
ATOM 1704 N ALA 198 28.217 5.019 55.326 1.00 5.01
ATOM 1706 CA ALA 198 27.753 6.147 54.555 1.00 7.99
ATOM 1707 CB ALA 198 27.463 7.317 55.465 1.00 3.91 ATOM 1708 C ALA 198 28.904 6.475 53.619 1.00 1 1.94
ATOM 1709 O ALA 198 28.707 6.710 52.422 1.00 13.23
ATOM 1710 N LYS 199 30.111 6.456 54.186 1.00 15.67
ATOM 1712 CA LYS 199 31.345 6.760 53.462 1.00 16.72 ATOM 1713 CB LYS 199 32.512 6.840 54.448 1.00 21.76
ATOM 1714 CG LYS 199 33.784 7.412 53.854 1.00 30.13
ATOM 1715 CD LYS 199 34.836 7.695 54.931 1.00 37.34
ATOM 1716 CE LYS 199 35.888 6.581 55.026 1.0040.16 ATOM 1717 NZ LYS 199 36.928 6.639 53.947 1.0041.97
ATOM 1721 C LYS 199 31.653 5.750 52.354 1.00 14.57
ATOM 1722 0 LYS 199 31.939 6.140 51.219 1.00 12.90
ATOM 1723 N LEU 200 31.595 4.461 52.678 1.00 11.30
ATOM 1725 CA LEU 200 31.847 3.429 51.683 1.00 9.78 ATOM 1726 CB LEU 200 31.778 2.041 52.318 1.00 8.25
ATOM 1727 CG LEU 200 31.661 0.833 51.374 1.00 9.13
ATOM 1728 CD1 LEU 200 32.778 0.835 50.335 1.00 2.77
ATOM 1729 CD2 LEU 200 31.714 -0.446 52.198 1.00 8.02
ATOM 1730 C LEU 200 30.807 3.528 50.576 1.00 9.47 ATOM 1731 O LEU 200 31.1 10 3.286 49.415 1.00 9.75
ATOM 1732 N LEU 201 29.577 3.892 50.940 1.00 12.06
ATOM 1734 CA LEU 201 28.488 4.015 49.967 1.00 9.43
ATOM 1735 CB LEU 201 27.133 4.147 50.672 1.00 5.97
ATOM 1736 CG LEU 201 25.944 4.199 49.700 1.00 5.66 ATOM 1737 CD 1 LEU 201 25.784 2.853 48.983 1.00 2.46
ATOM 1738 CD2 LEU 201 24.680 4.584 50.468 1.00 2.46
ATOM 1739 C LEU 201 28.680 5.205 49.046 1.00 9.78
ATOM 1740 O LEU 201 28.576 5.077 47.829 1.00 7.84
ATOM 1741 N LYS 202 28.960 6.366 49.628 1.00 11.62 ATOM 1743 C A LYS 202 29.161 7.566 48.831 1.00 15.54
ATOM 1744 CB LYS 202 29.592 8.729 49.722 1.00 14.06
ATOM 1745 CG LYS 202 29.857 10.036 48.961 1.00 16.43
ATOM 1746 CD LYS 202 30.148 1 1.193 49.917 1.00 21.09
ATOM 1747 CE LYS 202 30.566 12.439 49.154 1.00 24.48 ATOM 1748 NZ LYS 202 31.537 13.293 49.912 1.00 29.64
ATOM 1752 C LYS 202 30.209 7.361 47.735 1.00 18.67
ATOM 1753 O LYS 202 30.094 7.920 46.645 1.00 18.95
ATOM 1754 N SER 203 31.222 6.549 48.032 1.00 20.66
ATOM 1756 CA SER 203 32.313 6.285 47.098 1.00 20.64 ATOM 1757 CB SER 203 33.526 5.765 47.862 1.00 21.34
ATOM 1758 OG SER 203 33.186 5.508 49.215 1.00 21.57
ATOM 1760 C SER 203 31.963 5.301 45.998 1.00 20.32
ATOM 1761 O SER 203 32.127 5.596 44.813 1.00 21.54 ATOM 1762 N LYS 204 31.488 4.126 46.390 1.00 20.07
ATOM 1764 CA LYS 204 31.133 3.103 45.420 1.00 21.66
ATOM 1765 CB LYS 204 30.544 1.884 46.134 1.00 23.20
ATOM 1766 CG LYS 204 30.157 0.748 45.199 1.00 27.91 ATOM 1767 CD LYS 204 31.195 -0.372 45.190 1.00 31.57
ATOM 1768 CE LYS 204 31.007 -1.295 43.985 1.00 31.50
ATOM 1769 NZ LYS 204 30.087 -2.436 44.284 1.00 31.62
ATOM 1773 C LYS 204 30.151 3.614 44.362 1.00 22.94
ATOM 1774 O LYS 204 30.332 3.359 43.173 1.00 23.42 ATOM 1775 N TYR 205 29.128 4.354 44.783 1.00 25.38
ATOM 1777 CA TYR 205 28.130 4.859 43.836 1.00 25.18
ATOM 1778 CB TYR 205 26.758 4.263 44.157 1.00 19.80
ATOM 1779 CG TYR 205 26.755 2.764 44.243 1.00 16.89
ATOM 1780 CD1 TYR 205 26.619 2.1 17 45.469 1.00 16.08 ATOM 1781 CE1 TYR 205 26.61 1 0.724 45.550 1.00 18.59
ATOM 1782 CD2 TYR 205 26.885 1.988 43.096 1.00 18.63
ATOM 1783 CE2 TYR 205 26.880 0.600 43.161 1.00 19.78
ATOM 1784 CZ TYR 205 26.743 -0.024 44.388 1.00 19.65
ATOM 1785 OH TYR 205 26.748 -1.394 44.447 1.00 21.41 ATOM 1787 C TYR 205 27.989 6.377 43.735 1.00 27.13
ATOM 1788 O TYR 205 26.871 6.897 43.612 1.00 27.97
ATOM 1789 N GLY 206 29.106 7.094 43.783 1.00 26.53
ATOM 1791 CA GLY 206 29.025 8.541 43.664 1.00 26.05
ATOM 1792 C GLY 206 28.686 8.863 42.222 1.00 25.46 ATOM 1793 O GLY 206 28.404 10.012 41.849 1.00 20.68
ATOM 1794 N LYS 207 28.719 7.805 41.415 1.00 27.04
ATOM 1796 CA LYS 207 28.440 7.864 39.991 1.00 28.16
ATOM 1797 CB LYS 207 29.061 6.632 39.314 1.00 27.14
ATOM 1798 CG LYS 207 30.563 6.510 39.504 0.00 25.79 ATOM 1799 CD LYS 207 31.144 5.406 38.634 0.00 2.46
ATOM 1800 CE LYS 207 30.860 4.030 39.218 0.00 2.46
ATOM 1801 NZ LYS 207 31.168 3.965 40.674 0.00 2.46
ATOM 1805 C LYS 207 26.931 7.912 39.712 1.00 27.65
ATOM 1806 O LYS 207 26.506 7.910 38.550 1.00 29.58 ATOM 1807 N ALA 208 26.134 7.976 40.778 1.00 24.32
ATOM 1809 CA ALA 208 24.679 7.984 40.676 1.00 21.35
ATOM 1810 CB ALA 208 24.084 7.800 42.055 1.00 20.91
ATOM 1811 C ALA 208 24.010 9.178 39.990 1.00 23.50 ATOM 1812 O ALA 208 24.299 10.347 40.281 1.00 22.53
ATOM 1813 N LYS 209 23.095 8.852 39.079 1.00 24.60
ATOM 1815 CA LYS 209 22.312 9.842 38.345 1.00 25.25
ATOM 1816 CB LYS 209 21.812 9.227 37.035 1.00 28.72 ATOM 1817 CG LYS 209 22.346 9.884 35.778 1.00 34.53
ATOM 1818 CD LYS 209 21.637 11.218 35.510 1.0042.72
ATOM 1819 CE LYS 209 20.121 11.055 35.307 1.0044.48
ATOM 1820 NZ LYS 209 19.477 12.331 34.870 1.00 42.84
ATOM 1824 C LYS 209 21.123 10.157 39.255 1.00 24.06 ATOM 1825 O LYS 209 20.760 1 1.318 39.487 1.00 25.42
ATOM 1826 N LEU 210 20.540 9.088 39.784 1.00 19.95
ATOM 1828 CA LEU 210 19.407 9.187 40.673 1.00 16.70
ATOM 1829 CB LEU 210 18.167 8.686 39.950 1.00 18.67
ATOM 1830 CG LEU 210 17.718 9.625 38.840 1.00 18.89 ATOM 1831 CD 1 LEU 210 16.880 8.872 37.834 1.00 12.56
ATOM 1832 CD2 LEU 210 16.948 10.791 39.464 1.00 17.47
ATOM 1833 C LEU 210 19.614 8.378 41.947 1.00 15.19
ATOM 1834 O LEU 210 20.251 7.319 41.927 1.00 16.94
ATOM 1835 N VAL 211 19.071 8.892 43.049 1.00 1 1.66 ATOM 1837 CA VAL 21 1 19.137 8.244 44.365 1.00 9.24
ATOM 1838 CB VAL 21 1 20.079 8.995 45.325 1.00 9.84
ATOM 1839 CGI VAL 21 1 20.123 8.292 46.680 1.00 2.46
ATOM 1840 CG2 VAL 211 21.464 9.105 44.709 1.00 7.75
ATOM 1841 C VAL 211 17.726 8.318 44.939 1.00 10.22 ATOM 1842 O VAL 21 1 17.245 9.403 45.289 1.00 9.46
ATOM 1843 N VAL 212 17.064 7.168 45.035 1.00 1 1.59
ATOM 1845 CA VAL 212 15.691 7.120 45.533 1.00 9.72
ATOM 1846 CB VAL 212 14.824 6.108 44.690 1.00 8.07
ATOM 1847 CGI VAL 212 13.397 6.021 45.246 1.00 2.46 ATOM 1848 CG2 VAL 212 14.800 6.534 43.221 1.00 2.46
ATOM 1849 C VAL 212 15.575 6.764 47.012 1.00 9.29
ATOM 1850 O VAL 212 15.682 5.596 47.371 1.00 8.98
ATOM 1851 N PRO 213 15.409 7.779 47.892 1.00 8.48
ATOM 1852 CD PRO 213 15.436 9.219 47.586 1.00 4.38 ATOM 1853 CA PRO 213 15.269 7.539 49.337 1.00 7.89
ATOM 1854 CB PRO 213 15.352 8.936 49.959 1.00 3.38
ATOM 1855 CG PRO 213 15.012 9.859 48.879 1.00 3.65
ATOM 1856 C PRO 213 13.942 6.850 49.666 1.00 9.33 ATOM 1857 O PRO 213 13.123 6.605 48.775 1.00 1 1.37
ATOM 1858 N SER 214 13.735 6.548 50.945 1.00 8.51
ATOM 1860 CA SER 214 12.515 5.875 51.395 1.00 5.98
ATOM 1861 CB SER 214 12.829 4.898 52.544 1.00 3.15 ATOM 1862 OG SER 214 12.982 3.566 52.090 1.00 2.46
ATOM 1864 C SER 214 11.424 6.835 51.860 1.00 5.72
ATOM 1865 O SER 214 10.244 6.498 51.811 1.00 8.56
ATOM 1866 N HIS 215 1 1.808 8.022 52.318 1.00 6.06
ATOM 1868 CA HIS 215 10.825 8.994 52.806 1.00 3.49 ATOM 1869 CB HIS 215 10.655 8.833 54.316 1.00 2.46
ATOM 1870 CG HIS 215 10.741 7.416 54.786 1.00 2.46
ATOM 1871 CD2 HIS 215 11.731 6.746 55.424 1.00 2.46
ATOM 1872 ND1 HIS 215 9.714 6.514 54.619 1.00 2.46
ATOM 1874 CE1 HIS 215 10.064 5.348 55.137 1.00 2.50 ATOM 1875 NE2 HIS 215 1 1.285 5.463 55.631 1.00 2.46
ATOM 1877 C HIS 215 1 1.204 10.441 52.498 1.00 6.09
ATOM 1878 O HIS 215 11.195 1 1.296 53.387 1.00 7.27
ATOM 1879 N SER 216 11.555 10.699 51.244 1.00 9.48
ATOM 1881 CA SER 216 11.955 12.033 50.798 1.00 14.26 ATOM 1882 CB SER 216 13.395 12.352 51.234 1.00 13.34
ATOM 1883 OG SER 216 13.619 12.047 52.601 1.00 12.25
ATOM 1885 C SER 216 11.869 12.078 49.270 1.00 18.76
ATOM 1886 0 SER 216 11.691 1 1.043 48.609 1.00 17.94
ATOM 1887 N GLU 217 11.994 13.273 48.704 1.00 21.68 ATOM 1889 CA GLU 217 1 1.918 13.393 47.259 1.00 23.19
ATOM 1890 CB GLU 217 1 1.821 14.873 46.843 1.00 27.91
ATOM 1891 CG GLU 217 10.816 15.709 47.680 1.00 33.59
ATOM 1892 CD GLU 217 9.621 16.273 46.876 1.00 35.10
ATOM 1893 OE1 GLU 217 9.620 16.221 45.621 1.00 35.13 ATOM 1894 OE2 GLU 217 8.673 16.777 47.520 1.00 31.94
ATOM 1895 C GLU 217 13.162 12.740 46.668 1.00 21.25
ATOM 1896 O GLU 217 14.226 12.752 47.291 1.00 22.87
ATOM 1897 N VAL 218 13.002 12.137 45.490 1.00 19.42
ATOM 1899 CA VAL 218 14.085 11.481 44.756 1.00 15.85 ATOM 1900 CB VAL 218 13.562 11.045 43.362 1.00 1 1.20
ATOM 1901 CGI VAL 218 14.589 1 1.300 42.292 1.00 13.09
ATOM 1902 CG2 VAL 218 13.186 9.598 43.390 1.00 1 1.37
ATOM 1903 C VAL 218 15.241 12.494 44.621 1.00 18.98 ATOM 1904 O VAL 218 15.016 13.702 44.723 1.00 21.23
ATOM 1905 N GLY 219 16.472 12.029 44.403 1.00 19.04
ATOM 1907 CA GLY 219 17.574 12.974 44.292 1.00 19.99
ATOM 1908 C GLY 219 18.721 12.628 43.358 1.00 21.37 ATOM 1909 O GLY 219 18.553 1 1.952 42.341 1.00 24.03
ATOM 1910 N ASP 220 19.903 13.121 43.696 1.00 19.97
ATOM 1912 CA ASP 220 21.090 12.864 42.902 1.00 19.65
ATOM 1913 CB ASP 220 21.478 14.114 42.109 1.00 20.96
ATOM 1914 CG ASP 220 21.494 15.374 42.969 1.00 20.41 ATOM 1915 OD1 ASP 220 20.444 16.051 43.083 1.00 21.25
ATOM 1916 OD2 ASP 220 22.561 15.689 43.539 1.00 18.90
ATOM 1917 C ASP 220 22.186 12.496 43.889 1.00 18.98
ATOM 1918 O ASP 220 22.004 12.643 45.094 1.00 18.41
ATOM 1919 N ALA 221 23.316 12.020 43.380 1.00 16.31 ATOM 1921 CA ALA 221 24.435 1 1.614 44.223 1.00 12.98
ATOM 1922 CB ALA 221 25.716 1 1.688 43.434 1.00 14.02
ATOM 1923 C ALA 221 24.577 12.425 45.497 1.00 13.11
ATOM 1924 O ALA 221 24.931 11.893 46.542 1.00 11.33
ATOM 1925 N SER 222 24.306 13.720 45.402 1.00 13.91 ATOM 1927 CA SER 222 24.419 14.614 46.548 1.00 15.13
ATOM 1928 CB SER 222 23.792 15.970 46.218 1.00 13.97
ATOM 1929 OG SER 222 22.636 16.201 47.001 1.00 13.18
ATOM 1931 C SER 222 23.762 14.032 47.798 1.00 15.29
ATOM 1932 O SER 222 24.245 14.210 48.924 1.00 17.49 ATOM 1933 N LEU 223 22.659 13.330 47.604 1.00 13.36
ATOM 1935 CA LEU 223 21.975 12.758 48.740 1.00 13.61
ATOM 1936 CB LEU 223 20.777 1 1.933 48.263 1.00 16.23
ATOM 1937 CG LEU 223 19.517 12.753 47.974 1.00 12.09
ATOM 1938 CD 1 LEU 223 18.373 1 1.842 47.539 1.00 7.52 ATOM 1939 CD2 LEU 223 19.151 13.537 49.228 1.00 9.71
ATOM 1940 C LEU 223 22.927 1 1.912 49.587 1.00 12.39
ATOM 1941 O LEU 223 22.741 11.803 50.804 1.00 12.45
ATOM 1942 N LEU 224 23.947 11.332 48.945 1.00 9.56
ATOM 1944 CA LEU 224 24.935 10.489 49.637 1.00 6.50 ATOM 1945 CB LEU 224 25.807 9.725 48.619 1.00 3.46
ATOM 1946 CG LEU 224 25.143 8.968 47.449 1.00 4.36
ATOM 1947 CD1 LEU 224 26.042 8.989 46.217 1.00 2.46
ATOM 1948 CD2 LEU 224 24.870 7.528 47.843 1.00 4.63 ATOM 1949 C LEU 224 25.824 1 1.337 50.556 1.00 5.65
ATOM 1950 O LEU 224 26.028 1 1.007 51.736 1.00 2.46
ATOM 1951 N LYS 225 26.353 12.428 50.008 1.00 5.98
ATOM 1953 CA LYS 225 27.196 13.335 50.776 1.00 10.24 ATOM 1954 CB LYS 225 27.577 14.538 49.920 1.00 1 1.77
ATOM 1955 CG LYS 225 28.672 15.426 50.500 1.00 21.10
ATOM 1956 CD LYS 225 29.206 16.414 49.447 1.00 25.30
ATOM 1957 CE LYS 225 29.283 15.790 48.036 1.00 30.82
ATOM 1958 NZ LYS 225 27.956 15.652 47.319 1.00 29.17 ATOM 1962 C LYS 225 26.403 13.812 51.991 1.00 1 1.73
ATOM 1963 O LYS 225 26.908 13.812 53.125 1.00 13.61
ATOM 1964 N LEU 226 25.155 14.21 1 51.730 1.00 9.82
ATOM 1966 CA LEU 226 24.235 14.705 52.751 1.00 6.57
ATOM 1967 CB LEU 226 22.905 15.046 52.101 1.00 5.66 ATOM 1968 CG LEU 226 22.921 16.362 51.329 1.00 7.17
ATOM 1969 CD1 LEU 226 22.247 16.198 49.969 1.00 6.65
ATOM 1970 CD2 LEU 226 22.216 17.421 52.162 1.00 3.31
ATOM 1971 C LEU 226 23.999 13.716 53.885 1.00 8.20
ATOM 1972 O LEU 226 24.115 14.056 55.065 1.00 7.75 ATOM 1973 N THR 227 23.650 12.490 53.522 1.00 7.76
ATOM 1975 CA THR 227 23.406 11.456 54.517 1.00 8.20
ATOM 1976 CB THR 227 23.01 1 10.123 53.859 1.00 6.91
ATOM 1977 OG1 THR 227 21.813 10.306 53.095 1.00 5.49
ATOM 1979 CG2 THR 227 22.788 9.050 54.912 1.00 5.1 1 ATOM 1980 C THR 227 24.685 1 1.247 55.307 1.00 10.14
ATOM 1981 O THR 227 24.651 10.880 56.478 1.00 7.31
ATOM 1982 N LEU 228 25.818 11.485 54.657 1.00 13.35
ATOM 1984 CA LEU 228 27.090 11.309 55.329 1.00 14.05
ATOM 1985 CB LEU 228 28.244 11.484 54.351 1.00 16.32 ATOM 1986 CG LEU 228 29.610 11.079 54.916 1.00 18.54
ATOM 1987 CD1 LEU 228 29.454 10.217 56.160 1.00 14.58
ATOM 1988 CD2 LEU 228 30.381 10.333 53.842 1.00 22.93
ATOM 1989 C LEU 228 27.213 12.307 56.463 1.00 13.68
ATOM 1990 O LEU 228 27.458 11.925 57.604 1.00 15.94 ATOM 1991 N GLU 229 27.039 13.584 56.152 1.00 1 1.55
ATOM 1993 CA GLU 229 27.117 14.613 57.176 1.00 16.09
ATOM 1994 CB GLU 229 26.859 15.975 56.559 1.00 21.32
ATOM 1995 CG GLU 229 28.098 16.641 56.034 1.00 33.61 ATOM 1996 CD GLU 229 27.926 17.090 54.601 1.00 39.72
ATOM 1997 OE1 GLU 229 27.891 16.212 53.704 1.0043.46
ATOM 1998 OE2 GLU 229 27.820 18.317 54.372 1.0046.44
ATOM 1999 C GLU 229 26.094 14.368 58.286 1.00 14.56 ATOM 2000 O GLU 229 26.402 14.498 59.476 1.00 10.56
ATOM 2001 N GLN 230 24.873 14.018 57.895 1.00 13.79
ATOM 2003 CA GLN 230 23.826 13.763 58.870 1.00 1 1.31
ATOM 2004 CB GLN 230 22.496 13.494 58.163 1.00 6.47
ATOM 2005 CG GLN 230 21.304 13.446 59.095 0.00 14.97 ATOM 2006 CD GLN 230 20.678 14.804 59.255 0.00 2.46
ATOM 2007 OE1 GLN 230 19.786 15.007 60.078 0.00 4.67
ATOM 2008 NE2 GLN 230 21.146 15.754 58.457 1.00 36.14
ATOM 201 1 C GLN 230 24.200 12.578 59.764 1.00 11.16
ATOM 2012 O GLN 230 23.999 12.634 60.980 1.00 11.08 ATOM 2013 N ALA 231 24.766 11.530 59.155 1.00 10.39
ATOM 2015 CA ALA 231 25.171 10.308 59.864 1.00 8.29
ATOM 2016 CB ALA 231 25.521 9.214 58.866 1.00 2.46
ATOM 2017 C ALA 231 26.341 10.512 60.814 1.00 12.00
ATOM 2018 O ALA 231 26.406 9.870 61.872 1.00 1 1.08 ATOM 2019 N VAL 232 27.270 11.391 60.433 1.00 13.64
ATOM 2021 CA VAL 232 28.441 11.673 61.261 1.00 14.31
ATOM 2022 CB VAL 232 29.536 12.363 60.448 1.00 14.80
ATOM 2023 CGI VAL 232 29.917 1 1.481 59.255 1.00 13.21
ATOM 2024 CG2 VAL 232 29.058 13.727 59.985 1.00 12.33 ATOM 2025 C VAL 232 28.031 12.574 62.404 1.00 14.49
ATOM 2026 O VAL 232 28.487 12.410 63.542 1.00 12.32
ATOM 2027 N LYS 233 27.157 13.525 62.080 1.00 17.25
ATOM 2029 CA LYS 233 26.626 14.471 63.055 1.00 18.81
ATOM 2030 CB LYS 233 25.650 15.431 62.362 1.00 20.66 ATOM 2031 CG LYS 233 24.869 16.370 63.290 1.00 23.33
ATOM 2032 CD LYS 233 23.891 17.258 62.488 1.00 25.95
ATOM 2033 CE LYS 233 24.131 18.771 62.686 1.00 28.02
ATOM 2034 NZ LYS 233 25.257 19.335 61.852 1.00 25.78
ATOM 2038 C LYS 233 25.902 13.642 64.104 1.00 18.82 ATOM 2039 O LYS 233 25.997 13.901 65.298 1.00 16.83
ATOM 2040 N GLY 234 25.189 12.626 63.635 1.00 20.45
ATOM 2042 CA GLY 234 24.459 11.759 64.536 1.00 25.08
ATOM 2043 C GLY 234 25.388 1 1.052 65.493 1.00 27.96 ATOM 2044 O GLY 234 25.050 10.838 66.653 1.00 26.17
ATOM 2045 N LEU 235 26.570 10.691 65.012 1.00 34.32
ATOM 2047 CA LEU 235 27.527 10.001 65.858 1.00 41.98
ATOM 2048 CB LEU 235 28.654 9.396 65.020 1.00 44.41 ATOM 2049 CG LEU 235 29.662 8.484 65.738 1.0044.19
ATOM 2050 CD1 LEU 235 29.134 8.037 67.098 1.00 45.43
ATOM 2051 CD2 LEU 235 29.947 7.272 64.854 1.00 46.90
ATOM 2052 C LEU 235 28.1 10 10.959 66.880 1.0045.59
ATOM 2053 O LEU 235 28.204 10.637 68.063 1.0047.17 ATOM 2054 N ASN 236 28.508 12.138 66.423 1.0047.06
ATOM 2056 CA ASN 236 29.073 13.128 67.326 1.00 50.25
ATOM 2057 CB ASN 236 29.465 14.386 66.547 1.00 53.31
ATOM 2058 CG ASN 236 30.854 14.290 65.943 1.00 55.48
ATOM 2059 OD1 ASN 236 31.008 14.277 64.720 1.00 56.49 ATOM 2060 ND2 ASN 236 31.875 14.221 66.798 1.00 57.78
ATOM 2063 C ASN 236 28.040 13.492 68.385 1.00 50.56
ATOM 2064 O ASN 236 28.305 13.412 69.584 1.0048.79
ATOM 2065 N GLU 237 26.860 13.878 67.907 1.00 53.59
ATOM 2067 CA GLU 237 25.735 14.296 68.739 1.00 56.26 ATOM 2068 CB GLU 237 24.514 14.572 67.855 1.00 57.09
ATOM 2069 CG GLU 237 23.815 15.880 68.158 1.00 59.66
ATOM 2070 CD GLU 237 24.755 17.070 68.077 1.00 63.06
ATOM 2071 OE1 GLU 237 24.959 17.589 66.958 1.00 64.03
ATOM 2072 OE2 GLU 237 25.292 17.484 69.129 1.00 64.38 ATOM 2073 C GLU 237 25.321 13.345 69.855 1.00 57.39
ATOM 2074 O GLU 237 24.423 13.670 70.633 1.00 59.08
ATOM 2075 N SER 238 25.953 12.177 69.934 1.00 58.22
ATOM 2077 CA SER 238 25.611 1 1.212 70.976 1.00 58.74
ATOM 2078 CB SER 238 25.365 9.822 70.372 1.00 58.15 ATOM 2079 OG SER 238 26.318 9.509 69.370 1.00 56.13
ATOM 2081 C SER 238 26.680 11.121 72.062 1.00 60.48
ATOM 2082 O SER 238 26.400 10.677 73.173 1.00 61.49
ATOM 2083 N LYS 239 27.901 11.549 71.742 1.00 63.10
ATOM 2085 CA LYS 239 29.007 1 1.518 72.701 1.00 63.24 ATOM 2086 CB LYS 239 30.243 10.857 72.069 1.00 62.41
ATOM 2087 CG LYS 239 30.398 11.100 70.573 1.00 61.68
ATOM 2088 CD LYS 239 31.557 10.301 70.000 1.0061.13
ATOM 2089 CE LYS 239 32.486 11.182 69.177 1.00 61.30 ATOM 2090 NZ LYS 239 33.622 10.400 68.61 1 1.00 61.69 ATOM 2094 C LYS 239 29.370 12.921 73.209 1.00 63.28 ATOM 2095 O LYS 239 30.569 13.274 73.172 1.00 63.02 ATOM 2096 OT LYS 239 28.451 13.650 73.644 1.00 62.39 ATOM 2097 ZN ZN 500 13.356 1.287 58.837 1.00 15.23 ATOM 2098 ZN ZN 501 11.355 3.517 56.995 1.00 23.99 END
Table IB Atomic coordinates of the IMP-1 complex with SB-252619
CRYSTl 49.333 51.192 203.254 90.00 90.00 90.00 P 212121
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE 1 0.020270 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019534 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004920 0.00000
ATOM 1 CB LEU A 4 -2.164 3.929 80.593 1.00 58.13
ATOM 2 CG LEU A 4 -3.003 2.874 79.874 1.00 62.58
ATOM 3 CD1 LEU A 4 -4.517 3.099 80.137 1.00 58.96
ATOM 4 CD2 LEU A 4 -2.632 2.897 78.390 1.00 61.45
ATOM 5 C LEU A 4 -2.716 2.832 82.816 1.00 53.34
ATOM 6 O LEU A 4 -3.665 2.704 83.595 1.00 54.35
ATOM 7 N LEU A 4 -1.508 5.029 82.688 1.00 57.21
ATOM 8 CA LEU A 4 -2.523 4.155 82.066 1.00 55.66
ATOM 9 N PRO A 5 -1.834 1.827 82.612 1.00 50.28
ATOM 10 CD PRO A 5 -0.631 1.673 81.770 1.0048.1 1
ATOM 11 CA PRO A 5 -2.077 0.587 83.366 1.00 44.93
ATOM 12 CB PRO A 5 -1.009 -0.357 82.811 1.0047.08
ATOM 13 CG PRO A 5 -0.736 0.226 81.404 1.0045.37
ATOM 14 C PRO A 5 -1.925 0.801 84.889 1.00 40.70
ATOM 15 O PRO A 5 -1.331 1.787 85.332 1.00 37.20
ATOM 16 N ASP A 6 -2.477 -0.102 85.692 1.00 36.42
ATOM 17 CA ASP A 6 -2.312 0.055 87.126 1.00 39.21
ATOM 18 CB ASP A 6 -3.398 -0.680 87.936 1.00 48.61
ATOM 19 CG ASP A 6 -4.773 -0.007 87.842 1.00 56.70
ATOM 20 OD1 ASP A 6 -4.858 1.240 87.956 1.00 55.50
ATOM 21 OD2 ASP A 6 -5.776 -0.737 87.682 1.00 62.74
ATOM 22 C ASP A 6 -0.947 -0.493 87.516 1.00 33.49 ATOM 23 O ASP A 6 -0.251 -1.127 86.706 1.00 27.31
ATOM 24 N LEU A 7 -0.607 -0.255 88.772 1.00 29.14
ATOM 25 CA LEU A 7 0.641 -0.687 89.360 1.00 29.25
ATOM 26 CB LEU A 7 0.667 -0.329 90.852 1.00 26.67
ATOM 27 CG LEU A 7 1.873 -0.812 91.664 1.00 26.69
ATOM 28 CD1 LEU A 7 3.042 0.115 91.441 1.00 17.99
ATOM 29 CD2 LEU A 7 1.497 -0.824 93.142 1.00 26.98
ATOM 30 C LEU A 7 0.737 -2.181 89.237 1.00 28.20
ATOM 31 O LEU A 7 -0.186 -2.894 89.612 1.00 29.80
AATTOOMM 3322 NN LLYYSS AA 88 1.868 -2.667 88.739 1.00 24.30
ATOM 33 CA LYS A 8 2.024 -4.093 88.640 1.00 28.44
ATOM 34 CB LYS A 8 2.198 -4.521 87.186 1.00 36.78
ATOM 35 CG LYS A 8 3.505 -4.124 86.543 1.00 48.22
ATOM 36 CD LYS A 8 3.574 -4.721 85.151 1.00 54.97
AATTOOMM 3377 CCEE LLYYSS AA 88 4.883 -4.441 84.454 1.00 57.80
ATOM 38 NZ LYS A 8 4.840 -5.067 83.107 1.00 60.88
ATOM 39 C LYS A 8 3.226 -4.515 89.485 1.00 27.25
ATOM 40 O LYS A 8 4.204 -3.757 89.677 1.00 19.48
ATOM 41 N ILE A 9 3.122 -5.729 90.001 1.00 22.12
AATTOOMM 4422 CCAA IILLEE AA 99 4.132 -6.327 90.872 1.00 26.82
ATOM 43 CB ILE A 9 3.575 -6.479 92.285 1.00 26.16
ATOM 44 CG2 ILE A 9 4.603 -7.178 93.158 1.00 27.95
ATOM 45 CGI ILE A 9 3.125 -5.108 92.825 1.00 24.04
ATOM 46 CD1 ILE A 9 2.443 -5.151 94.152 1.00 25.94
AATTOOMM 4477 CC IILLEE AA 99 4.407 -7.719 90.359 1.00 31.98
ATOM 48 O ILE A 9 3.531 -8.589 90.425 1.00 30.94
ATOM 49 N GLU A 10 5.591 -7.952 89.825 1.00 28.39
ATOM 50 CA GLU A 10 5.868 -9.294 89.329 1.00 32.35
ATOM 51 CB GLU A 10 5.713 -9.340 87.789 1.00 37.47
AATTOOMM 5522 CCGG GGLLUU AA 1100 6.569 -8.392 86.982 1.00 55.29
ATOM 53 CD GLU A 10 6.118 -8.323 85.51 1 1.00 62.55
ATOM 54 OE1 GLU A 10 4.987 -7.857 85.262 1.00 63.79
ATOM 55 OE2 GLU A 10 6.881 -8.739 84.610 1.00 64.16
ATOM 56 C GLU A 10 7.226 -9.806 89.792 1.00 29.96
AATTOOMM 5577 OO GGLLUU AA 1100 8.173 -9.037 89.985 1.00 27.32
ATOM 58 N LYS A 11 7.318 -1 1.105 90.006 1.00 28.05
ATOM 59 CA LYS A 11 8.573 -11.691 90.470 1.00 31.90
ATOM 60 CB LYS A 1 1 8.351 -13.157 90.828 1.00 36.99 ATOM 61 CG LYS A 11 9.470-13.75291.653 1.0044.43
ATOM 62 CD LYS A 11 9.070-15.10292.205 1.0049.21
ATOM 63 CE LYS A 11 10.114-15.62393.173 1.0054.83
ATOM 64 NZ LYS A 11 9.707-16.955 93.677 1.0061.22
ATOM 65 C LYS A 11 9.675-11.54989.426 1.0032.49
ATOM 66 0 LYS A 11 9.427-11.70488.231 1.0032.37
ATOM 67 N LEU A 12 10.888-11.213 89.878 1.0030.38
ATOM 68 CA LEU A 12 12.045-11.05788.996 1.0026.64
ATOM 69 CB LEU A 12 12.762 -9.721 89.247 1.0027.54
AATTOOMM 7700 CCGG LLEEUU AA 1122 14.122 -9.47788.567 1.0018.35
ATOM 71 CD1LEUA 12 13.983 -9.43887.058 1.0027.65
ATOM 72 CD2LEUA 12 14.693 -8.12389.041 1.0022.95
ATOM 73 C LEU A 12 13.029-12.19789.240 1.0028.78
ATOM 74 0 LEU A 12 13.630-12.69488.309 1.0033.61
AATTOOMM 7755 NN AASSPP AA 1133 13.204-12.59390.497 1.0027.99
ATOM 76 CA ASP A 13 14.117-13.68990.813 1.0029.62
ATOM 77 CB ASP A 13 15.576-13.19590.697 1.0032.19
ATOM 78 CG ASP A 13 16.584-14.34090.678 1.0040.29
ATOM 79 OD1ASPA 13 16.233-15.461 91.122 1.0044.53
AATTOOMM 8800 OODD22AASSPPAA 1133 17.736-14.10590.248 1.0033.30
ATOM 81 C ASP A 13 13.773-14.10292.244 1.0026.73
ATOM 82 O ASP A 13 12.897-13.50492.871 1.0025.57
ATOM 83 N GLU A 14 14.430-15.121 92.784 1.0028.91
ATOM 84 CA GLU A 14 14.067-15.51794.142 1.0031.64
AATTOOMM 8855 CCBB GGLLUU AA 1144 14.897-16.71294.607 1.0040.63
ATOM 86 CG GLU A 14 14.274-18.04694.240 1.0051.90
ATOM 87 CD GLU A 14 12.819-18.14694.692 1.0058.87
ATOM 88 OE1 GLU A 14 12.521-17.86695.883 1.0059.33
ATOM 89 OE2GLUA 14 11.970-18.51393.846 1.0064.20
AATTOOMM 9900 CC GGLLUU AA 1144 14.168-14.38795.169 1.0026.23
ATOM 91 0 GLU A 14 15.186-13.69995.245 1.0028.24
ATOM 92 N GLY A 15 13.080-14.19495.913 1.0031.39
ATOM 93 CA GLY A 15 13.010-13.15496.940 1.0032.68
ATOM 94 C GLY A 15 13.055-11.71396.421 1.0023.18
AATTOOMM 9955 OO GGLLYY AA 1155 13.256-10.77497.205 1.0025.21
ATOM 96 N VAL A 16 12.888-11.54495.114 1.0021.88
ATOM 97 CA VAL A 16 12.924-10.22494.499 1.0023.35
ATOM 98 CB VAL A 16 14.255 -9.94093.783 1.0020.47 ATOM 99 CGI VAL A 16 14.233 -8.487 93.229 1.00 22.80
ATOM 100 CG2 VAL A 16 15.401 -10.164 94.748 1.00 23.26
ATOM 101 C VAL A 16 11.831 -9.965 93.489 1.00 26.03
ATOM 102 O VAL A 16 11.692 -10.681 92.482 1.00 27.57
ATOM 103 N TYR A 17 11.061 -8.912 93.761 1.00 27.71
ATOM 104 CA TYR A 17 9.982 -8.498 92.885 1.00 24.73
ATOM 105 CB TYR A 17 8.674 -8.457 93.660 1.00 22.24
ATOM 106 CG TYR A 17 8.201 -9.789 94.137 1.0026.22
ATOM 107 CD1 TYR A 17 8.837 -10.453 95.183 1.00 30.58 A ATTOOMM 1 10088 C CEE11 TTYYRR AA 1177 8.375 -11.702 95.625 1.00 35.90
ATOM 109 CD2 TYR A 17 7.087 -10.402 93.541 1.00 32.05
ATOM 1 10 CE2 TYR A 17 6.624 -1 1.654 93.982 1.00 37.30
ATOM 1 11 CZ TYR A 17 7.270 -12.290 95.024 1.00 39.57
ATOM 112 OH TYR A 17 6.785 -13.493 95.503 1.0048.35 A ATTOOMM 1 1 1133 C C TTYYRR AA 1177 10.225 -7.108 92.328 1.00 24.27
ATOM 1 14 O TYR A 17 10.842 -6.255 92.978 1.00 16.48
ATOM 115 N VAL A 18 9.693 -6.867 91.140 1.00 20.22
ATOM 116 CA VAL A 18 9.788 -5.568 90.508 1.00 22.03
ATOM 117 CB VAL A 18 10.218 -5.650 89.025 1.00 20.40
AATTOOMM 11 1188 CCGGII VVAALL AA 1188 10.150 -4.227 88.378 1.00 24.18
ATOM 1 19 CG2 VAL A 18 11.602 -6.228 88.904 1.00 25.74
ATOM 120 C VAL A 18 8.385 -4.930 90.559 1.00 25.08
ATOM 121 O VAL A 18 7.370 -5.563 90.205 1.00 23.28
ATOM 122 N HIS A 19 8.297 -3.714 91.078 1.00 20.12
AATTOOMM 112233 CCAA HHIISS AA 1199 6.993 -3.052 91.052 1.00 22.71
ATOM 124 C HIS A 19 7.082 -1.969 89.973 1.00 22.30
ATOM 125 O HIS A 19 8.098 -1.253 89.840 1.00 20.1 1
ATOM 126 CB HIS A 19 6.577 -2.530 92.433 1.00 17.71
ATOM 127 CG HIS A 19 7.532 -1.573 93.066 1.00 21.93
AATTOOMM 112288 NNDD11 HHIISS AA 1199 7.460 -0.222 92.829 1.00 20.60
ATOM 129 CE1 HIS A 19 8.368 0.321 93.617 1.00 25.32
ATOM 130 CD2 HIS A 19 8.504 -1.819 93.982 1.00 18.87 ATOM 131 NE2 HIS A 19 9.033 -0.613 94.333 1.00 18.08 ATOM 132 N THR A 20 6.044 -1.879 89.148 1.00 23.96 ATOM 133 CA THR A 20 6.083 -0.927 88.037 1.00 19.66 ATOM 134 CB THR A 20 6.263 -1.688 86.686 1.00 27.44 ATOM 135 OG1 THR A 20 7.457 -2.479 86.711 1.0026.45 ATOM 136 CG2 THR A 20 6.334 -0.717 85.506 1.00 26.18 ATOM 137 C THR A 20 4.800 -0.095 87.951 1.00 25.59
ATOM 138 O THR A 20 3.713 -0.647 87.996 1.00 20.43
ATOM 139 N SER A 21 4.946 1.226 87.888 1.00 24.99
ATOM 140 CA SER A 21 3.805 2.1 13 87.668 1.00 29.81
ATOM 141 CB SER A 21 3.712 3.21 1 88.71 1 1.00 30.93
ATOM 142 OG SER A 21 4.726 4.174 88.472 1.00 35.28 ATOM 143 C SER A 21 4.142 2.785 86.325 1.00 34.23 ATOM 144 O SER A 21 5.299 2.731 85.847 1.00 24.19 ATOM 145 N PHE A 22 3.138 3.413 85.718 1.00 38.01 ATOM 146 CA PHE A 22 3.330 4.102 84.450 1.00 40.35 ATOM 147 CB PHE A 22 2.590 3.391 83.323 1.0040.49 ATOM 148 CG PHE A 22 2.916 1.944 83.234 1.00 34.52 ATOM 149 CD1 PHE A 22 2.404 1.055 84.173 1.00 39.12 ATOM 150 CD2 PHE A 22 3.816 1.487 82.302 1.00 34.23 ATOM 151 CE1 PHE A 22 2.791 -0.271 84.183 1.00 41.47 ATOM 152 CE2 PHE A 22 4.213 0.162 82.298 1.0042.09 ATOM 153 CZ PHE A 22 3.699 -0.721 83.242 1.0041.05 ATOM 154 C PHE A 22 2.840 5.516 84.595 1.0043.14 ATOM 155 O PHE A 22 1.959 5.804 85.405 1.0044.52 ATOM 156 N GLU A 23 3.445 6.401 83.818 1.00 43.37 ATOM 157 CA GLU A 23 3.1 17 7.817 83.862 1.0044.97 ATOM 158 CB GLU A 23 4.061 8.537 84.830 1.00 51.18 ATOM 159 CG GLU A 23 3.629 8.517 86.264 1.00 54.56 ATOM 160 CD GLU A 23 2.426 9.383 86.477 1.00 57.84 ATOM 161 OE1 GLU A 23 2.518 10.605 86.204 1.00 58.12 ATOM 162 OE2 GLU A 23 1.393 8.837 86.908 1.00 59.33 ATOM 163 C GLU A 23 3.257 8.475 82.509 1.00 41.73 ATOM 164 O GLU A 23 4.141 8.1 14 81.745 1.00 35.33 ATOM 165 N GLU A 24 2.379 9.435 82.223 1.0044.51 ATOM 166 CA GLU A 24 2.477 10.190 80.982 1.00 45.35 ATOM 167 CB GLU A 24 1.115 10.721 80.510 1.00 50.65 ATOM 168 CG GLU A 24 1.222 1 1.670 79.290 1.00 55.89 ATOM 169 CD GLU A 24 2.065 11.087 78.147 1.00 58.55 ATOM 170 OE1 GLU A 24 1.863 9.903 77.826 1.00 59.94 ATOM 171 OE2 GLU A 24 2.913 11.801 77.559 1.00 57.56 ATOM 172 C GLU A 24 3.350 11.354 81.371 1.0042.36 ATOM 173 O GLU A 24 3.011 12.104 82.285 1.00 38.36 ATOM 174 N VAL A 25 4.488 11.482 80.698 1.0043.07 ATOM 175 CA VAL A 25 5.41 1 12.559 80.987 1.00 42.05
ATOM 176 CB VAL A 25 6.796 12.002 81.312 1.00 42.15
ATOM 177 CGI VAL A 25 7.768 13.147 81.567 1.00 45.10
ATOM 178 CG2 VAL A 25 6.699 1 1.079 82.513 1.00 38.73
ATOM 179 C VAL A 25 5.498 13.500 79.787 1.0043.12
ATOM 180 O VAL A 25 5.918 13.101 78.710 1.0040.46
ATOM 181 N ASN A 26 5.088 14.749 79.979 1.0045.13
ATOM 182 CA ASN A 26 5.123 15.726 78.897 1.0047.23
ATOM 183 CB ASN A 26 4.856 17.138 79.417 1.00 55.91
AATTOOMM 118844 CCGG AASSNN AA 2266 3.368 17.400 79.650 1.0068.16
ATOM 185 OD1 ASN A 26 2.569 17.414 78.701 1.00 66.84
ATOM 186 ND2 ASN A 26 2.989 17.595 80.915 1.00 70.03
ATOM 187 C ASN A 26 6.416 15.713 78.115 1.0045.51
ATOM 188 0 ASN A 26 7.527 15.782 78.668 1.00 38.61
AATTOOMM 118899 NN GGLLYY AA 2277 6.250 15.607 76.807 1.00 44.24
ATOM 190 CA GLY A 27 7.395 15.583 75.934 1.0041.04
ATOM 191 C GLY A 27 7.995 14.202 75.796 1.0043.27
ATOM 192 O GLY A 27 8.793 13.999 74.876 1.0041.25
ATOM 193 N TRP A 28 7.615 13.250 76.661 1.00 37.66 ATOM 194 CA TRP A 28 8.205 11.912 76.571 1.00 37.46 ATOM 195 CB TRP A 28 9.018 11.592 77.832 1.00 29.93 ATOM 196 CG TRP A 28 10.066 12.597 78.167 1.0040.64 ATOM 197 CD2 TRP A 28 1 1.385 12.679 77.615 1.00 38.10 ATOM 198 CE2 TRP A 28 12.012 13.810 78.197 1.00 37.73 ATOM 199 CE3 TRP A 28 12.097 11.907 76.681 1.00 38.94 ATOM 200 CD1 TRP A 28 9.950 13.660 79.044 1.0041.98 ATOM 201 NE1 TRP A 28 1 1.115 14.383 79.060 1.00 37.81 ATOM 202 CZ2 TRP A 28 13.322 14.190 77.882 1.00 41.52 ATOM 203 CZ3 TRP A 28 13.416 12.287 76.358 1.00 38.85 ATOM 204 CH2 TRP A 28 14.009 13.420 76.964 1.0042.93 ATOM 205 C TRP A 28 7.254 10.751 76.310 1.00 37.71 ATOM 206 O TRP A 28 7.710 9.664 75.972 1.00 38.63 ATOM 207 N GLY A 29 5.948 10.971 76.452 1.00 32.19 ATOM 208 CA GLY A 29 5.005 9.889 76.250 1.00 36.98 ATOM 209 C GLY A 29 4.840 9.042 77.517 1.00 36.85 ATOM 210 O GLY A 29 5.070 9.554 78.626 1.00 32.93 ATOM 211 N VAL A 30 4.439 7.774 77.367 1.00 33.88 ATOM 212 CA VAL A 30 4.275 6.878 78.524 1.00 35.15 ATOM 213 CB VAL A 30 3.444 5.617 78.224 1.00 36.17
ATOM 214 CGI VAL A 30 3.404 4.712 79.470 1.00 34.55
ATOM 215 CG2 VAL A 30 2.030 6.007 77.817 1.00 37.20
ATOM 216 C VAL A 30 5.650 6.402 78.945 1.00 33.60 ATOM 217 O VAL A 30 6.465 5.976 78.110 1.00 31.87
ATOM 218 N VAL A 31 5.893 6.480 80.246 1.00 32.52
ATOM 219 CA VAL A 31 7.186 6.084 80.805 1.00 29.78
ATOM 220 CB VAL A 31 8.008 7.310 81.265 1.00 29.17
ATOM 221 CGI VAL A 31 9.306 6.815 81.900 1.00 29.81 ATOM 222 CG2 VAL A 31 8.360 8.238 80.060 1.00 23.27
ATOM 223 C VAL A 31 6.964 5.204 82.026 1.00 29.54
ATOM 224 O VAL A 31 6.211 5.557 82.923 1.00 25.30
ATOM 225 N PRO A 32 7.61 1 4.040 82.067 1.00 30.79
ATOM 226 CD PRO A 32 8.493 3.395 81.076 1.00 24.58 ATOM 227 CA PRO A 32 7.416 3.178 83.240 1.00 25.29
ATOM 228 CB PRO A 32 7.827 1.812 82.708 1.00 27.39
ATOM 229 CG PRO A 32 9.054 2.185 81.873 1.00 27.72
ATOM 230 C PRO A 32 8.326 3.629 84.389 1.00 25.01
ATOM 231 O PRO A 32 9.290 4.379 84.152 1.00 27.34 ATOM 232 N LYS A 33 7.992 3.224 85.618 1.00 22.36
ATOM 233 CA LYS A 33 8.841 3.471 86.786 1.00 22.10
ATOM 234 CB LYS A 33 8.309 4.541 87.741 1.00 18.87
ATOM 235 CG LYS A 33 9.198 4.723 88.997 1.00 17.02
ATOM 236 CD LYS A 33 10.685 5.037 88.619 1.00 14.29 ATOM 237 CE LYS A 33 11.571 5.251 89.921 1.00 17.57
ATOM 238 NZ LYS A 33 11.663 4.002 90.783 1.00 11.28
ATOM 239 C LYS A 33 8.907 2.130 87.536 1.00 22.59
ATOM 240 O LYS A 33 7.916 1.647 88.069 1.00 18.80
ATOM 241 N HIS A 34 10.099 1.543 87.547 1.00 19.07 ATOM 242 CA HIS A 34 10.376 0.261 88.199 1.00 18.44
ATOM 243 C HIS A 34 1 1.089 0.512 89.515 1.00 15.45
ATOM 244 0 HIS A 34 12.021 1.311 89.573 1.00 15.76
ATOM 245 CB HIS A 34 1 1.348 -0.615 87.364 1.00 16.94
ATOM 246 CG HIS A 34 10.901 -0.858 85.966 1.00 21.99 ATOM 247 ND1 HIS A 34 1 1.620 -0.475 84.849 1.00 24.05
ATOM 248 CD2 HIS A 34 9.758 -1.422 85.501 1.00 21.13
ATOM 249 NE2 HIS A 34 9.765 -1.385 84.071 1.00 25.00
ATOM 250 CE1 HIS A 34 10.906 -0.803 83.745 1.00 17.82 ATOM 251 N GLY A 35 10.675 -0.22590.534 1.0019.18
ATOM 252 CA GLY A 35 11.306 -0.16091.842 1.0017.91
ATOM 253 C GLY A 35 11.343 -1.63892.221 1.0018.62
ATOM 254 O GLY A 35 10.894 -2.50891.445 1.0016.35 ATOM 255 N LEUA 36 11.860 -1.96693.383 1.0013.50
ATOM 256 CA LEUA 36 11.875 -3.38793.720 1.0015.13
ATOM 257 CB LEUA 36 13.317 -3.93993.725 1.0011.60
ATOM 258 CG LEUA 36 14.234 -3.83292.501 1.0014.82
ATOM 259 CD1LEUA 36 15.639 -4.47692.803 1.0017.33 ATOM 260 CD2 LEU A 36 13.550 -4.51091.345 1.0015.99
ATOM 261 C LEUA 36 11.344 -3.59695.099 1.0017.72
ATOM 262 O LEUA 36 11.155 -2.62995.840 1.0019.00
ATOM 263 N VAL A 37 11.030 -4.85695.410 1.0016.91
ATOM 264 CA VAL A 37 10.702 -5.23096.786 1.0018.80 ATOM 265 CB VAL A 37 9.241 -5.631 97.004 1.0025.47
ATOM 266 CGI VAL A 37 9.090 -6.11798.441 1.0023.25
ATOM 267 CG2VALA 37 8.298 -4.41896.765 1.0016.43
ATOM 268 C VAL A 37 11.636 -6.43597.008 1.0018.70
ATOM 269 O VAL A 37 11.696 -7.34696.159 1.0017.08 ATOM 270 N VAL A 38 12.396 -6.42798.098 1.0018.62
ATOM 271 CA VAL A 38 13.332 -7.51698.367 1.0019.97
ATOM 272 CB VAL A 38 14.797 -7.03598.502 1.0021.29
ATOM 273 CGI VAL A 38 15.715 -8.24298.865 1.0020.16
ATOM 274 CG2VALA 38 15.262 -6.40297.200 1.0019.22 ATOM 275 C VAL A 38 12.912 -8.13899.667 1.0023.64
ATOM 2760 VAL A 38 12.650 -7.448100.653 1.0020.82
ATOM 277 N LEUA 39 12.850 -9.45999.659 1.0020.34
ATOM 278 CA LEUA 39 12.442-10.193100.843 1.0024.16
ATOM 279 CB LEUA 39 11.496-11.361100.467 1.0027.60 ATOM 280 CG LEUA 39 10.258-11.05299.623 1.0032.23
ATOM 281 CD1 LEU A 39 9.438-12.33099.457 1.0036.65
ATOM 282 CD2LEUA 39 9.437 -9.968100.271 1.0020.78
ATOM 283 C LEUA 39 13.674-10.777101.505 1.0025.94
ATOM 2840 LEUA 39 14.517-11.340100.838 1.0027.30 ATOM 285 N VALA 40 13.758-10.610102.814 1.0030.93
ATOM 286 CA VAL A 40 14.822-11.147103.634 1.0030.43
ATOM 287 CB VAL A 40 15.688-10.011104.206 1.0031.26
ATOM 288 CGI VAL A 40 16.645-10.564105.254 1.0037.86 ATOM 289 CG2VALA 40 16.472 -9.345103.088 1.0020.09
ATOM 290 C VAL A 40 14.045-11.868104.7 1 1.0033.59
ATOM 291 O VAL A 40 13.316-11.239105.513 1.0035.33
ATOM 292 N ASN A 41 14.132-13.196104.804 1.0039.61 ATOM 293 CA ASN A 41 13.410-13.961105.844 1.0039.48
ATOM 294 CB ASN A 41 14.276-14.142107.113 1.0041.45
ATOM 295 CG ASN A 41 15.650-14.677106.813 1.0047.94
ATOM 2960D1ASNA 41 15.793-15.613106.017 1.0043.75
ATOM 297 ND2 ASN A 41 16.676-14.104107.459 1.0039.43 ATOM 298 C ASN A 41 12.087-13.334106.332 1.0039.98
ATOM 299 O ASN A 41 12.091-12.647107.366 1.0041.60
ATOM 300 N ALAA 42 10.972-13.535105.637 1.0041.91
ATOM 301 CA ALA A 42 9.690-12.990106.150 1.0037.03
ATOM 302 CB ALA A 42 9.421-13.553107.552 1.0039.67 ATOM 303 C ALA A 42 9.496-11.477106.208 1.0035.82
ATOM 304 O ALA A 42 8.423-11.012106.611 1.0034.67
ATOM 305 N GLUA 43 10.521-10.700105.857 1.0033.42
ATOM 306 CA GLUA 43 10.397 -9.241105.884 1.0029.56
ATOM 307 CB GLUA 43 11.399 -8.669106.875 1.0033.21 ATOM 308 CG GLUA 43 11.279 -9.357108.217 1.0045.30
ATOM 309 CD GLUA 43 12.190 -8.778109.252 1.0042.90
ATOM 310 OE1 GLU A 43 13.408 -8.665108.961 1.0051.64
ATOM 3H OE2GLUA 43 11.680 -8.455110.352 1.0048.62
ATOM 312 C GLUA 43 10.636 -8.683104.484 1.0023.09 ATOM 313 O GLUA 43 11.444 -9.244103.721 1.0028.72
ATOM 314 N ALA A 44 9.982 -7.568104.167 1.0019.46
ATOM 315 CA ALA A 44 10.067 -6.966102.808 1.0020.49
ATOM 316 CB ALA A 44 8.639 -6.820102.196 1.0013.93
ATOM 317 C ALA A 44 10.708 -5.593102.858 1.0016.27 ATOM 318 O ALA A 44 10.432 -4.821103.790 1.0015.63
ATOM 319 N TYRA 45 11.574 -5.307101.883 1.0018.37
ATOM 320 CA TYRA 45 12.196 -3.987101.801 1.0020.53
ATOM 321 CB TYRA 45 13.729 -4.050101.903 1.0018.91
ATOM 322 CG TYRA 45 14.199 -4.428103.270 1.0026.42 ATOM 323 CD1 TYR A 45 14.130 -5.759103.701 1.0029.53
ATOM 324 CE1 TYR A 45 14.510 -6.117104.997 1.0032.17
ATOM 325 CD2TYRA 45 14.657 -3.461104.1601.0023.81
ATOM 326 CE2TYRA 45 15.038 -3.809105.462 1.0028.88 ATOM 327 CZ TYR A 45 14.956 -5.140 105.861 1.00 28.78
ATOM 328 OH TYR A 45 15.286 -5.504 107.144 1.00 34.57
ATOM 329 C TYR A 45 1 1.825 -3.359 100.473 1.00 16.76
ATOM 330 O TYR A 45 1 1.927 -3.995 99.427 1.00 14.90 ATOM 331 N LEU A 46 11.351 -2.1 17 100.519 1.00 17.19
ATOM 332 CA LEU A 46 11.002 -1.403 99.297 1.00 16.35
ATOM 333 CB LEU A 46 9.965 -0.324 99.615 1.00 17.09
ATOM 334 CG LEU A 46 8.479 -0.705 99.468 1.00 26.82
ATOM 335 CD1 LEU A 46 8.215 -2.046 100.065 1.00 21.87 ATOM 336 CD2 LEU A 46 7.581 0.390 100.107 1.00 21.61
ATOM 337 C LEU A 46 12.264 -0.731 98.746 1.00 16.66
ATOM 338 O LEU A 46 12.945 -0.024 99.506 1.00 19.27
ATOM 339 N ILE A 47 12.576 -0.938 97.459 1.00 16.81
ATOM 340 CA ILE A 47 13.725 -0.272 96.827 1.00 17.02 ATOM 341 CB ILE A 47 14.644 -1.236 96.048 1.00 17.25
ATOM 342 CG2 ILE A 47 15.898 -0.469 95.606 1.00 14.58
ATOM 343 CGI ILE A 47 14.954 -2.483 96.897 1.00 20.67
ATOM 344 CD1 ILE A 47 15.449 -2.265 98.304 1.00 13.82
ATOM 345 C ILE A 47 13.016 0.685 95.861 1.00 12.22 ATOM 346 O ILE A 47 12.588 0.313 94.785 1.00 12.94
ATOM 347 N ASP A 48 12.942 1.937 96.295 1.00 12.02
ATOM 348 CA ASP A 48 12.196 3.012 95.661 1.00 13.41
ATOM 349 CB ASP A 48 12.396 3.109 94.153 1.00 13.83
ATOM 350 CG ASP A 48 13.546 4.086 93.790 1.00 17.60 ATOM 351 0D1 ASP A 48 14.381 4.330 94.670 1.00 18.89
ATOM 352 OD2 ASP A 48 13.627 4.584 92.652 1.00 20.84
ATOM 353 C ASP A 48 10.706 2.815 96.003 1.00 19.98
ATOM 354 O ASP A 48 10.204 1.696 96.056 1.00 15.72
ATOM 355 N THR A 49 10.042 3.913 96.351 1.00 20.16 ATOM 356 CA THR A 49 8.635 3.840 96.633 1.00 21.09
ATOM 357 CB THR A 49 8.147 4.949 97.597 1.00 24.73
ATOM 358 OG1 THR A 49 8.319 6.234 96.958 1.00 15.83
ATOM 359 CG2 THR A 49 8.889 4.901 98.915 1.00 23.21
ATOM 360 C THR A 49 7.979 4.211 95.339 1.00 24.18 ATOM 361 O THR A 49 8.639 4.692 94.424 1.00 22.45
ATOM 362 N PRO A 50 6.680 3.882 95.203 1.00 21.72
ATOM 363 CD PRO A 50 5.909 3.000 96.093 1.00 21.33
ATOM 364 CA PRO A 50 5.907 4.237 94.024 1.00 15.60 ATOM 365 CB PRO A 50 4.578 3.481 94.237 1.00 18.81
ATOM 366 CG PRO A 50 5.081 2.224 95.087 1.00 23.39
ATOM 367 C PRO A 50 5.756 5.764 94.164 1.00 16.66
ATOM 368 0 PRO A 50 6.1 1 1 6.365 95.183 1.00 17.91 ATOM 369 N PHE A 51 5.168 6.362 93.148 1.00 24.16
ATOM 370 CA PHE A 51 4.989 7.790 93.001 1.00 22.95
ATOM 371 CB PHE A 51 4.689 8.011 91.505 1.00 33.10
ATOM 372 CG PHE A 51 4.626 9.434 91.076 1.00 37.74
ATOM 373 CD1 PHE A 51 5.788 10.152 90.828 1.00 34.64 ATOM 374 CD2 PHE A 51 3.386 10.047 90.853 1.00 41.86
ATOM 375 CE1 PHE A 51 5.734 1 1.466 90.354 1.0045.10
ATOM 376 CE2 PHE A 51 3.312 1 1.365 90.381 1.0046.39
ATOM 377 CZ PHE A 51 4.495 12.078 90.129 1.00 46.38
ATOM 378 C PHE A 51 3.923 8.424 93.886 1.00 24.51 ATOM 379 0 PHE A 51 4.078 9.562 94.325 1.00 16.72
ATOM 380 N THR A 52 2.869 7.672 94.195 1.00 25.77
ATOM 381 CA THR A 52 1.788 8.198 95.002 1.00 25.29
ATOM 382 CB THR A 52 0.475 8.138 94.221 1.00 27.01
ATOM 383 OG1 THR A 52 0.218 6.771 93.876 1.00 26.81 ATOM 384 CG2 THR A 52 0.567 8.990 92.911 1.00 31.62
ATOM 385 C THR A 52 1.552 7.457 96.302 1.00 26.25
ATOM 386 O THR A 52 1.975 6.319 96.460 1.00 25.60
ATOM 387 N ALA A 53 0.827 8.097 97.207 1.00 21.53
ATOM 388 CA ALA A 53 0.517 7.471 98.463 1.00 25.88 ATOM 389 CB ALA A 53 -0.242 8.446 99.400 1.00 25.12
ATOM 390 C ALA A 53 -0.346 6.247 98.186 1.00 23.35
ATOM 391 O ALA A 53 -0.167 5.217 98.829 1.00 18.97
ATOM 392 N LYS A 54 -1.303 6.362 97.261 1.00 21.51
ATOM 393 CA LYS A 54 -2.165 5.205 96.977 1.00 27.02 ATOM 394 CB LYS A 54 -3.425 5.604 96.200 1.00 37.81
ATOM 395 CG LYS A 54 -3.234 6.305 94.911 1.00 46.84
ATOM 396 CD LYS A 54 -4.603 6.545 94.236 1.00 56.09
ATOM 397 CE LYS A 54 -5.208 5.250 93.684 1.00 56.76
ATOM 398 NZ LYS A 54 -4.282 4.607 92.690 1.00 54.58 ATOM 399 C LYS A 54 -1.445 4.030 96.313 1.00 25.12
ATOM 400 O LYS A 54 -1.781 2.893 96.626 1.00 22.86
ATOM 401 N ASP A 55 -0.461 4.263 95.423 1.00 17.35
ATOM 402 CA ASP A 55 0.271 3.123 94.859 1.00 22.09 ATOM 403 CB ASP A 55 1.158 3.472 93.649 1.00 21.48
ATOM 404 CG ASP A 55 0.373 3.464 92.334 1.00 33.72
ATOM 405 OD1 ASP A 55 -0.804 3.035 92.332 1.00 27.98
ATOM 406 OD2 ASP A 55 0.930 3.855 91.301 1.00 26.25 ATOM 407 C ASP A 55 1.166 2.535 95.943 1.00 20.67
ATOM 408 O ASP A 55 1.400 1.347 95.943 1.00 20.07
ATOM 409 N THR A 56 1.649 3.362 96.864 1.00 19.24
ATOM 410 CA THR A 56 2.497 2.847 97.946 1.00 18.06
ATOM 411 CB THR A 56 3.201 4.009 98.712 1.00 18.58 ATOM 412 OG1 THR A 56 3.978 4.777 97.789 1.00 16.31
ATOM 413 CG2 THR A 56 4.106 3.465 99.817 1.00 13.61
ATOM 414 C THR A 56 1.679 2.004 98.904 1.00 14.97
ATOM 415 O THR A 56 2.139 0.977 99.414 1.00 17.56
ATOM 416 N GLU A 57 0.421 2.401 99.130 1.00 16.66 ATOM 417 CA GLU A 57 -0.429 1.641 100.030 1.00 16.37
ATOM 418 CB GLU A 57 -1.714 2.411 100.304 1.00 18.38
ATOM 419 CG GLU A 57 -2.654 1.822 101.362 1.00 30.23
ATOM 420 CD GLU A 57 -3.403 0.639 100.859 1.0040.06
ATOM 421 OE1 GLU A 57 -3.627 0.573 99.622 1.0043.23 ATOM 422 OE2 GLU A 57 -3.794 -0.210 101.692 1.00 50.81
ATOM 423 C GLU A 57 -0.726 0.288 99.391 1.00 14.64
ATOM 424 0 GLU A 57 -0.766 -0.724 100.071 1.00 16.63
ATOM 425 N LYS A 58 -0.919 0.291 98.083 1.00 15.93
ATOM 426 CA LYS A 58 -1.207 -0.904 97.295 1.00 19.89 ATOM 427 CB LYS A 58 -1.419 -0.509 95.825 1.00 18.75
ATOM 428 CG LYS A 58 -1.732 -1.690 94.879 1.00 27.05
ATOM 429 CD LYS A 58 -2.044 -1.249 93.436 1.00 32.67
ATOM 430 CE LYS A 58 -3.335 -0.462 93.403 1.00 40.53
ATOM 431 NZ LYS A 58 -3.290 0.672 94.380 1.0043.99 ATOM 432 C LYS A 58 -0.047 -1.882 97.348 1.00 26.65
ATOM 433 O LYS A 58 -0.225 -3.087 97.567 1.00 21.28
ATOM 434 N LEU A 59 1.154 -1.350 97.117 1.00 23.33
ATOM 435 CA LEU A 59 2.351 -2.176 97.124 1.00 20.37
ATOM 436 CB LEU A 59 3.567 -1.321 96.749 1.00 16.92 ATOM 437 CG LEU A 59 4.905 -2.102 96.710 1.00 23.34
ATOM 438 CD1 LEU A 59 4.870 -3.143 95.600 1.00 20.53
ATOM 439 CD2 LEU A 59 6.062 -1.1 18 96.472 1.00 18.40
ATOM 440 C LEU A 59 2.559 -2.853 98.471 1.00 22.24 ATOM 441 O LEUA 59 2.788 -4.07798.531 1.0025.73
ATOM 442 N VAL A 60 2.481 -2.05699.536 1.0016.97
ATOM 443 CA VAL A 60 2.638 -2.497100.928 1.0018.25
ATOM 444 CB VAL A 60 2.514 -1.299101.926 1.0017.04 ATOM 445 CGI VAL A 60 2.286 -1.787103.444 1.0015.69
ATOM 446 CG2VALA 60 3.782 -0.495101.914 1.0019.56
ATOM 447 C VAL A 60 1.570 -3.536101.238 1.0024.19
ATOM 448 O VAL A 60 1.860 -4.593101.774 1.0023.02
ATOM 449 N THRA 61 0.328 -3.230100.893 1.0020.16 ATOM 450 C A THRA 61 -0.776 -4.137101.172 1.0018.24
ATOM 451 CB THRA 61 -2.111 -3.464100.832 1.0021.37
ATOM 452 OG1THRA 61 -2.285 -2.327101.685 1.0022.42
ATOM 453 CG2THRA 61 -3.293 -4.437101.075 1.0025.33
ATOM 454 C THRA 61 -0.620 -5.490100.422 1.0019.89 ATOM 455 O THRA 61 -0.967 -6.535100.939 1.0025.57
ATOM 456 N TRP A 62 -0.057 -5.47399.242 1.0018.39
ATOM 457 CA TRP A 62 0.136 -6.70098.485 1.0019.12
ATOM 458 CB TRPA 62 0.735 -6.37497.127 1.0019.67
ATOM 459 CG TRPA 62 0.673 -7.50796.128 1.0022.58 ATOM 460 CD2 TRP A 62 1.671 -8.511 95.890 1.0026.28
ATOM 461 CE2TRPA 62 1.191 -9.34394.850 1.0028.83
ATOM 462 CE3TRPA 62 2.918 -8.78496.447 1.0026.23
ATOM 463 CD1TRPA 62 -0.349 -7.77495.248 1.0030.27
ATOM 464 NE1TRPA 62 -0.039 -8.87094.479 1.0028.72 ATOM 465 CZ2 TRP A 62 1.922-10.431 94.361 1.0036.12
ATOM 466 CZ3TRPA 62 3.649 -9.86095.962 1.0033.12
ATOM 467 CH2TRPA 62 3.151-10.67494.926 1.0031.00
ATOM 468 C TRPA 62 1.074 -7.66699.232 1.0026.29
ATOM 469 O TRPA 62 0.838 -8.89299.244 1.0020.33 ATOM 470 N PHE A 63 2.135 -7.12699.852 1.0019.07
ATOM 471 CA PHE A 63 3.060 -7.960100.611 1.0024.39
ATOM 472 CB PHE A 63 4.453 -7.307100.658 1.0020.59
ATOM 473 CG PHE A 63 5.189 -7.45499.364 1.0021.02
ATOM 474 CD1PHEA 63 5.888 -8.64299.066 1.0017.13 ATOM 475 CD2PHEA 63 5.075 -6.47898.373 1.0013.59
ATOM 476 CE1PHEA 63 6.441 -8.83797.808 1.0023.43
ATOM 477 CE2PHEA 63 5.626 -6.671 97.112 1.0015.59
ATOM 478 CZ PHE A 63 6.308 -7.84896.824 1.0027.69 ATOM 479 C PHE A 63 2.517 -8.283101.992 1.0025.57
ATOM 480 O PHE A 63 2.693 -9.403102.461 1.0023.67
ATOM 481 N VALA 64 1.824 -7.332102.629 1.0021.33
ATOM 482 CA VALA 64 1.231 -7.610103.940 1.0022.19 ATOM 483 CB VALA 64 0.533 -6.334104.551 1.0022.61
ATOM 484 CGI VAL A 64 -0.298 -6.714105.729 1.0027.13
ATOM 485 CG2VALA 64 1.637 -5.304105.020 1.0021.90
ATOM 486 C VALA 64 0.222 -8.779103.820 1.0023.96
ATOM 487 O VALA 64 0.217 -9.702104.641 1.0022.72 ATOM 488 N GLUA 65 -0.605 -8.750102.786 1.0023.87
ATOM 489 CA GLUA 65 -1.599 -9.805102.552 1.0025.85
ATOM 490 CB GLUA 65 -2.565 -9.384101.447 1.0026.15
ATOM 491 CG GLUA 65 -3.391 -8.151101.878 1.0031.30
ATOM 492 CD GLUA 65 -4.585 -7.855100.962 1.0039.60 ATOM 493 OE1 GLU A 65 -4.550 -8.27299.792 1.0040.00
ATOM 494 OE2 GLU A 65 -5.538 -7.182101.416 1.0037.67
ATOM 495 C GLUA 65 -1.000-11.156102.244 1.0030.49
ATOM 4960 GLUA 65 -1.723-12.145102.087 1.0031.84
ATOM 497 N ARG A 66 0.330-11.208102.181 1.0028.23 ATOM 498 CA ARG A 66 1.033-12.447101.907 1.0025.84
ATOM 499 CB ARG A 66 1.822-12.327100.615 1.0021.79
ATOM 500 CG ARG A 66 0.909-12.27899.428 1.0021.81
ATOM 501 CD ARG A 66 1.630-11.92098.155 1.0019.58
ATOM 502 NE ARG A 66 0.730-12.07397.019 1.0032.78 ATOM 503 CZ ARG A 66 -0.418-11.41396.838 1.0024.91
ATOM 504 NH1ARGA 66 -0.863-10.511 97.723 1.0029.51
ATOM 505 NH2ARGA 66 -1.130-11.65795.751 1.0025.63
ATOM 506 C ARG A 66 1.940 -12.794103.060 1.0026.23
ATOM 507 O ARG A 66 2.889-13.560102.925 1.0022.80 ATOM 508 N GLYA 67 1.655-12.153104.180 1.0023.76
ATOM 509 CA GLY A 67 2.372-12.415105.405 1.0026.92
ATOM 510 C GLY A 67 3.701 -11.708105.633 1.0029.19
ATOM 511 O GLY A 67 4.376-12.028106.597 1.0020.98
ATOM 512 N TYRA 68 4.066-10.737104.794 1.0023.38 ATOM 513 CA TYRA 68 5.335-10.045104.984 1.0023.97
ATOM 514 CB TYRA 68 5.973 -9.754103.640 1.0024.09
ATOM 515 CG TYRA 68 6.378-10.964102.872 1.0028.76
ATOM 516 CD1 TYRA 68 7.496-11.710103.243 1.0031.90 ATOM 517 CE1 TYRA 68 7.828-12.892102.560 1.0033.38
ATOM 518 CD2 TYR A 68 5.604-11.412101.804 1.0028.07
ATOM 519 CE2 TYR A 68 5.919-12.566101.127 1.0032.61
ATOM 520 CZ TYRA 68 7.029-13.309101.506 1.0030.12 ATOM 521 OH TYRA 68 7.314-14.457100.806 1.0033.21
ATOM 522 C TYRA 68 5.172 -8.726105.728 1.0028.95
ATOM 523 O TYRA 68 4.228 -7.973105.506 1.0027.96
ATOM 524 N LYS A 69 6.074 -8.469106.649 1.0026.29
ATOM 525 CA LYS A 69 6.056 -7.191107.344 1.0026.08 ATOM 526 CB LYS A 69 6.583 -7.381108.761 1.0037.70
ATOM 527 CG LYS A 69 6.792 -6.088109.550 1.0035.53
ATOM 528 CD LYS A 69 7.496 -6.409110.865 1.0045.63
ATOM 529 CE LYS A 69 7.818 -5.144111.652 1.0053.04
ATOM 530 NZ LYS A 69 6.604 -4.364111.973 1.0053.36 ATOM 531 C LYS A 69 7.031 -6.288106.547 1.0024.68
ATOM 532 O LYS A 69 8.111 -6.754106.143 1.0019.97
ATOM 533 N ILE A 70 6.645 -5.034106.288 1.0019.04
ATOM 534 CA ILE A 70 7.509 -4.070105.569 1.0020.65
ATOM 535 CB ILE A 70 6.706 -2.867105.076 1.0020.44 ATOM 536 CG2 ILE A 70 7.568 -2.043104.113 1.0016.76
ATOM 537 CGI ILE A 70 5.378 -3.333104.441 1.0023.65
ATOM 538 CD1 ILE A 70 5.493 -4.388103.298 1.0014.39
ATOM 539 C ILE A 70 8.563 -3.546106.568 1.0020.13
ATOM 540 O ILE A 70 8.247 -2.731107.450 1.0026.79 ATOM 541 N LYS A 71 9.800 -3.992106.449 1.0019.99
ATOM 542 CA LYS A 71 10.810 -3.590107.415 1.0021.46
ATOM 543 CB LYS A 71 11.925 -4.641107.454 1.0030.94
ATOM 544 CG LYS A 71 12.861 -4.544108.640 1.0043.19
ATOM 545 CD LYS A 71 12.064 -4.539109.954 1.0049.54 ATOM 546 CE LYS A 71 12.899 -5.024111.142 1.0057.41
ATOM 547 NZ LYS A 71 14.215 -4.335111.291 1.0059.90
ATOM 548 C LYS A 71 11.365 -2.204107.092 1.0019.38
ATOM 5490 LYS A 71 11.914 -1.536107.946 1.0019.32
ATOM 550 N GLY A 72 11.231 -1.790105.845 1.0017.85 ATOM 551 CA GLYA 72 11.675 -0.460105.499 1.0021.32
ATOM 552 C GLYA 72 11.678 -0.198104.020 1.0019.07
ATOM 553 O GLYA 72 11.373 -1.084103.217 1.0020.52
ATOM 554 N SER A 73 11.957 1.052103.655 1.0015.19 ATOM 555 CA SER A 73 12.089 1.414 102.250 1.00 14.55
ATOM 556 CB SER A 73 10.870 2.224 101.750 1.0020.90
ATOM 557 OG SER A 73 10.775 3.460 102.430 1.00 26.87
ATOM 558 C SER A 73 13.341 2.289 102.104 1.00 16.80 ATOM 559 0 SER A 73 13.722 2.991 103.070 1.00 17.98
ATOM 560 N ILE A 74 13.987 2.222 100.938 1.00 14.98
ATOM 561 CA ILE A 74 15.1 18 3.082 100.657 1.00 1 1.26
ATOM 562 CB ILE A 74 16.470 2.300 100.622 1.00 13.82
ATOM 563 CG2 ILE A 74 16.431 1.1 19 99.639 1.00 10.69 ATOM 564 CGI ILE A 74 17.613 3.287 100.400 1.00 14.36
ATOM 565 CD1 ILE A 74 17.889 3.525 98.904 1.00 25.16
ATOM 566 C ILE A 74 14.801 3.800 99.330 1.00 16.93
ATOM 567 O ILE A 74 14.303 3.192 98.367 1.00 20.15
ATOM 568 N SER A 75 15.009 5.1 13 99.298 1.00 15.57 ATOM 569 CA SER A 75 14.745 5.876 98.067 1.00 12.74
ATOM 570 CB SER A 75 14.008 7.168 98.406 1.00 14.08
ATOM 571 OG SER A 75 12.678 6.898 98.917 1.00 15.01
ATOM 572 C SER A 75 16.095 6.184 97.420 1.00 12.34
ATOM 573 0 SER A 75 16.927 6.744 98.063 1.00 14.77 ATOM 574 N SER A 76 16.232 5.912 96.129 1.00 15.1 1
ATOM 575 CA SER A 76 17.492 6.072 95.422 1.00 16.03
ATOM 576 CB SER A 76 17.489 5.186 94.167 1.00 18.91
ATOM 577 OG SER A 76 16.459 5.524 93.281 1.00 16.06
ATOM 578 C SER A 76 17.874 7.491 95.083 1.00 18.60 ATOM 579 0 SER A 76 19.025 7.756 94.794 1.00 14.47
ATOM 580 N HIS A 77 16.894 8.396 95.060 1.00 11.15
ATOM 581 CA HIS A 77 17.202 9.798 94.831 1.00 15.30
ATOM 582 CB HIS A 77 17.676 10.069 93.380 1.00 10.1 1
ATOM 583 CG HIS A 77 16.598 10.065 92.376 1.00 18.97 ATOM 584 CD2 HIS A 77 16.389 10.866 91.307 1.00 20.34
ATOM 585 ND1 HIS A 77 15.649 9.074 92.31 1 1.00 16.26
ATOM 586 CE1 HIS A 77 14.900 9.261 91.242 1.00 30.57
ATOM 587 NE2 HIS A 77 15.333 10.338 90.616 1.00 19.71
ATOM 588 C HIS A 77 15.973 10.61 1 95.213 1.00 20.95 ATOM 589 0 HIS A 77 14.898 10.017 95.497 1.00 15.33
ATOM 590 N PHE A 78 16.120 1 1.937 95.241 1.00 17.93
ATOM 591 CA PHE A 78 15.019 12.781 95.715 1.00 21.89
ATOM 592 CB PHE A 78 15.547 14.148 96.189 1.00 17.77 ATOM 593 CG PHE A 78 15.703 15.188 95.088 1.00 22.33
ATOM 594 CD1 PHE A 78 16.757 15.122 94.155 1.00 17.44
ATOM 595 CD2 PHE A 78 14.792 16.245 94.999 1.00 19.30
ATOM 596 CE1 PHE A 78 16.911 16.083 93.151 1.00 21.94 ATOM 597 CE2 PHE A 78 14.924 17.235 93.986 1.00 19.37
ATOM 598 CZ PHE A 78 15.980 17.154 93.068 1.00 23.45
ATOM 599 C PHE A 78 13.769 13.002 94.865 1.00 18.19
ATOM 600 O PHE A 78 12.742 13.358 95.419 1.00 22.33
ATOM 601 N HIS A 79 13.809 12.786 93.556 1.00 19.59 ATOM 602 CA HIS A 79 12.594 13.034 92.789 1.00 18.09
ATOM 603 CB HIS A 79 12.840 12.806 91.309 1.00 14.91
ATOM 604 CG HIS A 79 13.803 13.799 90.717 1.00 23.65
ATOM 605 CD2 HIS A 79 14.126 15.056 91.097 1.00 12.39
ATOM 606 ND1 HIS A 79 14.484 13.576 89.542 1.00 25.65 ATOM 607 CE1 HIS A 79 15.182 14.652 89.216 1.00 19.58
ATOM 608 NE2 HIS A 79 14.985 '15.566 90.143 1.00 23.82
ATOM 609 C HIS A 79 11.438 12.152 93.306 1.00 21.65
ATOM 610 O HIS A 79 1 1.657 11.055 93.841 1.00 18.21
ATOM 611 N SER A 80 10.218 12.635 93.107 1.00 20.61 ATOM 612 CA SER A 80 9.014 11.964 93.592 1.00 18.21
ATOM 613 CB SER A 80 7.768 12.812 93.207 1.00 13.68
ATOM 614 OG ASER A 80 7.782 13.076 91.822 0.50 16.20
ATOM 3798 OG BSER A 80 7.935 14.128 93.682 0.50 24.09
ATOM 615 C SER A 80 8.840 10.541 93.114 1.00 12.91 ATOM 616 O SER A 80 8.225 9.743 93.805 1.00 21.14
ATOM 617 N ASP A 81 9.333 10.200 91.922 1.00 16.48
ATOM 618 CA ASP A 81 9.146 8.825 91.529 1.00 15.49
ATOM 619 CB ASP A 81 9.449 8.628 90.070 1.00 17.69
ATOM 620 CG ASP A 81 10.893 8.971 89.725 1.00 17.52 ATOM 621 OD1 ASP A 81 1 1.593 9.728 90.422 1.00 17.64
ATOM 622 OD2 ASP A 81 1 1.282 8.474 88.710 1.00 21.62
ATOM 623 C ASP A 81 9.912 7.822 92.387 1.00 18.09
ATOM 624 O ASP A 81 9.661 6.618 92.265 1.00 12.32
ATOM 625 N SER A 82 10.824 8.302 93.246 1.00 19.17 ATOM 626 CA SER A 82 11.542 7.407 94.180 1.0021.25
ATOM 627 CB SER A 82 13.090 7.626 94.146 1.00 14.33
ATOM 628 OG SER A 82 13.630 7.271 92.888 1.00 18.50
ATOM 629 C SER A 82 11.106 7.630 95.620 1.00 18.07 ATOM 630 O SERA 82 11.242 6.72396.472 1.0015.78
ATOM 631 N THRA 83 10.576 8.82795.903 1.0016.48
ATOM 632 CA THRA 83 10.237 9.23297.285 1.0010.86
ATOM 633 CB THRA 83 10.927 10.53797.672 1.0014.59 ATOM 634 OG1 THR A 83 10.532 11.54796.739 1.0013.43
ATOM 635 CG2THRA 83 12.487 10.43297.617 1.0010.91
ATOM 636 C THRA 83 8.724 9.54897.529 1.007.94
ATOM 637 O THRA 83 8.347 9.87698.629 1.0011.64
ATOM 638 N GLYA 84 7.940 9.42396.486 1.0012.08 ATOM 639 CA GLYA 84 6.517 9.71696.514 1.0012.05
ATOM 640 C GLYA 84 5.765 9.00897.616 1.0020.70
ATOM 641 O GLYA 84 4.697 9.45698.009 1.0016.20
ATOM 642 N GLYA 85 6.314 7.88898.072 1.0017.05
ATOM 643 CA GLYA 85 5.697 7.09599.115 1.0012.76 ATOM 644 C GLY A 85 6.196 7.327100.537 1.0021.63
ATOM 645 O GLYA 85 5.602 6.825101.483 1.0018.00
ATOM 646 N ILE A 86 7.251 8.135100.711 1.0015.77
ATOM 647 CA ILE A 86 7.784 8.374102.051 1.0013.19
ATOM 648 CB ILE A 86 9.026 9.263101.975 1.0012.10 ATOM 649 CG2 ILE A 86 9.368 9.868103.365 1.0011.25
ATOM 650 CG1ILEA 86 10.176 8.413101.385 1.0016.21
ATOM 651 CD1 ILE A 86 11.411 9.204101.237 1.0013.41
ATOM 652 C ILE A 86 6.783 8.987103.002 1.0018.35
ATOM 6530 D EA 86 6.676 8.574104.135 1.0013.92 ATOM 654 N GLUA 87 6.001 9.952102.548 1.0017.13
ATOM 655 CA GLUA 87 5.056 10.500103.510 1.0018.17
ATOM 656 CB GLUA 87 4.204 11.628102.867 1.0017.36
ATOM 657 CG GLUA 87 4.834 12.994102.790 1.0031.41
ATOM 658 CD GLUA 87 3.817 14.120102.447 1.0039.91 ATOM 659 OE1 GLUA 87 2.764 14.198103.111 1.0042.75
ATOM 660 OE2 GLU A 87 4.093 14.940101.543 1.0039.48
ATOM 661 C GLUA 87 4.109 9.414104.082 1.0013.04
ATOM 662 O GLUA 87 3.889 9.345105.287 1.0011.57
ATOM 663 N TRPA 88 3.567 8.569103.218 1.0017.07 ATOM 664 CA TRPA 88 2.614 7.536103.662 1.0016.03
ATOM 665 CB TRPA 88 1.983 6.853102.452 1.0015.29
ATOM 666 CG TRPA 88 0.847 5.934102.862 1.0019.50
ATOM 667 CD2 TRP A 88 0.932 4.517103.067 1.0024.71 ATOM 668 CE2 TRP A 88 -0.345 4.071 103.476 1.00 23.00
ATOM 669 CE3 TRP A 88 1.973 3.580 102.949 1.00 23.62
ATOM 670 CD1 TRP A 88 -0.438 6.288 103.148 1.00 20.09
ATOM 671 NE1 TRP A 88 -1.168 5.167 103.516 1.00 23.67 ATOM 672 CZ2 TRP A 88 -0.618 2.710 103.771 1.00 22.61
ATOM 673 CZ3 TRP A 88 1.707 2.231 103.249 1.00 30.53
ATOM 674 CH2 TRP A 88 0.416 1.81 1 103.654 1.00 28.17
ATOM 675 C TRP A 88 3.307 6.507 104.523 1.00 19.07
ATOM 676 0 TRP A 88 2.796 6.094 105.585 1.00 17.48 ATOM 677 N LEU A 89 4.507 6.099 104.098 1.00 19.70
ATOM 678 CA LEU A 89 5.250 5.138 104.896 1.00 18.35
ATOM 679 CB LEU A 89 6.586 4.762 104.203 1.00 16.62
ATOM 680 CG LEU A 89 6.359 4.059 102.851 1.00 22.27
ATOM 681 CD1 LEU A 89 7.701 3.896 102.150 1.00 15.25 ATOM 682 CD2 LEU A 89 5.654 2.663 103.057 1.00 15.27
ATOM 683 C LEU A 89 5.490 5.746 106.270 1.00 13.42
ATOM 684 O LEU A 89 5.270 5.097 107.269 1.00 17.83
ATOM 685 N ASN A 90 5.971 6.984 106.339 1.00 14.90
ATOM 686 CA ASN A 90 6.202 7.550 107.655 1.00 15.98 ATOM 687 CB ASN A 90 6.740 8.965 107.576 1.00 17.44
ATOM 688 CG ASN A 90 8.131 9.052 107.016 1.00 15.53
ATOM 689 OD1 ASN A 90 8.762 8.047 106.704 1.00 14.91
ATOM 690 ND2 ASN A 90 8.615 10.286 106.873 1.00 13.96
ATOM 691 C ASN A 90 4.905 7.609 108.469 1.00 19.44 ATOM 692 0 ASN A 90 4.913 7.442 109.698 1.00 18.51
ATOM 693 N SER A 91 3.784 7.844 107.793 1.00 19.80
ATOM 694 CA SER A 91 2.526 7.959 108.540 1.00 20.86
ATOM 695 CB SER A 91 1.391 8.516 107.660 1.00 15.58
ATOM 696 OG SER A 91 0.822 7.482 106.865 1.00 17.32 ATOM 697 C SER A 91 2.113 6.581 109.075 1.00 26.47
ATOM 698 0 SER A 91 1.346 6.506 1 10.032 1.00 29.1 1
ATOM 699 N ARG A 92 2.605 5.510 108.450 1.00 19.85
ATOM 700 CA ARG A 92 2.307 4.158 108.897 1.00 17.51
ATOM 701 CB ARG A 92 2.187 3.242 107.683 1.00 17.46 ATOM 702 CG ARG A 92 1.105 3.612 106.705 1.00 28.26
ATOM 703 CD ARG A 92 -0.217 3.286 107.335 1.0043.69
ATOM 704 NE ARG A 92 -0.248 1.858 107.658 1.0054.19
ATOM 705 CZ ARG A 92 -1.273 1.242 108.234 1.00 61.90 ATOM 706 NH1 ARG A 92 -2.365 1.934 108.553 1.00 66.79
ATOM 707 NH2 ARG A 92 -1.200 -0.059 108.513 1.00 62.31
ATOM 708 C ARG A 92 3.423 3.637 109.846 1.00 24.69
ATOM 709 O ARG A 92 3.459 2.458 110.200 1.00 27.20 ATOM 710 N SER A 93 4.320 4.518 1 10.265 1.00 26.16
ATOM 711 CA SER A 93 5.432 4.131 1 1 1.128 1.00 25.45
ATOM 712 CB SER A 93 4.922 3.677 1 12.505 1.00 34.85
ATOM 713 OG SER A 93 4.338 4.761 1 13.21 1 1.00 28.54
ATOM 714 C SER A 93 6.310 3.033 1 10.501 1.00 28.50 ATOM 715 0 SER A 93 6.896 2.189 1 1 1.198 1.00 25.77
ATOM 716 N ILE A 94 6.385 3.026 109.176 1.00 19.75
ATOM 717 CA ILE A 94 7.261 2.074 108.496 1.00 22.77
ATOM 718 CB ILE A 94 6.649 1.682 107.155 1.00 18.35
ATOM 719 CG2 ILE A 94 7.651 0.962 106.279 1.00 21.12 ATOM 720 CGI ILE A 94 5.398 0.816 107.446 1.00 23.93
ATOM 721 CD1 ILE A 94 4.476 0.587 106.251 1.00 19.40
ATOM 722 C ILE A 94 8.584 2.815 108.303 1.00 22.31
ATOM 723 O ILE A 94 8.585 3.897 107.729 1.00 15.01
ATOM 724 N PRO A 95 9.724 2.245 108.778 1.00 16.67 ATOM 725 CD PRO A 95 9.924 0.945 109.435 1.00 15.14
ATOM 726 CA PRO A 95 11.014 2.938 108.608 1.00 18.69
ATOM 727 CB PRO A 95 12.051 1.892 109.139 .1.00 13.28
ATOM 728 CG PRO A 95 11.256 1.188 1 10.237 1.00 19.35
ATOM 729 C PRO A 95 1 1.335 3.349 107.165 1.0020.05 ATOM 730 O PRO A 95 1 1.298 2.528 106.239 1.00 15.87
ATOM 731 N THR A 96 1 1.652 4.618 106.952 1.00 17.02
ATOM 732 CA THR A 96 12.068 5.013 105.623 1.00 16.26
ATOM 733 CB THR A 96 11.226 6.200 105.088 1.00 16.88
ATOM 734 OG1 THR A 96 11.262 7.265 106.037 1.00 15.77 ATOM 735 CG2 THR A 96 9.728 5.737 104.872 1.00 9.22
ATOM 736 C THR A 96 13.563 5.406 105.654 1.00 11.90
ATOM 737 0 THR A 96 14.068 5.944 106.655 1.00 15.01
ATOM 738 N TYR A 97 14.230 5.200 104.540 1.00 10.54
ATOM 739 CA TYR A 97 15.657 5.551 104.431 1.00 19.05 ATOM 740 CB TYR A 97 16.543 4.286 104.416 1.00 18.01
ATOM 741 CG TYR A 97 16.422 3.380 105.640 1.00 18.20
ATOM 742 CD1 TYR A 97 15.277 2.627 105.868 1.00 27.80
ATOM 743 CE1 TYR A 97 15.141 1.840 107.034 1.00 28.62 ATOM 744 CD2 TYR A 97 17.444 3.332 106.595 1.00 23.44
ATOM 745 CE2 TYR A 97 17.320 2.555 107.764 1.00 23.79
ATOM 746 CZ TYR A 97 16.167 1.816 107.971 1.00 28.61
ATOM 747 OH TYR A 97 16.030 1.027 109.089 1.00 35.23 ATOM 748 C TYR A 97 15.993 6.343 103.176 1.00 15.77
ATOM 749 O TYR A 97 15.398 6.145 102.104 1.00 15.92
ATOM 750 N ALA A 98 16.958 7.251 103.308 1.00 17.93
ATOM 751 CA ALA A 98 17.494 7.971 102.137 1.00 16.10
ATOM 752 CB ALA A 98 16.571 9.100 101.634 1.00 9.10 ATOM 753 C ALA A 98 18.855 8.553 102.563 1.00 12.89
ATOM 754 O ALA A 98 19.108 8.706 103.749 1.00 16.06
ATOM 755 N SER A 99 19.701 8.868 101.596 1.00 19.16
ATOM 756 CA SER A 99 21.018 9.405 101.949 1.00 22.42
ATOM 757 CB SER A 99 21.909 9.425 100.734 1.00 17.10 ATOM 758 OG SER A 99 21.591 10.490 99.859 1.00 19.50
ATOM 759 C SER A 99 20.896 10.832 102.516 1.00 25.77
ATOM 760 O SER A 99 19.845 1 1.492 102.371 1.00 14.58
ATOM 761 N GLU A 100 21.943 1 1.306 103.186 1.00 16.64
ATOM 762 CA GLU A 100 21.882 12.668 103.720 1.00 21.50 ATOM 763 CB GLU A 100 23.161 13.132 104.450 1.00 22.88
ATOM 764 CG GLU A 100 23.506 12.521 105.734 1.00 37.67
ATOM 765 CD GLU A 100 24.523 13.399 106.474 1.00 35.02
ATOM 766 OE1 GLU A 100 25.355 14.031 105.793 1.00 29.49
ATOM 767 OE2 GLU A 100 24.488 13.444 107.724 1.0049.41 ATOM 768 C GLU A 100 21.692 13.625 102.585 1.00 12.78
ATOM 769 O GLU A 100 20.971 14.607 102.766 1.00 19.34
ATOM 770 N LEU A 101 22.293 13.377 101.402 1.00 15.92
ATOM 771 CA LEU A 101 22.102 14.315 100.285 1.00 15.46
ATOM 772 CB LEU A 101 22.987 14.010 99.048 1.00 15.80 ATOM 773 CG LEU A 101 24.514 14.058 99.245 1.00 20.73
ATOM 774 CD1 LEU A 101 25.188 13.774 97.919 1.0020.94
ATOM 775 CD2 LEU A 101 24.946 15.395 99.818 1.00 20.60
ATOM 776 C LEU A 101 20.651 14.325 99.816 1.00 22.94
ATOM 777 O LEU A 101 20.077 15.376 99.531 1.00 18.26 ATOM 778 N THR A 102 20.062 13.138 99.709 1.00 16.26
ATOM 779 CA THR A 102 18.683 13.070 99.301 1.00 13.28
ATOM 780 CB THR A 102 18.243 11.596 99.181 1.00 15.02
ATOM 781 OG1 THR A 102 19.019 10.967 98.153 1.00 18.24 ATOM 782 CG2THRA102 16.735 11.51398.828 1.0013.43
ATOM 783 C THRA 102 17.763 13.813100.293 1.0015.70
ATOM 784 O THRA 102 16.878 14.56399.882 1.0020.18
ATOM 785 N ASN A 103 17.929 13.582101.587 1.0013.76 ATOM 786 CA ASN A 103 17.080 14.277102.550 1.0015.10
ATOM 787 CB ASN A 103 17.353 13.796103.963 1.0012.69
ATOM 788 CG ASN A 103 16.409 12.684104.384 1.0019.43
ATOM 789 OD1 ASN A 103 15.490 12.361103.658 1.0019.54
ATOM 790 ND2 ASN A 103 16.603 12.139105.574 1.0021.40 ATOM 791 C ASN A 103 17.233 15.781102.522 1.0021.36
ATOM 7920 ASN A 103 16.303 16.526102.817 1.0014.23
ATOM 793 N GLUA 104 18.430 16.243102.184 1.0017.21
ATOM 794 CA GLUA 104 18.654 17.670102.151 1.0021.27
ATOM 795 CB GLUA 104 20.160 17.959102.163 1.0021.08 ATOM 796 CG GLU A 104 20.504 19.428102.288 1.0030.20
ATOM 797 CDAGLUA 104 20.29520.244101.0400.5026.45
ATOM 798 OE1AGLUA 104 20.571 19.75099.9170.5020.57
ATOM 799 OE2AGLU A 104 19.91021.432101.1960.5023.46
ATOM 3799 CD B GLU A 104 19.921 20.088103.5550.5029.24 ATOM 3800 OE1BGLUA 104 19.95021.339103.6400.5038.04
ATOM 3801 OE2BGLUA104 19.457 19.371104.4680.5031.67
ATOM 800 C GLUA 104 17.977 18.243100.937 1.0019.38
ATOM 801 O GLUA 104 17.449 19.368100.989 1.0022.49
ATOM 802 N LEU A 105 17.982 17.501 99.833 1.0012.60 ATOM 803 CA LEU A 105 17.331 17.98498.630 1.0018.10
ATOM 804 CB LEU A 105 17.660 17.10597.432 1.0017.62
ATOM 805 CG LEU A 105 19.129 17.32596.923 1.0020.21
ATOM 806 CD1 LEUA 105 19.610 16.20596.001 1.0022.33
ATOM 807 CD2LEUA 105 19.185 18.68396.211 1.0022.17 ATOM 808 C LEUA 105 15.817 18.00098.888 1.0024.30
ATOM 809 O LEUA 105 15.118 18.90898.445 1.0022.46
ATOM 810 N LEUA 106 15.320 16.97999.584 1.0017.89
ATOM 811 CA LEUA 106 13.898 16.93499.908 1.0023.86
ATOM 812 CB LEU A 106 13.533 15.633100.659 1.0017.99 ATOM 813 CG LEUA 106 13.613 14.32999.837 1.0019.87
ATOM 814 CD1 LEU A 106 13.442 13.103100.749 1.0015.57
ATOM 815 CD2LEUA106 12.559 14.34298.772 1.0012.91
ATOM 816 C LEUA 106 13.540 18.127100.788 1.0025.30 ATOM 817 O LEU A 106 12.472 18.755 100.599 1.00 28.63
ATOM 818 N LYS A 107 14.408 18.426 101.755 1.00 25.44
ATOM 819 CA LYS A 107 14.173 19.530 102.687 1.00 29.90
ATOM 820 CB LYS A 107 15.264 19.558 103.756 1.00 34.79 ATOM 821 CG LYS A 107 15.196 20.720 104.761 1.00 39.26
ATOM 822 CD LYS A 107 16.557 20.842 105.457 1.00 51.37
ATOM 823 CE LYS A 107 16.584 21.908 106.537 1.00 55.67
ATOM 824 NZ LYS A 107 15.809 21.520 107.743 1.00 54.74
ATOM 825 C LYS A 107 14.158 20.846 101.921 1.00 32.97 ATOM 826 0 LYS A 107 13.214 21.652 102.026 1.00 26.75
ATOM 827 N LYS A 108 15.206 21.070 101.141 1.00 27.52
ATOM 828 CA LYS A 108 15.273 22.284 100.345 1.00 31.83
ATOM 829 CB LYS A 108 16.457 22.236 99.390 1.00 32.53
ATOM 830 CG LYS A 108 16.281 23.034 98.121 1.0042.12 ATOM 831 CD LYS A 108 17.331 22.649 97.053 1.0049.42
ATOM 832 CE LYS A 108 17.235 21.148 96.674 1.00 57.56
ATOM 833 NZ LYS A 108 15.876 20.596 96.247 1.00 27.69
ATOM 834 C LYS A 108 14.000 22.384 99.530 1.00 34.09
ATOM 835 O LYS A 108 13.490 23.477 99.296 1.00 33.33 ATOM 836 N ASP A 109 13.493 21.234 99.095 1.00 32.04
ATOM 837 CA ASP A 109 12.299 21.196 98.260 1.00 30.03
ATOM 838 CB ASP A 109 12.368 19.939 97.404 1.00 37.27
ATOM 839 CG ASP A 109 12.332 20.231 95.942 1.00 50.80
ATOM 840 OD1 ASP A 109 13.208 20.997 95.484 1.00 58.35 ATOM 841 OD2 ASP A 109 11.435 19.681 95.251 1.00 56.78
ATOM 842 C ASP A 109 10.937 21.248 99.018 1.00 24.55
ATOM 843 O ASP A 109 9.898 21.136 98.404 1.00 29.76
ATOM 844 N GLY A 1 10 10.941 21.417 100.333 1.00 26.08
ATOM 845 CA GLY A 1 10 9.682 21.433 101.068 1.00 28.75 ATOM 846 C GLY A 110 8.950 20.086 101.026 1.0025.78
ATOM 847 0 GLY A 110 7.715 20.055 101.089 1.00 25.46
ATOM 848 N LYS A 1 11 9.698 18.973 100.912 1.00 22.73
ATOM 849 CA LYS A 111 9.115 17.627 100.890 1.00 19.02
ATOM 850 CB LYS A 11 1 9.642 16.778 99.737 1.00 19.03 ATOM 851 CG LYS A 1 1 1 9.464 17.361 98.353 1.00 26.72
ATOM 852 CD LYS A 1 1 1 7.982 17.460 98.003 1.00 28.71
ATOM 853 CE LYS A 1 11 7.804 17.923 96.551 1.00 33.06
ATOM 854 NZ LYS A 1 11 8.491 16.980 95.608 1.00 46.40 ATOM 855 C LYS A 111 9.428 16.910102.196 1.0019.32
ATOM 856 O LYS A 111 10.368 17.258102.907 1.0025.10
ATOM 857 N VAL A 112 8.639 15.889102.512 1.0019.42
ATOM 858 CA VALA 112 8.842 15.174103.750 1.0016.33 ATOM 859 CB VAL A 112 7.567 14.322104.069 1.0021.55
ATOM 860 CGI VALA 112 7.869 13.260105.137 1.0020.07
ATOM 861 CG2VALA112 6.464 15.283104.607 1.0019.08
ATOM 862 C VALA 112 10.127 14.329103.577 1.0014.13
ATOM 863 O VALA 112 10.379 13.791102.510 1.0020.47 ATOM 864 N GLN A 113 10.952 14.289104.602 1.0018.58
ATOM 865 CA GLN A 113 12.214 13.524104.540 1.0018.25
ATOM 866 CB GLNA113 13.233 14.232105.401 1.0022.55
ATOM 867 CG GLN A 113 13.494 15.643104.917 1.0028.10
ATOM 868 CD GLNA113 14.281 16.450105.918 1.0032.04 ATOM 869 OE1GLNA113 13.866 17.550106.321 1.0029.36
ATOM 870 NE2GLNA 113 15.416 15.914106.339 1.0024.40
ATOM 871 C GLN A 113 12.103 12.077105.043 1.0017.42
ATOM 872 O GLNA113 11.176 11.744105.781 1.0015.93
ATOM 873 N ALA A 114 13.081 11.252104.669 1.0016.03 ATOM 874 CA ALA A 114 13.161 9.870105.147 1.0017.61
ATOM 875 CB ALA A 114 14.405 9.150104.548 1.0012.13
ATOM 876 C ALAA114 13.409 10.055106.621 1.0018.38
ATOM 877 O ALA A 114 14.040 11.035107.015 1.0019.41
ATOM 878 N THRA 115 12.989 9.085107.413 1.0016.00 ATOM 879 CA THR A 115 13.194 9.120108.842 1.0021.91
ATOM 880 CB THR A 115 12.306 8.063109.489 1.0018.77
ATOM 881 OG1 THRA 115 10.955 8.351109.132 1.0029.48
ATOM 882 CG2 THR A 115 12.444 8.091111.021 1.0029.53
ATOM 883 C THRA 115 14.659 8.787109.172 1.0023.97 ATOM 884 O THRA 115 15.192 9.233110.176 1.0021.82
ATOM 885 N ASN A 116 15.327 8.030108.305 1.0019.29
ATOM 886 CA ASN A 116 16.702 7.619108.606 1.0020.70
ATOM 887 CB ASNA116 16.715 6.102108.808 1.0020.25
ATOM 888 CG ASN A 116 15.793 5.668109.945 1.0028.94 ATOM 889 OD1 ASNA116 16.152 5.777111.118 1.0032.39
ATOM 890 ND2ASNA116 14.583 5.205109.600 1.0021.32
ATOM 891 C ASN A 116 17.592 7.967107.463 1.0022.84
ATOM 892 O ASN A 116 17.195 7.786106.324 1.0019.24 ATOM 893 N SERA 117 18.801 8.458107.747 1.0020.03
ATOM 894 CA SER A 117 19.701 8.784106.664 1.0020.51
ATOM 895 CB SERA 117 19.902 10.291106.558 1.0021.72
ATOM 896 OG SERA 117 20.511 10.756107.735 1.0035.45 ATOM 897 C SERA 117 21.059 8.097106.843 1.0020.01
ATOM 8980 SERA 117 21.365 7.509107.889 1.0020.75
ATOM 899 N PHEA 118 21.854 8.203105.792 1.0025.06
ATOM 900 CA PHE A 118 23.167 7.600105.741 1.0027.32
ATOM 901 CB PHE A 118 23.030 6.118105.296 1.0021.67 ATOM 902 CG PHE A 118 22.372 5.949103.953 1.0027.18
ATOM 903 CD1 PHEA 118 23.100 6.096102.773 1.0025.82
ATOM 904 CD2 PHE A 118 20.990 5.698103.863 1.0021.17
ATOM 905 CE1 PHEA 118 22.481 6.003101.510 1.0018.80
ATOM 906 CE2 PHE A 118 20.354 5.600102.597 1.0022.74 ATOM 907 CZ PHEA 118 21.097 5.752101.422 1.0018.97
ATOM 908 C PHEA 118 24.002 8.367104.738 1.0021.01
ATOM 909 O PHEA 118 23.495 9.094103.882 1.0021.06
ATOM 910 N SERA 119 25.310 8.215104.836 1.0026.24
ATOM 911 CA SERA 119 26.199 8.857103.888 1.0027.22 ATOM 912 CB SERA 119 26.730 10.193104.451 1.0023.42
ATOM 913 OG SERA 119 27.282 10.010105.732 1.0027.92
ATOM 914 C SERA 119 27.347 7.893103.598 1.0027.82
ATOM 9150 SERA 119 27.365 6.788104.099 1.0031.00
ATOM 916 N GLYA 120 28.294 8.320102.788 1.0028.89 ATOM 917 CA GLYA 120 29.407 7.462102.452 1.0027.31
ATOM 918 C GLYA 120 29.194 6.877101.064 1.0032.25
ATOM 9190 GLYA 120 28.122 7.025100.417 1.0026.67
ATOM 920 N VALA 121 30.237 6.207100.605 1.0027.08
ATOM 921 CA VALA 121 30.242 5.56299.326 1.0026.44 ATOM 922 CB VALA 121 31.676 5.19298.914 1.0031.06
ATOM 923 CGI VAL A 121 31.655 4.32997.667 1.0029.50
ATOM 924 CG2 VAL A 121 32.474 6.46498.665 1.0033.04
ATOM 925 C VALA 121 29.388 4.301 99.439 1.0025.72
ATOM 9260 VALA 121 28.618 4.00698.526 1.0029.30 ATOM 927 N ASN A 122 29.500 3.582100.557 1.0022.95
ATOM 928 CA ASN A 122 28.699 2.366100.729 1.0027.01
ATOM 929 CB ASN A 122 29.485 1.065100.577 1.0033.95
ATOM 930 CG ASNA122 30.892 1.283100.208 1.0045.35 ATOM 931 OD1 ASN A 122 31.678 1.815 101.007 1.00 44.70
ATOM 932 ND2 ASN A 122 31.249 0.888 98.980 1.0040.54
ATOM 933 C ASN A 122 28.054 2.331 102.035 1.00 30.41
ATOM 934 0 ASN A 122 28.598 2.786 103.042 1.00 33.18 ATOM 935 N TYR A 123 26.869 1.758 102.022 1.00 26.12
ATOM 936 CA TYR A 123 26.093 1.667 103.207 1.00 25.64
ATOM 937 CB TYR A 123 25.179 2.887 103.269 1.00 22.87
ATOM 938 CG TYR A 123 24.226 2.792 104.380 1.00 24.22
ATOM 939 CD1 TYR A 123 24.673 2.893 105.693 1.00 25.90 ATOM 940 CE1 TYR A 123 23.802 2.760 106.737 1.00 24.27
ATOM 941 CD2 TYR A 123 22.869 2.548 104.139 1.00 24.33
ATOM 942 CE2 TYR A 123 21.989 2.406 105.178 1.00 26.89
ATOM 943 CZ TYR A 123 22.459 2.515 106.475 1.00 27.74
ATOM 944 OH TYR A 123 21.602 2.390 107.530 1.00 27.27 ATOM 945 C TYR A 123 25.255 0.381 103.169 1.00 26.42
ATOM 946 0 TYR A 123 24.534 0.113 102.190 1.00 21.88
ATOM 947 N TRP A 124 25.341 -0.426 104.219 1.00 21.67
ATOM 948 CA TRP A 124 24.513 -1.622 104.238 1.00 24.70
ATOM 949 CB TRP A 124 25.132 -2.746 105.076 1.00 28.22 ATOM 950 CG TRP A 124 26.325 -3.366 104.428 1.00 37.50
ATOM 951 CD2 TRP A 124 26.327 -4.305 103.330 1.00 33.30
ATOM 952 CE2 TRP A 124 27.674 -4.514 102.965 1.00 37.71
ATOM 953 CE3 TRP A 124 25.324 -4.987 102.625 1.00 25.52
ATOM 954 CD1 TRP A 124 27.620 -3.064 104.675 1.00 39.02 ATOM 955 NE1 TRP A 124 28.440 -3.745 103.800 1.0046.38
ATOM 956 CZ2 TRP A 124 28.054 -5.373 101.918 1.00 33.89
ATOM 957 CZ3 TRP A 124 25.696 -5.841 101.585 1.00 32.41
ATOM 958 CH2 TRP A 124 27.061 -6.025 101.239 1.00 32.35
ATOM 959 C TRP A 124 23.153 -1.330 104.809 1.00 28.28 ATOM 960 O TRP A 124 23.044 -1.019 105.998 1.00 29.65
ATOM 961 N LEU A 125 22.103 -1.416 103.991 1.00 23.07
ATOM 962 CA LEU A 125 20.778 -1.224 104.552 1.00 26.74
ATOM 963 CB LEU A 125 19.739 -1.145 103.438 1.00 22.86
ATOM 964 CG LEU A 125 18.267 -1.105 103.828 1.00 28.00 ATOM 965 CD1 LEU A 125 17.993 0.089 104.740 1.00 26.72
ATOM 966 CD2 LEU A 125 17.472 -1.017 102.539 1.00 25.06
ATOM 967 C LEU A 125 20.579 -2.488 105.422 1.00 26.95
ATOM 968 O LEU A 125 20.153 -2.397 106.565 1.00 29.70 ATOM 969 N VALA 126 20.894 -3.664104.865 1.0021.92
ATOM 970 CA VALA 126 20.831 -4.932105.604 1.0024.04
ATOM 971 CB VAL A 126 19.738 -5.869105.046 1.0026.39
ATOM 972 CGI VALA 126 19.681 -7.204105.882 1.0030.98 ATOM 973 CG2 VALA 126 18.377 -5.148105.102 1.0026.79
ATOM 974 C VAL A 126 22.239 -5.563105.430 1.0021.80
ATOM 975 O VALA 126 22.675 -5.849104.311 1.0023.04
ATOM 976 N LYS A 127 22.959 -5.754106.528 1.0023.69
ATOM 977 CA LYS A 127 24.318 -6.294106.398 1.0027.06 ATOM 978 CB LYS A 127 24.910 -6.623107.780 1.0037.05
ATOM 979 CG LYS A 127 23.871 -6.878108.847 1.0053.02
ATOM 980 CD LYS A 127 24.459 -7.477110.140 1.0062.46
ATOM 981 CE LYS A 127 23.410 -7.501111.271 1.0067.79
ATOM 982 NZ LYS A 127 22.102 -8.095110.849 1.0067.57 ATOM 983 C LYS A 127 24.411 -7.511105.481 1.0023.41
ATOM 984 O LYS A 127 23.646 -8.478105.617 1.0022.10
ATOM 985 N ASN A 128 25.310 -7.402104.509 1.0023.73
ATOM 986 CA ASN A 128 25.606 -8.433103.524 1.0027.01
ATOM 987 CB ASN A 128 26.257 -9.639104.216 1.0036.68 ATOM 988 CG ASN A 128 27.685 -9.340104.696 1.0034.75
ATOM 989 OD1 ASN A 128 27.963 -9.350105.892 1.0040.12
ATOM 990 ND2ASNA 128 28.588 -9.074103.749 1.0036.51
ATOM 991 C ASN A 128 24.467 -8.903102.663 1.0028.84
ATOM 992 O ASN A 128 24.597 -9.924101.974 1.0027.20 ATOM 993 N LYS A 129 23.348 -8.170102.672 1.0026.51
ATOM 994 CA LYS A 129 22.230 -8.576101.828 1.0023.14
ATOM 995 CB LYS A 129 21.146 -9.210102.710 1.0026.47
ATOM 996 CG LYS A 129 21.648-10.508103.394 1.0025.74
ATOM 997 CD LYS A 129 20.494-11.251104.060 1.0032.09 ATOM 998 CE LYS A 129 20.989-12.534104.780 1.0028.74
ATOM 999 NZ LYS A 129 19.847-13.023105.599 1.0028.32
ATOM 1000 C LYS A 129 21.649 -7.460100.963 1.0025.54
ATOM 1001 O LYS A 129 21.203 -7.71699.846 1.0022.82
ATOM 1002 N ILEA130 21.633 -6.228101.488 1.0022.68 ATOM 1003 CA ILE A 130 21.149 -5.071100.719 1.0019.01
ATOM 1004 CB ILE A 130 19.752 -4.599101.138 1.0021.43
ATOM 1005 CG2ILEA130 19.303 -3.471100.172 1.0023.60
ATOM 1006 CGI ILE A 130 18.757 -5.758101.083 1.0019.13 ATOM 1007 CD 1 ILE A 130 17.280 -5.352101.361 1.0021.50
ATOM 1008 C ILE A 130 22.118 -3.922100.978 1.0015.85
ATOM 1009 O ILEA130 22.151 -3.367102.084 1.0020.58
ATOM 1010 N GLUA 131 22.900 -3.60099.957 1.0017.70 ATOM 1011 CA GLU A 131 23.899 -2.552100.012 1.0020.03
ATOM 1012 CB GLUA 131 25.232 -3.10299.513 1.0019.43
ATOM 1013 CG GLUA 131 26.257 -2.01799.221 1.0025.22
ATOM 1014 CD GLUA 131 27.625 -2.56698.751 1.0038.83
ATOM 1015 OE1GLUA131 27.772 -3.05497.576 1.0028.33 ATOM 1016 OE2 GLU A 131 28.551 -2.49599.592 1.0041.65
ATOM 1017 C GLUA 131 23.495 -1.33499.162 1.0022.65
ATOM 1018 O GLUA 131 22.907 -1.47898.093 1.0017.22
ATOM 1019 N VALA 132 23.824 -0.14699.652 1.0016.35
ATOM 1020 CA VAL A 132 23.535 1.121 98.943 1.0014.03 ATOM 1021 CB VAL A 132 22.814 2.10899.918 1.0012.60
ATOM 1022 CGI VAL A 132 22.532 3.42399.200 1.0018.11
ATOM 1023 CG2 VAL A 132 21.485 1.457100.418 1.0013.56
ATOM 1024 C VALA 132 24.889 1.70698.524 1.0016.40
ATOM 1025 O VALA 132 25.764 1.82599.353 1.0025.34 ATOM 1026 N PHEA 133 25.053 2.07097.260 1.0016.70
ATOM 1027 CA PHEA 133 26.309 2.601 96.764 1.0019.33
ATOM 1028 CB PHEA 133 26.889 1.62395.744 1.0015.27
ATOM 1029 CG PHEA 133 28.141 2.07995.116 1.0019.47
ATOM 1030 CD1 PHEA 133 29.349 2.08995.842 1.0019.76 ATOM 1031 CD2PHEA133 28.143 2.50293.801 1.0016.17
ATOM 1032 CE1 PHE A 133 30.527 2.51395.237 1.0024.32
ATOM 1033 CE2 PHE A 133 29.333 2.92893.197 1.0022.70
ATOM 1034 CZ PHE A 133 30.519 2.92893.926 1.0017.27
ATOM 1035 C PHEA 133 26.074 3.93896.080 1.0021.02 ATOM 1036 O PHEA 133 25.144 4.08095.2561.0017.66
ATOM 1037 N TYRA 134 26.920 4.91796.414 1.0018.69
ATOM 1038 CA TYRA 134 26.826 6.25395.804 1.0019.83
ATOM 1039 CB TYR A 134 26.979 7.32696.900 1.0019.45
ATOM 1040 CG TYR A 134 27.029 8.75796.387 1.0020.78 ATOM 1041 CD1TYRA134 25.967 9.27595.655 1.0020.93
ATOM 1042 CE1 TYRA 134 25.976 10.58895.182 1.0024.55
ATOM 1043 CD2TYRA134 28.145 9.60796.656 1.0023.63
ATOM 1044 CE2 TYR A 134 28.165 10.95496.187 1.0018.92 ATOM 1045 CZ TYR A 134 27.062 1 1.422 95.442 1.00 24.33
ATOM 1046 OH TYR A 134 26.997 12.686 94.912 1.00 19.99
ATOM 1047 C TYR A 134 27.949 6.372 94.771 1.00 22.96
ATOM 1048 O TYR A 134 29.127 6.464 95.132 1.00 25.17 ATOM 1049 N PRO A 135 27.613 6.355 93.474 1.0022.23
ATOM 1050 CD PRO A 135 26.278 6.222 92.842 1.00 24.19
ATOM 1051 CA PRO A 135 28.674 6.464 92.470 1.00 21.73
ATOM 1052 CB PRO A 135 28.018 5.894 91.202 1.00 19.07
ATOM 1053 CG PRO A 135 26.549 6.493 91.351 1.00 20.91 ATOM 1054 C PRO A 135 29.1 16 7.893 92.247 1.00 23.01
ATOM 1055 O PRO A 135 30.154 8.127 91.635 1.00 21.89
ATOM 1056 N GLY A 136 28.332 8.836 92.763 1.00 20.98
ATOM 1057 CA GLY A 136 28.608 10.249 92.561 1.00 22.28
ATOM 1058 C GLY A 136 27.482 10.905 91.743 1.00 24.79 ATOM 1059 O GLY A 136 26.587 10.188 91.251 1.00 21.56
ATOM 1060 N PRO A 137 27.499 12.246 91.552 1.00 21.78
ATOM 1061 CD PRO A 137 28.510 13.215 92.012 1.00 21.41
ATOM 1062 CA PRO A 137 26.455 12.948 90.782 1.00 21.48
ATOM 1063 CB PRO A 137 26.939 14.416 90.783 1.00 23.20 ATOM 1064 CG PRO A 137 27.683 14.543 92.081 1.00 18.46
ATOM 1065 C PRO A 137 26.292 12.433 89.357 1.00 19.91
ATOM 1066 O PRO A 137 27.260 12.025 88.684 1.00 21.81
ATOM 1067 N GLY A 138 25.040 12.443 88.895 1.00 24.51
ATOM 1068 CA GLY A 138 24.744 12.027 87.536 1.00 19.87 ATOM 1069 C GLY A 138 23.369 12.597 87.185 1.00 19.81
ATOM 1070 O GLY A 138 23.192 13.806 87.040 1.00 24.64
ATOM 1071 N HIS A 139 22.403 1 1.701 87.051 1.00 19.69
ATOM 1072 CA HIS A 139 21.006 12.084 86.782 1.00 22.29
ATOM 1073 CB HIS A 139 20.131 10.857 87.000 1.00 21.50 ATOM 1074 CG HIS A 139 18.687 11.175 87.055 1.0022.97
ATOM 1075 CD2 HIS A 139 17.807 11.147 88.080 1.00 18.75
ATOM 1076 ND1 HIS A 139 18.011 11.683 85.971 1.00 22.02
ATOM 1077 CE1 HIS A 139 16.773 11.962 86.327 1.00 24.75
ATOM 1078 NE2 HIS A 139 16.627 1 1.644 87.599 1.00 16.63 ATOM 1079 C HIS A 139 20.624 13.207 87.765 1.00 19.95
ATOM 1080 O HIS A 139 19.994 14.213 87.391 1.00 22.37
ATOM 1081 N THR A 140 20.978 13.012 89.041 1.00 20.77
ATOM 1082 CA THR A 140 20.783 14.031 90.075 1.00 17.86 ATOM 1083 CB THRA 140 19.558 13.74590.987 1.0024.36
ATOM 1084 OG1THRA140 19.665 12.42391.526 1.0021.78
ATOM 1085 CG2THRA140 18.220 13.94390.179 1.0016.34
ATOM 1086 C THR A 140 22.049 14.06890.917 1.0022.88 ATOM 1087 O THRA 140 22.924 13.21690.749 1.0018.09
ATOM 1088 N PROA 141 22.169 15.04691.841 1.0024.65
ATOM 1089 CD PROA 141 21.206 16.11292.174 1.0021.10
ATOM 1090 CA PROA 141 23.351 15.181 92.697 1.0023.71
ATOM 1091 CB PROA 141 23.088 16.50793.433 1.0021.28 ATOM 1092 CG PROA 141 22.128 17.26692.450 1.0022.00
ATOM 1093 C PROA 141 23.521 14.071 93.707 1.0028.62
ATOM 1094 O PRO A 141 24.645 13.74594.086 1.0018.32
ATOM 1095 N ASP A 142 22.387 13.48794.109 1.0019.04
ATOM 1096 CA ASPA 142 22.305 12.49595.172 1.0016.90 ATOM 1097 CB ASPA 142 21.104 12.89696.084 1.0013.09
ATOM 1098 CG ASPA 142 19.779 12.881 95.302 1.0015.48
ATOM 1099 OD1 ASPA 142 19.791 13.23694.092 1.0018.13
ATOM 1100 OD2 ASP A 142 18.707 12.54595.875 1.0021.62
ATOM 1101 C ASP A 142 22.085 11.03794.740 1.0016.47 ATOM 1102 O ASP A 142 22.057 10.14695.607 1.0017.64
ATOM 1103 N ASN A 143 21.956 10.76293.450 1.0016.79
ATOM 1104 CA ASN A 143 21.599 9.40693.120 1.0017.21
ATOM 1105 CB ASN A 143 21.301 9.27891.620 1.0017.51
ATOM 1106 CG ASN A 143 22.447 9.771 90.716 1.0026.43 ATOM 1107 OD1 ASN A 143 22.231 10.125 89.546 1.0019.43
ATOM 1108 ND2 ASN A 143 23.657 9.76391.243 1.0019.16
ATOM 1109 C ASN A 143 22.500 8.281 93.615 1.0019.15
ATOM 1110 O ASNA143 23.746 8.33593.481 1.0016.12
ATOM 1111 N VAL A 144 21.846 7.27694.208 1.0014.65 ATOM 1112 CA VALA 144 22.523 6.07894.684 1.0011.76
ATOM 1113 CB VAL A 144 22.453 5.90796.241 1.008.82
ATOM 1114 CGI VALA 144 22.981 7.17496.989 1.0012.41
ATOM 1115 CG2 VAL A 144 21.013 5.57096.675 1.0013.10
ATOM 1116 C VAL A 144 21.890 4.82894.032 1.0014.33 ATOM 11170 VAL A 144 20.783 4.87493.467 1.0016.43
ATOM 1118 N VALA 145 22.604 3.69994.085 1.0017.42
ATOM 1119 CA VALA 145 22.087 2.451 93.541 1.0015.80
ATOM 1120 CB VALA 145 23.003 1.89492.404 1.0020.01 ATOM 1121 CGI VALA 145 23.056 2.87891.254 1.0016.88
ATOM 1122 CG2 VAL A 145 24.397 1.61092.973 1.0015.94
ATOM 1123 C VALA 145 22.003 1.42894.686 1.0017.46
ATOM 1124 O VAL A 145 22.619 1.62895.746 1.0014.83 ATOM 1125 N VAL A 146 21.277 0.32394.454 1.0013.67
ATOM 1126 CA VALA 146 21.102 -0.68895.481 1.0016.35
ATOM 1127 CB VAL A 146 19.612 -0.731 95.944 1.0019.72
ATOM 1128 CGI VALA 146 19.341 -1.88896.883 1.0016.06
ATOM 1129 CG2 VAL A 146 19.264 0.53396.644 1.0018.44 ATOM 1130 C VALA 146 21.573 -2.02394.871 1.0020.10
ATOM 1131 O VAL A 146 21.192 -2.39093.765 1.0013.04
ATOM 1132 N TRPA 147 22.432 -2.73495.601 1.0016.70
ATOM 1133 CA TRPA 147 23.002 -3.99795.124 1.0015.48
ATOM 1134 CB TRPA 147 24.532 -3.83495.097 1.0015.80 ATOM 1135 CG TRPA 147 25.325 -5.13894.932 1.0020.97
ATOM 1136 CD2 TRP A 147 25.441 -5.91593.739 1.0019.14
ATOM 1137 CE2TRPA147 26.347 -6.98194.007 1.0023.28
ATOM 1138 CE3TRPA147 24.870 -5.81892.464 1.0018.66
ATOM 1139 CD1TRPA 147 26.136 -5.74495.870 1.0023.58 ATOM 1140 NE1 TRPA 147 26.759 -6.85995.308 1.0019.83
ATOM 1141 CZ2TRPA147 26.695 -7.94393.033 1.0028.22
ATOM 1142 CZ3TRPA147 25.222 -6.78391.480 1.0025.89
ATOM 1143 CH2TRPA147 26.123 -7.82591.776 1.0027.73
ATOM 1144 C TRPA 147 22.568 -5.13996.055 1.0015.25 ATOM 1145 O TRPA 147 22.573 -4.99697.308 1.0018.89
ATOM 1146 N LEUA 148 22.185 -6.26695.454 1.0011.67
ATOM 1147 CA LEU A 148 21.741 -7.431 96.202 1.0013.55
ATOM 1148 CB LEUA 148 20.380 -7.88295.656 1.0017.55
ATOM 1149 CG LEUA 148 19.339 -6.78295.644 1.0018.14 ATOM 1150 CD1 LEUA 148 18.046 -7.371 95.157 1.0021.36
ATOM 1151 CD2LEUA148 19.167 -6.18997.035 1.0017.69
ATOM 1152 C LEU A 148 22.803 -8.48295.896 1.0018.92
ATOM 1153 O LEU A 148 22.794 -9.09394.822 1.0021.41
ATOM 1154 N PRO A 149 23.698 -8.741 96.848 1.0016.74 ATOM 1155 CD PROA 149 23.748 -8.23298.230 1.0017.57
ATOM 1156 CA PROA 149 24.783 -9.72096.616 1.0020.21
ATOM 1157 CB PRO A 149 25.554 -9.70697.942 1.0022.54
ATOM 1158 CG PROA 149 25.254 -8.32098.494 1.0022.36 ATOM 1159 C PRO A 149 24.446-11.14396.206 1.0022.38
ATOM 1160 O PRO A 149 25.100-11.67295.320 1.0026.79
ATOM 1161 N GLUA 150 23.458-11.77796.838 1.0025.06
ATOM 1162 CA GLUA 150 23.157-13.16096.505 1.0027.15 ATOM 1163 CB GLUA 150 21.999-13.69697.324 1.0032.67
ATOM 1164 CG GLUA 150 21.643-15.15396.913 1.0032.61
ATOM 1165 CD GLU A 150 20.574-15.80597.793 1.0033.03
ATOM 1166 OE1 GLU A 150 20.106-15.17498.767 1.0032.28
ATOM 1167 OE2 GLU A 150 20.208-16.96997.504 1.0037.31 ATOM 1168 C GLUA 150 22.844-13.37995.037 1.0033.75
ATOM 1169 O GLU A 150 23.505-14.16494.347 1.0030.53
ATOM 1170 N ARGA151 21.835-12.66994.556 1.0032.62
ATOM 1171 CA ARG A 151 21.412-12.81593.183 1.0029.16
ATOM 1172 CB ARG A 151 19.921-12.521 93.076 1.0028.28 ATOM 1173 CG ARGA 151 19.056-13.58293.682 1.0042.13
ATOM 1174 CD ARGA 151 19.050-14.74292.714 1.0049.78
ATOM 1175 NE ARGA 151 19.063-16.02893.375 1.0052.52
ATOM 1176 CZ ARGA 151 19.186-17.16992.711 1.0057.82
ATOM 1177 NH1 ARGA 151 19.299-17.141 91.389 1.0059.55 ATOM 1178 NH2 ARG A 151 19.210-18.32293.361 1.0053.03
ATOM 1179 C ARGA 151 22.177-11.96092.206 1.0026.61
ATOM 1180 O ARGA 151 21.959-12.05590.998 1.0023.09
ATOM 1181 N LYS A 152 23.077-11.12792.707 1.0024.45
ATOM 1182 CA LYS A 152 23.865-10.28091.807 1.0025.50 ATOM 1183 CB LYS A 152 24.622-11.15390.798 1.0029.45
ATOM 1184 CG LYS A 152 25.438-12.28291.456 1.0030.91
ATOM 1185 CD LYS A 152 26.684-11.73092.137 1.0033.05
ATOM 1186 CE LYS A 152 27.553-12.831 92.824 1.0036.07
ATOM 1187 NZ LYS A 152 26.826-13.58093.908 1.0034.11 ATOM 1188 C LYS A 152 22.928 -9.31291.067 1.0024.59
ATOM 1189 O LYS A 152 23.089 -9.09389.863 1.0024.92
ATOM 1190 N ILE A 153 21.918 -8.78391.769 1.0022.71
ATOM 1191 CA ILE A 153 20.994 -7.831 91.133 1.0019.25
ATOM 1192 CB ILEA153 19.521 -8.12691.485 1.0020.34 ATOM 1193 CG2 ILE A 153 18.613 -6.98991.005 1.0017.50
ATOM 1194 CGI ILE A 153 19.121 -9.49890.899 1.0027.41
ATOM 1195 CD1ILEA153 17.832-10.05991.492 1.0026.52
ATOM 1196 C ILEA153 21.320 -6.41591.574 1.0014.93 ATOM 1197 O ILE A 153 21.474 -6.158 92.776 1.00 15.59
ATOM 1198 N LEU A 154 21.473 -5.532 90.590 1.00 14.30
ATOM 1 199 CA LEU A 154 21.752 -4.096 90.822 1.00 18.77
ATOM 1200 CB LEU A 154 22.930 -3.608 89.970 1.00 20.84 ATOM 1201 CG LEU A 154 23.319 -2.123 90.170 1.00 17.98
ATOM 1202 CD1 LEU A 154 24.008 -1.912 91.540 1.00 18.67
ATOM 1203 CD2 LEU A 154 24.191 -1.639 89.034 1.00 21.06
ATOM 1204 C LEU A 154 20.530 -3.224 90.462 1.00 19.34
ATOM 1205 O LEU A 154 20.047 -3.234 89.325 1.00 18.36 ATOM 1206 N PHE A 155 19.980 -2.508 91.427 1.00 20.36
ATOM 1207 CA PHE A 155 18.911 -1.592 91.056 1.00 15.08
ATOM 1208 CB PHE A 155 17.890 -1.425 92.187 1.00 15.15
ATOM 1209 CG PHE A 155 16.877 -0.373 91.888 1.00 16.16
ATOM 1210 CD1 PHE A 155 15.870 -0.617 90.941 1.00 14.91 ATOM 121 1 CD2 PHE A 155 16.960 0.899 92.504 1.00 17.55
ATOM 1212 CE1 PHE A 155 14.958 0.388 90.599 1.00 22.09
ATOM 1213 CE2 PHE A 155 16.044 1.924 92.156 1.00 17.54
ATOM 1214 CZ PHE A 155 15.046 1.664 91.203 1.00 20.08
ATOM 1215 C PHE A 155 19.580 -0.253 90.793 1.00 15.17 ATOM 1216 O PHE A 155 19.965 0.429 91.736 1.00 15.53
ATOM 1217 N GLY A 156 19.684 0.134 89.523 1.00 19.62
ATOM 1218 CA GLY A 156 20.333 1.380 89.155 1.00 20.40
ATOM 1219 C GLY A 156 19.503 2.647 89.216 1.00 23.30
ATOM 1220 O GLY A 156 20.033 3.736 89.085 1.00 18.07 ATOM 1221 N GLY A 157 18.200 2.523 89.413 1.00 21.76
ATOM 1222 CA GLY A 157 17.384 3.726 89.485 1.00 20.85
ATOM 1223 C GLY A 157 17.422 4.622 88.243 1.00 20.26
ATOM 1224 O GLY A 157 17.562 4.150 87.108 1.00 19.20
ATOM 1225 N CYS A 158 17.333 5.925 88.463 1.00 21.09 ATOM 1226 CA CYS A 158 17.264 6.848 87.335 1.00 21.61
ATOM 1227 CB CYS A 158 16.431 8.065 87.752 1.00 19.04
ATOM 1228 SG CYS A 158 14.835 7.504 88.560 1.0021.53
ATOM 1229 C CYS A 158 18.645 7.233 86.815 1.00 24.12
ATOM 1230 O CYS A 158 18.759 8.045 85.905 1.00 23.91 ATOM 1231 N PHE A 159 19.678 6.605 87.391 1.00 21.95
ATOM 1232 CA PHE A 159 21.069 6.795 86.961 1.00 21.36
ATOM 1233 CB PHE A 159 22.015 6.331 88.061 1.00 19.55
ATOM 1234 CG PHE A 159 23.482 6.576 87.763 1.00 25.08 ATOM 1235 CD1 PHE A 159 24.200 5.692 86.951 1.00 23.92
ATOM 1236 CD2 PHE A 159 24.133 7.687 88.297 1.00 18.49
ATOM 1237 CE1 PHE A 159 25.553 5.900 86.676 1.00 22.53
ATOM 1238 CE2 PHE A 159 25.496 7.923 88.035 1.00 25.61 ATOM 1239 CZ PHE A 159 26.21 1 7.020 87.222 1.00 18.16
ATOM 1240 C PHE A 159 21.318 5.977 85.685 1.00 25.70
ATOM 1241 O PHE A 159 21.976 6.439 84.758 1.00 23.64
ATOM 1242 N ILE A 160 20.766 4.767 85.632 1.00 23.08
ATOM 1243 CA ILE A 160 20.947 3.885 84.469 1.00 23.13 ATOM 1244 CB ILE A 160 20.543 2.423 84.834 1.00 19.92
ATOM 1245 CG2 ILE A 160 20.682 1.532 83.653 1.00 16.53
ATOM 1246 CGI ILE A 160 21.472 1.899 85.952 1.00 26.23
ATOM 1247 CD1 ILE A 160 22.959 1.804 85.553 1.00 24.16
ATOM 1248 C ILE A 160 20.101 4.386 83.31 1 1.00 29.73 ATOM 1249 O ILE A 160 18.854 4.295 83.350 1.00 20.70
ATOM 1250 N LYS A 161 20.780 4.905 82.288 1.00 26.26
ATOM 1251 CA LYS A 161 20.1 12 5.480 81.110 1.00 30.25
ATOM 1252 CB LYS A 161 20.148 7.016 81.206 1.0026.96
ATOM 1253 CG LYS A 161 19.277 7.682 82.307 1.00 22.72 ATOM 1254 CD LYS A 161 17.809 7.688 81.860 1.00 25.96
ATOM 1255 CE LYS A 161 16.851 8.048 83.005 1.00 19.61
ATOM 1256 NZ LYS A 161 17.191 9.330 83.630 1.00 18.69
ATOM 1257 C LYS A 161 20.898 5.002 79.874 1.00 27.74
ATOM 1258 O LYS A 161 21.712 5.735 79.327 1.00 28.20 ATOM 1259 N PRO A 162 20.655 3.766 79.428 1.00 30.52
ATOM 1260 CD PRO A 162 19.709 2.768 79.972 1.00 32.07
ATOM 1261 CA PRO A 162 21.362 3.211 78.279 1.00 33.29
ATOM 1262 CB PRO A 162 21.030 1.734 78.381 1.00 33.21
ATOM 1263 CG PRO A 162 19.605 1.786 78.840 1.00 37.38 ATOM 1264 C PRO A 162 21.033 3.795 76.903 1.00 37.86
ATOM 1265 O PRO A 162 21.909 3.873 76.058 1.00 39.15
ATOM 1266 N TYR A 163 19.800 4.244 76.697 1.00 34.04
ATOM 1267 CA TYR A 163 19.396 4.769 75.396 1.00 38.73
ATOM 1268 CB TYR A 163 18.089 4.086 74.997 1.00 32.48 ATOM 1269 CG TYR A 163 18.193 2.593 75.1 14 1.00 33.71
ATOM 1270 CD1 TYR A 163 19.098 1.871 74.333 1.00 35.30
ATOM 1271 CE1 TYR A 163 19.263 0.498 74.511 1.00 33.76
ATOM 1272 CD2 TYR A 163 17.461 1.904 76.060 1.00 30.91 ATOM 1273 CE2 TYR A 163 17.624 0.534 76.244 1.00 36.85
ATOM 1274 CZ TYR A 163 18.527 -0.159 75.469 1.00 33.85
ATOM 1275 OH TYR A 163 18.716 -1.505 75.692 1.00 33.94
ATOM 1276 C TYR A 163 19.260 6.294 75.295 1.00 36.83 ATOM 1277 0 TYR A 163 19.046 6.836 74.213 1.00 39.86
ATOM 1278 N GLY A 164 19.380 6.974 76.427 1.00 37.24
ATOM 1279 CA GLY A 164 19.296 8.424 76.456 1.00 37.80
ATOM 1280 C GLY A 164 19.315 8.847 77.907 1.00 37.67
ATOM 1281 O GLY A 164 18.913 8.052 78.746 1.00 36.52 ATOM 1282 N LEU A 165 19.753 10.072 78.200 1.00 32.88
ATOM 1283 CA LEU A 165 19.848 10.563 79.572 1.00 35.38
ATOM 1284 CB LEU A 165 20.901 1 1.665 79.662 1.00 33.96
ATOM 1285 CG LEU A 165 22.295 1 1.195 79.225 1.00 37.70
ATOM 1286 CD1 LEU A 165 23.316 12.239 79.594 1.00 32.50 ATOM 1287 CD2 LEU A 165 22.656 9.894 79.911 1.00 38.64
ATOM 1288 C LEU A 165 18.557 11.046 80.223 1.00 36.12
ATOM 1289 O LEU A 165 18.496 11.198 81.457 1.00 34.44
ATOM 1290 N GLY A 166 17.538 1 1.307 79.405 1.00 33.58
ATOM 1291 CA GLY A 166 16.256 1 1.752 79.935 1.00 30.23 ATOM 1292 C GLY A 166 16.224 13.218 80.297 1.00 36.56
ATOM 1293 O GLY A 166 16.817 14.052 79.613 1.0045.27
ATOM 1294 N ASN A 167 15.547 13.543 81.386 1.00 32.83
ATOM 1295 CA ASN A 167 15.439 14.927 81.813 1.00 35.04
ATOM 1296 CB ASN A 167 14.224 15.070 82.720 1.0042.89 ATOM 1297 CG ASN A 167 13.888 16.496 83.005 1.00 47.06
ATOM 1298 OD1 ASN A 167 14.742 17.277 83.450 1.0048.03
ATOM 1299 ND2 ASN A 167 12.627 16.862 82.758 1.00 51.40
ATOM 1300 C ASN A 167 16.703 15.382 82.547 1.00 39.32
ATOM 1301 O ASN A 167 16.992 14.907 83.646 1.00 32.24 ATOM 1302 N LEU A 168 17.418 16.342 81.954 1.00 35.61
ATOM 1303 CA LEU A 168 18.670 16.851 82.507 1.00 34.29
ATOM 1304 CB LEU A 168 19.597 17.258 81.357 1.00 37.76
ATOM 1305 CG LEU A 168 19.944 16.188 80.331 1.00 36.56
ATOM 1306 CD1 LEU A 168 20.975 16.732 79.356 1.00 34.15 ATOM 1307 CD2 LEU A 168 20.496 14.984 81.044 1.00 36.77
ATOM 1308 C LEU A 168 18.554 18.020 83.474 1.00 33.26
ATOM 1309 O LEU A 168 19.582 18.592 83.897 1.00 29.28
ATOM 1310 N GLY A 169 17.319 18.376 83.823 1.00 29.92 ATOM 1311 CA GLY A 169 17.099 19.488 84.728 1.00 24.48
ATOM 1312 C GLY A 169 17.904 19.524 86.019 1.00 31.56
ATOM 1313 O GLY A 169 18.290 20.608 86.473 1.00 30.30
ATOM 1314 N ASP A 170 18.154 18.373 86.652 1.00 28.19 ATOM 1315 CA ASP A 170 18.941 18.390 87.887 1.00 22.92
ATOM 1316 CB ASP A 170 18.153 17.860 89.081 1.00 33.30
ATOM 1317 CG ASP A 170 16.918 18.678 89.382 1.00 35.02
ATOM 1318 OD1 ASP A 170 17.051 19.883 89.665 1.0043.03
ATOM 1319 OD2 ASP A 170 15.807 18.1 18 89.346 1.00 33.71 ATOM 1320 C ASP A 170 20.174 17.524 87.705 1.00 27.94
ATOM 1321 O ASP A 170 20.806 17.138 88.690 1.00 32.21
ATOM 1322 N ALA A 171 20.507 17.21 1 86.456 1.00 21.72
ATOM 1323 CA ALA A 171 21.671 16.387 86.170 1.00 27.21
ATOM 1324 CB ALA A 171 21.593 15.802 84.723 1.00 20.46 ATOM 1325 C ALA A 171 22.982 17.174 86.346 1.00 32.55
ATOM 1326 O ALA A 171 23.002 18.416 86.463 1.00 26.10
ATOM 1327 N ASN A 172 24.077 16.430 86.415 1.00 34.31
ATOM 1328 CA ASN A 172 25.398 17.031 86.536 1.00 29.79
ATOM 1329 CB ASN A 172 26.050 16.694 87.880 1.00 26.08 ATOM 1330 CG ASN A 172 27.424 17.369 88.044 1.00 28.08
ATOM 1331 OD1 ASN A 172 28.142 17.550 87.073 1.00 28.51
ATOM 1332 ND2 ASN A 172 27.787 17.699 89.276 1.00 17.60
ATOM 1333 C ASN A 172 26.127 16.348 85.391 1.00 29.7.4
ATOM 1334 O ASN A 172 26.787 15.315 85.557 1.00 31.13 ATOM 1335 N ILE A 173 25.966 16.919 84.207 1.00 29.21
ATOM 1336 CA ILE A 173 26.544 16.382 83.006 1.00 32.01
ATOM 1337 CB ILE A 173 26.193 17.243 81.782 1.00 41.27
ATOM 1338 CG2 ILE A 173 27.254 18.328 81.576 1.00 41.67
ATOM 1339 CGI ILE A 173 26.1 12 16.359 80.538 1.00 47.96 ATOM 1340 CD1 ILE A 173 25.054 15.287 80.623 1.00 53.84
ATOM 1341 C ILE A 173 28.065 16.301 83.137 1.00 31.59
ATOM 1342 O ILE A 173 28.666 15.372 82.634 1.00 28.59
ATOM 1343 N GLU A 174 28.674 17.246 83.835 1.00 33.20
ATOM 1344 CA GLU A 174 30.124 17.208 83.983 1.00 37.98 ATOM 1345 CB GLU A 174 30.614 18.446 84.717 1.00 40.68
ATOM 1346 CG GLU A 174 30.640 19.693 83.845 1.00 57.84
ATOM 1347 CD GLU A 174 31.638 19.571 82.686 1.00 65.79
ATOM 1348 OE1 GLU A 174 32.852 19.425 82.956 1.00 71.30 ATOM 1349 OE2GLUA174 31.210 19.61581.506 1.0070.14
ATOM 1350 C GLUA 174 30.596 15.97384.718 1.0039.67
ATOM 1351 O GLUA 174 31.543 15.32284.291 1.0043.08
ATOM 1352 N ALAA175 29.891 15.62885.796 1.0038.03 ATOM 1353 CA ALA A 175 30.259 14.50586.646 1.0033.43
ATOM 1354 CB ALAA175 29.818 14.791 88.088 1.0031.50
ATOM 1355 C ALAA175 29.787 13.13486.259 1.0031.12
ATOM 1356 O ALAA175 30.433 12.15486.603 1.0035.27
ATOM 1357 N TRP A 176 28.659 13.04685.560 1.0035.00 ATOM 1358 CA TRPA 176 28.074 11.753 85.191 1.0028.20
ATOM 1359 CB TRPA 176 26.873 11.98484.245 1.0032.74
ATOM 1360 CG TRP A 176 25.756 10.93684.367 1.0029.36
ATOM 1361 CD2TRPA176 24.362 11.12484.056 1.0025.88
ATOM 1362 CE2 TRP A 176 23.728 9.861 84.166 1.0029.45 ATOM 1363 CE3TRPA176 23.594 12.23683.698 1.0024.03
ATOM 1364 CD1 TRPA 176 25.902 9.59984.652 1.0024.51
ATOM 1365 NE1 TRPA 176 24.688 8.94884.529 1.0026.04
ATOM 1366 CZ2 TRP A 176 22.347 9.68383.924 1.0029.88
ATOM 1367 CZ3TRPA176 22.210 12.05983.454 1.0029.37 ATOM 1368 CH2TRPA176 21.612 10.79283.569 1.0027.92
ATOM 1369 C TRPA 176 29.040 10.69984.601 1.0033.03
ATOM 1370 O TRP A 176 29.023 9.53085.016 1.0026.88
ATOM 1371 N PRO A 177 29.862 11.07083.589 1.0036.53
ATOM 1372 CD PRO A 177 29.982 12.31782.817 1.0039.03 ATOM 1373 CA PRO A 177 30.782 10.05483.052 1.0036.18
ATOM 1374 CB PROA 177 31.494 10.80281.917 1.0035.43
ATOM 1375 CG PROA 177 31.426 12.26082.405 1.0046.83
ATOM 1376 C PRO A 177 31.745 9.465 84.113 1.0028.57
ATOM 1377 O PROA 177 32.029 8.27384.079 1.0032.99 ATOM 1378 N LYS A 178 32.244 10.28785.037 1.0029.55
ATOM 1379 CA LYS A 178 33.118 9.785 86.107 1.0025.91
ATOM 1380 CB LYS A 178 33.647 10.92986.980 1.0031.42
ATOM 1381 CG LYS A 178 34.393 10.44488.227 1.0037.87
ATOM 1382 CD LYS A 178 34.529 11.51689.337 1.0042.22 ATOM 1383 CE LYS A 178 35.448 12.68988.977 1.0046.19
ATOM 1384 NZ LYS A 178 35.575 13.70690.104 1.0048.88
ATOM 1385 C LYS A 178 32.275 8.85986.993 1.0027.22
ATOM 13860 LYS A 178 32.689 7.76687.378 1.0022.68 ATOM 1387 N SER A 179 31.068 9.318 87.315 1.00 27.05
ATOM 1388 CA SER A 179 30.162 8.528 88.149 1.00 29.93
ATOM 1389 CB SER A 179 28.892 9.346 88.481 1.00 25.14
ATOM 1390 OG SER A 179 29.272 10.435 89.334 1.00 22.85 ATOM 1391 C SER A 179 29.811 7.201 87.479 1.00 21.44
ATOM 1392 0 SER A 179 29.800 6.154 88.132 1.00 25.99
ATOM 1393 N ALA A 180 29.545 7.226 86.183 1.00 24.18
ATOM 1394 CA ALA A 180 29.201 5.993 85.478 1.00 22.29
ATOM 1395 CB ALA A 180 28.680 6.317 84.063 1.00 27.05 ATOM 1396 C ALA A 180 30.420 5.053 85.381 1.00 29.30
ATOM 1397 O ALA A 180 30.269 3.822 85.413 1.00 25.86
ATOM 1398 N LYS A 181 31.618 5.626 85.250 1.00 29.88
ATOM 1399 CA LYS A 181 32.833 4.808 85.154 1.00 31.99
ATOM 1400 CB LYS A 181 34.071 5.684 84.933 1.00 33.45 ATOM 1401 CG LYS A 181 35.236 5.032 84.143 1.0047.03
ATOM 1402 CD LYS A 181 35.555 3.572 84.542 1.00 55.52
ATOM 1403 CE LYS A 181 34.531 2.565 83.954 1.00 59.21
ATOM 1404 NZ LYS A 181 34.739 1.122 84.310 1.0049.46
ATOM 1405 C LYS A 181 32.972 4.051 86.481 1.00 26.84 ATOM 1406 O LYS A 181 33.065 2.837 86.502 1.00 34.25
ATOM 1407 N LEU A 182 32.971 4.773 87.591 1.00 28.04
ATOM 1408 CA LEU A 182 33.068 4.127 88.907 1.00 27.61
ATOM 1409 CB LEU A 182 32.939 5.186 90.005 1.00 31.00
ATOM 1410 CG LEU A 182 32.814 4.720 91.468 1.00 34.39 ATOM 1411 CD1 LEU A 182 34.138 4.083 91.924 1.0040.47
ATOM 1412 CD2 LEU A 182 32.476 5.906 92.378 1.0040.59
ATOM 1413 C LEU A 182 31.990 3.036 89.101 1.00 28.51
ATOM 1414 O LEU A 182 32.268 1.955 89.610 1.00 25.26
ATOM 1415 N LEU A 183 30.754 3.332 88.711 1.00 24.14 ATOM 1416 CA LEU A 183 29.670 2.355 88.845 1.00 26.12
ATOM 1417 CB LEU A 183 28.343 2.978 88.413 1.00 20.96
ATOM 1418 CG LEU A 183 27.203 1.985 88.576 1.00 24.08
ATOM 1419 CD1 LEU A 183 26.995 1.727 90.062 1.0024.88
ATOM 1420 CD2 LEU A 183 25.927 2.603 87.943 1.0023.18 ATOM 1421 C LEU A 183 29.911 1.089 88.003 1.00 25.63
ATOM 1422 O LEU A 183 29.687 -0.026 88.458 1.00 23.07
ATOM 1423 N LYS A 184 30.324 1.260 86.756 1.00 26.25
ATOM 1424 CA LYS A 184 30.594 0.106 85.910 1.00 27.52 ATOM 1425 CB LYS A 184 30.889 0.551 84.458 1.00 32.17
ATOM 1426 CG LYS A 184 31.405 -0.577 83.557 1.00 36.61
ATOM 1427 CD LYS A 184 31.724 -0.055 82.154 1.00 41.85
ATOM 1428 CE LYS A 184 32.579 -1.051 81.346 1.00 42.72 ATOM 1429 NZ LYS A 184 31.888 -2.342 81.084 1.00 42.13
ATOM 1430 C LYS A 184 31.783 -0.689 86.476 1.00 30.32
ATOM 1431 O LYS A 184 31.809 -1.922 86.411 1.00 31.98
ATOM 1432 N SER A 185 32.765 -0.01 1 87.047 1.00 29.54
ATOM 1433 CA SER A 185 33.902 -0.772 87.591 1.00 31.51 ATOM 1434 CB SER A 185 35.028 0.164 88.065 1.00 33.72
ATOM 1435 OG SER A 185 35.595 0.867 86.980 1.0040.23
ATOM 1436 C SER A 185 33.464 -1.630 88.763 1.00 33.34
ATOM 1437 O SER A 185 33.873 -2.780 88.919 1.00 34.78
ATOM 1438 N LYS A 186 32.612 -1.044 89.584 1.00 35.29 ATOM 1439 CA LYS A 186 32.114 -1.671 90.790 1.00 32.91
ATOM 1440 CB LYS A 186 31.406 -0.583 91.625 1.00 35.27
ATOM 1441 CG LYS A 186 30.752 -1.024 92.920 1.00 39.23
ATOM 1442 CD LYS A 186 31.749 -1.250 94.010 1.00 39.62
ATOM 1443 CE LYS A 186 31.023 -1.579 95.294 1.0044.12 ATOM 1444 NZ LYS A 186 31.958 -1.719 96.406 1.00 35.64
ATOM 1445 C LYS A 186 31.177 -2.865 90.581 1.00 30.04
ATOM 1446 O LYS A 186 31.287 -3.861 91.263 1.00 18.99
ATOM 1447 N TYR A 187 30.281 -2.776 89.608 1.00 30.12
ATOM 1448 CA TYR A 187 29.284 -3.804 89.421 1.00 26.29 ATOM 1449 CB TYR A 187 27.910 -3.153 89.702 1.00 21.67
ATOM 1450 CG TYR A 187 27.803 -2.696 91.1 11 1.00 20.68
ATOM 1451 CD1 TYR A 187 27.807 -3.622 92.147 1.00 15.91
ATOM 1452 CE1 TYR A 187 27.667 -3.242 93.469 1.00 23.84
ATOM 1453 CD2 TYR A 187 27.661 -1.343 91.429 1.00 23.06 ATOM 1454 CE2 TYR A 187 27.514 -0.948 92.767 1.00 22.09
ATOM 1455 CZ TYR A 187 27.513 -1.901 93.767 1.00 22.95
ATOM 1456 OH TYR A 187 27.318 -1.565 95.066 1.00 19.41
ATOM 1457 C TYR A 187 29.245 -4.578 88.104 1.00 29.32
ATOM 1458 O TYR A 187 28.166 -5.022 87.663 1.00 31.84 ATOM 1459 N GLY A 188 30.411 -4.742 87.487 1.00 36.84
ATOM 1460 CA GLY A 188 30.497 -5.492 86.247 1.00 38.21
ATOM 1461 C GLY A 188 30.057 -6.901 86.548 1.00 33.95
ATOM 1462 O GLY A 188 29.626 -7.614 85.656 1.00 37.12 ATOM 1463 N LYS A 189 30.153 -7.271 87.827 1.00 30.49
ATOM 1464 CA LYS A 189 29.757 -8.575 88.349 1.00 31.27
ATOM 1465 CB LYS A 189 30.326 -8.780 89.768 1.00 37.73
ATOM 1466 CG LYS A 189 29.993 -7.626 90.758 1.00 40.57 ATOM 1467 CD LYS A 189 30.309 -7.903 92.249 1.00 38.87
ATOM 1468 CE LYS A 189 30.034 -6.617 93.090 1.00 38.15
ATOM 1469 NZ LYS A 189 30.251 -6.661 94.573 1.00 34.27
ATOM 1470 C LYS A 189 28.224 -8.756 88.416 1.00 33.30
ATOM 1471 O LYS A 189 27.747 -9.821 88.799 1.00 33.41 ATOM 1472 N ALA A 190 27.458 -7.719 88.075 1.00 29.26
ATOM 1473 CA ALA A 190 25.995 -7.829 88.112 1.00 25.12
ATOM 1474 CB ALA A 190 25.356 -6.432 87.920 1.00 23.88
ATOM 1475 C ALA A 190 25.436 -8.768 87.037 1.00 26.97
ATOM 1476 O ALA A 190 25.850 -8.699 85.869 1.00 26.97 ATOM 1477 N LYS A 191 24.491 -9.621 87.435 1.00 22.33
ATOM 1478 CA LYS A 191 23.785 -10.493 86.504 1.00 30.48
ATOM 1479 CB LYS A 191 23.328 -1 1.771 87.196 1.00 26.99
ATOM 1480 CG LYS A 191 24.518 -12.772 87.293 1.00 37.65
ATOM 1481 CD LYS A 191 24.386 -13.889 88.345 1.00 38.79 ATOM 1482 CE LYS A 191 23.297 -14.885 88.052 1.00 49.90
ATOM 1483 NZ LYS A 191 23.307 -15.982 89.087 1.00 58.39
ATOM 1484 C LYS A 191 22.594 -9.724 85.944 1.00 30.44
ATOM 1485 O LYS A 191 22.281 -9.843 84.770 1.00 34.92
ATOM 1486 N LEU A 192 21.934 -8.921 86.775 1.00 24.88 ATOM 1487 CA LEU A 192 20.798 -8.131 86.292 1.00 25.62
ATOM 1488 CB LEU A 192 19.454 -8.671 86.861 1.00 24.00
ATOM 1489 CG LEU A 192 18.867 -10.043 86.460 1.00 30.98
ATOM 1490 CD1 LEU A 192 17.746 -10.462 87.404 1.00 26.18
ATOM 1491 CD2 LEU A 192 18.324 -9.970 85.029 1.00 25.66 ATOM 1492 C LEU A 192 20.950 -6.677 86.755 1.00 22.71
ATOM 1493 O LEU A 192 21.306 -6.435 87.898 1.00 21.19
ATOM 1494 N VAL A 193 20.686 -5.731 85.857 1.00 23.69
ATOM 1495 CA VAL A 193 20.680 -4.307 86.181 1.00 20.67
ATOM 1496 CB VAL A 193 21.651 -3.495 85.359 1.00 20.41 ATOM 1497 CGI VAL A 193 21.525 -2.040 85.723 1.00 20.38
ATOM 1498 CG2 VAL A 193 23.096 -3.956 85.683 1.00 19.89
ATOM 1499 C VAL A 193 19.251 -3.839 85.886 1.00 21.01
ATOM 1500 O VAL A 193 18.730 -3.977 84.752 1.00 20.62 ATOM 1501 N VAL A 194 18.628 -3.290 86.914 1.00 13.41
ATOM 1502 CA VAL A 194 17.219 -2.828 86.833 1.00 16.45
ATOM 1503 CB VAL A 194 16.426 -3.287 88.053 1.00 17.73
ATOM 1504 CGI VAL A 194 14.935 -2.871 87.913 1.00 15.56 ATOM 1505 CG2 VAL A 194 16.524 -4.802 88.222 1.00 24.70
ATOM 1506 C VAL A 194 17.133 -1.312 86.806 1.00 18.24
ATOM 1507 O VAL A 194 17.350 -0.664 87.842 1.00 19.33
ATOM 1508 N PRO A 195 16.875 -0.715 85.629 1.00 16.33
ATOM 1509 CD PRO A 195 16.741 -1.277 84.274 1.00 19.61 ATOM 1510 CA PRO A 195 16.771 0.738 85.558 1.00 16.87
ATOM 1511 CB PRO A 195 16.909 1.042 84.052 1.00 15.28
ATOM 1512 CG PRO A 195 17.472 -0.230 83.455 1.00 18.49
ATOM 1513 C PRO A 195 15.398 1.164 86.026 1.00 20.29
ATOM 1514 O PRO A 195 14.445 0.382 86.017 1.00 19.33 ATOM 1515 N SER A 196 15.284 2.431 86.363 1.00 19.59
ATOM 1516 CA SER A 196 14.009 2.959 86.758 1.00 16.66
ATOM 1517 CB SER A 196 14.172 4.362 87.323 1.00 17.99
ATOM 1518 OG SER A 196 14.531 4.320 88.698 1.00 18.73
ATOM 1519 C SER A 196 13.066 3.078 85.575 1.00 20.48 ATOM 1520 O SER A 196 1 1.884 2.747 85.684 1.00 18.88
ATOM 1521 N HIS A 197 13.606 3.548 84.447 1.00 24.85
ATOM 1522 CA HIS A 197 12.781 3.860 83.285 1.00 25.60
ATOM 1523 CB HIS A 197 12.933 5.325 82.956 1.00 20.66
ATOM 1524 CG HIS A 197 12.590 6.217 84.089 1.00 21.06 ATOM 1525 CD2 HIS A 197 13.321 7.140 84.751 1.00 23.38
ATOM 1526 ND1 HIS A 197 1 1.342 6.220 84.672 1.00 18.05
ATOM 1527 CE1 HIS A 197 1 1.314 7.107 85.645 1.00 23.26
ATOM 1528 NE2 HIS A 197 12.504 7.678 85.712 1.00 20.16
ATOM 1529 C HIS A 197 12.909 3.092 82.012 1.00 26.84 ATOM 1530 O HIS A 197 12.422 3.542 80.978 1.00 29.13
ATOM 1531 N SER A 198 13.553 1.944 82.076 1.00 25.76
ATOM 1532 CA SER A 198 13.690 1.104 80.910 1.00 29.69
ATOM 1533 CB SER A 198 14.930 1.489 80.087 1.00 30.83
ATOM 1534 OG SER A 198 16.125 1.526 80.841 1.00 34.86 ATOM 1535 C SER A 198 13.718 -0.343 81.389 1.00 29.12
ATOM 1536 0 SER A 198 13.739 -0.596 82.591 1.00 25.34
ATOM 1537 N GLU A 199 13.703 -1.285 80.458 1.00 25.67
ATOM 1538 CA GLU A 199 13.669 -2.706 80.786 1.00 27.04 ATOM 1539 CB GLU A 199 13.467 -3.545 79.515 1.0040.95
ATOM 1540 CG GLU A 199 12.126 -3.288 78.832 1.00 54.50
ATOM 1541 CD GLU A 199 10.950 -3.454 79.794 1.00 61.37
ATOM 1542 OE1 GLU A 199 10.722 -4.584 80.290 1.00 53.81 ATOM 1543 OE2 GLU A 199 10.262 -2.440 80.059 1.00 68.12
ATOM 1544 C GLU A 199 14.905 -3.201 81.496 1.00 24.96
ATOM 1545 O GLU A 199 15.978 -2.623 81.374 1.00 24.34
ATOM 1546 N VAL A 200 14.722 -4.266 82.255 1.00 24.49
ATOM 1547 CA VAL A 200 15.825 -4.904 82.958 1.00 31.29 ATOM 1548 CB VAL A 200 15.330 -6.138 83.743 1.00 30.33
ATOM 1549 CGI VAL A 200 16.518 -6.890 84.365 1.00 26.02
ATOM 1550 CG2 VAL A 200 14.363 -5.688 84.824 1.00 22.79
ATOM 1551 C VAL A 200 16.829 -5.363 81.889 1.00 30.04
ATOM 1552 O VAL A 200 16.447 -5.724 80.775 1.00 31.58 ATOM 1553 N GLY A 201 18.108 -5.324 82.220 1.00 30.90
ATOM 1554 CA GLY A 201 19.124 -5.756 81.275 1.00 28.50
ATOM 1555 C GLY A 201 20.214 -6.445 82.055 1.00 28.92
ATOM 1556 O GLY A 201 20.002 -6.812 83.207 1.00 25.63
ATOM 1557 N ASP A 202 21.381 -6.613 81.440 1.00 27.43 ATOM 1558 CA ASP A 202 22.498 -7.272 82.1 13 1.00 31.75
ATOM 1559 CB ASP A 202 23.052 -8.428 81.253 1.00 30.87
ATOM 1560 CG ASP A 202 23.812 -7.943 80.034 1.00 41.14
ATOM 1561 OD1 ASP A 202 23.347 -7.009 79.355 1.00 43.56
ATOM 1562 OD2 ASP A 202 24.885 -8.512 79.747 1.00 54.43 ATOM 1563 C ASP A 202 23.562 -6.21 1 82.348 1.00 26.91
ATOM 1564 O ASP A 202 23.287 -5.020 82.183 1.00 29.82
ATOM 1565 N ALA A 203 24.770 -6.619 82.727 1.00 28.86
ATOM 1566 CA ALA A 203 25.807 -5.647 83.021 1.00 25.99
ATOM 1567 CB ALA A 203 27.076 -6.356 83.513 1.00 24.60 ATOM 1568 C ALA A 203 26.126 -4.676 81.893 1.00 27.13
ATOM 1569 O ALA A 203 26.655 -3.574 82.141 1.00 25.69
ATOM 1570 N SER A 204 25.784 -5.045 80.662 1.00 29.17
ATOM 1571 CA SER A 204 26.047 -4.167 79.529 1.00 31.08
ATOM 1572 CB SER A 204 25.598 -4.811 78.206 1.00 33.65 ATOM 1573 OG SER A 204 24.194 -5.002 78.167 1.0040.65
ATOM 1574 C SER A 204 25.340 -2.832 79.717 1.00 32.94
ATOM 1575 O SER A 204 25.752 -1.835 79.137 1.00 34.71
ATOM 1576 N LEU A 205 24.273 -2.792 80.523 1.00 33.02 ATOM 1577 CA LEU A 205 23.602 -1.523 80.736 1.00 27.06
ATOM 1578 CB LEU A 205 22.268 -1.686 81.504 1.00 28.77
ATOM 1579 CG LEU A 205 21.188 -2.540 80.807 1.00 23.30
ATOM 1580 CD1 LEU A 205 19.825 -2.382 81.466 1.00 26.59 ATOM 1581 CD2 LEU A 205 21.088 -2.097 79.361 1.00 29.97
ATOM 1582 C LEU A 205 24.495 -0.477 81.413 1.00 27.77
ATOM 1583 O LEU A 205 24.268 0.728 81.239 1.00 24.22
ATOM 1584 N LEU A 206 25.511 -0.921 82.159 1.00 25.83
ATOM 1585 CA LEU A 206 26.457 0.000 82.826 1.00 26.70 ATOM 1586 CB LEU A 206 27.348 -0.762 83.812 1.00 27.29
ATOM 1587 CG LEU A 206 26.541 -1.422 84.909 1.00 32.21
ATOM 1588 CD1 LEU A 206 27.394 -2.416 85.642 1.00 29.67
ATOM 1589 CD2 LEU A 206 25.952 -0.328 85.851 1.00 26.95
ATOM 1590 C LEU A 206 27.350 0.647 81.779 1.00 27.28 ATOM 1591 O LEU A 206 27.720 1.844 81.883 1.00 24.89
ATOM 1592 N LYS A 207 27.681 -0.143 80.759 1.00 27.44
ATOM 1593 CA LYS A 207 28.520 0.347 79.676 1.00 30.94
ATOM 1594 CB LYS A 207 29.023 -0.834 78.839 1.00 37.23
ATOM 1595 CG LYS A 207 30.049 -0.470 77.758 1.00 45.09 ATOM 1596 CD LYS A 207 30.702 -1.745 77.195 1.00 50.50
ATOM 1597 CE LYS A 207 31.761 -1.430 76.128 1.00 54.71
ATOM 1598 NZ LYS A 207 32.439 -2.660 75.620 1.00 56.70
ATOM 1599 C LYS A 207 27.717 1.343 78.832 1.00 32.43
ATOM 1600 O LYS A 207 28.211 2.434 78.501 1.00 34.74 ATOM 1601 N LEU A 208 26.472 0.981 78.506 1.00 33.39
ATOM 1602 CA LEU A 208 25.585 1.866 77.738 1.00 32.45
ATOM 1603 CB LEU A 208 24.249 1.176 77.458 1.00 35.09
ATOM 1604 CG LEU A 208 24.354 -0.019 76.502 1.00 43.61
ATOM 1605 CD 1 LEU A 208 23.041 -0.799 76.391 1.0040.84 ATOM 1606 CD2 LEU A 208 24.795 0.520 75.142 1.0049.80
ATOM 1607 C LEU A 208 25.355 3.198 78.448 1.00 33.13
ATOM 1608 O LEU A 208 25.291 4.248 77.804 1.00 32.13
ATOM 1609 N THR A 209 25.244 3.166 79.778 1.00 31.48
ATOM 1610 CA THR A 209 25.049 4.388 80.536 1.00 29.76 ATOM 161 1 CB THR A 209 24.642 4.077 82.023 1.00 27.14
ATOM 1612 OGl THR A 209 23.354 3.426 82.027 1.00 26.06
ATOM 1613 CG2 THR A 209 24.560 5.364 82.842 1.00 21.78
ATOM 1614 C THR A 209 26.319 5.245 80.480 1.00 32.82 ATOM 1615 O THR A 209 26.234 6.468 80.370 1.00 31.55
ATOM 1616 N LEU A 210 27.492 4.618 80.574 1.00 33.36
ATOM 1617 CA LEU A 210 28.723 5.394 80.486 1.00 31.93
ATOM 1618 CB LEU A 210 29.943 4.498 80.647 1.00 32.28 ATOM 1619 CG LEU A 210 31.278 5.212 80.404 1.00 30.51
ATOM 1620 CD1 LEU A 210 31.423 6.396 81.312 1.00 31.06
ATOM 1621 CD2 LEU A 210 32.399 4.237 80.630 1.00 36.85
ATOM 1622 C LEU A 210 28.772 6.094 79.129 1.00 34.51
ATOM 1623 O LEU A 210 29.045 7.291 79.045 1.00 32.59 ATOM 1624 N GLU A 21 1 28.475 5.345 78.069 1.00 37.80
ATOM 1625 CA GLU A 21 1 28.481 5.903 76.719 1.00 38.04
ATOM 1626 CB GLU A 21 1 28.106 4.806 75.716 1.00 43.99
ATOM 1627 CG GLU A 21 1 29.220 3.811 75.384 1.0045.61
ATOM 1628 CD GLU A 211 28.691 2.580 74.680 1.00 52.70 ATOM 1629 OE1 GLU A 21 1 27.639 2.686 74.010 1.00 58.36
ATOM 1630 OE2 GLU A 211 29.324 1.506 74.781 1.00 56.83
ATOM 1631 C GLU A 21 1 27.518 7.094 76.605 1.00 38.89
ATOM 1632 O GLU A 21 1 27.887 8.169 76.137 1.00 37.33
ATOM 1633 N GLN A 212 26.276 6.912 77.042 1.00 36.96 ATOM 1634 CA GLN A 212 25.299 7.997 76.982 1.00 34.24
ATOM 1635 CB GLN A 212 23.946 7.522 77.510 1.00 33.94
ATOM 1636 CG GLN A 212 23.296 6.430 76.701 1.00 37.54
ATOM 1637 CD GLN A 212 23.092 6.842 75.257 1.0041.82
ATOM 1638 OE1 GLN A 212 22.837 8.010 74.974 1.00 35.62 ATOM 1639 NE2 GLN A 212 23.172 5.877 74.340 1.00 38.09
ATOM 1640 C GLN A 212 25.739 9.227 77.784 1.00 35.38
ATOM 1641 O GLN A 212 25.466 10.358 77.387 1.00 33.23
ATOM 1642 N ALA A 213 26.398 9.006 78.920 1.00 26.48
ATOM 1643 CA ALA A 213 26.853 10.1 15 79.760 1.00 32.17 ATOM 1644 CB ALA A 213 27.307 9.589 81.135 1.00 22.01
ATOM 1645 C ALA A 213 28.022 10.822 79.054 1.00 32.82
ATOM 1646 O ALA A 213 28.1 13 12.039 79.028 1.00 31.10
ATOM 1647 N VAL A 214 28.931 10.036 78.505 1.00 37.33
ATOM 1648 CA VAL A 214 30.061 10.608 77.806 1.0041.02 ATOM 1649 CB VAL A 214 30.950 9.476 77.263 1.0044.83
ATOM 1650 CGI VAL A 214 32.008 10.024 76.289 1.0045.69
ATOM 1651 CG2 VAL A 214 31.612 8.770 78.435 1.00 35.89
ATOM 1652 C VAL A 214 29.475 11.476 76.690 1.00 46.10 ATOM 1653 O VAL A 214 29.773 12.672 76.581 1.0049.28
ATOM 1654 N LYS A 215 28.596 10.877 75.900 1.0043.71
ATOM 1655 CA LYS A 215 27.934 1 1.562 74.799 1.0048.80
ATOM 1656 CB LYS A 215 26.880 10.642 74.192 1.00 50.58 ATOM 1657 CG LYS A 215 26.119 1 1.238 73.032 1.00 54.12
ATOM 1658 CD LYS A 215 25.187 10.204 72.417 1.00 54.55
ATOM 1659 CE LYS A 215 24.399 10.823 71.290 1.00 61.64
ATOM 1660 NZ LYS A 215 25.308 1 1.366 70.240 1.00 68.45
ATOM 1661 C LYS A 215 27.276 12.879 75.212 1.00 48.58 ATOM 1662 O LYS A 215 27.320 13.862 74.475 1.00 48.12
ATOM 1663 N GLY A 216 26.663 12.890 76.390 1.0045.22
ATOM 1664 CA GLY A 216 25.993 14.083 76.873 1.0045.88
ATOM 1665 C GLY A 216 26.930 15.176 77.343 1.00 49.84
ATOM 1666 O GLY A 216 26.582 16.359 77.298 1.0049.28 ATOM 1667 N LEU A 217 28.1 13 14.801 77.810 1.0049.52
ATOM 1668 CA LEU A 217 29.049 15.814 78.260 1.00 54.76
ATOM 1669 CB LEU A 217 30.256 15.180 78.973 1.00 51.91
ATOM 1670 CG LEU A 217 31.310 16.170 79.484 1.00 51.69
ATOM 1671 CD1 LEU A 217 30.622 17.265 80.279 1.00 52.07 ATOM 1672 CD2 LEU A 217 32.355 15.465 80.334 1.00 50.00
ATOM 1673 C LEU A 217 29.498 16.635 77.053 1.00 57.94
ATOM 1674 O LEU A 217 29.557 17.861 77.125 1.00 62.59
ATOM 1675 N ASN A 218 29.789 15.976 75.938 1.00 60.96
ATOM 1676 CA ASN A 218 30.221 16.706 74.748 1.00 69.27 ATOM 1677 CB ASN A 218 30.391 15.757 73.561 1.00 69.58
ATOM 1678 CG ASN A 218 31.360 14.637 73.848 1.00 73.52
ATOM 1679 OD1 ASN A 218 32.461 14.860 74.357 1.00 77.42
ATOM 1680 ND2 ASN A 218 30.965 13.420 73.505 1.00 72.47
ATOM 1681 C ASN A 218 29.212 17.795 74.372 1.00 72.82 ATOM 1682 O ASN A 218 29.402 18.982 74.671 1.00 75.20
ATOM 1683 N GLU A 219 28.142 17.366 73.712 1.00 74.69
ATOM 1684 CA GLU A 219 27.066 18.241 73.269 1.00 76.71
ATOM 1685 CB GLU A 219 26.099 17.434 72.398 1.00 80.30
ATOM 1686 CG GLU A 219 25.671 16.125 73.024 1.00 83.36 ATOM 1687 CD GLU A 219 25.067 15.164 72.01 1 1.00 89.02
ATOM 1688 OE1 GLU A 219 25.783 14.773 71.059 1.00 87.10
ATOM 1689 OE2 GLU A 219 23.878 14.796 72.167 1.00 92.25
ATOM 1690 C GLU A 219 26.317 18.930 74.406 1.00 75.85 ATOM 1691 O GLU A 219 26.911 19.121 75.493 1.00 71.10
ATOM 1692 OXT GLU A 219 25.148 19.305 74.168 1.00 73.58 TER GLU A 219
ATOM 1693 CB LEU B 4 28.906 2.024 130.728 1.00 56.39 ATOM 1694 CG LEU B 4 29.256 0.640 130.177 1.00 51.97
ATOM 1695 CD1 LEU B 4 28.364 -0.396 130.833 1.00 55.23
ATOM 1696 CD2 LEU B 4 29.047 0.612 128.675 1.00 58.20
ATOM 1697 C LEU B 4 30.943 2.373 132.156 1.00 56.24
ATOM 1698 O LEU B 4 31.569 1.617 132.900 1.00 59.89 ATOM 1699 N LEU B 4 28.775 3.580 132.675 1.00 54.39
ATOM 1700 CA LEU B 4 29.404 2.328 132.149 1.00 57.1 1
ATOM 1701 N PRO B 5 31.576 3.232 131.321 1.0052.57
ATOM 1702 CD PRO B 5 31.1 10 4.191 130.303 1.00 54.49
ATOM 1703 C A PRO B 5 33.041 3.236 131.371 1.0048.10 ATOM 1704 CB PRO B 5 33.419 4.341 130.378 1.0048.20
ATOM 1705 CG PRO B 5 32.193 5.222 130.358 1.00 50.54
ATOM 1706 C PRO B 5 33.580 3.464 132.792 1.0048.12
ATOM 1707 O PRO B 5 32.959 4.139 133.618 1.0043.33
ATOM 1708 N ASP B 6 34.743 2.889 133.062 1.0044.80 ATOM 1709 C A ASP B 6 35.344 2.967 134.376 1.0048.95
ATOM 1710 CB ASP B 6 36.477 1.960 134.489 1.00 52.24
ATOM 171 1 CG ASP B 6 36.067 0.587 134.019 1.00 58.37
ATOM 1712 OD1 ASP B 6 34.968 0.132 134.412 1.00 59.04
ATOM 1713 OD2 ASP B 6 36.847 -0.034 133.265 1.00 65.12 ATOM 1714 C ASP B 6 35.873 4.316 134.726 1.00 46.1 1
ATOM 1715 O ASP B 6 36.312 5.067 133.858 1.0046.15
ATOM 1716 N LEU B 7 35.842 4.601 136.020 1.0043.33
ATOM 1717 CA LEU B 7 36.328 5.855 136.562 1.0040.94
ATOM 1718 CB LEU B 7 36.358 5.772 138.096 1.0046.06 ATOM 1719 CG LEU B 7 36.880 6.958 138.927 1.0045.92
ATOM 1720 CD1 LEU B 7 35.983 8.166 138.732 1.0044.11
ATOM 1721 CD2 LEU B 7 36.901 6.579 140.401 1.0046.82
ATOM 1722 C LEU B 7 37.740 6.115 136.044 1.0042.36
ATOM 1723 0 LEU B 7 38.533 5.198 135.885 1.00 39.13 ATOM 1724 N LYS B 8 38.055 7.368 135.762 1.00 43.56
ATOM 1725 CA LYS B 8 39.403 7.673 135.319 1.0048.35
ATOM 1726 CB LYS B 8 39.470 7.975 133.806 1.0049.40
ATOM 1727 CG LYS B 8 38.725 9.187 133.285 1.00 56.81 ATOM 1728 CD LYS B 8 39.046 9.380131.788 1.0058.13
ATOM 1729 CE LYS B 8 38.285 10.547131.160 1.0059.25
ATOM 1730 NZ LYS B 8 38.636 10.747129.706 1.0058.10
ATOM 1731 C LYSB 8 39.964 8.826136.131 1.0045.74 ATOM 17320 LYSB 8 39.233 9.739136.543 1.0046.76
ATOM 1733 N ILE B 9 41.263 8.734136.390 1.0045.49
ATOM 1734 CA ILE B 9 42.019 9.722137.143 1.0046.29
ATOM 1735 CB ILE B 9 42.629 9.128138.429 1.0046.38
ATOM 1736 CG2ILEB 9 43.639 10.089139.010 1.0048.38 ATOM 1737 CGI ILE B 9 41.544 8.810139.451 1.0049.60
ATOM 1738 CD1ILEB 9 40.671 7.671139.081 1.0051.27
ATOM 1739 C ILEB 9 43.167 10.138136.247 1.0044.67
ATOM 1740 O ILEB 9 43.979 9.312135.854 1.0048.47
ATOM 1741 N GLU B 10 43.231 11.415135.912 1.0045.11 ATOM 1742 CA GLU B 10 44.292 11.912135.055 1.0046.82
ATOM 1743 CB GLU B 10 43.730 12.289133.682 1.0051.66
ATOM 1744 CG GLUB 10 43.250 11.129132.830 1.0063.51
ATOM 1745 CD GLUB 10 42.261 11.576131.754 1.0069.99
ATOM 1746 OE1 GLUB 10 41.092 11.884132.097 1.0068.93 ATOM 1747 OE2 GLUB 10 42.659 11.632130.570 1.0071.69
ATOM 1748 C GLUB 10 44.910 13.135135.695 1.0044.58
ATOM 1749 O GLUB 10 44.205 14.0301 6.169 1.0044.14
ATOM 1750 N LYSB 11 46.232 13.166135.705 1.0044.18
ATOM 1751 CA LYSB 11 46.965 14.280136.274 1.0044.30 ATOM 1752 CB LYSB 11 48.459 13.948136.278 1.0048.22
ATOM 1753 CG LYSB 11 49.402 15.035136.785 1.0051.00
ATOM 1754 CD LYSB 11 50.848 14.559136.638 1.0057.05
ATOM 1755 CE LYSB 11 51.885 15.606137.047 1.0063.96
ATOM 1756 NZ LYSB 11 51.892 15.916138.507 1.0067.87 ATOM 1757 C LYSB 11 46.691 15.518135.435 1.0043.20
ATOM 1758 O LYSB 11 46.882 15.518134.214 1.0042.35
ATOM 1759 N LEUB 12 46.230 16.575136.090 1.0040.09
ATOM 1760 C A LEUB 12 45.944 17.827135.415 1.0038.07
ATOM 1761 CB LEUB 12 44.705 18.475136.018 1.0031.15 ATOM 1762 CG LEUB 12 44.381 19.870135.500 1.0032.34
ATOM 1763 CD1LEUB 12 44.109 19.826134.005 1.0033.72
ATOM 1764 CD2 LEUB 12 43.17520.405136.268 1.0030.34
ATOM 1765 C LEUB 12 47.113 18.802135.531 1.0041.63 ATOM 17660 LEUB 12 47.481 19.470134.565 1.0040.43
ATOM 1767 N ASPB 13 47.680 18.889136.726 1.0043.09
ATOM 1768 CA ASPB 13 48.792 19.796137.004 1.0043.24
ATOM 1769 CB ASPB 13 48.24521.145137.491 1.0041.95 ATOM 1770 CG ASPB 13 49.20022.314137.248 1.0041.07
ATOM 1771 OD1ASPB 13 50.40922.111137.030 1.0036.83
ATOM 1772 OD2 ASPB 13 48.72623.468137.291 1.0048.74
ATOM 1773 C ASPB 13 49.475 19.089138.162 1.0047.37
ATOM 17740 ASPB 13 49.125 17.958138.490 1.0046.14 ATOM 1775 N GLUB 14 50.443 19.747138.788 1.0051.16
ATOM 1776 CA GLUB 14 51.116 19.150139.929 1.0052.15
ATOM 1777 CB GLUB 14 52.380 19.938140.281 1.0058.06
ATOM 1778 CG GLUB 14 53.521 19.729139.293 1.0065.68
ATOM 1779 CD GLUB 14 53.843 18.248139.089 1.0072.99 ATOM 1780 OE1 GLUB 14 53.997 17.519140.100 1.0075.77
ATOM 1781 OE2GLUB 14 53.947 17.816137.917 1.0076.23
ATOM 1782 C GLUB 14 50.172 19.107141.128 1.0049.86
ATOM 1783 O GLUB 14 49.55020.114141.467 1.0044.95
ATOM 1784 N GLY B 15 50.066 17.923141.734 1.0049.72 ATOM 1785 CA GLY B 15 49.220 17.710142.894 1.0045.92
ATOM 1786 C GLY B 15 47.740 17.906142.635 1.0046.90
ATOM 1787 O GLY B 15 46.939 18.019143.576 1.0047.35
ATOM 1788 N VAL B 16 47.363 17.934141.362 1.0045.17
ATOM 1789 CA VAL B 16 45.967 18.159141.003 1.0041.46 ATOM 1790 CB VAL B 16 45.777 19.603140.492 1.0038.99
ATOM 1791 CG1VALB 16 44.314 19.868140.155 1.0039.44
ATOM 1792 CG2VALB 16 46.281 20.563141.522 1.0036.03
ATOM 1793 C VAL B 16 45.525 17.178139.930 1.0043.38
ATOM 17940 VAL B 16 46.000 17.219138.781 1.0040.91 ATOM 1795 N TYRB 17 44.601 16.304140.308 1.0039.50
ATOM 1796 CA TYRB 17 44.093 15.290139.402 1.0036.27
ATOM 1797 CB TYRB 17 44.284 13.91 140.040 1.0039.98
ATOM 1798 CG TYRB 17 45.731 13.486140.157 1.0040.33
ATOM 1799 CD1TYRB 17 46.610 14.117141.049 1.0044.15 ATOM 1800 CE1 TYRB 17 47.976 13.759141.100 1.0044.85
ATOM 1801 CD2TYRB 17 46.236 12.487139.324 1.0040.78
ATOM 1802 CE2 TYRB 17 47.577 12.124139.363 1.0048.41
ATOM 1803 CZ TYRB 17 48.440 12.762140.247 1.0048.81 ATOM 1804 OH TYRB 17 49.763 12.396140.243 1.0053.18
ATOM 1805 C TYRB 17 42.625 15.523139.102 1.0035.10
ATOM 1806 O TYRB 17 41.925 16.129139.906 1.0034.35
ATOM 1807 N VALB 18 42.165 15.069137.937 1.0034.04 ATOM 1808 CA VALB 18 40.755 15.194137.568 1.0033.73
ATOM 1809 CB VALB 18 40.563 15.742136.117 1.0035.07
ATOM 1810 CGI VALB 18 39.079 15.789135.776 1.0031.83
ATOM 1811 CG2VALB 18 41.184 17.137135.966 1.0033.53
ATOM 1812 C VALB 18 40.187 13.775137.606 1.0036.15 ATOM 1813 O VALB 18 40.774 12.875136.999 1.0038.43
ATOM 1814 N HIS B 19 39.086 13.549138.332 1.0032.64
ATOM 1815 CA HIS B 19 38.483 12.214138.345 1.0029.96
ATOM 1816 CB HIS B 19 38.233 11.676139.789 1.0029.68
ATOM 1817 CG HIS B 19 37.356 12.540140.663 1.0030.48 ATOM 1818 CD2 HIS B 19 37.671 13.493141.580 1.0027.12
ATOM 1819 ND1 HIS B 19 35.980 12.414140.705 1.0031.70
ATOM 1820 CE1HISB 19 35.487 13.244141.610 1.0025.05
ATOM 1821 NE2HISB 19 36.492 13.909142.153 1.0030.76
ATOM 1822 C HIS B 19 37.200 12.311137.537 1.0033.03 ATOM 1823 O HIS B 19 36.419 13.249137.687 1.0035.68
ATOM 1824 N THR B 20 37.021 11.381136.615 1.0031.84
ATOM 1825 CA THR B 20 35.829 11.406135.796 1.0033.87
ATOM 1826 CB THR B 20 36.174 11.587134.297 1.0033.53
ATOM 1827 OG1THRB 20 37.056 12.715134.133 1.0036.17 ATOM 1828 CG2THRB 20 34.850 11.848133.493 1.0027.92
ATOM 1829 C THR B 20 35.045 10.118135.969 1.0033.19
ATOM 1830 O THR B 20 35.589 9.029135.812 1.0036.77
ATOM 1831 N SERB 21 33.772 10.244136.303 1.0033.55
ATOM 1832 CA SERB 21 32.935 9.072136.481 1.0033.04 ATOM 1833 CB SERB 21 32.389 9.021137.899 1.0031.67
ATOM 1834 OG SERB 21 31.758 10.238138.239 1.0030.04
ATOM 1835 C SERB 21 31.852 9.271135.463 1.0036.58
ATOM 1836 O SERB 21 31.689 10.391134.957 1.0038.68
ATOM 1837 N PHE B 22 31.103 8.219135.142 1.0039.81 ATOM 1838 CA PHE B 22 30.099 8.359134.100 1.0037.71
ATOM 1839 CB PHEB 22 30.559 7.614132.846 1.0038.10
ATOM 1840 CG PHEB 22 31.938 7.992132.377 1.0031.85
ATOM 1841 CD1PHEB 22 33.073 7.540133.050 1.0034.31 ATOM 1842 CD2 PHEB 22 32.098 8.833131.289 1.0030.69
ATOM 1843 CE1 PHEB 22 34.359 7.935132.645 1.0033.08
ATOM 1844 CE2 PHEB 22 33.372 9.232130.874 1.0027.27
ATOM 1845 CZ PHEB 22 34.508 8.787131.555 1.0033.57 ATOM 1846 C PHEB 22 28.693 7.911134.429 1.0043.35
ATOM 1847 O PHEB 22 28.476 7.082135.303 1.0041.26
ATOM 1848 N GLUB 23 27.745 8.468133.688 1.0043.34
ATOM 1849 CA GLUB 23 26.337 8.145133.837 1.0051.49
ATOM 1850 CB GLUB 23 25.676 9.086134.841 1.0057.38 ATOM 1851 CG GLUB 23 25.850 8.664136.288 1.0068.94
ATOM 1852 CD GLUB 23 25.091 7.393136.607 1.0076.78
ATOM 1853 OE1 GLUB 23 23.863 7.388136.368 1.0080.79
ATOM 1854 OE2GLUB 23 25.710 6.411137.091 1.0078.19
ATOM 1855 C GLUB 23 25.584 8.223132.517 1.0053.60 ATOM 1856 O GLUB 23 25.943 8.991131.618 1.0049.17
ATOM 1857 N GLU B 24 24.549 7.405132.398 1.0053.69
ATOM 1858 CA GLUB 24 23.721 7.401131.208 1.0062.69
ATOM 1859 CB GLUB 24 23.255 5.973130.902 1.0066.76
ATOM 1860 CG GLUB 24 22.038 5.881129.978 1.0077.38 ATOM 1861 CD GLU B 24 22.266 6.456128.583 1.0080.90
ATOM 1862 OE1GLUB 24 23.137 5.923127.854 1.0079.98
ATOM 1863 OE2 GLUB 24 21.564 7.434128.219 1.0082.31
ATOM 1864 C GLU B 24 22.524 8.316131.474 1.0065.24
ATOM 1865 O GLUB 24 21.618 7.963132.236 1.0066.27 ATOM 1866 N VAL B 25 22.529 9.504130.872 1.0066.80
ATOM 1867 CA VALB 25 21.416 10.424131.069 1.0070.68
ATOM 1868 CB VALB 25 21.874 11.892131.282 1.0071.06
ATOM 1869 CGI VALB 25 22.814 11.973132.460 1.0071.04
ATOM 1870 CG2VALB 25 22.519 12.430130.038 1.0078.53 ATOM 1871 C VALB 25 20.452 10.365129.897 1.0071.19
ATOM 1872 O VALB 25 20.839 10.459128.729 1.0070.17
ATOM 1873 N ASNB 26 19.186 10.190130.246 1.0072.55
ATOM 1874 CA ASNB 26 18.094 10.087129.295 1.0073.43
ATOM 1875 CB ASNB 26 16.773 10.287130.053 1.0077.36 ATOM 1876 CG ASNB 26 15.573 9.756129.299 1.0078.82
ATOM 1877 OD1 ASNB 26 15.312 10.151128.161 1.0080.02
ATOM 1878 ND2ASNB 26 14.827 8.854129.939 1.0078.18
ATOM 1879 C ASNB 26 18.214 11.090128.137 1.0071.88 ATOM 1880 O ASNB 26 17.989 12.293128.309 1.0068.20
ATOM 1881 N GLY B 27 18.590 10.584126.963 1.0070.63
ATOM 1882 CA GLY B 27 18.704 11.437125.790 1.0067.31
ATOM 1883 C GLY B 27 20.079 11.926125.359 1.0065.01 ATOM 1884 O GLY B 27 20.264 12.295124.198 1.0064.18
ATOM 1885 N TRPB 28 21.045 11.939126.266 1.0060.46
ATOM 1886 CA TRPB 28 22.366 12.419125.894 1.0059.84
ATOM 1887 CB TRPB 28 22.807 13.561126.811 1.0066.83
ATOM 1888 CG TRPB 28 21.879 14.732126.838 1.0075.16 ATOM 1889 CD2 TRPB 28 22.044 15.968126.131 1.0077.66
ATOM 1890 CE2 TRPB 28 20.929 16.776126.441 1.0078.45
ATOM 1891 CE3TRPB 28 23.026 16.470125.265 1.0076.83
ATOM 1892 CD1 TRPB 28 20.705 14.837127.527 1.0074.31
ATOM 1893 NE1TRPB 28 20.130 16.061127.296 1.0077.27 ATOM 1894 CZ2 TRPB 28 20.767 18.065125.916 1.0078.67
ATOM 1895 CZ3TRPB 28 22.867 17.751124.743 1.0077.49
ATOM 1896 CH2 TRPB 28 21.745 18.533125.072 1.0078.56
ATOM 1897 C TRPB 28 23.425 11.338125.928 1.0054.13
ATOM 1898 O TRPB 28 24.620 11.627125.834 1.0050.53 ATOM 1899 N GLY B 29 23.004 10.092126.063 1.0046.64
ATOM 1900 CA GLY B 29 23.989 9.028126.116 1.0045.66
ATOM 1901 C GLYB 29 24.834 9.124127.378 1.0040.75
ATOM 1902 O GLYB 29 24.359 9.655128.380 1.0043.02
ATOM 1903 N VAL B 30 26.075 8.632127.319 1.0037.97 ATOM 1904 CA VALB 30 26.983 8.631128.462 1.0034.29
ATOM 1905 CB VALB 30 28.083 7.574128.293 1.0040.57
ATOM 1906 CGI VALB 30 29.008 7.577129.499 1.0049.25
ATOM 1907 CG2VALB 30 27.460 6.197128.123 1.0046.45
ATOM 1908 C VALB 30 27.658 9.980128.661 1.0039.12 ATOM 1909 O VALB 30 28.513 10.384127.862 1.0034.23
ATOM 1910 N VALB 31 27.282 10.652129.744 1.0035.18
ATOM 1911 CA VALB 31 27.812 11.962130.109 1.0038.14
ATOM 1912 CB VALB 31 26.654 12.855130.572 1.0041.67
ATOM 1913 CGI VALB 31 27.155 14.198131.060 1.0041.98 ATOM 1914 CG2 VALB 31 25.692 13.019129.427 1.0040.07
ATOM 1915 C VALB 31 28.841 11.842131.233 1.0036.45
ATOM 1916 O VALB 31 28.625 11.096132.193 1.0032.52
ATOM 1917 N PROB 32 30.008 12.519131.095 1.0033.08 ATOM 1918 CD PROB 32 30.526 13.289129.939 1.0030.72
ATOM 1919 CA PROB 32 31.014 12.435132.156 1.0031.85
ATOM 1920 CB PROB 32 32.310 12.716131.405 1.0035.18
ATOM 1921 CG PROB 32 31.841 13.851130.458 1.0033.21 ATOM 1922 C PROB 32 30.746 13.501133.222 1.0033.63
ATOM 1923 O PROB 32 30.025 14.485132.966 1.0029.03
ATOM 1924 N LYSB 33 31.321 13.271134.403 1.0027.65
ATOM 1925 CA LYSB 33 31.272 14.186135.543 1.0028.36
ATOM 1926 CB LYSB 33 30.361 13.662136.660 1.0033.39 ATOM 1927 CG LYSB 33 30.403 14.424137.986 1.0028.12
ATOM 1928 CD LYSB 33 29.962 15.888137.897 1.0030.18
ATOM 1929 CE LYSB 33 30.159 16.590139.232 1.0028.64
ATOM 1930 NZ LYSB 33 31.590 16.511139.691 1.0020.12
ATOM 1931 C LYSB 33 32.708 14.281136.057 1.0029.85 ATOM 1932 O LYSB 33 33.292 13.296136.513 1.0028.94
ATOM 1933 N HIS B 34 33.280 15.471135.954 1.0028.53
ATOM 1934 CA HIS B 34 34.639 15.689136.413 1.0026.17
ATOM 1935 CB HIS B 34 35.352 16.685135.511 1.0027.79
ATOM 1936 CG HIS B 34 35.256 16.355134.060 1.0033.68 ATOM 1937 CD2 HIS B 34 34.689 17.030133.034 1.0031.72
ATOM 1938 ND1 HIS B 34 35.791 15.203133.521 1.0035.22
ATOM 1939 CE1HISB 34 35.559 15.187132.216 1.0035.58
ATOM 1940 NE2HISB 34 34.892 16.283131.896 1.0039.57
ATOM 1941 C HISB 34 34.586 16.280137.832 1.0029.41 ATOM 1942 O HISB 34 33.685 17.059138.178 1.0026.86
ATOM 1943 N GLYB 35 35.570 15.873138.617 1.0027.71
ATOM 1944 CA GLYB 35 35.756 16.332139.974 1.0029.93
ATOM 1945 C GLYB 35 37.271 16.364140.048 1.0030.42
ATOM 1946 O GLYB 35 37.938 15.930139.095 1.0032.15 ATOM 1947 N LEUB 36 37.827 16.881141.142 1.0030.30
ATOM 1948 CA LEUB 36 39.274 16.928141.302 1.0027.08
ATOM 1949 CB LEUB 36 39.754 18.375141.426 1.0029.02
ATOM 1950 CG LEUB 36 39.418 19.398140.352 1.0028.50
ATOM 1951 CD1LEUB 36 40.00620.748140.766 1.0029.88 ATOM 1952 CD2 LEU B 36 39.975 18.954139.036 1.0028.93
ATOM 1953 C LEUB 36 39.719 16.226142.589 1.0033.63
ATOM 1954 O LEUB 36 38.919 15.965143.480 1.0031.87
ATOM 1955 N VALB 37 41.011 15.929142.648 1.0033.16 ATOM 1956 CA VALB 37 41.649 15.382143.832 1.0037.31
ATOM 1957 CB VALB 37 42.119 13.936143.682 1.0039.14
ATOM 1958 CGI VALB 37 42.991 13.568144.889 1.0041.06
ATOM 1959 CG2 VALB 37 40.918 12.992143.625 1.0034.55 ATOM 1960 C VALB 37 42.880 16.268143.975 1.0038.96
ATOM 1961 O VALB 37 43.714 16.327143.058 1.0032.96
ATOM 1962 N VALB 38 42.975 16.979145.100 1.0039.03
ATOM 1963 CA VALB 38 44.103 17.874145.349 1.0042.86
ATOM 1964 CB VALB 38 43.635 19.270145.808 1.0041.96 ATOM 1965 CGI VALB 38 44.81920.170145.939 1.0037.75
ATOM 1966 CG2VALB 38 42.612 19.843144.830 1.0040.27
ATOM 1967 C VALB 38 45.023 17.312146.433 1.0047.00
ATOM 1968 O VALB 38 44.563 16.926147.520 1.0045.75
ATOM 1969 N LEUB 39 46.319 17.269146.141 1.0047.55 ATOM 1970 CA LEUB 39 47.297 16.747147.100 1.0047.63
ATOM 1971 CB LEUB 39 48.400 15.965146.390 1.0044.39
ATOM 1972 CG LEUB 39 47.947 14.934145.370 1.0048.55
ATOM 1973 CD1LEUB 39 49.141 14.097144.980 1.0054.58
ATOM 1974 CD2LEUB 39 46.861 14.057145.952 1.0051.54 ATOM 1975 C LEUB 39 47.968 17.857147.890 1.0050.06
ATOM 1976 O LEUB 39 48.396 18.855147.322 1.0049.71
ATOM 1977 N VALB 40 48.029 17.687149.208 1.0052.98
ATOM 1978 CA VALB 40 48.712 18.632150.074 1.0055.63
ATOM 1979 CB VALB 40 47.735 19.563150.881 1.0057.33 ATOM 1980 CGI VALB 40 46.93720.436149.937 1.0057.95
ATOM 1981 CG2VALB 40 46.801 18.756151.739 1.0061.79
ATOM 1982 C VAL B 40 49.511 17.744151.021 1.0058.47
ATOM 1983 O VALB 40 48.931 16.950151.768 1.0055.43
ATOM 1984 N ASNB 41 50.838 17.842150.937 1.0059.21 ATOM 1985 CA ASNB 41 51.755 17.065151.774 1.0061.77
ATOM 1986 CB ASNB 41 52.107 17.872153.041 1.0063.67
ATOM 1987 CG ASNB 41 50.878 18.308153.833 1.0067.41
ATOM 1988 OD1ASNB 41 50.160 17.484154.413 1.0065.38
ATOM 1989 ND2 ASNB 41 50.631 19.614153.856 1.0067.88 ATOM 1990 C ASNB 41 51.295 15.650152.160 1.0063.27
ATOM 1991 O ASNB 41 50.865 15.402153.284 1.0063.26
ATOM 1992 N ALAB 42 51.389 14.712151.228 1.0061.27
ATOM 1993 CA ALAB 42 50.986 13.331151.516 1.0062.56 ATOM 1994 CB ALAB 42 51.860 12.753152.623 1.0063.08
ATOM 1995 C ALAB 42 49.516 13.105151.874 1.0060.53
ATOM 1996 O ALAB 42 49.126 11.986152.209 1.0061.21
ATOM 1997 N GLUB 43 48.708 14.153151.826 1.0058.59 ATOM 1998 CA GLUB 43 47.294 14.014152.116 1.0058.12
ATOM 1999 CB GLUB 43 46.855 15.050153.134 1.0062.62
ATOM 2000 CG GLUB 43 47.583 15.010154.443 1.0070.18
ATOM 2001 CD GLUB 43 47.039 16.044155.398 1.0073.96
ATOM 2002 OE1GLUB 43 47.014 17.243155.040 1.0076.82 ATOM 2003 OE2GLUB 43 46.632 15.656156.508 1.0079.26
ATOM 2004 C GLUB 43 46.570 14.280150.804 1.0054.95
ATOM 2005 O GLUB 43 47.183 14.732149.837 1.0056.99
ATOM 2006 N ALAB 44 45.267 14.020150.765 1.0050.78
ATOM 2007 CA ALAB 44 44.500 14.263149.551 1.0044.83 ATOM 2008 CB ALAB 44 44.473 13.010148.689 1.0046.50
ATOM 2009 C ALAB 44 43.081 14.703149.865 1.0046.76
ATOM 2010 O ALAB 44 42.428 14.178150.773 1.0043.35
ATOM 2011 N TYRB 45 42.602 15.693149.132 1.0041.84
ATOM 2012 CA TYRB 45 41.237 16.127149.341 1.0042.56 ATOM 2013 CB TYRB 45 41.168 17.614149.696 1.0044.11
ATOM 2014 CG TYRB 45 41.762 17.958151.041 1.0050.12
ATOM 2015 CD1TYRB 45 43.136 17.897151.243 1.0051.38
ATOM 2016 CE1TYRB 45 43.688 18.163152.480 1.0052.34
ATOM 2017 CD2TYRB 45 40.945 18.301152.127 1.0050.29 ATOM 2018 CE2 TYRB 45 41.493 18.574153.381 1.0050.28
ATOM 2019 CZ TYRB 45 42.871 18.499153.542 1.0054.29
ATOM 2020 OH TYRB 45 43.464 18.762154.754 1.0061.81
ATOM 2021 C TYRB 45 40.448 15.867148.067 1.0038.46
ATOM 2022 O TYRB 45 40.906 16.165146.975 1.0039.24 ATOM 2023 N LEUB 46 39.270 15.294148.206 1.0038.45
ATOM 2024 CA LEUB 46 38.437 15.054147.042 1.0041.42
ATOM 2025 CB LEUB 46 37.423 13.933147.291 1.0039.13
ATOM 2026 CG LEUB 46 37.851 12.609147.916 1.0038.45
ATOM 2027 CD1LEUB 46 36.668 11.615147.772 1.0034.81 ATOM 2028 CD2LEUB 46 39.088 12.060147.220 1.0036.79
ATOM 2029 C LEUB 46 37.648 16.333146.801 1.0038.12
ATOM 2030 O LEUB 46 37.167 16.956147.743 1.0037.37
ATOM 2031 N ILE B 47 37.528 16.726145.537 1.0037.91 ATOM 2032 CA ILEB 47 36.735 17.895145.186 1.0036.74
ATOM 2033 CB ILEB 47 37.516 18.875144.314 1.0041.11
ATOM 2034 CG2ILEB 47 36.62820.069143.989 1.0034.73
ATOM 2035 CGI ILEB 47 38.796 19.301145.045 1.0043.37 ATOM 2036 CDIELEB 47 38.537 19.988146.400 1.0043.92
ATOM 2037 C ILEB 47 35.605 17.283144.388 1.0034.87
ATOM 2038 O ILEB 47 35.755 17.012143.190 1.0035.45
ATOM 2039 N ASPB 48 34.494 17.051145.084 1.0030.09
ATOM 2040 CA ASPB 48 33.291 16.400144.576 1.0030.97 ATOM 2041 CB ASPB 48 32.955 16.819143.132 1.0034.02
ATOM 2042 CG ASPB 48 31.997 17.989143.084 1.0038.34
ATOM 2043 OD1ASPB 48 32.051 18.800144.023 1.0036.48
ATOM 2044 OD2ASPB 48 31.208 18.110142.115 1.0035.73
ATOM 2045 C ASPB 48 33.563 14.924144.617 1.0029.71 ATOM 2046 O ASPB 48 34.705 14.497144.425 1.0030.02
ATOM 2047 N THR B 49 32.524 14.150144.905 1.0029.40
ATOM 2048 CA THR B 49 32.664 12.712144.928 1.0032.06
ATOM 2049 CB THR B 49 31.763 12.054146.018 1.0032.35
ATOM 2050 OGl THR B 49 30.380 12.146145.625 1.0027.17 ATOM 2051 CG2THRB 49 31.939 12.739147.362 1.0037.83
ATOM 2052 C THR B 49 32.113 12.207143.588 1.0034.37
ATOM 2053 O THR B 49 31.243 12.863142.983 1.0030.14
ATOM 2054 N PROB 50 32.618 11.053143.107 1.0033.06
ATOM 2055 CD PROB 50 33.743 10.258143.631 1.0033.94 ATOM 2056 CA PROB 50 32.148 10.456141.870 1.0035.11
ATOM 2057 CB PROB 50 32.905 9.137141.837 1.0032.48
ATOM 2058 CG PROB 50 34.198 9.545142.373 1.0034.75
ATOM 2059 C PROB 50 30.667 10.255142.121 1.0037.37
ATOM 2060 O PROB 50 30.178 10.537143.221 1.0042.03 ATOM 2061 N PHEB 51 29.950 9.741141.137 1.0038.13
ATOM 2062 CA PHEB 51 28.512 9.556141.284 1.0038.08
ATOM 2063 CB PHEB 51 27.891 9.284139.903 1.0041.93
ATOM 2064 CG PHEB 51 26.399 9.343139.898 1.0051.11
ATOM 2065 CD1PHEB 51 25.740 10.557140.038 1.0053.66 ATOM 2066 CD2 PHEB 51 25.643 8.183139.805 1.0059.68
ATOM 2067 CE1PHEB 51 24.359 10.622140.086 1.0056.15
ATOM 2068 CE2PHEB 51 24.245 8.236139.854 1.0062.86
ATOM 2069 CZ PHEB 51 23.606 9.462139.995 1.0060.93 ATOM 2070 C PHEB 51 28.072 8.455142.265 1.0038.31
ATOM 2071 O PHEB 51 27.104 8.632143.006 1.0037.24
ATOM 2072 N THR B 52 28.768 7.321142.264 1.0033.97
ATOM 2073 CA THR B 52 28.395 6.207143.145 1.0036.63 ATOM 2074 CB THRB 52 28.304 4.865142.376 1.0037.96
ATOM 2075 OGl THRB 52 29.589 4.575141.804 1.0034.04
ATOM 2076 CG2THRB 52 27.254 4.934141.277 1.0040.38
ATOM 2077 C THRB 52 29.404 5.979144.269 1.0037.59
ATOM 2078 O THRB 52 30.543 6.449144.212 1.0037.06 ATOM 2079 N ALA B 53 28.975 5.213145.271 1.0039.05
ATOM 2080 CA ALAB 53 29.809 4.877146.410 1.0037.26
ATOM 2081 CB ALAB 53 29.006 4.042147.413 1.0036.92
ATOM 2082 C ALA B 53 31.011 4.073145.921 1.0037.11
ATOM 2083 O ALAB 53 32.151 4.295146.348 1.0030.00 ATOM 2084 N LYS B 54 30.741 3.126145.032 1.0038.76
ATOM 2085 CA LYSB 54 31.799 2.262144.517 1.0042.47
ATOM 2086 CB LYSB 54 31.199 1.197143.587 1.0049.19
ATOM 2087 CG LYSB 54 32.189 0.131143.140 1.0059.12
ATOM 2088 CD LYSB 54 31.504 -0.974142.342 1.0066.14 ATOM 2089 CE LYSB 54 30.402 -1.644143.165 1.0068.45
ATOM 2090 NZ LYSB 54 29.755 -2.777142.443 1.0073.44
ATOM 2091 C LYSB 54 32.903 3.068143.824 1.0039.29
ATOM 2092 O LYSB 54 34.078 2.839144.093 1.0037.41
ATOM 2093 N ASPB 55 32.545 4.016142.950 1.0040.14 ATOM 2094 CA ASPB 55 33.585 4.839142.303 1.0038.68
ATOM 2095 CB ASPB 55 33.018 5.753141.204 1.0037.90
ATOM 2096 CG ASPB 55 32.791 5.020139.889 1.0039.54
ATOM 2097 OD1ASPB 55 33.435 3.980139.675 1.0040.01
ATOM 2098 OD2ASPB 55 32.001 5.495139.052 1.0043.69 ATOM 2099 C ASPB 55 34.306 5.693143.337 1.0040.12
ATOM 2100 O ASPB 55 35.524 5.902143.236 1.0039.81
ATOM 2101 N THRB 56 33.550 6.197144.319 1.0039.04
ATOM 2102 CA THRB 56 34.127 7.018145.391 1.0037.21
ATOM 2103 CB THRB 56 33.043 7.435146.409 1.0033.65 ATOM 2104 OGl THRB 56 31.992 8.132145.729 1.0040.72
ATOM 2105 CG2 THRB 56 33.622 8.357147.482 1.0031.97
ATOM 2106 C THRB 56 35.194 6.152146.071 1.0035.28
ATOM 2107 O THRB 56 36.322 6.588146.328 1.0032.01 ATOM 2108 N GLUB 57 34.860 4.894146.324 1.0038.23
ATOM 2109 CA GLUB 57 35.844 4.022146.938 1.0042.71
ATOM 2110 CB GLUB 57 35.252 2.668147.284 1.0047.29
ATOM 2111 CG GLUB 57 36.247 1.827148.028 1.0050.70 ATOM 2112 CD GLUB 57 35.708 0.478148.368 1.0058.20
ATOM 2113 OE1GLUB 57 34.599 0.408148.949 1.0054.04
ATOM 2114 OE2GLUB 57 36.409 -0.507148.061 1.0061.72
ATOM 2115 C GLUB 57 37.048 3.798146.027 1.0042.34
ATOM 2116 O GLUB 57 38.198 3.912146.479 1.0040.81 ATOM 2117 N LYSB 58 36.808 3.457144.758 1.0037.97
ATOM 2118 CA LYSB 58 37.949 3.240143.864 1.0038.95
ATOM 2119 CB LYSB 58 37.527 2.966142.415 1.0040.27
ATOM 2120 CG LYSB 58 36.788 1.673142.110 1.0047.76
ATOM 2121 CD LYSB 58 36.654 1.563140.576 1.0054.51 ATOM 2122 CE LYSB 58 35.967 0.293140.092 1.0057.41
ATOM 2123 NZ LYSB 58 34.531 0.190140.484 1.0057.42
ATOM 2124 C LYSB 58 38.820 4.494143.862 1.0036.96
ATOM 2125 O LYSB 58 40.039 4.404143.813 1.0034.54
ATOM 2126 N LEUB 59 38.191 5.662143.932 1.0035.40 ATOM 2127 CA LEUB 59 38.952 6.919143.906 1.0040.65
ATOM 2128 CB LEUB 59 38.013 8.132143.810 1.0035.92
ATOM 2129 CG LEUB 59 38.767 9.448143.581 1.0033.21
ATOM 2130 CD1 LEUB 59 39.416 9.414142.186 1.0029.68
ATOM 2131 CD2LEUB 59 37.824 10.636143.680 1.0037.71 ATOM 2132 C LEU B 59 39.835 7.073145.135 1.0041.06
ATOM 2133 O LEUB 59 41.042 7.359145.020 1.0038.12
ATOM 2134 N VALB 60 39.228 6.894146.310 1.0036.27
ATOM 2135 CA VALB 60 39.959 7.011147.567 1.0040.41
ATOM 2136 CB VALB 60 39.024 6.770148.782 1.0040.64 ATOM 2137 CGI VALB 60 39.858 6.663150.054 1.0040.96
ATOM 2138 CG2VALB 60 37.987 7.916148.907 1.0037.79
ATOM 2139 C VALB 60 41.134 6.023147.659 1.0042.28
ATOM 2140 O VALB 60 42.251 6.399148.052 1.0043.04
ATOM 2141 N THRB 61 40.862 4.770147.290 1.0039.77 ATOM 2142 CA THRB 61 41.844 3.691147.338 1.0042.67
ATOM 2143 CB THRB 61 41.157 2.326147.031 1.0044.95
ATOM 2144 OGl THRB 61 40.234 1.995148.081 1.0045.33
ATOM 2145 CG2 THRB 61 42.185 1.219146.847 1.0038.21 ATOM 2146 C THRB 61 42.986 3.907146.350 1.0045.57
ATOM 2147 O THRB 61 44.127 3.558146.635 1.0050.76
ATOM 2148 N TRPB 62 42.673 4.468145.183 1.0044.54
ATOM 2149 CA TRPB 62 43.678 4.727144.152 1.0043.04 ATOM 2150 CB TRPB 62 43.045 5.419142.939 1.0047.08
ATOM 2151 CG TRPB 62 43.961 5.559141.758 1.0051.60
ATOM 2152 CD2 TRPB 62 44.884 6.628141.507 1.0050.87
ATOM 2153 CE2TRPB 62 45.529 6.346140.294 1.0049.14
ATOM 2154 CE3 TRPB 62 45.224 7.799142.197 1.0051.23 ATOM 2155 CD1TRPB 62 44.086 4.696140.714 1.0055.31
ATOM 2156 NE1 TRPB 62 45.026 5.163139.827 1.0053.71
ATOM 2157 CZ2TRPB 62 46.496 7.187139.748 1.0052.16
ATOM 2158 CZ3 TRPB 62 46.181 8.635141.656 1.0052.34
ATOM 2159 CH2 TRPB 62 46.808 8.325140.440 1.0053.41 ATOM 2160 C TRPB 62 44.748 5.628144.740 1.0043.13
ATOM 2161 O TRPB 62 45.944 5.427144.501 1.0039.29
ATOM 2162 N PHEB 63 44.321 6.622145.514 1.0041.27
ATOM 2163 CA PHEB 63 45.264 7.539146.130 1.0044.47
ATOM 2164 CB PHEB 63 44.602 8.894146.400 1.0045.88 ATOM 2165 CG PHEB 63 44.370 9.706145.143 1.0048.34
ATOM 2166 CD1PHEB 63 43.236 9.510144.362 1.0046.83
ATOM 2167 CD2PHEB 63 45.336 10.617144.709 1.0050.72
ATOM 2168 CE1PHEB 63 43.069 10.216143.156 1.0046.52
ATOM 2169 CE2PHEB 63 45.185 11.322143.515 1.0047.16 ATOM 2170 CZ PHEB 63 44.050 11.123142.736 1.0048.30
ATOM 2171 C PHEB 63 45.904 6.976147.399 1.0049.70
ATOM 2172 O PHEB 63 47.108 7.199147.656 1.0048.12
ATOM 2173 N VALB 64 45.123 6.233148.179 1.0045.50
ATOM 2174 CA VALB 64 45.659 5.628149.396 1.0047.10 ATOM 2175 CB VALB 64 44.557 4.872150.152 1.0045.54
ATOM 2176 CGI VALB 64 45.172 3.915151.186 1.0046.99
ATOM 2177 CG2VALB 64 43.636 5.895150.846 1.0042.29
ATOM 2178 C VALB 64 46.861 4.702149.140 1.0047.30
ATOM 2179 O VALB 64 47.910 4.866149.753 1.0044.96 ATOM 2180 N GLU B 65 46.725 3.760148.213 1.0050.59
ATOM 2181 CA GLUB 65 47.808 2.831147.922 1.0056.92
ATOM 2182 CB GLUB 65 47.307 1.732146.974 1.0058.37
ATOM 2183 CG GLUB 65 46.084 0.991147.555 1.0062.93 ATOM 2184 CD GLUB 65 45.581 -0.169146.703 1.0066.39
ATOM 2185 OE1GLUB 65 45.293 0.045145.502 1.0069.61
ATOM 2186 OE2GLUB 65 45.458 -1.293147.243 1.0062.80
ATOM 2187 C GLU B 65 49.051 3.520147.363 1.0059.34 ATOM 2188 O GLUB 65 50.096 2.889147.175 1.0060.48
ATOM 2189 N ARG B 66 48.937 4.823147.118 1.0060.42
ATOM 2190 CA ARG B 66 50.050 5.602146.600 1.0058.54
ATOM 2191 CB ARGB 66 49.610 6.439145.402 1.0057.12
ATOM 2192 CG ARGB 66 49.339 5.596144.173 1.0057.52 ATOM 2193 CD ARGB 66 49.051 6.431142.937 1.0056.51
ATOM 2194 NE ARGB 66 49.002 5.590141.740 1.0057.60
ATOM 2195 CZ ARGB 66 48.141 4.593141.546 1.0064.44
ATOM 2196 NH1ARGB 66 47.232 4.291142.470 1.0062.00
ATOM 2197 NH2ARGB 66 48.197 3.884140.423 1.0065.12 ATOM 2198 C ARG B 66 50.654 6.493147.673 1.0060.84
ATOM 2199 O ARGB 66 51.501 7.336147.389 1.0061.83
ATOM 2200 N GLYB 67 50.215 6.310148.912 1.0058.97
ATOM 2201 CA GLYB 67 50.781 7.097149.986 1.0058.87
ATOM 2202 C GLYB 67 50.046 8.363150.342 1.0059.27 ATOM 2203 O GLYB 67 50.585 9.205151.047 1.0059.17
ATOM 2204 N TYRB 68 48.822 8.523149.863 1.0061.71
ATOM 2205 CA TYRB 68 48.082 9.716150.208 1.0060.63
ATOM 2206 CB TYRB 68 47.696 10.504148.964 1.0060.18
ATOM 2207 CG TYRB 68 48.870 10.911148.115 1.0060.63 ATOM 2208 CD1TYRB 68 49.450 10.018147.220 1.0058.83
ATOM 2209 CE1TYRB 68 50.571 10.374146.480 1.0062.52
ATOM 2210 CD2TYRB 68 49.440 12.175148.247 1.0060.63
ATOM 2211 CE2TYRB 68 50.564 12.541147.514 1.0063.11
ATOM 2212 CZ TYRB 68 51.128 11.636146.631 1.0063.83 ATOM 2213 OH TYRB 68 52.257 11.986145.918 1.0063.26
ATOM 2214 C TYRB 68 46.836 9.375150.997 1.0064.37
ATOM 2215 O TYRB 68 45.908 8.757150.477 1.0071.56
ATOM 2216 N LYSB 69 46.834 9.775152.264 1.0062.02
ATOM 2217 CA LYSB 69 45.712 9.561153.167 1.0061.81 ATOM 2218 CB LYSB 69 46.184 9.787154.612 1.0069.74
ATOM 2219 CG LYSB 69 46.901 11.136154.804 1.0075.19
ATOM 2220 CD LYSB 69 47.726 11.215156.089 1.0075.83
ATOM 2221 CE LYSB 69 48.556 12.498156.090 1.0076.37 ATOM 2222 NZ LYSB 69 49.494 12.641157.240 1.0073.61
ATOM 2223 C LYSB 69 44.672 10.600152.774 1.0058.49
ATOM 2224 O LYSB 69 44.996 11.784152.657 1.0058.98
ATOM 2225 N ILE B 70 43.433 10.173152.562 1.0050.49 ATOM 2226 CA ILEB 70 42.405 11.114152.165 1.0051.75
ATOM 2227 CB ILEB 70 41.199 10.397151.533 1.0050.84
ATOM 2228 CG2E EB 70 40.166 11.426151.066 1.0048.37
ATOM 2229 CG1D EB 70 41.667 9.502150.381 1.0048.60
ATOM 2230 CD1 ILEB 70 42.571 10.192149.385 1.0045.74 ATOM 2231 C ILEB 70 41.956 11.893153.390 1.0054.50
ATOM 2232 O ILE B 70 41.301 11.350154.271 1.0057.55
ATOM 2233 N LYSB 71 42.292 13.175153.440 1.0051.74
ATOM 2234 CA LYSB 71 41.946 13.973154.594 1.0050.75
ATOM 2235 CB LYSB 71 43.035 15.018154.857 1.0052.68 ATOM 2236 CG LYSB 71 42.794 15.770156.156 1.0062.03
ATOM 2237 CD LYSB 71 43.959 16.646156.540 1.0070.44
ATOM 2238 CE LYSB 71 43.721 17.324157.883 1.0071.57
ATOM 2239 NZ LYSB 71 44.864 18.219158.239 1.0075.37
ATOM 2240 C LYSB 71 40.582 14.642154.576 1.0048.01 ATOM 2241 O LYSB 71 40.077 15.038155.622 1.0043.24
ATOM 2242 N GLYB 72 39.967 14.772153.406 1.0045.71
ATOM 2243 CA GLYB 72 38.656 15.405153.376 1.0039.40
ATOM 2244 C GLYB 72 38.001 15.429152.007 1.0036.63
ATOM 2245 O GLYB 72 38.652 15.221150.990 1.0040.12 ATOM 2246 N SERB 73 36.712 15.720152.004 1.0036.28
ATOM 2247 CA SERB 73 35.914 15.771150.800 1.0039.96
ATOM 2248 CB SERB 73 35.200 14.432150.626 1.0038.42
ATOM 2249 OG SERB 73 34.248 14.493149.599 1.0041.43
ATOM 2250 C SERB 73 34.882 16.890150.831 1.0040.44 ATOM 2251 O SERB 73 34.063 16.952151.751 1.0041.11
ATOM 2252 N ILE B 74 34.934 17.777149.834 1.0035.30
ATOM 2253 CA ILEB 74 33.952 18.854149.723 1.0035.49
ATOM 2254 CB ILEB 74 34.61820.261149.684 1.0036.04
ATOM 2255 CG2ILEB 74 35.70020.322148.619 1.0033.75 ATOM 2256 CGI ILE B 74 33.52621.308149.455 1.0039.64
ATOM 2257 CDIILEB 74 34.011 22.728149.450 1.0047.74
ATOM 2258 C ILE B 74 33.102 18.681148.455 1.0033.72
ATOM 2259 O ILE B 74 33.653 18.439147.386 1.0034.08 ATOM 2260 N SERB 75 31.775 18.776148.593 1.0032.17
ATOM 2261 CA SERB 75 30.841 18.655147.476 1.0029.78
ATOM 2262 CB SERB 75 29.570 17.866147.867 1.0027.06
ATOM 2263 OG SERB 75 29.836 16.495148.165 1.0026.55 ATOM 2264 C SERB 75 30.44520.064147.088 1.0033.78
ATOM 2265 O SERB 75 30.03220.847147.953 1.0031.81
ATOM 2266 N SERB 76 30.53520.376145.789 1.0032.10
ATOM 2267 CA SERB 76 30.22521.710145.282 1.0027.64
ATOM 2268 CB SERB 76 30.89821.912143.917 1.0035.40 ATOM 2269 OG SERB 76 30.35621.010142.976 1.0033.24
ATOM 2270 C SERB 76 28.75022.051145.195 1.0021.43
ATOM 2271 O SERB 76 28.411 23.219145.034 1.0025.20
ATOM 2272 N HISB 77 27.86521.057145.243 1.0024.31
ATOM 2273 CA HISB 77 26.40721.320145.297 1.0025.46 ATOM 2274 CB HISB 77 25.83721.950144.022 1.0028.61
ATOM 2275 CG HISB 77 25.78321.018142.868 1.0029.76
ATOM 2276 CD2HISB 77 24.87420.876141.878 1.0025.42
ATOM 2277 ND1 HIS B 77 26.80720.148142.582 1.0028.18
ATOM 2278 CE1 HIS B 77 26.533 19.508141.460 1.0027.03 ATOM 2279 NE2HISB 77 25.369 19.931141.015 1.0028.91
ATOM 2280 C HISB 77 25.691 20.034145.654 1.0026.45
ATOM 2281 O HISB 77 26.332 18.987145.713 1.0029.09
ATOM 2282 N PHEB 78 24.38720.106145.927 1.0031.82
ATOM 2283 CA PHEB 78 23.656 18.920146.390 1.0031.47 ATOM 2284 CB PHEB 78 22.347 19.318147.103 1.0025.55
ATOM 2285 CG PHEB 78 21.179 19.550146.188 1.0029.91
ATOM 2286 CD1PHEB 78 21.06320.723145.447 1.0029.37
ATOM 2287 CD2 PHE B 78 20.167 18.594146.093 1.0029.77
ATOM 2288 CE1PHEB 78 19.94620.953144.624 1.0028.12 ATOM 2289 CE2PHEB 78 19.048 18.797145.281 1.0033.23
ATOM 2290 CZ PHEB 78 18.934 19.993144.537 1.0031.88
ATOM 2291 C PHEB 78 23.343 17.759145.450 1.0029.09
ATOM 2292 O PHEB 78 23.157 16.628145.932 1.0029.85
ATOM 2293 N HISB 79 23.274 18.008144.140 1.0026.94 ATOM 2294 CA HISB 79 22.951 16.928143.192 1.0029.97
ATOM 2295 CB HISB 79 22.956 17.454141.731 1.0022.38
ATOM 2296 CG HISB 79 21.777 18.318141.423 1.0032.71
ATOM 2297 CD2 HIS B 79 20.583 18.441142.054 1.0032.56 ATOM 2298 ND1 HIS B 79 21.742 19.203140.370 1.0031.70
ATOM 2299 CE1 HIS B 79 20.587 19.841140.366 1.0033.52
ATOM 2300 NE2 HISB 79 19.863 19.396141.378 1.0034.98
ATOM 2301 C HISB 79 23.861 15.727143.383 1.0030.31 ATOM 2302 O HISB 79 25.037 15.882143.765 1.0030.59
ATOM 2303 N SERB 80 23.301 14.535143.152 1.0029.05
ATOM 2304 CA SERB 80 24.015 13.252143.335 1.0033.20
ATOM 2305 CB SERB 80 23.167 12.086142.810 1.0036.61
ATOM 2306 OG SERB 80 21.924 12.000143.480 1.0055.44 ATOM 2307 C SERB 80 25.382 13.133142.691 1.0031.70
ATOM 2308 O SERB 80 26.223 12.362143.160 1.0029.26
ATOM 2309 N ASPB 81 25.607 13.856141.593 1.0028.27
ATOM 2310 CA ASPB 81 26.898 13.753140.935 1.0033.83
ATOM 2311 CB ASPB 81 26.783 14.155139.457 1.0029.61 ATOM 2312 CG ASPB 81 26.321 15.5771 9.245 1.0035.42
ATOM 2313 OD1ASPB 81 25.635 16.205140.083 1.0030.37
ATOM 2314 OD2ASPB 81 26.636 16.062138.159 1.0036.36
ATOM 2315 C ASPB 81 28.032 14.471141.655 1.0035.66
ATOM 2316 O ASPB 81 29.206 14.373141.267 1.0035.10 ATOM 2317 N SERB 82 27.683 15.193142.712 1.0032.07
ATOM 2318 CA SERB 82 28.701 15.837143.530 1.0034.28
ATOM 2319 CB SERB 82 28.413 17.327143.701 1.0032.19
ATOM 2320 OG SERB 82 28.592 18.010142.481 1.0031.25
ATOM 2321 C SERB 82 28.714 15.206144.927 1.0035.32 ATOM 2322 O SERB 82 29.749 15.161145.593 1.0035.97
ATOM 2323 N THRB 83 27.557 14.720145.365 1.0032.83
ATOM 2324 CA THRB 83 27.425 14.184146.725 1.0029.37
ATOM 2325 CB THRB 83 26.212 14.809147.390 1.0032.52
ATOM 2326 OGl THRB 83 25.100 14.624146.517 1.0026.25 ATOM 2327 CG2THRB 83 26.413 16.332147.638 1.0033.72
ATOM 2328 C THRB 83 27.266 12.681146.859 1.0033.74
ATOM 2329 O THRB 83 27.086 12.164147.968 1.0034.96
ATOM 2330 N GLYB 84 27.301 11.991145.734 1.0033.47
ATOM 2331 CA GLYB 84 27.127 10.556145.723 1.0036.71 ATOM 2332 C GLYB 84 27.898 9.740146.741 1.0032.83
ATOM 2333 O GLYB 84 27.340 8.839147.340 1.0036.85
ATOM 2334 N GLYB 85 29.165 10.056146.956 1.0033.53
ATOM 2335 CA GLYB 85 29.948 9.262147.883 1.0035.75 ATOM 2336 C GLYB 85 29.928 9.666149.345 1.0036.13
ATOM 2337 O GLYB 85 30.584 9.016150.142 1.0034.86
ATOM 2338 N ILEB 86 29.183 10.710149.711 1.0038.84
ATOM 2339 CA ILEB 86 29.170 11.155151.111 1.0040.77 ATOM 2340 CB ILEB 86 28.305 12.417151.313 1.0038.64
ATOM 2341 CG2ILEB 86 28.177 12.723152.803 1.0042.27
ATOM 2342 CGI ILEB 86 28.953 13.619150.603 1.0035.47
ATOM 2343 CD1ILEB 86 28.137 14.878150.664 1.0039.15
ATOM 2344 C ILE B 86 28.729 10.094152.119 1.0038.49 ATOM 2345 O ILEB 86 29.376 9.927153.152 1.0042.80
ATOM 2346 N GLUB 87 27.653 9.373151.831 1.0036.55
ATOM 2347 CA GLUB 87 27.204 8.343152.770 1.0041.11
ATOM 2348 CB GLUB 87 25.981 7.593152.229 1.0044.01
ATOM 2349 CG GLUB 87 25.432 6.541153.192 1.0051.11 ATOM 2350 CD GLUB 87 24.225 5.798152.650 1.0049.42
ATOM 2351 OE1GLUB 87 23.190 6.433152.359 1.0059.59
ATOM 2352 OE2 GLUB 87 24.308 4.563152.521 1.0061.26
ATOM 2353 C GLUB 87 28.349 7.361153.017 1.0041.25
ATOM 2354 O GLUB 87 28.599 6.963154.153 1.0039.84 ATOM 2355 N TRPB 88 29.065 6.994151.954 1.0041.17
ATOM 2356 CA TRPB 88 30.175 6.062152.085 1.0038.21
ATOM 2357 CB TRPB 88 30.632 5.568150.716 1.0044.31
ATOM 2358 CG TRPB 88 31.697 4.534150.846 1.0042.30
ATOM 2359 CD2 TRPB 88 33.106 4.754150.763 1.0045.48 ATOM 2360 CE2 TRPB 88 33.736 3.518151.021 1.0045.54
ATOM 2361 CE3TRPB 88 33.897 5.877150.497 1.0039.93
ATOM 2362 CD1TRPB 88 31.529 3.213151.144 1.0046.54
ATOM 2363 NE1TRPB 88 32.750 2.595151.249 1.0049.08
ATOM 2364 CZ2 TRPB 88 35.118 3.374151.021 1.0043.29 ATOM 2365 CZ3TRPB 88 35.273 5.733150.498 1.0045.18
ATOM 2366 CH2TRPB 88 35.870 4.491150.757 1.0044.50
ATOM 2367 C TRPB 88 31.382 6.638152.832 1.0040.80
ATOM 2368 O TRPB 88 31.992 5.966153.679 1.0040.94
ATOM 2369 N LEUB 89 31.717 7.882152.521 1.0039.30 ATOM 2370 CA LEUB 89 32.825 8.578153.148 1.0035.15
ATOM 2371 CB LEUB 89 32.991 9.955152.499 1.0032.95
ATOM 2372 CG LEUB 89 33.383 9.927151.006 1.0039.91
ATOM 2373 CD1LEUB 89 33.259 11.330150.364 1.0033.38 ATOM 2374 CD2 LEUB 89 34.804 9.375150.895 1.0026.05
ATOM 2375 C LEUB 89 32.583 8.749154.654 1.0034.30
ATOM 2376 O LEUB 89 33.509 8.632155.458 1.0033.92
ATOM 2377 N ASNB 90 31.343 9.047155.018 1.0033.07 ATOM 2378 CA ASNB 90 31.003 9.255156.419 1.0034.64
ATOM 2379 CB ASNB 90 29.575 9.793156.551 1.0034.26
ATOM 2380 CG ASNB 90 29.446 11.233156.100 1.0033.28
ATOM 2381 OD1ASNB 90 30.442 11.897155.834 1.0031.08
ATOM 2382 ND2ASNB 90 28.217 11.728156.024 1.0029.44 ATOM 2383 C ASNB 90 31.134 7.945157.205 1.0039.00
ATOM 2384 O ASN B 90 31.618 7.945158.341 1.0044.49
ATOM 2385 N SERB 91 30.708 6.842156.582 1.0036.70
ATOM 2386 CA SERB 91 30.758 5.514157.187 1.0035.81
ATOM 2387 CB SERB 91 30.001 4.492156.313 1.0033.15 ATOM 2388 OG SERB 91 30.727 4.054155.184 1.0033.78
ATOM 2389 C SERB 91 32.203 5.070157.436 1.0041.97
ATOM 2390 O SERB 91 32.458 4.233158.294 1.0044.08
ATOM 2391 N ARGB 92 33.146 5.635156.691 1.0039.99
ATOM 2392 CA ARGB 92 34.563 5.329156.888 1.0038.69 ATOM 2393 CB ARGB 92 35.307 5.250155.546 1.0042.04
ATOM 2394 CG ARGB 92 34.854 4.145154.630 1.0046.97
ATOM 2395 CD ARGB 92 34.906 2.812155.337 1.0054.67
ATOM 2396 NE ARGB 92 34.484 1.722154.463 1.0066.91
ATOM 2397 CZ ARGB 92 35.251 1.162153.530 1.0071.76 ATOM 2398 NH1 ARG B 92 36.494 1.590153.345 1.0071.28
ATOM 2399 NH2 ARGB 92 34.770 0.179152.773 1.0073.35
ATOM 2400 C ARGB 92 35.159 6.460157.718 1.0036.93
ATOM 2401 O ARGB 92 36.384 6.546157.890 1.0036.85
ATOM 2402 N SERB 93 34.288 7.326158.236 1.0035.50 ATOM 2403 CA SERB 93 34.716 8.480159.024 1.0037.68
ATOM 2404 CB SERB 93 35.402 8.032160.336 1.0040.07
ATOM 2405 OG SERB 93 34.511 7.288161.159 1.0030.13
ATOM 2406 C SERB 93 35.643 9.446158.283 1.0039.99
ATOM 2407 O SERB 93 36.477 10.094158.905 1.0039.29 ATOM 2408 N ILE B 94 35.517 9.552156.957 1.0041.26
ATOM 2409 CA ILEB 94 36.380 10.483156.215 1.0040.53
ATOM 2410 CB ILEB 94 36.582 10.022154.754 1.0042.62
ATOM 2411 CG2ILEB 94 37.360 11.067153.988 1.0035.71 ATOM 2412 CGI ILEB 94 37.310 8.675154.743 1.0042.84
ATOM 2413 CD1 ILEB 94 37.381 8.017153.372 1.0043.05
ATOM 2414 C ILE B 94 35.689 11.841156.260 1.0037.49
ATOM 2415 O ILEB 94 34.540 11.961155.877 1.0037.93 ATOM 2416 N PROB 95 36.389 12.892156.713 1.0037.64
ATOM 2417 CD PROB 95 37.804 12.950157.108 1.0039.76
ATOM 2418 CA PROB 95 35.797 14.231156.805 1.0038.68
ATOM 2419 CB PROB 95 36.992 15.082157.206 1.0042.55
ATOM 2420 CG PROB 95 37.784 14.109158.072 1.0039.60 ATOM 2421 C PROB 95 35.109 14.744155.534 1.0041.14
ATOM 2422 O PROB 95 35.765 14.914154.504 1.0040.55
ATOM 2423 N THRB 96 33.793 14.973155.611 1.0040.04
ATOM 2424 CA THRB 96 33.031 15.490154.475 1.0043.57
ATOM 2425 CB THRB 96 31.830 14.575154.096 1.0046.08 ATOM 2426 OGl THRB 96 30.990 14.364155.238 1.0040.62
ATOM 2427 CG2THRB 96 32.337 13.228153.543 1.0040.24
ATOM 2428 C THRB 96 32.530 16.907154.757 1.0044.81
ATOM 2429 O THRB 96 32.075 17.217155.864 1.0041.94
ATOM 2430 N TYR B 97 32.641 17.767153.744 1.0041.03 ATOM 2431 CA TYRB 97 32.236 19.168153.844 1.0036.23
ATOM 2432 CB TYRB 97 33.46620.087153.721 1.0034.96
ATOM 2433 CG TYRB 97 34.614 19.790154.670 1.0036.23
ATOM 2434 CD1TYRB 97 35.380 18.630154.525 1.0035.22
ATOM 2435 CE1TYRB 97 36.417 18.343155.404 1.0045.69 ATOM 2436 CD2 TYRB 97 34.91920.663155.727 1.0039.05
ATOM 2437 CE2 TYR B 97 35.95720.390156.618 1.0040.23
ATOM 2438 CZ TYRB 97 36.703 19.220156.447 1.0047.04
ATOM 2439 OH TYRB 97 37.735 18.913157.302 1.0049.69
ATOM 2440 C TYRB 97 31.261 19.551152.737 1.0039.60 ATOM 2441 O TYRB 97 31.379 19.073151.613 1.0040.39
ATOM 2442 N ALA B 98 30.30420.412153.061 1.0038.72
ATOM 2443 CA ALAB 98 29.33920.929152.088 1.0038.91
ATOM 2444 CB ALAB 98 28.163 19.963151.908 1.0039.91
ATOM 2445 C ALAB 98 28.85822.248152.682 1.0040.15 ATOM 2446 O ALAB 98 28.90722.422153.890 1.0039.55
ATOM 2447 N SERB 99 28.425 23.189151.855 1.0036.40
ATOM 2448 CA SERB 99 27.94524.457152.390 1.0039.32
ATOM 2449 CB SERB 99 27.59625.430151.266 1.0031.01 ATOM 2450 OG SERB 99 26.34425.090150.717 1.0029.36
ATOM 2451 C SERB 99 26.66724.192153.195 1.0039.51
ATOM 2452 O SERB 99 26.07623.106153.108 1.0035.15
ATOM 2453 N GLUB 100 26.24225.203153.957 1.0041.81 ATOM 2454 CA GLUB 100 25.03825.110154.771 1.0042.88
ATOM 2455 CB GLUB 100 24.76626.401155.549 1.0045.99
ATOM 2456 CG GLUB 100 25.86926.805156.494 1.0059.33
ATOM 2457 CD GLUB 100 25.42227.875157.477 1.0064.45
ATOM 2458 OE1 GLUB 100 24.96428.959157.044 1.0068.50 ATOM 2459 OE2 GLUB 100 25.531 27.624158.692 1.0067.71
ATOM 2460 C GLUB 100 23.88924.899153.838 1.0038.68
ATOM 2461 O GLUB 100 22.99924.108154.126 1.0039.92
ATOM 2462 N LEUB 101 23.911 25.623152.718 1.0033.53
ATOM 2463 CA LEUB 101 22.83025.512151.749 1.0036.88 ATOM 2464 CB LEUB 101 22.98926.536150.616 1.0036.39
ATOM 2465 CG LEUB 101 22.73928.000151.017 1.0038.38
ATOM 2466 CD1 LEUB 101 22.95228.931149.831 1.0037.48
ATOM 2467 CD2LEUB 101 21.29528.144151.529 1.0035.59
ATOM 2468 C LEUB 101 22.78024.105151.192 1.0032.73 ATOM 24690 LEUB 101 21.70723.509151.088 1.0035.33
ATOM 2470 N THRB 102 23.94223.563150.863 1.0030.71
ATOM 2471 CA THRB 102 23.98622.224150.320 1.0034.46
ATOM 2472 CB THRB 102 25.39421.867149.927 1.0034.96
ATOM 2473 OGl THRB 102 25.86622.860149.003 1.0037.51 ATOM 2474 CG2 THRB 102 25.41220.490149.260 1.0027.75
ATOM 2475 C THRB 102 23.41221.158151.267 1.0037.63
ATOM 2476 O THRB 102 22.58920.330150.847 1.0032.73
ATOM 2477 N ASNB 103 23.81621.174152.539 1.0034.48
ATOM 2478 CA ASNB 103 23.25620.196153.474 1.0032.95 ATOM 2479 CB ASNB 103 23.88720.310154.854 1.0032.95
ATOM 2480 CG ASNB 103 25.256 19.747154.882 1.0037.47
ATOM 2481 OD1 ASNB 103 25.524 18.738154.223 1.0035.82
ATOM 2482 ND2 ASNB 103 26.13620.359155.658 1.0039.00
ATOM 2483 C ASNB 103 21.751 20.328153.615 1.0033.20 ATOM 24840 ASNB 103 21.062 19.327153.724 1.0031.41
ATOM 2485 N GLUB 104 21.24421.558153.603 1.0034.50
ATOM 2486 C A GLU B 104 19.79821.799153.738 1.0037.74
ATOM 2487 CB GLU B 104 19.52723.302153.618 1.0049.19 ATOM 2488 CG GLUB 104 18.56023.910154.629 1.0062.92
ATOM 2489 CD GLUB 104 17.111 23.501154.430 1.0070.77
ATOM 2490 OE1 GLUB 104 16.83022.285154.462 1.0078.68
ATOM 2491 OE2 GLUB 104 16.25324.404154.254 1.0070.33 ATOM 2492 C GLUB 104 19.09821.055152.605 1.0039.57
ATOM 24930 GLUB 104 18.14620.297152.819 1.0039.65
ATOM 2494 N LEUB 105 19.59721.272151.391 1.0036.36
ATOM 2495 CA LEUB 105 19.04820.641150.198 1.0034.36
ATOM 2496 CB LEUB 105 19.67921.266148.949 1.0031.72 ATOM 2497 CG LEUB 105 19.36222.768148.855 1.0037.64
ATOM 2498 CD1LEUB 105 20.10023.407147.680 1.0036.84
ATOM 2499 CD2 LEUB 105 17.86522.966148.709 1.0037.87
ATOM 2500 C LEUB 105 19.219 19.116150.211 1.0030.25
ATOM 2501 O LEUB 105 18.288 18.381149.830 1.0029.85 ATOM 2502 N LEUB 106 20.383 18.627150.640 1.0030.51
ATOM 2503 CA LEUB 106 20.560 17.181150.715 1.0030.30
ATOM 2504 CB LEUB 106 21.950 16.839151.239 1.0031.05
ATOM 2505 CG LEUB 106 23.111 17.041150.249 1.0032.12
ATOM 2506 CD1LEUB 106 24.426 16.811150.967 1.0032.86 ATOM 2507 CD2 LEUB 106 22.971 16.076149.092 1.0024.24
ATOM 2508 C LEU B 106 19.463 16.662151.676 1.0037.06
ATOM 2509 O LEUB 106 18.708 15.748151.351 1.0036.38
ATOM 2510 N LYS B 107 19.358 17.286152.846 1.0037.29
ATOM 2511 CA LYSB 107 18.361 16.896153.844 1.0040.07 ATOM 2512 CB LYSB 107 18.313 17.907154.988 1.0045.95
ATOM 2513 CG LYS B 107 17.294 17.523156.088 1.0049.02
ATOM 2514 CD LYSB 107 16.915 18.708156.975 1.0054.81
ATOM 2515 CE LYSB 107 16.066 19.723156.202 1.0059.93
ATOM 2516 NZ LYSB 107 14.750 19.149155.723 1.0063.42 ATOM 2517 C LYS B 107 16.951 16.777153.295 1.0041.44
ATOM 2518 O LYS B 107 16.317 15.735153.412 1.0038.76
ATOM 2519 N LYS B 108 16.438 17.853152.709 1.0045.02
ATOM 2520 CA LYSB 108 15.075 17.825152.208 1.0043.67
ATOM 2521 CB LYSB 108 14.668 19.225151.751 1.0053.05 ATOM 2522 CG LYSB 108 13.241 19.381151.236 1.0057.77
ATOM 2523 CD LYSB 108 12.96720.845150.818 1.0064.24
ATOM 2524 CE LYSB 108 13.17321.859151.969 1.0063.98
ATOM 2525 NZ LYSB 108 14.58321.936152.476 1.0060.14 ATOM 2526 C LYS B 108 14.943 16.825151.076 1.0044.93
ATOM 25270 LYS B 108 13.857 16.328150.779 1.0042.05
ATOM 2528 N ASPB 109 16.067 16.498150.461 1.0043.23
ATOM 2529 CA ASPB 109 16.046 15.560149.355 1.0045.14 ATOM 2530 CB ASPB 109 17.127 15.981148.356 1.0050.29
ATOM 2531 CG ASPB 109 16.959 15.338147.012 1.0055.66
ATOM 2532 OD1 ASPB 109 15.841 15.445146.467 1.0057.11
ATOM 2533 OD2 ASPB 109 17.941 14.746146.498 1.0056.34
ATOM 2534 C ASPB 109 16.257 14.112149.859 1.0044.54 ATOM 2535 O ASPB 109 16.439 13.192149.069 1.0039.10
ATOM 2536 N GLYB 110 16.221 13.919151.180 1.0039.68
ATOM 2537 CA GLYB 110 16.403 12.584151.735 1.0039.50
ATOM 2538 C GLYB 110 17.807 12.016151.565 1.0038.49
ATOM 2539 O GLYB 110 18.009 10.793151.515 1.0037.12 ATOM 2540 N LYSB 111 18.796 12.895151.488 1.0035.34
ATOM 2541 CA LYSB 111 20.168 12.428151.306 1.0040.01
ATOM 2542 CB LYSB 111 20.808 13.114150.088 1.0039.34
ATOM 2543 CG LYS B 111 20.110 12.817148.765 1.0038.34
ATOM 2544 CD LYSB 111 20.217 11.363148.398 1.0039.93 ATOM 2545 CE LYSB 111 19.604 11.093147.032 1.0043.66
ATOM 2546 NZ LYS B 111 18.112 11.197147.010 1.0041.14
ATOM 2547 C LYSB 111 21.041 12.667152.515 1.0035.11
ATOM 2548 O LYS B 111 20.819 13.609153.272 1.0035.02
ATOM 2549 N VALB 112 22.035 11.805152.693 1.0035.53 ATOM 2550 CA VAL B 112 22.968 11.967153.799 1.0038.51
ATOM 2551 CB VALB 112 23.935 10.769153.909 1.0037.77
ATOM 2552 CGI VALB 112 25.006 11.066154.947 1.0039.52
ATOM 2553 CG2 VALB 112 23.154 9.515154.294 1.0041.16
ATOM 2554 C VALB 112 23.785 13.250153.597 1.0039.81 ATOM 2555 O VALB 112 24.298 13.513152.493 1.0037.29
ATOM 2556 N GLN B 113 23.927 14.030154.671 1.0039.23
ATOM 2557 CA GLN B 113 24.648 15.305154.620 1.0035.82
ATOM 2558 CB GLNB113 24.004 16.315155.570 1.0038.52
ATOM 2559 CG GLNB113 22.507 16.451155.411 1.0039.31 ATOM 2560 CD GLNB 113 21.890 17.363156.471 1.0051.15
ATOM 2561 OE1 GLNB 113 20.678 17.358156.672 1.0057.98
ATOM 2562 NE2 GLNB 113 22.719 18.156157.135 1.0046.70
ATOM 2563 C GLNB 113 26.126 15.215154.967 1.0038.51 ATOM 2564 O GLNB 113 26.580 14.259155.604 1.0033.33
ATOM 2565 N ALAB 114 26.872 16.225154.521 1.0032.23
ATOM 2566 CA ALAB 114 28.283 16.309154.792 1.0034.77
ATOM 2567 CB ALAB 114 28.848 17.518154.086 1.0029.88 ATOM 2568 C ALAB 114 28.350 16.492156.321 1.0038.36
ATOM 2569 O ALAB 114 27.506 17.147156.894 1.0031.64
ATOM 2570 N THRB 115 29.353 15.935156.977 1.0042.05
ATOM 2571 CA THRB 115 29.437 16.071158.430 1.0044.54
ATOM 2572 CB THRB 115 30.406 15.021158.993 1.0041.81 ATOM 2573 OGl THRB 115 31.747 15.339158.611 1.0046.95
ATOM 2574 CG2 THRB 115 30.081 13.684158.415 1.0029.74
ATOM 2575 C THRB 115 29.855 17.493158.886 1.0047.20
ATOM 25760 THRB 115 29.462 17.952159.961 1.0047.56
ATOM 2577 N ASNB 116 30.636 18.184158.056 1.0048.13 ATOM 2578 CA ASNB 116 31.115 19.545158.339 1.0042.87
ATOM 2579 CB ASNB 116 32.635 19.593158.144 1.0044.41
ATOM 2580 CG ASNB 116 33.360 18.574158.995 1.0044.84
ATOM 2581 OD1 ASNB 116 33.614 18.798160.186 1.0043.65
ATOM 2582 ND2 ASNB 116 33.670 17.428158.402 1.0041.48 ATOM 2583 C ASNB 116 30.44920.556157.391 1.0043.69
ATOM 25840 ASNB 116 30.36620.325156.186 1.0042.30
ATOM 2585 N SERB 117 29.99821.682157.931 1.0042.76
ATOM 2586 CA SERB 117 29.32422.708157.138 1.0045.09
ATOM 2587 CB SERB 117 27.92022.919157.688 1.0045.85 ATOM 2588 OG SERB 117 27.23023.889156.936 1.0057.16
ATOM 2589 C SERB 117 30.06624.063157.090 1.0047.73
ATOM 2590 O SERB 117 31.071 24.274157.775 1.0048.34
ATOM 2591 N PHEB 118 29.57624.973156.258 1.0045.79
ATOM 2592 CA PHEB 118 30.17626.298156.137 1.0045.38 ATOM 2593 CB PHEB 118 31.57626.213155.469 1.0047.46
ATOM 2594 CG PHEB 118 31.56325.678154.045 1.0047.20
ATOM 2595 CD1 PHEB 118 31.14426.471152.983 1.0048.89
ATOM 2596 CD2 PHEB 118 31.93224.364153.779 1.0047.91
ATOM 2597 CE1 PHEB 118 31.08825.959151.681 1.0049.22 ATOM 2598 CE2 PHEB 118 31.87823.846152.481 1.0048.70
ATOM 2599 CZ PHEB 118 31.45524.644151.434 1.0045.91
ATOM 2600 C PHEB 118 29.22527.178155.328 1.0046.91
ATOM 2601 O PHEB 118 28.35426.679154.612 1.0044.13 ATOM 2602 N SERB 119 29.37628.489155.456 1.0047.04
ATOM 2603 CA SERB 119 28.52929.423154.730 1.0048.21
ATOM 2604 CB SERB 119 27.351 29.880155.605 1.0049.12
ATOM 2605 OG SERB 119 27.81230.565156.765 1.0050.81 ATOM 2606 C SERB 119 29.36930.622154.343 1.0046.20
ATOM 2607 O SERB 119 30.57930.638154.562 1.0043.04
ATOM 2608 N GLYB 120 28.71931.627153.774 1.0048.05
ATOM 2609 CA GLYB 120 29.43732.825153.386 1.0053.42
ATOM 2610 C GLYB 120 30.08432.794152.010 1.0053.46 ATOM 2611 O GLYB 120 30.15431.752151.347 1.0052.82
ATOM 2612 N VALB 121 30.55833.962151.589 1.0051.06
ATOM 2613 CA VALB 121 31.20234.132150.301 1.0047.41
ATOM 2614 CB VALB 121 31.68735.583150.146 1.0047.24
ATOM 2615 CGI VALB 121 32.39735.783148.818 1.0045.74 ATOM 2616 CG2 VALB 121 30.47536.503150.220 1.0046.72
ATOM 2617 C VALB 121 32.33433.129150.147 1.0047.94
ATOM 2618 O VALB 121 32.301 32.299149.250 1.0047.45
ATOM 2619 N ASNB 122 33.34833.172150.994 1.0048.91
ATOM 2620 CA ASNB 122 34.361 32.148150.827 1.0050.39 ATOM 2621 CB ASNB 122 35.56832.662150.022 1.0055.81
ATOM 2622 CG ASNB 122 36.05534.004150.476 1.0057.53
ATOM 2623 OD1 ASNB 122 36.51534.161151.603 1.0059.45
ATOM 2624 ND2 ASN B 122 35.96534.991149.591 1.0058.77
ATOM 2625 C ASNB 122 34.77831.436152.093 1.0048.12 ATOM 2626 O ASNB 122 34.39431.803153.205 1.0045.22
ATOM 2627 N TYRB 123 35.54830.383151.913 1.0046.31
ATOM 2628 CA TYRB 123 35.96029.572153.035 1.0049.33
ATOM 2629 CB TYRB 123 34.81728.593153.346 1.0047.44
ATOM 2630 CG TYRB 123 35.141 27.501154.323 1.0052.27 ATOM 2631 CD1 TYRB 123 35.33527.768155.681 1.0055.87
ATOM 2632 CE1TYRB 123 35.64426.739156.576 1.0057.10
ATOM 2633 CD2 TYRB 123 35.26326.186153.887 1.0054.11
ATOM 2634 CE2 TYR B 123 35.57025.160154.762 1.0058.51
ATOM 2635 CZ TYRB 123 35.76025.439156.101 1.0057.26 ATOM 2636 OH TYRB 123 36.081 24.404156.940 1.0064.23
ATOM 2637 C TYRB 123 37.21928.831152.641 1.0049.23
ATOM 2638 O TYRB 123 37.261 28.221151.581 1.0048.66
ATOM 2639 N TRPB 124 38.25628.900153.465 1.0048.40 ATOM 2640 CA TRP B 124 39.478 28.184 153.151 1.00 53.86
ATOM 2641 CB TRP B 124 40.736 28.960 153.567 1.00 53.80
ATOM 2642 CG TRP B 124 40.912 30.185 152.773 1.00 61.17
ATOM 2643 CD2 TRP B 124 41.727 30.339 151.610 1.00 62.40 ATOM 2644 CE2 TRP B 124 41.496 31.642 151.106 1.00 63.38
ATOM 2645 CE3 TRP B 124 42.629 29.505 150.938 1.00 63.94
ATOM 2646 CD 1 TRP B 124 40.240 31.363 152.929 1.00 64.57
ATOM 2647 NE1 TRP B 124 40.585 32.242 151.933 1.00 64.49
ATOM 2648 CZ2 TRP B 124 42.138 32.135 149.956 1.00 65.18 ATOM 2649 CZ3 TRP B 124 43.271 29.997 149.789 1.0066.57
ATOM 2650 CH2 TRP B 124 43.018 31.302 149.313 1.00 62.86
ATOM 2651 C TRP B 124 39.458 26.842 153.839 1.00 53.53
ATOM 2652 O TRP B 124 39.675 26.746 155.041 1.00 55.09
ATOM 2653 N LEU B 125 39.170 25.808 153.064 1.0048.67 ATOM 2654 CA LEU B 125 39.143 24.457 153.573 1.0048.08
ATOM 2655 CB LEU B 125 38.639 23.529 152.474 1.00 45.84
ATOM 2656 CG LEU B 125 38.544 22.017 152.633 1.00 50.60
ATOM 2657 CD1 LEU B 125 37.566 21.643 153.746 1.00 52.41
ATOM 2658 CD2 LEU B 125 38.079 21.439 151.292 1.0044.40 ATOM 2659 C LEU B 125 40.591 24.151 153.965 1.00 48.61
ATOM 2660 O LEU B 125 40.842 23.325 154.840 1.00 49.15
ATOM 2661 N VAL B 126 41.539 24.831 153.319 1.0048.25
ATOM 2662 CA VAL B 126 42.972 24.678 153.615 1.0047.30
ATOM 2663 CB VAL B 126 43.606 23.504 152.843 1.0048.95 ATOM 2664 CGI VAL B 126 45.094 23.460 153.126 1.00 51.63
ATOM 2665 CG2 VAL B 126 42.979 22.187 153.251 1.0049.54
ATOM 2666 C VAL B 126 43.733 25.955 153.242 1.00 51.78
ATOM 2667 O VAL B 126 43.980 26.212 152.063 1.00 53.38
ATOM 2668 N LYS B 127 44.1 16 26.750 154.243 1.00 52.20 ATOM 2669 CA LYS B 127 44.826 28.017 154.021 1.00 56.03
ATOM 2670 CB LYS B 127 45.620 28.422 155.269 1.00 63.38
ATOM 2671 CG LYS B 127 44.852 28.438 156.579 1.00 65.61
ATOM 2672 CD LYS B 127 43.743 29.467 156.623 1.00 73.26
ATOM 2673 CE LYS B 127 43.076 29.433 158.005 1.00 74.24 ATOM 2674 NZ LYS B 127 41.914 30.358 158.132 1.00 73.08
ATOM 2675 C LYS B 127 45.792 28.015 152.839 1.00 56.66
ATOM 2676 O LYS B 127 46.758 27.253 152.819 1.00 58.88
ATOM 2677 N ASN B 128 45.536 28.885 151.866 1.00 56.61 ATOM 2678 CA ASN B 128 46.379 29.020 150.669 1.00 60.84
ATOM 2679 CB ASN B 128 47.821 29.388 151.047 1.00 65.66
ATOM 2680 CG ASN B 128 47.935 30.754 151.689 1.00 70.40
ATOM 2681 OD1 ASN B 128 47.355 31.734 151.216 1.00 72.72 ATOM 2682 ND2 ASN B 128 48.717 30.833 152.757 1.00 73.68
ATOM 2683 C ASN B 128 46.450 27.838 149.700 1.00 56.61
ATOM 2684 O ASN B 128 47.190 27.895 148.714 1.00 56.22
ATOM 2685 N LYS B 129 45.698 26.777 149.966 1.00 55.42
ATOM 2686 CA LYS B 129 45.722 25.607 149.088 1.00 53.61 ATOM 2687 CB LYS B 129 46.195 24.374 149.868 1.00 59.09
ATOM 2688 CG LYS B 129 47.541 24.525 150.576 1.00 60.64
ATOM 2689 CD LYS B 129 48.676 24.730 149.609 1.00 61.59
ATOM 2690 CE LYS B 129 50.003 24.768 150.343 1.00 63.90
ATOM 2691 NZ LYS B 129 50.236 23.512 151.106 1.00 62.35 ATOM 2692 C LYS B 129 44.359 25.305 148.450 1.0048.53
ATOM 2693 O LYS B 129 44.256 25.147 147.239 1.00 49.10
ATOM 2694 N ILE B 130 43.320 25.217 149.269 1.0043.83
ATOM 2695 CA ILE B 130 41.983 24.920 148.766 1.0042.49
ATOM 2696 CB ILE B 130 41.498 23.51 1 149.214 1.00 36.52 ATOM 2697 CG2 ILE B 130 40.145 23.219 148.627 1.00 39.44
ATOM 2698 CGI ILE B 130 42.494 22.436 148.799 1.00 36.50
ATOM 2699 CD1 ILE B 130 41.997 20.961 149.075 1.00 26.34
ATOM 2700 C ILE B 130 41.024 25.939 149.349 1.00 40.12
ATOM 2701 O ILE B 130 40.805 25.936 150.564 1.0040.92 ATOM 2702 N GLU B 131 40.493 26.829 148.504 1.00 36.53
ATOM 2703 CA GLU B 131 39.510 27.834 148.920 1.00 36.02
ATOM 2704 CB GLU B 131 39.904 29.238 148.454 1.00 38.45
ATOM 2705 CG GLU B 131 38.971 30.314 149.005 1.00 50.43
ATOM 2706 CD GLU B 131 39.021 31.661 148.261 1.00 59.80 ATOM 2707 OE1 GLU B 131 40.125 32.152 147.939 1.00 62.52
ATOM 2708 OE2 GLU B 131 37.937 32.246 148.025 1.00 59.18
ATOM 2709 C GLU B 131 38.161 27.492 148.279 1.00 38.50
ATOM 2710 O GLU B 131 38.102 26.995 147.151 1.00 39.67
ATOM 271 1 N VAL B 132 37.079 27.778 148.989 1.00 38.07 ATOM 2712 CA VAL B 132 35.730 27.524 148.494 1.00 38.39
ATOM 2713 CB VAL B 132 34.965 26.587 149.456 1.00 37.80
ATOM 2714 CGI VAL B 132 33.548 26.331 148.945 1.00 38.61
ATOM 2715 CG2 VAL B 132 35.708 25.305 149.598 1.00 34.38 ATOM 2716 C VALB 132 34.98228.857148.366 1.0038.36
ATOM 2717 O VALB 132 34.90929.618149.330 1.0036.07
ATOM 2718 N PHEB 133 34.43529.139147.178 1.0037.33
ATOM 2719 CA PHEB 133 33.711 30.393146.923 1.0032.48 ATOM 2720 CB PHEB 133 34.47631.214145.874 1.0034.69
ATOM 2721 CG PHEB 133 33.82332.534145.502 1.0036.37
ATOM 2722 CD1 PHEB 133 33.88533.634146.355 1.0035.14
ATOM 2723 CD2 PHE B 133 33.21232.694144.252 1.0037.40
ATOM 2724 CE1 PHEB 133 33.36434.873145.967 1.0037.73 ATOM 2725 CE2 PHEB 133 32.69033.926143.863 1.0036.00
ATOM 2726 CZ PHEB 133 32.76735.019144.720 1.0038.06
ATOM 2727 C PHEB 133 32.28430.173146.438 1.0035.12
ATOM 2728 O PHEB 133 32.041 29.330145.573 1.0036.77
ATOM 2729 N TYRB 134 31.36030.963146.986 1.0031.18 ATOM 2730 CA TYRB 134 29.94530.932146.641 1.0031.14
ATOM 2731 CB TYRB 134 29.09230.921147.929 1.0030.84
ATOM 2732 CG TYRB 134 27.611 30.989147.675 1.0033.00
ATOM 2733 CD 1 TYRB 134 26.96229.992146.941 1.0028.79
ATOM 2734 CE1 TYRB 134 25.60030.058146.687 1.0032.96 ATOM 2735 CD2 TYRB 134 26.85332.050148.146 1.0026.70
ATOM 2736 CE2 TYRB 134 25.471 32.119147.889 1.0025.65
ATOM 2737 CZ TYRB 134 24.85231.127147.161 1.0030.11
ATOM 2738 OH TYRB 134 23.48631.210146.867 1.0024.34
ATOM 2739 C TYRB 134 29.62632.188145.814 1.0033.32 ATOM 2740 O TYRB 134 29.49433.275146.349 1.0031.82
ATOM 2741 N PROB 135 29.50932.050144.487 1.0032.97
ATOM 2742 CD PROB 135 29.70630.839143.663 1.0035.77
ATOM 2743 CA PROB 135 29.20733.201143.631 1.0034.16
ATOM 2744 CB PROB 135 29.63332.699142.252 1.0033.55 ATOM 2745 CG PROB 135 29.11331.271142.310 1.0035.73
ATOM 2746 C PROB 135 27.72633.607143.638 1.0034.03
ATOM 2747 O PROB 135 27.37934.652143.112 1.0031.09
ATOM 2748 N GLYB 136 26.86632.772144.223 1.0034.10
ATOM 2749 CA GLYB 136 25.42633.045144.231 1.0033.19 ATOM 2750 C GLYB 136 24.63031.933143.540 1.0027.69
ATOM 2751 O GLYB 136 25.21531.072142.876 1.0031.30
ATOM 2752 N PROB 137 23.29831.935143.640 1.0030.36
ATOM 2753 CD PROB 137 22.36832.893144.270 1.0027.42 ATOM 2754 CA PRO B 137 22.556 30.855 142.975 1.00 29.37
ATOM 2755 CB PRO B 137 21.087 31.181 143.305 1.00 29.83
ATOM 2756 CG PRO B 137 21.192 31.978 144.645 1.00 25.13
ATOM 2757 C PRO B 137 22.810 30.865 141.466 1.00 31.09 ATOM 2758 O PRO B 137 23.248 31.880 140.903 1.00 31.51
ATOM 2759 N GLY B 138 22.540 29.734 140.819 1.00 31.80
ATOM 2760 CA GLY B 138 22.716 29.635 139.367 1.00 33.35
ATOM 2761 C GLY B 138 22.1 19 28.321 138.903 1.00 32.88
ATOM 2762 O GLY B 138 20.897 28.173 138.788 1.00 34.38 ATOM 2763 N HIS B 139 22.998 27.359 138.639 1.00 32.06
ATOM 2764 CA HIS B 139 22.593 26.003 138.247 1.00 29.68
ATOM 2765 CB HIS B 139 23.859 25.168 138.063 1.00 25.06
ATOM 2766 CG HIS B 139 23.608 23.708 138.064 1.00 32.85
ATOM 2767 CD2 HIS B 139 23.975 22.746 138.940 1.00 30.90 ATOM 2768 ND1 HIS B 139 22.835 23.086 137.109 1.00 37.96
ATOM 2769 CE1 HIS B 139 22.736 21.801 137.393 1.00 35.15
ATOM 27.70 NE2 HIS B 139 23.418 21.571 138.501 1.00 27.41
ATOM 2771 C HIS B 139 21.708 25.428 139.389 1.00 33.47
ATOM 2772 0 HIS B 139 20.720 24.698 139.156 1.00 28.90 ATOM 2773 N THR B 140 22.106 25.753 140.625 1.00 31.70
ATOM 2774 C A THR B 140 21.371 25.360 141.841 1.00 32.54
ATOM 2775 CB THR B 140 21.906 24.052 142.490 1.00 28.98
ATOM 2776 OGl THR B 140 23.313 24.165 142.700 1.00 29.03
ATOM 2777 CG2 THR B 140 21.591 22.826 141.604 1.00 31.22 ATOM 2778 C THR B 140 21.512 26.506 142.858 1.00 34.07
ATOM 2779 0 THR B 140 22.394 27.372 142.738 1.00 28.70
ATOM 2780 N PRO B 141 20.638 26.532 143.863 1.00 32.10
ATOM 2781 CD PRO B 141 19.530 25.605 144.119 1.0028.49
ATOM 2782 CA PRO B 141 20.675 27.585 144.887 1.00 34.53 ATOM 2783 CB PRO B 141 19.469 27.234 145.757 1.00 34.97
ATOM 2784 CG PRO B 141 18.523 26.546 144.740 1.00 37.86
ATOM 2785 C PRO B 141 21.970 27.646 145.706 1.00 33.32
ATOM 2786 0 PRO B 141 22.377 28.708 146.188 1.00 39.16
ATOM 2787 N ASP B 142 22.624 26.500 145.815 1.00 30.36 ATOM 2788 CA ASP B 142 23.804 26.332 146.651 1.00 30.58
ATOM 2789 CB ASP B 142 23.604 25.059 147.503 1.00 34.28
ATOM 2790 CG ASP B 142 23.424 23.812 146.626 1.00 31.68
ATOM 2791 OD1 ASP B 142 22.781 23.948 145.562 1.00 30.03 ATOM 2792 OD2ASPB 142 23.88722.715146.979 1.0028.38
ATOM 2793 C ASPB 142 25.12426.175145.966 1.0032.66
ATOM 27940 ASPB 142 26.14826.049146.651 1.0024.18
ATOM 2795 N ASN B 143 25.13426.160144.634 1.0029.55 ATOM 2796 CA ASNB 143 26.39025.884143.977 1.0029.93
ATOM 2797 CB ASN B 143 26.15225.812142.451 1.0030.41
ATOM 2798 CG ASNB 143 25.54227.080141.866 1.0034.58
ATOM 2799 OD1 ASNB 143 24.83627.013140.859 1.0035.01
ATOM 2800 ND2ASNB 143 25.83728.241142.467 1.0030.15 ATOM 2801 C ASNB 143 27.58526.769144.364 1.0030.02
ATOM 2802 O ASN B 143 27.47927.993144.400 1.0031.17
ATOM 2803 N VALB 144 28.70626.123144.684 1.0026.97
ATOM 2804 CA VALB 144 29.94326.826145.061 1.0032.34
ATOM 2805 CB VALB 144 30.37426.553146.551 1.0032.74 ATOM 2806 CGI VALB 144 29.22026.807147.474 1.0033.61
ATOM 2807 CG2 VALB 144 30.911 25.139146.722 1.0028.84
ATOM 2808 C VALB 144 31.04726.302144.153 1.0031.54
ATOM 2809 O VAL B 144 30.87225.265143.532 1.0030.07
ATOM 2810 N VAL B 145 32.171 27.015144.076 1.0032.50 ATOM 2811 CA VALB 145 33.30426.610143.249 1.0032.76
ATOM 2812 CB VALB 145 33.661 27.676142.177 1.0032.77
ATOM 2813 CGI VALB 145 32.44527.986141.366 1.0031.51
ATOM 2814 CG2 VALB 145 34.25928.946142.834 1.0028.13
ATOM 2815 C VAL B 145 34.505 26.459144.162 1.0034.15 ATOM 28160 VALB 145 34.50627.007145.270 1.0035.80
ATOM 2817 N VALB 146 35.52225.730143.710 1.0031.95
ATOM 2818 CA VALB 146 36.721 25.536144.512 1.0031.57
ATOM 2819 CB VALB 146 36.97424.045144.869 1.0029.54
ATOM 2820 CGI VALB 146 38.22223.926145.756 1.0034.45 ATOM 2821 CG2 VALB 146 35.78323.471145.603 1.0028.18
ATOM 2822 C VALB 146 37.91226.068143.752 1.0034.38
ATOM 28230 VAL B 146 38.14625.698142.601 1.0035.46
ATOM 2824 N TRPB 147 38.65926.948144.413 1.0035.41
ATOM 2825 CA TRPB 147 39.83827.604143.855 1.0034.53 ATOM 2826 CB TRPB 147 39.671 29.114144.050 1.0040.92
ATOM 2827 CG TRPB 147 40.871 29.957143.736 1.0042.91
ATOM 2828 CD2 TRP B 147 41.42030.238142.446 1.0045.21
ATOM 2829 CE2TRPB147 42.50731.119142.638 1.0045.00 ATOM 2830 CE3TRPB 147 41.09729.831141.143 1.0043.26
ATOM 2831 CD1 TRPB 147 41.62530.652144.630 1.0048.80
ATOM 2832 NE1 TRPB 147 42.60831.355143.982 1.0043.18
ATOM 2833 CZ2TRPB 147 43.27931.605141.578 1.0044.03 ATOM 2834 CZ3 TRP B 147 41.85830.314140.087 1.0038.43
ATOM 2835 CH2 TRPB 147 42.94031.195140.311 1.0045.95
ATOM 2836 C TRPB 147 41.14727.113144.493 1.0037.36
ATOM 2837 O TRPB 147 41.25927.057145.718 1.0034.37
ATOM 2838 N LEUB 148 42.11926.748143.659 1.0032.89 ATOM 2839 CA LEUB 148 43.42426.256144.122 1.0039.96
ATOM 2840 CB LEUB 148 43.76324.950143.409 1.0037.18
ATOM 2841 CG LEU B 148 42.63623.917143.434 1.0042.62
ATOM 2842 CD 1 LEUB 148 43.111 22.614142.765 1.0035.84
ATOM 2843 CD2 LEU B 148 42.20023.668144.891 1.0035.04 ATOM 2844 C LEU B 148 44.45027.337143.747 1.0045.56
ATOM 2845 O LEUB 148 45.03427.307142.666 1.0050.24
ATOM 2846 N PROB 149 44.70828.284144.660 1.0048.66
ATOM 2847 CD PROB 149 44.19228.317146.044 1.0045.51
ATOM 2848 CA PROB 149 45.64029.397144.447 1.0047.16 ATOM 2849 CB PRO B 149 45.67830.062145.821 1.0050.78
ATOM 2850 CG PROB 149 44.28429.796146.352 1.0048.81
ATOM 2851 C PRO B 149 47.021 29.025143.960 1.0048.84
ATOM 2852 O PRO B 149 47.60729.695143.123 1.0051.75
ATOM 2853 N GLUB 150 47.53327.940144.499 1.0053.32 ATOM 2854 CA GLUB 150 48.87027.465144.193 1.0056.15
ATOM 2855 CB GLUB 150 49.09326.240145.075 1.0061.23
ATOM 2856 CG GLUB 150 50.48325.731145.267 1.0069.70
ATOM 2857 CD GLUB 150 50.561 24.915146.550 1.0074.84
ATOM 2858 OE1 GLUB 150 50.57925.534147.639 1.0075.57 ATOM 2859 OE2 GLUB 150 50.56323.666146.476 1.0081.96
ATOM 2860 C GLUB 150 49.09427.178142.701 1.0056.80
ATOM 2861 O GLUB 150 50.18027.413142.170 1.0050.63
ATOM 2862 N ARGB 151 48.05326.698142.026 1.0057.91
ATOM 2863 CA ARGB 151 48.12926.379140.599 1.0053.82 ATOM 2864 CB ARGB 151 47.68724.933140.360 1.0058.29
ATOM 2865 CG ARGB 151 48.53923.919141.060 1.0063.82
ATOM 2866 CD ARGB 151 49.95524.085140.615 1.0064.60
ATOM 2867 NE ARGB 151 50.85623.240141.379 1.0074.71 ATOM 2868 CZ ARG B 151 52.175 23.245 141.227 1.00 78.49
ATOM 2869 NH 1 ARG B 151 52.732 24.057 140.333 1.00 79.76
ATOM 2870 NH2 ARG B 151 52.934 22.441 141.965 1.00 78.30
ATOM 2871 C ARG B 151 47.265 27.284 139.734 1.00 48.62 ATOM 2872 0 ARG B 151 47.344 27.227 138.51 1 1.0048.62
ATOM 2873 N LYS B 152 46.442 28.1 12 140.364 1.00 41.38
ATOM 2874 CA LYS B 152 45.534 28.982 139.636 1.00 41.53
ATOM 2875 CB LYS B 152 46.309 29.936 138.726 1.0042.40
ATOM 2876 CG LYS B 152 47.014 31.027 139.529 1.00 55.75 ATOM 2877 CD LYS B 152 47.834 31.979 138.679 1.00 58.25
ATOM 2878 CE LYS B 152 48.222 33.233 139.486 1.00 59.89
ATOM 2879 NZ LYS B 152 48.966 32.919 140.749 1.00 63.41
ATOM 2880 C LYS B 152 44.542 28.137 138.844 1.00 40.38
ATOM 2881 O LYS B 152 44.255 28.408 137.685 1.0041.25 ATOM 2882 N ILE B 153 44.016 27.109 139.508 1.00 38.47
ATOM 2883 CA ILE B 153 43.039 26.196 138.926 1.00 36.62
ATOM 2884 CB ILE B 153 43.533 24.728 139.061 1.00 32.54
ATOM 2885 CG2 ILE B 153 42.437 23.754 138.657 1.00 29.89
ATOM 2886 CGI ILE B 153 44.834 24.559 138.262 1.00 35.32 ATOM 2887 CD 1 ILE B 153 45.473 23.169 138.365 1.00 29.21
ATOM 2888 C ILE B 153 41.686 26.369 139.631 1.00 34.73
ATOM 2889 O ILE B 153 41.608 26.315 140.861 1.00 33.44
ATOM 2890 N LEU B 154 40.629 26.618 138.861 1.00 32.38
ATOM 2891 CA LEU B 154 39.285 26.774 139.428 1.00 35.80 ATOM 2892 CB LEU B 154 38.576 28.020 138.889 1.00 34.57
ATOM 2893 CG LEU B 154 37.163 28.307 139.465 1.00 36.69
ATOM 2894 CD 1 LEU B 154 37.253 28.754 140.953 1.00 37.84
ATOM 2895 CD2 LEU B 154 36.483 29.406 138.648 1.00 33.66
ATOM 2896 C LEU B 154 38.398 25.590 139.079 1.00 37.1 1 ATOM 2897 O LEU B 154 38.273 25.217 137.900 1.00 33.26
ATOM 2898 N PHE B 155 37.788 24.984 140.088 1.00 30.13
ATOM 2899 CA PHE B 155 36.844 23.908 139.791 1.00 32.84
ATOM 2900 CB PHE B 155 36.804 22.809 140.867 1.00 27.24
ATOM 2901 CG PHE B 155 35.786 21.746 140.570 1.00 28.26 ATOM 2902 CD 1 PHE B 155 35.926 20.936 139.449 1.00 27.31
ATOM 2903 CD2 PHE B 155 34.645 21.590 141.378 1.00 28.08
ATOM 2904 CE1 PHE B 155 34.956 19.984 139.131 1.00 26.97
ATOM 2905 CE2 PHE B 155 33.673 20.645 141.073 1.00 34.89 ATOM 2906 CZ PHE B 155 33.832 19.833 139.938 1.00 31.89
ATOM 2907 C PHE B 155 35.489 24.605 139.765 1.00 27.22
ATOM 2908 O PHE B 155 35.010 25.048 140.808 1.00 24.08
ATOM 2909 N GLY B 156 34.883 24.714 138.582 1.00 27.14 ATOM 2910 CA GLY B 156 33.597 25.393 138.448 1.00 25.10
ATOM 291 1 C GLY B 156 32.373 24.541 138.713 1.00 26.99
ATOM 2912 O GLY B 156 31.262 25.048 138.850 1.00 28.62
ATOM 2913 N GLY B 157 32.564 23.232 138.778 1.00 24.51
ATOM 2914 CA GLY B 157 31.439 22.353 139.025 1.00 31.68 ATOM 2915 C GLY B 157 30.412 22.441 137.917 1.00 31.48
ATOM 2916 0 GLY B 157 30.742 22.685 136.750 1.00 30.40
ATOM 2917 N CYS B 158 29.151 22.257 138.289 1.00 32.19
ATOM 2918 CA CYS B 158 28.061 22.306 137.334 1.00 32.88
ATOM 2919 CB CYS B 158 26.915 21.437 137.842 1.00 31.53 ATOM 2920 SG CYS B 158 27.598 19.840 138.353 1.00 30.92
ATOM 2921 C CYS B 158 27.610 23.731 137.087 1.00 33.95
ATOM 2922 O CYS B 158 26.685 23.969 136.310 1.00 35.57
ATOM 2923 N PHE B 159 28.283 24.685 137.728 1.00 34.78
ATOM 2924 CA PHE B 159 27.947 26.095 137.524 1.00 36.59 ATOM 2925 CB PHE B 159 28.504 26.950 138.677 1.00 36.52
ATOM 2926 CG PHE B 159 28.244 28.439 138.529 1.00 33.79
ATOM 2927 CD 1 PHE B 159 29.070 29.230 137.734 1.00 31.65
ATOM 2928 CD2 PHE B 159 27.179 29.047 139.209 1.00 28.16
ATOM 2929 CE1 PHE B 159 28.853 30.618 137.616 1.00 28.62 ATOM 2930 CE2 PHE B 159 26.948 30.430 139.102 1.00 30.78
ATOM 2931 CZ PHE B 159 27.790 31.222 138.303 1.00 32.26
ATOM 2932 C PHE B 159 28.513 26.577 136.170 1.00 37.62
ATOM 2933 O PHE B 159 27.880 27.352 135.451 1.00 37.82
ATOM 2934 N ILE B 160 29.708 26.112 135.833 1.00 34.33 ATOM 2935 CA ILE B 160 30.330 26.497 134.583 1.00 32.08
ATOM 2936 CB ILE B 160 31.832 26.209 134.620 1.00 26.87
ATOM 2937 CG2 ILE B 160 32.448 26.448 133.243 1.00 30.69
ATOM 2938 CGI ILE B 160 32.497 27.094 135.676 1.00 30.55
ATOM 2939 CD 1 ILE B 160 32.482 28.589 135.342 1.00 39.24 ATOM 2940 C ILE B 160 29.672 25.702 133.451 1.00 31.96
ATOM 2941 O ILE B 160 29.764 24.475 133.404 1.00 26.10
ATOM 2942 N LYS B 161 29.023 26.428 132.548 1.00 27.43
ATOM 2943 CA LYS B 161 28.293 25.855 131.429 1.00 34.86 ATOM 2944 CB LYS B 161 26.800 25.876 131.771 1.00 35.66
ATOM 2945 CG LYS B 161 26.404 24.925 132.918 1.00 37.93
ATOM 2946 CD LYS B 161 26.564 23.464 132.476 1.00 42.83
ATOM 2947 CE LYS B 161 26.104 22.473 133.553 1.00 38.94 ATOM 2948 NZ LYS B 161 24.664 22.619 133.863 1.00 38.55
ATOM 2949 C LYS B 161 28.598 26.723 130.197 1.00 36.31
ATOM 2950 O LYS B 161 27.846 27.641 129.857 1.00 35.41
ATOM 2951 N PRO B 162 29.712 26.436 129.511 1.00 34.99
ATOM 2952 CD PRO B 162 30.691 25.366 129.778 1.00 35.42 ATOM 2953 CA PRO B 162 30.132 27.193 128.334 1.00 33.58
ATOM 2954 CB PRO B 162 31.554 26.651 128.082 1.00 31.82
ATOM 2955 CG PRO B 162 31.968 26.055 129.403 1.00 31.27
ATOM 2956 C PRO B 162 29.266 27.088 127.072 1.00 37.56
ATOM 2957 O PRO B 162 29.216 28.025 126.274 1.00 32.98 ATOM 2958 N TYR B 163 28.563 25.972 126.906 1.00 37.22
ATOM 2959 CA TYR B 163 27.802 25.758 125.675 1.0040.53
ATOM 2960 CB TYR B 163 28.368 24.527 124.958 1.0040.17
ATOM 2961 CG TYR B 163 29.879 24.392 125.026 1.00 36.13
ATOM 2962 CD 1 TYR B 163 30.716 25.385 124.529 1.00 37.31 ATOM 2963 CE1 TYR B 163 32.105 25.286 124.659 1.00 48.33
ATOM 2964 CD2 TYR B 163 30.465 23.284 125.645 1.00 41.25
ATOM 2965 CE2 TYR B 163 31.848 23.174 125.779 1.0045.33
ATOM 2966 CZ TYR B 163 32.663 24.177 125.295 1.00 45.00
ATOM 2967 OH TYR B 163 34.031 24.098 125.51 1 1.00 54.80 ATOM 2968 C TYR B 163 26.308 25.571 125.815 1.0041.06
ATOM 2969 O TYR B 163 25.649 25.142 124.877 1.0044.01
ATOM 2970 N GLY B 164 25.766 25.896 126.978 1.00 43.57
ATOM 2971 CA GLY B 164 24.350 25.704 127.204 1.0043.53
ATOM 2972 C GLY B 164 24.194 25.450 128.683 1.0041.95 ATOM 2973 O GLY B 164 25.044 24.799 129.298 1.00 39.49
ATOM 2974 N LEU B 165 23.105 25.946 129.250 1.0041.53
ATOM 2975 CA LEU B 165 22.886 25.836 130.686 1.0043.18
ATOM 2976 CB LEU B 165 21.818 26.843 131.108 1.00 40.22
ATOM 2977 CG LEU B 165 22.233 28.287 130.794 1.00 41.85 ATOM 2978 CD 1 LEU B 165 21.103 29.210 131.222 1.0041.68
ATOM 2979 CD2 LEU B 165 23.540 28.654 131.502 1.00 31.41
ATOM 2980 C LEU B 165 22.574 24.446 131.253 1.0042.41
ATOM 2981 O LEU B 165 22.837 24.203 132.431 1.00 37.35 ATOM 2982 N GLYB 166 22.03623.548130.424 1.0036.27
ATOM 2983 CA GLYB 166 21.72522.203130.873 1.0037.12
ATOM 2984 C GLYB 166 20.37522.093131.562 1.0043.81
ATOM 2985 O GLYB 166 19.431 22.818131.233 1.0044.39 ATOM 2986 N ASNB 167 20.27621.185132.525 1.0045.46
ATOM 2987 CA ASNB 167 19.02520.980133.243 1.0047.93
ATOM 2988 CB ASNB 167 19.104 19.656134.019 1.0049.80
ATOM 2989 CG ASNB 167 17.857 19.373134.854 1.0057.34
ATOM 2990 OD1 ASNB 167 16.784 19.957134.649 1.0054.75 ATOM 2991 ND2ASNB167 17.993 18.447135.791 1.0062.72
ATOM 2992 C ASNB 167 18.74522.182134.155 1.0046.03
ATOM 2993 O ASNB 167 19.57222.544134.993 1.0047.61
ATOM 2994 N LEUB 168 17.58822.812133.960 1.0041.00
ATOM 2995 CA LEUB 168 17.19923.985134.739 1.0039.23 ATOM 2996 CB LEUB 168 16.49525.001133.847 1.0039.65
ATOM 2997 CG LEUB 168 17.24725.550132.641 1.0042.20
ATOM 2998 CD1 LEUB 168 16.34226.453131.834 1.0046.44
ATOM 2999 CD2 LEUB 168 18.44326.323133.126 1.0044.30
ATOM 3000 C LEUB 168 16.281 23.662135.910 1.0039.87 ATOM 3001 O LEUB 168 15.83924.575136.614 1.0043.50
ATOM 3002 N GLYB 169 15.99822.378136.122 1.0039.08
ATOM 3003 CA GLYB 169 15.11621.967137.209 1.0041.11
ATOM 3004 C GLYB 169 15.31922.692138.544 1.0040.59
ATOM 3005 O GLYB 169 14.36723.123139.181 1.0041.70 ATOM 3006 N ASPB 170 16.56922.852138.958 1.0040.02
ATOM 3007 CA ASPB 170 16.86323.502140.225 1.0038.85
ATOM 3008 CB ASPB 170 17.70322.559141.095 1.0040.16
ATOM 3009 CG ASPB 170 16.89521.371141.618 1.0038.13
ATOM 3010 OD1 ASPB 170 15.84421.648142.207 1.0037.19 ATOM 3011 OD2 ASPB 170 17.29220.182141.463 1.0034.98
ATOM 3012 C ASPB 170 17.56724.837140.071 1.0036.71
ATOM 3013 O ASPB 170 17.98525.434141.060 1.0036.84
ATOM 3014 N ALAB 171 17.68525.300138.828 1.0038.21
ATOM 3015 CA ALAB 171 18.34726.564138.495 1.0034.77 ATOM 3016 CB ALAB 171 18.57526.637136.970 1.0033.66
ATOM 3017 C ALAB 171 17.60927.822138.950 1.0035.44
ATOM 3018 O ALAB 171 16.39527.828139.104 1.0037.59
ATOM 3019 N ASNB 172 18.36528.890139.160 1.0035.77 ATOM 3020 CA ASNB 172 17.81830.186139.549 1.0036.96
ATOM 3021 CB ASNB 172 18.42030.647140.894 1.0034.02
ATOM 3022 CG ASNB 172 17.83331.982141.391 1.0036.55
ATOM 3023 OD1 ASNB 172 17.81632.261142.604 1.0039.38 ATOM 3024 ND2 ASNB 172 17.37332.815140.457 1.0030.25
ATOM 3025 C ASNB 172 18.27531.062138.392 1.0039.03
ATOM 3026 O ASNB 172 19.32031.719138.453 1.0039.37
ATOM 3027 N ILEB 173 17.47231.053137.330 1.0041.05
ATOM 3028 CA ILEB 173 17.79431.771136.102 1.0041.22 ATOM 3029 CB ILEB 173 16.76931.428134.968 1.0039.17
ATOM 3030 CG2 ILEB 173 15.62032.405134.954 1.0040.05
ATOM 3031 CGI ILEB 173 17.47231.488133.617 1.0043.20
ATOM 3032 CD 1 ILEB 173 18.57030.448133.463 1.0044.22
ATOM 3033 C ILEB 173 17.89333.272136.280 1.0037.52 ATOM 3034 O ILEB 173 18.67533.926135.604 1.0034.43
ATOM 3035 N GLUB 174 17.101 33.816137.197 1.0041.02
ATOM 3036 CA GLUB 174 17.12835.251137.445 1.0042.90
ATOM 3037 CB GLUB 174 15.96335.645138.370 1.0049.42
ATOM 3038 CG GLUB 174 14.52535.347137.870 1.0057.26 ATOM 3039 CD GLUB 174 14.16833.851137.786 1.0064.12
ATOM 3040 OE1 GLUB 174 14.511 33.079138.711 1.0068.83
ATOM 3041 OE2 GLUB 174 13.50333.443136.808 1.0065.97
ATOM 3042 C GLUB 174 18.46235.656138.106 1.0042.75
ATOM 3043 O GLUB 174 18.96936.764137.884 1.0042.49 ATOM 3044 N ALAB 175 19.04734.751138.895 1.0038.83
ATOM 3045 CA ALAB 175 20.28335.061139.620 1.0034.57
ATOM 3046 CB ALAB 175 20.25334.364140.999 1.0037.20
ATOM 3047 C ALAB 175 21.591 34.720138.922 1.0035.51
ATOM 3048 O ALAB 175 22.63335.359139.130 1.0030.30 ATOM 3049 N TRPB 176 21.53433.696138.096 1.0037.66
ATOM 3050 CA TRPB 176 22.71233.218137.410 1.0035.06
ATOM 3051 CB TRPB 176 22.30532.094136.450 1.0029.03
ATOM 3052 CG TRPB 176 23.37631.067136.262 1.0023.32
ATOM 3053 CD2 TRPB 176 23.19829.720135.822 1.0025.07 ATOM 3054 CE2 TRPB 176 24.48829.162135.650 1.0026.79
ATOM 3055 CE3 TRPB 176 22.07228.929135.548 1.0028.66
ATOM 3056 CD 1 TRPB 176 24.72931.268136.342 1.0022.74
ATOM 3057 NE1 TRPB 176 25.39830.130135.978 1.0027.85 ATOM 3058 CZ2 TRP B 176 24.689 27.842 135.218 1.00 25.39
ATOM 3059 CZ3 TRP B 176 22.263 27.620 135.1 16 1.00 26.23
ATOM 3060 CH2 TRP B 176 23.572 27.087 134.957 1.00 35.88
ATOM 3061 C TRP B 176 23.591 34.258 136.697 1.00 34.77 ATOM 3062 O TRP B 176 24.805 34.194 136.785 1.00 33.59
ATOM 3063 N PRO B 177 23.005 35.242 136.004 1.00 35.19
ATOM 3064 CD PRO B 177 21.618 35.638 135.730 1.00 32.55
ATOM 3065 CA PRO B 177 23.942 36.171 135.359 1.00 33.53
ATOM 3066 CB PRO B 177 23.004 37.090 134.549 1.00 32.25 ATOM 3067 CG PRO B 177 21.755 36.200 134.315 1.00 27.74
ATOM 3068 C PRO B 177 24.796 36.947 136.378 1.00 37.61
ATOM 3069 O PRO B 177 26.013 37.123 136.212 1.00 39.47
ATOM 3070 N LYS B 178 24.156 37.431 137.434 1.00 37.60
ATOM 3071 CA LYS B 178 24.885 38.174 138.457 1.00 35.96 ATOM 3072 CB LYS B 178 23.906 38.71 1 139.503 1.00 41.42
ATOM 3073 CG LYS B 178 22.810 39.534 138.851 1.00 56.34
ATOM 3074 CD LYS B 178 21.758 40.070 139.81 1 1.00 63.42
ATOM 3075 CE LYS B 178 20.668 40.808 139.008 1.00 69.97
ATOM 3076 NZ LYS B 178 19.541 41.317 139.843 1.00 73.08 ATOM 3077 C LYS B 178 25.937 37.279 139.108 1.00 33.67
ATOM 3078 O LYS B 178 27.086 37.713 139.347 1.00 29.65
ATOM 3079 N SER B 179 25.565 36.027 139.376 1.00 27.27
ATOM 3080 CA SER B 179 26.503 35.084 140.010 1.00 33.21
ATOM 3081 CB SER B 179 25.811 33.752 140.31 1 1.00 31.71 ATOM 3082 OG SER B 179 24.623 33.953 141.063 1.00 35.65
ATOM 3083 C SER B 179 27.694 34.827 139.105 1.00 35.00
ATOM 3084 O SER B 179 28.836 34.736 139.567 1.00 36.01
ATOM 3085 N ALA B 180 27.412 34.708 137.807 1.00 33.86
ATOM 3086 CA ALA B 180 28.443 34.463 136.805 1.00 33.96 ATOM 3087 CB ALA B 180 27.776 34.081 135.466 1.00 36.78
ATOM 3088 C ALA B 180 29.351 35.701 136.654 1.00 33.22
ATOM 3089 O ALA B 180 30.599 35.586 136.557 1.00 31.45
ATOM 3090 N LYS B 181 28.732 36.884 136.648 1.00 36.67
ATOM 3091 CA LYS B 181 29.490 38.138 136.567 1.00 36.06 ATOM 3092 CB LYS B 181 28.530 39.318 136.606 1.00 42.16
ATOM 3093 CG LYS B 181 29.173 40.653 136.940 1.00 47.44
ATOM 3094 CD LYS B 181 28.146 41.779 136.790 1.00 55.99
ATOM 3095 CE LYS B 181 28.627 43.095 137.401 1.00 59.53 ATOM 3096 NZ LYSB 181 29.95543.513136.907 1.0062.06
ATOM 3097 C LYSB 181 30.47838.199137.740 1.0038.92
ATOM 3098 O LYSB 181 31.68838.463137.564 1.0038.03
ATOM 3099 N LEUB 182 29.95937.934138.939 1.0038.61 ATOM 3100 CA LEUB 182 30.77337.912140.152 1.0038.73
ATOM 3101 CB LEUB 182 29.87337.590141.364 1.0040.91
ATOM 3102 CG LEUB 182 30.60237.500142.707 1.0046.97
ATOM 3103 CD1 LEUB 182 31.35038.802142.940 1.0047.63
ATOM 3104 CD2 LEUB 182 29.63037.195143.845 1.0047.21 ATOM 3105 C LEUB 182 31.92536.864140.025 1.0039.31
ATOM 3106 O LEUB 182 33.10237.191140.242 1.0042.51
ATOM 3107 N LEUB 183 31.58935.617139.672 1.0032.93
ATOM 3108 CA LEUB 183 32.611 34.580139.507 1.0033.20
ATOM 3109 CB LEUB 183 32.00233.285138.945 1.0030.43 ATOM 3110 CG LEUB 183 33.00232.112138.870 1.0031.89
ATOM 3111 CD1 LEUB 183 33.36831.699140.295 1.0028.26
ATOM 3112 CD2 LEUB 183 32.40330.904138.156 1.0025.79
ATOM 3113 C LEUB 183 33.68235.067138.537 1.0035.04
ATOM 3114 O LEUB 183 34.87435.007138.830 1.0039.33 ATOM 3115 N LYSB 184 33.25535.539137.367 1.0034.73
ATOM 3116 CA LYSB 184 34.21436.022136.372 1.0041.06
ATOM 3117 CB LYSB 184 33.48936.552135.131 1.0041.35
ATOM 3118 CG LYSB 184 34.43937.114134.068 1.0048.27
ATOM 3119 CD LYSB 184 33.68837.583132.819 1.0053.56 ATOM 3120 CE LYSB 184 34.65437.973131.706 1.0054.51
ATOM 3121 NZ LYSB 184 35.49336.797131.256 1.0060.61
ATOM 3122 C LYSB 184 35.16237.109136.914 1.0041.27
ATOM 3123 O LYSB 184 36.34837.119136.582 1.0036.74
ATOM 3124 N SERB 185 34.641 38.015137.747 1.0043.26 ATOM 3125 CA SERB 185 35.46539.087138.305 1.0044.49
ATOM 3126 CB SERB 185 34.60340.139139.006 1.0045.33
ATOM 3127 OG SERB 185 33.56940.611138.157 1.0055.48
ATOM 3128 C SERB 185 36.44438.531139.312 1.0044.65
ATOM 3129 O SERB 185 37.591 38.967139.374 1.0046.65 ATOM 3130 N LYSB 186 35.991 37.556140.092 1.0039.52
ATOM 3131 CA LYSB 186 36.82436.970141.141 1.0041.42
ATOM 3132 CB LYSB 186 35.92336.202142.139 1.0045.05
ATOM 3133 CG LYSB 186 36.67335.498143.274 1.0056.29 ATOM 3134 CD LYSB 186 37.471 36.485144.148 1.0063.03
ATOM 3135 CE LYSB 186 38.42935.780145.129 1.0064.65
ATOM 3136 NZ LYSB 186 37.74334.941146.154 1.0066.64
ATOM 3137 C LYSB 186 37.94736.072140.633 1.0041.52 ATOM 3138 O LYSB 186 39.07336.098141.154 1.0032.66
ATOM 3139 N TYRB 187 37.66335.284139.602 1.0041.78
ATOM 3140 CA TYRB 187 38.67834.373139.097 1.0045.80
ATOM 3141 CB TYRB 187 38.19232.928139.294 1.0048.81
ATOM 3142 CG TYRB 187 37.96732.581140.747 1.0045.91 ATOM 3143 CD1 TYRB 187 39.02332.582141.651 1.0047.56
ATOM 3144 CE1 TYRB 187 38.82032.308143.002 1.0047.61
ATOM 3145 CD2TYRB187 36.69332.291141.225 1.0047.99
ATOM 3146 CE2TYRB 187 36.47432.015142.575 1.0049.57
ATOM 3147 CZ TYRB 187 37.54332.029143.456 1.0048.72 ATOM 3148 OH TYRB 187 37.33231.797144.796 1.0051.12
ATOM 3149 C TYRB 187 39.09634.605137.647 1.0049.05
ATOM 3150 O TYRB 187 39.32533.649136.898 1.0042.10
ATOM 3151 N GLYB 188 39.19835.876137.263 1.0051.32
ATOM 3152 CA GLYB 188 39.60436.204135.912 1.0049.25 ATOM 3153 C GLYB 188 41.05435.825135.719 1.0050.63
ATOM 31540 GLYB 188 41.511 35.682134.591 1.0051.81
ATOM 3155 N LYSB 189 41.77535.654136.826 1.0050.08
ATOM 3156 CA LYSB 189 43.191 35.280136.790 1.0050.72
ATOM 3157 CB LYSB 189 43.93235.787138.047 1.0057.86 ATOM 3158 CG LYSB 189 44.013 37.319138.225 1.0065.23
ATOM 3159 CD LYSB 189 44.80837.701139.496 1.0065.74
ATOM 3160 CE LYSB 189 44.83539.214139.752 1.0065.31
ATOM 3161 NZ LYSB 189 45.501 39.959138.646 1.0064.65
ATOM 3162 C LYSB 189 43.36933.765136.699 1.0046.58 ATOM 3163 O LYSB 189 44.47633.252136.822 1.0045.90
ATOM 3164 N ALAB 190 42.26933.053136.503 1.0042.73
ATOM 3165 CA ALAB 190 42.29331.602136.386 1.0040.44
ATOM 3166 CB ALAB 190 40.86031.073136.181 1.0034.99
ATOM 3167 C ALAB 190 43.16631.148135.225 1.0040.87 ATOM 3168 O ALAB 190 43.08731.723134.130 1.0044.11
ATOM 3169 N LYS B 191 43.96930.109135.474 1.0039.98
ATOM 3170 CA LYSB 191 44.85829.481134.492 1.0036.90
ATOM 3171 CB LYS B 191 46.071 28.936135.213 1.0045.05 ATOM 3172 CG LYSB 191 47.11628.342134.322 1.0053.84
ATOM 3173 CD LYSB 191 48.391 28.170135.122 1.0059.96
ATOM 3174 CE LYSB 191 48.83429.524135.709 1.0064.39
ATOM 3175 NZ LYSB 191 50.10829.446136.500 1.0070.35 ATOM 3176 C LYSB 191 44.091 28.346133.795 1.0035.50
ATOM 31770 LYS B 191 44.18428.161132.565 1.0037.66
ATOM 3178 N LEUB 192 43.33627.589134.595 1.0030.79
ATOM 3179 CA LEUB 192 42.46326.515134.097 1.0024.98
ATOM 3180 CB LEUB 192 43.061 25.115134.313 1.0028.41 ATOM 3181 CG LEUB 192 44.441 24.720133.769 1.0030.46
ATOM 3182 CD1 LEUB 192 44.75523.399134.403 1.0034.90
ATOM 3183 CD2 LEUB 192 44.49424.618132.227 1.0026.34
ATOM 3184 C LEUB 192 41.15626.560134.883 1.0028.83
ATOM 3185 O LEUB 192 41.16426.742136.112 1.0028.67 ATOM 3186 N VALB 193 40.051 26.390134.163 1.0023.80
ATOM 3187 CA VALB 193 38.70026.339134.718 1.0028.96
ATOM 3188 CB VALB 193 37.75327.342134.039 1.0019.66
ATOM 3189 CGI VALB 193 36.31427.064134^485 1.0021.36
ATOM 3190 CG2VALB 193 38.09628.798134.477 1.0023.05 ATOM 3191 C VALB 193 38.22324.912134.392 1.0031.56
ATOM 3192 O VALB 193 38.27224.471133.222 1.0029.35
ATOM 3193 N VALB 194 37.79624.180135.412 1.0027.72
ATOM 3194 CA VALB 194 37.361 22.807135.193 1.0026.94
ATOM 3195 CB VALB 194 38.10821.848136.163 1.0033.32 ATOM 3196 CGI VALB 194 37.66620.405135.946 1.0030.28
ATOM 3197 CG2 VALB 194 39.60922.002135.997 1.0023.46
ATOM 3198 C VALB 194 35.85622.672135.406 1.0030.63
ATOM 3199 O VALB 194 35.38922.776136.541 1.0028.63
ATOM 3200 N PROB 195 35.07322.475134.319 1.0023.23 ATOM 3201 CD PROB 195 35.46822.461132.900 1.0020.15
ATOM 3202 CA PROB 195 33.61522.324134.399 1.0027.07
ATOM 3203 CB PROB 195 33.15722.579132.950 1.0022.40
ATOM 3204 CG PROB 195 34.35223.290132.331 1.0024.67
ATOM 3205 C PROB 195 33.29020.896134.815 1.0022.44 ATOM 3206 O PROB 195 34.12720.020134.682 1.0021.65
ATOM 3207 N SER B 196 32.05820.648135.270 1.0027.81
ATOM 3208 CA SERB 196 31.689 19.292135.658 1.0028.16
ATOM 3209 CB SERB 196 30.442 19.286136.551 1.0031.74 ATOM 3210 OG SER B 196 30.781 19.647 137.866 1.00 32.60
ATOM 321 1 C SER B 196 31.415 18.375 134.472 1.00 28.34
ATOM 3212 O SER B 196 31.835 17.221 134.467 1.00 29.34
ATOM 3213 N HIS B 197 30.751 18.912 133.461 1.00 30.79 ATOM 3214 CA HIS B 197 30.326 18.1 1 1 132.324 1.00 33.61
ATOM 3215 CB HIS B 197 28.81 1 18.178 132.279 1.00 34.17
ATOM 3216 CG HIS B 197 28.173 17.629 133.518 1.00 39.99
ATOM 3217 CD2 HIS B 197 27.282 18.171 134.385 1.00 38.1 1
ATOM 3218 ND1 HIS B 197 28.437 16.357 133.979 1.00 35.28 ATOM 3219 CE1 HIS B 197 27.734 16.138 135.077 1.00 41.73
ATOM 3220 NE2 HIS B 197 27.025 17.220 135.340 1.00 38.28
ATOM 3221 C HIS B 197 30.899 18.374 130.934 1.00 33.01
ATOM 3222 O HIS B 197 30.403 17.843 129.936 1.00 31.19
ATOM 3223 N SER B 198 31.947 19.174 130.870 1.00 31.77 ATOM 3224 CA SER B 198 32.570 19.475 129.598 1.00 31.20
ATOM 3225 CB SER B 198 31.994 20.758 128.966 1.00 30.84
ATOM 3226 OG SER B 198 32.263 21.929 129.721 1.0029.24
ATOM 3227 C SER B 198 34.028 19.610 129.904 1.00 33.55
ATOM 3228 O SER B 198 34.445 19.598 131.074 1.00 25.76 ATOM 3229 N GLU B 199 34.805 19.752 128.848 1.00 32.38
ATOM 3230 CA GLU B 199 36.245 19.827 128.942 1.00 30.39
ATOM 3231 CB GLU B 199 36.830 19.792 127.539 1.00 38.1 1
ATOM 3232 CG GLU B 199 36.098 18.892 126.559 1.00 54.60
ATOM 3233 CD GLU B 199 35.942 17.441 127.008 1.00 57.90 ATOM 3234 OE1 GLU B 199 36.869 16.878 127.635 1.00 66.63
ATOM 3235 OE2 GLU B 199 34.893 16.852 126.693 1.00 55.76
ATOM 3236 C GLU B 199 36.848 21.030 129.658 1.00 30.45
ATOM 3237 O GLU B 199 36.250 22.091 129.746 1.00 27.65
ATOM 3238 N VAL B 200 38.079 20.830 130.110 1.00 27.28 ATOM 3239 CA VAL B 200 38.899 21.853 130.751 1.00 32.89
ATOM 3240 CB VAL B 200 40.249 21.234 131.247 1.00 29.92
ATOM 3241 CGI VAL B 200 41.079 22.307 131.91 1 1.00 32.66
ATOM 3242 CG2 VAL B 200 40.001 20.041 132.176 1.00 31.92
ATOM 3243 C VAL B 200 39.288 22.966 129.724 1.00 31.54 ATOM 3244 0 VAL B 200 39.599 22.675 128.583 1.00 35.10
ATOM 3245 N GLY B 201 39.31 1 24.221 130.153 1.00 30.53
ATOM 3246 CA GLY B 201 39.694 25.319 129.280 1.00 32.55
ATOM 3247 C GLY B 201 40.305 26.375 130.188 1.00 33.13 ATOM 3248 O GLY B 201 40.708 26.040 131.305 1.00 34.92
ATOM 3249 N ASP B 202 40.406 27.624 129.744 1.00 30.86
ATOM 3250 CA ASP B 202 40.950 28.661 130.618 1.00 28.56
ATOM 3251 CB ASP B 202 42.095 29.448 129.957 1.00 30.21 ATOM 3252 CG ASP B 202 41.709 30.069 128.616 1.00 33.43
ATOM 3253 OD1 ASP B 202 40.574 30.532 128.452 1.00 35.41
ATOM 3254 OD2 ASP B 202 42.593 30.140 127.729 1.0049.44
ATOM 3255 C ASP B 202 39.904 29.632 131.131 1.00 29.88
ATOM 3256 O ASP B 202 38.728 29.342 131.126 1.00 29.28 ATOM 3257 N ALA B 203 40.345 30.800 131.574 1.00 33.53
ATOM 3258 CA ALA B 203 39.444 31.805 132.109 1.00 32.97
ATOM 3259 CB ALA B 203 40.243 33.036 132.441 1.00 31.20
ATOM 3260 C ALA B 203 38.269 32.162 131.177 1.00 35.98
ATOM 3261 O ALA B 203 37.228 32.648 131.632 1.00 30.19 ATOM 3262 N SER B 204 38.435 31.917 129.875 1.00 35.05
ATOM 3263 CA SER B 204 37.395 32.248 128.915 1.00 34.27
ATOM 3264 CB SER B 204 37.856 31.973 127.465 1.00 31.71
ATOM 3265 OG SER B 204 38.196 30.611 127.248 1.00 33.25
ATOM 3266 C SER B 204 36.101 31.503 129.191 1.00 35.36 ATOM 3267 O SER B 204 35.045 31.929 128.744 1.00 33.49
ATOM 3268 N LEU B 205 36.168 30.402 129.933 1.00 35.25
ATOM 3269 CA LEU B 205 34.944 29.668 130.209 1.00 29.62
ATOM 3270 CB LEU B 205 35.257 28.282 130.796 1.00 27.64
ATOM 3271 CG LEU B 205 36.168 27.353 129.967 1.00 31.26 ATOM 3272 CD 1 LEU B 205 36.138 25.923 130.575 1.00 32.71
ATOM 3273 CD2 LEU B 205 35.697 27.271 128.514 1.00 31.22
ATOM 3274 C LEU B 205 34.053 30.492 131.141 1.00 27.80
ATOM 3275 O LEU B 205 32.838 30.350 131.129 1.00 32.91
ATOM 3276 N LEU B 206 34.663 31.378 131.928 1.00 33.55 ATOM 3277 CA LEU B 206 33.899 32.230 132.845 1.00 32.81
ATOM 3278 CB LEU B 206 34.855 33.000 133.765 1.00 32.37
ATOM 3279 CG LEU B 206 35.738 32.023 134.560 1.00 30.27
ATOM 3280 CD 1 LEU B 206 36.805 32.755 135.336 1.00 32.48
ATOM 3281 CD2 LEU B 206 34.859 31.164 135.474 1.00 30.07 ATOM 3282 C LEU B 206 33.043 33.179 132.001 1.00 35.63
ATOM 3283 O LEU B 206 31.846 33.358 132.263 1.00 29.80
ATOM 3284 N LYS B 207 33.658 33.768 130.976 1.00 38.24
ATOM 3285 CA LYS B 207 32.941 34.658 130.048 1.00 39.19 ATOM 3286 CB LYS B 207 33.942 35.241 129.038 1.00 39.86
ATOM 3287 CG LYS B 207 33.326 36.066 127.939 1.00 43.21
ATOM 3288 CD LYS B 207 34.389 36.915 127.275 1.00 48.32
ATOM 3289 CE LYS B 207 33.834 37.674 126.072 1.00 55.67 ATOM 3290 NZ LYS B 207 33.489 36.751 124.920 1.00 57.26
ATOM 3291 C LYS B 207 31.786 33.934 129.315 1.00 36.86
ATOM 3292 O LYS B 207 30.661 34.463 129.202 1.00 34.36
ATOM 3293 N LEU B 208 32.057 32.730 128.808 1.00 35.39
ATOM 3294 CA LEU B 208 31.035 31.965 128.098 1.00 32.77 ATOM 3295 CB LEU B 208 31.626 30.666 127.534 1.00 38.56
ATOM 3296 CG LEU B 208 32.712 30.805 126.456 1.00 38.00
ATOM 3297 CD 1 LEU B 208 33.144 29.416 125.951 1.00 38.43
ATOM 3298 CD2 LEU B 208 32.154 31.624 125.314 1.00 31.90
ATOM 3299 C LEU B 208 29.871 31.638 129.019 1.00 38.55 ATOM 3300 O LEU B 208 28.694 31.761 128.637 1.00 34.03
ATOM 3301 N THR B 209 30.187 31.210 130.242 1.00 36.73
ATOM 3302 CA THR B 209 29.1 16 30.904 131.182 1.0029.21
ATOM 3303 CB THR B 209 29.676 30.468 132.554 1.00 27.75
ATOM 3304 OGl THR B 209 30.473 29.288 132.405 1.00 29.01 ATOM 3305 CG2 THR B 209 28.557 30.183 133.489 1.00 22.93
ATOM 3306 C THR B 209 28.228 32.143 131.385 1.00 27.33
ATOM 3307 O THR B 209 27.001 32.034 131.363 1.00 24.55
ATOM 3308 N LEU B 210 28.851 33.307 131.600 1.00 30.70
ATOM 3309 CA LEU B 210 28.112 34.557 131.809 1.00 32.95 ATOM 3310 CB LEU B 210 29.081 35.740 131.958 1.00 35.76
ATOM 3311 CG LEU B 210 28.465 37.146 132.141 1.00 40.23
ATOM 3312 CD1 LEU B 210 27.492 37.184 133.328 1.00 34.39
ATOM 3313 CD2 LEU B 210 29.559 38.167 132.332 1.00 35.75
ATOM 3314 C LEU B 210 27.186 34.779 130.632 1.00 35.34 ATOM 3315 O LEU B 210 25.971 34.890 130.805 1.00 36.50
ATOM 3316 N GLU B 211 27.768 34.823 129.433 1.00 36.18
ATOM 3317 CA GLU B 21 1 27.010 34.985 128.192 1.00 37.09
ATOM 3318 CB GLU B 21 1 27.910 34.747 126.965 1.00 37.33
ATOM 3319 CG GLU B 21 1 28.790 35.915 126.546 1.0045.93 ATOM 3320 CD GLU B 21 1 29.914 35.510 125.571 1.00 50.42
ATOM 3321 OE1 GLU B 21 1 29.672 34.731 124.625 1.0048.23
ATOM 3322 OE2 GLU B 21 1 31.048 35.992 125.750 1.00 52.20
ATOM 3323 C GLU B 21 1 25.840 34.010 128.135 1.00 37.57 ATOM 3324 O GLUB 211 24.72534.392127.788 1.0040.71
ATOM 3325 N GLNB 212 26.09332.742128.443 1.0036.38
ATOM 3326 CA GLNB 212 25.021 31.752128.419 1.0034.97
ATOM 3327 CB GLNB 212 25.56630.328128.690 1.0038.45 ATOM 3328 CG GLNB 212 26.38029.645127.554 1.0040.36
ATOM 3329 CD GLNB 212 25.58529.450126.264 1.0036.64
ATOM 3330 OE1 GLNB 212 24.36529.323126.278 1.0035.68
ATOM 3331 NE2 GLNB 212 26.28929.389125.152 1.0040.16
ATOM 3332 C GLNB 212 23.95832.072129.474 1.0037.33 ATOM 3333 O GLNB 212 22.76431.901129.232 1.0037.49
ATOM 3334 N ALAB 213 24.38632.507130.656 1.0034.06
ATOM 3335 CA ALAB213 23.41832.816131.701 1.0038.22
ATOM 3336 CB ALAB 213 24.13433.175133.039 1.0028.43
ATOM 3337 C ALAB213 22.56533.981131.216 1.0037.59 ATOM 3338 O ALAB213 21.34333.916131.267 1.0032.65
ATOM 3339 N VALB 214 23.211 35.050130.756 1.0040.42
ATOM 3340 CA VALB 214 22.47236.211130.249 1.0044.28
ATOM 3341 CB VALB 214 23.43537.251129.623 1.0042.92
ATOM 3342 CGI VALB 214 22.63938.312128.856 1.0041.63 ATOM 3343 CG2 VALB 214 24.26037.910130.709 1.0031.31
ATOM 3344 C VALB 214 21.45435.761129.190 1.0043.73
ATOM 3345 O VALB 214 20.275 36.122129.233 1.0045.17
ATOM 3346 N LYS B 215 21.92634.962128.243 1.0045.72
ATOM 3347 CA LYSB 215 21.08034.438127.176 1.0046.74 ATOM 3348 CB LYSB 215 21.93333.536126.282 1.0053.66
ATOM 3349 CG LYSB 215 21.271 32.943125.047 1.0057.05
ATOM 3350 CD LYS B 215 22.35632.259124.223 1.0062.41
ATOM 3351 CE LYS B 215 21.87431.769122.878 1.0064.82
ATOM 3352 NZ LYSB215 23.01931.155122.133 1.0065.22 ATOM 3353 C LYS B 215 19.95333.640127.818 1.0049.01
ATOM 3354 O LYS B 215 18.77733.804127.493 1.0049.54
ATOM 3355 N GLY B 216 20.32332.778128.751 1.0047.99
ATOM 3356 CA GLYB 216 19.33431.966129.420 1.0046.36
ATOM 3357 C GLYB 216 18.24332.804130.046 1.0049.13 ATOM 3358 O GLYB 216 17.06032.536129.849 1.0047.43
ATOM 3359 N LEUB217 18.62733.820130.811 1.0049.42
ATOM 3360 CA LEUB 217 17.62934.663131.452 1.0052.35
ATOM 3361 CB LEUB 217 18.28535.653132.421 1.0047.24 ATOM 3362 CG LEU B 217 17.376 36.780 132.936 1.00 43.03
ATOM 3363 CD1 LEU B 217 16.074 36.218 133.453 1.00 38.77
ATOM 3364 CD2 LEU B 217 18.101 37.570 134.015 1.00 43.22
ATOM 3365 C LEU B 217 16.816 35.423 130.421 1.00 57.98 ATOM 3366 0 LEU B 217 15.577 35.420 130.477 1.00 56.14
ATOM 3367 N ASN B 218 17.519 36.067 129.487 1.00 62.08
ATOM 3368 CA ASN B 218 16.868 36.854 128.450 1.0068.56
ATOM 3369 CB ASN B 218 17.861 37.355 127.409 1.00 67.48
ATOM 3370 CG ASN B 218 17.207 38.274 126.403 1.00 73.58 ATOM 3371 OD1 ASN B 218 16.704 39.343 126.761 1.0075.32
ATOM 3372 ND2 ASN B 218 17.189 37.860 125.138 1.00 76.14
ATOM 3373 C ASN B 218 15.795 36.036 127.765 1.00 71.49
ATOM 3374 0 ASN B 218 14.789 36.579 127.327 1.00 74.59
ATOM 3375 N GLU B 219 15.999 34.728 127.668 1.00 76.22 ATOM 3376 CA GLU B 219 14.988 33.867 127.063 1.00 81.29
ATOM 3377 CB GLU B 219 15.502 32.429 126.951 1.00 83.77
ATOM 3378 CG GLU B 219 16.756 32.263 126.098 1.00 87.01
ATOM 3379 CD GLU B 219 16.501 32.462 124.623 1.00 87.18
ATOM 3380 OE1 GLU B 219 15.968 33.524 124.248 1.00 91.06 ATOM 3381 OE2 GLU B 219 16.842 31.554 123.839 1.00 88.24
ATOM 3382 C GLU B 219 13.782 33.916 128.002 1.00 82.64
ATOM 3383 O GLU B 219 12.953 33.006 128.023 1.00 81.79
ATOM 3384 N SER B 220 13.713 34.999 128.777 1.00 84.00
ATOM 3385 CA SER B 220 12.654 35.243 129.742 1.00 84.50 ATOM 3386 CB SER B 220 11.427 35.843 129.042 1.00 86.35
ATOM 3387 OG SER B 220 10.413 36.193 129.970 1.00 87.23
ATOM 3388 C SER B 220 12.298 33.932 130.421 1.00 85.03
ATOM 3389 O SER B 220 11.108 33.549 130.377 1.00 84.02
ATOM 3390 OXT SER B 220 13.227 33.312 130.988 1.00 82.85 TER SER B 220
HETATM 3391 S S04 C 1 -4.390 -9.482 95.307 1.00 57.24
HET ATM 3392 Ol S04 C 1 -3.606 -9.592 96.576 1.00 60.44
HETATM 3393 02 S04 C 1 -4.609 -8.060 94.933 1.00 67.81
HETATM 3394 03 S04 C 1 -3.666 -10.141 94.187 1.0061.38 HETATM 3395 04 S04 C 1 -5.711 -10.126 95.538 1.00 56.88
HETATM 3396 ZN+2 ZN D 1 14.873 1 1.573 88.862 1.00 23.34
HETATM 3397 ZN+2 ZN D 2 13.067 8.708 87.639 1.00 24.85
HETATM 3398 ZN+2 ZN E 1 23.680 19.625 139.410 1.00 31.39 HETATM 3399 ZN+2 ZN E 2 26.252 18.098 137.474 1.00 36.72
HETATM 3400 C2 MCI F 1 7.763 10.082 86.005 1.00 35.89
HETATM 3401 Cl MCI F 1 7.084 9.795 87.232 1.00 31.37
HETATM 3402 C3 MCI F 1 8.014 9.01 1 85.104 1.00 34.76 HETATM 3403 C4 MCI F 1 7.609 7.698 85.415 1.00 28.22
HETATM 3404 C5 MCI F 1 6.950 7.438 86.631 1.00 39.01
HETATM 3405 C6 MCI F 1 6.687 8.486 87.541 1.00 35.99
HETATM 3406 C 12 MCI F 1 8.241 1 1.492 85.681 1.00 33.27
HETATM 3407 C13 MCI F 1 9.350 12.082 86.590 1.00 35.14 HETATM 3408 C 16 MCI F 1 10.791 1 1.583 86.341 1.0027.52
HETATM 3409 C19 MCI F 1 11.634 1 1.690 87.621 1.00 30.77
HETATM 3410 S20 MCI F 1 13.317 1 1.078 87.333 1.00 23.59
HETATM 3411 C23 MCI F 1 11.489 12.506 85.248 1.00 37.58
HETATM 3412 025 MCI F 1 11.536 13.706 85.428 1.00 45.62 HETATM 3413 N26 MCI F 1 12.046 12.001 84.135 1.00 43.01
HETATM 3414 C27 MCI F 1 12.776 10.773 83.856 1.0041.98
HETATM 3415 C28 MCI F 1 14.313 10.921 84.074 1.00 36.77
HETATM 3416 029 MCI F 1 14.977 1 1.805 83.648 1.00 29.06
HETATM 3417 O30 MCI F 1 14.820 9.889 84.760 1.00 30.21 HETATM 3418 C31 MCI F 1 12.535 10.389 82.427 1.0041.01
HETATM 3419 C33 MCI F 1 1 1.890 11.073 81.457 1.0042.97
HETATM 3420 C34 MCI F 1 11.71 1 10.271 80.237 1.0042.64
HETATM 3421 C35 MCI F 1 12.461 9.148 80.248 1.0048.32
HETATM 3422 S36 MCI F 1 13.163 8.877 81.844 1.00 37.94 HETATM 3423 C37 MCI F 1 12.754 8.147 79.1 19 1.00 51.82
HETATM 3424 N38 MCI F 1 14.128 8.039 78.488 1.00 63.21
HETATM 3425 C41 MCI F 1 15.334 8.470 79.105 1.00 62.35
HETATM 3426 N42 MCI F 1 16.267 9.010 78.238 1.00 65.99
HETATM 3427 N43 MCI F 1 15.573 9.1 10 77.039 1.00 64.02 HETATM 3428 N44 MCI F 1 14.199 8.783 77.262 1.00 63.13
HETATM 3429 C2 MCI G 1 25.427 12.800 135.586 1.00 50.09
HETATM 3430 Cl MCI G 1 25.705 12.121 136.817 1.00 50.08
HETATM 3431 C3 MCI G 1 26.462 12.902 134.616 1.00 49.08
HETATM 3432 C4 MCI G 1 27.735 12.329 134.868 1.00 49.15 HETATM 3433 C5 MCI G 1 27.985 11.657 136.099 1.00 45.74
HETATM 3434 C6 MCI G 1 26.971 1 1.559 137.068 1.0042.43
HETATM 3435 C12 MCI G 1 24.062 13.360 135.303 1.0049.85
HETATM 3436 C 13 MCI G 1 23.360 14.061 136.475 1.00 53.04 HETATM 3437 C 16 MCI G 1 23.449 15.579 136.413 1.00 48.65
HETATM 3438 C 19 MCI G 1 23.213 16.269 137.751 1.00 38.22
HETATM 3439 S20 MCI G 1 23.689 18.001 137.584 1.00 38.98
HETATM 3440 C23 MCI G 1 22.382 16.122 135.415 1.00 49.55 HETATM 3441 025 MCI G 1 21.428 15.41 1 135.086 1.00 57.00
HETATM 3442 N26 MCI G 1 22.514 17.372 134.939 1.00 52.64
HETATM 3443 C27 MCI G 1 23.521 17.969 134.058 1.00 52.03
HETATM 3444 C28 MCI G 1 23.500 19.515 134.281 1.0047.57
HETATM 3445 029 MCI G 1 22.536 20.198 134.090 1.00 44.42 HETATM 3446 O30 MCI G 1 24.682 20.007 134.713 1.00 39.62
HETATM 3447 C31 MCI G 1 23.151 17.577 132.638 1.00 58.58
HETATM 3448 C33 MCI G 1 21.941 17.71 1 132.035 1.00 57.90
HETATM 3449 C34 MCI G 1 22.050 17.596 130.599 1.00 59.88
HETATM 3450 C35 MCI G 1 23.335 17.556 130.231 1.00 61.78 HETATM 3451 S36 MCI G 1 24.307 16.861 131.520 1.00 62.29
HETATM 3452 C37 MCI G 1 24.024 18.040 128.951 1.00 65.07 HETATM 3453 AN38 MCI G 1 23.676 19.440 128.540 0.5062.39 HETATM 3454 AC41 MCI G 1 24.148 20.021 127.353 0.50 61.49 HETATM 3455 AN42 MCI G 1 23.293 20.904 126.758 0.50 59.60 HETATM 3456 AN43 MCI G 1 22.112 20.675 127.426 0.50 62.04 HETATM 3457 AN44 MCI G 1 22.276 19.569 128.301 0.50 61.62 HETATM 3802 BN38 MCI G 1 25.316 17.344 128.771 0.50 62.80 HETATM 3803 BC41 MCI G 1 25.378 16.037 128.283 0.50 63.66 HETATM 3804 BN42 MCI G 1 26.61 1 15.71 1 127.811 0.50 63.23 HETATM 3805 BN43 MCI G 1 27.085 16.950 127.431 0.50 66.37 HETATM 3806 BN44 MCI G 1 26.164 17.961 127.842 0.50 63.27
HETATM 3458 O HOH W 1 19.213 8.283 98.738 1.00 13.78
HETATM 3459 O HOH W 2 28.871 14.295 96.000 1.00 18.64
HETATM 3460 O HOH W 3 9.365 3.300 92.119 1.00 16.60 HETATM 3461 O HOH W 4 29.647 24.964 141.190 1.00 25.22
HETATM 3462 O HOH W 5 20.975 - 10.216 98.679 1.00 26.93
HETATM 3463 O HOH W 6 6.579 15.419 100.844 1.00 16.55
HETATM 3464 O HOH W 7 31.695 7.963 95.468 1.00 34.34
HETATM 3465 O HOH W 8 9.727 9.132 74.003 1.00 35.96 HETATM 3466 O HOH W 9 20.199 5.995 91.131 1.00 20.36 HETATM 3467 O HOH W 10 3.113 9.361 100.357 1.00 15.45 HETATM 3468 O HOH W 1 1 15.399 14.397 108.164 1.00 59.63
HETATM 3469 O HOH W 12 32.468 14.135 140.613 1.00 34.97 HETATM 3470 O HOH W 13 18.738 12.726 83.822 1.00 31.19
HETATM 3471 O HOH W 14 31.605 4.200 160.798 1.00 29.69
HETATM 3472 O HOH W 15 27.879 7.007 149.323 1.00 35.07
HETATM 3473 O HOH W 16 17.744 15.422 86.212 1.00 27.03 HETATM 3474 O HOH W 17 8.948 13.345 97.608 1.00 25.78
HETATM 3475 O HOH W 18 7.407 1.721 90.850 1.00 15.43
HETATM 3476 O HOH W 19 -7.496 4.773 109.950 1.0049.96
HETATM 3477 O HOH W 20 -2.144 9.143 96.379 1.00 23.56
HETATM 3478 O HOH W 21 46.428 25.191 145.653 1.00 42.48 HETATM 3479 0 HOH W 22 24.706 2.587 110.642 1.00 52.77
HETATM 3480 O HOH W 23 23.517 10.846 75.829 1.00 48.78
HETATM 3481 O HOH W 24 15.967 4.493 83.963 1.00 29.41
HETATM 3482 O HOH W 25 17.720 7.147 91.136 1.00 16.99
HETATM 3483 O HOH W 26 16.298 4.036 81.834 1.00 43.43 HETATM 3484 O HOH W 27 1.761 11.639 100.308 1.00 17.21
HETATM 3485 O HOH W 28 31.321 13.547 94.990 1.00 21.71
HETATM 3486 O HOH W 29 12.714 5.510 101.368 1.00 18.75
HETATM 3487 O HOH W 30 6.691 1 1.407 100.026 1.00 13.20
HETATM 3488 O HOH W 31 19.058 22.657 138.042 1.00 34.24 HETATM 3489 O HOH W 32 6.396 -4.785 87.625 1.00 24.45
HETATM 3490 O HOH W 33 5.915 7.239 1 13.541 1.00 36.37
HETATM 3491 O HOH W 34 30.199 7.262 139.518 1.00 35.96
HETATM 3492 O HOH W 35 18.391 14.514 77.357 1.00 42.90
HETATM 3493 O HOH W 36 29.335 21.576 133.812 1.00 23.86 HETATM 3494 O HOH W 37 21.477 20.099 78.625 1.00 63.88
HETATM 3495 O HOH W 38 23.284 10.743 98.055 1.00 20.91
HETATM 3496 O HOH W 39 39.682 2.284 92.518 1.00 56.98
HETATM 3497 O HOH W 40 27.504 2.952 84.409 1.00 25.90
HETATM 3498 O HOH W 41 6.293 15.824 91.828 1.00 60.98 HETATM 3499 O HOH W 42 25.643 -9.255 83.171 1.00 33.47
HETATM 3500 O HOH W 43 28.671 22.349 140.946 1.00 30.66
HETATM 3501 O HOH W 44 21.945 17.806 99.170 1.00 34.23
HETATM 3502 O HOH W 45 27.301 -2.879 143.703 1.00 77.64
HETATM 3503 O HOH W 46 -2.919 4.003 89.500 1.00 52.87 HETATM 3504 O HOH W 47 8.594 13.341 100.582 1.00 18.55
HETATM 3505 O HOH W 48 19.145 13.506 106.970 1.00 33.82
HETATM 3506 O HOH W 49 34.263 23.269 128.541 1.00 23.35
HETATM 3507 O HOH W 50 27.794 24.137 128.698 1.00 39.82 HETATM 3508 O HOH W 51 -4.293 9.949 97.959 1.00 19.88 HETATM 3509 O HOH W 52 23.013 18.359 96.342 1.00 26.65 HETATM 3510 O HOH W 53 20.059 -1 1.182 96.265 1.00 25.79 HETATM 351 1 O HOH W 54 19.405 8.696 1 10.572 1.00 23.01 HET ATM 3512 0 HOH W 55 32.401 9.771 92.144 1.00 22.64 HETATM 3513 O HOH W 56 15.832 19.403 109.279 1.00 35.85 HETATM 3514 O HOH W 57 3.463 1 1.764 96.984 1.00 27.81 HETATM 3515 O HOH W 58 23.484 20.577 92.492 1.00 50.48 HETATM 3516 O HOH W 59 26.449 21.035 90.639 1.00 28.40 HETATM 3517 O HOH W 60 9.505 5.923 109.144 1.00 28.56 HETATM 3518 O HOH W 61 -6.554 7.952 96.244 1.00 48.29 HETATM 3519 O HOH W 62 10.164 5.025 111.629 1.00 44.63 HETATM 3520 O HOH W 63 25.613 4.823 99.618 1.00 27.79 HETATM 3521 O HOH W 64 46.556 8.281 159.306 1.00 66.87 HETATM 3522 O HOH W 65 24.623 1 1.560 101.637 1.00 14.60 HETATM 3523 O HOH W 66 19.448 19.820 92.476 1.00 44.62 HETATM 3524 O HOH W 67 33.588 12.131 138.943 1.00 34.68 HETATM 3525 O HOH W 68 22.334 22.969 156.469 1.00 50.14 HETATM 3526 O HOH W 69 28.202 -1 1.239 95.268 1.00 50.23 HETATM 3527 O HOH W 70 25.370 17.422 91.1 11 1.00 24.47 HETATM 3528 O HOH W 71 10.493 28.612 100.783 1.00 66.05 HETATM 3529 O HOH W 72 12.875 4.431 1 1 1.707 1.00 21.29 HETATM 3530 O HOH W 73 22.582 19.009 111.083 1.00 39.15 HETATM 3531 O HOH W 74 34.047 16.848 83.690 1.00 60.04 HETATM 3532 O HOH W 75 31.859 14.856 92.471 1.00 29.65 HETATM 3533 O HOH W 76 53.512 30.429 137.048 1.00 54.23 HETATM 3534 O HOH W 77 29.279 12.749 104.225 1.00 24.04 HETATM 3535 O HOH W 78 22.243 20.135 94.821 1.00 27.88 HETATM 3536 O HOH W 79 2.043 -1.970 107.157 1.00 36.10 HETATM 3537 O HOH W 80 31.656 21.889 87.757 1.00 69.56 HETATM 3538 O HOH W 81 10.056 -15.648 96.604 1.00 55.68 HETATM 3539 O HOH W 82 31.739 11.752 89.555 1.00 27.06 HETATM 3540 O HOH W 83 42.834 32.043 131.459 1.00 37.57 HETATM 3541 O HOH W 84 13.227 1.901 1 13.179 1.00 35.36 HETATM 3542 O HOH W 85 1.136 -9.857 107.105 1.00 38.22 HETATM 3543 O HOH W 86 -9.363 -1.334 96.341 1.0047.16 HETATM 3544 O HOH W 87 9.251 12.417 89.645 1.00 38.43 HETATM 3545 O HOH W 88 11.622 17.319 92.963 1.00 43.87 HETATM 3546 O HOHW 89 17.274 -0.68479.635 1.0033.09
HETATM 3547 O HOHW 90 28.819-21.59095.611 1.0028.07
HETATM 3548 O HOHW 91 21.207 14.581146.009 1.0033.52
HETATM 3549 O HOHW 92 -3.159 9.58293.579 1.0036.75 HETATM 3550 O HOHW 93 11.975 -5.46882.345 1.0033.31
HETATM3551 O HOHW 94 31.21433.137135.093 1.0033.44
HETATM 3552 O HOHW 95 25.33935.988146.364 1.0041.02
HETATM 3553 O HOHW 96 35.478 12.701 94.844 1.0026.43
HETATM 3554 O HOHW 97 -3.384 -7.03597.744 1.0037.50 HETATM 3555 O HOHW 98 33.523 0.67996.599 1.0039.93
HETATM 3556 O HOHW 99 5.691 3.82490.593 1.0026.58
HETATM 3557 O HOHW 100 14.348 -1.050108.978 1.0030.29
HETATM3558 O HOHW 101 29.132 -3.24281.589 1.0027.03
HETATM 3559 O HOHW 102 25.572 7.477100.758 1.0025.71 HETATM 3560 O HOHW 103 18.072 5.35678.398 1.0030.61
HETATM 3561 O HOHW 104 25.18520.02988.296 1.0029.46
HETATM 3562 O HOHW 105 27.082 0.372106.412 1.0026.91
HETATM 3563 O HOHW 106 28.841 -8.58396.259 1.0032.58
HETATM 3564 O HOHW 107 10.694 15.17095.663 1.0027.37 HETATM 3565 O HOH W 108 23.980-10.780108.774 1.0036.34
HETATM 3566 O HOHW 109 10.222 15.07991.566 1.0032.24
HETATM 3567 O HOH WHO 23.563 2.218152.068 1.0032.55
HETATM 3568 O HOH W 111 11.525 3.94578.672 1.0028.99
HETATM 3569 O HOHW 112 45.92328.283130.713 1.0032.91 HETATM 3570 O HOHW 113 28.343 5.976137.630 1.0027.15
HETATM 3571 O HOHW 114 28.261 23.089149.073 1.0032.47
HETATM 35720 HOHW 115 11.508 18.374105.059 1.0030.32
HETATM 3573 O HOHW 116 32.847 14.01489.743 1.0030.51
HETATM 3574 O HOHW 117 31.842 15.965150.046 1.0036.36 HETATM 3575 O HOHW 118 21.540 -5.125109.187 1.0035.51
HETATM 3576 O HOHW 119 26.23527.516149.084 1.0033.99
HETATM 3577 O HOHW 120 32.080 5.802136.311 1.0034.03
HETATM 35780 HOHW 121 16.56027.712142.306 1.0040.82
HETATM 3579 O HOHW 122 21.205-17.97895.248 1.0033.39 HETATM 3580 O HOHW 123 25.477 9.56399.279 1.0033.56
HETATM 3581 O HOHW 124 -4.230 -2.63883.752 1.0041.43
HETATM 3582 O HOHW 125 -2.374 1.56690.350 1.0036.93
HETATM 3583 O HOHW 126 29.957 -4.42296.683 1.0032.81 HETATM 3584 O HOH W 127 2.908 5.294 91.505 1.00 32.41 HETATM 3585 O HOH W 128 9.978 10.663 109.843 1.00 30.34 HETATM 3586 O HOH W 129 39.486 12.155 134.348 1.00 31.22 HETATM 3587 O HOH W 130 24.605 12.203 149.993 1.00 35.35 HETATM 3588 O HOH W 131 0.651 2.787 86.869 1.00 32.70 HETATM 3589 O HOH W 132 23.291 10.655 107.883 1.00 40.15 HETATM 3590 O HOH W 133 38.790 23.642 126.189 1.00 36.36 HETATM 3591 O HOH W 134 26.047 6.671 107.549 1.00 27.82 HETATM 3592 O HOH W 135 12.145 15.468 87.382 1.00 38.54 HETATM 3593 O HOH W 136 13.067 -0.852 77.674 1.0041.18 HETATM 3594 O HOH W 137 17.858 1 1.046 1 10.786 1.00 36.57 HETATM 3595 O HOH W 138 22.782 35.462 147.181 1.00 37.97 HETATM 3596 O HOH W 139 5.435 -12.712 89.337 1.00 35.15 HETATM 3597 O HOH W 140 33.912 12.029 79.852 1.0043.92 HETATM 3598 O HOH W 141 29.722 22.112 131.136 1.00 32.29 HETATM 3599 O HOH W 142 29.486 41.316 140.219 1.00 54.84 HETATM 3600 O HOH W 143 25.747 10.041 149.717 1.00 38.23 HETATM 3601 O HOH W 144 -2.920 -4.254 104.777 1.00 37.1 1 HETATM 3602 O HOH W 145 19.605 -12.740 89.390 1.00 36.74 HETATM 3603 O HOH W 146 32.275 10.630 94.523 1.00 37.02 HETATM 3604 O HOH W 147 16.819 11.320 76.603 1.00 49.12 HETATM 3605 O HOH W 148 17.603 22.484 89.990 1.00 40.55 HETATM 3606 O HOH W 149 2.654 14.252 77.759 1.00 49.25 HETATM 3607 O HOH W 150 34.770 10.395 95.889 1.00 32.58 HETATM 3608 O HOH W 151 21.598 24.166 135.060 1.00 37.66 HETATM 3609 O HOH W 152 34.341 2.958 137.585 1.0040.72 HETATM 3610 O HOH W 153 25.649 36.334 143.679 1.00 33.51 HETATM 361 1 O HOH W 154 -5.026 -6.348 104.140 1.0044.89 HETATM 3612 O HOH W 155 42.396 30.732 125.142 1.00 36.05 HETATM 3613 O HOH W 156 32.060 6.255 74.869 1.00 39.33 HETATM 3614 O HOH W 157 28.501 21.375 75.904 1.00 41.73 HETATM 3615 O HOH W 158 22.988 12.665 147.470 1.00 39.49 HETATM 3616 O HOH W 159 22.131 29.935 127.292 1.00 36.55 HETATM 3617 O HOH W 160 10.655 14.843 82.779 1.00 35.10 HETATM 3618 O HOH W 161 19.705 -0.290 108.055 1.0041.13 HETATM 3619 O HOH W 162 37.843 12.370 93.745 1.00 35.72 HETATM 3620 O HOH W 163 50.945 10.197 142.470 1.0045.53 HETATM 3621 O HOH W 164 17.196 8.256 73.427 1.00 38.72 HETATM 3622 O HOH W 165 -4.287 2.440 97.676 1.00 39.03 HETATM 3623 O HOH W 166 19.936 -11.295 107.336 1.00 44.24 HETATM 3624 O HOH W 167 27.662 -19.568 94.419 1.0043.96 HETATM 3625 O HOH W 168 21.263 20.818 86.516 1.0044.34 HETATM 3626 O HOH W 169 23.706 6.191 108.788 1.00 38.75 HETATM 3627 O HOH W 170 28.521 -1.741 102.154 1.00 49.94 HETATM 3628 O HOH W 171 27.895 19.528 84.644 1.00 53.14 HETATM 3629 O HOH W 172 29.638 -4.719 78.933 1.0047.28 HETATM 3630 O HOH W 173 44.530 31.022 152.723 1.00 43.04 HETATM 3631 O HOH W 174 16.863 16.843 126.925 1.0048.87 HETATM 3632 O HOH W 175 37.823 30.835 155.578 1.00 39.33 HETATM 3633 O HOH W 176 34.343 5.260 95.245 1.00 42.13 HETATM 3634 O HOH W 177 34.645 38.404 145.950 1.00 45.42 HETATM 3635 O HOH W 178 30.791 4.858 105.337 1.0047.05 HETATM 3636 O HOH W 179 32.650 12.874 157.784 1.00 42.55 HETATM 3637 O HOH W 180 36.934 35.477 126.492 1.00 47.44 HETATM 3638 O HOH W 181 14.035 26.573 139.208 1.00 45.30 HETATM 3639 O HOH W 182 20.431 14.513 155.864 1.00 41.92 HETATM 3640 O HOH W 183 16.499 -10.235 81.662 1.00 44.00 HETATM 3641 O HOH W 184 20.419 -3.267 75.396 1.00 41.18 HETATM 3642 O HOH W 185 33.246 0.589 157.189 1.0049.64 HETATM 3643 O HOH W 186 -1.31 1 -2.261 104.129 1.00 44.80 HETATM 3644 O HOH W 187 21.392 35.831 144.781 1.00 35.93 HETATM 3645 O HOH W 188 -0.390 -5.908 91.546 1.00 51.64 HETATM 3646 O HOH W 189 31.110 9.296 160.552 1.0046.34 HETATM 3647 O HOH W 190 15.148 5.682 80.303 1.00 47.30 HETATM 3648 O HOH W 191 22.327 -4.879 76.150 1.00 48.05 HETATM 3649 O HOH W 192 14.843 29.377 141.470 1.00 45.09 HETATM 3650 O HOH W 193 -3.823 0.463 103.888 1.00 56.66 HETATM 3651 O HOH W 194 11.239 -14.727 102.263 1.0049.33 HETATM 3652 O HOH W 195 8.718 5.661 77.196 1.0047.21 HETATM 3653 O HOH W 196 10.785 18.296 81.030 1.00 58.07 HETATM 3654 O HOH W 197 38.418 17.021 132.275 1.0040.48 HETATM 3655 O HOH W 198 44.813 33.840 144.622 1.00 55.86 HETATM 3656 0 HOH W 199 20.664 14.558 142.257 1.00 38.34 HETATM 3657 O HOH W 200 23.179 -0.791 72.243 1.00 54.98 HETATM 3658 O HOH W 201 7.147 -2.913 114.687 1.00 57.83 HETATM 3659 O HOH W 202 35.260 1.432 81.256 1.0048.88 HETATM 3660 O HOH W 203 16.910 24.489 157.798 1.00 60.49
HETATM 3661 O HOH W 204 29.744 9.800 105.172 1.0044.91
HETATM 3662 O HOH W 205 27.504 -9.499 101.497 1.00 52.47
HETATM 3663 O HOH W 206 13.612 5.126 78.254 1.00 49.54 HETATM 3664 O HOH W 207 12.1 13 -8.324 83.164 1.00 51.14
HETATM 3665 O HOH W 208 9.340 -9.721 110.786 1.00 46.41
HETATM 3666 O HOH W 209 24.242 36.462 126.117 1.00 44.94
HETATM 3667 O HOH W 210 15.038 29.968 137.734 1.00 49.57
HETATM 3668 O HOH W 21 1 48.018 16.039 138.799 1.00 66.84 HETATM 3669 O HOH W 212 19.013 19.334 129.539 1.00 51.51
HETATM 3670 O HOH W 213 8.043 -1.580 109.860 1.00 37.30
HETATM 3671 O HOH W 214 12.887 22.104 142.230 1.00 50.98
HETATM 3672 O HOH W 215 16.238 -1 1.786 99.166 1.00 37.25
HETATM 3673 O HOH W 216 46.241 7.002 156.253 1.00 50.01 HETATM 3674 O HOH W 217 23.440 17.876 77.254 1.00 47.18
HETATM 3675 O HOH W 218 16.705 20.070 150.825 1.00 61.94
HETATM 3676 O HOH W 219 43.173 34.787 132.475 1.0050.12
HETATM 3677 O HOH W 220 40.384 14.075 132.526 1.00 46.45
HETATM 3678 O HOH W 221 42.532 32.547 156.524 1.00 49.37 HETATM 3679 O HOH W 222 3.837 -14.253 93.595 1.00 49.51
HETATM 3680 O HOH W 223 11.729 33.409 141.201 1.00 55.34
HETATM 3681 O HOH W 224 6.290 13.730 88.206 1.00 66.41
HETATM 3682 O HOH W 225 51.380 15.253 141.633 1.00 50.43
HETATM 3683 O HOH W 226 34.568 4.665 160.536 1.0047.83 HETATM 3684 O HOH W 227 28.892 -4.843 76.540 1.00 42.46
HETATM 3685 O HOH W 228 17.302 -12.710 96.718 1.0042.14
HETATM 3686 O HOH W 229 14.406 20.038 82.018 1.00 55.64
HETATM 3687 O HOH W 230 -2.313 -4.728 95.901 1.0041.99
HETATM 3688 O HOH W 231 10.295 -19.319 96.614 1.00 46.13 HETATM 3689 O HOH W 232 17.762 -15.236 99.858 1.0049.33
HETATM 3690 O HOH W 233 28.382 18.473 128.834 1.00 40.02
HETATM 3691 O HOH W 234 36.708 19.591 132.984 1.00 42.04
HETATM 3692 O HOH W 235 15.520 5.353 76.487 1.0049.25
HETATM 3693 O HOH W 236 23.342 13.275 157.535 1.0042.88 HETATM 3694 O HOH W 237 10.410 14.758 89.253 1.0042.48
HETATM 3695 O HOH W 238 18.454 -1 1.197 100.589 1.00 43.96
HETATM 3696 O HOH W 239 46.580 2.678 144.31 1 1.00 73.59
HETATM 3697 O HOH W 240 8.162 27.383 102.249 1.00 37.23 HETATM 3698 O HOH W 241 24.423 8.770 109.479 1.00 53.19
HETATM 3699 O HOH W 242 25.991 -18.785 89.937 1.00 55.60
HETATM 3700 O HOH W 243 43.077 6.243 158.971 1.00 50.16
HETATM 3701 O HOH W 244 20.447 32.762 134.081 1.00 65.78 HETATM 3702 O HOH W 245 22.981 13.403 139.541 1.00 56.17
HETATM 3703 O HOH W 246 35.355 -1.661 83.923 1.00 69.76
HETATM 3704 O HOH W 247 16.1 15 19.090 148.452 1.00 52.90
HETATM 3705 O HOH W 248 38.916 14.178 91.483 1.00 45.10
HETATM 3706 O HOH W 249 -0.329 3.785 88.952 1.00 50.22 HETATM 3707 O HOH W 250 13.760 -0.825 111.624 1.0041.66
HETATM 3708 O HOH W 251 33.253 16.752 87.510 1.00 58.15
HETATM 3709 O HOH W 252 35.420 3.419 79.505 1.00 58.34
HETATM 3710 O HOH W 253 34.256 2.333 94.354 1.0044.15
HETATM 371 1 O HOH W 254 12.194 -6.343 79.139 1.00 51.01 HETATM 3712 O HOH W 255 22.311 32.947 148.307 1.0046.76
HETATM 3713 O HOH W 256 28.262 4.413 105.532 1.00 56.41
HETATM 3714 O HOH W 257 35.091 15.445 160.369 1.0049.99
HETATM 3715 O HOH W 258 39.252 36.738 132.367 1.00 45.99
HETATM 3716 O HOH W 259 32.497 40.004 135.376 1.00 52.89 HETATM 3717 O HOH W 260 13.646 -2.595 85.002 1.00 50.27
HETATM 3718 O HOH W 261 29.269 -8.345 99.707 1.0049.78
HETATM 3719 O HOH W 262 50.625 10.241 138.923 1.00 52.92
HETATM 3720 O HOH W 263 22.963 10.244 146.303 1.0042.17
HETATM 3721 O HOH W 264 7.263 6.139 91.285 1.00 33.60 HETATM 3722 O HOH W 265 -5.274 1.610 95.366 1.00 54.33
HETATM 3723 O HOH W 266 8.695 2.235 1 12.813 1.00 52.81
HETATM 3724 O HOH W 267 17.203 39.155 137.282 1.00 58.27
HETATM 3725 O HOH W 268 21.378 40.092 135.065 1.00 49.85
HETATM 3726 O HOH W 269 13.855 6.413 113.560 1.0048.89 HETATM 3727 O HOH W 270 -4.102 -12.878 103.099 1.00 49.50
HETATM 3728 O HOH W 271 14.224 19.209 134.974 1.00 61.39
HETATM 3729 O HOH W 272 26.943 3.484 107.586 1.00 58.26
HETATM 3730 O HOH W 273 25.509 40.037 134.704 1.00 51.39
HETATM 3731 O HOH W 274 19.236 11.086 143.275 1.00 63.64 HETATM 3732 O HOH W 275 24.687 -0.274 108.208 1.00 56.26
HETATM 3733 O HOH W 276 45.203 10.240 157.930 1.00 56.96
HETATM 3734 O HOH W 277 39.968 17.240 156.952 1.00 52.38
HETATM 3735 O HOH W 278 21.892 3.832 153.910 1.00 50.99 HETATM 3736 O HOH W 279 55.932 22.478 141.742 1.00 54.14 HETATM 3737 O HOH W 280 7.268 -17.589 93.356 1.00 61.26 HETATM 3738 O HOH W 281 13.503 -17.150 104.461 1.00 50.59 HETATM 3739 O HOH W 282 20.649 -6.837 78.714 1.0048.32 HETATM 3740 O HOH W 283 28.190 -16.224 93.711 1.00 54.77 HETATM 3741 O HOH W 284 47.539 1 1.327 134.720 1.00 48.79 HETATM 3742 O HOH W 285 40.672 32.908 126.929 1.00 54.77 HETATM 3743 O HOH W 286 14.896 7.248 74.106 1.00 48.54 HETATM 3744 O HOH W 287 25.100 8.141 146.298 1.00 52.00 HETATM 3745 O HOH W 288 4.433 15.890 83.021 1.0040.78 HETATM 3746 O HOH W 289 23.395 41.312 142.757 1.00 57.30 HETATM 3747 O HOH W 290 16.693 12.205 108.759 1.00 60.41 HETATM 3748 O HOH W 291 42.301 6.651 134.105 1.00 60.51 HETATM 3749 O HOH W 292 0.722 -7.122 88.875 1.00 41.48 HETATM 3750 O HOH W 293 17.350 17.165 77.570 1.00 51.51 HETATM 3751 O HOH W 294 5.039 6.526 89.139 1.00 69.95 HETATM 3752 O HOH W 295 31.172 -2.455 98.725 1.0047.89 HETATM 3753 O HOH W 296 37.269 16.636 160.751 1.00 53.15 HETATM 3754 O HOH W 297 21.054 12.327 76.327 1.0046.56 HETATM 3755 O HOH W 298 0.526 11.883 90.988 1.00 57.62 HETATM 3756 O HOH W 299 26.914 20.893 130.198 1.00 58.01 HETATM 3757 O HOH W 300 23.273 36.124 142.303 1.00 52.77 HETATM 3758 O HOH W 301 30.014 3.176 137.200 1.00 55.20 HETATM 3759 O HOH W 302 -4.567 5.931 82.21 1 1.00 53.19 HETATM 3760 O HOH W 303 41.492 28.275 125.737 1.00 48.06 HETATM 3761 O HOH W 304 14.522 32.045 141.156 1.00 56.13 HETATM 3762 O HOH W 305 0.250 -0.582 106.340 1.00 60.95 HETATM 3763 O HOH W 306 24.734 -3.821 143.081 1.00 50.27 HETATM 3764 O HOH W 307 16.075 17.728 79.820 1.00 46.84 HETATM 3765 O HOH W 308 18.527 6.721 1 11.819 1.00 46.02 HETATM 3766 O HOH W 309 32.345 1.764 140.384 1.00 55.10 HETATM 3767 O HOH W 310 23.259 18.281 89.358 1.00 42.78 HETATM 3768 O HOH W 311 53.675 23.482 152.125 1.00 58.16 HETATM 3769 O HOH W 312 34.674 9.543 91.671 1.0041.89 HETATM 3770 O HOH W 313 30.276 22.679 160.535 1.00 54.05 HETATM 3771 O HOH W 314 21.823 44.026 133.865 1.00 53.69 HETATM 3772 O HOH W 315 19.091 3.492 153.473 1.00 53.73 HETATM 3773 O HOH W 316 5.346 -16.319 92.018 1.00 51.22 HETATM 3774 O HOH W 317 30.180 3.560 127.301 1.00 54.32
HETATM 3775 O HOH W 318 39.350 28.021 127.001 1.0044.56
HETATM 3776 O HOH W 319 34.122 0.921 78.913 1.00 59.07
HETATM 3777 O HOH W 320 38.1 15 36.169 128.718 1.00 51.90 HETATM 3778 O HOH W 321 32.248 -5.320 79.274 1.00 52.25
HETATM 3779 O HOH W 322 21.898 9.530 1 1 1.327 1.00 53.43
HETATM 3780 O HOH W 323 5.855 13.871 85.615 1.00 56.14
HETATM 3781 O HOH W 324 22.985 13.572 1 10.300 1.00 51.37
HETATM 3782 O HOH W 325 28.076 -2.005 75.602 1.00 61.09 HETATM 3783 O HOH W 326 23.980 5.470 133.975 1.00 50.07
HETATM 3784 O HOH W 327 40.387 31.293 156.171 1.00 58.00
HETATM 3785 O HOH W 328 17.956 22.350 101.704 1.00 54.88
HETATM 3786 O HOH W 329 17.979 41.675 124.610 1.00 55.85
HETATM 3787 O HOH W 330 21.527 42.921 142.792 1.0045.52 HETATM 3788 O HOH W 331 41.248 16.910 132.553 1.00 54.81
HETATM 3789 O HOH W 332 31.546 1.177 155.270 1.00 56.26
HETATM 3790 O HOH W 333 16.085 4.391 115.024 1.00 50.60
HETATM 3791 O HOH W 334 32.847 -5.062 93.309 1.00 52.91
HETATM 3792 O HOH W 335 9.833 -2.042 1 1 1.537 1.00 55.72 HETATM 3793 O HOH W 336 39.589 9.707 153.397 1.00 63.32
HETATM 3794 O HOH W 337 32.797 -5.150 97.347 1.00 54.33
HETATM 3795 O HOH W 338 25.188 -3.822 74.616 1.00 51.99
HETATM 3796 O HOH W 339 39.094 -0.031 152.039 1.00 52.76
HETATM 3797 O HOH W 340 54.153 29.982 134.683 1.00 52.63
Table II provides the distances, in A, between atoms within a 5.θA radius in the active site including the inhibitor residue, SB-252619.
TABLE II 3Q
Source atoms Target atoms Distance Source atoms Target atoms Distance
N GLU 41 N VAL 49 ... 4.61 ... CB GLU 42 ... 4.76
... C VAL 49 ... 4.28 ... N VAL 43 ... 4.94
... O VAL 49 ... 3.08 ... C4 SB2 1504 ... 4.52 ... C5 SB2 1504 ... 4.18 CB GL1 J 41 ... N GLU 42 ...
... C6 SB2 1504 ... 4.98 45 3.22 ... C4 SB2 1504 ... 4.26 ... CA GLU 42 ... 4.51 CA GLU 41 O VAL 49 ... 4.06 ... O VAL 49 ... 4.45 ... C5 SB2 1504 ... 4.42 ... C5 SB2 1504 ... 3.38 ... C6 SB2 1504 ... 4.86 ... C6 SB2 1504 ... 3.52 ...C GLU 42.. 4.73 OE2 GLU 41 ... N GLU 42...
... CGI VAL 43 ... 4.63 4.77
... C2 SB2 1504. .. 4.11 40 ... CG PHE 69... 4.96
... C3 SB2 1504. .. 3.98 ... CD2 PHE 69... 3.93
...C4 SB2 1504. .. 3.63 ...O GLU 42... 4.79
...Cl SB2 1504. .. 3.88 ... CE1 PHE 69... 4.66
CG GLU 41 ...N GLU 42... ... CE2 PHE 69... 3.07 3.16 45 ... CZ PHE 69... 3.55
... CA GLU 42... 4.26 ...Cl SB2 1504... 4.99
... CD2 PHE 69... 4.89 C GLU 41 ...CA VAL 48
... C5 SB2 1504... 4.34 4.79
... C6 SB2 1504... 4.05 ...N VAL 49... 4.24
... C GLU 42... 4.09 50 ...O VAL 49... 4.10
... O GLU 42... 4.04 ...CG GLU 42... 4.95
... N VAL 43... 4.51 ...CB GLU 42... 3.62
...CGI VAL 43... 4.16 ... N VAL 43... 3.63
... CE2 PHE 69... 4.54 ... CA VAL 43... 4.88
... CZ PHE 69... 4.87 55 ...CGI VAL 43... 4.56
... C2 SB2 1504... 4.18 O GLU 41 ...C GLY 47
...C3 SB2 1504... 4.46 4.96
... C4 SB2 1504... 4.54 ...O GLY 47... 4.15
...Cl SB2 1504... 3.96 ... N VAL 48... 4.88
... C12SB2 1504... 4.79 60 ... CA VAL 48... 3.77 CD GLU 41 N GLU 42... 3.77 ...CB VAL 48... 4.42
.. CA GLU 42... 4.91 ... C VAL 48... 3.89
..CD2PHE 69... 4.12 ... N VAL 49... 3.03
.. C6 SB2 1504... 4.80 ...C VAL 49... 4.07
..C GLU 42... 4.83 65 ... O VAL 49... 3.32
..O GLU 42... 4.48 ... CB GLU 42... 4.11
..CE2PHE 69... 3.67 ... N VAL 43... 3.49
.. CZ PHE 69... 4.30 ... CA VAL 43... 4.76
..Cl SB2 1504... 4.83 ...CGI VAL 43... 4.30
OE1 GLU 41 ... N GLU 42... 70 ...CGI VAL 49... 4.22
3.74 ... CA VAL 49... 3.98
.. CD2 PHE 69... 4.25 ... CB VAL 49... 4.45 ..O GLU 42... 5.00 ... CG2 VAL 49... 4.49 .. CE2 PHE 69... 4.08 ...C3 SB2 1504... 5.00
75 ...C4 SB2 1504... 4.79 N GLU 42 ... CB GLU 41... .. C VAL 43... 4.60
3.22 40 .. O VAL 43... 4.71
.. CG GLU 41 3.16 .. N ASN 44... 4.61
.. OEl GLU 41 ... 3.74 .. CA ASN 44.. 4.82
..CD GLU 41 ... 3.77 .. N VAL 43... 4.03
..CGI VAL 43 ... 4.81 .. CA VAL 43.. 5.00
.. OE2 GLU 41 ... 4.77 45 OEl GLU 42 ... CA GLY 47
CA GLU 42 ... C GLY 47... ...4.57
4.95 .. C GLY 47... 3.97
..0 GLY 47.. . 4.06 .. O GLY 47... 3.90
.. CA VAL 48 .. 4.71 .. N VAL 48... 4.12
..CB GLU 41 .. 4.51 50 .. CA VAL 48.. 4.29
.. CG GLU 41 .. 4.26 .. CB VAL 48.. 4.62
.. N ASN 44.. 4.82 .. CGI VAL 48. . 4.06
.. CD GLU 41 .. 4.91 ..N VAL 43... 4.70
.. CB VAL 43 .. 4.86 OE2 GLU 42 ... CA GLY 47
..CGI VAL 43 ... 4.78 55 ...4.18
CB GLU 42 ...0 GLY 47... .. C GLY 47... 4.06
4.95 .. O GLY 47... 3.74
.. CA GLU 41 .. 4.76 .. N VAL 48... 4.83
.. C GLU 41.. 3.62 .. C VAL 43... 4.00
.. O GLU 41.. . 4.11 60 .. O VAL 43... 3.93
..N VAL 43.. . 3.61 .. N ASN 44... 3.96
.. CA VAL 43 .. 4.81 .. CA ASN 44.. 3.90
CG GLU 42 ...0 GLY 47... .. CB ASN 44... 4.58
4.87 .. C ASN 44... 4.98
.. C GLU 41.. 4.95 65 ..N GLY 45... 4.90
.. C VAL 43.. 4.66 .. N GLY 47... 4.43
.. N ASN 44.. 4.45 ..N VAL 43... 4.08
.. CA ASN 44 .. 4.90 .. CA VAL 43.. 4.75
.. N VAL 43.. . 3.84 C GLU t 12 ...O GLY 4"/
.. CA VAL 43 .. 4.79 70 4.13
CD GLU 42 ... CA GLY 47... .. CB GLU 41... 4.73
4.74 .. CG GLU 41.. 4.09
.. C GLY 47.. 4.26 ..N ASN 44... 3.53
..0 GLY 47.. 3.92 .. CA ASN 44... 4.73
..N VAL 48.. 4.75 75 .. CD GLU 41.. 4.83
.. CA VAL 48 .. 4.99 .. CB VAL 43... 3.66 ... CGI VAL 43... 3.79 .. CA ASN 44.. 4.90
... CG2 VAL 43 ... 4.42 40 ..C GLU 42... 3.66
0 GLU 42... CG GLU 41... .. O GLU 42... 4.07
4.04 .. CGI VAL 49 .. 4.31
...OEl GLU 41 ... 5.00 .. CB TRP 46.. 4.81
...N ASN 44.. 3.39 .. CG TRP 46.. . 4.97
... CA ASN 44. .. 4.62 45 .. CD1 TRP 46. .. 4.37
...CD GLU 41 .. 4.48 .. C12SB2 1504 .. 4.59
... CB VAL 43. .. 4.07 CGI VAL 43 ...CB GLU 41
.. CGI VAL 43 ... 4.22 ...4.63
.. OE2 GLU 41 ... 4.79 .. CG GLU 41. . 4.16
N VAL 43... OEl GLU 42... 50 .. C GLU 41... 4.56
4.70 .. O GLU 41... 4.30
..C GLY 47.. 4.55 ..N GLU 42... 4.81
.. O GLY 47.. 3.35 .. CA GLU 42. . 4.78
.. CA GLU 41. .. 4.94 .. N ASN 44... 4.87
.. CG GLU 41. .. 4.51 55 ..C GLU 42... 3.79
.. C GLU 41.. 3.63 .. O GLU 42... 4.22
.. O GLU 41.. 3.49 .. CGI VAL 49 .. 4.09
.. CG GLU 42. .. 3.84 .. CB VAL 49. . 4.90
..CD GLU 42. .. 4.03 ..CG2VAL 49 .. 4.40
.. OE2 GLU 42 ... 4.08 60 ..C2 SB2 1504. . 3.80
..CB GLU 42. .. 3.61 .. C3 SB2 1504. . 3.79
.. CGI VAL 49 ... 4.66 .. C4 SB2 1504. . 4.81
CA VAL 43 ...O GLY 47... ..Cl SB2 1504. . 4.84
4.17 ..C12SB2 1504 .. 3.36
..C GLU 41... 4.88 65 ..C13SB2 1504 .. 4.74
.. O GLU 41.. 4.76 CG2 VAL 43 ...C GLY 47...
.. CG GLU 42. .. 4.79 4.82
.. CD GLU 42. .. 5.00 .. O GLY 47... 3.78
.. OE2 GLU 42 ... 4.75 ..N ASN 44... 4.25
.. CB ASN 44. . 4.87 70 .. N GLY 47... 4.50
..N GLY 45.. 4.96 ..C GLU 42... 4.42
..CB GLU 42. . 4.81 .. CGI VAL 49 .. 3.33
CB VAL 43 ...O GLY 47... ..CB VAL 49.. . 4.67
4.52 .. CG2 VAL 49 .. 4.84
.. CA GLU 42. .. 4.86 75 ..N TRP 46... 4.09
..N ASN 44... 3.67 .. CA TRP 46.. 4.18 ... CB TRP 46... 3.40 N ASN 44... CA GLU 42...
... CG TRP 46... 3.77 4.82
... CD1 TRP 46.. . 3.52 40 ..CG GLU 42 .. 4.45
... NE1 TRP 46.. 4.71 ..CD GLU 42 .. 4.61
... C TRP 46... 4.51 .. OE2 GLU 42 ... 3.96
... S36SB2 1504.. . 4.70 ..C GLU 42.. 3.53
C VAL 43 O GLY 47... ..O GLU 42.. . 3.39
4.06 45 ..CB VAL 43 .. 3.67
.. CG GLU 42. 4.66 ..CGI VAL 43 ... 4.87
.. CD GLU 42. 4.60 .. CG2 VAL 43 ... 4.25
.. OE2 GLU 42... 4.00 .. N TRP 46... 4.84
.. CB ASN 44.... 3.72 CA ASN 44 ... CG GLU 42...
.. N GLY 45.... 3.47 50 4.90
.. N GLY 47.... 4.59 .. CD GLU 42 .. 4.82
.. CG ASN 44... 4.55 .. OE2 GLU 42 ... 3.90 .. ND2 ASN 44... 4.36 .. C GLU 42.. 4.73
.. CA GLY 45... 4.55 .. O GLU 42.. . 4.62
.. C GLY 45... 4.87 55 ..CB VAL 43 .. 4.90
.. N TRP 46... 4.10 ..N TRP 46... 4.59
.. CD1 TRP 46... 4.83 CB ASN 44... OE2GLU 42
O VAL 43... CA GLY 47... ...4.58
4.40 .. C VAL 43.. 3.72
,.C GLY 47... 4.36 60 .. O VAL 43.. . 4.25 .. O GLY 47... 3.47 .. N GLY 45.. . 3.62 .. CD GLU 42... 4.71 .. CA VAL 43 .. 4.87 .. OE2 GLU 42... 3.93 ..CA GLY 45 .. 4.87 .. CB ASN 44... 4.25 CG ASN 44... C VAL 43... ,.N GLY 45... 2.83 65 4.55 ..N GLY 47... 3.45 .. N GLY 45.. . 4.07 .. CA GLY 45... 3.78 ODl ASN 44...N GLY 45... . C GLY 45... 3.83 4.61 ,. N TRP 46... 2.93 ND2 ASN 44 ...C VAL 43... . CA TRP 46... 3.80 70 4.36 . CB TRP 46... 4.05 .. N GLY 45.. 4.46 . CG TRP 46... 4.54 C ASN A \4... OE2GLU 42... .CDITRP 46... 4.18 4.98
C TRP 46... 4.05 ...N TRP 46... 3.66
75 ...CDITRP 46... 4.94 O ASN 44...N TRP 46... ... CE3 TRP 46... 4.74 4.13 40 ... CD1 TRP 46... 4.09
...CDITRP 46... 4.61 ... NE1TRP 46... 4.66
N GLY 45 ... OE2GLU 42... N TRP 46... C VAL 43... 4.90 4.10
...C VAL 43... 3.47 ...O VAL 43... 2.93 ...O VAL 43... 2.83 45 ...N ASN 44... 4.84 ... CB ASN 44... 3.62 ... CA ASN 44... 4.59 ... N GLY 47... 4.30 ... C ASN 44... 3.66 ... CA VAL 43... 4.96 ...0 ASN 44... 4.13 ... CG ASN 44... 4.07 ... CG2 VAL 43... 4.09 ... ODl ASN 44... 4.61 50 C CAA T TRRPP 4 466......00 VVAALL 4433... ... ND2 ASN 44... 4.46 3.80 ... CD1 TRP 46... 4.71 ... CG2 VAL 43... 4.18 CA GLY 45 ... C VAL 43 CB TRP 46... CA GLY 4~ ' ...
4.55 4.68
... O VAL 43... 3.78 55 ...C GLY 47... 4.98
... CB ASN 44... 4.87 ...0 GLY 47... 4.67
... N GLY 47... 4.69 ...O VAL 43... 4.05
... CB TRP 46... 4.69 ...N GLY 47... 3.45
... CG TRP 46... 4.55 ...CB VAL 43... 4.81
... CD1 TRP 46... 4.19 60 ... CGI VAL 49... 4.40
... NE1 TRP 46... 4.86 ... C35 SB2 1504... 4.79
C C GGLLYY 45 ... C VAL 43 .. 4.87 ... C37 SB2 1504... 4.34
...O VAL 43... 3.83 ... CG2 VAL 43... 3.40
...N GLY 47... 3.79 ... CA GLY 45... 4.69
...CB TRP 46... 3.46 65 ...C GLY 45... 3.46
... CG TRP 46... 3.50 ... O GLY 45... 3.81
... CD2TRP 46... 4.32 ... S36 SB2 1504... 4.51
... CE2 TRP 46... 4.79 CG TRP 46...O VAL 43
... CD1 TRP 46... 3.59 4.54
... NE1TRP 46... 4.40 70 ... N GLY 47... 4.74
0 GLY 45 ...N GLY 47 ... CB VAL 43... 4.97
4.40 ... C35 SB2 1504... 4.69
... CB TRP 46... 3.81 ... C37 SB2 1504... 4.30
... CG TRP 46... 3.76 ... CG2 VAL 43... 3.77
... CD2 TRP 46... 4.19 75 ... CA GLY 45... 4.55
... CE2 TRP 46... 4.73 ... C GLY 45... 3.50 ... O GLY 45... 3.76 ... S36SB2 1504... 4.43 ... S36SB2 1504... 4.04 40 CZ2TRP 46...S36SB2 1504... CD2TRP 46... C35SB2 1504 4.90
...4.51 ...CA GLY 184... 4.43
..C37SB2 1504 .. 3.88 ...0 GLY 184... 4.08
.. C GLY 45... 4.32 ... C GLY 184... 4.07
..0 GLY 45.. 4.19 45 ... N ASN 185... 4.38
.. S36SB2 1504 .. 4.01 ... CA ASN 185... 4.76
CE2 TRP 46 ... C37SB2 1504 CZ3 TRP 46... C35SB2 1504
...4.77 ...4.97
.. C GLY 45... 4.79 ...C37SB2 1504... 3.94
..0 GLY 45... 4.73 50 ... N38SB2 1504... 4.51
.. S36SB2 1504 .. 4.27 ...N44SB2 1504... 4.41
..C GLY 184.. . 4.96 ...N GLY 184... 4.98
CE3 TRP 46... C35SB2 1504 ... CA GLY 184... 4.47
...4.41 ...0 GLY 184... 4.96
..C37SB2 1504 .. 3.38 55 ... C GLY 184... 4.86
..0 GLY 45... 4.74 CH2 TRP 46... C37SB2 1504
.. S36SB2 1504. .. 4.42 ...4.83
.. N38SB2 1504 ... 4.20 ... N GLY 184... 4.67
.. N44SB2 1504 ... 4.54 ... CA GLY 184... 4.04
CDITRP 46... C VAL 43... 60 ...O GLY 184... 3.91
4.83 ...C GLY 184... 4.01
..O VAL 43... 4.18 ...N ASN 185... 4.70
..C ASN 44... 4.94 C TRP 46... N VAL 48. ..O ASN 44... 4.61 4.28
.. N GLY 45... 4.71 65 ... O VAL 43... 4.05
.. CB VAL 43. . 4.37 ... CGI VAL 49... 4.78
.. CG2 VAL 43 ... 3.52 ... CG2 VAL 43... 4.51
.. CA GLY 45. .. 4.19 0 TRP 46... N VAL 48. .. C GLY 45... 3.59 4.20
..0 GLY 45... 4.09 70 ...O VAL 48... 4.67
.. S36SB2 1504. .. 4.29 ... CGI VAL 49... 4.78
NE1 TRP 46... CG2VAL 43 N GLY 47...OE2GLU 42...
...4.71 4.43
.. CA GLY 45. . 4.86 ...C VAL 43... 4.59
..C GLY 45... 4.40 75 ...O VAL 43... 3.45
..0 GLY 45... 4.66 ... N GLY 45... 4.30 ... CGI VAL 49... 4.98 ... CD GLU 42... 3.92
... CG2 VAL 43 ... 4.50 40 ... OE2 GLU 42 .. 3.74
... CA GLY 45. .. 4.69 ...C VAL 43... 4.06
... C GLY 45... 3.79 ...O VAL 43... 3.47
...0 GLY 45... 4.40 ... CB GLU 42. . 4.95
... CB TRP 46.. . 3.45 ... C GLU 42... 4.13
... CG TRP 46.. . 4.74 45 ...N VAL 43... 3.35
CA GLY 47 ...OEl GLU 42 ... CA VAL 43. .. 4.17
...4.57 ...CB VAL 43. . 4.52
...CB VAL 48. . 4.97 ...CGI VAL 49 .. 3.56
...CGI VAL 48 ... 4.86 ... CA VAL 49. . 4.79
...CD GLU 42. .. 4.74 50 ...CB VAL 49. . 4.79
... OE2 GLU 42 .. 4.18 ... CG2 VAL 43 .. 3.78
... O VAL 43... 4.40 ... CB TRP 46.. 4.67
... CB TRP 46.. 4.68 N VAL 48... OEl GLU 42...
C GLY 47 ... OEl GLU 42... 4.12
3.97 55 ...O GLU 41... 4.88
...CB VAL 48. . 3.76 ... CD GLU 42. . 4.75
... CGI VAL 48 .. 3.96 ... OE2 GLU 42 .. 4.83
... CG2VAL 48 .. 4.71 ... O TRP 46... 4.20
... N VAL 49... 3.95 ...CGI VAL 49 .. 4.43
... O GLU 41... 4.96 60 ... C TRP 46... 4.28
... CA GLU 42. . 4.95 CA VAL 48 ...OEl GLU 42
...CD GLU 42. . 4.26 ...4.29
... OE2 GLU 42 .. 4.06 ...C GLU 41... 4.79
... O VAL 43... 4.36 ... O GLU 41... 3.77
...N VAL 43... 4.55 65 ... CA GLU 42. . 4.71
...CGI VAL 49 .. 4.13 ... CD GLU 42. . 4.99
... CG2 VAL 43 .. 4.82 ...CGI VAL 49 .. 4.12
... CB TRP 46.. 4.98 ...CB VAL 49. . 4.57
0 GLY 47 ... OEl GLU 42... CB VAL 48... OEl GLU 42
3.90 70 ...4.62
... CB VAL 48. . 4.20 ... CA GLY 47. . 4.97
... CGI VAL 48 .. 4.62 ... C GLY 47... 3.76
... N VAL 49... 3.71 ... O GLY 47... 4.20
... O GLU 41... 4.15 ... N VAL 49... 3.24
... CA GLU 42. . 4.06 75 ...O GLU 41... 4.42
... CG GLU 42. . 4.87 ... CA VAL 49. . 4.45 CGI VAL 48 ...OEl GLU 42 ... O GLU 41.. 3.98
...4.06 40 ... CD PRO 50. 2.86
... CA GLY 47... 4.86 ... CB PRO 50. 4.65 ... C GLY 47... 3.96 ... CG PRO 50. 4.31 ...O GLY 47... 4.62 ... C4 SB2 1504. 4.93 ...N VAL 49... 4.64 CB VAL 49...O GLY 47...
CG2VAL 48 ... C GLY 47... 45 4.79
4.71 . CA VAL 48. 4.57
... N VAL 49... 3.45 . C VAL 48... 3.30 ... C VAL 49... 4.76 .0 VAL 48... 3.45 ... CA VAL 49... 4.26 .0 GLU 41... 4.45
C VAL 48 ...O GLU 41... 50 .. CGI VAL 43 4.90
3.89 ,.N PRO 50... 3.32
.. N PRO 50... 4.35 . CD PRO 50. 3.66 .. CD PRO 50... 4.54 . CA PRO 50. 4.62 ..CGI VAL 49... 3.17 . C PRO 50... 4.90 .. CB VAL 49... 3.30 55 . O PRO 50... 4.35 .. CG2 VAL 49... 4.52 .. C35SB2 1504 4.96
O VAL 48...N PRO 50... 4.50 .. ND1 HIS 215. 4.92 .. CD PRO 50... 4.28 .. C3 SB2 1504. 4.50 ..O TRP 46... 4.67 .. C4 SB2 1504. 4.59
CGI VAL 49... 3.42 60 . CG2 VAL 43 4.67 ... CB VAL 49... 3.45 CGI VAL 49... C GLY 47 CG2 VAL 49... 4.86 4.13 N VAL 49... C GLY 47 . O GLY 47... 3.56 3.95 . N VAL 48... 4.43
.. O GLY 47... 3.71 65 . CA VAL 48.. 4.12
.. CB VAL 48... 3.24 . C VAL 48... 3.17
.. CGI VAL 48... 4.64 . O VAL 48... 3.42
..CG2VAL 48... 3.45 . O GLU 41... 4.22
.. N GLU 41... 4.61 . N GLY 47... 4.98
.. C GLU 41... 4.24 70 . N VAL 43... 4.66
.. O GLU 41... 3.03 . CB VAL 43.. 4.31
.. CD PRO 50... 4.05 . CGI VAL 43. 4.09 CA VAL 49 ... O GLY 47... N PRO 50... 4.71
4.79 O TRP 46... 4.78
.. CB VAL 48... 4.45 75 C35SB2 1504 4.84
..CG2VAL 48... 4.26 C3 SB2 1504. 4.92 .. CG2 VAL 43... 3.33 .. C GLU 41... 4.10
.. CB TRP 46.. . 4.40 40 .. O GLU 41... 3.32
..C TRP 46... 4.78 .. C5 SB2 1504... 4.28
.. S36SB2 1504 .. 4.92 .. CD PRO 50... 3.62
CG2 VAL 49...C VAL 48... ..CB PRO 50... 4.13
4.52 .. CG PRO 50... 4.56
..0 VAL 48.. 4.86 45 ..N LYS 51... 4.22
..O GLU 41.. 4.49 ..C3 SB2 1504... 4.37
..C5 SB2 1504. . 4.60 .. C4 SB2 1504... 3.53
..CGI VAL 43 ... 4.40 N PRO 50...C VAL 48...
..N PRO 50... 3.45 4.35
.. CD PRO 50. . 4.15 50 ..O VAL 48... 4.50
.. CA PRO 50. . 4.41 ..CGI VAL 49... 4.71
..C PRO 50... 4.27 .. CB VAL 49... 3.32
.. O PRO 50... 3.61 .. CG2 VAL 49... 3.45 .. CB HIS 215.. . 4.71 .. C4 SB2 1504... 4.78
..CG HIS 215.. . 4.48 55 CD PRO 50... C VAL 48...
..ND1H1S 215 .. 3.78 4.54
.. CE1 HIS 215. . 4.34 .. O VAL 48... 4.28
.. C2 SB2 1504. .. 4.40 ..N VAL 49... 4.05 .. C3 SB2 1504.. 3.10 .. C VAL 49... 2.50
.. C4 SB2 1504. . 3.24 60 .. O VAL 49... 3.62
.. CG2 VAL 43 ... 4.84 .. N LYS 51... 4.53
.. C12SB2 1504 .. 4.99 ..CA HIS 215... 4.90
C VAL ' \9...CG2VAL 48... .. C HIS 215... 4.76 4.76 ..O HIS 215... 4.28
.. N GLU 41... 4.28 65 .. CA VAL 49... 2.86
.. O GLU 41... 4.07 .. CB VAL 49... 3.66
.. CD PRO 50. . 2.50 .. CG2VAL 49... 4.15
..CB PRO 50.. . 3.57 CA PRO 50... CB VAL 49... .. CG PRO 50.. 3.64 4.62
..N LYS 51... 4.31 70 ..CG2VAL 49... 4.41
..C3 SB2 1504. . 4.83 .. C4 SB2 1504... 4.82
.. C4 SB2 1504. . 4.16 ..CB LYS 51... 4.67
O VAL 49... N GLU 41... CB PRO 50...C VAL 49...
3.08 3.57
..CA GLU 41. . 4.06 75 ..O VAL 49... 4.13
..CB GLU 41. 4.45 ..N LYS 51... 3.20 ... CA LYS 51... 4.47 ...CB LYS 51... 3.63
...C LYS 51... 4.91 40 ...CG LYS 51... 4.78
... CA VAL 49... 4.65 ...CD LYS 51... 4.69
CG PRO 50...C VAL 49 ...N HIS 215... 4.25
3.64 ... CD2 HIS 215... 4.92
... O VAL 49... 4.56 N LYS 51 ... C VAL 49
... N LYS 51... 4.04 45 4.31
... CA HIS 215... 4.54 ... O VAL 49... 4.22
... C HIS 215... 4.35 ... C5 SB2 1504... 4.52
... O HIS 215... 4.19 ...CD PRO so- 4.53
... CA VAL 49... 4.31 ...CB PRO so... 3.20
... N SER 216... 4.90 50 ...CG PRO 50... 4.04
C PRO 50...C5 SB2 1504 ... NDl HIS 215... 4.52
4.69 ...C4 SB2 1504... 4.39
... CA HIS 215... 4.52 CA LYS 51 .. C5 SB2 1504...
... CB VAL 49... 4.90 4.53
... CG2VAL . 49... 4.27 55 ...CB PRO 50... 4.47
... CG HIS 215... 4.95 ... NDl HIS 215... 4.12
... NDl HIS 215... 3.98 ... CE1 HIS 215... 4.48
... CE1 HIS 215... 4.81 ... C4 SB2 1504... 4.55
... C4 SB2 1504... 4.17 CB LYS 51 .. C5 SB2 1504...
... CB LYS 51... 3.39 60 3.48
... CG LYS 51... 4.74 ...C6 SB2 1504... 4.33
... CD LYS 51... 4.99 ...CA PRO 50... 4.67
O PRO 50...C5 SB2 1504 ...C PRO so- 3.39
4.74 ...O PRO so... 3.63
... CA HIS 215... 3.49 65 ...NDl HIS 215... 4.37
...C HIS 215... 4.38 ... CE1 HIS 215... 4.28
...O HIS 215... 4.62 ... C3 SB2 1504... 4.96
... CB VAL 49... 4.35 ... C4 SB2 1504... 3.87
... CG2 VAL 49... 3.61 ... CB ASP 99... 4.69
...CB HIS 215... 3.83 70 ... ODl ASP 99... 4.82
... CG HIS 215... 3.73 CG LYS 51 .. C5 SB2 1504..
...NDl HIS 215... 2.85 4.31
... CE1 HIS 215... 3.83 ... C6 SB2 1504... 4.77
... NE2 HIS 215... 4.94 ... C PRO 50... 4.74
...C3 SB2 1504... 4.74 75 ...O PRO 50... 4.78
...C4 SB2 1504... 3.96 ...NDl HIS 215... 4.78 .. CE1 HIS 215 .. 4.39
.. C4 SB2 1504 .. 4.82 40 C LYS 51 ...CB PRO 50...
.. CA ASP 99. . 4.67 4.91
..CB ASP 99. . 3.89 N PHE 69 ...O ASP 99...
.. CG ASP 99. . 4.42 4.79
..ODl ASP 99 ... 4.04 ..O SER 98... 4.72
.. C ASP 99... 4.50 45 CA PHE 69 ... CA ASP 99...
..0 ASP 99... 3.68 4.63
CD LYS 51 ...C PRO . 50... .. O SER 98... 3.97
4.99 .. C SER 98... 4.90
.. O PRO 50.. 4.69 CB PHE 69...C6 SB2 1504...
..CG HIS 215. . 4.88 50 4.34
..NDl HIS 215 ... 4.05 .. CA ASP 99... 4.88
.. CE1 HIS 215 .. 3.66 .. O SER 98... 4.79
.. NE2 HIS 215 .. 4.31 CG PHE 69 ... C5 SB2 1504...
.. CB ASP 99. . 4.16 4.97
.. CG ASP 99. . 4.14 55 .. C6 SB2 1504... 3.93
..ODl ASP 99 ... 3.45 ..OE2GLU 41... 4.96
..C ASP 99... 4.79 .. CA ASP 99... 4.79
.. O ASP 99... 4.10 ..Cl SB2 1504... 4.54
.. SG CYS 176 .. 4.89 ..O SER 98... 4.61
..ZN ZN 1501 .. 4.59 60 CD1 PHE 69 ... C5 SB2 1504
CE LYS 51 ... CE1 HIS 215... ...4.94
4.51 .. C6 SB2 1504... 3.70
.. NE2 HIS 215 .. 4.80 ..N ASP 99... 3.89
.. CA ASP 99. . 4.66 .. CA ASP 99... 3.77
.. CB ASP 99. . 4.04 65 ..CB ASP 99... 4.12
.. CG ASP 99. . 3.80 ..Cl SB2 1504... 3.97
..ODl ASP 99 .. 3.31 .. O SER 98... 3.67
.. OD2 ASP 99 .. 4.60 .. OG SER 98... 4.22
..C ASP 99... 4.00 .. CA SER 98... 4.70
..O ASP 99... 3.36 70 ..CB SER 98... 4.26
..SG CYS 176 .. 4.21 .. C SER 98... 3.83
.. ZN ZN 1501. .. 4.38 CD2 PHE 69 ...CG GLU 41
NZ LYS 51 ...CG ASP 99... ...4.89
4.99 ..OEl GLU 41... 4.25
.. ODl ASP 99 .. 4.69 75 .. C6 SB2 1504... 4.48
..C ASP 99... 4.26 ..CD GLU 41... 4.12 .. OE2 GLU 41... 3.93 ...0 HIS 97... 4.62
.. Cl SB2 1504. .. 4.96 40 ... N HIS 97... 3.42
CE1 PHE 69 ... C6 SB2 1504... 0 HIS 95 ... CA HIS 97...
4.07 4.54
.. OE2 GLU 41 ... 4.66 ...C HIS 97... 4.58
..N ASP 99... 4.12 ...0 HIS 97... 3.85
.. CA ASP 99. . 4.41 45 ...N HIS 97... 3.45
..CB ASP 99.. . 4.62 CB HIS 95 ... N HIS 97...
..Cl SB2 1504. .. 3.89 4.65
..0 SER 98... 4.23 CG HIS 95 ... CA HIS 97...
.. OG SER 98. . 3.35 4.87
..CA SER 98. . 4.53 50 ... CB HIS 97... 4.50
..CB SER 98.. . 3.77 ... CG HIS 97... 4.84
.. C SER 98... 4.06 ...NDl HIS 97... 4.79
CE2 PHE 69... CG GLU 41... ... CD2HIS 157... 4.62
4.54 ...ZN ZN 1500... 4.13
.. OEl GLU 41 ... 4.08 55 ...N HIS 97... 4.05
.. C6 SB2 1504. .. 4.80 NDl HIS 95 ... OD2ASP 99...
..CD GLU 41 .. 3.67 4.70
.. OE2 GLU 41 ... 3.07 ... CA HIS 97... 4.84
.. Cl SB2 1504. .. 4.90 ... O HIS 97... 4.58
CZ PHE 69 ... CG GLU 41... 60 ...CB CYS 176... 4.84
4.87 ...SG CYS 176... 4.34
.. C6 SB2 1504... 4.62 ... CB HIS 97... 4.46
..CD GLU 41... 4.30 ... ZN ZN 1500... 4.27
.. OE2 GLU 41... 3.55 ...N HIS 97... 4.26
..Cl SB2 1504... 4.38 65 CCDD22 HHIISS 9 955 ...... CCAA HHIISS 9977...
..OG SER 98... 4.10 4.50
..CB SER 98... 4.66 ..CB CYS 176... 4.65
C PHE 69...0 SER 98. .. SG CYS 176... 4.73
4.43 .. CB HIS 97... 3.78
0 PHE 69...0 SER 98 70 .. CG HIS 97... 3.84
3.99 .. NDl HIS 97... 3.55
...C SER 98... 4.95 .. CE1 HIS 97... 4.43
CA HIS 95 ...N HIS 97. .. CD2 HIS 97... 4.82
4.62 .. CG HIS 157... 4.76
C HIS 95 ... CA HIS 97. 75 .. CD2 HIS 157... 3.55
4.72 .. NE2 HIS 157... 3.97 ... ZN ZN 1500.. 2.88 ...NDl HIS 97... 4.41
...S20SB2 1504... 4.82 40 ... CD2 HIS 157... 4.58
...N HIS 97... 3.93 ... NE2 HIS 157... 4.75
NE2 HIS 95 ...CG ASP 99... ... ZN ZN 1500... 3.23 4.81 ... S20 SB2 1504... 4.41
... ODl ASP 99 4.91 ... N HIS 97... 4.28
... OD2 ASP 99 3.90 45 N HIS 9 977 ...... NNEE22HHIISS 9955
...C19SB2 1504 . 4.68 4.10
... CA HIS 97.. 4.25 ... CE1HIS 95... 4.28
... C HIS 97... 4.94 ...CA HIS 95... 4.62
... O HIS 97... 4.80 ...O HIS 95... 3.45
... CB CYS 176 3.99 50 ... CB HIS 95... 4.65
... SG CYS 176 3.70 ... CG HIS 95... 4.05
... ZN ZN 1501 4.08 ...NDl HIS 95... 4.26
... CE1 HIS 157 4.93 ... CD2 HIS 95... 3.93
... CB HIS 97.. 3.24 ... ZN ZN 1500... 4.97
... CG HIS 97.. 3.58 55 ...C HIS 95... 3.42
... NDl HIS 97. 3.25 CA HIS 97 ... N ASP 99
... CE1 HIS 97. 4.40 4.37
... CD2 HIS 97. 4.80 ... OD2 ASP 99.. 4.21
... CG HIS 157. 4.88 ... OG SER 98... 4.84
... CD2 HIS 157 3.54 60 ... CB SER 98... 4.87
... NE2 HIS 157 3.62 ... NE2 HIS 95... 4.25
...ZN ZN 1500 2.09 ... CE1 HIS 95... 4.47
... S20 SB2 1504 3.70 ...O HIS 95... 4.54
...N HIS 97... 4.10 ... CG HIS 95... 4.87
CE1 HIS 95 ... CG ASP 99 65 ... NDl HIS 95... 4.84
4.38 ... CD2 HIS 95... 4.50
. ODl ASP 99. . 4.53 ... ZN ZN 1500... 4.67
. OD2 ASP 99. . 3.58 ...C HIS 95... 4.72
. CA HIS 97... 4.47 C HIS 97 ...N ASP 99. . 3.12
.C HIS 97... 4.79 70 ... CA ASP 99... 4.40
.O HIS 97... 4.33 ... CG ASP 99... 4.85
.CB CYS 176. . 4.14 ... OD2 ASP 99... 3.78
. SG CYS 176. . 3.43 ...C ASP 99... 4.71
ZN ZN 1501.. . 4.10 ...OG SER 98... 4.00
.CB HIS 97... 3.74 75 ...CB SER 98... 3.73
. CG HIS 97... 4.48 ... NE2 HIS 95... 4.94 ... CE1 HIS 95... 4.79 .. ZN ZN 1500... 2.94 ...O HIS 95... 4.58 40 .. S20SB2 1504... 4.19
O HIS 97 ...N ASP 99... 2.92 NDl HIS 97 ...0D2ASP 99...
... CA ASP 99... 3.94 4.84
...CB ASP 99... 4.88 .. C19SB2 1504... 3.85
... CG ASP 99... 4.60 .. NE2 HIS 95... 3.25
... OD2 ASP 99.. 3.63 45 .. CE1 HIS 95... 4.41
...C ASP 99... 3.87 .. CG HIS 95... 4.79
... OG SER 98... 4.77 .. CE1 HIS 157... 4.22
... CB SER 98... 4.27 .. CD2 HIS 95... 3.55
... NE2 HIS 95... 4.80 .. CD2 HIS 157... 4.15
... CE1 HIS 95... 4.33 50 .. NE2 HIS 157... 3.40
...0 HIS 95... 3.85 .. ZN ZN 1500... 1.98
... NDl HIS 95... 4.58 .. S20 SB2 1504... 3.38
...C HIS 95... 4.62 CE1 HIS 97 ...C19SB2 1504...
CB HIS 97... N ASP 99 4.73
4.43 55 .. NE2 HIS 95... 4.40
... CG ASP 99... 4.61 ..CE1 HIS 157... 4.23
... OD2 ASP 99.. 3.39 .. CD2 HIS 95... 4.43
... C19SB2 1504.. . 4.00 .. CD2 HIS 157... 4.51
...N SER 98... 3.28 .. NE2 HIS 157... 3.75
...CA SER 98... 4.60 60 .. ZN ZN 1500... 3.02
... NE2 HIS 95... 3.24 .. S20 SB2 1504... 4.27
... CE1 HIS 95... 3.74 CD2 HIS 97 ... N SER 98
... CG HIS 95... 4.50 4.83
...NDl HIS 95... 4.46 .. NE2 HIS 95... 4.80
... CD2 HIS 95... 3.78 65 .. CD2 HIS 95... 4.82
... ZN ZN 1500... 3.24 .. ZN ZN 1500... 4.11
... S20SB2 1504... 4.25 NE2 HIS 97 ... ZN ZN 1500...
CG HIS 97 ...0D2ASP 99... 4.13
4.56 N SER 98 ... OD2ASP 99...
...C19SB2 1504.. 4.18 70 4.22
...N SER 98... 4.44 ... CB HIS 97... 3.28
... NE2 HIS 95... 3.58 ... CG HIS 97... 4.44
... CE1 HIS 95... 4.48 ... CD2 HIS 97... 4.83
... CG HIS 95... 4.84 CA SER 98 ... CDl PHE 69...
... CD2 HIS 95... 3.84 75 4.70
... NE2 HIS 157... 4.69 .. CE1 PHE 69... 4.53 ... CB ASP 99.. 4.89 .. CB ASP 99.. 4.11
... OD2 ASP 99 ... 4.65 40 ..0D2 ASP 99 ... 4.88
...CB HIS 97.. . 4.60 N ASP 99... CDl PHE 69...
CB SER 98...CDl PHE 69... 3.89
4.26 .. CEl PHE 69 .. 4.12
...CEl PHE 69 .. 3.77 .. OG SER 98. .. 3.64
... CZ PHE 69. . 4.66 45 .. CA HIS 97.. . 4.37
... N ASP 99... 3.41 .. C HIS 97... 3.12
... CA ASP 99. .. 4.64 .. O HIS 97... 2.92
... CA HIS 97.. . 4.87 .. CB SER 98. . 3.41
... C HIS 97... 3.73 .. CB HIS 97.. 4.43
...0 HIS 97... 4.27 50 CA ASP 99...CB PHE 69...
OG SER 98 ... CDl PHE 69... 4.88
4.22 .. CG PHE 69. .. 4.79
... CEl PHE 69 .. 3.35 ..CDl PHE 69 ... 3.77
... CZ PHE 69. . 4.10 .. C6 SB2 1504 .. 4.62
... N ASP 99... 3.64 55 .. CA PHE 69. .. 4.63
... CA ASP 99. .. 4.87 .. CEl PHE 69 .. 4.41
... CA HIS 97.. . 4.84 ..CG LYS 51. .. 4.67
... C HIS 97... 4.00 .. CE LYS 51. . 4.66
...0 HIS 97... 4.77 ..Cl SB2 1504 .. 4.78
C SER 98 ... CDl PHE 69... 60 .. OG SER 98. .. 4.87
3.83 ..C HIS 97... 4.40
... CA PHE 69. .. 4.90 .. O HIS 97... 3.94
...0 PHE 69.. 4.95 ..CB SER 98. . 4.64
... CEl PHE 69 .. 4.06 CB ASP 99 ...CDl PHE 69...
... CB ASP 99. . 3.67 65 4.12
... CG ASP 99. . 4.32 ..C5 SB2 1504 .. 4.37
...0D2 ASP 99 ... 3.97 .. C6 SB2 1504 .. 3.65
0 SER 98... CB PHE 69... .. CEl PHE 69 .. 4.62
4.79 ..CEl HIS 215. .. 4.76
... CG PHE 69. .. 4.61 70 ..C2 SB2 1504 .. 4.47
... CDl PHE 69 ... 3.67 .. CB LYS 51. . 4.69
... N PHE 69... 4.72 .. CG LYS 51. .. 3.89
... CA PHE 69. .. 3.97 .. CD LYS 51. .. 4.16
... C PHE 69... 4.43 ..CE LYS 51.. . 4.04
...0 PHE 69... 3.99 75 ..Cl SB2 1504. .. 3.71
... CEl PHE 69 .. 4.23 ..O SER 98... 4.11 ... C13SB2 1504.. 4.71 .. CB LYS 51.. 4.82
...C16SB2 1504. . 4.78 40 .. CG LYS 51.. . 4.04
...C19SB2 1504. . 4.52 .. CD LYS 51.. . 3.45
...0 HIS 97... 4.88 .. CE LYS 51.. 3.31
... CA SER 98... 4.89 .. Cl SB2 1504. . 4.56
...C SER 98... 3.67 .. C13SB2 1504 .. 4.47
... ZN ZN 1501.. . 4.42 45 .. C16SB2 1504 .. 3.79
CG ASP 99 ... C6 SB2 1504... .. C19SB2 1504 .. 3.45
4.64 .. CD2 HIS 215. .. 4.36
... NZ LYS 51... 4.99 .. NE2 HIS 95.. 4.91
...CEl HIS 215.. 4.20 ..CEl HIS 95.. 4.53
... NE2 HIS 215.. . 4.25 50 .. SG CYS 176. . 3.69
...C2 SB2 1504.. 4.74 .. ZN ZN 1501. . 2.12
... CG LYS 51.. 4.42 .. ZN ZN 1500. . 4.89
... CD LYS 51.. 4.14 .. S20SB2 1504. .. 3.76
... CE LYS 51... 3.80 OD2 ASP 99 ...NE2HIS 215
... Cl SB2 1504.. 4.38 55 ...4.94
... C13SB2 1504. .. 4.39 .. CE LYS 51.. 4.60
... C16SB2 1504. . 4.00 .. O SER 98... 4.88
... C19SB2 1504. .. 3.44 .. C13SB2 1504 .. 4.60
... C HIS 97... 4.85 ..C16SB2 1504 .. 4.13
... O HIS 97... 4.60 60 ..C19SB2 1504 .. 3.14
... C SER 98... 4.32 .. CA HIS 97... 4.21
... NE2 HIS 95... 4.81 ..C HIS 97... 3.78
... CEl HIS 95... 4.38 .. O HIS 97... 3.63
... SG CYS 176.. . 4.49 ..N SER 98... 4.22
... ZN ZN 1501.. . 3.04 65 .. CA SER 98.. . 4.65
... CB HIS 97... 4.61 ..C SER 98... 3.97
... ZN ZN 1500.. . 4.94 .. NE2 HIS 95.. 3.90
...S20SB2 1504. . 4.11 .. CEl HIS 95.. 3.58
ODl ASP 99... C6 SB2 1504 .. SG CYS 176. .. 4.53
...4.79 70 .. ZN ZN 1501. . 3.27
.NZ LYS 51... 4.69 .. NDl HIS 95.. . 4.70
NDl HIS 215... 4.33 ..CB HIS 97... 3.39
CEl HIS 215... 3.08 .. CG HIS 97... 4.56
. NE2HIS 215... 3.07 ..NDl HIS 97.. . 4.84
C2 SB2 1504... 4.62 75 .. ZN ZN 1500. . 4.11
C3 SB2 1504... 4.88 .. S20 SB2 1504. .. 3.73 C ASP 99...NZ LYS 51... .. CB CYS 176... 3.30
4.26 40 .. SG CYS 176... 4.49
..CG LYS 51 4.50 ..C CYS 176... 4.23
..CD LYS 51 4.79 .. CG HIS 95... 4.62
..CE LYS 51. 4.00 .. CD2 HIS 95... 3.55
..C HIS 97... 4.71 .. NDl HIS 97... 4.15
..O HIS 97... 3.87 45 .. CEl HIS 97... 4.51
O ASP 99...N PHE 69... .. ZN ZN 1500... 2.88
4.79 .. S20 SB2 1504... 4.08
... NZ LYS 51... 3.34 NDl HIS 157 ...O CYS 176.. ...CG LYS 51... 3.68 3.99 ... CD LYS 51... 4.10 50 .. NZ LYS 179... 3.64
... CE LYS 51... 3.36 .. O30 SB2 1504... 3.85
CA HIS 157 ...O CYS 176... ..CB CYS 176... 4.60 4.76 ..C CYS 176... 4.89 CB HIS 157 ... O CYS 176... ..O LEU 183... 4.81 3.40 55 ..O ASN 185... 3.99
...NZ LYS 179... 4.79 .. C28 SB2 1504... 4.50 ... CA CYS 176... 4.99 ..029 SB2 1504... 4.34 ... CB CYS 176... 4.64 .. ZN ZN 1500... 4.30 ... C CYS 176... 4.02 ..S20SB2 1504... 4.83
CG HIS 157 ...O CYS 176... 60 CEl HIS 57 ...O CYS 176
3.45 4.61
NZ LYS 179... 4.19 .. NZ LYS 179... 3.89
O30 SB2 1504.. . 4.59 .. O30 SB2 1504... 3.16
NE2 HIS 95... 4.88 .. NE2 HIS 95... 4.93
CA CYS 176.. 4.70 65 ..CB CYS 176... 4.47
CB CYS 176... 3.96 ..C ASN 185... 4.94
C CYS 176... 4.12 .. O ASN 185... 3.83
CD2 HIS 95... 4.76 .. C28 SB2 1504... 3.62
ZN ZN 1500... 4.13 ..029 SB2 1504... 3.46
CD2 HIS 157 ... O CYS 176... 70 ..NDl HIS 97... 4.22
3.86 .. CEl HIS 97... 4.23
..NZ LYS 179... 4.69 .. ZN ZN 1500... 3.33
.. O30SB2 1504... 4.44 .. S20 SB2 1504... 3.64
.. NE2 HIS 95... 3.54 NE2 HIS 157 ... C19SB2 1504
..CEl HIS 95... 4.58 75 ...4.65
.. CA CYS 176... 4.39 .. O CYS 176... 4.55 .. NZ LYS 179. 4.51 .. CEl HIS 157... 4.47
.. O30SB2 1504 ... 3.56 40 .. CD2 HIS 95. . 4.65
.. NE2 HIS 95.. . 3.62 ..CG HIS 157. . 3.96
..CEl HIS 95.. 4.75 .. CD2 HIS 157 .. 3.30
5 .. CA CYS 176 .. 4.98 .. NE2 HIS 157 .. 3.70
.. CB CYS 176 .. 3.70 .. ZN ZN 1500. .. 4.16
.. SG CYS 176. 4.55 45 .. S20 SB2 1504 .. 4.31
.. ZN ZN 1501. .. 4.45 .. CB HIS 157. . 4.64
.. C28 SB2 1504 .. 4.15 SG CYS 176...CEl HIS 215...
0 ..029 SB2 1504 ... 4.26 4.64
.. CD2 HIS 95.. . 3.97 .. NE2 HIS 215 .. 3.72
.. CG HIS 97... 4.69 50 .. CD LYS 51. . 4.89
..NDl HIS 97. . 3.40 .. CE LYS 51.. . 4.21
.. CEl HIS 97.. 3.75 .. CG ASP 99. . 4.49
5 .. ZN ZN 1500. .. 2.17 .. ODl ASP 99 .. 3.69
.. S20 SB2 1504 .. 2.99 .. OD2 ASP 99 .. 4.53
O HIS If 57 ... O ASN 185... 55 .. CD2 HIS 215 .. 4.06
4.85 .. O30 SB2 1504 ... 4.84
CA CYS 176...CE LYS 179 .. NE2 HIS 95. . 3.70
>0 ...4.35 .. CEl HIS 95.. . 3.43
.. NZ LYS 179. .. 4.53 .. ZN ZN 1501. .. 2.32
.. CD2 HIS 215. .. 4.98 60 ..NDl HIS 95. .. 4.34
.. ZN ZN 1501. . 4.65 .. CD2 HIS 95. . 4.73
.. CG HIS 157.. . 4.70 .. CD2 HIS 157 .. 4.49
15 .. CD2 HIS 157. .. 4.39 .. NE2 HIS 157 .. 4.55
.. NE2 HIS 157. .. 4.98 .. ZN ZN 1500. .. 4.16
.. CB HIS 157.. . 4.99 65 .. S20 SB2 1504 .. 3.97
CB CYS 176...NE2HIS 215 C CYS 1 76 ... CD LYS 179...
...4.65 4.98
(0 .. CE LYS 179. . 4.58 .. CE LYS 179. .. 4.10
.. NZ LYS 179. .. 4.40 .. NZ LYS 179 .. 4.12
.. CD2 HIS 215. .. 4.58 70 ..NDl HIS 157 .. 4.89
..030 SB2 1504 ... 4.30 ..CG HIS 157. . 4.12
.. NE2 HIS 95.. 3.99 .. CD2 HIS 157 .. 4.23
5 ..CEl HIS 95.. 4.14 .. CG LYS 179 .. 4.69
.. ZN ZN 1501. . 3.47 ..CB HIS 157. . 4.02
..NDl HIS 95.. . 4.84 75 0 CYS 1 76 ... CD LYS 179...
..NDl HIS 157. .. 4.60 4.14 .. CE LYS 179... 3.31 ... N PRO 180... 4.98
.. NZ LYS 179... 3.07 40 ...C GLY 182... 4.69
.. O30 SB2 1504... 4.70 ...O GLY 182... 3.78
.. NDl HIS 157... 3.99 ...N LEU 183... 4.89
5 ..CEl HIS 157... 4.61 ... CD2LEU 183... 4.71
.. CG HIS 157... 3.45 ... CA LEU 183... 4.12
.. CD2 HIS 157... 3.86 45 CD LYS 179... N42 SB2 1504
.. NE2 HIS 157... 4.55 ...4.87
.. CG LYS 179... 3.78 N43SB2 1504... 4.50
LO .. CA HIS 157... 4.76 O CYS 176... 4.14
..CB HIS 157... 3.40 O30SB2 1504... 4.65
N LYS 1 79...CD PRO 180 ... 50 ...C33SB2 1504... 4.64
3.45 C34SB2 1504... 4.89
.. CG PRO 180... 4.89 C CYS 176... 4.98
[5 CA LYS 179... CD PRO 180 C LEU 183... 4.03
...3.02 N GLY 184... 4.62
.. CB PRO 180... 4.74 55 ... CA GLY 184... 4.95
.. CG PRO 180... 4.46 O LEU 183... 3.71
.. N TYR 181... 4.59 C GLY 182... 4.67
>0 .. C GLY 182... 4.91 O GLY 182... 3.57
.. O GLY 182... 3.98 CA LEU 183... 4.44
CB LYS 179 ... C LEU 183 60 CE LYS 179... O CYS 176... 3.31
.. O LEU 183... 4.49 CD2HIS 215... 4.35 5 .. N PRO 180... 3.71 O30SB2 1504... 3.36
.. CD PRO 180... 4.47 C31SB2 1504... 4.79
.. CA PRO 180... 4.88 65 ...C33SB2 1504... 3.91
.. N GLY 182... 4.90 C34SB2 1504... 4.53
.. C GLY 182... 4.02 CA CYS 176... 4.35 0 .. O GLY 182... 3.20 CB CYS 176... 4.58
.. N LEU 183... 4.43 C CYS 176... 4.10
.. CD2 LEU 183... 4.14 70 ...C LEU 183... 4.67
.. CA LEU 183... 4.03 O LEU 183... 4.03
CG LYS 179...O CYS 17 C28SB2 1504... 4.34 5 3.78 O GLY 182... 4.94
... C CYS 176... 4.69 NZ LYS 179... O CYS 176... ...C LEU 183... 4.10 75 3.07 ...O LEU 183... 3.70 ... CD2HIS 215... 4.90 ...O30SB2 1504... 2.66 ... O GLY 182... 4.04
...C31SB2 1504... 4.77 40 ... CD2LEU 183... 4.61
.. C33SB2 1504... 4.29 N PRO 180...N GLY 182...
... CA CYS 176... 4.53 4.64
.. CB CYS 176... 4.40 ... O GLY 182... 4.86
... C CYS 176... 4.12 ... CB LYS 179... 3.71
.. C LEU 183... 4.16 45 ... CG LYS 179... 4.98
... N GLY 184... 4.78 CD PRO 180... CG TYR 181...
CA GLY 184... 4.60 4.99 ...NDl HIS 157... 3.64 CD2TYR 181... 4.68
CEl HIS 157... 3.89 CE2TYR 181... 4.89
O LEU 183... 3.22 50 OG SER 216... 4.42
C27SB2 1504... 4.71 CB SER 216... 4.54
C28SB2 1504... 3.65 N TYR 181... 3.60 ...029SB2 1504... 4.14 C LYS 179... 2.56
CG HIS 157... 4.19 O LYS 179... 3.64
CD2 HIS 157... 4.69 55 CA TYR 181... 4.99
NE2HIS 157... 4.51 N LYS 179... 3.45
CB HIS 157... 4.79 CA LYS 179... 3.02 C LYS 179...CD PRO 180 CB LYS 179... 4.47
2.56 CA PRO 180...CB TYR 181
CB PRO 180... 3.58 60 ...4.67
CG PRO 180... 3.67 CG TYR 181... 4.43
N TYR 181... 3.46 CD2TYR 181... 4.81
CA TYR 181... 4.79 CDl TYR 181... 4.47
N GLY 182... 4.39 CEl TYR 181... 4.87
C GLY 182... 4.81 65 N GLY 182... 4.63
O GLY 182... 4.11 .. CB LYS 179... 4.88
O LYS 179...CD PRO 180 CB PRO 180... CG TYR 181 3.64 ...4.36
... CB PRO 180... 4.11 ...CD2TYR 181... 4.45
... CG PRO 180... 4.53 70 ... CE2TYR 181... 4.41
... N TYR 181... 3.60 ... CZ TYR 181... 4.27
...CA TYR 181... 4.75 ...OH TYR 181... 4.91
...C TYR 181... 4.93 ...N TYR 181... 3.35
...N GLY 182... 4.07 ...CDl TYR 181... 4.21
... CA GLY 182... 4.86 75 ...CEl TYR 181... 4.17
...C GLY 182... 4.44 ...C LYS 179... 3.58 ...O LYS 179... 4.11 ...CG PRO 180... 3.46 ...CA TYR 181... 4.60 40 ... C LYS 179.. 3.46 ...CA LYS 179... 4.74 ... O LYS 179.. . 3.60 CG PRO 180... CB TYR 181...4.86 ... CA LYS 179 .. 4.59
... CG TYR 181... 4.10 CA TYR 181 ...CD PRO 180
...CD2TYR 181... 3.77 ...4.99
...CE2TYR 181... 3.70 45 ... CB PRO 180 .. 4.60
... CZ TYR 181... 3.98 ... CG PRO 180 ... 4.71
... OH TYR 181... 4.63 ... C LYS 179.. 4.79
... OG SER 216... 4.11 ...O LYS 179.. . 4.75
... CB SER 216... 4.69 CB TYR 181 ...CA PRO 180...
... N TYR 181... 3.46 50 4.67
... CDl TYR 181... 4.34 ...CG PRO 180 ... 4.86
...CEl TYR 181... 4.29 ...C PRO 180.. . 3.44
... C LYS 179... 3.67 ... O PRO 180.. . 3.80
...O LYS 179... 4.53 ... N GLY 182. . 3.59
... CA TYR 181... 4.71 55 ... CA GLY 182 ... 4.81
... N LYS 179... 4.89 CG TYR 181 ...CD PRO 180...4.99
... CA LYS 179... 4.46 ...CA PRO 180 .. 4.43
C PRO 180... CB TYR 181 ...CB PRO 180 .. 4.36
3.44 ... CG PRO 180 .. 4.10
... CG TYR 181... 3.46 60 ... C PRO 180.. . 3.46
... CD2 TYR 181... 4.21 ...O PRO 180.. . 3.81
... CE2 TYR 181... 4.87 ...N GLY 182. . 4.84
... CZ TYR 181... 4.88 CDl TYR 181 ...CA PRO 180...
...CDl TYR 181... 3.49 4.47
... CEl TYR 181... 4.25 65 ...CB PRO 180 .. 4.21
...N GLY 182... 3.62 ...CG PRO 180 .. 4.34
O PRO 180... CB TYR 181 ...C PRO 180.. . 3.49
3.80 ... O PRO 180.. . 3.44
... CG TYR 181... 3.81 CEl TYR 181 ...CA PRO 180
... CD2 TYR 181... 4.82 70 ...4.87
... CDl TYR 181... 3.44 ... CB PRO 180 .. 4.17
... CEl TYR 181... 4.21 ... CG PRO 180 .. 4.29
...N GLY 182... 4.06 ... C PRO 180.. 4.25
N TYR 181 ...CD PRO 180... ...O PRO 180.. 4.21
3.60 75 CD2TYR 181 ... OG SER 216..
...CB PRO 180... 3.35 4.01 ... CB SER 216.. 4.97 CA GLY 182...CB TYR 181...
...CD PRO 180. 4.68 4.81
...CA PRO 180. 4.81 40 ... N43 SB2 1504.. 4.45
...CB PRO 180. 4.45 ... N44 SB2 1504.. 4.80 ...CG PRO 180. 3.77 ...N GLY 184... 4.58
... C PRO 180... 4.21 ...O LYS 179... 4.86
... O PRO 180... 4.82 ...CB LEU 183... 4.85 CE2TYR 181 ...OG SER 216 45 C GLY 182...N43SB2 1504... ...3.68 4.16 ... CB SER 216... 4.91 ... N44 SB2 1504.. 4.51
... CD PRO 180... 4.89 ... CD LYS 179... 4.67
...CB PRO 180... 4.41 ...N GLY 184... 3.42
... CG PRO 180... 3.70 50 ... CA GLY 184.. 4.73
... C PRO 180. 4.87 ... C LYS 179... 4.81 CZ TYR 181 ... OG SER 216... ...O LYS 179... 4.44 4.82 ... CD2 LEU 183.. . 4.27
...CB PRO 180... 4.27 ... CA LYS 179... 4.91
... CG PRO 180... 3.98 55 ... CB LYS 179... 4.02
...C PRO 180... 4.88 ... CG LYS 179... 4.69 OH TYR 181 ... CB PRO 180... ...CB LEU 183... 3.69 4.91 ... CG LEU 183... 4.15
... CG PRO 180... 4.63 O GLY 182... N42SB2 1504 C TYR 181 ...N43SB2 1504... 60 ...4.39 4.75 ... N43 SB2 1504.. 3.41 ...O LYS 179... 4.93 ... N44 SB2 1504 „ 3.98
...N LEU 183... 4.77 ... CD LYS 179... 3.57 N GLY 182 ... CB TYR 181... ... CE LYS 179... 4.94 3.59 65 ... N GLY 184... 3.48
..CG TYR 181... 4.84 ... CA GLY 184.. 4.59 ...N43SB2 1504... 4.45 ... N PRO 180... 4.86
.. N PRO 180... 4.64 ...C LYS 179... 4.11
.. CA PRO 180... 4.63 ...O LYS 179... 4.04
-C PRO 180... 3.62 70 ... CD2 LEU 183.. . 4.62
-O PRO 180... 4.06 ... CA LYS 179... 3.98 ...C LYS 179... 4.39 ...CB LYS 179... 3.20
.. O LYS 179... 4.07 ... CG LYS 179... 3.78
.. CB LYS 179... 4.90 ...CB LEU 183... 4.24
75 ... CG LEU 183... 4.80 N LEU 183 ...C TYR 181... ... NDl HIS 157... 4.81
4.77 40 ...N ASN 185... 3.80
...CB LYS 179... 4.43 ...CA ASN 185... 4.86
... CG LYS 179... 4.89 ...C ASN 185... 4.74 CA LEU 183 ...CD LYS 179 ...O ASN 185... 4.62
...4.44 ...029 SB2 1504... 4.81
...CB LYS 179... 4.03 45 ...CB LYS 179... 4.49 ...CG LYS 179... 4.12 ... CG LYS 179... 3.70
CB LEU 183 ... N GLY 184... N GLY 184... N43SB2 1504.. 3.44 4.68
... CA GLY 184... 4.68 ... N44 SB2 1504... 4.30
... O GLY 184... 4.68 50 ... CD LYS 179... 4.62
...C GLY 184... 4.95 ... NZ LYS 179... 4.78
... CA GLY 182... 4.85 ... CZ3 TRP 46... 4.98
...C GLY 182... 3.69 ... CH2 TRP 46... 4.67
...O GLY 182... 4.24 ... CA GLY 182... 4.58
CG LEU 183 ... N GLY 184... 55 ...C GLY 182... 3.42
4.86 ... O GLY 182... 3.48
...C GLY 182... 4.15 ...CB LEU 183... 3.44 ...O GLY 182... 4.80 ... CG LEU 183... 4.86
CD2 LEU 183 ...O LYS 179 CA GLY 184...C35SB2 1504 ...4.61 60 ...4.69
...C GLY 182... 4.27 ... C37 SB2 1504... 4.71 ...O GLY 182... 4.62 ... S36 SB2 1504... 4.53 ...CB LYS 179... 4.14 ... N43 SB2 1504... 4.90 ...CG LYS 179... 4.71 ... N44 SB2 1504... 4.29
C LEU 183 ...CD LYS 179... 65 ... CD LYS 179... 4.95 4.03 ... NZ LYS 179... 4.60
... CE LYS 179... 4.67 ... O30 SB2 1504... 4.92 ... NZ LYS 179... 4.16 ...C31 SB2 1504... 4.49 ... N ASN 185... 4.10 ... C33 SB2 1504... 4.66 ... CB LYS 179... 4.51 70 ... C34 SB2 1504... 4.78 ...CG LYS 179... 4.10 ... CZ2 TRP 46... 4.43
O LEU 183 ...CD LYS 179... ... CZ3 TRP 46... 4.47 3.71 ...CH2TRP 46... 4.04
... CE LYS 179... 4.03 ...CB ASN 185... 4.85 ... NZ LYS 179... 3.22 75 ... C28 SB2 1504... 4.58 ... O30SB2 1504... 4.78 ...029 SB2 1504... 4.19 ...C GLY 182... 4.73 ... CA GLY 184... 4.85
...0 GLY 182... 4.59 40 ...0 GLY 184... 4.17
...CB LEU 183... 4.68 ... C GLY 184... 3.68
C GLY 184... CE2TRP 46.. ... C28 SB2 1504... 4.37
4.96 ...029 SB2 1504... 3.16
... CZ2 TRP 46... 4.07 CG ASN 185 ...025SB2 1504...
... CZ3 TRP 46... 4.86 45 4.67
... CH2 TRP 46... 4.01 ...C GLY 184... 4.93
...CB ASN 185... 3.68 ...029SB2 1504... 4.41
...C28SB2 1504... 4.73 ND2 ASN 185 ...025 SB2 1504...
...029SB2 1504... 3.95 4.19
...CG ASN 185... 4.93 50 ...029SB2 1504... 4.59
...CB LEU 183... 4.95 C ASN 185 ...CEl HIS 157...
0 GLY 184...CZ2TRP 46.. 4.08 4.94
... CZ3 TRP 46... 4.96 ... O LEU 183... 4.74
... CH2TRP 46... 3.91 ...029SB2 1504... 4.09
... CB ASN 185... 4.17 55 O ASN 185 ... NDl HIS 157...
... CB LEU 183... 4.68 3.99
N ASN 185 ...S36SB2 1504 L„ CEl HIS 157... 3.83
4.76 O LEU 183... 4.62
...O30SB2 1504... 4.55 C28SB2 1504... 4.85
...C31SB2 1504... 4.61 60 029SB2 1504... 3.76
... CZ2 TRP 46... 4.38 O HIS 157... 4.85
... CH2 TRP 46... 4.70 N HIS 215 ...O PRO 50...
...C LEU 183... 4.10 4.25
... O LEU 183... 3.80 ...CB SER 216... 4.78
... C27SB2 1504... 4.71 65 CA HIS 215 ...CD PRO 50...
... C28SB2 1504... 3.86 4.90
...029SB2 1504... 2.88 ... CG PRO 50... 4.54
CA ASN 185 ... CZ2TRP 46 ...C PRO 50... 4.52
...4.76 ... O PRO 50... 3.49
... O LEU 183... 4.86 70 ...CB SER 216... 4.52
... C28SB2 1504... 4.66 ...C34SB2 1504... 4.98
...029SB2 1504... 3.47 CB HIS 215 ...O PRO 50...
CB ASN 185 ...C23SB2 1504 3.83
4.91 ...C35SB2 1504... 4.68
...025SB2 1504... 4.11 75 ...CG2VAL 49... 4.71
...N26SB2 1504... 4.91 ...N SER 216... 3.55 ..CA SER 216... 4.76 .. C PRO 50... 3.98
-C41 SB2 1504... 4.89 40 ..0 PRO 50... 2.85
-C31 SB2 1504... 4.65 -N LYS 51... 4.52
.. C33 SB2 1504... 3.56 ..CA LYS 51... 4.12
.. C34 SB2 1504... 3.58 .. CB VAL 49... 4.92
CG HIS 215 ...C PRO 50 .. CG2 VAL 49.. 3.78
4.95 45 .. C2 SB2 1504... 4.96
„0 PRO 50... 3.73 -C3 SB2 1504... 4.04
.. C35 SB2 1504... 4.98 .. C4 SB2 1504... 4.02
.. CG2 VAL . 49... 4.48 ..CB LYS 51... 4.37
.. CD LYS 51... 4.88 ..CG LYS 51... 4.78
.. N SER 216... 4.81 50 ..CD LYS 51... 4.05
.. O30 SB2 1504... 4.84 ..ODl ASP 99... 4.33
-C31 SB2 1504... 4.22 .. C31SB2 1504... 4.83
.. C33 SB2 1504... 3.44 ..C33SB2 1504... 4.35
.. C34 SB2 1504... 3.95 ..C34SB2 1504... 4.87
.. ZN ZN 1501... 4.29 55 ..ZN ZN 1501... 4.22
.. C27 SB2 1504... 4.34 .. C27SB2 1504... 4.74
CD2 HIS ' 215 ...0 PRO 50 CEl HIS 215 „.C5 SB2 1504...
4.92 4.53
.. ODl ASP 99... 4.36 .. C PRO 50... 4.81
„ N26 SB2 1504... 4.47 60 -O PRO 50... 3.83
..C16SB2 1504... 4.94 .. CA LYS 51... 4.48
.. CE LYS 179... 4.35 .. CG2 VAL 49 „ 4.34
.. NZ LYS 179... 4.90 „ C2 SB2 1504... 4.20
.. O30 SB2 1504... 3.66 -C3 SB2 1504... 3.60
-C31 SB2 1504... 3.78 65 -C4 SB2 1504... 3.79
.. C33 SB2 1504... 3.16 .. CB LYS 51... 4.28
.. C34 SB2 1504... 4.07 -CG LYS 51... 4.39
.. CA CYS 176... 4.98 -CD LYS 51... 3.66
..CB CYS 176... 4.58 ..CE LYS 51... 4.51
.. SG CYS 176... 4.06 70 ..CB ASP 99... 4.76
.. ZN ZN 1501... 3.19 .. CG ASP 99... 4.20
.. C27 SB2 1504... 3.55 „ ODl ASP 99... 3.08
.. C28 SB2 1504... 4.14 „C1 SB2 1504... 4.86
.. S20 SB2 1504... 4.68 ..C12SB2 1504... 4.79
NDl HIS 215 ...C5 SB2 1504 75 ..C23SB2 1504... 4.91
...4.95 ..N26SB2 1504.. 4.55 ... C13SB2 1504... 4.95 O HIS 215 ...CD PRO 50... 4.28
... C16SB2 1504... 4.20 40 ... CG PRO 50... 4.19
...C19SB2 1504... 4.79 ...O PRO 50... 4.62
...C31 SB2 1504... 4.80 ... OG SER 216... 4.63 ...C33SB2 1504... 4.62 ... CB SER 216... 3.54
... SG CYS 176... 4.64 ... C41SB2 1504... 4.12
... ZN ZN 1501... 3.12 45 ... N42SB2 1504... 4.43
... C27 SB2 1504... 4.31 ...C34SB2 1504... 4.69
...S20SB2 1504... 4.85 N SER 216... CG PRO 50- NE2HIS 215 ...0 PRO 50. 4.90
4.94 ...CB HIS 215... 3.55
... C2 SB2 1504... 4.90 50 ...CG HIS 215... 4.81
...C3 SB2 1504... 4.52 CA SER 216...CB HIS 215... 4.76
...C4 SB2 1504... 4.97 CB SER 216...CA HIS 215... 4.52
... CD LYS 51... 4.31 . C HIS 215... 3.28
... CE LYS 51... 4.80 .O HIS 215... 3.54
... CG ASP 99... 4.25 55 ... CD2TYR 181... 4.97
... ODl ASP 99.. 3.07 CE2TYR 181... 4.91
...OD2ASP 99.. 4.94 N HIS 215... 4.78
... C23 SB2 1504.. . 4.37 CD PRO 180... 4.54
... N26 SB2 1504.. . 4.04 CG PRO 180... 4.69
...C13SB2 1504.. . 4.98 60 OG SER 216... C HIS 215..
... C16SB2 1504.. . 3.88 4.55
...C19SB2 1504.. 4.24 .. O HIS 215... 4.63
...O30SB2 1504.. . 3.93 ..CD2TYR 181... 4.01
... C31 SB2 1504.. 4.19 .. CE2TYR 181... 3.68
...C33SB2 1504.. 3.99 65 ...CZ TYR 181... 4.82
... CB CYS 176... 4.65 ..CD PRO 180... 4.42
... SG CYS 176... 3.72 .. CG PRO 180... 4.11
... ZN ZN 1501... 2.22 ZN ZN 1500...CG ASP 99
... C27 SB2 1504.. 3.52 4.94
... C28 SB2 1504.. 4.23 70 ... ODl ASP 99... 4.89
... S20 SB2 1504... 3.88 „ OD2 ASP 99... 4.11
C HIS 215 ...CD PRO 50. . 4.76 .. C23SB2 1504... 4.98
... CG PRO so.- 4.35 .. C16SB2 1504... 4.71
...O PRO so... 4.38 ..C19SB2 1504... 3.34
... OG SER 216... 4.55 75 ... CA HIS 97... 4.67
... CB SER 216... 3.28 O30SB2 1504... 4.65 „ NE2 HIS 95... 2.09 ..O30SB2 1504... 3.99
.. CEl HIS 95... 3.23 40 .. NE2 HIS 95... 4.08
..CB CYS 176... 4.16 ..CEl HIS 95... 4.10
.. SG CYS 176... 4.16 .. CA CYS 176... 4.65
.. ZN ZN 1501... 3.65 ..CB CYS 176... 3.47
..CG HIS 95... 4.13 .. SG CYS 176... 2.32
..NDl HIS 95... 4.27 45 .. C27 SB2 1504... 4.35
..NDl HIS 157... 4.30 .. C28 SB2 1504... 4.46
„ CEl HIS 157... 3.33 .. NE2 HIS 157... 4.45
.. CD2 HIS 95... 2.88 .. ZN ZN 1500... 3.65
..CB HIS 97... 3.24 ..S20SB2 1504... 2.40
„CG HIS 97... 2.94 50 C2 SB21504... CB GLU 41
..NDl HIS 97... 1.98 4.11
.. CEl HIS 97... 3.02 .. CG GLU 41... 4.18
.. CD2 HIS 97... 4.11 .. CGI VAL 43... 3.80
.. NE2 HIS 97... 4.13 .. CG2 VAL 49... 4.40
.. CG HIS 157... 4.13 55 ..NDl HIS 215... 4.96
.. CD2 HIS 157... 2.88 .. CEl HIS 215... 4.20
.. NE2 HIS 157... 2.17 .. NE2 HIS 215... 4.90
.. S20 SB2 1504... 2.11 ..CB ASP 99... 4.47
.. N HIS 97... 4.97 .. CG ASP 99... 4.74
ZN ZN 150 1 ...CG HIS 215 60 .. ODl ASP 99... 4.62
4.29 Cl SB215( )4...CB GLU 41
.. NDl HIS 215... 4.22 3.88
..CEl HIS 215... 3.12 „ CG GLU 41... 3.96
.. NE2 HIS 215... 2.22 .. CG PHE 69... 4.54
„ CD LYS 51... 4.59 65 .. CDl PHE 69... 3.97
.. CE LYS 51... 4.38 .. CD2 PHE 69... 4.96
..CB ASP 99... 4.42 .. CD GLU 41... 4.83
.. CG ASP 99... 3.04 .. CGI VAL 43... 4.84
.. ODl ASP 99... 2.12 .. OE2 GLU 41... 4.99
.. OD2 ASP 99... 3.27 70 .. CEl PHE 69... 3.89
.. C23 SB2 1504... 4.37 ..CE2PHE 69... 4.90
.. N26 SB2 1504.. 4.65 .. CZ PHE 69... 4.38
..C13SB2 1504... 4.88 ..CEl HIS 215... 4.86
..C16SB2 1504... 3.62 .. CA ASP 99... 4.78
.. C19SB2 1504... 3.12 75 .. CB ASP 99... 3.71
.. CD2 HIS 215... 3.19 ..CG ASP 99... 4.38 ... ODl ASP 99... 4.56 ... CB LYS 51... 3.87
C3 SB2 1504... CB GLU 41 40 ... CG LYS 51... 4.82
3.98 C5 SB21504... N GLU 41
...CG GLU 41... 4.46 4.18
-O GLU 41... 5.00 ... CA GLU 41... 4.42
-C VAL 49... 4.83 ..CB GLU 41... 3.38
-O VAL 49... 4.37 45 .. CG GLU 41... 4.34
..CGI VAL 43... 3.79 ..O VAL 49... 4.28
..0 PRO 50... 4.74 .. CG PHE 69... 4.97
..CGI VAL 49... 4.92 .. CDl PHE 69... 4.94
..CB VAL 49... 4.50 .. C PRO 50... 4.69
.. CG2 VAL 49... 3.10 50 .. O PRO 50... 4.74
.. NDl HIS 215... 4.04 -N LYS 51... 4.52
.. CEl HIS 215... 3.60 .. CA LYS 51... 4.53
.. NE2 HIS 215... 4.52 .. CG2 VAL 49... 4.60
..CB LYS 51... 4.96 ..NDl HIS 215... 4.95
.. ODl ASP 99... 4.88 55 .. CEl HIS 215... 4.53
C4 SB21504... N GLU 41 ..CB LYS 51... 3.48
4.26 .. CG LYS 51... 4.31 ... CA GLU 41... 4.52 ..CB ASP 99... 4.37
... CB GLU 41... 3.63 C6 SB21504... N GLU 41
... CG GLU 41... 4.54 60 4.98
... O GLU 41... 4.79 ... CA GLU 41... 4.86
...C VAL 49... 4.16 ...CB GLU 41... 3.52 ...0 VAL 49... 3.53 ...CG GLU 41... 4.05
... CGI VAL 43... 4.81 ... CB PHE 69... 4.34
-N PRO 50... 4.78 65 ... CG PHE 69... 3.93
... CA PRO 50... 4.82 ...CDl PHE 69... 3.70
... C PRO 50... 4.17 ... CD2 PHE 69... 4.48 ...0 PRO 50... 3.96 ...CD GLU 41... 4.80
... N LYS 51... 4.39 ... CEl PHE 69... 4.07
... CA LYS 51... 4.55 70 ... CE2 PHE 69... 4.80
... CA VAL 49... 4.93 ... CZ PHE 69... 4.62
... CB VAL 49... 4.59 ...CB LYS 51... 4.33 ... CG2 VAL 49... 3.24 ... CG LYS 51... 4.77
...NDl HIS 215... 4.02 ... CA ASP 99... 4.62
... CEl HIS 215... 3.79 75 ...CB ASP 99... 3.65
.. NE2 HIS 215... 4.97 .. CG ASP 99... 4.64 ... ODl ASP 99.. 4.79 .. CEl HIS 97... 4.73
C12SB21504... CG GLU 41... 40 .. NE2 HIS 157... 4.65
4.79 .. ZN ZN 1500... 3.34
... CB VAL 43. .. 4.59 S20SB21504...CEl HIS 215
...CGI VAL 43 ... 3.36 4.85
...CG2VAL 49 ... 4.99 .. NE2 HIS 215... 3.88
... CEl HIS 215. .. 4.79 45 .. CG ASP 99... 4.11
C13SB21504...CGI VAL 43... .. ODl ASP 99... 3.76
4.74 .. OD2 ASP 99... 3.73
...CEl HIS 215. . 4.95 .. CD2 HIS 215... 4.68
... NE2 HIS 215. .. 4.98 .. NE2 HIS 95... 3.70
... CB ASP 99.. . 4.71 50 ..CEl HIS 95... 4.41
... CG ASP 99.. . 4.39 „CB CYS 176... 4.31
... ODl ASP 99 .. 4.47 „ SG CYS 176... 3.97
... OD2 ASP 99 .. 4.60 .. ZN ZN 1501... 2.40
...ZN ZN 1501. .. 4.88 „ NDl HIS 157... 4.83
C16SB21504...CEl HIS 215... 55 .. CEl HIS 157... 3.64
4.20 .. CD2 HIS 95... 4.82
...NE2HIS 215. .. 3.88 „ CB HIS 91... 4.25
... CB ASP 99.. . 4.78 .. CG HIS 97... 4.19
... CG ASP 99.. . 4.00 .. NDl HIS 97... 3.38
...ODl ASP 99 .. 3.79 60 .. CEl HIS 97... 4.27
... OD2 ASP 99. .. 4.13 .. CD2 HIS 157... 4.08
...CD2HIS 215. .. 4.94 .. NE2 HIS 157... 2.99
... ZN ZN 1501. . 3.62 .. ZN ZN 1500... 2.11
... ZN ZN 1500. . 4.71 C23 SB215 04...CEl HIS 215
C19 SB21504... CEl HIS 215... 65 4.91
4.79 .. NE2 HIS 215... 4.37
... NE2HIS 215. .. 4.24 .. ZN ZN 1501... 4.37
... CB ASP 99.. 4.52 .. CB ASN 185... 4.91
... CG ASP 99.. . 3.44 .. ZN ZN 1500... 4.98
... ODl ASP 99. .. 3.45 70 025 SB215 04...CB ASN 18!
... OD2 ASP 99. .. 3.14 4.11
... NE2 HIS 95.. 4.68 .. CG ASN 185... 4.67
... ZN ZN 1501. . 3.12 .. ND2 ASN 185... 4.19
... CB HIS 97... 4.00 N26SB215( )4...CEl HIS 215
... CG HIS 97... 4.18 75 4.55
... NDl HIS 97.. . 3.85 .. NE2 HIS 215... 4.04 ...CD2HIS 215... 4.47 ... NE2 HIS 157... 4.26 ...ZN ZN 1501... 4.65 40 ... CG ASN 185... 4.41 ...CB ASN 185... 4.91 ... ND2 ASN 185... 4.59 C27SB21504... CG HIS 215...4.34 O30SB21504... CG HIS 215
...NDl HIS 215 .. 4.74 4.84
... CEl HIS 215. . 4.31 ... NE2 HIS 215... 3.93
... NE2 HIS 215. .. 3.52 45 -O CYS 176... 4.70
... NZ LYS 179. .. 4.71 ..CD LYS 179... 4.65
... CD2 HIS 215. .. 3.55 .. CE LYS 179... 3.36
... ZN ZN 1501. . 4.35 .. NZ LYS 179... 2.66
...N ASN 185.. . 4.71 .. CD2 HIS 215... 3.66
C28 SB21504... NE2 HIS 215... 50 ..CB CYS 176... 4.30
4.23 .. SG CYS 176... 4.84
... CE LYS 179. . 4.34 .. ZN ZN 1501... 3.99
... NZ LYS 179. „ 3.65 .. CA GLY 184... 4.92
... CD2 HIS 215. 4.14 .. NDl HIS 157... 3.85
... ZN ZN 1501. . 4.46 55 .. CEl HIS 157... 3.16
... CA GLY 184 ... 4.58 -O LEU 183... 4.78
...NDl HIS 157. „ 4.50 -N ASN 185... 4.55
... CEl HIS 157. . 3.62 „CG HIS 157... 4.59
...C GLY 184.. . 4.73 .. CD2 HIS 157... 4.44
...N ASN 185.. . 3.86 60 .. NE2 HIS 157... 3.56
... CA ASN 185 .. 4.66 .. ZN ZN 1500... 4.65
...CB ASN 185. „ 4.37 C31SB21504... CB HIS 215
...0 ASN 185.. 4.85 4.65
... NE2 HIS 157. . 4.15 ...CG HIS 215... 4.22
029 SB2 1504... NZ LYS 179 65 ..NDl HIS 215... 4.83
...4.14 „ CEl HIS 215... 4.80
...CA GLY 184 .. 4.19 .. NE2 HIS 215... 4.19
.. NDl HIS 157. .. 4.34 .. CE LYS 179... 4.79
..CEl HIS 157. . 3.46 .. NZ LYS 179... 4.77
..0 LEU 183.. 4.81 70 .. CD2 HIS 215... 3.78
-C GLY 184.. 3.95 .. CA GLY 184... 4.49
„N ASN 185.. 2.88 -N ASN 185... 4.61
.. CA ASN 185 .. 3.47 C33SB21504... CB HIS 215
..CB ASN 185. .. 3.16 3.56
.. C ASN 185.. 4.09 75 ...CG HIS 215... 3.44
..0 ASN 185.. 3.76 .. NDl HIS 215... 4.35 ... CEl HIS 215.. 4.62 .. CZ2 TRP 46... 4.90
... NE2 HIS 215. . 3.99 40 ..CA GLY 184... 4.53
... CD LYS 179. .. 4.64 -N ASN 185... 4.76
... CE LYS 179. . 3.91 C37 SB21504 ... CB TRP 46
... NZ LYS 179. . 4.29 4.34
... CD2 HIS 215. .. 3.16 „ CG TRP 46... 4.30
... CA GLY 184 .. 4.66 45 ..CD2TRP 46... 3.88
C34SB21504... CA HIS 215... ..CE2TRP 46... 4.77
4.98 „ CE3 TRP 46... 3.38
...o HIS : 215... 4.69 „ CZ3 TRP 46... 3.94
...CB HIS 215- 3.58 .. CH2 TRP 46... 4.83
... CG HIS 215.. . 3.95 50 ..CA GLY 184... 4.71
...NDl HIS 215. .. 4.87 N38 SB21504... CE3 TRP 46
... CD LYS 179. .. 4.89 4.20
... CE LYS 179. . 4.53 .. CZ3 TRP 46... 4.51
... CD2 HIS 215. „ 4.07 C41 SB21504...0 HIS 215.
...CA GLY 184 .. 4.78 55 4.12
C35 SB21504... CGI VAL 49... ..CB HIS 215... 4.89
4.84 N42SB21504... O HIS 215. .4.43
... CB VAL 49. . 4.96 ..CD LYS 179... 4.87
... CB HIS 215.. 4.68 -O GLY 182... 4.39
... CG HIS 215.. . 4.98 60 N43 SB21504... CD LYS 179
... CB TRP 46.. 4.79 4.50
... CG TRP 46.. . 4.69 .. N GLY 184... 4.68
...CD2TRP 46. .. 4.51 .. CA GLY 184... 4.90
... CE3 TRP 46. . 4.41 „ C TYR 181... 4.75
... CZ3 TRP 46. . 4.97 65 „ N GLY 182... 4.45
... CA GLY 184 „ 4.69 .. CA GLY 182... 4.45
S36SB21504... CGI VAL 49... „ C GLY 182... 4.16
4.92 „ O GLY 182... 3.41
... CG2 VAL 43 .. 4.70 N44 SB215 04 ...CE TRP 46
...CB TRP 46.. 4.51 70 4.54
... CG TRP 46.. 4.04 .. CZ3 TRP 46... 4.41
... CD2TRP 46. .. 4.01 ..N GLY 184... 4.30
... CE2TRP 46. . 4.27 .. CA GLY 184... 4.29
... CE3 TRP 46. . 4.42 ..CA GLY 182... 4.80
...CDITRP 46. . 4.29 75 -C GLY 182... 4.51
...NE1TRP 46. . 4.43 ..O GLY 182... 3.98 Table III provides the angles (°) between active site atoms that are within 4.0A of the inhibitor residue, SB2, or the metal ions, ZN+2. For simplicity, intra-residue angles are omitted
5 TABLE III 49CG2 502C2 990D1 100.80
Atoml Atom2 Atom3 Angle,0 49CG2 502C2 99CG 115.51 43CG1 502C2 41CB 71.46 40 49CG2 502C2 215NE2 67.82 43CG1 502C2 4 ICG 62.59 49CG2 502C2 215ND1 47.18 43CG1 502C2 215CE1 1 16.00 99CB 502C2 990D1 30.08
10 43CG1 502C2 49CG2 64.36 99CB 502C2 99CG 18.61 43CG1 502C2 99CB 172.99 99CB 502C2 215NE2 66.90 43CG1 502C2 990D1 148.78 45 99CB 502C2 215ND1 77.40 43CG1 502C2 99CG 157.24 99OD1 502C2 99CG 15.14 43CG1 502C2 215NE2 113.74 990D1 502C2 215NE2 37.53
15 43CG1 502C2 215ND1 106.10 990D1 502C2 215ND1 53.63 41CB 502C2 41CG 21.10 99CG 502C2 215NE2 52.26 41CB 502C2 215CE1 124.56 50 99CG 502C2 215ND1 68.48 41CB 502C2 49CG2 79.98 215NE2 502C2 215ND1 25.08 41CB 502C2 99CB 113.01 99CB 502C1 41CB 141.37
20 41CB 502C2 990D1 135.69 99CB 502C1 69CE1 74.92 41CB 502C2 99CG 131.26 99CB 502C1 4 ICG 154.67 41CB 502C2 215NE2 138.43 55 99CB 502C1 69CD1 64.78 41CB 502C2 215ND1 113.70 99CB 502C1 99CG 19.41 41CG 502C2 215CE1 145.26 99CB 502C1 69CZ 92.97
25 4 ICG 502C2 49CG2 93.07 99CB 502C1 69CG 75.32 41CG 502C2 99CB 1 19.58 99CB 502C1 990D1 31.08 41CG 502C2 990D1 148.47 60 99CB 502C1 99CA 15.01 41 CG 502C2 99CG 137.66 99CB 502C1 41CD 140.71 4 ICG 502C2 215NE2 158.48 99CB 502C1 43CG1 149.79
30 41CG 502C2 215ND1 133.41 99CB 502C 1 215CE1 65.89 215CE1 502C2 49CG2 60.46 99CB 502C1 69CE2 99.17 215CE1 502C2 99CB 66.48 65 99CB 502C1 69CD2 91.04 215CE1 502C2 990D1 40.60 99CB 502C1 410E2 135.37 215CE1 502C2 99CG 55.66 41CB 502C1 69CE1 99.29
35 215CE1 502C2 215NE2 14.21 41CB 502C1 41CG 22.32 215CE1 502C2 215ND1 13.59 41CB 502C1 69CD1 96.49 49CG2 502C2 99CB 121.06 70 41CB 502C1 99CG 155.46 CB 502C1 69CZ 84.48 69CD1 502C1 990D1 95.61 CB 502C1 69CG 80.26 40 69CD1 502C1 99CA 50.04 CB 502C1 990D1 146.49 69CD1 502C1 41CD 77.21 CB 502C1 99CA 135.91 69CD1 502C1 43CG1 142.34 CB 502C1 41CD 31.57 69CD1 502C1 215CE1 128.87 CB 502C1 43CG1 62.92 69CD1 502C 1 69CE2 34.50 CB 502C1 215CE1 1 14.10 45 69CD1 502C 1 69CD2 28.44 CB 502C1 69CE2 70.38 69CD1 502C 1 410E2 70.71 CB 502C1 69CD2 68.60 99CG 502C 1 69CZ 104.84 CB 502C1 410E2 45.99 99CG 502C1 69CG 93.72 CE1 502C1 41CG 88.61 99CG 502C 1 990D1 15.78 CE1 502C1 69CD1 20.42 50 99CG 502C1 99CA 31.94 CE 1 502C1 99CG 87.13 99CG 502C1 41CD 158.49 CE1 502C1 69CZ 18.09 99CG 502C1 43CG1 130.66 CE1 502C1 69CG 32.31 99CG 502C1 215CE1 53.81 CE1 502C1 990D1 102.85 99CG 502C1 69CE2 114.48 CE1 502C1 99CA 60.12 55 99CG 502C1 69CD2 108.93 CE1 502C1 41CD 72.48 99CG 502C1 410E2 148.78 CE1 502C1 43CG1 126.47 69CZ 502C1 69CG 36.55 CE1 502C1 215CE1 140.50 69CZ 502C1 990D1 120.62 CE1 502C1 69CE2 29.01 69CZ 502C1 99CA 78.11 CE1 502C1 69CD2 33.95 60 69CZ 502C1 41CD 55.47 CE1 502C1 410E2 61.86 69CZ 502C1 43CG1 1 10.12 CG 502C1 69CD1 93.30 69CZ 502C1 215CE1 158.53 CG 502C1 99CG 174.06 69CZ 502C1 69CE2 16.07 CG 502C1 69CZ 71.23 69CZ 502C1 69CD2 29.12 CG 502C1 69CG 80.48 65 69CZ 502C1 410E2 43.98 CG 502C1 990D1 167.24 69CG 502C1 990D1 106.20 CG 502C1 99CA 142.27 69CG 502C1 99CA 61.79 CG 502C1 41CD 16.36 69CG 502C1 41CD 65.39 CG 502C1 43CG1 55.28 69CG 502C1 43CG1 134.59 CG 502C1 215CE1 129.80 70 69CG 502C1 215CE1 132.30 CG 502C1 69CE2 60.67 69CG 502C1 69CE2 29.43 CG 502C1 69CD2 65.42 69CG 502C 1 69CD2 16.04 CG 502C1 410E2 27.82 69CG 502C1 410E2 62.47 CD1 502C1 99CG 81.29 990D1 502C1 99CA 45.58 CD1 502C1 69CZ 33.05 75 990D1 502C1 41CD 170.60 CD1 502C1 69CG 17.23 990D1 502C1 43CG1 119.19 990D1 502C1 215CE1 38.03 49CG2 502C3 410 62.28 990D1 502C1 69CE2 129.60 40 215CE1 502C3 43CG1 133.60 990D1 502C1 69CD2 122.06 215CE1 502C3 41CB 151.94 990D1 502C1 410E2 164.56 215CE1 502C3 215ND 1 18.83 5 99CA 502C1 41CD 126.86 215CE1 502C3 490 100.92 99CA 502C1 43CG1 161.06 215CE1 502C3 4 ICG 165.86 99CA 502C1 215CE1 80.86 45 215CE1 502C3 49CB 87.95 99CA 502C1 69CE2 84.28 215CE1 502C3 215NE2 13.43 99CA 502C1 69CD2 77.06 215CE1 502C3 500 52.49
10 99CA 502C1 410E2 120.42 215CE1 502C3 49C 90.74 41CD 502C1 43CG1 69.41 215CE1 502C3 990D1 39.07 41 CD 502C1 215CE1 144.90 50 215CE1 502C3 49CG1 99.86 41 CD 502C 1 69CE2 44.31 215CE1 502C3 51CB 57.42 41 CD 502C1 69CD2 49.82 215CE1 502C3 410 139.28
15 41 CD 502C1 410E2 14.52 43CG1 502C3 41CB 72.98 43CG1 502C1 215CE1 88.79 43CG1 502C3 215ND1 128.14 43CG1 502C1 69CE2 108.34 55 43CG1 502C3 490 92.12 43CG1 502C1 69CD2 118.65 43CG1 502C3 41CG 59.86 43CG1 502C1 410E2 72.70 43CG1 502C3 49CB 71.82
20 215CE1 502C1 69CE2 161.72 43CG1 502C3 215NE2 122.91 215CE1 502C1 69CD2 146.43 43CG1 502C3 50O 127.88 215CE1 502C1 410E2 157.41 60 43CG1 502C3 49C 91.99 69CE2 502C1 69CD2 16.27 43CG1 502C3 990D1 138.12 69CE2 502C1 410E2 36.23 43CG1 502C3 49CG1 54.15
25 69CD2 502C1 410E2 46.46 43CG1 502C3 51CB 163.19 49CG2 502C3 215CE1 80.30 43CG1 502C3 410 56.68 49CG2 502C3 43CG1 78.64 65 41CB 502C3 215ND1 143.14 49CG2 502C3 41CB 100.44 41CB 502C3 490 64.13 49CG2 502C3 215ND1 62.41 41CB 502C3 4 ICG 19.70
30 49CG2 502C3 490 44.51 41CB 502C3 49CB 94.50 49CG2 502C3 4 ICG 109.63 41CB 502C3 215NE2 164.1 1 49CG2 502C3 49CB 7.84 70 41CB 502C3 50O 106.78 49CG2 502C3 215NE2 83.93 41CB 502C3 49C 77.65 49CG2 502C3 50O 49.61 41CB 502C3 990D1 131.15
35 49CG2 502C3 49C 31.16 41CB 502C3 49CG1 89.95 49CG2 502C3 990D1 1 19.35 41CB 502C3 51CB 94.64 49CG2 502C3 49CG1 24.55 75 41CB 502C3 410 39.86 49CG2 502C3 51CB 92.91
Figure imgf000186_0001
215ND1 502C3 490 83.45 215ND1 502C3 41CG 162.80 215NE2 502C3 410 146.04 215ND1 502C3 49CB 70.20 40 500 502C3 49C 41.11 215ND1 502C3 215NE2 28.26 500 502C3 990D1 82.42 215ND1 502C3 50O 36.72 500 502C3 49CG1 73.84 5 215ND1 502C3 49C 72.35 500 502C3 51CB 43.91 215ND1 502C3 990D1 57.17 500 502C3 410 89.14 215ND1 502C3 49CG1 83.87 45 49C 502C3 990D1 123.48 215ND1 502C3 51CB 56.94 49C 502C3 49CG1 45.09 215ND1 502C3 410 120.51 49C 502C3 51CB 73.93 10 490 502C3 41CG 80.90 49C 502C3 410 48.88 490 502C3 49CB 43.14 990D1 502C3 49CG1 137.42 490 502C3 215NE2 1 1 1.69 50 990D1 502C3 51CB 58.67 490 502C3 50O 48.76 990D1 502C3 410 164.56 490 502C3 49C 14.34 49CG1 502C3 51CB 116.06 15 490 502C3 990D1 127.93 49CG1 502C3 410 50.33 490 502C3 49CG1 53.61 51CB 502C3 410 106.54 490 502C3 51CB 71.95 55 49CG2 502C4 490 53.65 490 502C3 410 40.84 49CG2 502C4 41CB 105.53 4 ICG 502C3 49CB 102.39 49CG2 502C4 215CE1 75.71 20 41CG 502C3 215NE2 166.21 49CG2 502C4 51CB 114.35 4 ICG 502C3 500 126.18 49CG2 502C4 50O 59.27 41CG 502C3 49C 93.20 60 49CG2 502C4 215ND1 61.68 4 ICG 502C3 990D1 129.81 49CG2 502C4 49C 40.57 41CG 502C3 49CG1 92.51 49CG2 502C4 50C 69.09 25 41CG 502C3 51CB 110.82 49CG2 502C4 41N 91.00 41CG 502C3 410 47.72 49CG2 502C4 5 IN 86.59 49CB 502C3 215NE2 91.00 65 49CG2 502C4 41CA 94.08 49CB 502C3 500 56.11 49CG2 502C4 4 ICG 105.17 49CB 502C3 49C 31.32 49CG2 502C4 51CA 96.05 30 49CB 502C3 990D1 127.01 49CG2 502C4 49CB 9.32 49CB 502C3 49CG1 17.75 49CG2 502C4 50N 46.09 49CB 502C3 51CB 98.56 70 49CG2 502C4 410 64.68 49CB 502C3 410 55.52 49CG2 502C4 43CG1 62.72 215NE2 502C3 500 64.41 49CG2 502C4 5 ICG 121.07 35 215NE2 502C3 49C 100.05 49CG2 502C4 50CA 62.76 215NE2 502C3 990D1 37.88 49CG2 502C4 49CA 26.97 215NE2 502C3 49CG1 99.54 75 49CG2 502C4 215NE2 75.49 215NE2 502C3 51CB 69.77 490 502C4 41CB 76.74
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41CA 502C5 50C 98.02 69CD1 502C5 215ND1 129.61 41CA 502C5 50O 104.84 40 69CD1 502C5 69CG 16.16 41CA 502C5 69CD1 100.32 215ND1 502Cf ϊ 69CG 144.08 41CA 502C5 215ND1 124.97 41CB 502C6 99CB 174.32 5 41CA 502C5 69CG 89.34 41CB 502C6 69CD1 108.51 5 IN 502C5 51CA 18.36 41CB 502C6 69CG 93.87 5 IN 502C5 215CE1 68.70 45 41CB 502C6 41CG 21.75 5 IN 502C5 49CG2 71.00 41CB 502C6 69CE1 102.11 5 IN 502C5 50C 16.40 41CB 502C6 51CB 1 14.28
10 5 IN 502C5 50O 28.04 41CB 502C6 69CB 98.16 5 IN 502C5 69CD1 136.09 41CB 502C6 69CD2 77.46 51N 502C5 215ND1 56.89 50 41CB 502C6 69CZ 85.21 5 IN 502C5 69CG 130.27 41CB 502C6 99CA 160.99 51CA 502C5 215CE1 59.25 41CB 502C6 99CG 162.52
15 51CA 502C5 49CG2 79.74 41CB 502C6 51CG 132.65 51CA 502C5 50C 30.20 41 CB 502C6 990D1 152.50 51CA 502C5 50O 34.36 55 41CB 502C6 41CD 30.91 51CA 502C5 69CD1 122.63 41CB 502C6 69CE2 74.26 51CA 502C5 215ND1 51.34 41CB 502C6 41CA 10.26
20 51CA 502C5 69CG 121.93 41CB 502C6 41N 27.14 215CE1 502C5 49CG2 56.67 99CB 502C6 69CD1 68.24 215CE1 502C5 50C 62.89 60 99CB 502C6 69CG 84.15 215CE1 502C5 50O 48.75 99CB 502C6 41CG 152.59 215CE1 502C5 69CD1 1 14.71 99CB 502C6 69CE1 73.25
25 215CE1 502C5 215ND1 15.22 99CB 502C6 51CB 71.37 215CE1 502C5 69CG 129.81 99CB 502C6 69CB 81.79 49CG2 502C5 50C 54.68 65 99CB 502C6 69CD2 99.94 49CG2 502C5 50O 45.47 99CB 502C6 69CZ 90.03 49CG2 502C5 69CD1 150.12 99CB 502C6 99CA 16.63
30 49CG2 502C5 215ND1 46.49 99CB 502C6 99CG 15.96 49CG2 502C5 69CG 158.21 99CB 502C6 5 ICG 53.03 50C 502C5 50O 15.1 1 70 99CB 502C6 990D1 28.58 50C 502C5 69CD1 152.11 99CB 502C6 41CD 144.09 50C 502C5 215ND1 48.75 99CB 502C6 69CE2 101.78
35 50C 502C5 69CG 146.29 99CB 502C6 41CA 175.41 50O 502C5 69CD1 153.81 99CB 502C6 41N 158.54 50O 502C5 215ND 1 34.09 75 69CD1 502C6 69CG 20.77 50O 502C5 69CG 156.27 69CD1 502C6 4 ICG 96.14 LO O t t H—
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69CD2 502C6 51CG 1 19.04 41CD 502C6 41N 55.79
69CD2 502C6 990D1 127.83 40 69CE2 502C6 41CA 81.14
69CD2 502C6 41CD 52.63 69CE2 502C6 41N 93.44
69CD2 502C6 69CE2 16.85 41CA 502C6 41N 16.89 69CD2 502C6 41CA 81.81 43CG1 502C12 43CB 12.68
69CD2 502C6 41N 90.23 43CG1 502C12 41CG 58.26
69CZ 502C6 99CA 77.47 45 43CG1 502C12 215CE1 1 11.76
69CZ 502C6 99CG 97.17 43CG1 502C12 49CG2 59.86
69CZ 502C6 51CG 132.82 43CB 502C12 41CG 68.44 69CZ 502C6 990D1 111.26 43CB 502C12 215CE1 116.40
69CZ 502C6 41CD 54.35 43CB 502C12 49CG2 67.22
69CZ 502C6 69CE2 16.87 50 41CG 502C12 215CE1 1 13.26
69CZ 502C6 41CA 93.55 41CG 502C12 49CG2 79.11
69CZ 502C6 41N 107.72 215CE1 502C12 49CG2 52.59 99CA 502C6 99CG 31.94 99CG 502C13 990D1 16.06
99CA 502C6 51CG 59.55 99CG 502C13 990D2 15.65
99CA 502C6 990D1 45.21 55 99CG 502C1 99CB 18.74
99CA 502C6 41CD 131.48 99CG 502C13 43CG1 133.20
99CA 502C6 69CE2 87.08 99CG 502C13 501ZN 37.84 99CA 502C6 41CA 163.61 99CG 502C13 215CE1 53.1 1
99CA 502C6 41N 156.98 99CG 502C13 215NE2 53.48
99CG 502C6 51CG 55.97 60 990D1 502C13 990D2 27.64
99CG 502C6 990D1 14.99 990D1 502C13 99CB 29.68
99CG 502C6 41CD 146.52 990D1 502C13 43CG1 123.51 99CG 502C6 69CE2 1 1 1.46 990D 1 502C 13 501 ZN 25.68
99CG 502C6 41CA 164.34 990D1 502C13 215CE1 37.81
99CG 502C6 41N 155.02 65 990D1 502C13 215NE2 37.46
5 ICG 502C6 990D1 50.00 99OD2 502C13 99CB 29.77
5 ICG 502C6 41CD 155.78 99OD2 502C 13 43CG1 148.85 5 ICG 502C6 69CE2 133.31 99OD2 502C13 501ZN 40.22
5 ICG 502C6 41CA 122.41 99OD2 502C13 215CE1 65.23
5 ICG 502C6 41N 105.52 70 990D2 502C 13 215NE2 61.97
990D1 502C6 41CD 154.22 99CB 502C13 43CG1 121.92
990D1 502C6 69CE2 126.19 99CB 502C 13 501ZN 54.83 990D1 502C6 41CA 150.26 99CB 502C13 215CE1 59.02
990D1 502C6 41N 140.36 99CB 502C13 215NE2 64.54
41 CD 502C6 69CE2 44.91 75 43CG1 502C1 501ZN 123.46
41 CD 502C6 41CA 39.87
Figure imgf000194_0001
43CG1 502C 13 215CE1 89.03 43CG1 502C13 215NE2 97.55 500ZN 502C16 215CD2 81.57 501ZN 502C13 215CE1 37.00 40 99CB 502C16 215CD2 84.06 501ZN 502C 13 215NE2 25.95 501ZN 502C19 990D2 63.05 215CE1 502C 13 215NE2 15.29 501ZN 502C19 500ZN 68.71 5 501ZN 502C 16 990D1 33.10 501ZN 502C19 99CG 55.05 501ZN 502C 16 215NE2 34.17 501ZN 502C19 990D1 37.20 501ZN 502C 16 99CG 46.75 45 501 ZN 502C19 97ND1 99.10 501ZN 502C 16 990D2 49.44 501ZN 502C19 97CB 97.57 501ZN 502C 16 215CE1 46.27 501ZN 502C19 97CG 106.24 10 501ZN 502C16 500ZN 49.85 501ZN 502C19 215NE2 30.49 501ZN 502C16 99CB 61.69 501 ZN 502C19 99CB 67.93 501ZN 502C16 215CD2 40.14 50 501ZN 502C19 157NE2 66.60 990D 1 502C 16 215NE2 47.20 501ZN 502C19 95NE2 59.05 990D1 502C16 99CG 18.05 501ZN 502C19 97CE1 107.95 15 990D 1 502C16 990D2 31.45 501ZN 502C 19 215CE1 39.77 990D1 502C16 215CE1 45.01 99OD2 502C19 500ZN 78.72 990D 1 502C 16 500ZN 69.30 55 99OD2 502C19 99CG 21.12 990D1 502C16 99CB 29.20 99OD2 502C19 990D1 38.09 99OD1 502C16 215CD2 58.19 99OD2 502C19 97ND1 87.03 20 215NE2 502C16 99CG 65.25 99OD2 502C 19 97CB 55.18 215NE2 502C 16 990D2 76.19 99OD2 502C19 97CG 75.55 215NE2 502C 16 215CE1 18.26 60 99OD2 502C19 215NE2 82.64 215NE2 502C16 500ZN 80.88 99OD2 502C19 99CB 30.17 215NE2 502C16 99CB 72.62 99OD2 502C19 157NE2 99.71 25 215NE2 502C16 215CD2 1 1.43 99OD2 502C19 95NE2 55.59 99CG 502C16 990D2 17.49 99OD2 502C19 97CE1 99.75 99CG 502C 16 215CE1 61.60 65 99OD2 502C19 215CE1 77.93 99CG 502C 16 500ZN 68.56 500ZN 502C19 99CG 93.57 99CG 502C16 99CB 17.09 500ZN 502C19 990D1 92.23 30 99CG 502C16 215CD2 76.22 500ZN 502C19 97ND1 30.94 990D2 502C 16 215CE 1 76.45 500ZN 502C19 97CB 51.45 99OD2 502C16 500ZN 55.00 70 500ZN 502C19 97CG 44.27 99OD2 502C16 99CB 30.06 500ZN 502C19 215NE2 94.70 990D2 502C 16 215CD2 86.00 500ZN 502C19 99CB 107.70 35 215CE1 502C 16 500ZN 95.84 500ZN 502C 19 157NE2 25.37 215CE1 502C 16 99CB 63.64 500ZN 502C 19 95NE2 23.22 215CE 1 502C 16 215CD2 26.22 75 500ZN 502C19 97CE1 39.45 500ZN 502C16 99CB 84.50
Figure imgf000195_0001
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Figure imgf000196_0001
501 ZN 502S20 157NE2 1 1 1.13 501ZN 502S20 97ND1 133.48 97ND1 502S20 990D2 85.72
501ZN 502S20 157CE1 1 18.66 40 97ND1 502S20 990D1 1 18.96
501ZN 502S20 95NE2 80.93 97ND1 502S20 215NE2 164.56
501ZN 502S20 990D2 60.02 97ND1 502S20 176SG 1 1 1.58
5 501ZN 502S20 990D1 31.24 97ND 1 502S20 157CD2 66.91
501ZN 502S20 215NE2 31.37 97ND1 502S20 99CG 103.01
501ZN 502S20 176SG 32.17 45 97ND1 502S20 97CG 16.73
501ZN 502S20 157CD2 99.32 97ND1 502S20 97CB 36.03
501ZN 502S20 99CG 47.33 97ND1 502S20 97CE1 14.72
10 501ZN 502S20 97CG 123.86 97ND1 502S20 176CB 104.43
501ZN 502S20 97CB 104.74 97ND1 502S20 95CE1 67.44
501ZN 502S20 97CE1 147.20 50 97ND1 502S20 215CD2 165.53
501ZN 502S20 176CB 53.57 97ND1 502S20 95CD2 47.40
501ZN 502S20 95CE1 66.58 97ND1 502S20 157ND1 76.58
15 501ZN 502S20 215CD2 38.78 97ND1 502S20 215CE1 158.19
501ZN 502S20 95CD2 90.17 157CE1 502S20 95NE2 84.44
501ZN 502S20 157ND1 111.41 55 157CE1 502S20 990D2 147.71
501ZN 502S20 215CE1 32.69 157CE1 502S20 990D1 148.87
157NE2 502S20 97ND1 64.27 157CE1 502S20 215NE2 1 14.28 0 157NE2 502S20 157CE1 20.05 157CE1 502S20 176SG 92.26
157NE2 502S20 95NE2 64.45 157CE1 502S20 157CD2 32.37
157NE2 502S20 990D2 127.73 60 157CE1 502S20 99CG 157.21
157NE2 502S20 990D1 135.92 157CE1 502S20 97CG 90.46
157NE2 502S20 215NE2 1 18.67 157CE1 502S20 97CB 107.62 5 157NE2 502S20 176SG 80.35 157CE1 502S20 97CE1 64.20
157NE2 502S20 157CD2 13.66 157CE1 502S20 176CB 67.86
157NE2 502S20 99CG 138.35 65 157CE1 502S20 95CE1 97.13
157NE2 502S20 97CG 79.73 157CE1 502S20 215CD2 99.30
157NE2 502S20 97CB 93.28 157CE1 502S20 95CD2 75.04 0 157NE2 502S20 97CE1 59.22 157CE1 502S20 157ND1 7.72
157NE2 502S20 176CB 57.56 157CE1 502S20 215CE1 125.74
157NE2 502S20 95CE1 77.18 70 95NE2 502S20 990D2 63.29
157NE2 502S20 215CD2 104.99 95NE2 502S20 990D1 82.24
157NE2 502S20 95CD2 55.29 95NE2 502S20 215NE2 1 11.69 5 157NE2 502S20 157ND1 16.38 95NE2 502S20 176SG 57.65
157NE2 502S20215CE1 130.27 95NE2 502S20 157CD2 53.88
97ND 1 502S20 157CE1 73.79 75 95NE2 502S20 99CG 75.91
97ND1 502S20 95NE2 54.54 95NE2 502S20 97CG 53.51 95NE2 502S20 97CB 47.53 215NE2 502S20 97CG 151.08 95NE2 502S20 97CE1 66.56 40 215NE2 502S20 97CB 130.70 95NE2 502S20 176CB 59.11 215NE2 502S20 97CE1 177.59 95NE2 502S20 95CE1 15.74 215NE2 502S20 176CB 68.94 95NE2 502S20 215CD2 112.88 215NE2 502S20 95CE1 97.87 95NE2 502S20 95CD2 10.76 215NE2 502S20 215CD2 15.02 95NE2 502S20 157ND1 80.12 45 215NE2 502S20 95CD2 120.06 95NE2 502S20 215CE1 113.03 215NE2 502S20 157ND1 109.78 990D2 502S20 990D1 33.68 215NE2 502S20 215CE1 11.77 99OD2 502S20 215NE2 81.05 176SG 502S20 157CD2 67.71 990D2 502S20 176SG 72.09 176SG 502S20 99CG 67.55 990D2 502S20 157CD2 1 16.40 50 176SG 502S20 97CG 1 10.41 99OD2 502S20 99CG 17.39 176SG 502S20 97CB 98.10 99OD2 502S20 97CG 70.09 176SG 502S20 97CE1 121.19 99OD2 502S20 97CB 49.83 176SG 502S20 176CB 24.46 990D2 502S20 97CE1 99.35 176SG 502S20 95CE1 47.93 990D2 502S20 176CB 94.41 55 176SG 502S20 215CD2 55.24 99OD2 502S20 95CE1 51.32 176SG 502S20 95CD2 64.19 990D2 502S20 215CD2 94.58 176SG 502S20 157ND1 84.54 99OD2 502S20 95CD2 72.72 176SG 502S20 215CE1 62.51 990D2 502S20 157ND1 143.05 157CD2 502S20 99CG 125.20 99OD2 502S20 215CE1 72.47 60 157CD2 502S20 97CG 80.32 990D1 502S20 215NE2 47.37 157CD2 502S20 97CB 89.90 990D1 502S20 176SG 56.93 157CD2 502S20 97CE1 65.44 990D1 502S20 157CD2 122.36 157CD2 502S20 176CB 46.25 990D1 502S20 99CG 17.44 157CD2 502S20 95CE1 65.12 990D1 502S20 97CG 103.73 65 157CD2 502S20 215CD2 100.33 990D1 502S20 97CB 83.39 157CD2 502S20 95CD2 46.04 990D1 502S20 97CE1 132.95 157CD2 502S20 157ND1 26.66 990D1 502S20 176CB 81.17 157CD2 502S20 215CE1 123.01 990D1 502S20 95CE1 66.68 99CG 502S20 97CG 87.11 99OD1 502S20 215CD2 61.07 70 99CG 502S20 97CB 67.01 990D1 502S20 95CD2 93.00 99CG 502S20 97CE1 1 16.34 990D 1 502S20 157ND 1 141.23 99CG 502S20 176CB 91.84 990D1 502S20 215CE1 39.43 99CG 502S20 95CE1 61.75 15NE2 502S20 176SG 56.63 99CG 502S20 215CD2 78.32 15NE2 502S20 157CD2 1 12.23 75 99CG 502S20 95CD2 86.22 15NE2 502S20 99CG 64.23 99CG 502S20 157ND1 150.05 99CG 502S20 215CE1 55.19 501 ZN 502C23 215CE1 38.74
97CG 502S20 97CB 20.39 40 501ZN 502C23 185CB 125.88
97CG 502S20 97CE1 29.26 501ZN 502C23 500ZN 45.31
97CG 502S20 176CB 110.58 215NE2 502C23 215CE1 14.97 97CG 502S20 95CE1 62.74 215NE2 502C23 185CB 128.15
97CG 502S20 215CD2 162.64 215NE2 502C23 500ZN 73.31
97CG 502S20 95CD2 49.82 45 215CE1 502C23 185CB 139.51
97CG 502S20 157ND1 92.95 215CE1 502C23 500ZN 84.05
97CG 502S20 215CE1 142.03 185CB 502C23 500ZN 93.94 97CB 502S20 97CE1 49.56 185CB 502025 185ND2 33.88
97CB 502S20 176CB 106.31 185CB 502025 185CG 18.55
97CB 502S20 95CE1 51.09 50 185ND2 502025 185CG 16.00
97CB 502S20 215CD2 143.05 215NE2 502N26 215CD2 17.60
97CB 502S20 95CD2 48.70 215NE2 502N26 215CE1 16.37 97CB 502S20 157ND1 108.48 215NE2 502N26 501ZN 28.45
97CB 502S20 215CE1 122.19 215NE2 502N26 185CB 137.89
97CE1 502S20 176CB 108.65 55 215CD2 502N26 215CE1 28.13
97CE1 502S20 95CE1 80.62 215CD2 502N26 501ZN 40.82
97CE 1 502S20 215CD2 163.47 215CD2 502N26 185CB 128.08 97CE1 502S20 95CD2 57.99 215CE1 502N26 501ZN 39.63
97CE1 502S20 157ND1 68.49 215CE1 502N26 185CB 154.20
97CE 1 502S20 215CE 1 170.02 60 501ZN 502N26 185CB 1 19.77
176CB 502S20 95CE1 56.65 215NE2 502C27 215CD2 22.35
176CB 502S20 215CD2 61.1 1 215NE2 502C27 215CE1 15.70 176CB 502S20 95CD2 60.84 215NE2 502C27 215CG 30.16
176CB 502S20 157ND1 60.15 215NE2 502C27 501ZN 30.48
176CB 502S20 215CE1 78.20 65 215NE2 502C27 185N 152.36
95CE1 502S20 215CD2 101.55 215NE2 502C27 179NZ 86.18
95CE1 502S20 95CD2 26.44 215NE2 502C27 215ND1 24.93 95CE1 502S20 157ND1 91.77 215CD2 502C27 215CE1 30.52
95CE1 502S20 215CE1 97.92 215CD2 502C27 215CG 16.08 15CD2 502S20 95CD2 1 18.95 70 215CD2 502C27 501ZN 46.24 15CD2 502S20 157ND1 95.00 215CD2 502C27 185N 136.31 15CD2 502S20 215CE 1 26.52 215CD2 502C27 179NZ 71.21 95CD2 502S20 157ND1 71.41 215CD2 502C27 215ND1 25.81
95CD2 502S20 215CE1 122.71 215CE1 502C27 215CG 29.51 157ND 1 502S20 215CE 1 121.49 75 215CE1 502C27 501ZN 42.25 01ZN 502C23 215NE2 29.38
Figure imgf000199_0001
215CE1 502C27 185N 166.66 215CE 1 502C27 179NZ 100.16 185N 502C28 157NE2 105.80 215CE 1 502C27 215ND 1 15.89 40 185N 502C28 215NE2 162.87 215CG 502C27 501ZN 59.13 185N 502C28 179CE 96.68 215CG 502C27 185N 139.78 185N 502C28 185CB 34.17 5 215CG 502C27 179NZ 81.25 185N 502C28 501ZN 167.61 215CG 502C27 215ND1 16.73 185N 502C28 157ND1 83.06 501ZN 502C27 185N 131.93 45 185N 502C28 184CA 31.93 501ZN 502C27 179NZ 79.86 185N 502C28 185CA 16.60 501ZN 502C27 215ND1 55.16 185N 502C28 184C 13.43
10 185N 502C27 179NZ 66.64 185N 502C28 1850 38.77 185N 502C27 215ND1 156.02 215CD2 502C28 157NE2 96.21 179NZ 502C27 215ND1 96.38 50 215CD2 502C28 215NE2 18.83 157CE1 502C28 179NZ 64.69 215CD2 502C28 179CE 61.74 157CE1 502C28 185N 88.24 215CD2 502C28 185CB 164.94
15 157CE1 502C28 215CD2 110.30 215CD2 502C28 501ZN 43.30 157CE1 502C28 157NE2 17.98 215CD2 502C28 157ND1 108.39 157CE1 502C28 215NE2 106.93 55 215CD2 502C28 184CA 1 15.80 157CE1 502C28 179CE 81.09 215CD2 502C28 185CA 163.51 157CE1 502C28 185CB 83.46 215CD2 502C28 184C 134.39 0 157CE1 502C28 501ZN 79.95 215CD2 502C28 1850 157.65 157CE1 502C28 157ND1 13.92 157NE2 502C28 215NE2 90.01 157CE1 502C28 184CA 100.55 60 157NE2 502C28 179CE 83.15 157CE1 502C28 185CA 80.60 157NE2 502C28 185CB 95.96 157CE1 502C28 184C 92.19 157NE2 502C28 501ZN 62.19 5 157CE1 502C28 1850 51.31 157NE2 502C28 157ND1 28.22 179NZ 502C28 185N 87.07 157NE2 502C28 184CA 117.64 179NZ 502C28 215CD2 77.70 65 157NE2 502C28 185CA 96.64 179NZ 502C28 157NE2 70.38 157NE2 502C28 184C 1 10.16 179NZ 502C28 215NE2 92.24 157NE2 502C28 1850 67.88 0 179NZ 502C28 179CE 18.71 215NE2 502C28 179CE 78.37 179NZ 502C28 185CB 114.89 215NE2 502C28 185CB 152.68 179NZ 502C28 501 ZN 91.20 70 215NE2 502C28 501ZN 29.41 179NZ 502C28 157ND 1 51.71 215NE2 502C28 157ND1 109.81 179NZ 502C28 184CA 66.86 215NE2 502C28 184CA 133.70 5 179NZ 502C28 185CA 96.99 215NE2 502C28 185C A 170.02 179NZ 502C28 184C 77.21 215NE2 502C28 184C 151.86 179NZ 502C28 1850 82.02 75 215NE2 502C28 1850 157.84 185N 502C28 215CD2 147.26
Figure imgf000200_0001
179CE 502C28 185CB 128.76 179CE 502C28 501ZN 85.24 185N 502029 185ND2 75.12 179CE 502C28 157ND1 69.05 40 185N 502029 1830 52.06 179CE 502C28 184CA 69.86 185CB 502029 157CE1 107.77 179CE 502C28 185CA 109.74 185CB 502029 185CA 26.1 1 5 179CE 502C28 184C 84.61 185CB 502029 1850 50.27 179CE 502C28 1850 99.57 185CB 502029 184C 61.12 185CB 502C28 501ZN 138.96 45 185CB 502029 185C 37.80 185CB 502C28 157ND1 86.45 185CB 502029 179NZ 135.46 185CB 502C28 184CA 65.53 185CB 502029 184CA 81.27
10 185CB 502C28 185CA 19.14 185CB 502029 157NE2 1 16.44 185CB 502C28 184C 47.51 185CB 502029 157ND1 107.17 185CB 502C28 1850 37.35 50 185CB 502029 185CG 13.32 501ZN 502C28 157ND1 86.23 185CB 502029 185ND2 29.65 501ZN 502C28 184CA 154.56 185CB 502029 1830 95.73
15 501ZN 502C28 185CA 153.17 157CE1 502029 185CA 102.71 501ZN 502C28 184C 168.02 157CE1 502029 1850 63.95 501ZN 502C28 1850 128.84 55 157CE1 502029 184C 109.63 157ND1 502C28 184CA 89.53 157CE1 502029 185C 81.27 157ND1 502C28 185CA 79.10 157CE1 502029 179NZ 60.71
20 157ND1 502C28 184C 84.20 157CE 1 502029 184CA 11 1.60 157ND1 502C28 1850 50.42 157CE1 502029 157NE2 15.77 184CA 502C28 185CA 48.49 60 157CE1 502029 157ND1 14.48 184CA 502C28 184C 18.63 157CE1 502029 185CG 97.39 184CA 502C28 1850 63.18 157CE1 502029 185ND2 88.1 1 5 185CA 502C28 184C 29.90 157CE1 502029 1830 77.61 185CA 502C28 1850 29.34 185CA 502029 1850 38.78 184C 502C28 1850 47.26 65 185CA 502029 184C 37.37 185N 502029 185CB 47.96 185CA 502029 185C 21.45 185N 502029 157CE 1 110.20 185CA 502029 179NZ 110.13 0 185N 502029 185CA 24.41 185CA 502029 184CA 58.50 185N 502029 1850 52.46 185CA 502029 157NE2 1 16.54 185N 502029 184C 13.23 70 185CA 502029 157ND1 95.96 185N 502029 185C 37.07 185CA 502029 185CG 34.98 185N 502029 179NZ 93.05 185CA 502029 185ND2 50.89 5 185N 502029 184CA 34.15 185CA 502029 1830 69.68 185N 502029 157NE2 125.94 1850 502029 184C 59.68 185N 502029 157ND1 98.76 75 1850 502029 185C 17.42 185N 502029 185CG 58.80
Figure imgf000201_0001
1850 502029 179NZ 91.10 1850 502029 184CA 76.76 157ND1 502029 1830 63.15 1850 502029 157NE2 77.95 40 185CG 502029 185ND2 16.75 1850 502029 157ND1 58.57 185CG 502029 1830 101.96 1850 502029 185CG 46.92 185ND2 502029 1830 1 13.59 1850 502029 185ND2 51.92 179NZ 502030 157CE1 83.44 1850 502029 1830 63.89 179NZ 502030 179CE 24.92 184C 502029 185C 46.65 45 179NZ 502030 157NE2 91.78 184C 502029 179NZ 81.61 - 179NZ 502030 215CD2 100.45 184C 502029 184C A 21.17 179NZ 502030 157ND1 64.96 184C 502029 157NE2 125.08 179NZ 502030 215NE2 118.20 184C 502029 157ND1 96.42 179NZ 502030 501 ZN 120.81 184C 502029 185CG 72.00 50 179NZ 502030 176CB 74.26 184C 502029 185ND2 88.23 179NZ 502030 157CD2 78.41 184C 502029 1830 41.75 179NZ 502030 185N 87.48 185C 502029 179NZ 98.92 179NZ 502030 157CG 64.26 185C 502029 184CA 66.34 179NZ 502030 500ZN 114.65 185C 502029 157NE2 95.37 55 179NZ 502030 179CD 23.13 185C 502029 157ND1 74.90 179NZ 502030 1760 37.94 185C 502029 185CG 39.20 179NZ 502030 1830 39.58 185C 502029 185ND2 50.04 179NZ 502030 176SG 93.09 185C 502029 1830 63.70 179NZ 502030 215CG 99.46 179NZ 502029 184CA 67.01 60 179NZ 502030 184CA 67.31 179NZ 502029 157NE2 64.92 157CE 1 502030 179CE 105.98 179NZ 502029 157ND1 50.67 157CE1 502030 157NE2 21.62 179NZ 502029 185CG 137.54 157CE1 502030 215CD2 138.61 179NZ 502029 185ND2 140.85 157CE1 502030 157ND1 18.49 179NZ 502029 1830 41.26 65 157CE1 502030 215NE2 125.95 184CA 502029 157NE2 124.43 157CE1 502030 501ZN 93.43 184CA 502029 157ND1 97.14 157CE 1 502030 176CB 71.89 184CA 502029 185CG 92.82 157CE1 502030 157CD2 27.52 184CA 502029 185ND2 109.26 157CE1 502030 185N 82.94 184CA 502029 1830 34.30 70 157CE1 502030 157CG 25.26 157NE2 502029 157ND1 28.75 157CE1 502030 500ZN 45.76 157NE2 502029 185CG 104.33 157CE1 502030 179CD 106.55 157NE2 502029 185ND2 91.77 157CE1 502030 1760 68.79 157NE2 502029 1830 90.15 157CE1 502030 1830 80.74 157ND1 502029 185CG 99.28 75 157CE1 502030 176SG 83.85 157ND1 502029 185ND2 93.65 157CE 1 502030 215CG 147.48 157CE 1 502030 184CA 101.29 215CD2 502030 157CG 122.41 179CE 502030 157NE2 108.98 40 215CD2 502030 500ZN 98.03 179CE 502030 215CD2 76.54 215CD2 502030 179CD 83.71 179CE 502030 157ND1 87.85 215CD2 502030 1760 89.06 5 179CE 502030 215NE2 95.67 215CD2 502030 1830 127.43 179CE 502030 501ZN 108.07 215CD2 502030 176SG 54.90 179CE 502030 176CB 72.33 45 215CD2 502030 215CG 8.89 179CE 502030 157CD2 93.94 215CD2 502030 184CA 1 18.37 179CE 502030 185N 100.54 157ND1 502030 215NE2 133.57
10 179CE 502030 157CG 83.49 157ND1 502030 501ZN 102.81 179CE 502030 500ZN 124.93 157ND1 502030 176CB 68.53 179CE 502030 179CD 1 1.36 50 157ND1 502030 157CD2 29.43 179CE 502030 1760 44.80 157ND1 502030 185N 82.51 179CE 502030 1830 56.1 1 157ND1 502030 157CG 15.81
15 179CE 502030 176SG 85.11 157ND1 502030 500ZN 59.94 179CE 502030 215CG 74.75 157ND1 502030 179CD 88.06 179CE 502030 184CA 73.60 55 157ND1 502030 1760 54.60 157NE2 502030 215CD2 1 17.43 157ND1 502030 1830 66.70 157NE2 502030 157ND1 33.24 157ND1 502030 176SG 85.63
20 157NE2 502030 215NE2 104.51 157ND1 502030 215CG 145.46 157NE2 502030 501ZN 72.06 157ND 1 502030 184CA 92.96 157NE2 502030 176CB 55.21 60 215NE2 502030 501ZN 32.52 157NE2 502030 157CD2 15.28 215NE2 502030 176CB 68.65 157NE2 502030 185N 103.23 215NE2 502030 157CD2 104.25
25 157NE2 502030 157CG 27.65 215NE2 502030 185N 141.07 157NE2 502030 500ZN 26.76 215NE2 502030 157CG 1 18.71 157NE2 502030 179CD 1 13.79 65 215NE2 502030 500ZN 81.19 157NE2 502030 1760 65.14 215NE2 502030 179CD 103.69 157NE2 502030 1830 99.86 215NE2 502030 1760 97.73
30 157NE2 502030 176SG 63.41 215NE2 502030 1830 147.79 157NE2 502030 215CG 126.32 215NE2 502030 176SG 48.87 157NE2 502030 184CA 122.88 70 215NE2 502030 215CG 26.40 215CD2 502030 157ND 1 138.15 215NE2 502030 184CA 132.47 215CD2 502030 215NE2 20.44 501ZN 502030 176CB 49.37
35 215CD2 502030 501ZN 49.03 501ZN 502030 157CD2 73.54 215CD2 502030 176CB 69.75 501ZN 502030 185N 151.01 215CD2 502030 157CD2 1 12.33 75 501ZN 502030 157CG 89.68 215CD2 502030 185N 138.07 501ZN 502030 500ZN 49.21 501ZN 502030 179CD 1 19.08 157CG 502030 215CG 130.03
501ZN 502030 1760 86.07 40 157CG 502030 184CA 106.12
501ZN 502030 1830 159.79 500ZN 502030 179CD 133.42
501ZN 502030 176SG 28.42 500ZN 502030 1760 80.87
5 501ZN 502030 215CG 57.09 500ZN 502030 1830 126.24
501ZN 502030 184CA 164.16 500ZN 502030 176SG 51.91
176CB 502030 157CD2 44.39 45 500ZN 502030 215CG 106.29
176CB 502030 185N 150.18 500ZN 502030 184CA 143.02
176CB 502030 157CG 52.73 179CD 502030 1760 52.56 0 176CB 502030 500ZN 55.23 179CD 502030 1830 46.26
176CB 502030 179CD 82.97 179CD 502030 176SG 96.45
176CB 502030 1760 37.08 50 179CD 502030 215CG 80.51
176CB 502030 1830 110.65 179CD 502030 184C A 62.25
176CB 502030 176SG 21.49 1760 502030 1830 ' 73.77 5 176CB 502030 215CG 77.73 1760 502030 176SG 57.66
176CB 502030 184CA 141.53 1760 502030 215CG 93.61
157CD2 502030 185N 109.60 55 1760 502030 184CA 104.60
157CD2 502030 157CG 17.1 1 1830 502030 176SG 131.38
157CD2 502030 500ZN 36.88 1830 502030 215CG 121.67 0 157CD2 502030 179CD 99.48 1830 502030 184CA 32.53
157CD2 502030 1760 49.86 176SG 502030 215CG 63.69
157CD2 502030 1830 93.83 60 176SG 502030 184CA 158.70
157CD2 502030 176SG 57.60 215CG 502030 184CA 109.75
157CD2 502030 215CG 120.94 215CD2 502C31 215NE2 : 18.94 5 157CD2 502030 184CA 122.28 215CD2 502C31 215CG 18.45
185N 502030 157CG 98.24 215CD2 502C31 184CA 126.35
185N 502030 500ZN 1 15.99 65 215CD2 502C31 185N 131.79
185N 502030 179CD 89.32 215CD2 502C31 215CB 33.89
185N 502030 1760 1 18.62 215CD2 502C31 179NZ 68.74 0 185N 502030 I830 47.90 215CD2 502C31 179CE 59.63
185N 502030 176SG 166.63 215CD2 502C31 215CE1 26.33
185N 502030 215CG 129.39 70 215CD2 502C31 215ND1 i 25.96
185N 502030 184CA 29.35 215NE2 502C31 215CG 30.23
157CG 502030 500ZN 53.05 215NE2 502C31 184CA 137.93 5 157CG 502030 179CD 86.74 215NE2 502C31 185N 130.52
157CG 502030 1760 43.56 215NE2 502C31 215CB 48.66
157CG 502030 1830 76.76 75 215NE2 502C31 179NZ 78.54
157CG 502030 176SG 70.16
Figure imgf000204_0001
215NE2 502C31 179CE 73.79 215NE2 502C31 215CE1 14.98 215CD2 502C33 184CA 140.94 215NE2 502C31 215ND1 26.29 40 215CG 502C33 215CB 24.57 215CG 502C31 184CA 132.72 215CG 502C33 179CE 87.99 215CG 502C31 185N 148.07 215CG 502C33 215NE2 33.29 5 215CG 502C31 215CB 18.59 215CG 502C33 179NZ 98.97 215CG 502C31 179NZ 81.71 215CG 502C33 215ND1 15.28 215CG 502C31 179CE 68.86 45 215CG 502C33 215CE1 26.92 215CG 502C31 215CE1 27.29 215CG 502C33 179CD 97.73 215CG 502C31 215ND1 15.78 215CG 502C33 184CA 160.39
10 184CA 502C31 185N 30.84 215CB 502C33 179CE 86.55 184CA 502C31 215CB 120.75 215CB 502C33 215NE2 57.73 184CA 502C31 179NZ 59.46 50 215CB 502C33 179NZ 103.45 184CA 502C31 179CE 66.73 215CB 502C33 215ND1 35.36 184CA 502C31 215CE1 151.84 215CB 502C33 215CE1 50.56
15 184CA 502C31 215ND1 148.46 215CB 502C33 179CD 89.35 185N 502C31 215CB 146.20 215CB 502C33 184CA 149.94 185N 502C31 179NZ 66.83 55 179CE 502C33 215NE2 86.42 185N 502C31 179CE 81.35 179CE 502C33 179NZ 19.93 185N 502C31 215CE1 143.79 179CE 502C33 215ND1 101.15
20 185N 502C31 215ND1 156.25 179CE 502C33 215CE1 99.26 215CB 502C31 179NZ 81.93 179CE 502C33 179CD 17.86 215CB 502C31 179CE 65.82 60 179CE 502C33 184CA 72.57 215CB 502C31 215CE1 45.06 215NE2 502C33 179NZ 86.75 215CB 502C31 215ND1 30.78 215NE2 502C33 215ND1 29.33
25 179NZ 502C31 179CE 17.64 215NE2 502C33 215CE1 15.52 179NZ 502C31 215CE1 92.52 215NE2 502C33 179CD 102.78 179NZ 502C31 215ND1 94.37 65 215NE2 502C33 184CA 138.79 179CE 502C31 215CE1 85.63 179NZ 502C33 215ND1 109.13 179CE 502C31 215ND1 83.33 179NZ 502C33 215CE1 101.80
30 215CE1 502C31 215ND1 15.77 179NZ 502C33 179CD 31.38 215CD2 502C33 215CG 23.20 179NZ 502C33 184CA 61.70 215CD2 502C33 215CB 44.89 70 215ND1 502C33 215CE1 16.58 215CD2 502C33 179CE 75.05 215ND 1 502C33 179CD 112.44 215CD2 502C33 215NE2 17.70 215ND 1 502C33 184C A 168.09
35 215CD2 502C33 179NZ 80.68 215CE1 502C33 179CD 1 14.15 215CD2 502C33 215ND1 28.56 215CE 1 502C33 184CA 152.35 215CD2 502C33 215CE1 24.71 75 179CD 502C33 184CA 64.29 215CD2 502C33 179CD 89.45
Figure imgf000205_0001
215CB 502C34 215CG 22.22 215CB 502C34 215CD2 38.97 46CE3 502C35 46CG 33.12 215CB 502C34 179CE 77.48 40 46CE3 502C35 46CB 41.95 215CB 502C34 215O 35.34 46CE3 502C35 49CG1 95.83 215CB 502C34 184CA 143.76 46CE3 502C35 49CB 1 12.23 5 215CB 502C34 215ND1 30.02 46CE3 502C35 46CZ3 15.54 215CB 502C34 179CD 85.36 46CE3 502C35 215CG 174.53 215CB 502C34 215CA 7.64 45 46CD2 502C35 215CB 168.79 215CG 502C34 215CD2 19.36 46CD2 502C35 184CA 73.64 215CG 502C34 179CE 73.87 46CD2 502C35 46CG 17.80
10 215CG 502C34 215O 57.04 46CD2 502C35 46CB 32.67 215CG 502C34 184CA 132.30 46CD2 502C35 49CG1 86.07 215CG 502C34 215ND1 13.39 50 46CD2 502C35 49CB 103.67 215CG 502C34 179CD 87.32 46CD2 502C35 46CZ3 28.76 215CG 502C34 215CA 29.86 46CD2 502C35 215CG 156.51
15 215CD2 502C34 179CE 60.48 215CB 502C35 184CA 116.10 215CD2 502C34 2150 74.23 215CB 502C35 46CG 150.99 215CD2 502C34 184CA 113.13 55 215CB 502C35 46CB 136.92 215CD2 502C34 215ND1 26.38 215CB 502C35 49CG1 82.96 215CD2 502C34 179CD 76.65 215CB 502C35 49CB 65.46
20 215CD2 502C34 215CA 46.21 215CB 502C35 46CZ3 161.76 179CE 502C34 215O 94.64 215CB 502C35 215CG 17.44 179CE 502C34 184CA 66.56 60 184CA 502C35 46CG 89.19 179CE 502C34 215ND1 85.57 184CA 502C35 46CB 106.23 179CE 502C34 179CD 17.95 184CA 502C35 49CG1 153.74
25 179CE 502C34 215CA 79.13 184CA 502C35 49CB 165.38 2150 502C34 184CA 148.30 184CA 502C35 46CZ3 54.96 2150 502C34 215ND1 60.96 65 184CA 502C35 215CG 1 1 1.30 2150 502C34 179CD 92.43 46CG 502C35 46CB 18.22 2150 502C34 215CA 28.03 46CG 502C35 49CG1 68.77
30 184CA 502C34 215ND1 136.78 46CG 502C35 49CB 86.47 184CA 502C34 179CD 61.63 46CG 502C35 46CZ3 46.17 184CA 502C34 215CA 145.56 70 46CG 502C35 215CG 141.78 215ND 1 502C34 179CD 100.07 46CB 502C35 49CG1 54.35 215ND1 502C34 215CA 37.09 46CB 502C35 49CB 71.57
35 179CD 502C34 215CA 84.78 46CB 502C35 46CZ3 57.22 46CE3 502C35 46CD2 18.03 46CB 502C35 215CG 134.31 46CE3 502C35 215CB 167.15 75 49CG1 502C35 49CB 17.71 46CE3 502C35 184CA 69.58
Figure imgf000206_0001
49CG1 502C35 46CZ3 1 1 1.33 CG1 502C35 215CG 81.23 46CD1 502S36 43CG2 45.78 CB 502C35 46CZ3 127.74 40 46CD1 502S36 185N 91.06 CB 502C35 215CG 65.47 46CD1 502S36 46CZ2 45.61 CZ3 502C35 215CG 166.26 46CD1 502S36 49CG1 79.12 CD2 502S36 46CG 20.54 46CE3 502S36 46NE1 47.47 CD2 502S36 46CE2 19.36 46CE3 502S36 46CB 43.52 CD2 502S36 46CD1 31.16 45 46CE3 502S36 184CA 70.95 CD2 502S36 46CE3 18.28 46CE3 502S36 43CG2 84.89 CD2 502S36 46NE1 30.38 46CE3 502S36 185N 83.63 CD2 502S36 46CB 35.35 46CE3 502S36 46CZ2 35.02 CD2 502S36 184CA 80.19 46CE3 502S36 49CG1 94.53 CD2 502S36 43CG2 70.90 50 46NE1 502S36 46CB 49.12 CD2 502S36 185N 83.94 46NE1 502S36 184CA 84.92 CD2 502S36 46CZ2 30.05 46NE1 502S36 43CG2 62.07 CD2 502S36 49CG1 90.70 46NE1 502S36 185N 73.06 CG 502S36 46CE2 31.91 46NE1 502S36 46CZ2 30.69 CG 502S36 46CD1 18.69 55 46NE1 502S36 49CG1 97.17 CG 502S36 46CE3 35.54 46CB 502S36 184CA 114.08 CG 502S36 46NE1 30.44 46CB 502S36 43CG2 43.33 CG 502S36 46CB 19.29 46CB 502S36 185N 1 18.20 CG 502S36 184CA 100.35 46CB 502S36 46CZ2 64.61 CG 502S36 43CG2 50.47 60 46CB 502S36 49CG1 55.42 CG 502S36 185N 99.39 184CA 502S36 43CG2 146.98 CG 502S36 46CZ2 46.76 184CA 502S36 185N 30.14 CG 502S36 49CG1 73.17 184CA 502S36 46CZ2 55.94 CE2 502S36 46CD1 30.27 184CA 502S36 49CG1 158.32 CE2 502S36 46CE3 32.34 65 43CG2 502S36 185N 127.84 CE2 502S36 46NE1 18.02 43CG2 502S36 46CZ2 91.39 CE2 502S36 46CB 50.63 43CG2 502S36 49CG1 40.48 CE2 502S36 184CA 71.56 185N 502S36 46CZ2 53.94 CE2 502S36 43CG2 75.98 185N 502S36 49CG1 168.29 CE2 502S36 185N 67.60 70 46CZ2 502S36 49CG1 119.83 CE2 502S36 46CZ2 15.68 46CE3 502C37 46CD2 20.85 CE2 502S36 49CG1 104.99 46CE3 502C37 46CZ3 19.99 CD1 502S36 46CE3 49.25 46CE3 502C37 46CG 37.29 CD1 502S36 46NE1 18.05 46CE3 502C37 46CB 48.93 CD1 502S36 46CB 33.97 75 46CE3 502C37 184CA 78.12 CD1 502S36 184CA 101.43 46CE3 502C37 46CE2 28.68 46CE3 502C37 46CH2 27.98 182C 502N43 181C 47.12 46CD2 502C37 46CZ3 35.72 40 182C 502N43 184CA 62.34 46CD2 502C37 46CG 19.30 182N 502N43 182CA 18.78 46CD2 502C37 46CB 36.80 182N 502N43 179CD 83.00 46CD2 502C37 184CA 79.34 182N 502N43 184N 76.52 46CD2 502C37 46CE2 14.68 182N 502N43 181C 16.07 46CD2 502C37 46CH2 35.22 45 182N 502N43 184CA 93.79 46CZ3 502C37 46CG 54.66 182CA 502N43 179CD 83.10 46CZ3 502C37 46CB 68.63 182CA 502N43 184N 60.18 46CZ3 502C37 184CA 61.45 182CA 502N43 181C 30.17 46CZ3 502C37 46CE2 35.24 182CA 502N43 184CA 77.01 46CZ3 502C37 46CH2 14.39 50 179CD 502N43 184N 60.48 46CG 502C37 46CB 20.05 179CD 502N43 181C 97.00 46CG 502C37 184CA 93.85 179CD 502N43 184CA 63.44 46CG 502C37 46CE2 28.73 184N 502N43 181C 90.31 46CG 502C37 46CH2 54.25 184N 502N43 184CA 17.32 46CB 502C37 184CA 1 13.90 55 18 IC 502N43 184CA 107.17 46CB 502C37 46CE2 48.48 1820 502N44 184CA 67.30 46CB 502C37 46CH2 71.69 1820 502N44 184N 49.50 184CA 502C37 46CE2 65.87 1820 502N44 46CZ3 111.29 184CA 502C37 46CH2 50.15 1820 502N44 182C 15.02 46CE2 502C37 46CH2 28.54 60 1820 502N44 46CE3 128.65 46CE3 502N38 46CZ3 17.84 1820 502N44 182CA 29.44 2150 502C41 215CB 33.81 184CA 502N44 184N 19.55 1820 502N42 215O 138.86 184CA 502N44 46CZ3 61.79 1820 502N42 179CD 45.05 184CA 502N44 182C 64.99 2150 502N42 179CD 95.96 65 184CA 502N44 46CE3 72.07 1820 502N43 182C 14.77 184CA 502N44 182CA 79.62 1820 502N43 182N 36.66 184N 502N44 46CZ3 69.82 1820 502N43 182CA 31.63 184N 502N44 182C 45.57 1820 502N43 179CD 51.52 184N 502N44 46CE3 84.00 1820 502N43 184N 47.85 70 184N 502N44 182CA 60.17 1820 502N43 181C 52.73 46CZ3 502N44 182C 98.57 1820 502N43 184CA 64.18 46CZ3 502N44 46CE3 17.73 182C 502N43 182N 31.96 46CZ3 502N44 182CA 97.28 182C 502N43 182CA 19.88 182C 502N44 46CE3 116.28 182C 502N43 179CD 65.08 75 182C 502N44 182CA 18.39 182C 502N43 184N 45.02 46CE3 502N44 182CA 1 14.26
20' 7 - 97ND1 500ZN 95NE2 106.44 95NE2 500ZN 990D2 69.26
97ND1 500ZN 502S20 1 1 1.20 40 95NE2 500ZN 157CG 98.16
97ND1 500ZN 157NE2 109.98 95NE2 500ZN 95CG 17.48
97ND1 500ZN 157CD2 1 16.32 95NE2 500ZN 97NE2 109.38
97ND 1 500ZN 95CD2 92.01 95NE2 500ZN 176SG 62.87
97ND 1 500ZN 97CG 23.13 95NE2 500ZN 176CB 70.67
97ND1 500ZN 97CE1 18.97 45 95NE2 500ZN 95ND1 1.25
97ND1 500ZN 95CE1 1 13.40 95NE2 500ZN 157ND1 116.70
97ND1 500ZN 97CB 50.48 95NE2 500ZN 502030 127.91
97ND1 500ZN 157CE1 102.25 95NE2 500ZN 97CA 65.26
97ND1 500ZN 502C19 88.90 95NE2 500ZN 502C 16 123.13
97ND1 500ZN 97CD2 12.22 50 95NE2 500ZN 990D1 78.19
97ND1 500ZN 990D2 99.20 95NE2 500ZN 99CG 74.24
97ND1 500ZN 157CG 1 12.37 95NE2 500ZN 97N 53.86
97ND1 500ZN 95CG 97.13 95NE2 500ZN 502C23 139.99
97ND1 500ZN 97NE2 7.58 502S20 500ZN 157NE2 88.37
97ND1 500ZN 176SG 164.05 55 502S20 500ZN 157CD2 108.67
97ND1 500ZN 176CB 167.39 502S20 500ZN 95CD2 149.34
97ND1 500ZN 95ND1 107.20 502S20 500ZN 97CG 1 10.98
97ND 1 500ZN 157ND1 106.30 502S20 500ZN 97CE1 111.15
97ND1 500ZN 502030 125.62 502S20 500ZN 95CE1 109.44
97ND1 500ZN 97CA 51.59 60 502S20 500ZN 97CB 103.02
97ND1 500ZN 502C 16 94.54 502S20 500ZN 157CE1 80.60
97ND1 500ZN 990D1 121.27 502S20 500ZN 502C19 28.69
97ND1 500ZN 99CG 108.47 502S20 500ZN 97CD2 113.44
97ND 1 500ZN 97N 55.04 502S20 500ZN 990D2 64.50
97ND1 500ZN 502C23 92.53 65 502S20 500ZN 157CG 104.37
95NE2 500ZN 502S20 123.53 502S20 500ZN 95CG 140.67
95NE2 500ZN 157NE2 116.23 502S20 500ZN 97NE2 113.49
95NE2 500ZN 157CD2 89.53 502S20 500ZN 176SG 70.01
95NE2 500ZN 95CD2 26.39 502S20 500ZN 176CB 79.63
95NE2 500ZN 97CG 89.14 70 502S20 500ZN 95ND1 122.28
95NE2 500ZN 97CE1 1 17.73 502S20 500ZN 157ND1 91.21
95NE2 500ZN 95CE1 14.25 502S20 500ZN 502030 41.55
95NE2 500ZN 97CB 71.32 502S20 500ZN 97CA 1 10.07
95NE2 500ZN 157CE1 129.84 502S20 500ZN 502C16 19.55
95NE2 500ZN 502C19 1 17.68 75 502S20 500ZN 990D1 46.53
95NE2 500ZN 97CD2 96.23 502S20 500ZN 99CG 54.89 502S20 500ZN 97N 126.22 157CD2 500ZN 176SG 76.82
502S20 500ZN 502C23 19.97 40 157CD2 500ZN 176CB 52.21
157NE2 500ZN 157CD2 27.22 157CD2 500ZN 95ND1 90.06
157NE2 500ZN 95CD2 102.66 157CD2 500ZN 157ND1 27.19 157NE2 500ZN 97CG 132.65 157CD2 500ZN 502030 67.60
157NE2 500ZN 97CE1 91.03 157CD2 500ZN 97CA 140.99
157NE2 500ZN 95CE1 121.63 45 157CD2 500ZN 502C16 127.14
157NE2 500ZN 97CB 159.83 157CD2 500ZN 990D1 122.30 157NE2 500ZN 157CE1 13.62 157CD2 500ZN 99CG 135.07 157NE2 500ZN 502C19 113.52 157CD2 500ZN 97N 124.18
157NE2 500ZN 97CD2 121.46 157CD2 500ZN 502C23 113.49
157NE2 500ZN 990D2 146.03 50 95CD2 500ZN 97CG 82.51
157NE2 500ZN 157CG 19.11 95CD2 500ZN 97CE1 97.33
157NE2 500ZN 95CG 107.48 95CD2 500ZN 95CE1 40.64 157NE2 500ZN 97NE2 102.58 95CD2 500ZN 97CB 75.96
157NE2 500ZN 176SG 85.84 95CD2 500ZN 157CE1 1 14.81
157NE2 500ZN 176CB 62.61 55 95CD2 500ZN 502C19 141.07
157NE2 500ZN 95ND1 116.64 95CD2 500ZN 97CD2 85.28 157NE2 500ZN 157ND1 4.00 95CD2 500ZN 990D2 93.05 157NE2 500ZN 502030 47.52 95CD2 500ZN 157CG 83.59
157NE2 500ZN 97CA 157.18 95CD2 500ZN 95CG 8.91
157NE2 500ZN 502C16 104.09 60 95CD2 500ZN 97NE2 92.18
157NE2 500ZN 990D1 119.93 95CD2 500ZN 176SG 82.21
157NE2 500ZN 99CG 134.31 95CD2 500ZN 176CB 80.36 157NE2 500ZN 97N 144.68 95CD2 500ZN 95ND1 27.63
157NE2 500ZN 502C23 88.17 95CD2 500ZN 157ND1 101.51
157CD2 500ZN 95CD2 76.02 65 95CD2 500ZN 502030 136.05
157CD2 500ZN 97CG 132.92 95CD2 500ZN 97CA 68.44
157CD2 500ZN 97CE1 99.84 95CD2 500ZN 502C 16 148.32 157CD2 500ZN 95CE1 96.88 95CD2 500ZN 990D1 104.57
157CD2 500ZN 97CB 148.27 95CD2 500ZN 99CG 99.69
157CD2 500ZN 157CE1 40.56 70 95CD2 500ZN 97N 52.19
157CD2 500ZN 502C19 136.84 95CD2 500ZN 502C23 166.03
157CD2 500ZN 97CD2 124.06 97CG 500ZN 97CE1 42.01 157CD2 500ZN 990D2 142.85 97CG 500ZN 95CE1 93.01 157CD2 500ZN 157CG 8.70 97CG 500ZN 97CB 27.46
157CD2 500ZN 95CG 80.33 75 97CG 500ZN 157CE1 125.37
157CD2 500ZN 97NE2 109.02
Figure imgf000210_0001
97CG 500ZN 502C19 83.35 97CG 500ZN 97CD2 1 1.21 95CE1 500ZN 502C19 104.52
97CG 500ZN 990D2 78.71 40 95CE1 500ZN 97CD2 101.92
97CG 500ZN 157CG 131.51 95CE1 500ZN 990D2 56.82
97CG 500ZN 95CG 84.77 95CE1 500ZN 157CG 105.54
97CG 500ZN 97NE2 30.24 95CE1 500ZN 95CG 31.73
97CG 500ZN 176SG 140.93 95CE1 500ZN 97NE2 117.82
97CG 500ZN 176CB 159.64 45 95CE1 500ZN 176SG 53.52
97CG 500ZN 95ND1 89.61 95CE1 500ZN 176CB 66.77
97CG 500ZN 157ND1 128.84 95CE1 500ZN 95ND1 13.01
97CG 500ZN 502030 140.88 95CE1 500ZN 157ND1 123.11
97CG 500ZN 97CA 28.62 95CE1 500ZN 502030 120.01
97CG 500ZN 502C16 91.61 50 95CE1 500ZN 97CA 65.94
97CG 500ZN 990D1 103.37 95CE1 500ZN 502C16 109.28
97CG 500ZN 99CG 89.29 95CE1 500ZN 990D1 63.95
97CG 500ZN 97N 35.32 95CE1 500ZN 99CG 60.61
97CG 500ZN 502C23 96.73 95CE1 500ZN 97N 58.47
97CE1 500ZN 95CE1 127.77 55 95CE1 500ZN 502C23 125.81
97CE1 500ZN 97CB 69.43 97CB 500ZN 157CE1 152.25
97CE1 500ZN 157CE1 83.51 97CB 500ZN 502C19 74.85
97CE1 500ZN 502C19 95.96 97CB 500ZN 97CD2 38.67
97CE1 500ZN 97CD2 30.88 97CB 500ZN 990D2 53.37
97CE1 500ZN 990D2 116.88 60 97CB 500ZN 157CG 151.92
97CE1 500ZN 157CG 94.77 97CB 500ZN 95CG 74.13
97CE1 500ZN 95CG 104.46 97CB 500ZN 97NE2 57.70
97CE1 500ZN 97NE2 1 1.83 97CB 500ZN 176SG 1 13.57
97CE1 500ZN 176SG 176.65 97CB 500ZN 176CB 135.31
97CE1 500ZN 176CB 151.85 65 97CB 500ZN 95ND1 71.34
97CE1 500ZN 95ND1 1 18.74 97CB 500ZN 157ND1 155.88
97CE1 500ZN 157ND1 87.38 97CB 500ZN 502030 144.04
97CE1 500ZN 502030 112.13 97CB 500ZN 97CA 7.63
97CE1 500ZN 97CA 70.17 97CB 500ZN 502C16 84.52
97CE1 500ZN 502C16 98.86 70 97CB 500ZN 990D1 79.30
97CE1 500ZN 990D1 135.86 97CB 500ZN 99CG 64.82
97CE1 500ZN 99CG 124.92 97CB 500ZN 97N 24.60
97CE1 500ZN 97N 71.32 97CB 500ZN 502C23 96.91
97CE1 500ZN 502C23 91.19 157CE1 500ZN 502C19 102.95
95CE1 500ZN 97CB 70.56 75 157CE1 500ZN 97CD2 114.36
95CE1 500ZN 157CE1 134.82 157CE1 500ZN 990D2 143.80 157CE1 500ZN 157CG 32.13 97CD2 500ZN 502030 135.62 157CE1 500ZN 95CG 120.35 40 97CD2 500ZN 97CA 39.40 157CE1 500ZN 97NE2 95.34 97CD2 500ZN 502C16 94.95 157CE1 500ZN 176SG 93.66 97CD2 500ZN 990D1 1 13.30 5 157CE1 500ZN 176CB 72.42 97CD2 500ZN 99CG 99.56 157CE1 500ZN 95ND1 130.26 97CD2 500ZN 97N 43.46 157CE1 500ZN 157ND1 13.53 45 97CD2 500ZN 502C23 96.67 157CE1 500ZN 502030 42.75 990D2 500ZN 157CG 148.32 157CE1 500ZN 97CA 153.61 990D2 500ZN 95CG 85.03
10 157CE1 500ZN 502C16 94.00 990D2 500ZN 97NE2 106.75 157CE1 500ZN 990D1 1 19.16 990D2 500ZN 176SG 66.47 157CE1 500ZN 99CG 132.42 50 990D2 500ZN 176CB 91.27 157CE1 500ZN 97N 148.13 990D2 500ZN 95ND1 68.22 157CE1 500ZN 502C23 77.05 990D2 500ZN 157ND1 149.98
15 502C19 500ZN 97CD2 87.76 990D2 500ZN 502030 101.14 502C19 500ZN 990D2 48.56 990D2 500ZN 97CA 56.79 502C19 500ZN 157CG 131.42 55 990D2 500ZN 502C16 55.31 502C19 500ZN 95CG 133.50 990D2 500ZN "990D1 26.10 502C19 500ZN 97NE2 93.51 990D2 500ZN 99CG 11.78
20 502C19 500ZN 176SG 86.41 990D2 500ZN 97N 67.45 502C19 500ZN 176CB 103.36 990D2 500ZN 502C23 73.18 502C19 500ZN 95ND1 1 16.60 60 157CG 500ZN 95CG 88.41 502C19 500ZN 157ND1 1 15.54 157CG 500ZN 97NE2 104.85 502C19 500ZN 502030 69.23 157CG 500ZN 176SG 81.88
25 502C19 500ZN 97CA 82.17 157CG 500ZN 176CB 57.08 502C19 500ZN 502C 16 9.71 157CG 500ZN 95ND1 98.71 502C19 500ZN 990D1 44.80 65 157CG 500ZN 157ND1 18.65 502C19 500ZN 99CG 44.05 157CG 500ZN 502030 62.83 502C19 500ZN 97N 98.91 157CG 500ZN 97CA 145.42
30 502C19 500ZN 502C23 25.97 157CG 500ZN 502C16 121.75 97CD2 500ZN 990D2 89.37 157CG 500ZN 990D1 125.08 97CD2 500ZN 157CG 121.53 70 157CG 500ZN 99CG 138.89 97CD2 500ZN 95CG 89.09 157CG 500ZN 97N 129.34 97CD2 500ZN 97NE2 19.07 157CG 500ZN 502C23 106.79
35 97CD2 500ZN 176SG 151.97 95CG 500ZN 97NE2 98.22 97CD2 500ZN 176CB 165.64 95CG 500ZN 176SG 75.40 97CD2 500ZN 95ND1 96.86 75 95CG 500ZN 176CB 76.67 97CD2 500ZN 157ND1 1 17.66
Figure imgf000212_0001
95CG 500ZN 95ND1 18.72 95CG 500ZN 157ND1 106.84 95ND1 500ZN 157ND1 1 17.20 95CG 500ZN 502030 134.35 40 95ND1 500ZN 502030 127.18 95CG 500ZN 97CA 66.91 95ND1 500ZN 97CA 65.39 95CG 500ZN 502C 16 139.99 95ND1 500ZN 502C16 121.96 95CG 500ZN 990D1 95.67 95ND1 500ZN 990D1 76.95 95CG 500ZN 99CG 91.13 95ND1 500ZN 99CG 73.08 95CG 500ZN 97N 51.83 45 95ND1 500ZN 97N 54.30 95CG 500ZN 502C23 157.34 95ND1 500ZN 502C23 138.77 97NE2 500ZN 176SG 170.78 157ND1 500ZN 502030 50.79 97NE2 500ZN 176CB 160.91 157ND1 500ZN 97CA 153.23 97NE2 500ZN 95ND1 110.25 157ND1 500ZN 502C16 106.27 97NE2 500ZN 157ND1 98.86 50 157ND1 500ZN 990D1 123.88 97NE2 500ZN 502030 122.05 157ND1 500ZN 99CG 138.23 97NE2 500ZN 97CA 58.34 157ND1 500ZN 97N 141.31 97NE2 500ZN 502C16 98.25 157ND1 500ZN 502C23 89.88 97NE2 500ZN 990D1 128.36 502030 500ZN 97CA 151.40 97NE2 500ZN 99CG 1 15.87 55 502030 500ZN 502C16 59.54 97NE2 500ZN 97N 60.17 502030 500ZN 990D1 76.66 97NE2 500ZN 502C23 94.05 502030 500ZN 99CG 89.67 176SG 500ZN 176CB 24.80 502030 500ZN 97N 167.70 176SG 500ZN 95ND1 61.91 502030 500ZN 502C23 47.96 176SG 500ZN 157ND1 89.46 60 97CA 500ZN 502C16 91.87 176SG 500ZN 502030 66.49 97CA 500ZN 990D1 82.89 176SG 500ZN 97CA 112.58 97CA 500ZN 99CG 68.50 176SG 500ZN 502C16 83.10 97CA 500ZN 97N 17.00 176SG 500ZN 990D1 47.27 97CA 500ZN 502C23 104.53 176SG 500ZN 99CG 58.40 65 502C16 500ZN 990D1 46.50 176SG 500ZN 97N 1 10.71 502C16 500ZN 99CG 48.93 176SG 500ZN 502C23 89.92 502C16 500ZN 97N 108.63 176CB 500ZN 95ND1 70.15 502C16 500ZN 502C23 17.89 176CB 500ZN 157ND1 65.93 990D1 500ZN 99CG 14.48 176CB 500ZN 502030 58.17 70 990D1 500ZN 97N 92.68 176CB 500ZN 97CA 132.21 990D1 500ZN 502C23 61.92 176CB 500ZN 502C16 97.21 99CG 500ZN 97N 79.11 176CB 500ZN 990D1 70.71 99CG 500ZN 502C23 66.34 176CB 500ZN 99CG 82.86 97N 500ZN 502C23 121.50 176CB 500ZN 97N 124.38 75 990D1 501ZN 215NE2 90.23 176CB 500ZN 502C23 97.25 990D1 501ZN 176SG 1 12.35 990D 1 501ZN 502S20 1 12.82 215NE2 501ZN 502C23 75.42
990D1 501ZN 99CG 18.69 40 215NE2 501ZN 51CE 86.87
990D1 501ZN 502C19 79.98 215NE2 501ZN 99CB 96.93
990D1 501ZN 215CE1 69.12 215NE2 501ZN 157NE2 121.60
5 990D1 501ZN 215CD2 108.93 215NE2 501ZN 502C28 69.50
990D1 501ZN 990D2 40.86 215NE2 501ZN 51CD 68.50
990D1 501ZN 176CB 139.73 45 215NE2 501ZN 176CA 96.32
990D1 501ZN 502C16 77.94 215NE2 501ZN 502N26 60.24
990D1 501ZN 502030 150.01 215NE2 501ZN 502C13 79.44
10 990D1 501ZN 95NE2 99.91 176SG 501ZN 502S20 1 14.49
990D1 501ZN 95CE1 87.33 176SG 501ZN 99CG 1 12.94
990D 1 501ZN 215ND1 78.57 50 176SG 501ZN 502C19 143.20
990D1 501ZN 215CG 96.84 176SG 501ZN 215CE1 1 16.28
990D1 501ZN 502C27 117.71 176SG 501ZN 215CD2 93.58
15 990D1 501ZN 502C23 96.89 176SG 501ZN 990D2 107.01
990D1 501ZN 51CE 46.59 176SG 501ZN 176CB 27.80
990D1 501ZN 99CB 9.94 55 176SG 501ZN 502C16 165.26
990D1 501ZN 157NE2 142.33 176SG 501ZN 502030 96.71
990D1 501ZN 502C28 134.97 176SG 501ZN 95NE2 64.00
20 990D1 501ZN 51CD 45.17 176SG 501ZN 95CE1 56.72
990D1 501ZN 176CA 134.94 176SG 501ZN 215ND1 107.08
990D1 501ZN 502N26 102.58 60 176SG 501 ZN 215CG 96.81
990D1 501ZN 502C13 66.09 176SG 501ZN 502C27 126.45
215NE2 501ZN 176SG 110.20 176SG 501ZN 502C23 149.88
25 215NE2 501ZN 502S20 1 14.39 176SG 501ZN 5 ICE 70.15
215NE2 501ZN 99CG 106.70 176SG 501ZN 99CB 1 16.30
215NE2 501ZN 502C19 104.04 65 176SG 501ZN 157NE2 77.35
215NE2 501ZN 215CE1 21.14 176SG 501ZN 502C28 1 12.34
215NE2 501ZN 215CD2 21.02 176SG 501ZN 51CD 82.94
30 215NE2 501ZN 990D2 127.40 176SG 501ZN 176CA 24.92
215NE2 501ZN 176CB 107.52 176SG 501ZN 502N26 144.10
215NE2 501ZN 502C16 79.34 70 176SG 501ZN 502C13 170.35
215NE2 501ZN 502030 72.20 502S20 501ZN 99CG 97.30
215NE2 501ZN 95NE2 169.64 502S20 501ZN 502C 19 35.05
35 215NE2 501ZN 95CE1 164.04 502S20 501ZN 215CE1 122.79
215NE2 501ZN 215ND1 14.16 502S20 501ZN 215CD2 1 13.12
215NE2 501ZN 215CG 13.46 75 502S20501ZN 990D2 80.61
215NE2 501ZN 502C27 53.76
Figure imgf000214_0001
502S20 501ZN 176CB 92.72 502S20 501ZN 502C16 50.78 502C 19 501ZN 215CD2 1 15.79
502S20 501ZN 502030 57.42 40 502C19 501ZN 990D2 58.89
502S20 501ZN 95NE2 63.61 502C19 501ZN 176CB 127.13
502S20 501ZN 95CE1 80.98 502C19 501ZN 502C16 24.78
5 502S20 501ZN 215ND1 126.35 502C 19 501ZN 502030 81.01
502S20 501ZN 215CG 121.54 502C 19 501ZN 95NE2 80.04
502S20 501ZN 502C27 61.32 45 502C19 501ZN 95CE1 91.08
502S20 501ZN 502C23 42.86 502C19 501ZN 215ND1 109.38
502S20 501ZN 5 ICE 152.44 502C 19 501ZN 215CG 116.67
10 502S20 501ZN 99CB 103.24 502C19 501ZN 502C27 65.97
502S20 501ZN 157NE2 38.75 502C 19 501ZN 502C23 33.36
502S20 501ZN 502C28 50.40 50 502C19 501ZN 5 ICE 125.84
502S20 501ZN 51CD 157.66 502C19 501ZN 99CB 71.28
502S20 501ZN 176CA 104.74 502C19 501ZN 157NE2 73.46
15 502S20 501ZN 502N26 55.16 502C19 501ZN 502C28 67.59
502S20 501ZN 502C13 59.79 502C19 501ZN 51CD 122.99
99CG 501ZN 502C19 67.92 55 502C19 501ZN 176CA 139.70
99CG 501ZN 215CE1 86.00 502C19 501ZN 502N26 49.83
99CG 501 ZN 215CD2 126.56 502C19 501ZN 502C13 28.30
20 99CG 501ZN 990D2 22.30 215CE1 501ZN 215CD2 40.68
99CG 501ZN 176CB 136.19 215CE1 501ZN 990D2 107.46
99CG 501ZN 502C16 73.23 60 215CE1 501ZN 176CB 123.02
99CG 501ZN 502030 147.86 215CE1 501ZN 502C16 76.75
99CG 501 ZN 95NE2 83.65 215CE1 501ZN 502030 91.96
25 99CG 501ZN 95CE1 73.97 215CE1 501ZN 95NE2 168.57
99CG 501ZN 215ND1 96.20 215CE1 501ZN 95CE1 151.17
99CG 501ZN 215CG 1 14.75 65 215CE1 501ZN 215ND1 1 1.53
99CG 501ZN 502C27 120.59 215CE1 501ZN 215CG 29.59
99CG 501ZN 502C23 92.38 215CE1 501ZN 502C27 68.17
30 99CG 501ZN 5 ICE 58.22 215CE1 501ZN 502C23 80.03
99CG 501ZN 99CB 9.90 215CE1 501ZN 5 ICE 71.78
99CG 501ZN 157NE2 123.66 70 215CE1 501ZN 99CB 76.14
99CG 501ZN 502C28 132.54 215CE1 501ZN 157NE2 141.32
99CG 501ZN 51CD 61.79 215CE1 501ZN 502C28 86.53
35 99CG 501ZN 176CA 137.85 215CE1 501ZN 51CD 52.54
99CG 501ZN 502N26 102.78 215CE1 501ZN 176CA 1 10.09
99CG 501ZN 502C13 62.29 75 215CE1 501ZN 502N26 68.36
502C19 501ZN 215CE1 100.52 215CE1 501ZN 502C13 72.57 215CD2 501ZN 990D2 148.10 176CB 501ZN 95CE1 65.68
215CD2 501ZN 176CB 86.82 40 176CB 501ZN 215ND1 1 1 1.57
215CD2 501ZN 502C16 92.79 176CB 501ZN 215CG 95.13
215CD2 501ZN 502030 60.08 176CB 501ZN 502C27 101.61
5 215CD2 501ZN 95NE2 148.86 176CB 501ZN 502C23 122.18
215CD2 501ZN 95CE1 150.18 176CB 501ZN 5 ICE 97.40
215CD2 501ZN 215ND1 30.41 45 176CB 501ZN 99CB 142.06
215CD2 501ZN 215CG 12.24 176CB 501ZN 157NE2 53.97
215CD2 501ZN 502C27 53.54 176CB 501ZN 502C28 85.28
10 215CD2 501ZN 502C23 83.16 176CB 501ZN 51CD 107.76
215CD2 501ZN 51CE 93.05 176CB 501ZN 176CA 13.62
215CD2 501ZN 99CB 1 16.66 50 176CB 501ZN 502N26 1 17.65
215CD2 501ZN 157NE2 106.51 176CB 501ZN 502C13 151.17
215CD2 501ZN 502C28 62.98 502C16 501ZN 502030 75.08
15 215CD2 501ZN 51CD 77.72 502C16 501ZN 95NE2 104.73
215CD2 501ZN 176CA 76.35 502C16 501ZN 95CE1 1 15.46
215CD2 501ZN 502N26 66.57 55 502C16 501ZN 215ND1 84.87
215CD2 501ZN 502C13 95.90 502C16 501ZN 215CG 92.20
99OD2 501ZN 176CB 122.41 502C16 501ZN 502C27 49.71
20 99OD2 501ZN 502C16 73.38 502C16 501ZN 502C23 19.31
990D2 501ZN 502030 137.57 502C16 501ZN 51CE 122.75
990D2 501ZN 95NE2 62.90 60 502C16 501ZN 99CB 72.17
99OD2 501ZN 95CE1 56.76 502C16 501ZN 157NE2 88.10
99OD2 501ZN 215ND1 1 18.11 502C16 501ZN 502C28 59.43 5 990D2 501ZN 215CG 136.74 502C16 501ZN 51CD 1 1 1.43
990D2 501ZN 502C27 122.86 502C 16 501ZN 176CA 147.09
990D2 501ZN 502C23 90.13 65 502C16 501ZN 502N26 31.36
990D2 501ZN 51CE 72.31 502C16 501ZN 502C13 11.86
990D2 501ZN 99CB 32.08 502030 501ZN 95NE2 99.39 0 99OD2 501ZN 157NE2 101.70 502030 501ZN 95CE1 1 16.04
99OD2 501ZN 502C28 126.18 502030 501ZN 215ND1 86.18
99OD2 501ZN 51CD 80.88 70 502030 501ZN 215CG 71.55
99OD2 501ZN 176CA 129.85 502030 501ZN 502C27 32.45
990D2 501ZN 502N26 104.70 502030 501ZN 502C23 55.79 5 990D2 501ZN 502C13 65.24 502030 501ZN 5 ICE 150.02
176CB 501ZN 502C16 139.78 502030 501ZN 99CB 146.90
176CB 501ZN 502030 70.01 75 502030501ZN 157NE2 49.51
176CB 501 ZN 95NE2 63.15 502030 501ZN 502C28 15.74
21. 502030 501ZN 51CD 137.73 215ND1 501ZN 502N26 71.24 502030 501ZN 176CA 72.58 40 215ND1 501ZN 502C13 82.17 502030 501ZN 502N26 47.69 215CG 501ZN 502C27 60.35 502030 501ZN 502C13 86.48 215CG 501ZN 502C23 86.31 5 95NE2 501ZN 95CE1 18.52 215CG 501ZN 5 ICE 83.09 95NE2 501ZN 215ND1 169.83 215CG 501ZN 99CB 104.86 95NE2 501ZN 215CG 158.28 45 215CG 501ZN 157NE2 1 18.73 95NE2 501ZN 502C27 121.63 215CG 501ZN 502C28 72.70 95NE2 501ZN 502C23 105.19 215CG 501ZN 51 CD 66.58 10 95NE2 501ZN 5 ICE 98.52 215CG 501ZN 176CA 83.36 95NE2 501ZN 99CB 93.40 215CG 501ZN 502N26 70.27 95NE2 501ZN 157NE2 49.92 50 215CG 501ZN 502C13 92.84 95NE2 501ZN 502C28 104.06 502C27 501ZN 502C23 33.03 95NE2 501ZN 51CD 1 17.56 502C27 501ZN 5 ICE 139.83 15 95NE2 501ZN 176CA 75.02 502C27 501ZN 99CB 116.28 95NE2 501ZN 502N26 118.76 502C27 501ZN 157NE2 74.84 95NE2 501ZN 502C13 106.54 55 502C27 501ZN 502C28 19.86 95CE1 501ZN 215ND1 152.39 502C27 501ZN 51CD 120.67 95CE1 501ZN 215CG 152.25 502C27 501ZN 176CA 101.53 20 95CE1 501ZN 502C27 140.14 502C27 501ZN 502N26 18.41 95CE1 501ZN 502C23 120.54 502C27 501ZN 502C 13 59.20 95CE1 501ZN 5 ICE 80.00 60 502C23 501ZN 51CE 139.78 95CE1 501ZN 99CB 82.91 502C23 501ZN 99CB 91.45 95CE1 501ZN 157NE2 67.30 502C23 501ZN 157NE2 74.98 25 95CE1 501ZN 502C28 122.30 502C23 501ZN 502C28 40.19 95CE1 501ZN 51CD 99.08 502C23 501ZN 51CD 124.98 95CE1 501ZN 176CA 74.60 65 502C23 501ZN 176CA 127.94 95CE1 501ZN 502N26 135.63 502C23 501ZN 502N26 16.61 95CE1 501ZN 502C13 1 13.71 502C23 501ZN 502C13 30.94 30 215ND1 501ZN 215CG 18.63 5 ICE 501ZN 99CB 54.68 215ND1 501ZN 502C27 67.13 5 ICE 501ZN 157NE2 142.94 215ND1 501ZN 502C23 84.98 70 5 ICE 501ZN 502C28 155.79 215ND1 501ZN 5 ICE 73.04 51CE 501ZN 51CD 19.24 215ND1 501ZN 99CB 86.31 51CE 501ZN 176CA 89.19 35 215ND1 501ZN 157NE2 135.32 5 ICE 501ZN 502N26 136.90 215ND1 501ZN 502C28 83.56 5 ICE 501ZN 502C13 1 1 1.05 215ND1 501ZN 51CD 54.43 75 99CB 501ZN 157NE2 132.76 215ND1 501ZN 176CA 98.81 99CB 501ZN 502C28 131.18 99CB 501ZN 51 CD 54.94 502C28 501ZN 176CA 88.32 99CB 501ZN 176CA 140.48 502C28 501ZN 502N26 32.41 99CB 501 ZN 502N26 99.52 502C28 501ZN 502C13 70.76 99CB 501ZN 502C13 60.57 51CD 501ZN 176CA 96.70 5 157NE2 501ZN 502C28 55.48 15 51 CD 501 ZN 502N26 1 18.66 157NE2 501ZN 51CD 160.03 51 CD 501 ZN 502C13 100.84 157NE2 501ZN 176CA 66.25 176CA 501 ZN 502N26 1 19.33 157NE2 501ZN 502N26 80.16 176CA 501ZN 502C13 158.87 157NE2 501ZN 502C13 98.14 502N26 501ZN 502C13 40.87 10 502C28 501ZN 51CD 137.99 20
TABLE IV
A. Atomic Distances, in Angstroms, between atoms within a radius of 5 A from the metal center formed by Znl (500Zn) and Zn2 (501Zn) in the native IMP-1 metallo beta-lactamase active site.
te
Figure imgf000219_0001
97ND1 500ZN 176CB 150.57 157CD2 500ZN 990D1 155.93
97ND1 500ZN 95ND1 89.92 40 157CD2 500ZN 157ND1 27.06
97ND1 500ZN 157CG 104.42 157CD2 500ZN 97NE2 99.65
97ND1 500ZN 990D1 92.19 157CD2 500ZN 97CD2 1 12.40
97ND1 500ZN 157ND1 103.37 157CD2 500ZN 95CG 74.93
97ND1 500ZN 97NE2 9.73 157CD2 500ZN 99CG 140.46
97ND1 500ZN 97CD2 8.87 45 95CE1 500ZN 97CE1 107.10
97ND1 500ZN 95CG 74.51 95CE1 500ZN 97CG 81.46
97ND1 500ZN 99CG 105.65 95CE1 500ZN 157CE1 126.43
95NE2 500ZN 157CD2 86.89 95CE1 500ZN 95CD2 37.89
95NE2 500ZN 95CE1 24.96 95CE1 500ZN 97CB 65.62
95NE2 500ZN 97CE1 82.13 $0 95CE1 500ZN 176SG 62.10
95NE2 500ZN 97CG 60.21 95CE1 500ZN 990D2 60.55
95NE2 500ZN 157CE1 123.72 95CE1 500ZN 176CB 66.75
95NE2 500ZN 95CD2 15.19 95CE1 500ZN 95ND1 9.23
95NE2 500ZN 97CB 51.42 95CE1 500ZN 157CG 95.28
95NE2 500ZN 176SG 86.90 $5 95CE1 500ZN 990D1 75.15
95NE2 500ZN 990D2 79.19 95CE1 500ZN 157ND1 1 13.61
95NE2 500ZN 176CB 87.24 95CE1 500ZN 97NE2 101.55
95NE2 500ZN 95ND1 20.79 95CE1 500ZN 97CD2 89.52
95NE2 500ZN 157CG 94.90 95CE1 500ZN 95CG 25.88
95NE2 500ZN 990D1 83.09 60 95CE1 500ZN 99CG 66.86
95NE2 500ZN 157ND1 1 11.96 97CE1 500ZN 97CG 38.47
95NE2 500ZN 97NE2 76.90 97CE1 500ZN 157CE1 82.76
95NE2 500ZN 97CD2 66.59 97CE1 500ZN 95CD2 70.67
95NE2 500ZN 95CG 12.06 97CE1 500ZN 97CB 63.10
95NE2 500ZN 99CG 80.72 £5 97CE1 500ZN 176SG 167.66
157CD2 500ZN 95CE1 86.61 97CE1 500ZN 990D2 136.16
157CD2 500ZN 97CE1 91.67 97CE1 500ZN 176CB 145.56
157CD2 500ZN 97CG 118.73 97CE1 500ZN 95ND1 101.61
157CD2 500ZN 157CE1 39.91 97CE1 500ZN 157CG 89.46
157CD2 500ZN 95CD2 77.70 70 97CE1 500ZN 990D1 108.46
157CD2 500ZN 97CB 131.81 97CE1 500ZN 157ND1 85.35
157CD2 500ZN 176SG 82.08 97CE1 500ZN 97NE2 9.89
157CD2 500ZN 990D2 126.16 97CE1 500ZN 97CD2 27.73
157CD2 500ZN 176CB 54.96 97CE1 500ZN 95CG 84.24
157CD2 500ZN 95ND1 79.18 75 97CE1 500ZN 99CG 123.13
157CD2 500ZN 157CG 8.68 97CG 500ZN 157CE1 121.15 97CG 500ZN 95CD2 57.10 97CB 500ZN 176SG 1 13.72
97CG 500ZN 97CB 24.63 40 97CB 500ZN 990D2 74.29
97CG 500ZN 176SG 137.53 97CB 500ZN 176CB 130.83
97CG 500ZN 990D2 98.49 97CB 500ZN 95ND1 68.04
97CG 500ZN 176CB 147.44 97CB 500ZN 157CG 136.97
97CG 500ZN 95ND1 80.54 97CB 500ZN 990D1 53.61
97CG 500ZN 157CG 120.47 45 97CB 500ZN 157ND1 144.63
97CG 500ZN 990D1 74.50 97CB 500ZN 97NE2 53.28
97CG 500ZN 157ND1 122.12 97CB 500ZN 97CD2 35.41
97CG 500ZN 97NE2 28.66 97CB 500ZN 95CG 62.91
97CG 500ZN 97CD2 10.82 97CB 500ZN 99CG 63.87
97CG 500ZN 95CG 68.77 $0 176SG 500ZN 990D2 45.77
97CG 500ZN 99CG 86.97 176SG 500ZN 176CB 27.15
157CE1 500ZN 95CD2 1 1 1.04 176SG 500ZN 95ND1 66.85
157CE1 500ZN 97CB 145.65 176SG 500ZN 157CG 85.86
157CE1 500ZN 176SG 98.82 176SG 500ZN 990D1 75.59
157CE1 500ZN 990D2 139.95 $5 176SG 500ZN 157ND1 93.59
157CE1 500ZN 176CB 76.17 176SG 500ZN 97NE2 163.54
157CE1 500ZN 95ND1 1 19.08 176SG 500ZN 97CD2 148.05
157CE1 500ZN 157CG 31.24 176SG 500ZN 95CG 83.86
157CE1 500ZN 990D1 152.70 176SG 500ZN 99CG 59.99
157CE1 500ZN 157ND1 12.86 60 990D2 500ZN 176CB 72.49
157CE1 500ZN 97NE2 92.64 990D2 500ZN 95ND1 69.68
157CE1 500ZN 97CD2 1 10.48 990D2 500ZN 157CG 131.23
157CE1 500ZN 95CG 1 12.55 990D2 500ZN 990D1 30.22
157CE1 500ZN 99CG 148.65 990D2 500ZN 157ND1 138.46
95CD2 500ZN 97CB 55.92 65 990D2 500ZN 97NE2 126.35
95CD2 500ZN 176SG 97.51 990D2 500ZN 97CD2 108.87
95CD2 500ZN 990D2 94.38 990D2 500ZN 95CG 85.46
95CD2 500ZN 176CB 91.77 990D2 500ZN 99CG 14.44
95CD2 500ZN 95ND1 31.07 176CB 500ZN 95ND1 66.96
95CD2 500ZN 157CG 84.86 70 176CB 500ZN 157CG 58.83
95CD2 500ZN 990D1 96.24 176CB 500ZN 990D1 102.58
95CD2 500ZN 157ND1 100.34 176CB 500ZN 157ND1 68.47
95CD2 500ZN 97NE2 67.18 176CB 500ZN 97NE2 151.14
95CD2 500ZN 97CD2 60.72 176CB 500ZN 97CD2 152.44
95CD2 500ZN 95CG 13.67 75 176CB 500ZN 95CG 79.22
95CD2 500ZN 99CG 95.44 176CB 500ZN 99CG 86.87 95ND1 500ZN 157CG 87.85 215NE2 501ZN 215CG 8.21
95ND1 500ZN 990D1 83.82 40 215NE2 501ZN 95CE1 129.29
95ND1 500ZN 157ND1 106.22 215NE2 501ZN 157NE2 121.33
95ND1 500ZN 97NE2 97.25 215NE2 501ZN 95NE2 142.20
95ND1 500ZN 97CD2 87.35 215NE2 501ZN 176CA 71.65
95ND1 500ZN 95CG 17.96 990D2 501ZN 176SG 77.17
95ND1 500ZN 99CG 76.04 45 990D2 501ZN 215CE1 98.32
157CG 500ZN 990D1 161.41 990D2 501ZN 99CG 20.15
157CG 500ZN 157ND1 18.38 990D2 501ZN 215CD2 128.13
157CG 500ZN 97NE2 98.22 990D2 501ZN 990D1 35.06
157CG 500ZN 97CD2 1 12.78 990D2 501ZN 176CB 95.12
157CG 500ZN 95CG 83.04 $0 990D2 501ZN 215ND1 105.40
157CG 500ZN 99CG 145.66 990D2 501ZN 99CB 27.75
990D1 500ZN 157ND1 161.29 990D2 501ZN 179NZ 155.79
990D1 500ZN 97NE2 99.30 990D2 501ZN 215CG 119.83
990D1 500ZN 97CD2 83.47 990D2 501 ZN 95CE1 50.45
990D1 500ZN 95CG 93.64 $5 990D2 501ZN 157NE2 104.01
990D1 500ZN 99CG 15.78 990D2 501ZN 95NE2 58.19
157ND1 500ZN 97NE2 95.10 990D2 501ZN 176CA 98.69
157ND1 500ZN 97CD2 112.24 176SG 501 ZN 215CE1 93.12
157ND1 500ZN 95CG 100.43 176SG 501ZN 99CG 97.29
157ND1 500ZN 99CG 150.90 60 176SG 501ZN 215CD2 80.09
97NE2 500ZN 97CD2 17.87 176SG 501ZN 990D1 109.01
97NE2 500ZN 95CG 80.84 176SG 501ZN 176CB 23.34
97NE2 500ZN 99CG 1 13.59 176SG 501ZN 215ND1 94.52
97CD2 500ZN 95CG 73.54 176SG 501 ZN 99CB 98.12
97CD2 500ZN 99CG 96.79 $5 176SG 501ZN 179NZ 79.85
95CG 500ZN 99CG 89.33 176SG 501ZN 215CG 88.09
215NE2 501ZN 990D2 1 17.08 176SG 501ZN 95CE1 50.30
215NE2 501ZN 176SG 79.89 176SG 501ZN 157NE2 70.15
215NE2 501ZN 215CE1 26.59 176SG 501ZN 95NE2 62.34
215NE2 501ZN 99CG 120.78 to 176SG 501ZN 176CA 21.66
215NE2 501ZN 215CD2 11.88 215CE1 501ZN 99CG 96.45
215NE2 501ZN 990D 1 136.51 215CE1 501ZN 215CD2 37.42
215NE2 501ZN 176CB 84.50 215CE1 501ZN 990D1 1 10.30
215NE2 501ZN 215ND 1 21.78 215CE1 501ZN 176CB 105.32
215NE2 501ZN 99CB 103.82 t5 215CE1 501ZN 215ND1 7.08
215NE2 501ZN 179NZ 65.50 215CE1 501ZN 99CB 79.19 215CE1 501ZN 179NZ 90.39 176CB 501ZN 179NZ 60.73
215CE1 501ZN 215CG 23.90 40 176CB 501 ZN 215CG 91.97
215CE1 501ZN 95CE1 132.51 176CB 501 ZN 95CE1 54.34
215CE1 501ZN 157NE2 147.89 176CB 501ZN 157NE2 50.40 215CE1 501ZN 95NE2 147.96 176CB 501ZN 95NE2 60.36
215CE1 501ZN 176CA 92.34 176CB 501ZN 176CA 13.06
99CG 501ZN 215CD2 132.64 45 215ND1 501ZN 99CB 85.89
99CG 501ZN 990D1 19.32 215ND1 501 ZN 179NZ 83.81
99CG 501ZN 176CB 114.76 215ND1 501 ZN 215CG 17.62
99CG 501ZN 215ND1 103.12 215ND1 501 ZN 95CE1 137.46
99CG 501ZN 99CB 17.25 215ND1 501ZN 157NE2 142.60
99CG 501ZN 179NZ 172.75 $0 215ND1 501ZN 95NE2 153.00
99CG 501ZN 215CG 120.28 215ND1 501ZN 176CA 91.09
99CG 501ZN 95CE1 65.59 99CB 501ZN 179NZ 169.30
99CG 501ZN 157NE2 1 12.34 99CB 501ZN 215CG 103.03
99CG 501ZN 95NE2 68.89 99CB 501ZN 95CE1 78.05
99CG 501 ZN 176CA 118.84 $5 99CB 501 ZN 157NE2 128.93
215CD2 501ZN 990D1 147.72 99CB 501ZN 95NE2 84.08
215CD2 501ZN 176CB 79.95 99CB 501ZN 176CA 1 19.25
215CD2 501ZN 215ND1 31.64 179NZ 501ZN 215CG 66.50
215CD2 501ZN 99CB 115.63 179NZ 501ZN 95CE1 107.87
215CD2 501ZN 179NZ 53.71 60 179NZ 501ZN 157NE2 60.44
215CD2 501ZN 215CG 14.24 179NZ 501ZN 95NE2 103.95
215CD2 501ZN 95CE1 130.37 179NZ 501ZN 176CA 58.21
215CD2 501ZN 157NE2 1 10.96 215CG 501ZN 95CE1 137.38
215CD2 501ZN 95NE2 140.18 215CG 501ZN 157NE2 125.06
215CD2 501ZN 176CA 67.83 $5 215CG 501ZN 95NE2 150.39
990D1 501 ZN 176CB 120.74 215CG 501 ZN 176CA 79.27
990D1 501ZN 215ND1 116.17 95CE1 501ZN 157NE2 55.82
990D1 501ZN 99CB 33.98 95CE1 501ZN 95NE2 15.55
990D1 501ZN 179NZ 156.47 95CE1 501ZN 176CA 64.47
990D1 501ZN 215CG 133.76 to 157NE2 501ZN 95NE2 45.82
990D1 501ZN 95CE1 66.65 157NE2 501ZN 176CA 61.91
990D1 501ZN 157NE2 101.17 95NE2 501ZN 176CA 72.35
990D1 501ZN 95NE2 64.30
990D1 501 ZN 176CA 128.90
176CB 501ZN 215ND1 104.15
176CB 501ZN 99CB 119.51 Discussion of the Figures
Figure 1 shows a figure of the native IMP-1 metallo beta-lactamase from P. aeruginosa of this invention.
Figure 2A and 2B give a schematic representation of the fold and arrangement of the secondary structure elements in the structure of IMP- 1. The two views are related by a 90° rotation about the horizontal. Shown in the active site are the two zinc ions (purple spheres) and a ball-and-stick representation of the bound inhibitor. The numbering scheme corresponds to the full length IMP-1 including the N-terminal 18 residues corresponding to the signal sequence. Secondary structural elements of IMP- 1 : betal , 26-31 ; beta2, 34-43; beta3, 47-58; beta4, 61-65; alphal, 71-82; beta5, 87-92; alpha2, 98-109; betaό, 114-117; alpha3, 118-126; beta7, 134-1 6; beta8, 140-144; beta9, 148-151 ; betalO, 163-166; betal 1, 171-175; alpha4, 193-205; betal2, 210-213; alpha5, 222-236. Zn ligands located in loops beta5/alpha2, beta9/betal0, betal l/alpha4, and betal2/alpha5.
Figure 3A and 3B is a stereo diagram of the inhibitor SB-252619 bound in the active site of IMP-1. The thiol atom of the inhibitor is bound between the two Zn(II) (purple spheres). Two water molecules (light blue spheres) are tightly bound to the carbonyl oxygen of the inhibitor. Dotted lines represent polar interactions between atoms. The numbering scheme used for the figure corresponds to the numbering of the mature enzyme in which the first 18 residues are missing. Figures 4A and 4B is a stereo diagram of the comparison of the native IMP-1 and SB-
252619 inhibitor complex structures showing the conformational changes upon inhibitor binding and represent the superposition of the native, unbound IMP-1 structure (red) and the mercaptocarboxylate complex (blue). Shown are the superposed C» atom trace and the side chains of Trp28, Phe51, Val25 and Val31. On binding of the inhibitor, Phe51 rotates 100° around C*-C» bond to give access to the incoming inhibitor while Val25 and Val31 are displaced by approximately 2.9A compared to the native structure. The lateral movement of the flap widens the hydrophobic pocket. The uncertainty in the position of three residues in the native IMP-1 structure is indicated by the color gray of Trp28 and the adjacent residues. The numbering scheme used for the figure corresponds to the numbering of the mature enzyme in which the first 18 residues are missing. Mutants and Derivatives
The invention further provides homologues, co-complexes, mutants and derivatives of the IMP-1 metallo beta-lactamase crystal structure of the invention.
The term "homologue" means a protein having at least 30% amino acid sequence identity with a functional domain of IMP-1 metallo beta-lactamase. Preferably the percentage identity will be 40, or 50%, more preferably 60or 70% and most preferably 80 or 90%. A 95% identity is most particularly preferred.
The term "co-complex" means the IMP-1 metallo beta-lactamase or a mutant or homologue of the IMP-1 metallo beta-lactamase in covalent or non-covalent association with a chemical entity or compound.
The term "mutant" refers to the IMP-1 metallo beta-lactamase polypeptide, i.e., a polypeptide displaying the biological activity of wild-type IMP-1 metallo beta-lactamase activity, characterized by the replacement of at least one active-site amino acid from the wild- type beta-lactamase sequence. Such a mutant may be prepared, for example, by expression of the IMP-1 beta-lactamase cDNA previously altered in its coding sequence by oligonucleotide- directed mutagenesis.
IMP- 1 metallo beta-lactamase mutants may also be generated by site-specific incoφoration of unnatural amino acids into the IMP- 1 metallo beta-lactamase protein using the general biosynthetic method of C. J. Noren et al, Science. 244: 182- 188 ( 1989). In this method, the codon encoding the amino acid of interest in wild-type IMP-1 metallo beta-lactamase is replaced by a "blank" nonsense codon, TAG, using oligonucleotide-directed mutagenesis. A suppressor directed against this codon is then chemically aminoacylated in vitro with the desired unnatural amino acid. The aminoacylated residue is then added to an in vitro translation system to yield a mutant IMP-1 metallo beta-lactamase enzyme with the site-specific incoφorated unnatural amino acid.
Selenocysteine or selenomethionine may be incorporated into wild-type or mutant metallo IMP-1 beta-lactamase by expression of IMP-1 metallo beta-lactamase-encoding cDNAs in auxotrophic E. coli strains [W. A. Hendrickson et al, EMBO J.. 9(5): 1665- 1672 (1990)]. In this method, the wild-type or mutated metallo beta-lactamase cDNA may be expressed in a host organism on a growth medium depleted of either natural cysteine or methionine (or both) but enriched in selenocysteine or selenomethionine (or both).
The term "heavy atom derivative" refers to derivatives of IMP-1 metallo beta- lactamase produced by chemically modifying a crystal of IMP-1 metallo beta-lactamase. In practice, a crystal is immersed in a solution containing the desired metal salt, or organometallic compound, e.g., lead chloride, gold thiomalate, thimerosal or uranyl acetate, which upon diffusion into the protein crystal can bind to the protein. The location of the bound heavy metal atom site(s) can be determined by X-ray diffraction analysis of the soaked crystal. This information, in turn, is used to generate the phase angle information needed to construct a three-dimensional electron density map from which a model of the atomic structure of the enzyme is derived [T. L. Blundel and N. L. Johnson, Protein Crystallography. Academic Press (1976)].
Methods of Identifying Inhibitors of the Novel IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa Crystalline Structure Another aspect of this invention involves a method for identifying inhibitors of a IMP-
1 metallo beta-lactamase characterized by the crystal structure and novel active site described herein, and the inhibitors themselves. The novel beta-lactamase crystalline structure of the invention permits the identification of inhibitors of beta-lactamase activity. Such inhibitors may be competitive, binding to all or a portion of the active site of the IMP- 1 metallo beta- lactamase; or non-competitive and bind to and inhibit metallo beta-lactamase whether or not it is bound to another chemical entity.
One design approach is to probe the IMP-1 metallo beta-lactamase crystal of the invention with molecules composed of a variety of different chemical entities to determine optimal sites for interaction between candidate IMP-1 metallo beta-lactamase inhibitors and the enzyme. For example, high resolution X-ray diffraction data collected from crystals saturated with solvent allows the determination of where each type of solvent molecule binds. Small molecules that bind tightly to those sites can then be designed and synthesized and tested for their IMP-1 metallo beta-lactamase inhibitor activity.
This invention also enables the development of compounds that can isomerize to short- lived reaction intermediates in the chemical reaction of a substrate or other compound that binds to or with the IMP-1 metallo beta-lactamase. Thus, the time-dependent analysis of structural changes in the IMP-1 metallo beta-lactamase during its interaction with other molecules is permitted. The reaction intermediates of the IMP-1 metallo beta-lactamase can also be deduced from the reaction product in co-complex with the IMP-1 metallo beta- lactamase. Such information is useful to design improved analogues of known IMP-1 metallo beta-lactamase inhibitors or to design novel classes of inhibitors based on the reaction intermediates of the IMP- 1 metallo beta-lactamase enzyme and IMP- 1 metallo beta-lactamase inhibitor co-complex. This provides a novel route for designing IMP-1 metallo beta-lactamase inhibitors with both high specificity and stability. Another approach made possible by this invention is to screen computationally small molecule databases for chemical entities or compounds that can bind in whole, or in part, to the IMP-1 metallo beta-lactamase enzyme. Details on this process and the results it can provide are now documented in the art. For a description of this type of technology please refer to PCT application WO 97/16177 published 09 May 1997; the techniques described there for computer modeling are incoφorated herein by reference. Once identified by the modeling techniques, the beta-lactamase inhibitor may be tested for bioactivity using standard techniques. For example, the structure of the invention may be used in enzymatic activity assays to determine the inhibitory activity of the compounds or binding assays using conventional formats to screen inhibitors. One particularly suitable assay format includes the enzyme-linked immunosorbent assay (ELISA). Other assay formats may be used; these assay formats are not a limitation on the present invention.
In another aspect, the metallo beta-lactamase structure of the invention permit the design and identification of synthetic compounds and/or other molecules which are characterized by the conformation of the metallo beta-lactamase of the invention. Using known computer systems, the coordinates of the metallo beta-lactamase structure of the invention may be provided in machine readable form, the test compounds designed and/or screened and their conformations superimposed on the structure of the metallo beta-lactamase of the invention. Subsequently, suitable candidates identified as above may be screened for the desired metallo beta-lactamase inhibitory bioactivity, stability, and the like. Once identified and screened for biological activity, these inhibitors may be used therapeutically or prophylactically to block metallo beta-lactamase activity, and thus, overcome bacterial resistance to antibiotics of the beta-lactam class, e.g. imipenem, penicillins, cephalosporins, etc.
INHIBITORS OF IMP-1 METALLO BETA-LACTAMASE ACTIVITY The present invention also provides inhibitors of the IMP-1 metallo beta-lactamase activity identified or designed by the methods of the invention. These inhibitors are useful as anti-bacterial agents. One particularly desirable inhibitor is the tetrazoyl mercapto carboxylate compound 2-[5-( l-tetrazolylmethyl)thien-3-yl]-N-[2-(mercaptomethyl)-4- phenylbutyrylglycine)] identified throughout herein as SB-252619. The structure of this compound is as follows:
Figure imgf000227_0001
Its preparation is given in a patent application published 30 April 1998 as WO 98/17639. That disclosure is incoφorated herein by reference to the extent the data and teachings therein are seminal to the preparation of SB-252619. This tetrazoyl mercaptocarboxylate inhibits metallo beta-lactamase catalytic activity as measured by any of the techniques described in the examples below. Estimates of the potency of inhibition are obtained by performing enzyme assays in the presence of a range of inhibitor concentrations, and fitting the effect of inhibitor concentration on enzyme velocity to a four parameter logistic function that allows calculation of an IC50 (the inhibitor concentration at which enzymatic activity is 50% of the uninhibited control). This parameter is related to the dissociation constant for inhibitor binding (Kj) and has a value of approximately 0.09 μM for mercaptocarboxylate SB-252619 when tested against IMP-1.
The following examples illustrate various aspects of this invention. These examples do not limit the scope of this invention, which is defined by the appended claims.
Example 1 - The expression and purification of the IMP- 1 beta-lactamase from Pseudomonas aeruginosa in Escherichia coli.
The mature IMP- 1 metallo beta-lactamase from Pseudomonas aeruginosa lacking the 18 amino-terminal residues that correspond to the signal sequence was over expressed in E. coli, strain BL21(DE3), and purified as previously described [Laraki, N., Franceschini, N., Rossolini, G. M., Santucci, P., Meunier, C, De Pauw, E., Amicosante, G., Frere, J-M., and Galleni, M. (1999) Antimicrob. Agents Chemother. 43, 902-906]. The soluble polypeptide includes 228 amino acid residues with a molecular weight of 25,1 12. This product was greater than 95% pure by SDS PAGE and has the desired enzymatic activity. N-terminal amino acid analysis confirmed its identity.
1 A. Measurement of IMP- 1 metallo beta-lactamase activity. The half-maximal inhibitory concentration, IC50, was calculated as the concentration of inhibitor that caused a 50% reduction in the rate of hydrolysis of nitrocefin [Payne, D. J., Cramp, R., Winstanley, D., and Knowles, D. (1994) Antimicrob. Agents Chemother. 38, 767- 772]. Kilo's were determined following a pre-incubation of enzyme and inhibitor at 37 °C in 25 mM in PIPES buffer, pH 7.0 with a final concentration of 100 μM Zn(Il)S0 . IC50's of B. fragilis CfiA enzyme and IMP- 1 were determined using 91 μM and 400μM nitrocefin, which was the same multiple of the Km of nitrocefin for each enzyme. l.B. Ligand binding to IMP-1.
It is also possible to define ligand interactions with IMP-1 in experiments that are not dependent upon enzyme catalyzed turnover of substrates. This type of experiment can be done in a number of ways: l .B.1. Effects of ligand binding upon enzyme intrinsic fluorescence (e.g. of tryptophan). Binding of either natural ligands or inhibitors may result in enzyme conformational changes, which alter enzyme fluorescence. Using stopped-flow fluorescence equipment, this can be used to define the microscopic rate constants that describe binding. Alternatively, steady-state fluorescence titration methods can yield the overall dissociation constant for binding in the same way that these are accessed through enzyme inhibition experiments.
Example 2 - Crystallization, structure determination and refinement of the crystal structure of the IMP-1 metallo beta-lactamase from P. aeruginosa 2. A. Crystallization
The native IMP-1 crystals grew as plates from sitting drops equilibrated through the vapor phase at room temperature against 500 μL of reservoir solution for 2-3 weeks in Cryschem plates. The drops were prepared by mixing 5 μL of the protein solution (14.3 mg/ml in 20mM HEPES, pH 7.5) with an equal volume of reservoir solution containing 30% PEG 4000, 0.2M sodium acetate and 0.1M citrate, pH 5.6. The pH of the reservoir solution was 6.5. The crystals belong to the space group P2(l) with unit cell dimensions a = 50.3A, b = 105.8A, c = 1 12.3A, β=93.9°, an estimated solvent content of 60% with four copies of the IMP- 1 metallo beta-lactamase in the asymmetric unit (the monomer has a relative molecular mass of 25,112). The crystals of the complex between IMP-1 and SB-252619 were grown from a protein solution containing excess inhibitor. The crystals were grown from sitting drops equilibrated against 30%PEG2000 monomethyl ether, 0.1M sodium acetate, pH 5.0 and 0.2M ammonium sulfate. The crystals belong to the space group P2(l)2(l)2(l) with unit cell dimensions a = 50.0A b = 51.6A c = 205.6A, an estimated solvent content of 50% with two molecules of IMP- 1 metallo beta-lactamase complex in the asymmetric unit. 2.B. X-ray diffraction data collection
The x-ray diffraction data were collected from a single IMP- 1 beta-lactamase native crystal mounted in a sealed borosilicate capillary tube using a Siemens multiwire area detector mounted on a 4-circle goniostat. Monochromated CuKα x-rays were supplied by a Rigaku RU200 generator operating at 50kV, 100mA. The reciprocal space was sampled at 0.25° oscillation steps around the ω or φ goniostat's axes. The data were processed with XDS [Kabsch, W. (1988) J. Appl. Cryst. 21, 916-924]. A second native data set was collected on a MAR image plate using monochromated CuKα radiation supplied by a Rigaku-RU200 rotating anode generator operating at 100 mA x 50 kV. The reciprocal space was sampled at 1.0° oscillation steps per frame about the goniostat's φ axis. The data were processed with the program package DENZO/SCALEPACK [Otwinowski, Z. (1993) in Proceedings of the CCP4 Study Weekend: "Data Collection and Processing", 29-30 January, SERC Daresbury Laboratory, England].
Complete diffraction data for the IMP-1 enzyme complex with SB252619 were collected from two crystals mounted in siliconized borosilicate glass capillary tubes at room temperature using a MAR image plate. The reciprocal space was sampled at 0.75° oscillation step intervals around the goniostat's φ axis. The data from the two crystals was merged and processed with DENZO/SCALEPACK. 2.C. Structure Determination The crystal structure of the P. aeruginosa IMP-1 metallo beta-lactamase was determined by molecular replacement with the program package AMoRe [Navaza, J. (1994) Ada Cryst. A50, 157-163] using the crystal structure of the metallo β-lactamase from Bacteroides fragilis [Concha, N. O. et al. (1995) Structure 4, 823-836] as search model. The B. fragilis and the IMP-1 metallo beta-lactamase enzymes share 34% amino acid sequence identity. After removing solvent molecules and metal ions, the B. fragilis amino acid residues were mutated to the corresponding residues in the IMP- 1 after aligning both sequences and the search molecule was placed in a orthogonal cell of dimensions 90A x 71 A x 70A. The cross rotation and translation searches were carried using data from 39A to 4A resolution and a radius of integration of 25A. The top four solutions of the cross rotation function corresponding to the four molecules in the asymmetric unit were unambiguously discriminated from the noise peaks. The search for the correct translation for each molecule in the asymmetric unit produced a solution for the tetramer with an R-factor of 0.50 and a correlation coefficient of 0.54 after rigid body refinement in AMoRe. The tetramer is formed by a dimer of dimers with 222 local symmetry. The native self Patterson map (20-4A data) shows a non-origin peak 1/2 the height of the origin peak, at u=0.500, v=0.46, w=0.500 which corresponds to the 2-fold rotation axis relating the two dimers in the tetramer. This axis lies close, but not exactly parallel to the crystallographic b-axis.
The structure determination of the IMP-1 complex with SB252619 was accomplished by molecular replacement using a partially refined model of the native IMP- 1 structure as search model. The cross rotation function top solution corresponded to one of the molecules in the asymmetric unit while the second molecule solution was the 87th solution. However, the top two translation function solutions corresponded to the two molecules in the dimer with an R-factor of 0.40 and a correlation coefficient of 0.59 after rigid body refinement. 2.D. Model Building and Refinement
The native tetramer was built from the molecular replacement solutions and used to calculate a 2Fo-Fc electron density map from which the polypeptide chain for the protomer was traced using the interactive computer graphics program O [Jones, T.A. et al. (1991) Ada Crystallogr. A47, 110-1 19]. Rounds of simulated annealing and positional refinement using X- PLOR [A. Brunger et al, Science, 235, 458-460 (1987)] were followed by manual intervention. The refinement and manual rebuilding was monitored by the quality of the 2Fo-Fc and Fo-Fc electron density maps and the value of the crystallographic R and Rfree- Strict non- crystallographic restraints were used throughout the refinement and reflection data from infinity to 3.1 A was used in the refinement including a simple model for bulk solvent contribution to the scattering. The final model of the protomer includes residues 20 to 239 [SEQ ID NO: l], and 2 Zn+2. The R factor of the model is 0.25 and the Rfree is 0.29 for 19287 reflection for which F>2σF. The r.m.s. deviations from the standard geometry [Engh, R.A. and Huber, R. (1991) Ada Cryst. A47, 392-400] are 0.01 A for bond lengths, and 1.7° for bond angles. Residues 46- 47 are disordered and were not included in the model. The IMP-1 complex with SB252619 model was build using a 2Fo-Fc map generated with the coordinates of the translated and rotated solutions. One difference with respect to the native structure was the position and the electron density for Tφ46 in the flap. In the complex, the flap is ordered and in the closed conformation. The model was refined against all the data to 2.7A using a simple bulk solvent correction model. Rounds of simulated annealing, positional refinement and individual temperature factor refinement were followed by manual intervention. The two molecules were refined using non-crystallographic symmetry restrains using a 300 kcal/mol energy restrain for all residues except 45-48 which have a different conformation in both molecules. The conformation of the haiφin loop in which Tφ46 is located differs in both molecules due to crystal packing effects. While in molecule A the inhibitor binding site is closely associated to a neighboring molecule, in molecule B the crystal contacts are fewer. The inhibitor and solvent molecules were included in the model near the end of the refinement. Further refinement of the model of the complex was performed against a new set of diffraction data to 2A resolution collected at the beamline X25, National Synchrotron Light Source, Brookhaven National Laboratory. This final model includes residues 4 to 219 (numbering scheme that does not include the first 18 residues of the signal sequence) in molecule A, residues 4 to 220 in molecule B, two zinc ions per protein molecule, one inhibitor molecule bound to each protein molecule and a total of 340 water molecules.
Example 3 - Characterization of Inhibition by SB-252619 The characterization of the compound as an inhibitor of the catalytic activity of IMP- 1 was performed using a procedure similar to that described in Example 2E above, except that multiple assays were performed in the presence of inhibitor concentrations ranging (in two-fold dilution steps) from 100 mM down to 0.1 mM (final concentrations). These were added from stocks prepared at 10-fold higher concentrations and added to each reaction mixture. The stock of inhibitor was prepared freshly in dimethylsulfoxide. The enzyme concentration used for these assays was selected so that around 50% of the nitrocefin available was hydrolyzed during the reaction time course. The hydrolysis activity (relative to controls in the absence of inhibitor) were plotted as a function of inhibitor concentration and fitted to a four-parameter logistic function (using the Grafit package; Erithacus Software Ltd.) to yield IC50, the inhibitor concentration required to inhibit half the enzyme activity.

Claims

WHAT IS CLAIMED IS:
1. An IMP-1 metallo beta-lactamase which is derived from Pseudomonas aeruginosa and comprising a protein having the sequence of sequence ID 1, the coordinates of Table IA, and the interatomic distances and angles of active site residues listed in Table IV in an essentially pure native form or a homolog thereof.
2. A beta-lactamase of claim 1 which is in its native crystalline form.
3. A beta-lactamase according to claims 1 or 2 wherein said beta-lactamase has an active site formed by the amino acids His95, His97 and Hisl57 as ligands to Znl, Asp99, Cysl76 and His215 as ligands to Zn2, Glu41, Val43, Val49, Lys51 , Phe69, Asnl 85, Lysl79, Trp46, Ser216, Tyrl 81 and Glyl 82 (This numbering scheme includes the 18 residues at the N- terminus corresponding to the signal sequence).
4. A composition comprising the beta-lactamase of claim 1 complexed with the inhibitor SB-252619 as characterized by the coordinates selected from the group consisting of the coordinates of Tables IB, II and III.
5. A heavy atom derivative of a Pseudomonas aeruginosa IMP-1 metallo beta- lactamase crystal wherein the beta-lactamase comprises a protein having the coordinates represented in Figures 1, 2, 3 and 4, and listed in Tables la, lb, II, III and IV.
6. A beta-lactamase according to claim 1 wherein said beta-lactamase is characterized by an alpha+beta fold with four layers, alpha/beta/beta/alpha, wherein the beta strands form a beta sandwich with a seven, mixed strand beta sheet on the N-terminal side and a five, mixed strand beta sheet on the C-terminal side of the molecule and two alpha helices pack against the faces on either side of the sandwich and a third alpha helix is located at the edge of the beta sandwich.
7. A process of identifying an inhibitor compound capable of inhibiting the enzymatic activity of a Pseudomonas aeruginosa IMP- 1 metallo beta-lactamase according to claim 1 , said process comprising: introducing into a suitable computer program information defining an active site conformation of a IMP-1 metallo beta-lactamase inhibitor complex molecule comprising a conformation defined by the coordinates of Figures 1 , 2, 3 and 4 and listed in Tables la or lb, II and III and IV, wherein said program displays the three-dimensional structure thereof; creating a three dimensional structure of a test compound in said computer program; displaying and superimposing the model of said test compound on the model of said active site; assessing whether said test compound model fits spatially into the active site; incoφorating said test compound in a biological beta-lactamase activity assay for a beta-lactamase characterized by said active site; and determining whether said test compound inhibits enzymatic activity in said assay.
8. A process of identifying an inhibitor compound capable of inhibiting the enzymatic activity of a Pseudomonas aeruginosa IMP- 1 metallo beta-lactamase according to claim 1, said process comprising: carrying out an in vitro assay by introducing said compound in a biological beta- lactamase activity assay containing a beta-lactamase according to claim 1 and determining whether said test compound inhibits the enzymatic activity of the beta- lactamase in said assay.
9. A product of the process of claim 7 or 8 which is a peptide, peptidomimetic or synthetic molecule and is useful for inhibiting the metallo beta lactamase in the treatment of bacterial infections in a mammal.
10. A product according to claim 9 wherein said product is a competitive or non- competitive inhibitor of the Pseudomonas aeruginosa beta-lactamase.
1 1. A process for determining a crystal structure form using the structural coordinates of a Pseudomonas aeruginosa IMP-1 metallo beta-lactamase crystal or portions thereof, to determine a crystal form of a mutant, homologue or co-complex of said beta- lactamase by molecular replacement.
12. A process for designing drugs useful for inhibiting Pseudomonas aeruginosa
IMP-1 metallo beta- lactamase comprising using the atomic coordinates of a Pseudomonas aeruginosa IMP-1 metallo beta-lactamase crystal or the atomic coordinates of a P. aeruginosa IMP-1 metallo beta-lactamase complex with SB-252619 to computationally evaluate a chemical entity for associating with the active site of a Pseudomonas aeruginosa IMP-1 metallo beta-lactamase.
13. The process according to claim 13 comprising the step of using the structure coordinates of Pseudomonas aeruginosa IMP-1 metallo beta-lactamase to identify an intermediate in a chemical reaction between said beta-lactamase and a compound with is a substrate or inhibitor of said beta-lactamase.
14. The process according to claims 12 or 13 wherein said structure coordinates comprise the coordinates of Figures 1, 2, 3 and 4 and listed in Tables I, II, III and IV .
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Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP3034186B1 (en) * 2014-12-16 2018-09-19 Luxembourg Institute of Science and Technology (LIST) Method of degradation and inactivation of antibiotics in water by immobilized enzymes onto functionalized supports
CN109337889A (en) * 2018-12-26 2019-02-15 广州白云山拜迪生物医药有限公司 A kind of metallo-β-lactamase mutant and its construction method that enzyme activity improves

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4331597A (en) * 1979-10-02 1982-05-25 Meiji Seika Kaisha, Ltd. Penicillin compounds
US4406898A (en) * 1981-09-08 1983-09-27 Eli Lilly And Company Oxazole and oxadiazole cephalosporins
EP0238061A2 (en) * 1986-03-20 1987-09-23 Banyu Pharmaceutical Co., Ltd. Cephalosporin derivatives, processes for their preparation and antibacterial agents

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4331597A (en) * 1979-10-02 1982-05-25 Meiji Seika Kaisha, Ltd. Penicillin compounds
US4406898A (en) * 1981-09-08 1983-09-27 Eli Lilly And Company Oxazole and oxadiazole cephalosporins
EP0238061A2 (en) * 1986-03-20 1987-09-23 Banyu Pharmaceutical Co., Ltd. Cephalosporin derivatives, processes for their preparation and antibacterial agents

Non-Patent Citations (2)

* Cited by examiner, † Cited by third party
Title
LACHAPELLE ET AL.: "Characterization of bla-CARB-3 gene encoding the carbenicillinase-3 B-lactamase of Pseudomonas aeruginosa", GENE, vol. 102, 1991, pages 7 - 12, XP002937631 *
NORDMANN ET AL.: "Sequence analysis of PER-1 extended-spectrum B-lactamase from Pseudomonas aeruginosa and comparison with class A B-lactamases", ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, vol. 38, no. 1, January 1994 (1994-01-01), pages 104 - 114, XP002937632 *

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP3034186B1 (en) * 2014-12-16 2018-09-19 Luxembourg Institute of Science and Technology (LIST) Method of degradation and inactivation of antibiotics in water by immobilized enzymes onto functionalized supports
CN109337889A (en) * 2018-12-26 2019-02-15 广州白云山拜迪生物医药有限公司 A kind of metallo-β-lactamase mutant and its construction method that enzyme activity improves

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