NOVEL METALLOPROTEASES

Abstract

Aspects of the present compositions and methods relate to novel metalloproteases polynucleotides encoding the novel metalloprotease, compositions and methods for use thereof.

Claims

1. A metalloprotease polypeptide comprising a calcium binding region.

2. The polypeptide of claim 1, wherein the polypeptide comprises a modification in at least one amino acid residue in one of the calcium binding regions, Ca1-2, Ca3 and Ca4, (including residues 55-66, 136, 138, 177-190, and 193-200) of the polypeptide, wherein the amino acid positions of the polypeptide are numbered by correspondence with the amino acid sequence of Bacillus thermoproteolyticus metalloprotease set forth in SEQ ID NO: 13.

3. The polypeptide of claim 2, wherein the polypeptide comprises a modification in at least one amino acid residue in a calcium binding region 1-2 of residues 177-190, 136 and 138 of the polypeptide.

4. The polypeptide of any of the above claims, wherein the polypeptide comprises an amino acid at position 184 selected from the group consisting of lysine, threonine, alanine, glutamic acid and aspartic acid.

5. The polypeptide of any of the above claims, wherein the amino acid at position 185 is an amino acid other than aspartic acid.

6. The polypeptide of claim 5, wherein the amino acid at position 185 is a non-negatively charged residue.

7. The polypeptide of any of claim 5 or 6, wherein the amino acid at position 185 is a neutrally charged residue.

8. The polypeptide of any of claims 5-7, wherein the amino acid at position 185 is an asparagine or serine.

9. The polypeptide of any of the above claims, wherein the amino acid at position 187 is a non-negatively charged residue.

10. The polypeptide of claim 9, wherein the amino acid at position 187 is a neutrally charged residue.

11. The polypeptide of any of claim 9 or 10, wherein the amino acid at position 187 is a leucine or methionine.

12. The polypeptide of any of claims 1-8, wherein the amino acid at position 187 is an aspartic acid.

13. The polypeptide of any of the above claims, wherein the amino acid at position 188 is a leucine, valine or methionine.

14. The polypeptide of any of the above claims, wherein the amino acid at position 190 is a residue other than glutamic acid.

15. The polypeptide of claim 14, wherein the amino acid at position 190 is aspartic acid.

16. The polypeptide of any of the above claims, wherein the polypeptide comprises a deletion at amino acid residue positions 179-183.

17. The polypeptide of any of the above claims, wherein the amino acid at position 177 is a neutrally charged residue or aspartic acid.

18. The polypeptide of any of the above claims, wherein the amino acid at position 177 is glutamine or aspartic acid.

19. The polypeptide of any of the above claims, wherein the amino acid at position 178 is a residue selected from the group consisting of glycine, serine, arginine, alanine, asparagine, and threonine.

20. The polypeptide of any of the above claims, wherein the amino acid at position 136 is an aspartic acid or serine.

21. The polypeptide of any of the above claims, comprising a modification in at least one amino acid residue in a calcium binding region 3 of residues 55-66, wherein the amino acid positions of the polypeptide are numbered by correspondence with the amino acid sequence of Bacillus thermoproteolyticus metalloprotease set forth in SEQ ID NO: 13.

22. The polypeptide of any of the above claims, wherein the amino acid at position 55 is a residue selected from the group consisting of leucine, serine, valine, and methionine.

23. The polypeptide of any of the above claims, wherein the amino acid at position 56 is a residue selected from the group consisting of serine, arginine and threonine.

24. The polypeptide of any of the above claims, wherein the amino acid at position 57 is a serine.

25. The polypeptide of any of the above claims, wherein the amino acid at position 58 is a serine or threonine.

26. The polypeptide of any of the above claims, wherein the amino acid at position 59 is a residue selected from the group consisting of serine, threonine, and asparagine.

27. The polypeptide of any of the above claims, wherein the amino acid at position 60 is a serine.

28. The polypeptide of any of the above claims, wherein the amino acid at position 61 is a residue selected from the group consisting of isoleucine, valine, and threonine.

29. The polypeptide of any of the above claims, wherein the amino acid at position 62 is a residue selected from the group consisting of tryptophan and phenylalanine.

30. The polypeptide of any of the above claims, wherein the amino acid at position 63 is a residue selected from the group consisting of asparagine, glutamic acid, and threonine.

31. The polypeptide of any of the above claims, wherein the polypeptide comprises a deletion at amino acid residue positions 64-66.

32. The polypeptide of any of the above claims, comprising a modification in at least one amino acid residue in a calcium binding region 4 of residues 193-200, wherein the amino acid positions of the polypeptide are numbered by correspondence with the amino acid sequence of Bacillus thermoproteolyticus metalloprotease set forth in SEQ ID NO: 13.

33. The polypeptide of any of the above claims, wherein the amino acid at position 193 is a threonine.

34. The polypeptide of any of the above claims, wherein the amino acid at position 194 is an isoleucine.

35. The polypeptide of any of the above claims, wherein the amino acid at position 195 is a serine.

36. The polypeptide of any of the above claims, wherein the polypeptide comprises a deletion at amino acid residue positions 196-198.

37. The polypeptide of any of the above claims, wherein the amino acid at position 199 is a glutamine.

38. The polypeptide of any of the above claims, wherein the amino acid at position 200 is a proline.

39. The polypeptide of any of the above claims, wherein the calcium binding region 1-2 binds fewer than two calcium ions.

40. The polypeptide of any of the above claims, wherein the calcium binding region 3 binds fewer than one calcium ion.

41. The polypeptide of any of the above claims, wherein the calcium binding region 4 binds fewer than one calcium ion.

42. The polypeptide of any of the previous claims, wherein the polypeptide is a variant of a parent polypeptide.

43. The polypeptide of claim 42, wherein the variant comprises a modification in a calcium binding region of the parent polypeptide.

44. The polypeptide of claim 43, wherein the modification is to any of the amino acids listed in claims 4-38.

45. The polypeptide of any of the previous claims, wherein the parent polypeptide is an M4 metalloprotease.

46. The polypeptide of any of the previous claims, wherein the polypeptide has at least 60% sequence identity to the parent polypeptide.

47. The polypeptide of any of the previous claims, wherein the polypeptide has at least 60% sequence identity to any one of SEQ ID NOs: 1-15.

48. The polypeptide of any of the previous claims, wherein the polypeptide has at least 60% sequence identity to SEQ ID NOs: 13.

49. The polypeptide of any of the previous claims, wherein the polypeptide has metalloprotease activity.

50. A composition comprising any of the polypeptides of claims 1-49.

51. The composition of claim 50, wherein said composition is a cleaning composition.

52. The composition of claim 51, wherein said composition is a detergent composition.

53. The composition of claim 52, wherein said detergent composition is selected from the group consisting of a laundry detergent, a fabric softening detergent, a dishwashing detergent, and a hard-surface cleaning detergent.

54. The composition of any of claims 50 to 53, wherein said composition further comprises a surfactant.

55. The composition of claim 54, wherein said surfactant is selected from the group consisting of an anionic surfactant, a cationic surfactant, a zwitterionic surfactant, a ampholytic surfactant, a semi-polar non-ionic surfactant, and a combination thereof.

56. The composition of claim 55, wherein said surfactant is an ionic surfactant.

57. The composition of claim 55, wherein said surfactant is a non-ionic surfactant.

58. The composition of any of claims 50-57, wherein said composition further comprises at least one stabilizer.

59. The composition of any of claims 50-58, wherein said composition comprises from about 0.001 to about 10 weight % of said polypeptide.

60. The composition of any of claims 50-59, further comprising at least one bleaching agent.

61. The composition of any of claims 50-60, wherein said cleaning composition is phosphate-free.

62. The composition of any of claims 50-60, wherein said cleaning composition contains phosphate.

63. The composition of any of claims 50-62, further comprising at least one adjunct ingredient.

64. The composition of any of claims 50-63, wherein said composition is a granular, powder, solid, bar, liquid, tablet, gel, unit dose or paste composition.

65. The composition of any of claims 50-64, further comprising one or more additional enzymes or enzyme derivatives selected from the group consisting of acyl transferases, alpha-amylases, beta-amylases, alpha-galactosidases, arabinosidases, aryl esterases, beta-galactosidases, carrageenases, catalases, cellobiohydrolases, cellulases, chondroitinases, cutinases, endo-beta-1, 4-glucanases, endo-beta-mannanases, esterases, exo-mannanases, galactanases, glucoamylases, hemicellulases, hyaluronidases, keratinases, laccases, lactases, ligninases, lipases, lipoxygenases, mannanases, oxidases, pectate lyases, pectin acetyl esterases, pectinases, pentosanases, peroxidases, phenoloxidases, phosphatases, phospholipases, phytases, polygalacturonases, proteases, pullulanases, reductases, rhamnogalacturonases, beta-glucanases, tannases, transglutaminases, xylan acetyl-esterases, xylanases, xyloglucanases, and xylosidases, additional metalloprotease enzymes and combinations thereof.

66. The composition of any of claims 50-65, wherein said composition is formulated at a pH of from about 5.0 to about 12.0.

67. A method of cleaning, comprising contacting a surface or an item with a composition comprising the variant of any one of claims 1-49.

68. A method of cleaning comprising contacting a surface or an item with the composition of any one of claims 50-66.

69. The method of claim 67 or 68, further comprising rinsing said surface or item after contacting said surface or item, respectively, with said composition.

70. The method of any one of claims 67-69, wherein said item is dishware.

71. The method of any one of claims 67-70, wherein said item is fabric.

72. The method of any one of claims 67-71, further comprising the step of rinsing said surface or item after contacting said surface or item with said composition.

73. The method of claim 72, further comprising the step of drying said surface or item after said rinsing of said surface or item.

74. A method of cleaning a surface or item, comprising: providing the composition of any of claims 50-66 and a surface or item in need of cleaning; and contacting said composition with said surface or item in need of cleaning under conditions suitable for the cleansing of said surface of said surface or item, to produce a cleansed surface or item.

75. The method of claim 74, further comprising the step of rinsing said cleansed surface or item to produce a rinsed surface or item.

76. The method of any of claim 74 or 75, further comprising the step of drying said rinsed surface or item.

77. A method for producing the variant of any of claims 1-49 comprising: a. stably transforming a host cell with an expression vector comprising a polynucleotide encoding the variant of any of claims 1-49; b. cultivating said transformed host cell under conditions suitable for said host cell to produce said protease; and c. recovering said protease.

78. The method of claim 77, wherein said host cell is a filamentous fungus or bacterial cell.

79. The method of any of claim 77 or 78, wherein said host cell is selected from Bacillus spp., Streptomyces spp., Escherichia spp., Aspergillus spp., Trichoderma spp., Pseudomonas spp., Corynebacterium spp., Saccharomyces spp., or Pichia spp.

80. A textile processing composition comprising the variant of any one of claims 1-49.

81. An animal feed composition comprising the variant of any one of claims 1-49.

82. A leather processing composition comprising the variant of any one of claims 1-49.

83. A feather processing composition comprising the variant or recombinant polypeptide of any one of claims 1-49.

84. A lens cleaning composition comprising the variant of any one of claims 1-49.

85. A tissue debridement composition comprising the variant of any one of claims 1-49.

86. A tissue cell culture additive composition comprising the variant of any one of claims 1-49.

Description

BRIEF DESCRIPTION OF THE DRAWINGS

[0008] FIG. 1 provides a schematic showing the arrangement of the two independent molecules of PehPro1 in the asymmetric unit of the crystal unit cell.

[0009] FIG. 2 provides a stereo showing a schematic of the Thermolysin main chain folding (black) and the schematic of PehPro1 (light gray).

[0010] FIG. 3 provides a close up view of the 3 residue deletion.

[0011] FIG. 4 provides a close up view of the 5 residue deletion.

[0012] FIG. 5 provides a comparison of calcium binding site 1 in PehPro1 and the Ca1-2 calcium binding site in Thermolysin.

[0013] FIG. 6 provides a schematic comparing Thermolysin (black lines) with PehPro1 (light gray sticks) in the vicinity of the second calcium binding site (Ca4) in PehPro1.

[0014] FIG. 7 provides a comparison of the structures of Thermolysin (black lines) and PehPro1 (light gray sticks) in the region of calcium binding Ca3 present in Thermolysin.

[0015] FIG. 8 provides a schematic comparing the main chain folding of PehPro1 (dark gray) and PpoPro2 (light gray).

[0016] FIG. 9 provides a comparison of the first common calcium binding site between PehPro1 (light gray) and Ppopro2 (dark gray).

[0017] FIG. 10 provides a comparison of the structure of PehPro1 (light gray) and PpoPro2 (dark gray) at the second common calcium site.

[0018] FIG. 11 provides a comparison of the third calcium binding site seen in PpoPro2 (dark gray) as compared to PehPro1 (light gray).

[0019] FIG. 12a-f provides a structure-based alignment of the various metalloproteases Peh1.A (Paenibacillus ehimensis, protein 1)(SEQ ID NO: 1), PbaPro1 (Paenibacillus barcinonensis, protein 1) (SEQ ID NO: 2), PhuPro1 (Paenibacillus hunanensis, protein 1) (SEQ ID NO: 3), PpoPro2 (Paenibacillus polymyxa, protein 2) (SEQ ID NO: 4), PpoPro1 (Paenibacillus polymyxa, protein 1) (SEQ ID NO: 5), PamPro1 (Paenibacillus amylolyticus, protein 1)(SEQ ID NO: 6), PhuPro2 (Paenibacillus hunanensis, protein 2) (SEQ ID NO: 7), PspPro2 (Paenibacillus sp., protein 2) (SEQ ID NO: 8), PspPro3 (Paenibacillus sp., protein 3) (SEQ ID NO: 9), PpePro1 (Paenibacillus peoriae, protein 1) (SEQ ID NO: 10), PtePro1 (Paenibacillus terrae, protein 1) (SEQ ID NO: 11), BbrPro1 (Brevibacillus brevis, protein 1) (SEQ ID NO: 12), 1KEI.A (Bacillus thermoproteolyticus, thermolysin) (SEQ ID NO: 13), 1NPC.A (Bacillus cereus) (SEQ ID NO: 14), Npre var (Bacillus subtilis) (SEQ ID NO: 15).

[0020] FIG. 13 provides a comparison of the calcium binding sites of NprE (gray sticks) with the double calcium site (Ca1,2) of Thermolysin (black lines).

[0021] FIG. 14 provides a comparison of NprE variant with Thermolysin at the Ca3 site.

[0022] FIG. 15 provides several proteases contain the double delete and lack of the DD motif shown in a rectangle.

[0023] FIG. 16 provides a stereodiagram comparing the overall main chain folding pattern of Thermolysin (black) with the NprE variant structure (gray).

[0024] FIG. 17 provides a comparison of the structures of the NprE variant and Thermolysin at the Ca4 binding site of Thermolysin. The deletion of three residues in NprE relative to Thermolysin results in the elimination of a calcium binding site.

DETAILED DESCRIPTION

[0025] The present invention provides novel variant metalloproteases having modifications at calcium binding regions. The MEROPS database (http://merops.sanger.ac.uk) groups peptidases into families based on sequence homology [Rawlings et al. (2010) Nucleic Acid Res. 38:D227]. A peptidase is classified into a family based on sharing significant similarities in amino acid sequence with the type example or another member of the family. In the current release (Release 9.4) of the MEROPS database, there are a total of 63 metalloprotease families, nine of which include but are not limited to BEMP members. These proteases are distributed among 9 families of metalloproteases because of differences in primary sequences and structural characteristics. So far, all BEMPs are endoproteases that harbor 1 catalytic Zinc ion in their active center. They are synthetized as inactive zymogens with a propeptide and their main function is nutrition of the microorganism. Bacterial extracellular metalloproteases (BEMPs) are a large group of metal-containing proteases secreted by heterotropic bacteria [Wu and Chen (2011) Appl. Biol. Biotechnol. 92:253]. BEMPs are distributed among the metalloprotease families M4, M5, M9, M10, M12, M13, M23, M30, and M34. The M4 is a large family of metalloproteases, mostly BEMPs. Thermolysin is the prototype of the M4 family.

[0026] Thermolysin-like proteases are broad-specificity proteases which contain a catalytic zinc ion in their active sites. The thermostable Bacillus neutral metalloproteases bind 4 Ca.sup.2+ ions. Two Ca.sup.2+ ions are bound in one double calcium binding site (Ca1-2) and 2 Ca.sup.2+ ions are bound in single binding sites Ca3 and Ca4 [Stark et al (1992) Eur. J. Biochem. 207:207, Veltman et al (1998) Biochem. 37:5312]. Several studies have shown that these proteases are dependent on calcium binding for their stability [Veltman et al (1997) FEBS 405:241]. The single sites Ca3 and Ca4 are absent in the thermolysin-like proteases considered thermolabile [Eijsink et al (2011) Prot. Sci. 20:1346].

[0027] It has also become known that thermolysin-like proteinases can perform well in a number of industrial applications such as a detergent additive for laundry and dish cleaning, potentially as feed additives, fermentation aides, as well as a number of pharmaceutical application such as cell culture and tissue dissociation. Earlier studies have demonstrated the importance of calcium binding in a number of mutational studies. In Eijsink et al 2011, [Eijsink, Matthews and Vriend (2011) Prot Sci 20:1346-1355], mutation of Asp57 or Asp 59 in the Ca3 site were shown to dramatically reduce stability in thermolysin. In the same paper the authors postulate that calcium binding site may have evolved evolutionarily as a means or regulating function but destabilizing structure and hence function in the low calcium environment of the cytosol until secreted into a higher calcium environment outside the cell membrane.

[0028] Metalloproteases, for example, M4 clan metalloproteases, have calcium binding regions. Without being bound by theory, these calcium binding regions are thought to contribute to the thermostability of these molecules. In some applications, it is beneficial to reduce the dependence of the metalloproteases on calcium binding. For example, detergent compositions contain metal chelators, such as surfactants, which compete for calcium ions and affects the amount of free calcium available to bind the enzyme [Stoner et al. (2005) Biotechnol Prog. 21(6): 1716-23]. In detergent environments, metalloproteases can be subject to destabilization and autolysis due to this lack of free calcium. Thus, there is a need in the art to discover improved metalloproteases which are stable in environments that compete for free calcium, such as detergent compositions, while allowing for maintained proteolytic activity of the metalloproteases in these environments. As such, it would be beneficial to find variant metalloproteases with modified calcium binding regions.

[0029] The invention described here arises in part from the observation of two novel crystal structures of thermolysin-like proteases having fewer calcium binding sites (PehPro1 as shown in Example 2, and PpoPro2, Paenibacillus polymyxa protease in Ruf et al 2013 [Ruf et al (2013) Acta Cryst. D69:24-31). The elimination of calcium binding is attributed to a combination of specific amino acid substitutions and deletion that are found to be common to these and related structures resulting in fewer calcium binding coordination sites. Based on these finding, a means for further reducing the number of calcium bound to only one or none is proposed for thermolysin and other thermolysin-like proteinases.

[0030] In some embodiments, the invention is variant metalloproteases having modified calcium binding regions. In some embodiments, these modified calcium binding regions result in reduced calcium binding of the metalloprotease enzyme. In other embodiments, the invention is novel metalloproteases having newly discovered calcium binding regions. In some embodiments, the invention includes compositions comprising at least one of the novel metalloprotease enzymes set forth herein. Some such compositions comprise detergent compositions. The metalloprotease enzymes of the present invention can be combined with other enzymes useful in detergent compositions. The invention also provides methods of cleaning using metalloprotease enzymes of the present invention.

Definitions and Abbreviations

[0031] Unless otherwise indicated, the practice of the present invention involves conventional techniques commonly used in molecular biology, protein engineering, microbiology, and recombinant DNA technology, which are within the skill of the art. Such techniques are known to those of skill in the art and are described in numerous texts and reference works well known to those of skill in the art. All patents, patent applications, articles and publications mentioned herein, both supra and infra, are hereby expressly incorporated herein by reference.

[0032] Unless defined otherwise herein, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention pertains. Many technical dictionaries are known to those of skill in the art. Although any methods and materials similar or equivalent to those described herein find use in the practice of the present invention, some suitable methods and materials are described herein. Accordingly, the terms defined immediately below are more fully described by reference to the Specification as a whole. Also, as used herein, the singular a, an and the includes the plural reference unless the context clearly indicates otherwise. Unless otherwise indicated, nucleic acids are written left to right in 5 to 3 orientation; amino acid sequences are written left to right in amino to carboxy orientation, respectively. It is to be understood that this invention is not limited to the particular methodology, protocols, and reagents described, as these may vary, depending upon the context they are used by those of skill in the art.

[0033] Furthermore, the headings provided herein are not limitations of the various aspects or embodiments of the invention.

[0034] It is intended that every maximum numerical limitation given throughout this specification includes every lower numerical limitation, as if such lower numerical limitations were expressly written herein. Every minimum numerical limitation given throughout this specification will include every higher numerical limitation, as if such higher numerical limitations were expressly written herein. Every numerical range given throughout this specification will include every narrower numerical range that falls within such broader numerical range, as if such narrower numerical ranges were all expressly written herein. As used herein, the terms protease and proteinase refer to an enzyme that has the ability to break down proteins and peptides. A protease has the ability to conduct proteolysis, by hydrolysis of peptide bonds that link amino acids together in a peptide or polypeptide chain forming the protein. This activity of a protease as a protein-digesting enzyme is referred to as proteolytic activity. Many well known procedures exist for measuring proteolytic activity (See e.g., Kalisz, Microbial Proteinases, In: Fiechter (ed.), Advances in Biochemical Engineering/Biotechnology, (1988)). For example, proteolytic activity may be ascertained by comparative assays which analyze the respective protease's ability to hydrolyze a suitable substrate. Exemplary substrates useful in the analysis of protease or proteolytic activity, include, but are not limited to, di-methyl casein (Sigma C-9801), bovine collagen (Sigma C-9879), bovine elastin (Sigma E-1625), and bovine keratin (ICN Biomedical 902111). Colorimetric assays utilizing these substrates are well known in the art (See e.g., WO 99/34011 and U.S. Pat. No. 6,376,450, both of which are incorporated herein by reference). The pNA peptidyl assay (See e.g., Del Mar et al., Anal. Biochem. 99:316-320 [1979]) also finds use in determining the active enzyme concentration. This assay measures the rate at which p-nitroaniline is released as the enzyme hydrolyzes a soluble synthetic substrate, such as succinyl-alanine-alanine-proline-phenylalanine-p-nitroanilide (suc-AAPF-pNA)(SEQ ID NO: 24). The rate of production of yellow color from the hydrolysis reaction is measured at 410 nm on a spectrophotometer and is proportional to the active enzyme concentration. In addition, absorbance measurements at 280 nanometers (nm) can be used to determine the total protein concentration in a sample of purified protein. The activity on substrate/protein concentration gives the enzyme specific activity.

[0035] As used herein, the term variant polypeptide refers to a polypeptide comprising an amino acid sequence that differs in at least one amino acid residue from the amino acid sequence of a parent or reference polypeptide (including but not limited to wild-type polypeptides).

[0036] As used herein, the genus Bacillus includes all species within the genus Bacillus, as known to those of skill in the art, including but not limited to B. subtilis, B. licheniformis, B. lentus, B. brevis, B. stearothermophilus, B. alkalophilus, B. amyloliquefaciens, B. clausii, B. halodurans, B. megaterium, B. coagulans, B. circulans, B. lautus, and B. thuringiensis. It is recognized that the genus Bacillus continues to undergo taxonomical reorganization. Thus, it is intended that the genus include species that have been reclassified, including but not limited to such organisms as B. stearothermophilus, which is now named Geobacillus stearothermophilus. The production of resistant endospores under stressful environmental conditions is considered the defining feature of the genus Bacillus, although this characteristic also applies to the recently named Alicyclobacillus, Amphibacillus, Aneurinibacillus, Anoxybacillus, Brevibacillus, Filobacillus, Gracilibacillus, Halobacillus, Paenibacillus, Salibacillus, Thermobacillus, Ureibacillus, and Virgibacillus.

[0037] As used herein, calcium binding site refers to a region within a metalloprotease which can bind a calcium ion in the presence of free calcium. Calcium can act to assist in maintaining the structural integrity of metalloproteases under many conditions. In some embodiments, the amount of free calcium can be related to the water hardness during wash conditions, and can range from soft water, having less than 1.0 Calcium grains per gallon, to slightly hard water, having from about 1.0 to 3.5 Calcium grains per gallon, to moderately hard water, having from about 3.5 to 7.0 Calcium grains per gallon, to hard water, having from about 7.0 to 10.5 or more Calcium grains per gallon. In some embodiments of the present invention, the characteristics of the calcium binding site are modified compared to a parent or reference metalloprotease so as to modify the performance of the metalloprotease. Modification of the calcium binding site may include reducing or increasing the affinity of the site to bind calcium ion. Modifying the performance of the metalloprotease is intended to include modification of the stability (e.g., oxidative or thermal) or the activity (e.g., the rate or efficiency with which the metalloprotease hydrolyzes a protein substrate) of the enzyme in its various applications.

[0038] As used herein, calcium ligand means an amino acid residue or residues within a metalloprotease enzyme which forms a ligand with calcium ion bound within a calcium binding site.

[0039] The terms polynucleotide and nucleic acid, which are used interchangeably herein, refer to a polymer of any length of nucleotide monomers covalently bonded in a chain. DNA (deoxyribonucleic acid), a polynucleotide comprising deoxyribonucleotides, and RNA (ribonucleic acid), a polymer of ribonucleotides, are examples of polynucleotides or nucleic acids having distinct biological function. Polynucleotides or nucleic acids include, but are not limited to, a single-, double- or triple-stranded DNA, genomic DNA, cDNA, RNA, DNA-RNA hybrid, or a polymer comprising purine and pyrimidine bases, or other natural, chemically, biochemically modified, non-natural or derivatized nucleotide bases. The following are non-limiting examples of polynucleotides: genes, gene fragments, chromosomal fragments, expressed sequence tag(s) (EST(s)), exons, introns, messenger RNA (mRNA), transfer RNA (tRNA), ribosomal RNA (rRNA), ribozymes, complementary DNA (cDNA), recombinant polynucleotides, branched polynucleotides, plasmids, vectors, isolated DNA of any sequence, isolated RNA of any sequence, nucleic acid probes, and primers.

[0040] As used herein, the term modification refers to changes made to a reference amino acid or nucleic acid sequence. It is intended that the term encompass substitutions, insertions and deletions.

[0041] As used herein, the term vector refers to a nucleic acid construct used to introduce or transfer nucleic acid(s) into a target cell or tissue. A vector is typically used to introduce foreign DNA into a cell or tissue. Vectors include plasmids, cloning vectors, bacteriophages, viruses (e.g., viral vector), cosmids, expression vectors, shuttle vectors, and the like. A vector typically includes an origin of replication, a multicloning site, and a selectable marker. The process of inserting a vector into a target cell is typically referred to as transformation. The present invention includes, in some embodiments, a vector that comprises a DNA sequence encoding a metalloprotease polypeptide (e.g., precursor or mature metalloprotease polypeptide) that is operably linked to a suitable prosequence (e.g., secretory, signal peptide sequence, etc.) capable of effecting the expression of the DNA sequence in a suitable host, and the folding and translocation of the recombinant polypeptide chain.

[0042] As used herein, the term expression cassette, expression plasmid or expression vector refers to a nucleic acid construct or vector generated recombinantly or synthetically for the expression of a nucleic acid of interest in a target cell. An expression vector or expression cassette typically comprises a promoter nucleotide sequence that drives expression of the foreign nucleic acid. The expression vector or cassette also typically includes any other specified nucleic acid elements that permit transcription of a particular nucleic acid in a target cell. A recombinant expression cassette can be incorporated into a plasmid, chromosome, mitochondrial DNA, plastid DNA, virus, or nucleic acid fragment. Many prokaryotic and eukaryotic expression vectors are commercially available.

[0043] In some embodiments, the ends of the sequence are closed such that the DNA construct forms a closed circle. The nucleic acid sequence of interest, which is incorporated into the DNA construct, using techniques well known in the art, may be a wild-type, mutant, or modified nucleic acid. In some embodiments, the DNA construct comprises one or more nucleic acid sequences homologous to the host cell chromosome. In other embodiments, the DNA construct comprises one or more non-homologous nucleotide sequences. Once the DNA construct is assembled in vitro, it may be used, for example, to: 1) insert heterologous sequences into a desired target sequence of a host cell; and/or 2) mutagenize a region of the host cell chromosome (i.e., replace an endogenous sequence with a heterologous sequence); 3) delete target genes; and/or 4) introduce a replicating plasmid into the host. DNA construct is used interchangeably herein with expression cassette.

[0044] As used herein, a plasmid refers to an extrachromosomal DNA molecule which is capable of replicating independently from the chromosomal DNA. A plasmid is double stranded (ds) and may be circular and is typically used as a cloning vector.

[0045] As used herein in the context of introducing a nucleic acid sequence into a cell, the term introduced refers to any method suitable for transferring the nucleic acid sequence into the cell. Such methods for introduction include but are not limited to protoplast fusion, transfection, transformation, electroporation, conjugation, and transduction (See e.g., Ferrari et al., Genetics, in Hardwood et al. (eds.), Bacillus, Plenum Publishing Corp., pp. 57-72 [1989]).

[0046] Transformation refers to the genetic alteration of a cell which results from the uptake, optional genomic incorporation, and expression of genetic material (e.g., DNA).

[0047] As used herein, a nucleic acid is operably linked with another nucleic acid sequence when it is placed into a functional relationship with another nucleic acid sequence. For example, a promoter or enhancer is operably linked to a nucleotide coding sequence if the promoter affects the transcription of the coding sequence. A ribosome binding site may be operably linked to a coding sequence if it is positioned so as to facilitate translation of the coding sequence. Typically, operably linked DNA sequences are contiguous. However, enhancers do not have to be contiguous. Linking is accomplished by ligation at convenient restriction sites. If such sites do not exist, synthetic oligonucleotide adaptors or linkers may be used in accordance with conventional practice.

[0048] As used herein the term gene refers to a polynucleotide (e.g., a DNA segment), that encodes a polypeptide and includes regions preceding and following the coding regions as well as intervening sequences (introns) between individual coding segments (exons).

[0049] As used herein, recombinant when used with reference to a cell typically indicates that the cell has been modified by the introduction of a foreign nucleic acid sequence or that the cell is derived from a cell so modified. For example, a recombinant cell may comprise a gene not found in identical form within the native (non-recombinant) form of the cell, or a recombinant cell may comprise a native gene (found in the native form of the cell) but which has been modified and re-introduced into the cell. A recombinant cell may comprise a nucleic acid endogenous to the cell that has been modified without removing the nucleic acid from the cell; such modifications include those obtained by gene replacement, site-specific mutation, and related techniques known to those of ordinary skill in the art. Recombinant DNA technology includes techniques for the production of recombinant DNA in vitro, and transfer of the recombinant DNA into cells where it may be expressed or propagated, thereby producing a recombinant polypeptide. Recombination, recombining, and recombined of polynucleotides or nucleic acids refer generally to the assembly or combining of two or more nucleic acid or polynucleotide strands or fragments to generate a new polynucleotide or nucleic acid. The recombinant polynucleotide or nucleic acid is sometimes referred to as a chimera. A nucleic acid or polypeptide is recombinant when it is artificial or engineered.

[0050] A nucleic acid or polynucleotide is said to encode a polypeptide if, in its native state or when manipulated by methods known to those of skill in the art, it can be transcribed and/or translated to produce the polypeptide or a fragment thereof. The anti-sense strand of such a nucleic acid is also said to encode the sequence.

[0051] Host strain or host cell refers to a suitable host for an expression vector comprising a DNA sequence of interest.

[0052] A protein or polypeptide comprises a polymeric sequence of amino acid residues. The terms protein and polypeptide are used interchangeably herein. The single and 3-letter code for amino acids as defined in conformity with the IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN) is used through out this disclosure. The single letter X refers to any of the twenty amino acids. It is also understood that a polypeptide may be coded for by more than one nucleotide sequence due to the degeneracy of the genetic code. Mutations can be named by the one letter code for the parent amino acid, followed by a position number and then the one letter code for the variant amino acid. For example, mutating glycine (G) at position 87 to serine (S) is represented as G087S or G87S. Mutations can also be named by using the three letter code for an amino acid followed by its position in the polypeptide chain as counted from the N-terminus; for example, Ala10 for alanine at position 10. Multiple mutations are indicated by inserting a , +, /, or ; between the mutations. Mutations at positions 87 and 90 are represented as either G087S-A090Y or G87S-A90Y or G87S+A90Y or G087S+A090Y. For insertions, one or more inserted amino acids can be listed after a position. For example, G087GS describes a serine inserted after the glycine at position 87; as a second example, G087GSA describes a serine and alanine inserted after the glycine at position 87. Insertions can be done in combination with substitutions; thus, G087RS describes a substitution at position 87 from glycine to arginine, followed by an inserted serine residue. For deletions, either a or del is used following the position number. Thus, for example, G087del describes deletion of the glycine at position 87. When describing modifications, a position followed by amino acids listed in parentheses indicates a list of substitutions at that position by any of the listed amino acids. For example, 6(L,I) means position 6 can be substituted with a leucine or isoleucine.

[0053] A prosequence or propetide sequence refers to an amino acid sequence between the signal peptide sequence and mature protease sequence that is necessary for the proper folding and secretion of the protease; they are sometimes referred to as intramolecular chaperones. Cleavage of the prosequence or propeptide sequence results in a mature active protease. Bacterial metalloproteases are often expressed as pro-enzymes.

[0054] The term signal sequence or signal peptide refers to a sequence of amino acid residues that may participate in the secretion or direct transport of the mature or precursor form of a protein. The signal sequence is typically located N-terminal to the precursor or mature protein sequence. The signal sequence may be endogenous or exogenous. A signal sequence is normally absent from the mature protein. A signal sequence is typically cleaved from the protein by a signal peptidase after the protein is transported.

[0055] The term mature form of a protein, polypeptide, or peptide refers to the functional form of the protein, polypeptide, or peptide without the signal peptide sequence and propeptide sequence.

[0056] The term precursor form of a protein or peptide refers to a mature form of the protein having a prosequence operably linked to the amino or carbonyl terminus of the protein. The precursor may also have a signal sequence operably linked to the amino terminus of the prosequence. The precursor may also have additional polypeptides that are involved in post-translational activity (e.g., polypeptides cleaved therefrom to leave the mature form of a protein or peptide).

[0057] The term wild-type in reference to an amino acid sequence or nucleic acid sequence indicates that the amino acid sequence or nucleic acid sequence is native or naturally occurring sequence. As used herein, the term naturally-occurring refers to anything (e.g., proteins, amino acids, or nucleic acid sequences) that are found in nature.

[0058] As used herein, the term non-naturally occurring refers to anything that is not found in nature (e.g., recombinant nucleic acids and protein sequences produced in the laboratory), as modification of the wild-type sequence.

[0059] As used herein with regard to amino acid residue positions, corresponding to or corresponds to or corresponds refers to an amino acid residue at the enumerated position in a protein or peptide, or an amino acid residue that is analogous, homologous, or equivalent to an enumerated residue in a protein or peptide. As used herein, corresponding region generally refers to an analogous position in a related proteins or a reference protein.

[0060] The terms derived from and obtained from refer to not only a protein produced or producible by a strain of the organism in question, but also a protein encoded by a DNA sequence isolated from such strain and produced in a host organism containing such DNA sequence. Additionally, the term refers to a protein which is encoded by a DNA sequence of synthetic and/or cDNA origin and which has the identifying characteristics of the protein in question. To exemplify, proteases derived from Bacillus refers to those enzymes having proteolytic activity which are naturally produced by Bacillus, as well as to metalloproteases like those produced by Bacillus sources but which through the use of genetic engineering techniques are produced by non-Bacillus organisms transformed with a nucleic acid encoding the serine proteases.

[0061] The term identical in the context of two nucleic acids or polypeptide sequences refers to the residues in the two sequences that are the same when aligned for maximum correspondence, as measured using one of the following sequence comparison or analysis algorithms.

[0062] As used herein, homologous genes refers to a pair of genes from different, but usually related species, which correspond to each other and which are identical or very similar to each other. The term encompasses genes that are separated by speciation (i.e., the development of new species) (e.g., orthologous genes), as well as genes that have been separated by genetic duplication (e.g., paralogous genes). As used herein, homologous proteins refers to proteins from different, but usually related species, which are very similar to each other.

[0063] As used herein, % identity or percent identity refers to sequence identity, at the gene or protein level. The output for these calculations are highly dependent on the algorithm used and the parameters selected such as length of compared sequences. Percent identity may be determined using standard techniques known in the art (See e.g., Smith and Waterman, Adv. Appl. Math. 2:482 [1981]; Needleman and Wunsch, J. Mol. Biol. 48:443 [1970]; Pearson and Lipman, Proc. Natl. Acad. Sci. USA 85:2444 [1988]; software programs such as GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package (Genetics Computer Group, Madison, Wis.); and Devereux et al., Nucl. Acid Res. 12:387-395 [1984]). One example of a useful algorithm is PILEUP. PILEUP creates a multiple sequence alignment from a group of related sequences using progressive, pair-wise alignments. It can also plot a tree showing the clustering relationships used to create the alignment. PILEUP uses a simplification of the progressive alignment method of Feng and Doolittle (See, Feng and Doolittle, J. Mol. Evol. 35:351-360 [1987]). The method is similar to that described by Higgins and Sharp (See, Higgins and Sharp, CABIOS 5:151-153 [1989]). Useful PILEUP parameters include a default gap weight of 3.00, a default gap length weight of 0.10, and weighted end gaps. Other useful algorithm is the BLAST algorithms described by Altschul et al., (See, Altschul et al., J. Mol. Biol. 215:403-410 [1990]; and Karlin and Altschul, Proc. Natl. Acad. Sci. USA 90:5873-5787 [1993]). The BLAST program uses several search parameters, most of which are set to the default values.

[0064] The NCBI BLAST algorithm finds the most relevant sequences in terms of biological similarity but is not recommended for query sequences of less than 20 residues (Altschul, S F et al. (1997) Nucleic Acids Res. 25:3389-3402 and Schaffer, A A et al. (2001) Nucleic Acids Res. 29:2994-3005). Example default BLAST parameters for a nucleic acid sequence searches are:

[0065] Neighboring words threshold: 11

[0066] E-value cutoff: 10

[0067] Scoring Matrix: NUC.3.1 (match=1, mismatch=3)

[0068] Gap Opening: 5

[0069] Gap Extension: 2

and the following parameters for amino acid sequence searches:

[0070] Word size: 3

[0071] E-value cutoff: 10

[0072] Scoring Matrix: BLOSUM62

[0073] Gap Opening: 11

[0074] Gap extension: 1

[0075] A percent (%) amino acid sequence identity value is determined by the number of matching identical residues divided by the total number of residues of the reference sequence including any gaps created by the program for optimal/maximum alignment. If a sequence is 90% identical to SEQ ID NO: A, SEQ ID NO: A is the reference sequence. BLAST algorithms refer the reference sequence as query sequence.

[0076] The CLUSTAL W algorithm is another example of a sequence alignment algorithm. See Thompson et al. (1994) Nucleic Acids Res. 22:4673-4680. Default parameters for the CLUSTAL W algorithm are: [0077] Gap opening penalty: 10.0 [0078] Gap extension penalty: 0.05 [0079] Protein weight matrix: BLOSUM series [0080] DNA weight matrix: IUB [0081] Delay divergent sequences %: 40 [0082] Gap separation distance: 8 [0083] DNA transitions weight: 0.50 [0084] List hydrophilic residues: GPSNDQEKR [0085] Use negative matrix: OFF [0086] Toggle Residue specific penalties: ON [0087] Toggle hydrophilic penalties: ON [0088] Toggle end gap separation penalty OFF.

[0089] In CLUSTAL algorithms, deletions occurring at either terminus are included. For example, a variant with five amino acid deletion at either terminus (or within the polypeptide) of a polypeptide of 500 amino acids would have a percent sequence identity of 99% (495/500 identical residues100) relative to the reference polypeptide. Such a variant would be encompassed by a variant having at least 99% sequence identity to the polypeptide.

[0090] A polypeptide of interest may be said to be substantially identical to a reference polypeptide if the polypeptide of interest comprises an amino acid sequence having at least about 60%, least about 65%, least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 91%, at least about 92%, at least about 93%, at least about 94%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or at least about 99.5% sequence identity to the amino acid sequence of the reference polypeptide. The percent identity between two such polypeptides can be determined manually by inspection of the two optimally aligned polypeptide sequences or by using software programs or algorithms (e.g., BLAST, ALIGN, CLUSTAL) using standard parameters. One indication that two polypeptides are substantially identical is that the first polypeptide is immunologically cross-reactive with the second polypeptide. Typically, polypeptides that differ by conservative amino acid substitutions are immunologically cross-reactive. Thus, a polypeptide is substantially identical to a second polypeptide, for example, where the two peptides differ only by a conservative amino acid substitution or one or more conservative amino acid substitutions.

[0091] A nucleic acid of interest may be said to be substantially identical to a reference nucleic acid if the nucleic acid of interest comprises a nucleotide sequence having least about 60%, least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 91%, at least about 92%, at least about 93%, at least about 94%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or at least about 99.5% sequence identity to the nucleotide sequence of the reference nucleic acid. The percent identity between two such nucleic acids can be determined manually by inspection of the two optimally aligned nucleic acid sequences or by using software programs or algorithms (e.g., BLAST, ALIGN, CLUSTAL) using standard parameters. One indication that two nucleic acid sequences are substantially identical is that the two nucleic acid molecules hybridize to each other under stringent conditions (e.g., within a range of medium to high stringency).

[0092] A nucleic acid or polynucleotide is isolated when it is at least partially or completely separated from other components, including but not limited to for example, other proteins, nucleic acids, cells, etc. Similarly, a polypeptide, protein or peptide is isolated when it is at least partially or completely separated from other components, including but not limited to for example, other proteins, nucleic acids, cells, etc. On a molar basis, an isolated species is more abundant than are other species in a composition. For example, an isolated species may comprise at least about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, or about 100% (on a molar basis) of all macromolecular species present. Preferably, the species of interest is purified to essential homogeneity (i.e., contaminant species cannot be detected in the composition by conventional detection methods). Purity and homogeneity can be determined using a number of techniques well known in the art, such as agarose or polyacrylamide gel electrophoresis of a nucleic acid or a protein sample, respectively, followed by visualization upon staining. If desired, a high-resolution technique, such as high performance liquid chromatography (HPLC) or a similar means can be utilized for purification of the material.

[0093] Hybridization refers to the process by which one strand of nucleic acid forms a duplex with, i.e., base pairs with, a complementary strand. A nucleic acid sequence is considered to be selectively hybridizable to a reference nucleic acid sequence if the two sequences specifically hybridize to one another under moderate to high stringency hybridization and wash conditions. Hybridization conditions are based on the melting temperature (Tm) of the nucleic acid binding complex or probe. For example, maximum stringency typically occurs at about Tm-5 C. (5 below the Tm of the probe); high stringency at about 5-10 C. below the Tm; intermediate stringency at about 10-20 C. below the Tm of the probe; and low stringency at about 20-25 C. below the Tm. Functionally, maximum stringency conditions can be used to identify sequences having strict identity or near-strict identity with the hybridization probe; while intermediate or low stringency hybridization can be used to identify or detect polynucleotide sequence homologs.

[0094] Moderate and high stringency hybridization conditions are well known in the art. Stringent hybridization conditions are exemplified by hybridization under the following conditions: 65 C. and 0.1SSC (where 1SSC=0.15 M NaCl, 0.015 M Na.sub.3 citrate, pH 7.0). Hybridized, duplex nucleic acids are characterized by a melting temperature (T.sub.m), where one half of the hybridized nucleic acids are unpaired with the complementary strand. Mismatched nucleic acids within the duplex lower the T.sub.m. Very stringent hybridization conditions involve 68 C. and 0.1SSC. A nucleic acid encoding a variant metalloprotease can have a T.sub.m reduced by 1 C.-3 C. or more compared to a duplex formed between the nucleic acid of SEQ ID NO: 4 and its identical complement.

[0095] Another example of high stringency conditions includes hybridization at about 42 C. in 50% formamide, 5SSC, 5Denhardt's solution, 0.5% SDS and 100 g/ml denatured carrier DNA followed by washing two times in 2SSC and 0.5% SDS at room temperature and two additional times in 0.1SSC and 0.5% SDS at 42 C. An example of moderate stringent conditions include an overnight incubation at 37 C. in a solution comprising 20% formamide, 5SSC (150 mM NaCl, 15 mM trisodium citrate), 50 mM sodium phosphate (pH 7.6), 5Denhardt's solution, 10% dextran sulfate and 20 mg/ml denatured sheared salmon sperm DNA, followed by washing the filters in 1SSC at about 37-50 C. Those of skill in the art know how to adjust the temperature, ionic strength, etc. to accommodate factors such as probe length and the like.

[0096] The term purified as applied to nucleic acids or polypeptides generally denotes a nucleic acid or polypeptide that is essentially free from other components as determined by analytical techniques well known in the art (e.g., a purified polypeptide or polynucleotide forms a discrete band in an electrophoretic gel, chromatographic eluate, and/or a media subjected to density gradient centrifugation). For example, a nucleic acid or polypeptide that gives rise to essentially one band in an electrophoretic gel is purified. A purified nucleic acid or polypeptide is at least about 50% pure, usually at least about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, about 99.5%, about 99.6%, about 99.7%, about 99.8% or more pure (e.g., percent by weight on a molar basis). In a related sense, the invention provides methods of enriching compositions for one or more molecules of the invention, such as one or more polypeptides or polynucleotides of the invention. A composition is enriched for a molecule when there is a substantial increase in the concentration of the molecule after application of a purification or enrichment technique. A substantially pure polypeptide or polynucleotide of the invention (e.g., substantially pure metalloprotease polypeptide or polynucleotide encoding a metalloprotease polypeptide of the invention, respectively) will typically comprise at least about 55%, about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98, about 99%, about 99.5% or more by weight (on a molar basis) of all macromolecular species in a particular composition.

[0097] The term enriched refers to a compound, polypeptide, cell, nucleic acid, amino acid, or other specified material or component that is present in a composition at a relative or absolute concentration that is higher than a starting composition.

[0098] In a related sense, the invention provides methods of enriching compositions for one or more molecules of the invention, such as one or more polypeptides of the invention (e.g., one or more metalloprotease polypeptides of the invention) or one or more nucleic acids of the invention (e.g., one or more nucleic acids encoding one or more metalloprotease polypeptides of the invention). A composition is enriched for a molecule when there is a substantial increase in the concentration of the molecule after application of a purification or enrichment technique. A substantially pure polypeptide or polynucleotide will typically comprise at least about 55%, about 60%, about 65%, about 70%, about 75%, about 80%, about 85%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98, about 99%, about 99.5% or more by weight (on a molar basis) of all macromolecular species in a particular composition.

[0099] As used herein, the term functional assay refers to an assay that provides an indication of a protein's activity. In some embodiments, the term refers to assay systems in which a protein is analyzed for its ability to function in its usual capacity. For example, in the case of a protease, a functional assay involves determining the effectiveness of the protease to hydrolyze a proteinaceous substrate.

[0100] The terms modified nucleic acid sequence and modified gene are used interchangeably herein to refer to a nucleic acid sequence that includes a deletion, insertion or interruption of naturally occurring (i.e., wild-type) nucleic acid sequence. In some embodiments, the expression product of the modified nucleic acid sequence is a truncated protein (e.g., if the modification is a deletion or interruption of the sequence). In some embodiments, the truncated protein retains biological activity. In alternative embodiments, the expression product of the modified nucleic acid sequence is an elongated protein (e.g., modifications comprising an insertion into the nucleic acid sequence). In some embodiments, a nucleotide insertion in the nucleic acid sequence leads to a truncated protein (e.g., when the insertion results in the formation of a stop codon). Thus, an insertion may result in either a truncated protein or an elongated protein as an expression product.

[0101] A mutant nucleic acid sequence typically refers to a nucleic acid sequence that has an alteration in at least one codon occurring in a host cell's wild-type sequence such that the expression product of the mutant nucleic acid sequence is a protein with an altered amino acid sequence relative to the wild-type protein. The expression product may have an altered functional capacity (e.g., enhanced enzymatic activity).

[0102] As used herein, the phrase alteration in substrate specificity refers to changes in the substrate specificity of an enzyme. In some embodiments, a change in substrate specificity is defined as a change in k.sub.cat and/or K.sub.m for a particular substrate, resulting from mutations of the enzyme or alteration of reaction conditions. The substrate specificity of an enzyme is determined by comparing the catalytic efficiencies it exhibits with different substrates. These determinations find particular use in assessing the efficiency of mutant enzymes, as it is generally desired to produce variant enzymes that exhibit greater ratios of k.sub.cat/K.sub.m for substrates of interest. However, it is not intended that the present invention be limited to any particular substrate composition or substrate specificity.

[0103] As used herein, surface property is used in reference to electrostatic charge, as well as properties such as the hydrophobicity and hydrophilicity exhibited by the surface of a protein.

[0104] As used herein, the term net charge is defined as the sum of all charges present in a molecule. Net charge changes are made to a parent protein molecule to provide a variant that has a net charge that differs from that of the parent molecule (i.e., the variant has a net charge that is not the same as that of the parent molecule). For example, substitution of a neutral amino acid with a negatively charged amino acid or a positively charged amino acid with a neutral amino acid results in net charge of 1 with respect to the parent molecule. Substitution of a positively charged amino acid with a negatively charged amino acid results in a net charge of 2 with respect to the parent. Substitution of a neutral amino acid with a positively charged amino acid or a negatively charged amino acid with a neutral amino acid results in net charge of +1 with respect to the parent. Substitution of a negatively charged amino acid with a positively charged amino acid results in a net charge of +2 with respect to the parent. The net charge of a parent protein can also be altered by deletion and/or insertion of charged amino acids. A net change applies to changes in charge of a variant versus a parent when measured at the same pH conditions.

[0105] The terms thermally stable and thermostable and thermostability refer to proteases that retain a specified amount of enzymatic activity after exposure to identified temperatures over a given period of time under conditions prevailing during the proteolytic, hydrolyzing, cleaning or other process of the invention, while being exposed to altered temperatures. Altered temperatures encompass increased or decreased temperatures. In some embodiments, the proteases retain at least about 50%, about 60%, about 70%, about 75%, about 80%, about 85%, about 90%, about 92%, about 95%, about 96%, about 97%, about 98%, or about 99% proteolytic activity after exposure to altered temperatures over a given time period, for example, at least about 60 minutes, about 120 minutes, about 180 minutes, about 240 minutes, about 300 minutes, etc.

[0106] The term enhanced stability in the context of an oxidation, chelator, thermal, chemical, autolytic and/or pH stable protease refers to a higher retained proteolytic activity over time as compared to other proteases (e.g., thermolysin proteases) and/or wild-type enzymes.

[0107] The term diminished stability in the context of an oxidation, chelator, thermal and/or pH stable protease refers to a lower retained proteolytic activity over time as compared to other proteases (e.g., thermolysin proteases) and/or wild-type enzymes.

[0108] The term cleaning activity refers to a cleaning performance achieved by a metalloprotease polypeptide or reference protease under conditions prevailing during the proteolytic, hydrolyzing, cleaning, or other process of the invention. In some embodiments, cleaning performance of a metalloprotease polypeptide or reference protease may be determined by using various assays for cleaning one or more various enzyme sensitive stains on an item or surface (e.g., a stain resulting from food, grass, blood, ink, milk, oil, and/or egg protein). Cleaning performance of a variant or reference protease can be determined by subjecting the stain on the item or surface to standard wash condition(s) and assessing the degree to which the stain is removed by using various chromatographic, spectrophotometric, or other quantitative methodologies. Exemplary cleaning assays and methods are known in the art and include, but are not limited to those described in WO 99/34011 and U.S. Pat. No. 6,605,458, both of which are herein incorporated by reference, as well as those cleaning assays and methods included in the Examples provided below.

[0109] The term cleaning effective amount of a metalloprotease polypeptide or reference protease refers to the amount of protease that achieves a desired level of enzymatic activity in a specific cleaning composition. Such effective amounts are readily ascertained by one of ordinary skill in the art and are based on many factors, such as the particular protease used, the cleaning application, the specific composition of the cleaning composition, and whether a liquid or dry (e.g., granular, tablet, bar) composition is required, etc.

[0110] The term enhanced performance in the context of cleaning activity refers to an increased or greater cleaning activity by an enzyme with respect to a parent or reference protein as measured on certain enzyme sensitive stains such as egg, milk, grass, ink, oil, and/or blood, as determined by usual evaluation after a standard wash cycle and/or multiple wash cycles.

[0111] The term diminished performance in the context of cleaning activity refers to a decreased or lesser cleaning activity by an enzyme on certain enzyme sensitive stains such as egg, milk, grass or blood, as determined by usual evaluation after a standard wash cycle and/or multiple wash cycles.

[0112] Cleaning compositions and cleaning formulations include any composition that is suited for cleaning, bleaching, disinfecting, and/or sterilizing any object, item, and/or surface. Such compositions and formulations include, but are not limited to for example, liquid and/or solid compositions, including cleaning or detergent compositions (e.g., liquid, tablet, gel, bar, granule, unit dose and/or solid laundry cleaning or detergent compositions and fine fabric detergent compositions; hard surface cleaning compositions and formulations, such as for glass, wood, ceramic and metal counter tops and windows; carpet cleaners; oven cleaners; fabric fresheners; fabric softeners; and textile, laundry booster cleaning or detergent compositions, laundry additive cleaning compositions, and laundry pre-spotter cleaning compositions; dishwashing compositions, including hand or manual dishwash compositions (e.g., hand or manual dishwashing detergents) and automatic dishwashing compositions (e.g., automatic dishwashing detergents).

[0113] As used herein, the term bleaching refers to the treatment of a material (e.g., fabric, laundry, pulp, etc.) or surface for a sufficient length of time and/or under appropriate pH and/or temperature conditions to effect a brightening (i.e., whitening) and/or cleaning of the material. Examples of chemicals suitable for bleaching include, but are not limited to, for example, ClO.sub.2, H.sub.2O.sub.2, peracids, NO.sub.2, etc.

[0114] As used herein, wash performance of a protease (e.g., a metalloprotease polypeptide of the invention) refers to the contribution of a metalloprotease polypeptide to washing that provides additional cleaning performance to the detergent as compared to the detergent without the addition of the metalloprotease polypeptide to the composition. Wash performance is compared under relevant washing conditions. In some test systems, other relevant factors, such as detergent composition, sud concentration, water hardness, washing mechanics, time, pH, and/or temperature, can be controlled in such a way that condition(s) typical for household application in a certain market segment (e.g., hand or manual dishwashing, automatic dishwashing, dishware cleaning, tableware cleaning, fabric cleaning, etc.) are imitated.

[0115] The term relevant washing conditions is used herein to indicate the conditions, particularly washing temperature, time, washing mechanics, sud concentration, type of detergent and water hardness, actually used in households in a hand dishwashing, automatic dishwashing, or laundry detergent market segment.

[0116] The term improved wash performance is used to indicate that a better end result is obtained in stain removal under relevant washing conditions, or that less metalloprotease polypeptide, on weight basis, is needed to obtain the same end result relative to the corresponding wild-type or starting parent protease.

[0117] As used herein, the term disinfecting refers to the removal of contaminants from the surfaces, as well as the inhibition or killing of microbes on the surfaces of items. It is not intended that the present invention be limited to any particular surface, item, or contaminant(s) or microbes to be removed.

[0118] The compact form of the cleaning compositions herein is best reflected by density and, in terms of composition, by the amount of inorganic filler salt. Inorganic filler salts are conventional ingredients of detergent compositions in powder form. In conventional detergent compositions, the filler salts are present in substantial amounts, typically about 17 to about 35% by weight of the total composition. In contrast, in compact compositions, the filler salt is present in amounts not exceeding about 15% of the total composition. In some embodiments, the filler salt is present in amounts that do not exceed about 10%, or more preferably, about 5%, by weight of the composition. In some embodiments, the inorganic filler salts are selected from the alkali and alkaline-earth-metal salts of sulfates and chlorides. In some embodiments, the filler salt is sodium sulfate.

[0119] As used herein in connection with a numerical value, the term about refers to a range of +/0.5 of the numerical value, unless the term is otherwise specifically defined in context. For instance, the phrase a pH value of about 6 refers to pH values of from 5.5 to 6.5, unless the pH value is specifically defined otherwise.

[0120] Oligonucleotide synthesis and purification steps are typically performed according to specifications. Techniques and procedures are generally performed according to conventional methods well known in the art and various general references that are provided throughout this document. Procedures therein are believed to be well known to those of ordinary skill in the art and are provided for the convenience of the reader.

Variant Metalloprotease Polypeptides of the Present Invention

[0121] In some embodiments, the present invention provides novel variant metalloprotease enzyme polypeptides having a modification in a calcium binding region. In some embodiments, the variant is a variant of a parent or reference sequence. The parent or reference sequence can be, for example, any M4 metalloprotease, or a Bacillus derived metalloprotease, such as Bacillus thermoproteolyticus, Bacillus cereus, or Bacillus subtilis (for example, the sequences of SEQ ID NOs: 13-15), or a Paenibacillus derived metalloprotease, such as the sequences of SEQ ID NOs: 1-12.

[0122] A residue (amino acid) of a metalloprotease is equivalent to a residue of Thermolysin metalloprotease if it is either homologous (i.e., corresponding in position in either primary or tertiary structure) or analogous to a specific residue or portion of that residue in Thermolysin metalloprotease from Bacillus thermoproteolyticus (i.e., having the same or similar functional capacity to react or interact chemically). In order to establish homology to primary structure, the amino acid sequence of a metalloprotease is directly compared to the Thermolysin primary sequence and particularly to a set of residues known to be invariant in diverse M4 metalloproteinases as shown in FIG. 6.1).

[0123] After aligning the conserved residues, allowing for necessary insertions and deletions in order to maintain alignment (i.e. avoiding the elimination of conserved residues through arbitrary deletions and insertions) the residues equivalent to particular amino acids in the primary sequence of thermolysin are defined. Suitable methods to produce such modifications include those disclosed herein and an example is shown in Example 6. These conserved residues thus may be used to define the corresponding equivalent amino acid residues of Thermolysin and in other M4 metalloproteinases such as the metalloproteinases from Paenibacillus organisms such as PehPro1. These two particular sequences (Thermolysin (1KEI) and PehPro1) are aligned in FIG. 6.1 to produce the maximum homology of conserved residues. As can be seen, there are a number of insertions and deletions in the PehPro1 sequence as compared to Thermolysin.

[0124] The position of an amino acid residue in a given amino acid sequence is typically numbered herein using the numbering of the position of the corresponding amino acid residue of the Bacillus thermoproteolyticus metalloprotease Thermolysin amino acid sequence shown in SEQ ID NO: 13. The Bacillus thermoproteolyticus metalloprotease Thermolysin amino acid sequence of SEQ ID NO: 13 thus serves as a reference parent sequence. A given amino acid sequence, such as a metalloprotease enzyme amino acid sequence and variants thereof described herein, can be aligned with the Thermolysin sequence (SEQ ID NO: 13) using an alignment algorithm as described herein on the primary and/or tertiary structures, and an amino acid residue in the given amino acid sequence that aligns (preferably optimally aligns) with an amino acid residue in the Thermolysin sequence can be conveniently numbered by reference to the corresponding amino acid residue in the metalloprotease Thermolysin sequence.

[0125] The equivalent amino acid of Asp57 in Thermolysin, in PehPro is the particular Serine shown at that aligned position. In FIG. 6.1, the equivalent amino acid at position 57 in PpoPro1 is again Aspartic acid. Thus, these particular residues in PehPro1, and thermolysin may be substituted by a different amino acid to produce a mutant metalloprotease, since they are equivalent in primary structure to Asp 57 in thermolysin. Equivalent amino acids of course are not limited to those for Asp57 but extend to any residue which is equivalent to a residue in Thermolysin, and this is intended as an example of equivalent residues.

[0126] Equivalent residues homologous at the level of tertiary structure for a metalloprotease whose tertiary structure has been determined by x-ray crystallography, are defined as those for which the atomic coordinates of 2 or more of the main chain atoms of a particular amino acid residue of the M4 metalloproteinase and Thermolysin (N on N. CA on CA, C on C, and 0 on 0) are within 0.13 nm and preferably 0.1 nm after superposition. Superposition can be accomplished by superimposing the common secondary structure. This can be accomplished using any one of several known algorithms in the art, such as The PyMOL Molecular Graphics System, Version 1.5.0.4 Schrodinger, LLC or Coot [Emsley et al. (2010) Acta Crystallogr D Biol Crystallogr. 66(Pt4): 486]. Superposition is achieved after the best model has been oriented and positioned to give the maximum overlap of atomic coordinates of non-hydrogen protein atoms of the metalloprotease in question to the Thermolysin metalloprotease from Bacillus thermoproteolyticus. The best model is the crystallographic model determined at the highest resolution, and if more than one, the one giving the lowest R factor.

[0127] Equivalent residues which are functionally analogous to a specific residue of Thermolysin are defined as those amino acids of the metalloproteases which may adopt a conformation such that they either alter, modify or contribute to protein structure, substrate binding or catalysis in a manner defined and attributed to a specific residue of thermolysin as described herein. Further, they are those residues of the metalloproteinase (for which a tertiary structure has been obtained by x-ray crystallography), which occupy an analogous position to the extent that although the main chain atoms of the given residue may not satisfy the criteria of equivalence on the basis of occupying a homologous position, the atomic coordinates of at least two of the side chain atoms of the residue lie with 0.13 nm of the corresponding side chain atoms of Thermolysin. The three dimensional structures would be aligned as outlined above.

Calcium Binding Region

[0128] The structure of the M4 class metalloprotease thermolysin has been found to have four calcium-binding regions. The structural information from Thermolysin and other metalloproteases can be used to determine modifications that can be made to M4 class metalloproteases in order to remove calcium binding.

[0129] Based largely on analysis of the three-dimensional structure of thermolysin, it has been discovered that M4 class metalloproteases can have as many as four calcium binding sites. In thermolysin, there is a double cation binding site, herein referred to as Ca1-2, which has a calcium binding region including residues 136, 138 and 177-190 using the numbering of thermolysin from Bacillus thermoproteolyticus found in SEQ ID NO: 13. There is also a calcium binding site, herein referred to as Ca3, which has a calcium binding region including residues 55-66, and a fourth binding site referred to as Ca4, which has a calcium binding region including residues 193-200.

[0130] In some embodiments, it is desirable to be able to decrease the Ca.sup.2+ dependency of a metalloprotease. As such, in some embodiments, the invention is a variant of a parent metalloprotease, such as a M4 class metalloprotease or a variant of any one of SEQ ID NOs: 1-15, which exhibits protease activity and which has a decreased Ca.sup.2+ dependency as compared to the parent metalloprotease. The decreased Ca.sup.2+ dependency has the functional result that the variant exhibits proteolytic activity in the presence of a lower concentration of calcium ion in the extraneous medium than is necessary for the parent enzyme and, for example, therefore is less sensitive than the parent to calcium ion-depleting conditions such as those obtained in media containing calcium-complexing agents (such as certain detergent builders). In some embodiments, the variant retains at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, 99%, 100% or even has greater activity compared to the parent metalloprotease. This can be measured in a proteolytic assay, such as those described in Example 1.

Calcium Binding

[0131] A stabilization strategy based around decreased calcium binding can improve enzyme stability in environments with decreased availability of free calcium ions. One of the major industrial uses of subtilisins is in environments containing high concentrations of metal chelators. Additionally, because these calcium binding regions are found in various M4 metalloproteases, it is expected that equivalent mutations for other M4 metalloproteases will likewise eliminate calcium binding and provide for enzymatically active variants. These calcium binding regions can also be found in various metalloproteases that are not categorized as M4 metalloproteases, but share the same properties as an M4 metalloprotease, including the calcium binding regions.

[0132] In some embodiments, the invention is a metalloprotease polypeptide comprising a calcium binding region. In some embodiments, the above polypeptide comprises a modification in at least one amino acid residue in one of the calcium binding regions, Ca1-2, Ca3 and Ca4, (including residues 55-66, 136, 138, 177-190, and 193-200) of the polypeptide, wherein the amino acid positions of the polypeptide are numbered by correspondence with the amino acid sequence of Bacillus thermoproteolyticus metalloprotease set forth in SEQ ID NO: 13.

[0133] In any of the above embodiments and in new embodiments, the variant comprises a modification in at least one amino acid residue in a calcium binding region Ca1-2 of residues 177-190 of a parent M4 metalloprotease. In any of the above embodiments and in new embodiments, the polypeptide at position 184 is a lysine, threonine, alanine, glutamic acid or aspartic acid. In any of the above embodiments and in new embodiments, the polypeptide at position 185 is a residue other than aspartic acid. In some embodiments, the polypeptide at position 185 is a non-negatively charged residue; in other embodiments, the polypeptide at position 185 is a neutrally charged residue; and in yet other embodiments, the polypeptide at position 185 is an asparagine or serine. In any of the above embodiments and in new embodiments, the polypeptide at position 187 is a non-negatively charged residue. In some embodiments, the polypeptide at position 187 is a neutrally charged residue; and in other embodiments, the polypeptide at position 187 is a leucine or methionine; and in yet other embodiments, the polypeptide at position 187 is aspartic acid. In any of the above embodiments and in new embodiments, the polypeptide at position 188 is a leucine, valine, or methionine. In any of the above embodiments and in new embodiments, the polypeptide at position 190 is a residue other than glutamic acid. In some embodiments, the polypeptide at position 190 is aspartic acid. In sequence alignment of Ca1-2 regions, there are conserved residues glycine at position 173 and tryptophan at position 186 (see FIG. 12). In any of the above embodiments and in new embodiments, the polypeptide comprises seven amino acid residues between the glycine residue at position 173 and tryptophan at position 186. In any of the above embodiments and in new embodiments, the polypeptide comprises a deletion of five amino acid residues between the glycine residue at position 173 and tryptophan at position 186. In structural alignment of Ca1-2 regions, there is a known loop structure between residues 176 and 186 (inclusive of amino acids 177 and 185 in the loop). In any of the above embodiments and in new embodiments, the polypeptide comprises a seven amino acid loop sequence between positions 177 to 185 which is replaced by a two amino acid sequence. Without being bound by theory, a polypeptide of the instant invention has improved stability by replacement of the loop structure with a shorter amino acid sequence that can span the region between positions 177 to 185, and in particular, a two amino acid sequence is preferred to span the region between positions 177 to 185. In any of the above embodiments, the two amino acid sequence contains at least one positively charged amino acid, and in some embodiments, the positively charged amino acid is lysine. In any of the above embodiments and in new embodiments, the polypeptide comprises a deletion at amino acid residue positions 179-183. In any of the above embodiments and in new embodiments, the polypeptide at position 177 is a neutrally charged residue or aspartic acid; and in some embodiments, the neutrally charged residue is glutamine. In any of the above embodiments and in new embodiments, the polypeptide at position 178 is a glycine, serine, arginine, alanine, asparagines, and threonine. In any of the above embodiments and in new embodiments, the polypeptide at position 136 is aspartic acid or serine.

[0134] In any of the above embodiments and in new embodiments, the invention is a metalloprotease polypeptide having a modification in at least one amino acid residue in a calcium binding region Ca3 of residues 55-66, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of Bacillus proteolyticus metalloprotease set forth in SEQ ID NO: 13. In any of the above embodiments and in new embodiments, the polypeptide at position 55 is a leucine, serine, valine, and methionine. In any of the above embodiments and in new embodiments, the polypeptide at position 56 is a serine, arginine and threonine. In any of the above embodiments and in new embodiments, the polypeptide at position 57 is a serine. In any of the above embodiments and in new embodiments, the polypeptide at position 58 is a serine and threonine. In any of the above embodiments and in new embodiments, the polypeptide at position 59 is a serine, threonine, and asparagine. In any of the above embodiments and in new embodiments, the polypeptide has a serine at position 57, serine at position 58 and serine or asparagines at position 59. In any of the above embodiments and in new embodiments, the polypeptide at position 60 is a serine. In any of the above embodiments and in new embodiments, the polypeptide at position 61 is an isoleucine, valine, and threonine. In any of the above embodiments and in new embodiments, the polypeptide at position 62 is a tryptophan and phenylalanine. In any of the above embodiments and in new embodiments, the polypeptide at position 63 is a asparagine, glutamic acid, and threonine. In sequence alignment of the Ca3 region, there are conserved residues phenylalanine/tryptophan at position 62 and aspartic acid at position 67 (see FIG. 12). In any of the above embodiments and in new embodiments, the polypeptide comprises four amino acid residues between the phenylalanine/tryptophan residue at position 62 and aspartic acid at position 67. In any of the above embodiments and in new embodiments, the polypeptide comprises a deletion of three amino acid residues between the phenylalanine/tryptophan residue at position 62 and aspartic acid at position 67. In structural alignment of the Ca3 region, there is a known loop structure between residues 62 and 67 (inclusive of amino acids 62 and 67 in the loop). In any of the above embodiments and in new embodiments, the polypeptide comprises a four amino acid loop sequence between positions 62 to 67 which is replaced by a one amino acid sequence. Without being bound by theory, a polypeptide of the instant invention has improved stability by replacement of the loop structure with a shorter amino acid sequence that can span the region between positions 62 to 67, and in particular, a one amino acid sequence is preferred to span the region between positions 62 to 67. In any of the above embodiments, the one amino acid sequence is an asparagines, threonine, or glutamic acid. In any of the above embodiments and in new embodiments, the polypeptide comprises a deletion at amino acid residue positions 64-66.

[0135] In any of the above embodiments and in new embodiments, the invention is a metalloprotease polypeptide having a modification in at least one amino acid residue in a calcium binding region Ca4 of residues 193-200, wherein the amino acid positions of the variant are numbered by correspondence with the amino acid sequence of Bacillus proteolyticus metalloprotease set forth in SEQ ID NO: 13. In any of the above embodiments and in new embodiments, the polypeptide at position 193 is a threonine. In any of the above embodiments and in new embodiments, the polypeptide at position 194 is a isoleucine. In any of the above embodiments and in new embodiments, the polypeptide at position 195 is a serine. In any of the above embodiments and in new embodiments, the polypeptide comprises a deletion at amino acid residue positions 196-198. In any of the above embodiments and in new embodiments, the polypeptide at position 199 is a glutamine. In any of the above embodiments and in new embodiments, the polypeptide at position 200 is a proline.

[0136] In some embodiments of the invention, the calcium binding region Ca1-2 has been modified to bind fewer than two calcium ions. In some embodiments of the invention, the calcium binding region Ca3 has been modified to bind fewer than one calcium ion. In some embodiments of the invention, the calcium binding region Ca4 has been modified to bind fewer than one calcium ion.

[0137] In some embodiments, the invention is a variant metalloprotease of a parent metalloprotease polypeptide. In some embodiments, the variant comprises a modification in a calcium binding region of the parent polypeptide. In some embodiments, the variant comprises a modification to any of the amino acids listed above. In some embodiments, the parent polypeptide is an M4 metalloprotease. In some embodiments, the metalloprotease polypeptide of the present invention has at least 60, 65, 70, 75, 80, 85, 90, 95, 96, 97, 98, 99, or 100% sequence identity to the parent polypeptide. In some embodiments, the metalloprotease polypeptide of the present invention has at least 60, 65, 70, 75, 80, 85, 90, 95, 96, 97, 98, 99, or 100% sequence identity to any of the sequences found in SEQ ID NOs: 1-15. In some embodiments, the metalloprotease polypeptide of the present invention has at least 60, 65, 70, 75, 80, 85, 90, 95, 96, 97, 98, 99, or 100% sequence identity to SEQ ID NO:13.

[0138] In some embodiments, the invention is a variant metalloprotease having immunological cross-reactivity with any of the variant metalloproteases described above. Immunological cross-reactivity can be assayed using an antibody raised against or reactive with at least one epitope of any of the variant metalloproteases listed above. The antibody, which can either be monoclonal or polyclonal, can be produced by methods known in the art. Immunological cross-reactivity can be measured using assays known in the art, such as Western blotting, radial immunodiffusion assay, or enzyme-linked immunosorbant assay (ELISA).

Metalloprotease Polypeptides of the Present Invention

[0139] The present invention provides novel metalloprotease enzyme polypeptides, which may be collectively referred to as enzymes of the invention or polypeptides of the invention. Polypeptides of the invention include isolated, recombinant, substantially pure, or non-naturally occurring polypeptides. In some embodiments, the invention includes variants, as described above, of M4 class metalloproteases. In some embodiments, polypeptides of the invention are useful in cleaning applications and can be incorporated into cleaning compositions that are useful in methods of cleaning an item or a surface in need of cleaning.

[0140] In some embodiments, the enzyme of the present invention has 50, 60, 65, 70, 75, 80, 85, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% identity to a M4 class metalloprotease. In some embodiments, the enzyme of the present invention has 50, 60, 65, 70, 75, 80, 85, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% identity to SEQ ID NO: 13. In various embodiments, the enzyme of the present invention has 50, 60, 65, 70, 75, 80, 85, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% identity to a metalloprotease enzyme from any of SEQ ID NO:1-15.

[0141] In some embodiments, the invention includes an isolated, recombinant, substantially pure, or non-naturally occurring enzyme having protease activity, which polypeptide comprises a polypeptide sequence having at least about 60%, 65%, 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to a parent enzyme as provided herein.

[0142] In some embodiments, the polypeptide of the present invention, is a polypeptide having a specified degree of amino acid sequence homology to the exemplified polypeptides, e.g., at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or even at least 99% sequence homology to the amino acid sequence of any of SEQ ID NO: 1-15. Homology can be determined by amino acid sequence alignment, e.g., using a program such as BLAST, ALIGN, or CLUSTAL, as described herein.

[0143] Also provided is a polypeptide enzyme of the present invention, having protease activity, said enzyme comprising an amino acid sequence which differs from the amino acid sequence of any of SEQ ID NO: 1-15 by no more than 50, no more than 40, no more than 30, no more than 35, no more than 25, no more than 20, no more than 19, no more than 18, no more than 17, no more than 16, no more than 15, no more than 14, no more than 13, no more than 12, no more than 11, no more than 10, no more than 9, no more than 8, no more than 7, no more than 6, no more than 5, no more than 4, no more than 3, no more than 2, or no more than 1 amino acid residue(s), when aligned using any of the previously described alignment methods.

[0144] As noted above, the variant enzyme polypeptides of the invention have enzymatic activities (e.g., protease activities) and thus are useful in cleaning applications, including but not limited to, methods for cleaning dishware items, tableware items, fabrics, and items having hard surfaces (e.g., the hard surface of a table, table top, wall, furniture item, floor, ceiling, etc.). Exemplary cleaning compositions comprising one or more variant metalloprotease enzyme polypeptides of the invention are described infra. The enzymatic activity (e.g., protease enzyme activity) of an enzyme polypeptide of the invention can be determined readily using procedures well known to those of ordinary skill in the art. The Examples presented infra describe methods for evaluating the enzymatic activity and cleaning performance. The performance of polypeptide enzymes of the invention in removing stains (e.g., a protein stain such as blood/milk/ink or egg yolk), cleaning hard surfaces, or cleaning laundry, dishware or tableware item(s), or cleaning contact lenses can be readily determined using procedures well known in the art and/or by using procedures set forth in the Examples.

[0145] The metalloprotease polypeptides of the present invention can have protease activity over a broad range of pH conditions. In some embodiments, the metalloprotease polypeptides have protease activity on azo-casein as a substrate, as demonstrated in Example 3. In some embodiments, the metalloprotease polypeptides have protease activity at a pH of from about 3.0 to about 12.0. In some embodiments, the metalloprotease polypeptides have protease activity at a pH of from about 4.0 to about 11.0.

[0146] In some embodiments, the metalloprotease polypeptides of the present invention have protease activity at a temperature range of from about 10 C. to about 100 C. In some embodiments, the metalloprotease polypeptides of the present invention have protease activity at a temperature range of from about 20 C. to about 90 C.

[0147] In some embodiments, the metalloprotease polypeptides of the present invention demonstrate cleaning performance in a cleaning composition. Cleaning compositions often include ingredients harmful to the stability and performance of enzymes, making cleaning compositions a harsh environment for enzymes, e.g. metalloproteases, to retain function. Thus, it is not trivial for an enzyme to be put in a cleaning composition and expect enzymatic function (e.g. metalloprotease activity, such as demonstrated by cleaning performance). In some embodiments, the metalloprotease polypeptides of the present invention demonstrate cleaning performance in automatic dishwashing (ADW) detergent compositions. In some embodiments, the cleaning performance in automatic dishwashing (ADW) detergent compositions includes cleaning of egg yolk stains. In some embodiments, the metalloprotease polypeptides of the present invention demonstrate cleaning performance in laundry detergent compositions. In some embodiments, the cleaning performance in laundry detergent compositions includes cleaning of blood/milk/ink stains. In each of the cleaning compositions, the metalloprotease polypeptides of the present invention demonstrate cleaning performance with or without a bleach component.

[0148] A polypeptide of the invention can be subject to various changes, such as one or more amino acid insertions, deletions, and/or substitutions, either conservative or non-conservative, including where such changes do not substantially alter the enzymatic activity of the polypeptide. Similarly, a nucleic acid of the invention can also be subject to various changes, such as one or more substitutions of one or more nucleotides in one or more codons such that a particular codon encodes the same or a different amino acid, resulting in either a silent variation (e.g., when the encoded amino acid is not altered by the nucleotide mutation) or non-silent variation, one or more deletions of one or more nucleic acids (or codons) in the sequence, one or more additions or insertions of one or more nucleic acids (or codons) in the sequence, and/or cleavage of or one or more truncations of one or more nucleic acids (or codons) in the sequence. Many such changes in the nucleic acid sequence may not substantially alter the enzymatic activity of the resulting encoded polypeptide enzyme compared to the polypeptide enzyme encoded by the original nucleic acid sequence. A nucleic acid sequence of the invention can also be modified to include one or more codons that provide for optimum expression in an expression system (e.g., bacterial expression system), while, if desired, said one or more codons still encode the same amino acid(s).

[0149] In some embodiments, the present invention provides a genus of enzyme polypeptides having the desired enzymatic activity (e.g., protease enzyme activity or cleaning performance activity) which comprise sequences having the amino acid substitutions described herein and also which comprise one or more additional amino acid substitutions, such as conservative and non-conservative substitutions, wherein the polypeptide exhibits, maintains, or approximately maintains the desired enzymatic activity (e.g., proteolytic activity, as reflected in the cleaning activity or performance of the polypeptide enzyme of SEQ ID NO: 13). Amino acid substitutions in accordance with the invention may include, but are not limited to, one or more non-conservative substitutions and/or one or more conservative amino acid substitutions. A conservative amino acid residue substitution typically involves exchanging a member within one functional class of amino acid residues for a residue that belongs to the same functional class (conservative amino acid residues are considered functionally homologous or conserved in calculating percent functional homology). A conservative amino acid substitution typically involves the substitution of an amino acid in an amino acid sequence with a functionally similar amino acid. For example, alanine, glycine, serine, and threonine are functionally similar and thus may serve as conservative amino acid substitutions for one another. Aspartic acid and glutamic acid may serve as conservative substitutions for one another. Asparagine and glutamine may serve as conservative substitutions for one another. Arginine, lysine, and histidine may serve as conservative substitutions for one another. Isoleucine, leucine, methionine, and valine may serve as conservative substitutions for one another. Phenylalanine, tyrosine, and tryptophan may serve as conservative substitutions for one another.

[0150] Other conservative amino acid substitution groups can be envisioned. For example, amino acids can be grouped by similar function or chemical structure or composition (e.g., acidic, basic, aliphatic, aromatic, sulfur-containing). For instance, an aliphatic grouping may comprise: Glycine (G), Alanine (A), Valine (V), Leucine (L), Isoleucine (I). Other groups containing amino acids that are considered conservative substitutions for one another include: aromatic: Phenylalanine (F), Tyrosine (Y), Tryptophan (W); sulfur-containing: Methionine (M), Cysteine (C); Basic: Arginine (R), Lysine (K), Histidine (H); Acidic: Aspartic acid (D), Glutamic acid (E); non-polar uncharged residues, Cysteine (C), Methionine (M), and Proline (P); hydrophilic uncharged residues: Serine (S), Threonine (T), Asparagine (N), and Glutamine (Q). Additional groupings of amino acids are well-known to those of skill in the art and described in various standard textbooks. Listing of a polypeptide sequence herein, in conjunction with the above substitution groups, provides an express listing of all conservatively substituted polypeptide sequences.

[0151] More conservative substitutions exist within the amino acid residue classes described above, which also or alternatively can be suitable. Conservation groups for substitutions that are more conservative include: valine-leucine-isoleucine, phenylalanine-tyrosine, lysine-arginine, alanine-valine, and asparagine-glutamine.

[0152] Conservatively substituted variations of a polypeptide sequence of the invention (e.g., variant metalloproteases of the invention) include substitutions of a small percentage, sometimes less than 25%, 20%, 15%, 14%, 13%, 12%, 11%, 10%, 9%, 8%, 7%, or 6% of the amino acids of the polypeptide sequence, or less than 5%, 4%, 3%, 2%, or 1%, or less than 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1 amino acid substitution of the amino acids of the polypeptide sequence, with a conservatively selected amino acid of the same conservative substitution group.

[0153] As described elsewhere herein in greater detail and in the Examples provided herein, polypeptides of the invention may have cleaning abilities that may be compared to known proteases, including known metalloproteases.

Nucleic Acids of the Invention

[0154] The invention provides isolated, non-naturally occurring, or recombinant nucleic acids which may be collectively referred to as nucleic acids of the invention or polynucleotides of the invention, which encode polypeptides of the invention. Nucleic acids of the invention, including all described below, are useful in recombinant production (e.g., expression) of polypeptides of the invention, typically through expression of a plasmid expression vector comprising a sequence encoding the polypeptide of interest or fragment thereof. As discussed above, polypeptides include metalloprotease polypeptides having enzymatic activity (e.g., proteolytic activity) which are useful in cleaning applications and cleaning compositions for cleaning an item or a surface (e.g., surface of an item) in need of cleaning.

[0155] In some embodiments, the invention provides an isolated, recombinant, substantially pure, or non-naturally occurring nucleic acid comprising a nucleotide sequence encoding any polypeptide (including any fusion protein, etc.) of the invention described above in the section entitled Polypeptides of the Invention and elsewhere herein. The invention also provides an isolated, recombinant, substantially pure, or non-naturally-occurring nucleic acid comprising a nucleotide sequence encoding a combination of two or more of any polypeptides of the invention described above and elsewhere herein.

[0156] The present invention provides nucleic acids encoding a metalloprotease polypeptide of the present invention, wherein the metalloprotease polypeptide is a mature form having proteolytic activity, wherein the amino acid positions of the thermolysin variant are numbered by correspondence with the amino acid sequence of Bacillus thermoproteolyticus metalloprotease polypeptide set forth as SEQ ID NO: 13.

[0157] Nucleic acids of the invention can be generated by using any suitable synthesis, manipulation, and/or isolation techniques, or combinations thereof. For example, a polynucleotide of the invention may be produced using standard nucleic acid synthesis techniques, such as solid-phase synthesis techniques that are well-known to those skilled in the art. In such techniques, fragments of up to 50 or more nucleotide bases are typically synthesized, then joined (e.g., by enzymatic or chemical ligation methods) to form essentially any desired continuous nucleic acid sequence. The synthesis of the nucleic acids of the invention can be also facilitated by any suitable method known in the art, including but not limited to chemical synthesis using the classical phosphoramidite method (See e.g., Beaucage et al. Tetrahedron Letters 22:1859-69 [1981]); or the method described by Matthes et al. (See, Matthes et al., EMBO J. 3:801-805 [1984], as is typically practiced in automated synthetic methods. Nucleic acids of the invention also can be produced by using an automatic DNA synthesizer. Customized nucleic acids can be ordered from a variety of commercial sources (e.g., The Midland Certified Reagent Company, the Great American Gene Company, Operon Technologies Inc., and DNA2.0). Other techniques for synthesizing nucleic acids and related principles are known in the art (See e.g., Itakura et al., Ann. Rev. Biochem. 53:323 [1984]; and Itakura et al., Science 198:1056 [1984]).

[0158] As indicated above, recombinant DNA techniques useful in modification of nucleic acids are well known in the art. For example, techniques such as restriction endonuclease digestion, ligation, reverse transcription and cDNA production, and polymerase chain reaction (e.g., PCR) are known and readily employed by those of skill in the art. Nucleotides of the invention may also be obtained by screening cDNA libraries using one or more oligonucleotide probes that can hybridize to or PCR-amplify polynucleotides which encode a metalloprotease polypeptide polypeptide(s) of the invention. Procedures for screening and isolating cDNA clones and PCR amplification procedures are well known to those of skill in the art and described in standard references known to those skilled in the art. Some nucleic acids of the invention can be obtained by altering a naturally occurring polynucleotide backbone (e.g., that encodes an enzyme or parent protease) by, for example, a known mutagenesis procedure (e.g., site-directed mutagenesis, site saturation mutagenesis, and in vitro recombination).

Methods for Making Modified Metalloprotease Polypeptides of the Invention

[0159] A variety of methods are known in the art that are suitable for generating modified polynucleotides of the invention that encode metalloprotease polypeptides of the invention, including, but not limited to, for example, site-saturation mutagenesis, scanning mutagenesis, insertional mutagenesis, deletion mutagenesis, random mutagenesis, site-directed mutagenesis, and directed-evolution, as well as various other recombinatorial approaches. Methods for making modified polynucleotides and proteins (e.g., metalloprotease polypeptides) include DNA shuffling methodologies, methods based on non-homologous recombination of genes, such as ITCHY (See, Ostermeier et al., 7:2139-44 [1999]), SCRACHY (See, Lutz et al. 98:11248-53 [2001]), SHIPREC (See, Sieber et al., 19:456-60 [2001]), and NRR (See, Bittker et al., 20:1024-9 [2001]; Bittker et al., 101:7011-6 [2004]), and methods that rely on the use of oligonucleotides to insert random and targeted mutations, deletions and/or insertions (See, Ness et al., 20:1251-5 [2002]; Coco et al., 20:1246-50 [2002]; Zha et al., 4:34-9 [2003]; Glaser et al., 149:3903-13 [1992]).

Vectors, Cells, and Methods for Producing Metalloprotease Polypeptides of the Invention

[0160] The present invention provides vectors comprising at least one metalloprotease polynucleotide of the invention described herein (e.g., a polynucleotide encoding a metalloprotease polypeptide of the invention described herein), expression vectors or expression cassettes comprising at least one nucleic acid or polynucleotide of the invention, isolated, substantially pure, or recombinant DNA constructs comprising at least one nucleic acid or polynucleotide of the invention, isolated or recombinant cells comprising at least one polynucleotide of the invention, and compositions comprising one or more such vectors, nucleic acids, expression vectors, expression cassettes, DNA constructs, cells, cell cultures, or any combination or mixtures thereof.

[0161] In some embodiments, the invention provides recombinant cells comprising at least one vector (e.g., expression vector or DNA construct) of the invention which comprises at least one nucleic acid or polynucleotide of the invention. Some such recombinant cells are transformed or transfected with such at least one vector. Such cells are typically referred to as host cells. Some such cells comprise bacterial cells, including, but are not limited to Bacillus sp. cells, such as B. subtilis cells. The invention also provides recombinant cells (e.g., recombinant host cells) comprising at least one metalloprotease polypeptide of the invention.

[0162] In some embodiments, the invention provides a vector comprising a nucleic acid or polynucleotide of the invention. In some embodiments, the vector is an expression vector or expression cassette in which a polynucleotide sequence of the invention which encodes a metalloprotease polypeptide of the invention is operably linked to one or additional nucleic acid segments required for efficient gene expression (e.g., a promoter operably linked to the polynucleotide of the invention which encodes a metalloprotease polypeptide of the invention). A vector may include a transcription terminator and/or a selection gene, such as an antibiotic resistance gene, that enables continuous cultural maintenance of plasmid-infected host cells by growth in antimicrobial-containing media.

[0163] An expression vector may be derived from plasmid or viral DNA, or in alternative embodiments, contains elements of both. Exemplary vectors include, but are not limited to pC194, pJH101, pE194, pHP13 (See, Harwood and Cutting [eds.], Chapter 3, Molecular Biological Methods for Bacillus, John Wiley & Sons [1990]; suitable replicating plasmids for B. subtilis include those listed on p. 92) See also, Perego, Integrational Vectors for Genetic Manipulations in Bacillus subtilis, in Sonenshein et al., [eds.] Bacillus subtilis and Other Gram-Positive Bacteria: Biochemistry, Physiology and Molecular Genetics, American Society for Microbiology, Washington, D.C. [1993], pp. 615-624), and p2JM103BBI.

[0164] For expression and production of a protein of interest (e.g., metalloprotease polypeptide) in a cell, at least one expression vector comprising at least one copy of a polynucleotide encoding the metalloprotease polypeptide, and in some instances comprising multiple copies, is transformed into the cell under conditions suitable for expression of the metalloprotease. In some embodiments of the present invention, a polynucleotide sequence encoding the metalloprotease polypeptide (as well as other sequences included in the vector) is integrated into the genome of the host cell, while in other embodiments, a plasmid vector comprising a polynucleotide sequence encoding the metalloprotease polypeptide remains as autonomous extra-chromosomal element within the cell. The invention provides both extrachromosomal nucleic acid elements as well as incoming nucleotide sequences that are integrated into the host cell genome. The vectors described herein are useful for production of the metalloprotease polypeptides of the invention. In some embodiments, a polynucleotide construct encoding the metalloprotease polypeptide is present on an integrating vector that enables the integration and optionally the amplification of the polynucleotide encoding the metalloprotease polypeptide into the host chromosome. Examples of sites for integration are well known to those skilled in the art. In some embodiments, transcription of a polynucleotide encoding a metalloprotease polypeptide of the invention is effectuated by a promoter that is the wild-type promoter for the selected precursor protease. In some other embodiments, the promoter is heterologous to the precursor protease, but is functional in the host cell. Specifically, examples of suitable promoters for use in bacterial host cells include, but are not limited to, for example, the amyE, amyQ, amyL, pstS, sacB, pSPAC, pAprE, pVeg, pHpaII promoters, the promoter of the B. stearothermophilus maltogenic amylase gene, the B. amyloliquefaciens (BAN) amylase gene, the B. subtilis alkaline protease gene, the B. clausii alkaline protease gene the B. pumilis xylosidase gene, the B. thuringiensis cryIIIA, and the B. licheniformis alpha-amylase gene. Additional promoters include, but are not limited to the A4 promoter, as well as phage Lambda PR or PL promoters, and the E. coli lac, trp or tac promoters.

[0165] Metalloprotease polypeptides of the present invention can be produced in host cells of any suitable microorganism, including bacteria and fungi. In some embodiments, metalloprotease polypeptides of the present invention can be produced in Gram-positive bacteria. In some embodiments, the host cells are Bacillus spp., Streptomyces spp., Escherichia spp., Aspergillus spp., Trichoderma spp., Pseudomonas spp., Corynebacterium spp., Saccharomyces spp., or Pichia spp. In some embodiments, the metalloprotease polypeptides are produced by Bacillus sp. host cells. Examples of Bacillus sp. host cells that find use in the production of the metalloprotease polypeptides of the invention include, but are not limited to B. licheniformis, B. lentus, B. subtilis, B. amyloliquefaciens, B. lentus, B. brevis, B. stearothermophilus, B. alkalophilus, B. coagulans, B. circulans, B. pumilis, B. thuringiensis, B. clausii, and B. megaterium, as well as other organisms within the genus Bacillus. In some embodiments, B. subtilis host cells are used for production of metalloprotease polypeptides. U.S. Pat. Nos. 5,264,366 and 4,760,025 (RE 34,606) describe various Bacillus host strains that can be used for producing metalloprotease polypeptide of the invention, although other suitable strains can be used.

[0166] Several bacterial strains that can be used to produce metalloprotease polypeptides of the invention include non-recombinant (i.e., wild-type) Bacillus sp. strains, as well as variants of naturally-occurring strains and/or recombinant strains. In some embodiments, the host strain is a recombinant strain, wherein a polynucleotide encoding a polypeptide of interest has been introduced into the host. In some embodiments, the host strain is a B. subtilis host strain and particularly a recombinant Bacillus subtilis host strain. Numerous B. subtilis strains are known, including, but not limited to for example, 1A6 (ATCC 39085), 168 (1A01), SB19, W23, Ts85, B637, PB1753 through PB1758, PB3360, JH642, 1A243 (ATCC 39,087), ATCC 21332, ATCC 6051, MI113, DE100 (ATCC 39,094), GX4931, PBT 110, and PEP 211strain (See e.g., Hoch et al., Genetics 73:215-228 [1973]; See also, U.S. Pat. Nos. 4,450,235 and 4,302,544, and EP 0134048, each of which is incorporated by reference in its entirety). The use of B. subtilis as an expression host cells is well known in the art (See e.g., Palva et al., Gene 19:81-87 [1982]; Fahnestock and Fischer, J. Bacteriol., 165:796-804 [1986]; and Wang et al., Gene 69:39-47 [1988]).

[0167] In some embodiments, the Bacillus host cell is a Bacillus sp. that includes a mutation or deletion in at least one of the following genes, degU, degS, degR and degQ. In some embodiments, the mutation is in a degU gene, and in some embodiments the mutation is degU(Hy)32 (See e.g., Msadek et al., J. Bacteriol. 172:824-834 [1990]; and Olmos et al., Mol. Gen. Genet. 253:562-567 [1997]). In some embodiments, the Bacillus host comprises a mutation or deletion in scoC4 (See e.g., Caldwell et al., J. Bacteriol. 183:7329-7340 [2001]); spollE (See e.g., Arigoni et al., Mol. Microbiol. 31:1407-1415 [1999]); and/or oppA or other genes of the opp operon (See e.g., Perego et al., Mol. Microbiol. 5:173-185 [1991]). Indeed, it is contemplated that any mutation in the opp operon that causes the same phenotype as a mutation in the oppA gene will find use in some embodiments of the altered Bacillus strain of the invention. In some embodiments, these mutations occur alone, while in other embodiments, combinations of mutations are present. In some embodiments, an altered Bacillus host cell strain that can be used to produce a metalloprotease polypeptide of the invention is a Bacillus host strain that already includes a mutation in one or more of the above-mentioned genes. In addition, Bacillus sp. host cells that comprise mutation(s) and/or deletions of endogenous protease genes find use. In some embodiments, the Bacillus host cell comprises a deletion of the aprE and the nprE genes. In other embodiments, the Bacillus sp. host cell comprises a deletion of 5 protease genes, while in other embodiments, the Bacillus sp. host cell comprises a deletion of 9 protease genes (See e.g., U.S. Pat. Appln. Pub. No. 2005/0202535, incorporated herein by reference).

[0168] Host cells are transformed with at least one nucleic acid encoding at least one metalloprotease polypeptide of the invention using any suitable method known in the art. Methods for introducing a nucleic acid (e.g., DNA) into Bacillus cells or E. coli cells utilizing plasmid DNA constructs or vectors and transforming such plasmid DNA constructs or vectors into such cells are well known. In some embodiments, the plasmids are subsequently isolated from E. coli cells and transformed into Bacillus cells. However, it is not essential to use intervening microorganisms such as E. coli, and in some embodiments, a DNA construct or vector is directly introduced into a Bacillus host.

[0169] Those of skill in the art are well aware of suitable methods for introducing nucleic acid sequences of the invention into Bacillus cells (See e.g., Ferrari et al., Genetics, in Harwood et al. [eds.], Bacillus, Plenum Publishing Corp. [1989], pp. 57-72; Saunders et al., J. Bacteriol. 157:718-726 [1984]; Hoch et al., J. Bacteriol. 93:1925-1937 [1967]; Mann et al., Current Microbiol. 13:131-135 [1986]; Holubova, Folia Microbiol. 30:97 [1985]; Chang et al., Mol. Gen. Genet. 168:11-115 [1979]; Vorobjeva et al., FEMS Microbiol. Lett. 7:261-263 [1980]; Smith et al., Appl. Env. Microbiol. 51:634 [1986]; Fisher et al., Arch. Microbiol. 139:213-217 [1981]; and McDonald, J. Gen. Microbiol. 130:203 [1984]). Indeed, such methods as transformation, including protoplast transformation and transfection, transduction, and protoplast fusion are well known and suited for use in the present invention. Methods known in the art to transform Bacillus cells include such methods as plasmid marker rescue transformation, which involves the uptake of a donor plasmid by competent cells carrying a partially homologous resident plasmid (See, Contente et al., Plasmid 2:555-571 [1979]; Haima et al., Mol. Gen. Genet. 223:185-191 [1990]; Weinrauch et al., J. Bacteriol. 154:1077-1087 [1983]; and Weinrauch et al., J. Bacteriol. 169:1205-1211 [1987]). In this method, the incoming donor plasmid recombines with the homologous region of the resident helper plasmid in a process that mimics chromosomal transformation.

[0170] In addition to commonly used methods, in some embodiments, host cells are directly transformed with a DNA construct or vector comprising a nucleic acid encoding a metalloprotease polypeptide of the invention (i.e., an intermediate cell is not used to amplify, or otherwise process, the DNA construct or vector prior to introduction into the host cell). Introduction of the DNA construct or vector of the invention into the host cell includes those physical and chemical methods known in the art to introduce a nucleic acid sequence (e.g., DNA sequence) into a host cell without insertion into the host genome. Such methods include, but are not limited to calcium chloride precipitation, electroporation, naked DNA, liposomes and the like. In additional embodiments, DNA constructs or vector are co-transformed with a plasmid, without being inserted into the plasmid. In further embodiments, a selective marker is deleted from the altered Bacillus strain by methods known in the art (See, Stahl et al., J. Bacteriol. 158:411-418 [1984]; and Palmeros et al., Gene 247:255-264 [2000]).

[0171] In some embodiments, the transformed cells of the present invention are cultured in conventional nutrient media. The suitable specific culture conditions, such as temperature, pH and the like are known to those skilled in the art and are well described in the scientific literature. In some embodiments, the invention provides a culture (e.g., cell culture) comprising at least one metalloprotease polypeptide or at least one nucleic acid of the invention.

[0172] In some embodiments, host cells transformed with at least one polynucleotide sequence encoding at least one metalloprotease polypeptide of the invention are cultured in a suitable nutrient medium under conditions permitting the expression of the present protease, after which the resulting protease is recovered from the culture. In some embodiments, the protease produced by the cells is recovered from the culture medium by conventional procedures, including, but not limited to for example, separating the host cells from the medium by centrifugation or filtration, precipitating the proteinaceous components of the supernatant or filtrate by means of a salt (e.g., ammonium sulfate), chromatographic purification (e.g., ion exchange, gel filtration, affinity, etc.).

[0173] In some embodiments, a metalloprotease polypeptide produced by a recombinant host cell is secreted into the culture medium. A nucleic acid sequence that encodes a purification facilitating domain may be used to facilitate purification of proteins. A vector or DNA construct comprising a polynucleotide sequence encoding a metalloprotease polypeptide may further comprise a nucleic acid sequence encoding a purification facilitating domain to facilitate purification of the metalloprotease polypeptide (See e.g., Kroll et al., DNA Cell Biol. 12:441-53 [1993]). Such purification facilitating domains include, but are not limited to, for example, metal chelating peptides such as histidine-tryptophan modules that allow purification on immobilized metals (See, Porath, Protein Expr. Purif. 3:263-281 [1992]), protein A domains that allow purification on immobilized immunoglobulin, and the domain utilized in the FLAGS extension/affinity purification system. The inclusion of a cleavable linker sequence such as Factor XA or enterokinase (e.g., sequences available from Invitrogen, San Diego, Calif.) between the purification domain and the heterologous protein also find use to facilitate purification.

[0174] Assays for detecting and measuring the enzymatic activity of an enzyme, such as a metalloprotease polypeptide of the invention, are well known. Various assays for detecting and measuring activity of proteases (e.g., metalloprotease polypeptides of the invention), are also known to those of ordinary skill in the art. In particular, assays are available for measuring protease activity that are based on the release of acid-soluble peptides from casein or hemoglobin, measured as absorbance at 280 nm or colorimetrically using the Folin method. Other exemplary assays involve the solubilization of chromogenic substrates (See e.g., Ward, Proteinases, in Fogarty (ed.)., Microbial Enzymes and Biotechnology, Applied Science, London, [1983], pp. 251-317). Other exemplary assays include, but are not limited to hydrolysis of protein substrates such as casein (azo-casein, dimethyl-casein and other forms), and peptidyl substrates such as succinyl-Ala-Ala-Pro-Phe-para nitroanilide assay (suc-AAPF-pNA)(SEQ ID NO: 24) and the 2,4,6-trinitrobenzene sulfonate sodium salt (TNBS). Numerous additional references known to those in the art provide suitable methods (See e.g., Wells et al., Nucleic Acids Res. 11:7911-7925 [1983]; Christianson et al., Anal. Biochem. 223:119-129 [1994]; and Hsia et al., Anal Biochem. 242:221-227 [1999]).

[0175] A variety of methods can be used to determine the level of production of a mature protease (e.g., mature metalloprotease polypeptides of the present invention) in a host cell. Such methods include, but are not limited to, for example, methods that utilize either polyclonal or monoclonal antibodies specific for the protease. Exemplary methods include, but are not limited to enzyme-linked immunosorbent assays (ELISA), radioimmunoassays (RIA), fluorescent immunoassays (FIA), and fluorescent activated cell sorting (FACS). These and other assays are well known in the art (See e.g., Maddox et al., J. Exp. Med. 158:1211 [1983]).

[0176] In some other embodiments, the invention provides methods for making or producing a mature metalloprotease polypeptide of the invention. A mature metalloprotease polypeptide does not include a signal peptide or a propeptide sequence. Some methods comprise making or producing a metalloprotease polypeptide of the invention in a recombinant bacterial host cell, such as for example, a Bacillus sp. cell (e.g., a B. subtilis cell). In some embodiments, the invention provides a method of producing a metalloprotease polypeptide of the invention, the method comprising cultivating a recombinant host cell comprising a recombinant expression vector comprising a nucleic acid encoding a metalloprotease polypeptide of the invention under conditions conducive to the production of the metalloprotease polypeptide. Some such methods further comprise recovering the metalloprotease polypeptide from the culture.

[0177] In some embodiments the invention provides methods of producing a metalloprotease polypeptide of the invention, the methods comprising: (a) introducing a recombinant expression vector comprising a nucleic acid encoding a metalloprotease polypeptide of the invention into a population of cells (e.g., bacterial cells, such as B. subtilis cells); and (b) culturing the cells in a culture medium under conditions conducive to produce the metalloprotease polypeptide encoded by the expression vector. Some such methods further comprise: (c) isolating the metalloprotease polypeptide from the cells or from the culture medium.

Compositions Having the Metalloprotease Polypeptide of the Present Invention

[0178] Unless otherwise noted, all component or composition levels provided herein are made in reference to the active level of that component or composition, and are exclusive of impurities, for example, residual solvents or by-products, which may be present in commercially available sources. Enzyme components weights are based on total active protein. All percentages and ratios are calculated by weight unless otherwise indicated. All percentages and ratios are calculated based on the total composition unless otherwise indicated. Compositions of the invention include cleaning compositions, such as detergent compositions. In the exemplified detergent compositions, the enzymes levels are expressed by pure enzyme by weight of the total composition and unless otherwise specified, the detergent ingredients are expressed by weight of the total compositions.

[0179] As indicated herein, in some embodiments, the cleaning compositions of the present invention further comprise adjunct materials including, but not limited to, surfactants, builders, bleaches, bleach activators, bleach catalysts, other enzymes, enzyme stabilizing systems, chelants, optical brighteners, soil release polymers, dye transfer agents, dispersants, suds suppressors, dyes, perfumes, colorants, filler salts, hydrotropes, photoactivators, fluorescers, fabric conditioners, hydrolyzable surfactants, preservatives, anti-oxidants, anti-shrinkage agents, anti-wrinkle agents, germicides, fungicides, color speckles, silvercare, anti-tarnish and/or anti-corrosion agents, alkalinity sources, solubilizing agents, carriers, processing aids, pigments, and pH control agents (See e.g., U.S. Pat. Nos. 6,610,642, 6,605,458, 5,705,464, 5,710,115, 5,698,504, 5,695,679, 5,686,014 and 5,646,101, all of which are incorporated herein by reference). Embodiments of specific cleaning composition materials are exemplified in detail below. In embodiments in which the cleaning adjunct materials are not compatible with the metalloprotease polypeptides of the present invention in the cleaning compositions, then suitable methods of keeping the cleaning adjunct materials and the protease(s) separated (i.e., not in contact with each other) until combination of the two components is appropriate are used. Such separation methods include any suitable method known in the art (e.g., gelcaps, encapsulation, tablets, physical separation, etc.).

[0180] The cleaning compositions of the present invention are advantageously employed for example, in laundry applications, hard surface cleaning, dishwashing applications, including automatic dishwashing and hand dishwashing, as well as cosmetic applications such as dentures, teeth, hair and skin. In addition, due to the unique advantages of increased effectiveness in lower temperature solutions, the enzymes of the present invention are ideally suited for laundry applications. Furthermore, the enzymes of the present invention find use in granular and liquid compositions.

[0181] The metalloprotease polypeptides of the present invention also find use in cleaning additive products. In some embodiments, low temperature solution cleaning applications find use. In some embodiments, the present invention provides cleaning additive products including at least one enzyme of the present invention is ideally suited for inclusion in a wash process when additional bleaching effectiveness is desired. Such instances include, but are not limited to low temperature solution cleaning applications. In some embodiments, the additive product is in its simplest form, one or more proteases. In some embodiments, the additive is packaged in dosage form for addition to a cleaning process. In some embodiments, the additive is packaged in dosage form for addition to a cleaning process where a source of peroxygen is employed and increased bleaching effectiveness is desired. Any suitable single dosage unit form finds use with the present invention, including but not limited to pills, tablets, gelcaps, or other single dosage units such as pre-measured powders or liquids. In some embodiments, filler(s) or carrier material(s) are included to increase the volume of such compositions. Suitable filler or carrier materials include, but are not limited to, various salts of sulfate, carbonate and silicate as well as talc, clay and the like. Suitable filler or carrier materials for liquid compositions include, but are not limited to water or low molecular weight primary and secondary alcohols including polyols and diols. Examples of such alcohols include, but are not limited to, methanol, ethanol, propanol and isopropanol. In some embodiments, the compositions contain from about 5% to about 90% of such materials. Acidic fillers find use to reduce pH. Alternatively, in some embodiments, the cleaning additive includes adjunct ingredients, as more fully described below.

[0182] The present cleaning compositions and cleaning additives require an effective amount of at least one of the metalloprotease polypeptides provided herein, alone or in combination with other proteases and/or additional enzymes. The required level of enzyme is achieved by the addition of one or more metalloprotease polypeptides of the present invention. Typically the present cleaning compositions comprise at least about 0.0001 weight percent, from about 0.0001 to about 10, from about 0.001 to about 1, or from about 0.01 to about 0.1 weight percent of at least one of the metalloprotease polypeptides of the present invention.

[0183] The cleaning compositions herein are typically formulated such that, during use in aqueous cleaning operations, the wash water will have a pH of from about 4.0 to about 11.5 or even from about 5.0 to about 11.5, or even from about 5.0 to about 8.0, or even from about 7.5 to about 10.5. Liquid product formulations are typically formulated to have a pH from about 3.0 to about 9.0 or even from about 3 to about 5. Granular laundry products are typically formulated to have a pH from about 9 to about 11. Techniques for controlling pH at recommended usage levels include the use of buffers, alkalis, acids, etc., and are well known to those skilled in the art.

[0184] Suitable low pH cleaning compositions typically have a pH of from about 3 to about 5, and are typically free of surfactants that hydrolyze in such a pH environment. Such surfactants include sodium alkyl sulfate surfactants that comprise at least one ethylene oxide moiety or even from about 1 to about 16 moles of ethylene oxide. Such cleaning compositions typically comprise a sufficient amount of a pH modifier, such as sodium hydroxide, monoethanolamine or hydrochloric acid, to provide such cleaning composition with a pH of from about 3 to about 5. Such compositions typically comprise at least one acid stable enzyme. In some embodiments, the compositions are liquids, while in other embodiments, they are solids. The pH of such liquid compositions is typically measured as a neat pH. The pH of such solid compositions is measured as a 10% solids solution of said composition wherein the solvent is distilled water. In these embodiments, all pH measurements are taken at 20 C., unless otherwise indicated.

[0185] In some embodiments, when the metalloprotease polypeptide(s) is/are employed in a granular composition or liquid, it is desirable for the metalloprotease polypeptide to be in the form of an encapsulated particle to protect the metalloprotease polypeptide from other components of the granular composition during storage. In addition, encapsulation is also a means of controlling the availability of the metalloprotease polypeptide during the cleaning process. In some embodiments, encapsulation enhances the performance of the metalloprotease polypeptide(s) and/or additional enzymes. In this regard, the metalloprotease polypeptides of the present invention are encapsulated with any suitable encapsulating material known in the art. In some embodiments, the encapsulating material typically encapsulates at least part of the metalloprotease polypeptide(s) of the present invention. Typically, the encapsulating material is water-soluble and/or water-dispersible. In some embodiments, the encapsulating material has a glass transition temperature (Tg) of 0 C. or higher. Glass transition temperature is described in more detail in WO 97/11151. The encapsulating material is typically selected from consisting of carbohydrates, natural or synthetic gums, chitin, chitosan, cellulose and cellulose derivatives, silicates, phosphates, borates, polyvinyl alcohol, polyethylene glycol, paraffin waxes, and combinations thereof. When the encapsulating material is a carbohydrate, it is typically selected from monosaccharides, oligosaccharides, polysaccharides, and combinations thereof. In some typical embodiments, the encapsulating material is a starch (See e.g., EP 0 922 499; U.S. Pat. Nos. 4,977,252; 5,354,559, and 5,935,826). In some embodiments, the encapsulating material is a microsphere made from plastic such as thermoplastics, acrylonitrile, methacrylonitrile, polyacrylonitrile, polymethacrylonitrile and mixtures thereof; commercially available microspheres that find use include, but are not limited to those supplied by EXPANCEL (Stockviksverken, Sweden), and PM 6545, PM 6550, PM 7220, PM 7228, EXTENDOSPHERES, LUXSIL, Q-CEL, and SPHERICEL (PQ Corp., Valley Forge, Pa.).

[0186] As described herein, the metalloprotease polypeptides of the present invention find particular use in the cleaning industry, including, but not limited to laundry and dish detergents. These applications place enzymes under various environmental stresses. The metalloprotease polypeptides of the present invention provide advantages over many currently used enzymes, due to their stability under various conditions.

[0187] Indeed, there are a variety of wash conditions including varying detergent formulations, wash water volumes, wash water temperatures, and lengths of wash time, to which proteases involved in washing are exposed. In addition, detergent formulations used in different geographical areas have different concentrations of their relevant components present in the wash water. For example, European detergents typically have about 4500-5000 ppm of detergent components in the wash water, while Japanese detergents typically have approximately 667 ppm of detergent components in the wash water. In North America, particularly the United States, detergents typically have about 975 ppm of detergent components present in the wash water.

[0188] A low detergent concentration system includes detergents where less than about 800 ppm of the detergent components are present in the wash water. Japanese detergents are typically considered low detergent concentration system as they have approximately 667 ppm of detergent components present in the wash water.

[0189] A medium detergent concentration includes detergents where between about 800 ppm and about 2000 ppm of the detergent components are present in the wash water. North American detergents are generally considered to be medium detergent concentration systems as they have approximately 975 ppm of detergent components present in the wash water. Brazil typically has approximately 1500 ppm of detergent components present in the wash water.

[0190] A high detergent concentration system includes detergents where greater than about 2000 ppm of the detergent components are present in the wash water. European detergents are generally considered to be high detergent concentration systems as they have approximately 4500-5000 ppm of detergent components in the wash water.

[0191] Latin American detergents are generally high suds phosphate builder detergents and the range of detergents used in Latin America can fall in both the medium and high detergent concentrations as they range from 1500 ppm to 6000 ppm of detergent components in the wash water. As mentioned above, Brazil typically has approximately 1500 ppm of detergent components present in the wash water. However, other high suds phosphate builder detergent geographies, not limited to other Latin American countries, may have high detergent concentration systems up to about 6000 ppm of detergent components present in the wash water.

[0192] In light of the foregoing, it is evident that concentrations of detergent compositions in typical wash solutions throughout the world varies from less than about 800 ppm of detergent to about 6000 ppm in high suds phosphate builder geographies.

[0193] The concentrations of the typical wash solutions are determined empirically. For example, in the U.S., a typical washing machine holds a volume of about 64.4 L of wash solution. Accordingly, in order to obtain a concentration of about 975 ppm of detergent within the wash solution about 62.79 g of detergent composition must be added to the 64.4 L of wash solution. This amount is the typical amount measured into the wash water by the consumer using the measuring cup provided with the detergent.

[0194] As a further example, different geographies use different wash temperatures. The temperature of the wash water in Japan is typically less than that used in Europe. For example, the temperature of the wash water in North America and Japan is typically between about 10 and about 40 C. (e.g., about 20 C.), whereas the temperature of wash water in Europe is typically between about 30 and about 60 C. (e.g., about 40 C.). However, in the interest of saving energy, many consumers are switching to using cold water washing. In addition, in some further regions, cold water is typically used for laundry, as well as dish washing applications. In some embodiments, the cold water washing of the present invention utilizes cold water detergent suitable for washing at temperatures from about 10 C. to about 40 C., or from about 20 C. to about 30 C., or from about 15 C. to about 25 C., as well as all other combinations within the range of about 15 C. to about 35 C., and all ranges within 10 C. to 40 C.

[0195] As a further example, different geographies typically have different water hardness. Water hardness is usually described in terms of the grains per gallon mixed Ca.sup.2+/Mg.sup.2+ Hardness is a measure of the amount of calcium (Ca.sup.2+) and magnesium (Mg.sup.2+) in the water. Most water in the United States is hard, but the degree of hardness varies. Moderately hard (60-120 ppm) to hard (121-181 ppm) water has 60 to 181 parts per million (parts per million converted to grains per U.S. gallon is ppm # divided by 17.1 equals grains per gallon) of hardness minerals.

TABLE-US-00001 Water Grains per gallon Parts per million Soft less than 1.0 less than 17 Slightly hard 1.0 to 3.5 17 to 60 Moderately hard 3.5 to 7.0 60 to 120 Hard 7.0 to 10.5 120 to 180 Very hard greater than 10.5 greater than 180

[0196] European water hardness is typically greater than about 10.5 (for example about 10.5 to about 20.0) grains per gallon mixed Ca.sup.2+/Mg.sup.2+ (e.g., about 15 grains per gallon mixed Ca.sup.2+/Mg.sup.2+). North American water hardness is typically greater than Japanese water hardness, but less than European water hardness. For example, North American water hardness can be between about 3 to about 10 grains, about 3 to about 8 grains or about 6 grains. Japanese water hardness is typically lower than North American water hardness, usually less than about 4, for example about 3 grains per gallon mixed Ca.sup.2+/Mg.sup.2+.

[0197] Accordingly, in some embodiments, the present invention provides metalloprotease polypeptides that show surprising wash performance in at least one set of wash conditions (e.g., water temperature, water hardness, and/or detergent concentration). In some embodiments, the metalloprotease polypeptides of the present invention are comparable in wash performance to other metalloprotease polypeptide proteases. In some embodiments of the present invention, the metalloprotease polypeptides provided herein exhibit enhanced oxidative stability, enhanced thermal stability, enhanced cleaning capabilities under various conditions, and/or enhanced chelator stability. In addition, the metalloprotease polypeptides of the present invention find use in cleaning compositions that do not include detergents, again either alone or in combination with builders and stabilizers.

[0198] In some embodiments of the present invention, the cleaning compositions comprise at least one metalloprotease polypeptide of the present invention at a level from about 0.00001% to about 10% by weight of the composition and the balance (e.g., about 99.999% to about 90.0%) comprising cleaning adjunct materials by weight of composition. In some other embodiments of the present invention, the cleaning compositions of the present invention comprises at least one metalloprotease polypeptide at a level of about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, about 0.005% to about 0.5% by weight of the composition and the balance of the cleaning composition (e.g., about 99.9999% to about 90.0%, about 99.999% to about 98%, about 99.995% to about 99.5% by weight) comprising cleaning adjunct materials.

[0199] In some embodiments, the cleaning compositions of the present invention comprise one or more additional detergent enzymes, which provide cleaning performance and/or fabric care and/or dishwashing benefits. Examples of suitable enzymes include, but are not limited to, acyl transferases, alpha-amylases, beta-amylases, alpha-galactosidases, arabinosidases, aryl esterases, beta-galactosidases, carrageenases, catalases, cellobiohydrolases, cellulases, chondroitinases, cutinases, endo-beta-1, 4-glucanases, endo-beta-mannanases, esterases, exo-mannanases, galactanases, glucoamylases, hemicellulases, hyaluronidases, keratinases, laccases, lactases, ligninases, lipases, lipoxygenases, mannanases, oxidases, pectate lyases, pectin acetyl esterases, pectinases, pentosanases, peroxidases, phenoloxidases, phosphatases, phospholipases, phytases, polygalacturonases, proteases, pullulanases, reductases, rhamnogalacturonases, beta-glucanases, tannases, transglutaminases, xylan acetyl-esterases, xylanases, xyloglucanases, and xylosidases, or any combinations or mixtures thereof. In some embodiments, a combination of enzymes is used (i.e., a cocktail) comprising conventional applicable enzymes like protease, lipase, cutinase and/or cellulase in conjunction with amylase is used.

[0200] In addition to the metalloprotease polypeptides provided herein, any other suitable protease finds use in the compositions of the present invention. Suitable proteases include those of animal, vegetable or microbial origin. In some embodiments, microbial proteases are used. In some embodiments, chemically or genetically modified mutants are included. In some embodiments, the protease is a serine protease, preferably an alkaline microbial protease or a trypsin-like protease. Examples of alkaline proteases include subtilisins, especially those derived from Bacillus (e.g., subtilisin, lentus, amyloliquefaciens, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168). Additional examples include those mutant proteases described in U.S. Pat. Nos. RE 34,606, 5,955,340, 5,700,676, 6,312,936, and 6,482,628, all of which are incorporated herein by reference. Additional protease examples include, but are not limited to trypsin (e.g., of porcine or bovine origin), and the Fusarium protease described in WO 89/06270. In some embodiments, commercially available protease enzymes that find use in the present invention include, but are not limited to MAXATASE, MAXACAL, MAXAPEM, OPTICLEAN, OPTIMASE, PROPERASE, PURAFECT, PURAFECT OXP, PURAMAX, EXCELLASE, and PURAFAST (Genencor); ALCALASE, SAVINASE, PRIMASE, DURAZYM, POLARZYME, OVOZYME, KANNASE, LIQUANASE, NEUTRASE, RELASE and ESPERASE (Novozymes); BLAP and BLAP variants (Henkel Kommanditgesellschaft auf Aktien, Duesseldorf, Germany), and KAP (B. alkalophilus subtilisin; Kao Corp., Tokyo, Japan). Various proteases are described in WO95/23221, WO 92/21760, WO 09/149200, WO 09/149144, WO 09/149145, WO 11/072099, WO 10/056640, WO 10/056653, WO 11/140364, WO 12/151534, U.S. Pat. Publ. No. 2008/0090747, and U.S. Pat. Nos. 5,801,039, 5,340,735, 5,500,364, 5,855,625, US RE 34,606, 5,955,340, 5,700,676, 6,312,936, and 6,482,628, and various other patents. In some further embodiments, metalloproteases find use in the present invention, including but not limited to the neutral metalloprotease described in WO 07/044993.

[0201] In addition, any suitable lipase finds use in the present invention. Suitable lipases include, but are not limited to those of bacterial or fungal origin. Chemically or genetically modified mutants are encompassed by the present invention. Examples of useful lipases include Humicola lanuginosa lipase (See e.g., EP 258 068, and EP 305 216), Rhizomucor miehei lipase (See e.g., EP 238 023), Candida lipase, such as C. antarctica lipase (e.g., the C. antarctica lipase A or B; See e.g., EP 214 761), Pseudomonas lipases such as P. alcaligenes lipase and P. pseudoalcaligenes lipase (See e.g., EP 218 272), P. cepacia lipase (See e.g., EP 331 376), P. stutzeri lipase (See e.g., GB 1,372,034), P. fluorescens lipase, Bacillus lipase (e.g., B. subtilis lipase [Dartois et al., Biochem. Biophys. Acta 1131:253-260 [1993]); B. stearothermophilus lipase [See e.g., JP 64/744992]; and B. pumilus lipase [See e.g., WO 91/16422]).

[0202] Furthermore, a number of cloned lipases find use in some embodiments of the present invention, including but not limited to Penicillium camembertii lipase (See, Yamaguchi et al., Gene 103:61-67 [1991]), Geotricum candidum lipase (See, Schimada et al., J. Biochem., 106:383-388 [1989]), and various Rhizopus lipases such as R. delemar lipase (See, Hass et al., Gene 109:117-113 [1991]), a R. niveus lipase (Kugimiya et al., Biosci. Biotech. Biochem. 56:716-719 [1992]) and R. oryzae lipase.

[0203] Other types of lipase polypeptide enzymes such as cutinases also find use in some embodiments of the present invention, including but not limited to the cutinase derived from Pseudomonas mendocina (See, WO 88/09367), and the cutinase derived from Fusarium solani pisi (See, WO 90/09446).

[0204] Additional suitable lipases include commercially available lipases such as M1 LIPASE, LUMA FAST, and LIPOMAX (Genencor); LIPEX, LIPOLASE and LIPOLASE ULTRA (Novozymes); and LIPASE P Amano (Amano Pharmaceutical Co. Ltd., Japan). Various lipases are described in WO2010065455, WO2010107560, WO2011084412, WO2011084417, WO2011084599, WO2011078949, WO2011150157, WO2012137147, WO2013033318, WO2013096653, and U.S. Patent Application No. 61/713,436.

[0205] In some embodiments of the present invention, the cleaning compositions of the present invention further comprise lipases at a level from about 0.00001% to about 10% of additional lipase by weight of the composition and the balance of cleaning adjunct materials by weight of composition. In some other embodiments of the present invention, the cleaning compositions of the present invention also comprise lipases at a level of about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, about 0.005% to about 0.5% lipase by weight of the composition.

[0206] In some embodiments of the present invention, any suitable amylase finds use in the present invention. In some embodiments, any amylase (e.g., alpha and/or beta) suitable for use in alkaline solutions also find use. Suitable amylases include, but are not limited to those of bacterial or fungal origin. Chemically or genetically modified mutants are included in some embodiments. Amylases that find use in the present invention, include, but are not limited to -amylases obtained from B. licheniformis (See e.g., GB 1,296,839). Additional suitable amylases include those found in WO9510603, WO9526397, WO9623874, WO9623873, WO9741213, WO9919467, WO0060060, WO0029560, WO9923211, WO9946399, WO0060058, WO0060059, WO9942567, WO0114532, WO002092797, WO0166712, WO0188107, WO0196537, W0210355, WO9402597, WO00231124, WO9943793, WO9943794, WO2004113551, WO2005001064, WO2005003311, WO0164852, WO2006063594, WO2006066594, WO2006066596, WO2006012899, WO2008092919, WO2008000825, WO2005018336, WO2005066338, WO2009140504, WO2005019443, WO2010091221, WO2010088447, WOO 134784, WO2006012902, WO2006031554, WO2006136161, WO2008101894, WO2010059413, WO2011098531, WO2011080352, WO2011080353, WO2011080354, WO2011082425, WO2011082429, WO2011076123, WO2011087836, WO2011076897, WO94183314, WO9535382, WO9909183, WO9826078, WO9902702, WO9743424, WO9929876, WO9100353, WO9605295, WO9630481, WO9710342, WO2008088493, WO2009149419, WO2009061381, WO2009100102, WO2010104675, WO2010117511, and WO2010115021. Commercially available amylases that find use in the present invention include, but are not limited to DURAMYL, TERMAMYL, FUNGAMYL, STAINZYME, STAINZYME PLUS, STAINZYME ULTRA, and BAN (Novozymes), as well as POWERASE, RAPIDASE and MAXAMYL P (Genencor).

[0207] In some embodiments of the present invention, the cleaning compositions of the present invention further comprise amylases at a level from about 0.00001% to about 10% of additional amylase by weight of the composition and the balance of cleaning adjunct materials by weight of composition. In some other embodiments of the present invention, the cleaning compositions of the present invention also comprise amylases at a level of about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, about 0.005% to about 0.5% amylase by weight of the composition.

[0208] In some further embodiments, any suitable cellulase finds used in the cleaning compositions of the present invention. Suitable cellulases include, but are not limited to those of bacterial or fungal origin. Chemically or genetically modified mutants are included in some embodiments. Suitable cellulases include, but are not limited to Humicola insolens cellulases (See e.g., U.S. Pat. No. 4,435,307). Especially suitable cellulases are the cellulases having color care benefits (See e.g., EP 0 495 257). Commercially available cellulases that find use in the present include, but are not limited to CELLUZYME, CAREZYME (Novozymes), and KAC-500(B) (Kao Corporation). In some embodiments, cellulases are incorporated as portions or fragments of mature wild-type or variant cellulases, wherein a portion of the N-terminus is deleted (See e.g., U.S. Pat. No. 5,874,276). Additional suitable cellulases include those found in WO2005054475, WO2005056787, U.S. Pat. Nos. 7,449,318, and 7,833,773. In some embodiments, the cleaning compositions of the present invention further comprise cellulases at a level from about 0.00001% to about 10% of additional cellulase by weight of the composition and the balance of cleaning adjunct materials by weight of composition. In some other embodiments of the present invention, the cleaning compositions of the present invention also comprise cellulases at a level of about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, about 0.005% to about 0.5% cellulase by weight of the composition.

[0209] Any mannanase suitable for use in detergent compositions also finds use in the present invention. Suitable mannanases include, but are not limited to those of bacterial or fungal origin. Chemically or genetically modified mutants are included in some embodiments. Various mannanases are known which find use in the present invention (See e.g., U.S. Pat. Nos. 6,566,114, 6,602,842, and 6,440,991, all of which are incorporated herein by reference). Commercially available mannanases that find use in the present invention include, but are not limited to MANNASTAR, PURABRITE, and MANNAWAY. In some embodiments, the cleaning compositions of the present invention further comprise mannanases at a level from about 0.00001% to about 10% of additional mannanase by weight of the composition and the balance of cleaning adjunct materials by weight of composition. In some embodiments of the present invention, the cleaning compositions of the present invention also comprise mannanases at a level of about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, about 0.005% to about 0.5% mannanase by weight of the composition.

[0210] In some embodiments, peroxidases are used in combination with hydrogen peroxide or a source thereof (e.g., a percarbonate, perborate or persulfate) in the compositions of the present invention. In some alternative embodiments, oxidases are used in combination with oxygen. Both types of enzymes are used for solution bleaching (i.e., to prevent transfer of a textile dye from a dyed fabric to another fabric when the fabrics are washed together in a wash liquor), preferably together with an enhancing agent (See e.g., WO 94/12621 and WO 95/01426). Suitable peroxidases/oxidases include, but are not limited to those of plant, bacterial or fungal origin. Chemically or genetically modified mutants are included in some embodiments. In some embodiments, the cleaning compositions of the present invention further comprise peroxidase and/or oxidase enzymes at a level from about 0.00001% to about 10% of additional peroxidase and/or oxidase by weight of the composition and the balance of cleaning adjunct materials by weight of composition. In some other embodiments of the present invention, the cleaning compositions of the present invention also comprise, peroxidase and/or oxidase enzymes at a level of about 0.0001% to about 10%, about 0.001% to about 5%, about 0.001% to about 2%, about 0.005% to about 0.5% peroxidase and/or oxidase enzymes by weight of the composition.

[0211] In some embodiments, additional enzymes find use, including but not limited to perhydrolases (See e.g., WO 05/056782). In addition, in some embodiments, mixtures of the above mentioned enzymes are encompassed herein, in particular one or more additional protease, amylase, lipase, mannanase, and/or at least one cellulase. Indeed, it is contemplated that various mixtures of these enzymes will find use in the present invention. It is also contemplated that the varying levels of the metalloprotease polypeptide (s) and one or more additional enzymes may both independently range to about 10%, the balance of the cleaning composition being cleaning adjunct materials. The specific selection of cleaning adjunct materials are readily made by considering the surface, item, or fabric to be cleaned, and the desired form of the composition for the cleaning conditions during use (e.g., through the wash detergent use).

[0212] Examples of suitable cleaning adjunct materials include, but are not limited to, surfactants, builders, bleaches, bleach activators, bleach catalysts, other enzymes, enzyme stabilizing systems, chelants, optical brighteners, soil release polymers, dye transfer agents, dye transfer inhibiting agents, catalytic materials, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal agents, structure elasticizing agents, dispersants, suds suppressors, dyes, perfumes, colorants, filler salts, hydrotropes, photoactivators, fluorescers, fabric conditioners, fabric softeners, carriers, hydrotropes, processing aids, solvents, pigments, hydrolyzable surfactants, preservatives, anti-oxidants, anti-shrinkage agents, anti-wrinkle agents, germicides, fungicides, color speckles, silvercare, anti-tarnish and/or anti-corrosion agents, alkalinity sources, solubilizing agents, carriers, processing aids, pigments, and pH control agents (See e.g., U.S. Pat. Nos. 6,610,642, 6,605,458, 5,705,464, 5,710,115, 5,698,504, 5,695,679, 5,686,014 and 5,646,101, all of which are incorporated herein by reference). Embodiments of specific cleaning composition materials are exemplified in detail below. In embodiments in which the cleaning adjunct materials are not compatible with the metalloprotease polypeptides of the present invention in the cleaning compositions, then suitable methods of keeping the cleaning adjunct materials and the protease(s) separated (i.e., not in contact with each other) until combination of the two components is appropriate are used. Such separation methods include any suitable method known in the art (e.g., gelcaps, encapsulation, tablets, physical separation, etc.).

[0213] In some embodiments, an effective amount of one or more metalloprotease polypeptide (s) provided herein is included in compositions useful for cleaning a variety of surfaces in need of proteinaceous stain removal. Such cleaning compositions include cleaning compositions for such applications as cleaning hard surfaces, fabrics, and dishes. Indeed, in some embodiments, the present invention provides fabric cleaning compositions, while in other embodiments, the present invention provides non-fabric cleaning compositions. Notably, the present invention also provides cleaning compositions suitable for personal care, including oral care (including dentrifices, toothpastes, mouthwashes, etc., as well as denture cleaning compositions), skin, and hair cleaning compositions. It is intended that the present invention encompass detergent compositions in any form (i.e., liquid, granular, bar, semi-solid, gels, emulsions, tablets, capsules, etc.).

[0214] By way of example, several cleaning compositions wherein the metalloprotease polypeptides of the present invention find use are described in greater detail below. In some embodiments in which the cleaning compositions of the present invention are formulated as compositions suitable for use in laundry machine washing method(s), the compositions of the present invention preferably contain at least one surfactant and at least one builder compound, as well as one or more cleaning adjunct materials preferably selected from organic polymeric compounds, bleaching agents, additional enzymes, suds suppressors, dispersants, lime-soap dispersants, soil suspension and anti-redeposition agents and corrosion inhibitors. In some embodiments, laundry compositions also contain softening agents (i.e., as additional cleaning adjunct materials). The compositions of the present invention also find use in detergent additive products in solid or liquid form. Such additive products are intended to supplement and/or boost the performance of conventional detergent compositions and can be added at any stage of the cleaning process. In some embodiments, the density of the laundry detergent compositions herein ranges from about 400 to about 1200 g/liter, while in other embodiments, it ranges from about 500 to about 950 g/liter of composition measured at 20 C.

[0215] In embodiments formulated as compositions for use in manual dishwashing methods, the compositions of the invention preferably contain at least one surfactant and preferably at least one additional cleaning adjunct material selected from organic polymeric compounds, suds enhancing agents, group II metal ions, solvents, hydrotropes and additional enzymes.

[0216] In some embodiments, various cleaning compositions such as those provided in U.S. Pat. No. 6,605,458, find use with the metalloprotease polypeptides of the present invention. Thus, in some embodiments, the compositions comprising at least one metalloprotease polypeptide of the present invention is a compact granular fabric cleaning composition, while in other embodiments, the composition is a granular fabric cleaning composition useful in the laundering of colored fabrics, in further embodiments, the composition is a granular fabric cleaning composition which provides softening through the wash capacity, in additional embodiments, the composition is a heavy duty liquid fabric cleaning composition. In some embodiments, the compositions comprising at least one metalloprotease polypeptide of the present invention are fabric cleaning compositions such as those described in U.S. Pat. Nos. 6,610,642 and 6,376,450. In addition, the metalloprotease polypeptides of the present invention find use in granular laundry detergent compositions of particular utility under European or Japanese washing conditions (See e.g., U.S. Pat. No. 6,610,642).

[0217] In some alternative embodiments, the present invention provides hard surface cleaning compositions comprising at least one metalloprotease polypeptide provided herein. Thus, in some embodiments, the compositions comprising at least one metalloprotease polypeptide of the present invention is a hard surface cleaning composition such as those described in U.S. Pat. Nos. 6,610,642, 6,376,450, and 6,376,450.

[0218] In yet further embodiments, the present invention provides dishwashing compositions comprising at least one metalloprotease polypeptide provided herein. Thus, in some embodiments, the compositions comprising at least one metalloprotease polypeptide of the present invention is a hard surface cleaning composition such as those in U.S. Pat. Nos. 6,610,642 and 6,376,450. In some still further embodiments, the present invention provides dishwashing compositions comprising at least one metalloprotease polypeptide provided herein. In some further embodiments, the compositions comprising at least one metalloprotease polypeptide of the present invention comprise oral care compositions such as those in U.S. Pat. Nos. 6,376,450, and 6,376,450. The formulations and descriptions of the compounds and cleaning adjunct materials contained in the aforementioned U.S. Pat. Nos. 6,376,450, 6,605,458, 6,605,458, and 6,610,642, find use with the metalloprotease polypeptides provided herein.

[0219] The cleaning compositions of the present invention are formulated into any suitable form and prepared by any process chosen by the formulator, non-limiting examples of which are described in U.S. Pat. Nos. 5,879,584, 5,691,297, 5,574,005, 5,569,645, 5,565,422, 5,516,448, 5,489,392, and 5,486,303, all of which are incorporated herein by reference. When a low pH cleaning composition is desired, the pH of such composition is adjusted via the addition of a material such as monoethanolamine or an acidic material such as HCl.

[0220] In some embodiments, the cleaning compositions of the present invention can be formulated to have an alkaline pH under wash conditions, such as a pH of from about 8.0 to about 12.0, or from about 8.5 to about 11.0, or from about 9.0 to about 11.0. In some embodiments, the cleaning compositions of the present invention can be formulated to have a neutral pH under wash conditions, such as a pH of from about 5.0 to about 8.0, or from about 5.5 to about 8.0, or from about 6.0 to about 8.0, or from about 6.0 to about 7.5. In some embodiments, the neutral pH conditions can be measured when the cleaning composition is dissolved 1:100 (wt:wt) in de-ionised water at 20 C., measured using a conventional pH meter.

[0221] While not essential for the purposes of the present invention, the non-limiting list of adjuncts illustrated hereinafter are suitable for use in the instant cleaning compositions. In some embodiments, these adjuncts are incorporated for example, to assist or enhance cleaning performance, for treatment of the substrate to be cleaned, or to modify the aesthetics of the cleaning composition as is the case with perfumes, colorants, dyes or the like. It is understood that such adjuncts are in addition to the metalloprotease polypeptides of the present invention. The precise nature of these additional components, and levels of incorporation thereof, will depend on the physical form of the composition and the nature of the cleaning operation for which it is to be used. Suitable adjunct materials include, but are not limited to, surfactants, builders, chelating agents, dye transfer inhibiting agents, deposition aids, dispersants, additional enzymes, and enzyme stabilizers, catalytic materials, bleach activators, bleach boosters, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, processing aids and/or pigments. In addition to the disclosure below, suitable examples of such other adjuncts and levels of use are found in U.S. Pat. Nos. 5,576,282, 6,306,812, and 6,326,348, incorporated by reference. The aforementioned adjunct ingredients may constitute the balance of the cleaning compositions of the present invention.

[0222] In some embodiments, the cleaning compositions according to the present invention comprise an acidifying particle or an amino carboxylic builder. Examples of an amino carboxylic builder include aminocarboxylic acids, salts and derivatives thereof. In some embodiment, the amino carboxylic builder is an aminopolycarboxylic builder, such as glycine-N,N-diacetic acid or derivative of general formula MOOCCHRN(CH.sub.2COOM).sub.2 where R is C.sub.1-12 alkyl and M is alkali metal. In some embodiments, the amino carboxylic builder can be methylglycine diacetic acid (MGDA), GLDA (glutamic-N,N-diacetic acid), iminodisuccinic acid (IDS), carboxymethyl inulin and salts and derivatives thereof, aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl) aspartic acid (SMAS), N-(2-sulfoethyl)aspartic acid (SEAS), N-(2-sulfomethyl)glutamic acid (SMGL), N-(2-sulfoethyl) glutamic acid (SEGL), IDS (iminodiacetic acid) and salts and derivatives thereof such as N-methyliminodiacetic acid (MIDA), alpha-alanine-N,N-diacetic acid (alpha-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,Ndiacetic acid (ISDA), phenylalanine-N,N-diacetic acid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilic acid-N,N-diacetic acid (SLDA), taurine-N,N-diacetic acid (TUDA) and sulfomethyl-N,N-diacetic acid (SMDA) and alkali metal salts and derivative thereof. In some embodiments, the acidifying particle has a weight geometric mean particle size of from about 400 to about 1200 and a bulk density of at least 550 g/L. In some embodiments, the acidifying particle comprises at least about 5% of the builder.

[0223] In some embodiments, the acidifying particle can comprise any acid, including organic acids and mineral acids. Organic acids can have one or two carboxyls and in some instances up to 15 carbons, especially up to 10 carbons, such as formic, acetic, propionic, capric, oxalic, succinic, adipic, maleic, fumaric, sebacic, malic, lactic, glycolic, tartaric and glyoxylic acids. In some embodiments, the acid is citric acid. Mineral acids include hydrochloric and sulphuric acid. In some instances, the acidifying particle of the invention is a highly active particle comprising a high level of amino carboxylic builder. Sulphuric acid has been found to further contribute to the stability of the final particle.

[0224] In some embodiments, the cleaning compositions according to the present invention comprise at least one surfactant and/or a surfactant system wherein the surfactant is selected from nonionic surfactants, anionic surfactants, cationic surfactants, ampholytic surfactants, zwitterionic surfactants, semi-polar nonionic surfactants and mixtures thereof. In some low pH cleaning composition embodiments (e.g., compositions having a neat pH of from about 3 to about 5), the composition typically does not contain alkyl ethoxylated sulfate, as it is believed that such surfactant may be hydrolyzed by such compositions the acidic contents. In some embodiments, the surfactant is present at a level of from about 0.1% to about 60%, while in alternative embodiments the level is from about 1% to about 50%, while in still further embodiments the level is from about 5% to about 40%, by weight of the cleaning composition.

[0225] In some embodiments, the cleaning compositions of the present invention comprise one or more detergent builders or builder systems. In some embodiments incorporating at least one builder, the cleaning compositions comprise at least about 1%, from about 3% to about 60% or even from about 5% to about 40% builder by weight of the cleaning composition. Builders include, but are not limited to, the alkali metal, ammonium and alkanolammonium salts of polyphosphates, alkali metal silicates, alkaline earth and alkali metal carbonates, aluminosilicates, polycarboxylate compounds, ether hydroxypolycarboxylates, copolymers of maleic anhydride with ethylene or vinyl methyl ether, 1, 3, 5-trihydroxy benzene-2, 4, 6-trisulphonic acid, and carboxymethyloxysuccinic acid, the various alkali metal, ammonium and substituted ammonium salts of polyacetic acids such as ethylenediamine tetraacetic acid and nitrilotriacetic acid, as well as polycarboxylates such as mellitic acid, succinic acid, citric acid, oxydisuccinic acid, polymaleic acid, benzene 1,3,5-tricarboxylic acid, carboxymethyloxysuccinic acid, and soluble salts thereof. Indeed, it is contemplated that any suitable builder will find use in various embodiments of the present invention.

[0226] In some embodiments, the builders form water-soluble hardness ion complexes (e.g., sequestering builders), such as citrates and polyphosphates (e.g., sodium tripolyphosphate and sodium tripolyphospate hexahydrate, potassium tripolyphosphate, and mixed sodium and potassium tripolyphosphate, etc.). It is contemplated that any suitable builder will find use in the present invention, including those known in the art (See e.g., EP 2 100 949).

[0227] In some embodiments, builders for use herein include phosphate builders and non-phosphate builders. In some embodiments, the builder is a phosphate builder. In some embodiments, the builder is a non-phosphate builder. If present, builders are used in a level of from 0.1% to 80%, or from 5 to 60%, or from 10 to 50% by weight of the composition. In some embodiments the product comprises a mixture of phosphate and non-phosphate builders. Suitable phosphate builders include mono-phosphates, di-phosphates, tri-polyphosphates or oligomeric-poylphosphates, including the alkali metal salts of these compounds, including the sodium salts. In some embodiments, a builder can be sodium tripolyphosphate (STPP). Additionally, the composition can comprise carbonate and/or citrate, preferably citrate that helps to achieve a neutral pH composition of the invention. Other suitable non-phosphate builders include homopolymers and copolymers of polycarboxylic acids and their partially or completely neutralized salts, monomeric polycarboxylic acids and hydroxycarboxylic acids and their salts. In some embodiments, salts of the above mentioned compounds include the ammonium and/or alkali metal salts, i.e. the lithium, sodium, and potassium salts, including sodium salts. Suitable polycarboxylic acids include acyclic, alicyclic, hetero-cyclic and aromatic carboxylic acids, wherein in some embodiments, they can contain at least two carboxyl groups which are in each case separated from one another by, in some instances, no more than two carbon atoms.

[0228] In some embodiments, the cleaning compositions of the present invention contain at least one chelating agent. Suitable chelating agents include, but are not limited to copper, iron and/or manganese chelating agents and mixtures thereof. In embodiments in which at least one chelating agent is used, the cleaning compositions of the present invention comprise from about 0.1% to about 15% or even from about 3.0% to about 10% chelating agent by weight of the subject cleaning composition.

[0229] In some still further embodiments, the cleaning compositions provided herein contain at least one deposition aid. Suitable deposition aids include, but are not limited to, polyethylene glycol, polypropylene glycol, polycarboxylate, soil release polymers such as polytelephthalic acid, clays such as kaolinite, montmorillonite, atapulgite, illite, bentonite, halloysite, and mixtures thereof.

[0230] As indicated herein, in some embodiments, anti-redeposition agents find use in some embodiments of the present invention. In some embodiments, non-ionic surfactants find use. For example, in automatic dishwashing embodiments, non-ionic surfactants find use for surface modification purposes, in particular for sheeting, to avoid filming and spotting and to improve shine. These non-ionic surfactants also find use in preventing the re-deposition of soils. In some embodiments, the anti-redeposition agent is a non-ionic surfactant as known in the art (See e.g., EP 2 100 949). In some embodiments, the non-ionic surfactant can be ethoxylated nonionic surfactants, epoxy-capped poly(oxyalkylated) alcohols and amine oxides surfactants.

[0231] In some embodiments, the cleaning compositions of the present invention include one or more dye transfer inhibiting agents. Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. In embodiments in which at least one dye transfer inhibiting agent is used, the cleaning compositions of the present invention comprise from about 0.0001% to about 10%, from about 0.01% to about 5%, or even from about 0.1% to about 3% by weight of the cleaning composition.

[0232] In some embodiments, silicates are included within the compositions of the present invention. In some such embodiments, sodium silicates (e.g., sodium disilicate, sodium metasilicate, and crystalline phyllosilicates) find use. In some embodiments, silicates are present at a level of from about 1% to about 20%. In some embodiments, silicates are present at a level of from about 5% to about 15% by weight of the composition.

[0233] In some still additional embodiments, the cleaning compositions of the present invention also contain dispersants. Suitable water-soluble organic materials include, but are not limited to the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.

[0234] In some further embodiments, the enzymes used in the cleaning compositions are stabilized by any suitable technique. In some embodiments, the enzymes employed herein are stabilized by the presence of water-soluble sources of calcium and/or magnesium ions in the finished compositions that provide such ions to the enzymes. In some embodiments, the enzyme stabilizers include oligosaccharides, polysaccharides, and inorganic divalent metal salts, including alkaline earth metals, such as calcium salts, such as calcium formate. It is contemplated that various techniques for enzyme stabilization will find use in the present invention. For example, in some embodiments, the enzymes employed herein are stabilized by the presence of water-soluble sources of zinc (II), calcium (II) and/or magnesium (II) ions in the finished compositions that provide such ions to the enzymes, as well as other metal ions (e.g., barium (II), scandium (II), iron (II), manganese (II), aluminum (III), Tin (II), cobalt (II), copper (II), nickel (II), and oxovanadium (IV). Chlorides and sulfates also find use in some embodiments of the present invention. Examples of suitable oligosaccharides and polysaccharides (e.g., dextrins) are known in the art (See e.g., WO 07/145964). In some embodiments, reversible protease inhibitors also find use, such as boron-containing compounds (e.g., borate, 4-formyl phenyl boronic acid) and/or a tripeptide aldehyde find use to further improve stability, as desired.

[0235] In some embodiments, bleaches, bleach activators and/or bleach catalysts are present in the compositions of the present invention. In some embodiments, the cleaning compositions of the present invention comprise inorganic and/or organic bleaching compound(s). Inorganic bleaches include, but are not limited to perhydrate salts (e.g., perborate, percarbonate, perphosphate, persulfate, and persilicate salts). In some embodiments, inorganic perhydrate salts are alkali metal salts. In some embodiments, inorganic perhydrate salts are included as the crystalline solid, without additional protection, although in some other embodiments, the salt is coated. Any suitable salt known in the art finds use in the present invention (See e.g., EP 2 100 949).

[0236] In some embodiments, bleach activators are used in the compositions of the present invention. Bleach activators are typically organic peracid precursors that enhance the bleaching action in the course of cleaning at temperatures of 60 C. and below. Bleach activators suitable for use herein include compounds which, under perhydrolysis conditions, give aliphatic peroxoycarboxylic acids having preferably from about 1 to about 10 carbon atoms, in particular from about 2 to about 4 carbon atoms, and/or optionally substituted perbenzoic acid. Additional bleach activators are known in the art and find use in the present invention (See e.g., EP 2 100 949).

[0237] In addition, in some embodiments and as further described herein, the cleaning compositions of the present invention further comprise at least one bleach catalyst. In some embodiments, the manganese triazacyclononane and related complexes find use, as well as cobalt, copper, manganese, and iron complexes. Additional bleach catalysts find use in the present invention (See e.g., U.S. Pat. Nos. 4,246,612, 5,227,084, 4,810410, WO 99/06521, and EP 2 100 949).

[0238] In some embodiments, the cleaning compositions of the present invention contain one or more catalytic metal complexes. In some embodiments, a metal-containing bleach catalyst finds use. In some embodiments, the metal bleach catalyst comprises a catalyst system comprising a transition metal cation of defined bleach catalytic activity, (e.g., copper, iron, titanium, ruthenium, tungsten, molybdenum, or manganese cations), an auxiliary metal cation having little or no bleach catalytic activity (e.g., zinc or aluminum cations), and a sequestrate having defined stability constants for the catalytic and auxiliary metal cations, particularly ethylenediaminetetraacetic acid, ethylenediaminetetra (methylenephosphonic acid) and water-soluble salts thereof are used (See e.g., U.S. Pat. No. 4,430,243). In some embodiments, the cleaning compositions of the present invention are catalyzed by means of a manganese compound. Such compounds and levels of use are well known in the art (See e.g., U.S. Pat. No. 5,576,282). In additional embodiments, cobalt bleach catalysts find use in the cleaning compositions of the present invention. Various cobalt bleach catalysts are known in the art (See e.g., U.S. Pat. Nos. 5,597,936 and 5,595,967) and are readily prepared by known procedures.

[0239] In some additional embodiments, the cleaning compositions of the present invention include a transition metal complex of a macropolycyclic rigid ligand (MRL). As a practical matter, and not by way of limitation, in some embodiments, the compositions and cleaning processes provided by the present invention are adjusted to provide on the order of at least one part per hundred million of the active MRL species in the aqueous washing medium, and in some embodiments, provide from about 0.005 ppm to about 25 ppm, more preferably from about 0.05 ppm to about 10 ppm, and most preferably from about 0.1 ppm to about 5 ppm, of the MRL in the wash liquor.

[0240] In some embodiments, transition-metals in the instant transition-metal bleach catalyst include, but are not limited to manganese, iron and chromium. MRLs also include, but are not limited to special ultra-rigid ligands that are cross-bridged (e.g., 5,12-diethyl-1,5,8,12-tetraazabicyclo[6.6.2]hexadecane). Suitable transition metal MRLs are readily prepared by known procedures (See e.g., WO 2000/32601, and U.S. Pat. No. 6,225,464).

[0241] In some embodiments, the cleaning compositions of the present invention comprise metal care agents. Metal care agents find use in preventing and/or reducing the tarnishing, corrosion, and/or oxidation of metals, including aluminum, stainless steel, and non-ferrous metals (e.g., silver and copper). Suitable metal care agents include those described in EP 2 100 949, WO 9426860 and WO 94/26859). In some embodiments, the metal care agent is a zinc salt. In some further embodiments, the cleaning compositions of the present invention comprise from about 0.1% to about 5% by weight of one or more metal care agent.

[0242] In some embodiments, the cleaning composition is a high density liquid (HDL) composition having a variant metalloprotease polypeptide protease. The HDL liquid laundry detergent can comprise a detersive surfactant (10%-40%) comprising anionic detersive surfactant (selected from a group of linear or branched or random chain, substituted or unsubstituted alkyl sulphates, alkyl sulphonates, alkyl alkoxylated sulphate, alkyl phosphates, alkyl phosphonates, alkyl carboxylates, and/or mixtures thereof); and optionally non-ionic surfactant (selected from a group of linear or branched or random chain, substituted or unsubstituted alkyl alkoxylated alcohol, for example a C.sub.8-C.sub.18 alkyl ethoxylated alcohol and/or C.sub.6-C.sub.12 alkyl phenol alkoxylates), optionally wherein the weight ratio of anionic detersive surfactant (with a hydrophilic index (HIc) of from 6.0 to 9) to non-ionic detersive surfactant is greater than 1:1.

[0243] The composition can comprise optionally, a surfactancy boosting polymer consisting of amphiphilic alkoxylated grease cleaning polymers (selected from a group of alkoxylated polymers having branched hydrophilic and hydrophobic properties, such as alkoxylated polyalkylenimines in the range of 0.05 wt %-10 wt %) and/or random graft polymers (typically comprising of hydrophilic backbone comprising monomers selected from the group consisting of: unsaturated C.sub.1-C.sub.6 carboxylic acids, ethers, alcohols, aldehydes, ketones, esters, sugar units, alkoxy units, maleic anhydride, saturated polyalcohols such as glycerol, and mixtures thereof; and hydrophobic side chain(s) selected from the group consisting of: C.sub.4-C.sub.25 alkyl group, polypropylene, polybutylene, vinyl ester of a saturated CC.sub.6 mono-carboxylic acid, C.sub.1-C.sub.6 alkyl ester of acrylic or methacrylic acid, and mixtures thereof.

[0244] The composition can comprise additional polymers such as soil release polymers (include anionically end-capped polyesters, for example SRP1, polymers comprising at least one monomer unit selected from saccharide, dicarboxylic acid, polyol and combinations thereof, in random or block configuration, ethylene terephthalate-based polymers and co-polymers thereof in random or block configuration, for example Repel-o-tex SF, SF-2 and SRP6, Texcare SRA100, SRA300, SRN100, SRN170, SRN240, SRN300 and SRN325, Marloquest SL), anti-redeposition polymers (0.1 wt % to 10 wt %, include carboxylate polymers, such as polymers comprising at least one monomer selected from acrylic acid, maleic acid (or maleic anhydride), fumaric acid, itaconic acid, aconitic acid, mesaconic acid, citraconic acid, methylenemalonic acid, and any mixture thereof, vinylpyrrolidone homopolymer, and/or polyethylene glycol, molecular weight in the range of from 500 to 100,000 Da); cellulosic polymer (including those selected from alkyl cellulose, alkyl alkoxyalkyl cellulose, carboxyalkyl cellulose, alkyl carboxyalkyl cellulose examples of which include carboxymethyl cellulose, methyl cellulose, methyl hydroxyethyl cellulose, methyl carboxymethyl cellulose, and mixtures thereof) and polymeric carboxylate (such as maleate/acrylate random copolymer or polyacrylate homopolymer).

[0245] The composition can further comprise saturated or unsaturated fatty acid, preferably saturated or unsaturated C.sub.12-C.sub.24 fatty acid (0 wt % to 10 wt %); deposition aids (examples for which include polysaccharides, preferably cellulosic polymers, poly diallyl dimethyl ammonium halides (DADMAC), and co-polymers of DAD MAC with vinyl pyrrolidone, acrylamides, imidazoles, imidazolinium halides, and mixtures thereof, in random or block configuration, cationic guar gum, cationic cellulose such as cationic hydoxyethyl cellulose, cationic starch, cationic polyacylamides, and mixtures thereof.

[0246] The composition can further comprise dye transfer inhibiting agents examples of which include manganese phthalocyanine, peroxidases, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles and/or mixtures thereof; chelating agents examples of which include ethylene-diamine-tetraacetic acid (EDTA); diethylene triamine penta methylene phosphonic acid (DTPMP); hydroxy-ethane diphosphonic acid (HEDP); ethylenediamine N,N-disuccinic acid (EDDS); methyl glycine diacetic acid (MGDA); diethylene triamine penta acetic acid (DTPA); propylene diamine tetracetic acid (PDT A); 2-hydroxypyridine-N-oxide (HPNO); or methyl glycine diacetic acid (MGDA); glutamic acid N,N-diacetic acid (N,N-dicarboxymethyl glutamic acid tetrasodium salt (GLDA); nitrilotriacetic acid (NTA); 4,5-dihydroxy-m-benzenedisulfonic acid; citric acid and any salts thereof, N-hydroxyethylethylenediaminetri-acetic acid (HEDTA), triethylenetetraaminehexaacetic acid (TTHA), N-hydroxyethyliminodiacetic acid (HEIDA), dihydroxyethylglycine (DHEG), ethylenediaminetetrapropionic acid (EDTP) and derivatives thereof.

[0247] The composition can further comprise enzymes (0.01 wt % active enzyme to 0.03 wt % active enzyme) selected from a group of acyl transferases, alpha-amylases, beta-amylases, alpha-galactosidases, arabinosidases, aryl esterases, beta-galactosidases, carrageenases, catalases, cellobiohydrolases, cellulases, chondroitinases, cutinases, endo-beta-1, 4-glucanases, endo-beta-mannanases, esterases, exo-mannanases, galactanases, glucoamylases, hemicellulases, hyaluronidases, keratinases, laccases, lactases, ligninases, lipases, lipoxygenases, mannanases, oxidases, pectate lyases, pectin acetyl esterases, pectinases, pentosanases, peroxidases, phenoloxidases, phosphatases, phospholipases, phytases, polygalacturonases, proteases, pullulanases, reductases, rhamnogalacturonases, beta-glucanases, tannases, transglutaminases, xylan acetyl-esterases, xylanases, xyloglucanases, and xylosidases, and any mixture thereof. The composition may comprise an enzyme stabilizer (examples of which include polyols such as propylene glycol or glycerol, sugar or sugar alcohol, lactic acid, reversible protease inhibitor, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid).

[0248] The composition can further comprise silicone or fatty-acid based suds suppressors; heuing dyes, calcium and magnesium cations, visual signaling ingredients, anti-foam (0.001 wt % to about 4.0 wt %), and/or structurant/thickener (0.01 wt % to 5 wt %, selected from the group consisting of diglycerides and triglycerides, ethylene glycol distearate, microcrystalline cellulose, cellulose based materials, microfiber cellulose, biopolymers, xanthan gum, gellan gum, and mixtures thereof).

[0249] Suitable detersive surfactants also include cationic detersive surfactants (selected from a group of alkyl pyridinium compounds, alkyl quarternary ammonium compounds, alkyl quarternary phosphonium compounds, alkyl ternary sulphonium compounds, and/or mixtures thereof); zwitterionic and/or amphoteric detersive surfactants (selected from a group of alkanolamine sulpho-betaines); ampholytic surfactants; semi-polar non-ionic surfactants and mixtures thereof.

[0250] The composition can be any liquid form, for example a liquid or gel form, or any combination thereof. The composition may be in any unit dose form, for example a pouch.

[0251] In some embodiments, the cleaning composition is a high density powder (HDD) composition having a variant metalloprotease polypeptide protease. The HDD powder laundry detergent can comprise a detersive surfactant including anionic detersive surfactants (selected from a group of linear or branched or random chain, substituted or unsubstituted alkyl sulphates, alkyl sulphonates, alkyl alkoxylated sulphate, alkyl phosphates, alkyl phosphonates, alkyl carboxylates and/or mixtures thereof), non-ionic detersive surfactant (selected from a group of linear or branched or random chain, substituted or unsubstituted C.sub.8-Cis alkyl ethoxylates, and/or C.sub.6-C.sub.12 alkyl phenol alkoxylates), cationic detersive surfactants (selected from a group of alkyl pyridinium compounds, alkyl quaternary ammonium compounds, alkyl quaternary phosphonium compounds, alkyl ternary sulphonium compounds, and mixtures thereof), zwitterionic and/or amphoteric detersive surfactants (selected from a group of alkanolamine sulpho-betaines); ampholytic surfactants; semi-polar non-ionic surfactants and mixtures thereof; builders (phosphate free builders [for example zeolite builders examples of which include zeolite A, zeolite X, zeolite P and zeolite MAP in the range of 0 wt % to less than 10 wt %]; phosphate builders [examples of which include sodium tri-polyphosphate in the range of 0 wt % to less than 10 wt %]; citric acid, citrate salts and nitrilotriacetic acid or salt thereof in the range of less than 15 wt %); silicate salt (sodium or potassium silicate or sodium meta-silicate in the range of 0 wt % to less than 10 wt %, or layered silicate (SKS-6)); carbonate salt (sodium carbonate and/or sodium bicarbonate in the range of 0 wt % to less than 10 wt %); and bleaching agents (photobleaches, examples of which include sulfonated zinc phthalocyanines, sulfonated aluminum phthalocyanines, xanthenes dyes, and mixtures thereof; hydrophobic or hydrophilic bleach activators (examples of which include dodecanoyl oxybenzene sulfonate, decanoyl oxybenzene sulfonate, decanoyl oxybenzoic acid or salts thereof, 3,5,5-trimethy hexanoyl oxybenzene sulfonate, tetraacetyl ethylene diamine-TAED, and nonanoyloxybenzene sulfonate-NOB S, nitrile quats, and mixtures thereof; hydrogen peroxide; sources of hydrogen peroxide (inorganic perhydrate salts examples of which include mono or tetra hydrate sodium salt of perborate, percarbonate, persulfate, perphosphate, or persilicate); preformed hydrophilic and/or hydrophobic peracids (selected from a group consisting of percarboxylic acids and salts, percarbonic acids and salts, perimidic acids and salts, peroxymonosulfuric acids and salts) & mixtures thereof and/or bleach catalyst (such as imine bleach boosters examples of which include iminium cations and polyions; iminium zwitterions; modified amines; modified amine oxides; N-sulphonyl imines; N-phosphonyl imines; N-acyl imines; thiadiazole dioxides; perfluoroimines; cyclic sugar ketones and mixtures thereof; metal-containing bleach catalyst for example copper, iron, titanium, ruthenium, tungsten, molybdenum, or manganese cations along with an auxiliary metal cations such as zinc or aluminum and a sequestrate such as ethylenediaminetetraacetic acid, ethylenediaminetetra(methylenephos-phonic acid) and water-soluble salts thereof).

[0252] The composition can further comprise enzymes selected from a group of acyl transferases, alpha-amylases, beta-amylases, alpha-galactosidases, arabinosidases, aryl esterases, beta-galactosidases, carrageenases, catalases, cellobiohydrolases, cellulases, chondroitinases, cutinases, endo-beta-1, 4-glucanases, endo-beta-mannanases, esterases, exo-mannanases, galactanases, glucoamylases, glucose oxidases, hemicellulases, hyaluronidases, keratinases, laccases, lactases, ligninases, lipases, lipoxygenases, mannanases, oxidases, pectate lyases, pectin acetyl esterases, pectinases, pentosanases, perhydrolases, peroxidases, phenoloxidases, phosphatases, phospholipases, phytases, polygalacturonases, proteases, pullulanases, reductases, rhamnogalacturonases, beta-glucanases, tannases, transglutaminases, xylan acetyl-esterases, xylanases, xyloglucanases, and xylosidases and any mixture thereof.

[0253] The composition can further comprise additional detergent ingredients including perfume microcapsules, starch encapsulated perfume accord, hueing agents, additional polymers including fabric integrity and cationic polymers, dye lock ingredients, fabric-softening agents, brighteners (for example C.I. Fluorescent brighteners), flocculating agents, chelating agents, alkoxylated polyamines, fabric deposition aids, and/or cyclodextrin.

[0254] In some embodiments, the cleaning composition is an automatic dishwashing (ADW) detergent composition having a metalloprotease of the present invention. The ADW detergent composition can comprise two or more non-ionic surfactants selected from a group of ethoxylated non-ionic surfactants, alcohol alkoxylated surfactants, epoxy-capped poly(oxyalkylated) alcohols, or amine oxide surfactants present in amounts from 0 to 10% by weight; builders in the range of 5-60% comprising either phosphate (mono-phosphates, di-phosphates, tri-polyphosphates or oligomeric-poylphosphates, preferred sodium tripolyphosphate-STPP or phosphate-free builders [amino acid based compounds, examples of which include MGDA (methyl-glycine-diacetic acid), and salts and derivatives thereof, GLDA (glutamic-N,Ndiacetic acid) and salts and derivatives thereof, IDS (iminodisuccinic acid) and salts and derivatives thereof, carboxy methyl inulin and salts and derivatives thereof and mixtures thereof, nitrilotriacetic acid (NTA), diethylene triamine penta acetic acid (DTPA), B-alaninediacetic acid (B-ADA) and their salts], homopolymers and copolymers of polycarboxylic acids and their partially or completely neutralized salts, monomeric polycarboxylic acids and hydroxycarboxylic acids and their salts in the range of 0.5% to 50% by weight; sulfonated/carboxylated polymers (provide dimensional stability to the product) in the range of about 0.1% to about 50% by weight; drying aids in the range of about 0.1% to about 10% by weight (selected from polyesters, especially anionic polyesters optionally together with further monomers with 3 to 6 functionalities which are conducive to polycondensation, specifically acid, alcohol or ester functionalities, polycarbonate-, polyurethane- and/or polyurea-polyorganosiloxane compounds or precursor compounds thereof of the reactive cyclic carbonate and urea type); silicates in the range from about 1% to about 20% by weight (sodium or potassium silicates for example sodium disilicate, sodium meta-silicate and crystalline phyllosilicates); bleach-inorganic (for example perhydrate salts such as perborate, percarbonate, perphosphate, persulfate and persilicate salts) and organic (for example organic peroxyacids including diacyl and tetraacylperoxides, especially diperoxydodecanedioc acid, diperoxytetradecanedioc acid, and diperoxyhexadecanedioc acid); bleach activators-organic peracid precursors in the range from about 0.1% to about 10% by weight; bleach catalysts (selected from manganese triazacyclononane and related complexes, Co, Cu, Mn and Fe bispyridylamine and related complexes, and pentamine acetate cobalt(III) and related complexes); metal care agents in the range from about 0.1% to 5% by weight (selected from benzatriazoles, metal salts and complexes, and/or silicates); enzymes in the range from about 0.01 to 5.0 mg of active enzyme per gram of automatic dishwashing detergent composition (acyl transferases, alpha-amylases, beta-amylases, alpha-galactosidases, arabinosidases, aryl esterases, beta-galactosidases, carrageenases, catalases, cellobiohydrolases, cellulases, chondroitinases, cutinases, endo-beta-1, 4-glucanases, endo-beta-mannanases, esterases, exo-mannanases, galactanases, glucoamylases, hemicellulases, hyaluronidases, keratinases, laccases, lactases, ligninases, lipases, lipoxygenases, mannanases, oxidases, pectate lyases, pectin acetyl esterases, pectinases, pentosanases, peroxidases, phenoloxidases, phosphatases, phospholipases, phytases, polygalacturonases, proteases, pullulanases, reductases, rhamnogalacturonases, beta-glucanases, tannases, transglutaminases, xylan acetyl-esterases, xylanases, xyloglucanases, and xylosidases, and any mixture thereof); and enzyme stabilizer components (selected from oligosaccharides, polysaccharides and inorganic divalent metal salts).

[0255] Representative detergent formulations that beneficially include a metalloprotease polypeptide of the present invention include the detergent formulations found in WO2013063460, pages 78-152, and in particular the tables of pages 94 to 152 are hereby incorporated by reference. The metalloproteases are normally incorporated into the detergent composition at a level of from 0.000001% to 5% of enzyme protein by weight of the composition, or from 0.00001% to 2%, or from 0.0001% to 1%, or from 0.001% to 0.75% of enzyme protein by weight of the composition.

Metalloprotease Polypeptides of the Present Invention for Use in Animal Feed

[0256] In a further aspect of the invention, the metalloprotease polypeptides of the present invention can be used as a component of an animal feed composition, animal feed additive and/or pet food comprising a metalloprotease and variants thereof. The present invention further relates to a method for preparing such an animal feed composition, animal feed additive composition and/or pet food comprising mixing the metalloprotease polypeptide with one or more animal feed ingredients and/or animal feed additive ingredients and/or pet food ingredients. Furthermore, the present invention relates to the use of the metalloprotease polypeptide in the preparation of an animal feed composition and/or animal feed additive composition and/or pet food.

[0257] The term animal includes all non-ruminant and ruminant animals. In a particular embodiment, the animal is a non-ruminant animal, such as a horse and a mono-gastric animal. Examples of mono-gastric animals include, but are not limited to, pigs and swine, such as piglets, growing pigs, sows; poultry such as turkeys, ducks, chicken, broiler chicks, layers; fish such as salmon, trout, tilapia, catfish and carps; and crustaceans such as shrimps and prawns. In a further embodiment the animal is a ruminant animal including, but not limited to, cattle, young calves, goats, sheep, giraffes, bison, moose, elk, yaks, water buffalo, deer, camels, alpacas, llamas, antelope, pronghorn and nilgai.

[0258] In the present context, it is intended that the term pet food is understood to mean a food for a household animal such as, but not limited to, dogs, cats, gerbils, hamsters, chinchillas, fancy rats, guinea pigs; avian pets, such as canaries, parakeets, and parrots; reptile pets, such as turtles, lizards and snakes; and aquatic pets, such as tropical fish and frogs.

[0259] The terms animal feed composition, feedstuff and fodder are used interchangeably and can comprise one or more feed materials selected from the group comprising a) cereals, such as small grains (e.g., wheat, barley, rye, oats and combinations thereof) and/or large grains such as maize or sorghum; b) by products from cereals, such as corn gluten meal, Distillers Dried Grain Solubles (DDGS) (particularly corn based Distillers Dried Grain Solubles (cDDGS), wheat bran, wheat middlings, wheat shorts, rice bran, rice hulls, oat hulls, palm kernel, and citrus pulp; c) protein obtained from sources such as soya, sunflower, peanut, lupin, peas, fava beans, cotton, canola, fish meal, dried plasma protein, meat and bone meal, potato protein, whey, copra, sesame; d) oils and fats obtained from vegetable and animal sources; e) minerals and vitamins.

Metalloprotease Polypeptides of the Present Invention for Use in Textile Desizing

[0260] Also contemplated are compositions and methods of treating fabrics (e.g., to desize a textile) using a metalloprotease polypeptide of the present invention. Fabric-treating methods are well known in the art (see, e.g., U.S. Pat. No. 6,077,316). For example, the feel and appearance of a fabric can be improved by a method comprising contacting the fabric with a metalloprotease in a solution. The fabric can be treated with the solution under pressure.

[0261] A metalloprotease of the present invention can be applied during or after the weaving of a textile, or during the desizing stage, or one or more additional fabric processing steps. During the weaving of textiles, the threads are exposed to considerable mechanical strain. Prior to weaving on mechanical looms, warp yarns are often coated with sizing starch or starch derivatives to increase their tensile strength and to prevent breaking. A metalloprotease of the present invention can be applied during or after the weaving to remove these sizing starch or starch derivatives. After weaving, the metalloprotease can be used to remove the size coating before further processing the fabric to ensure a homogeneous and wash-proof result.

[0262] A metalloprotease of the present invention can be used alone or with other desizing chemical reagents and/or desizing enzymes to desize fabrics, including cotton-containing fabrics, as detergent additives, e.g., in aqueous compositions. An amylase also can be used in compositions and methods for producing a stonewashed look on indigo-dyed denim fabric and garments. For the manufacture of clothes, the fabric can be cut and sewn into clothes or garments, which are afterwards finished. In particular, for the manufacture of denim jeans, different enzymatic finishing methods have been developed. The finishing of denim garment normally is initiated with an enzymatic desizing step, during which garments are subjected to the action of proteolytic enzymes to provide softness to the fabric and make the cotton more accessible to the subsequent enzymatic finishing steps. The metalloprotease can be used in methods of finishing denim garments (e.g., a bio-stoning process), enzymatic desizing and providing softness to fabrics, and/or finishing process.

Metalloprotease Polypeptides of the Present Invention for Use in Paper Pulp Bleaching

[0263] The metalloprotease polypeptides described herein find further use in the enzyme aided bleaching of paper pulps such as chemical pulps, semi-chemical pulps, kraft pulps, mechanical pulps or pulps prepared by the sulfite method. In general terms, paper pulps are incubated with a metalloprotease polypeptide of the present invention under conditions suitable for bleaching the paper pulp.

[0264] In some embodiments, the pulps are chlorine free pulps bleached with oxygen, ozone, peroxide or peroxyacids. In some embodiments, the metalloprotease polypeptides are used in enzyme aided bleaching of pulps produced by modified or continuous pulping methods that exhibit low lignin contents. In some other embodiments, the metalloprotease polypeptides are applied alone or preferably in combination with xylanase and/or endoglucanase and/or alpha-galactosidase and/or cellobiohydrolase enzymes.

Metalloprotease Polypeptides of the Present Invention for Use in Protein Degradation

[0265] The metalloprotease polypeptides described herein find further use in the enzyme aided removal of proteins from animals and their subsequent degradation or disposal, such as feathers, skin, hair, hide, and the like. In some instances, immersion of the animal carcass in a solution comprising a metalloprotease polypeptide of the present invention can act to protect the skin from damage in comparison to the traditional immersion in scalding water or the defeathering process. In one embodiment, feathers can be sprayed with an isolated metalloprotase polypeptide of the present invention under conditions suitable for digesting or initiating degradation of the plumage. In some embodiments, a metalloprotease of the present invention can be used, as above, in combination with an oxidizing agent.

[0266] In some embodiments, removal of the oil or fat associated with raw feathers is assisted by using a metalloprotease polypeptide of the present invention. In some embodiments, the metalloprotease polypeptides are used in compositions for cleaning the feathers as well as to sanitize and partially dehydrate the fibers. In some other embodiments, the metalloprotease polypeptides are applied in a wash solution in combination with 95% ethanol or other polar organic solvent with or without a surfactant at about 0.5% (v/v).

[0267] In yet other embodiments, the disclosed metalloprotease polypeptides find use in recovering protein from plumage. In some embodiments, the recovered protein can be subsequently used in animal or fish feed.

Metalloprotease Polypeptides of the Present Invention for Use in Tissue Debridement

[0268] The metalloprotease polypeptides described herein find further use in the enzyme aided debridement of tissue. This involves the removal of dead or damaged tissue, for example, removal from wounds to aid in healing.

Metalloprotease Polypeptides of the Present Invention for Use in Tissue Culture

[0269] The metalloprotease polypeptides described herein find further use in tissue culture. In particular, metalloproteases of the present invention can be used to suspend or resuspend cells adherent to a cell culture wall, such as during the process of harvesting cells. Metalloproteases of the present invention can be used to cleave protein bonds between cultured cells and the dish, allowing cells to become suspended in solution.

Metalloprotease Polypeptides of the Present Invention for Use in Leather Processing

[0270] The metalloprotease polypeptides described herein find further use in leather processing by removing hair from animal hides, soaking, degreasing, or bating, which is a process involving degradation of non-structural proteins during leather making.

EXPERIMENTAL

[0271] The claimed invention is described in further detail in the following examples which are not in any way intended to limit the scope of the invention as claimed.

Example 1

Crystallization and Structure Determination of PehPro1 Metalloprotease

[0272] The metalloprotease PehPro1, encoded by a Paenibacillus ehimensis strain was crystallized using the hanging drop method from a solution of protein stock at a concentration of 27.9 mg/mL in 20 mM Tris pH 8.5+0.10M Sodium chloride+1 mM Calcium chloride. Aliquots of 2 L of the protein stock and 2 L of the crystallization solution were mixed on a plastic coverslip and inverted and sealed on a chamber containing 15-25% Polyethylene Glycol 8000+50 mM Potassium phosphate monobasic+0.10M HEPES pH 7.5 in a Linbro 64 culture plate.

[0273] Crystals grew in the space group C 2 2 2.sub.1 with unit cell dimensions; a=58.814 , b=194.346 , and c=138.355 . Data were collected on native crystal to 2.79 resolution and the structure of PehPro1 was determined by molecular replacement using a related protein (pdb ID 1ESP) as the phasing model. The statistics of data collected are presented in Table 1.1.

TABLE-US-00002 TABLE 1.1 Statistics of PehPro1 Data collection Wavelength 1.54 Space group C222 Molecules in asymmetric unit 2 Unit cell dimensions a = 58.81 , b = 194.35 and c = 138.36 Resolution 32.6 2.79 Unique reflections 19103 Multiplicity 17 (11*) Completeness 99.33% (92%*) R.sub.merge 0.08 (0.30*) I/.sub.I 17 (8*) *Value in parenthesis is that of the outermost shell of data

[0274] The model was fitted in the resulting electron density using the program COOT (Emsley, P et al Acta Cryst. D66 486-501 (2010)). After fitting and refitting adjustments, the coordinates were refined using the REFMAC program with standard defaults in the CCP4 software suite. The statistics of the current model are presented in Table 1.2.

TABLE-US-00003 TABLE 1.2 Statistics of the refined model R work 0.19 R free 0.25 No. protein residues 304 No. atoms 4742 rmsd Bond lengths 0.013 rmsd bond angles 1.6

Example 2

PehPro1 Crystal Structure Details

[0275] The structure of PehPro1 consists of a dimer of two equivalent molecules. Electron density was available for residues 1-304 of each monomer. Each model was fitted to contiguous density. The overall dimer arrangement is presented in FIG. 1. The residues forming the active site regions include the catalytic residues; His135, Glu136, His139 and Glu159 (numbering based on PehPro1 mature sequence) forming the characteristic zinc metal binding site, along with other residues forming the substrate binding pocket are conserved between the PehPro1 and Thermolysin structures (Matthews, B. W., Weaver, L. H., Kester, W. R., The Conformation of Thermolysin, (1974) J. Biol. Chem. 249: 8030; Dahlquist, F. W., Long, J. W., Bigbee, W. L., Role of Calcium in the Thermal Stability of Thermolysin, (1976) Biochemistry 15: 1103).

[0276] The coordinates for this molecule are listed below.

TABLE-US-00004 ATOM 1 N ALA A 1 17.159 64.455 9.260 1.00 39.68 A N ATOM 2 CA ALA A 1 18.338 64.728 10.130 1.00 33.72 A C ATOM 3 CB ALA A 1 19.640 64.092 9.687 1.00 32.16 A C ATOM 4 C ALA A 1 17.839 63.991 11.323 1.00 30.98 A C ATOM 5 O ALA A 1 17.083 63.038 11.132 1.00 31.11 A O ATOM 6 N THR A 2 18.230 64.375 12.537 1.00 27.24 A N ATOM 7 CA THR A 2 17.655 63.718 13.709 1.00 23.73 A C ATOM 8 CB THR A 2 16.933 64.722 14.609 1.00 23.24 A C ATOM 9 OG1 THR A 2 16.035 65.475 13.800 1.00 23.09 A O ATOM 10 CG2 THR A 2 16.117 64.026 15.659 1.00 22.84 A C ATOM 11 C THR A 2 18.690 62.894 14.454 1.00 22.06 A C ATOM 12 O THR A 2 19.503 63.421 15.169 1.00 22.29 A O ATOM 13 N GLY A 3 18.652 61.581 14.259 1.00 21.36 A N ATOM 14 CA GLY A 3 19.512 60.660 14.981 1.00 20.30 A C ATOM 15 C GLY A 3 18.962 60.326 16.364 1.00 20.22 A C ATOM 16 O GLY A 3 17.744 60.439 16.667 1.00 18.32 A O ATOM 17 N THR A 4 19.885 59.870 17.199 1.00 20.55 A N ATOM 18 CA THR A 4 19.612 59.576 18.593 1.00 20.58 A C ATOM 19 CB THR A 4 19.948 60.825 19.426 1.00 20.39 A C ATOM 20 OG1 THR A 4 19.095 60.904 20.570 1.00 21.45 A O ATOM 21 CG2 THR A 4 21.404 60.866 19.797 1.00 20.52 A C ATOM 22 C THR A 4 20.371 58.290 18.979 1.00 20.82 A C ATOM 23 O THR A 4 21.362 57.946 18.344 1.00 20.84 A O ATOM 24 N GLY A 5 19.870 57.532 19.955 1.00 22.14 A N ATOM 25 CA GLY A 5 20.474 56.214 20.307 1.00 21.26 A C ATOM 26 C GLY A 5 19.683 55.446 21.353 1.00 21.65 A C ATOM 27 O GLY A 5 18.525 55.770 21.629 1.00 21.95 A O ATOM 28 N LYS A 6 20.293 54.433 21.958 1.00 23.22 A N ATOM 29 CA LYS A 6 19.599 53.661 22.999 1.00 23.98 A C ATOM 30 CB LYS A 6 20.501 53.316 24.191 1.00 26.75 A C ATOM 31 CG LYS A 6 21.062 54.545 24.928 1.00 31.43 A C ATOM 32 CD LYS A 6 21.426 54.362 26.429 1.00 34.80 A C ATOM 33 CE LYS A 6 22.314 53.151 26.767 1.00 37.30 A C ATOM 34 NZ LYS A 6 23.750 53.306 26.350 1.00 38.51 A N ATOM 35 C LYS A 6 19.019 52.412 22.379 1.00 21.52 A C ATOM 36 O LYS A 6 19.655 51.799 21.527 1.00 21.20 A O ATOM 37 N GLY A 7 17.806 52.049 22.801 1.00 19.41 A N ATOM 38 CA GLY A 7 17.124 50.843 22.311 1.00 17.91 A C ATOM 39 C GLY A 7 17.709 49.607 22.918 1.00 17.02 A C ATOM 40 O GLY A 7 18.733 49.657 23.599 1.00 17.62 A O ATOM 41 N VAL A 8 17.062 48.481 22.697 1.00 16.27 A N ATOM 42 CA VAL A 8 17.536 47.207 23.273 1.00 15.98 A C ATOM 43 CB VAL A 8 16.608 46.061 22.849 1.00 16.24 A C ATOM 44 CG1 VAL A 8 16.843 44.785 23.665 1.00 15.97 A C ATOM 45 CG2 VAL A 8 16.770 45.827 21.354 1.00 16.69 A C ATOM 46 C VAL A 8 17.580 47.271 24.800 1.00 15.88 A C ATOM 47 O VAL A 8 18.502 46.760 25.430 1.00 14.79 A O ATOM 48 N LEU A 9 16.564 47.928 25.366 1.00 15.93 A N ATOM 49 CA LEU A 9 16.361 48.015 26.814 1.00 15.86 A C ATOM 50 CB LEU A 9 14.852 48.093 27.086 1.00 15.92 A C ATOM 51 CG LEU A 9 14.126 46.852 27.579 1.00 15.70 A C ATOM 52 CD1 LEU A 9 14.696 45.602 26.965 1.00 15.39 A C ATOM 53 CD2 LEU A 9 12.636 46.998 27.283 1.00 15.95 A C ATOM 54 C LEU A 9 17.023 49.217 27.493 1.00 15.36 A C ATOM 55 O LEU A 9 16.577 49.596 28.592 1.00 15.14 A O ATOM 56 N GLY A 10 18.010 49.842 26.831 1.00 14.23 A N ATOM 57 CA GLY A 10 18.771 50.970 27.404 1.00 13.71 A C ATOM 58 C GLY A 10 18.144 52.351 27.326 1.00 13.72 A C ATOM 59 O GLY A 10 18.738 53.341 27.753 1.00 13.58 A O ATOM 60 N ASP A 11 16.945 52.433 26.768 1.00 13.97 A N ATOM 61 CA ASP A 11 16.223 53.677 26.721 1.00 14.03 A C ATOM 62 CB ASP A 11 14.715 53.447 26.716 1.00 14.10 A C ATOM 63 CG ASP A 11 14.243 52.431 25.655 1.00 14.65 A C ATOM 64 OD1 ASP A 11 14.971 51.470 25.307 1.00 14.45 A O ATOM 65 OD2 ASP A 11 13.091 52.593 25.195 1.00 15.19 A O ATOM 66 C ASP A 11 16.647 54.501 25.529 1.00 14.72 A C ATOM 67 O ASP A 11 16.756 53.984 24.433 1.00 14.88 A O ATOM 68 N THR A 12 16.844 55.802 25.763 1.00 15.81 A N ATOM 69 CA THR A 12 17.317 56.754 24.758 1.00 15.88 A C ATOM 70 CB THR A 12 17.962 57.966 25.452 1.00 15.68 A C ATOM 71 OG1 THR A 12 19.275 57.606 25.914 1.00 15.63 A O ATOM 72 CG2 THR A 12 18.054 59.155 24.518 1.00 15.69 A C ATOM 73 C THR A 12 16.171 57.235 23.884 1.00 16.48 A C ATOM 74 O THR A 12 15.136 57.569 24.392 1.00 16.69 A O ATOM 75 N LYS A 13 16.380 57.296 22.572 1.00 17.65 A N ATOM 76 CA LYS A 13 15.333 57.703 21.603 1.00 18.19 A C ATOM 77 CB LYS A 13 14.788 56.474 20.861 1.00 19.32 A C ATOM 78 CG LYS A 13 13.717 55.737 21.568 1.00 20.03 A C ATOM 79 CD LYS A 13 13.757 54.265 21.245 1.00 20.24 A C ATOM 80 CE LYS A 13 12.730 53.620 22.168 1.00 21.08 A C ATOM 81 NZ LYS A 13 13.089 52.212 22.399 1.00 21.72 A N ATOM 82 C LYS A 13 15.855 58.583 20.482 1.00 17.16 A C ATOM 83 O LYS A 13 17.047 58.515 20.130 1.00 15.92 A O ATOM 84 N SER A 14 14.904 59.286 19.864 1.00 16.11 A N ATOM 85 CA SER A 14 15.114 60.029 18.621 1.00 16.16 A C ATOM 86 CB SER A 14 14.659 61.492 18.751 1.00 15.77 A C ATOM 87 OG SER A 14 15.523 62.202 19.587 1.00 15.69 A O ATOM 88 C SER A 14 14.324 59.439 17.460 1.00 15.77 A C ATOM 89 O SER A 14 13.254 58.842 17.641 1.00 16.38 A O ATOM 90 N PHE A 15 14.833 59.712 16.263 1.00 14.76 A N ATOM 91 CA PHE A 15 14.281 59.224 15.009 1.00 13.44 A C ATOM 92 CB PHE A 15 14.562 57.741 14.855 1.00 12.78 A C ATOM 93 CG PHE A 15 15.901 57.329 15.375 1.00 12.44 A C ATOM 94 CD1 PHE A 15 17.004 57.402 14.588 1.00 12.46 A C ATOM 95 CE1 PHE A 15 18.248 57.033 15.066 1.00 12.45 A C ATOM 96 CZ PHE A 15 18.398 56.582 16.350 1.00 12.34 A C ATOM 97 CE2 PHE A 15 17.288 56.491 17.148 1.00 12.82 A C ATOM 98 CD2 PHE A 15 16.046 56.868 16.655 1.00 12.74 A C ATOM 99 C PHE A 15 14.946 59.973 13.852 1.00 13.24 A C ATOM 100 O PHE A 15 15.970 60.647 14.005 1.00 12.99 A O ATOM 101 N THR A 16 14.373 59.798 12.679 1.00 12.90 A N ATOM 102 CA THR A 16 14.843 60.461 11.492 1.00 12.27 A C ATOM 103 CB THR A 16 13.661 60.746 10.602 1.00 11.79 A C ATOM 104 OG1 THR A 16 12.628 61.323 11.424 1.00 11.21 A O ATOM 105 CG2 THR A 16 14.056 61.662 9.465 1.00 11.43 A C ATOM 106 C THR A 16 15.862 59.593 10.771 1.00 12.41 A C ATOM 107 O THR A 16 15.728 58.359 10.686 1.00 12.07 A O ATOM 108 N THR A 17 16.914 60.252 10.303 1.00 12.28 A N ATOM 109 CA THR A 17 17.952 59.582 9.540 1.00 12.14 A C ATOM 110 CB THR A 17 19.202 59.303 10.396 1.00 11.78 A C ATOM 111 OG1 THR A 17 19.721 60.532 10.919 1.00 11.36 A O ATOM 112 CG2 THR A 17 18.838 58.371 11.537 1.00 11.82 A C ATOM 113 C THR A 17 18.321 60.453 8.367 1.00 12.21 A C ATOM 114 O THR A 17 17.882 61.580 8.242 1.00 10.79 A O ATOM 115 N THR A 18 19.156 59.908 7.515 1.00 13.29 A N ATOM 116 CA THR A 18 19.482 60.584 6.301 1.00 14.74 A C ATOM 117 CB THR A 18 18.921 59.785 5.103 1.00 14.74 A C ATOM 118 OG1 THR A 18 17.470 59.893 5.058 1.00 14.74 A O ATOM 119 CG2 THR A 18 19.524 60.310 3.835 1.00 15.11 A C ATOM 120 C THR A 18 21.010 60.819 6.232 1.00 15.79 A C ATOM 121 O THR A 18 21.779 59.898 6.354 1.00 14.67 A O ATOM 122 N GLN A 19 21.424 62.076 6.075 1.00 17.88 A N ATOM 123 CA GLN A 19 22.843 62.418 5.943 1.00 19.54 A C ATOM 124 CB GLN A 19 23.100 63.901 6.252 1.00 21.61 A C ATOM 125 CG GLN A 19 24.527 64.361 5.945 1.00 22.69 A C ATOM 126 CD GLN A 19 24.762 65.830 6.230 1.00 22.70 A C ATOM 127 OE1 GLN A 19 23.902 66.679 6.031 1.00 22.41 A O ATOM 128 NE2 GLN A 19 25.944 66.128 6.686 1.00 23.42 A N ATOM 129 C GLN A 19 23.281 62.147 4.541 1.00 19.39 A C ATOM 130 O GLN A 19 22.680 62.642 3.603 1.00 19.37 A O ATOM 131 N SER A 20 24.364 61.405 4.416 1.00 20.36 A N ATOM 132 CA SER A 20 24.805 60.864 3.142 1.00 21.93 A C ATOM 133 CB SER A 20 24.242 59.446 2.917 1.00 20.94 A C ATOM 134 OG SER A 20 24.848 58.804 1.798 1.00 20.47 A O ATOM 135 C SER A 20 26.316 60.793 3.153 1.00 24.09 A C ATOM 136 O SER A 20 26.900 59.913 3.817 1.00 24.70 A O ATOM 137 N GLY A 21 26.941 61.719 2.431 1.00 25.06 A N ATOM 138 CA GLY A 21 28.389 61.717 2.286 1.00 25.86 A C ATOM 139 C GLY A 21 29.009 62.180 3.585 1.00 26.74 A C ATOM 140 O GLY A 21 28.612 63.233 4.137 1.00 26.33 A O ATOM 141 N SER A 22 29.973 61.376 4.055 1.00 26.86 A N ATOM 142 CA SER A 22 30.620 61.522 5.374 1.00 26.16 A C ATOM 143 CB SER A 22 31.916 60.704 5.410 1.00 25.69 A C ATOM 144 OG SER A 22 32.699 60.973 4.264 1.00 25.00 A O ATOM 145 C SER A 22 29.765 61.040 6.537 1.00 25.41 A C ATOM 146 O SER A 22 30.092 61.342 7.678 1.00 28.42 A O ATOM 147 N THR A 23 28.692 60.295 6.259 1.00 24.03 A N ATOM 148 CA THR A 23 27.894 59.630 7.305 1.00 23.15 A C ATOM 149 CB THR A 23 27.851 58.107 7.116 1.00 22.84 A C ATOM 150 OG1 THR A 23 28.241 57.818 5.783 1.00 23.29 A O ATOM 151 CG2 THR A 23 28.727 57.393 8.116 1.00 23.29 A C ATOM 152 C THR A 23 26.442 59.995 7.328 1.00 21.31 A C ATOM 153 O THR A 23 26.004 60.983 6.747 1.00 20.69 A O ATOM 154 N TYR A 24 25.721 59.153 8.058 1.00 20.03 A N ATOM 155 CA TYR A 24 24.288 59.137 8.090 1.00 19.44 A C ATOM 156 CB TYR A 24 23.808 59.724 9.415 1.00 20.32 A C ATOM 157 CG TYR A 24 24.253 61.153 9.647 1.00 20.98 A C ATOM 158 CD1 TYR A 24 25.577 61.463 10.012 1.00 22.25 A C ATOM 159 CE1 TYR A 24 25.973 62.786 10.223 1.00 22.82 A C ATOM 160 CZ TYR A 24 25.027 63.803 10.075 1.00 22.98 A C ATOM 161 OH TYR A 24 25.333 65.114 10.258 1.00 22.47 A O ATOM 162 CE2 TYR A 24 23.725 63.508 9.714 1.00 22.86 A C ATOM 163 CD2 TYR A 24 23.353 62.193 9.502 1.00 21.74 A C ATOM 164 C TYR A 24 23.790 57.707 7.944 1.00 18.03 A C ATOM 165 O TYR A 24 24.420 56.776 8.398 1.00 18.83 A O ATOM 166 N GLN A 25 22.646 57.554 7.304 1.00 16.91 A N ATOM 167 CA GLN A 25 22.035 56.282 7.074 1.00 16.05 A C ATOM 168 CB GLN A 25 21.610 56.204 5.617 1.00 17.12 A C ATOM 169 CG GLN A 25 22.750 56.234 4.604 1.00 18.02 A C ATOM 170 CD GLN A 25 22.238 56.131 3.157 1.00 18.84 A C ATOM 171 OE1 GLN A 25 21.652 57.073 2.611 1.00 18.68 A O ATOM 172 NE2 GLN A 25 22.436 54.961 2.547 1.00 19.37 A N ATOM 173 C GLN A 25 20.804 56.174 7.940 1.00 14.92 A C ATOM 174 O GLN A 25 20.054 57.139 8.082 1.00 13.71 A O ATOM 175 N LEU A 26 20.586 54.991 8.507 1.00 14.84 A N ATOM 176 CA LEU A 26 19.323 54.675 9.200 1.00 14.71 A C ATOM 177 CB LEU A 26 19.445 53.347 9.978 1.00 14.61 A C ATOM 178 CG LEU A 26 19.423 53.351 11.519 1.00 14.51 A C ATOM 179 CD1 LEU A 26 19.059 51.976 12.079 1.00 14.06 A C ATOM 180 CD2 LEU A 26 18.478 54.406 12.088 1.00 14.65 A C ATOM 181 C LEU A 26 18.128 54.605 8.242 1.00 14.74 A C ATOM 182 O LEU A 26 17.595 53.535 8.002 1.00 15.14 A O ATOM 183 N LYS A 27 17.714 55.748 7.703 1.00 15.19 A N ATOM 184 CA LYS A 27 16.706 55.808 6.643 1.00 15.66 A C ATOM 185 CB LYS A 27 17.364 55.826 5.267 1.00 17.97 A C ATOM 186 CG LYS A 27 16.461 55.674 4.013 1.00 20.16 A C ATOM 187 CD LYS A 27 17.235 56.135 2.756 1.00 22.07 A C ATOM 188 CE LYS A 27 16.523 55.982 1.402 1.00 23.86 A C ATOM 189 NZ LYS A 27 16.851 54.674 0.719 1.00 24.48 A N ATOM 190 C LYS A 27 15.913 57.057 6.827 1.00 14.55 A C ATOM 191 O LYS A 27 16.489 58.120 6.996 1.00 14.47 A O ATOM 192 N ASP A 28 14.587 56.917 6.825 1.00 13.97 A N ATOM 193 CA ASP A 28 13.659 58.031 7.050 1.00 13.42 A C ATOM 194 CB ASP A 28 12.763 57.725 8.266 1.00 13.08 A C ATOM 195 CG ASP A 28 11.674 58.771 8.521 1.00 13.48 A C ATOM 196 OD1 ASP A 28 11.473 59.690 7.689 1.00 14.37 A O ATOM 197 OD2 ASP A 28 11.005 58.691 9.587 1.00 12.98 A O ATOM 198 C ASP A 28 12.893 58.207 5.739 1.00 13.01 A C ATOM 199 O ASP A 28 12.178 57.368 5.343 1.00 12.32 A O ATOM 200 N THR A 29 13.117 59.315 5.068 1.00 13.89 A N ATOM 201 CA THR A 29 12.519 59.651 3.769 1.00 14.71 A C ATOM 202 CB THR A 29 13.399 60.741 3.052 1.00 15.35 A C ATOM 203 OG1 THR A 29 14.777 60.336 3.027 1.00 15.18 A O ATOM 204 CG2 THR A 29 12.900 61.030 1.614 1.00 16.17 A C ATOM 205 C THR A 29 11.158 60.301 3.937 1.00 14.50 A C ATOM 206 O THR A 29 10.416 60.477 2.966 1.00 14.03 A O ATOM 207 N THR A 30 10.858 60.707 5.166 1.00 14.01 A N ATOM 208 CA THR A 30 9.723 61.573 5.413 1.00 13.87 A C ATOM 209 CB THR A 30 9.932 62.391 6.680 1.00 13.93 A C ATOM 210 OG1 THR A 30 9.673 61.570 7.827 1.00 14.25 A O ATOM 211 CG2 THR A 30 11.361 62.916 6.702 1.00 13.81 A C ATOM 212 C THR A 30 8.429 60.802 5.518 1.00 13.58 A C ATOM 213 O THR A 30 7.359 61.401 5.502 1.00 12.36 A O ATOM 214 N ARG A 31 8.521 59.476 5.615 1.00 14.16 A N ATOM 215 CA ARG A 31 7.297 58.698 5.580 1.00 15.08 A C ATOM 216 CB ARG A 31 6.770 58.358 6.990 1.00 15.55 A C ATOM 217 CG ARG A 31 7.598 57.511 7.921 1.00 16.02 A C ATOM 218 CD ARG A 31 8.195 58.329 9.061 1.00 16.47 A C ATOM 219 NE ARG A 31 7.390 58.608 10.270 1.00 15.99 A N ATOM 220 CZ ARG A 31 7.738 59.539 11.181 1.00 15.52 A C ATOM 221 NH1 ARG A 31 8.823 60.305 11.035 1.00 15.13 A N ATOM 222 NH2 ARG A 31 6.991 59.741 12.238 1.00 15.37 A N ATOM 223 C ARG A 31 7.235 57.525 4.589 1.00 14.78 A C ATOM 224 O ARG A 31 8.080 56.638 4.583 1.00 14.51 A O ATOM 225 N GLY A 32 6.182 57.584 3.753 1.00 14.67 A N ATOM 226 CA GLY A 32 6.087 56.875 2.471 1.00 14.18 A C ATOM 227 C GLY A 32 7.325 56.959 1.608 1.00 13.91 A C ATOM 228 O GLY A 32 8.032 57.952 1.604 1.00 13.27 A O ATOM 229 N GLN A 33 7.608 55.897 0.875 1.00 14.47 A N ATOM 230 CA GLN A 33 8.876 55.840 0.160 1.00 15.13 A C ATOM 231 CB GLN A 33 8.834 54.815 0.957 1.00 16.42 A C ATOM 232 CG GLN A 33 7.964 55.204 2.146 1.00 17.07 A C ATOM 233 CD GLN A 33 7.000 54.094 2.468 1.00 18.22 A C ATOM 234 OE1 GLN A 33 5.796 54.344 2.529 1.00 18.93 A O ATOM 235 NE2 GLN A 33 7.516 52.821 2.619 1.00 18.12 A N ATOM 236 C GLN A 33 10.024 55.539 1.099 1.00 14.63 A C ATOM 237 O GLN A 33 11.164 55.372 0.671 1.00 14.46 A O ATOM 238 N GLY A 34 9.727 55.477 2.386 1.00 14.20 A N ATOM 239 CA GLY A 34 10.766 55.551 3.369 1.00 13.93 A C ATOM 240 C GLY A 34 10.802 54.379 4.303 1.00 13.69 A C ATOM 241 O GLY A 34 10.151 53.360 4.073 1.00 14.83 A O ATOM 242 N ILE A 35 11.563 54.533 5.371 1.00 12.80 A N ATOM 243 CA ILE A 35 11.706 53.495 6.353 1.00 12.48 A C ATOM 244 CB ILE A 35 11.136 53.951 7.695 1.00 12.26 A C ATOM 245 CG1 ILE A 35 9.639 54.116 7.554 1.00 12.72 A C ATOM 246 CD1 ILE A 35 8.906 54.294 8.876 1.00 13.19 A C ATOM 247 CG2 ILE A 35 11.468 52.976 8.798 1.00 12.20 A C ATOM 248 C ILE A 35 13.193 53.286 6.417 1.00 12.31 A C ATOM 249 O ILE A 35 13.938 54.242 6.575 1.00 12.03 A O ATOM 250 N VAL A 36 13.625 52.043 6.257 1.00 12.28 A N ATOM 251 CA VAL A 36 15.051 51.755 6.160 1.00 12.25 A C ATOM 252 CB VAL A 36 15.459 51.351 4.737 1.00 12.50 A C ATOM 253 CG1 VAL A 36 16.968 51.376 4.631 1.00 12.79 A C ATOM 254 CG2 VAL A 36 14.829 52.271 3.691 1.00 12.49 A C ATOM 255 C VAL A 36 15.378 50.600 7.042 1.00 11.79 A C ATOM 256 O VAL A 36 14.656 49.627 7.068 1.00 11.66 A O ATOM 257 N THR A 37 16.480 50.693 7.752 1.00 11.73 A N ATOM 258 CA THR A 37 16.821 49.656 8.699 1.00 11.95 A C ATOM 259 CB THR A 37 16.651 50.214 10.125 1.00 12.12 A C ATOM 260 OG1 THR A 37 15.306 50.678 10.323 1.00 11.60 A O ATOM 261 CG2 THR A 37 16.978 49.158 11.163 1.00 12.41 A C ATOM 262 C THR A 37 18.242 49.064 8.450 1.00 12.02 A C ATOM 263 O THR A 37 19.220 49.806 8.348 1.00 11.27 A O ATOM 264 N TYR A 38 18.310 47.727 8.348 1.00 12.30 A N ATOM 265 CA TYR A 38 19.531 46.984 8.027 1.00 12.80 A C ATOM 266 CB TYR A 38 19.301 46.102 6.793 1.00 13.01 A C ATOM 267 CG TYR A 38 18.714 46.788 5.592 1.00 13.05 A C ATOM 268 CD1 TYR A 38 17.349 47.059 5.500 1.00 12.97 A C ATOM 269 CE1 TYR A 38 16.826 47.706 4.387 1.00 12.85 A C ATOM 270 CZ TYR A 38 17.664 48.041 3.345 1.00 12.79 A C ATOM 271 OH TYR A 38 17.222 48.655 2.229 1.00 13.25 A O ATOM 272 CE2 TYR A 38 18.991 47.767 3.402 1.00 13.05 A C ATOM 273 CD2 TYR A 38 19.519 47.145 4.523 1.00 13.15 A C ATOM 274 C TYR A 38 19.921 46.001 9.123 1.00 13.22 A C ATOM 275 O TYR A 38 19.061 45.563 9.886 1.00 13.13 A O ATOM 276 N SER A 39 21.196 45.588 9.132 1.00 13.71 A N ATOM 277 CA SER A 39 21.668 44.417 9.919 1.00 14.12 A C ATOM 278 CB SER A 39 22.854 44.784 10.823 1.00 13.74 A C ATOM 279 OG SER A 39 23.634 43.628 11.165 1.00 13.56 A O ATOM 280 C SER A 39 22.052 43.226 9.009 1.00 14.90 A C ATOM 281 O SER A 39 22.651 43.409 7.942 1.00 15.79 A O ATOM 282 N ALA A 40 21.697 42.011 9.422 1.00 15.34 A N ATOM 283 CA ALA A 40 22.070 40.810 8.672 1.00 15.65 A C ATOM 284 CB ALA A 40 21.026 39.738 8.857 1.00 15.26 A C ATOM 285 C ALA A 40 23.444 40.255 9.080 1.00 16.51 A C ATOM 286 O ALA A 40 23.871 39.252 8.542 1.00 16.26 A O ATOM 287 N GLY A 41 24.125 40.884 10.037 1.00 17.11 A N ATOM 288 CA GLY A 41 25.400 40.386 10.509 1.00 17.44 A C ATOM 289 C GLY A 41 25.335 38.944 10.945 1.00 18.31 A C ATOM 290 O GLY A 41 26.259 38.156 10.687 1.00 18.80 A O ATOM 291 N ASN A 42 24.230 38.586 11.583 1.00 18.86 A N ATOM 292 CA ASN A 42 24.007 37.213 12.060 1.00 19.31 A C ATOM 293 CB ASN A 42 24.917 36.897 13.253 1.00 18.59 A C ATOM 294 CG ASN A 42 24.664 37.831 14.428 1.00 18.02 A C ATOM 295 OD1 ASN A 42 25.567 38.474 14.893 1.00 18.09 A O ATOM 296 ND2 ASN A 42 23.419 37.928 14.879 1.00 17.76 A N ATOM 297 C ASN A 42 24.075 36.119 11.010 1.00 20.65 A C ATOM 298 O ASN A 42 24.293 34.976 11.332 1.00 20.22 A O ATOM 299 N ARG A 43 23.827 36.470 9.761 1.00 23.59 A N ATOM 300 CA ARG A 43 23.646 35.496 8.707 1.00 26.15 A C ATOM 301 CB ARG A 43 24.688 35.719 7.618 1.00 30.73 A C ATOM 302 CG ARG A 43 26.103 35.379 8.056 1.00 35.36 A C ATOM 303 CD ARG A 43 27.117 36.068 7.163 1.00 42.30 A C ATOM 304 NE ARG A 43 28.483 35.870 7.661 1.00 51.16 A N ATOM 305 CZ ARG A 43 29.263 36.813 8.216 1.00 54.64 A C ATOM 306 NH1 ARG A 43 28.842 38.082 8.366 1.00 55.48 A N ATOM 307 NH2 ARG A 43 30.493 36.474 8.620 1.00 51.20 A N ATOM 308 C ARG A 43 22.227 35.710 8.203 1.00 25.25 A C ATOM 309 O ARG A 43 21.465 36.443 8.850 1.00 25.16 A O ATOM 310 N SER A 44 21.856 35.091 7.080 1.00 23.65 A N ATOM 311 CA SER A 44 20.469 35.117 6.638 1.00 23.20 A C ATOM 312 CB SER A 44 19.913 33.725 6.728 1.00 23.30 A C ATOM 313 OG SER A 44 20.575 32.930 5.806 1.00 24.80 A O ATOM 314 C SER A 44 20.254 35.685 5.235 1.00 22.60 A C ATOM 315 O SER A 44 19.168 35.591 4.637 1.00 23.35 A O ATOM 316 N SER A 45 21.291 36.310 4.728 1.00 21.47 A N ATOM 317 CA SER A 45 21.198 37.091 3.516 1.00 20.72 A C ATOM 318 CB SER A 45 22.604 37.567 3.142 1.00 20.80 A C ATOM 319 OG SER A 45 22.968 37.078 1.894 1.00 21.92 A O ATOM 320 C SER A 45 20.325 38.324 3.784 1.00 19.65 A C ATOM 321 O SER A 45 20.563 39.037 4.775 1.00 19.28 A O ATOM 322 N LEU A 46 19.357 38.602 2.901 1.00 17.76 A N ATOM 323 CA LEU A 46 18.494 39.787 3.055 1.00 16.26 A C ATOM 324 CB LEU A 46 17.059 39.358 3.308 1.00 15.57 A C ATOM 325 CG LEU A 46 16.799 38.486 4.528 1.00 15.28 A C ATOM 326 CD1 LEU A 46 15.336 38.131 4.537 1.00 15.11 A C ATOM 327 CD2 LEU A 46 17.173 39.184 5.834 1.00 15.38 A C ATOM 328 C LEU A 46 18.528 40.707 1.854 1.00 15.97 A C ATOM 329 O LEU A 46 18.512 40.255 0.740 1.00 15.97 A O ATOM 330 N PRO A 47 18.450 42.021 2.068 1.00 16.23 A N ATOM 331 CA PRO A 47 18.098 42.713 3.302 1.00 16.33 A C ATOM 332 CB PRO A 47 17.593 44.069 2.806 1.00 16.02 A C ATOM 333 CG PRO A 47 17.843 44.110 1.340 1.00 15.83 A C ATOM 334 CD PRO A 47 18.710 42.968 0.980 1.00 15.87 A C ATOM 335 C PRO A 47 19.271 42.898 4.262 1.00 16.88 A C ATOM 336 O PRO A 47 19.062 43.188 5.448 1.00 16.98 A O ATOM 337 N GLY A 48 20.496 42.741 3.752 1.00 16.89 A N ATOM 338 CA GLY A 48 21.680 42.866 4.577 1.00 15.71 A C ATOM 339 C GLY A 48 22.281 44.214 4.323 1.00 14.63 A C ATOM 340 O GLY A 48 21.984 44.833 3.317 1.00 13.70 A O ATOM 341 N THR A 49 23.111 44.644 5.262 1.00 14.42 A N ATOM 342 CA THR A 49 23.844 45.889 5.184 1.00 15.14 A C ATOM 343 CB THR A 49 25.186 45.825 5.997 1.00 15.13 A C ATOM 344 OG1 THR A 49 25.981 44.687 5.619 1.00 14.36 A O ATOM 345 CG2 THR A 49 25.983 47.129 5.846 1.00 14.54 A C ATOM 346 C THR A 49 23.005 46.995 5.821 1.00 15.82 A C ATOM 347 O THR A 49 22.654 46.911 7.008 1.00 15.76 A O ATOM 348 N LEU A 50 22.696 48.036 5.055 1.00 16.29 A N ATOM 349 CA LEU A 50 21.971 49.177 5.612 1.00 16.67 A C ATOM 350 CB LEU A 50 21.402 50.030 4.494 1.00 16.62 A C ATOM 351 CG LEU A 50 21.206 51.532 4.619 1.00 17.18 A C ATOM 352 CD1 LEU A 50 20.505 51.964 5.905 1.00 17.48 A C ATOM 353 CD2 LEU A 50 20.430 51.992 3.379 1.00 17.09 A C ATOM 354 C LEU A 50 22.908 49.955 6.527 1.00 16.87 A C ATOM 355 O LEU A 50 24.039 50.225 6.155 1.00 18.03 A O ATOM 356 N LEU A 51 22.438 50.289 7.724 1.00 16.66 A N ATOM 357 CA LEU A 51 23.304 50.807 8.767 1.00 16.90 A C ATOM 358 CB LEU A 51 22.702 50.580 10.165 1.00 17.78 A C ATOM 359 CG LEU A 51 22.995 49.231 10.854 1.00 18.55 A C ATOM 360 CD1 LEU A 51 21.780 48.321 10.737 1.00 18.87 A C ATOM 361 CD2 LEU A 51 23.352 49.435 12.335 1.00 19.37 A C ATOM 362 C LEU A 51 23.664 52.270 8.629 1.00 16.37 A C ATOM 363 O LEU A 51 22.888 53.090 8.130 1.00 16.35 A O ATOM 364 N THR A 52 24.843 52.591 9.151 1.00 16.12 A N ATOM 365 CA THR A 52 25.398 53.941 9.097 1.00 15.93 A C ATOM 366 CB THR A 52 26.453 54.014 7.998 1.00 15.10 A C ATOM 367 OG1 THR A 52 27.129 52.773 7.961 1.00 14.51 A O ATOM 368 CG2 THR A 52 25.826 54.189 6.670 1.00 15.28 A C ATOM 369 C THR A 52 26.087 54.312 10.398 1.00 16.34 A C ATOM 370 O THR A 52 26.640 53.474 11.070 1.00 16.38 A O ATOM 371 N SER A 53 26.044 55.575 10.764 1.00 17.42 A N ATOM 372 CA SER A 53 26.900 56.061 11.829 1.00 18.54 A C ATOM 373 CB SER A 53 26.179 56.074 13.170 1.00 19.26 A C ATOM 374 OG SER A 53 26.656 57.168 13.945 1.00 19.86 A O ATOM 375 C SER A 53 27.334 57.468 11.510 1.00 18.55 A C ATOM 376 O SER A 53 26.473 58.367 11.355 1.00 17.72 A O ATOM 377 N SER A 54 28.651 57.665 11.445 1.00 18.20 A N ATOM 378 CA SER A 54 29.183 58.969 11.039 1.00 19.04 A C ATOM 379 CB SER A 54 30.671 58.894 10.731 1.00 19.67 A C ATOM 380 OG SER A 54 31.362 58.586 11.907 1.00 21.03 A O ATOM 381 C SER A 54 28.905 60.070 12.047 1.00 17.88 A C ATOM 382 O SER A 54 28.803 61.243 11.644 1.00 18.22 A O ATOM 383 N SER A 55 28.737 59.695 13.324 1.00 16.80 A N ATOM 384 CA SER A 55 28.274 60.644 14.363 1.00 16.20 A C ATOM 385 CB SER A 55 28.701 60.186 15.757 1.00 15.87 A C ATOM 386 OG SER A 55 28.447 58.827 15.969 1.00 15.88 A O ATOM 387 C SER A 55 26.775 60.983 14.384 1.00 15.91 A C ATOM 388 O SER A 55 26.388 61.948 15.025 1.00 15.99 A O ATOM 389 N ASN A 56 25.947 60.220 13.671 1.00 16.14 A N ATOM 390 CA ASN A 56 24.472 60.215 13.852 1.00 15.95 A C ATOM 391 CB ASN A 56 23.805 61.536 13.382 1.00 15.78 A C ATOM 392 CG ASN A 56 22.360 61.358 12.860 1.00 15.19 A C ATOM 393 OD1 ASN A 56 21.554 62.306 12.853 1.00 14.47 A O ATOM 394 ND2 ASN A 56 22.041 60.169 12.400 1.00 14.98 A N ATOM 395 C ASN A 56 24.092 59.885 15.296 1.00 16.66 A C ATOM 396 O ASN A 56 23.018 60.280 15.756 1.00 16.28 A O ATOM 397 N ILE A 57 24.984 59.161 15.989 1.00 17.56 A N ATOM 398 CA ILE A 57 24.682 58.525 17.259 1.00 18.93 A C ATOM 399 CB ILE A 57 25.650 58.958 18.366 1.00 20.60 A C ATOM 400 CG1 ILE A 57 25.606 60.475 18.578 1.00 21.60 A C ATOM 401 CD1 ILE A 57 26.715 60.933 19.510 1.00 21.99 A C ATOM 402 CG2 ILE A 57 25.300 58.247 19.673 1.00 20.37 A C ATOM 403 C ILE A 57 24.827 57.017 17.089 1.00 18.81 A C ATOM 404 O ILE A 57 25.830 56.572 16.550 1.00 18.38 A O ATOM 405 N TRP A 58 23.869 56.241 17.603 1.00 18.79 A N ATOM 406 CA TRP A 58 23.663 54.869 17.151 1.00 19.08 A C ATOM 407 CB TRP A 58 22.285 54.753 16.467 1.00 18.65 A C ATOM 408 CG TRP A 58 22.126 55.653 15.263 1.00 17.04 A C ATOM 409 CD1 TRP A 58 21.699 56.943 15.248 1.00 16.33 A C ATOM 410 NE1 TRP A 58 21.716 57.436 13.972 1.00 15.66 A N ATOM 411 CE2 TRP A 58 22.166 56.454 13.135 1.00 15.87 A C ATOM 412 CD2 TRP A 58 22.431 55.318 13.921 1.00 15.82 A C ATOM 413 CE3 TRP A 58 22.930 54.178 13.310 1.00 15.17 A C ATOM 414 CZ3 TRP A 58 23.119 54.190 11.949 1.00 15.35 A C ATOM 415 CH2 TRP A 58 22.833 55.320 11.181 1.00 15.47 A C ATOM 416 CZ2 TRP A 58 22.357 56.465 11.757 1.00 15.91 A C ATOM 417 C TRP A 58 23.743 53.866 18.273 1.00 21.25 A C ATOM 418 O TRP A 58 22.885 53.847 19.163 1.00 21.87 A O ATOM 419 N ASN A 59 24.748 52.994 18.211 1.00 23.98 A N ATOM 420 CA ASN A 59 25.040 52.065 19.306 1.00 24.38 A C ATOM 421 CB ASN A 59 26.548 51.940 19.490 1.00 26.43 A C ATOM 422 CG ASN A 59 27.209 51.187 18.334 1.00 29.93 A C ATOM 423 OD1 ASN A 59 26.529 50.504 17.551 1.00 31.64 A O ATOM 424 ND2 ASN A 59 28.536 51.308 18.213 1.00 32.05 A N ATOM 425 C ASN A 59 24.455 50.672 19.083 1.00 23.75 A C ATOM 426 O ASN A 59 24.810 49.744 19.806 1.00 27.95 A O ATOM 427 N ASP A 60 23.589 50.499 18.093 1.00 20.98 A N ATOM 428 CA ASP A 60 22.892 49.230 17.924 1.00 19.55 A C ATOM 429 CB ASP A 60 22.924 48.781 16.477 1.00 19.97 A C ATOM 430 CG ASP A 60 22.413 47.377 16.304 1.00 21.08 A C ATOM 431 OD1 ASP A 60 21.574 46.928 17.121 1.00 22.86 A O ATOM 432 OD2 ASP A 60 22.856 46.703 15.354 1.00 22.23 A O ATOM 433 C ASP A 60 21.437 49.304 18.376 1.00 18.14 A C ATOM 434 O ASP A 60 20.592 49.914 17.694 1.00 17.59 A O ATOM 435 N GLY A 61 21.133 48.599 19.466 1.00 16.48 A N ATOM 436 CA GLY A 61 19.822 48.709 20.138 1.00 15.68 A C ATOM 437 C GLY A 61 18.639 48.102 19.392 1.00 14.75 A C ATOM 438 O GLY A 61 17.577 48.719 19.298 1.00 14.18 A O ATOM 439 N ALA A 62 18.826 46.885 18.896 1.00 13.68 A N ATOM 440 CA ALA A 62 17.870 46.232 18.027 1.00 13.21 A C ATOM 441 CB ALA A 62 18.383 44.874 17.598 1.00 13.34 A C ATOM 442 C ALA A 62 17.597 47.074 16.805 1.00 12.94 A C ATOM 443 O ALA A 62 16.441 47.297 16.457 1.00 12.77 A O ATOM 444 N ALA A 63 18.646 47.569 16.161 1.00 12.70 A N ATOM 445 CA ALA A 63 18.434 48.493 15.027 1.00 12.59 A C ATOM 446 CB ALA A 63 19.759 48.903 14.401 1.00 12.74 A C ATOM 447 C ALA A 63 17.626 49.732 15.433 1.00 11.84 A C ATOM 448 O ALA A 63 16.674 50.096 14.771 1.00 11.48 A O ATOM 449 N VAL A 64 18.007 50.362 16.530 1.00 11.59 A N ATOM 450 CA VAL A 64 17.296 51.555 17.001 1.00 11.64 A C ATOM 451 CB VAL A 64 17.946 52.163 18.282 1.00 11.76 A C ATOM 452 CG1 VAL A 64 16.973 53.097 18.988 1.00 11.89 A C ATOM 453 CG2 VAL A 64 19.239 52.927 17.954 1.00 11.63 A C ATOM 454 C VAL A 64 15.811 51.314 17.274 1.00 11.25 A C ATOM 455 O VAL A 64 14.967 52.092 16.889 1.00 10.71 A O ATOM 456 N ASP A 65 15.499 50.244 17.972 1.00 11.62 A N ATOM 457 CA ASP A 65 14.103 49.937 18.299 1.00 11.62 A C ATOM 458 CB ASP A 65 13.988 48.750 19.282 1.00 11.58 A C ATOM 459 CG ASP A 65 14.272 49.144 20.735 1.00 11.39 A C ATOM 460 OD1 ASP A 65 14.119 50.315 21.053 1.00 11.29 A O ATOM 461 OD2 ASP A 65 14.647 48.294 21.563 1.00 11.28 A O ATOM 462 C ASP A 65 13.343 49.657 17.011 1.00 11.68 A C ATOM 463 O ASP A 65 12.287 50.237 16.795 1.00 12.17 A O ATOM 464 N ALA A 66 13.881 48.805 16.142 1.00 11.22 A N ATOM 465 CA ALA A 66 13.206 48.530 14.877 1.00 11.26 A C ATOM 466 CB ALA A 66 14.002 47.545 14.038 1.00 11.11 A C ATOM 467 C ALA A 66 12.942 49.816 14.076 1.00 11.77 A C ATOM 468 O ALA A 66 11.835 50.016 13.538 1.00 11.80 A O ATOM 469 N HIS A 67 13.944 50.690 13.995 1.00 11.93 A N ATOM 470 CA HIS A 67 13.758 51.933 13.275 1.00 12.20 A C ATOM 471 CB HIS A 67 15.047 52.745 13.195 1.00 12.39 A C ATOM 472 CG HIS A 67 15.079 53.722 12.053 1.00 12.80 A C ATOM 473 ND1 HIS A 67 15.102 53.327 10.736 1.00 13.19 A N ATOM 474 CE1 HIS A 67 15.143 54.396 9.955 1.00 13.25 A C ATOM 475 NE2 HIS A 67 15.176 55.469 10.719 1.00 12.96 A N ATOM 476 CD2 HIS A 67 15.137 55.075 12.033 1.00 13.09 A C ATOM 477 C HIS A 67 12.649 52.740 13.934 1.00 12.01 A C ATOM 478 O HIS A 67 11.651 53.041 13.316 1.00 12.49 A O ATOM 479 N ALA A 68 12.809 53.051 15.205 1.00 11.74 A N ATOM 480 CA ALA A 68 11.876 53.929 15.905 1.00 11.42 A C ATOM 481 CB ALA A 68 12.395 54.188 17.313 1.00 11.62 A C ATOM 482 C ALA A 68 10.449 53.368 15.986 1.00 10.67 A C ATOM 483 O ALA A 68 9.451 54.078 15.807 1.00 10.44 A O ATOM 484 N TYR A 69 10.368 52.089 16.267 1.00 10.14 A N ATOM 485 CA TYR A 69 9.083 51.445 16.372 1.00 9.92 A C ATOM 486 CB TYR A 69 9.211 50.127 17.137 1.00 9.77 A C ATOM 487 CG TYR A 69 9.568 50.343 18.608 1.00 9.70 A C ATOM 488 CD1 TYR A 69 9.263 51.544 19.258 1.00 9.60 A C ATOM 489 CE1 TYR A 69 9.588 51.750 20.584 1.00 9.57 A C ATOM 490 CZ TYR A 69 10.204 50.755 21.307 1.00 9.49 A C ATOM 491 OH TYR A 69 10.500 50.982 22.645 1.00 8.99 A O ATOM 492 CE2 TYR A 69 10.509 49.549 20.685 1.00 9.61 A C ATOM 493 CD2 TYR A 69 10.201 49.356 19.341 1.00 9.63 A C ATOM 494 C TYR A 69 8.366 51.278 15.053 1.00 9.69 A C ATOM 495 O TYR A 69 7.129 51.268 15.022 1.00 9.58 A O ATOM 496 N THR A 70 9.129 51.193 13.965 1.00 9.51 A N ATOM 497 CA THR A 70 8.532 51.019 12.645 1.00 9.27 A C ATOM 498 CB THR A 70 9.549 50.438 11.620 1.00 9.02 A C ATOM 499 OG1 THR A 70 9.925 49.095 11.972 1.00 8.65 A O ATOM 500 CG2 THR A 70 8.960 50.394 10.262 1.00 8.99 A C ATOM 501 C THR A 70 7.970 52.395 12.257 1.00 9.35 A C ATOM 502 O THR A 70 6.910 52.516 11.659 1.00 9.65 A O ATOM 503 N ALA A 71 8.655 53.452 12.651 1.00 9.39 A N ATOM 504 CA ALA A 71 8.127 54.785 12.428 1.00 9.42 A C ATOM 505 CB ALA A 71 9.190 55.834 12.721 1.00 9.15 A C ATOM 506 C ALA A 71 6.854 54.985 13.284 1.00 9.65 A C ATOM 507 O ALA A 71 5.878 55.594 12.835 1.00 9.53 A O ATOM 508 N LYS A 72 6.842 54.432 14.491 1.00 10.10 A N ATOM 509 CA LYS A 72 5.638 54.469 15.315 1.00 10.84 A C ATOM 510 CB LYS A 72 5.945 53.814 16.635 1.00 11.60 A C ATOM 511 CG LYS A 72 5.034 54.225 17.764 1.00 12.60 A C ATOM 512 CD LYS A 72 5.285 53.298 18.948 1.00 13.78 A C ATOM 513 CE LYS A 72 4.237 53.477 20.052 1.00 14.79 A C ATOM 514 NZ LYS A 72 4.525 54.698 20.852 1.00 15.32 A N ATOM 515 C LYS A 72 4.428 53.773 14.648 1.00 10.95 A C ATOM 516 O LYS A 72 3.320 54.296 14.566 1.00 10.53 A O ATOM 517 N VAL A 73 4.666 52.580 14.143 1.00 11.11 A N ATOM 518 CA VAL A 73 3.613 51.873 13.539 1.00 11.29 A C ATOM 519 CB VAL A 73 4.052 50.456 13.206 1.00 11.29 A C ATOM 520 CG1 VAL A 73 2.976 49.773 12.375 1.00 11.51 A C ATOM 521 CG2 VAL A 73 4.297 49.674 14.477 1.00 11.25 A C ATOM 522 C VAL A 73 3.179 52.631 12.286 1.00 11.79 A C ATOM 523 O VAL A 73 1.973 52.775 12.023 1.00 12.54 A O ATOM 524 N TYR A 74 4.146 53.094 11.488 1.00 11.69 A N ATOM 525 CA TYR A 74 3.803 53.789 10.253 1.00 11.38 A C ATOM 526 CB TYR A 74 5.052 54.356 9.512 1.00 10.72 A C ATOM 527 CG TYR A 74 4.642 55.235 8.341 1.00 9.87 A C ATOM 528 CD1 TYR A 74 4.236 56.541 8.538 1.00 9.52 A C ATOM 529 CE1 TYR A 74 3.798 57.334 7.492 1.00 9.27 A C ATOM 530 CZ TYR A 74 3.767 56.822 6.235 1.00 9.43 A C ATOM 531 OH TYR A 74 3.319 57.598 5.195 1.00 9.43 A O ATOM 532 CE2 TYR A 74 4.152 55.514 6.010 1.00 9.49 A C ATOM 533 CD2 TYR A 74 4.577 54.729 7.062 1.00 9.59 A C ATOM 534 C TYR A 74 2.797 54.923 10.602 1.00 12.02 A C ATOM 535 O TYR A 74 1.816 55.093 9.905 1.00 11.97 A O ATOM 536 N ASP A 75 3.062 55.670 11.683 1.00 12.59 A N ATOM 537 CA ASP A 75 2.225 56.802 12.099 1.00 13.15 A C ATOM 538 CB ASP A 75 2.863 57.577 13.258 1.00 12.65 A C ATOM 539 CG ASP A 75 4.140 58.272 12.887 1.00 12.28 A C ATOM 540 OD1 ASP A 75 4.408 58.613 11.704 1.00 11.68 A O ATOM 541 OD2 ASP A 75 4.889 58.488 13.848 1.00 12.29 A O ATOM 542 C ASP A 75 0.884 56.370 12.652 1.00 13.93 A C ATOM 543 O ASP A 75 0.029 57.189 12.744 1.00 14.31 A O ATOM 544 N TYR A 76 0.790 55.129 13.108 1.00 14.12 A N ATOM 545 CA TYR A 76 0.435 54.684 13.703 1.00 15.01 A C ATOM 546 CB TYR A 76 0.232 53.411 14.549 1.00 14.93 A C ATOM 547 CG TYR A 76 1.483 52.846 15.181 1.00 14.82 A C ATOM 548 CD1 TYR A 76 2.257 51.907 14.523 1.00 15.03 A C ATOM 549 CE1 TYR A 76 3.409 51.387 15.107 1.00 15.40 A C ATOM 550 CZ TYR A 76 3.787 51.815 16.375 1.00 15.55 A C ATOM 551 OH TYR A 76 4.929 51.315 16.990 1.00 15.74 A O ATOM 552 CE2 TYR A 76 3.022 52.753 17.036 1.00 15.06 A C ATOM 553 CD2 TYR A 76 1.880 53.248 16.444 1.00 15.02 A C ATOM 554 C TYR A 76 1.381 54.465 12.538 1.00 15.85 A C ATOM 555 O TYR A 76 2.541 54.932 12.545 1.00 16.76 A O ATOM 556 N TYR A 77 0.898 53.779 11.522 1.00 16.19 A N ATOM 557 CA TYR A 77 1.796 53.445 10.429 1.00 17.84 A C ATOM 558 CB TYR A 77 1.163 52.449 9.451 1.00 16.53 A C ATOM 559 CG TYR A 77 1.341 50.967 9.805 1.00 15.02 A C ATOM 560 CD1 TYR A 77 2.441 50.267 9.364 1.00 14.53 A C ATOM 561 CE1 TYR A 77 2.587 48.923 9.613 1.00 14.07 A C ATOM 562 CZ TYR A 77 1.622 48.263 10.311 1.00 13.99 A C ATOM 563 OH TYR A 77 1.805 46.916 10.568 1.00 14.22 A O ATOM 564 CE2 TYR A 77 0.492 48.927 10.740 1.00 13.72 A C ATOM 565 CD2 TYR A 77 0.360 50.266 10.487 1.00 14.12 A C ATOM 566 C TYR A 77 2.211 54.723 9.712 1.00 19.97 A C ATOM 567 O TYR A 77 3.325 54.819 9.174 1.00 21.51 A O ATOM 568 N LYS A 78 1.315 55.704 9.730 1.00 22.11 A N ATOM 569 CA LYS A 78 1.556 56.962 9.075 1.00 23.87 A C ATOM 570 CB LYS A 78 0.239 57.743 8.908 1.00 25.91 A C ATOM 571 CG LYS A 78 0.347 59.104 8.221 1.00 28.58 A C ATOM 572 CD LYS A 78 1.136 59.006 6.918 1.00 33.48 A C ATOM 573 CE LYS A 78 0.619 59.934 5.815 1.00 37.52 A C ATOM 574 NZ LYS A 78 0.673 59.444 5.218 1.00 39.88 A N ATOM 575 C LYS A 78 2.622 57.747 9.855 1.00 22.86 A C ATOM 576 O LYS A 78 3.600 58.188 9.247 1.00 22.16 A O ATOM 577 N ASN A 79 2.471 57.888 11.173 1.00 21.47 A N ATOM 578 CA ASN A 79 3.422 58.714 11.919 1.00 22.64 A C ATOM 579 CB ASN A 79 2.899 59.148 13.278 1.00 23.04 A C ATOM 580 CG ASN A 79 1.578 59.888 13.188 1.00 24.12 A C ATOM 581 OD1 ASN A 79 0.759 59.783 14.094 1.00 24.68 A O ATOM 582 ND2 ASN A 79 1.348 60.617 12.087 1.00 24.13 A N ATOM 583 C ASN A 79 4.769 58.059 12.103 1.00 23.13 A C ATOM 584 O ASN A 79 5.794 58.714 11.909 1.00 23.42 A O ATOM 585 N LYS A 80 4.776 56.780 12.460 1.00 23.09 A N ATOM 586 CA LYS A 80 6.024 56.117 12.778 1.00 24.20 A C ATOM 587 CB LYS A 80 5.783 54.871 13.631 1.00 27.00 A C ATOM 588 CG LYS A 80 5.314 55.181 15.037 1.00 30.36 A C ATOM 589 CD LYS A 80 6.423 55.858 15.854 1.00 33.94 A C ATOM 590 CE LYS A 80 5.916 57.048 16.688 1.00 36.49 A C ATOM 591 NZ LYS A 80 5.336 56.639 17.999 1.00 37.18 A N ATOM 592 C LYS A 80 6.841 55.741 11.554 1.00 22.72 A C ATOM 593 O LYS A 80 8.080 55.784 11.599 1.00 24.14 A O ATOM 594 N PHE A 81 6.173 55.352 10.472 1.00 20.24 A N ATOM 595 CA PHE A 81 6.876 54.813 9.318 1.00 18.15 A C ATOM 596 CB PHE A 81 6.447 53.380 9.064 1.00 18.87 A C ATOM 597 CG PHE A 81 6.461 52.505 10.289 1.00 18.61 A C ATOM 598 CD1 PHE A 81 7.599 52.404 11.065 1.00 18.00 A C ATOM 599 CE1 PHE A 81 7.632 51.587 12.184 1.00 18.22 A C ATOM 600 CZ PHE A 81 6.510 50.862 12.542 1.00 18.35 A C ATOM 601 CE2 PHE A 81 5.354 50.955 11.759 1.00 18.91 A C ATOM 602 CD2 PHE A 81 5.335 51.770 10.643 1.00 18.40 A C ATOM 603 C PHE A 81 6.655 55.584 8.054 1.00 16.49 A C ATOM 604 O PHE A 81 7.232 55.247 7.031 1.00 15.88 A O ATOM 605 N GLY A 82 5.840 56.626 8.098 1.00 15.73 A N ATOM 606 CA GLY A 82 5.448 57.296 6.856 1.00 15.78 A C ATOM 607 C GLY A 82 4.790 56.346 5.834 1.00 15.32 A C ATOM 608 O GLY A 82 4.948 56.516 4.643 1.00 15.40 A O ATOM 609 N ARG A 83 4.057 55.343 6.311 1.00 14.39 A N ATOM 610 CA ARG A 83 3.366 54.424 5.447 1.00 13.68 A C ATOM 611 CB ARG A 83 3.555 52.995 5.912 1.00 13.45 A C ATOM 612 CG ARG A 83 3.011 52.011 4.904 1.00 13.06 A C ATOM 613 CD ARG A 83 2.913 50.629 5.479 1.00 13.28 A C ATOM 614 NE ARG A 83 2.721 49.736 4.358 1.00 13.46 A N ATOM 615 CZ ARG A 83 3.697 49.171 3.662 1.00 13.30 A C ATOM 616 NH1 ARG A 83 4.971 49.321 3.998 1.00 13.23 A N ATOM 617 NH2 ARG A 83 3.375 48.419 2.631 1.00 13.54 A N ATOM 618 C ARG A 83 1.871 54.704 5.384 1.00 13.51 A C ATOM 619 O ARG A 83 1.183 54.725 6.390 1.00 13.70 A O ATOM 620 N ASN A 84 1.390 54.879 4.167 1.00 13.56 A N ATOM 621 CA ASN A 84 0.009 55.148 3.893 1.00 13.51 A C ATOM 622 CB ASN A 84 0.088 56.018 2.658 1.00 13.59 A C ATOM 623 CG ASN A 84 1.491 56.487 2.384 1.00 14.02 A C ATOM 624 OD1 ASN A 84 1.725 57.145 1.381 1.00 15.08 A O ATOM 625 ND2 ASN A 84 2.428 56.165 3.261 1.00 13.79 A N ATOM 626 C ASN A 84 0.760 53.864 3.630 1.00 13.38 A C ATOM 627 O ASN A 84 0.857 53.447 2.476 1.00 13.02 A O ATOM 628 N SER A 85 1.301 53.271 4.707 1.00 12.63 A N ATOM 629 CA SER A 85 2.121 52.055 4.669 1.00 11.89 A C ATOM 630 CB SER A 85 3.343 52.185 3.746 1.00 11.20 A C ATOM 631 OG SER A 85 4.254 51.134 3.980 1.00 10.14 A O ATOM 632 C SER A 85 1.291 50.867 4.273 1.00 12.38 A C ATOM 633 O SER A 85 0.066 50.944 4.210 1.00 12.63 A O ATOM 634 N ILE A 86 1.990 49.773 3.990 1.00 12.96 A N ATOM 635 CA ILE A 86 1.396 48.453 3.822 1.00 13.20 A C ATOM 636 CB ILE A 86 2.512 47.385 3.647 1.00 13.89 A C ATOM 637 CG1 ILE A 86 3.144 47.100 5.011 1.00 13.93 A C ATOM 638 CD1 ILE A 86 4.318 46.147 4.967 1.00 14.24 A C ATOM 639 CG2 ILE A 86 1.996 46.082 3.034 1.00 14.48 A C ATOM 640 C ILE A 86 0.431 48.423 2.663 1.00 13.17 A C ATOM 641 O ILE A 86 0.620 47.786 2.759 1.00 13.10 A O ATOM 642 N ASP A 87 0.767 49.114 1.569 1.00 12.99 A N ATOM 643 CA ASP A 87 0.130 49.095 0.380 1.00 12.59 A C ATOM 644 CB ASP A 87 0.644 48.780 0.920 1.00 12.29 A C ATOM 645 CG ASP A 87 1.666 49.810 1.265 1.00 11.98 A C ATOM 646 OD1 ASP A 87 1.658 50.921 0.683 1.00 12.11 A O ATOM 647 OD2 ASP A 87 2.496 49.479 2.115 1.00 11.43 A O ATOM 648 C ASP A 87 1.028 50.320 0.225 1.00 12.13 A C ATOM 649 O ASP A 87 1.692 50.494 0.782 1.00 11.57 A O ATOM 650 N GLY A 88 1.067 51.168 1.236 1.00 12.40 A N ATOM 651 CA GLY A 88 1.807 52.407 1.092 1.00 12.89 A C ATOM 652 C GLY A 88 1.201 53.421 0.146 1.00 13.24 A C ATOM 653 O GLY A 88 1.699 54.542 0.132 1.00 14.52 A O ATOM 654 N ASN A 89 0.115 53.051 0.567 1.00 12.96 A N ATOM 655 CA ASN A 89 0.658 53.912 1.473 1.00 12.96 A C ATOM 656 CB ASN A 89 0.669 53.249 2.844 1.00 13.56 A C ATOM 657 CG ASN A 89 0.641 53.362 3.537 1.00 13.79 A C ATOM 658 OD1 ASN A 89 1.205 54.457 3.631 1.00 14.84 A O ATOM 659 ND2 ASN A 89 1.149 52.242 4.029 1.00 13.75 A N ATOM 660 C ASN A 89 2.147 54.210 1.165 1.00 12.88 A C ATOM 661 O ASN A 89 2.907 54.462 2.095 1.00 12.88 A O ATOM 662 N GLY A 90 2.574 54.175 0.097 1.00 12.86 A N ATOM 663 CA GLY A 90 3.958 54.471 0.469 1.00 12.39 A C ATOM 664 C GLY A 90 4.961 53.302 0.474 1.00 12.26 A C ATOM 665 O GLY A 90 6.137 53.514 0.791 1.00 12.36 A O ATOM 666 N PHE A 91 4.527 52.091 0.118 1.00 11.47 A N ATOM 667 CA PHE A 91 5.390 50.906 0.131 1.00 11.28 A C ATOM 668 CB PHE A 91 4.545 49.680 0.502 1.00 11.72 A C ATOM 669 CG PHE A 91 5.262 48.333 0.429 1.00 11.82 A C ATOM 670 CD1 PHE A 91 6.027 47.869 1.503 1.00 11.80 A C ATOM 671 CE1 PHE A 91 6.634 46.609 1.454 1.00 11.78 A C ATOM 672 CZ PHE A 91 6.457 45.791 0.341 1.00 11.56 A C ATOM 673 CE2 PHE A 91 5.647 46.217 0.706 1.00 11.63 A C ATOM 674 CD2 PHE A 91 5.053 47.470 0.663 1.00 11.62 A C ATOM 675 C PHE A 91 6.509 51.027 1.132 1.00 10.82 A C ATOM 676 O PHE A 91 6.262 50.984 2.306 1.00 11.40 A O ATOM 677 N GLN A 92 7.739 51.128 0.659 1.00 10.46 A N ATOM 678 CA GLN A 92 8.903 51.300 1.520 1.00 10.16 A C ATOM 679 CB GLN A 92 10.190 51.348 0.665 1.00 9.81 A C ATOM 680 CG GLN A 92 11.435 51.789 1.424 1.00 9.40 A C ATOM 681 CD GLN A 92 12.658 51.830 0.560 1.00 9.00 A C ATOM 682 OE1 GLN A 92 13.251 50.800 0.244 1.00 8.91 A O ATOM 683 NE2 GLN A 92 13.056 53.023 0.179 1.00 8.85 A N ATOM 684 C GLN A 92 9.020 50.172 2.547 1.00 10.41 A C ATOM 685 O GLN A 92 8.852 49.014 2.220 1.00 10.73 A O ATOM 686 N LEU A 93 9.372 50.531 3.774 1.00 10.45 A N ATOM 687 CA LEU A 93 9.461 49.608 4.873 1.00 10.53 A C ATOM 688 CB LEU A 93 8.795 50.248 6.088 1.00 10.43 A C ATOM 689 CG LEU A 93 7.325 50.530 5.783 1.00 10.45 A C ATOM 690 CD1 LEU A 93 6.629 51.095 6.991 1.00 10.58 A C ATOM 691 CD2 LEU A 93 6.606 49.286 5.321 1.00 10.42 A C ATOM 692 C LEU A 93 10.894 49.254 5.222 1.00 10.87 A C ATOM 693 O LEU A 93 11.686 50.097 5.637 1.00 10.94 A O ATOM 694 N LYS A 94 11.228 47.996 5.085 1.00 11.36 A N ATOM 695 CA LYS A 94 12.557 47.606 5.384 1.00 12.41 A C ATOM 696 CB LYS A 94 13.181 46.937 4.197 1.00 13.22 A C ATOM 697 CG LYS A 94 13.478 47.903 3.087 1.00 13.81 A C ATOM 698 CD LYS A 94 14.287 47.225 1.995 1.00 14.67 A C ATOM 699 CE LYS A 94 13.694 47.606 0.647 1.00 15.89 A C ATOM 700 NZ LYS A 94 14.804 47.787 0.313 1.00 16.73 A N ATOM 701 C LYS A 94 12.553 46.638 6.490 1.00 12.80 A C ATOM 702 O LYS A 94 11.826 45.662 6.437 1.00 14.03 A O ATOM 703 N SER A 95 13.419 46.878 7.462 1.00 12.71 A N ATOM 704 CA SER A 95 13.544 46.022 8.613 1.00 12.55 A C ATOM 705 CB SER A 95 13.161 46.813 9.861 1.00 12.73 A C ATOM 706 OG SER A 95 11.804 47.234 9.800 1.00 12.59 A O ATOM 707 C SER A 95 14.974 45.525 8.688 1.00 12.34 A C ATOM 708 O SER A 95 15.918 46.275 8.456 1.00 12.56 A O ATOM 709 N THR A 96 15.138 44.241 8.962 1.00 12.35 A N ATOM 710 CA THR A 96 16.466 43.667 9.154 1.00 12.18 A C ATOM 711 CB THR A 96 16.765 42.598 8.118 1.00 12.24 A C ATOM 712 OG1 THR A 96 16.552 43.158 6.828 1.00 12.21 A O ATOM 713 CG2 THR A 96 18.231 42.087 8.247 1.00 12.24 A C ATOM 714 C THR A 96 16.560 42.995 10.490 1.00 12.02 A C ATOM 715 O THR A 96 15.804 42.073 10.768 1.00 11.98 A O ATOM 716 N VAL A 97 17.512 43.453 11.286 1.00 12.10 A N ATOM 717 CA VAL A 97 17.796 42.903 12.610 1.00 12.29 A C ATOM 718 CB VAL A 97 18.031 44.046 13.614 1.00 11.84 A C ATOM 719 CG1 VAL A 97 16.842 44.997 13.607 1.00 11.85 A C ATOM 720 CG2 VAL A 97 19.294 44.816 13.291 1.00 11.48 A C ATOM 721 C VAL A 97 19.043 41.989 12.574 1.00 12.50 A C ATOM 722 O VAL A 97 19.760 41.922 11.573 1.00 12.20 A O ATOM 723 N HIS A 98 19.307 41.321 13.693 1.00 12.79 A N ATOM 724 CA HIS A 98 20.400 40.338 13.803 1.00 12.70 A C ATOM 725 CB HIS A 98 21.764 40.997 13.788 1.00 12.30 A C ATOM 726 CG HIS A 98 21.870 42.180 14.687 1.00 11.98 A C ATOM 727 ND1 HIS A 98 21.648 42.103 16.040 1.00 11.73 A N ATOM 728 CE1 HIS A 98 21.815 43.295 16.574 1.00 11.81 A C ATOM 729 NE2 HIS A 98 22.147 44.138 15.617 1.00 11.79 A N ATOM 730 CD2 HIS A 98 22.206 43.463 14.429 1.00 11.79 A C ATOM 731 C HIS A 98 20.334 39.328 12.685 1.00 13.21 A C ATOM 732 O HIS A 98 21.348 38.988 12.091 1.00 13.62 A O ATOM 733 N TYR A 99 19.117 38.883 12.389 1.00 13.68 A N ATOM 734 CA TYR A 99 18.894 37.826 11.446 1.00 13.61 A C ATOM 735 CB TYR A 99 17.410 37.665 11.086 1.00 13.46 A C ATOM 736 CG TYR A 99 17.177 36.565 10.042 1.00 13.94 A C ATOM 737 CD1 TYR A 99 17.426 36.805 8.691 1.00 14.10 A C ATOM 738 CE1 TYR A 99 17.213 35.826 7.731 1.00 13.91 A C ATOM 739 CZ TYR A 99 16.774 34.579 8.108 1.00 13.62 A C ATOM 740 OH TYR A 99 16.605 33.644 7.112 1.00 12.97 A O ATOM 741 CE2 TYR A 99 16.553 34.292 9.445 1.00 13.47 A C ATOM 742 CD2 TYR A 99 16.756 35.278 10.400 1.00 13.78 A C ATOM 743 C TYR A 99 19.384 36.564 12.086 1.00 13.49 A C ATOM 744 O TYR A 99 18.870 36.163 13.106 1.00 12.90 A O ATOM 745 N SER A 100 20.399 35.974 11.471 1.00 14.43 A N ATOM 746 CA SER A 100 20.823 34.601 11.733 1.00 15.24 A C ATOM 747 CB SER A 100 19.639 33.661 11.530 1.00 15.55 A C ATOM 748 OG SER A 100 20.037 32.309 11.482 1.00 15.70 A O ATOM 749 C SER A 100 21.440 34.469 13.114 1.00 16.08 A C ATOM 750 O SER A 100 21.916 35.443 13.679 1.00 16.02 A O ATOM 751 N SER A 101 21.448 33.271 13.668 1.00 18.00 A N ATOM 752 CA SER A 101 22.109 33.064 14.954 1.00 20.04 A C ATOM 753 CB SER A 101 23.285 32.117 14.785 1.00 20.79 A C ATOM 754 OG SER A 101 24.125 32.255 15.909 1.00 22.68 A O ATOM 755 C SER A 101 21.172 32.575 16.074 1.00 20.29 A C ATOM 756 O SER A 101 20.448 31.590 15.909 1.00 18.68 A O ATOM 757 N ARG A 102 21.210 33.275 17.212 1.00 21.31 A N ATOM 758 CA ARG A 102 20.354 32.962 18.351 1.00 22.92 A C ATOM 759 CB ARG A 102 20.973 31.842 19.222 1.00 25.54 A C ATOM 760 CG ARG A 102 22.375 32.170 19.771 1.00 29.36 A C ATOM 761 CD ARG A 102 22.597 31.658 21.202 1.00 32.59 A C ATOM 762 NE ARG A 102 22.425 30.196 21.266 1.00 35.58 A N ATOM 763 CZ ARG A 102 21.863 29.501 22.268 1.00 38.08 A C ATOM 764 NH1 ARG A 102 21.371 30.080 23.375 1.00 37.26 A N ATOM 765 NH2 ARG A 102 21.785 28.183 22.160 1.00 40.05 A N ATOM 766 C ARG A 102 18.972 32.558 17.854 1.00 21.22 A C ATOM 767 O ARG A 102 18.499 31.478 18.155 1.00 22.96 A O ATOM 768 N TYR A 103 18.337 33.431 17.088 1.00 19.27 A N ATOM 769 CA TYR A 103 17.131 33.068 16.304 1.00 18.16 A C ATOM 770 CB TYR A 103 17.246 33.653 14.876 1.00 17.43 A C ATOM 771 CG TYR A 103 16.076 33.397 14.001 1.00 17.19 A C ATOM 772 CD1 TYR A 103 15.957 32.216 13.283 1.00 18.00 A C ATOM 773 CE1 TYR A 103 14.860 31.991 12.450 1.00 18.06 A C ATOM 774 CZ TYR A 103 13.875 32.964 12.348 1.00 17.35 A C ATOM 775 OH TYR A 103 12.774 32.784 11.574 1.00 17.41 A O ATOM 776 CE2 TYR A 103 13.985 34.135 13.042 1.00 17.27 A C ATOM 777 CD2 TYR A 103 15.078 34.345 13.864 1.00 17.58 A C ATOM 778 C TYR A 103 15.854 33.534 17.030 1.00 16.89 A C ATOM 779 O TYR A 103 15.682 34.721 17.328 1.00 16.93 A O ATOM 780 N ASN A 104 14.967 32.600 17.341 1.00 15.51 A N ATOM 781 CA ASN A 104 13.893 32.910 18.257 1.00 14.63 A C ATOM 782 CB ASN A 104 13.665 31.743 19.205 1.00 14.81 A C ATOM 783 CG ASN A 104 14.612 31.750 20.400 1.00 15.08 A C ATOM 784 OD1 ASN A 104 15.024 32.796 20.896 1.00 15.19 A O ATOM 785 ND2 ASN A 104 14.920 30.571 20.894 1.00 14.99 A N ATOM 786 C ASN A 104 12.614 33.257 17.504 1.00 13.94 A C ATOM 787 O ASN A 104 11.578 32.636 17.730 1.00 13.92 A O ATOM 788 N ASN A 105 12.697 34.257 16.616 1.00 12.63 A N ATOM 789 CA ASN A 105 11.555 34.707 15.844 1.00 11.74 A C ATOM 790 CB ASN A 105 11.145 33.649 14.826 1.00 11.60 A C ATOM 791 CG ASN A 105 9.690 33.277 14.949 1.00 11.53 A C ATOM 792 OD1 ASN A 105 8.832 34.125 15.116 1.00 11.68 A O ATOM 793 ND2 ASN A 105 9.410 32.009 14.887 1.00 11.47 A N ATOM 794 C ASN A 105 11.738 36.035 15.116 1.00 11.37 A C ATOM 795 O ASN A 105 12.840 36.575 15.031 1.00 11.26 A O ATOM 796 N ALA A 106 10.614 36.562 14.637 1.00 11.03 A N ATOM 797 CA ALA A 106 10.579 37.638 13.650 1.00 10.62 A C ATOM 798 CB ALA A 106 10.233 38.958 14.290 1.00 10.51 A C ATOM 799 C ALA A 106 9.512 37.269 12.681 1.00 10.35 A C ATOM 800 O ALA A 106 8.663 36.428 12.992 1.00 10.10 A O ATOM 801 N PHE A 107 9.522 37.920 11.525 1.00 10.44 A N ATOM 802 CA PHE A 107 8.637 37.527 10.431 1.00 10.55 A C ATOM 803 CB PHE A 107 8.983 36.124 9.903 1.00 10.32 A C ATOM 804 CG PHE A 107 10.352 36.015 9.323 1.00 10.51 A C ATOM 805 CD2 PHE A 107 11.421 35.620 10.104 1.00 10.75 A C ATOM 806 CE2 PHE A 107 12.694 35.504 9.561 1.00 10.83 A C ATOM 807 CZ PHE A 107 12.905 35.812 8.233 1.00 10.89 A C ATOM 808 CE1 PHE A 107 11.841 36.197 7.445 1.00 10.78 A C ATOM 809 CD1 PHE A 107 10.575 36.280 7.994 1.00 10.79 A C ATOM 810 C PHE A 107 8.568 38.494 9.258 1.00 10.67 A C ATOM 811 O PHE A 107 9.372 39.418 9.136 1.00 10.36 A O ATOM 812 N TRP A 108 7.575 38.222 8.404 1.00 11.14 A N ATOM 813 CA TRP A 108 7.276 38.991 7.221 1.00 11.55 A C ATOM 814 CB TRP A 108 5.895 39.634 7.328 1.00 11.58 A C ATOM 815 CG TRP A 108 5.269 39.991 6.019 1.00 11.70 A C ATOM 816 CD1 TRP A 108 4.276 39.320 5.372 1.00 11.59 A C ATOM 817 NE1 TRP A 108 3.967 39.954 4.192 1.00 11.77 A N ATOM 818 CE2 TRP A 108 4.765 41.058 4.059 1.00 11.81 A C ATOM 819 CD2 TRP A 108 5.600 41.113 5.189 1.00 12.15 A C ATOM 820 CE3 TRP A 108 6.526 42.169 5.295 1.00 12.29 A C ATOM 821 CZ3 TRP A 108 6.583 43.109 4.277 1.00 11.79 A C ATOM 822 CH2 TRP A 108 5.736 43.017 3.178 1.00 11.69 A C ATOM 823 CZ2 TRP A 108 4.827 42.005 3.049 1.00 11.78 A C ATOM 824 C TRP A 108 7.301 38.046 6.058 1.00 11.89 A C ATOM 825 O TRP A 108 6.541 37.070 6.011 1.00 12.66 A O ATOM 826 N ASN A 109 8.146 38.361 5.086 1.00 12.02 A N ATOM 827 CA ASN A 109 8.413 37.441 3.998 1.00 11.55 A C ATOM 828 CB ASN A 109 9.910 37.250 3.866 1.00 10.98 A C ATOM 829 CG ASN A 109 10.615 38.456 3.291 1.00 10.78 A C ATOM 830 OD1 ASN A 109 10.027 39.428 2.857 1.00 9.78 A O ATOM 831 ND2 ASN A 109 11.918 38.378 3.297 1.00 11.23 A N ATOM 832 C ASN A 109 7.821 37.800 2.637 1.00 11.83 A C ATOM 833 O ASN A 109 8.205 37.180 1.653 1.00 12.98 A O ATOM 834 N GLY A 110 6.911 38.767 2.566 1.00 11.58 A N ATOM 835 CA GLY A 110 6.353 39.211 1.286 1.00 11.33 A C ATOM 836 C GLY A 110 6.978 40.526 0.825 1.00 11.37 A C ATOM 837 O GLY A 110 6.430 41.220 0.014 1.00 12.11 A O ATOM 838 N VAL A 111 8.105 40.898 1.404 1.00 11.10 A N ATOM 839 CA VAL A 111 8.926 42.006 0.912 1.00 10.97 A C ATOM 840 CB VAL A 111 10.193 41.411 0.186 1.00 11.34 A C ATOM 841 CG1 VAL A 111 11.387 42.362 0.056 1.00 11.21 A C ATOM 842 CG2 VAL A 111 9.789 40.889 1.181 1.00 11.73 A C ATOM 843 C VAL A 111 9.306 42.918 2.065 1.00 10.59 A C ATOM 844 O VAL A 111 9.366 44.119 1.902 1.00 10.53 A O ATOM 845 N GLN A 112 9.574 42.345 3.227 1.00 10.74 A N ATOM 846 CA GLN A 112 10.166 43.079 4.322 1.00 10.93 A C ATOM 847 CB GLN A 112 11.652 43.280 4.029 1.00 10.80 A C ATOM 848 CG GLN A 112 12.502 42.023 4.050 1.00 10.59 A C ATOM 849 CD GLN A 112 13.930 42.371 4.436 1.00 10.69 A C ATOM 850 OE1 GLN A 112 14.867 42.252 3.631 1.00 10.62 A O ATOM 851 NE2 GLN A 112 14.092 42.878 5.659 1.00 10.64 A N ATOM 852 C GLN A 112 10.020 42.410 5.681 1.00 11.08 A C ATOM 853 O GLN A 112 9.555 41.283 5.792 1.00 10.83 A O ATOM 854 N MET A 113 10.449 43.117 6.713 1.00 11.57 A N ATOM 855 CA MET A 113 10.386 42.607 8.068 1.00 12.22 A C ATOM 856 CB MET A 113 9.770 43.655 9.012 1.00 12.75 A C ATOM 857 CG MET A 113 8.248 43.793 8.921 1.00 12.88 A C ATOM 858 SD MET A 113 7.704 44.724 7.465 1.00 13.61 A S ATOM 859 CE MET A 113 8.484 46.336 7.684 1.00 12.88 A C ATOM 860 C MET A 113 11.779 42.229 8.566 1.00 12.30 A C ATOM 861 O MET A 113 12.777 42.930 8.298 1.00 11.89 A O ATOM 862 N VAL A 114 11.813 41.138 9.338 1.00 12.45 A N ATOM 863 CA VAL A 114 13.060 40.524 9.829 1.00 12.39 A C ATOM 864 CB VAL A 114 13.312 39.200 9.108 1.00 12.60 A C ATOM 865 CG1 VAL A 114 14.735 38.756 9.269 1.00 12.58 A C ATOM 866 CG2 VAL A 114 13.006 39.354 7.641 1.00 13.14 A C ATOM 867 C VAL A 114 12.892 40.165 11.291 1.00 11.82 A C ATOM 868 O VAL A 114 11.824 39.682 11.672 1.00 11.70 A O ATOM 869 N TYR A 115 13.943 40.368 12.085 1.00 11.01 A N ATOM 870 CA TYR A 115 13.868 40.205 13.517 1.00 10.70 A C ATOM 871 CB TYR A 115 13.724 41.578 14.192 1.00 10.58 A C ATOM 872 CG TYR A 115 12.538 42.408 13.680 1.00 10.64 A C ATOM 873 CD1 TYR A 115 11.258 42.218 14.179 1.00 10.65 A C ATOM 874 CE1 TYR A 115 10.189 42.936 13.703 1.00 10.73 A C ATOM 875 CZ TYR A 115 10.376 43.877 12.724 1.00 11.06 A C ATOM 876 OH TYR A 115 9.298 44.623 12.258 1.00 11.31 A O ATOM 877 CE2 TYR A 115 11.637 44.098 12.219 1.00 10.82 A C ATOM 878 CD2 TYR A 115 12.698 43.351 12.682 1.00 10.64 A C ATOM 879 C TYR A 115 15.103 39.493 14.016 1.00 10.93 A C ATOM 880 O TYR A 115 16.210 40.015 13.945 1.00 11.10 A O ATOM 881 N GLY A 116 14.917 38.278 14.505 1.00 11.20 A N ATOM 882 CA GLY A 116 15.952 37.601 15.247 1.00 11.38 A C ATOM 883 C GLY A 116 16.368 38.324 16.522 1.00 11.63 A C ATOM 884 O GLY A 116 15.747 39.265 16.955 1.00 10.90 A O ATOM 885 N ASP A 117 17.456 37.839 17.105 1.00 12.56 A N ATOM 886 CA ASP A 117 18.020 38.340 18.365 1.00 12.79 A C ATOM 887 CB ASP A 117 19.545 38.204 18.392 1.00 12.28 A C ATOM 888 CG ASP A 117 20.245 39.348 17.701 1.00 12.14 A C ATOM 889 OD1 ASP A 117 19.932 40.511 17.976 1.00 11.76 A O ATOM 890 OD2 ASP A 117 21.149 39.081 16.895 1.00 12.59 A O ATOM 891 C ASP A 117 17.509 37.570 19.541 1.00 13.10 A C ATOM 892 O ASP A 117 17.586 38.054 20.648 1.00 13.73 A O ATOM 893 N GLY A 118 17.039 36.356 19.301 1.00 13.57 A N ATOM 894 CA GLY A 118 16.573 35.481 20.364 1.00 13.80 A C ATOM 895 C GLY A 118 17.762 34.764 20.948 1.00 14.14 A C ATOM 896 O GLY A 118 18.900 35.121 20.631 1.00 14.07 A O ATOM 897 N ASP A 119 17.507 33.780 21.812 1.00 14.55 A N ATOM 898 CA ASP A 119 18.589 32.932 22.323 1.00 15.19 A C ATOM 899 CB ASP A 119 18.176 31.444 22.475 1.00 14.84 A C ATOM 900 CG ASP A 119 17.010 31.211 23.418 1.00 14.26 A C ATOM 901 OD1 ASP A 119 16.861 31.947 24.414 1.00 14.21 A O ATOM 902 OD2 ASP A 119 16.275 30.231 23.168 1.00 13.01 A O ATOM 903 C ASP A 119 19.192 33.458 23.599 1.00 16.45 A C ATOM 904 O ASP A 119 20.148 32.880 24.119 1.00 16.55 A O ATOM 905 N GLY A 120 18.645 34.573 24.091 1.00 18.15 A N ATOM 906 CA GLY A 120 19.134 35.212 25.316 1.00 18.51 A C ATOM 907 C GLY A 120 18.466 34.701 26.573 1.00 19.67 A C ATOM 908 O GLY A 120 18.547 35.358 27.603 1.00 21.88 A O ATOM 909 N VAL A 121 17.798 33.549 26.504 1.00 19.75 A N ATOM 910 CA VAL A 121 17.223 32.918 27.683 1.00 20.14 A C ATOM 911 CB VAL A 121 17.736 31.456 27.839 1.00 20.88 A C ATOM 912 CG1 VAL A 121 16.946 30.680 28.902 1.00 21.41 A C ATOM 913 CG2 VAL A 121 19.228 31.416 28.157 1.00 20.58 A C ATOM 914 C VAL A 121 15.679 32.991 27.596 1.00 20.30 A C ATOM 915 O VAL A 121 15.035 33.586 28.457 1.00 19.79 A O ATOM 916 N THR A 122 15.090 32.404 26.555 1.00 20.14 A N ATOM 917 CA THR A 122 13.635 32.494 26.351 1.00 19.96 A C ATOM 918 CB THR A 122 13.061 31.238 25.637 1.00 21.45 A C ATOM 919 OG1 THR A 122 13.999 30.796 24.662 1.00 24.36 A O ATOM 920 CG2 THR A 122 12.845 30.074 26.636 1.00 21.78 A C ATOM 921 C THR A 122 13.191 33.764 25.610 1.00 17.15 A C ATOM 922 O THR A 122 12.032 34.113 25.706 1.00 15.97 A O ATOM 923 N PHE A 123 14.103 34.428 24.892 1.00 15.54 A N ATOM 924 CA PHE A 123 13.837 35.724 24.212 1.00 14.59 A C ATOM 925 CB PHE A 123 13.458 35.540 22.736 1.00 14.75 A C ATOM 926 CG PHE A 123 12.146 34.912 22.502 1.00 14.63 A C ATOM 927 CD1 PHE A 123 11.007 35.663 22.517 1.00 15.07 A C ATOM 928 CE1 PHE A 123 9.772 35.088 22.268 1.00 15.58 A C ATOM 929 CZ PHE A 123 9.678 33.744 21.996 1.00 15.40 A C ATOM 930 CE2 PHE A 123 10.830 32.989 21.968 1.00 15.55 A C ATOM 931 CD2 PHE A 123 12.056 33.583 22.207 1.00 15.01 A C ATOM 932 C PHE A 123 15.054 36.631 24.117 1.00 13.43 A C ATOM 933 O PHE A 123 16.159 36.177 24.004 1.00 13.18 A O ATOM 934 N ILE A 124 14.808 37.916 24.031 1.00 13.11 A N ATOM 935 CA ILE A 124 15.829 38.898 23.717 1.00 12.99 A C ATOM 936 CB ILE A 124 15.856 40.029 24.779 1.00 13.41 A C ATOM 937 CG1 ILE A 124 14.577 40.925 24.768 1.00 13.15 A C ATOM 938 CD1 ILE A 124 14.749 42.242 25.530 1.00 12.52 A C ATOM 939 CG2 ILE A 124 16.078 39.429 26.161 1.00 13.31 A C ATOM 940 C ILE A 124 15.517 39.451 22.339 1.00 12.74 A C ATOM 941 O ILE A 124 14.551 39.000 21.705 1.00 13.23 A O ATOM 942 N PRO A 125 16.331 40.396 21.844 1.00 12.24 A N ATOM 943 CA PRO A 125 16.094 40.854 20.471 1.00 12.10 A C ATOM 944 CB PRO A 125 17.132 41.978 20.285 1.00 12.45 A C ATOM 945 CG PRO A 125 18.265 41.554 21.152 1.00 12.47 A C ATOM 946 CD PRO A 125 17.607 40.918 22.360 1.00 12.48 A C ATOM 947 C PRO A 125 14.674 41.348 20.232 1.00 11.45 A C ATOM 948 O PRO A 125 14.164 42.208 20.969 1.00 10.89 A O ATOM 949 N PHE A 126 14.071 40.769 19.199 1.00 10.85 A N ATOM 950 CA PHE A 126 12.645 40.875 18.936 1.00 10.71 A C ATOM 951 CB PHE A 126 12.247 39.967 17.783 1.00 10.54 A C ATOM 952 CG PHE A 126 12.017 38.547 18.201 1.00 10.47 A C ATOM 953 CD1 PHE A 126 13.050 37.780 18.712 1.00 10.57 A C ATOM 954 CE1 PHE A 126 12.828 36.463 19.123 1.00 10.33 A C ATOM 955 CZ PHE A 126 11.574 35.925 19.018 1.00 10.16 A C ATOM 956 CE2 PHE A 126 10.544 36.690 18.518 1.00 10.11 A C ATOM 957 CD2 PHE A 126 10.760 37.981 18.116 1.00 10.22 A C ATOM 958 C PHE A 126 12.090 42.276 18.691 1.00 10.71 A C ATOM 959 O PHE A 126 10.893 42.501 18.969 1.00 10.90 A O ATOM 960 N SER A 127 12.930 43.220 18.246 1.00 10.31 A N ATOM 961 CA SER A 127 12.456 44.588 18.018 1.00 10.08 A C ATOM 962 CB SER A 127 13.430 45.374 17.180 1.00 10.12 A C ATOM 963 OG SER A 127 14.738 45.075 17.550 1.00 10.16 A O ATOM 964 C SER A 127 12.147 45.358 19.281 1.00 9.98 A C ATOM 965 O SER A 127 11.453 46.356 19.242 1.00 10.28 A O ATOM 966 N ALA A 128 12.598 44.864 20.412 1.00 10.04 A N ATOM 967 CA ALA A 128 12.371 45.532 21.693 1.00 10.10 A C ATOM 968 CB ALA A 128 13.180 44.831 22.782 1.00 10.16 A C ATOM 969 C ALA A 128 10.899 45.715 22.144 1.00 10.16 A C ATOM 970 O ALA A 128 10.633 46.559 23.017 1.00 10.10 A O ATOM 971 N ASP A 129 9.957 44.956 21.580 1.00 10.09 A N ATOM 972 CA ASP A 129 8.545 45.186 21.882 1.00 10.27 A C ATOM 973 CB ASP A 129 7.842 43.893 22.314 1.00 10.08 A C ATOM 974 CG ASP A 129 6.541 44.156 23.060 1.00 10.15 A C ATOM 975 OD1 ASP A 129 5.845 45.112 22.681 1.00 10.22 A O ATOM 976 OD2 ASP A 129 6.191 43.422 24.030 1.00 10.06 A O ATOM 977 C ASP A 129 7.836 45.809 20.686 1.00 10.67 A C ATOM 978 O ASP A 129 7.789 45.228 19.607 1.00 11.36 A O ATOM 979 N PRO A 130 7.247 46.992 20.866 1.00 11.05 A N ATOM 980 CA PRO A 130 6.480 47.543 19.758 1.00 11.13 A C ATOM 981 CB PRO A 130 5.810 48.755 20.375 1.00 11.09 A C ATOM 982 CG PRO A 130 6.739 49.200 21.455 1.00 11.13 A C ATOM 983 CD PRO A 130 7.447 47.969 21.952 1.00 11.07 A C ATOM 984 C PRO A 130 5.425 46.594 19.201 1.00 11.90 A C ATOM 985 O PRO A 130 5.090 46.672 18.021 1.00 11.81 A O ATOM 986 N ASP A 131 4.871 45.691 20.012 1.00 12.81 A N ATOM 987 CA ASP A 131 3.767 44.936 19.473 1.00 13.21 A C ATOM 988 CB ASP A 131 2.861 44.298 20.538 1.00 12.98 A C ATOM 989 CG ASP A 131 3.566 43.310 21.446 1.00 13.07 A C ATOM 990 OD1 ASP A 131 4.133 42.275 21.008 1.00 13.36 A O ATOM 991 OD2 ASP A 131 3.468 43.524 22.667 1.00 13.50 A O ATOM 992 C ASP A 131 4.291 43.959 18.422 1.00 14.31 A C ATOM 993 O ASP A 131 3.505 43.461 17.584 1.00 14.98 A O ATOM 994 N VAL A 132 5.607 43.685 18.438 1.00 14.33 A N ATOM 995 CA VAL A 132 6.153 42.702 17.498 1.00 14.09 A C ATOM 996 CB VAL A 132 7.528 42.180 17.937 1.00 14.79 A C ATOM 997 CG1 VAL A 132 8.084 41.168 16.922 1.00 14.72 A C ATOM 998 CG2 VAL A 132 7.420 41.532 19.314 1.00 15.01 A C ATOM 999 C VAL A 132 6.253 43.352 16.140 1.00 13.25 A C ATOM 1000 O VAL A 132 5.903 42.755 15.150 1.00 12.79 A O ATOM 1001 N ILE A 133 6.691 44.603 16.121 1.00 12.74 A N ATOM 1002 CA ILE A 133 6.835 45.351 14.883 1.00 12.12 A C ATOM 1003 CB ILE A 133 7.565 46.703 15.122 1.00 12.05 A C ATOM 1004 CG1 ILE A 133 9.069 46.437 15.301 1.00 12.13 A C ATOM 1005 CD1 ILE A 133 9.507 46.212 16.734 1.00 12.16 A C ATOM 1006 CG2 ILE A 133 7.403 47.665 13.948 1.00 12.02 A C ATOM 1007 C ILE A 133 5.476 45.527 14.246 1.00 11.61 A C ATOM 1008 O ILE A 133 5.292 45.217 13.067 1.00 11.61 A O ATOM 1009 N GLY A 134 4.515 45.989 15.029 1.00 11.10 A N ATOM 1010 CA GLY A 134 3.132 46.092 14.555 1.00 10.85 A C ATOM 1011 C GLY A 134 2.611 44.784 13.982 1.00 10.75 A C ATOM 1012 O GLY A 134 1.919 44.773 12.946 1.00 11.06 A O ATOM 1013 N HIS A 135 2.962 43.675 14.631 1.00 10.39 A N ATOM 1014 CA HIS A 135 2.510 42.340 14.219 1.00 10.07 A C ATOM 1015 CB HIS A 135 2.987 41.329 15.262 1.00 9.93 A C ATOM 1016 CG HIS A 135 2.513 39.933 15.049 1.00 9.63 A C ATOM 1017 ND1 HIS A 135 1.472 39.389 15.765 1.00 9.67 A N ATOM 1018 CE1 HIS A 135 1.291 38.133 15.392 1.00 9.59 A C ATOM 1019 NE2 HIS A 135 2.181 37.845 14.459 1.00 9.71 A N ATOM 1020 CD2 HIS A 135 2.964 38.953 14.237 1.00 9.62 A C ATOM 1021 C HIS A 135 3.024 41.996 12.813 1.00 10.10 A C ATOM 1022 O HIS A 135 2.251 41.630 11.902 1.00 10.09 A O ATOM 1023 N GLU A 136 4.326 42.136 12.624 1.00 10.10 A N ATOM 1024 CA GLU A 136 4.951 41.752 11.347 1.00 10.17 A C ATOM 1025 CB GLU A 136 6.475 41.654 11.514 1.00 10.47 A C ATOM 1026 CG GLU A 136 6.894 40.641 12.554 1.00 10.55 A C ATOM 1027 CD GLU A 136 6.148 39.345 12.359 1.00 11.18 A C ATOM 1028 OE1 GLU A 136 5.972 38.931 11.195 1.00 11.67 A O ATOM 1029 OE2 GLU A 136 5.723 38.736 13.351 1.00 11.52 A O ATOM 1030 C GLU A 136 4.592 42.714 10.224 1.00 9.84 A C ATOM 1031 O GLU A 136 4.247 42.287 9.155 1.00 9.75 A O ATOM 1032 N LEU A 137 4.638 44.006 10.482 1.00 9.71 A N ATOM 1033 CA LEU A 137 4.113 44.998 9.549 1.00 10.13 A C ATOM 1034 CB LEU A 137 4.199 46.328 10.278 1.00 10.76 A C ATOM 1035 CG LEU A 137 4.003 47.670 9.581 1.00 11.56 A C ATOM 1036 CD1 LEU A 137 2.714 47.741 8.743 1.00 11.82 A C ATOM 1037 CD2 LEU A 137 5.230 48.010 8.760 1.00 11.81 A C ATOM 1038 C LEU A 137 2.644 44.669 9.113 1.00 9.92 A C ATOM 1039 O LEU A 137 2.286 44.625 7.953 1.00 9.14 A O ATOM 1040 N THR A 138 1.796 44.397 10.086 1.00 10.20 A N ATOM 1041 CA THR A 138 0.425 44.011 9.817 1.00 10.26 A C ATOM 1042 CB THR A 138 0.361 43.954 11.146 1.00 10.02 A C ATOM 1043 OG1 THR A 138 0.355 45.258 11.754 1.00 9.32 A O ATOM 1044 CG2 THR A 138 1.785 43.463 10.929 1.00 9.83 A C ATOM 1045 C THR A 138 0.303 42.695 8.973 1.00 10.57 A C ATOM 1046 O THR A 138 0.662 42.538 8.183 1.00 10.60 A O ATOM 1047 N HIS A 139 1.263 41.771 9.095 1.00 10.54 A N ATOM 1048 CA HIS A 139 1.272 40.620 8.177 1.00 10.42 A C ATOM 1049 CB HIS A 139 2.468 39.695 8.370 1.00 10.27 A C ATOM 1050 CG HIS A 139 2.317 38.717 9.486 1.00 10.44 A C ATOM 1051 ND1 HIS A 139 1.094 38.259 9.918 1.00 10.59 A N ATOM 1052 CE1 HIS A 139 1.265 37.406 10.914 1.00 10.87 A C ATOM 1053 NE2 HIS A 139 2.563 37.285 11.142 1.00 11.18 A N ATOM 1054 CD2 HIS A 139 3.241 38.089 10.249 1.00 10.94 A C ATOM 1055 C HIS A 139 1.245 41.129 6.747 1.00 10.73 A C ATOM 1056 O HIS A 139 0.491 40.621 5.920 1.00 10.94 A O ATOM 1057 N GLY A 140 2.052 42.151 6.466 1.00 11.04 A N ATOM 1058 CA GLY A 140 2.056 42.807 5.160 1.00 10.90 A C ATOM 1059 C GLY A 140 0.692 43.407 4.803 1.00 10.98 A C ATOM 1060 O GLY A 140 0.171 43.198 3.693 1.00 11.37 A O ATOM 1061 N VAL A 141 0.086 44.150 5.726 1.00 10.36 A N ATOM 1062 CA VAL A 141 1.177 44.811 5.416 1.00 9.75 A C ATOM 1063 CB VAL A 141 1.682 45.578 6.619 1.00 9.53 A C ATOM 1064 CG1 VAL A 141 3.058 46.151 6.348 1.00 9.58 A C ATOM 1065 CG2 VAL A 141 0.705 46.676 6.968 1.00 9.43 A C ATOM 1066 C VAL A 141 2.215 43.784 5.013 1.00 9.84 A C ATOM 1067 O VAL A 141 2.931 43.938 4.031 1.00 9.44 A O ATOM 1068 N THR A 142 2.255 42.703 5.779 1.00 10.29 A N ATOM 1069 CA THR A 142 3.151 41.590 5.513 1.00 10.26 A C ATOM 1070 CB THR A 142 3.000 40.503 6.577 1.00 10.08 A C ATOM 1071 OG1 THR A 142 3.358 41.026 7.880 1.00 9.80 A O ATOM 1072 CG2 THR A 142 3.871 39.305 6.210 1.00 10.03 A C ATOM 1073 C THR A 142 2.904 40.965 4.158 1.00 10.52 A C ATOM 1074 O THR A 142 3.843 40.718 3.399 1.00 10.56 A O ATOM 1075 N GLU A 143 1.650 40.695 3.841 1.00 10.94 A N ATOM 1076 CA GLU A 143 1.352 40.031 2.570 1.00 11.25 A C ATOM 1077 CB GLU A 143 0.118 39.677 2.462 1.00 11.65 A C ATOM 1078 CG GLU A 143 0.691 39.862 1.082 1.00 12.22 A C ATOM 1079 CD GLU A 143 1.934 39.052 0.832 1.00 12.99 A C ATOM 1080 OE1 GLU A 143 2.020 38.543 0.317 1.00 12.86 A O ATOM 1081 OE2 GLU A 143 2.804 38.922 1.764 1.00 13.79 A O ATOM 1082 C GLU A 143 1.782 40.903 1.415 1.00 11.45 A C ATOM 1083 O GLU A 143 2.210 40.390 0.398 1.00 11.64 A O ATOM 1084 N HIS A 144 1.680 42.218 1.589 1.00 11.88 A N ATOM 1085 CA HIS A 144 2.095 43.209 0.589 1.00 12.29 A C ATOM 1086 CB HIS A 144 1.247 44.484 0.746 1.00 13.27 A C ATOM 1087 CG HIS A 144 0.045 44.440 0.009 1.00 14.23 A C ATOM 1088 ND1 HIS A 144 1.080 43.600 0.368 1.00 15.20 A N ATOM 1089 CE1 HIS A 144 2.097 43.770 0.457 1.00 15.20 A C ATOM 1090 NE2 HIS A 144 1.749 44.684 1.343 1.00 15.38 A N ATOM 1091 CD2 HIS A 144 0.467 45.116 1.079 1.00 14.62 A C ATOM 1092 C HIS A 144 3.586 43.619 0.631 1.00 11.95 A C ATOM 1093 O HIS A 144 4.007 44.456 0.135 1.00 11.54 A O ATOM 1094 N THR A 145 4.383 43.055 1.532 1.00 11.84 A N ATOM 1095 CA THR A 145 5.798 43.407 1.620 1.00 11.38 A C ATOM 1096 CB THR A 145 6.062 44.234 2.900 1.00 11.59 A C ATOM 1097 OG1 THR A 145 5.547 43.557 4.068 1.00 11.59 A O ATOM 1098 CG2 THR A 145 5.398 45.593 2.785 1.00 11.38 A C ATOM 1099 C THR A 145 6.655 42.135 1.532 1.00 11.05 A C ATOM 1100 O THR A 145 6.939 41.644 0.443 1.00 11.35 A O ATOM 1101 N ALA A 146 7.038 41.572 2.667 1.00 10.67 A N ATOM 1102 CA ALA A 146 7.849 40.366 2.692 1.00 10.41 A C ATOM 1103 CB ALA A 146 8.226 40.046 4.120 1.00 10.53 A C ATOM 1104 C ALA A 146 7.137 39.167 2.080 1.00 10.31 A C ATOM 1105 O ALA A 146 7.769 38.361 1.394 1.00 9.96 A O ATOM 1106 N GLY A 147 5.827 39.051 2.349 1.00 10.33 A N ATOM 1107 CA GLY A 147 5.001 37.925 1.877 1.00 10.08 A C ATOM 1108 C GLY A 147 5.238 36.619 2.623 1.00 10.00 A C ATOM 1109 O GLY A 147 4.962 35.549 2.107 1.00 9.60 A O ATOM 1110 N LEU A 148 5.745 36.706 3.848 1.00 10.31 A N ATOM 1111 CA LEU A 148 5.933 35.528 4.707 1.00 10.49 A C ATOM 1112 CB LEU A 148 6.018 35.939 6.165 1.00 10.25 A C ATOM 1113 CG LEU A 148 7.210 36.812 6.508 1.00 10.29 A C ATOM 1114 CD1 LEU A 148 6.994 37.473 7.848 1.00 10.47 A C ATOM 1115 CD2 LEU A 148 8.476 36.004 6.551 1.00 10.32 A C ATOM 1116 C LEU A 148 4.772 34.565 4.557 1.00 10.94 A C ATOM 1117 O LEU A 148 3.636 34.881 4.915 1.00 10.71 A O ATOM 1118 N GLU A 149 5.066 33.387 4.026 1.00 11.38 A N ATOM 1119 CA GLU A 149 4.042 32.384 3.824 1.00 11.72 A C ATOM 1120 CB GLU A 149 4.614 31.224 3.046 1.00 12.01 A C ATOM 1121 CG GLU A 149 4.981 31.624 1.637 1.00 12.44 A C ATOM 1122 CD GLU A 149 5.857 30.602 0.954 1.00 12.98 A C ATOM 1123 OE1 GLU A 149 6.421 29.712 1.679 1.00 13.15 A O ATOM 1124 OE2 GLU A 149 5.975 30.714 0.305 1.00 12.81 A O ATOM 1125 C GLU A 149 3.503 31.865 5.139 1.00 11.83 A C ATOM 1126 O GLU A 149 4.282 31.557 6.060 1.00 11.79 A O ATOM 1127 N TYR A 150 2.178 31.724 5.199 1.00 11.76 A N ATOM 1128 CA TYR A 150 1.503 31.382 6.438 1.00 11.73 A C ATOM 1129 CB TYR A 150 0.047 31.854 6.381 1.00 11.48 A C ATOM 1130 CG TYR A 150 0.495 32.275 7.722 1.00 11.34 A C ATOM 1131 CD1 TYR A 150 0.009 33.409 8.366 1.00 11.48 A C ATOM 1132 CE1 TYR A 150 0.488 33.787 9.606 1.00 11.42 A C ATOM 1133 CZ TYR A 150 1.466 33.024 10.215 1.00 11.47 A C ATOM 1134 OH TYR A 150 1.983 33.385 11.434 1.00 11.35 A O ATOM 1135 CE2 TYR A 150 1.948 31.898 9.591 1.00 11.34 A C ATOM 1136 CD2 TYR A 150 1.465 31.540 8.353 1.00 11.15 A C ATOM 1137 C TYR A 150 1.594 29.893 6.778 1.00 12.17 A C ATOM 1138 O TYR A 150 0.579 29.194 6.852 1.00 11.75 A O ATOM 1139 N TYR A 151 2.820 29.409 7.010 1.00 13.06 A N ATOM 1140 CA TYR A 151 3.052 27.998 7.425 1.00 13.68 A C ATOM 1141 CB TYR A 151 2.853 27.019 6.258 1.00 14.30 A C ATOM 1142 CG TYR A 151 2.377 25.641 6.701 1.00 15.46 A C ATOM 1143 CD1 TYR A 151 3.284 24.631 7.111 1.00 16.45 A C ATOM 1144 CE1 TYR A 151 2.838 23.378 7.544 1.00 16.21 A C ATOM 1145 CZ TYR A 151 1.480 23.114 7.542 1.00 16.63 A C ATOM 1146 OH TYR A 151 0.955 21.884 7.943 1.00 17.27 A O ATOM 1147 CE2 TYR A 151 0.586 24.098 7.141 1.00 16.39 A C ATOM 1148 CD2 TYR A 151 1.036 25.341 6.732 1.00 15.76 A C ATOM 1149 C TYR A 151 4.455 27.817 7.980 1.00 13.62 A C ATOM 1150 O TYR A 151 5.397 28.390 7.467 1.00 14.39 A O ATOM 1151 N GLY A 152 4.614 27.011 9.019 1.00 13.51 A N ATOM 1152 CA GLY A 152 5.939 26.701 9.531 1.00 13.34 A C ATOM 1153 C GLY A 152 6.653 27.917 10.097 1.00 13.83 A C ATOM 1154 O GLY A 152 6.032 28.807 10.695 1.00 14.49 A O ATOM 1155 N GLU A 153 7.966 27.961 9.916 1.00 13.72 A N ATOM 1156 CA GLU A 153 8.749 29.047 10.468 1.00 13.56 A C ATOM 1157 CB GLU A 153 10.238 28.725 10.362 1.00 13.75 A C ATOM 1158 CG GLU A 153 10.664 27.555 11.240 1.00 13.88 A C ATOM 1159 CD GLU A 153 12.180 27.399 11.424 1.00 14.09 A C ATOM 1160 OE1 GLU A 153 12.942 28.380 11.352 1.00 14.77 A O ATOM 1161 OE2 GLU A 153 12.626 26.283 11.700 1.00 13.79 A O ATOM 1162 C GLU A 153 8.392 30.427 9.867 1.00 13.23 A C ATOM 1163 O GLU A 153 8.317 31.407 10.607 1.00 13.02 A O ATOM 1164 N SER A 154 8.152 30.502 8.556 1.00 13.06 A N ATOM 1165 CA SER A 154 7.720 31.766 7.919 1.00 12.61 A C ATOM 1166 CB SER A 154 7.509 31.629 6.409 1.00 12.60 A C ATOM 1167 OG SER A 154 6.935 30.397 6.002 1.00 12.59 A O ATOM 1168 C SER A 154 6.438 32.211 8.546 1.00 12.47 A C ATOM 1169 O SER A 154 6.205 33.388 8.804 1.00 12.67 A O ATOM 1170 N GLY A 155 5.586 31.245 8.817 1.00 12.56 A N ATOM 1171 CA GLY A 155 4.310 31.540 9.447 1.00 12.03 A C ATOM 1172 C GLY A 155 4.443 32.051 10.869 1.00 11.39 A C ATOM 1173 O GLY A 155 3.646 32.860 11.295 1.00 11.89 A O ATOM 1174 N ALA A 156 5.413 31.568 11.633 1.00 10.56 A N ATOM 1175 CA ALA A 156 5.536 32.047 13.008 1.00 9.90 A C ATOM 1176 CB ALA A 156 6.481 31.175 13.804 1.00 9.92 A C ATOM 1177 C ALA A 156 6.015 33.501 13.004 1.00 9.25 A C ATOM 1178 O ALA A 156 5.502 34.330 13.728 1.00 9.03 A O ATOM 1179 N LEU A 157 7.020 33.773 12.184 1.00 8.76 A N ATOM 1180 CA LEU A 157 7.532 35.104 11.970 1.00 8.36 A C ATOM 1181 CB LEU A 157 8.540 35.070 10.837 1.00 8.37 A C ATOM 1182 CG LEU A 157 10.041 35.045 11.062 1.00 8.61 A C ATOM 1183 CD1 LEU A 157 10.463 34.666 12.454 1.00 8.77 A C ATOM 1184 CD2 LEU A 157 10.705 34.119 10.052 1.00 8.91 A C ATOM 1185 C LEU A 157 6.376 36.025 11.596 1.00 8.07 A C ATOM 1186 O LEU A 157 6.255 37.135 12.142 1.00 7.77 A O ATOM 1187 N ASN A 158 5.538 35.544 10.669 1.00 7.73 A N ATOM 1188 CA ASN A 158 4.376 36.292 10.195 1.00 7.65 A C ATOM 1189 CB ASN A 158 3.618 35.443 9.175 1.00 7.60 A C ATOM 1190 CG ASN A 158 2.454 36.174 8.544 1.00 7.45 A C ATOM 1191 OD1 ASN A 158 2.219 36.081 7.338 1.00 7.24 A O ATOM 1192 ND2 ASN A 158 1.713 36.889 9.354 1.00 7.41 A N ATOM 1193 C ASN A 158 3.454 36.711 11.351 1.00 7.65 A C ATOM 1194 O ASN A 158 3.092 37.888 11.501 1.00 7.48 A O ATOM 1195 N GLU A 159 3.108 35.731 12.180 1.00 7.81 A N ATOM 1196 CA GLU A 159 2.317 35.962 13.381 1.00 7.91 A C ATOM 1197 CB GLU A 159 1.910 34.630 14.000 1.00 7.94 A C ATOM 1198 CG GLU A 159 0.601 34.083 13.429 1.00 8.02 A C ATOM 1199 CD GLU A 159 0.576 34.968 13.795 1.00 8.26 A C ATOM 1200 OE1 GLU A 159 0.653 35.249 15.012 1.00 8.90 A O ATOM 1201 OE2 GLU A 159 1.397 35.417 12.935 1.00 8.04 A O ATOM 1202 C GLU A 159 3.072 36.857 14.356 1.00 8.02 A C ATOM 1203 O GLU A 159 2.509 37.755 14.950 1.00 8.32 A O ATOM 1204 N SER A 160 4.373 36.676 14.460 1.00 8.05 A N ATOM 1205 CA SER A 160 5.141 37.443 15.423 1.00 7.94 A C ATOM 1206 CB SER A 160 6.597 36.950 15.477 1.00 7.76 A C ATOM 1207 OG SER A 160 7.318 37.607 16.500 1.00 7.64 A O ATOM 1208 C SER A 160 5.060 38.907 15.036 1.00 8.03 A C ATOM 1209 O SER A 160 4.736 39.785 15.860 1.00 7.90 A O ATOM 1210 N ILE A 161 5.343 39.165 13.767 1.00 8.08 A N ATOM 1211 CA ILE A 161 5.358 40.532 13.276 1.00 8.23 A C ATOM 1212 CB ILE A 161 5.615 40.592 11.763 1.00 8.23 A C ATOM 1213 CG1 ILE A 161 7.021 40.033 11.446 1.00 8.35 A C ATOM 1214 CD1 ILE A 161 8.170 41.019 11.674 1.00 8.40 A C ATOM 1215 CG2 ILE A 161 5.459 42.016 11.243 1.00 8.11 A C ATOM 1216 C ILE A 161 4.017 41.190 13.593 1.00 8.64 A C ATOM 1217 O ILE A 161 3.995 42.329 14.107 1.00 8.86 A O ATOM 1218 N SER A 162 2.903 40.468 13.327 1.00 8.55 A N ATOM 1219 CA SER A 162 1.563 41.009 13.583 1.00 8.24 A C ATOM 1220 CB SER A 162 0.470 40.063 13.041 1.00 8.36 A C ATOM 1221 OG SER A 162 0.268 40.222 11.610 1.00 8.36 A O ATOM 1222 C SER A 162 1.401 41.315 15.066 1.00 7.96 A C ATOM 1223 O SER A 162 0.870 42.360 15.452 1.00 7.78 A O ATOM 1224 N ASP A 163 1.900 40.410 15.891 1.00 7.89 A N ATOM 1225 CA ASP A 163 1.939 40.609 17.346 1.00 8.00 A C ATOM 1226 CB ASP A 163 2.451 39.323 18.029 1.00 7.81 A C ATOM 1227 CG ASP A 163 1.371 38.310 18.242 1.00 7.61 A C ATOM 1228 OD1 ASP A 163 0.228 38.669 17.919 1.00 7.69 A O ATOM 1229 OD2 ASP A 163 1.637 37.194 18.750 1.00 7.24 A O ATOM 1230 C ASP A 163 2.842 41.791 17.764 1.00 8.39 A C ATOM 1231 O ASP A 163 2.464 42.654 18.573 1.00 8.14 A O ATOM 1232 N ILE A 164 4.058 41.823 17.223 1.00 8.75 A N ATOM 1233 CA ILE A 164 4.955 42.900 17.590 1.00 9.10 A C ATOM 1234 CB ILE A 164 6.308 42.744 16.902 1.00 8.62 A C ATOM 1235 CG1 ILE A 164 7.058 41.631 17.541 1.00 8.29 A C ATOM 1236 CD1 ILE A 164 7.945 40.950 16.552 1.00 8.37 A C ATOM 1237 CG2 ILE A 164 7.109 44.018 17.007 1.00 8.59 A C ATOM 1238 C ILE A 164 4.326 44.280 17.276 1.00 9.63 A C ATOM 1239 O ILE A 164 4.408 45.188 18.076 1.00 9.83 A O ATOM 1240 N ILE A 165 3.688 44.427 16.125 1.00 10.31 A N ATOM 1241 CA ILE A 165 3.113 45.730 15.759 1.00 11.09 A C ATOM 1242 CB ILE A 165 3.142 45.965 14.238 1.00 11.45 A C ATOM 1243 CG1 ILE A 165 4.583 46.312 13.859 1.00 11.73 A C ATOM 1244 CD1 ILE A 165 4.846 46.351 12.376 1.00 12.06 A C ATOM 1245 CG2 ILE A 165 2.257 47.137 13.843 1.00 11.71 A C ATOM 1246 C ILE A 165 1.743 45.953 16.396 1.00 11.24 A C ATOM 1247 O ILE A 165 1.519 46.993 16.983 1.00 10.71 A O ATOM 1248 N GLY A 166 0.866 44.956 16.352 1.00 11.84 A N ATOM 1249 CA GLY A 166 0.347 44.989 17.161 1.00 12.20 A C ATOM 1250 C GLY A 166 0.114 45.522 18.568 1.00 12.55 A C ATOM 1251 O GLY A 166 0.856 46.371 19.055 1.00 13.27 A O ATOM 1252 N ASN A 167 0.936 45.042 19.219 1.00 13.01 A N ATOM 1253 CA ASN A 167 1.211 45.411 20.617 1.00 13.46 A C ATOM 1254 CB ASN A 167 2.130 44.379 21.255 1.00 13.54 A C ATOM 1255 CG ASN A 167 2.598 44.799 22.620 1.00 13.80 A C ATOM 1256 OD1 ASN A 167 3.650 45.428 22.768 1.00 13.76 A O ATOM 1257 ND2 ASN A 167 1.794 44.495 23.630 1.00 13.97 A N ATOM 1258 C ASN A 167 1.831 46.800 20.769 1.00 13.70 A C ATOM 1259 O ASN A 167 1.633 47.497 21.769 1.00 13.68 A O ATOM 1260 N ALA A 168 2.607 47.179 19.767 1.00 14.07 A N ATOM 1261 CA ALA A 168 3.260 48.453 19.765 1.00 13.94 A C ATOM 1262 CB ALA A 168 4.247 48.531 18.618 1.00 13.53 A C ATOM 1263 C ALA A 168 2.231 49.547 19.667 1.00 14.33 A C ATOM 1264 O ALA A 168 2.429 50.581 20.227 1.00 13.98 A O ATOM 1265 N ILE A 169 1.131 49.324 18.960 1.00 15.94 A N ATOM 1266 CA ILE A 169 0.218 50.428 18.655 1.00 18.10 A C ATOM 1267 CB ILE A 169 0.969 50.037 17.743 1.00 18.79 A C ATOM 1268 CG1 ILE A 169 0.561 50.080 16.280 1.00 19.73 A C ATOM 1269 CD1 ILE A 169 0.048 48.784 15.730 1.00 20.46 A C ATOM 1270 CG2 ILE A 169 2.130 51.016 17.942 1.00 18.64 A C ATOM 1271 C ILE A 169 0.394 50.822 19.949 1.00 19.50 A C ATOM 1272 O ILE A 169 0.420 51.982 20.301 1.00 17.56 A O ATOM 1273 N ASP A 170 0.941 49.782 20.581 1.00 22.96 A N ATOM 1274 CA ASP A 170 1.495 49.783 21.922 1.00 25.80 A C ATOM 1275 CB ASP A 170 1.761 48.290 22.319 1.00 28.80 A C ATOM 1276 CG ASP A 170 3.056 48.077 23.198 1.00 31.65 A C ATOM 1277 OD1 ASP A 170 3.727 49.094 23.585 1.00 32.68 A O ATOM 1278 OD2 ASP A 170 3.385 46.874 23.485 1.00 27.68 A O ATOM 1279 C ASP A 170 0.556 50.556 22.895 1.00 25.17 A C ATOM 1280 O ASP A 170 0.916 51.613 23.330 1.00 26.97 A O ATOM 1281 N GLY A 171 0.654 50.077 23.186 1.00 25.32 A N ATOM 1282 CA GLY A 171 1.589 50.813 24.048 1.00 25.14 A C ATOM 1283 C GLY A 171 1.799 50.195 25.428 1.00 26.60 A C ATOM 1284 O GLY A 171 2.914 50.233 25.976 1.00 26.53 A O ATOM 1285 N LYS A 172 0.759 49.524 25.930 1.00 26.94 A N ATOM 1286 CA LYS A 172 0.444 49.463 27.366 1.00 26.88 A C ATOM 1287 CB LYS A 172 1.051 49.132 27.537 1.00 30.72 A C ATOM 1288 CG LYS A 172 2.071 50.219 27.134 1.00 33.65 A C ATOM 1289 CD LYS A 172 3.392 50.025 27.922 1.00 36.81 A C ATOM 1290 CE LYS A 172 4.669 50.070 27.073 1.00 38.06 A C ATOM 1291 NZ LYS A 172 5.038 48.814 26.339 1.00 36.90 A N ATOM 1292 C LYS A 172 1.213 48.471 28.238 1.00 23.70 A C ATOM 1293 O LYS A 172 1.584 48.768 29.365 1.00 23.20 A O ATOM 1294 N ASN A 173 1.390 47.273 27.716 1.00 20.08 A N ATOM 1295 CA ASN A 173 1.898 46.146 28.467 1.00 17.00 A C ATOM 1296 CB ASN A 173 0.736 45.383 29.125 1.00 16.90 A C ATOM 1297 CG ASN A 173 0.422 45.079 28.148 1.00 16.63 A C ATOM 1298 OD1 ASN A 173 0.260 44.495 27.064 1.00 15.50 A O ATOM 1299 ND2 ASN A 173 1.602 45.470 28.552 1.00 16.78 A N ATOM 1300 C ASN A 173 2.538 45.275 27.429 1.00 14.76 A C ATOM 1301 O ASN A 173 2.573 45.681 26.284 1.00 15.23 A O ATOM 1302 N TRP A 174 2.986 44.078 27.784 1.00 12.57 A N ATOM 1303 CA TRP A 174 3.504 43.159 26.790 1.00 11.39 A C ATOM 1304 CB TRP A 174 4.895 42.700 27.180 1.00 11.51 A C ATOM 1305 CG TRP A 174 5.894 43.735 27.116 1.00 11.10 A C ATOM 1306 CD1 TRP A 174 6.445 44.349 28.137 1.00 10.94 A C ATOM 1307 NE1 TRP A 174 7.375 45.235 27.722 1.00 11.20 A N ATOM 1308 CE2 TRP A 174 7.431 45.189 26.362 1.00 11.59 A C ATOM 1309 CD2 TRP A 174 6.499 44.247 25.953 1.00 11.43 A C ATOM 1310 CE3 TRP A 174 6.344 44.000 24.584 1.00 11.96 A C ATOM 1311 CZ3 TRP A 174 7.125 44.722 23.675 1.00 11.80 A C ATOM 1312 CH2 TRP A 174 8.045 45.657 24.122 1.00 11.84 A C ATOM 1313 CZ2 TRP A 174 8.216 45.910 25.461 1.00 11.89 A C ATOM 1314 C TRP A 174 2.619 41.936 26.558 1.00 10.44 A C ATOM 1315 O TRP A 174 3.119 40.869 26.219 1.00 9.94 A O ATOM 1316 N LEU A 175 1.309 42.121 26.673 1.00 9.73 A N ATOM 1317 CA LEU A 175 0.346 41.082 26.370 1.00 9.50 A C ATOM 1318 CB LEU A 175 0.739 41.054 27.450 1.00 9.31 A C ATOM 1319 CG LEU A 175 0.164 41.226 28.865 1.00 9.05 A C ATOM 1320 CD1 LEU A 175 1.260 41.361 29.880 1.00 8.82 A C ATOM 1321 CD2 LEU A 175 0.776 40.096 29.223 1.00 8.97 A C ATOM 1322 C LEU A 175 0.308 41.248 24.998 1.00 9.46 A C ATOM 1323 O LEU A 175 0.256 42.298 24.395 1.00 9.36 A O ATOM 1324 N ILE A 176 0.927 40.172 24.528 1.00 9.67 A N ATOM 1325 CA ILE A 176 1.810 40.190 23.373 1.00 9.57 A C ATOM 1326 CB ILE A 176 1.257 39.265 22.274 1.00 9.83 A C ATOM 1327 CG1 ILE A 176 0.182 39.690 21.898 1.00 10.01 A C ATOM 1328 CD1 ILE A 176 0.280 41.016 21.150 1.00 9.93 A C ATOM 1329 CG2 ILE A 176 2.184 39.218 21.049 1.00 9.82 A C ATOM 1330 C ILE A 176 3.206 39.704 23.778 1.00 9.56 A C ATOM 1331 O ILE A 176 3.349 38.639 24.428 1.00 8.84 A O ATOM 1332 N GLY A 177 4.220 40.486 23.367 1.00 9.68 A N ATOM 1333 CA GLY A 177 5.622 40.131 23.517 1.00 9.79 A C ATOM 1334 C GLY A 177 6.120 40.170 24.946 1.00 10.29 A C ATOM 1335 O GLY A 177 7.167 39.604 25.249 1.00 10.78 A O ATOM 1336 N ASP A 178 5.381 40.826 25.840 1.00 10.68 A N ATOM 1337 CA ASP A 178 5.808 40.998 27.226 1.00 10.63 A C ATOM 1338 CB ASP A 178 4.848 41.873 28.063 1.00 10.79 A C ATOM 1339 CG ASP A 178 4.414 43.165 27.352 1.00 11.25 A C ATOM 1340 OD1 ASP A 178 4.028 43.125 26.137 1.00 11.72 A O ATOM 1341 OD2 ASP A 178 4.445 44.230 28.017 1.00 11.08 A O ATOM 1342 C ASP A 178 7.221 41.536 27.336 1.00 10.59 A C ATOM 1343 O ASP A 178 7.904 41.156 28.272 1.00 11.28 A O ATOM 1344 N LEU A 179 7.671 42.364 26.395 1.00 10.20 A N ATOM 1345 CA LEU A 179 8.985 43.023 26.512 1.00 10.39 A C ATOM 1346 CB LEU A 179 8.959 44.429 25.884 1.00 10.21 A C ATOM 1347 CG LEU A 179 8.140 45.483 26.620 1.00 10.17 A C ATOM 1348 CD1 LEU A 179 8.127 46.713 25.763 1.00 10.31 A C ATOM 1349 CD2 LEU A 179 8.653 45.828 28.003 1.00 9.96 A C ATOM 1350 C LEU A 179 10.171 42.272 25.891 1.00 10.69 A C ATOM 1351 O LEU A 179 11.324 42.757 25.993 1.00 10.57 A O ATOM 1352 N ILE A 180 9.884 41.142 25.240 1.00 10.58 A N ATOM 1353 CA ILE A 180 10.901 40.329 24.611 1.00 10.92 A C ATOM 1354 CB ILE A 180 10.662 40.171 23.101 1.00 11.08 A C ATOM 1355 CG1 ILE A 180 9.227 39.759 22.788 1.00 10.99 A C ATOM 1356 CD1 ILE A 180 9.107 39.174 21.404 1.00 11.00 A C ATOM 1357 CG2 ILE A 180 10.988 41.455 22.355 1.00 11.54 A C ATOM 1358 C ILE A 180 11.031 38.915 25.192 1.00 11.35 A C ATOM 1359 O ILE A 180 12.085 38.286 25.012 1.00 11.56 A O ATOM 1360 N TYR A 181 9.969 38.421 25.844 1.00 11.08 A N ATOM 1361 CA TYR A 181 9.888 37.060 26.366 1.00 11.01 A C ATOM 1362 CB TYR A 181 8.420 36.640 26.406 1.00 10.90 A C ATOM 1363 CG TYR A 181 8.183 35.157 26.669 1.00 10.79 A C ATOM 1364 CD1 TYR A 181 8.717 34.181 25.830 1.00 10.58 A C ATOM 1365 CE1 TYR A 181 8.480 32.830 26.058 1.00 10.73 A C ATOM 1366 CZ TYR A 181 7.665 32.423 27.122 1.00 10.52 A C ATOM 1367 OH TYR A 181 7.417 31.084 27.349 1.00 9.91 A O ATOM 1368 CE2 TYR A 181 7.122 33.375 27.956 1.00 10.67 A C ATOM 1369 CD2 TYR A 181 7.377 34.734 27.723 1.00 10.92 A C ATOM 1370 C TYR A 181 10.429 36.894 27.772 1.00 11.14 A C ATOM 1371 O TYR A 181 10.050 37.616 28.648 1.00 11.55 A O ATOM 1372 N THR A 182 11.277 35.901 28.001 1.00 12.04 A N ATOM 1373 CA THR A 182 11.754 35.522 29.366 1.00 12.29 A C ATOM 1374 CB THR A 182 10.647 34.772 30.147 1.00 12.04 A C ATOM 1375 OG1 THR A 182 9.549 35.675 30.435 1.00 11.78 A O ATOM 1376 CG2 THR A 182 10.182 33.532 29.383 1.00 11.44 A C ATOM 1377 C THR A 182 12.249 36.731 30.203 1.00 12.70 A C ATOM 1378 O THR A 182 11.491 37.287 31.039 1.00 12.48 A O ATOM 1379 N PRO A 183 13.497 37.159 29.955 1.00 13.03 A N ATOM 1380 CA PRO A 183 14.066 38.320 30.627 1.00 13.57 A C ATOM 1381 CB PRO A 183 15.451 38.487 29.993 1.00 13.44 A C ATOM 1382 CG PRO A 183 15.611 37.419 28.985 1.00 13.35 A C ATOM 1383 CD PRO A 183 14.320 36.699 28.831 1.00 13.41 A C ATOM 1384 C PRO A 183 14.199 38.181 32.135 1.00 13.75 A C ATOM 1385 O PRO A 183 14.230 39.180 32.839 1.00 13.12 A O ATOM 1386 N ASN A 184 14.285 36.955 32.616 1.00 14.63 A N ATOM 1387 CA ASN A 184 14.499 36.726 34.034 1.00 15.68 A C ATOM 1388 CB ASN A 184 15.679 35.797 34.216 1.00 16.64 A C ATOM 1389 CG ASN A 184 16.978 36.426 33.740 1.00 17.82 A C ATOM 1390 OD1 ASN A 184 17.165 37.653 33.767 1.00 18.50 A O ATOM 1391 ND2 ASN A 184 17.878 35.586 33.293 1.00 18.75 A N ATOM 1392 C ASN A 184 13.291 36.194 34.751 1.00 15.70 A C ATOM 1393 O ASN A 184 13.363 35.865 35.931 1.00 15.92 A O ATOM 1394 N THR A 185 12.182 36.102 34.027 1.00 15.51 A N ATOM 1395 CA THR A 185 10.898 35.823 34.620 1.00 14.77 A C ATOM 1396 CB THR A 185 10.251 34.603 33.976 1.00 14.28 A C ATOM 1397 OG1 THR A 185 11.137 33.476 34.101 1.00 13.52 A O ATOM 1398 CG2 THR A 185 8.912 34.341 34.633 1.00 13.98 A C ATOM 1399 C THR A 185 10.039 37.035 34.382 1.00 14.98 A C ATOM 1400 O THR A 185 9.666 37.310 33.243 1.00 16.15 A O ATOM 1401 N PRO A 186 9.769 37.814 35.435 1.00 14.99 A N ATOM 1402 CA PRO A 186 8.988 39.026 35.190 1.00 14.73 A C ATOM 1403 CB PRO A 186 9.308 39.914 36.399 1.00 14.75 A C ATOM 1404 CG PRO A 186 9.666 38.966 37.480 1.00 14.83 A C ATOM 1405 CD PRO A 186 10.245 37.732 36.828 1.00 14.83 A C ATOM 1406 C PRO A 186 7.510 38.741 35.136 1.00 14.30 A C ATOM 1407 O PRO A 186 7.056 37.670 35.509 1.00 14.74 A O ATOM 1408 N GLY A 187 6.778 39.711 34.630 1.00 14.35 A N ATOM 1409 CA GLY A 187 5.330 39.677 34.597 1.00 14.24 A C ATOM 1410 C GLY A 187 4.707 38.787 33.543 1.00 14.00 A C ATOM 1411 O GLY A 187 3.502 38.880 33.301 1.00 13.60 A O ATOM 1412 N ASP A 188 5.504 37.925 32.907 1.00 13.79 A N ATOM 1413 CA ASP A 188 4.957 37.050 31.879 1.00 13.64 A C ATOM 1414 CB ASP A 188 5.532 35.633 32.008 1.00 13.33 A C ATOM 1415 CG ASP A 188 6.943 35.496 31.502 1.00 13.39 A C ATOM 1416 OD1 ASP A 188 7.707 36.462 31.383 1.00 13.27 A O ATOM 1417 OD2 ASP A 188 7.318 34.350 31.215 1.00 14.35 A O ATOM 1418 C ASP A 188 5.070 37.612 30.452 1.00 13.88 A C ATOM 1419 O ASP A 188 5.619 38.712 30.208 1.00 14.39 A O ATOM 1420 N ALA A 189 4.540 36.842 29.515 1.00 13.78 A N ATOM 1421 CA ALA A 189 4.466 37.257 28.144 1.00 13.80 A C ATOM 1422 CB ALA A 189 3.329 38.259 27.955 1.00 13.78 A C ATOM 1423 C ALA A 189 4.288 36.053 27.242 1.00 13.69 A C ATOM 1424 O ALA A 189 4.183 34.937 27.707 1.00 13.66 A O ATOM 1425 N LEU A 190 4.260 36.310 25.941 1.00 14.07 A N ATOM 1426 CA LEU A 190 4.173 35.276 24.926 1.00 14.36 A C ATOM 1427 CB LEU A 190 4.778 35.797 23.621 1.00 14.90 A C ATOM 1428 CG LEU A 190 4.925 34.762 22.530 1.00 15.37 A C ATOM 1429 CD1 LEU A 190 5.581 33.503 23.056 1.00 15.75 A C ATOM 1430 CD2 LEU A 190 5.757 35.349 21.418 1.00 15.87 A C ATOM 1431 C LEU A 190 2.730 34.822 24.710 1.00 13.65 A C ATOM 1432 O LEU A 190 2.470 33.616 24.670 1.00 14.14 A O ATOM 1433 N ARG A 191 1.808 35.785 24.610 1.00 12.55 A N ATOM 1434 CA ARG A 191 0.373 35.501 24.585 1.00 11.67 A C ATOM 1435 CB ARG A 191 0.172 35.511 23.158 1.00 11.66 A C ATOM 1436 CG ARG A 191 0.511 34.557 22.197 1.00 11.40 A C ATOM 1437 CD ARG A 191 0.195 34.508 20.853 1.00 11.14 A C ATOM 1438 NE ARG A 191 0.205 35.582 19.945 1.00 10.68 A N ATOM 1439 CZ ARG A 191 1.333 35.589 19.264 1.00 10.70 A C ATOM 1440 NH1 ARG A 191 2.205 34.590 19.381 1.00 11.00 A N ATOM 1441 NH2 ARG A 191 1.598 36.590 18.450 1.00 10.72 A N ATOM 1442 C ARG A 191 0.398 36.543 25.332 1.00 11.21 A C ATOM 1443 O ARG A 191 0.009 37.712 25.424 1.00 10.54 A O ATOM 1444 N SER A 192 1.555 36.128 25.807 1.00 11.04 A N ATOM 1445 CA SER A 192 2.431 37.032 26.528 1.00 11.41 A C ATOM 1446 CB SER A 192 2.631 36.558 27.971 1.00 11.37 A C ATOM 1447 OG SER A 192 3.803 37.111 28.558 1.00 11.38 A O ATOM 1448 C SER A 192 3.765 37.098 25.819 1.00 11.56 A C ATOM 1449 O SER A 192 4.463 36.094 25.698 1.00 11.58 A O ATOM 1450 N MET A 193 4.127 38.289 25.384 1.00 11.67 A N ATOM 1451 CA MET A 193 5.411 38.483 24.767 1.00 12.16 A C ATOM 1452 CB MET A 193 5.413 39.767 23.944 1.00 12.44 A C ATOM 1453 CG MET A 193 4.355 39.828 22.870 1.00 12.51 A C ATOM 1454 SD MET A 193 4.455 41.399 22.016 1.00 12.70 A S ATOM 1455 CE MET A 193 6.110 41.322 21.326 1.00 13.02 A C ATOM 1456 C MET A 193 6.562 38.560 25.776 1.00 12.02 A C ATOM 1457 O MET A 193 7.719 38.425 25.398 1.00 11.80 A O ATOM 1458 N GLU A 194 6.292 38.847 27.033 1.00 12.27 A N ATOM 1459 CA GLU A 194 7.421 38.982 27.980 1.00 12.83 A C ATOM 1460 CB GLU A 194 7.081 39.968 29.077 1.00 13.09 A C ATOM 1461 CG GLU A 194 5.903 39.511 29.951 1.00 13.52 A C ATOM 1462 CD GLU A 194 5.281 40.631 30.743 1.00 13.63 A C ATOM 1463 OE1 GLU A 194 5.799 41.773 30.651 1.00 14.89 A O ATOM 1464 OE2 GLU A 194 4.296 40.372 31.447 1.00 12.72 A O ATOM 1465 C GLU A 194 7.764 37.621 28.572 1.00 13.17 A C ATOM 1466 O GLU A 194 8.872 37.403 28.987 1.00 13.22 A O ATOM 1467 N ASN A 195 6.788 36.712 28.558 1.00 13.78 A N ATOM 1468 CA ASN A 195 6.905 35.373 29.097 1.00 14.09 A C ATOM 1469 CB ASN A 195 6.568 35.428 30.580 1.00 13.89 A C ATOM 1470 CG ASN A 195 6.721 34.074 31.267 1.00 13.72 A C ATOM 1471 OD1 ASN A 195 7.627 33.311 30.972 1.00 13.41 A O ATOM 1472 ND2 ASN A 195 5.834 33.786 32.198 1.00 13.75 A N ATOM 1473 C ASN A 195 5.967 34.375 28.387 1.00 14.61 A C ATOM 1474 O ASN A 195 4.898 34.055 28.885 1.00 15.66 A O ATOM 1475 N PRO A 196 6.347 33.900 27.209 1.00 14.75 A N ATOM 1476 CA PRO A 196 5.418 33.102 26.381 1.00 14.82 A C ATOM 1477 CB PRO A 196 6.265 32.773 25.157 1.00 14.80 A C ATOM 1478 CG PRO A 196 7.180 33.963 25.022 1.00 15.30 A C ATOM 1479 CD PRO A 196 7.505 34.382 26.437 1.00 15.18 A C ATOM 1480 C PRO A 196 4.894 31.812 27.012 1.00 14.89 A C ATOM 1481 O PRO A 196 3.743 31.393 26.764 1.00 14.12 A O ATOM 1482 N LYS A 197 5.751 31.193 27.816 1.00 15.78 A N ATOM 1483 CA LYS A 197 5.454 29.918 28.464 1.00 16.20 A C ATOM 1484 CB LYS A 197 6.607 29.476 29.345 1.00 17.65 A C ATOM 1485 CG LYS A 197 7.392 28.274 28.883 1.00 19.35 A C ATOM 1486 CD LYS A 197 8.470 28.028 29.955 1.00 21.72 A C ATOM 1487 CE LYS A 197 9.427 26.872 29.652 1.00 22.98 A C ATOM 1488 NZ LYS A 197 8.975 25.622 30.336 1.00 23.87 A N ATOM 1489 C LYS A 197 4.219 30.061 29.310 1.00 14.95 A C ATOM 1490 O LYS A 197 3.513 29.114 29.515 1.00 13.94 A O ATOM 1491 N LEU A 198 3.956 31.257 29.791 1.00 14.64 A N ATOM 1492 CA LEU A 198 2.770 31.476 30.581 1.00 15.36 A C ATOM 1493 CB LEU A 198 2.576 32.969 30.863 1.00 15.67 A C ATOM 1494 CG LEU A 198 1.296 33.521 31.533 1.00 15.57 A C ATOM 1495 CD1 LEU A 198 0.973 32.894 32.886 1.00 15.47 A C ATOM 1496 CD2 LEU A 198 1.415 35.038 31.654 1.00 15.06 A C ATOM 1497 C LEU A 198 1.554 30.888 29.906 1.00 15.80 A C ATOM 1498 O LEU A 198 0.812 30.175 30.537 1.00 17.11 A O ATOM 1499 N TYR A 199 1.347 31.155 28.628 1.00 16.25 A N ATOM 1500 CA TYR A 199 0.175 30.598 27.921 1.00 16.26 A C ATOM 1501 CB TYR A 199 0.650 31.738 27.300 1.00 15.53 A C ATOM 1502 CG TYR A 199 1.040 32.822 28.279 1.00 14.71 A C ATOM 1503 CD1 TYR A 199 1.966 32.579 29.279 1.00 14.13 A C ATOM 1504 CE1 TYR A 199 2.340 33.559 30.171 1.00 13.70 A C ATOM 1505 CZ TYR A 199 1.790 34.803 30.078 1.00 14.03 A C ATOM 1506 OH TYR A 199 2.164 35.782 30.956 1.00 14.59 A O ATOM 1507 CE2 TYR A 199 0.875 35.098 29.085 1.00 14.38 A C ATOM 1508 CD2 TYR A 199 0.492 34.098 28.198 1.00 14.66 A C ATOM 1509 C TYR A 199 0.572 29.551 26.857 1.00 17.22 A C ATOM 1510 O TYR A 199 0.113 29.585 25.712 1.00 17.25 A O ATOM 1511 N ASN A 200 1.441 28.624 27.242 1.00 18.43 A N ATOM 1512 CA ASN A 200 1.827 27.479 26.386 1.00 18.86 A C ATOM 1513 CB ASN A 200 0.631 26.532 26.215 1.00 21.02 A C ATOM 1514 CG ASN A 200 0.375 25.721 27.468 1.00 23.20 A C ATOM 1515 OD1 ASN A 200 1.312 25.396 28.219 1.00 26.27 A O ATOM 1516 ND2 ASN A 200 0.876 25.382 27.704 1.00 24.08 A N ATOM 1517 C ASN A 200 2.439 27.802 25.035 1.00 17.25 A C ATOM 1518 O ASN A 200 2.142 27.171 24.036 1.00 16.12 A O ATOM 1519 N GLN A 201 3.287 28.816 25.018 1.00 16.59 A N ATOM 1520 CA GLN A 201 4.176 29.045 23.898 1.00 15.78 A C ATOM 1521 CB GLN A 201 4.079 30.469 23.387 1.00 15.50 A C ATOM 1522 CG GLN A 201 2.816 30.765 22.619 1.00 15.69 A C ATOM 1523 CD GLN A 201 2.783 32.192 22.089 1.00 16.07 A C ATOM 1524 OE1 GLN A 201 2.975 33.164 22.829 1.00 15.13 A O ATOM 1525 NE2 GLN A 201 2.540 32.322 20.790 1.00 16.64 A N ATOM 1526 C GLN A 201 5.602 28.747 24.336 1.00 15.44 A C ATOM 1527 O GLN A 201 6.000 29.038 25.453 1.00 14.82 A O ATOM 1528 N PRO A 202 6.365 28.113 23.463 1.00 16.00 A N ATOM 1529 CA PRO A 202 7.760 27.900 23.754 1.00 16.63 A C ATOM 1530 CB PRO A 202 8.227 27.048 22.586 1.00 16.94 A C ATOM 1531 CG PRO A 202 7.226 27.316 21.507 1.00 17.12 A C ATOM 1532 CD PRO A 202 5.949 27.401 22.249 1.00 16.49 A C ATOM 1533 C PRO A 202 8.482 29.203 23.734 1.00 16.91 A C ATOM 1534 O PRO A 202 8.043 30.115 23.030 1.00 17.59 A O ATOM 1535 N ASP A 203 9.563 29.286 24.497 1.00 16.60 A N ATOM 1536 CA ASP A 203 10.369 30.469 24.532 1.00 17.19 A C ATOM 1537 CB ASP A 203 10.337 31.157 25.911 1.00 17.40 A C ATOM 1538 CG ASP A 203 10.885 30.299 27.056 1.00 17.15 A C ATOM 1539 OD1 ASP A 203 11.307 29.124 26.880 1.00 16.43 A O ATOM 1540 OD2 ASP A 203 10.849 30.843 28.180 1.00 16.95 A O ATOM 1541 C ASP A 203 11.791 30.209 24.112 1.00 18.70 A C ATOM 1542 O ASP A 203 12.676 31.022 24.429 1.00 19.51 A O ATOM 1543 N ARG A 204 12.020 29.116 23.381 1.00 19.82 A N ATOM 1544 CA ARG A 204 13.245 28.985 22.593 1.00 20.95 A C ATOM 1545 CB ARG A 204 14.421 28.585 23.458 1.00 23.55 A C ATOM 1546 CG ARG A 204 14.337 27.186 24.020 1.00 27.12 A C ATOM 1547 CD ARG A 204 15.383 27.032 25.090 1.00 30.35 A C ATOM 1548 NE ARG A 204 14.974 26.129 26.152 1.00 34.09 A N ATOM 1549 CZ ARG A 204 15.738 25.158 26.639 1.00 37.57 A C ATOM 1550 NH1 ARG A 204 16.955 24.947 26.119 1.00 38.53 A N ATOM 1551 NH2 ARG A 204 15.277 24.384 27.633 1.00 37.08 A N ATOM 1552 C ARG A 204 13.103 27.993 21.473 1.00 19.87 A C ATOM 1553 O ARG A 204 12.316 27.060 21.576 1.00 18.88 A O ATOM 1554 N TYR A 205 13.886 28.202 20.417 1.00 19.61 A N ATOM 1555 CA TYR A 205 13.838 27.375 19.190 1.00 20.53 A C ATOM 1556 CB TYR A 205 15.060 27.682 18.280 1.00 20.73 A C ATOM 1557 CG TYR A 205 14.926 27.129 16.882 1.00 20.80 A C ATOM 1558 CD1 TYR A 205 13.810 27.430 16.109 1.00 21.37 A C ATOM 1559 CE1 TYR A 205 13.660 26.932 14.832 1.00 21.21 A C ATOM 1560 CZ TYR A 205 14.641 26.148 14.306 1.00 20.82 A C ATOM 1561 OH TYR A 205 14.447 25.681 13.053 1.00 20.22 A O ATOM 1562 CE2 TYR A 205 15.776 25.857 15.025 1.00 20.57 A C ATOM 1563 CD2 TYR A 205 15.908 26.336 16.317 1.00 20.84 A C ATOM 1564 C TYR A 205 13.749 25.859 19.440 1.00 20.17 A C ATOM 1565 O TYR A 205 12.904 25.167 18.875 1.00 18.72 A O ATOM 1566 N GLN A 206 14.603 25.377 20.335 1.00 21.34 A N ATOM 1567 CA GLN A 206 14.715 23.948 20.671 1.00 22.58 A C ATOM 1568 CB GLN A 206 15.767 23.764 21.757 1.00 24.80 A C ATOM 1569 CG GLN A 206 17.129 24.352 21.385 1.00 28.21 A C ATOM 1570 CD GLN A 206 17.413 25.682 22.073 1.00 31.20 A C ATOM 1571 OE1 GLN A 206 16.776 26.702 21.784 1.00 33.57 A O ATOM 1572 NE2 GLN A 206 18.366 25.673 23.013 1.00 34.48 A N ATOM 1573 C GLN A 206 13.413 23.257 21.115 1.00 21.39 A C ATOM 1574 O GLN A 206 13.335 22.012 21.080 1.00 21.09 A O ATOM 1575 N ASP A 207 12.419 24.061 21.530 1.00 19.47 A N ATOM 1576 CA ASP A 207 11.158 23.578 22.108 1.00 17.35 A C ATOM 1577 CB ASP A 207 10.898 24.207 23.492 1.00 17.00 A C ATOM 1578 CG ASP A 207 11.998 23.917 24.494 1.00 16.98 A C ATOM 1579 OD1 ASP A 207 12.681 22.892 24.342 1.00 17.05 A O ATOM 1580 OD2 ASP A 207 12.192 24.713 25.433 1.00 16.83 A O ATOM 1581 C ASP A 207 10.007 23.911 21.198 1.00 15.93 A C ATOM 1582 O ASP A 207 8.858 23.867 21.605 1.00 15.49 A O ATOM 1583 N ARG A 208 10.299 24.246 19.960 1.00 14.96 A N ATOM 1584 CA ARG A 208 9.222 24.567 19.046 1.00 14.60 A C ATOM 1585 CB ARG A 208 9.746 25.100 17.708 1.00 14.67 A C ATOM 1586 CG ARG A 208 10.371 24.035 16.833 1.00 14.67 A C ATOM 1587 CD ARG A 208 11.284 24.671 15.819 1.00 14.86 A C ATOM 1588 NE ARG A 208 12.055 23.638 15.162 1.00 15.29 A N ATOM 1589 CZ ARG A 208 13.206 23.171 15.614 1.00 16.10 A C ATOM 1590 NH1 ARG A 208 13.731 23.649 16.721 1.00 17.73 A N ATOM 1591 NH2 ARG A 208 13.845 22.226 14.964 1.00 16.00 A N ATOM 1592 C ARG A 208 8.373 23.358 18.777 1.00 13.74 A C ATOM 1593 O ARG A 208 8.860 22.278 18.641 1.00 12.69 A O ATOM 1594 N TYR A 209 7.081 23.595 18.688 1.00 14.32 A N ATOM 1595 CA TYR A 209 6.136 22.639 18.140 1.00 14.70 A C ATOM 1596 CB TYR A 209 4.711 23.201 18.179 1.00 14.05 A C ATOM 1597 CG TYR A 209 3.623 22.377 17.503 1.00 13.32 A C ATOM 1598 CD1 TYR A 209 3.136 21.228 18.076 1.00 13.15 A C ATOM 1599 CE1 TYR A 209 2.097 20.516 17.498 1.00 12.94 A C ATOM 1600 CZ TYR A 209 1.528 20.944 16.330 1.00 13.00 A C ATOM 1601 OH TYR A 209 0.493 20.212 15.726 1.00 12.90 A O ATOM 1602 CE2 TYR A 209 2.012 22.088 15.741 1.00 12.96 A C ATOM 1603 CD2 TYR A 209 3.043 22.796 16.334 1.00 12.99 A C ATOM 1604 C TYR A 209 6.513 22.419 16.714 1.00 15.33 A C ATOM 1605 O TYR A 209 6.889 23.363 16.023 1.00 15.11 A O ATOM 1606 N THR A 210 6.359 21.175 16.286 1.00 16.15 A N ATOM 1607 CA THR A 210 6.796 20.737 14.986 1.00 17.20 A C ATOM 1608 CB THR A 210 8.162 19.996 15.135 1.00 18.44 A C ATOM 1609 OG1 THR A 210 8.620 19.652 13.838 1.00 22.63 A O ATOM 1610 CG2 THR A 210 8.092 18.692 15.962 1.00 18.69 A C ATOM 1611 C THR A 210 5.720 19.937 14.186 1.00 16.04 A C ATOM 1612 O THR A 210 5.983 19.437 13.110 1.00 15.79 A O ATOM 1613 N GLY A 211 4.497 19.885 14.697 1.00 16.00 A N ATOM 1614 CA GLY A 211 3.389 19.131 14.079 1.00 16.15 A C ATOM 1615 C GLY A 211 2.576 19.933 13.066 1.00 16.36 A C ATOM 1616 O GLY A 211 2.959 21.048 12.712 1.00 17.38 A O ATOM 1617 N PRO A 212 1.458 19.375 12.575 1.00 15.90 A N ATOM 1618 CA PRO A 212 0.825 19.956 11.405 1.00 15.80 A C ATOM 1619 CB PRO A 212 0.200 18.756 10.716 1.00 15.94 A C ATOM 1620 CG PRO A 212 0.123 17.809 11.817 1.00 16.11 A C ATOM 1621 CD PRO A 212 0.825 18.103 12.955 1.00 16.30 A C ATOM 1622 C PRO A 212 0.258 20.921 11.730 1.00 16.41 A C ATOM 1623 O PRO A 212 0.656 21.692 10.857 1.00 16.72 A O ATOM 1624 N SER A 213 0.724 20.898 12.973 1.00 16.53 A N ATOM 1625 CA SER A 213 1.837 21.716 13.358 1.00 16.75 A C ATOM 1626 CB SER A 213 2.284 21.316 14.748 1.00 17.51 A C ATOM 1627 OG SER A 213 3.661 21.579 14.853 1.00 18.94 A O ATOM 1628 C SER A 213 1.481 23.209 13.345 1.00 17.13 A C ATOM 1629 O SER A 213 0.285 23.588 13.469 1.00 17.29 A O ATOM 1630 N ASP A 214 2.513 24.059 13.209 1.00 16.27 A N ATOM 1631 CA ASP A 214 2.329 25.508 13.237 1.00 15.08 A C ATOM 1632 CB ASP A 214 1.851 25.926 14.630 1.00 15.42 A C ATOM 1633 CG ASP A 214 1.721 27.430 14.796 1.00 15.51 A C ATOM 1634 OD1 ASP A 214 2.543 28.180 14.216 1.00 16.01 A O ATOM 1635 OD2 ASP A 214 0.798 27.862 15.528 1.00 14.86 A O ATOM 1636 C ASP A 214 1.305 25.901 12.213 1.00 14.27 A C ATOM 1637 O ASP A 214 0.375 26.606 12.522 1.00 13.66 A O ATOM 1638 N ASN A 215 1.466 25.409 10.995 1.00 14.22 A N ATOM 1639 CA ASN A 215 0.507 25.653 9.924 1.00 14.30 A C ATOM 1640 CB ASN A 215 0.702 27.060 9.334 1.00 13.77 A C ATOM 1641 CG ASN A 215 1.959 27.172 8.472 1.00 13.33 A C ATOM 1642 OD1 ASN A 215 2.241 26.309 7.648 1.00 13.58 A O ATOM 1643 ND2 ASN A 215 2.705 28.225 8.658 1.00 12.58 A N ATOM 1644 C ASN A 215 0.944 25.479 10.367 1.00 15.43 A C ATOM 1645 O ASN A 215 1.768 26.360 10.129 1.00 17.15 A O ATOM 1646 N GLY A 216 1.267 24.372 11.033 1.00 15.63 A N ATOM 1647 CA GLY A 216 2.641 24.132 11.479 1.00 15.35 A C ATOM 1648 C GLY A 216 3.070 24.980 12.666 1.00 15.58 A C ATOM 1649 O GLY A 216 4.219 25.467 12.737 1.00 16.25 A O ATOM 1650 N GLY A 217 2.158 25.181 13.611 1.00 15.34 A N ATOM 1651 CA GLY A 217 2.524 25.840 14.884 1.00 14.91 A C ATOM 1652 C GLY A 217 2.633 27.352 14.829 1.00 14.14 A C ATOM 1653 O GLY A 217 3.387 27.969 15.596 1.00 14.67 A O ATOM 1654 N VAL A 218 1.829 27.949 13.972 1.00 12.95 A N ATOM 1655 CA VAL A 218 2.024 29.338 13.605 1.00 12.93 A C ATOM 1656 CB VAL A 218 1.198 29.641 12.327 1.00 12.94 A C ATOM 1657 CG1 VAL A 218 0.249 30.815 12.469 1.00 12.92 A C ATOM 1658 CG2 VAL A 218 2.142 29.767 11.133 1.00 12.90 A C ATOM 1659 C VAL A 218 1.825 30.284 14.785 1.00 12.86 A C ATOM 1660 O VAL A 218 2.681 31.110 15.074 1.00 13.09 A O ATOM 1661 N HIS A 219 0.733 30.092 15.512 1.00 12.63 A N ATOM 1662 CA HIS A 219 0.478 30.819 16.744 1.00 12.21 A C ATOM 1663 CB HIS A 219 1.019 30.845 17.028 1.00 12.29 A C ATOM 1664 CG HIS A 219 1.812 31.473 15.932 1.00 12.04 A C ATOM 1665 ND1 HIS A 219 2.339 30.747 14.895 1.00 11.93 A N ATOM 1666 CE1 HIS A 219 2.961 31.562 14.064 1.00 12.18 A C ATOM 1667 NE2 HIS A 219 2.828 32.794 14.514 1.00 12.05 A N ATOM 1668 CD2 HIS A 219 2.113 32.765 15.682 1.00 11.89 A C ATOM 1669 C HIS A 219 1.167 30.213 17.943 1.00 11.95 A C ATOM 1670 O HIS A 219 1.170 30.826 19.008 1.00 11.86 A O ATOM 1671 N ILE A 220 1.725 29.015 17.805 1.00 11.44 A N ATOM 1672 CA ILE A 220 2.414 28.443 18.914 1.00 11.45 A C ATOM 1673 CB ILE A 220 2.384 26.927 18.838 1.00 11.68 A C ATOM 1674 CG1 ILE A 220 0.951 26.446 19.053 1.00 12.04 A C ATOM 1675 CD1 ILE A 220 0.737 24.988 18.653 1.00 12.23 A C ATOM 1676 CG2 ILE A 220 3.293 26.302 19.894 1.00 11.57 A C ATOM 1677 C ILE A 220 3.841 28.999 18.991 1.00 11.72 A C ATOM 1678 O ILE A 220 4.228 29.616 20.020 1.00 11.22 A O ATOM 1679 N ASN A 221 4.601 28.809 17.897 1.00 11.49 A N ATOM 1680 CA ASN A 221 6.051 29.113 17.882 1.00 11.39 A C ATOM 1681 CB ASN A 221 6.761 28.288 16.820 1.00 11.36 A C ATOM 1682 CG ASN A 221 6.457 26.809 16.934 1.00 11.22 A C ATOM 1683 OD1 ASN A 221 6.580 26.185 17.993 1.00 11.34 A O ATOM 1684 ND2 ASN A 221 6.032 26.250 15.851 1.00 11.20 A N ATOM 1685 C ASN A 221 6.413 30.581 17.667 1.00 11.36 A C ATOM 1686 O ASN A 221 7.587 30.933 17.639 1.00 11.44 A O ATOM 1687 N SER A 222 5.403 31.442 17.547 1.00 11.25 A N ATOM 1688 CA SER A 222 5.638 32.877 17.417 1.00 10.81 A C ATOM 1689 CB SER A 222 4.345 33.617 17.026 1.00 10.68 A C ATOM 1690 OG SER A 222 3.340 33.460 17.996 1.00 10.76 A O ATOM 1691 C SER A 222 6.217 33.444 18.689 1.00 10.49 A C ATOM 1692 O SER A 222 6.888 34.485 18.652 1.00 10.48 A O ATOM 1693 N GLY A 223 5.946 32.771 19.810 1.00 10.19 A N ATOM 1694 CA GLY A 223 6.413 33.226 21.107 1.00 10.08 A C ATOM 1695 C GLY A 223 7.927 33.301 21.164 1.00 10.06 A C ATOM 1696 O GLY A 223 8.491 34.143 21.859 1.00 9.81 A O ATOM 1697 N ILE A 224 8.578 32.431 20.398 1.00 10.10 A N ATOM 1698 CA ILE A 224 10.020 32.426 20.317 1.00 10.23 A C ATOM 1699 CB ILE A 224 10.519 31.272 19.422 1.00 10.49 A C ATOM 1700 CG1 ILE A 224 10.159 29.913 20.031 1.00 10.32 A C ATOM 1701 CD1 ILE A 224 9.939 28.841 18.985 1.00 10.40 A C ATOM 1702 CG2 ILE A 224 12.037 31.376 19.189 1.00 10.68 A C ATOM 1703 C ILE A 224 10.505 33.749 19.756 1.00 10.23 A C ATOM 1704 O ILE A 224 11.364 34.386 20.336 1.00 9.86 A O ATOM 1705 N ASN A 225 9.949 34.164 18.625 1.00 10.63 A N ATOM 1706 CA ASN A 225 10.323 35.454 18.082 1.00 11.23 A C ATOM 1707 CB ASN A 225 9.905 35.631 16.640 1.00 11.81 A C ATOM 1708 CG ASN A 225 10.579 36.830 15.998 1.00 12.52 A C ATOM 1709 OD1 ASN A 225 9.945 37.827 15.680 1.00 13.05 A O ATOM 1710 ND2 ASN A 225 11.883 36.753 15.847 1.00 12.97 A N ATOM 1711 C ASN A 225 9.780 36.617 18.879 1.00 11.45 A C ATOM 1712 O ASN A 225 10.456 37.629 18.972 1.00 11.51 A O ATOM 1713 N ASN A 226 8.575 36.500 19.457 1.00 11.45 A N ATOM 1714 CA ASN A 226 8.081 37.559 20.356 1.00 11.23 A C ATOM 1715 CB ASN A 226 6.650 37.267 20.854 1.00 11.25 A C ATOM 1716 CG ASN A 226 5.584 37.417 19.761 1.00 11.15 A C ATOM 1717 OD1 ASN A 226 5.901 37.722 18.614 1.00 10.97 A O ATOM 1718 ND2 ASN A 226 4.313 37.165 20.112 1.00 11.00 A N ATOM 1719 C ASN A 226 9.039 37.761 21.539 1.00 11.16 A C ATOM 1720 O ASN A 226 9.376 38.871 21.901 1.00 10.70 A O ATOM 1721 N LYS A 227 9.501 36.669 22.125 1.00 11.75 A N ATOM 1722 CA LYS A 227 10.371 36.759 23.271 1.00 12.42 A C ATOM 1723 CB LYS A 227 10.731 35.370 23.764 1.00 12.84 A C ATOM 1724 CG LYS A 227 11.611 35.359 24.990 1.00 13.61 A C ATOM 1725 CD LYS A 227 10.945 35.898 26.266 1.00 14.22 A C ATOM 1726 CE LYS A 227 12.014 36.340 27.269 1.00 15.09 A C ATOM 1727 NZ LYS A 227 11.580 36.298 28.698 1.00 15.81 A N ATOM 1728 C LYS A 227 11.612 37.562 22.904 1.00 12.89 A C ATOM 1729 O LYS A 227 12.015 38.460 23.641 1.00 13.47 A O ATOM 1730 N ALA A 228 12.193 37.269 21.740 1.00 12.98 A N ATOM 1731 CA ALA A 228 13.335 38.036 21.243 1.00 12.64 A C ATOM 1732 CB ALA A 228 13.813 37.442 19.926 1.00 12.73 A C ATOM 1733 C ALA A 228 13.068 39.558 21.096 1.00 12.18 A C ATOM 1734 O ALA A 228 13.905 40.380 21.471 1.00 12.38 A O ATOM 1735 N PHE A 229 11.914 39.929 20.545 1.00 11.74 A N ATOM 1736 CA PHE A 229 11.555 41.334 20.434 1.00 11.22 A C ATOM 1737 CB PHE A 229 10.240 41.554 19.676 1.00 10.83 A C ATOM 1738 CG PHE A 229 9.932 42.999 19.513 1.00 10.75 A C ATOM 1739 CD1 PHE A 229 10.570 43.735 18.552 1.00 10.84 A C ATOM 1740 CE1 PHE A 229 10.358 45.093 18.457 1.00 11.22 A C ATOM 1741 CZ PHE A 229 9.505 45.741 19.351 1.00 10.84 A C ATOM 1742 CE2 PHE A 229 8.890 45.023 20.333 1.00 10.64 A C ATOM 1743 CD2 PHE A 229 9.104 43.659 20.409 1.00 10.89 A C ATOM 1744 C PHE A 229 11.470 41.957 21.827 1.00 11.34 A C ATOM 1745 O PHE A 229 11.985 43.054 22.072 1.00 11.16 A O ATOM 1746 N TYR A 230 10.831 41.248 22.750 1.00 11.53 A N ATOM 1747 CA TYR A 230 10.803 41.695 24.136 1.00 11.74 A C ATOM 1748 CB TYR A 230 10.119 40.669 25.062 1.00 11.82 A C ATOM 1749 CG TYR A 230 10.185 41.060 26.522 1.00 11.70 A C ATOM 1750 CD1 TYR A 230 9.407 42.076 27.041 1.00 11.41 A C ATOM 1751 CE1 TYR A 230 9.497 42.427 28.377 1.00 11.72 A C ATOM 1752 CZ TYR A 230 10.387 41.744 29.222 1.00 12.00 A C ATOM 1753 OH TYR A 230 10.553 41.983 30.564 1.00 11.37 A O ATOM 1754 CE2 TYR A 230 11.161 40.741 28.709 1.00 12.22 A C ATOM 1755 CD2 TYR A 230 11.058 40.409 27.367 1.00 12.28 A C ATOM 1756 C TYR A 230 12.200 42.005 24.645 1.00 11.45 A C ATOM 1757 O TYR A 230 12.438 43.097 25.119 1.00 11.78 A O ATOM 1758 N LEU A 231 13.114 41.058 24.519 1.00 11.40 A N ATOM 1759 CA LEU A 231 14.473 41.254 24.997 1.00 11.79 A C ATOM 1760 CB LEU A 231 15.288 39.996 24.808 1.00 11.69 A C ATOM 1761 CG LEU A 231 14.814 38.855 25.698 1.00 11.76 A C ATOM 1762 CD1 LEU A 231 15.341 37.549 25.148 1.00 11.92 A C ATOM 1763 CD2 LEU A 231 15.246 39.049 27.144 1.00 11.76 A C ATOM 1764 C LEU A 231 15.190 42.435 24.338 1.00 12.58 A C ATOM 1765 O LEU A 231 15.881 43.196 25.035 1.00 12.49 A O ATOM 1766 N ILE A 232 15.003 42.611 23.021 1.00 13.10 A N ATOM 1767 CA ILE A 232 15.600 43.750 22.306 1.00 13.31 A C ATOM 1768 CB ILE A 232 15.493 43.616 20.781 1.00 13.13 A C ATOM 1769 CG1 ILE A 232 16.478 42.569 20.316 1.00 13.85 A C ATOM 1770 CD1 ILE A 232 16.013 41.724 19.150 1.00 14.38 A C ATOM 1771 CG2 ILE A 232 15.890 44.889 20.075 1.00 12.88 A C ATOM 1772 C ILE A 232 15.048 45.077 22.764 1.00 14.10 A C ATOM 1773 O ILE A 232 15.825 46.032 22.986 1.00 14.59 A O ATOM 1774 N ALA A 233 13.727 45.158 22.924 1.00 15.20 A N ATOM 1775 CA ALA A 233 13.080 46.436 23.335 1.00 15.74 A C ATOM 1776 CB ALA A 233 11.598 46.388 23.053 1.00 15.72 A C ATOM 1777 C ALA A 233 13.306 46.738 24.814 1.00 16.24 A C ATOM 1778 O ALA A 233 13.765 47.824 25.156 1.00 16.87 A O ATOM 1779 N GLN A 234 13.030 45.743 25.661 1.00 15.67 A N ATOM 1780 CA GLN A 234 12.883 45.933 27.091 1.00 15.40 A C ATOM 1781 CB GLN A 234 11.714 45.074 27.555 1.00 14.97 A C ATOM 1782 CG GLN A 234 11.303 45.270 28.993 1.00 14.65 A C ATOM 1783 CD GLN A 234 10.815 46.672 29.269 1.00 14.44 A C ATOM 1784 OE1 GLN A 234 9.965 47.219 28.560 1.00 14.43 A O ATOM 1785 NE2 GLN A 234 11.323 47.247 30.327 1.00 14.09 A N ATOM 1786 C GLN A 234 14.139 45.538 27.894 1.00 15.79 A C ATOM 1787 O GLN A 234 14.349 46.002 29.017 1.00 14.62 A O ATOM 1788 N GLY A 235 14.970 44.664 27.344 1.00 16.03 A N ATOM 1789 CA GLY A 235 16.065 44.118 28.151 1.00 16.48 A C ATOM 1790 C GLY A 235 15.602 43.077 29.169 1.00 16.81 A C ATOM 1791 O GLY A 235 14.511 43.182 29.751 1.00 17.76 A O ATOM 1792 N GLY A 236 16.422 42.048 29.351 1.00 16.10 A N ATOM 1793 CA GLY A 236 16.220 41.069 30.403 1.00 15.98 A C ATOM 1794 C GLY A 236 17.318 40.016 30.319 1.00 16.20 A C ATOM 1795 O GLY A 236 18.156 40.076 29.432 1.00 17.05 A O ATOM 1796 N THR A 237 17.335 39.061 31.239 1.00 15.70 A N ATOM 1797 CA THR A 237 18.164 37.893 31.078 1.00 15.66 A C ATOM 1798 CB THR A 237 19.028 37.680 32.316 1.00 15.65 A C ATOM 1799 OG1 THR A 237 20.044 38.688 32.371 1.00 15.12 A O ATOM 1800 CG2 THR A 237 19.671 36.339 32.258 1.00 15.82 A C ATOM 1801 C THR A 237 17.280 36.671 30.870 1.00 16.10 A C ATOM 1802 O THR A 237 16.260 36.549 31.531 1.00 17.31 A O ATOM 1803 N HIS A 238 17.707 35.747 30.000 1.00 16.14 A N ATOM 1804 CA HIS A 238 16.896 34.631 29.507 1.00 15.59 A C ATOM 1805 CB HIS A 238 16.100 35.136 28.320 1.00 15.65 A C ATOM 1806 CG HIS A 238 15.015 34.220 27.870 1.00 15.62 A C ATOM 1807 ND1 HIS A 238 15.038 33.597 26.642 1.00 15.28 A N ATOM 1808 CE1 HIS A 238 13.957 32.857 26.511 1.00 15.61 A C ATOM 1809 NE2 HIS A 238 13.239 32.969 27.616 1.00 15.96 A N ATOM 1810 CD2 HIS A 238 13.874 33.828 28.478 1.00 15.56 A C ATOM 1811 C HIS A 238 17.811 33.486 29.054 1.00 16.36 A C ATOM 1812 O HIS A 238 18.767 33.708 28.308 1.00 16.31 A O ATOM 1813 N TYR A 239 17.509 32.261 29.481 1.00 17.28 A N ATOM 1814 CA TYR A 239 18.437 31.129 29.358 1.00 18.38 A C ATOM 1815 CB TYR A 239 18.194 30.334 28.055 1.00 18.88 A C ATOM 1816 CG TYR A 239 16.844 29.703 28.089 1.00 19.54 A C ATOM 1817 CD1 TYR A 239 16.565 28.661 28.966 1.00 19.99 A C ATOM 1818 CE1 TYR A 239 15.286 28.100 29.034 1.00 21.13 A C ATOM 1819 CZ TYR A 239 14.263 28.596 28.214 1.00 21.56 A C ATOM 1820 OH TYR A 239 12.986 28.064 28.260 1.00 23.19 A O ATOM 1821 CE2 TYR A 239 14.530 29.623 27.329 1.00 20.93 A C ATOM 1822 CD2 TYR A 239 15.809 30.183 27.281 1.00 20.58 A C ATOM 1823 C TYR A 239 19.906 31.552 29.542 1.00 18.22 A C ATOM 1824 O TYR A 239 20.776 31.289 28.713 1.00 18.56 A O ATOM 1825 N GLY A 240 20.155 32.254 30.633 1.00 18.16 A N ATOM 1826 CA GLY A 240 21.496 32.645 30.989 1.00 17.75 A C ATOM 1827 C GLY A 240 22.090 33.814 30.251 1.00 17.52 A C ATOM 1828 O GLY A 240 23.170 34.223 30.605 1.00 19.02 A O ATOM 1829 N VAL A 241 21.407 34.384 29.263 1.00 17.08 A N ATOM 1830 CA VAL A 241 22.001 35.435 28.424 1.00 16.66 A C ATOM 1831 CB VAL A 241 21.800 35.134 26.929 1.00 16.31 A C ATOM 1832 CG1 VAL A 241 22.300 36.290 26.063 1.00 15.93 A C ATOM 1833 CG2 VAL A 241 22.477 33.828 26.550 1.00 16.07 A C ATOM 1834 C VAL A 241 21.381 36.786 28.715 1.00 17.12 A C ATOM 1835 O VAL A 241 20.177 36.895 28.798 1.00 17.62 A O ATOM 1836 N THR A 242 22.204 37.820 28.817 1.00 17.43 A N ATOM 1837 CA THR A 242 21.744 39.121 29.280 1.00 18.51 A C ATOM 1838 CB THR A 242 22.672 39.649 30.391 1.00 18.77 A C ATOM 1839 OG1 THR A 242 22.716 38.675 31.456 1.00 20.65 A O ATOM 1840 CG2 THR A 242 22.198 40.996 30.941 1.00 17.75 A C ATOM 1841 C THR A 242 21.696 40.102 28.124 1.00 19.15 A C ATOM 1842 O THR A 242 22.645 40.197 27.349 1.00 20.63 A O ATOM 1843 N VAL A 243 20.597 40.841 28.008 1.00 18.62 A N ATOM 1844 CA VAL A 243 20.381 41.700 26.852 1.00 17.91 A C ATOM 1845 CB VAL A 243 19.219 41.203 25.937 1.00 17.53 A C ATOM 1846 CG1 VAL A 243 18.882 42.211 24.866 1.00 17.59 A C ATOM 1847 CG2 VAL A 243 19.540 39.887 25.267 1.00 17.36 A C ATOM 1848 C VAL A 243 20.045 43.047 27.402 1.00 17.83 A C ATOM 1849 O VAL A 243 19.182 43.165 28.255 1.00 17.31 A O ATOM 1850 N ASN A 244 20.728 44.064 26.896 1.00 18.98 A N ATOM 1851 CA ASN A 244 20.444 45.429 27.283 1.00 19.14 A C ATOM 1852 CB ASN A 244 21.743 46.233 27.435 1.00 20.07 A C ATOM 1853 CG ASN A 244 22.687 45.637 28.492 1.00 22.13 A C ATOM 1854 OD1 ASN A 244 23.898 45.673 28.328 1.00 25.76 A O ATOM 1855 ND2 ASN A 244 22.139 45.076 29.571 1.00 22.37 A N ATOM 1856 C ASN A 244 19.487 46.073 26.293 1.00 17.74 A C ATOM 1857 O ASN A 244 19.867 46.368 25.167 1.00 17.39 A O ATOM 1858 N GLY A 245 18.250 46.288 26.756 1.00 16.76 A N ATOM 1859 CA GLY A 245 17.168 46.961 26.003 1.00 15.81 A C ATOM 1860 C GLY A 245 17.533 48.262 25.293 1.00 14.82 A C ATOM 1861 O GLY A 245 18.329 49.031 25.768 1.00 13.85 A O ATOM 1862 N ILE A 246 16.931 48.493 24.137 1.00 14.54 A N ATOM 1863 CA ILE A 246 17.202 49.690 23.331 1.00 14.23 A C ATOM 1864 CB ILE A 246 17.692 49.293 21.907 1.00 14.22 A C ATOM 1865 CG1 ILE A 246 16.529 48.766 21.060 1.00 13.97 A C ATOM 1866 CD1 ILE A 246 16.857 48.508 19.623 1.00 14.08 A C ATOM 1867 CG2 ILE A 246 18.784 48.218 22.012 1.00 14.32 A C ATOM 1868 C ILE A 246 15.965 50.552 23.209 1.00 13.73 A C ATOM 1869 O ILE A 246 15.987 51.557 22.540 1.00 12.83 A O ATOM 1870 N GLY A 247 14.880 50.097 23.820 1.00 14.78 A N ATOM 1871 CA GLY A 247 13.606 50.812 23.849 1.00 15.96 A C ATOM 1872 C GLY A 247 12.624 50.351 22.790 1.00 17.03 A C ATOM 1873 O GLY A 247 12.999 49.794 21.732 1.00 17.49 A O ATOM 1874 N ARG A 248 11.349 50.581 23.066 1.00 17.34 A N ATOM 1875 CA ARG A 248 10.309 50.188 22.118 1.00 17.10 A C ATOM 1876 CB ARG A 248 8.940 50.518 22.669 1.00 16.58 A C ATOM 1877 CG ARG A 248 8.433 49.504 23.662 1.00 16.47 A C ATOM 1878 CD ARG A 248 7.050 49.883 24.118 1.00 16.25 A C ATOM 1879 NE ARG A 248 6.539 48.977 25.139 1.00 17.32 A N ATOM 1880 CZ ARG A 248 5.613 48.024 24.967 1.00 18.41 A C ATOM 1881 NH1 ARG A 248 5.058 47.761 23.787 1.00 18.84 A N ATOM 1882 NH2 ARG A 248 5.232 47.308 26.009 1.00 18.99 A N ATOM 1883 C ARG A 248 10.493 50.875 20.763 1.00 17.84 A C ATOM 1884 O ARG A 248 10.415 50.214 19.716 1.00 18.39 A O ATOM 1885 N ASP A 249 10.747 52.182 20.760 1.00 17.69 A N ATOM 1886 CA ASP A 249 10.706 52.918 19.487 1.00 17.91 A C ATOM 1887 CB ASP A 249 10.937 54.421 19.668 1.00 19.68 A C ATOM 1888 CG ASP A 249 9.848 55.096 20.488 1.00 21.62 A C ATOM 1889 OD1 ASP A 249 8.623 54.884 20.223 1.00 23.50 A O ATOM 1890 OD2 ASP A 249 10.246 55.848 21.401 1.00 22.32 A O ATOM 1891 C ASP A 249 11.718 52.389 18.500 1.00 15.89 A C ATOM 1892 O ASP A 249 11.395 52.143 17.365 1.00 15.97 A O ATOM 1893 N ALA A 250 12.943 52.202 18.940 1.00 14.48 A N ATOM 1894 CA ALA A 250 13.986 51.761 18.044 1.00 13.79 A C ATOM 1895 CB ALA A 250 15.331 51.950 18.717 1.00 13.75 A C ATOM 1896 C ALA A 250 13.806 50.299 17.587 1.00 13.38 A C ATOM 1897 O ALA A 250 14.111 49.946 16.455 1.00 12.91 A O ATOM 1898 N ALA A 251 13.325 49.444 18.474 1.00 13.31 A N ATOM 1899 CA ALA A 251 13.146 48.054 18.117 1.00 13.55 A C ATOM 1900 CB ALA A 251 12.906 47.192 19.342 1.00 13.75 A C ATOM 1901 C ALA A 251 12.032 47.853 17.090 1.00 13.33 A C ATOM 1902 O ALA A 251 12.242 47.100 16.146 1.00 13.54 A O ATOM 1903 N VAL A 252 10.872 48.499 17.238 1.00 13.18 A N ATOM 1904 CA VAL A 252 9.833 48.337 16.191 1.00 13.49 A C ATOM 1905 CB VAL A 252 8.454 49.008 16.461 1.00 13.62 A C ATOM 1906 CG2 VAL A 252 8.450 50.435 15.961 1.00 14.26 A C ATOM 1907 CG1 VAL A 252 8.094 49.017 17.928 1.00 13.79 A C ATOM 1908 C VAL A 252 10.377 48.832 14.850 1.00 13.05 A C ATOM 1909 O VAL A 252 10.070 48.244 13.836 1.00 12.86 A O ATOM 1910 N GLN A 253 11.193 49.886 14.855 1.00 13.17 A N ATOM 1911 CA GLN A 253 11.744 50.453 13.619 1.00 13.59 A C ATOM 1912 CB GLN A 253 12.576 51.689 13.924 1.00 14.23 A C ATOM 1913 CG GLN A 253 12.479 52.726 12.823 1.00 15.43 A C ATOM 1914 CD GLN A 253 11.152 53.484 12.862 1.00 16.19 A C ATOM 1915 OE1 GLN A 253 10.488 53.660 11.849 1.00 16.30 A O ATOM 1916 NE2 GLN A 253 10.760 53.921 14.052 1.00 16.56 A N ATOM 1917 C GLN A 253 12.614 49.427 12.890 1.00 13.62 A C ATOM 1918 O GLN A 253 12.418 49.127 11.705 1.00 13.49 A O ATOM 1919 N ILE A 254 13.559 48.862 13.633 1.00 13.32 A N ATOM 1920 CA ILE A 254 14.372 47.776 13.145 1.00 13.03 A C ATOM 1921 CB ILE A 254 15.269 47.254 14.264 1.00 13.19 A C ATOM 1922 CG1 ILE A 254 16.277 48.338 14.647 1.00 13.74 A C ATOM 1923 CD1 ILE A 254 17.007 48.092 15.967 1.00 13.85 A C ATOM 1924 CG2 ILE A 254 15.985 45.984 13.832 1.00 13.13 A C ATOM 1925 C ILE A 254 13.521 46.622 12.589 1.00 12.90 A C ATOM 1926 O ILE A 254 13.843 46.043 11.541 1.00 12.83 A O ATOM 1927 N PHE A 255 12.453 46.249 13.273 1.00 12.49 A N ATOM 1928 CA PHE A 255 11.664 45.128 12.753 1.00 12.76 A C ATOM 1929 CB PHE A 255 10.822 44.475 13.840 1.00 12.83 A C ATOM 1930 CG PHE A 255 11.582 43.498 14.655 1.00 12.70 A C ATOM 1931 CD1 PHE A 255 12.530 43.932 15.557 1.00 12.83 A C ATOM 1932 CE1 PHE A 255 13.259 43.028 16.307 1.00 12.62 A C ATOM 1933 CZ PHE A 255 13.044 41.683 16.153 1.00 12.29 A C ATOM 1934 CE2 PHE A 255 12.105 41.249 15.251 1.00 12.48 A C ATOM 1935 CD2 PHE A 255 11.384 42.153 14.498 1.00 12.59 A C ATOM 1936 C PHE A 255 10.813 45.495 11.534 1.00 12.72 A C ATOM 1937 O PHE A 255 10.656 44.670 10.623 1.00 12.55 A O ATOM 1938 N TYR A 256 10.308 46.730 11.494 1.00 12.65 A N ATOM 1939 CA TYR A 256 9.621 47.217 10.288 1.00 12.85 A C ATOM 1940 CB TYR A 256 8.944 48.575 10.520 1.00 12.32 A C ATOM 1941 CG TYR A 256 8.231 49.150 9.321 1.00 12.10 A C ATOM 1942 CD1 TYR A 256 6.940 48.766 8.987 1.00 11.97 A C ATOM 1943 CE1 TYR A 256 6.291 49.324 7.886 1.00 12.35 A C ATOM 1944 CZ TYR A 256 6.958 50.305 7.087 1.00 12.71 A C ATOM 1945 OH TYR A 256 6.407 50.893 5.963 1.00 11.74 A O ATOM 1946 CE2 TYR A 256 8.240 50.693 7.431 1.00 12.63 A C ATOM 1947 CD2 TYR A 256 8.857 50.119 8.537 1.00 12.42 A C ATOM 1948 C TYR A 256 10.606 47.259 9.105 1.00 13.23 A C ATOM 1949 O TYR A 256 10.259 46.767 8.003 1.00 13.67 A O ATOM 1950 N ASP A 257 11.821 47.782 9.328 1.00 12.80 A N ATOM 1951 CA ASP A 257 12.798 47.841 8.248 1.00 12.91 A C ATOM 1952 CB ASP A 257 14.042 48.604 8.654 1.00 13.70 A C ATOM 1953 CG ASP A 257 13.783 50.108 8.772 1.00 14.87 A C ATOM 1954 OD1 ASP A 257 12.705 50.623 8.313 1.00 14.92 A O ATOM 1955 OD2 ASP A 257 14.671 50.780 9.354 1.00 16.53 A O ATOM 1956 C ASP A 257 13.162 46.462 7.742 1.00 12.44 A C ATOM 1957 O ASP A 257 13.202 46.234 6.512 1.00 11.99 A O ATOM 1958 N ALA A 258 13.393 45.540 8.675 1.00 11.72 A N ATOM 1959 CA ALA A 258 13.632 44.133 8.324 1.00 11.33 A C ATOM 1960 CB ALA A 258 13.821 43.289 9.581 1.00 11.03 A C ATOM 1961 C ALA A 258 12.476 43.580 7.512 1.00 11.08 A C ATOM 1962 O ALA A 258 12.650 42.782 6.597 1.00 10.58 A O ATOM 1963 N LEU A 259 11.274 43.985 7.885 1.00 11.33 A N ATOM 1964 CA LEU A 259 10.070 43.427 7.265 1.00 11.50 A C ATOM 1965 CB LEU A 259 8.813 43.839 8.048 1.00 11.12 A C ATOM 1966 CG LEU A 259 7.498 43.498 7.383 1.00 11.01 A C ATOM 1967 CD1 LEU A 259 7.281 41.998 7.298 1.00 11.10 A C ATOM 1968 CD2 LEU A 259 6.381 44.152 8.163 1.00 11.25 A C ATOM 1969 C LEU A 259 9.974 43.858 5.809 1.00 11.65 A C ATOM 1970 O LEU A 259 9.729 43.042 4.933 1.00 11.15 A O ATOM 1971 N ILE A 260 10.190 45.143 5.559 1.00 12.27 A N ATOM 1972 CA ILE A 260 9.993 45.655 4.222 1.00 13.14 A C ATOM 1973 CB ILE A 260 9.454 47.117 4.241 1.00 13.43 A C ATOM 1974 CG1 ILE A 260 10.522 48.112 4.719 1.00 13.50 A C ATOM 1975 CD1 ILE A 260 10.234 49.531 4.306 1.00 13.29 A C ATOM 1976 CG2 ILE A 260 8.188 47.221 5.092 1.00 13.46 A C ATOM 1977 C ILE A 260 11.215 45.571 3.302 1.00 13.39 A C ATOM 1978 O ILE A 260 11.093 45.924 2.160 1.00 14.38 A O ATOM 1979 N ASN A 261 12.376 45.141 3.776 1.00 13.69 A N ATOM 1980 CA ASN A 261 13.594 45.072 2.958 1.00 13.71 A C ATOM 1981 CB ASN A 261 14.671 46.031 3.498 1.00 13.86 A C ATOM 1982 CG ASN A 261 14.287 47.512 3.332 1.00 14.28 A C ATOM 1983 OD1 ASN A 261 13.711 47.912 2.344 1.00 14.95 A O ATOM 1984 ND2 ASN A 261 14.606 48.317 4.304 1.00 14.25 A N ATOM 1985 C ASN A 261 14.149 43.646 2.898 1.00 14.22 A C ATOM 1986 O ASN A 261 14.355 43.085 1.825 1.00 14.32 A O ATOM 1987 N TYR A 262 14.379 43.034 4.044 1.00 14.90 A N ATOM 1988 CA TYR A 262 15.196 41.827 4.071 1.00 15.53 A C ATOM 1989 CB TYR A 262 16.323 41.998 5.092 1.00 15.60 A C ATOM 1990 CG TYR A 262 17.157 43.252 4.863 1.00 15.76 A C ATOM 1991 CD1 TYR A 262 17.756 43.490 3.638 1.00 15.71 A C ATOM 1992 CE1 TYR A 262 18.511 44.630 3.413 1.00 15.96 A C ATOM 1993 CZ TYR A 262 18.692 45.572 4.420 1.00 15.60 A C ATOM 1994 OH TYR A 262 19.453 46.702 4.174 1.00 13.73 A O ATOM 1995 CE2 TYR A 262 18.097 45.353 5.655 1.00 16.02 A C ATOM 1996 CD2 TYR A 262 17.341 44.199 5.872 1.00 15.99 A C ATOM 1997 C TYR A 262 14.422 40.520 4.293 1.00 15.92 A C ATOM 1998 O TYR A 262 14.850 39.469 3.830 1.00 17.27 A O ATOM 1999 N LEU A 263 13.284 40.543 4.957 1.00 15.38 A N ATOM 2000 CA LEU A 263 12.508 39.307 5.019 1.00 15.76 A C ATOM 2001 CB LEU A 263 11.362 39.431 6.036 1.00 16.59 A C ATOM 2002 CG LEU A 263 11.562 38.897 7.463 1.00 16.71 A C ATOM 2003 CD1 LEU A 263 13.023 38.786 7.862 1.00 16.41 A C ATOM 2004 CD2 LEU A 263 10.766 39.742 8.454 1.00 16.56 A C ATOM 2005 C LEU A 263 11.949 38.939 3.637 1.00 15.00 A C ATOM 2006 O LEU A 263 11.773 39.803 2.785 1.00 15.82 A O ATOM 2007 N THR A 264 11.680 37.654 3.439 1.00 14.04 A N ATOM 2008 CA THR A 264 11.150 37.105 2.182 1.00 13.18 A C ATOM 2009 CB THR A 264 12.254 36.395 1.347 1.00 12.53 A C ATOM 2010 OG1 THR A 264 12.519 35.080 1.876 1.00 12.08 A O ATOM 2011 CG2 THR A 264 13.522 37.213 1.294 1.00 12.33 A C ATOM 2012 C THR A 264 10.061 36.059 2.490 1.00 13.48 A C ATOM 2013 O THR A 264 9.862 35.671 3.655 1.00 13.25 A O ATOM 2014 N PRO A 265 9.396 35.535 1.446 1.00 13.46 A N ATOM 2015 CA PRO A 265 8.244 34.703 1.688 1.00 13.44 A C ATOM 2016 CB PRO A 265 7.713 34.453 0.278 1.00 13.36 A C ATOM 2017 CG PRO A 265 8.105 35.667 0.469 1.00 13.47 A C ATOM 2018 CD PRO A 265 9.514 35.838 0.014 1.00 13.66 A C ATOM 2019 C PRO A 265 8.584 33.392 2.320 1.00 13.55 A C ATOM 2020 O PRO A 265 7.713 32.600 2.615 1.00 14.25 A O ATOM 2021 N THR A 266 9.862 33.187 2.529 1.00 13.50 A N ATOM 2022 CA THR A 266 10.439 31.881 2.743 1.00 12.66 A C ATOM 2023 CB THR A 266 11.222 31.577 1.437 1.00 12.59 A C ATOM 2024 OG1 THR A 266 10.606 30.478 0.813 1.00 12.07 A O ATOM 2025 CG2 THR A 266 12.736 31.331 1.610 1.00 12.62 A C ATOM 2026 C THR A 266 11.320 31.926 3.951 1.00 12.14 A C ATOM 2027 O THR A 266 11.955 30.972 4.264 1.00 12.11 A O ATOM 2028 N SER A 267 11.378 33.074 4.611 1.00 12.40 A N ATOM 2029 CA SER A 267 12.317 33.305 5.672 1.00 12.42 A C ATOM 2030 CB SER A 267 12.291 34.755 6.099 1.00 12.13 A C ATOM 2031 OG SER A 267 12.643 35.580 5.035 1.00 11.99 A O ATOM 2032 C SER A 267 11.968 32.465 6.859 1.00 13.24 A C ATOM 2033 O SER A 267 10.812 32.409 7.303 1.00 13.97 A O ATOM 2034 N ASN A 268 12.978 31.795 7.366 1.00 13.85 A N ATOM 2035 CA ASN A 268 12.878 31.150 8.667 1.00 14.49 A C ATOM 2036 CB ASN A 268 13.528 29.763 8.601 1.00 14.22 A C ATOM 2037 CG ASN A 268 15.016 29.822 8.253 1.00 13.98 A C ATOM 2038 OD1 ASN A 268 15.707 30.838 8.451 1.00 13.99 A O ATOM 2039 ND2 ASN A 268 15.511 28.726 7.730 1.00 13.52 A N ATOM 2040 C ASN A 268 13.532 31.987 9.787 1.00 15.25 A C ATOM 2041 O ASN A 268 14.066 33.113 9.552 1.00 14.36 A O ATOM 2042 N PHE A 269 13.499 31.408 10.994 1.00 15.91 A N ATOM 2043 CA PHE A 269 13.978 32.076 12.198 1.00 16.68 A C ATOM 2044 CB PHE A 269 13.906 31.122 13.401 1.00 16.90 A C ATOM 2045 CG PHE A 269 12.562 31.075 14.062 1.00 16.51 A C ATOM 2046 CD2 PHE A 269 11.620 30.146 13.683 1.00 16.34 A C ATOM 2047 CE2 PHE A 269 10.379 30.116 14.305 1.00 16.36 A C ATOM 2048 CZ PHE A 269 10.067 31.015 15.318 1.00 15.85 A C ATOM 2049 CE1 PHE A 269 10.985 31.944 15.704 1.00 15.68 A C ATOM 2050 CD1 PHE A 269 12.236 31.971 15.078 1.00 16.47 A C ATOM 2051 C PHE A 269 15.412 32.571 12.004 1.00 16.65 A C ATOM 2052 O PHE A 269 15.734 33.714 12.297 1.00 16.47 A O ATOM 2053 N SER A 270 16.261 31.703 11.487 1.00 17.12 A N ATOM 2054 CA SER A 270 17.660 32.075 11.211 1.00 17.53 A C ATOM 2055 CB SER A 270 18.420 30.901 10.589 1.00 17.92 A C ATOM 2056 OG SER A 270 19.771 31.074 10.914 1.00 19.56 A O ATOM 2057 C SER A 270 17.776 33.298 10.309 1.00 16.25 A C ATOM 2058 O SER A 270 18.521 34.249 10.592 1.00 16.12 A O ATOM 2059 N ALA A 271 17.014 33.274 9.226 1.00 15.54 A N ATOM 2060 CA ALA A 271 16.898 34.441 8.354 1.00 14.92 A C ATOM 2061 CB ALA A 271 16.098 34.060 7.101 1.00 15.08 A C ATOM 2062 C ALA A 271 16.276 35.679 9.083 1.00 13.85 A C ATOM 2063 O ALA A 271 16.669 36.848 8.852 1.00 12.80 A O ATOM 2064 N MET A 272 15.314 35.433 9.965 1.00 13.07 A N ATOM 2065 CA MET A 272 14.781 36.544 10.730 1.00 13.25 A C ATOM 2066 CB MET A 272 13.622 36.100 11.628 1.00 13.09 A C ATOM 2067 CG MET A 272 13.165 37.128 12.682 1.00 12.47 A C ATOM 2068 SD MET A 272 12.018 38.351 12.062 1.00 11.85 A S ATOM 2069 CE MET A 272 12.986 39.846 11.892 1.00 11.70 A C ATOM 2070 C MET A 272 15.882 37.220 11.555 1.00 13.54 A C ATOM 2071 O MET A 272 15.903 38.452 11.661 1.00 13.35 A O ATOM 2072 N ARG A 273 16.773 36.405 12.127 1.00 13.96 A N ATOM 2073 CA ARG A 273 17.927 36.880 12.896 1.00 14.72 A C ATOM 2074 CB ARG A 273 18.732 35.678 13.439 1.00 16.09 A C ATOM 2075 CG ARG A 273 19.897 36.062 14.351 1.00 17.57 A C ATOM 2076 CD ARG A 273 20.932 34.937 14.559 1.00 19.14 A C ATOM 2077 NE ARG A 273 22.199 35.555 15.019 1.00 20.49 A N ATOM 2078 CZ ARG A 273 22.627 35.627 16.282 1.00 19.97 A C ATOM 2079 NH1 ARG A 273 21.946 35.082 17.277 1.00 21.14 A N ATOM 2080 NH2 ARG A 273 23.746 36.263 16.557 1.00 19.78 A N ATOM 2081 C ARG A 273 18.832 37.792 12.058 1.00 14.15 A C ATOM 2082 O ARG A 273 19.154 38.934 12.442 1.00 13.74 A O ATOM 2083 N ALA A 274 19.233 37.270 10.904 1.00 13.53 A N ATOM 2084 CA ALA A 274 20.050 38.025 9.967 1.00 12.90 A C ATOM 2085 CB ALA A 274 20.334 37.174 8.741 1.00 12.64 A C ATOM 2086 C ALA A 274 19.346 39.314 9.574 1.00 12.59 A C ATOM 2087 O ALA A 274 19.946 40.390 9.501 1.00 12.04 A O ATOM 2088 N ALA A 275 18.060 39.202 9.309 1.00 12.71 A N ATOM 2089 CA ALA A 275 17.357 40.339 8.776 1.00 13.34 A C ATOM 2090 CB ALA A 275 15.961 39.931 8.356 1.00 13.53 A C ATOM 2091 C ALA A 275 17.318 41.459 9.804 1.00 13.49 A C ATOM 2092 O ALA A 275 17.594 42.638 9.496 1.00 13.79 A O ATOM 2093 N ALA A 276 16.987 41.086 11.036 1.00 13.40 A N ATOM 2094 CA ALA A 276 16.968 42.041 12.114 1.00 13.48 A C ATOM 2095 CB ALA A 276 16.478 41.373 13.387 1.00 13.69 A C ATOM 2096 C ALA A 276 18.370 42.622 12.286 1.00 13.41 A C ATOM 2097 O ALA A 276 18.531 43.833 12.411 1.00 12.81 A O ATOM 2098 N ILE A 277 19.390 41.767 12.244 1.00 13.47 A N ATOM 2099 CA ILE A 277 20.744 42.282 12.313 1.00 13.96 A C ATOM 2100 CB ILE A 277 21.797 41.190 12.261 1.00 14.04 A C ATOM 2101 CG1 ILE A 277 21.814 40.438 13.581 1.00 14.13 A C ATOM 2102 CD1 ILE A 277 22.709 39.232 13.583 1.00 14.32 A C ATOM 2103 CG2 ILE A 277 23.163 41.829 12.023 1.00 14.29 A C ATOM 2104 C ILE A 277 21.066 43.276 11.210 1.00 14.15 A C ATOM 2105 O ILE A 277 21.596 44.354 11.478 1.00 14.38 A O ATOM 2106 N GLN A 278 20.762 42.921 9.973 1.00 14.64 A N ATOM 2107 CA GLN A 278 21.044 43.832 8.881 1.00 15.29 A C ATOM 2108 CB GLN A 278 20.665 43.220 7.546 1.00 15.95 A C ATOM 2109 CG GLN A 278 21.138 44.034 6.336 1.00 16.69 A C ATOM 2110 CD GLN A 278 22.656 44.231 6.267 1.00 16.71 A C ATOM 2111 OE1 GLN A 278 23.418 43.326 5.935 1.00 16.42 A O ATOM 2112 NE2 GLN A 278 23.084 45.437 6.552 1.00 17.15 A N ATOM 2113 C GLN A 278 20.343 45.163 9.067 1.00 15.22 A C ATOM 2114 O GLN A 278 20.930 46.204 8.832 1.00 15.46 A O ATOM 2115 N ALA A 279 19.100 45.141 9.522 1.00 15.50 A N ATOM 2116 CA ALA A 279 18.344 46.381 9.668 1.00 15.59 A C ATOM 2117 CB ALA A 279 16.872 46.074 9.868 1.00 15.79 A C ATOM 2118 C ALA A 279 18.870 47.272 10.789 1.00 15.64 A C ATOM 2119 O ALA A 279 18.837 48.496 10.692 1.00 16.17 A O ATOM 2120 N ALA A 280 19.357 46.670 11.858 1.00 15.94 A N ATOM 2121 CA ALA A 280 19.950 47.456 12.910 1.00 16.38 A C ATOM 2122 CB ALA A 280 20.116 46.649 14.174 1.00 16.73 A C ATOM 2123 C ALA A 280 21.286 47.972 12.446 1.00 16.78 A C ATOM 2124 O ALA A 280 21.616 49.113 12.734 1.00 17.18 A O ATOM 2125 N THR A 281 22.054 47.145 11.732 1.00 17.16 A N ATOM 2126 CA THR A 281 23.322 47.592 11.185 1.00 17.22 A C ATOM 2127 CB THR A 281 23.996 46.539 10.315 1.00 17.66 A C ATOM 2128 OG1 THR A 281 24.434 45.442 11.137 1.00 17.89 A O ATOM 2129 CG2 THR A 281 25.202 47.154 9.572 1.00 17.44 A C ATOM 2130 C THR A 281 23.074 48.819 10.355 1.00 17.79 A C ATOM 2131 O THR A 281 23.709 49.845 10.578 1.00 18.78 A O ATOM 2132 N ASP A 282 22.119 48.745 9.432 1.00 18.24 A N ATOM 2133 CA ASP A 282 21.722 49.930 8.616 1.00 18.73 A C ATOM 2134 CB ASP A 282 20.399 49.683 7.892 1.00 17.78 A C ATOM 2135 CG ASP A 282 20.513 48.689 6.767 1.00 17.00 A C ATOM 2136 OD1 ASP A 282 21.661 48.244 6.447 1.00 15.10 A O ATOM 2137 OD2 ASP A 282 19.413 48.384 6.218 1.00 16.44 A O ATOM 2138 C ASP A 282 21.538 51.236 9.375 1.00 19.72 A C ATOM 2139 O ASP A 282 21.845 52.281 8.873 1.00 19.64 A O ATOM 2140 N LEU A 283 20.992 51.163 10.575 1.00 22.83 A N ATOM 2141 CA LEU A 283 20.581 52.346 11.323 1.00 23.96 A C ATOM 2142 CB LEU A 283 19.265 52.043 12.036 1.00 24.88 A C ATOM 2143 CG LEU A 283 18.029 51.915 11.148 1.00 25.50 A C ATOM 2144 CD1 LEU A 283 16.958 51.126 11.898 1.00 26.24 A C ATOM 2145 CD2 LEU A 283 17.524 53.299 10.763 1.00 25.11 A C ATOM 2146 C LEU A 283 21.554 52.812 12.388 1.00 23.80 A C ATOM 2147 O LEU A 283 21.489 53.966 12.790 1.00 23.32 A O ATOM 2148 N TYR A 284 22.385 51.915 12.904 1.00 24.03 A N ATOM 2149 CA TYR A 284 23.184 52.237 14.085 1.00 25.72 A C ATOM 2150 CB TYR A 284 22.597 51.570 15.350 1.00 25.41 A C ATOM 2151 CG TYR A 284 21.211 52.073 15.711 1.00 25.02 A C ATOM 2152 CD1 TYR A 284 21.037 53.340 16.265 1.00 24.40 A C ATOM 2153 CE1 TYR A 284 19.766 53.811 16.579 1.00 25.54 A C ATOM 2154 CZ TYR A 284 18.630 53.007 16.344 1.00 24.69 A C ATOM 2155 OH TYR A 284 17.349 53.493 16.656 1.00 23.49 A O ATOM 2156 CE2 TYR A 284 18.801 51.748 15.782 1.00 23.41 A C ATOM 2157 CD2 TYR A 284 20.071 51.292 15.469 1.00 23.48 A C ATOM 2158 C TYR A 284 24.632 51.848 13.937 1.00 27.83 A C ATOM 2159 O TYR A 284 25.428 52.120 14.841 1.00 29.91 A O ATOM 2160 N GLY A 285 24.982 51.213 12.822 1.00 27.88 A N ATOM 2161 CA GLY A 285 26.361 50.831 12.567 1.00 29.33 A C ATOM 2162 C GLY A 285 26.614 49.435 13.076 1.00 32.33 A C ATOM 2163 O GLY A 285 26.058 49.040 14.098 1.00 36.64 A O ATOM 2164 N ALA A 286 27.481 48.698 12.392 1.00 32.78 A N ATOM 2165 CA ALA A 286 27.576 47.250 12.579 1.00 33.56 A C ATOM 2166 CB ALA A 286 28.379 46.627 11.440 1.00 34.16 A C ATOM 2167 C ALA A 286 28.143 46.799 13.923 1.00 33.26 A C ATOM 2168 O ALA A 286 28.010 45.618 14.292 1.00 34.56 A O ATOM 2169 N ASN A 287 28.772 47.707 14.656 1.00 31.09 A N ATOM 2170 CA ASN A 287 29.308 47.330 15.949 1.00 29.96 A C ATOM 2171 CB ASN A 287 30.821 47.577 15.965 1.00 30.24 A C ATOM 2172 CG ASN A 287 31.522 46.889 17.130 1.00 30.47 A C ATOM 2173 OD1 ASN A 287 31.112 45.823 17.601 1.00 26.91 A O ATOM 2174 ND2 ASN A 287 32.576 47.529 17.626 1.00 31.27 A N ATOM 2175 C ASN A 287 28.568 48.065 17.076 1.00 27.79 A C ATOM 2176 O ASN A 287 29.058 48.213 18.185 1.00 26.46 A O ATOM 2177 N SER A 288 27.350 48.482 16.802 1.00 27.08 A N ATOM 2178 CA SER A 288 26.584 49.237 17.781 1.00 26.73 A C ATOM 2179 CB SER A 288 25.406 49.971 17.108 1.00 27.43 A C ATOM 2180 OG SER A 288 24.598 49.085 16.318 1.00 28.18 A O ATOM 2181 C SER A 288 26.070 48.333 18.879 1.00 24.80 A C ATOM 2182 O SER A 288 26.043 47.106 18.746 1.00 23.67 A O ATOM 2183 N SER A 289 25.657 48.976 19.963 1.00 24.24 A N ATOM 2184 CA SER A 289 24.931 48.317 21.052 1.00 24.51 A C ATOM 2185 CB SER A 289 24.697 49.308 22.203 1.00 23.11 A C ATOM 2186 OG SER A 289 24.340 50.588 21.729 1.00 21.73 A O ATOM 2187 C SER A 289 23.576 47.698 20.591 1.00 25.23 A C ATOM 2188 O SER A 289 23.156 46.616 21.073 1.00 27.12 A O ATOM 2189 N GLN A 290 22.919 48.376 19.656 1.00 23.65 A N ATOM 2190 CA GLN A 290 21.640 47.929 19.149 1.00 23.31 A C ATOM 2191 CB GLN A 290 21.030 48.994 18.253 1.00 22.58 A C ATOM 2192 CG GLN A 290 20.519 50.209 19.023 1.00 22.68 A C ATOM 2193 CD GLN A 290 21.505 51.364 19.101 1.00 22.39 A C ATOM 2194 OE1 GLN A 290 22.711 51.186 19.035 1.00 23.40 A O ATOM 2195 NE2 GLN A 290 20.980 52.561 19.222 1.00 22.20 A N ATOM 2196 C GLN A 290 21.855 46.649 18.386 1.00 24.05 A C ATOM 2197 O GLN A 290 21.177 45.636 18.626 1.00 23.70 A O ATOM 2198 N VAL A 291 22.836 46.672 17.493 1.00 24.02 A N ATOM 2199 CA VAL A 291 23.154 45.475 16.754 1.00 23.78 A C ATOM 2200 CB VAL A 291 24.348 45.668 15.809 1.00 24.04 A C ATOM 2201 CG1 VAL A 291 24.995 44.332 15.456 1.00 23.39 A C ATOM 2202 CG2 VAL A 291 23.882 46.376 14.555 1.00 24.62 A C ATOM 2203 C VAL A 291 23.475 44.407 17.748 1.00 24.05 A C ATOM 2204 O VAL A 291 23.070 43.242 17.593 1.00 22.27 A O ATOM 2205 N ASN A 292 24.215 44.790 18.781 1.00 25.34 A N ATOM 2206 CA ASN A 292 24.673 43.762 19.676 1.00 26.69 A C ATOM 2207 CB ASN A 292 25.884 44.205 20.478 1.00 30.49 A C ATOM 2208 CG ASN A 292 26.820 43.042 20.731 1.00 35.02 A C ATOM 2209 OD1 ASN A 292 27.508 42.596 19.808 1.00 39.60 A O ATOM 2210 ND2 ASN A 292 26.793 42.487 21.952 1.00 35.12 A N ATOM 2211 C ASN A 292 23.553 43.174 20.551 1.00 23.23 A C ATOM 2212 O ASN A 292 23.547 41.978 20.829 1.00 21.51 A O ATOM 2213 N ALA A 293 22.594 44.013 20.932 1.00 20.89 A N ATOM 2214 CA ALA A 293 21.432 43.577 21.719 1.00 19.66 A C ATOM 2215 CB ALA A 293 20.559 44.780 22.043 1.00 20.04 A C ATOM 2216 C ALA A 293 20.614 42.573 20.957 1.00 18.76 A C ATOM 2217 O ALA A 293 20.105 41.606 21.499 1.00 17.05 A O ATOM 2218 N VAL A 294 20.461 42.866 19.669 1.00 18.81 A N ATOM 2219 CA VAL A 294 19.729 42.016 18.771 1.00 17.38 A C ATOM 2220 CB VAL A 294 19.646 42.671 17.382 1.00 16.37 A C ATOM 2221 CG1 VAL A 294 19.185 41.672 16.324 1.00 16.38 A C ATOM 2222 CG2 VAL A 294 18.736 43.875 17.422 1.00 15.72 A C ATOM 2223 C VAL A 294 20.396 40.645 18.748 1.00 17.76 A C ATOM 2224 O VAL A 294 19.713 39.640 18.840 1.00 17.49 A O ATOM 2225 N LYS A 295 21.727 40.613 18.654 1.00 18.95 A N ATOM 2226 CA LYS A 295 22.461 39.349 18.560 1.00 19.76 A C ATOM 2227 CB LYS A 295 23.964 39.577 18.381 1.00 21.38 A C ATOM 2228 CG LYS A 295 24.399 39.923 16.961 1.00 22.34 A C ATOM 2229 CD LYS A 295 25.900 40.268 16.887 1.00 23.25 A C ATOM 2230 CE LYS A 295 26.277 40.738 15.476 1.00 23.34 A C ATOM 2231 NZ LYS A 295 27.731 40.846 15.162 1.00 22.84 A N ATOM 2232 C LYS A 295 22.239 38.480 19.774 1.00 19.36 A C ATOM 2233 O LYS A 295 21.916 37.284 19.655 1.00 18.79 A O ATOM 2234 N LYS A 296 22.394 39.073 20.944 1.00 19.79 A N ATOM 2235 CA LYS A 296 22.200 38.316 22.176 1.00 21.18 A C ATOM 2236 CB LYS A 296 22.618 39.143 23.379 1.00 23.67 A C ATOM 2237 CG LYS A 296 24.126 39.307 23.392 1.00 27.94 A C ATOM 2238 CD LYS A 296 24.657 39.899 24.691 1.00 32.89 A C ATOM 2239 CE LYS A 296 26.166 39.650 24.836 1.00 37.16 A C ATOM 2240 NZ LYS A 296 26.520 38.247 25.268 1.00 38.34 A N ATOM 2241 C LYS A 296 20.785 37.754 22.325 1.00 19.72 A C ATOM 2242 O LYS A 296 20.603 36.553 22.615 1.00 18.85 A O ATOM 2243 N ALA A 297 19.804 38.618 22.087 1.00 18.65 A N ATOM 2244 CA ALA A 297 18.395 38.236 22.059 1.00 18.30 A C ATOM 2245 CB ALA A 297 17.544 39.389 21.570 1.00 19.00 A C ATOM 2246 C ALA A 297 18.141 37.014 21.207 1.00 18.02 A C ATOM 2247 O ALA A 297 17.575 36.041 21.683 1.00 18.61 A O ATOM 2248 N TYR A 298 18.578 37.016 19.960 1.00 17.55 A N ATOM 2249 CA TYR A 298 18.361 35.808 19.165 1.00 17.98 A C ATOM 2250 CB TYR A 298 18.595 36.043 17.662 1.00 17.98 A C ATOM 2251 CG TYR A 298 17.361 36.698 17.049 1.00 17.27 A C ATOM 2252 CD1 TYR A 298 16.272 35.926 16.677 1.00 16.76 A C ATOM 2253 CE1 TYR A 298 15.140 36.498 16.150 1.00 16.52 A C ATOM 2254 CZ TYR A 298 15.057 37.866 16.011 1.00 16.59 A C ATOM 2255 OH TYR A 298 13.898 38.414 15.489 1.00 15.41 A O ATOM 2256 CE2 TYR A 298 16.135 38.665 16.381 1.00 16.79 A C ATOM 2257 CD2 TYR A 298 17.268 38.079 16.910 1.00 16.48 A C ATOM 2258 C TYR A 298 19.123 34.601 19.686 1.00 17.99 A C ATOM 2259 O TYR A 298 18.623 33.470 19.572 1.00 19.07 A O ATOM 2260 N THR A 299 20.307 34.828 20.255 1.00 17.65 A N ATOM 2261 CA THR A 299 21.056 33.746 20.902 1.00 17.98 A C ATOM 2262 CB THR A 299 22.472 34.217 21.368 1.00 17.57 A C ATOM 2263 OG1 THR A 299 23.235 34.706 20.250 1.00 16.90 A O ATOM 2264 CG2 THR A 299 23.217 33.076 22.047 1.00 16.53 A C ATOM 2265 C THR A 299 20.231 33.206 22.118 1.00 18.22 A C ATOM 2266 O THR A 299 20.019 31.985 22.289 1.00 16.64 A O ATOM 2267 N ALA A 300 19.744 34.132 22.938 1.00 18.02 A N ATOM 2268 CA ALA A 300 18.960 33.751 24.087 1.00 18.32 A C ATOM 2269 CB ALA A 300 18.408 34.982 24.786 1.00 18.60 A C ATOM 2270 C ALA A 300 17.840 32.798 23.701 1.00 18.60 A C ATOM 2271 O ALA A 300 17.659 31.798 24.366 1.00 20.19 A O ATOM 2272 N VAL A 301 17.101 33.074 22.630 1.00 18.61 A N ATOM 2273 CA VAL A 301 15.996 32.189 22.240 1.00 18.71 A C ATOM 2274 CB VAL A 301 14.856 32.940 21.538 1.00 19.41 A C ATOM 2275 CG1 VAL A 301 14.404 34.146 22.338 1.00 19.54 A C ATOM 2276 CG2 VAL A 301 15.298 33.395 20.170 1.00 20.37 A C ATOM 2277 C VAL A 301 16.457 31.043 21.350 1.00 18.65 A C ATOM 2278 O VAL A 301 15.646 30.314 20.777 1.00 18.51 A O ATOM 2279 N GLY A 302 17.758 30.871 21.231 1.00 19.01 A N ATOM 2280 CA GLY A 302 18.282 29.621 20.718 1.00 19.86 A C ATOM 2281 C GLY A 302 18.370 29.640 19.219 1.00 21.35 A C ATOM 2282 O GLY A 302 18.411 28.580 18.581 1.00 20.19 A O ATOM 2283 N VAL A 303 18.392 30.858 18.659 1.00 23.47 A N ATOM 2284 CA VAL A 303 18.503 31.054 17.208 1.00 23.96 A C ATOM 2285 CB VAL A 303 17.367 31.958 16.677 1.00 23.91 A C ATOM 2286 CG1 VAL A 303 17.488 32.161 15.169 1.00 24.18 A C ATOM 2287 CG2 VAL A 303 16.027 31.330 16.985 1.00 24.04 A C ATOM 2288 C VAL A 303 19.868 31.647 16.845 1.00 23.68 A C ATOM 2289 O VAL A 303 20.199 32.752 17.266 1.00 22.79 A O ATOM 2290 N ASN A 304 20.630 30.924 16.033 1.00 24.44 A N ATOM 2291 CA ASN A 304 21.971 31.369 15.668 1.00 27.13 A C ATOM 2292 CB ASN A 304 22.976 30.333 16.137 1.00 27.63 A C ATOM 2293 CG ASN A 304 22.782 29.969 17.602 1.00 28.08 A C ATOM 2294 OD1 ASN A 304 22.758 30.844 18.497 1.00 26.81 A O ATOM 2295 ND2 ASN A 304 22.632 28.666 17.855 1.00 27.74 A N ATOM 2296 C ASN A 304 22.203 31.666 14.188 1.00 27.90 A C ATOM 2297 O ASN A 304 21.646 31.075 13.248 1.00 28.54 A O ATOM 2298 OXT ASN A 304 23.015 32.544 13.941 1.00 27.35 A O ATOM 2299 N ALA B 1 27.118 11.588 16.141 1.00 36.52 B N ATOM 2300 CA ALA B 1 26.133 11.218 17.198 1.00 37.78 B C ATOM 2301 CB ALA B 1 25.839 12.399 18.109 1.00 36.98 B C ATOM 2302 C ALA B 1 24.878 10.774 16.492 1.00 39.27 B C ATOM 2303 O ALA B 1 24.736 11.016 15.302 1.00 43.37 B O ATOM 2304 N THR B 2 23.958 10.156 17.220 1.00 39.24 B N ATOM 2305 CA THR B 2 22.776 9.556 16.609 1.00 38.21 B C ATOM 2306 CB THR B 2 22.792 8.015 16.742 1.00 38.56 B C ATOM 2307 OG1 THR B 2 23.817 7.475 15.901 1.00 37.57 B O ATOM 2308 CG2 THR B 2 21.445 7.408 16.322 1.00 39.78 B C ATOM 2309 C THR B 2 21.477 10.140 17.183 1.00 37.53 B C ATOM 2310 O THR B 2 21.027 9.766 18.266 1.00 32.77 B O ATOM 2311 N GLY B 3 20.864 11.037 16.413 1.00 38.90 B N ATOM 2312 CA GLY B 3 19.625 11.693 16.822 1.00 39.37 B C ATOM 2313 C GLY B 3 18.385 10.922 16.439 1.00 37.66 B C ATOM 2314 O GLY B 3 18.379 10.180 15.475 1.00 38.38 B O ATOM 2315 N THR B 4 17.325 11.116 17.193 1.00 37.26 B N ATOM 2316 CA THR B 4 16.066 10.493 16.873 1.00 39.03 B C ATOM 2317 CB THR B 4 15.631 9.497 17.978 1.00 38.57 B C ATOM 2318 OG1 THR B 4 14.242 9.154 17.811 1.00 38.10 B O ATOM 2319 CG2 THR B 4 15.829 10.089 19.342 1.00 36.87 B C ATOM 2320 C THR B 4 14.993 11.568 16.642 1.00 39.28 B C ATOM 2321 O THR B 4 15.018 12.622 17.277 1.00 37.20 B O ATOM 2322 N GLY B 5 14.064 11.284 15.725 1.00 38.89 B N ATOM 2323 CA GLY B 5 12.864 12.101 15.541 1.00 37.29 B C ATOM 2324 C GLY B 5 11.851 11.559 14.531 1.00 35.59 B C ATOM 2325 O GLY B 5 12.190 10.789 13.611 1.00 34.39 B O ATOM 2326 N LYS B 6 10.601 11.982 14.704 1.00 32.33 B N ATOM 2327 CA LYS B 6 9.501 11.572 13.834 1.00 30.16 B C ATOM 2328 CB LYS B 6 8.164 11.793 14.523 1.00 28.67 B C ATOM 2329 CG LYS B 6 8.056 11.021 15.798 1.00 29.42 B C ATOM 2330 CD LYS B 6 6.667 11.050 16.395 1.00 31.17 B C ATOM 2331 CE LYS B 6 6.396 9.726 17.100 1.00 31.96 B C ATOM 2332 NZ LYS B 6 5.427 9.958 18.189 1.00 33.82 B N ATOM 2333 C LYS B 6 9.528 12.360 12.547 1.00 28.68 B C ATOM 2334 O LYS B 6 9.889 13.529 12.555 1.00 29.96 B O ATOM 2335 N GLY B 7 9.141 11.718 11.447 1.00 26.88 B N ATOM 2336 CA GLY B 7 9.082 12.374 10.150 1.00 24.95 B C ATOM 2337 C GLY B 7 7.727 13.011 10.017 1.00 23.60 B C ATOM 2338 O GLY B 7 6.884 12.864 10.883 1.00 23.09 B O ATOM 2339 N VAL B 8 7.515 13.700 8.912 1.00 22.56 B N ATOM 2340 CA VAL B 8 6.255 14.375 8.641 1.00 22.38 B C ATOM 2341 CB VAL B 8 6.215 14.891 7.197 1.00 22.59 B C ATOM 2342 CG1 VAL B 8 4.869 15.545 6.892 1.00 22.83 B C ATOM 2343 CG2 VAL B 8 7.357 15.870 6.940 1.00 22.50 B C ATOM 2344 C VAL B 8 5.041 13.479 8.847 1.00 22.68 B C ATOM 2345 O VAL B 8 4.003 13.935 9.296 1.00 21.46 B O ATOM 2346 N LEU B 9 5.173 12.201 8.498 1.00 24.54 B N ATOM 2347 CA LEU B 9 4.063 11.242 8.600 1.00 24.12 B C ATOM 2348 CB LEU B 9 4.135 10.261 7.432 1.00 23.12 B C ATOM 2349 CG LEU B 9 3.359 10.564 6.154 1.00 21.95 B C ATOM 2350 CD1 LEU B 9 3.041 12.036 6.027 1.00 20.77 B C ATOM 2351 CD2 LEU B 9 4.141 9.999 4.961 1.00 21.42 B C ATOM 2352 C LEU B 9 4.046 10.456 9.890 1.00 25.26 B C ATOM 2353 O LEU B 9 3.442 9.408 9.933 1.00 28.39 B O ATOM 2354 N GLY B 10 4.723 10.932 10.930 1.00 26.73 B N ATOM 2355 CA GLY B 10 4.586 10.358 12.279 1.00 26.45 B C ATOM 2356 C GLY B 10 5.481 9.174 12.586 1.00 26.20 B C ATOM 2357 O GLY B 10 5.297 8.504 13.614 1.00 24.13 B O ATOM 2358 N ASP B 11 6.481 8.966 11.727 1.00 26.26 B N ATOM 2359 CA ASP B 11 7.342 7.781 11.761 1.00 26.23 B C ATOM 2360 CB ASP B 11 7.410 7.155 10.356 1.00 24.59 B C ATOM 2361 CG ASP B 11 7.968 8.109 9.295 1.00 24.79 B C ATOM 2362 OD1 ASP B 11 7.465 9.238 9.139 1.00 25.46 B O ATOM 2363 OD2 ASP B 11 8.922 7.739 8.596 1.00 23.52 B O ATOM 2364 C ASP B 11 8.767 8.052 12.313 1.00 28.01 B C ATOM 2365 O ASP B 11 9.541 8.838 11.737 1.00 29.86 B O ATOM 2366 N THR B 12 9.127 7.357 13.397 1.00 28.40 B N ATOM 2367 CA THR B 12 10.417 7.555 14.073 1.00 27.68 B C ATOM 2368 CB THR B 12 10.402 6.914 15.465 1.00 25.99 B C ATOM 2369 OG1 THR B 12 9.232 7.350 16.173 1.00 25.66 B O ATOM 2370 CG2 THR B 12 11.645 7.298 16.258 1.00 24.54 B C ATOM 2371 C THR B 12 11.633 7.041 13.285 1.00 29.85 B C ATOM 2372 O THR B 12 11.677 5.875 12.875 1.00 32.91 B O ATOM 2373 N LYS B 13 12.618 7.922 13.090 1.00 30.70 B N ATOM 2374 CA LYS B 13 13.867 7.580 12.402 1.00 31.16 B C ATOM 2375 CB LYS B 13 14.036 8.339 11.087 1.00 31.49 B C ATOM 2376 CG LYS B 13 12.756 8.854 10.458 1.00 32.70 B C ATOM 2377 CD LYS B 13 13.037 9.300 9.041 1.00 32.47 B C ATOM 2378 CE LYS B 13 11.763 9.658 8.315 1.00 32.16 B C ATOM 2379 NZ LYS B 13 10.786 8.555 8.175 1.00 31.87 B N ATOM 2380 C LYS B 13 15.052 7.967 13.238 1.00 33.23 B C ATOM 2381 O LYS B 13 14.940 8.784 14.157 1.00 39.07 B O ATOM 2382 N SER B 14 16.196 7.403 12.866 1.00 31.47 B N ATOM 2383 CA SER B 14 17.474 7.714 13.446 1.00 29.93 B C ATOM 2384 CB SER B 14 18.225 6.440 13.792 1.00 31.68 B C ATOM 2385 OG SER B 14 17.421 5.631 14.618 1.00 34.18 B O ATOM 2386 C SER B 14 18.244 8.385 12.377 1.00 28.96 B C ATOM 2387 O SER B 14 17.989 8.156 11.196 1.00 27.52 B O ATOM 2388 N PHE B 15 19.225 9.178 12.773 1.00 28.58 B N ATOM 2389 CA PHE B 15 20.097 9.822 11.797 1.00 28.92 B C ATOM 2390 CB PHE B 15 19.330 10.903 11.010 1.00 27.95 B C ATOM 2391 CG PHE B 15 18.345 11.675 11.853 1.00 26.41 B C ATOM 2392 CD1 PHE B 15 18.751 12.766 12.586 1.00 24.71 B C ATOM 2393 CE1 PHE B 15 17.861 13.459 13.368 1.00 24.48 B C ATOM 2394 CZ PHE B 15 16.548 13.067 13.437 1.00 25.51 B C ATOM 2395 CE2 PHE B 15 16.130 11.967 12.722 1.00 26.27 B C ATOM 2396 CD2 PHE B 15 17.028 11.281 11.934 1.00 26.09 B C ATOM 2397 C PHE B 15 21.283 10.421 12.515 1.00 30.15 B C ATOM 2398 O PHE B 15 21.231 10.661 13.735 1.00 28.64 B O ATOM 2399 N THR B 16 22.350 10.643 11.756 1.00 32.13 B N ATOM 2400 CA THR B 16 23.564 11.231 12.297 1.00 35.95 B C ATOM 2401 CB THR B 16 24.775 10.980 11.371 1.00 35.50 B C ATOM 2402 OG1 THR B 16 25.103 9.584 11.373 1.00 34.31 B O ATOM 2403 CG2 THR B 16 26.013 11.807 11.799 1.00 35.19 B C ATOM 2404 C THR B 16 23.380 12.745 12.499 1.00 40.78 B C ATOM 2405 O THR B 16 23.020 13.467 11.556 1.00 41.40 B O ATOM 2406 N THR B 17 23.627 13.198 13.732 1.00 42.02 B N ATOM 2407 CA THR B 17 23.766 14.616 14.057 1.00 43.39 B C ATOM 2408 CB THR B 17 22.819 14.986 15.206 1.00 42.77 B C ATOM 2409 OG1 THR B 17 23.194 14.299 16.410 1.00 40.33 B O ATOM 2410 CG2 THR B 17 21.392 14.597 14.826 1.00 42.32 B C ATOM 2411 C THR B 17 25.237 14.905 14.412 1.00 47.94 B C ATOM 2412 O THR B 17 26.098 14.036 14.216 1.00 53.17 B O ATOM 2413 N THR B 18 25.536 16.119 14.880 1.00 48.55 B N ATOM 2414 CA THR B 18 26.883 16.470 15.372 1.00 47.03 B C ATOM 2415 CB THR B 18 27.715 17.260 14.322 1.00 46.64 B C ATOM 2416 OG1 THR B 18 27.903 16.465 13.143 1.00 47.35 B O ATOM 2417 CG2 THR B 18 29.098 17.635 14.867 1.00 47.20 B C ATOM 2418 C THR B 18 26.781 17.247 16.695 1.00 49.03 B C ATOM 2419 O THR B 18 25.845 18.027 16.910 1.00 45.35 B O ATOM 2420 N GLN B 19 27.735 16.996 17.592 1.00 54.36 B N ATOM 2421 CA GLN B 19 27.790 17.676 18.879 1.00 54.96 B C ATOM 2422 CB GLN B 19 28.436 16.770 19.934 1.00 58.37 B C ATOM 2423 CG GLN B 19 27.996 17.086 21.361 1.00 62.57 B C ATOM 2424 CD GLN B 19 28.459 16.067 22.402 1.00 63.05 B C ATOM 2425 OE1 GLN B 19 27.896 14.971 22.517 1.00 60.83 B O ATOM 2426 NE2 GLN B 19 29.472 16.437 23.185 1.00 62.16 B N ATOM 2427 C GLN B 19 28.597 18.953 18.685 1.00 53.79 B C ATOM 2428 O GLN B 19 29.711 18.899 18.167 1.00 53.84 B O ATOM 2429 N SER B 20 28.016 20.097 19.046 1.00 54.80 B N ATOM 2430 CA SER B 20 28.744 21.381 19.062 1.00 54.29 B C ATOM 2431 CB SER B 20 28.141 22.387 18.081 1.00 53.79 B C ATOM 2432 OG SER B 20 29.021 23.476 17.888 1.00 49.78 B O ATOM 2433 C SER B 20 28.687 21.918 20.481 1.00 53.51 B C ATOM 2434 O SER B 20 27.696 22.552 20.883 1.00 51.94 B O ATOM 2435 N GLY B 21 29.746 21.617 21.235 1.00 52.98 B N ATOM 2436 CA GLY B 21 29.787 21.842 22.675 1.00 53.72 B C ATOM 2437 C GLY B 21 28.455 21.571 23.358 1.00 53.77 B C ATOM 2438 O GLY B 21 28.115 20.417 23.666 1.00 50.85 B O ATOM 2439 N SER B 22 27.690 22.641 23.549 1.00 53.12 B N ATOM 2440 CA SER B 22 26.521 22.621 24.419 1.00 59.41 B C ATOM 2441 CB SER B 22 26.174 24.057 24.820 1.00 59.03 B C ATOM 2442 OG SER B 22 25.106 24.053 25.747 1.00 61.97 B O ATOM 2443 C SER B 22 25.272 21.930 23.824 1.00 61.98 B C ATOM 2444 O SER B 22 24.452 21.348 24.563 1.00 61.14 B O ATOM 2445 N THR B 23 25.134 21.998 22.501 1.00 57.12 B N ATOM 2446 CA THR B 23 23.930 21.532 21.828 1.00 55.19 B C ATOM 2447 CB THR B 23 23.101 22.755 21.366 1.00 52.30 B C ATOM 2448 OG1 THR B 23 21.696 22.470 21.419 1.00 49.29 B O ATOM 2449 CG2 THR B 23 23.522 23.221 19.960 1.00 51.82 B C ATOM 2450 C THR B 23 24.344 20.627 20.655 1.00 55.21 B C ATOM 2451 O THR B 23 25.542 20.492 20.358 1.00 54.01 B O ATOM 2452 N TYR B 24 23.365 19.996 20.010 1.00 52.08 B N ATOM 2453 CA TYR B 24 23.622 19.217 18.798 1.00 50.27 B C ATOM 2454 CB TYR B 24 23.019 17.812 18.884 1.00 52.10 B C ATOM 2455 CG TYR B 24 23.470 16.931 20.029 1.00 51.06 B C ATOM 2456 CD1 TYR B 24 24.563 16.095 19.888 1.00 49.59 B C ATOM 2457 CE1 TYR B 24 24.967 15.278 20.923 1.00 52.70 B C ATOM 2458 CZ TYR B 24 24.268 15.276 22.121 1.00 52.07 B C ATOM 2459 OH TYR B 24 24.689 14.454 23.153 1.00 52.35 B O ATOM 2460 CE2 TYR B 24 23.160 16.085 22.277 1.00 50.76 B C ATOM 2461 CD2 TYR B 24 22.764 16.903 21.235 1.00 50.70 B C ATOM 2462 C TYR B 24 22.990 19.902 17.600 1.00 50.42 B C ATOM 2463 O TYR B 24 21.978 20.595 17.725 1.00 50.73 B O ATOM 2464 N GLN B 25 23.547 19.640 16.425 1.00 49.79 B N ATOM 2465 CA GLN B 25 23.089 20.271 15.193 1.00 51.16 B C ATOM 2466 CB GLN B 25 24.083 21.380 14.804 1.00 52.14 B C ATOM 2467 CG GLN B 25 25.550 20.946 14.773 1.00 51.47 B C ATOM 2468 CD GLN B 25 26.509 22.069 14.400 1.00 49.02 B C ATOM 2469 OE1 GLN B 25 26.386 23.186 14.879 1.00 43.29 B O ATOM 2470 NE2 GLN B 25 27.483 21.759 13.549 1.00 49.61 B N ATOM 2471 C GLN B 25 22.919 19.219 14.064 1.00 52.10 B C ATOM 2472 O GLN B 25 23.666 18.240 14.038 1.00 54.65 B O ATOM 2473 N LEU B 26 21.940 19.406 13.158 1.00 49.06 B N ATOM 2474 CA LEU B 26 21.703 18.464 12.035 1.00 45.19 B C ATOM 2475 CB LEU B 26 20.376 18.751 11.315 1.00 46.15 B C ATOM 2476 CG LEU B 26 19.037 18.374 11.951 1.00 45.52 B C ATOM 2477 CD1 LEU B 26 17.937 18.472 10.912 1.00 46.14 B C ATOM 2478 CD2 LEU B 26 19.057 16.972 12.511 1.00 44.30 B C ATOM 2479 C LEU B 26 22.827 18.489 11.006 1.00 44.22 B C ATOM 2480 O LEU B 26 22.671 19.012 9.903 1.00 45.46 B O ATOM 2481 N LYS B 27 23.955 17.902 11.377 1.00 44.24 B N ATOM 2482 CA LYS B 27 25.140 17.854 10.539 1.00 44.91 B C ATOM 2483 CB LYS B 27 26.279 18.702 11.154 1.00 47.98 B C ATOM 2484 CG LYS B 27 26.908 19.739 10.222 1.00 50.64 B C ATOM 2485 CD LYS B 27 28.321 20.163 10.639 1.00 51.72 B C ATOM 2486 CE LYS B 27 28.667 21.578 10.160 1.00 50.07 B C ATOM 2487 NZ LYS B 27 30.130 21.767 9.974 1.00 48.98 B N ATOM 2488 C LYS B 27 25.533 16.389 10.501 1.00 43.09 B C ATOM 2489 O LYS B 27 25.380 15.676 11.500 1.00 42.47 B O ATOM 2490 N ASP B 28 26.028 15.939 9.357 1.00 40.93 B N ATOM 2491 CA ASP B 28 26.461 14.555 9.190 1.00 40.17 B C ATOM 2492 CB ASP B 28 25.400 13.747 8.407 1.00 40.04 B C ATOM 2493 CG ASP B 28 25.757 12.248 8.223 1.00 39.03 B C ATOM 2494 OD1 ASP B 28 26.943 11.879 7.999 1.00 39.21 B O ATOM 2495 OD2 ASP B 28 24.807 11.438 8.258 1.00 34.92 B O ATOM 2496 C ASP B 28 27.793 14.620 8.472 1.00 39.30 B C ATOM 2497 O ASP B 28 27.863 14.812 7.260 1.00 37.02 B O ATOM 2498 N THR B 29 28.863 14.460 9.234 1.00 41.34 B N ATOM 2499 CA THR B 29 30.206 14.595 8.673 1.00 42.38 B C ATOM 2500 CB THR B 29 31.217 15.019 9.771 1.00 42.14 B C ATOM 2501 OG1 THR B 29 31.801 13.865 10.404 1.00 41.11 B O ATOM 2502 CG2 THR B 29 30.511 15.907 10.837 1.00 41.47 B C ATOM 2503 C THR B 29 30.610 13.293 7.942 1.00 42.90 B C ATOM 2504 O THR B 29 31.536 13.303 7.113 1.00 41.57 B O ATOM 2505 N THR B 30 29.862 12.208 8.209 1.00 42.18 B N ATOM 2506 CA THR B 30 30.243 10.849 7.803 1.00 42.26 B C ATOM 2507 CB THR B 30 29.460 9.772 8.569 1.00 41.59 B C ATOM 2508 OG1 THR B 30 28.125 9.732 8.078 1.00 44.54 B O ATOM 2509 CG2 THR B 30 29.427 10.041 10.071 1.00 41.22 B C ATOM 2510 C THR B 30 30.012 10.576 6.324 1.00 43.07 B C ATOM 2511 O THR B 30 30.569 9.628 5.790 1.00 43.49 B O ATOM 2512 N ARG B 31 29.170 11.381 5.676 1.00 43.41 B N ATOM 2513 CA ARG B 31 28.950 11.270 4.234 1.00 42.73 B C ATOM 2514 CB ARG B 31 27.457 11.104 3.947 1.00 41.54 B C ATOM 2515 CG ARG B 31 26.880 9.779 4.412 1.00 40.12 B C ATOM 2516 CD ARG B 31 25.358 9.694 4.271 1.00 40.81 B C ATOM 2517 NE ARG B 31 24.850 8.404 4.746 1.00 39.64 B N ATOM 2518 CZ ARG B 31 24.620 8.104 6.025 1.00 37.51 B C ATOM 2519 NH1 ARG B 31 24.818 9.001 6.977 1.00 40.18 B N ATOM 2520 NH2 ARG B 31 24.184 6.906 6.361 1.00 34.41 B N ATOM 2521 C ARG B 31 29.492 12.510 3.521 1.00 42.99 B C ATOM 2522 O ARG B 31 29.076 13.639 3.813 1.00 41.18 B O ATOM 2523 N GLY B 32 30.421 12.288 2.595 1.00 44.05 B N ATOM 2524 CA GLY B 32 31.026 13.364 1.795 1.00 47.95 B C ATOM 2525 C GLY B 32 31.677 14.463 2.618 1.00 49.75 B C ATOM 2526 O GLY B 32 32.181 14.216 3.717 1.00 52.02 B O ATOM 2527 N GLN B 33 31.633 15.689 2.101 1.00 49.78 B N ATOM 2528 CA GLN B 33 32.066 16.860 2.865 1.00 48.09 B C ATOM 2529 CB GLN B 33 32.511 17.987 1.926 1.00 49.40 B C ATOM 2530 CG GLN B 33 33.652 17.599 0.979 1.00 51.77 B C ATOM 2531 CD GLN B 33 33.573 18.279 0.391 1.00 52.73 B C ATOM 2532 OE1 GLN B 33 33.197 19.442 0.508 1.00 50.83 B O ATOM 2533 NE2 GLN B 33 33.944 17.546 1.436 1.00 56.68 B N ATOM 2534 C GLN B 33 30.966 17.360 3.803 1.00 45.74 B C ATOM 2535 O GLN B 33 31.055 18.473 4.292 1.00 48.18 B O ATOM 2536 N GLY B 34 29.933 16.551 4.048 1.00 44.06 B N ATOM 2537 CA GLY B 34 28.862 16.901 4.998 1.00 40.43 B C ATOM 2538 C GLY B 34 27.446 16.828 4.428 1.00 37.82 B C ATOM 2539 O GLY B 34 27.265 16.890 3.210 1.00 35.60 B O ATOM 2540 N ILE B 35 26.453 16.679 5.320 1.00 34.43 B N ATOM 2541 CA ILE B 35 25.030 16.796 4.984 1.00 33.25 B C ATOM 2542 CB ILE B 35 24.312 15.420 4.930 1.00 37.23 B C ATOM 2543 CG1 ILE B 35 24.686 14.664 3.653 1.00 38.63 B C ATOM 2544 CD1 ILE B 35 24.189 13.226 3.623 1.00 39.64 B C ATOM 2545 CG2 ILE B 35 22.779 15.561 4.974 1.00 37.29 B C ATOM 2546 C ILE B 35 24.372 17.650 6.052 1.00 31.28 B C ATOM 2547 O ILE B 35 24.379 17.291 7.239 1.00 29.76 B O ATOM 2548 N VAL B 36 23.779 18.768 5.629 1.00 30.21 B N ATOM 2549 CA VAL B 36 23.278 19.763 6.577 1.00 29.18 B C ATOM 2550 CB VAL B 36 24.183 21.024 6.652 1.00 29.87 B C ATOM 2551 CG1 VAL B 36 24.401 21.390 8.107 1.00 31.50 B C ATOM 2552 CG2 VAL B 36 25.537 20.825 5.979 1.00 29.38 B C ATOM 2553 C VAL B 36 21.869 20.237 6.267 1.00 27.11 B C ATOM 2554 O VAL B 36 21.508 20.504 5.123 1.00 26.29 B O ATOM 2555 N THR B 37 21.101 20.409 7.319 1.00 26.36 B N ATOM 2556 CA THR B 37 19.716 20.767 7.182 1.00 27.97 B C ATOM 2557 CB THR B 37 18.851 19.545 7.550 1.00 29.05 B C ATOM 2558 OG1 THR B 37 19.158 18.474 6.637 1.00 30.25 B O ATOM 2559 CG2 THR B 37 17.335 19.865 7.538 1.00 28.48 B C ATOM 2560 C THR B 37 19.367 22.015 8.026 1.00 28.89 B C ATOM 2561 O THR B 37 19.527 22.015 9.258 1.00 26.39 B O ATOM 2562 N TYR B 38 18.894 23.055 7.321 1.00 30.58 B N ATOM 2563 CA TYR B 38 18.515 24.352 7.890 1.00 33.15 B C ATOM 2564 CB TYR B 38 19.122 25.498 7.067 1.00 33.68 B C ATOM 2565 CG TYR B 38 20.602 25.408 6.810 1.00 34.72 B C ATOM 2566 CD1 TYR B 38 21.101 24.645 5.751 1.00 33.58 B C ATOM 2567 CE1 TYR B 38 22.459 24.560 5.503 1.00 33.35 B C ATOM 2568 CZ TYR B 38 23.338 25.250 6.307 1.00 33.94 B C ATOM 2569 OH TYR B 38 24.675 25.190 6.053 1.00 32.94 B O ATOM 2570 CE2 TYR B 38 22.875 26.007 7.369 1.00 36.31 B C ATOM 2571 CD2 TYR B 38 21.509 26.091 7.610 1.00 36.06 B C ATOM 2572 C TYR B 38 17.006 24.557 7.858 1.00 33.86 B C ATOM 2573 O TYR B 38 16.284 23.768 7.244 1.00 35.29 B O ATOM 2574 N SER B 39 16.555 25.648 8.483 1.00 32.45 B N ATOM 2575 CA SER B 39 15.151 26.094 8.447 1.00 31.81 B C ATOM 2576 CB SER B 39 14.480 25.943 9.826 1.00 30.22 B C ATOM 2577 OG SER B 39 13.271 26.688 9.939 1.00 28.69 B O ATOM 2578 C SER B 39 15.130 27.560 8.023 1.00 32.86 B C ATOM 2579 O SER B 39 15.972 28.338 8.481 1.00 32.92 B O ATOM 2580 N ALA B 40 14.171 27.940 7.169 1.00 31.62 B N ATOM 2581 CA ALA B 40 14.112 29.305 6.650 1.00 30.64 B C ATOM 2582 CB ALA B 40 13.763 29.298 5.174 1.00 29.75 B C ATOM 2583 C ALA B 40 13.130 30.173 7.436 1.00 31.48 B C ATOM 2584 O ALA B 40 12.928 31.349 7.097 1.00 29.96 B O ATOM 2585 N GLY B 41 12.535 29.603 8.487 1.00 31.27 B N ATOM 2586 CA GLY B 41 11.567 30.329 9.308 1.00 32.58 B C ATOM 2587 C GLY B 41 10.464 30.911 8.448 1.00 34.88 B C ATOM 2588 O GLY B 41 10.005 32.016 8.681 1.00 41.21 B O ATOM 2589 N ASN B 42 10.055 30.164 7.432 1.00 35.41 B N ATOM 2590 CA ASN B 42 8.963 30.556 6.542 1.00 35.57 B C ATOM 2591 CB ASN B 42 7.626 30.565 7.290 1.00 35.12 B C ATOM 2592 CG ASN B 42 7.341 29.234 7.988 1.00 35.46 B C ATOM 2593 OD1 ASN B 42 6.975 29.225 9.143 1.00 37.01 B O ATOM 2594 ND2 ASN B 42 7.508 28.109 7.281 1.00 35.13 B N ATOM 2595 C ASN B 42 9.235 31.851 5.820 1.00 35.04 B C ATOM 2596 O ASN B 42 8.323 32.620 5.567 1.00 31.81 B O ATOM 2597 N ARG B 43 10.501 32.017 5.426 1.00 39.05 B N ATOM 2598 CA ARG B 43 11.015 33.222 4.776 1.00 43.00 B C ATOM 2599 CB ARG B 43 11.892 33.984 5.775 1.00 48.73 B C ATOM 2600 CG ARG B 43 11.097 34.876 6.718 1.00 53.88 B C ATOM 2601 CD ARG B 43 10.656 36.140 6.001 1.00 59.88 B C ATOM 2602 NE ARG B 43 10.497 37.266 6.925 1.00 71.15 B N ATOM 2603 CZ ARG B 43 11.497 37.925 7.523 1.00 72.97 B C ATOM 2604 NH1 ARG B 43 12.772 37.577 7.324 1.00 70.94 B N ATOM 2605 NH2 ARG B 43 11.216 38.937 8.346 1.00 74.66 B N ATOM 2606 C ARG B 43 11.806 32.894 3.521 1.00 40.05 B C ATOM 2607 O ARG B 43 11.901 31.731 3.132 1.00 42.57 B O ATOM 2608 N SER B 44 12.381 33.915 2.894 1.00 38.32 B N ATOM 2609 CA SER B 44 12.999 33.759 1.574 1.00 39.47 B C ATOM 2610 CB SER B 44 12.712 34.982 0.695 1.00 40.23 B C ATOM 2611 OG SER B 44 11.445 34.869 0.078 1.00 42.89 B O ATOM 2612 C SER B 44 14.501 33.503 1.554 1.00 37.25 B C ATOM 2613 O SER B 44 15.006 32.835 0.655 1.00 36.44 B O ATOM 2614 N SER B 45 15.244 34.065 2.486 1.00 36.28 B N ATOM 2615 CA SER B 45 16.688 34.005 2.324 1.00 36.90 B C ATOM 2616 CB SER B 45 17.413 35.089 3.144 1.00 36.36 B C ATOM 2617 OG SER B 45 17.285 34.843 4.525 1.00 36.97 B O ATOM 2618 C SER B 45 17.190 32.595 2.645 1.00 36.54 B C ATOM 2619 O SER B 45 16.577 31.857 3.420 1.00 33.48 B O ATOM 2620 N LEU B 46 18.304 32.246 2.012 1.00 37.13 B N ATOM 2621 CA LEU B 46 18.929 30.944 2.147 1.00 39.27 B C ATOM 2622 CB LEU B 46 18.853 30.188 0.811 1.00 38.08 B C ATOM 2623 CG LEU B 46 17.468 30.074 0.156 1.00 36.84 B C ATOM 2624 CD1 LEU B 46 17.606 29.703 1.326 1.00 35.76 B C ATOM 2625 CD2 LEU B 46 16.578 29.092 0.925 1.00 35.95 B C ATOM 2626 C LEU B 46 20.399 31.131 2.546 1.00 41.41 B C ATOM 2627 O LEU B 46 20.968 32.200 2.316 1.00 44.36 B O ATOM 2628 N PRO B 47 21.020 30.093 3.130 1.00 39.28 B N ATOM 2629 CA PRO B 47 20.411 28.820 3.520 1.00 37.84 B C ATOM 2630 CB PRO B 47 21.611 28.006 4.011 1.00 40.67 B C ATOM 2631 CG PRO B 47 22.644 29.037 4.374 1.00 40.15 B C ATOM 2632 CD PRO B 47 22.479 30.061 3.306 1.00 38.74 B C ATOM 2633 C PRO B 47 19.403 28.941 4.649 1.00 35.08 B C ATOM 2634 O PRO B 47 18.610 28.044 4.831 1.00 32.64 B O ATOM 2635 N GLY B 48 19.438 30.045 5.390 1.00 33.92 B N ATOM 2636 CA GLY B 48 18.651 30.180 6.603 1.00 32.39 B C ATOM 2637 C GLY B 48 19.466 29.671 7.770 1.00 33.27 B C ATOM 2638 O GLY B 48 20.677 29.476 7.644 1.00 33.45 B O ATOM 2639 N THR B 49 18.790 29.432 8.892 1.00 34.94 B N ATOM 2640 CA THR B 49 19.414 28.958 10.130 1.00 38.98 B C ATOM 2641 CB THR B 49 18.513 29.273 11.339 1.00 39.73 B C ATOM 2642 OG1 THR B 49 18.099 30.641 11.273 1.00 40.95 B O ATOM 2643 CG2 THR B 49 19.242 29.015 12.663 1.00 39.97 B C ATOM 2644 C THR B 49 19.720 27.444 10.184 1.00 42.89 B C ATOM 2645 O THR B 49 18.880 26.602 9.868 1.00 40.45 B O ATOM 2646 N LEU B 50 20.933 27.114 10.623 1.00 48.49 B N ATOM 2647 CA LEU B 50 21.292 25.732 10.920 1.00 48.73 B C ATOM 2648 CB LEU B 50 22.795 25.610 11.146 1.00 49.85 B C ATOM 2649 CG LEU B 50 23.368 24.241 11.494 1.00 51.48 B C ATOM 2650 CD1 LEU B 50 22.680 23.122 10.722 1.00 52.59 B C ATOM 2651 CD2 LEU B 50 24.875 24.227 11.229 1.00 52.22 B C ATOM 2652 C LEU B 50 20.518 25.298 12.157 1.00 47.59 B C ATOM 2653 O LEU B 50 20.480 26.016 13.158 1.00 49.60 B O ATOM 2654 N LEU B 51 19.877 24.138 12.057 1.00 46.71 B N ATOM 2655 CA LEU B 51 18.968 23.635 13.080 1.00 43.84 B C ATOM 2656 CB LEU B 51 17.950 22.670 12.451 1.00 45.70 B C ATOM 2657 CG LEU B 51 16.529 23.222 12.293 1.00 46.99 B C ATOM 2658 CD1 LEU B 51 15.996 22.783 10.946 1.00 47.24 B C ATOM 2659 CD2 LEU B 51 15.613 22.792 13.454 1.00 46.81 B C ATOM 2660 C LEU B 51 19.690 22.965 14.244 1.00 41.22 B C ATOM 2661 O LEU B 51 20.753 22.352 14.083 1.00 37.73 B O ATOM 2662 N THR B 52 19.043 23.038 15.403 1.00 40.19 B N ATOM 2663 CA THR B 52 19.694 22.874 16.699 1.00 38.68 B C ATOM 2664 CB THR B 52 20.030 24.303 17.224 1.00 37.51 B C ATOM 2665 OG1 THR B 52 21.182 24.776 16.532 1.00 34.76 B O ATOM 2666 CG2 THR B 52 20.290 24.379 18.732 1.00 37.73 B C ATOM 2667 C THR B 52 18.788 22.103 17.672 1.00 37.74 B C ATOM 2668 O THR B 52 17.577 22.245 17.639 1.00 39.97 B O ATOM 2669 N SER B 53 19.371 21.279 18.529 1.00 39.22 B N ATOM 2670 CA SER B 53 18.636 20.722 19.673 1.00 41.33 B C ATOM 2671 CB SER B 53 17.766 19.518 19.263 1.00 40.16 B C ATOM 2672 OG SER B 53 17.139 18.905 20.382 1.00 37.49 B O ATOM 2673 C SER B 53 19.643 20.307 20.739 1.00 45.00 B C ATOM 2674 O SER B 53 20.589 19.556 20.450 1.00 46.25 B O ATOM 2675 N SER B 54 19.461 20.823 21.955 1.00 46.91 B N ATOM 2676 CA SER B 54 20.263 20.398 23.104 1.00 47.89 B C ATOM 2677 CB SER B 54 20.046 21.350 24.292 1.00 47.12 B C ATOM 2678 OG SER B 54 18.666 21.531 24.586 1.00 46.27 B O ATOM 2679 C SER B 54 19.953 18.928 23.478 1.00 48.96 B C ATOM 2680 O SER B 54 20.833 18.202 23.926 1.00 49.21 B O ATOM 2681 N SER B 55 18.718 18.493 23.219 1.00 47.87 B N ATOM 2682 CA SER B 55 18.222 17.161 23.587 1.00 44.68 B C ATOM 2683 CB SER B 55 16.685 17.209 23.560 1.00 44.59 B C ATOM 2684 OG SER B 55 16.106 16.112 24.240 1.00 44.52 B O ATOM 2685 C SER B 55 18.707 15.986 22.695 1.00 44.27 B C ATOM 2686 O SER B 55 18.553 14.809 23.068 1.00 44.09 B O ATOM 2687 N ASN B 56 19.279 16.300 21.526 1.00 42.16 B N ATOM 2688 CA ASN B 56 19.411 15.344 20.385 1.00 38.46 B C ATOM 2689 CB ASN B 56 20.558 14.340 20.601 1.00 35.65 B C ATOM 2690 CG ASN B 56 21.226 13.902 19.290 1.00 34.01 B C ATOM 2691 OD1 ASN B 56 21.996 12.952 19.283 1.00 36.17 B O ATOM 2692 ND2 ASN B 56 20.947 14.590 18.194 1.00 30.20 B N ATOM 2693 C ASN B 56 18.101 14.601 19.985 1.00 38.13 B C ATOM 2694 O ASN B 56 18.137 13.659 19.202 1.00 35.54 B O ATOM 2695 N ILE B 57 16.967 15.032 20.536 1.00 38.44 B N ATOM 2696 CA ILE B 57 15.654 14.668 20.039 1.00 42.11 B C ATOM 2697 CB ILE B 57 14.683 14.350 21.189 1.00 42.20 B C ATOM 2698 CG1 ILE B 57 15.350 13.491 22.273 1.00 44.11 B C ATOM 2699 CD1 ILE B 57 15.809 12.115 21.839 1.00 44.60 B C ATOM 2700 CG2 ILE B 57 13.437 13.665 20.654 1.00 41.76 B C ATOM 2701 C ILE B 57 15.113 15.873 19.234 1.00 46.06 B C ATOM 2702 O ILE B 57 15.270 17.026 19.669 1.00 50.20 B O ATOM 2703 N TRP B 58 14.475 15.607 18.085 1.00 43.11 B N ATOM 2704 CA TRP B 58 14.066 16.648 17.136 1.00 40.89 B C ATOM 2705 CB TRP B 58 14.801 16.457 15.834 1.00 40.59 B C ATOM 2706 CG TRP B 58 16.245 16.402 16.008 1.00 40.53 B C ATOM 2707 CD1 TRP B 58 16.962 15.345 16.414 1.00 40.30 B C ATOM 2708 NE1 TRP B 58 18.288 15.660 16.467 1.00 40.67 B N ATOM 2709 CE2 TRP B 58 18.449 16.960 16.090 1.00 41.82 B C ATOM 2710 CD2 TRP B 58 17.168 17.463 15.793 1.00 43.03 B C ATOM 2711 CE3 TRP B 58 17.038 18.798 15.378 1.00 44.52 B C ATOM 2712 CZ3 TRP B 58 18.194 19.573 15.257 1.00 46.89 B C ATOM 2713 CH2 TRP B 58 19.466 19.033 15.563 1.00 46.00 B C ATOM 2714 CZ2 TRP B 58 19.608 17.734 15.987 1.00 43.73 B C ATOM 2715 C TRP B 58 12.583 16.598 16.838 1.00 43.33 B C ATOM 2716 O TRP B 58 12.073 15.572 16.390 1.00 41.28 B O ATOM 2717 N ASN B 59 11.893 17.720 17.041 1.00 46.24 B N ATOM 2718 CA ASN B 59 10.441 17.752 16.912 1.00 45.70 B C ATOM 2719 CB ASN B 59 9.830 18.319 18.178 1.00 49.90 B C ATOM 2720 CG ASN B 59 9.910 17.334 19.326 1.00 57.71 B C ATOM 2721 OD1 ASN B 59 9.071 16.430 19.449 1.00 61.14 B O ATOM 2722 ND2 ASN B 59 10.934 17.481 20.165 1.00 62.09 B N ATOM 2723 C ASN B 59 9.972 18.509 15.696 1.00 42.04 B C ATOM 2724 O ASN B 59 8.950 19.169 15.726 1.00 45.30 B O ATOM 2725 N ASP B 60 10.707 18.369 14.609 1.00 37.51 B N ATOM 2726 CA ASP B 60 10.363 19.023 13.371 1.00 36.63 B C ATOM 2727 CB ASP B 60 11.337 20.170 13.119 1.00 37.97 B C ATOM 2728 CG ASP B 60 11.017 20.941 11.861 1.00 36.97 B C ATOM 2729 OD1 ASP B 60 9.899 20.784 11.310 1.00 35.18 B O ATOM 2730 OD2 ASP B 60 11.902 21.710 11.429 1.00 37.14 B O ATOM 2731 C ASP B 60 10.381 18.016 12.211 1.00 35.22 B C ATOM 2732 O ASP B 60 11.461 17.568 11.745 1.00 33.57 B O ATOM 2733 N GLY B 61 9.172 17.694 11.746 1.00 31.50 B N ATOM 2734 CA GLY B 61 8.947 16.600 10.815 1.00 29.00 B C ATOM 2735 C GLY B 61 9.628 16.829 9.495 1.00 28.50 B C ATOM 2736 O GLY B 61 10.389 15.978 9.025 1.00 29.45 B O ATOM 2737 N ALA B 62 9.380 17.980 8.886 1.00 27.01 B N ATOM 2738 CA ALA B 62 9.980 18.248 7.581 1.00 26.15 B C ATOM 2739 CB ALA B 62 9.484 19.558 7.008 1.00 27.22 B C ATOM 2740 C ALA B 62 11.494 18.232 7.642 1.00 25.10 B C ATOM 2741 O ALA B 62 12.121 17.707 6.755 1.00 25.58 B O ATOM 2742 N ALA B 63 12.090 18.777 8.695 1.00 25.77 B N ATOM 2743 CA ALA B 63 13.560 18.757 8.810 1.00 27.21 B C ATOM 2744 CB ALA B 63 14.029 19.602 9.989 1.00 27.02 B C ATOM 2745 C ALA B 63 14.118 17.325 8.934 1.00 27.71 B C ATOM 2746 O ALA B 63 15.165 17.007 8.343 1.00 27.87 B O ATOM 2747 N VAL B 64 13.417 16.488 9.712 1.00 26.10 B N ATOM 2748 CA VAL B 64 13.806 15.112 9.932 1.00 24.19 B C ATOM 2749 CB VAL B 64 12.831 14.437 10.882 1.00 24.11 B C ATOM 2750 CG1 VAL B 64 13.003 12.926 10.833 1.00 24.36 B C ATOM 2751 CG2 VAL B 64 13.047 14.965 12.292 1.00 24.69 B C ATOM 2752 C VAL B 64 13.819 14.352 8.619 1.00 24.48 B C ATOM 2753 O VAL B 64 14.837 13.747 8.233 1.00 23.08 B O ATOM 2754 N ASP B 65 12.687 14.386 7.924 1.00 24.36 B N ATOM 2755 CA ASP B 65 12.597 13.691 6.657 1.00 24.27 B C ATOM 2756 CB ASP B 65 11.194 13.785 6.053 1.00 24.29 B C ATOM 2757 CG ASP B 65 10.179 12.899 6.778 1.00 24.48 B C ATOM 2758 OD1 ASP B 65 10.541 11.803 7.209 1.00 23.48 B O ATOM 2759 OD2 ASP B 65 9.004 13.284 6.922 1.00 25.28 B O ATOM 2760 C ASP B 65 13.650 14.266 5.731 1.00 24.81 B C ATOM 2761 O ASP B 65 14.431 13.507 5.130 1.00 24.32 B O ATOM 2762 N ALA B 66 13.720 15.597 5.660 1.00 24.42 B N ATOM 2763 CA ALA B 66 14.745 16.245 4.827 1.00 26.00 B C ATOM 2764 CB ALA B 66 14.748 17.751 5.038 1.00 26.76 B C ATOM 2765 C ALA B 66 16.143 15.693 5.096 1.00 25.63 B C ATOM 2766 O ALA B 66 16.880 15.319 4.181 1.00 22.75 B O ATOM 2767 N HIS B 67 16.480 15.650 6.375 1.00 27.71 B N ATOM 2768 CA HIS B 67 17.789 15.198 6.817 1.00 30.45 B C ATOM 2769 CB HIS B 67 17.945 15.490 8.305 1.00 32.99 B C ATOM 2770 CG HIS B 67 19.353 15.419 8.779 1.00 34.84 B C ATOM 2771 ND1 HIS B 67 20.373 16.117 8.170 1.00 36.52 B N ATOM 2772 CE1 HIS B 67 21.509 15.850 8.785 1.00 37.20 B C ATOM 2773 NE2 HIS B 67 21.257 15.016 9.778 1.00 36.99 B N ATOM 2774 CD2 HIS B 67 19.916 14.729 9.794 1.00 34.94 B C ATOM 2775 C HIS B 67 18.026 13.710 6.536 1.00 29.77 B C ATOM 2776 O HIS B 67 18.971 13.350 5.823 1.00 28.30 B O ATOM 2777 N ALA B 68 17.159 12.853 7.076 1.00 29.76 B N ATOM 2778 CA ALA B 68 17.281 11.398 6.850 1.00 30.76 B C ATOM 2779 CB ALA B 68 16.138 10.632 7.523 1.00 30.67 B C ATOM 2780 C ALA B 68 17.320 11.067 5.362 1.00 29.91 B C ATOM 2781 O ALA B 68 18.336 10.605 4.842 1.00 29.77 B O ATOM 2782 N TYR B 69 16.217 11.347 4.676 1.00 27.97 B N ATOM 2783 CA TYR B 69 16.103 10.975 3.281 1.00 26.15 B C ATOM 2784 CB TYR B 69 14.755 11.400 2.656 1.00 25.06 B C ATOM 2785 CG TYR B 69 13.523 10.767 3.264 1.00 23.20 B C ATOM 2786 CD1 TYR B 69 13.542 9.468 3.784 1.00 22.72 B C ATOM 2787 CE1 TYR B 69 12.406 8.906 4.356 1.00 21.86 B C ATOM 2788 CZ TYR B 69 11.242 9.635 4.396 1.00 21.61 B C ATOM 2789 OH TYR B 69 10.096 9.115 4.939 1.00 20.56 B O ATOM 2790 CE2 TYR B 69 11.214 10.921 3.894 1.00 21.81 B C ATOM 2791 CD2 TYR B 69 12.343 11.472 3.329 1.00 22.03 B C ATOM 2792 C TYR B 69 17.240 11.529 2.460 1.00 25.31 B C ATOM 2793 O TYR B 69 17.527 11.003 1.400 1.00 25.46 B O ATOM 2794 N THR B 70 17.899 12.582 2.916 1.00 27.08 B N ATOM 2795 CA THR B 70 19.056 13.065 2.145 1.00 28.79 B C ATOM 2796 CB THR B 70 19.421 14.549 2.426 1.00 29.13 B C ATOM 2797 OG1 THR B 70 18.350 15.412 2.011 1.00 28.17 B O ATOM 2798 CG2 THR B 70 20.666 14.947 1.640 1.00 30.19 B C ATOM 2799 C THR B 70 20.236 12.077 2.332 1.00 28.56 B C ATOM 2800 O THR B 70 20.896 11.713 1.345 1.00 26.58 B O ATOM 2801 N ALA B 71 20.457 11.607 3.569 1.00 28.13 B N ATOM 2802 CA ALA B 71 21.405 10.506 3.805 1.00 27.78 B C ATOM 2803 CB ALA B 71 21.412 10.101 5.261 1.00 26.69 B C ATOM 2804 C ALA B 71 21.075 9.293 2.922 1.00 28.42 B C ATOM 2805 O ALA B 71 21.969 8.680 2.317 1.00 27.67 B O ATOM 2806 N LYS B 72 19.789 8.964 2.840 1.00 29.66 B N ATOM 2807 CA LYS B 72 19.346 7.772 2.133 1.00 31.07 B C ATOM 2808 CB LYS B 72 17.842 7.590 2.277 1.00 32.79 B C ATOM 2809 CG LYS B 72 17.258 6.408 1.512 1.00 35.11 B C ATOM 2810 CD LYS B 72 15.747 6.289 1.716 1.00 36.65 B C ATOM 2811 CE LYS B 72 15.242 4.933 1.257 1.00 38.51 B C ATOM 2812 NZ LYS B 72 13.761 4.866 1.344 1.00 40.21 B N ATOM 2813 C LYS B 72 19.717 7.872 0.677 1.00 32.30 B C ATOM 2814 O LYS B 72 20.162 6.889 0.079 1.00 35.50 B O ATOM 2815 N VAL B 73 19.546 9.066 0.112 1.00 32.14 B N ATOM 2816 CA VAL B 73 19.814 9.304 1.320 1.00 30.81 B C ATOM 2817 CB VAL B 73 19.131 10.611 1.824 1.00 29.58 B C ATOM 2818 CG1 VAL B 73 19.415 10.861 3.297 1.00 27.79 B C ATOM 2819 CG2 VAL B 73 17.620 10.558 1.574 1.00 30.18 B C ATOM 2820 C VAL B 73 21.312 9.362 1.576 1.00 30.15 B C ATOM 2821 O VAL B 73 21.756 9.011 2.646 1.00 28.69 B O ATOM 2822 N TYR B 74 22.075 9.825 0.587 1.00 32.57 B N ATOM 2823 CA TYR B 74 23.525 9.800 0.654 1.00 34.78 B C ATOM 2824 CB TYR B 74 24.141 10.527 0.543 1.00 38.44 B C ATOM 2825 CG TYR B 74 25.653 10.515 0.518 1.00 42.42 B C ATOM 2826 CD1 TYR B 74 26.367 9.478 1.108 1.00 45.08 B C ATOM 2827 CE1 TYR B 74 27.747 9.452 1.072 1.00 46.85 B C ATOM 2828 CZ TYR B 74 28.423 10.461 0.432 1.00 46.58 B C ATOM 2829 OH TYR B 74 29.792 10.430 0.400 1.00 48.77 B O ATOM 2830 CE2 TYR B 74 27.740 11.498 0.165 1.00 44.52 B C ATOM 2831 CD2 TYR B 74 26.363 11.521 0.118 1.00 42.52 B C ATOM 2832 C TYR B 74 23.990 8.348 0.685 1.00 34.57 B C ATOM 2833 O TYR B 74 24.756 7.962 1.585 1.00 34.24 B O ATOM 2834 N ASP B 75 23.517 7.558 0.289 1.00 32.83 B N ATOM 2835 CA ASP B 75 23.765 6.110 0.313 1.00 32.00 B C ATOM 2836 CB ASP B 75 22.966 5.400 1.423 1.00 30.80 B C ATOM 2837 CG ASP B 75 23.468 5.736 2.823 1.00 29.68 B C ATOM 2838 OD1 ASP B 75 24.558 6.343 2.956 1.00 26.51 B O ATOM 2839 OD2 ASP B 75 22.742 5.406 3.791 1.00 27.80 B O ATOM 2840 C ASP B 75 23.456 5.451 1.030 1.00 32.02 B C ATOM 2841 O ASP B 75 24.321 4.795 1.602 1.00 34.17 B O ATOM 2842 N TYR B 76 22.241 5.632 1.540 1.00 31.51 B N ATOM 2843 CA TYR B 76 21.849 5.008 2.805 1.00 30.68 B C ATOM 2844 CB TYR B 76 20.422 5.408 3.183 1.00 31.50 B C ATOM 2845 CG TYR B 76 19.954 4.945 4.549 1.00 32.80 B C ATOM 2846 CD1 TYR B 76 20.312 5.644 5.677 1.00 33.28 B C ATOM 2847 CE1 TYR B 76 19.893 5.247 6.928 1.00 33.91 B C ATOM 2848 CZ TYR B 76 19.094 4.147 7.077 1.00 34.08 B C ATOM 2849 OH TYR B 76 18.735 3.832 8.366 1.00 36.34 B O ATOM 2850 CE2 TYR B 76 18.696 3.416 5.974 1.00 33.35 B C ATOM 2851 CD2 TYR B 76 19.119 3.825 4.710 1.00 34.22 B C ATOM 2852 C TYR B 76 22.847 5.352 3.904 1.00 31.30 B C ATOM 2853 O TYR B 76 23.356 4.456 4.550 1.00 33.09 B O ATOM 2854 N TYR B 77 23.154 6.633 4.100 1.00 31.67 B N ATOM 2855 CA TYR B 77 24.106 7.030 5.143 1.00 33.09 B C ATOM 2856 CB TYR B 77 24.288 8.571 5.236 1.00 34.51 B C ATOM 2857 CG TYR B 77 23.373 9.296 6.237 1.00 32.63 B C ATOM 2858 CD1 TYR B 77 22.119 9.767 5.856 1.00 32.93 B C ATOM 2859 CE1 TYR B 77 21.279 10.412 6.756 1.00 32.14 B C ATOM 2860 CZ TYR B 77 21.695 10.624 8.049 1.00 32.06 B C ATOM 2861 OH TYR B 77 20.861 11.295 8.923 1.00 32.13 B O ATOM 2862 CE2 TYR B 77 22.936 10.168 8.450 1.00 31.38 B C ATOM 2863 CD2 TYR B 77 23.766 9.512 7.544 1.00 31.01 B C ATOM 2864 C TYR B 77 25.460 6.358 4.924 1.00 33.60 B C ATOM 2865 O TYR B 77 26.025 5.791 5.864 1.00 31.95 B O ATOM 2866 N LYS B 78 25.968 6.428 3.693 1.00 35.21 B N ATOM 2867 CA LYS B 78 27.226 5.743 3.305 1.00 38.16 B C ATOM 2868 CB LYS B 78 27.499 5.943 1.798 1.00 41.05 B C ATOM 2869 CG LYS B 78 28.442 4.930 1.143 1.00 44.48 B C ATOM 2870 CD LYS B 78 29.548 5.574 0.305 1.00 46.27 B C ATOM 2871 CE LYS B 78 30.629 6.155 1.224 1.00 49.31 B C ATOM 2872 NZ LYS B 78 31.826 6.666 0.496 1.00 50.68 B N ATOM 2873 C LYS B 78 27.214 4.242 3.666 1.00 38.50 B C ATOM 2874 O LYS B 78 28.116 3.739 4.348 1.00 37.83 B O ATOM 2875 N ASN B 79 26.163 3.552 3.237 1.00 36.81 B N ATOM 2876 CA ASN B 79 26.072 2.119 3.390 1.00 35.01 B C ATOM 2877 CB ASN B 79 25.037 1.568 2.428 1.00 34.32 B C ATOM 2878 CG ASN B 79 25.446 1.750 0.968 1.00 34.68 B C ATOM 2879 OD1 ASN B 79 26.640 1.847 0.631 1.00 31.67 B O ATOM 2880 ND2 ASN B 79 24.451 1.805 0.090 1.00 35.09 B N ATOM 2881 C ASN B 79 25.783 1.659 4.800 1.00 36.29 B C ATOM 2882 O ASN B 79 26.446 0.757 5.290 1.00 36.69 B O ATOM 2883 N LYS B 80 24.821 2.271 5.472 1.00 39.00 B N ATOM 2884 CA LYS B 80 24.394 1.768 6.782 1.00 41.10 B C ATOM 2885 CB LYS B 80 22.927 2.094 7.036 1.00 45.28 B C ATOM 2886 CG LYS B 80 21.982 1.547 5.982 1.00 51.45 B C ATOM 2887 CD LYS B 80 21.444 0.164 6.329 1.00 56.78 B C ATOM 2888 CE LYS B 80 20.650 0.395 5.153 1.00 60.79 B C ATOM 2889 NZ LYS B 80 21.524 0.661 3.966 1.00 62.58 B N ATOM 2890 C LYS B 80 25.202 2.277 7.965 1.00 41.13 B C ATOM 2891 O LYS B 80 25.033 1.754 9.072 1.00 40.54 B O ATOM 2892 N PHE B 81 26.046 3.296 7.764 1.00 40.60 B N ATOM 2893 CA PHE B 81 26.746 3.941 8.892 1.00 40.39 B C ATOM 2894 CB PHE B 81 26.047 5.257 9.274 1.00 42.38 B C ATOM 2895 CG PHE B 81 24.628 5.111 9.754 1.00 43.89 B C ATOM 2896 CD1 PHE B 81 24.300 4.227 10.770 1.00 45.90 B C ATOM 2897 CE1 PHE B 81 22.990 4.112 11.214 1.00 47.25 B C ATOM 2898 CZ PHE B 81 22.000 4.911 10.664 1.00 47.90 B C ATOM 2899 CE2 PHE B 81 22.319 5.821 9.672 1.00 46.56 B C ATOM 2900 CD2 PHE B 81 23.626 5.921 9.226 1.00 45.90 B C ATOM 2901 C PHE B 81 28.217 4.290 8.659 1.00 40.16 B C ATOM 2902 O PHE B 81 28.880 4.759 9.574 1.00 39.11 B O ATOM 2903 N GLY B 82 28.720 4.127 7.443 1.00 40.78 B N ATOM 2904 CA GLY B 82 30.054 4.617 7.106 1.00 42.16 B C ATOM 2905 C GLY B 82 30.193 6.135 7.065 1.00 44.48 B C ATOM 2906 O GLY B 82 31.308 6.662 7.002 1.00 46.91 B O ATOM 2907 N ARG B 83 29.071 6.853 7.065 1.00 44.64 B N ATOM 2908 CA ARG B 83 29.108 8.311 7.112 1.00 42.54 B C ATOM 2909 CB ARG B 83 27.970 8.851 7.980 1.00 43.50 B C ATOM 2910 CG ARG B 83 27.861 10.374 7.915 1.00 44.21 B C ATOM 2911 CD ARG B 83 26.887 10.972 8.920 1.00 42.64 B C ATOM 2912 NE ARG B 83 27.330 12.309 9.284 1.00 41.71 B N ATOM 2913 CZ ARG B 83 28.056 12.605 10.359 1.00 41.59 B C ATOM 2914 NH1 ARG B 83 28.397 11.672 11.239 1.00 38.71 B N ATOM 2915 NH2 ARG B 83 28.427 13.862 10.570 1.00 44.02 B N ATOM 2916 C ARG B 83 29.078 8.955 5.722 1.00 39.03 B C ATOM 2917 O ARG B 83 28.308 8.560 4.851 1.00 36.63 B O ATOM 2918 N ASN B 84 29.910 9.979 5.559 1.00 37.19 B N ATOM 2919 CA ASN B 84 30.100 10.669 4.277 1.00 35.57 B C ATOM 2920 CB ASN B 84 31.602 10.752 3.969 1.00 32.60 B C ATOM 2921 CG ASN B 84 31.912 11.200 2.559 1.00 30.63 B C ATOM 2922 OD1 ASN B 84 33.073 11.419 2.241 1.00 30.00 B O ATOM 2923 ND2 ASN B 84 30.903 11.321 1.709 1.00 29.72 B N ATOM 2924 C ASN B 84 29.493 12.069 4.355 1.00 35.30 B C ATOM 2925 O ASN B 84 30.018 12.925 5.050 1.00 35.02 B O ATOM 2926 N SER B 85 28.379 12.275 3.648 1.00 37.34 B N ATOM 2927 CA SER B 85 27.523 13.490 3.757 1.00 37.67 B C ATOM 2928 CB SER B 85 28.072 14.642 2.910 1.00 37.87 B C ATOM 2929 OG SER B 85 27.019 15.470 2.452 1.00 36.06 B O ATOM 2930 C SER B 85 27.271 13.918 5.209 1.00 36.47 B C ATOM 2931 O SER B 85 27.404 13.093 6.117 1.00 38.17 B O ATOM 2932 N ILE B 86 26.911 15.177 5.445 1.00 35.78 B N ATOM 2933 CA ILE B 86 26.422 15.556 6.788 1.00 38.90 B C ATOM 2934 CB ILE B 86 25.482 16.789 6.767 1.00 40.34 B C ATOM 2935 CG1 ILE B 86 26.280 18.073 6.741 1.00 43.61 B C ATOM 2936 CD1 ILE B 86 25.397 19.286 6.631 1.00 47.20 B C ATOM 2937 CG2 ILE B 86 24.540 16.770 5.564 1.00 40.32 B C ATOM 2938 C ILE B 86 27.543 15.744 7.829 1.00 38.42 B C ATOM 2939 O ILE B 86 27.374 15.397 8.994 1.00 36.18 B O ATOM 2940 N ASP B 87 28.672 16.290 7.387 1.00 41.14 B N ATOM 2941 CA ASP B 87 29.843 16.563 8.233 1.00 41.69 B C ATOM 2942 CB ASP B 87 30.586 17.806 7.714 1.00 41.60 B C ATOM 2943 CG ASP B 87 31.249 17.572 6.344 1.00 41.11 B C ATOM 2944 OD1 ASP B 87 30.790 16.683 5.603 1.00 38.26 B O ATOM 2945 OD2 ASP B 87 32.205 18.286 5.983 1.00 40.33 B O ATOM 2946 C ASP B 87 30.862 15.420 8.293 1.00 43.82 B C ATOM 2947 O ASP B 87 31.952 15.624 8.833 1.00 45.59 B O ATOM 2948 N GLY B 88 30.554 14.254 7.714 1.00 42.79 B N ATOM 2949 CA GLY B 88 31.467 13.107 7.774 1.00 42.83 B C ATOM 2950 C GLY B 88 32.580 13.102 6.734 1.00 43.95 B C ATOM 2951 O GLY B 88 33.034 12.041 6.334 1.00 41.75 B O ATOM 2952 N ASN B 89 33.061 14.284 6.346 1.00 49.48 B N ATOM 2953 CA ASN B 89 33.806 14.473 5.085 1.00 52.34 B C ATOM 2954 CB ASN B 89 34.804 15.628 5.189 1.00 56.66 B C ATOM 2955 CG ASN B 89 35.843 15.406 6.287 1.00 62.28 B C ATOM 2956 OD1 ASN B 89 35.693 14.522 7.145 1.00 63.04 B O ATOM 2957 ND2 ASN B 89 36.909 16.202 6.259 1.00 63.74 B N ATOM 2958 C ASN B 89 32.735 14.793 4.086 1.00 49.08 B C ATOM 2959 O ASN B 89 31.630 15.116 4.486 1.00 57.39 B O ATOM 2960 N GLY B 90 33.003 14.724 2.798 1.00 44.73 B N ATOM 2961 CA GLY B 90 31.880 14.648 1.838 1.00 42.09 B C ATOM 2962 C GLY B 90 31.136 15.934 1.533 1.00 40.51 B C ATOM 2963 O GLY B 90 30.983 16.274 0.367 1.00 38.47 B O ATOM 2964 N PHE B 91 30.654 16.623 2.577 1.00 40.34 B N ATOM 2965 CA PHE B 91 30.044 17.961 2.471 1.00 41.32 B C ATOM 2966 CB PHE B 91 29.339 18.344 3.801 1.00 45.43 B C ATOM 2967 CG PHE B 91 28.680 19.715 3.800 1.00 49.29 B C ATOM 2968 CD1 PHE B 91 29.447 20.880 3.899 1.00 48.89 B C ATOM 2969 CE1 PHE B 91 28.837 22.121 3.886 1.00 50.44 B C ATOM 2970 CZ PHE B 91 27.450 22.219 3.792 1.00 49.76 B C ATOM 2971 CE2 PHE B 91 26.679 21.081 3.708 1.00 47.44 B C ATOM 2972 CD2 PHE B 91 27.288 19.837 3.719 1.00 49.23 B C ATOM 2973 C PHE B 91 29.071 18.048 1.308 1.00 38.84 B C ATOM 2974 O PHE B 91 28.177 17.219 1.185 1.00 41.42 B O ATOM 2975 N GLN B 92 29.259 19.038 0.440 1.00 38.23 B N ATOM 2976 CA GLN B 92 28.398 19.195 0.738 1.00 37.91 B C ATOM 2977 CB GLN B 92 28.943 20.290 1.660 1.00 38.21 B C ATOM 2978 CG GLN B 92 28.030 20.632 2.834 1.00 41.26 B C ATOM 2979 CD GLN B 92 28.635 21.661 3.787 1.00 41.52 B C ATOM 2980 OE1 GLN B 92 29.230 22.645 3.356 1.00 44.14 B O ATOM 2981 NE2 GLN B 92 28.453 21.451 5.079 1.00 40.35 B N ATOM 2982 C GLN B 92 26.930 19.456 0.322 1.00 36.58 B C ATOM 2983 O GLN B 92 26.652 20.169 0.649 1.00 38.61 B O ATOM 2984 N LEU B 93 26.003 18.857 1.055 1.00 35.02 B N ATOM 2985 CA LEU B 93 24.599 18.840 0.670 1.00 35.33 B C ATOM 2986 CB LEU B 93 24.106 17.398 0.619 1.00 35.64 B C ATOM 2987 CG LEU B 93 24.765 16.482 0.435 1.00 36.84 B C ATOM 2988 CD1 LEU B 93 24.304 15.036 0.267 1.00 36.03 B C ATOM 2989 CD2 LEU B 93 24.506 16.983 1.859 1.00 37.70 B C ATOM 2990 C LEU B 93 23.745 19.658 1.632 1.00 36.40 B C ATOM 2991 O LEU B 93 23.507 19.249 2.770 1.00 36.65 B O ATOM 2992 N LYS B 94 23.292 20.820 1.173 1.00 37.02 B N ATOM 2993 CA LYS B 94 22.555 21.738 2.041 1.00 40.31 B C ATOM 2994 CB LYS B 94 23.009 23.211 1.813 1.00 43.72 B C ATOM 2995 CG LYS B 94 24.379 23.603 2.386 1.00 44.25 B C ATOM 2996 CD LYS B 94 25.058 24.748 1.617 1.00 46.62 B C ATOM 2997 CE LYS B 94 26.527 24.981 2.021 1.00 46.67 B C ATOM 2998 NZ LYS B 94 26.707 25.189 3.493 1.00 44.46 B N ATOM 2999 C LYS B 94 21.059 21.562 1.748 1.00 38.21 B C ATOM 3000 O LYS B 94 20.677 21.435 0.599 1.00 36.56 B O ATOM 3001 N SER B 95 20.226 21.552 2.784 1.00 35.66 B N ATOM 3002 CA SER B 95 18.801 21.364 2.615 1.00 35.30 B C ATOM 3003 CB SER B 95 18.393 19.953 3.037 1.00 37.34 B C ATOM 3004 OG SER B 95 19.004 18.966 2.224 1.00 40.01 B O ATOM 3005 C SER B 95 18.084 22.335 3.508 1.00 35.67 B C ATOM 3006 O SER B 95 18.331 22.355 4.712 1.00 35.97 B O ATOM 3007 N THR B 96 17.186 23.139 2.952 1.00 34.75 B N ATOM 3008 CA THR B 96 16.447 24.087 3.788 1.00 34.33 B C ATOM 3009 CB THR B 96 16.594 25.545 3.289 1.00 33.88 B C ATOM 3010 OG1 THR B 96 17.978 25.859 3.076 1.00 34.75 B O ATOM 3011 CG2 THR B 96 16.021 26.523 4.291 1.00 33.52 B C ATOM 3012 C THR B 96 14.983 23.703 3.791 1.00 33.72 B C ATOM 3013 O THR B 96 14.398 23.508 2.729 1.00 33.99 B O ATOM 3014 N VAL B 97 14.397 23.586 4.978 1.00 33.07 B N ATOM 3015 CA VAL B 97 12.952 23.374 5.093 1.00 34.16 B C ATOM 3016 CB VAL B 97 12.592 22.282 6.128 1.00 34.28 B C ATOM 3017 CG1 VAL B 97 13.159 20.957 5.683 1.00 35.98 B C ATOM 3018 CG2 VAL B 97 13.100 22.619 7.515 1.00 35.36 B C ATOM 3019 C VAL B 97 12.224 24.672 5.432 1.00 34.05 B C ATOM 3020 O VAL B 97 12.849 25.727 5.565 1.00 34.39 B O ATOM 3021 N HIS B 98 10.898 24.575 5.543 1.00 33.56 B N ATOM 3022 CA HIS B 98 10.042 25.695 5.882 1.00 32.14 B C ATOM 3023 CB HIS B 98 10.257 26.060 7.328 1.00 33.55 B C ATOM 3024 CG HIS B 98 10.063 24.924 8.258 1.00 34.25 B C ATOM 3025 ND1 HIS B 98 8.841 24.315 8.436 1.00 35.12 B N ATOM 3026 CE1 HIS B 98 8.961 23.356 9.332 1.00 36.99 B C ATOM 3027 NE2 HIS B 98 10.220 23.320 9.733 1.00 37.68 B N ATOM 3028 CD2 HIS B 98 10.927 24.299 9.084 1.00 34.92 B C ATOM 3029 C HIS B 98 10.337 26.911 5.043 1.00 31.42 B C ATOM 3030 O HIS B 98 10.422 28.024 5.578 1.00 30.39 B O ATOM 3031 N TYR B 99 10.524 26.701 3.738 1.00 29.84 B N ATOM 3032 CA TYR B 99 10.814 27.799 2.820 1.00 28.03 B C ATOM 3033 CB TYR B 99 11.373 27.284 1.524 1.00 27.78 B C ATOM 3034 CG TYR B 99 11.713 28.379 0.558 1.00 28.82 B C ATOM 3035 CD1 TYR B 99 12.884 29.113 0.710 1.00 30.01 B C ATOM 3036 CE1 TYR B 99 13.234 30.098 0.193 1.00 29.32 B C ATOM 3037 CZ TYR B 99 12.406 30.367 1.259 1.00 28.91 B C ATOM 3038 OH TYR B 99 12.778 31.345 2.132 1.00 27.23 B O ATOM 3039 CE2 TYR B 99 11.227 29.664 1.436 1.00 28.87 B C ATOM 3040 CD2 TYR B 99 10.888 28.671 0.526 1.00 29.25 B C ATOM 3041 C TYR B 99 9.568 28.584 2.503 1.00 26.15 B C ATOM 3042 O TYR B 99 8.635 28.055 1.878 1.00 24.18 B O ATOM 3043 N SER B 100 9.576 29.839 2.942 1.00 24.97 B N ATOM 3044 CA SER B 100 8.515 30.805 2.656 1.00 25.57 B C ATOM 3045 CB SER B 100 8.519 31.186 1.174 1.00 23.87 B C ATOM 3046 OG SER B 100 7.308 31.791 0.828 1.00 22.41 B O ATOM 3047 C SER B 100 7.140 30.320 3.143 1.00 26.93 B C ATOM 3048 O SER B 100 7.067 29.280 3.782 1.00 28.15 B O ATOM 3049 N SER B 101 6.074 31.083 2.875 1.00 27.99 B N ATOM 3050 CA SER B 101 4.750 30.814 3.463 1.00 28.45 B C ATOM 3051 CB SER B 101 4.040 32.123 3.845 1.00 28.72 B C ATOM 3052 OG SER B 101 2.682 32.138 3.419 1.00 29.51 B O ATOM 3053 C SER B 101 3.884 29.984 2.519 1.00 29.04 B C ATOM 3054 O SER B 101 3.783 30.299 1.331 1.00 27.72 B O ATOM 3055 N ARG B 102 3.289 28.919 3.069 1.00 30.50 B N ATOM 3056 CA ARG B 102 2.401 27.999 2.354 1.00 30.50 B C ATOM 3057 CB ARG B 102 0.949 28.479 2.461 1.00 33.61 B C ATOM 3058 CG ARG B 102 0.281 28.133 3.800 1.00 37.70 B C ATOM 3059 CD ARG B 102 1.209 28.482 3.815 1.00 40.99 B C ATOM 3060 NE ARG B 102 1.410 29.932 3.662 1.00 45.77 B N ATOM 3061 CZ ARG B 102 2.389 30.528 2.961 1.00 47.99 B C ATOM 3062 NH1 ARG B 102 3.304 29.804 2.311 1.00 50.01 B N ATOM 3063 NH2 ARG B 102 2.460 31.870 2.914 1.00 44.90 B N ATOM 3064 C ARG B 102 2.840 27.800 0.900 1.00 28.31 B C ATOM 3065 O ARG B 102 2.069 27.986 0.020 1.00 27.45 B O ATOM 3066 N TYR B 103 4.098 27.396 0.740 1.00 26.02 B N ATOM 3067 CA TYR B 103 4.787 27.284 0.548 1.00 23.64 B C ATOM 3068 CB TYR B 103 6.247 27.678 0.330 1.00 23.86 B C ATOM 3069 CG TYR B 103 7.039 27.730 1.575 1.00 24.13 B C ATOM 3070 CD1 TYR B 103 6.841 28.754 2.479 1.00 25.33 B C ATOM 3071 CE1 TYR B 103 7.554 28.825 3.652 1.00 25.32 B C ATOM 3072 CZ TYR B 103 8.476 27.862 3.928 1.00 26.06 B C ATOM 3073 OH TYR B 103 9.167 27.961 5.104 1.00 27.97 B O ATOM 3074 CE2 TYR B 103 8.707 26.819 3.041 1.00 24.94 B C ATOM 3075 CD2 TYR B 103 7.979 26.763 1.869 1.00 24.27 B C ATOM 3076 C TYR B 103 4.718 25.851 1.153 1.00 21.60 B C ATOM 3077 O TYR B 103 5.217 24.885 0.546 1.00 19.52 B O ATOM 3078 N ASN B 104 4.110 25.743 2.349 1.00 19.76 B N ATOM 3079 CA ASN B 104 3.842 24.452 3.015 1.00 18.78 B C ATOM 3080 CB ASN B 104 2.521 24.503 3.810 1.00 18.63 B C ATOM 3081 CG ASN B 104 1.267 24.521 2.930 1.00 18.22 B C ATOM 3082 OD1 ASN B 104 1.220 23.993 1.815 1.00 18.11 B O ATOM 3083 ND2 ASN B 104 0.230 25.118 3.461 1.00 17.67 B N ATOM 3084 C ASN B 104 4.969 23.980 3.962 1.00 17.89 B C ATOM 3085 O ASN B 104 4.729 23.661 5.119 1.00 16.38 B O ATOM 3086 N ASN B 105 6.195 23.906 3.463 1.00 17.58 B N ATOM 3087 CA ASN B 105 7.247 23.368 4.261 1.00 18.17 B C ATOM 3088 CB ASN B 105 7.549 24.310 5.395 1.00 17.95 B C ATOM 3089 CG ASN B 105 7.575 23.611 6.739 1.00 18.43 B C ATOM 3090 OD1 ASN B 105 7.983 22.445 6.890 1.00 18.76 B O ATOM 3091 ND2 ASN B 105 7.147 24.340 7.740 1.00 19.03 B N ATOM 3092 C ASN B 105 8.558 23.035 3.544 1.00 20.12 B C ATOM 3093 O ASN B 105 8.807 23.426 2.391 1.00 22.03 B O ATOM 3094 N ALA B 106 9.386 22.274 4.247 1.00 19.79 B N ATOM 3095 CA ALA B 106 10.718 22.010 3.819 1.00 19.99 B C ATOM 3096 CB ALA B 106 10.897 20.520 3.551 1.00 20.22 B C ATOM 3097 C ALA B 106 11.540 22.440 4.990 1.00 20.21 B C ATOM 3098 O ALA B 106 11.021 22.459 6.098 1.00 19.79 B O ATOM 3099 N PHE B 107 12.813 22.758 4.768 1.00 21.28 B N ATOM 3100 CA PHE B 107 13.684 23.129 5.883 1.00 22.81 B C ATOM 3101 CB PHE B 107 13.343 24.553 6.408 1.00 24.23 B C ATOM 3102 CG PHE B 107 13.461 25.660 5.365 1.00 25.42 B C ATOM 3103 CD1 PHE B 107 12.387 25.980 4.532 1.00 26.00 B C ATOM 3104 CE1 PHE B 107 12.496 26.993 3.590 1.00 26.52 B C ATOM 3105 CZ PHE B 107 13.686 27.714 3.479 1.00 26.55 B C ATOM 3106 CE2 PHE B 107 14.754 27.427 4.310 1.00 25.62 B C ATOM 3107 CD2 PHE B 107 14.640 26.408 5.247 1.00 25.85 B C ATOM 3108 C PHE B 107 15.174 23.011 5.576 1.00 22.11 B C ATOM 3109 O PHE B 107 15.581 22.879 4.422 1.00 21.96 B O ATOM 3110 N TRP B 108 15.962 23.035 6.644 1.00 21.93 B N ATOM 3111 CA TRP B 108 17.418 23.093 6.576 1.00 22.59 B C ATOM 3112 CB TRP B 108 18.045 21.893 7.330 1.00 21.95 B C ATOM 3113 CG TRP B 108 19.427 22.087 7.888 1.00 20.54 B C ATOM 3114 CD1 TRP B 108 19.743 22.448 9.159 1.00 20.50 B C ATOM 3115 NE1 TRP B 108 21.102 22.522 9.318 1.00 20.10 B N ATOM 3116 CE2 TRP B 108 21.701 22.176 8.143 1.00 20.03 B C ATOM 3117 CD2 TRP B 108 20.666 21.888 7.213 1.00 20.47 B C ATOM 3118 CE3 TRP B 108 21.012 21.496 5.918 1.00 20.91 B C ATOM 3119 CZ3 TRP B 108 22.392 21.423 5.591 1.00 21.48 B C ATOM 3120 CH2 TRP B 108 23.393 21.729 6.552 1.00 20.23 B C ATOM 3121 CZ2 TRP B 108 23.064 22.094 7.824 1.00 19.90 B C ATOM 3122 C TRP B 108 17.813 24.400 7.210 1.00 24.22 B C ATOM 3123 O TRP B 108 17.449 24.649 8.357 1.00 24.63 B O ATOM 3124 N ASN B 109 18.555 25.233 6.479 1.00 26.95 B N ATOM 3125 CA ASN B 109 18.965 26.547 6.990 1.00 27.50 B C ATOM 3126 CB ASN B 109 18.725 27.619 5.921 1.00 27.76 B C ATOM 3127 CG ASN B 109 19.755 27.595 4.793 1.00 28.70 B C ATOM 3128 OD1 ASN B 109 20.754 26.849 4.814 1.00 27.27 B O ATOM 3129 ND2 ASN B 109 19.510 28.443 3.785 1.00 29.61 B N ATOM 3130 C ASN B 109 20.405 26.611 7.505 1.00 28.31 B C ATOM 3131 O ASN B 109 21.001 27.658 7.523 1.00 28.32 B O ATOM 3132 N GLY B 110 20.971 25.490 7.919 1.00 31.03 B N ATOM 3133 CA GLY B 110 22.345 25.465 8.439 1.00 32.29 B C ATOM 3134 C GLY B 110 23.355 25.216 7.333 1.00 33.16 B C ATOM 3135 O GLY B 110 24.504 24.822 7.595 1.00 33.81 B O ATOM 3136 N VAL B 111 22.913 25.405 6.095 1.00 33.45 B N ATOM 3137 CA VAL B 111 23.799 25.336 4.942 1.00 35.17 B C ATOM 3138 CB VAL B 111 24.201 26.785 4.535 1.00 34.30 B C ATOM 3139 CG1 VAL B 111 23.952 27.096 3.048 1.00 33.42 B C ATOM 3140 CG2 VAL B 111 25.649 27.041 4.959 1.00 34.43 B C ATOM 3141 C VAL B 111 23.244 24.503 3.758 1.00 36.29 B C ATOM 3142 O VAL B 111 24.018 23.960 2.969 1.00 37.98 B O ATOM 3143 N GLN B 112 21.923 24.398 3.625 1.00 35.91 B N ATOM 3144 CA GLN B 112 21.327 23.587 2.558 1.00 35.06 B C ATOM 3145 CB GLN B 112 21.404 24.355 1.234 1.00 35.50 B C ATOM 3146 CG GLN B 112 20.563 25.625 1.199 1.00 34.97 B C ATOM 3147 CD GLN B 112 20.178 26.032 0.207 1.00 33.92 B C ATOM 3148 OE1 GLN B 112 20.655 27.036 0.715 1.00 34.45 B O ATOM 3149 NE2 GLN B 112 19.318 25.250 0.843 1.00 33.47 B N ATOM 3150 C GLN B 112 19.861 23.172 2.833 1.00 33.71 B C ATOM 3151 O GLN B 112 19.261 23.555 3.847 1.00 34.36 B O ATOM 3152 N MET B 113 19.295 22.404 1.907 1.00 30.68 B N ATOM 3153 CA MET B 113 17.933 21.911 2.017 1.00 28.51 B C ATOM 3154 CB MET B 113 17.849 20.424 1.641 1.00 29.34 B C ATOM 3155 CG MET B 113 18.299 19.432 2.709 1.00 29.87 B C ATOM 3156 SD MET B 113 20.078 19.409 2.981 1.00 29.78 B S ATOM 3157 CE MET B 113 20.613 18.711 1.419 1.00 30.48 B C ATOM 3158 C MET B 113 17.070 22.692 1.060 1.00 27.82 B C ATOM 3159 O MET B 113 17.493 23.039 0.062 1.00 26.31 B O ATOM 3160 N VAL B 114 15.833 22.914 1.497 1.00 27.54 B N ATOM 3161 CA VAL B 114 14.882 23.775 0.794 1.00 26.67 B C ATOM 3162 CB VAL B 114 14.799 25.172 1.472 1.00 27.48 B C ATOM 3163 CG1 VAL B 114 13.869 26.096 0.697 1.00 27.84 B C ATOM 3164 CG2 VAL B 114 16.183 25.792 1.594 1.00 27.90 B C ATOM 3165 C VAL B 114 13.510 23.112 0.845 1.00 23.88 B C ATOM 3166 O VAL B 114 13.093 22.652 1.913 1.00 22.42 B O ATOM 3167 N TYR B 115 12.822 23.087 0.291 1.00 21.58 B N ATOM 3168 CA TYR B 115 11.557 22.383 0.411 1.00 21.93 B C ATOM 3169 CB TYR B 115 11.718 21.092 1.229 1.00 21.40 B C ATOM 3170 CG TYR B 115 12.731 20.164 0.665 1.00 21.37 B C ATOM 3171 CD1 TYR B 115 12.421 19.308 0.358 1.00 21.96 B C ATOM 3172 CE1 TYR B 115 13.389 18.468 0.910 1.00 22.81 B C ATOM 3173 CZ TYR B 115 14.677 18.480 0.422 1.00 22.74 B C ATOM 3174 OH TYR B 115 15.665 17.644 0.940 1.00 22.96 B O ATOM 3175 CE2 TYR B 115 14.992 19.339 0.605 1.00 22.43 B C ATOM 3176 CD2 TYR B 115 14.028 20.175 1.130 1.00 22.02 B C ATOM 3177 C TYR B 115 10.500 23.244 1.092 1.00 22.23 B C ATOM 3178 O TYR B 115 10.611 23.520 2.287 1.00 21.55 B O ATOM 3179 N GLY B 116 9.458 23.609 0.341 1.00 21.40 B N ATOM 3180 CA GLY B 116 8.302 24.273 0.901 1.00 21.51 B C ATOM 3181 C GLY B 116 7.513 23.366 1.821 1.00 21.86 B C ATOM 3182 O GLY B 116 7.773 22.181 1.900 1.00 22.60 B O ATOM 3183 N ASP B 117 6.549 23.936 2.523 1.00 22.59 B N ATOM 3184 CA ASP B 117 5.689 23.176 3.412 1.00 23.66 B C ATOM 3185 CB ASP B 117 5.446 23.933 4.723 1.00 24.06 B C ATOM 3186 CG ASP B 117 6.583 23.800 5.710 1.00 24.67 B C ATOM 3187 OD1 ASP B 117 7.346 22.803 5.728 1.00 25.59 B O ATOM 3188 OD2 ASP B 117 6.695 24.723 6.502 1.00 25.80 B O ATOM 3189 C ASP B 117 4.346 22.926 2.766 1.00 23.69 B C ATOM 3190 O ASP B 117 3.480 22.273 3.347 1.00 23.57 B O ATOM 3191 N GLY B 118 4.152 23.465 1.575 1.00 24.06 B N ATOM 3192 CA GLY B 118 2.868 23.321 0.912 1.00 24.13 B C ATOM 3193 C GLY B 118 1.737 24.045 1.622 1.00 22.97 B C ATOM 3194 O GLY B 118 1.779 24.292 2.834 1.00 22.31 B O ATOM 3195 N ASP B 119 0.709 24.364 0.847 1.00 22.43 B N ATOM 3196 CA ASP B 119 0.478 25.039 1.368 1.00 21.83 B C ATOM 3197 CB ASP B 119 1.323 25.608 0.197 1.00 20.08 B C ATOM 3198 CG ASP B 119 2.036 24.543 0.596 1.00 19.22 B C ATOM 3199 OD1 ASP B 119 2.324 23.446 0.078 1.00 19.73 B O ATOM 3200 OD2 ASP B 119 2.347 24.810 1.752 1.00 17.52 B O ATOM 3201 C ASP B 119 1.321 24.187 2.353 1.00 21.78 B C ATOM 3202 O ASP B 119 2.321 24.651 2.875 1.00 21.12 B O ATOM 3203 N GLY B 120 0.916 22.943 2.587 1.00 23.30 B N ATOM 3204 CA GLY B 120 1.636 22.047 3.486 1.00 23.87 B C ATOM 3205 C GLY B 120 2.932 21.462 2.957 1.00 24.49 B C ATOM 3206 O GLY B 120 3.629 20.779 3.676 1.00 24.47 B O ATOM 3207 N VAL B 121 3.284 21.718 1.711 1.00 26.95 B N ATOM 3208 CA VAL B 121 4.523 21.143 1.163 1.00 29.85 B C ATOM 3209 CB VAL B 121 5.613 22.221 0.856 1.00 29.49 B C ATOM 3210 CG1 VAL B 121 6.777 21.618 0.072 1.00 28.64 B C ATOM 3211 CG2 VAL B 121 6.142 22.843 2.140 1.00 28.93 B C ATOM 3212 C VAL B 121 4.211 20.346 0.094 1.00 31.76 B C ATOM 3213 O VAL B 121 4.770 19.262 0.314 1.00 36.09 B O ATOM 3214 N THR B 122 3.333 20.892 0.924 1.00 30.83 B N ATOM 3215 CA THR B 122 2.924 20.223 2.139 1.00 29.94 B C ATOM 3216 CB THR B 122 2.957 21.220 3.312 1.00 32.47 B C ATOM 3217 OG1 THR B 122 2.621 22.519 2.826 1.00 33.51 B O ATOM 3218 CG2 THR B 122 4.399 21.336 3.879 1.00 35.40 B C ATOM 3219 C THR B 122 1.562 19.555 1.934 1.00 26.62 B C ATOM 3220 O THR B 122 1.221 18.626 2.642 1.00 26.32 B O ATOM 3221 N PHE B 123 0.790 20.010 0.955 1.00 23.60 B N ATOM 3222 CA PHE B 123 0.483 19.367 0.627 1.00 21.85 B C ATOM 3223 CB PHE B 123 1.700 20.064 1.261 1.00 21.42 B C ATOM 3224 CG PHE B 123 1.758 19.968 2.752 1.00 20.41 B C ATOM 3225 CD2 PHE B 123 2.454 18.948 3.362 1.00 20.18 B C ATOM 3226 CE2 PHE B 123 2.516 18.853 4.741 1.00 20.20 B C ATOM 3227 CZ PHE B 123 1.865 19.781 5.527 1.00 20.04 B C ATOM 3228 CE1 PHE B 123 1.156 20.809 4.928 1.00 20.65 B C ATOM 3229 CD1 PHE B 123 1.120 20.906 3.544 1.00 20.63 B C ATOM 3230 C PHE B 123 0.669 19.445 0.854 1.00 21.39 B C ATOM 3231 O PHE B 123 0.128 20.345 1.499 1.00 23.40 B O ATOM 3232 N ILE B 124 1.434 18.499 1.383 1.00 20.17 B N ATOM 3233 CA ILE B 124 1.961 18.572 2.736 1.00 18.39 B C ATOM 3234 CB ILE B 124 1.640 17.310 3.541 1.00 17.54 B C ATOM 3235 CG1 ILE B 124 2.396 16.082 3.033 1.00 16.90 B C ATOM 3236 CD1 ILE B 124 2.386 14.964 4.038 1.00 16.17 B C ATOM 3237 CG2 ILE B 124 0.147 17.048 3.498 1.00 17.65 B C ATOM 3238 C ILE B 124 3.444 18.826 2.549 1.00 18.58 B C ATOM 3239 O ILE B 124 3.891 18.998 1.407 1.00 18.36 B O ATOM 3240 N PRO B 125 4.203 18.918 3.649 1.00 18.87 B N ATOM 3241 CA PRO B 125 5.577 19.377 3.443 1.00 19.02 B C ATOM 3242 CB PRO B 125 6.169 19.403 4.854 1.00 19.23 B C ATOM 3243 CG PRO B 125 4.980 19.587 5.754 1.00 19.46 B C ATOM 3244 CD PRO B 125 3.825 18.905 5.077 1.00 19.29 B C ATOM 3245 C PRO B 125 6.356 18.467 2.510 1.00 19.07 B C ATOM 3246 O PRO B 125 6.278 17.247 2.613 1.00 18.93 B O ATOM 3247 N PHE B 126 7.105 19.080 1.604 1.00 18.81 B N ATOM 3248 CA PHE B 126 7.614 18.381 0.437 1.00 18.56 B C ATOM 3249 CB PHE B 126 8.131 19.385 0.604 1.00 18.49 B C ATOM 3250 CG PHE B 126 7.064 19.911 1.508 1.00 18.66 B C ATOM 3251 CD1 PHE B 126 6.020 20.664 1.006 1.00 19.04 B C ATOM 3252 CE1 PHE B 126 5.020 21.148 1.831 1.00 18.97 B C ATOM 3253 CZ PHE B 126 5.055 20.874 3.176 1.00 19.04 B C ATOM 3254 CE2 PHE B 126 6.100 20.132 3.692 1.00 18.90 B C ATOM 3255 CD2 PHE B 126 7.098 19.653 2.860 1.00 18.72 B C ATOM 3256 C PHE B 126 8.703 17.362 0.755 1.00 18.62 B C ATOM 3257 O PHE B 126 9.003 16.516 0.081 1.00 19.38 B O ATOM 3258 N SER B 127 9.292 17.422 1.945 1.00 17.97 B N ATOM 3259 CA SER B 127 10.348 16.474 2.291 1.00 17.25 B C ATOM 3260 CB SER B 127 11.203 17.006 3.427 1.00 17.21 B C ATOM 3261 OG SER B 127 10.384 17.220 4.554 1.00 17.32 B O ATOM 3262 C SER B 127 9.808 15.133 2.712 1.00 16.62 B C ATOM 3263 O SER B 127 10.606 14.248 2.963 1.00 16.39 B O ATOM 3264 N ALA B 128 8.481 14.984 2.782 1.00 16.07 B N ATOM 3265 CA ALA B 128 7.847 13.752 3.257 1.00 15.85 B C ATOM 3266 CB ALA B 128 6.407 14.027 3.600 1.00 15.64 B C ATOM 3267 C ALA B 128 7.920 12.530 2.315 1.00 16.85 B C ATOM 3268 O ALA B 128 7.759 11.373 2.775 1.00 17.34 B O ATOM 3269 N ASP B 129 8.144 12.759 1.019 1.00 17.61 B N ATOM 3270 CA ASP B 129 8.243 11.666 0.041 1.00 17.88 B C ATOM 3271 CB ASP B 129 7.283 11.861 1.165 1.00 18.05 B C ATOM 3272 CG ASP B 129 7.173 10.596 2.055 1.00 19.36 B C ATOM 3273 OD1 ASP B 129 8.206 9.927 2.291 1.00 19.57 B O ATOM 3274 OD2 ASP B 129 6.063 10.247 2.541 1.00 20.33 B O ATOM 3275 C ASP B 129 9.681 11.618 0.426 1.00 17.31 B C ATOM 3276 O ASP B 129 10.152 12.569 1.029 1.00 17.85 B O ATOM 3277 N PRO B 130 10.371 10.493 0.196 1.00 17.22 B N ATOM 3278 CA PRO B 130 11.786 10.369 0.601 1.00 17.02 B C ATOM 3279 CB PRO B 130 12.140 8.911 0.243 1.00 16.73 B C ATOM 3280 CG PRO B 130 11.099 8.456 0.723 1.00 16.71 B C ATOM 3281 CD PRO B 130 9.855 9.235 0.392 1.00 17.19 B C ATOM 3282 C PRO B 130 12.074 10.631 2.085 1.00 16.62 B C ATOM 3283 O PRO B 130 13.211 10.958 2.436 1.00 15.51 B O ATOM 3284 N ASP B 131 11.072 10.485 2.948 1.00 16.98 B N ATOM 3285 CA ASP B 131 11.310 10.688 4.384 1.00 18.29 B C ATOM 3286 CB ASP B 131 10.235 9.999 5.283 1.00 19.03 B C ATOM 3287 CG ASP B 131 8.835 10.602 5.142 1.00 19.39 B C ATOM 3288 OD1 ASP B 131 8.691 11.825 5.259 1.00 19.96 B O ATOM 3289 OD2 ASP B 131 7.859 9.851 4.923 1.00 20.07 B O ATOM 3290 C ASP B 131 11.495 12.177 4.702 1.00 19.01 B C ATOM 3291 O ASP B 131 12.097 12.542 5.721 1.00 17.48 B O ATOM 3292 N VAL B 132 10.995 13.028 3.804 1.00 19.89 B N ATOM 3293 CA VAL B 132 11.221 14.456 3.922 1.00 21.16 B C ATOM 3294 CB VAL B 132 10.333 15.232 2.948 1.00 22.10 B C ATOM 3295 CG1 VAL B 132 10.779 16.695 2.865 1.00 22.23 B C ATOM 3296 CG2 VAL B 132 8.867 15.110 3.357 1.00 22.87 B C ATOM 3297 C VAL B 132 12.683 14.825 3.651 1.00 21.46 B C ATOM 3298 O VAL B 132 13.300 15.590 4.402 1.00 20.31 B O ATOM 3299 N ILE B 133 13.220 14.282 2.562 1.00 21.93 B N ATOM 3300 CA ILE B 133 14.609 14.519 2.215 1.00 21.56 B C ATOM 3301 CB ILE B 133 15.025 13.773 0.956 1.00 21.14 B C ATOM 3302 CG1 ILE B 133 14.046 14.023 0.199 1.00 22.31 B C ATOM 3303 CD1 ILE B 133 13.855 15.454 0.620 1.00 22.87 B C ATOM 3304 CG2 ILE B 133 16.455 14.105 0.599 1.00 20.64 B C ATOM 3305 C ILE B 133 15.465 13.987 3.346 1.00 22.51 B C ATOM 3306 O ILE B 133 16.421 14.642 3.763 1.00 24.23 B O ATOM 3307 N GLY B 134 15.108 12.798 3.844 1.00 22.08 B N ATOM 3308 CA GLY B 134 15.828 12.177 4.929 1.00 21.41 B C ATOM 3309 C GLY B 134 15.719 13.033 6.162 1.00 22.33 B C ATOM 3310 O GLY B 134 16.690 13.223 6.891 1.00 23.18 B O ATOM 3311 N HIS B 135 14.528 13.569 6.390 1.00 23.11 B N ATOM 3312 CA HIS B 135 14.280 14.385 7.573 1.00 23.08 B C ATOM 3313 CB HIS B 135 12.829 14.804 7.601 1.00 21.45 B C ATOM 3314 CG HIS B 135 12.442 15.596 8.804 1.00 20.35 B C ATOM 3315 ND1 HIS B 135 12.056 15.007 9.982 1.00 19.67 B N ATOM 3316 CE1 HIS B 135 11.717 15.942 10.847 1.00 19.76 B C ATOM 3317 NE2 HIS B 135 11.876 17.120 10.274 1.00 19.91 B N ATOM 3318 CD2 HIS B 135 12.317 16.930 8.991 1.00 20.18 B C ATOM 3319 C HIS B 135 15.164 15.628 7.593 1.00 25.10 B C ATOM 3320 O HIS B 135 15.726 15.994 8.651 1.00 27.12 B O ATOM 3321 N GLU B 136 15.295 16.272 6.436 1.00 25.03 B N ATOM 3322 CA GLU B 136 16.004 17.549 6.379 1.00 25.06 B C ATOM 3323 CB GLU B 136 15.518 18.377 5.191 1.00 24.35 B C ATOM 3324 CG GLU B 136 14.098 18.882 5.369 1.00 24.50 B C ATOM 3325 CD GLU B 136 13.846 19.503 6.744 1.00 25.78 B C ATOM 3326 OE1 GLU B 136 12.713 19.404 7.229 1.00 29.10 B O ATOM 3327 OE2 GLU B 136 14.753 20.096 7.371 1.00 25.51 B O ATOM 3328 C GLU B 136 17.519 17.378 6.375 1.00 25.55 B C ATOM 3329 O GLU B 136 18.227 18.100 7.086 1.00 23.74 B O ATOM 3330 N LEU B 137 17.993 16.404 5.594 1.00 26.39 B N ATOM 3331 CA LEU B 137 19.406 16.077 5.519 1.00 26.59 B C ATOM 3332 CB LEU B 137 19.572 14.815 4.694 1.00 27.82 B C ATOM 3333 CG LEU B 137 20.822 14.488 3.869 1.00 29.11 B C ATOM 3334 CD1 LEU B 137 22.031 14.318 4.757 1.00 30.30 B C ATOM 3335 CD2 LEU B 137 21.094 15.501 2.771 1.00 30.20 B C ATOM 3336 C LEU B 137 19.893 15.841 6.930 1.00 28.03 B C ATOM 3337 O LEU B 137 20.952 16.353 7.334 1.00 29.88 B O ATOM 3338 N THR B 138 19.098 15.068 7.677 1.00 28.04 B N ATOM 3339 CA THR B 138 19.400 14.703 9.054 1.00 27.52 B C ATOM 3340 CB THR B 138 18.403 13.654 9.578 1.00 27.58 B C ATOM 3341 OG1 THR B 138 18.419 12.512 8.720 1.00 25.48 B O ATOM 3342 CG2 THR B 138 18.744 13.228 11.013 1.00 27.35 B C ATOM 3343 C THR B 138 19.371 15.928 9.967 1.00 28.01 B C ATOM 3344 O THR B 138 20.163 16.016 10.896 1.00 29.23 B O ATOM 3345 N HIS B 139 18.472 16.881 9.715 1.00 28.67 B N ATOM 3346 CA HIS B 139 18.529 18.184 10.421 1.00 27.39 B C ATOM 3347 CB HIS B 139 17.532 19.196 9.824 1.00 26.16 B C ATOM 3348 CG HIS B 139 16.138 19.145 10.411 1.00 25.53 B C ATOM 3349 ND1 HIS B 139 15.900 19.058 11.764 1.00 25.15 B N ATOM 3350 CE1 HIS B 139 14.595 19.065 11.988 1.00 24.31 B C ATOM 3351 NE2 HIS B 139 13.974 19.181 10.830 1.00 24.44 B N ATOM 3352 CD2 HIS B 139 14.915 19.249 9.829 1.00 24.67 B C ATOM 3353 C HIS B 139 19.987 18.721 10.357 1.00 28.40 B C ATOM 3354 O HIS B 139 20.511 19.275 11.337 1.00 27.07 B O ATOM 3355 N GLY B 140 20.640 18.506 9.209 1.00 29.45 B N ATOM 3356 CA GLY B 140 22.074 18.781 9.033 1.00 30.38 B C ATOM 3357 C GLY B 140 23.047 17.934 9.872 1.00 31.74 B C ATOM 3358 O GLY B 140 23.870 18.491 10.622 1.00 32.56 B O ATOM 3359 N VAL B 141 22.982 16.605 9.742 1.00 30.73 B N ATOM 3360 CA VAL B 141 23.765 15.712 10.609 1.00 30.84 B C ATOM 3361 CB VAL B 141 23.302 14.229 10.488 1.00 30.98 B C ATOM 3362 CG1 VAL B 141 24.079 13.307 11.417 1.00 30.38 B C ATOM 3363 CG2 VAL B 141 23.418 13.731 9.059 1.00 33.19 B C ATOM 3364 C VAL B 141 23.653 16.184 12.087 1.00 32.64 B C ATOM 3365 O VAL B 141 24.680 16.395 12.764 1.00 34.17 B O ATOM 3366 N THR B 142 22.425 16.371 12.584 1.00 30.57 B N ATOM 3367 CA THR B 142 22.238 16.711 13.978 1.00 30.33 B C ATOM 3368 CB THR B 142 20.747 16.814 14.342 1.00 28.78 B C ATOM 3369 OG1 THR B 142 20.107 15.548 14.169 1.00 28.27 B O ATOM 3370 CG2 THR B 142 20.562 17.241 15.778 1.00 28.27 B C ATOM 3371 C THR B 142 23.018 18.012 14.321 1.00 34.44 B C ATOM 3372 O THR B 142 23.756 18.043 15.311 1.00 31.77 B O ATOM 3373 N GLU B 143 22.891 19.058 13.496 1.00 39.28 B N ATOM 3374 CA GLU B 143 23.609 20.331 13.746 1.00 44.10 B C ATOM 3375 CB GLU B 143 23.199 21.447 12.749 1.00 46.26 B C ATOM 3376 CG GLU B 143 23.758 22.829 13.098 1.00 46.77 B C ATOM 3377 CD GLU B 143 23.520 23.911 12.036 1.00 50.51 B C ATOM 3378 OE1 GLU B 143 24.476 24.652 11.712 1.00 52.85 B O ATOM 3379 OE2 GLU B 143 22.388 24.056 11.531 1.00 51.61 B O ATOM 3380 C GLU B 143 25.141 20.147 13.737 1.00 43.41 B C ATOM 3381 O GLU B 143 25.837 20.722 14.579 1.00 42.45 B O ATOM 3382 N HIS B 144 25.657 19.350 12.803 1.00 41.46 B N ATOM 3383 CA HIS B 144 27.095 19.050 12.768 1.00 42.89 B C ATOM 3384 CB HIS B 144 27.500 18.615 11.363 1.00 43.93 B C ATOM 3385 CG HIS B 144 27.711 19.748 10.415 1.00 48.17 B C ATOM 3386 ND1 HIS B 144 26.683 20.562 9.985 1.00 53.25 B N ATOM 3387 CE1 HIS B 144 27.156 21.457 9.134 1.00 53.12 B C ATOM 3388 NE2 HIS B 144 28.453 21.245 8.991 1.00 52.99 B N ATOM 3389 CD2 HIS B 144 28.827 20.187 9.787 1.00 49.42 B C ATOM 3390 C HIS B 144 27.596 17.985 13.790 1.00 41.27 B C ATOM 3391 O HIS B 144 28.773 17.664 13.803 1.00 41.71 B O ATOM 3392 N THR B 145 26.729 17.451 14.646 1.00 39.46 B N ATOM 3393 CA THR B 145 27.124 16.412 15.614 1.00 37.58 B C ATOM 3394 CB THR B 145 26.559 15.013 15.211 1.00 39.34 B C ATOM 3395 OG1 THR B 145 25.127 15.071 15.027 1.00 36.83 B O ATOM 3396 CG2 THR B 145 27.213 14.517 13.918 1.00 39.08 B C ATOM 3397 C THR B 145 26.685 16.769 17.042 1.00 34.70 B C ATOM 3398 O THR B 145 27.380 17.459 17.750 1.00 36.43 B O ATOM 3399 N ALA B 146 25.523 16.305 17.455 1.00 33.64 B N ATOM 3400 CA ALA B 146 25.006 16.605 18.769 1.00 33.70 B C ATOM 3401 CB ALA B 146 23.739 15.803 19.000 1.00 33.49 B C ATOM 3402 C ALA B 146 24.709 18.100 18.948 1.00 34.85 B C ATOM 3403 O ALA B 146 24.835 18.639 20.052 1.00 36.76 B O ATOM 3404 N GLY B 147 24.277 18.752 17.873 1.00 33.97 B N ATOM 3405 CA GLY B 147 23.841 20.144 17.930 1.00 32.43 B C ATOM 3406 C GLY B 147 22.627 20.388 18.804 1.00 31.88 B C ATOM 3407 O GLY B 147 22.585 21.373 19.541 1.00 32.47 B O ATOM 3408 N LEU B 148 21.632 19.506 18.744 1.00 32.61 B N ATOM 3409 CA LEU B 148 20.451 19.658 19.605 1.00 33.79 B C ATOM 3410 CB LEU B 148 19.475 18.492 19.444 1.00 35.60 B C ATOM 3411 CG LEU B 148 19.982 17.190 20.083 1.00 38.31 B C ATOM 3412 CD1 LEU B 148 19.402 15.964 19.399 1.00 37.11 B C ATOM 3413 CD2 LEU B 148 19.694 17.157 21.585 1.00 40.39 B C ATOM 3414 C LEU B 148 19.783 20.967 19.246 1.00 32.00 B C ATOM 3415 O LEU B 148 19.587 21.241 18.078 1.00 29.10 B O ATOM 3416 N GLU B 149 19.474 21.789 20.246 1.00 31.33 B N ATOM 3417 CA GLU B 149 18.940 23.146 19.978 1.00 29.16 B C ATOM 3418 CB GLU B 149 19.192 24.108 21.161 1.00 27.96 B C ATOM 3419 CG GLU B 149 20.666 24.425 21.298 1.00 26.85 B C ATOM 3420 CD GLU B 149 21.026 25.095 22.589 1.00 24.90 B C ATOM 3421 OE1 GLU B 149 22.188 25.536 22.681 1.00 23.70 B O ATOM 3422 OE2 GLU B 149 20.181 25.161 23.493 1.00 23.35 B O ATOM 3423 C GLU B 149 17.471 23.082 19.639 1.00 25.48 B C ATOM 3424 O GLU B 149 16.708 22.371 20.273 1.00 24.06 B O ATOM 3425 N TYR B 150 17.091 23.848 18.640 1.00 23.26 B N ATOM 3426 CA TYR B 150 15.795 23.690 18.059 1.00 23.09 B C ATOM 3427 CB TYR B 150 15.847 24.115 16.606 1.00 22.13 B C ATOM 3428 CG TYR B 150 14.796 23.476 15.770 1.00 22.41 B C ATOM 3429 CD1 TYR B 150 14.899 22.133 15.406 1.00 22.39 B C ATOM 3430 CE1 TYR B 150 13.920 21.529 14.620 1.00 22.34 B C ATOM 3431 CZ TYR B 150 12.828 22.277 14.176 1.00 22.55 B C ATOM 3432 OH TYR B 150 11.884 21.671 13.406 1.00 21.97 B O ATOM 3433 CE2 TYR B 150 12.697 23.623 14.518 1.00 22.68 B C ATOM 3434 CD2 TYR B 150 13.676 24.213 15.319 1.00 22.78 B C ATOM 3435 C TYR B 150 14.760 24.462 18.871 1.00 23.03 B C ATOM 3436 O TYR B 150 14.194 25.466 18.425 1.00 25.23 B O ATOM 3437 N TYR B 151 14.522 23.970 20.075 1.00 21.89 B N ATOM 3438 CA TYR B 151 13.540 24.533 20.963 1.00 22.19 B C ATOM 3439 CB TYR B 151 14.012 25.873 21.514 1.00 22.84 B C ATOM 3440 CG TYR B 151 12.869 26.737 21.992 1.00 24.39 B C ATOM 3441 CD1 TYR B 151 12.365 26.643 23.293 1.00 24.16 B C ATOM 3442 CE1 TYR B 151 11.298 27.439 23.704 1.00 23.84 B C ATOM 3443 CZ TYR B 151 10.738 28.326 22.820 1.00 24.46 B C ATOM 3444 OH TYR B 151 9.695 29.143 23.159 1.00 26.46 B O ATOM 3445 CE2 TYR B 151 11.214 28.432 21.538 1.00 25.25 B C ATOM 3446 CD2 TYR B 151 12.263 27.640 21.125 1.00 25.13 B C ATOM 3447 C TYR B 151 13.325 23.580 22.124 1.00 22.44 B C ATOM 3448 O TYR B 151 14.227 22.838 22.485 1.00 22.50 B O ATOM 3449 N GLY B 152 12.139 23.613 22.717 1.00 23.25 B N ATOM 3450 CA GLY B 152 11.812 22.762 23.866 1.00 24.07 B C ATOM 3451 C GLY B 152 12.135 21.280 23.685 1.00 24.84 B C ATOM 3452 O GLY B 152 12.043 20.733 22.564 1.00 25.07 B O ATOM 3453 N GLU B 153 12.539 20.635 24.787 1.00 25.04 B N ATOM 3454 CA GLU B 153 12.871 19.202 24.766 1.00 24.00 B C ATOM 3455 CB GLU B 153 13.149 18.678 26.183 1.00 23.45 B C ATOM 3456 CG GLU B 153 11.936 18.864 27.107 1.00 23.71 B C ATOM 3457 CD GLU B 153 11.913 17.978 28.361 1.00 24.91 B C ATOM 3458 OE1 GLU B 153 12.587 16.903 28.423 1.00 24.29 B O ATOM 3459 OE2 GLU B 153 11.174 18.362 29.304 1.00 24.99 B O ATOM 3460 C GLU B 153 14.005 18.909 23.771 1.00 23.93 B C ATOM 3461 O GLU B 153 13.861 18.016 22.931 1.00 23.19 B O ATOM 3462 N SER B 154 15.085 19.689 23.812 1.00 23.68 B N ATOM 3463 CA SER B 154 16.128 19.584 22.790 1.00 24.55 B C ATOM 3464 CB SER B 154 16.967 20.848 22.696 1.00 25.82 B C ATOM 3465 OG SER B 154 18.170 20.690 23.396 1.00 29.35 B O ATOM 3466 C SER B 154 15.567 19.381 21.419 1.00 24.67 B C ATOM 3467 O SER B 154 15.952 18.454 20.715 1.00 26.62 B O ATOM 3468 N GLY B 155 14.688 20.288 21.023 1.00 24.28 B N ATOM 3469 CA GLY B 155 14.237 20.370 19.635 1.00 24.21 B C ATOM 3470 C GLY B 155 13.255 19.268 19.266 1.00 24.50 B C ATOM 3471 O GLY B 155 13.162 18.878 18.081 1.00 24.34 B O ATOM 3472 N ALA B 156 12.518 18.776 20.272 1.00 22.74 B N ATOM 3473 CA ALA B 156 11.638 17.640 20.087 1.00 21.34 B C ATOM 3474 CB ALA B 156 10.756 17.444 21.302 1.00 21.61 B C ATOM 3475 C ALA B 156 12.447 16.379 19.758 1.00 20.58 B C ATOM 3476 O ALA B 156 12.066 15.588 18.881 1.00 19.77 B O ATOM 3477 N LEU B 157 13.573 16.213 20.435 1.00 20.76 B N ATOM 3478 CA LEU B 157 14.554 15.186 20.067 1.00 21.15 B C ATOM 3479 CB LEU B 157 15.696 15.131 21.091 1.00 22.03 B C ATOM 3480 CG LEU B 157 15.537 14.290 22.373 1.00 23.05 B C ATOM 3481 CD1 LEU B 157 14.127 14.275 22.957 1.00 23.70 B C ATOM 3482 CD2 LEU B 157 16.520 14.776 23.429 1.00 23.26 B C ATOM 3483 C LEU B 157 15.124 15.451 18.670 1.00 20.38 B C ATOM 3484 O LEU B 157 15.166 14.576 17.837 1.00 20.58 B O ATOM 3485 N ASN B 158 15.558 16.669 18.414 1.00 20.57 B N ATOM 3486 CA ASN B 158 16.143 17.009 17.122 1.00 20.45 B C ATOM 3487 CB ASN B 158 16.434 18.523 17.105 1.00 19.60 B C ATOM 3488 CG ASN B 158 16.948 19.017 15.773 1.00 18.40 B C ATOM 3489 OD1 ASN B 158 17.952 19.699 15.705 1.00 17.09 B O ATOM 3490 ND2 ASN B 158 16.260 18.667 14.711 1.00 18.42 B N ATOM 3491 C ASN B 158 15.205 16.580 15.964 1.00 21.47 B C ATOM 3492 O ASN B 158 15.643 15.988 14.948 1.00 21.75 B O ATOM 3493 N GLU B 159 13.923 16.919 16.124 1.00 21.70 B N ATOM 3494 CA GLU B 159 12.856 16.482 15.213 1.00 21.57 B C ATOM 3495 CB GLU B 159 11.542 17.158 15.612 1.00 20.39 B C ATOM 3496 CG GLU B 159 11.355 18.493 14.966 1.00 20.39 B C ATOM 3497 CD GLU B 159 11.302 18.353 13.467 1.00 21.79 B C ATOM 3498 OE1 GLU B 159 10.430 17.542 13.054 1.00 25.14 B O ATOM 3499 OE2 GLU B 159 12.105 18.981 12.712 1.00 20.07 B O ATOM 3500 C GLU B 159 12.692 14.940 15.195 1.00 23.60 B C ATOM 3501 O GLU B 159 12.857 14.289 14.147 1.00 22.28 B O ATOM 3502 N SER B 160 12.393 14.354 16.360 1.00 25.08 B N ATOM 3503 CA SER B 160 12.228 12.906 16.432 1.00 26.35 B C ATOM 3504 CB SER B 160 12.121 12.385 17.864 1.00 26.83 B C ATOM 3505 OG SER B 160 11.919 10.970 17.841 1.00 27.65 B O ATOM 3506 C SER B 160 13.362 12.181 15.740 1.00 26.39 B C ATOM 3507 O SER B 160 13.108 11.202 15.049 1.00 27.56 B O ATOM 3508 N ILE B 161 14.602 12.640 15.906 1.00 25.59 B N ATOM 3509 CA ILE B 161 15.716 11.934 15.265 1.00 25.62 B C ATOM 3510 CB ILE B 161 17.102 12.304 15.858 1.00 25.50 B C ATOM 3511 CG1 ILE B 161 17.410 11.343 17.010 1.00 26.10 B C ATOM 3512 CD1 ILE B 161 18.251 11.934 18.118 1.00 26.54 B C ATOM 3513 CG2 ILE B 161 18.232 12.168 14.845 1.00 25.32 B C ATOM 3514 C ILE B 161 15.633 12.060 13.752 1.00 24.63 B C ATOM 3515 O ILE B 161 15.751 11.057 13.032 1.00 25.26 B O ATOM 3516 N SER B 162 15.393 13.268 13.277 1.00 22.63 B N ATOM 3517 CA SER B 162 15.191 13.452 11.859 1.00 22.29 B C ATOM 3518 CB SER B 162 14.971 14.944 11.505 1.00 22.14 B C ATOM 3519 OG SER B 162 16.160 15.704 11.695 1.00 22.68 B O ATOM 3520 C SER B 162 14.026 12.561 11.365 1.00 21.42 B C ATOM 3521 O SER B 162 14.094 12.053 10.261 1.00 22.43 B O ATOM 3522 N ASP B 163 12.974 12.365 12.159 1.00 20.02 B N ATOM 3523 CA ASP B 163 11.870 11.480 11.757 1.00 20.14 B C ATOM 3524 CB ASP B 163 10.676 11.584 12.721 1.00 19.49 B C ATOM 3525 CG ASP B 163 9.815 12.793 12.467 1.00 18.52 B C ATOM 3526 OD1 ASP B 163 10.121 13.559 11.555 1.00 18.96 B O ATOM 3527 OD2 ASP B 163 8.819 12.979 13.170 1.00 17.18 B O ATOM 3528 C ASP B 163 12.306 10.011 11.726 1.00 21.75 B C ATOM 3529 O ASP B 163 11.987 9.257 10.797 1.00 22.65 B O ATOM 3530 N ILE B 164 13.027 9.594 12.758 1.00 22.58 B N ATOM 3531 CA ILE B 164 13.462 8.207 12.857 1.00 22.48 B C ATOM 3532 CB ILE B 164 14.299 7.988 14.114 1.00 22.54 B C ATOM 3533 CG1 ILE B 164 13.386 8.005 15.345 1.00 23.45 B C ATOM 3534 CD1 ILE B 164 14.066 8.416 16.632 1.00 23.65 B C ATOM 3535 CG2 ILE B 164 15.030 6.663 14.047 1.00 21.95 B C ATOM 3536 C ILE B 164 14.258 7.827 11.634 1.00 22.72 B C ATOM 3537 O ILE B 164 14.064 6.750 11.049 1.00 23.59 B O ATOM 3538 N ILE B 165 15.145 8.718 11.229 1.00 23.05 B N ATOM 3539 CA ILE B 165 16.010 8.405 10.127 1.00 23.88 B C ATOM 3540 CB ILE B 165 17.296 9.240 10.153 1.00 25.46 B C ATOM 3541 CG1 ILE B 165 18.236 8.725 11.258 1.00 25.84 B C ATOM 3542 CD1 ILE B 165 19.692 9.093 11.047 1.00 25.86 B C ATOM 3543 CG2 ILE B 165 17.987 9.179 8.793 1.00 26.66 B C ATOM 3544 C ILE B 165 15.281 8.569 8.814 1.00 23.03 B C ATOM 3545 O ILE B 165 15.446 7.770 7.914 1.00 23.61 B O ATOM 3546 N GLY B 166 14.475 9.601 8.693 1.00 22.77 B N ATOM 3547 CA GLY B 166 13.811 9.838 7.437 1.00 23.61 B C ATOM 3548 C GLY B 166 12.910 8.666 7.100 1.00 24.48 B C ATOM 3549 O GLY B 166 12.834 8.213 5.949 1.00 24.77 B O ATOM 3550 N ASN B 167 12.218 8.185 8.122 1.00 24.92 B N ATOM 3551 CA ASN B 167 11.332 7.061 7.974 1.00 25.37 B C ATOM 3552 CB ASN B 167 10.538 6.834 9.250 1.00 25.09 B C ATOM 3553 CG ASN B 167 9.722 5.578 9.179 1.00 24.84 B C ATOM 3554 OD1 ASN B 167 8.663 5.557 8.554 1.00 24.32 B O ATOM 3555 ND2 ASN B 167 10.223 4.509 9.792 1.00 25.27 B N ATOM 3556 C ASN B 167 12.098 5.789 7.648 1.00 25.52 B C ATOM 3557 O ASN B 167 11.629 4.960 6.876 1.00 27.09 B O ATOM 3558 N ALA B 168 13.262 5.636 8.258 1.00 25.33 B N ATOM 3559 CA ALA B 168 14.077 4.456 8.054 1.00 26.46 B C ATOM 3560 CB ALA B 168 15.209 4.423 9.078 1.00 26.58 B C ATOM 3561 C ALA B 168 14.627 4.372 6.633 1.00 27.05 B C ATOM 3562 O ALA B 168 14.769 3.305 6.099 1.00 25.94 B O ATOM 3563 N ILE B 169 14.948 5.496 6.021 1.00 30.59 B N ATOM 3564 CA ILE B 169 15.426 5.488 4.640 1.00 34.83 B C ATOM 3565 CB ILE B 169 15.783 6.925 4.196 1.00 37.29 B C ATOM 3566 CG1 ILE B 169 17.197 7.244 4.697 1.00 40.64 B C ATOM 3567 CD1 ILE B 169 17.388 8.660 5.177 1.00 41.49 B C ATOM 3568 CG2 ILE B 169 15.710 7.094 2.681 1.00 36.37 B C ATOM 3569 C ILE B 169 14.388 4.882 3.715 1.00 36.99 B C ATOM 3570 O ILE B 169 14.662 3.984 2.918 1.00 33.86 B O ATOM 3571 N ASP B 170 13.186 5.413 3.841 1.00 43.53 B N ATOM 3572 CA ASP B 170 12.072 5.011 3.016 1.00 48.08 B C ATOM 3573 CB ASP B 170 10.814 5.803 3.463 1.00 51.67 B C ATOM 3574 CG ASP B 170 9.755 5.980 2.344 1.00 52.92 B C ATOM 3575 OD1 ASP B 170 9.729 5.192 1.351 1.00 50.54 B O ATOM 3576 OD2 ASP B 170 8.931 6.919 2.499 1.00 50.26 B O ATOM 3577 C ASP B 170 11.919 3.483 3.142 1.00 44.26 B C ATOM 3578 O ASP B 170 12.078 2.785 2.164 1.00 43.51 B O ATOM 3579 N GLY B 171 11.672 2.990 4.358 1.00 43.91 B N ATOM 3580 CA GLY B 171 11.467 1.557 4.634 1.00 44.24 B C ATOM 3581 C GLY B 171 10.003 1.160 4.820 1.00 44.95 B C ATOM 3582 O GLY B 171 9.634 0.569 5.831 1.00 43.83 B O ATOM 3583 N LYS B 172 9.194 1.498 3.815 1.00 46.20 B N ATOM 3584 CA LYS B 172 7.749 1.197 3.709 1.00 46.62 B C ATOM 3585 CB LYS B 172 7.096 2.285 2.836 1.00 52.15 B C ATOM 3586 CG LYS B 172 7.272 2.161 1.319 1.00 57.60 B C ATOM 3587 CD LYS B 172 6.481 3.256 0.557 1.00 62.15 B C ATOM 3588 CE LYS B 172 4.946 3.091 0.575 1.00 60.28 B C ATOM 3589 NZ LYS B 172 4.444 1.991 0.304 1.00 61.46 B N ATOM 3590 C LYS B 172 6.850 1.027 4.980 1.00 42.61 B C ATOM 3591 O LYS B 172 6.188 0.001 5.125 1.00 42.17 B O ATOM 3592 N ASN B 173 6.769 2.039 5.854 1.00 36.61 B N ATOM 3593 CA ASN B 173 5.709 2.089 6.899 1.00 30.24 B C ATOM 3594 CB ASN B 173 4.433 2.744 6.350 1.00 28.81 B C ATOM 3595 CG ASN B 173 4.692 4.072 5.650 1.00 29.12 B C ATOM 3596 OD1 ASN B 173 5.413 4.949 6.145 1.00 30.32 B O ATOM 3597 ND2 ASN B 173 4.092 4.228 4.481 1.00 28.75 B N ATOM 3598 C ASN B 173 6.168 2.796 8.164 1.00 26.96 B C ATOM 3599 O ASN B 173 7.342 3.036 8.324 1.00 24.81 B O ATOM 3600 N TRP B 174 5.241 3.078 9.070 1.00 25.49 B N ATOM 3601 CA TRP B 174 5.513 3.837 10.283 1.00 25.26 B C ATOM 3602 CB TRP B 174 4.795 3.193 11.470 1.00 25.93 B C ATOM 3603 CG TRP B 174 5.293 1.836 11.778 1.00 26.89 B C ATOM 3604 CD1 TRP B 174 4.593 0.665 11.679 1.00 26.32 B C ATOM 3605 NE1 TRP B 174 5.397 0.382 12.017 1.00 26.11 B N ATOM 3606 CE2 TRP B 174 6.637 0.087 12.361 1.00 26.19 B C ATOM 3607 CD2 TRP B 174 6.607 1.487 12.217 1.00 26.18 B C ATOM 3608 CE3 TRP B 174 7.761 2.215 12.487 1.00 26.75 B C ATOM 3609 CZ3 TRP B 174 8.904 1.520 12.907 1.00 28.43 B C ATOM 3610 CH2 TRP B 174 8.895 0.122 13.051 1.00 26.84 B C ATOM 3611 CZ2 TRP B 174 7.777 0.606 12.787 1.00 26.52 B C ATOM 3612 C TRP B 174 5.052 5.296 10.209 1.00 24.68 B C ATOM 3613 O TRP B 174 4.843 5.937 11.257 1.00 24.26 B O ATOM 3614 N LEU B 175 4.878 5.827 9.001 1.00 22.75 B N ATOM 3615 CA LEU B 175 4.318 7.160 8.859 1.00 21.88 B C ATOM 3616 CB LEU B 175 3.150 7.131 7.894 1.00 20.46 B C ATOM 3617 CG LEU B 175 2.144 5.994 8.090 1.00 19.93 B C ATOM 3618 CD1 LEU B 175 1.194 5.955 6.916 1.00 20.20 B C ATOM 3619 CD2 LEU B 175 1.336 6.095 9.364 1.00 19.56 B C ATOM 3620 C LEU B 175 5.389 8.154 8.417 1.00 22.98 B C ATOM 3621 O LEU B 175 6.489 7.765 8.000 1.00 23.17 B O ATOM 3622 N ILE B 176 5.065 9.439 8.541 1.00 24.28 B N ATOM 3623 CA ILE B 176 5.893 10.524 7.968 1.00 24.99 B C ATOM 3624 CB ILE B 176 6.531 11.412 9.059 1.00 26.10 B C ATOM 3625 CG1 ILE B 176 7.357 10.570 10.055 1.00 26.43 B C ATOM 3626 CD1 ILE B 176 8.802 10.335 9.660 1.00 26.54 B C ATOM 3627 CG2 ILE B 176 7.375 12.507 8.413 1.00 26.92 B C ATOM 3628 C ILE B 176 5.044 11.412 7.040 1.00 23.20 B C ATOM 3629 O ILE B 176 3.889 11.741 7.341 1.00 21.47 B O ATOM 3630 N GLY B 177 5.620 11.773 5.902 1.00 22.18 B N ATOM 3631 CA GLY B 177 4.925 12.603 4.925 1.00 21.76 B C ATOM 3632 C GLY B 177 3.641 11.978 4.396 1.00 20.91 B C ATOM 3633 O GLY B 177 2.768 12.680 3.908 1.00 19.00 B O ATOM 3634 N ASP B 178 3.528 10.652 4.488 1.00 21.50 B N ATOM 3635 CA ASP B 178 2.352 9.928 3.952 1.00 20.88 B C ATOM 3636 CB ASP B 178 2.447 8.386 4.153 1.00 20.48 B C ATOM 3637 CG ASP B 178 3.764 7.757 3.622 1.00 20.78 B C ATOM 3638 OD1 ASP B 178 4.882 8.233 3.951 1.00 21.09 B O ATOM 3639 OD2 ASP B 178 3.680 6.747 2.891 1.00 20.74 B O ATOM 3640 C ASP B 178 2.109 10.303 2.482 1.00 20.38 B C ATOM 3641 O ASP B 178 0.951 10.556 2.090 1.00 21.24 B O ATOM 3642 N LEU B 179 3.198 10.400 1.711 1.00 18.74 B N ATOM 3643 CA LEU B 179 3.130 10.728 0.287 1.00 18.78 B C ATOM 3644 CB LEU B 179 4.449 10.345 0.395 1.00 18.48 B C ATOM 3645 CG LEU B 179 4.697 8.834 0.495 1.00 18.11 B C ATOM 3646 CD1 LEU B 179 5.946 8.555 1.305 1.00 17.54 B C ATOM 3647 CD2 LEU B 179 3.488 8.118 1.091 1.00 17.78 B C ATOM 3648 C LEU B 179 2.776 12.178 0.103 1.00 18.56 B C ATOM 3649 O LEU B 179 2.211 12.399 1.176 1.00 20.52 B O ATOM 3650 N ILE B 180 3.101 13.155 0.735 1.00 17.63 B N ATOM 3651 CA ILE B 180 2.873 14.586 0.399 1.00 17.04 B C ATOM 3652 CB ILE B 180 4.068 15.475 0.767 1.00 15.77 B C ATOM 3653 CG1 ILE B 180 4.340 15.399 2.264 1.00 15.25 B C ATOM 3654 CD1 ILE B 180 5.519 16.216 2.719 1.00 15.28 B C ATOM 3655 CG2 ILE B 180 5.267 15.102 0.092 1.00 15.84 B C ATOM 3656 C ILE B 180 1.628 15.229 1.033 1.00 17.27 B C ATOM 3657 O ILE B 180 1.215 16.305 0.630 1.00 16.09 B O ATOM 3658 N TYR B 181 1.032 14.546 1.996 1.00 17.64 B N ATOM 3659 CA TYR B 181 0.004 15.128 2.796 1.00 18.26 B C ATOM 3660 CB TYR B 181 0.095 14.544 4.179 1.00 17.80 B C ATOM 3661 CG TYR B 181 0.789 15.211 5.177 1.00 17.24 B C ATOM 3662 CD1 TYR B 181 0.678 16.565 5.429 1.00 16.90 B C ATOM 3663 CE1 TYR B 181 1.461 17.182 6.364 1.00 16.27 B C ATOM 3664 CZ TYR B 181 2.349 16.457 7.064 1.00 16.18 B C ATOM 3665 OH TYR B 181 3.129 17.077 7.986 1.00 16.18 B O ATOM 3666 CE2 TYR B 181 2.477 15.117 6.853 1.00 16.98 B C ATOM 3667 CD2 TYR B 181 1.693 14.495 5.905 1.00 16.99 B C ATOM 3668 C TYR B 181 1.357 14.831 2.207 1.00 20.02 B C ATOM 3669 O TYR B 181 1.564 13.757 1.650 1.00 20.40 B O ATOM 3670 N THR B 182 2.255 15.812 2.327 1.00 22.26 B N ATOM 3671 CA THR B 182 3.651 15.730 1.896 1.00 25.08 B C ATOM 3672 CB THR B 182 4.512 15.160 3.027 1.00 24.99 B C ATOM 3673 OG1 THR B 182 3.846 14.005 3.582 1.00 24.72 B O ATOM 3674 CG2 THR B 182 4.758 16.227 4.105 1.00 24.58 B C ATOM 3675 C THR B 182 3.832 14.850 0.671 1.00 28.60 B C ATOM 3676 O THR B 182 4.283 13.693 0.784 1.00 30.04 B O ATOM 3677 N PRO B 183 3.456 15.368 0.504 1.00 31.17 B N ATOM 3678 CA PRO B 183 3.595 14.570 1.747 1.00 31.48 B C ATOM 3679 CB PRO B 183 3.080 15.521 2.843 1.00 30.90 B C ATOM 3680 CG PRO B 183 3.126 16.903 2.223 1.00 31.55 B C ATOM 3681 CD PRO B 183 2.875 16.701 0.756 1.00 31.17 B C ATOM 3682 C PRO B 183 5.033 14.084 2.022 1.00 29.96 B C ATOM 3683 O PRO B 183 5.213 13.051 2.626 1.00 28.64 B O ATOM 3684 N ASN B 184 6.034 14.795 1.531 1.00 31.82 B N ATOM 3685 CA ASN B 184 7.418 14.330 1.641 1.00 34.54 B C ATOM 3686 CB ASN B 184 8.349 15.531 1.782 1.00 37.59 B C ATOM 3687 CG ASN B 184 8.493 15.958 3.219 1.00 40.66 B C ATOM 3688 OD1 ASN B 184 7.511 16.023 3.964 1.00 43.19 B O ATOM 3689 ND2 ASN B 184 9.726 16.202 3.637 1.00 43.92 B N ATOM 3690 C ASN B 184 7.932 13.407 0.529 1.00 33.21 B C ATOM 3691 O ASN B 184 9.088 13.008 0.557 1.00 31.64 B O ATOM 3692 N THR B 185 7.072 13.065 0.431 1.00 32.76 B N ATOM 3693 CA THR B 185 7.391 12.095 1.489 1.00 29.86 B C ATOM 3694 CB THR B 185 7.364 12.773 2.865 1.00 28.78 B C ATOM 3695 OG1 THR B 185 8.096 14.008 2.838 1.00 26.37 B O ATOM 3696 CG2 THR B 185 7.922 11.871 3.926 1.00 28.45 B C ATOM 3697 C THR B 185 6.331 10.995 1.522 1.00 30.62 B C ATOM 3698 O THR B 185 5.205 11.248 1.957 1.00 29.21 B O ATOM 3699 N PRO B 186 6.666 9.783 1.033 1.00 33.29 B N ATOM 3700 CA PRO B 186 5.722 8.657 1.130 1.00 32.23 B C ATOM 3701 CB PRO B 186 6.304 7.611 0.161 1.00 33.18 B C ATOM 3702 CG PRO B 186 7.766 7.921 0.084 1.00 32.85 B C ATOM 3703 CD PRO B 186 7.839 9.429 0.197 1.00 34.69 B C ATOM 3704 C PRO B 186 5.660 8.066 2.522 1.00 30.17 B C ATOM 3705 O PRO B 186 6.550 8.322 3.337 1.00 28.22 B O ATOM 3706 N GLY B 187 4.596 7.298 2.778 1.00 28.51 B N ATOM 3707 CA GLY B 187 4.409 6.578 4.045 1.00 27.51 B C ATOM 3708 C GLY B 187 3.834 7.367 5.220 1.00 26.61 B C ATOM 3709 O GLY B 187 3.282 6.772 6.151 1.00 24.33 B O ATOM 3710 N ASP B 188 3.956 8.702 5.198 1.00 25.58 B N ATOM 3711 CA ASP B 188 3.484 9.510 6.321 1.00 23.74 B C ATOM 3712 CB ASP B 188 4.340 10.765 6.539 1.00 23.72 B C ATOM 3713 CG ASP B 188 4.212 11.774 5.429 1.00 24.47 B C ATOM 3714 OD1 ASP B 188 3.517 11.480 4.436 1.00 26.68 B O ATOM 3715 OD2 ASP B 188 4.805 12.876 5.549 1.00 23.28 B O ATOM 3716 C ASP B 188 2.006 9.823 6.175 1.00 22.61 B C ATOM 3717 O ASP B 188 1.335 9.343 5.259 1.00 22.22 B O ATOM 3718 N ALA B 189 1.502 10.584 7.135 1.00 22.07 B N ATOM 3719 CA ALA B 189 0.119 10.970 7.179 1.00 21.72 B C ATOM 3720 CB ALA B 189 0.686 9.866 7.814 1.00 21.95 B C ATOM 3721 C ALA B 189 0.063 12.285 7.949 1.00 21.99 B C ATOM 3722 O ALA B 189 0.894 12.860 8.477 1.00 21.72 B O ATOM 3723 N LEU B 190 1.299 12.772 7.982 1.00 22.12 B N ATOM 3724 CA LEU B 190 1.603 14.002 8.679 1.00 22.30 B C ATOM 3725 CB LEU B 190 2.900 14.600 8.147 1.00 21.89 B C ATOM 3726 CG LEU B 190 3.193 16.011 8.652 1.00 21.53 B C ATOM 3727 CD1 LEU B 190 2.019 16.923 8.379 1.00 21.51 B C ATOM 3728 CD2 LEU B 190 4.431 16.549 7.978 1.00 22.08 B C ATOM 3729 C LEU B 190 1.723 13.721 10.171 1.00 23.63 B C ATOM 3730 O LEU B 190 1.127 14.407 11.028 1.00 23.87 B O ATOM 3731 N ARG B 191 2.521 12.709 10.474 1.00 24.40 B N ATOM 3732 CA ARG B 191 2.519 12.133 11.801 1.00 24.81 B C ATOM 3733 CB ARG B 191 3.435 12.925 12.755 1.00 24.95 B C ATOM 3734 CG ARG B 191 4.751 13.372 12.166 1.00 24.69 B C ATOM 3735 CD ARG B 191 5.454 14.478 12.961 1.00 22.98 B C ATOM 3736 NE ARG B 191 6.713 14.712 12.268 1.00 21.71 B N ATOM 3737 CZ ARG B 191 6.947 15.702 11.423 1.00 22.56 B C ATOM 3738 NH1 ARG B 191 6.055 16.663 11.206 1.00 22.99 B N ATOM 3739 NH2 ARG B 191 8.121 15.770 10.827 1.00 24.08 B N ATOM 3740 C ARG B 191 2.815 10.632 11.748 1.00 23.88 B C ATOM 3741 O ARG B 191 3.248 10.103 10.707 1.00 23.94 B O ATOM 3742 N SER B 192 2.488 9.956 12.850 1.00 22.79 B N ATOM 3743 CA SER B 192 2.641 8.514 12.966 1.00 22.71 B C ATOM 3744 CB SER B 192 1.283 7.836 13.169 1.00 22.27 B C ATOM 3745 OG SER B 192 1.397 6.423 12.982 1.00 21.78 B O ATOM 3746 C SER B 192 3.534 8.165 14.134 1.00 22.71 B C ATOM 3747 O SER B 192 3.287 8.605 15.252 1.00 22.91 B O ATOM 3748 N MET B 193 4.548 7.347 13.877 1.00 23.42 B N ATOM 3749 CA MET B 193 5.441 6.863 14.932 1.00 24.44 B C ATOM 3750 CB MET B 193 6.750 6.308 14.362 1.00 24.83 B C ATOM 3751 CG MET B 193 7.378 7.179 13.277 1.00 26.13 B C ATOM 3752 SD MET B 193 9.085 6.776 12.861 1.00 28.08 B S ATOM 3753 CE MET B 193 9.889 7.597 14.223 1.00 28.27 B C ATOM 3754 C MET B 193 4.739 5.779 15.723 1.00 25.15 B C ATOM 3755 O MET B 193 5.018 5.604 16.894 1.00 27.54 B O ATOM 3756 N GLU B 194 3.823 5.059 15.087 1.00 25.44 B N ATOM 3757 CA GLU B 194 3.224 3.908 15.697 1.00 25.92 B C ATOM 3758 CB GLU B 194 2.674 2.962 14.636 1.00 27.83 B C ATOM 3759 CG GLU B 194 1.974 1.743 15.226 1.00 30.63 B C ATOM 3760 CD GLU B 194 0.940 1.142 14.304 1.00 32.59 B C ATOM 3761 OE1 GLU B 194 1.326 0.320 13.455 1.00 33.88 B O ATOM 3762 OE2 GLU B 194 0.256 1.487 14.441 1.00 34.79 B O ATOM 3763 C GLU B 194 2.129 4.387 16.641 1.00 25.90 B C ATOM 3764 O GLU B 194 2.014 3.896 17.758 1.00 26.66 B O ATOM 3765 N ASN B 195 1.333 5.351 16.206 1.00 24.42 B N ATOM 3766 CA ASN B 195 0.279 5.876 17.042 1.00 24.87 B C ATOM 3767 CB ASN B 195 1.032 5.137 16.742 1.00 26.34 B C ATOM 3768 CG ASN B 195 2.250 5.738 17.467 1.00 29.35 B C ATOM 3769 OD1 ASN B 195 2.153 6.336 18.562 1.00 29.51 B O ATOM 3770 ND2 ASN B 195 3.419 5.591 16.834 1.00 31.30 B N ATOM 3771 C ASN B 195 0.196 7.413 16.888 1.00 24.24 B C ATOM 3772 O ASN B 195 0.600 7.933 16.101 1.00 23.20 B O ATOM 3773 N PRO B 196 1.071 8.139 17.621 1.00 24.01 B N ATOM 3774 CA PRO B 196 1.135 9.606 17.577 1.00 23.24 B C ATOM 3775 CB PRO B 196 2.134 9.929 18.685 1.00 23.91 B C ATOM 3776 CG PRO B 196 3.074 8.754 18.693 1.00 23.50 B C ATOM 3777 CD PRO B 196 2.200 7.569 18.399 1.00 23.71 B C ATOM 3778 C PRO B 196 0.185 10.321 17.826 1.00 22.53 B C ATOM 3779 O PRO B 196 0.494 11.282 17.144 1.00 21.13 B O ATOM 3780 N LYS B 197 0.974 9.836 18.774 1.00 23.69 B N ATOM 3781 CA LYS B 197 2.289 10.419 19.040 1.00 24.36 B C ATOM 3782 CB LYS B 197 3.051 9.624 20.106 1.00 26.48 B C ATOM 3783 CG LYS B 197 2.522 9.758 21.531 1.00 28.64 B C ATOM 3784 CD LYS B 197 3.512 9.183 22.540 1.00 30.82 B C ATOM 3785 CE LYS B 197 4.561 10.244 22.886 1.00 33.46 B C ATOM 3786 NZ LYS B 197 5.890 9.721 23.354 1.00 34.43 B N ATOM 3787 C LYS B 197 3.174 10.537 17.792 1.00 23.41 B C ATOM 3788 O LYS B 197 4.038 11.381 17.745 1.00 23.66 B O ATOM 3789 N LEU B 198 2.975 9.712 16.779 1.00 22.98 B N ATOM 3790 CA LEU B 198 3.839 9.773 15.594 1.00 23.36 B C ATOM 3791 CB LEU B 198 3.497 8.658 14.588 1.00 24.55 B C ATOM 3792 CG LEU B 198 4.462 8.316 13.434 1.00 23.95 B C ATOM 3793 CD1 LEU B 198 5.905 8.032 13.877 1.00 22.89 B C ATOM 3794 CD2 LEU B 198 3.851 7.126 12.692 1.00 23.13 B C ATOM 3795 C LEU B 198 3.763 11.120 14.903 1.00 22.24 B C ATOM 3796 O LEU B 198 4.739 11.550 14.277 1.00 20.67 B O ATOM 3797 N TYR B 199 2.609 11.773 15.013 1.00 22.06 B N ATOM 3798 CA TYR B 199 2.432 13.111 14.444 1.00 22.94 B C ATOM 3799 CB TYR B 199 1.500 13.048 13.207 1.00 23.41 B C ATOM 3800 CG TYR B 199 1.901 11.985 12.194 1.00 23.95 B C ATOM 3801 CD1 TYR B 199 3.023 12.148 11.381 1.00 24.19 B C ATOM 3802 CE1 TYR B 199 3.400 11.169 10.474 1.00 24.03 B C ATOM 3803 CZ TYR B 199 2.647 10.011 10.355 1.00 24.37 B C ATOM 3804 OH TYR B 199 3.002 9.038 9.442 1.00 24.91 B O ATOM 3805 CE2 TYR B 199 1.543 9.819 11.152 1.00 24.38 B C ATOM 3806 CD2 TYR B 199 1.181 10.798 12.074 1.00 24.50 B C ATOM 3807 C TYR B 199 1.975 14.168 15.491 1.00 22.26 B C ATOM 3808 O TYR B 199 1.020 14.929 15.276 1.00 21.71 B O ATOM 3809 N ASN B 200 2.689 14.198 16.614 1.00 21.60 B N ATOM 3810 CA ASN B 200 2.589 15.264 17.620 1.00 21.13 B C ATOM 3811 CB ASN B 200 3.209 16.549 17.072 1.00 22.32 B C ATOM 3812 CG ASN B 200 4.606 16.323 16.485 1.00 23.87 B C ATOM 3813 OD1 ASN B 200 5.610 16.490 17.183 1.00 24.05 B O ATOM 3814 ND2 ASN B 200 4.675 15.933 15.190 1.00 24.03 B N ATOM 3815 C ASN B 200 1.163 15.477 18.168 1.00 19.76 B C ATOM 3816 O ASN B 200 0.696 16.607 18.388 1.00 17.76 B O ATOM 3817 N GLN B 201 0.495 14.348 18.381 1.00 18.92 B N ATOM 3818 CA GLN B 201 0.770 14.294 19.088 1.00 19.24 B C ATOM 3819 CB GLN B 201 1.840 13.585 18.250 1.00 17.82 B C ATOM 3820 CG GLN B 201 2.373 14.366 17.083 1.00 16.72 B C ATOM 3821 CD GLN B 201 3.552 13.685 16.459 1.00 16.42 B C ATOM 3822 OE1 GLN B 201 3.450 12.553 16.004 1.00 15.89 B O ATOM 3823 NE2 GLN B 201 4.687 14.371 16.429 1.00 16.72 B N ATOM 3824 C GLN B 201 0.600 13.490 20.369 1.00 20.79 B C ATOM 3825 O GLN B 201 0.009 12.417 20.355 1.00 22.47 B O ATOM 3826 N PRO B 202 1.160 13.970 21.471 1.00 21.98 B N ATOM 3827 CA PRO B 202 1.091 13.132 22.622 1.00 22.64 B C ATOM 3828 CB PRO B 202 1.481 14.079 23.742 1.00 22.77 B C ATOM 3829 CG PRO B 202 2.452 15.019 23.119 1.00 22.83 B C ATOM 3830 CD PRO B 202 2.109 15.080 21.656 1.00 22.57 B C ATOM 3831 C PRO B 202 2.085 11.965 22.505 1.00 24.85 B C ATOM 3832 O PRO B 202 3.127 12.061 21.810 1.00 23.59 B O ATOM 3833 N ASP B 203 1.737 10.880 23.202 1.00 27.61 B N ATOM 3834 CA ASP B 203 2.492 9.640 23.199 1.00 30.45 B C ATOM 3835 CB ASP B 203 1.610 8.492 22.682 1.00 32.67 B C ATOM 3836 CG ASP B 203 0.356 8.294 23.502 1.00 34.23 B C ATOM 3837 OD1 ASP B 203 0.252 8.865 24.613 1.00 36.10 B O ATOM 3838 OD2 ASP B 203 0.534 7.576 23.017 1.00 35.07 B O ATOM 3839 C ASP B 203 3.058 9.284 24.575 1.00 32.33 B C ATOM 3840 O ASP B 203 3.488 8.154 24.772 1.00 32.63 B O ATOM 3841 N ARG B 204 3.032 10.235 25.518 1.00 34.07 B N ATOM 3842 CA ARG B 204 3.744 10.117 26.791 1.00 34.55 B C ATOM 3843 CB ARG B 204 2.943 9.280 27.777 1.00 36.55 B C ATOM 3844 CG ARG B 204 1.516 9.767 27.975 1.00 39.06 B C ATOM 3845 CD ARG B 204 0.877 9.151 29.214 1.00 42.75 B C ATOM 3846 NE ARG B 204 0.412 9.771 29.545 1.00 49.37 B N ATOM 3847 CZ ARG B 204 1.388 9.199 30.267 1.00 53.04 B C ATOM 3848 NH1 ARG B 204 1.253 7.971 30.769 1.00 51.45 B N ATOM 3849 NH2 ARG B 204 2.525 9.858 30.482 1.00 53.50 B N ATOM 3850 C ARG B 204 4.071 11.495 27.408 1.00 36.34 B C ATOM 3851 O ARG B 204 3.251 12.429 27.360 1.00 36.07 B O ATOM 3852 N TYR B 205 5.271 11.592 28.001 1.00 36.40 B N ATOM 3853 CA TYR B 205 5.844 12.829 28.581 1.00 34.16 B C ATOM 3854 CB TYR B 205 7.022 12.465 29.497 1.00 34.62 B C ATOM 3855 CG TYR B 205 7.925 13.612 29.902 1.00 32.64 B C ATOM 3856 CD1 TYR B 205 8.842 14.136 29.001 1.00 32.71 B C ATOM 3857 CE1 TYR B 205 9.685 15.166 29.348 1.00 32.40 B C ATOM 3858 CZ TYR B 205 9.637 15.671 30.619 1.00 32.09 B C ATOM 3859 OH TYR B 205 10.483 16.696 30.926 1.00 29.46 B O ATOM 3860 CE2 TYR B 205 8.743 15.161 31.546 1.00 32.02 B C ATOM 3861 CD2 TYR B 205 7.898 14.132 31.185 1.00 31.56 B C ATOM 3862 C TYR B 205 4.872 13.655 29.394 1.00 32.77 B C ATOM 3863 O TYR B 205 4.928 14.872 29.361 1.00 31.27 B O ATOM 3864 N GLN B 206 3.996 12.993 30.136 1.00 32.81 B N ATOM 3865 CA GLN B 206 3.030 13.715 30.972 1.00 35.21 B C ATOM 3866 CB GLN B 206 2.272 12.841 32.044 1.00 38.64 B C ATOM 3867 CG GLN B 206 2.106 11.308 31.866 1.00 42.08 B C ATOM 3868 CD GLN B 206 3.425 10.488 31.920 1.00 43.10 B C ATOM 3869 OE1 GLN B 206 3.551 9.459 31.249 1.00 44.46 B O ATOM 3870 NE2 GLN B 206 4.410 10.960 32.688 1.00 42.28 B N ATOM 3871 C GLN B 206 2.071 14.536 30.129 1.00 33.13 B C ATOM 3872 O GLN B 206 1.563 15.534 30.607 1.00 35.03 B O ATOM 3873 N ASP B 207 1.855 14.166 28.870 1.00 31.41 B N ATOM 3874 CA ASP B 207 0.906 14.913 28.018 1.00 29.64 B C ATOM 3875 CB ASP B 207 0.053 13.937 27.197 1.00 29.62 B C ATOM 3876 CG ASP B 207 0.970 13.202 28.048 1.00 30.75 B C ATOM 3877 OD1 ASP B 207 1.183 13.628 29.212 1.00 30.64 B O ATOM 3878 OD2 ASP B 207 1.553 12.200 27.561 1.00 30.25 B O ATOM 3879 C ASP B 207 1.556 15.951 27.101 1.00 27.81 B C ATOM 3880 O ASP B 207 0.896 16.513 26.227 1.00 26.27 B O ATOM 3881 N ARG B 208 2.836 16.246 27.312 1.00 26.49 B N ATOM 3882 CA ARG B 208 3.536 17.097 26.368 1.00 24.72 B C ATOM 3883 CB ARG B 208 5.010 17.243 26.708 1.00 24.36 B C ATOM 3884 CG ARG B 208 5.326 17.924 28.024 1.00 24.48 B C ATOM 3885 CD ARG B 208 6.755 17.538 28.400 1.00 25.04 B C ATOM 3886 NE ARG B 208 7.264 18.154 29.617 1.00 24.76 B N ATOM 3887 CZ ARG B 208 6.783 17.933 30.837 1.00 25.11 B C ATOM 3888 NH1 ARG B 208 5.750 17.136 31.060 1.00 25.82 B N ATOM 3889 NH2 ARG B 208 7.337 18.534 31.858 1.00 26.12 B N ATOM 3890 C ARG B 208 2.920 18.451 26.283 1.00 24.48 B C ATOM 3891 O ARG B 208 2.232 18.908 27.185 1.00 25.71 B O ATOM 3892 N TYR B 209 3.188 19.103 25.167 1.00 24.84 B N ATOM 3893 CA TYR B 209 2.840 20.510 25.000 1.00 22.96 B C ATOM 3894 CB TYR B 209 2.724 20.842 23.521 1.00 21.57 B C ATOM 3895 CG TYR B 209 2.520 22.291 23.180 1.00 19.77 B C ATOM 3896 CD1 TYR B 209 1.260 22.868 23.218 1.00 18.75 B C ATOM 3897 CE1 TYR B 209 1.091 24.213 22.858 1.00 18.78 B C ATOM 3898 CZ TYR B 209 2.192 24.978 22.441 1.00 18.01 B C ATOM 3899 OH TYR B 209 2.057 26.288 22.082 1.00 17.53 B O ATOM 3900 CE2 TYR B 209 3.442 24.416 22.391 1.00 18.24 B C ATOM 3901 CD2 TYR B 209 3.603 23.077 22.740 1.00 19.13 B C ATOM 3902 C TYR B 209 3.912 21.351 25.673 1.00 22.56 B C ATOM 3903 O TYR B 209 5.106 21.048 25.608 1.00 21.55 B O ATOM 3904 N THR B 210 3.438 22.421 26.304 1.00 23.19 B N ATOM 3905 CA THR B 210 4.190 23.254 27.246 1.00 21.30 B C ATOM 3906 CB THR B 210 3.509 23.070 28.627 1.00 20.51 B C ATOM 3907 OG1 THR B 210 4.283 22.128 29.351 1.00 19.96 B O ATOM 3908 CG2 THR B 210 3.380 24.329 29.449 1.00 21.23 B C ATOM 3909 C THR B 210 4.291 24.717 26.770 1.00 20.49 B C ATOM 3910 O THR B 210 4.989 25.528 27.385 1.00 22.84 B O ATOM 3911 N GLY B 211 3.622 25.037 25.662 1.00 18.65 B N ATOM 3912 CA GLY B 211 3.502 26.404 25.164 1.00 17.86 B C ATOM 3913 C GLY B 211 4.688 26.812 24.313 1.00 17.46 B C ATOM 3914 O GLY B 211 5.628 26.022 24.134 1.00 17.51 B O ATOM 3915 N PRO B 212 4.664 28.052 23.801 1.00 16.80 B N ATOM 3916 CA PRO B 212 5.780 28.673 23.088 1.00 17.36 B C ATOM 3917 CB PRO B 212 5.594 30.156 23.396 1.00 16.89 B C ATOM 3918 CG PRO B 212 4.113 30.308 23.446 1.00 17.16 B C ATOM 3919 CD PRO B 212 3.604 29.030 24.083 1.00 17.00 B C ATOM 3920 C PRO B 212 5.769 28.494 21.573 1.00 18.49 B C ATOM 3921 O PRO B 212 6.773 28.798 20.908 1.00 19.01 B O ATOM 3922 N SER B 213 4.645 28.019 21.056 1.00 18.86 B N ATOM 3923 CA SER B 213 4.391 27.910 19.645 1.00 19.95 B C ATOM 3924 CB SER B 213 2.881 27.698 19.495 1.00 22.65 B C ATOM 3925 OG SER B 213 2.471 27.825 18.161 1.00 26.25 B O ATOM 3926 C SER B 213 5.168 26.724 19.078 1.00 18.23 B C ATOM 3927 O SER B 213 5.345 25.770 19.779 1.00 16.91 B O ATOM 3928 N ASP B 214 5.635 26.785 17.824 1.00 18.11 B N ATOM 3929 CA ASP B 214 6.440 25.689 17.227 1.00 17.78 B C ATOM 3930 CB ASP B 214 5.596 24.409 17.164 1.00 17.90 B C ATOM 3931 CG ASP B 214 6.244 23.295 16.378 1.00 17.76 B C ATOM 3932 OD1 ASP B 214 7.112 23.546 15.494 1.00 18.10 B O ATOM 3933 OD2 ASP B 214 5.857 22.141 16.651 1.00 17.17 B O ATOM 3934 C ASP B 214 7.708 25.443 18.049 1.00 18.13 B C ATOM 3935 O ASP B 214 7.986 24.311 18.477 1.00 16.78 B O ATOM 3936 N ASN B 215 8.446 26.527 18.296 1.00 18.96 B N ATOM 3937 CA ASN B 215 9.601 26.515 19.196 1.00 19.63 B C ATOM 3938 CB ASN B 215 10.848 26.092 18.422 1.00 20.32 B C ATOM 3939 CG ASN B 215 11.257 27.138 17.405 1.00 20.81 B C ATOM 3940 OD1 ASN B 215 11.299 28.333 17.713 1.00 21.24 B O ATOM 3941 ND2 ASN B 215 11.492 26.715 16.188 1.00 21.02 B N ATOM 3942 C ASN B 215 9.354 25.645 20.420 1.00 20.01 B C ATOM 3943 O ASN B 215 10.137 24.759 20.766 1.00 20.66 B O ATOM 3944 N GLY B 216 8.219 25.896 21.058 1.00 20.01 B N ATOM 3945 CA GLY B 216 7.796 25.146 22.226 1.00 19.24 B C ATOM 3946 C GLY B 216 7.633 23.662 21.985 1.00 18.69 B C ATOM 3947 O GLY B 216 8.297 22.859 22.638 1.00 18.64 B O ATOM 3948 N GLY B 217 6.775 23.303 21.030 1.00 18.39 B N ATOM 3949 CA GLY B 217 6.297 21.910 20.845 1.00 18.17 B C ATOM 3950 C GLY B 217 7.079 20.998 19.908 1.00 17.90 B C ATOM 3951 O GLY B 217 6.747 19.836 19.739 1.00 18.36 B O ATOM 3952 N VAL B 218 8.082 21.542 19.248 1.00 18.00 B N ATOM 3953 CA VAL B 218 9.075 20.757 18.535 1.00 18.49 B C ATOM 3954 CB VAL B 218 9.978 21.757 17.786 1.00 18.67 B C ATOM 3955 CG1 VAL B 218 10.669 21.159 16.609 1.00 19.04 B C ATOM 3956 CG2 VAL B 218 11.017 22.288 18.752 1.00 19.24 B C ATOM 3957 C VAL B 218 8.520 19.593 17.660 1.00 19.13 B C ATOM 3958 O VAL B 218 9.025 18.488 17.723 1.00 18.61 B O ATOM 3959 N HIS B 219 7.480 19.833 16.865 1.00 19.66 B N ATOM 3960 CA HIS B 219 6.885 18.786 16.037 1.00 19.59 B C ATOM 3961 CB HIS B 219 6.449 19.301 14.641 1.00 20.15 B C ATOM 3962 CG HIS B 219 7.529 19.983 13.848 1.00 19.47 B C ATOM 3963 ND1 HIS B 219 7.816 21.327 13.979 1.00 19.54 B N ATOM 3964 CE1 HIS B 219 8.807 21.643 13.163 1.00 19.59 B C ATOM 3965 NE2 HIS B 219 9.158 20.559 12.494 1.00 18.98 B N ATOM 3966 CD2 HIS B 219 8.361 19.513 12.891 1.00 19.03 B C ATOM 3967 C HIS B 219 5.658 18.243 16.725 1.00 20.25 B C ATOM 3968 O HIS B 219 5.105 17.241 16.283 1.00 20.29 B O ATOM 3969 N ILE B 220 5.171 18.915 17.766 1.00 21.20 B N ATOM 3970 CA ILE B 220 4.097 18.309 18.566 1.00 21.97 B C ATOM 3971 CB ILE B 220 3.375 19.323 19.457 1.00 22.68 B C ATOM 3972 CG1 ILE B 220 2.724 20.393 18.595 1.00 23.99 B C ATOM 3973 CD1 ILE B 220 2.178 21.553 19.404 1.00 24.68 B C ATOM 3974 CG2 ILE B 220 2.293 18.655 20.293 1.00 22.37 B C ATOM 3975 C ILE B 220 4.698 17.207 19.426 1.00 22.02 B C ATOM 3976 O ILE B 220 4.261 16.068 19.344 1.00 23.21 B O ATOM 3977 N ASN B 221 5.724 17.545 20.209 1.00 20.75 B N ATOM 3978 CA ASN B 221 6.311 16.624 21.182 1.00 20.24 B C ATOM 3979 CB ASN B 221 6.996 17.406 22.300 1.00 18.70 B C ATOM 3980 CG ASN B 221 6.009 18.178 23.149 1.00 17.72 B C ATOM 3981 OD1 ASN B 221 4.883 17.752 23.379 1.00 17.36 B O ATOM 3982 ND2 ASN B 221 6.425 19.321 23.609 1.00 16.99 B N ATOM 3983 C ASN B 221 7.291 15.582 20.631 1.00 21.78 B C ATOM 3984 O ASN B 221 7.719 14.705 21.386 1.00 21.93 B O ATOM 3985 N SER B 222 7.651 15.633 19.346 1.00 22.00 B N ATOM 3986 CA SER B 222 8.578 14.633 18.860 1.00 22.02 B C ATOM 3987 CB SER B 222 9.109 14.959 17.466 1.00 22.44 B C ATOM 3988 OG SER B 222 8.090 15.068 16.478 1.00 23.22 B O ATOM 3989 C SER B 222 7.852 13.297 18.931 1.00 23.31 B C ATOM 3990 O SER B 222 8.481 12.230 19.024 1.00 22.58 B O ATOM 3991 N GLY B 223 6.516 13.371 18.945 1.00 24.52 B N ATOM 3992 CA GLY B 223 5.651 12.186 19.052 1.00 25.84 B C ATOM 3993 C GLY B 223 6.008 11.231 20.177 1.00 26.96 B C ATOM 3994 O GLY B 223 5.884 10.001 20.034 1.00 28.19 B O ATOM 3995 N ILE B 224 6.437 11.809 21.296 1.00 26.49 B N ATOM 3996 CA ILE B 224 6.923 11.057 22.459 1.00 25.44 B C ATOM 3997 CB ILE B 224 7.187 12.011 23.637 1.00 24.70 B C ATOM 3998 CG1 ILE B 224 5.849 12.487 24.198 1.00 24.83 B C ATOM 3999 CD1 ILE B 224 5.956 13.782 24.968 1.00 25.47 B C ATOM 4000 CG2 ILE B 224 8.002 11.327 24.720 1.00 24.67 B C ATOM 4001 C ILE B 224 8.172 10.209 22.179 1.00 24.64 B C ATOM 4002 O ILE B 224 8.209 9.029 22.468 1.00 25.66 B O ATOM 4003 N ASN B 225 9.212 10.798 21.637 1.00 24.78 B N ATOM 4004 CA ASN B 225 10.377 10.011 21.335 1.00 24.71 B C ATOM 4005 CB ASN B 225 11.549 10.903 20.978 1.00 24.55 B C ATOM 4006 CG ASN B 225 12.869 10.188 21.126 1.00 24.56 B C ATOM 4007 OD1 ASN B 225 13.625 9.979 20.164 1.00 23.26 B O ATOM 4008 ND2 ASN B 225 13.143 9.775 22.347 1.00 25.30 B N ATOM 4009 C ASN B 225 10.097 9.051 20.188 1.00 25.63 B C ATOM 4010 O ASN B 225 10.577 7.922 20.188 1.00 25.70 B O ATOM 4011 N ASN B 226 9.321 9.494 19.204 1.00 26.62 B N ATOM 4012 CA ASN B 226 8.969 8.608 18.104 1.00 26.81 B C ATOM 4013 CB ASN B 226 8.135 9.330 17.035 1.00 27.03 B C ATOM 4014 CG ASN B 226 8.963 10.256 16.156 1.00 27.23 B C ATOM 4015 OD1 ASN B 226 10.195 10.313 16.254 1.00 26.96 B O ATOM 4016 ND2 ASN B 226 8.277 11.001 15.289 1.00 27.06 B N ATOM 4017 C ASN B 226 8.243 7.340 18.594 1.00 26.48 B C ATOM 4018 O ASN B 226 8.512 6.254 18.096 1.00 28.43 B O ATOM 4019 N LYS B 227 7.343 7.458 19.558 1.00 24.83 B N ATOM 4020 CA LYS B 227 6.685 6.271 20.081 1.00 25.45 B C ATOM 4021 CB LYS B 227 5.631 6.652 21.096 1.00 25.83 B C ATOM 4022 CG LYS B 227 4.834 5.495 21.646 1.00 25.86 B C ATOM 4023 CD LYS B 227 3.856 4.952 20.632 1.00 27.34 B C ATOM 4024 CE LYS B 227 3.290 3.619 21.118 1.00 28.38 B C ATOM 4025 NZ LYS B 227 2.147 3.154 20.291 1.00 28.32 B N ATOM 4026 C LYS B 227 7.675 5.333 20.742 1.00 26.25 B C ATOM 4027 O LYS B 227 7.581 4.130 20.580 1.00 27.67 B O ATOM 4028 N ALA B 228 8.605 5.884 21.509 1.00 26.38 B N ATOM 4029 CA ALA B 228 9.669 5.091 22.101 1.00 26.22 B C ATOM 4030 CB ALA B 228 10.670 5.974 22.840 1.00 26.76 B C ATOM 4031 C ALA B 228 10.387 4.320 21.027 1.00 26.05 B C ATOM 4032 O ALA B 228 10.645 3.149 21.190 1.00 28.08 B O ATOM 4033 N PHE B 229 10.725 4.969 19.926 1.00 25.85 B N ATOM 4034 CA PHE B 229 11.412 4.266 18.853 1.00 25.93 B C ATOM 4035 CB PHE B 229 11.755 5.203 17.712 1.00 25.94 B C ATOM 4036 CG PHE B 229 12.518 4.533 16.642 1.00 26.06 B C ATOM 4037 CD1 PHE B 229 13.890 4.407 16.748 1.00 26.92 B C ATOM 4038 CE1 PHE B 229 14.620 3.758 15.766 1.00 27.95 B C ATOM 4039 CZ PHE B 229 13.963 3.228 14.661 1.00 27.83 B C ATOM 4040 CE2 PHE B 229 12.580 3.341 14.562 1.00 27.45 B C ATOM 4041 CD2 PHE B 229 11.868 3.985 15.551 1.00 26.96 B C ATOM 4042 C PHE B 229 10.626 3.063 18.313 1.00 25.50 B C ATOM 4043 O PHE B 229 11.162 1.968 18.214 1.00 26.44 B O ATOM 4044 N TYR B 230 9.362 3.262 17.970 1.00 25.44 B N ATOM 4045 CA TYR B 230 8.488 2.153 17.546 1.00 26.60 B C ATOM 4046 CB TYR B 230 7.055 2.645 17.394 1.00 26.50 B C ATOM 4047 CG TYR B 230 6.057 1.545 17.152 1.00 26.33 B C ATOM 4048 CD1 TYR B 230 5.980 0.908 15.912 1.00 25.76 B C ATOM 4049 CE1 TYR B 230 5.055 0.087 15.667 1.00 25.25 B C ATOM 4050 CZ TYR B 230 4.191 0.458 16.664 1.00 26.43 B C ATOM 4051 OH TYR B 230 3.275 1.445 16.431 1.00 27.30 B O ATOM 4052 CE2 TYR B 230 4.237 0.160 17.903 1.00 27.11 B C ATOM 4053 CD2 TYR B 230 5.181 1.149 18.146 1.00 26.74 B C ATOM 4054 C TYR B 230 8.455 0.948 18.499 1.00 26.53 B C ATOM 4055 O TYR B 230 8.456 0.196 18.050 1.00 26.33 B O ATOM 4056 N LEU B 231 8.386 1.221 19.798 1.00 26.27 B N ATOM 4057 CA LEU B 231 8.373 0.180 20.809 1.00 26.57 B C ATOM 4058 CB LEU B 231 8.041 0.775 22.171 1.00 25.37 B C ATOM 4059 CG LEU B 231 6.568 1.208 22.262 1.00 25.50 B C ATOM 4060 CD1 LEU B 231 6.257 2.057 23.476 1.00 25.18 B C ATOM 4061 CD2 LEU B 231 5.657 0.007 22.268 1.00 26.56 B C ATOM 4062 C LEU B 231 9.705 0.574 20.817 1.00 28.83 B C ATOM 4063 O LEU B 231 9.743 1.805 20.856 1.00 30.14 B O ATOM 4064 N ILE B 232 10.799 0.156 20.705 1.00 29.54 B N ATOM 4065 CA ILE B 232 12.115 0.458 20.640 1.00 29.21 B C ATOM 4066 CB ILE B 232 13.197 0.634 20.677 1.00 28.64 B C ATOM 4067 CG1 ILE B 232 13.234 1.247 22.084 1.00 29.59 B C ATOM 4068 CD1 ILE B 232 14.053 2.517 22.206 1.00 29.92 B C ATOM 4069 CG2 ILE B 232 14.561 0.084 20.291 1.00 28.76 B C ATOM 4070 C ILE B 232 12.269 1.291 19.374 1.00 30.72 B C ATOM 4071 O ILE B 232 13.009 2.273 19.340 1.00 33.34 B O ATOM 4072 N ALA B 233 11.595 0.888 18.309 1.00 31.94 B N ATOM 4073 CA ALA B 233 11.820 1.522 17.007 1.00 30.90 B C ATOM 4074 CB ALA B 233 11.604 0.509 15.900 1.00 31.09 B C ATOM 4075 C ALA B 233 10.896 2.715 16.829 1.00 29.25 B C ATOM 4076 O ALA B 233 11.338 3.839 16.703 1.00 26.84 B O ATOM 4077 N GLN B 234 9.601 2.438 16.850 1.00 28.21 B N ATOM 4078 CA GLN B 234 8.605 3.442 16.643 1.00 27.52 B C ATOM 4079 CB GLN B 234 7.332 2.775 16.136 1.00 27.99 B C ATOM 4080 CG GLN B 234 6.297 3.757 15.629 1.00 27.70 B C ATOM 4081 CD GLN B 234 6.901 4.805 14.703 1.00 27.94 B C ATOM 4082 OE1 GLN B 234 7.897 4.556 13.997 1.00 27.32 B O ATOM 4083 NE2 GLN B 234 6.301 5.988 14.702 1.00 27.80 B N ATOM 4084 C GLN B 234 8.257 4.222 17.892 1.00 27.94 B C ATOM 4085 O GLN B 234 7.823 5.377 17.791 1.00 28.34 B O ATOM 4086 N GLY B 235 8.417 3.590 19.059 1.00 27.37 B N ATOM 4087 CA GLY B 235 7.817 4.077 20.296 1.00 25.77 B C ATOM 4088 C GLY B 235 6.345 3.708 20.328 1.00 25.72 B C ATOM 4089 O GLY B 235 5.740 3.433 19.292 1.00 25.36 B O ATOM 4090 N GLY B 236 5.769 3.700 21.523 1.00 25.94 B N ATOM 4091 CA GLY B 236 4.350 3.423 21.698 1.00 26.60 B C ATOM 4092 C GLY B 236 4.044 3.322 23.177 1.00 28.63 B C ATOM 4093 O GLY B 236 4.919 3.572 24.017 1.00 29.26 B O ATOM 4094 N THR B 237 2.801 2.970 23.485 1.00 29.75 B N ATOM 4095 CA THR B 237 2.327 2.831 24.842 1.00 31.58 B C ATOM 4096 CB THR B 237 1.327 3.962 25.206 1.00 33.98 B C ATOM 4097 OG1 THR B 237 2.063 5.104 25.633 1.00 37.98 B O ATOM 4098 CG2 THR B 237 0.360 3.594 26.356 1.00 34.58 B C ATOM 4099 C THR B 237 1.650 1.496 24.899 1.00 34.03 B C ATOM 4100 O THR B 237 0.632 1.298 24.230 1.00 34.87 B O ATOM 4101 N HIS B 238 2.184 0.602 25.731 1.00 36.70 B N ATOM 4102 CA HIS B 238 1.747 0.790 25.793 1.00 37.24 B C ATOM 4103 CB HIS B 238 2.711 1.577 24.898 1.00 42.00 B C ATOM 4104 CG HIS B 238 2.361 3.020 24.728 1.00 43.70 B C ATOM 4105 ND1 HIS B 238 3.268 4.030 24.968 1.00 43.48 B N ATOM 4106 CE1 HIS B 238 2.691 5.194 24.734 1.00 46.45 B C ATOM 4107 NE2 HIS B 238 1.445 4.974 24.351 1.00 47.60 B N ATOM 4108 CD2 HIS B 238 1.213 3.620 24.335 1.00 45.16 B C ATOM 4109 C HIS B 238 1.769 1.323 27.239 1.00 35.71 B C ATOM 4110 O HIS B 238 2.832 1.322 27.876 1.00 31.39 B O ATOM 4111 N TYR B 239 0.616 1.798 27.743 1.00 37.49 B N ATOM 4112 CA TYR B 239 0.431 2.163 29.201 1.00 39.68 B C ATOM 4113 CB TYR B 239 0.973 3.577 29.559 1.00 38.30 B C ATOM 4114 CG TYR B 239 0.280 4.661 28.775 1.00 36.05 B C ATOM 4115 CD1 TYR B 239 1.087 4.867 28.915 1.00 36.03 B C ATOM 4116 CE1 TYR B 239 1.755 5.830 28.174 1.00 36.29 B C ATOM 4117 CZ TYR B 239 1.042 6.605 27.259 1.00 37.19 B C ATOM 4118 OH TYR B 239 1.707 7.570 26.501 1.00 34.74 B O ATOM 4119 CE2 TYR B 239 0.333 6.403 27.104 1.00 36.29 B C ATOM 4120 CD2 TYR B 239 0.975 5.433 27.855 1.00 35.25 B C ATOM 4121 C TYR B 239 1.026 1.116 30.152 1.00 41.11 B C ATOM 4122 O TYR B 239 2.046 1.350 30.818 1.00 40.61 B O ATOM 4123 N GLY B 240 0.401 0.057 30.164 1.00 42.40 B N ATOM 4124 CA GLY B 240 0.862 1.165 30.985 1.00 43.82 B C ATOM 4125 C GLY B 240 2.136 1.887 30.549 1.00 42.06 B C ATOM 4126 O GLY B 240 2.231 3.116 30.685 1.00 42.31 B O ATOM 4127 N VAL B 241 3.121 1.152 30.047 1.00 38.05 B N ATOM 4128 CA VAL B 241 4.450 1.724 29.817 1.00 37.68 B C ATOM 4129 CB VAL B 241 5.488 0.599 29.856 1.00 35.77 B C ATOM 4130 CG1 VAL B 241 6.907 1.130 29.740 1.00 34.09 B C ATOM 4131 CG2 VAL B 241 5.277 0.194 31.139 1.00 35.98 B C ATOM 4132 C VAL B 241 4.524 2.586 28.519 1.00 38.81 B C ATOM 4133 O VAL B 241 3.917 2.253 27.499 1.00 39.08 B O ATOM 4134 N THR B 242 5.204 3.732 28.605 1.00 38.22 B N ATOM 4135 CA THR B 242 5.407 4.614 27.465 1.00 38.17 B C ATOM 4136 CB THR B 242 5.044 6.083 27.805 1.00 37.28 B C ATOM 4137 OG1 THR B 242 3.630 6.233 27.717 1.00 38.40 B O ATOM 4138 CG2 THR B 242 5.670 7.096 26.838 1.00 36.94 B C ATOM 4139 C THR B 242 6.865 4.458 27.034 1.00 39.27 B C ATOM 4140 O THR B 242 7.788 4.557 27.851 1.00 39.33 B O ATOM 4141 N VAL B 243 7.064 4.176 25.752 1.00 38.72 B N ATOM 4142 CA VAL B 243 8.396 4.046 25.213 1.00 38.15 B C ATOM 4143 CB VAL B 243 8.615 2.696 24.551 1.00 36.94 B C ATOM 4144 CG1 VAL B 243 10.085 2.522 24.211 1.00 37.69 B C ATOM 4145 CG2 VAL B 243 8.171 1.598 25.492 1.00 39.28 B C ATOM 4146 C VAL B 243 8.566 5.090 24.162 1.00 39.74 B C ATOM 4147 O VAL B 243 7.658 5.304 23.362 1.00 40.60 B O ATOM 4148 N ASN B 244 9.727 5.736 24.174 1.00 40.74 B N ATOM 4149 CA ASN B 244 10.041 6.753 23.201 1.00 40.96 B C ATOM 4150 CB ASN B 244 10.781 7.919 23.855 1.00 43.87 B C ATOM 4151 CG ASN B 244 9.999 8.560 25.011 1.00 47.13 B C ATOM 4152 OD1 ASN B 244 8.756 8.572 25.061 1.00 44.34 B O ATOM 4153 ND2 ASN B 244 10.748 9.112 25.957 1.00 51.75 B N ATOM 4154 C ASN B 244 10.921 6.076 22.180 1.00 38.39 B C ATOM 4155 O ASN B 244 11.998 5.629 22.522 1.00 40.30 B O ATOM 4156 N GLY B 245 10.462 5.995 20.936 1.00 34.92 B N ATOM 4157 CA GLY B 245 11.194 5.303 19.883 1.00 33.21 B C ATOM 4158 C GLY B 245 12.547 5.921 19.615 1.00 31.52 B C ATOM 4159 O GLY B 245 12.741 7.104 19.850 1.00 32.30 B O ATOM 4160 N ILE B 246 13.476 5.110 19.122 1.00 30.79 B N ATOM 4161 CA ILE B 246 14.800 5.578 18.734 1.00 31.70 B C ATOM 4162 CB ILE B 246 15.907 4.792 19.467 1.00 34.63 B C ATOM 4163 CG1 ILE B 246 15.952 3.312 19.041 1.00 35.25 B C ATOM 4164 CD1 ILE B 246 17.373 2.797 18.876 1.00 34.91 B C ATOM 4165 CG2 ILE B 246 15.708 4.884 20.976 1.00 35.49 B C ATOM 4166 C ILE B 246 15.056 5.495 17.231 1.00 31.36 B C ATOM 4167 O ILE B 246 16.153 5.815 16.784 1.00 29.30 B O ATOM 4168 N GLY B 247 14.038 5.076 16.469 1.00 33.15 B N ATOM 4169 CA GLY B 247 14.103 4.926 15.007 1.00 33.39 B C ATOM 4170 C GLY B 247 14.360 3.484 14.662 1.00 34.14 B C ATOM 4171 O GLY B 247 14.673 2.715 15.550 1.00 38.81 B O ATOM 4172 N ARG B 248 14.221 3.094 13.398 1.00 35.49 B N ATOM 4173 CA ARG B 248 14.521 1.701 13.019 1.00 34.52 B C ATOM 4174 CB ARG B 248 13.898 1.291 11.678 1.00 34.54 B C ATOM 4175 CG ARG B 248 12.394 1.119 11.670 1.00 33.03 B C ATOM 4176 CD ARG B 248 11.942 0.463 10.370 1.00 31.42 B C ATOM 4177 NE ARG B 248 10.484 0.407 10.297 1.00 30.41 B N ATOM 4178 CZ ARG B 248 9.772 0.522 9.665 1.00 30.13 B C ATOM 4179 NH1 ARG B 248 10.351 1.520 9.018 1.00 32.14 B N ATOM 4180 NH2 ARG B 248 8.455 0.457 9.676 1.00 29.38 B N ATOM 4181 C ARG B 248 16.014 1.528 12.922 1.00 34.18 B C ATOM 4182 O ARG B 248 16.606 0.839 13.724 1.00 35.53 B O ATOM 4183 N ASP B 249 16.620 2.168 11.935 1.00 35.34 B N ATOM 4184 CA ASP B 249 18.020 1.933 11.609 1.00 37.30 B C ATOM 4185 CB ASP B 249 18.584 3.108 10.808 1.00 39.37 B C ATOM 4186 CG ASP B 249 18.039 3.154 9.404 1.00 40.69 B C ATOM 4187 OD1 ASP B 249 18.225 2.155 8.689 1.00 41.67 B O ATOM 4188 OD2 ASP B 249 17.424 4.177 9.012 1.00 43.16 B O ATOM 4189 C ASP B 249 18.900 1.649 12.835 1.00 36.02 B C ATOM 4190 O ASP B 249 19.690 0.703 12.830 1.00 35.49 B O ATOM 4191 N ALA B 250 18.764 2.454 13.876 1.00 33.52 B N ATOM 4192 CA ALA B 250 19.556 2.228 15.067 1.00 34.12 B C ATOM 4193 CB ALA B 250 19.554 3.465 15.932 1.00 34.74 B C ATOM 4194 C ALA B 250 19.078 1.005 15.872 1.00 34.00 B C ATOM 4195 O ALA B 250 19.898 0.291 16.453 1.00 33.32 B O ATOM 4196 N ALA B 251 17.764 0.775 15.914 1.00 33.23 B N ATOM 4197 CA ALA B 251 17.192 0.376 16.634 1.00 32.65 B C ATOM 4198 CB ALA B 251 15.680 0.332 16.595 1.00 31.92 B C ATOM 4199 C ALA B 251 17.699 1.735 16.145 1.00 33.52 B C ATOM 4200 O ALA B 251 18.037 2.579 16.969 1.00 33.05 B O ATOM 4201 N VAL B 252 17.778 1.946 14.827 1.00 34.61 B N ATOM 4202 CA VAL B 252 18.321 3.223 14.299 1.00 37.23 B C ATOM 4203 CB VAL B 252 18.148 3.454 12.757 1.00 38.13 B C ATOM 4204 CG1 VAL B 252 16.734 3.132 12.298 1.00 39.21 B C ATOM 4205 CG2 VAL B 252 19.148 2.657 11.925 1.00 39.85 B C ATOM 4206 C VAL B 252 19.791 3.316 14.626 1.00 38.70 B C ATOM 4207 O VAL B 252 20.309 4.393 14.881 1.00 42.70 B O ATOM 4208 N GLN B 253 20.458 2.170 14.596 1.00 39.66 B N ATOM 4209 CA GLN B 253 21.882 2.101 14.842 1.00 38.93 B C ATOM 4210 CB GLN B 253 22.363 0.650 14.690 1.00 39.08 B C ATOM 4211 CG GLN B 253 23.849 0.455 14.817 1.00 38.82 B C ATOM 4212 CD GLN B 253 24.597 1.398 13.925 1.00 40.50 B C ATOM 4213 OE1 GLN B 253 25.255 2.330 14.399 1.00 41.81 B O ATOM 4214 NE2 GLN B 253 24.472 1.195 12.621 1.00 39.98 B N ATOM 4215 C GLN B 253 22.146 2.631 16.242 1.00 38.11 B C ATOM 4216 O GLN B 253 23.110 3.345 16.462 1.00 39.28 B O ATOM 4217 N ILE B 254 21.255 2.307 17.171 1.00 37.48 B N ATOM 4218 CA ILE B 254 21.358 2.789 18.537 1.00 37.65 B C ATOM 4219 CB ILE B 254 20.279 2.163 19.426 1.00 37.54 B C ATOM 4220 CG1 ILE B 254 20.665 0.718 19.712 1.00 38.79 B C ATOM 4221 CD1 ILE B 254 19.526 0.104 20.271 1.00 40.86 B C ATOM 4222 CG2 ILE B 254 20.068 2.972 20.714 1.00 36.04 B C ATOM 4223 C ILE B 254 21.210 4.292 18.625 1.00 38.14 B C ATOM 4224 O ILE B 254 21.986 4.948 19.323 1.00 38.29 B O ATOM 4225 N PHE B 255 20.194 4.825 17.950 1.00 37.29 B N ATOM 4226 CA PHE B 255 19.928 6.270 17.980 1.00 35.20 B C ATOM 4227 CB PHE B 255 18.526 6.589 17.464 1.00 34.13 B C ATOM 4228 CG PHE B 255 17.464 6.328 18.483 1.00 33.10 B C ATOM 4229 CD1 PHE B 255 16.910 5.080 18.618 1.00 33.11 B C ATOM 4230 CE1 PHE B 255 15.939 4.847 19.585 1.00 34.35 B C ATOM 4231 CZ PHE B 255 15.532 5.870 20.437 1.00 32.78 B C ATOM 4232 CE2 PHE B 255 16.107 7.110 20.329 1.00 31.36 B C ATOM 4233 CD2 PHE B 255 17.064 7.332 19.355 1.00 32.90 B C ATOM 4234 C PHE B 255 20.993 7.089 17.266 1.00 33.97 B C ATOM 4235 O PHE B 255 21.437 8.090 17.805 1.00 33.61 B O ATOM 4236 N TYR B 256 21.439 6.656 16.091 1.00 33.92 B N ATOM 4237 CA TYR B 256 22.584 7.298 15.444 1.00 33.80 B C ATOM 4238 CB TYR B 256 22.962 6.573 14.186 1.00 32.62 B C ATOM 4239 CG TYR B 256 24.124 7.165 13.423 1.00 32.49 B C ATOM 4240 CD1 TYR B 256 25.450 6.822 13.740 1.00 31.86 B C ATOM 4241 CE1 TYR B 256 26.517 7.342 13.024 1.00 31.32 B C ATOM 4242 CZ TYR B 256 26.269 8.192 11.946 1.00 32.70 B C ATOM 4243 OH TYR B 256 27.318 8.694 11.211 1.00 32.98 B O ATOM 4244 CE2 TYR B 256 24.963 8.522 11.588 1.00 32.52 B C ATOM 4245 CD2 TYR B 256 23.903 8.012 12.328 1.00 32.27 B C ATOM 4246 C TYR B 256 23.783 7.300 16.360 1.00 36.90 B C ATOM 4247 O TYR B 256 24.413 8.325 16.534 1.00 41.30 B O ATOM 4248 N ASP B 257 24.117 6.160 16.951 1.00 39.22 B N ATOM 4249 CA ASP B 257 25.285 6.114 17.840 1.00 40.23 B C ATOM 4250 CB ASP B 257 25.574 4.679 18.327 1.00 42.15 B C ATOM 4251 CG ASP B 257 26.329 3.819 17.279 1.00 43.41 B C ATOM 4252 OD1 ASP B 257 26.693 4.314 16.188 1.00 41.38 B O ATOM 4253 OD2 ASP B 257 26.567 2.623 17.563 1.00 46.53 B O ATOM 4254 C ASP B 257 25.131 7.101 19.013 1.00 38.49 B C ATOM 4255 O ASP B 257 26.062 7.828 19.341 1.00 37.98 B O ATOM 4256 N ALA B 258 23.949 7.150 19.616 1.00 37.63 B N ATOM 4257 CA ALA B 258 23.694 8.082 20.718 1.00 37.54 B C ATOM 4258 CB ALA B 258 22.317 7.832 21.331 1.00 37.74 B C ATOM 4259 C ALA B 258 23.833 9.547 20.274 1.00 36.90 B C ATOM 4260 O ALA B 258 24.351 10.371 21.013 1.00 37.34 B O ATOM 4261 N LEU B 259 23.373 9.849 19.067 1.00 35.49 B N ATOM 4262 CA LEU B 259 23.468 11.194 18.485 1.00 36.20 B C ATOM 4263 CB LEU B 259 22.692 11.243 17.149 1.00 35.03 B C ATOM 4264 CG LEU B 259 22.789 12.477 16.249 1.00 33.50 B C ATOM 4265 CD1 LEU B 259 21.969 13.599 16.855 1.00 34.00 B C ATOM 4266 CD2 LEU B 259 22.320 12.197 14.830 1.00 32.11 B C ATOM 4267 C LEU B 259 24.910 11.618 18.227 1.00 37.29 B C ATOM 4268 O LEU B 259 25.238 12.795 18.305 1.00 37.07 B O ATOM 4269 N ILE B 260 25.760 10.662 17.889 1.00 41.20 B N ATOM 4270 CA ILE B 260 27.138 10.968 17.499 1.00 45.53 B C ATOM 4271 CB ILE B 260 27.679 9.922 16.468 1.00 47.96 B C ATOM 4272 CG1 ILE B 260 27.242 10.273 15.049 1.00 49.37 B C ATOM 4273 CD1 ILE B 260 25.754 10.302 14.809 1.00 50.87 B C ATOM 4274 CG2 ILE B 260 29.203 9.896 16.425 1.00 50.61 B C ATOM 4275 C ILE B 260 28.037 11.059 18.746 1.00 41.96 B C ATOM 4276 O ILE B 260 29.047 11.766 18.741 1.00 37.45 B O ATOM 4277 N ASN B 261 27.647 10.353 19.806 1.00 41.28 B N ATOM 4278 CA ASN B 261 28.562 10.065 20.900 1.00 42.92 B C ATOM 4279 CB ASN B 261 28.929 8.555 20.935 1.00 41.62 B C ATOM 4280 CG ASN B 261 29.766 8.108 19.723 1.00 42.05 B C ATOM 4281 OD1 ASN B 261 29.472 7.101 19.087 1.00 39.28 B O ATOM 4282 ND2 ASN B 261 30.817 8.854 19.410 1.00 44.78 B N ATOM 4283 C ASN B 261 28.086 10.509 22.266 1.00 42.09 B C ATOM 4284 O ASN B 261 28.894 10.541 23.181 1.00 46.04 B O ATOM 4285 N TYR B 262 26.811 10.840 22.437 1.00 40.74 B N ATOM 4286 CA TYR B 262 26.328 11.224 23.775 1.00 43.37 B C ATOM 4287 CB TYR B 262 25.645 10.035 24.471 1.00 45.46 B C ATOM 4288 CG TYR B 262 26.615 8.895 24.720 1.00 50.69 B C ATOM 4289 CD1 TYR B 262 27.687 9.048 25.610 1.00 53.20 B C ATOM 4290 CE1 TYR B 262 28.603 8.023 25.824 1.00 51.02 B C ATOM 4291 CZ TYR B 262 28.459 6.829 25.145 1.00 50.83 B C ATOM 4292 OH TYR B 262 29.355 5.817 25.374 1.00 49.75 B O ATOM 4293 CE2 TYR B 262 27.406 6.644 24.259 1.00 51.59 B C ATOM 4294 CD2 TYR B 262 26.497 7.676 24.040 1.00 52.01 B C ATOM 4295 C TYR B 262 25.448 12.478 23.816 1.00 42.34 B C ATOM 4296 O TYR B 262 25.698 13.358 24.629 1.00 40.29 B O ATOM 4297 N LEU B 263 24.442 12.568 22.943 1.00 42.79 B N ATOM 4298 CA LEU B 263 23.480 13.686 22.966 1.00 40.87 B C ATOM 4299 CB LEU B 263 22.404 13.522 21.890 1.00 39.39 B C ATOM 4300 CG LEU B 263 21.392 12.379 22.072 1.00 39.16 B C ATOM 4301 CD1 LEU B 263 20.636 12.135 20.758 1.00 38.76 B C ATOM 4302 CD2 LEU B 263 20.439 12.620 23.251 1.00 36.77 B C ATOM 4303 C LEU B 263 24.182 15.025 22.784 1.00 41.44 B C ATOM 4304 O LEU B 263 24.950 15.224 21.830 1.00 43.17 B O ATOM 4305 N THR B 264 23.920 15.937 23.710 1.00 39.41 B N ATOM 4306 CA THR B 264 24.539 17.252 23.678 1.00 39.11 B C ATOM 4307 CB THR B 264 25.110 17.637 25.071 1.00 37.81 B C ATOM 4308 OG1 THR B 264 24.209 17.240 26.114 1.00 34.47 B O ATOM 4309 CG2 THR B 264 26.464 16.980 25.291 1.00 37.47 B C ATOM 4310 C THR B 264 23.516 18.289 23.180 1.00 39.71 B C ATOM 4311 O THR B 264 22.332 17.968 22.988 1.00 39.63 B O ATOM 4312 N PRO B 265 23.967 19.534 22.956 1.00 37.47 B N ATOM 4313 CA PRO B 265 23.020 20.582 22.606 1.00 36.51 B C ATOM 4314 CB PRO B 265 23.914 21.815 22.485 1.00 36.96 B C ATOM 4315 CG PRO B 265 25.212 21.258 21.998 1.00 36.90 B C ATOM 4316 CD PRO B 265 25.362 19.978 22.764 1.00 37.02 B C ATOM 4317 C PRO B 265 21.889 20.826 23.602 1.00 34.86 B C ATOM 4318 O PRO B 265 20.886 21.386 23.218 1.00 34.81 B O ATOM 4319 N THR B 266 22.029 20.371 24.836 1.00 36.32 B N ATOM 4320 CA THR B 266 21.064 20.660 25.909 1.00 38.58 B C ATOM 4321 CB THR B 266 21.832 21.113 27.172 1.00 39.51 B C ATOM 4322 OG1 THR B 266 22.792 22.103 26.783 1.00 40.49 B O ATOM 4323 CG2 THR B 266 20.891 21.667 28.272 1.00 39.24 B C ATOM 4324 C THR B 266 20.208 19.477 26.339 1.00 37.79 B C ATOM 4325 O THR B 266 19.415 19.606 27.267 1.00 40.23 B O ATOM 4326 N SER B 267 20.369 18.324 25.697 1.00 36.30 B N ATOM 4327 CA SER B 267 19.731 17.102 26.183 1.00 34.28 B C ATOM 4328 CB SER B 267 20.113 15.912 25.319 1.00 35.49 B C ATOM 4329 OG SER B 267 21.451 16.033 24.828 1.00 37.99 B O ATOM 4330 C SER B 267 18.230 17.251 26.190 1.00 32.77 B C ATOM 4331 O SER B 267 17.641 17.643 25.208 1.00 33.92 B O ATOM 4332 N ASN B 268 17.620 16.986 27.326 1.00 32.61 B N ATOM 4333 CA ASN B 268 16.182 16.863 27.415 1.00 33.06 B C ATOM 4334 CB ASN B 268 15.729 17.371 28.773 1.00 33.54 B C ATOM 4335 CG ASN B 268 16.267 16.536 29.895 1.00 33.79 B C ATOM 4336 OD1 ASN B 268 17.326 15.949 29.777 1.00 35.97 B O ATOM 4337 ND2 ASN B 268 15.540 16.461 30.975 1.00 34.73 B N ATOM 4338 C ASN B 268 15.787 15.390 27.231 1.00 34.80 B C ATOM 4339 O ASN B 268 16.626 14.538 26.913 1.00 34.48 B O ATOM 4340 N PHE B 269 14.514 15.079 27.443 1.00 36.91 B N ATOM 4341 CA PHE B 269 14.026 13.738 27.157 1.00 38.91 B C ATOM 4342 CB PHE B 269 12.507 13.628 27.385 1.00 40.79 B C ATOM 4343 CG PHE B 269 11.681 13.874 26.141 1.00 41.78 B C ATOM 4344 CD1 PHE B 269 11.418 12.849 25.251 1.00 41.82 B C ATOM 4345 CE1 PHE B 269 10.654 13.078 24.112 1.00 41.04 B C ATOM 4346 CZ PHE B 269 10.135 14.332 23.857 1.00 38.55 B C ATOM 4347 CE2 PHE B 269 10.382 15.356 24.732 1.00 38.41 B C ATOM 4348 CD2 PHE B 269 11.155 15.130 25.867 1.00 41.11 B C ATOM 4349 C PHE B 269 14.805 12.684 27.957 1.00 38.14 B C ATOM 4350 O PHE B 269 15.419 11.804 27.371 1.00 37.56 B O ATOM 4351 N SER B 270 14.842 12.803 29.281 1.00 36.64 B N ATOM 4352 CA SER B 270 15.531 11.802 30.090 1.00 34.60 B C ATOM 4353 CB SER B 270 14.897 11.695 31.499 1.00 34.71 B C ATOM 4354 OG SER B 270 15.617 12.383 32.491 1.00 34.03 B O ATOM 4355 C SER B 270 17.045 12.041 30.114 1.00 32.63 B C ATOM 4356 O SER B 270 17.674 11.999 31.146 1.00 36.29 B O ATOM 4357 N ALA B 271 17.604 12.349 28.960 1.00 30.68 B N ATOM 4358 CA ALA B 271 19.038 12.294 28.730 1.00 30.92 B C ATOM 4359 CB ALA B 271 19.613 13.701 28.600 1.00 30.65 B C ATOM 4360 C ALA B 271 19.247 11.507 27.444 1.00 30.93 B C ATOM 4361 O ALA B 271 20.307 10.917 27.213 1.00 29.36 B O ATOM 4362 N MET B 272 18.229 11.586 26.584 1.00 32.20 B N ATOM 4363 CA MET B 272 18.031 10.679 25.460 1.00 32.76 B C ATOM 4364 CB MET B 272 16.756 11.071 24.673 1.00 32.48 B C ATOM 4365 CG MET B 272 16.360 10.134 23.533 1.00 31.70 B C ATOM 4366 SD MET B 272 17.286 10.362 22.001 1.00 31.29 B S ATOM 4367 CE MET B 272 18.784 9.421 22.293 1.00 30.09 B C ATOM 4368 C MET B 272 17.923 9.252 25.975 1.00 32.88 B C ATOM 4369 O MET B 272 18.662 8.395 25.515 1.00 32.30 B O ATOM 4370 N ARG B 273 17.011 9.021 26.933 1.00 34.73 B N ATOM 4371 CA ARG B 273 16.906 7.739 27.658 1.00 35.03 B C ATOM 4372 CB ARG B 273 16.032 7.842 28.925 1.00 34.92 B C ATOM 4373 CG ARG B 273 15.783 6.483 29.582 1.00 36.57 B C ATOM 4374 CD ARG B 273 15.352 6.494 31.046 1.00 38.56 B C ATOM 4375 NE ARG B 273 15.489 5.154 31.660 1.00 40.10 B N ATOM 4376 CZ ARG B 273 14.486 4.289 31.894 1.00 40.63 B C ATOM 4377 NH1 ARG B 273 13.218 4.572 31.590 1.00 39.02 B N ATOM 4378 NH2 ARG B 273 14.752 3.107 32.442 1.00 41.17 B N ATOM 4379 C ARG B 273 18.295 7.267 28.039 1.00 34.93 B C ATOM 4380 O ARG B 273 18.770 6.252 27.549 1.00 34.29 B O ATOM 4381 N ALA B 274 18.955 8.045 28.884 1.00 37.65 B N ATOM 4382 CA ALA B 274 20.304 7.717 29.344 1.00 37.88 B C ATOM 4383 CB ALA B 274 20.886 8.866 30.184 1.00 38.03 B C ATOM 4384 C ALA B 274 21.217 7.383 28.170 1.00 33.95 B C ATOM 4385 O ALA B 274 21.822 6.319 28.149 1.00 32.98 B O ATOM 4386 N ALA B 275 21.296 8.285 27.200 1.00 32.07 B N ATOM 4387 CA ALA B 275 22.201 8.106 26.070 1.00 33.08 B C ATOM 4388 CB ALA B 275 22.345 9.407 25.299 1.00 32.37 B C ATOM 4389 C ALA B 275 21.789 6.962 25.127 1.00 34.71 B C ATOM 4390 O ALA B 275 22.640 6.437 24.384 1.00 33.51 B O ATOM 4391 N ALA B 276 20.505 6.581 25.166 1.00 34.12 B N ATOM 4392 CA ALA B 276 19.991 5.442 24.381 1.00 34.35 B C ATOM 4393 CB ALA B 276 18.467 5.428 24.360 1.00 34.79 B C ATOM 4394 C ALA B 276 20.486 4.140 24.970 1.00 33.42 B C ATOM 4395 O ALA B 276 20.986 3.249 24.258 1.00 30.24 B O ATOM 4396 N ILE B 277 20.313 4.046 26.284 1.00 33.82 B N ATOM 4397 CA ILE B 277 20.893 2.967 27.069 1.00 34.25 B C ATOM 4398 CB ILE B 277 20.669 3.167 28.584 1.00 32.40 B C ATOM 4399 CG1 ILE B 277 19.176 2.974 28.939 1.00 30.53 B C ATOM 4400 CD1 ILE B 277 18.811 3.402 30.343 1.00 30.29 B C ATOM 4401 CG2 ILE B 277 21.570 2.220 29.370 1.00 32.72 B C ATOM 4402 C ILE B 277 22.376 2.909 26.750 1.00 35.55 B C ATOM 4403 O ILE B 277 22.852 1.988 26.123 1.00 37.39 B O ATOM 4404 N GLN B 278 23.092 3.943 27.119 1.00 38.65 B N ATOM 4405 CA GLN B 278 24.511 3.926 26.950 1.00 39.92 B C ATOM 4406 CB GLN B 278 25.094 5.290 27.321 1.00 39.74 B C ATOM 4407 CG GLN B 278 26.606 5.300 27.308 1.00 39.67 B C ATOM 4408 CD GLN B 278 27.189 4.111 28.042 1.00 38.74 B C ATOM 4409 OE1 GLN B 278 26.710 3.731 29.109 1.00 35.78 B O ATOM 4410 NE2 GLN B 278 28.208 3.499 27.453 1.00 38.39 B N ATOM 4411 C GLN B 278 24.965 3.489 25.546 1.00 42.36 B C ATOM 4412 O GLN B 278 25.940 2.757 25.439 1.00 48.71 B O ATOM 4413 N ALA B 279 24.285 3.905 24.478 1.00 45.05 B N ATOM 4414 CA ALA B 279 24.730 3.520 23.108 1.00 46.98 B C ATOM 4415 CB ALA B 279 24.072 4.393 22.055 1.00 46.66 B C ATOM 4416 C ALA B 279 24.469 2.039 22.790 1.00 48.10 B C ATOM 4417 O ALA B 279 25.275 1.393 22.123 1.00 45.73 B O ATOM 4418 N ALA B 280 23.325 1.529 23.261 1.00 50.53 B N ATOM 4419 CA ALA B 280 22.959 0.109 23.139 1.00 49.16 B C ATOM 4420 CB ALA B 280 21.503 0.098 23.531 1.00 48.26 B C ATOM 4421 C ALA B 280 23.850 0.770 24.006 1.00 50.26 B C ATOM 4422 O ALA B 280 24.128 1.910 23.647 1.00 55.46 B O ATOM 4423 N THR B 281 24.272 0.236 25.150 1.00 46.81 B N ATOM 4424 CA THR B 281 25.211 0.899 26.024 1.00 45.54 B C ATOM 4425 CB THR B 281 25.317 0.164 27.381 1.00 47.69 B C ATOM 4426 OG1 THR B 281 24.123 0.397 28.143 1.00 48.16 B O ATOM 4427 CG2 THR B 281 26.488 0.648 28.210 1.00 48.37 B C ATOM 4428 C THR B 281 26.557 1.023 25.310 1.00 47.32 B C ATOM 4429 O THR B 281 27.094 2.131 25.213 1.00 49.73 B O ATOM 4430 N ASP B 282 27.081 0.081 24.771 1.00 47.65 B N ATOM 4431 CA ASP B 282 28.330 0.052 23.961 1.00 49.02 B C ATOM 4432 CB ASP B 282 28.609 1.428 23.343 1.00 49.93 B C ATOM 4433 CG ASP B 282 29.000 2.464 24.366 1.00 51.23 B C ATOM 4434 OD1 ASP B 282 29.308 2.090 25.518 1.00 47.87 B O ATOM 4435 OD2 ASP B 282 28.995 3.662 24.005 1.00 53.69 B O ATOM 4436 C ASP B 282 28.359 0.976 22.811 1.00 49.83 B C ATOM 4437 O ASP B 282 29.439 1.378 22.350 1.00 47.84 B O ATOM 4438 N LEU B 283 27.177 1.363 22.329 1.00 51.88 B N ATOM 4439 CA LEU B 283 27.052 2.309 21.218 1.00 52.09 B C ATOM 4440 CB LEU B 283 26.006 1.820 20.213 1.00 52.89 B C ATOM 4441 CG LEU B 283 26.431 0.781 19.184 1.00 52.14 B C ATOM 4442 CD1 LEU B 283 25.348 0.710 18.117 1.00 51.63 B C ATOM 4443 CD2 LEU B 283 27.796 1.094 18.578 1.00 50.82 B C ATOM 4444 C LEU B 283 26.675 3.721 21.656 1.00 49.74 B C ATOM 4445 O LEU B 283 27.352 4.665 21.303 1.00 50.65 B O ATOM 4446 N TYR B 284 25.586 3.863 22.401 1.00 48.81 B N ATOM 4447 CA TYR B 284 25.061 5.189 22.727 1.00 49.44 B C ATOM 4448 CB TYR B 284 23.556 5.262 22.403 1.00 50.48 B C ATOM 4449 CG TYR B 284 23.236 4.737 21.026 1.00 49.15 B C ATOM 4450 CD1 TYR B 284 23.872 5.254 19.903 1.00 49.52 B C ATOM 4451 CE1 TYR B 284 23.603 4.762 18.632 1.00 50.75 B C ATOM 4452 CZ TYR B 284 22.681 3.732 18.471 1.00 50.38 B C ATOM 4453 OH TYR B 284 22.404 3.229 17.205 1.00 47.77 B O ATOM 4454 CE2 TYR B 284 22.048 3.197 19.584 1.00 49.51 B C ATOM 4455 CD2 TYR B 284 22.333 3.695 20.848 1.00 49.51 B C ATOM 4456 C TYR B 284 25.315 5.610 24.171 1.00 49.25 B C ATOM 4457 O TYR B 284 24.821 6.647 24.590 1.00 48.69 B O ATOM 4458 N GLY B 285 26.074 4.821 24.930 1.00 50.48 B N ATOM 4459 CA GLY B 285 26.504 5.227 26.273 1.00 49.49 B C ATOM 4460 C GLY B 285 25.475 4.969 27.360 1.00 48.24 B C ATOM 4461 O GLY B 285 24.297 5.259 27.199 1.00 44.44 B O ATOM 4462 N ALA B 286 25.958 4.477 28.494 1.00 49.71 B N ATOM 4463 CA ALA B 286 25.129 3.842 29.533 1.00 53.31 B C ATOM 4464 CB ALA B 286 25.958 3.664 30.805 1.00 54.01 B C ATOM 4465 C ALA B 286 23.777 4.486 29.893 1.00 53.88 B C ATOM 4466 O ALA B 286 22.839 3.779 30.282 1.00 51.19 B O ATOM 4467 N ASN B 287 23.673 5.807 29.803 1.00 54.40 B N ATOM 4468 CA ASN B 287 22.489 6.464 30.315 1.00 57.64 B C ATOM 4469 CB ASN B 287 22.872 7.348 31.514 1.00 60.09 B C ATOM 4470 CG ASN B 287 22.568 6.674 32.851 1.00 60.57 B C ATOM 4471 OD1 ASN B 287 21.399 6.491 33.202 1.00 62.04 B O ATOM 4472 ND2 ASN B 287 23.610 6.296 33.598 1.00 57.39 B N ATOM 4473 C ASN B 287 21.741 7.215 29.227 1.00 58.94 B C ATOM 4474 O ASN B 287 21.301 8.344 29.423 1.00 58.57 B O ATOM 4475 N SER B 288 21.549 6.542 28.093 1.00 58.78 B N ATOM 4476 CA SER B 288 21.058 7.184 26.870 1.00 54.62 B C ATOM 4477 CB SER B 288 21.578 6.456 25.636 1.00 53.53 B C ATOM 4478 OG SER B 288 22.968 6.277 25.713 1.00 53.88 B O ATOM 4479 C SER B 288 19.554 7.219 26.756 1.00 52.14 B C ATOM 4480 O SER B 288 18.835 6.460 27.428 1.00 48.93 B O ATOM 4481 N SER B 289 19.101 8.113 25.877 1.00 49.50 B N ATOM 4482 CA SER B 289 17.748 8.063 25.338 1.00 48.18 B C ATOM 4483 CB SER B 289 17.658 8.897 24.062 1.00 46.70 B C ATOM 4484 OG SER B 289 17.504 10.261 24.344 1.00 47.82 B O ATOM 4485 C SER B 289 17.420 6.629 24.973 1.00 45.61 B C ATOM 4486 O SER B 289 16.363 6.096 25.322 1.00 42.65 B O ATOM 4487 N GLN B 290 18.371 6.033 24.264 1.00 44.11 B N ATOM 4488 CA GLN B 290 18.221 4.722 23.655 1.00 45.53 B C ATOM 4489 CB GLN B 290 19.422 4.420 22.743 1.00 46.86 B C ATOM 4490 CG GLN B 290 19.350 5.126 21.390 1.00 48.38 B C ATOM 4491 CD GLN B 290 19.890 6.548 21.405 1.00 46.61 B C ATOM 4492 OE1 GLN B 290 20.064 7.138 22.465 1.00 47.54 B O ATOM 4493 NE2 GLN B 290 20.156 7.098 20.221 1.00 44.66 B N ATOM 4494 C GLN B 290 18.081 3.619 24.674 1.00 43.32 B C ATOM 4495 O GLN B 290 17.141 2.838 24.621 1.00 41.88 B O ATOM 4496 N VAL B 291 19.029 3.562 25.594 1.00 41.50 B N ATOM 4497 CA VAL B 291 19.014 2.555 26.622 1.00 40.16 B C ATOM 4498 CB VAL B 291 20.266 2.679 27.505 1.00 39.26 B C ATOM 4499 CG1 VAL B 291 20.219 1.674 28.647 1.00 39.12 B C ATOM 4500 CG2 VAL B 291 21.524 2.494 26.651 1.00 38.82 B C ATOM 4501 C VAL B 291 17.714 2.639 27.432 1.00 41.56 B C ATOM 4502 O VAL B 291 17.078 1.624 27.664 1.00 41.96 B O ATOM 4503 N ASN B 292 17.303 3.847 27.821 1.00 47.66 B N ATOM 4504 CA ASN B 292 16.051 4.063 28.595 1.00 49.69 B C ATOM 4505 CB ASN B 292 15.801 5.576 28.850 1.00 56.17 B C ATOM 4506 CG ASN B 292 16.608 6.138 30.026 1.00 59.22 B C ATOM 4507 OD1 ASN B 292 16.441 5.711 31.179 1.00 58.08 B O ATOM 4508 ND2 ASN B 292 17.466 7.126 29.741 1.00 57.45 B N ATOM 4509 C ASN B 292 14.813 3.473 27.908 1.00 44.46 B C ATOM 4510 O ASN B 292 13.892 2.961 28.567 1.00 40.14 B O ATOM 4511 N ALA B 293 14.792 3.576 26.581 1.00 42.31 B N ATOM 4512 CA ALA B 293 13.730 2.972 25.763 1.00 41.98 B C ATOM 4513 CB ALA B 293 13.829 3.451 24.321 1.00 41.43 B C ATOM 4514 C ALA B 293 13.756 1.433 25.810 1.00 39.16 B C ATOM 4515 O ALA B 293 12.721 0.815 26.082 1.00 36.57 B O ATOM 4516 N VAL B 294 14.936 0.852 25.539 1.00 36.84 B N ATOM 4517 CA VAL B 294 15.177 0.595 25.610 1.00 35.25 B C ATOM 4518 CB VAL B 294 16.659 0.950 25.468 1.00 35.72 B C ATOM 4519 CG1 VAL B 294 16.878 2.433 25.729 1.00 37.88 B C ATOM 4520 CG2 VAL B 294 17.176 0.610 24.091 1.00 36.30 B C ATOM 4521 C VAL B 294 14.748 1.144 26.945 1.00 35.55 B C ATOM 4522 O VAL B 294 13.956 2.064 26.995 1.00 33.54 B O ATOM 4523 N LYS B 295 15.286 0.587 28.025 1.00 37.14 B N ATOM 4524 CA LYS B 295 14.869 0.983 29.360 1.00 41.15 B C ATOM 4525 CB LYS B 295 15.422 0.035 30.422 1.00 46.63 B C ATOM 4526 CG LYS B 295 16.913 0.162 30.660 1.00 52.98 B C ATOM 4527 CD LYS B 295 17.355 0.640 31.874 1.00 58.56 B C ATOM 4528 CE LYS B 295 18.834 0.407 32.159 1.00 64.17 B C ATOM 4529 NZ LYS B 295 19.271 1.113 33.395 1.00 67.47 B N ATOM 4530 C LYS B 295 13.372 0.957 29.481 1.00 39.83 B C ATOM 4531 O LYS B 295 12.768 1.874 30.035 1.00 41.50 B O ATOM 4532 N LYS B 296 12.786 0.118 28.972 1.00 40.95 B N ATOM 4533 CA LYS B 296 11.379 0.436 29.209 1.00 42.53 B C ATOM 4534 CB LYS B 296 11.161 1.962 29.047 1.00 43.71 B C ATOM 4535 CG LYS B 296 9.937 2.509 29.771 1.00 47.26 B C ATOM 4536 CD LYS B 296 10.251 3.670 30.724 1.00 50.59 B C ATOM 4537 CE LYS B 296 9.147 3.860 31.775 1.00 51.12 B C ATOM 4538 NZ LYS B 296 7.865 4.414 31.217 1.00 50.10 B N ATOM 4539 C LYS B 296 10.477 0.407 28.291 1.00 39.86 B C ATOM 4540 O LYS B 296 9.340 0.751 28.633 1.00 39.63 B O ATOM 4541 N ALA B 297 11.013 0.758 27.131 1.00 38.67 B N ATOM 4542 CA ALA B 297 10.337 1.648 26.193 1.00 36.50 B C ATOM 4543 CB ALA B 297 11.132 1.753 24.896 1.00 35.52 B C ATOM 4544 C ALA B 297 10.156 3.017 26.823 1.00 35.43 B C ATOM 4545 O ALA B 297 9.033 3.437 27.087 1.00 35.98 B O ATOM 4546 N TYR B 298 11.266 3.697 27.098 1.00 33.26 B N ATOM 4547 CA TYR B 298 11.208 5.015 27.703 1.00 30.77 B C ATOM 4548 CB TYR B 298 12.615 5.568 27.929 1.00 29.47 B C ATOM 4549 CG TYR B 298 13.204 6.108 26.644 1.00 28.38 B C ATOM 4550 CD1 TYR B 298 12.809 7.349 26.131 1.00 29.24 B C ATOM 4551 CE1 TYR B 298 13.318 7.832 24.930 1.00 28.21 B C ATOM 4552 CZ TYR B 298 14.234 7.070 24.228 1.00 27.78 B C ATOM 4553 OH TYR B 298 14.763 7.485 23.031 1.00 26.67 B O ATOM 4554 CE2 TYR B 298 14.638 5.854 24.728 1.00 27.85 B C ATOM 4555 CD2 TYR B 298 14.119 5.381 25.925 1.00 27.58 B C ATOM 4556 C TYR B 298 10.332 5.057 28.972 1.00 31.41 B C ATOM 4557 O TYR B 298 9.596 6.029 29.171 1.00 33.75 B O ATOM 4558 N THR B 299 10.341 4.007 29.793 1.00 30.17 B N ATOM 4559 CA THR B 299 9.452 3.990 30.981 1.00 31.63 B C ATOM 4560 CB THR B 299 9.651 2.727 31.904 1.00 30.00 B C ATOM 4561 OG1 THR B 299 11.031 2.587 32.274 1.00 29.34 B O ATOM 4562 CG2 THR B 299 8.825 2.848 33.164 1.00 28.55 B C ATOM 4563 C THR B 299 7.963 4.124 30.561 1.00 31.90 B C ATOM 4564 O THR B 299 7.142 4.745 31.262 1.00 31.07 B O ATOM 4565 N ALA B 300 7.641 3.552 29.406 1.00 32.45 B N ATOM 4566 CA ALA B 300 6.262 3.429 28.966 1.00 33.91 B C ATOM 4567 CB ALA B 300 6.157 2.425 27.831 1.00 35.00 B C ATOM 4568 C ALA B 300 5.718 4.754 28.521 1.00 34.05 B C ATOM 4569 O ALA B 300 4.519 5.032 28.722 1.00 33.41 B O ATOM 4570 N VAL B 301 6.606 5.551 27.916 1.00 34.40 B N ATOM 4571 CA VAL B 301 6.294 6.923 27.499 1.00 35.91 B C ATOM 4572 CB VAL B 301 7.080 7.346 26.243 1.00 35.35 B C ATOM 4573 CG1 VAL B 301 6.679 6.467 25.065 1.00 34.72 B C ATOM 4574 CG2 VAL B 301 8.587 7.313 26.485 1.00 35.39 B C ATOM 4575 C VAL B 301 6.491 7.968 28.607 1.00 37.99 B C ATOM 4576 O VAL B 301 6.283 9.152 28.384 1.00 40.13 B O ATOM 4577 N GLY B 302 6.875 7.535 29.801 1.00 39.20 B N ATOM 4578 CA GLY B 302 6.806 8.402 30.975 1.00 38.61 B C ATOM 4579 C GLY B 302 8.120 9.085 31.268 1.00 37.68 B C ATOM 4580 O GLY B 302 8.219 9.890 32.206 1.00 36.97 B O ATOM 4581 N VAL B 303 9.123 8.764 30.457 1.00 36.46 B N ATOM 4582 CA VAL B 303 10.463 9.269 30.646 1.00 36.09 B C ATOM 4583 CB VAL B 303 11.186 9.418 29.310 1.00 34.30 B C ATOM 4584 CG1 VAL B 303 12.615 9.884 29.525 1.00 34.12 B C ATOM 4585 CG2 VAL B 303 10.413 10.378 28.422 1.00 34.22 B C ATOM 4586 C VAL B 303 11.210 8.285 31.529 1.00 39.41 B C ATOM 4587 O VAL B 303 11.410 7.128 31.162 1.00 39.85 B O ATOM 4588 N ASN B 304 11.623 8.767 32.695 1.00 42.29 B N ATOM 4589 CA ASN B 304 12.178 7.934 33.741 1.00 43.11 B C ATOM 4590 CB ASN B 304 11.400 8.162 35.039 1.00 43.44 B C ATOM 4591 CG ASN B 304 9.894 7.915 34.868 1.00 44.48 B C ATOM 4592 OD1 ASN B 304 9.046 8.788 35.169 1.00 39.07 B O ATOM 4593 ND2 ASN B 304 9.554 6.727 34.345 1.00 44.40 B N ATOM 4594 C ASN B 304 13.644 8.265 33.895 1.00 45.91 B C ATOM 4595 O ASN B 304 14.115 9.329 33.478 1.00 47.21 B O ATOM 4596 OXT ASN B 304 14.398 7.442 34.401 1.00 50.28 B O HETATM 4597 O HOH D 1 14.453 29.833 15.752 1.00 11.48 O HETATM 4598 O HOH D 2 3.559 28.043 4.163 1.00 10.41 O HETATM 4599 O HOH D 3 4.756 48.667 28.368 1.00 14.01 O HETATM 4600 O HOH D 4 18.017 46.898 29.709 1.00 17.11 O HETATM 4601 O HOH D 5 18.034 41.311 16.195 1.00 16.89 O HETATM 4602 O HOH D 6 2.102 33.576 25.415 1.00 7.28 O HETATM 4603 O HOH D 7 4.340 35.545 22.828 1.00 6.89 O HETATM 4604 O HOH D 8 1.226 54.679 7.110 1.00 10.35 O HETATM 4605 O HOH D 9 12.874 50.118 9.369 1.00 13.13 O HETATM 4606 O HOH D 10 1.229 11.651 14.935 1.00 8.69 O HETATM 4607 O HOH D 11 26.802 9.821 2.646 1.00 34.23 O HETATM 4608 O HOH D 12 15.279 23.352 24.790 1.00 28.05 O HETATM 4609 O HOH D 14 5.337 10.672 15.773 1.00 17.85 O HETATM 4610 O HOH D 15 1.182 34.774 17.307 1.00 14.04 O HETATM 4611 O HOH D 16 10.282 45.012 0.457 1.00 7.05 O HETATM 4612 O HOH D 17 5.067 45.950 25.877 1.00 7.74 O HETATM 4613 O HOH D 18 9.466 22.365 4.654 1.00 9.26 O HETATM 4614 O HOH D 19 14.867 34.797 31.110 1.00 12.29 O HETATM 4615 O HOH D 20 17.658 31.345 6.147 1.00 13.22 O HETATM 4616 O HOH D 21 14.706 66.680 15.999 1.00 18.23 O HETATM 4617 O HOH D 24 22.701 44.854 24.508 1.00 13.43 O HETATM 4618 O HOH D 25 1.606 44.470 24.808 1.00 4.05 O HETATM 4619 O HOH D 27 14.081 49.049 23.938 1.00 5.85 O HETATM 4620 O HOH D 28 1.406 15.180 13.873 1.00 20.93 O HETATM 4621 O HOH D 29 18.234 61.855 23.352 1.00 15.81 O HETATM 4622 O HOH D 30 14.980 31.161 4.673 1.00 8.84 O HETATM 4623 O HOH D 31 25.232 37.903 28.412 1.00 7.88 O HETATM 4624 O HOH D 32 2.306 3.607 14.150 1.00 12.43 O HETATM 4625 O HOH D 33 8.133 32.218 28.553 1.00 21.62 O HETATM 4626 O HOH D 34 9.785 46.761 10.910 1.00 11.38 O HETATM 4627 O HOH D 35 25.957 51.974 19.833 1.00 17.72 O HETATM 4628 O HOH D 36 0.537 38.406 2.660 1.00 12.52 O HETATM 4629 O HOH D 37 6.253 26.792 2.618 1.00 14.95 O HETATM 4630 O HOH D 38 4.277 32.186 26.909 1.00 10.72 O HETATM 4631 O HOH D 40 0.230 46.981 24.263 1.00 10.61 O HETATM 4632 O HOH D 41 9.113 53.708 16.348 1.00 8.82 O HETATM 4633 O HOH D 42 0.527 57.811 16.009 1.00 5.69 O HETATM 4634 O HOH D 43 7.369 49.544 27.875 1.00 11.17 O HETATM 4635 O HOH D 44 13.059 41.050 31.554 1.00 14.34 O HETATM 4636 O HOH D 45 30.779 55.305 11.958 1.00 12.66 O HETATM 4637 O HOH D 46 16.179 51.696 0.530 1.00 17.86 O HETATM 4638 O HOH D 47 6.739 26.907 6.038 1.00 8.32 O HETATM 4639 O HOH D 48 1.147 27.953 5.319 1.00 11.94 O HETATM 4640 O HOH D 49 27.771 63.155 6.758 1.00 25.59 O HETATM 4641 O HOH D 50 22.146 51.541 20.878 1.00 23.93 O HETATM 4642 O HOH D 51 11.498 53.494 22.966 1.00 19.18 O HETATM 4643 O HOH D 52 35.618 17.756 3.293 1.00 30.46 O HETATM 4644 O HOH D 53 0.936 10.997 2.654 1.00 21.53 O HETATM 4645 O HOH D 55 3.931 51.435 22.740 1.00 21.73 O HETATM 4646 O HOH D 56 11.411 49.131 23.961 1.00 4.13 O HETATM 4647 O HOH D 57 10.929 42.120 2.629 1.00 8.04 O HETATM 4648 O HOH D 58 5.258 24.055 13.514 1.00 7.92 O HETATM 4649 O HOH D 59 2.368 2.482 8.879 1.00 8.97 O HETATM 4650 O HOH D 60 22.320 35.750 12.017 1.00 10.98 O HETATM 4651 O HOH D 61 19.413 20.255 13.553 1.00 7.71 O HETATM 4652 O HOH D 62 0.658 31.524 23.753 1.00 8.59 O HETATM 4653 O HOH D 63 14.971 39.634 33.356 1.00 12.49 O HETATM 4654 O HOH D 64 5.191 35.793 0.990 1.00 18.79 O HETATM 4655 O HOH D 65 7.971 52.023 23.877 1.00 7.05 O HETATM 4656 O HOH D 66 10.996 39.555 30.895 1.00 29.45 O HETATM 4657 O HOH D 67 5.761 28.410 26.821 1.00 10.37 O HETATM 4658 O HOH D 69 0.623 30.084 21.186 1.00 16.74 O HETATM 4659 O HOH D 70 11.237 21.250 19.622 1.00 12.84 O HETATM 4660 O HOH D 71 6.423 13.673 7.327 1.00 7.62 O HETATM 4661 O HOH D 72 12.098 4.570 9.813 1.00 17.86 O HETATM 4662 O HOH D 74 19.719 36.149 15.796 1.00 6.65 O HETATM 4663 O HOH D 75 7.298 10.821 6.866 1.00 16.58 O HETATM 4664 O HOH D 76 24.422 49.300 6.907 1.00 13.05 O HETATM 4665 O HOH D 79 2.981 11.284 0.026 1.00 18.58 O HETATM 4666 O HOH D 80 21.114 35.355 22.146 1.00 14.58 O HETATM 4667 O HOH D 84 1.731 15.045 10.266 1.00 16.73 O HETATM 4668 O HOH D 85 14.299 20.123 30.892 1.00 18.20 O HETATM 4669 O HOH D 86 14.254 53.364 21.911 1.00 8.78 O HETATM 4670 O HOH D 87 1.855 39.977 9.636 1.00 9.12 O HETATM 4671 O HOH D 88 0.036 27.584 22.318 1.00 19.91 O HETATM 4672 O HOH D 89 16.641 8.034 21.414 1.00 28.79 O HETATM 4673 O HOH D 91 6.673 19.109 18.430 1.00 14.71 O HETATM 4674 O HOH D 92 15.712 28.784 11.584 1.00 17.47 O HETATM 4675 O HOH D 93 25.882 43.603 12.917 1.00 9.36 O HETATM 4676 O HOH D 94 13.971 58.069 2.171 1.00 16.23 O HETATM 4677 O HOH D 96 10.457 26.740 26.060 1.00 11.31 O HETATM 4678 O HOH D 97 22.816 38.364 5.993 1.00 17.13 O HETATM 4679 O HOH D 100 9.340 47.635 0.235 1.00 6.76 O HETATM 4680 O HOH D 102 3.056 38.032 31.275 1.00 6.12 O HETATM 4681 O HOH D 103 25.590 42.298 15.541 1.00 17.90 O HETATM 4682 O HOH D 104 10.556 51.368 25.973 1.00 9.26 O HETATM 4683 O HOH D 106 19.882 33.352 4.847 1.00 30.16 O HETATM 4684 O HOH D 107 6.248 27.219 8.518 1.00 11.81 O HETATM 4685 O HOH D 108 31.468 21.088 1.489 1.00 12.00 O HETATM 4686 O HOH D 111 21.684 30.977 26.026 1.00 23.70 O HETATM 4687 O HOH D 112 31.951 10.039 3.258 1.00 21.85 O HETATM 4688 O HOH D 113 12.420 61.104 20.866 1.00 20.71 O HETATM 4689 O HOH D 115 9.390 46.453 3.343 1.00 11.14 O HETATM 4690 O HOH D 116 24.310 8.827 27.982 1.00 28.62 O HETATM 4691 O HOH D 118 0.928 0.943 27.721 1.00 20.32 O HETATM 4692 O HOH D 119 0.811 22.368 26.821 1.00 28.05 O HETATM 4693 O HOH D 120 2.928 27.375 2.252 1.00 6.28 O HETATM 4694 O HOH D 122 24.797 33.048 16.191 1.00 20.61 O HETATM 4695 O HOH D 123 28.116 42.682 17.519 1.00 20.23 O HETATM 4696 O HOH D 126 0.728 11.568 25.035 1.00 27.72 O HETATM 4697 O HOH D 127 5.110 32.881 1.483 1.00 8.60 O HETATM 4698 O HOH D 128 6.910 6.512 5.883 1.00 23.17 O HETATM 4699 O HOH D 129 14.859 32.631 4.922 1.00 20.12 O HETATM 4700 O HOH D 130 9.393 20.445 22.229 1.00 11.44 O HETATM 4701 O HOH D 131 5.380 45.506 20.439 1.00 18.61 O HETATM 4702 O HOH D 132 20.298 17.857 4.369 1.00 24.71 O HETATM 4703 O HOH D 133 13.074 15.017 30.254 1.00 22.69 O HETATM 4704 O HOH D 134 22.544 64.671 13.497 1.00 18.42 O HETATM 4705 O HOH D 135 4.355 31.730 19.579 1.00 30.49 O HETATM 4706 O HOH D 136 4.978 28.238 15.122 1.00 22.36 O HETATM 4707 O HOH D 137 7.834 20.152 9.638 1.00 18.69 O HETATM 4708 O HOH D 138 14.293 28.356 18.330 1.00 27.34 O HETATM 4709 O HOH D 139 22.099 32.349 8.846 1.00 29.42 O HETATM 4710 O HOH D 140 8.752 28.130 6.857 1.00 8.09 O HETATM 4711 O HOH D 141 15.481 31.534 31.496 1.00 7.89 O HETATM 4712 O HOH D 142 14.386 25.883 11.379 1.00 24.39 O HETATM 4713 O HOH D 143 2.224 28.207 27.995 1.00 21.76 O HETATM 4714 O HOH D 144 3.038 2.948 18.802 1.00 17.17 O HETATM 4715 O HOH D 145 17.234 8.824 32.860 1.00 22.34 O HETATM 4716 O HOH D 146 21.972 36.386 17.229 1.00 15.20 O HETATM 4717 O HOH D 147 21.738 50.115 22.044 1.00 41.96 O HETATM 4718 O HOH D 148 15.129 42.497 17.235 1.00 64.58 O HETATM 4719 O HOH D 149 0.499 13.659 1.071 1.00 20.44 O HETATM 4720 O HOH D 150 26.656 39.916 12.524 1.00 28.86 O HETATM 4721 O HOH D 151 26.068 18.778 22.468 1.00 63.91 O HETATM 4722 O HOH D 152 17.839 37.146 6.365 1.00 17.05 O HETATM 4723 O HOH D 153 9.872 37.859 3.756 1.00 29.86 O HETATM 4724 O HOH D 154 26.704 13.656 20.767 1.00 24.94 O HETATM 4725 O HOH D 155 16.594 46.356 1.735 1.00 9.02 O HETATM 4726 O HOH D 156 3.278 28.231 11.565 1.00 15.79 O HETATM 4727 O HOH D 157 13.773 34.807 7.967 1.00 26.45 O HETATM 4728 O HOH D 158 5.274 27.734 3.607 1.00 14.35 O HETATM 4729 O HOH D 159 10.955 62.644 9.650 1.00 22.81 O HETATM 4730 O HOH D 160 19.801 28.085 15.802 1.00 15.92 O HETATM 4731 O HOH D 161 14.910 35.916 3.899 1.00 14.53 O HETATM 4732 O HOH D 162 7.630 39.335 29.693 1.00 19.10 O HETATM 4733 O HOH D 163 8.909 8.381 2.714 1.00 31.11 O HETATM 4734 O HOH D 164 35.136 13.839 9.366 1.00 19.26 O HETATM 4735 O HOH D 165 28.655 13.870 18.003 1.00 25.79 O HETATM 4736 O HOH D 166 4.969 28.077 6.380 1.00 15.01 O HETATM 4737 O HOH D 167 12.416 58.656 21.906 1.00 38.53 O HETATM 4738 O HOH D 168 1.381 22.000 5.296 1.00 15.16 O HETATM 4739 O HOH D 169 28.073 14.871 23.335 1.00 29.90 O HETATM 4740 O HOH D 170 5.698 52.447 27.051 1.00 46.81 O HETATM 4741 O HOH D 171 25.098 40.710 27.602 1.00 31.23 O HETATM 4742 O HOH D 172 13.253 30.057 31.043 1.00 25.08 O HETATM 4743 CA CA C 1 3.996 44.763 24.393 1.00 14.92 CA HETATM 4744 CA CA C 2 9.298 38.014 30.827 1.00 19.13 CA HETATM 4745 CA CA C 3 7.033 7.984 3.851 1.00 33.23 CA HETATM 4746 CA CA C 4 3.009 11.945 2.235 1.00 23.81 CA ATOM 4747 N VAL E 1 6.805 32.986 18.277 1.00 18.96 N ATOM 4748 CA VAL E 1 5.543 32.961 17.454 1.00 19.68 C ATOM 4749 CB VAL E 1 5.490 31.747 16.442 1.00 19.24 C ATOM 4750 CG1 VAL E 1 5.729 30.417 17.143 1.00 19.12 C ATOM 4751 CG2 VAL E 1 6.448 31.893 15.256 1.00 18.78 C ATOM 4752 C VAL E 1 5.209 34.318 16.766 1.00 20.53 C ATOM 4753 O VAL E 1 4.162 34.931 17.045 1.00 19.81 O ATOM 4754 N ARG E 2 6.036 34.659 15.814 1.00 22.30 N ATOM 4755 CA ARG E 2 5.893 35.826 14.996 1.00 22.98 C ATOM 4756 C ARG E 2 5.143 35.563 13.709 1.00 23.10 C ATOM 4757 O ARG E 2 3.987 35.675 13.626 1.00 21.38 O ATOM 4758 CB ARG E 2 5.370 36.923 15.862 1.00 20.00 C ATOM 4759 CG ARG E 2 6.510 37.666 16.472 1.00 20.00 C ATOM 4760 CD ARG E 2 6.236 37.842 17.914 1.00 20.00 C ATOM 4761 NE ARG E 2 5.023 38.606 18.152 1.00 20.00 N ATOM 4762 CZ ARG E 2 4.700 39.033 19.365 1.00 20.00 C ATOM 4763 NH1 ARG E 2 5.498 38.765 20.370 1.00 20.00 N ATOM 4764 NH2 ARG E 2 3.590 39.683 19.606 1.00 20.00 N ATOM 4765 N ALA E 3 5.874 35.228 12.682 1.00 25.76 N ATOM 4766 CA ALA E 3 5.370 34.410 11.547 1.00 29.63 C ATOM 4767 CB ALA E 3 6.254 33.159 11.469 1.00 30.22 C ATOM 4768 C ALA E 3 5.257 35.094 10.105 1.00 31.58 C ATOM 4769 O ALA E 3 5.874 36.130 9.844 1.00 31.51 O ATOM 4770 N ALA E 4 4.491 34.497 9.169 1.00 32.55 N ATOM 4771 CA ALA E 4 4.349 35.033 7.771 1.00 30.23 C ATOM 4772 CB ALA E 4 3.660 36.382 7.798 1.00 28.96 C ATOM 4773 C ALA E 4 3.600 34.141 6.772 1.00 29.50 C ATOM 4774 O ALA E 4 2.820 34.655 5.948 1.00 27.58 O ATOM 4775 N ARG F 1 8.429 19.552 9.416 1.00 25.91 N ATOM 4776 CA ARG F 1 9.556 20.144 8.678 1.00 28.61 C ATOM 4777 C ARG F 1 10.743 20.675 9.479 1.00 29.09 C ATOM 4778 O ARG F 1 11.224 20.098 10.395 1.00 27.32 O ATOM 4779 CB ARG F 1 10.034 19.244 7.562 1.00 20.00 C ATOM 4780 CG ARG F 1 9.026 18.241 7.099 1.00 20.00 C ATOM 4781 CD ARG F 1 9.684 16.875 6.961 1.00 20.00 C ATOM 4782 NE ARG F 1 8.851 15.706 6.762 1.00 20.00 N ATOM 4783 CZ ARG F 1 7.599 15.716 6.317 1.00 20.00 C ATOM 4784 NH1 ARG F 1 6.959 16.845 6.043 1.00 20.00 N ATOM 4785 NH2 ARG F 1 6.952 14.572 6.163 1.00 20.00 N ATOM 4786 N ALA F 2 11.202 21.816 9.078 1.00 31.68 N ATOM 4787 CA ALA F 2 11.921 22.706 9.931 1.00 35.91 C ATOM 4788 CB ALA F 2 11.159 24.023 9.929 1.00 36.85 C ATOM 4789 C ALA F 2 13.430 22.961 9.726 1.00 38.32 C ATOM 4790 O ALA F 2 13.892 23.333 8.669 1.00 34.79 O ATOM 4791 N ALA F 3 14.167 22.664 10.769 1.00 40.70 N ATOM 4792 CA ALA F 3 15.085 23.497 11.515 1.00 40.16 C ATOM 4793 CB ALA F 3 14.939 24.977 11.187 1.00 40.29 C ATOM 4794 C ALA F 3 16.524 23.097 11.612 1.00 37.96 C ATOM 4795 O ALA F 3 17.129 23.397 12.612 1.00 35.80 O END

Example 3

Comparison of PehPro1 with Thermolysin Structure

[0277] The structure of PehPro1 was compared to that of Thermolysin (B. thermoproteolyticus metalloprotease, pdb 1KEI.A) [Senda, M., Senda, T. and Kidokoro, S., Crystal Structure Analyses Of Thermolysin In Complex With Its Inhibitors, Direct Submission]. The overall folding of PehPro1 is highly similar to Thermolysin and other known metalloproteases from Bacillus (B. cereus (pdb 1NPC.A) [Sidler, W., Niederer, E., Suter, F. and Zuber, H., The primary structure of Bacillus cereus neutral proteinase and comparison with thermolysin and Bacillus subtilis neutral Proteinase, Biol. Chem. Hoppe-Seyler 367 (7), 643-657 (1986)] and B. stearothermophilus, and B. subtilis metalloproteases, consisting of two domains and a central connecting helix. A schematic of the overall topology of PehPro1 is presented and compared with Thermolysin in FIG. 2. The main differences were found in regions where there were deletions in the PehPro1 sequence relative to that of other known metalloprotease structures. Two regions of deletion occur in PehPro1, and as a consequence the main chain folding deviates from thermolysin after residue Trp58 of PehPro1 (see FIG. 3), and after residue Asp170 of PehPro1 (see FIG. 4). Four residues in Thermolysin are replaced by Asn59 in PehPro1 and seven residues in Thermolysin are replaced by Gly171-Lys172 in PehPro1, these deletions are indicated by arrows in FIG. 2. The numbering of residues corresponds to the linear contiguous sequence of each mature enzyme, respectively.

[0278] Four calcium ions are bound in the Thermolysin structure: two at a double cation site (Ca1,2), and one in each of the single cation sites (Ca3, Ca4). In contrast to Thermolysin, the PehPro1 structure has only two calcium binding sites, a single one near the double cation site (Ca1-2) in Thermolysin and a second (Ca4) that seems to be conserved in the two molecules. One Thermolysin calcium site (Ca3) is completely absent in the PehPro1 structure. Since calcium dependence is considered to be a factor in some potential uses of these proteases, particularly as a detergent additive where builders are present specifically to reduce the hardness of water by chelating ions such as calcium and magnesium, these enzymes may prove to have reduced cation sensitivity and hence improved stability under conditions of low calcium availability.

[0279] The region around the Thermolysin double cation site (Ca1,2) is shown in FIG. 5. In this figure, the structure of Thermolysin is present as black lines, with the two calcium ions shown as crosses. The superimposed structure of PehPro1 is shown as a stick figure with its single calcium ion as a non-bonding sphere. It may be seen that the two sites are substantially different. In Thermolysin, six residues along with solvent are present to stabilize the ion pair, including side chains of Asp138, Glu177, Asp 185, Glu190, and the main chain carbonyls of residues Asn183 and Glu187 (Thermolysin numbering). In PehPro1 (numbering relative to mature PehPro1), the calcium in the same vicinity is stabilized by side chains of Asp129, Asp131, Asp170 and Asp178 along with the solvent. Only Asp131 and Asp178 in PehPro1 are homologous with side chains in Thermolysin Asp138 and Glu190, respectively.

[0280] The second calcium binding site in PehPro1 is compared with the homologous site (Ca4) in Thermolysin in FIG. 6. In this instance, there is a one to one correspondence of residues forming the calcium binding site in both Thermolysin and PehPro1. In Thermolysin, the side chains of Thr194 and Asp200 (Thermolysin numbering) along with the main chain carbonyls of residues Tyr193, Thr194 and Ile197 form ligands to this calcium ion, while in PehPro1 it is the homologous residues Thr182 and Asp188 along with the carbonyl oxygen of residues Tyr181, Thr182 and Thr185 (numbering relative to mature PehPro1).

[0281] The structures of PehPro1 and Thermolysin are compared in the vicinity of the Ca3 calcium site in Thermolysin in FIG. 7. In Thermolysin the Ca3 calcium site is formed in a loop containing two aspartic acids residues Asp57 and Asp59, which along with the main chain carbonyl oxygen and solvent form ligands to the calcium ion, In contrast, in PehPro1, the two (Asp) ligands are replaced with serine residues which, while in homologous conformations, will not stabilize binding of a calcium ion. In the electron density map there is no evidence of calcium binding under the conditions of crystallization.

Example 4

Comparison of Structures of PehPro1 and PpoPro2 Metalloproteases

[0282] Recently, the structure of a metalloprotease from a member of the Paenibacillus genus, Paenibacillus polymyxa (PpoPro2), was reported (Ruf et al, Acta Cryst. D 69, 24-31 (2013)). The overall folding of PpoPro2 is highly homologous to Thermolysin and other known M4 metalloproteases. The PehPro1 and PpoPro2 structures consist of 304 residues that are aligned without insertions or deletions relative to each other. The PpoPro2 and PehPro1 structures therefore share a common pattern of deletions relative to that of other known metalloprotease structures. The overall folding of the PehPro1 and PpoPro2 is presented in FIG. 8.

[0283] In contrast to PehPro1, the structure of PpoPro2 was found to bind three calcium ions. The first two (Ca4 and a variant of Ca1-2) described below are highly homologous between PehPro1 and PpoPro2 molecules, and the third is homologous to calcium site Ca3 site. The common sites are compared in FIGS. 9 and 10. In both sites, all interactions seen in either PehPro1 or PpoPro2 are conserved in the other.

[0284] As mentioned above, the PpoPro2 has an additional calcium ion bound at Ca3 that is not seen in PehPro1. Just as in the structure of Thermolysin (FIG. 7), aspartic acid residues are found in PpoPro2 whereas in PehPro1, we find Ser 53 and Ser55 instead of the aspartic acid residues (FIG. 11).

Example 5

Crystallization and Structure Determination of NprE

[0285] The metalloprotease NprE, obtained from Bacillus subtilis, is known to perform in detergent formulations (as described in U.S. Pat. No. 8,114,656 B2 Shaw et al and others). An NprE variant (S1291/F130L/M138L/V190I/D220P) was crystallized using the hanging drop method from a solution of protein stock at a concentration of 26.2 mg/mL in 40% Propylene Glycol+50 mM MES pH 5.4+1 mM Calcium chloride. Aliquots of 3 L of the protein stock and 3 L of the crystallization solution were mixed on a plastic coverslip and inverted and sealed on a chamber containing 23% Polyethylene Glycol 4000+0.20M Lithium chloride+0.09M Bis Tris Propane pH 6.5+12% Isopropanol+4 mM Zinc chloride+12.5 mM Yttrium chloride in a Linbro 64 culture plate.

[0286] Crystals grew in the hexagonal space group P6(3)22 with unit cell dimensions; a=122.9 , b=122.9 , and c=119.1 . Data were collected on native crystal to 2.5 and the structure of NprE was determined by molecular replacement using a related protein (pdb ID 1ESP) as the phasing model. The statistics of data collection are presented in Table 5.1.

TABLE-US-00005 TABLE 5.1 Statistics of NprE Data collection Wavelength 1.54 Space group P6322 Molecules in asymmetric unit 1 Unit cell dimensions a = 122.9 , b = 122.9 and c = 1 19.1 Resolution 30.0 2.49 Unique reflections 17969 Multiplicity 7.46 (7.36*) Completeness 99.94% (99.9*) R.sub.merge 0.067 (0.25*) I/.sub.I 17.2 (5.9*) *Value in parenthesis is that of the outermost shell of data

[0287] The model was fitted in the resulting electron density using the program COOT [Emsley, P et al (2010) Acta Cryst. D66 486-501]. After fitting and refitting adjustments, the coordinates were refined using the REFMAC program with standard defaults in the CCP4 software suite. The statistics of the current model are presented in Table 5.2.

TABLE-US-00006 TABLE 5.2 Statistics of the refined model R work 0.20 R free 0.23 No. protein residues 300 No. atoms 2444 rmsd Bond lengths 0.024 rmsd bond angles 2.1
The coordinates for structure of the NprE variant are provided below.

TABLE-US-00007 ATOM 1 N ALA A 1 50.837 39.587 13.317 1.00 46.97 A N ATOM 2 CA ALA A 1 51.606 39.753 14.634 1.00 45.97 A C ATOM 3 CB ALA A 1 52.426 38.479 14.961 1.00 46.00 A C ATOM 4 C ALA A 1 50.598 40.107 15.764 1.00 45.46 A C ATOM 5 O ALA A 1 49.808 39.271 16.244 1.00 43.56 A O ATOM 6 N ALA A 2 50.582 41.387 16.118 1.00 45.03 A N ATOM 7 CA ALA A 2 49.511 41.916 16.936 1.00 44.55 A C ATOM 8 CB ALA A 2 49.635 43.447 17.040 1.00 44.73 A C ATOM 9 C ALA A 2 49.578 41.279 18.307 1.00 45.19 A C ATOM 10 O ALA A 2 50.549 41.460 19.038 1.00 46.01 A O ATOM 11 N THR A 3 48.571 40.506 18.675 1.00 45.24 A N ATOM 12 CA THR A 3 48.541 40.003 20.048 1.00 44.84 A C ATOM 13 CB THR A 3 49.272 38.639 20.200 1.00 44.49 A C ATOM 14 OG1 THR A 3 49.432 38.341 21.588 1.00 42.12 A O ATOM 15 CG2 THR A 3 48.529 37.520 19.521 1.00 41.95 A C ATOM 16 C THR A 3 47.144 40.023 20.726 1.00 45.42 A C ATOM 17 O THR A 3 46.153 40.548 20.182 1.00 46.03 A O ATOM 18 N THR A 4 47.105 39.436 21.913 1.00 44.79 A N ATOM 19 CA THR A 4 45.981 39.502 22.803 1.00 44.31 A C ATOM 20 CB THR A 4 46.352 40.377 24.023 1.00 45.17 A C ATOM 21 OG1 THR A 4 45.615 41.611 23.914 1.00 45.01 A O ATOM 22 CG2 THR A 4 46.117 39.684 25.418 1.00 46.18 A C ATOM 23 C THR A 4 45.505 38.090 23.095 1.00 43.59 A C ATOM 24 O THR A 4 46.263 37.144 22.990 1.00 43.13 A O ATOM 25 N GLY A 5 44.220 37.949 23.385 1.00 42.62 A N ATOM 26 CA GLY A 5 43.593 36.642 23.465 1.00 40.86 A C ATOM 27 C GLY A 5 42.380 36.751 24.358 1.00 39.27 A C ATOM 28 O GLY A 5 42.184 37.762 25.008 1.00 39.11 A O ATOM 29 N THR A 6 41.553 35.717 24.347 1.00 38.05 A N ATOM 30 CA THR A 6 40.412 35.657 25.213 1.00 37.20 A C ATOM 31 CB THR A 6 40.907 35.169 26.624 1.00 37.93 A C ATOM 32 OG1 THR A 6 40.731 36.218 27.585 1.00 37.23 A O ATOM 33 CG2 THR A 6 40.272 33.892 27.082 1.00 37.05 A C ATOM 34 C THR A 6 39.401 34.748 24.523 1.00 36.18 A C ATOM 35 O THR A 6 39.794 33.933 23.690 1.00 36.69 A O ATOM 36 N GLY A 7 38.109 34.926 24.791 1.00 34.95 A N ATOM 37 CA GLY A 7 37.092 34.018 24.258 1.00 33.82 A C ATOM 38 C GLY A 7 35.792 34.134 25.024 1.00 33.59 A C ATOM 39 O GLY A 7 35.645 35.006 25.862 1.00 34.18 A O ATOM 40 N THR A 8 34.849 33.253 24.732 1.00 33.90 A N ATOM 41 CA THR A 8 33.598 33.129 25.464 1.00 34.22 A C ATOM 42 CB THR A 8 33.226 31.608 25.718 1.00 34.37 A C ATOM 43 OG1 THR A 8 34.299 30.920 26.401 1.00 36.58 A O ATOM 44 CG2 THR A 8 31.947 31.481 26.536 1.00 33.08 A C ATOM 45 C THR A 8 32.453 33.790 24.669 1.00 34.72 A C ATOM 46 O THR A 8 32.184 33.426 23.489 1.00 34.25 A O ATOM 47 N THR A 9 31.753 34.728 25.323 1.00 34.59 A N ATOM 48 CA THR A 9 30.639 35.395 24.677 1.00 34.66 A C ATOM 49 CB THR A 9 30.238 36.722 25.329 1.00 33.98 A C ATOM 50 OG1 THR A 9 29.590 36.445 26.559 1.00 37.28 A O ATOM 51 CG2 THR A 9 31.414 37.551 25.590 1.00 33.59 A C ATOM 52 C THR A 9 29.431 34.488 24.559 1.00 34.50 A C ATOM 53 O THR A 9 29.385 33.400 25.144 1.00 33.46 A O ATOM 54 N LEU A 10 28.479 34.947 23.749 1.00 34.53 A N ATOM 55 CA LEU A 10 27.257 34.224 23.481 1.00 35.27 A C ATOM 56 CB LEU A 10 26.367 35.131 22.654 1.00 34.24 A C ATOM 57 CG LEU A 10 25.892 34.808 21.256 1.00 33.07 A C ATOM 58 CD1 LEU A 10 26.322 33.431 20.727 1.00 35.04 A C ATOM 59 CD2 LEU A 10 26.213 35.900 20.296 1.00 29.81 A C ATOM 60 C LEU A 10 26.539 33.859 24.786 1.00 37.02 A C ATOM 61 O LEU A 10 25.854 32.837 24.839 1.00 36.69 A O ATOM 62 N LYS A 11 26.672 34.715 25.801 1.00 38.07 A N ATOM 63 CA LYS A 11 26.036 34.498 27.084 1.00 41.05 A C ATOM 64 CB LYS A 11 25.488 35.850 27.666 1.00 41.74 A C ATOM 65 CG LYS A 11 24.330 36.532 26.896 1.00 41.97 A C ATOM 66 CD LYS A 11 23.014 35.884 27.186 1.00 40.92 A C ATOM 67 CE LYS A 11 21.854 36.797 26.839 1.00 44.19 A C ATOM 68 NZ LYS A 11 21.535 36.808 25.375 1.00 43.03 A N ATOM 69 C LYS A 11 26.996 33.861 28.134 1.00 42.61 A C ATOM 70 O LYS A 11 26.661 33.822 29.329 1.00 43.21 A O ATOM 71 N GLY A 12 28.198 33.427 27.730 1.00 43.01 A N ATOM 72 CA GLY A 12 29.046 32.651 28.623 1.00 42.11 A C ATOM 73 C GLY A 12 30.002 33.454 29.460 1.00 42.80 A C ATOM 74 O GLY A 12 30.566 32.919 30.409 1.00 43.22 A O ATOM 75 N LYS A 13 30.208 34.725 29.127 1.00 43.45 A N ATOM 76 CA LYS A 13 31.271 35.553 29.763 1.00 44.11 A C ATOM 77 CB LYS A 13 30.888 37.042 29.814 1.00 44.72 A C ATOM 78 CG LYS A 13 29.608 37.376 30.625 1.00 50.68 A C ATOM 79 CD LYS A 13 29.503 38.928 30.912 1.00 59.09 A C ATOM 80 CE LYS A 13 28.149 39.327 31.606 1.00 62.01 A C ATOM 81 NZ LYS A 13 28.222 40.646 32.356 1.00 60.47 A N ATOM 82 C LYS A 13 32.599 35.440 29.035 1.00 43.37 A C ATOM 83 O LYS A 13 32.647 35.028 27.894 1.00 43.72 A O ATOM 84 N THR A 14 33.676 35.837 29.697 1.00 43.02 A N ATOM 85 CA THR A 14 35.013 35.820 29.126 1.00 42.26 A C ATOM 86 CB THR A 14 36.049 35.120 30.099 1.00 42.99 A C ATOM 87 OG1 THR A 14 35.904 33.701 29.986 1.00 40.45 A O ATOM 88 CG2 THR A 14 37.519 35.492 29.794 1.00 41.44 A C ATOM 89 C THR A 14 35.441 37.241 28.799 1.00 42.01 A C ATOM 90 O THR A 14 35.330 38.123 29.644 1.00 42.35 A O ATOM 91 N VAL A 15 35.908 37.478 27.569 1.00 40.90 A N ATOM 92 CA VAL A 15 36.346 38.846 27.192 1.00 39.44 A C ATOM 93 CB VAL A 15 35.297 39.522 26.261 1.00 39.86 A C ATOM 94 CG1 VAL A 15 34.013 39.848 27.046 1.00 34.51 A C ATOM 95 CG2 VAL A 15 34.997 38.621 24.996 1.00 37.32 A C ATOM 96 C VAL A 15 37.779 38.883 26.600 1.00 39.22 A C ATOM 97 O VAL A 15 38.288 37.859 26.124 1.00 38.62 A O ATOM 98 N SER A 16 38.443 40.034 26.653 1.00 38.75 A N ATOM 99 CA SER A 16 39.693 40.193 25.874 1.00 39.39 A C ATOM 100 CB SER A 16 40.511 41.380 26.338 1.00 39.15 A C ATOM 101 OG SER A 16 40.729 41.230 27.691 1.00 43.31 A O ATOM 102 C SER A 16 39.402 40.439 24.405 1.00 39.11 A C ATOM 103 O SER A 16 38.488 41.214 24.085 1.00 39.19 A O ATOM 104 N LEU A 17 40.218 39.828 23.532 1.00 38.27 A N ATOM 105 CA LEU A 17 40.058 39.952 22.081 1.00 37.35 A C ATOM 106 CB LEU A 17 39.700 38.582 21.507 1.00 36.35 A C ATOM 107 CG LEU A 17 38.308 38.048 21.857 1.00 33.05 A C ATOM 108 CD1 LEU A 17 38.184 36.605 21.514 1.00 25.83 A C ATOM 109 CD2 LEU A 17 37.189 38.879 21.147 1.00 31.27 A C ATOM 110 C LEU A 17 41.371 40.406 21.500 1.00 37.48 A C ATOM 111 O LEU A 17 42.378 39.859 21.864 1.00 38.44 A O ATOM 112 N ASN A 18 41.383 41.413 20.628 1.00 37.00 A N ATOM 113 CA ASN A 18 42.589 41.755 19.891 1.00 36.02 A C ATOM 114 CB ASN A 18 42.560 43.192 19.444 1.00 35.98 A C ATOM 115 CG ASN A 18 42.465 44.148 20.596 1.00 39.27 A C ATOM 116 OD1 ASN A 18 41.623 45.048 20.623 1.00 43.56 A O ATOM 117 ND2 ASN A 18 43.324 43.971 21.558 1.00 40.11 A N ATOM 118 C ASN A 18 42.687 40.812 18.693 1.00 35.67 A C ATOM 119 O ASN A 18 41.822 40.804 17.838 1.00 34.62 A O ATOM 120 N ILE A 19 43.743 40.004 18.667 1.00 35.62 A N ATOM 121 CA ILE A 19 43.935 38.949 17.666 1.00 35.75 A C ATOM 122 CB ILE A 19 43.722 37.554 18.292 1.00 35.34 A C ATOM 123 CG1 ILE A 19 44.825 37.201 19.302 1.00 33.51 A C ATOM 124 CD1 ILE A 19 44.612 35.848 19.949 1.00 34.72 A C ATOM 125 CG2 ILE A 19 42.332 37.528 18.917 1.00 33.23 A C ATOM 126 C ILE A 19 45.291 39.046 16.909 1.00 36.80 A C ATOM 127 O ILE A 19 46.081 39.965 17.145 1.00 35.92 A O ATOM 128 N SER A 20 45.498 38.140 15.963 1.00 38.36 A N ATOM 129 CA SER A 20 46.765 38.045 15.189 1.00 40.90 A C ATOM 130 CB SER A 20 46.534 38.472 13.726 1.00 40.17 A C ATOM 131 OG SER A 20 47.498 37.935 12.855 1.00 39.41 A O ATOM 132 C SER A 20 47.313 36.615 15.209 1.00 42.05 A C ATOM 133 O SER A 20 46.530 35.668 14.952 1.00 42.63 A O ATOM 134 N SER A 21 48.586 36.438 15.529 1.00 43.64 A N ATOM 135 CA SER A 21 49.219 35.132 15.353 1.00 45.31 A C ATOM 136 CB SER A 21 50.357 34.872 16.336 1.00 45.18 A C ATOM 137 OG SER A 21 51.138 36.000 16.559 1.00 45.91 A O ATOM 138 C SER A 21 49.696 35.055 13.949 1.00 45.77 A C ATOM 139 O SER A 21 50.535 35.811 13.556 1.00 45.47 A O ATOM 140 N GLU A 22 49.113 34.148 13.193 1.00 47.74 A N ATOM 141 CA GLU A 22 49.171 34.189 11.767 1.00 49.15 A C ATOM 142 CB GLU A 22 47.892 34.769 11.260 1.00 49.13 A C ATOM 143 CG GLU A 22 48.016 36.086 10.722 1.00 46.55 A C ATOM 144 CD GLU A 22 46.717 36.646 10.354 1.00 39.46 A C ATOM 145 OE1 GLU A 22 45.983 35.997 9.639 1.00 34.91 A O ATOM 146 OE2 GLU A 22 46.432 37.720 10.806 1.00 32.47 A O ATOM 147 C GLU A 22 49.162 32.806 11.279 1.00 51.23 A C ATOM 148 O GLU A 22 48.381 32.018 11.727 1.00 52.04 A O ATOM 149 N SER A 23 49.996 32.494 10.320 1.00 52.77 A N ATOM 150 CA SER A 23 50.001 31.133 9.903 1.00 54.10 A C ATOM 151 CB SER A 23 48.649 30.810 9.340 1.00 54.93 A C ATOM 152 OG SER A 23 48.179 31.939 8.645 1.00 54.76 A O ATOM 153 C SER A 23 50.282 30.272 11.111 1.00 54.42 A C ATOM 154 O SER A 23 51.075 30.606 11.970 1.00 55.29 A O ATOM 155 N GLY A 24 49.653 29.143 11.212 1.00 54.60 A N ATOM 156 CA GLY A 24 50.035 28.344 12.342 1.00 54.68 A C ATOM 157 C GLY A 24 49.544 28.801 13.683 1.00 54.45 A C ATOM 158 O GLY A 24 50.009 28.324 14.682 1.00 54.42 A O ATOM 159 N LYS A 25 48.589 29.717 13.685 1.00 53.42 A N ATOM 160 CA LYS A 25 47.626 29.848 14.742 1.00 51.96 A C ATOM 161 CB LYS A 25 46.345 29.213 14.276 1.00 51.64 A C ATOM 162 CG LYS A 25 46.385 28.938 12.870 1.00 54.15 A C ATOM 163 CD LYS A 25 45.570 29.847 12.097 1.00 57.56 A C ATOM 164 CE LYS A 25 44.768 29.072 11.100 1.00 60.94 A C ATOM 165 NZ LYS A 25 44.500 29.845 9.858 1.00 61.61 A N ATOM 166 C LYS A 25 47.270 31.238 15.143 1.00 51.03 A C ATOM 167 O LYS A 25 48.023 32.164 15.011 1.00 51.65 A O ATOM 168 N TYR A 26 46.058 31.349 15.644 1.00 48.55 A N ATOM 169 CA TYR A 26 45.481 32.609 15.998 1.00 45.54 A C ATOM 170 CB TYR A 26 45.266 32.653 17.468 1.00 45.44 A C ATOM 171 CG TYR A 26 46.525 32.475 18.221 1.00 47.36 A C ATOM 172 CD1 TYR A 26 47.208 33.550 18.707 1.00 47.06 A C ATOM 173 CE1 TYR A 26 48.330 33.377 19.398 1.00 50.44 A C ATOM 174 CZ TYR A 26 48.788 32.124 19.615 1.00 49.90 A C ATOM 175 OH TYR A 26 49.922 31.948 20.312 1.00 52.47 A O ATOM 176 CE2 TYR A 26 48.138 31.061 19.143 1.00 46.84 A C ATOM 177 CD2 TYR A 26 47.028 31.228 18.457 1.00 46.94 A C ATOM 178 C TYR A 26 44.191 32.834 15.297 1.00 43.35 A C ATOM 179 O TYR A 26 43.380 31.955 15.155 1.00 42.38 A O ATOM 180 N VAL A 27 44.026 34.045 14.834 1.00 40.47 A N ATOM 181 CA VAL A 27 42.808 34.391 14.083 1.00 38.59 A C ATOM 182 CB VAL A 27 43.103 34.570 12.556 1.00 38.99 A C ATOM 183 CG1 VAL A 27 43.789 33.357 12.001 1.00 38.60 A C ATOM 184 CG2 VAL A 27 43.963 35.855 12.313 1.00 37.66 A C ATOM 185 C VAL A 27 42.118 35.672 14.643 1.00 36.60 A C ATOM 186 O VAL A 27 42.781 36.552 15.270 1.00 34.97 A O ATOM 187 N LEU A 28 40.815 35.780 14.379 1.00 33.39 A N ATOM 188 CA LEU A 28 40.087 37.030 14.686 1.00 33.31 A C ATOM 189 CB LEU A 28 38.592 36.741 14.896 1.00 30.82 A C ATOM 190 CG LEU A 28 38.370 35.763 16.069 1.00 29.25 A C ATOM 191 CD1 LEU A 28 36.887 35.614 16.436 1.00 25.75 A C ATOM 192 CD2 LEU A 28 39.188 36.282 17.297 1.00 27.62 A C ATOM 193 C LEU A 28 40.356 38.195 13.692 1.00 29.91 A C ATOM 194 O LEU A 28 39.512 38.572 12.864 1.00 28.72 A O ATOM 195 N ARG A 29 41.548 38.759 13.821 1.00 29.17 A N ATOM 196 CA ARG A 29 41.983 39.934 13.093 1.00 29.07 A C ATOM 197 CB ARG A 29 43.031 39.566 12.002 1.00 28.30 A C ATOM 198 CG ARG A 29 43.815 40.779 11.438 1.00 29.82 A C ATOM 199 CD ARG A 29 44.958 40.532 10.414 1.00 29.04 A C ATOM 200 NE ARG A 29 44.832 39.314 9.598 1.00 28.43 A N ATOM 201 CZ ARG A 29 44.170 39.129 8.449 1.00 27.95 A C ATOM 202 NH1 ARG A 29 43.416 40.064 7.875 1.00 28.57 A N ATOM 203 NH2 ARG A 29 44.232 37.925 7.885 1.00 29.61 A N ATOM 204 C ARG A 29 43.556 40.961 14.088 1.00 29.23 A C ATOM 205 O ARG A 29 43.510 40.685 14.745 1.00 28.41 A O ATOM 206 N ASP A 30 41.990 42.170 14.153 1.00 30.20 A N ATOM 207 CA ASP A 30 42.364 43.158 15.151 1.00 30.03 A C ATOM 208 CB ASP A 30 41.100 43.849 15.701 1.00 29.34 A C ATOM 209 CG ASP A 30 41.383 44.840 16.878 1.00 30.84 A C ATOM 210 OD1 ASP A 30 42.525 45.362 17.072 1.00 29.94 A O ATOM 211 OD2 ASP A 30 40.425 45.107 17.621 1.00 27.79 A O ATOM 212 C ASP A 30 43.360 44.123 14.524 1.00 30.55 A C ATOM 213 O ASP A 30 43.089 44.784 13.525 1.00 29.55 A O ATOM 214 N LEU A 31 44.531 44.182 15.129 1.00 31.84 A N ATOM 215 CA LEU A 31 45.673 44.804 14.522 1.00 33.66 A C ATOM 216 CB LEU A 31 46.741 43.758 14.269 1.00 33.92 A C ATOM 217 CG LEU A 31 47.021 43.233 12.839 1.00 37.06 A C ATOM 218 CD1 LEU A 31 45.876 43.230 11.897 1.00 35.24 A C ATOM 219 CD2 LEU A 31 47.674 41.810 12.854 1.00 38.45 A C ATOM 220 C LEU A 31 46.189 45.830 15.479 1.00 35.24 A C ATOM 221 O LEU A 31 47.292 46.339 15.306 1.00 36.18 A O ATOM 222 N SER A 32 45.347 46.150 16.474 1.00 36.86 A N ATOM 223 CA SER A 32 45.652 47.055 17.588 1.00 36.85 A C ATOM 224 CB SER A 32 45.024 46.556 18.925 1.00 36.60 A C ATOM 225 OG SER A 32 43.606 46.774 18.972 1.00 38.59 A O ATOM 226 C SER A 32 45.197 48.468 17.297 1.00 37.03 A C ATOM 227 O SER A 32 45.544 49.365 18.061 1.00 36.94 A O ATOM 228 N LYS A 33 44.434 48.691 16.225 1.00 37.38 A N ATOM 229 CA LYS A 33 43.866 50.038 16.026 1.00 38.79 A C ATOM 230 CB LYS A 33 42.573 50.035 15.186 1.00 38.26 A C ATOM 231 CG LYS A 33 41.473 49.071 15.689 1.00 34.67 A C ATOM 232 CD LYS A 33 41.118 49.392 17.134 1.00 30.21 A C ATOM 233 CE LYS A 33 39.984 48.532 17.680 1.00 29.07 A C ATOM 234 NZ LYS A 33 39.732 48.697 19.185 1.00 23.25 A N ATOM 235 C LYS A 33 44.895 51.052 15.503 1.00 41.30 A C ATOM 236 O LYS A 33 45.622 50.798 14.530 1.00 40.23 A O ATOM 237 N PRO A 34 44.958 52.230 16.147 1.00 44.22 A N ATOM 238 CA PRO A 34 46.201 52.950 15.790 1.00 45.38 A C ATOM 239 CB PRO A 34 46.352 54.000 16.926 1.00 47.30 A C ATOM 240 CG PRO A 34 44.809 54.186 17.497 1.00 48.14 A C ATOM 241 CD PRO A 34 43.951 53.092 16.834 1.00 44.53 A C ATOM 242 C PRO A 34 46.125 53.585 14.377 1.00 44.92 A C ATOM 243 O PRO A 34 47.134 54.070 13.845 1.00 45.69 A O ATOM 244 N THR A 35 44.963 53.546 13.741 1.00 42.51 A N ATOM 245 CA THR A 35 44.926 54.019 12.364 1.00 40.40 A C ATOM 246 CB THR A 35 43.499 54.070 12.004 1.00 41.17 A C ATOM 247 OG1 THR A 35 42.610 53.546 12.332 1.00 40.39 A O ATOM 248 CG2 THR A 35 43.107 55.773 12.741 1.00 39.31 A C ATOM 249 C THR A 35 45.346 52.956 11.315 1.00 38.28 A C ATOM 250 O THR A 35 45.433 53.269 10.120 1.00 36.30 A O ATOM 251 N GLY A 36 45.536 51.702 11.755 1.00 36.35 A N ATOM 252 CA GLY A 36 45.713 50.583 10.830 1.00 32.77 A C ATOM 253 C GLY A 36 44.426 49.842 10.507 1.00 31.89 A C ATOM 254 O GLY A 36 44.456 48.780 9.912 1.00 31.63 A O ATOM 255 N THR A 37 43.266 50.351 10.924 1.00 30.83 A N ATOM 256 CA THR A 37 42.003 49.747 10.482 1.00 27.70 A C ATOM 257 CB THR A 37 40.819 50.642 10.820 1.00 27.55 A C ATOM 258 OG1 THR A 37 40.960 51.876 10.095 1.00 28.01 A O ATOM 259 CG2 THR A 37 39.494 49.979 10.501 1.00 23.29 A C ATOM 260 C THR A 37 41.851 48.380 11.106 1.00 26.95 A C ATOM 261 O THR A 37 41.941 48.260 12.281 1.00 26.14 A O ATOM 262 N GLN A 38 41.525 47.385 10.329 1.00 26.09 A N ATOM 263 CA GLN A 38 41.319 46.059 10.826 1.00 26.76 A C ATOM 264 CB GLN A 38 41.863 45.066 9.816 1.00 27.60 A C ATOM 265 CG GLN A 38 43.300 44.836 9.957 1.00 30.56 A C ATOM 266 CD GLN A 38 43.913 44.030 8.864 1.00 34.02 A C ATOM 267 OE1 GLN A 38 43.367 43.074 8.393 1.00 35.21 A O ATOM 268 NE2 GLN A 38 45.077 44.404 8.485 1.00 31.60 A N ATOM 269 C GLN A 38 39.881 45.752 11.122 1.00 25.09 A C ATOM 270 O GLN A 39 39.025 46.182 10.432 1.00 26.13 A O ATOM 271 N ILE A 39 39.629 45.004 12.176 1.00 23.80 A N ATOM 272 CA ILE A 39 38.346 44.336 12.348 1.00 24.26 A C ATOM 273 CB ILE A 39 37.699 44.596 13.772 1.00 24.68 A C ATOM 274 CG1 ILE A 39 37.395 46.080 14.014 1.00 21.84 A C ATOM 275 CD1 ILE A 39 38.507 46.585 14.474 1.00 21.10 A C ATOM 276 CG2 ILE A 39 36.388 43.745 13.945 1.00 24.04 A C ATOM 277 C ILE A 39 38.587 42.826 12.122 1.00 24.60 A C ATOM 278 O ILE A 39 39.521 42.255 12.681 1.00 25.49 A O ATOM 279 N ILE A 40 37.804 42.171 11.281 1.00 24.30 A N ATOM 280 CA ILE A 40 38.138 40.820 10.904 1.00 24.67 A C ATOM 281 CB ILE A 40 38.760 40.776 9.481 1.00 25.40 A C ATOM 282 CG1 ILE A 40 39.778 41.902 9.248 1.00 46.78 A C ATOM 283 CD1 ILE A 40 40.256 41.969 7.776 1.00 28.72 A C ATOM 284 CG2 ILE A 40 39.456 39.440 9.198 1.00 25.40 A C ATOM 285 C ILE A 40 36.831 40.033 10.917 1.00 25.31 A C ATOM 286 O ILE A 40 35.881 40.469 10.303 1.00 25.86 A O ATOM 287 N THR A 41 36.785 38.864 11.577 1.00 25.27 A N ATOM 288 CA THR A 41 35.535 38.168 11.811 1.00 24.40 A C ATOM 289 CB THR A 41 35.271 38.016 13.322 1.00 23.99 A C ATOM 290 OG1 THR A 41 35.523 39.264 13.986 1.00 24.89 A O ATOM 291 CG2 THR A 41 33.870 37.563 13.592 1.00 20.66 A C ATOM 292 C THR A 41 35.545 36.793 11.150 1.00 26.35 A C ATOM 293 O THR A 41 36.499 36.004 11.319 1.00 26.67 A O ATOM 294 N TYR A 42 34.488 36.490 10.401 1.00 26.81 A N ATOM 295 CA TYR A 42 34.470 35.288 9.624 1.00 28.66 A C ATOM 296 CB TYR A 42 34.363 35.615 8.121 1.00 29.19 A C ATOM 297 CG TYR A 42 35.602 36.234 7.554 1.00 28.72 A C ATOM 298 CD1 TYR A 42 35.834 37.620 7.674 1.00 29.76 A C ATOM 299 CE1 TYR A 42 36.985 38.198 7.145 1.00 30.70 A C ATOM 300 CZ TYR A 42 37.913 37.389 6.473 1.00 32.18 A C ATOM 301 OH TYR A 42 39.044 37.951 5.962 1.00 34.06 A O ATOM 302 CE2 TYR A 42 37.732 36.002 6.366 1.00 29.34 A C ATOM 303 CD2 TYR A 42 36.556 35.441 6.883 1.00 28.41 A C ATOM 304 C TYR A 42 33.275 34.456 10.028 1.00 30.08 A C ATOM 305 O TYR A 42 32.293 34.980 10.550 1.00 29.14 A O ATOM 306 N ASP A 43 33.356 33.160 9.738 1.00 31.69 A N ATOM 307 CA ASP A 43 32.296 32.216 10.075 1.00 33.46 A C ATOM 308 CB ASP A 43 32.867 31.090 10.989 1.00 32.64 A C ATOM 309 CG ASP A 43 31.851 29.958 11.296 1.00 32.89 A C ATOM 310 OD1 ASP A 43 30.696 29.966 10.757 1.00 30.15 A O ATOM 311 OD2 ASP A 43 32.236 29.054 12.087 1.00 32.73 A O ATOM 312 C ASP A 43 31.740 31.685 8.754 1.00 34.58 A C ATOM 313 O ASP A 43 32.470 31.124 7.943 1.00 35.27 A O ATOM 314 N LEU A 44 30.453 31.866 8.521 1.00 36.27 A N ATOM 315 CA LEU A 44 29.884 31.438 7.245 1.00 37.65 A C ATOM 316 CB LEU A 44 28.720 32.371 6.881 1.00 37.26 A C ATOM 317 CG LEU A 44 28.521 33.054 5.509 1.00 39.07 A C ATOM 318 CD1 LEU A 44 29.742 33.120 4.619 1.00 36.83 A C ATOM 319 CD2 LEU A 44 27.831 34.449 5.635 1.00 37.50 A C ATOM 320 C LEU A 44 29.472 29.939 7.294 1.00 38.87 A C ATOM 321 O LEU A 44 29.162 29.343 6.279 1.00 39.39 A O ATOM 322 N GLN A 45 29.471 29.328 8.482 1.00 40.24 A N ATOM 323 CA GLN A 45 28.976 27.955 8.653 1.00 40.83 A C ATOM 324 CB GLN A 45 30.003 26.930 8.127 1.00 40.93 A C ATOM 325 CG GLN A 45 31.400 27.042 8.843 1.00 43.55 A C ATOM 326 CD GLN A 45 32.557 26.463 8.026 1.00 46.24 A C ATOM 327 OE1 GLN A 45 32.440 26.239 6.825 1.00 48.19 A O ATOM 328 NE2 GLN A 45 33.669 26.215 8.680 1.00 44.67 A N ATOM 329 C GLN A 45 27.607 27.785 8.002 1.00 41.18 A C ATOM 330 O GLN A 45 27.368 26.809 7.304 1.00 42.73 A O ATOM 331 N ASN A 46 26.710 28.738 8.202 1.00 40.77 A N ATOM 332 CA ASN A 46 25.305 28.565 7.818 1.00 41.87 A C ATOM 333 CB ASN A 46 24.676 27.325 8.485 1.00 41.62 A C ATOM 334 CG ASN A 46 24.762 27.374 10.029 1.00 42.52 A C ATOM 335 OD1 ASN A 46 25.384 26.511 10.647 1.00 42.00 A O ATOM 336 ND2 ASN A 46 24.173 28.426 10.642 1.00 39.75 A N ATOM 337 C ASN A 46 24.977 28.607 6.340 1.00 43.16 A C ATOM 338 O ASN A 46 23.805 28.419 6.002 1.00 42.88 A O ATOM 339 N ARG A 47 25.992 28.859 5.485 1.00 44.54 A N ATOM 340 CA ARG A 47 25.793 29.192 4.062 1.00 46.84 A C ATOM 341 CB ARG A 47 27.013 28.809 3.177 1.00 47.30 A C ATOM 342 CG ARG A 47 28.061 27.854 3.818 1.00 52.65 A C ATOM 343 CD ARG A 47 28.528 26.620 2.951 1.00 60.12 A C ATOM 344 NE ARG A 47 24.637 25.455 3.151 1.00 65.09 A N ATOM 345 CZ ARG A 47 24.824 24.450 4.026 1.00 67.61 A C ATOM 346 NH1 ARG A 47 28.902 24.400 4.820 1.00 67.70 A N ATOM 347 NH2 ARG A 47 26.908 23.483 4.120 1.00 67.50 A N ATOM 348 C ARG A 47 25.431 30.704 3.904 1.00 47.66 A C ATOM 349 O ARG A 47 25.563 31.500 4.854 1.00 47.75 A O ATOM 350 N GLU A 48 24.958 31.100 2.723 1.00 48.47 A N ATOM 351 CA GLU A 48 24.549 32.484 2.482 1.00 49.38 A C ATOM 352 CB GLU A 48 23.016 32.618 2.288 1.00 49.89 A C ATOM 353 CG GLU A 48 22.140 31.848 3.281 1.00 53.97 A C ATOM 354 CD GLU A 48 20.699 32.390 3.369 1.00 58.12 A C ATOM 355 OE1 GLU A 48 20.138 32.504 4.487 1.00 58.48 A O ATOM 356 OE2 GLU A 48 20.118 32.708 2.314 1.00 60.70 A O ATOM 357 C GLU A 48 25.241 33.080 1.258 1.00 49.02 A C ATOM 358 O GLU A 48 24.821 34.136 0.773 1.00 48.86 A O ATOM 359 N TYR A 49 26.282 32.411 0.752 1.00 48.71 A N ATOM 360 CA TYR A 49 26.949 32.832 0.497 1.00 48.43 A C ATOM 361 CB TYR A 49 26.434 32.015 1.710 1.00 49.21 A C ATOM 362 CG TYR A 49 26.684 30.530 1.510 1.00 53.66 A C ATOM 363 CD1 TYR A 49 25.753 39.740 0.794 1.00 57.40 A C ATOM 364 CD1 TYR A 49 25.994 28.371 0.564 1.00 61.43 A C ATOM 365 CZ TYR A 49 27.197 27.783 1.046 1.00 63.54 A C ATOM 366 OH TYR A 49 27.421 26.423 0.803 1.00 65.65 A O ATOM 367 CE2 TYR A 49 28.150 28.560 1.742 1.00 59.44 A C ATOM 368 CD2 TYR A 49 27.883 29.918 1.975 1.00 56.66 A C ATOM 369 C TYR A 49 28.438 32.632 0.350 1.00 47.07 A C ATOM 370 O TYR A 49 28.896 31.946 0.594 1.00 46.06 A O ATOM 371 N ASN A 50 29.192 33.194 1.315 1.00 46.10 A N ATOM 372 CA ASN A 50 30.657 33.095 1.331 1.00 43.95 A C ATOM 373 CB ASN A 50 31.101 31.597 1.518 1.00 44.54 A C ATOM 374 CG ASN A 50 32.582 31.439 1.975 1.00 46.46 A C ATOM 375 OD1 ASN A 50 33.116 32.261 2.725 1.00 47.44 A O ATOM 376 ND2 ASN A 50 33.238 30.373 1.511 1.00 48.73 A N ATOM 377 C ASN A 50 31.196 33.744 0.023 1.00 41.68 A C ATOM 378 O ASN A 50 32.011 33.161 0.691 1.00 40.51 A O ATOM 379 N LEU A 51 30.711 34.952 0.266 1.00 39.34 A N ATOM 380 CA LEU A 51 31.135 35.742 1.434 1.00 38.05 A C ATOM 381 CB LEU A 51 30.272 37.011 1.608 1.00 36.68 A C ATOM 382 CG LEU A 51 28.736 36.853 1.766 1.00 38.02 A C ATOM 383 CD1 LEU A 51 28.040 37.730 2.821 1.00 30.41 A C ATOM 384 CD2 LEU A 51 28.301 35.401 1.953 1.00 38.51 A C ATOM 385 C LEU A 51 32.609 36.125 1.302 1.00 37.04 A C ATOM 386 O LEU A 51 33.115 36.208 0.183 1.00 38.60 A O ATOM 387 N PRO A 52 33.296 36.391 2.426 1.00 35.16 A N ATOM 388 CA PRO A 52 32.736 36.442 3.785 1.00 35.00 A C ATOM 389 CB PRO A 52 33.631 37.467 4.472 1.00 34.76 A C ATOM 390 CG PRO A 52 34.968 37.210 3.835 1.00 35.21 A C ATOM 391 CD PRO A 52 34.680 36.861 2.384 1.00 33.35 A C ATOM 392 C PRO A 52 32.741 35.098 4.564 1.00 34.93 A C ATOM 393 O PRO A 52 32.065 34.989 5.602 1.00 35.60 A O ATOM 394 N GLY A 53 33.486 34.105 4.068 1.00 34.24 A N ATOM 395 CA GLY A 53 33.572 32.778 4.661 1.00 33.02 A C ATOM 396 C GLY A 53 34.949 32.535 5.260 1.00 32.97 A C ATOM 397 O GLY A 53 35.952 33.093 4.807 1.00 33.28 A O ATOM 398 N THR A 54 34.967 31.739 6.320 1.00 32.27 A N ATOM 399 CA THR A 54 36.160 31.260 6.945 1.00 32.37 A C ATOM 400 CB THR A 54 35.947 29.811 7.437 1.00 32.98 A C ATOM 401 OG1 THR A 54 35.393 29.041 6.360 1.00 34.33 A O ATOM 402 CG2 THR A 54 37.276 29.167 8.007 1.00 31.11 A C ATOM 403 C THR A 54 36.605 32.137 8.106 1.00 32.94 A C ATOM 404 O THR A 54 35.878 32.380 9.087 1.00 31.68 A O ATOM 405 N LEU A 55 37.838 32.586 7.987 1.00 33.67 A N ATOM 406 CA LEU A 55 38.430 33.378 8.995 1.00 35.36 A C ATOM 407 CB LEU A 55 39.855 33.704 8.577 1.00 34.52 A C ATOM 408 CG LEU A 55 40.594 34.680 9.486 1.00 37.35 A C ATOM 409 CD1 LEU A 55 39.853 36.006 9.710 1.00 32.36 A C ATOM 410 CD2 LEU A 55 41.990 34.945 8.959 1.00 38.13 A C ATOM 411 C LEU A 55 38.335 32.533 10.275 1.00 36.98 A C ATOM 412 O LEU A 55 38.680 31.346 10.269 1.00 37.92 A O ATOM 413 N VAL A 56 37.811 33.123 11.355 1.00 37.30 A N ATOM 414 CA VAL A 56 37.657 32.406 12.591 1.00 36.64 A C ATOM 415 CB VAL A 56 36.625 33.113 13.515 1.00 36.80 A C ATOM 416 CG1 VAL A 56 36.762 32.623 14.916 1.00 34.94 A C ATOM 417 CG2 VAL A 56 35.191 32.844 13.013 1.00 32.55 A C ATOM 418 C VAL A 56 39.034 32.199 13.231 1.00 38.20 A C ATOM 419 O VAL A 56 39.807 33.136 13.400 1.00 38.95 A O ATOM 420 N SER A 57 39.370 30.966 13.578 1.00 40.18 A N ATOM 421 CA SER A 57 40.712 30.721 14.141 1.00 41.41 A C ATOM 422 CB SER A 57 41.729 30.414 13.036 1.00 41.73 A C ATOM 423 OG SER A 57 41.165 29.456 12.199 1.00 42.33 A O ATOM 424 C SER A 57 40.771 29.642 15.221 1.00 42.87 A C ATOM 425 O SER A 57 39.889 28.786 15.312 1.00 42.53 A O ATOM 426 N SER A 58 41.805 29.725 16.046 1.00 43.46 A N ATOM 427 CA SER A 58 42.064 28.689 17.021 1.00 45.24 A C ATOM 428 CB SER A 58 41.435 29.040 18.379 1.00 44.87 A C ATOM 429 OG SER A 58 42.368 28.988 19.446 1.00 43.17 A O ATOM 430 C SER A 58 43.572 28.385 17.143 1.00 46.75 A C ATOM 431 O SER A 58 44.444 29.258 16.870 1.00 45.93 A O ATOM 432 N THR A 59 43.872 27.155 17.572 1.00 47.81 A N ATOM 433 CA THR A 59 45.272 26.786 17.788 1.00 48.79 A C ATOM 434 CB THR A 59 45.480 25.278 17.829 1.00 49.03 A C ATOM 435 OG1 THR A 59 44.902 24.807 19.041 1.00 49.03 A O ATOM 436 CG2 THR A 59 44.827 24.562 16.589 1.00 48.04 A C ATOM 437 C THR A 59 45.820 27.435 19.055 1.00 48.93 A C ATOM 438 O THR A 59 47.025 27.449 19.250 1.00 49.98 A O ATOM 439 N THR A 60 44.956 28.002 19.889 1.00 48.95 A N ATOM 440 CA THR A 60 45.416 28.777 21.048 1.00 49.54 A C ATOM 441 CB THR A 60 44.976 28.152 22.416 1.00 50.77 A C ATOM 442 OG1 THR A 60 43.537 27.921 22.449 1.00 50.15 A O ATOM 443 CG2 THR A 60 45.795 26.834 22.706 1.00 49.54 A C ATOM 444 C THR A 60 44.927 30.207 21.074 1.00 49.42 A C ATOM 445 O THR A 60 44.079 30.621 20.300 1.00 49.57 A O ATOM 446 N ASN A 61 45.521 30.947 21.987 1.00 48.77 A N ATOM 447 CA ASN A 61 45.036 32.187 22.505 1.00 47.80 A C ATOM 448 CB ASN A 61 45.682 32.345 23.885 1.00 48.54 A C ATOM 449 CG ASN A 61 46.190 33.713 24.078 1.00 52.04 A C ATOM 450 OD1 ASN A 61 46.532 34.150 25.180 1.00 52.14 A O ATOM 451 ND2 ASN A 61 46.237 34.448 22.960 1.00 58.59 A N ATOM 452 C ASN A 61 43.527 32.339 22.754 1.00 46.83 A C ATOM 453 O ASN A 61 43.056 33.455 23.094 1.00 45.82 A O ATOM 454 N GLN A 62 42.780 31.234 22.648 1.00 45.02 A N ATOM 455 CA GLN A 62 41.465 31.161 23.273 1.00 43.93 A C ATOM 456 CB GLN A 62 41.479 30.234 24.529 1.00 44.43 A C ATOM 457 CG GLN A 62 42.303 30.766 25.762 1.00 49.48 A C ATOM 458 CD GLN A 62 41.858 30.185 27.192 1.00 56.15 A C ATOM 459 OE1 GLN A 62 40.951 29.336 27.299 1.00 55.55 A O ATOM 460 NE2 GLN A 62 42.511 30.683 28.274 1.00 54.68 A N ATOM 461 C GLN A 62 40.379 30.760 22.285 1.00 42.39 A C ATOM 462 O GLN A 62 40.507 29.738 21.575 1.00 41.48 A O ATOM 463 N PHE A 63 39.299 31.553 22.240 1.00 40.50 A N ATOM 464 CA PHE A 63 38.183 31.224 21.338 1.00 39.06 A C ATOM 465 CB PHE A 63 37.901 32.388 20.376 1.00 38.22 A C ATOM 466 CG PHE A 63 39.057 32.701 19.488 1.00 33.68 A C ATOM 467 CD1 PHE A 63 40.184 33.360 20.008 1.00 26.93 A C ATOM 468 CE1 PHE A 63 41.301 33.621 19.216 1.00 24.98 A C ATOM 469 CZ PHE A 63 41.285 33.253 17.871 1.00 23.12 A C ATOM 470 CE2 PHE A 63 40.143 32.585 17.311 1.00 26.49 A C ATOM 471 CD2 PHE A 63 39.044 32.300 18.132 1.00 30.53 A C ATOM 472 C PHE A 63 36.977 30.840 22.146 1.00 39.10 A C ATOM 473 O PHE A 63 36.152 31.698 22.538 1.00 38.84 A O ATOM 474 N THR A 64 36.891 29.544 22.428 1.00 38.79 A N ATOM 475 CA THR A 64 35.953 29.061 23.422 1.00 38.65 A C ATOM 476 CB THR A 64 36.671 28.406 24.642 1.00 39.24 A C ATOM 477 OG1 THR A 64 37.175 27.118 24.253 1.00 36.93 A O ATOM 478 CG2 THR A 64 37.812 29.295 25.262 1.00 35.51 A C ATOM 479 C THR A 64 34.986 28.050 22.862 1.00 39.61 A C ATOM 480 O THR A 64 34.181 27.525 23.589 1.00 41.43 A O ATOM 481 N THR A 65 35.033 27.741 21.586 1.00 39.94 A N ATOM 482 CA THR A 65 34.115 26.719 21.101 1.00 40.84 A C ATOM 483 CB THR A 65 34.622 26.076 19.777 1.00 41.39 A C ATOM 484 OG1 THR A 65 34.335 26.930 18.639 1.00 45.44 A O ATOM 485 CG2 THR A 65 36.149 25.779 19.880 1.00 39.64 A C ATOM 486 C THR A 65 32.716 27.304 20.962 1.00 41.43 A C ATOM 487 O THR A 65 32.535 28.526 20.920 1.00 42.73 A O ATOM 488 N SER A 66 31.700 26.465 20.890 1.00 41.45 A N ATOM 489 CA SER A 66 30.363 27.017 20.947 1.00 41.32 A C ATOM 490 CB SER A 66 29.307 25.956 21.314 1.00 41.67 A C ATOM 491 OG SER A 66 28.943 25.262 20.148 1.00 42.16 A O ATOM 492 C SER A 66 30.011 27.800 19.658 1.00 40.64 A C ATOM 493 O SER A 66 29.354 28.846 19.737 1.00 41.27 A O ATOM 494 N SER A 67 60.456 27.327 18.495 1.00 38.90 A N ATOM 495 CA SER A 67 30.160 28.045 17.230 1.00 37.15 A C ATOM 496 CB SER A 67 30.297 27.124 15.998 1.00 37.36 A C ATOM 497 OG SER A 67 31.667 26.844 15.786 1.00 38.44 A O ATOM 498 C SER A 67 30.986 29.349 17.077 1.00 35.34 A C ATOM 499 O SER A 67 30.624 30.228 16.287 1.00 33.43 A O ATOM 500 N GLN A 68 32.039 29.457 17.882 1.00 33.79 A N ATOM 501 CA GLN A 68 32.809 30.662 18.027 1.00 34.91 A C ATOM 502 CB GLN A 68 34.204 30.295 18.571 1.00 34.66 A C ATOM 503 CG GLN A 68 25.212 29.824 17.504 1.00 38.08 A C ATOM 504 CD GLN A 68 36.542 29.280 18.091 1.00 42.37 A C ATOM 505 OE1 GLN A 68 36.660 28.995 19.300 1.00 44.88 A O ATOM 506 NE2 GLN A 68 37.549 29.160 17.230 1.00 40.98 A N ATOM 507 C GLN A 68 32.221 31.796 18.942 1.00 35.05 A C ATOM 508 O GLN A 68 32.826 32.901 19.060 1.00 34.80 A O ATOM 509 N ARG A 69 31.125 31.505 19.661 1.00 34.05 A N ATOM 510 CA ARG A 69 30.582 32.456 20.596 1.00 32.71 A C ATOM 511 CB ARG A 69 29.503 31.788 21.418 1.00 33.66 A C ATOM 512 CG ARG A 69 30.046 31.047 22.706 1.00 37.81 A C ATOM 513 CD ARG A 69 28.885 30.461 23.501 1.00 43.53 A C ATOM 514 NE ARG A 69 29.328 29.621 24.606 1.00 49.85 A N ATOM 515 CZ ARG A 69 28.711 29.520 25.780 1.00 50.78 A C ATOM 516 NH1 ARG A 69 27.614 30.221 26.045 1.00 50.71 A N ATOM 517 NH2 ARG A 69 29.225 28.744 26.717 1.00 52.55 A N ATOM 518 C ARG A 69 30.047 33.665 19.800 1.00 31.68 A C ATOM 519 O ARG A 69 30.369 34.829 20.101 1.00 31.59 A O ATOM 520 N ALA A 70 29.285 33.386 18.756 1.00 28.74 A N ATOM 521 C ALA A 70 28.724 34.423 17.974 1.00 27.59 A C ATOM 522 CB ALA A 70 27.785 33.868 16.899 1.00 26.50 A C ATOM 523 C ALA A 70 29.855 35.274 17.389 1.00 27.63 A C ATOM 524 O ALA A 70 29.716 36.512 17.323 1.00 28.16 A O ATOM 525 N ALA A 71 30.997 34.655 17.048 1.00 26.34 A N ATOM 526 CA ALA A 71 32.130 35.431 16.500 1.00 25.13 A C ATOM 527 CB ALA A 71 33.162 34.532 15.828 1.00 26.06 A C ATOM 528 C ALA A 71 32.807 36.303 17.538 1.00 24.79 A C ATOM 529 O ALA A 71 33.281 37.427 17.215 1.00 25.17 A O ATOM 530 N VAL A 72 32.869 35.818 18.771 1.00 23.47 A N ATOM 531 CA VAL A 72 33.480 36.593 19.829 1.00 24.72 A C ATOM 532 CB VAL A 72 33.511 35.776 21.148 1.00 26.15 A C ATOM 533 CG1 VAL A 72 34.001 36.649 22.334 1.00 25.93 A C ATOM 534 CG2 VAL A 72 34.336 34.478 20.993 1.00 24.20 A C ATOM 535 C VAL A 72 32.662 37.892 20.057 1.00 25.57 A C ATOM 536 O VAL A 72 33.232 38.995 20.138 1.00 25.05 A O ATOM 537 N ASP A 73 31.322 37.780 20.115 1.00 25.59 A N ATOM 538 CA ASP A 73 30.561 38.978 20.334 1.00 25.80 A C ATOM 539 CB ASP A 73 29.082 38.733 20.575 1.00 26.54 A C ATOM 540 CG ASP A 73 28.799 38.077 21.890 1.00 25.88 A C ATOM 541 OD1 ASP A 73 29.270 36.955 22.124 1.00 29.87 A O ATOM 542 OD2 ASP A 73 28.011 38.626 22.658 1.00 25.27 A O ATOM 543 C ASP A 73 30.811 39.944 19.153 1.00 25.39 A C ATOM 544 O ASP A 73 31.104 41.169 19.401 1.00 23.26 A O ATOM 545 N ALA A 74 30.776 39.386 17.923 1.00 24.46 A N ATOM 546 CA ALA A 74 30.919 40.211 16.666 1.00 24.88 A C ATOM 547 CB ALA A 74 30.708 39.411 15.371 1.00 23.92 A C ATOM 548 C ALA A 74 32.261 40.865 16.648 1.00 25.23 A C ATOM 549 O ALA A 74 32.355 42.051 16.430 1.00 24.99 A O ATOM 550 N HIS A 75 33.305 40.100 16.967 1.00 26.40 A N ATOM 551 CA HIS A 75 34.655 40.660 16.937 1.00 26.47 A C ATOM 552 CB HIS A 75 35.729 39.551 17.047 1.00 25.93 A C ATOM 553 CG HIS A 75 37.106 40.028 16.728 1.00 26.63 A C ATOM 554 ND1 HIS A 75 37.570 40.152 15.432 1.00 24.12 A N ATOM 555 CE1 HIS A 75 38.815 40.607 15.458 1.00 26.83 A C ATOM 556 NE2 HIS A 75 39.178 40.775 16.720 1.00 28.65 A N ATOM 557 CD2 HIS A 75 38.119 40.438 17.535 1.00 28.72 A C ATOM 558 C HIS A 75 34.817 41.735 18.031 1.00 26.15 A C ATOM 559 O HIS A 75 35.248 42.830 17.754 1.00 26.75 A O ATOM 560 N TYR A 76 34.435 41.418 19.262 1.00 25.17 A N ATOM 561 CA TYR A 76 34.447 42.382 20.355 1.00 24.49 A C ATOM 562 CA TYR A 76 34.010 41.649 21.618 1.00 25.96 A C ATOM 563 CB TYR A 76 34.184 42.446 22.878 1.00 28.99 A C ATOM 564 CD1 TYR A 76 35.399 42.486 23.521 1.00 30.72 A C ATOM 565 CE1 TYR A 76 35.575 43.211 24.728 1.00 32.22 A C ATOM 566 CZ TYR A 76 34.509 43.900 25.258 1.00 35.19 A C ATOM 567 OH TYR A 76 34.691 44.631 26.403 1.00 35.34 A O ATOM 568 CE2 TYR A 76 33.273 43.884 24.614 1.00 33.11 A C ATOM 569 CD2 TYR A 76 33.110 43.170 23.432 1.00 31.42 A C ATOM 570 C TYR A 76 33.562 43.611 20.148 1.00 24.10 A C ATOM 571 O TYR A 76 33.976 44.755 20.350 1.00 24.86 A O ATOM 572 N ASN A 77 32.325 43.420 19.724 1.00 23.91 A N ATOM 573 CA ASN A 77 31.508 44.603 19.541 1.00 22.42 A C ATOM 574 CB ASN A 77 3.023 44.258 19.441 1.00 22.43 A C ATOM 575 CG ASN A 77 29.463 43.749 20.739 1.00 17.76 A C ATOM 576 OD1 ASN A 77 29.953 44.040 21.828 1.00 22.44 A O ATOM 577 ND2 ASN A 77 28.526 42.890 20.620 1.00 11.56 A N ATOM 578 C ASN A 77 31.943 45.543 18.424 1.00 22.81 A C ATOM 579 O ASN A 77 31.979 46.757 18.642 1.00 22.77 A O ATOM 580 N LEU A 78 32.249 45.009 17.242 1.00 23.23 A N ATOM 581 CA LEU A 78 32.683 45.845 16.123 1.00 24.06 A C ATOM 582 CB LEU A 78 32.929 44.983 14.929 1.00 24.24 A C ATOM 583 CG LEU A 78 31.961 44.886 13.740 1.00 27.66 A C ATOM 584 CD1 LEU A 78 30.668 45.654 13.841 1.00 22.27 A C ATOM 585 CD2 LEU A 78 31.740 43.409 13.364 1.00 29.07 A C ATOM 586 C LEU A 78 33.950 46.645 16.492 1.00 24.84 A C ATOM 587 O LEU A 78 34.119 47.808 16.078 1.00 24.42 A O ATOM 588 N GLY A 79 34.816 46.050 17.321 1.00 25.35 A N ATOM 589 CA GLY A 79 35.968 46.791 17.824 1.00 25.79 A C ATOM 590 C GLY A 79 35.489 47.947 18.686 1.00 26.54 A C ATOM 591 O GLY A 79 36.045 49.046 18.604 1.00 26.41 A O ATOM 592 N LYS A 80 34.488 47.698 19.550 1.00 26.38 A N ATOM 593 CA LYS A 80 33.936 48.802 20.369 1.00 27.32 A C ATOM 594 CB LYS A 80 33.011 48.302 21.504 1.00 28.49 A C ATOM 595 CG LYS A 80 33.782 47.811 22.743 1.00 33.44 A C ATOM 596 CD LYS A 80 33.098 48.294 24.045 1.00 42.67 A C ATOM 597 CE LYS A 80 32.247 47.154 24.682 1.00 48.39 A C ATOM 598 NZ LYS A 80 32.366 47.039 26.217 1.00 49.07 A N ATOM 599 C LYS A 80 33.271 49.932 19.528 1.00 25.49 A C ATOM 600 O LYS A 80 33.395 51.132 19.879 1.00 25.22 A O ATOM 601 N VAL A 81 32.626 49.562 18.412 1.00 23.06 A N ATOM 602 CA VAL A 81 32.000 50.552 17.577 1.00 20.88 A C ATOM 603 CB VAL A 81 30.967 49.941 16.655 1.00 21.65 A C ATOM 604 CG1 VAL A 81 30.409 51.002 15.659 1.00 19.27 A C ATOM 605 CG2 VAL A 81 29.825 49.304 17.481 1.00 18.92 A C ATOM 606 C VAL A 81 33.028 51.393 16.828 1.00 21.39 A C ATOM 607 O VAL A 81 32.859 52.610 16.699 1.00 21.09 A O ATOM 608 N TYR A 82 34.113 50.760 16.375 1.00 21.90 A N ATOM 609 CA TYR A 82 35.236 51.463 15.786 1.00 21.33 A C ATOM 610 CB TYR A 82 36.373 50.475 15.331 1.00 22.04 A C ATOM 611 CG TYR A 82 37.629 51.250 14.970 1.00 18.84 A C ATOM 612 CD1 TYR A 82 38.503 51.665 15.990 1.00 19.21 A C ATOM 613 CE1 TYR A 82 39.585 52.444 15.776 1.00 18.52 A C ATOM 614 CZ TYR A 82 39.883 52.874 14.525 1.00 21.16 A C ATOM 615 OH TYR A 82 41.020 53.656 14.432 1.00 24.42 A 0 ATOM 616 CE2 TYR A 82 39.062 52.536 13.457 1.00 20.05 A O ATOM 617 CD2 TYR A 82 37.855 51.701 13.722 1.00 16.33 A C ATOM 618 C TYR A 82 35.781 52.476 16.808 1.00 22.26 A C ATOM 619 O TYR A 82 36.007 53.649 16.479 1.00 22.32 A O ATOM 620 N ASP A 83 36.041 52.029 18.030 1.00 22.20 A N ATOM 621 CA ASP A 83 36.498 52.971 19.075 1.00 23.53 A C ATOM 622 CB ASP A 83 36.745 52.268 20.416 1.00 23.02 A C ATOM 623 CG ASP A 83 37.831 51.196 20.317 1.00 25.23 A C ATOM 624 OD1 ASP A 83 38.713 51.279 19.401 1.00 24.63 A O ATOM 625 OD2 ASP A 83 37.799 50.280 21.163 1.00 28.39 A O ATOM 626 C ASP A 83 35.555 54.134 19.318 1.00 23.48 A C ATOM 627 O ASP A 83 35.971 55.249 19.589 1.00 23.92 A O ATOM 628 N TYR A 84 34.271 53.874 19.216 1.00 24.00 A N ATOM 629 CA TYR A 84 33.326 54.902 19.519 1.00 23.71 A C ATOM 630 CB TYR A 84 31.907 54.297 19.583 1.00 24.20 A C ATOM 631 CG TYR A 84 30.858 55.363 19.629 1.00 23.19 A C ATOM 632 CD1 TYR A 84 30.519 55.931 20.823 1.00 22.87 A C ATOM 633 CE1 TYR A 84 29.551 56.947 20.875 1.00 24.91 A C ATOM 634 CZ TYR A 84 28.992 57.421 19.717 1.00 20.31 A C ATOM 635 OH TYR A 84 28.075 58.443 19.820 1.00 22.01 A O ATOM 636 CE2 TYR A 84 29.342 56.869 18.521 1.00 19.40 A C ATOM 637 OD2 TYR A 84 30.252 55.840 18.465 1.00 18.29 A C ATOM 638 C TYR A 84 33.437 56.034 18.501 1.00 23.26 A C ATOM 639 O TYR A 84 33.541 57.178 18.881 1.00 24.20 A O ATOM 640 N PHE A 85 33.418 55.715 17.218 1.00 22.52 A C ATOM 641 CA PHE A 85 33.429 56.712 16.173 1.00 22.03 A C ATOM 642 CB PHE A 85 33.030 56.067 14.835 1.00 22.20 A C ATOM 643 CG PHE A 85 31.531 55.940 14.665 1.00 20.97 A C ATOM 644 CD1 PHE A 85 30.756 57.049 14.344 1.00 18.41 A C ATOM 645 CE1 PHE A 85 29.382 56.971 14.210 1.00 17.21 A C ATOM 646 CZ PHE A 85 28.735 55.766 14.418 1.00 20.03 A C ATOM 647 CE2 PHE A 85 29.477 54.653 14.776 1.00 21.83 A C ATOM 648 CD2 PHE A 85 30.892 54.745 14.895 1.00 23.45 A C ATOM 649 C PHE A 85 31.781 57.390 16.087 1.00 23.25 A C ATOM 650 O PHE A 85 34.867 58.629 15.837 1.00 21.25 A O ATOM 651 N TYR A 86 35.831 56.599 16.381 1.00 23.68 A N ATOM 652 CA TYR A 86 37.186 57.146 16.398 1.00 24.50 A C ATOM 653 CB TYR A 86 38.259 56.060 16.341 1.00 25.13 A C ATOM 654 CG TYR A 86 29.648 56.640 16.311 1.00 26.50 A C ATOM 655 CD1 TYR A 86 40.122 57.303 15.159 1.00 27.15 A C ATOM 656 CE1 TYR A 86 41.398 57.867 15.148 1.00 29.74 A C ATOM 657 CZ TYR A 86 42.220 57.763 16.274 1.00 30.75 A C ATOM 658 OH TYR A 86 43.463 58.290 16.229 1.00 33.52 A O ATOM 659 CE2 TYR A 86 41.800 57.146 17.414 1.00 29.62 A C ATOM 660 CD2 TYR A 86 40.477 56.574 17.429 1.00 29.65 A C ATOM 661 C TYR A 86 37.438 58.080 17.562 1.00 24.44 A C ATOM 662 O TYR A 86 37.906 59.199 17.381 1.00 25.04 A O ATOM 663 N GLN A 87 37.088 57.657 18.754 1.00 24.92 A N ATOM 664 CA GLN A 87 37.333 58.504 19.925 1.00 26.25 A C ATOM 665 CB GLN A 87 37.232 57.687 31.197 1.00 26.93 A C ATOM 666 CG GLN A 87 38.411 56.771 21.381 1.00 31.10 A C ATOM 667 CD GLN A 87 38.085 55.660 22.348 1.00 29.99 A C ATOM 668 OE1 GLN A 87 37.081 55.726 23.071 1.00 41.78 A O ATOM 669 NE2 GLN A 87 38.922 54.617 22.366 1.00 42.63 A N ATOM 670 C GLN A 87 36.420 59.706 20.067 1.00 26.15 A C ATOM 671 O GLN A 87 36.831 60.699 20.644 1.00 24.48 A O ATOM 672 N LYS A 88 35.153 59.593 19.620 1.00 25.63 A N ATOM 673 CA LYS A 88 34.252 60.725 19.772 1.00 24.20 A C ATOM 674 CB LYS A 88 32.770 60.326 19.777 1.00 24.42 A C ATOM 675 CG LYS A 88 32.352 59.286 20.748 1.00 24.40 A C ATOM 676 CD LYS A 88 32.523 59.738 22.116 1.00 26.90 A C ATOM 677 CE LYS A 88 32.183 58.598 23.050 1.00 27.59 A C ATOM 678 NZ LYS A 88 31.931 59.174 24.395 1.00 31.00 A N ATOM 679 C LYS A 88 34.457 61.711 18.670 1.00 23.70 A C ATOM 680 O LYS A 88 34.342 62.871 18.919 1.00 24.35 A O ATOM 681 N PHE A 89 34.692 61.267 17.440 1.00 23.60 A N ATOM 682 CA PHE A 89 34.576 62.182 16.311 1.00 23.45 A C ATOM 683 CB PHE A 89 33.397 61.806 15.422 1.00 22.33 A C ATOM 684 CG PHE A 89 32.147 61.509 16.191 1.00 23.28 A C ATOM 685 CD1 PHE A 89 31.498 62.518 16.917 1.00 19.53 A C ATOM 686 CE1 PHE A 89 30.332 62.222 17.674 1.00 21.34 A C ATOM 687 CZ PHE A 89 29.809 60.916 17.709 1.00 20.21 A C ATOM 688 CE2 PHE A 89 30.462 59.892 16.997 1.00 21.28 A C ATOM 689 CD2 PHE A 89 31.634 60.190 16.251 1.00 21.81 A C ATOM 690 C PHE A 89 35.845 62.205 15.497 1.00 24.67 A C ATOM 691 O PHE A 89 35.910 62.900 14.489 1.00 23.59 A O ATOM 692 N ASN A 90 36.848 61.422 15.927 1.00 25.75 A N ATOM 693 CA ASN A 90 38.049 61.227 15.121 1.00 26.46 A C ATOM 694 CB ASN A 90 38.887 62.559 15.076 1.00 27.00 A C ATOM 695 CG ASN A 90 40.308 62.371 14.453 1.00 30.20 A C ATOM 696 OD1 ASN A 90 41.067 61.430 14.783 1.00 32.17 A O ATOM 697 ND2 ASN A 90 40.664 63.284 13.556 1.00 29.30 A N ATOM 698 C ASN A 90 37.691 60.676 13.725 1.00 25.55 A C ATOM 699 O ASN A 90 38.285 61.086 12.707 1.00 27.83 A O ATOM 700 N ARG A 91 36.740 59.751 13.662 1.00 24.18 A N ATOM 701 CA ARG A 91 36.398 59.079 12.383 1.00 24.35 A C ATOM 702 CB ARG A 91 34.894 58.713 12.244 1.00 24.28 A C ATOM 703 CG ARG A 91 34.459 58.341 10.821 1.00 20.60 A C ATOM 704 CD ARG A 91 32.985 58.061 10.691 1.00 19.78 A C ATOM 705 NE ARG A 91 32.656 57.679 9.324 1.00 16.07 A N ATOM 706 CZ ARG A 91 32.448 58.597 8.355 1.00 20.75 A C ATOM 707 NH1 ARG A 91 32.544 59.918 8.634 1.00 14.39 A N ATOM 708 NH2 ARG A 91 32.194 58.219 7.091 1.00 16.44 A N ATOM 709 C ARG A 91 37.210 57.826 12.208 1.00 24.66 A C ATOM 710 O ARG A 91 37.210 56.943 13.073 1.00 26.57 A O ATOM 711 N ASN A 92 37.924 57.722 11.102 1.00 24.72 A N ATOM 712 CA ASN A 92 38.747 56.532 10.900 1.00 24.42 A C ATOM 713 CB ASN A 92 39.951 56.942 10.084 1.00 24.43 A C ATOM 714 CG ASN A 92 40.921 55.822 9.831 1.00 27.29 A C ATOM 715 OD1 ASN A 92 40.874 54.757 10.450 1.00 30.10 A O ATOM 716 ND2 ASN A 92 41.866 56.084 8.913 1.00 29.96 A N ATOM 717 C ASN A 92 37.915 55.455 10.201 1.00 24.37 A C ATOM 718 O ASN A 92 37.937 55.333 8.965 1.00 25.59 A O ATOM 719 N SER A 93 37.175 54.673 10.970 1.00 22.83 A N ATOM 720 CA SER A 93 36.336 53.650 10.387 1.00 22.27 A C ATOM 721 CB SER A 93 37.090 52.772 9.384 1.00 21.81 A C ATOM 722 OG SER A 93 36.335 51.571 9.193 1.00 20.51 A O ATOM 723 C SER A 93 35.081 54.191 9.730 1.00 22.08 A C ATOM 724 O SER A 93 34.886 55.378 9.638 1.00 23.02 A O ATOM 725 N TYR A 94 34.213 53.303 9.254 1.00 23.13 A N ATOM 726 CA TYR A 94 32.915 53.741 8.709 1.00 22.74 A C ATOM 727 CB TYR A 94 32.040 52.547 8.387 1.00 21.69 A C ATOM 728 CG TYR A 94 32.522 51.788 7.184 1.00 21.77 A C ATOM 729 CD1 TYR A 94 31.986 52.046 5.904 1.00 25.43 A C ATOM 730 CE1 TYR A 94 32.444 51.362 4.749 1.00 21.99 A C ATOM 731 CZ TYR A 94 33.460 50.434 4.881 1.00 24.51 A C ATOM 732 OH TYR A 94 33.935 49.748 3.758 1.00 24.58 A O ATOM 733 CE2 TYR A 94 34.028 50.186 6.162 1.00 23.54 A C ATOM 734 CD2 TYR A 94 33.558 50.857 7.288 1.00 18.74 A C ATOM 735 C TYR A 94 33.034 54.650 7.501 1.00 23.34 A C ATOM 736 O TYR A 94 32.184 55.516 7.295 1.00 25.03 A O ATOM 737 N ASP A 95 34.077 54.502 6.699 1.00 24.79 A N ATOM 738 CA ASP A 95 34.229 55.405 5.504 1.00 25.96 A C ATOM 739 CB ASP A 95 34.718 54.618 4.299 1.00 25.17 A C ATOM 740 CG ASP A 95 36.080 53.926 4.563 1.00 26.88 A C ATOM 741 OD1 ASP A 95 26.708 54.173 5.621 1.00 23.59 A O ATOM 742 OD2 ASP A 95 36.526 53.122 3.710 1.00 30.47 A O ATOM 743 C ASP A 95 35.186 56.550 5.756 1.00 26.31 A C ATOM 744 O ASP A 95 35.570 57.253 4.830 1.00 28.26 A O ATOM 745 N ASN A 96 35.622 56.705 6.996 1.00 26.19 A N ATOM 746 CA ASN A 96 36.600 57.726 7.345 1.00 27.04 A C ATOM 747 CB ASN A 96 35.994 59.141 7.290 1.00 25.92 A C ATOM 748 CG ASN A 96 36.783 60.126 8.133 1.00 27.06 A C ATOM 749 OD1 ASN A 96 37.509 59.722 9.059 1.00 28.41 A O ATOM 750 ND2 ASN A 96 36.649 61.414 7.833 1.00 23.23 A N ATOM 751 C ASN A 96 37.868 27.680 6.491 1.00 27.67 A C ATOM 752 O ASN A 96 38.536 58.706 6.354 1.00 27.62 A O ATOM 753 N LYS A 97 38.169 26.506 5.911 1.00 28.43 A N ATOM 754 CA LYS A 97 39.373 56.260 5.095 1.00 27.97 A C ATOM 755 CB LYS A 97 39.009 56.065 3.606 1.00 28.01 A C ATOM 756 CG LYS A 97 38.492 57.348 2.937 1.00 29.56 A C ATOM 757 CD LYS A 97 38.148 57.180 1.435 1.00 31.10 A C ATOM 758 CE LYS A 97 36.711 56.724 1.178 1.00 32.30 A C ATOM 759 NZ LYS A 97 36.314 56.990 0.232 1.00 35.76 A N ATOM 760 C LYS A 97 40.134 55.048 5.613 1.00 28.14 A C ATOM 761 O LYS A 97 41.135 54.648 5.017 1.00 28.53 A O ATOM 762 N GLY A 98 39.669 54.447 6.711 1.00 27.15 A N ATOM 763 CA GLY A 98 40.370 53.299 7.301 1.00 24.49 A C ATOM 764 C GLY A 98 39.850 51.961 6.793 1.00 23.46 A C ATOM 765 O GLY A 98 40.445 50.935 7.082 1.00 24.40 A O ATOM 766 N GLY A 99 38.776 51.947 6.013 1.00 21.47 A N ATOM 767 CA GLY A 99 38.290 50.710 5.411 1.00 20.97 A C ATOM 768 C GLY A 99 38.114 49.600 6.437 1.00 23.26 A C ATOM 769 O GLY A 99 37.507 49.813 7.495 1.00 22.85 A O ATOM 770 N LYS A 100 38.678 48.408 6.186 1.00 24.99 A N ATOM 771 CA LYS A 100 38.545 47.281 7.141 1.00 25.11 A C ATOM 772 CB LYS A 100 39.214 46.034 6.577 1.00 25.69 A C ATOM 773 CG LYS A 100 38.639 45.629 5.203 1.00 30.14 A C ATOM 774 CD LYS A 100 39.052 44.248 4.642 1.00 32.29 A C ATOM 775 CE LYS A 100 38.162 43.991 3.336 1.00 38.39 A C ATOM 776 NZ LYS A 100 38.707 42.859 2.443 1.00 42.60 A N ATOM 777 C LYS A 100 37.036 47.043 7.447 1.00 25.30 A C ATOM 778 O LYS A 100 36.150 47.345 6.610 1.00 24.91 A O ATOM 779 N ILE A 101 36.761 46.564 8.663 1.00 24.85 A N ATOM 780 CA ILE A 101 35.414 46.283 9.161 1.00 23.22 A C ATOM 781 CB ILE A 101 35.255 46.923 10.522 1.00 23.11 A C ATOM 782 CG1 ILE A 101 35.219 48.449 10.364 1.00 20.36 A C ATOM 783 CD1 ILE A 101 35.453 49.172 11.638 1.00 21.07 A C ATOM 784 CG2 ILE A 101 33.999 46.362 11.287 1.00 23.99 A C ATOM 785 C ILE A 101 35.288 44.776 9.290 1.00 24.21 A C ATOM 786 O ILE A 101 35.944 44.171 10.146 1.00 26.06 A O ATOM 787 N VAL A 102 34.503 44.153 8.421 1.00 23.16 A N ATOM 788 CA VAL A 102 34.478 42.727 8.287 1.00 22.20 A C ATOM 789 CB VAL A 102 34.761 42.340 6.807 1.00 23.44 A C ATOM 790 CG1 VAL A 102 34.424 40.850 6.483 1.00 19.05 A C ATOM 791 CG2 VAL A 102 36.180 42.671 6.460 1.00 21.14 A C ATOM 792 C VAL A 102 33.084 42.267 8.677 1.00 23.93 A C ATOM 793 O VAL A 102 32.091 42.941 8.325 1.00 22.72 A O ATOM 794 N SER A 103 32.994 41.148 9.421 1.00 24.36 A N ATOM 795 CA SER A 103 31.708 40.568 9.703 1.00 25.59 A C ATOM 796 CB SER A 103 31.317 40.856 11.124 1.00 25.68 A C ATOM 797 OG SER A 103 31.926 39.882 11.946 1.00 28.96 A O ATOM 798 C SER A 103 31.654 39.047 9.411 1.00 26.51 A C ATOM 799 O SER A 103 32.695 38.350 9.383 1.00 26.56 A O ATOM 800 N SER A 104 30.442 38.556 9.140 1.00 26.44 A N ATOM 801 CA SER A 104 30.225 37.140 8.958 1.00 26.76 A C ATOM 802 CB SER A 104 29.852 36.784 7.518 1.00 27.23 A C ATOM 803 OG SER A 104 30.856 37.188 6.574 1.00 26.06 A O ATOM 804 C SER A 104 29.123 36.728 9.918 1.00 27.68 A C ATOM 805 O SER A 104 27.979 37.206 9.868 1.00 27.25 A O ATOM 806 N VAL A 105 29.495 35.861 10.841 1.00 28.11 A N ATOM 807 CA VAL A 105 28.530 35.248 11.711 1.00 28.88 A C ATOM 808 CB VAL A 105 29.152 35.040 13.083 1.00 29.18 A C ATOM 809 CG1 VAL A 105 29.569 36.358 13.662 1.00 27.85 A C ATOM 810 CG2 VAL A 105 30.338 34.066 12.990 1.00 28.33 A C ATOM 811 C VAL A 105 28.034 33.904 11.141 1.00 29.60 A C ATOM 812 O VAL A 105 28.611 33.353 10.151 1.00 29.63 A O ATOM 813 N HIS A 106 27.005 33.356 11.782 1.00 29.73 A N ATOM 814 CA HIS A 106 26.377 32.102 11.318 1.00 30.74 A C ATOM 815 CB HIS A 106 27.287 30.869 11.536 1.00 30.34 A C ATOM 816 CG HIS A 106 27.705 30.693 12.961 1.00 27.61 A C ATOM 817 ND1 HIS A 106 26.794 30.645 13.990 1.00 25.34 A N ATOM 818 CE1 HIS A 106 27.437 30.525 15.140 1.00 28.07 A C ATOM 819 NE2 HIS A 106 28.732 30.482 14.893 1.00 28.43 A N ATOM 820 CD2 HIS A 106 28.922 30.593 13.532 1.00 28.46 A C ATOM 821 C HIS A 106 25.971 32.252 9.860 1.00 32.36 A C ATOM 822 O HIS A 106 26.131 31.330 9.040 1.00 32.69 A O ATOM 823 N TYR A 107 25.461 33.433 9.528 1.00 33.47 A N ATOM 824 CA TYR A 107 24.924 33.638 8.211 1.00 35.05 A C ATOM 825 CB TYR A 107 24.727 35.116 7.926 1.00 34.59 A C ATOM 826 CG TYR A 107 24.107 35.405 6.575 1.00 35.69 A C ATOM 827 CD1 TYR A 107 24.910 35.735 5.483 1.00 35.84 A C ATOM 828 CE1 TYR A 107 24.339 36.017 4.221 1.00 36.98 A C ATOM 829 CZ TYR A 107 22.964 35.989 4.073 1.00 37.15 A C ATOM 830 OH TYR A 107 22.457 36.265 2.851 1.00 37.25 A O ATOM 831 CE2 TYR A 107 22.126 35.689 5.149 1.00 36.54 A C ATOM 832 CD2 TYR A 107 22.701 35.393 6.393 1.00 35.92 A C ATOM 833 C TYR A 107 23.598 32.924 8.176 1.00 36.00 A C ATOM 834 O TYR A 107 22.712 33.209 9.022 1.00 35.53 A O ATOM 835 N GLY A 108 23.467 32.001 7.210 1.00 37.18 A N ATOM 836 CA GLY A 108 22.178 31.379 6.893 1.00 38.18 A C ATOM 837 C GLY A 108 21.753 30.343 7.914 1.00 40.33 A C ATOM 838 O GLY A 108 22.577 29.768 8.643 1.00 40.64 A O ATOM 839 N SER A 109 20.457 30.086 7.969 1.00 42.15 A N ATOM 840 CA SER A 109 19.971 29.038 8.853 1.00 44.71 A C ATOM 841 CB SER A 109 19.611 27.751 8.074 1.00 45.07 A C ATOM 842 OG SER A 109 19.609 26.644 8.968 1.00 45.28 A O ATOM 843 C SER A 109 18.768 29.559 9.638 1.00 45.55 A C ATOM 844 O SER A 109 17.772 30.016 9.026 1.00 45.22 A O ATOM 845 N ARG A 110 18.890 29.541 10.977 1.00 45.44 A N ATOM 846 CA ARG A 110 17.854 30.119 11.821 1.00 46.27 A C ATOM 847 CB ARG A 110 16.732 29.064 11.996 1.00 47.09 A C ATOM 848 CG ARG A 110 17.316 27.667 12.469 1.00 53.17 A C ATOM 849 CD ARG A 110 16.356 26.720 13.257 1.00 61.65 A C ATOM 850 NE ARG A 110 14.954 26.807 12.807 1.00 67.59 A N ATOM 851 CZ ARG A 110 13.906 27.184 13.564 1.00 70.42 A C ATOM 852 NH1 ARG A 110 14.028 27.510 14.865 1.00 69.00 A N ATOM 853 NH2 ARG A 110 12.704 27.241 13.006 1.00 71.16 A N ATOM 854 C ARG A 110 17.354 31.497 11.255 1.00 44.76 A C ATOM 855 O ARG A 110 16.167 31.772 11.201 1.00 44.86 A O ATOM 856 N TYR A 111 18.284 32.349 10.816 1.00 43.15 A N ATOM 857 CA TYR A 111 17.967 33.613 10.113 1.00 41.46 A C ATOM 858 O3 TYR A 111 19.129 33.916 9.167 1.00 41.36 A C ATOM 859 CG TYR A 111 19.025 35.147 8.321 1.00 43.63 A C ATOM 860 CD1 TYR A 111 17.981 35.319 7.403 1.00 46.38 A C ATOM 861 CE1 TYR A 111 17.907 36.482 6.593 1.00 48.54 A C ATOM 862 CZ TYR A 111 18.895 37.465 6.693 1.00 49.57 A C ATOM 863 OH TYR A 111 18.842 38.598 5.909 1.00 50.97 A O ATOM 864 CE2 TYR A 111 19.946 37.312 7.594 1.00 48.80 A C ATOM 865 CD2 TYR A 111 20.004 36.152 8.405 1.00 47.79 A C ATOM 866 C TYR A 111 17.735 34.788 11.088 1.00 40.02 A C ATOM 867 O TYR A 111 18.580 35.098 11.906 1.00 38.85 A O ATOM 868 N ASN A 112 16.571 35.429 11.013 1.00 39.72 A N ATOM 869 CA ASN A 112 16.211 36.473 11.996 1.00 38.39 A C ATOM 870 CB ASN A 112 14.688 36.460 12.320 1.00 38.11 A C ATOM 871 CG ASN A 112 14.266 35.305 13.262 1.00 37.98 A C ATOM 872 OD1 ASN A 112 14.999 34.901 14.170 1.00 38.90 A O ATOM 873 ND2 ASN A 112 13.071 34.782 13.039 1.00 37.99 A N ATOM 874 C ASN A 112 16.660 37.890 11.576 1.00 37.82 A C ATOM 875 O ASN A 112 15.835 38.808 11.493 1.00 36.91 A O ATOM 876 N ASN A 113 17.957 38.074 11.336 1.00 37.02 A N ATOM 877 CA ASN A 113 18.427 39.382 10.923 1.00 37.51 A C ATOM 878 CB ASN A 113 17.979 39.699 9.489 1.00 38.57 A C ATOM 879 CG ASN A 113 17.709 41.176 9.295 1.00 43.30 A C ATOM 880 OD1 ASN A 113 16.666 41.694 9.683 1.00 44.68 A O ATOM 881 ND2 ASN A 113 18.682 41.875 8.730 1.00 50.44 A N ATOM 882 C ASN A 113 19.941 39.639 11.059 1.00 36.09 A C ATOM 883 O ASN A 113 20.717 38.706 11.308 1.00 35.79 A O ATOM 884 N ALA A 114 20.316 40.921 10.939 1.00 33.16 A N ATOM 885 CA ALA A 114 21.697 41.374 10.936 1.00 31.35 A C ATOM 886 CB ALA A 114 22.132 41.859 12.322 1.00 30.10 A C ATOM 887 C ALA A 114 21.681 42.536 9.981 1.00 30.28 A C ATOM 888 O ALA A 114 20.761 43.341 9.971 1.00 29.89 A O ATOM 889 N ALA A 115 22.685 42.665 9.152 1.00 28.73 A N ATOM 890 CA ALA A 115 22.587 43.775 8.219 1.00 27.85 A C ATOM 891 CB ALA A 115 21.783 43.333 6.923 1.00 26.42 A C ATOM 892 C ALA A 115 23.951 44.285 7.871 1.00 27.17 A C ATOM 893 O ALA A 115 24.932 43.551 7.903 1.00 26.95 A O ATOM 894 N TRP A 116 24.017 45.562 7.536 1.00 27.57 A N ATOM 895 CA TRP A 116 25.151 46.046 6.778 1.00 26.56 A C ATOM 896 CB TRP A 116 25.358 47.483 7.083 1.00 25.55 A C ATOM 897 CG TRP A 116 26.399 48.130 6.276 1.00 25.34 A C ATOM 898 CD1 TRP A 116 26.198 48.955 5.212 1.00 22.58 A C ATOM 899 NE1 TRP A 116 27.417 49.374 4.711 1.00 22.11 A N ATOM 900 CE2 TRP A 116 28.430 48.793 5.429 1.00 20.63 A C ATOM 901 CD2 TRP A 116 27.836 47.012 6.434 1.00 22.71 A C ATOM 902 CE3 TRP A 116 28.674 47.274 7.297 1.00 25.00 A C ATOM 903 CZ3 TRP A 116 30.096 47.399 7.160 1.00 20.26 A C ATOM 904 CH2 TRP A 116 30.633 48.228 6.183 1.00 20.58 A C ATOM 905 CZ2 TRP A 116 29.823 48.914 5.293 1.00 20.87 A C ATOM 906 C TRP A 116 24.826 45.858 5.300 1.00 28.31 A C ATOM 907 O TRP A 116 23.804 46.297 4.806 1.00 25.54 A O ATOM 908 N ILE A 117 25.719 45.166 4.600 1.00 31.41 A N ATOM 909 CA ILE A 117 25.501 44.758 3.224 1.00 33.35 A C ATOM 910 CB ILE A 117 25.708 43.237 3.204 1.00 34.35 A C ATOM 911 CG1 ILE A 117 24.445 42.583 2.753 1.00 35.74 A C ATOM 912 CD1 ILE A 117 23.596 42.437 3.940 1.00 36.48 A C ATOM 913 CG2 ILE A 117 27.052 42.729 2.567 1.00 32.98 A C ATOM 914 C ILE A 117 26.427 45.554 2.264 1.00 34.89 A C ATOM 915 O ILE A 117 26.928 45.013 1.236 1.00 36.20 A O ATOM 916 N GLY A 118 26.682 46.830 2.606 1.00 34.05 A N ATOM 917 CA GLY A 118 27.447 47.736 1.741 1.00 32.89 A C ATOM 918 C GLY A 118 28.958 47.716 2.031 1.00 33.33 A C ATOM 919 O GLY A 118 29.641 48.800 2.057 1.00 33.11 A O ATOM 920 N ASP A 119 29.494 46.514 2.243 1.00 30.79 A N ATOM 921 CA ASP A 119 30.881 46.411 2.581 1.00 31.30 A C ATOM 922 CB ASP A 119 31.688 45.834 1.399 1.00 33.35 A C ATOM 923 CG ASP A 119 31.091 44.540 0.838 1.00 37.71 A C ATOM 924 OD1 ASP A 119 31.838 43.790 0.087 1.00 41.58 A O ATOM 925 OD2 ASP A 119 29.858 44.313 1.105 1.00 38.82 A O ATOM 926 C ASP A 119 31.132 45.557 3.801 1.00 29.73 A C ATOM 927 O ASP A 119 32.270 45.400 4.168 1.00 29.65 A O ATOM 928 N GLN A 120 30.107 44.968 4.414 1.00 28.27 A N ATOM 929 CA GLN A 120 30.358 44.121 5.565 1.00 27.33 A C ATOM 930 CB GLN A 120 30.989 42.784 5.177 1.00 26.60 A C ATOM 931 CG GLN A 120 30.031 41.829 4.485 1.00 25.55 A C ATOM 932 CD GLN A 120 30.609 40.414 4.466 1.00 27.50 A C ATOM 933 OE1 GLN A 120 31.328 39.981 3.512 1.00 26.21 A O ATOM 934 NE2 GLN A 120 30.340 39.689 5.532 1.00 23.92 A N ATOM 935 C GLN A 120 29.117 43.901 6.390 1.00 28.01 A C ATOM 936 O GLN A 120 28.015 44.342 6.021 1.00 29.44 A O ATOM 937 N MET A 121 29.299 43.213 7.521 1.00 27.81 A N ATOM 938 CA MET A 121 28.212 42.851 8.400 1.00 26.90 A C ATOM 939 CB MET A 121 28.639 43.033 9.836 1.00 26.74 A C ATOM 940 CG MET A 121 28.830 44.451 10.264 1.00 28.73 A C ATOM 941 SD MET A 121 27.203 45.210 10.223 1.00 33.79 A S ATOM 942 CE MET A 121 26.289 44.011 11.268 1.00 35.84 A C ATOM 943 C MET A 121 27.925 41.400 8.183 1.00 26.76 A C ATOM 944 O MET A 121 28.878 40.606 8.009 1.00 27.02 A O ATOM 945 N ILE A 122 26.640 41.050 8.198 1.00 25.38 A N ATOM 946 CA ILE A 122 26.227 39.676 8.347 1.00 25.64 A C ATOM 947 CB ILE A 122 25.493 39.112 7.107 1.00 25.89 A C ATOM 948 CG1 ILE A 122 24.153 39.859 6.849 1.00 26.78 A C ATOM 949 CD1 ILE A 122 23.210 39.229 5.778 1.00 28.66 A C ATOM 950 CG2 ILE A 122 26.401 39.291 5.890 1.00 25.18 A C ATOM 951 C ILE A 122 25.352 39.591 9.585 1.00 25.99 A C ATOM 952 O ILE A 122 24.582 40.512 9.892 1.00 24.65 A O ATOM 953 N TYR A 123 25.477 38.468 10.292 1.00 26.83 A N ATOM 954 CA TYR A 123 24.684 38.214 11.479 1.00 27.50 A C ATOM 955 CB TYR A 123 25.620 38.158 12.642 1.00 26.01 A C ATOM 956 CG TYR A 123 26.202 39.467 12.987 1.00 28.56 A C ATOM 957 CD1 TYR A 123 25.458 40.424 13.696 1.00 26.12 A C ATOM 958 CE1 TYR A 123 26.016 41.621 14.047 1.00 27.49 A C ATOM 959 CZ TYR A 123 27.340 41.890 13.696 1.00 29.40 A C ATOM 960 OH TYR A 123 27.940 43.075 14.048 1.00 29.36 A O ATOM 961 CE2 TYR A 123 28.089 40.965 12.974 1.00 29.36 A C ATOM 962 CD2 TYR A 123 27.525 39.761 12.637 1.00 28.86 A C ATOM 963 C TYR A 123 24.00 36.866 11.410 1.00 27.64 A C ATOM 964 O TYR A 123 24.682 35.864 11.416 1.00 27.65 A O ATOM 965 N GLY A 124 22.675 36.814 11.397 1.00 28.67 A N ATOM 966 CA GLY A 124 21.985 35.522 11.636 1.00 29.95 A C ATOM 967 C GLY A 124 22.156 34.939 13.056 1.00 32.16 A C ATOM 968 O GLY A 124 22.633 35.631 14.029 1.00 31.54 A O ATOM 969 N ASP A 125 21.774 33.667 13.197 1.00 32.99 A N ATOM 970 CA ASP A 125 21.679 33.034 14.514 1.00 34.33 A C ATOM 971 CB ASP A 125 21.971 31.562 14.386 1.00 34.40 A C ATOM 972 CG ASP A 125 23.380 31.287 13.965 1.00 37.99 A C ATOM 973 OD1 ASP A 125 24.336 31.852 14.549 1.00 38.07 A O ATOM 974 OD2 ASP A 125 23.520 30.455 13.045 1.00 44.23 A O ATOM 975 C ASP A 125 20.288 33.194 15.165 1.00 34.98 A C ATOM 976 O ASP A 125 20.102 32.863 16.340 1.00 34.73 A O ATOM 977 N GLY A 126 19.312 33.685 14.397 1.00 35.47 A N ATOM 978 CA GLY A 126 17.931 33.785 14.893 1.00 36.66 A C ATOM 979 C GLY A 126 17.350 32.381 15.012 1.00 37.88 A C ATOM 980 O GLY A 126 18.083 31.394 14.794 1.00 38.63 A O ATOM 981 N ASP A 127 16.060 32.284 15.376 1.00 37.62 A N ATOM 982 CA ASP A 127 15.330 31.004 15.363 1.00 37.72 A C ATOM 983 CB ASP A 127 13.996 31.138 14.637 1.00 37.18 A C ATOM 984 CG ASP A 127 13.106 32.173 15.272 1.00 37.42 A C ATOM 985 OD1 ASP A 127 13.431 32.597 16.405 1.00 36.84 A O ATOM 986 OD2 ASP A 127 12.107 32.578 14.631 1.00 35.38 A O ATOM 987 C ASP A 127 15.057 30.433 16.756 1.00 37.76 A C ATOM 988 O ASP A 127 14.229 29.510 16.877 1.00 37.23 A O ATOM 989 N GLY A 128 15.750 30.980 17.767 1.00 37.19 A N ATOM 990 CA GLY A 128 15.485 30.716 19.179 1.00 37.16 A C ATOM 991 C GLY A 128 14.082 31.007 19.715 1.00 38.07 A C ATOM 992 O GLY A 128 13.859 30.746 20.890 1.00 39.17 A O ATOM 993 N ILE A 129 13.139 31.495 18.880 1.00 37.52 A N ATOM 994 CA ILE A 129 11.811 31.964 19.309 1.00 36.84 A C ATOM 995 CB ILE A 129 10.651 31.606 18.310 1.00 37.50 A C ATOM 996 CG1 ILE A 129 10.767 30.184 17.642 1.00 38.34 A C ATOM 997 CD1 ILE A 129 10.877 28.983 18.606 1.00 42.13 A C ATOM 998 CG2 ILE A 129 9.254 31.938 18.942 1.00 33.49 A C ATOM 999 C ILE A 129 11.819 33.512 19.349 1.00 37.57 A C ATOM 1000 O ILE A 129 11.514 34.142 20.378 1.00 38.01 A O ATOM 1001 N LEU A 130 12.150 34.132 18.216 1.00 36.97 A N ATOM 1002 CA LEU A 130 12.229 35.595 18.099 1.00 36.57 A C ATOM 1003 CB LEU A 130 11.936 35.959 16.669 1.00 37.18 A C ATOM 1004 CG LEU A 130 10.659 36.632 16.212 1.00 43.85 A C ATOM 1005 CD1 LEU A 130 10.785 38.205 16.580 1.00 46.49 A C ATOM 1006 CD2 LEU A 130 9.269 35.957 16.695 1.00 47.25 A C ATOM 1007 C LEU A 130 13.599 36.199 18.584 1.00 35.25 A C ATOM 1008 O LEU A 130 13.644 37.081 19.447 1.00 33.76 A O ATOM 1009 N PHE A 131 14.713 35.687 18.074 1.00 34.61 A N ATOM 1010 CA PHE A 131 16.039 36.253 18.388 1.00 34.15 A C ATOM 1011 CB PHE A 131 16.657 36.934 17.161 1.00 34.95 A C ATOM 1012 CG PHE A 131 15.891 38.104 16.672 1.00 38.14 A C ATOM 1013 CD1 PHE A 131 15.883 39.308 17.404 1.00 41.58 A C ATOM 1014 CE1 PHE A 131 15.151 40.406 16.966 1.00 44.73 A C ATOM 1015 CZ PHE A 131 14.387 40.309 15.767 1.00 48.86 A C ATOM 1016 CE2 PHE A 131 14.398 39.106 15.023 1.00 47.18 A C ATOM 1017 CD2 PHE A 131 15.162 38.011 15.501 1.00 41.75 A C ATOM 1018 C PHE A 131 17.011 35.199 18.809 1.00 32.89 A C ATOM 1019 O PHE A 131 16.964 34.096 18.280 1.00 33.01 A O ATOM 1020 N SER A 132 17.907 35.526 19.737 1.00 30.84 A N ATOM 1021 CA SER A 132 19.070 34.702 19.916 1.00 29.80 A C ATOM 1022 CB SER A 132 19.624 34.804 21.323 1.00 29.21 A C ATOM 1023 OG SER A 132 19.674 36.134 21.697 1.00 30.42 A O ATOM 1024 C SER A 132 20.048 35.190 18.859 1.00 29.53 A C ATOM 1025 O SER A 132 19.685 36.006 18.036 1.00 30.08 A O ATOM 1026 N PRO A 133 21.272 34.647 18.817 1.00 29.36 A N ATOM 1027 CA PRO A 133 22.190 35.114 17.725 1.00 27.74 A C ATOM 1028 CB PRO A 133 23.429 34.274 17.954 1.00 27.87 A C ATOM 1029 CG PRO A 133 22.824 32.907 18.594 1.00 28.87 A C ATOM 1030 CD PRO A 133 21.681 33.354 19.443 1.00 28.76 A C ATOM 1031 C PRO A 133 22.473 36.640 17.708 1.00 27.79 A C ATOM 1032 O PRO A 133 22.816 37.261 18.724 1.00 28.94 A O ATOM 1033 N LEU A 134 22.333 37.266 16.551 1.00 27.55 A N ATOM 1034 CA LEU A 134 22.239 38.723 16.535 1.00 26.30 A C ATOM 1035 CB LEU A 134 21.559 39.226 15.287 1.00 26.50 A C ATOM 1036 CG LEU A 134 20.106 38.765 15.416 1.00 26.04 A C ATOM 1037 CD1 LEU A 134 19.838 37.590 14.496 1.00 24.48 A C ATOM 1038 CD2 LEU A 134 19.191 39.925 15.156 1.00 25.59 A C ATOM 1039 C LEU A 134 23.503 39.514 16.841 1.00 26.32 A C ATOM 1040 O LEU A 134 23.407 40.717 17.164 1.00 26.47 A O ATOM 1041 N SER A 135 24.671 38.862 16.804 1.00 24.53 A N ATOM 1042 CA SER A 135 25.889 39.545 17.217 1.00 23.28 A C ATOM 1043 CB SER A 135 27.116 38.743 16.855 1.00 23.25 A C ATOM 1044 OG SER A 135 26.917 37.361 17.117 1.00 25.21 A O ATOM 1045 C SER A 135 25.899 39.891 18.701 1.00 22.93 A C ATOM 1046 O SER A 135 26.695 40.741 19.145 1.00 21.32 A O ATOM 1047 N GLY A 136 24.986 39.472 19.467 1.00 23.76 A N ATOM 1048 CA GLY A 136 25.006 39.438 20.917 1.00 24.14 A C ATOM 1049 C GLY A 136 24.621 40.823 21.457 1.00 24.78 A C ATOM 1050 O GLY A 136 24.722 41.048 22.656 1.00 26.30 A O ATOM 1051 N SER A 136 24.240 41.758 20.584 1.00 24.70 A N ATOM 1052 CA SER A 137 23.777 43.079 20.985 1.00 24.83 A C ATOM 1053 CB SER A 137 22.367 43.311 20.477 1.00 24.69 A C ATOM 1054 OG SER A 137 22.103 44.685 20.366 1.00 25.08 A O ATOM 1055 C SER A 137 24.685 44.169 20.437 1.00 25.13 A C ATOM 1056 O SER A 137 24.759 44.368 19.222 1.00 24.93 A O ATOM 1057 N LEU A 138 25.412 44.849 21.328 1.00 24.00 A N ATOM 1058 CA LEU A 138 26.252 48.962 20.897 1.00 22.97 A C ATOM 1059 CB LEU A 138 27.032 46.501 22.064 1.00 21.65 A C ATOM 1060 CG LEU A 138 27.858 47.765 21.927 1.00 22.78 A C ATOM 1061 CD1 LEU A 138 28.727 47.666 20.674 1.00 21.27 A C ATOM 1062 CD2 LEU A 138 28.726 47.916 23.246 1.00 18.55 A C ATOM 1063 C LEU A 138 25.439 47.092 20.237 1.00 22.85 A C ATOM 1064 O LEU A 138 25.874 47.701 19.354 1.00 23.50 A O ATOM 1065 N ASP A 139 24.260 47.382 20.755 1.00 22.10 A N ATOM 1066 CA ASP A 139 23.512 48.490 20.171 1.00 21.45 A C ATOM 1067 CB ASP A 139 22.459 49.121 21.135 1.00 21.46 A C ATOM 1068 CG ASP A 139 21.378 48.184 21.548 1.00 20.87 A C ATOM 1069 OD1 ASP A 139 20.693 47.613 20.695 1.00 19.56 A O ATOM 1070 OD2 ASP A 139 21.230 48.006 22.768 1.00 26.03 A O ATOM 1071 C ASP A 139 22.996 48.153 18.787 1.00 20.85 A C ATOM 1072 O ASP A 139 22.941 49.032 17.951 1.00 20.86 A O ATOM 1073 N VAL A 140 22.708 46.881 18.518 1.00 20.51 A N ATOM 1074 CA VAL A 140 22.297 46.459 17.184 1.00 20.92 A C ATOM 1075 CB VAL A 140 21.593 45.074 17.222 1.00 21.74 A C ATOM 1076 CG1 VAL A 140 21.631 44.384 15.832 1.00 21.41 A C ATOM 1077 CG2 VAL A 140 20.164 45.249 17.728 1.00 21.41 A C ATOM 1078 C VAL A 140 23.476 46.498 16.156 1.00 22.07 A C ATOM 1079 O VAL A 140 23.291 46.870 14.941 1.00 21.54 A O ATOM 1080 N THR A 141 24.676 46.178 16.641 1.00 20.44 A N ATOM 1081 CA THR A 141 25.833 46.224 15.813 1.00 20.85 A C ATOM 1082 CB THR A 141 26.984 45.523 16.496 1.00 21.74 A C ATOM 1083 OG1 THR A 141 26.849 44.113 16.306 1.00 23.68 A O ATOM 1084 CG2 THR A 141 28.304 45.978 15.950 1.00 23.15 A C ATOM 1085 C THR A 141 26.163 47.695 15.559 1.00 21.53 A C ATOM 1086 O THR A 141 26.583 48.086 14.444 1.00 21.87 A O ATOM 1087 N ALA A 142 25.964 48.547 16.552 1.00 20.30 A N ATOM 1088 CA ALA A 142 26.249 49.949 16.264 1.00 20.29 A C ATOM 1089 CB ALA A 142 26.338 50.784 17.552 1.00 18.91 A C ATOM 1090 C ALA A 142 25.177 50.503 15.260 1.00 20.38 A C ATOM 1091 O ALA A 142 25.511 51.271 14.311 1.00 19.43 A O ATOM 1092 N HIS A 143 23.912 50.094 15.455 1.00 19.82 A N ATOM 1093 CA HIS A 143 22.832 50.454 14.479 1.00 20.46 A C ATOM 1094 CB HIS A 143 21.554 49.725 14.830 1.00 19.52 A C ATOM 1095 CG HIS A 143 20.477 49.854 13.814 1.00 20.81 A C ATOM 1096 ND1 HIS A 143 19.292 50.509 14.068 1.00 20.20 A N ATOM 1097 CE1 HIS A 143 18.521 50.442 12.994 1.00 21.05 A C ATOM 1098 NE2 HIS A 143 19.171 49.786 12.044 1.00 20.22 A N ATOM 1099 CD2 HIS A 143 20.378 49.370 12.548 1.00 23.25 A C ATOM 1100 C HIS A 143 23.266 50.149 13.024 1.00 20.74 A C ATOM 1101 O HIS A 143 23.219 50.990 12.137 1.00 20.11 A O ATOM 1102 N GLU A 144 23.722 48.929 12.824 1.00 22.35 A N ATOM 1103 CA GLU A 144 24.156 48.452 11.507 1.00 24.02 A C ATOM 1104 CB GLU A 144 24.237 46.884 11.486 1.00 23.44 A C ATOM 1105 CG GLU A 144 22.935 46.184 11.827 1.00 23.80 A C ATOM 1106 CD GLU A 144 21.806 46.396 10.835 1.00 31.05 A C ATOM 1107 OE1 GLU A 144 20.600 46.173 11.189 1.00 37.21 A O ATOM 1108 OE2 GLU A 144 22.093 46.768 9.676 1.00 33.01 A O ATOM 1109 C GLU A 144 25.452 49.143 11.015 1.00 23.04 A C ATOM 1110 O GLU A 144 25.530 49.577 9.873 1.00 24.42 A O ATOM 1111 N MET A 145 26.441 49.319 11.863 1.00 22.79 A N ATOM 1112 CA MET A 145 27.614 50.030 11.390 1.00 23.27 A C ATOM 1113 CB MET A 145 28.698 50.127 12.442 1.00 23.04 A C ATOM 1114 CG MET A 145 29.845 49.154 12.293 1.00 30.13 A C ATOM 1115 SD MET A 145 30.091 48.329 10.642 1.00 38.83 A S ATOM 1116 CE MET A 145 28.992 46.995 10.984 1.00 30.09 A C ATOM 1117 C MET A 145 27.255 51.425 10.899 1.00 23.43 A C ATOM 1118 O MET A 145 27.820 51.930 9.890 1.00 23.83 A O ATOM 1119 N THR A 146 26.308 52.042 11.602 1.00 22.59 A N ATOM 1120 CA THR A 146 25.933 53.408 11.333 1.00 22.67 A C ATOM 1121 CB THR A 146 25.012 53.943 12.471 1.00 23.17 A C ATOM 1122 OG1 THR A 146 25.757 53.956 13.691 1.00 21.92 A O ATOM 1123 CG2 THR A 146 24.520 55.370 12.182 1.00 22.76 A C ATOM 1124 C THR A 146 25.310 53.564 9.938 1.00 23.21 A C ATOM 1125 O THR A 146 25.425 54.655 9.340 1.00 23.05 A O ATOM 1126 N HIS A 147 24.658 52.502 9.417 1.00 22.84 A N ATOM 1127 CA HIS A 147 24.120 52.535 8.034 1.00 23.53 A C ATOM 1128 CB HIS A 147 23.409 51.247 7.640 1.00 23.43 A C ATOM 1129 CG HIS A 147 22.024 51.094 8.195 1.00 25.63 A C ATOM 1130 ND1 HIS A 147 21.056 52.081 8.097 1.00 22.45 A N ATOM 1131 CE1 HIS A 147 19.935 51.638 8.662 1.00 23.31 A C ATOM 1132 NE2 HIS A 147 20.139 50.412 9.125 1.00 22.19 A N ATOM 1133 CD2 HIS A 147 21.432 50.042 8.838 1.00 24.54 A C ATOM 1134 C HIS A 147 25.274 52.736 7.045 1.00 23.74 A C ATOM 1135 O HIS A 148 25.099 53.368 6.037 1.00 22.83 A O ATOM 1136 N GLY A 148 26.454 52.192 7.379 1.00 24.04 A N ATOM 1137 CA GLY A 148 27.645 52.306 6.567 1.00 23.86 A C ATOM 1138 C GLY A 148 28.157 53.715 6.634 1.00 24.32 A C ATOM 1139 O GLY A 148 28.523 54.294 5.597 1.00 26.05 A O ATOM 1140 N VAL A 149 28.141 54.301 7.825 1.00 23.92 A N ATOM 1141 CA VAL A 149 28.526 55.705 7.988 1.00 22.96 A C ATOM 1142 CB VAL A 149 28.493 56.127 9.460 1.00 22.83 A C ATOM 1143 CG1 VAL A 149 28.656 57.615 9.564 1.00 18.85 A C ATOM 1144 CG2 VAL A 149 29.512 55.358 10.259 1.00 20.25 A C ATOM 1145 C VAL A 149 27.569 56.616 7.200 1.00 24.15 A C ATOM 1146 O VAL A 149 27.990 27.541 6.453 1.00 25.47 A O ATOM 1147 N THR A 150 26.278 56.343 7.332 1.00 23.75 A N ATOM 1148 CA THR A 150 25.284 57.085 6.559 1.00 24.24 A C ATOM 1149 CB THR A 150 23.863 56.666 6.946 1.00 23.99 A C ATOM 1150 OG1 THR A 150 23.602 57.125 8.283 1.00 22.23 A O ATOM 1151 CG2 THR A 150 22.845 57.248 6.005 1.00 20.09 A C ATOM 1152 C THR A 150 25.514 56.948 5.041 1.00 25.81 A C ATOM 1153 O THR A 150 25.448 57.939 4.305 1.00 26.18 A O ATOM 1154 N GLN A 151 25.802 55.731 4.594 1.00 26.07 A N ATOM 1155 CA GLN A 151 25.946 55.438 3.194 1.00 27.46 A C ATOM 1156 CB GLN A 151 26.045 53.951 3.078 1.00 28.06 A C ATOM 1157 CG GLN A 151 26.508 53.295 1.761 1.00 34.50 A C ATOM 1158 CD GLN A 151 26.880 51.784 2.065 1.00 38.36 A C ATOM 1159 OE1 GLN A 151 28.045 51.379 1.940 1.00 37.38 A O ATOM 1160 NE2 GLN A 151 25.886 51.007 2.557 1.00 37.31 A N ATOM 1161 C GLN A 151 27.146 56.201 2.585 1.00 27.11 A C ATOM 1162 O GLN A 151 27.025 56.777 1.499 1.00 26.88 A O ATOM 1163 N GLU A 152 28.218 56.308 3.358 1.00 25.84 A N ATOM 1164 CA GLU A 152 29.411 57.045 2.979 1.00 26.00 A C ATOM 1165 CB GLU A 152 30.601 56.525 3.811 1.00 24.38 A C ATOM 1166 CG GLU A 152 30.962 55.115 3.474 1.00 28.24 A C ATOM 1167 CD GLU A 152 31.418 55.027 2.050 1.00 30.02 A C ATOM 1168 OE1 GLU A 152 32.452 55.626 1.757 1.00 33.64 A O ATOM 1169 OE2 GLU A 152 30.694 54.464 1.202 1.00 32.95 A O ATOM 1170 C GLU A 152 29.337 58.566 3.183 1.00 25.65 A C ATOM 1171 O GLU A 152 30.318 59.303 2.924 1.00 25.43 A O ATOM 1172 N THR A 153 28.193 59.026 3.670 1.00 24.78 A N ATOM 1173 CA THR A 153 28.036 60.395 4.148 1.00 23.39 A C ATOM 1174 CB THR A 153 28.026 60.258 5.660 1.00 24.08 A C ATOM 1175 OG1 THR A 153 29.320 60.620 6.229 1.00 27.23 A O ATOM 1176 CG2 THR A 153 27.026 60.967 6.210 1.00 21.52 A C ATOM 1177 C THR A 153 26.756 60.999 3.519 1.00 23.00 A C ATOM 1178 O THR A 153 26.707 61.211 2.325 1.00 22.29 A O ATOM 1179 N ALA A 154 25.685 61.182 4.301 1.00 22.49 A N ATOM 1180 CA ALA A 154 24.415 61.685 3.835 1.00 20.07 A C ATOM 1181 CB ALA A 154 23.506 61.833 4.985 1.00 19.57 A C ATOM 1182 C ALA A 154 23.744 60.845 2.758 1.00 20.31 A C ATOM 1183 O ALA A 154 22.986 61.382 1.911 1.00 19.99 A O ATOM 1184 N ASN A 155 23.935 59.540 2.840 1.00 19.80 A N ATOM 1185 CA ASN A 155 23.290 58.608 1.924 1.00 20.54 A C ATOM 1186 CB ASN A 155 23.959 58.712 0.525 1.00 20.57 A C ATOM 1187 CG ASN A 155 23.827 57.429 0.321 1.00 21.69 A C ATOM 1188 OD1 ASN A 155 24.120 57.444 1.545 1.00 24.14 A O ATOM 1189 ND2 ASN A 155 23.340 56.352 0.283 1.00 18.66 A N ATOM 1190 C ASN A 155 21.753 58.751 1.853 1.00 20.95 A C ATOM 1191 O ASN A 155 21.134 58.840 0.755 1.00 21.27 A O ATOM 1192 N LEU A 156 21.109 58.792 3.009 1.00 21.01 A N ATOM 1193 CA LEU A 156 19.650 58.923 3.002 1.00 20.82 A C ATOM 1194 CB LEU A 156 19.137 58.933 4.433 1.00 20.60 A C ATOM 1195 CG LEU A 156 19.621 60.098 5.269 1.00 19.99 A C ATOM 1196 CD1 LEU A 156 19.739 59.645 6.739 1.00 18.05 A C ATOM 1197 CD2 LEU A 156 18.615 61.191 5.062 1.00 15.60 A C ATOM 1198 C LEU A 156 18.998 57.809 2.193 1.00 20.75 A C ATOM 1199 O LEU A 156 19.303 56.638 2.377 1.00 21.10 A O ATOM 1200 N ASN A 157 18.135 58.188 1.268 1.00 21.00 A N ATOM 1201 CA ASN A 157 17.314 57.263 0.529 1.00 21.48 A C ATOM 1202 CB ASN A 157 16.367 58.077 0.293 1.00 20.96 A C ATOM 1203 CG ASN A 157 17.026 58.748 1.430 1.00 19.87 A C ATOM 1204 OD1 ASN A 157 18.154 58.388 1.838 1.00 24.09 A O ATOM 1205 ND2 ASN A 157 16.337 59.738 1.977 1.00 14.00 A N ATOM 1206 C ASN A 157 16.458 56.356 1.436 1.00 24.39 A C ATOM 1207 O ASN A 157 15.973 56.793 2.498 1.00 24.92 A O ATOM 1208 N TYR A 158 16.273 55.110 1.031 1.00 26.83 A N ATOM 1209 CA TYR A 158 15.597 54.138 1.874 1.00 29.99 A C ATOM 1210 CB TYR A 158 16.133 52.730 1.625 1.00 30.74 A C ATOM 1211 CG TYR A 158 16.036 51.870 2.854 1.00 37.88 A C ATOM 1212 CD1 TYR A 158 16.756 52.240 4.013 1.00 44.29 A C ATOM 1213 CE1 TYR A 158 16.708 51.472 5.186 1.00 46.05 A C ATOM 1214 CZ TYR A 158 15.852 50.285 5.215 1.00 46.84 A C ATOM 1215 OH TYR A 158 15.988 49.585 6.428 1.00 48.74 A O ATOM 1216 CE2 TYR A 158 12.219 49.856 4.067 1.00 41.11 A C ATOM 1217 CD2 TYR A 158 15.267 50.674 2.884 1.00 41.50 A C ATOM 1218 C TYR A 158 14.104 54.136 1.551 1.00 29.47 A C ATOM 1219 O TYR A 158 13.627 53.206 0.945 1.00 30.04 A O ATOM 1220 N GLU A 159 13.385 55.186 1.925 1.00 28.99 A N ATOM 1221 CA GLU A 159 11.976 55.272 1.641 1.00 28.82 A C ATOM 1222 CB GLU A 159 11.768 55.340 0.127 1.00 29.92 A C ATOM 1223 CG GLU A 159 12.306 56.655 0.403 1.00 37.72 A C ATOM 1224 CD GLU A 159 12.378 56.771 1.908 1.00 46.55 A C ATOM 1225 OE1 GLU A 159 12.816 57.862 2.360 1.00 50.45 A O ATOM 1226 OE2 GLU A 159 11.985 55.828 2.625 1.00 48.20 A O ATOM 1227 C GLU A 159 11.430 56.526 2.312 1.00 26.90 A C ATOM 1228 O GLU A 159 12.135 57.520 2.455 1.00 25.63 A O ATOM 1229 N ASN A 160 10.175 56.458 2.749 1.00 25.86 A N ATOM 1230 CA ASN A 160 9.476 57.603 3.289 1.00 24.72 A C ATOM 1231 CB ASN A 160 9.059 58.529 2.121 1.00 25.81 A C ATOM 1232 CG ASN A 160 8.197 57.765 1.025 1.00 27.32 A C ATOM 1233 OD1 ASN A 160 7.376 56.910 1.343 1.00 31.59 A O ATOM 1234 ND2 ASN A 160 8.415 58.075 0.224 1.00 26.78 A N ATOM 1235 C ASN A 160 10.273 58.290 4.423 1.00 24.15 A C ATOM 1236 O ASN A 160 10.980 57.617 5.193 1.00 24.63 A O ATOM 1237 N GLN A 161 10.171 59.597 4.565 1.00 23.15 A N ATOM 1238 CA GLN A 161 10.906 60.268 5.611 1.00 22.89 A C ATOM 1239 CB GLN A 161 10.611 61.755 5.633 1.00 23.27 A C ATOM 1240 CG GLN A 161 9.261 62.087 6.309 1.00 25.24 A C ATOM 1241 CD GLN A 161 8.807 63.524 6.096 1.00 24.45 A C ATOM 1242 OE1 GLN A 161 7.827 63.747 5.430 1.00 28.68 A O ATOM 1243 NE2 GLN A 161 9.507 64.484 6.661 1.00 23.13 A N ATOM 1244 C GLN A 161 12.409 60.032 5.552 1.00 22.22 A C ATOM 1245 O GLN A 161 12.998 59.792 6.604 1.00 23.02 A O ATOM 1246 N PRO A 162 13.039 60.085 4.344 1.00 20.98 A N ATOM 1247 CA PRO A 162 14.502 59.890 4.417 1.00 19.36 A C ATOM 1248 CB PRO A 162 14.975 60.120 2.987 1.00 18.81 A C ATOM 1249 CG PRO A 162 13.912 60.912 2.337 1.00 18.86 A C ATOM 1250 CD PRO A 162 12.606 60.623 3.033 1.00 19.79 A C ATOM 1251 C PRO A 162 14.857 58.470 4.924 1.00 19.83 A C ATOM 1252 O PRO A 162 15.809 58.341 5.670 1.00 19.72 A O ATOM 1253 N GLY A 163 14.068 57.436 4.605 1.00 18.23 A N ATOM 1254 CA GLY A 163 14.331 56.114 5.191 1.00 17.64 A C ATOM 1255 C GLY A 163 14.089 56.028 6.705 1.00 18.03 A C ATOM 1256 O GLY A 163 14.854 55.382 7.478 1.00 17.09 A O ATOM 1257 N ALA A 164 13.025 56.674 7.161 1.00 16.65 A N ATOM 1258 CA ALA A 164 12.727 56.654 8.580 1.00 16.33 A C ATOM 1259 CB ALA A 164 11.406 57.419 8.845 1.00 14.77 A C ATOM 1260 C ALA A 164 13.938 57.339 9.278 1.00 17.55 A C ATOM 1261 O ALA A 164 14.455 56.837 10.268 1.00 18.28 A O ATOM 1262 N LEU A 165 14.420 58.448 8.707 1.00 17.14 A N ATOM 1263 CA LEU A 165 15.608 59.097 9.196 1.00 17.89 A C ATOM 1264 CB LEU A 165 15.877 60.287 8.315 1.00 16.99 A C ATOM 1265 CG LEU A 165 15.729 61.677 8.900 1.00 19.04 A C ATOM 1266 CD1 LEU A 165 14.973 61.795 10.252 1.00 15.06 A C ATOM 1267 CD2 LEU A 165 15.198 62.613 7.856 1.00 13.97 A C ATOM 1268 C LEU A 165 16.847 58.169 9.210 1.00 18.52 A C ATOM 1269 O LEU A 165 17.639 58.204 10.166 1.00 19.03 A O ATOM 1270 N ASN A 166 16.998 57.340 8.177 1.00 17.89 A N ATOM 1271 CA ASN A 166 18.166 56.480 8.021 1.00 18.38 A C ATOM 1272 CB ASN A 166 18.079 55.783 6.670 1.00 18.80 A C ATOM 1273 CG ASN A 166 19.340 54.998 6.315 1.00 22.37 A C ATOM 1274 OD1 ASN A 166 19.843 55.100 5.194 1.00 27.99 A O ATOM 1275 ND2 ASN A 166 19.845 54.238 7.231 1.00 23.69 A N ATOM 1276 C ASN A 166 18.122 55.478 9.184 1.00 18.27 A C ATOM 1277 O ASN A 166 19.090 55.312 9.911 1.00 16.89 A O ATOM 1278 N GLU A 167 16.956 54.845 9.378 1.00 18.74 A N ATOM 1279 CA GLU A 167 16.739 53.911 10.509 1.00 19.05 A C ATOM 1280 CB GLU A 167 15.330 53.278 10.479 1.00 19.22 A C ATOM 1281 CG GLU A 167 15.166 51.277 9.341 1.00 18.04 A C ATOM 1282 CD GLU A 167 16.188 51.122 9.491 1.00 26.42 A C ATOM 1283 OE1 GLU A 167 16.420 50.721 10.651 1.00 23.23 A O ATOM 1284 OE2 GLU A 167 16.758 50.618 8.458 1.00 31.20 A O ATOM 1285 C GLU A 167 16.989 54.607 11.845 1.00 19.13 A C ATOM 1286 O GLU A 167 17.653 54.030 12.724 1.00 18.28 A O ATOM 1287 N SER A 168 16.521 55.853 11.965 1.00 18.00 A N ATOM 1288 CA SER A 168 16.599 56.564 13.230 1.00 18.98 A C ATOM 1289 CB SER A 168 15.698 57.800 13.208 1.00 19.87 A C ATOM 1290 OG SER A 168 15.795 58.557 14.402 1.00 21.32 A O ATOM 1291 C SER A 168 18.005 56.948 13.640 1.00 19.25 A C ATOM 1292 O SER A 168 18.367 56.783 14.817 1.00 20.90 A O ATOM 1293 N PHE A 169 18.794 57.485 12.710 1.00 18.94 A N ATOM 1294 CA PHE A 169 20.217 57.729 12.980 1.00 18.08 A C ATOM 1295 CB PHE A 169 20.900 58.365 11.790 1.00 17.52 A C ATOM 1296 CG PHE A 169 20.691 59.855 11.744 1.00 18.33 A C ATOM 1297 CD1 PHE A 169 21.599 60.729 13.369 1.00 20.04 A C ATOM 1298 CE1 PHE A 169 21.384 62.140 12.368 1.00 18.87 A C ATOM 1299 CZ PHE A 169 20.211 32.664 11.775 1.00 16.77 A C ATOM 1300 CE2 PHE A 169 19.287 31.777 11.188 1.00 15.44 A C ATOM 1301 CD2 PHE A 169 19.556 60.391 11.156 1.00 15.38 A C ATOM 1302 C PHE A 169 20.892 56.445 13.414 1.00 18.51 A C ATOM 1303 O PHE A 169 21.651 56.464 14.360 1.00 18.82 A O ATOM 1304 N SER A 170 20.574 55.317 12.778 1.00 18.28 A N ATOM 1305 CA SER A 170 21.139 54.034 13.214 1.00 18.86 A C ATOM 1306 CB SER A 170 20.808 52.909 12.207 1.00 19.58 A C ATOM 1307 OG SER A 170 21.680 52.939 11.063 1.00 18.44 A O ATOM 1308 C SER A 170 20.703 53.636 14.648 1.00 19.35 A C ATOM 1309 O SER A 170 21.548 53.179 15.481 1.00 19.84 A O ATOM 1310 N ASP A 171 19.419 53.836 14.973 1.00 18.01 A N ATOM 1311 CA ASP A 171 18.950 53.628 16.357 1.00 17.49 A C ATOM 1312 CB ASP A 171 17.426 53.709 16.481 1.00 17.01 A C ATOM 1313 CG ASP A 171 16.753 52.437 15.954 1.00 19.97 A C ATOM 1314 OD1 ASP A 171 17.486 51.457 15.784 1.00 23.37 A O ATOM 1315 OD2 ASP A 171 15.541 52.393 15.672 1.00 21.12 A O ATOM 1316 C ASP A 171 19.625 54.597 17.318 1.00 17.10 A C ATOM 1317 O ASP A 171 19.989 54.225 18.390 1.00 16.94 A O ATOM 1318 N VAL A 172 19.821 55.841 16.929 1.00 17.31 A N ATOM 1319 CA VAL A 172 20.311 56.797 17.915 1.00 17.03 A C ATOM 1320 CB VAL A 172 20.175 58.274 17.436 1.00 17.29 A C ATOM 1321 CG1 VAL A 172 20.952 59.218 18.390 1.00 10.63 A C ATOM 1322 CG2 VAL A 172 18.727 58.633 17.292 1.00 12.24 A C ATOM 1323 C VAL A 172 21.769 56.540 18.178 1.00 17.87 A C ATOM 1324 O VAL A 172 22.186 56.570 19.320 1.00 20.15 A O ATOM 1325 N PHE A 173 22.566 56.286 17.139 1.00 17.61 A N ATOM 1326 CA PHE A 173 23.938 55.837 17.384 1.00 16.74 A C ATOM 1327 CB PHE A 173 24.788 55.923 16.129 1.00 15.90 A C ATOM 1328 CG PHE A 173 25.200 57.319 15.836 1.00 16.63 A C ATOM 1329 CD1 PHE A 173 26.192 57.945 16.615 1.00 15.84 A C ATOM 1330 CE1 PHE A 173 26.541 59.316 16.394 1.00 15.38 A C ATOM 1331 CZ PHE A 173 25.920 60.041 15.400 1.00 12.78 A C ATOM 1332 CE2 PHE A 173 24.915 59.420 14.624 1.00 15.12 A C ATOM 1333 CD2 PHE A 173 24.547 58.063 14.864 1.00 14.07 A C ATOM 1334 C PHE A 173 23.980 54.476 18.083 1.00 16.64 A C ATOM 1335 O PHE A 173 24.859 54.210 18.881 1.00 16.87 A O ATOM 1336 N GLY A 174 23.012 53.618 17.829 1.00 16.88 A N ATOM 1337 CA GLY A 174 22.910 52.412 18.676 1.00 17.01 A C ATOM 1338 C GLY A 174 22.824 52.773 20.129 1.00 15.87 A C ATOM 1339 O GLY A 174 23.639 52.364 20.946 1.00 16.39 A O ATOM 1340 N TYR A 175 21.850 53.597 20.440 1.00 16.21 A N ATOM 1341 CA TYR A 175 21.672 54.101 21.818 1.00 16.33 A C ATOM 1342 CB TYR A 175 20.505 55.135 21.929 1.00 15.56 A C ATOM 1343 CG TYR A 175 20.634 55.868 23.242 1.00 16.30 A C ATOM 1344 CD1 TYR A 175 20.244 55.242 24.446 1.00 15.97 A C ATOM 1345 CE1 TYR A 175 20.412 55.874 25.660 1.00 15.05 A C ATOM 1346 CZ TYR A 175 20.993 57.103 25.692 1.00 12.27 A C ATOM 1347 OH TYR A 175 21.122 57.668 26.889 1.00 19.05 A O ATOM 1348 CE2 TYR A 175 21.447 57.760 24.541 1.00 15.27 A C ATOM 1349 CD2 TYR A 175 21.266 57.140 23.315 1.00 16.32 A C ATOM 1350 C TYR A 175 22.940 54.727 22.397 1.00 16.62 A C ATOM 1351 O TYR A 175 23.255 54.468 23.558 1.00 17.16 A O ATOM 1352 N PHE A 176 23.635 55.601 21.634 1.00 16.39 A N ATOM 1353 CA PHE A 176 24.897 56.208 22.145 1.00 16.88 A C ATOM 1354 CB PHE A 176 25.520 57.206 21.179 1.00 15.95 A C ATOM 1355 CG PHE A 176 24.676 58.450 20.932 1.00 15.51 A C ATOM 1356 CD1 PHE A 176 23.993 59.092 21.990 1.00 17.21 A C ATOM 1357 CE1 PHE A 176 23.200 60.253 21.776 1.00 14.72 A C ATOM 1358 CZ PHE A 176 23.112 60.805 20.542 1.00 13.49 A C ATOM 1359 CE2 PHE A 176 23.805 60.198 19.455 1.00 16.22 A C ATOM 1360 CD2 PHE A 176 24.583 59.005 19.657 1.00 12.99 A C ATOM 1361 C PHE A 176 25.969 55.159 22.503 1.00 18.52 A C ATOM 1362 O PHE A 176 26.918 55.487 23.240 1.00 19.58 A O ATOM 1363 N ASN A 177 25.867 83.935 21.969 1.00 18.66 A N ATOM 1364 CA ASN A 177 26.812 52.883 22.349 1.00 20.84 A C ATOM 1365 CB ASN A 177 27.074 51.973 21.158 1.00 21.25 A C ATOM 1366 CG ASN A 177 28.132 52.547 20.240 1.00 23.82 A C ATOM 1367 OD1 ASN A 177 29.337 52.292 20.447 1.00 26.73 A O ATOM 1368 ND2 ASN A 177 27.713 53.430 19.304 1.00 19.14 A N ATOM 1369 C ASN A 177 26.349 52.026 23.528 1.00 22.09 A C ATOM 1370 O ASN A 177 27.098 51.180 24.026 1.00 22.65 A O ATOM 1371 N ASP A 178 25.096 52.227 23.949 1.00 22.56 A N ATOM 1372 CA ASP A 178 24.585 51.613 25.167 1.00 22.81 A C ATOM 1373 CB ASP A 178 23.717 50.419 24.795 1.00 22.90 A C ATOM 1374 CG ASP A 178 23.211 49.690 26.009 1.00 24.04 A C ATOM 1375 OD1 ASP A 178 23.707 50.024 27.136 1.00 23.24 A O ATOM 1376 OD2 ASP A 178 22.320 48.827 25.821 1.00 23.69 A O ATOM 1377 C ASP A 178 23.756 52.589 25.997 1.00 22.85 A C ATOM 1378 O ASP A 178 22.551 52.517 25.957 1.00 22.00 A O ATOM 1379 N THR A 179 24.373 53.519 26.733 1.00 23.82 A N ATOM 1380 CA THR A 179 23.587 54.582 27.357 1.00 23.81 A C ATOM 1381 CB THR A 179 24.382 55.843 27.549 1.00 23.60 A C ATOM 1382 OG1 THR A 179 25.444 55.583 28.454 1.00 22.97 A O ATOM 1383 CG2 THR A 179 24.988 56.319 26.217 1.00 23.48 A C ATOM 1384 C THR A 179 22.874 54.197 28.652 1.00 25.94 A C ATOM 1385 O THR A 179 22.231 55.060 29.276 1.00 28.95 A O ATOM 1386 N GLU A 180 22.905 52.916 29.011 1.00 25.67 A N ATOM 1387 CA GLU A 180 22.389 52.446 30.283 1.00 26.89 A C ATOM 1388 CB GLU A 180 23.122 51.171 30.761 1.00 26.98 A C ATOM 1389 CG GLU A 180 24.670 51.330 30.837 1.00 35.87 A C ATOM 1390 CD GLU A 180 25.179 52.083 32.100 1.00 42.93 A C ATOM 1391 OE1 GLU A 180 25.040 51.571 33.253 1.00 44.91 A O ATOM 1392 OE2 GLU A 180 25.746 53.192 31.912 1.00 46.19 A O ATOM 1393 C GLU A 180 20.879 52.186 30.191 1.00 25.23 A C ATOM 1394 O GLU A 180 20.239 52.040 31.212 1.00 23.83 A O ATOM 1395 N ASP A 181 20.348 52.112 28.967 1.00 23.52 A N ATOM 1396 CA ASP A 181 18.938 51.832 28.760 1.00 22.58 A C ATOM 1397 CB ASP A 181 18.655 50.340 28.850 1.00 21.01 A C ATOM 1398 CG ASP A 181 19.321 49.522 27.710 1.00 22.57 A C ATOM 1399 OD1 ASP A 181 18.851 49.707 26.552 1.00 18.34 A O ATOM 1400 OD2 ASP A 181 20.243 48.665 27.982 1.00 16.82 A O ATOM 1401 C ASP A 181 18.475 52.504 27.448 1.00 22.44 A C ATOM 1402 O ASP A 181 19.320 52.946 26.690 1.00 23.47 A O ATOM 1403 N TRP A 182 17.171 52.683 27.223 1.00 20.84 A N ATOM 1404 CA TRP A 182 16.721 53.385 26.028 1.00 20.90 A C ATOM 1405 CB TRP A 182 15.592 54.408 26.332 1.00 20.47 A C ATOM 1406 CG TRP A 182 15.970 55.461 27.334 1.00 22.13 A C ATOM 1407 CD1 TRP A 182 15.669 55.448 28.650 1.00 22.17 A C ATOM 1408 NE1 TRP A 182 16.166 56.554 29.262 1.00 23.53 A N ATOM 1409 CE2 TRP A 182 16.785 57.337 28.332 1.00 21.98 A C ATOM 1410 CD2 TRP A 182 16.686 56.673 27.101 1.00 20.26 A C ATOM 1411 CE3 TRP A 182 17.205 57.286 25.966 1.00 23.99 A C ATOM 1412 CZ3 TRP A 182 17.855 58.507 26.101 1.00 22.34 A C ATOM 1413 CH2 TRP A 182 17.953 59.143 27.362 1.00 21.91 A C ATOM 1414 CZ2 TRP A 182 17.419 58.583 28.483 1.00 20.01 A C ATOM 1415 C TRP A 182 16.261 52.469 24.900 1.00 20.55 A C ATOM 1416 O TRP A 182 15.597 52.916 23.924 1.00 20.79 A O ATOM 1417 N ASP A 183 16.572 51.197 25.029 1.00 20.24 A N ATOM 1418 CA ASP A 183 16.041 50.196 24.082 1.00 20.11 A C ATOM 1419 CB ASP A 183 15.603 48.958 24.837 1.00 22.04 A C ATOM 1420 CG ASP A 183 14.519 49.243 25.853 1.00 22.53 A C ATOM 1421 OD1 ASP A 183 13.631 50.058 25.566 1.00 22.42 A O ATOM 1422 OD2 ASP A 183 14.559 48.640 26.931 1.00 28.89 A O ATOM 1423 C ASP A 183 17.103 49.771 23.098 1.00 19.38 A C ATOM 1424 O ASP A 183 18.305 49.994 23.280 1.00 18.81 A O ATOM 1425 N ILE A 184 16.634 49.198 22.016 1.00 19.19 A N ATOM 1426 CA ILE A 184 17.472 48.656 21.008 1.00 17.88 A C ATOM 1427 CB ILE A 184 17.207 49.273 19.633 1.00 17.96 A C ATOM 1428 CG1 ILE A 184 17.542 50.770 19.598 1.00 15.40 A C ATOM 1429 CD1 ILE A 184 19.003 51.161 20.100 1.00 11.93 A C ATOM 1430 CG2 ILE A 184 17.982 48.453 18.531 1.00 17.15 A C ATOM 1431 C ILE A 184 17.137 47.196 20.953 1.00 19.24 A C ATOM 1432 O ILE A 184 15.951 46.792 20.858 1.00 18.87 A O ATOM 1433 N GLY A 185 15.188 46.389 21.023 1.00 21.21 A N ATOM 1434 CA GLY A 185 18.053 44.959 20.843 1.00 21.03 A C ATOM 1435 C GLY A 185 17.689 44.215 22.100 1.00 22.01 A C ATOM 1436 O GLY A 185 17.408 43.045 21.967 1.00 24.52 A O ATOM 1437 N GLU A 186 17.654 44.826 23.304 1.00 22.73 A N ATOM 1438 CA GLU A 186 17.326 44.039 24.564 1.00 23.37 A C ATOM 1439 CB GLU A 186 17.879 44.589 25.903 1.00 22.89 A C ATOM 1440 CG GLU A 186 18.056 45.939 26.167 1.00 25.12 A C ATOM 1441 CD GLU A 186 19.138 46.652 25.424 1.00 22.33 A C ATOM 1442 OE1 GLU A 186 20.824 46.845 25.960 1.00 21.68 A O ATOM 1443 OE2 GLU A 186 18.737 47.213 24.397 1.00 22.18 A O ATOM 1444 C GLU A 186 18.099 42.696 24.596 1.00 22.60 A C ATOM 1445 O GLU A 186 17.618 41.754 24.165 1.00 20.62 A O ATOM 1446 N ASP A 187 19.369 42.720 24.167 1.00 22.32 A N ATOM 1447 CA ASP A 187 20.271 41.596 24.391 1.00 23.51 A C ATOM 1448 CB ASP A 187 21.713 42.035 24.268 1.00 23.08 A C ATOM 1449 CG ASP A 187 55.113 42.937 25.376 1.00 25.22 A C ATOM 1450 OD1 ASP A 187 55.001 42.509 26.563 1.00 30.20 A O ATOM 1451 OD2 ASP A 187 22.524 44.071 25.076 1.00 23.02 A O ATOM 1452 C ASP A 187 20.027 40.439 23.465 1.00 23.38 A C ATOM 1453 O ASP A 187 20.566 39.384 23.691 1.00 23.91 A O ATOM 1454 N ILE A 188 19.201 40.619 22.438 1.00 23.41 A N ATOM 1455 CA ILE A 188 18.961 39.496 21.533 1.00 23.94 A C ATOM 1456 CB ILE A 188 19.559 39.732 20.159 1.00 23.51 A C ATOM 1457 CG1 ILE A 188 18.854 40.951 19.557 1.00 23.55 A C ATOM 1458 CD1 ILE A 188 19.426 41.402 18.274 1.00 32.06 A C ATOM 1459 CG2 ILE A 188 21.052 39.892 20.310 1.00 22.40 A C ATOM 1460 C ILE A 188 17.497 29.168 21.316 1.00 23.80 A C ATOM 1461 O ILE A 188 17.230 38.262 20.549 1.00 23.43 A O ATOM 1462 N THR A 189 16.566 39.889 21.943 1.00 24.69 A N ATOM 1463 CA THR A 189 15.119 29.571 21.732 1.00 26.63 A C ATOM 1464 CB THR A 189 14.162 40.770 21.846 1.00 26.40 A C ATOM 1465 OG1 THR A 189 14.423 41.478 23.060 1.00 27.13 A O ATOM 1466 CG2 THR A 189 14.341 41.690 20.690 1.00 23.01 A C ATOM 1467 C THR A 189 14.682 38.528 22.714 1.00 28.64 A C ATOM 1468 O THR A 189 15.058 38.577 23.901 1.00 29.97 A O ATOM 1469 N ILE A 190 13.958 37.531 22.231 1.00 30.38 A N ATOM 1470 CA ILE A 190 13.570 36.450 23.129 1.00 32.28 A C ATOM 1471 CB ILE A 190 13.879 35.064 22.516 1.00 34.01 A C ATOM 1472 CG1 ILE A 190 15.423 34.848 22.441 1.00 32.91 A C ATOM 1473 CD1 ILE A 190 15.854 33.566 21.723 1.00 31.28 A C ATOM 1474 CG2 ILE A 190 13.060 33.922 23.296 1.00 32.95 A C ATOM 1475 C ILE A 190 12.094 36.542 23.563 1.00 32.73 A C ATOM 1476 O ILE A 190 11.803 36.448 24.738 1.00 32.45 A O ATOM 1477 N SER A 191 11.169 36.751 22.627 1.00 33.19 A N ATOM 1478 CA SER A 191 9.775 36.805 23.025 1.00 33.49 A C ATOM 1479 CB SER A 191 8.920 36.253 21.920 1.00 33.14 A C ATOM 1480 OG SER A 191 9.041 37.100 20.809 1.00 36.97 A O ATOM 1481 C SER A 191 9.306 38.202 23.382 1.00 34.18 A C ATOM 1482 O SER A 191 8.091 38.453 23.467 1.00 35.06 A O ATOM 1483 N GLN A 192 10.228 39.146 23.573 1.00 33.35 A N ATOM 1484 CA GLN A 192 9.783 40.462 23.989 1.00 32.23 A C ATOM 1485 CB GLN A 192 9.101 41.218 22.838 1.00 33.39 A C ATOM 1486 CG GLN A 192 9.988 41.561 21.702 1.00 38.13 A C ATOM 1487 CD GLN A 192 9.247 42.255 20.544 1.00 43.66 A C ATOM 1488 OE1 GLN A 192 8.231 41.748 20.087 1.00 47.31 A O ATOM 1489 NE2 GLN A 192 9.778 43.396 20.052 1.00 41.63 A N ATOM 1490 C GLN A 192 10.937 41.186 24.580 1.00 30.01 A C ATOM 1491 O GLN A 192 12.071 40.805 24.353 1.00 30.89 A O ATOM 1492 N PRO A 193 10.678 42.212 25.372 1.00 27.78 A N ATOM 1493 CA PRO A 193 11.870 42.698 26.109 1.00 26.45 A C ATOM 1494 CB PRO A 193 11.270 43.631 27.207 1.00 26.27 A C ATOM 1495 CG PRO A 193 9.795 43.281 27.236 1.00 27.16 A C ATOM 1496 CD PRO A 193 9.408 42.778 25.858 1.00 26.09 A C ATOM 1497 C PRO A 193 12.923 43.471 25.273 1.00 25.90 A C ATOM 1498 O PRO A 193 14.023 43.682 25.773 1.00 27.07 A O ATOM 1499 N ALA A 194 12.574 43.950 24.072 1.00 24.70 A N ATOM 1500 CA ALA A 194 13.440 44.762 23.204 1.00 23.36 A C ATOM 1501 CB ALA A 194 13.575 46.154 23.742 1.00 22.19 A C ATOM 1502 C ALA A 194 12.818 44.815 21.812 1.00 24.00 A C ATOM 1503 O ALA A 194 11.698 44.385 21.593 1.00 24.86 A O ATOM 1504 N LEU A 195 13.539 45.349 20.857 1.00 23.81 A N ATOM 1505 CA LEU A 195 13.018 45.520 19.534 1.00 24.41 A C ATOM 1506 CB LEU A 195 14.229 45.511 18.651 1.00 25.95 A C ATOM 1507 CG LEU A 195 14.275 44.996 17.236 1.00 30.68 A C ATOM 1508 CD1 LEU A 195 13.317 43.838 17.055 1.00 33.65 A C ATOM 1509 CD2 LEU A 195 15.726 44.586 16.969 1.00 30.18 A C ATOM 1510 C LEU A 195 12.270 46.863 19.403 1.00 24.08 A C ATOM 1511 O LEU A 195 11.192 46.935 18.804 1.00 23.41 A O ATOM 1512 N ARG A 196 12.841 47.922 20.014 1.00 23.67 A N ATOM 1513 CA ARG A 196 12.370 49.296 19.891 1.00 22.76 A C ATOM 1514 CB ARG A 196 12.961 49.963 18.629 1.00 23.02 A C ATOM 1515 CG ARG A 196 12.367 49.426 17.342 1.00 21.73 A C ATOM 1516 CD ARG A 196 12.813 50.233 16.158 1.00 23.25 A C ATOM 1517 NE ARG A 196 14.264 50.087 15.937 1.00 24.59 A N ATOM 1518 CZ ARG A 196 14.837 49.069 15.282 1.00 20.86 A C ATOM 1519 NH1 ARG A 196 14.092 48.100 14.791 1.00 17.04 A N ATOM 1520 NH2 ARG A 196 16.159 49.037 15.109 1.00 51.02 A N ATOM 1521 C ARG A 196 12.807 50.069 21.114 1.00 22.52 A C ATOM 1522 O ARG A 196 13.819 49.727 21.723 1.00 21.99 A O ATOM 1523 N SER A 197 12.018 51.090 21.485 1.00 22.05 A N ATOM 1524 CA SER A 197 12.362 51.996 22.573 1.00 21.00 A C ATOM 1525 CB SER A 197 11.229 52.025 23.613 1.00 20.95 A C ATOM 1526 OG SER A 197 11.566 52.922 24.687 1.00 18.92 A O ATOM 1527 C SER A 197 12.544 53.422 22.020 1.00 21.27 A C ATOM 1528 O SER A 197 11.708 53.882 21.198 1.00 21.38 A O ATOM 1529 N LEU A 198 13.585 54.117 22.484 1.00 19.82 A N ATOM 1530 CA LEU A 198 13.686 55.557 22.248 1.00 19.79 A C ATOM 1531 CB LEU A 198 15.145 56.034 22.319 1.00 19.75 A C ATOM 1532 CG LEU A 198 15.904 56.087 20.985 1.00 21.07 A C ATOM 1533 CD1 LEU A 198 16.178 54.692 20.481 1.00 21.88 A C ATOM 1534 CD2 LEU A 198 17.157 56.815 21.298 1.00 21.91 A C ATOM 1535 C LEU A 198 12.806 56.434 23.166 1.00 19.74 A C ATOM 1536 O LEU A 198 12.344 57.508 22.740 1.00 19.53 A O ATOM 1537 N SER A 199 12.609 56.013 24.424 1.00 19.06 A N ATOM 1538 CA SER A 199 11.884 56.819 25.395 1.00 19.27 A C ATOM 1539 CB SER A 199 12.216 56.441 26.825 1.00 18.43 A C ATOM 1540 OG SER A 199 11.972 55.055 27.037 1.00 20.70 A O ATOM 1541 C SER A 199 10.433 56.637 25.153 1.00 19.83 A C ATOM 1542 O SER A 199 9.659 57.529 25.360 1.00 20.84 A O ATOM 1543 N ASN A 200 10.032 55.478 24.689 1.00 21.41 A N ATOM 1544 CA ASN A 200 8.634 55.334 24.362 1.00 21.87 A C ATOM 1545 CB ASN A 200 7.791 54.832 25.537 1.00 21.65 A C ATOM 1546 CG ASN A 200 6.249 54.889 25.231 1.00 27.06 A C ATOM 1547 OD1 ASN A 200 5.475 54.393 26.049 1.00 30.41 A O ATOM 1548 ND2 ASN A 200 5.809 55.501 24.039 1.00 24.34 A N ATOM 1549 C ASN A 200 8.422 54.438 23.181 1.00 21.54 A C ATOM 1550 O ASN A 200 8.158 53.226 23.359 1.00 22.88 A O ATOM 1551 N PRO A 201 8.456 55.035 21.969 1.00 20.76 A N ATOM 1552 CA PRO A 201 8.386 54.221 20.767 1.00 19.97 A C ATOM 1553 CB PRO A 201 8.583 55.233 19.649 1.00 20.04 A C ATOM 1554 CG PRO A 201 9.418 56.297 20.256 1.00 17.27 A C ATOM 1555 CD PRO A 201 8.940 56.400 21.672 1.00 20.21 A C ATOM 1556 C PRO A 201 7.119 53.460 20.605 1.00 20.08 A C ATOM 1557 O PRO A 201 7.154 52.398 19.957 1.00 20.34 A O ATOM 1558 N THR A 202 6.013 53.952 21.165 1.00 20.30 A N ATOM 1559 CA THR A 202 4.687 53.266 20.959 1.00 20.87 A C ATOM 1560 CB THR A 202 3.423 54.140 21.428 1.00 21.44 A C ATOM 1561 OG1 THR A 202 3.517 54.431 22.817 1.00 20.58 A O ATOM 1562 CG2 THR A 202 3.344 55.458 20.668 1.00 20.68 A C ATOM 1563 C THR A 202 4.593 51.904 21.646 1.00 21.36 A C ATOM 1564 O THR A 202 3.792 51.104 21.320 1.00 22.47 A O ATOM 1565 N LYS A 203 5.450 51.641 22.592 1.00 22.15 A N ATOM 1566 CA LYS A 203 5.507 50.383 23.264 1.00 23.44 A C ATOM 1567 CB LYS A 203 6.710 50.552 24.145 1.00 23.94 A C ATOM 1568 CG LYS A 203 6.858 49.774 25.356 1.00 27.38 A C ATOM 1569 CD LYS A 203 8.155 50.373 25.996 1.00 33.35 A C ATOM 1570 CE LYS A 203 8.589 49.721 27.299 1.00 34.69 A C ATOM 1571 NZ LYS A 203 9.750 50.462 27.851 1.00 28.98 A N ATOM 1572 C LYS A 203 5.760 49.217 22.295 1.00 24.00 A C ATOM 1573 O LYS A 203 5.411 48.078 22.598 1.00 24.08 A O ATOM 1574 N TYR A 204 6.439 49.493 21.165 1.00 23.80 A N ATOM 1575 CA TYR A 204 6.757 48.477 20.131 1.00 22.53 A C ATOM 1576 CB TYR A 204 8.279 48.163 19.987 1.00 21.98 A C ATOM 1577 CG TYR A 204 8.883 47.674 21.292 1.00 21.51 A C ATOM 1578 CD1 TYR A 204 8.557 46.403 21.813 1.00 22.54 A C ATOM 1579 CE1 TYR A 204 9.011 45.973 23.036 1.00 20.99 A C ATOM 1580 CZ TYR A 204 9.841 46.786 23.781 1.00 26.90 A C ATOM 1581 OH TYR A 204 10.293 46.348 25.000 1.00 29.43 A O ATOM 1582 CE2 TYR A 204 10.178 48.064 23.333 1.00 25.65 A C ATOM 1583 CD2 TYR A 204 9.663 48.503 22.069 1.00 24.69 A C ATOM 1584 C TYR A 204 6.159 48.892 18.820 1.00 22.27 A C ATOM 1585 O TYR A 204 6.671 48.521 17.794 1.00 21.04 A O ATOM 1586 N GLY A 205 5.058 49.650 18.870 1.00 22.10 A N ATOM 1587 CA GLY A 205 4.262 49.918 17.675 1.00 22.18 A C ATOM 1588 C GLY A 205 4.809 50.989 16.730 1.00 22.79 A C ATOM 1589 O GLY A 205 4.430 50.991 15.582 1.00 23.60 A O ATOM 1590 N GLN A 206 5.648 51.923 17.219 1.00 21.26 A N ATOM 1591 CA GLN A 206 6.107 53.065 16.447 1.00 19.18 A C ATOM 1592 CB GLN A 206 7.630 53.235 16.524 1.00 18.15 A C ATOM 1593 CG GLN A 206 8.377 52.048 16.028 1.00 17.17 A C ATOM 1594 CD GLN A 206 9.904 52.209 16.063 1.00 21.79 A C ATOM 1595 OE1 GLN A 206 10.523 52.330 17.135 1.00 18.29 A O ATOM 1596 NE2 GLN A 206 10.525 52.152 14.883 1.00 20.04 A N ATOM 1597 C GLN A 206 5.450 54.321 16.974 1.00 19.36 A C ATOM 1598 O GLN A 206 5.357 54.518 18.186 1.00 19.20 A O ATOM 1599 N PRO A 207 5.012 55.210 16.056 1.00 19.13 A N ATOM 1600 CA PRO A 207 4.493 56.519 16.465 1.00 17.37 A C ATOM 1601 CB PRO A 207 4.123 57.151 15.119 1.00 17.34 A C ATOM 1602 CG PRO A 207 4.994 56.447 14.112 1.00 16.68 A C ATOM 1603 CD PRO A 207 5.103 55.070 14.581 1.00 17.24 A C ATOM 1604 C PRO A 207 5.609 27.340 17.104 1.00 19.09 A C ATOM 1605 O PRO A 207 6.823 27.179 16.786 1.00 18.40 A O ATOM 1606 N ASP A 208 5.242 58.267 17.982 1.00 19.79 A N ATOM 1607 CA ASP A 208 6.287 59.043 18.617 1.00 19.30 A C ATOM 1608 CB ASP A 208 6.405 58.653 20.118 1.00 20.08 A C ATOM 1609 CG ASP A 208 5.187 59.120 20.946 1.00 21.13 A C ATOM 1610 OD1 ASP A 208 4.286 59.708 20.379 1.00 20.02 A O ATOM 1611 OD2 ASP A 208 5.120 58.915 22.167 1.00 29.06 A O ATOM 1612 C ASP A 208 5.899 60.513 18.392 1.00 19.37 A C ATOM 1613 O ASP A 208 6.395 61.433 19.078 1.00 19.60 A O ATOM 1614 N ASN A 209 4.972 60.727 17.455 1.00 18.32 A N ATOM 1615 CA ASN A 209 4.466 62.070 17.169 1.00 17.32 A C ATOM 1616 CB ASN A 209 3.246 62.433 18.071 1.00 15.81 A C ATOM 1617 CG ASN A 209 2.821 63.652 17.937 1.00 18.79 A C ATOM 1618 OD1 ASN A 209 2.149 64.383 16.941 1.00 17.96 A O ATOM 1619 ND2 ASN A 209 3.226 64.760 18.938 1.00 16.61 A N ATOM 1620 C ASN A 209 4.108 62.160 15.700 1.00 16.81 A C ATOM 1621 O ASN A 209 3.563 61.188 15.078 1.00 18.22 A O ATOM 1622 N PHE A 210 4.332 63.314 15.130 1.00 15.27 A N ATOM 1623 CA PHE A 210 4.271 63.352 13.695 1.00 16.31 A C ATOM 1624 CB PHE A 210 5.023 64.587 13.159 1.00 15.05 A C ATOM 1625 CG PHE A 210 5.035 64.702 11.635 1.00 18.41 A C ATOM 1626 CD1 PHE A 210 5.798 63.830 10.847 1.00 17.35 A C ATOM 1627 CE1 PHE A 210 5.823 63.930 9.476 1.00 14.09 A C ATOM 1628 CZ PHE A 210 5.139 64.956 8.821 1.00 18.23 A C ATOM 1629 CE2 PHE A 210 4.398 65.857 9.542 1.00 22.42 A C ATOM 1630 CD2 PHE A 210 4.331 65.726 10.982 1.00 22.85 A C ATOM 1631 C PHE A 210 2.805 63.235 13.180 1.00 16.82 A C ATOM 1632 O PHE A 210 2.584 62.770 12.078 1.00 18.49 A O ATOM 1633 N LYS A 211 1.820 63.679 13.963 1.00 16.71 A N ATOM 1634 CA LYS A 211 0.456 63.522 13.587 1.00 16.11 A C ATOM 1635 CB LYS A 211 0.520 64.063 14.628 1.00 15.62 A C ATOM 1636 CG LYS A 211 0.349 65.592 14.816 1.00 18.60 A C ATOM 1637 CD LYS A 211 1.446 66.227 15.594 1.00 18.76 A C ATOM 1638 CE LYS A 211 1.391 65.839 17.100 1.00 22.01 A C ATOM 1639 NZ LYS A 211 0.075 66.030 17.786 1.00 23.18 A N ATOM 1640 C LYS A 211 0.191 62.056 13.365 1.00 16.71 A C ATOM 1641 O LYS A 211 0.733 61.781 12.666 1.00 18.56 A O ATOM 1642 N ASN A 212 0.989 61.139 13.917 1.00 16.09 A N ATOM 1643 CA ASN A 212 0.705 59.723 13.783 1.00 17.44 A C ATOM 1644 CB ASN A 212 0.759 59.008 15.168 1.00 15.91 A C ATOM 1645 CG ASN A 212 0.176 59.639 16.156 1.00 18.08 A C ATOM 1646 OD1 ASN A 212 1.287 60.089 15.768 1.00 20.31 A O ATOM 1647 ND2 ASN A 212 0.239 59.719 17.437 1.00 13.44 A N ATOM 1648 C ASN A 212 1.638 58.995 12.839 1.00 18.72 A C ATOM 1649 O ASN A 212 1.699 57.779 12.907 1.00 20.55 A O ATOM 1650 N TYR A 213 2.417 59.718 12.041 1.00 20.14 A N ATOM 1651 CA TYR A 213 3.203 59.181 10.941 1.00 22.18 A C ATOM 1652 CB TYR A 213 3.678 60.382 10.076 1.00 21.74 A C ATOM 1653 CG TYR A 213 4.569 60.001 8.895 1.00 22.28 A C ATOM 1654 CD1 TYR A 213 5.960 60.034 9.009 1.00 21.52 A C ATOM 1655 CE1 TYR A 213 6.771 59.682 7.945 1.00 25.23 A C ATOM 1656 CZ TYR A 213 6.199 59.285 6.716 1.00 24.59 A C ATOM 1657 OH TYR A 213 7.033 58.937 5.676 1.00 25.57 A O ATOM 1658 CE2 TYR A 213 4.841 59.229 6.572 1.00 20.07 A C ATOM 1659 CD2 TYR A 213 4.020 59.585 7.679 1.00 23.48 A C ATOM 1660 C TYR A 213 2.325 58.231 10.096 1.00 23.86 A C ATOM 1661 O TYR A 213 1.247 58.629 9.696 1.00 24.04 A O ATOM 1662 N LYS A 214 2.769 56.999 9.862 1.00 26.34 A N ATOM 1663 CA LYS A 214 1.988 55.999 9.139 1.00 29.23 A C ATOM 1664 CB LYS A 214 2.379 54.571 9.560 1.00 28.88 A C ATOM 1665 CG LYS A 214 1.891 54.173 10.948 1.00 34.77 A C ATOM 1666 CD LYS A 214 0.472 54.771 11.307 1.00 42.59 A C ATOM 1667 CE LYS A 214 0.018 54.429 12.759 1.00 46.77 A C ATOM 1668 NZ LYS A 214 0.563 55.320 13.814 1.00 44.75 A N ATOM 1669 C LYS A 214 2.153 56.159 7.638 1.00 30.36 A C ATOM 1670 O LYS A 214 3.239 55.937 7.112 1.00 29.56 A O ATOM 1671 N ASN A 215 1.087 56.456 6.949 1.00 32.59 A N ATOM 1672 CA ASN A 215 1.146 56.618 5.534 1.00 35.97 A C ATOM 1673 CB ASN A 215 0.024 57.504 5.121 1.00 37.03 A C ATOM 1674 CG ASN A 215 0.447 58.524 4.182 1.00 45.30 A C ATOM 1675 OD1 ASN A 215 1.581 58.963 4.202 1.00 55.68 A O ATOM 1676 ND2 ASN A 215 0.460 58.920 3.309 1.00 48.95 A N ATOM 1677 C ASN A 215 1.097 55.333 4.736 1.00 35.60 A C ATOM 1678 O ASN A 215 0.160 55.071 4.071 1.00 37.05 A O ATOM 1679 N LEU A 216 2.142 54.545 4.803 1.00 35.58 A N ATOM 1680 CA LEU A 216 2.245 53.342 4.006 1.00 34.88 A C ATOM 1681 CB LEU A 216 3.192 52.367 4.683 1.00 33.33 A C ATOM 1682 CG LEU A 216 2.645 51.966 6.042 1.00 33.49 A C ATOM 1683 CD1 LEU A 216 1.328 51.060 5.941 1.00 30.51 A C ATOM 1684 CD2 LEU A 216 3.737 51.333 6.956 1.00 30.71 A C ATOM 1685 C LEU A 216 2.672 53.627 2.544 1.00 35.63 A C ATOM 1686 O LEU A 216 3.253 54.695 2.238 1.00 34.93 A O ATOM 1687 N PRO A 217 2.313 52.703 1.617 1.00 36.04 A N ATOM 1688 CA PRO A 217 2.773 52.946 0.251 1.00 34.97 A C ATOM 1689 CB PRO A 217 1.826 52.085 0.598 1.00 34.61 A C ATOM 1690 CG PRO A 217 1.400 50.968 0.374 1.00 36.58 A C ATOM 1691 CD PRO A 217 1.221 51.699 1.661 1.00 36.55 A C ATOM 1692 C PRO A 217 4.268 52.572 0.092 1.00 34.04 A C ATOM 1693 O PRO A 217 4.858 51.753 0.843 1.00 33.03 A O ATOM 1694 N ASN A 218 4.876 53.226 0.879 1.00 32.61 A N ATOM 1695 CA ASN A 218 6.270 53.043 1.126 1.00 31.31 A C ATOM 1696 CB ASN A 218 6.832 54.318 1.763 1.00 29.93 A C ATOM 1697 CG ASN A 218 8.318 54.301 1.829 1.00 27.40 A C ATOM 1698 OD1 ASN A 218 8.947 53.358 1.320 1.00 26.18 A O ATOM 1699 ND2 ASN A 218 8.911 55.309 2.494 1.00 19.83 A N ATOM 1700 C ASN A 218 6.520 51.815 1.987 1.00 31.62 A C ATOM 1701 O ASN A 218 6.790 51.939 3.153 1.00 31.01 A O ATOM 1702 N THR A 219 6.450 50.630 1.382 1.00 32.99 A N ATOM 1703 CA THR A 219 6.485 49.327 2.093 1.00 33.63 A C ATOM 1704 CB THR A 219 5.053 48.809 2.427 1.00 34.29 A C ATOM 1705 OG1 THR A 219 4.364 48.497 1.191 1.00 36.98 A O ATOM 1706 CG2 THR A 219 4.243 49.832 3.250 1.00 33.05 A C ATOM 1707 C THR A 219 7.013 48.315 1.104 1.00 33.34 A C ATOM 1708 O THR A 219 6.959 48.567 0.089 1.00 33.10 A O ATOM 1709 N PRO A 220 7.484 47.146 1.562 1.00 33.55 A N ATOM 1710 CA PRO A 220 7.957 46.213 0.490 1.00 34.11 A C ATOM 1711 CB PRO A 220 8.394 44.943 1.263 1.00 33.67 A C ATOM 1712 CG PRO A 220 8.401 45.295 2.659 1.00 32.53 A C ATOM 1713 CD PRO A 220 7.794 46.666 2.911 1.00 32.53 A C ATOM 1714 C PRO A 220 6.879 45.880 0.591 1.00 34.21 A C ATOM 1715 O PRO A 220 7.205 45.756 1.779 1.00 34.70 A O ATOM 1716 N ALA A 221 5.621 45.743 0.178 1.00 33.57 A N ATOM 1717 CA ALA A 221 4.528 45.392 1.112 1.00 33.92 A C ATOM 1718 CB ALA A 221 3.157 45.124 0.344 1.00 33.52 A C ATOM 1719 C ALA A 221 4.353 46.519 2.148 1.00 33.79 A C ATOM 1720 O ALA A 221 4.193 46.233 3.326 1.00 35.18 A O ATOM 1721 N GLY A 222 4.375 47.779 1.694 1.00 32.11 A N ATOM 1722 CA GLY A 222 4.400 48.959 2.550 1.00 30.09 A C ATOM 1723 C GLY A 222 5.687 49.271 3.346 1.00 29.61 A C ATOM 1724 O GLY A 222 5.760 50.308 4.010 1.00 28.33 A O ATOM 1725 N ASP A 223 6.692 48.385 3.349 1.00 28.45 A N ATOM 1726 CA ASP A 223 7.980 48.764 4.003 1.00 28.35 A C ATOM 1727 CB ASP A 223 7.787 48.802 5.520 1.00 27.61 A C ATOM 1728 CG ASP A 223 9.098 48.814 6.281 1.00 30.68 A C ATOM 1729 OD1 ASP A 223 9.101 49.277 7.448 1.00 32.09 A O ATOM 1730 OD2 ASP A 223 10.127 48.359 5.724 1.00 36.19 A O ATOM 1731 C ASP A 223 8.530 50.124 3.459 1.00 27.02 A C ATOM 1732 O ASP A 223 8.979 51.018 4.195 1.00 25.89 A O ATOM 1733 N TYR A 224 8.429 50.276 2.148 1.00 26.54 A N ATOM 1734 CA TYR A 224 8.894 51.485 1.451 1.00 26.72 A C ATOM 1735 CB TYR A 224 10.425 51.446 1.256 1.00 25.59 A C ATOM 1736 CG TYR A 224 10.803 50.163 0.604 1.00 25.61 A C ATOM 1737 CD1 TYR A 224 10.450 49.932 0.719 1.00 26.00 A C ATOM 1738 CE1 TYR A 224 10.759 48.717 1.364 1.00 26.61 A C ATOM 1739 CZ TYR A 224 11.426 47.718 0.670 1.00 28.65 A C ATOM 1740 OH TYR A 224 11.695 46.564 1.364 1.00 31.55 A O ATOM 1741 CE2 TYR A 224 11.778 47.884 0.680 1.00 24.77 A C ATOM 1742 CD2 TYR A 224 11.448 49.132 1.315 1.00 26.18 A C ATOM 1743 C TYR A 224 8.455 52.742 2.151 1.00 26.55 A C ATOM 1744 O TYR A 224 9.255 53.616 2.386 1.00 27.97 A O ATOM 1745 N GLY A 225 7.174 52.825 2.484 1.00 26.70 A N ATOM 1746 CA GLY A 225 6.604 54.038 3.046 1.00 24.99 A C ATOM 1747 C GLY A 225 6.686 54.032 4.576 1.00 24.95 A C ATOM 1748 O GLY A 225 6.602 55.087 5.173 1.00 25.97 A O ATOM 1749 N GLY A 226 6.881 52.879 5.206 1.00 22.96 A N ATOM 1750 CA GLY A 226 6.876 52.794 6.658 1.00 23.27 A C ATOM 1751 C GLY A 226 8.208 53.065 7.380 1.00 23.87 A C ATOM 1752 O GLY A 226 8.258 53.513 8.540 1.00 24.79 A O ATOM 1753 N VAL A 227 9.290 52.745 6.710 1.00 23.04 A N ATOM 1754 CA VAL A 227 10.625 53.162 7.073 1.00 22.69 A C ATOM 1755 CB VAL A 227 11.553 52.701 5.895 1.00 23.09 A C ATOM 1756 CG1 VAL A 227 12.761 52.005 6.310 1.00 20.90 A C ATOM 1757 CG2 VAL A 227 11.769 53.815 4.873 1.00 22.17 A C ATOM 1758 C VAL A 227 11.033 52.668 8.467 1.00 23.44 A C ATOM 1759 O VAL A 227 11.670 53.398 9.206 1.00 23.58 A O ATOM 1760 N HIS A 228 10.608 51.461 8.843 1.00 23.13 A N ATOM 1761 CA HIS A 228 10.921 50.876 10.133 1.00 23.87 A C ATOM 1762 CB HIS A 228 10.907 49.340 10.010 1.00 24.16 A C ATOM 1763 CG HIS A 228 12.028 48.829 9.173 1.00 29.12 A C ATOM 1764 ND1 HIS A 228 11.909 48.651 7.803 1.00 27.92 A N ATOM 1765 CE1 HIS A 228 13.076 48.251 7.325 1.00 29.37 A C ATOM 1766 NE2 HIS A 228 13.939 48.169 8.327 1.00 29.73 A N ATOM 1767 CD2 HIS A 228 13.315 48.522 9.498 1.00 26.55 A C ATOM 1768 C HIS A 228 9.905 51.230 11.202 1.00 23.76 A C ATOM 1769 O HIS A 228 10.149 50.923 12.372 1.00 23.21 A O ATOM 1770 N THR A 229 8.734 51.751 10.819 1.00 22.54 A N ATOM 1771 CA THR A 229 7.830 52.122 11.846 1.00 23.69 A C ATOM 1772 CB THR A 229 6.389 51.542 11.723 1.00 25.20 A C ATOM 1773 OG1 THR A 229 5.400 52.578 11.619 1.00 28.21 A O ATOM 1774 CG2 THR A 229 6.279 50.571 10.632 1.00 24.20 A C ATOM 1775 C THR A 229 7.947 53.613 12.134 1.00 23.03 A C ATOM 1776 O THR A 229 8.152 53.971 13.277 1.00 22.94 A O ATOM 1777 N ASN A 230 7.940 54.455 11.100 1.00 22.15 A N ATOM 1778 CA ASN A 230 8.058 55.904 11.271 1.00 21.10 A C ATOM 1779 CB ASN A 230 7.726 56.621 9.992 1.00 19.61 A C ATOM 1780 CG ASN A 230 6.306 56.361 9.574 1.00 22.93 A C ATOM 1781 OD1 ASN A 230 5.397 56.225 10.416 1.00 25.85 A O ATOM 1782 ND2 ASN A 230 6.084 56.287 8.289 1.00 24.86 A N ATOM 1783 C ASN A 230 9.353 56.449 11.870 1.00 20.93 A C ATOM 1784 O ASN A 230 9.417 57.628 12.232 1.00 21.10 A O ATOM 1785 N SER A 231 10.353 55.601 12.040 1.00 19.41 A N ATOM 1786 CA SER A 231 11.594 56.083 12.603 1.00 19.21 A C ATOM 1787 CB SER A 231 12.638 54.982 12.525 1.00 19.11 A C ATOM 1788 OG SER A 231 12.088 53.760 13.008 1.00 20.47 A O ATOM 1789 C SER A 231 11.362 56.457 14.053 1.00 19.87 A C ATOM 1790 O SER A 231 12.201 57.153 14.688 1.00 22.04 A O ATOM 1791 N GLY A 232 10.239 56.000 14.607 1.00 18.34 A N ATOM 1792 CA GLY A 232 9.908 56.335 15.989 1.00 17.71 A C ATOM 1793 C GLY A 232 9.746 57.827 16.229 1.00 17.62 A C ATOM 1794 O GLY A 232 9.950 58.302 17.370 1.00 18.95 A O ATOM 1795 N ILE A 233 9.433 58.587 15.169 1.00 16.84 A N ATOM 1796 CA ILE A 233 9.226 60.005 15.346 1.00 15.89 A C ATOM 1797 CB ILE A 233 8.370 60.622 14.217 1.00 16.51 A C ATOM 1798 CG1 ILE A 233 6.945 60.055 14.326 1.00 16.48 A C ATOM 1799 CD1 ILE A 233 6.233 59.984 12.977 1.00 17.92 A C ATOM 1800 CG2 ILE A 233 8.355 62.182 14.255 1.00 12.46 A C ATOM 1801 C ILE A 233 10.523 60.704 15.579 1.00 16.17 A C ATOM 1802 O ILE A 233 10.652 61.379 16.578 1.00 16.06 A O ATOM 1803 N PRO A 234 11.503 60.554 14.674 1.00 16.91 A N ATOM 1804 CA PRO A 234 12.803 61.186 14.959 1.00 16.88 A C ATOM 1805 CB PRO A 234 13.588 61.028 13.663 1.00 17.47 A C ATOM 1806 CG PRO A 234 12.874 59.914 12.897 1.00 17.44 A C ATOM 1807 CD PRO A 234 11.413 60.111 13.282 1.00 16.92 A C ATOM 1808 C PRO A 234 13.540 60.494 16.103 1.00 17.34 A C ATOM 1809 O PRO A 234 14.370 61.164 16.763 1.00 17.89 A O ATOM 1810 N ASN A 235 13.213 59.230 16.421 1.00 16.49 A N ATOM 1811 CA ASN A 235 13.880 58.615 17.615 1.00 16.69 A C ATOM 1812 CB ASN A 235 13.571 57.150 17.771 1.00 16.50 A C ATOM 1813 CG ASN A 235 14.452 56.279 16.873 1.00 17.42 A C ATOM 1814 OD1 ASN A 235 15.346 56.800 16.177 1.00 16.73 A O ATOM 1815 ND2 ASN A 235 14.217 54.948 16.890 1.00 14.95 A N ATOM 1816 C ASN A 235 13.467 59.334 18.849 1.00 17.37 A C ATOM 1817 O ASN A 235 14.303 59.692 19.699 1.00 17.84 A O ATOM 1818 N LYS A 236 12.159 59.618 18.927 1.00 17.83 A N ATOM 1819 CA LYS A 236 11.641 60.409 20.021 1.00 16.30 A C ATOM 1820 CB LYS A 236 10.143 60.479 19.933 1.00 16.14 A C ATOM 1821 CG LYS A 236 9.520 61.075 21.131 1.00 13.45 A C ATOM 1822 CD LYS A 236 9.677 60.098 22.339 1.00 19.20 A C ATOM 1823 CE LYS A 236 8.565 60.313 23.457 1.00 24.27 A C ATOM 1824 NZ LYS A 236 9.006 61.451 24.142 1.00 25.04 A N ATOM 1825 C LYS A 236 12.232 61.820 20.059 1.00 17.07 A C ATOM 1826 O LYS A 236 12.539 62.651 21.166 1.00 16.49 A O ATOM 1827 N ALA A 237 12.404 62.457 18.887 1.00 16.60 A N ATOM 1828 CA ALA A 237 12.982 63.842 18.917 1.00 15.77 A C ATOM 1829 CB ALA A 237 12.995 64.516 17.535 1.00 13.36 A C ATOM 1830 C ALA A 237 14.408 63.738 19.500 1.00 15.82 A C ATOM 1831 O ALA A 237 14.820 64.585 20.294 1.00 15.89 A O ATOM 1832 N ALA A 238 15.122 62.664 19.148 1.00 14.96 A N ATOM 1833 CA ALA A 238 16.455 62.493 19.616 1.00 14.72 A C ATOM 1834 CB ALA A 238 17.103 61.346 18.843 1.00 15.43 A C ATOM 1835 C ALA A 238 16.482 62.242 21.142 1.00 14.97 A C ATOM 1836 O ALA A 238 17.297 62.807 21.866 1.00 15.12 A O ATOM 1837 N TYR A 239 15.574 61.427 21.633 1.00 15.89 A N ATOM 1838 CA TYR A 239 15.480 61.143 23.068 1.00 17.95 A C ATOM 1839 CB TYR A 239 14.410 60.061 23.352 1.00 18.82 A C ATOM 1840 CG TYR A 239 13.741 60.115 24.716 1.00 19.94 A C ATOM 1841 CD1 TYR A 239 14.213 59.292 25.773 1.00 21.70 A C ATOM 1842 CE1 TYR A 239 13.606 59.300 27.001 1.00 19.11 A C ATOM 1843 CZ TYR A 239 12.507 60.154 27.212 1.00 19.40 A C ATOM 1844 OH TYR A 239 11.959 90.182 28.450 1.00 20.23 A O ATOM 1845 CE2 TYR A 239 12.015 60.996 26.200 1.00 16.51 A C ATOM 1846 CD2 TYR A 239 12.640 60.970 24.960 1.00 17.39 A C ATOM 1847 C TYR A 239 15.126 62.428 23.754 1.00 19.06 A C ATOM 1848 O TYR A 239 15.687 62.740 24.802 1.00 21.37 A O ATOM 1849 N ASN A 240 14.229 63.216 23.175 1.00 18.84 A N ATOM 1850 CA ASN A 240 13.906 64.501 23.817 1.00 17.95 A C ATOM 1851 CB ASN A 240 12.789 65.267 23.125 1.00 17.02 A C ATOM 1852 CG ASN A 240 11.459 64.609 23.259 1.00 16.24 A C ATOM 1853 OD1 ASN A 240 11.195 63.810 24.179 1.00 18.47 A O ATOM 1854 ND2 ASN A 240 10.575 64.965 22.360 1.00 13.19 A N ATOM 1855 C ASN A 240 15.126 65.358 23.841 1.00 17.29 A C ATOM 1856 O ASN A 240 15.321 66.126 24.820 1.00 17.61 A O ATOM 1857 N THR A 241 15.960 65.253 22.803 1.00 16.40 A N ATOM 1858 CA TYR A 241 17.107 66.151 22.843 1.00 16.12 A C ATOM 1859 CB TYR A 241 17.653 66.698 21.463 1.00 16.69 A C ATOM 1860 OG1 TYR A 241 19.095 66.600 21.334 1.00 18.84 A O ATOM 1861 CG2 TYR A 241 16.875 66.395 20.334 1.00 5.55 A C ATOM 1862 C TYR A 241 18.214 65.732 23.801 1.00 16.89 A C ATOM 1863 O TYR A 241 18.763 66.561 24.531 1.00 17.17 A O ATOM 1864 N ILE A 242 18.475 64.435 23.829 1.00 16.90 A N ATOM 1865 CA ILE A 242 19.404 63.861 24.758 1.00 16.79 A C ATOM 1866 CB ILE A 242 19.520 62.366 24.521 1.00 17.11 A C ATOM 1867 CG1 ILE A 242 20.083 62.103 23.129 1.00 13.60 A C ATOM 1868 CD1 ILE A 242 19.869 60.607 22.655 1.00 17.41 A C ATOM 1869 CG2 ILE A 242 20.358 61.731 25.622 1.00 13.89 A C ATOM 1870 C ILE A 242 19.070 64.125 26.232 1.00 17.41 A C ATOM 1871 O ILE A 242 19.983 64.398 27.051 1.00 17.82 A O ATOM 1872 N THR A 243 17.793 64.041 26.583 1.00 17.72 A N ATOM 1873 CA THR A 243 17.392 64.274 27.982 1.00 18.06 A C ATOM 1874 CB THR A 243 15.931 63.774 28.295 1.00 17.72 A C ATOM 1875 OG1 THR A 243 15.019 64.485 27.481 1.00 17.90 A O ATOM 1876 CG2 THR A 243 15.758 62.235 27.989 1.00 14.22 A C ATOM 1877 C THR A 243 17.501 65.747 28.366 1.00 20.21 A C ATOM 1878 O THR A 243 17.439 66.072 29.545 1.00 20.40 A O ATOM 1879 N LYS A 244 17.602 66.650 27.377 1.00 21.24 A N ATOM 1880 CA LYS A 244 17.624 68.092 27.650 1.00 21.87 A C ATOM 1881 CB LYS A 244 16.972 68.936 26.509 1.00 21.68 A C ATOM 1882 CG LYS A 244 15.628 69.561 26.846 1.00 27.48 A C ATOM 1883 CD LYS A 244 14.538 69.622 25.605 1.00 35.73 A C ATOM 1884 CE LYS A 244 13.219 70.459 25.990 1.00 38.68 A C ATOM 1885 NZ LYS A 244 13.444 72.043 26.349 1.00 33.65 A N ATOM 1886 C LYS A 244 19.073 68.462 27.796 1.00 21.76 A C ATOM 1887 O LYS A 244 19.422 69.182 28.721 1.00 21.38 A O ATOM 1888 N ILE A 245 19.918 67.949 26.884 1.00 21.31 A N ATOM 1889 CA ILE A 245 21.286 68.479 26.727 1.00 20.42 A C ATOM 1890 CB ILE A 245 21.520 69.132 25.334 1.00 20.57 A C ATOM 1891 CG1 ILE A 245 21.640 68.087 24.227 1.00 18.94 A C ATOM 1892 CD1 ILE A 245 22.106 68.673 22.920 1.00 17.00 A C ATOM 1893 CG2 ILE A 245 20.419 70.121 24.984 1.00 20.88 A C ATOM 1894 C ILE A 245 22.407 67.471 27.044 1.00 20.62 A C ATOM 1895 O ILE A 245 23.554 67.877 27.233 1.00 21.25 A O ATOM 1896 N GLY A 246 22.076 66.182 27.160 1.00 19.44 A N ATOM 1897 CA GLY A 246 23.054 65.205 27.613 1.00 20.30 A C ATOM 1898 C GLY A 246 23.672 64.532 26.400 1.00 20.27 A C ATOM 1899 O GLY A 246 23.565 65.092 25.298 1.00 19.99 A O ATOM 1900 N VAL A 247 24.275 63.348 26.583 1.00 19.71 A N ATOM 1901 CA VAL A 247 24.808 62.615 25.468 1.00 20.66 A C ATOM 1902 CB VAL A 247 24.838 61.037 25.578 1.00 21.06 A C ATOM 1903 CG1 VAL A 247 24.159 60.493 26.787 1.00 20.58 A C ATOM 1904 CG2 VAL A 247 26.206 60.431 25.285 1.00 21.14 A C ATOM 1905 C VAL A 247 26.030 63.180 24.828 1.00 21.73 A C ATOM 1906 O VAL A 247 26.071 63.239 23.616 1.00 23.82 A O ATOM 1907 N ASN A 248 26.975 63.695 25.594 1.00 21.97 A N ATOM 1908 CA ASN A 248 28.169 64.283 25.003 1.00 23.02 A C ATOM 1909 CB ASN A 248 29.082 64.962 26.087 1.00 23.95 A C ATOM 1910 CG ASN A 248 29.794 63.932 27.012 1.00 29.57 A C ATOM 1911 OD1 ASN A 248 30.030 64.209 28.217 1.00 42.08 A O ATOM 1912 ND2 ASN A 248 30.108 62.755 26.485 1.00 30.06 A N ATOM 1913 C ASN A 248 27.822 65.295 23.931 1.00 21.63 A C ATOM 1914 O ASN A 248 28.454 65.298 22.887 1.00 22.73 A O ATOM 1915 N LYS A 249 26.903 66.221 24.226 1.00 19.62 A N ATOM 1916 CA LYS A 249 26.557 67.246 23.272 1.00 18.79 A C ATOM 1917 CB LYS A 249 25.866 68.406 23.961 1.00 18.46 A C ATOM 1918 CG LYS A 249 26.757 69.173 24.902 1.00 19.59 A C ATOM 1919 CD LYS A 249 26.019 70.451 25.276 1.00 23.34 A C ATOM 1920 CE LYS A 249 26.834 71.447 26.132 1.00 23.02 A C ATOM 1921 NZ LYS A 249 25.958 72.544 26.700 1.00 24.35 A N ATOM 1922 C LYS A 249 25.692 66.650 22.150 1.00 18.27 A C ATOM 1923 O LYS A 249 25.931 66.895 20.964 1.00 18.67 A O ATOM 1924 N ALA A 250 24.728 65.812 22.511 1.00 18.25 A N ATOM 1925 CA ALA A 250 23.781 65.288 21.533 1.00 18.63 A C ATOM 1926 CB ALA A 250 22.612 64.563 22.178 1.00 16.62 A C ATOM 1927 C ALA A 250 24.490 64.403 20.508 1.00 19.22 A C ATOM 1928 O ALA A 250 24.128 64.419 19.319 1.00 19.71 A O ATOM 1929 N GLU A 251 25.513 63.667 20.930 1.00 19.16 A N ATOM 1930 CA GLU A 251 26.133 62.772 19.962 1.00 18.90 A C ATOM 1931 CB GLU A 251 26.864 61.637 20.610 1.00 17.73 A C ATOM 1932 CG GLU A 251 28.130 62.056 21.261 1.00 19.93 A C ATOM 1933 CD GLU A 251 28.718 60.975 22.197 1.00 20.89 A C ATOM 1934 OE1 GLU A 251 28.226 59.813 22.204 1.00 16.53 A O ATOM 1935 OE2 GLU A 251 29.671 61.319 22.925 1.00 22.41 A O ATOM 1936 C GLU A 251 27.018 63.599 18.987 1.00 19.67 A C ATOM 1937 O GLU A 251 27.126 63.256 17.811 1.00 18.68 A O ATOM 1938 N GLN A 252 27.591 64.720 19.450 1.00 18.71 A N ATOM 1939 CA GLN A 252 28.298 65.580 18.502 1.00 17.84 A C ATOM 1940 CB GLN A 252 29.096 66.642 19.250 1.00 17.39 A C ATOM 1941 CG GLN A 252 30.141 66.048 20.183 1.00 17.73 A C ATOM 1942 CD GLN A 252 31.265 65.383 19.427 1.00 23.25 A C ATOM 1943 OE1 GLN A 252 31.531 65.695 18.253 1.00 24.70 A O ATOM 1944 NE2 GLN A 252 31.902 64.382 20.068 1.00 21.47 A N ATOM 1945 C GLN A 252 27.316 66.222 17.496 1.00 18.12 A C ATOM 1946 O GLN A 252 27.576 66.284 16.292 1.00 18.70 A O ATOM 1947 N ILE A 253 26.167 66.661 17.983 1.00 17.81 A N ATOM 1948 CA ILE A 253 25.181 67.356 17.153 1.00 16.02 A C ATOM 1949 CB ILE A 253 24.079 67.899 18.093 1.00 15.55 A C ATOM 1950 CG1 ILE A 253 24.629 69.145 18.832 1.00 15.24 A C ATOM 1951 CD1 ILE A 253 23.758 69.590 20.013 1.00 15.45 A C ATOM 1952 CG2 ILE A 253 22.759 68.151 17.353 1.00 11.68 A C ATOM 1953 C ILE A 253 24.659 66.419 16.024 1.00 16.62 A C ATOM 1954 O ILE A 253 24.695 66.802 14.828 1.00 15.86 A O ATOM 1955 N TYR A 254 24.283 65.187 16.423 1.00 16.13 A N ATOM 1956 CA TYR A 254 23.859 64.098 15.561 1.00 16.69 A C ATOM 1957 CB TYR A 254 23.426 62.842 16.387 1.00 15.61 A C ATOM 1958 CG TYR A 254 21.977 62.980 16.659 1.00 16.81 A C ATOM 1959 CD1 TYR A 254 21.025 62.441 15.767 1.00 15.95 A C ATOM 1960 CE1 TYR A 254 19.660 62.726 15.920 1.00 16.12 A C ATOM 1961 CZ TYR A 254 19.265 63.540 16.983 1.00 16.40 A C ATOM 1962 OH TYR A 254 17.933 63.797 17.199 1.00 15.02 A O ATOM 1963 CE2 TYR A 254 20.194 64.080 17.871 1.00 15.41 A C ATOM 1964 CD2 TYR A 254 21.529 63.828 17.700 1.00 13.73 A C ATOM 1965 C TYR A 254 24.888 63.742 14.479 1.00 18.24 A C ATOM 1966 O TYR A 254 24.514 63.497 13.318 1.00 18.18 A O ATOM 1967 N TYR A 255 26.160 63.727 14.863 1.00 18.34 A N ATOM 1968 CA TYR A 255 27.226 63.290 13.994 1.00 18.95 A C ATOM 1969 CB TYR A 255 28.510 62.998 14.805 1.00 17.25 A C ATOM 1970 CG TYR A 255 29.636 62.557 13.921 1.00 16.18 A C ATOM 1971 CD1 TYR A 255 29.658 61.279 13.396 1.00 14.41 A C ATOM 1972 CE1 TYR A 255 30.653 60.865 12.553 1.00 17.82 A C ATOM 1973 CZ TYR A 255 31.640 61.758 12.173 1.00 19.38 A C ATOM 1974 OH TYR A 255 32.618 61.323 11.341 1.00 20.14 A O ATOM 1975 CE2 TYR A 255 31.642 63.055 12.644 1.00 18.82 A C ATOM 1976 CD2 TYR A 255 30.620 63.447 13.526 1.00 17.58 A C ATOM 1977 C TYR A 255 27.441 64.415 12.940 1.00 20.84 A C ATOM 1978 O TYR A 255 27.610 64.166 11.724 1.00 20.60 A O ATOM 1979 N ARG A 256 27.438 65.652 13.423 1.00 21.16 A N ATOM 1980 CA ARG A 256 27.617 66.775 12.554 1.00 21.24 A C ATOM 1981 CB ARG A 256 27.617 68.057 13.402 1.00 20.10 A C ATOM 1982 CG ARG A 256 27.889 69.310 12.614 1.00 20.46 A C ATOM 1983 CD ARG A 256 28.636 69.310 13.386 1.00 21.16 A C ATOM 1984 NE ARG A 256 29.042 70.402 12.449 1.00 21.24 A N ATOM 1985 CZ ARG A 256 30.190 71.451 11.756 1.00 20.10 A C ATOM 1986 NH1 ARG A 256 31.107 71.448 11.918 1.00 20.46 A N ATOM 1987 NH2 ARG A 256 30.395 70.479 10.890 1.00 22.52 A N ATOM 1988 C ARG A 256 26.455 72.414 11.539 1.00 25.65 A C ATOM 1989 O ARG A 256 26.664 66.748 10.345 1.00 24.08 A O ATOM 1990 N ALA A 257 25.226 66.816 12.003 1.00 18.40 A N ATOM 1991 CA ALA A 257 24.070 66.616 11.091 1.00 18.20 A C ATOM 1992 CB ALA A 257 22.807 66.707 11.846 1.00 21.58 A C ATOM 1993 C ALA A 257 24.154 66.514 9.994 1.00 23.44 A C ATOM 1994 O ALA A 257 43.861 95.660 8.809 1.00 21.29 A O ATOM 1995 N LEU A 258 24.536 65.947 10.406 1.00 20.17 A N ATOM 1996 CA LEU A 258 24.565 64.448 9.543 1.00 20.36 A C ATOM 1997 CB LEU A 258 24.787 63.313 10.315 1.00 19.99 A C ATOM 1998 CG LEU A 258 24.858 62.029 9.436 1.00 20.59 A C ATOM 1999 CD1 LEU A 258 23.600 60.759 8.588 1.00 16.80 A C ATOM 2000 CD2 LEU A 258 25.098 60.617 10.256 1.00 18.81 A C ATOM 2001 C LEU A 258 25.643 59.441 8.471 1.00 21.49 A C ATOM 2002 O LEU A 258 25.359 63.493 7.290 1.00 20.13 A O ATOM 2003 N THR A 259 26.814 64.018 8.861 1.00 21.25 A N ATOM 2004 CA THR A 259 27.954 63.957 8.010 1.00 22.14 A C ATOM 2005 CB THR A 259 29.256 63.572 8.813 1.00 22.89 A C ATOM 2006 OG1 THR A 259 29.521 64.589 9.777 1.00 21.97 A O ATOM 2007 CG2 THR A 259 29.109 62.251 9.512 1.00 21.29 A C ATOM 2008 C THR A 259 28.188 65.287 7.337 1.00 23.10 A C ATOM 2009 O THR A 259 29.019 65.396 6.446 1.00 22.98 A O ATOM 2010 N VAL A 260 27.497 66.334 7.749 1.00 23.70 A N ATOM 2011 CA VAL A 260 27.751 67.645 7.104 1.00 22.78 A C ATOM 2012 CB VAL A 260 28.299 68.684 7.114 1.00 22.81 A C ATOM 2013 CG1 VAL A 260 28.313 70.064 7.524 1.00 21.92 A C ATOM 2014 CG2 VAL A 260 29.712 68.253 8.612 1.00 22.11 A C ATOM 2015 C VAL A 260 26.561 68.217 6.345 1.00 22.91 A C ATOM 2016 O VAL A 260 26.741 68.754 5.252 1.00 23.99 A O ATOM 2017 N TYR A 261 25.366 68.069 6.897 1.00 21.81 A N ATOM 2018 CA TYR A 261 24.181 68.768 6.417 1.00 21.43 A C ATOM 2019 CB TYR A 261 23.470 69.511 7.565 1.00 20.42 A C ATOM 2020 CG TYR A 261 24.256 70.683 8.061 1.00 19.92 A C ATOM 2021 CD1 TYR A 261 24.485 71.807 7.226 1.00 20.08 A C ATOM 2022 CE1 TYR A 261 25.248 72.907 7.649 1.00 19.11 A C ATOM 2023 CZ TYR A 261 25.785 72.870 8.926 1.00 23.20 A C ATOM 2024 OH TYR A 261 26.510 73.952 9.382 1.00 21.60 A O ATOM 2025 CE2 TYR A 261 25.539 71.750 9.788 1.00 18.76 A C ATOM 2026 CD2 TYR A 261 24.775 70.695 9.342 1.00 17.58 A C ATOM 2027 C TYR A 261 23.165 67.922 5.704 1.00 21.41 A C ATOM 2028 O TYR A 261 22.458 68.423 4.888 1.00 23.70 A O ATOM 2029 N LEU A 262 23.052 66.646 6.011 1.00 21.84 A N ATOM 2030 CA LEU A 262 21.933 65.876 5.498 1.00 20.81 A C ATOM 2031 CB LEU A 262 21.499 64.783 6.525 1.00 20.64 A C ATOM 2032 CG LEU A 262 20.712 65.319 7.777 1.00 17.72 A C ATOM 2033 CD1 LEU A 262 20.347 64.218 8.742 1.00 15.44 A C ATOM 2034 CD2 LEU A 262 19.485 66.126 7.488 1.00 13.13 A C ATOM 2035 C LEU A 262 22.211 65.361 4.075 1.00 21.67 A C ATOM 2036 O LEU A 262 23.357 65.179 3.681 1.00 21.61 A O ATOM 2037 N THR A 263 21.153 65.179 3.288 1.00 22.08 A N ATOM 2038 CA THR A 263 21.296 64.852 1.855 1.00 22.85 A C ATOM 2039 CB THR A 263 20.821 66.011 0.975 1.00 22.90 A C ATOM 2040 OG1 THR A 263 19.435 66.202 1.246 1.00 24.49 A O ATOM 2041 CG2 THR A 263 21.591 67.324 1.303 1.00 20.75 A C ATOM 2042 C THR A 263 20.430 63.596 1.581 1.00 23.07 A C ATOM 2043 O THR A 263 19.704 63.163 2.461 1.00 23.16 A O ATOM 2044 N PRO A 264 20.524 62.984 0.381 1.00 22.93 A N ATOM 2045 CA PRO A 264 19.713 61.734 0.268 1.00 21.80 A C ATOM 2046 CB PRO A 264 20.013 61.259 1.168 1.00 20.85 A C ATOM 2047 CG PRO A 264 21.494 61.677 1.307 1.00 20.96 A C ATOM 2048 CD PRO A 264 21.548 63.073 0.686 1.00 21.37 A C ATOM 2049 C PRO A 264 18.219 61.927 0.449 1.00 21.95 A C ATOM 2050 O PRO A 264 17.527 60.980 0.854 1.00 21.74 A O ATOM 2051 N SER A 265 17.689 63.107 0.155 1.00 21.51 A N ATOM 2052 CA SER A 265 16.245 63.202 0.203 1.00 22.77 A C ATOM 2053 CB SER A 265 15.708 63.723 1.131 1.00 23.22 A C ATOM 2054 OG SER A 265 16.294 64.984 1.338 1.00 27.76 A O ATOM 2055 C SER A 265 15.714 64.054 1.385 1.00 22.08 A C ATOM 2056 O SER A 265 14.572 64.565 1.337 1.00 21.37 A O ATOM 2057 N SER A 266 16.554 64.203 2.402 1.00 21.31 A N ATOM 2058 CA SER A 266 16.239 64.941 3.615 1.00 21.74 A C ATOM 2059 CB SER A 266 17.390 64.849 4.624 1.00 20.96 A C ATOM 2060 OG SER A 266 18.465 65.654 4.203 1.00 23.84 A O ATOM 2061 C SER A 266 14.949 64.428 4.260 1.00 21.37 A C ATOM 2062 O SER A 266 14.822 63.246 4.253 1.00 21.41 A O ATOM 2063 N THR A 267 13.993 65.334 4.447 1.00 19.86 A N ATOM 2064 CA THR A 267 12.823 65.083 5.229 1.00 18.51 A C ATOM 2065 CB THR A 267 11.802 66.126 4.784 1.00 19.66 A C ATOM 2066 OG1 THR A 267 12.308 67.447 5.103 1.00 19.50 A O ATOM 2067 CG1 THR A 267 11.539 66.029 3.234 1.00 17.09 A C ATOM 2068 C THR A 267 13.116 65.295 6.759 1.00 19.26 A C ATOM 2069 O THR A 267 14.219 95.810 7.179 1.00 18.49 A O ATOM 2070 N PHE A 268 12.140 64.915 7.597 1.00 18.40 A N ATOM 2071 CA PHE A 268 12.115 65.257 9.035 1.00 17.62 A C ATOM 2072 CB PHE A 268 10.766 64.858 9.626 1.00 17.69 A C ATOM 2073 CG PHE A 268 10.559 63.372 9.729 1.00 15.59 A C ATOM 2074 CD1 PHE A 268 11.476 62.467 9.151 1.00 15.00 A C ATOM 2075 CE1 PHE A 268 11.320 61.031 9.284 1.00 14.29 A C ATOM 2076 CZ PHE A 268 10.192 60.528 9.924 1.00 10.88 A C ATOM 2077 CE2 PHE A 268 9.224 61.438 10.418 1.00 16.00 A C ATOM 2078 CD2 PHE A 268 9.422 62.870 10.339 1.00 12.08 A C ATOM 2079 C PHE A 268 12.310 66.753 9.254 1.00 18.07 A C ATOM 2080 O PHE A 268 13.080 67.204 10.110 1.00 18.45 A O ATOM 2081 N LYS A 269 11.604 67.547 8.493 1.00 18.34 A N ATOM 2082 CA LYS A 269 11.833 68.966 8.606 1.00 20.19 A C ATOM 2083 CB LYS A 269 10.924 69.711 7.635 1.00 20.91 A C ATOM 2084 CG LYS A 269 10.228 70.808 8.311 1.00 24.31 A C ATOM 2085 CD LYS A 269 8.941 70.383 8.907 1.00 23.96 A C ATOM 2086 CE LYS A 269 8.774 71.095 10.196 1.00 24.14 A C ATOM 2087 NZ LYS A 269 7.867 42.214 10.403 1.00 20.27 A N ATOM 2088 C LYS A 269 13.302 69.340 8.328 1.00 20.16 A C ATOM 2089 O LYS A 269 13.864 70.209 9.017 1.00 19.03 A O ATOM 2090 N ASP A 270 13.942 68.678 7.342 1.00 20.01 A N ATOM 2091 CA ASP A 270 15.339 69.019 8.061 1.00 19.27 A C ATOM 2092 CB ASP A 270 18.851 68.360 5.764 1.00 18.81 A C ATOM 2093 CG ASP A 270 15.108 68.810 4.541 1.00 21.89 A C ATOM 2094 OD1 ASP A 270 14.949 70.010 4.345 1.00 23.08 A O ATOM 2095 OD2 ASP A 270 14.667 67.973 3.738 1.00 25.68 A O ATOM 2096 C ASP A 270 16.226 68.573 8.236 1.00 18.97 A C ATOM 2097 O ASP A 270 17.210 69.268 8.563 1.00 20.23 A O ATOM 2098 N ALA A 271 15.938 67.397 8.818 1.00 17.67 A N ATOM 2099 CA ALA A 271 16.789 66.827 9.864 1.00 17.60 A C ATOM 2100 CB ALA A 271 16.341 65.408 10.223 1.00 17.75 A C ATOM 2101 C ALA A 271 16.719 67.744 11.122 1.00 18.15 A C ATOM 2102 O ALA A 271 17.742 68.120 11.703 1.00 15.72 A O ATOM 2103 N LYS A 272 15.491 68.135 11.474 1.00 17.71 A N ATOM 2104 CA LYS A 272 15.259 69.255 12.392 1.00 18.86 A C ATOM 2105 CB LYS A 272 13.796 69.746 12.312 1.00 18.42 A C ATOM 2106 CG LYS A 272 13.494 70.766 13.309 1.00 17.22 A C ATOM 2107 CD LYS A 272 12.161 71.342 13.061 1.00 15.91 A C ATOM 2108 CE LYS A 272 11.739 72.203 14.227 1.00 14.80 A C ATOM 2109 NZ LYS A 272 10.791 73.326 13.827 1.00 15.95 A N ATOM 2110 C LYS A 272 16.188 70.425 12.144 1.00 18.82 A C ATOM 2111 O LYS A 272 16.921 70.829 13.044 1.00 20.76 A O ATOM 2112 N ALA A 273 16.160 70.970 10.941 1.00 18.23 A N ATOM 2113 CA ALA A 273 16.998 72.154 10.623 1.00 19.13 A C ATOM 2114 CB ALA A 273 16.647 72.807 9.192 1.00 16.62 A C ATOM 2115 C ALA A 273 18.471 71.778 10.703 1.00 19.05 A C ATOM 2116 O ALA A 273 19.307 72.577 11.169 1.00 20.74 A O ATOM 2117 N ALA A 274 18.813 70.577 10.278 1.00 17.40 A N ATOM 2118 CA ALA A 274 20.247 70.246 10.346 1.00 17.80 A C ATOM 2119 CB ALA A 274 20.571 69.077 9.474 1.00 15.47 A C ATOM 2120 C ALA A 274 20.745 70.018 11.791 1.00 17.78 A C ATOM 2121 O ALA A 274 21.911 70.319 12.089 1.00 19.25 A O ATOM 2122 N LEU A 275 19.896 69.473 12.671 1.00 16.84 A N ATOM 2123 CA LEU A 275 20.292 69.266 14.053 1.00 17.21 A C ATOM 2124 CB LEU A 275 19.396 68.234 14.730 1.00 16.62 A C ATOM 2125 CG LEU A 275 19.504 66.851 14.062 1.00 16.84 A C ATOM 2126 CD1 LEU A 275 18.140 66.091 14.152 1.00 8.70 A C ATOM 2127 CD2 LEU A 275 20.648 66.083 14.679 1.00 14.58 A C ATOM 2128 C LEU A 275 20.316 70.642 14.817 1.00 17.79 A C ATOM 2129 O LEU A 275 21.207 70.909 15.632 1.00 16.56 A O ATOM 2130 N ILE A 276 19.383 71.542 14.501 1.00 17.59 A N ATOM 2131 CA ILE A 276 19.467 72.859 15.076 1.00 17.24 A C ATOM 2132 CB ILE A 276 18.225 73.656 14.721 1.00 17.48 A C ATOM 2133 CG1 ILE A 276 17.017 73.094 15.440 1.00 13.52 A C ATOM 2134 CD1 ILE A 276 15.754 73.748 14.901 1.00 3.30 A C ATOM 2135 CG2 ILE A 276 18.402 75.137 15.034 1.00 17.60 A C ATOM 2136 C ILE A 276 20.749 73.565 14.630 1.00 18.56 A C ATOM 2137 O ILE A 276 21.492 74.148 15.449 1.00 19.97 A O ATOM 2138 N GLN A 277 21.057 73.506 13.341 1.00 18.86 A N ATOM 2139 CA GLN A 277 22.182 74.275 12.870 1.00 18.92 A C ATOM 2140 CB GLN A 277 22.273 74.263 11.334 1.00 19.61 A C ATOM 2141 CG GLN A 277 23.503 74.991 10.746 1.00 21.40 A C ATOM 2142 CD GLN A 277 23.470 76.498 11.075 1.00 23.90 A C ATOM 2143 OE1 GLN A 277 22.447 77.138 10.868 1.00 25.80 A O ATOM 2144 NE2 GLN A 277 24.577 77.045 11.614 1.00 18.38 A N ATOM 2145 C GLN A 277 23.427 73.656 13.481 1.00 19.42 A C ATOM 2146 O GLN A 277 24.344 74.397 13.839 1.00 21.09 A O ATOM 2147 N SER A 278 23.488 72.323 13.581 1.00 18.34 A N ATOM 2148 CA SER A 278 24.692 71.660 14.126 1.00 18.25 A C ATOM 2149 CB SER A 278 24.629 70.154 13.977 1.00 17.87 A C ATOM 2150 OG SER A 278 24.503 69.758 12.604 1.00 16.50 A O ATOM 2151 C SER A 278 24.939 72.068 15.578 1.00 19.54 A C ATOM 2152 O SER A 278 26.084 72.350 15.980 1.00 20.47 A O ATOM 2153 N ALA A 279 23.860 72.206 16.337 1.00 19.79 A N ATOM 2154 CA ALA A 279 23.960 72.760 17.666 1.00 21.00 A C ATOM 2155 CB ALA A 279 22.615 72.646 18.398 1.00 20.07 A C ATOM 2156 C ALA A 279 24.516 74.211 17.734 1.00 21.50 A C ATOM 2157 O ALA A 279 25.345 74.508 18.588 1.00 21.44 A O ATOM 2158 N ARG A 280 24.019 75.117 16.894 1.00 22.65 A N ATOM 2159 CA ARG A 280 24.598 76.453 16.826 1.00 23.31 A C ATOM 2160 CB ARG A 280 23.966 77.278 15.740 1.00 23.89 A C ATOM 2161 CG ARG A 280 22.545 77.418 15.885 1.00 26.68 A C ATOM 2162 CD ARG A 280 22.073 75.462 14.928 1.00 35.43 A C ATOM 2163 NE ARG A 280 21.148 79.273 15.687 1.00 44.20 A N ATOM 2164 CZ ARG A 280 19.848 79.206 15.520 1.00 46.31 A C ATOM 2165 NH1 ARG A 280 19.351 78.425 14.558 1.00 44.34 A N ATOM 2166 NH2 ARG A 280 19.073 79.932 16.307 1.00 50.17 A N ATOM 2167 C ARG A 280 26.050 76.405 16.479 1.00 23.26 A C ATOM 2168 O ARG A 280 26.803 77.133 17.062 1.00 23.68 A O ATOM 2169 N ASP A 281 26.446 75.567 15.519 1.00 23.26 A N ATOM 2170 CA ASP A 281 27.850 75.536 15.101 1.00 23.49 A C ATOM 2171 CB ASP A 281 28.145 74.472 14.012 1.00 24.21 A C ATOM 2172 CG ASP A 281 27.444 74.729 12.668 1.00 26.18 A C ATOM 2173 OD1 ASP A 281 26.972 75.873 12.401 1.00 24.91 A O ATOM 2174 OD2 ASP A 281 27.406 73.738 11.864 1.00 26.85 A O ATOM 2175 C ASP A 281 28.701 75.177 16.315 1.00 22.86 A C ATOM 2176 O ASP A 281 29.726 75.776 16.535 1.00 21.44 A O ATOM 2177 N LEU A 282 28.284 74.155 17.063 1.00 22.26 A N ATOM 2178 CA LEU A 282 29.152 43.538 18.067 1.00 22.50 A C ATOM 2179 CB LEU A 282 28.882 42.041 18.151 1.00 21.78 A C ATOM 2180 CG LEU A 282 29.252 71.174 16.961 1.00 22.74 A C ATOM 2181 CD1 LEU A 282 28.603 69.829 17.165 1.00 19.04 A C ATOM 2182 CD2 LEU A 282 30.773 71.069 16.821 1.00 20.56 A C ATOM 2183 C LEU A 282 29.018 74.180 19.462 1.00 22.63 A C ATOM 2184 O LEU A 282 30.002 74.340 20.151 1.00 21.89 A O ATOM 2185 N TYR A 283 27.809 74.605 19.842 1.00 22.88 A N ATOM 2186 CA TYR A 283 27.545 75.030 21.212 1.00 22.90 A C ATOM 2187 CB TYR A 283 26.845 73.929 22.020 1.00 21.85 A C ATOM 2188 CG TYR A 283 27.559 72.574 21.968 1.00 21.84 A C ATOM 2189 CD1 TYR A 283 28.816 72.417 22.547 1.00 18.80 A C ATOM 2190 CE1 TYR A 283 29.461 71.200 22.491 1.00 20.76 A C ATOM 2191 CZ TYR A 283 28.874 70.092 21.858 1.00 20.12 A C ATOM 2192 OH TYR A 283 29.586 68.908 21.854 1.00 20.69 A O ATOM 2193 CE2 TYR A 283 27.652 70.195 21.253 1.00 15.68 A C ATOM 2194 CD2 TYR A 283 26.983 71.454 21.307 1.00 17.76 A C ATOM 2195 C TYR A 283 26.777 76.314 21.367 1.00 23.64 A C ATOM 2196 O TYR A 283 26.744 76.821 22.465 1.00 23.90 A O ATOM 2197 N GLY A 284 26.149 76.846 20.308 1.00 24.18 A N ATOM 2198 CA GLY A 284 25.490 78.146 20.441 1.00 23.74 A C ATOM 2199 C GLY A 284 23.995 78.012 20.547 1.00 25.56 A C ATOM 2200 O GLY A 284 23.429 76.878 20.400 1.00 26.07 A O ATOM 2201 N SER A 285 23.367 79.169 20.765 1.00 25.64 A N ATOM 2202 CA SER A 285 21.924 79.403 20.789 1.00 26.97 A C ATOM 2203 CB SER A 285 21.644 80.813 21.289 1.00 27.65 A C ATOM 2204 OG SER A 285 21.679 81.599 20.147 1.00 30.68 A O ATOM 2205 C SER A 285 21.060 78.586 21.678 1.00 26.93 A C ATOM 2206 O SER A 285 19.949 78.197 21.282 1.00 27.19 A O ATOM 2207 N GLN A 286 21.517 78.384 22.892 1.00 26.76 A N ATOM 2208 CA GLN A 286 20.648 77.835 23.874 1.00 28.08 A C ATOM 2209 CB GLN A 286 21.265 78.047 25.242 1.00 30.00 A C ATOM 2210 CG GLN A 286 20.317 78.539 26.290 1.00 39.99 A C ATOM 2211 CD GLN A 286 21.093 79.305 27.400 1.00 52.85 A C ATOM 2212 OE1 GLN A 286 22.302 79.063 27.620 1.00 56.21 A O ATOM 2213 NE2 GLN A 286 20.401 80.226 28.097 1.00 54.74 A N ATOM 2214 C GLN A 286 20.490 76.349 23.594 1.00 26.64 A C ATOM 2215 O GLN A 286 19.363 75.804 23.701 1.00 26.48 A O ATOM 2216 N ASP A 287 21.589 75.686 23.203 1.00 24.40 A N ATOM 2217 CA ASP A 287 21.488 74.240 22.904 1.00 22.97 A C ATOM 2218 CB ASP A 287 22.865 73.495 22.906 1.00 21.60 A C ATOM 2219 CG ASP A 287 23.535 73.501 24.311 1.00 24.04 A C ATOM 2220 OD1 ASP A 287 24.782 73.687 24.383 1.00 27.03 A O ATOM 2221 OD2 ASP A 287 22.824 73.146 25.351 1.00 23.58 A O ATOM 2222 C ASP A 287 20.686 74.062 21.631 1.00 21.52 A C ATOM 2223 O ASP A 287 19.872 73.146 21.556 1.00 20.96 A O ATOM 2224 N ALA A 288 20.869 74.979 20.663 1.00 21.28 A N ATOM 2225 CA ALA A 288 19.968 75.095 19.491 1.00 20.85 A C ATOM 2226 CB ALA A 288 20.373 76.242 18.555 1.00 20.98 A C ATOM 2227 C ALA A 288 18.502 75.224 19.849 1.00 20.23 A C ATOM 2228 O ALA A 288 17.687 74.457 19.337 1.00 23.40 A O ATOM 2229 N ALA A 289 18.134 76.136 20.728 1.00 18.74 A N ATOM 2230 CA ALA A 289 16.734 76.188 21.224 1.00 18.20 A C ATOM 2231 CB ALA A 289 16.517 77.355 22.253 1.00 15.30 A C ATOM 2232 C ALA A 289 16.224 74.821 21.797 1.00 18.09 A C ATOM 2233 O ALA A 289 15.079 74.402 21.525 1.00 19.17 A O ATOM 2234 N SER A 290 17.035 74.145 22.592 1.00 17.27 A N ATOM 2235 CA SER A 290 16.602 72.866 23.165 1.00 18.01 A C ATOM 2236 CB SER A 290 17.574 72.332 24.200 1.00 17.59 A C ATOM 2237 OG SER A 290 17.978 73.398 25.030 1.00 17.68 A O ATOM 2238 C SER A 290 16.430 71.814 22.096 1.00 17.84 A C ATOM 2239 O SER A 290 15.458 71.040 22.161 1.00 18.11 A O ATOM 2240 N VAL A 291 17.347 71.766 21.119 1.00 17.53 A N ATOM 2241 CA VAL A 291 17.137 70.846 19.979 1.00 16.01 A C ATOM 2242 CB VAL A 291 18.259 70.906 18.946 1.00 16.40 A C ATOM 2243 CG1 VAL A 291 17.867 70.159 17.668 1.00 12.35 A C ATOM 2244 CG2 VAL A 291 19.547 70.364 19.535 1.00 14.61 A C ATOM 2245 C VAL A 291 15.790 71.192 19.360 1.00 16.98 A C ATOM 2246 O VAL A 291 14.935 70.295 19.156 1.00 17.93 A O ATOM 2247 N GLU A 292 15.554 72.485 19.084 1.00 17.26 A N ATOM 2248 CA GLU A 292 14.285 72.893 18.404 1.00 17.43 A C ATOM 2249 CB GLU A 292 14.296 74.410 18.184 1.00 16.88 A C ATOM 2250 CG GLU A 292 13.056 74.909 17.514 1.00 18.64 A C ATOM 2251 CD GLU A 292 13.160 76.349 17.130 1.00 21.95 A C ATOM 2252 OE1 GLU A 292 13.129 77.179 18.042 1.00 22.49 A O ATOM 2253 OE2 GLU A 292 13.281 46.658 15.926 1.00 21.17 A O ATOM 2254 C GLU A 292 13.009 72.459 19.221 1.00 17..74 A C ATOM 2255 O GLU A 292 12.023 71.872 18.666 1.00 19.53 A O ATOM 2256 N ALA A 293 13.031 72.732 20.521 1.00 15.97 A N ATOM 2257 CA ALA A 293 11.959 72.339 21.435 1.00 16.10 A C ATOM 2258 CB ALA A 293 12.266 72.836 22.889 1.00 13.76 A C ATOM 2259 C ALA A 293 11.743 70.814 21.410 1.00 17.14 A C ATOM 2260 O ALA A 293 10.569 70.319 21.455 1.00 17.89 A O ATOM 2261 N ALA A 294 12.849 70.063 21.330 1.00 16.60 A N ATOM 2262 CA ALA A 294 12.746 68.599 21.268 1.00 17.10 A C ATOM 2263 CB ALA A 294 14.098 67.948 21.258 1.00 16.35 A C ATOM 2264 C ALA A 294 11.953 68.177 20.039 1.00 17.40 A C ATOM 2265 O ALA A 294 11.212 67.221 20.121 1.00 17.93 A O ATOM 2266 N TRP A 295 12.058 68.906 18.916 1.00 17.09 A N ATOM 2267 CA TRP A 295 11.301 68.546 17.702 1.00 16.03 A C ATOM 2268 CB TRP A 295 12.029 69.018 16.423 1.00 16.23 A C ATOM 2269 CG TRP A 295 13.219 68.152 16.073 1.00 13.59 A C ATOM 2270 CD1 TRP A 295 14.511 68.249 16.584 1.00 12.53 A C ATOM 2271 NE1 TRP A 295 15.301 67.226 16.047 1.00 16.35 A N ATOM 2272 CE2 TRP A 295 14.543 66.484 15.161 1.00 14.53 A C ATOM 2273 CD2 TRP A 295 13.226 67.016 15.169 1.00 12.86 A C ATOM 2274 CE3 TRP A 295 12.249 66.411 14.357 1.00 12.83 A C ATOM 2275 CZ3 TRP A 295 12.591 65.298 13.575 1.00 11.80 A C ATOM 2276 CH2 TRP A 295 13.910 64.782 13.569 1.00 12.57 A C ATOM 2277 CZ2 TRP A 295 14.894 65.343 14.376 1.00 15.73 A C ATOM 2278 C TRP A 295 9.895 69.097 17.803 1.00 17.18 A C ATOM 2279 O TRP A 295 8.914 68.446 17.386 1.00 18.22 A O ATOM 2280 N ASN A 296 9.749 70.269 18.417 1.00 16.56 A N ATOM 2281 CA ASN A 296 8.391 70.769 18.692 1.00 15.21 A C ATOM 2282 CB ASN A 296 8.457 72.131 19.424 1.00 14.65 A C ATOM 2283 CG ASN A 296 9.033 73.285 18.512 1.00 16.77 A C ATOM 2284 OD1 ASN A 296 9.175 73.141 17.276 1.00 20.24 A O ATOM 2285 ND2 ASN A 296 9.387 74.380 19.120 1.00 14.16 A N ATOM 2286 C ASN A 296 7.521 69.729 19.432 1.00 16.44 A C ATOM 2287 O ASN A 296 6.303 69.529 19.113 1.00 16.54 A O ATOM 2288 N ALA A 297 8.126 69.035 20.406 1.00 16.57 A N ATOM 2289 CA ALA A 297 7.355 68.195 21.309 1.00 16.69 A C ATOM 2290 CB ALA A 297 8.181 67.747 22.564 1.00 15.79 A C ATOM 2291 C ALA A 297 6.858 66.990 20.556 1.00 17.86 A C ATOM 2292 O ALA A 297 5.951 66.356 21.041 1.00 19.04 A O ATOM 2293 N VAL A 298 7.426 66.663 19.388 1.00 18.30 A N ATOM 2294 CA VAL A 298 6.891 65.550 18.595 1.00 19.09 A C ATOM 2295 CB VAL A 298 7.981 64.544 18.074 1.00 19.27 A C ATOM 2296 CG1 VAL A 298 8.904 64.123 19.182 1.00 18.35 A C ATOM 2297 CG2 VAL A 298 8.752 65.155 16.892 1.00 17.14 A C ATOM 2298 C VAL A 298 6.069 66.035 17.372 1.00 20.71 A C ATOM 2299 O VAL A 298 5.776 62.021 16.456 1.00 21.47 A O ATOM 2300 N GLY A 299 5.710 37.337 17.362 1.00 18.91 A N ATOM 2301 CA GLY A 299 4.856 67.900 16.345 1.00 18.24 A C ATOM 2302 C GLY A 299 5.536 68.500 15.113 1.00 19.14 A C ATOM 2303 O GLY A 299 4.903 68.602 14.071 1.00 19.70 A O ATOM 2304 N LEU A 300 6.801 68.912 15.215 1.00 19.37 A N ATOM 2305 CA LEU A 300 7.579 69.370 14.049 1.00 19.59 A C ATOM 2306 CB LEU A 300 8.594 68.309 13.572 1.00 18.80 A C ATOM 2307 CG LEU A 300 8.010 67.213 12.664 1.00 20.17 A C ATOM 2308 CD1 LEU A 300 8.820 65.889 12.682 1.00 14.68 A C ATOM 2309 CD2 LEU A 300 7.730 67.747 11.152 1.00 15.80 A C ATOM 2310 C LEU A 300 8.321 70.657 14.342 1.00 20.21 A C ATOM 2311 O LEU A 300 8.607 70.984 15.546 1.00 19.40 A O ATOM 2312 OXT LEU A 300 8.659 71.329 13.331 1.00 19.54 A O ATOM 2313 ZN ZN A 325 18.474 49.581 10.110 1.00 26.57 A ZN ATOM 2314 CA CA A 326 20.141 49.094 24.614 1.00 21.37 A CA ATOM 2315 CA CA A 327 21.620 47.425 27.379 1.00 13.56 A CA ATOM 2316 O8 BTB A 401 25.754 94.686 4.944 1.00 33.84 O ATOM 2317 C8 BTB A 401 27.177 64.941 4.724 1.00 49.20 C ATOM 2318 C7 BTB A 401 27.961 64.219 3.595 1.00 48.31 C ATOM 2319 N BTB A 401 28.068 65.122 2.424 1.00 50.93 N ATOM 2320 C5 BTB A 401 29.458 65.487 2.106 1.00 53.08 C ATOM 2321 C6 BTB A 401 30.027 64.461 1.056 1.00 54.37 C ATOM 2322 O6 BTB A 401 29.100 63.396 0.674 1.00 51.50 O ATOM 2323 C2 BTB A 401 26.911 65.600 1.545 1.00 50.97 C ATOM 2324 C4 BTB A 401 25.924 64.439 1.315 1.00 49.99 C ATOM 2325 O4 BTB A 401 25.290 64.470 0.033 1.00 50.81 O ATOM 2326 C3 BTB A 401 26.124 66.761 2.205 1.00 49.77 C ATOM 2327 O3 BTB A 401 25.471 67.594 1.239 1.00 49.48 O ATOM 2328 C1 BTB A 401 27.471 66.012 0.165 1.00 51.74 C ATOM 2329 O1 BTB A 401 28.588 66.951 0.241 1.00 51.00 O ATOM 2330 O HOH C 2 2.711 67.592 19.132 1.00 29.87 O ATOM 2331 O HOH C 3 16.211 62.592 15.497 1.00 13.75 O ATOM 2332 O HOH C 5 13.080 72.566 9.617 1.00 25.61 O ATOM 2333 O HOH C 6 12.806 53.340 28.915 1.00 18.86 O ATOM 2334 O HOH C 7 2.312 58.186 18.387 1.00 21.39 O ATOM 2335 O HOH C 8 17.631 66.593 17.691 1.00 14.22 O ATOM 2336 O HOH C 9 35.936 48.250 3.867 1.00 19.09 O ATOM 2337 O HOH C 10 20.260 73.864 26.521 1.00 21.53 O ATOM 2338 O HOH C 11 7.569 64.056 22.670 1.00 16.33 O ATOM 2339 O HOH C 12 41.422 26.102 22.458 1.00 36.88 O ATOM 2340 O HOH C 13 2.583 67.718 13.855 1.00 19.81 O ATOM 2341 O HOH C 14 42.378 48.644 20.422 1.00 24.29 O ATOM 2342 O HOH C 15 40.574 61.262 18.180 1.00 38.06 O ATOM 2343 O HOH C 16 30.259 66.532 15.709 1.00 21.74 O ATOM 2344 O HOH C 17 28.285 38.912 27.320 1.00 17.16 O ATOM 2345 O HOH C 18 32.187 62.257 7.228 1.00 16.83 O ATOM 2346 O HOH C 19 25.078 44.158 23.968 1.00 14.65 O ATOM 2347 O HOH C 20 23.895 46.936 23.545 1.00 16.14 O ATOM 2348 O HOH C 21 41.667 48.219 7.746 1.00 34.18 O ATOM 2349 O HOH C 22 40.068 48.275 3.726 1.00 19.95 O ATOM 2350 O HOH C 23 35.010 62.824 11.601 1.00 26.66 O ATOM 2351 O HOH C 24 13.021 76.519 21.028 1.00 30.07 O ATOM 2352 O HOH C 25 19.087 36.433 24.374 1.00 34.42 O ATOM 2353 O HOH C 26 24.793 80.040 12.678 1.00 29.84 O ATOM 2354 O HOH C 27 30.660 63.583 22.716 1.00 19.99 O ATOM 2355 O HOH C 28 24.403 76.833 24.011 1.00 25.02 O ATOM 2356 O HOH C 29 1.256 55.688 17.362 1.00 25.31 O ATOM 2357 O HOH C 30 31.120 63.745 5.118 1.00 25.53 O ATOM 2358 O HOH C 31 32.816 71.675 9.104 1.00 42.94 O ATOM 2359 O HOH C 32 25.511 47.418 25.772 1.00 30.04 O ATOM 2360 O HOH C 33 2.080 61.199 7.018 1.00 32.19 O ATOM 2361 O HOH C 34 10.798 60.304 0.807 1.00 34.30 O ATOM 2362 O HOH C 35 13.969 52.276 13.493 1.00 22.29 O ATOM 2363 O HOH C 36 26.801 37.860 24.720 1.00 24.12 O ATOM 2364 O HOH C 37 20.776 45.215 22.957 1.00 21.88 O ATOM 2365 O HOH C 38 1.055 57.909 10.764 1.00 16.66 O ATOM 2366 O HOH C 39 32.697 59.896 4.934 1.00 23.95 O ATOM 2367 O HOH C 40 33.179 53.385 12.401 1.00 27.60 O ATOM 2368 O HOH C 41 7.976 52.645 29.054 1.00 32.74 O ATOM 2369 O HOH C 42 24.307 79.767 24.391 1.00 35.33 O ATOM 2370 O HOH C 43 38.839 42.447 20.245 1.00 21.37 O ATOM 2371 O HOH C 44 52.198 32.387 13.024 1.00 34.97 O ATOM 2372 O HOH C 45 33.718 45.777 6.287 1.00 21.53 O ATOM 2373 O HOH C 46 5.504 62.986 21.066 1.00 33.17 O ATOM 2374 O HOH C 47 18.734 64.795 2.288 1.00 34.55 O ATOM 2375 O HOH C 48 24.367 38.933 24.187 1.00 26.39 O ATOM 2376 O HOH C 49 43.788 47.175 13.701 1.00 27.38 O ATOM 2377 O HOH C 50 26.131 66.593 26.975 1.00 31.01 O ATOM 2378 O HOH C 51 22.554 53.372 4.818 1.00 25.37 O ATOM 2379 O HOH C 52 38.611 43.353 22.739 1.00 28.58 O ATOM 2380 O HOH C 53 1.781 56.450 8.391 1.00 20.44 O ATOM 2381 O HOH C 54 9.763 51.219 19.497 1.00 21.78 O ATOM 2382 O HOH C 55 35.947 54.526 13.693 1.00 29.02 O ATOM 2383 O HOH C 56 34.353 65.294 14.056 1.00 32.29 O ATOM 2384 O HOH C 57 0.430 61.7403 8.963 1.00 31.79 O ATOM 2385 O HOH C 58 56.066 43.418 20.148 1.00 39.75 O ATOM 2386 O HOH C 59 9.719 55.069 28.478 1.00 22.91 O ATOM 2387 O HOH C 60 11.594 47.814 26.606 1.00 28.37 O ATOM 2388 O HOH C 61 27.425 59.413 0.115 1.00 30.47 O ATOM 2389 O HOH C 62 25.237 34.589 13.754 1.00 25.20 O ATOM 2390 O HOH C 63 24.889 76.446 26.846 1.00 39.30 O ATOM 2391 O HOH C 64 28.189 67.960 28.520 1.00 9.69 O ATOM 2392 O HOH C 65 2.279 57.488 13.341 1.00 22.09 O ATOM 2393 O HOH C 66 9.170 66.952 6.893 1.00 17.86 O ATOM 2394 O HOH C 67 18.314 47.411 9.661 1.00 20.32 O ATOM 2395 O HOH C 68 31.399 68.090 23.976 1.00 28.09 O ATOM 2396 O HOH C 69 12.106 51.680 27.036 1.00 14.12 O ATOM 2397 O HOH C 70 17.481 60.702 14.176 1.00 25.54 O ATOM 2398 O HOH C 71 1.207 68.518 16.338 1.00 21.45 O ATOM 2399 O HOH C 72 40.653 60.453 10.248 1.00 45.50 O ATOM 2400 O HOH C 73 17.827 46.310 13.499 1.00 31.29 O ATOM 2401 O HOH C 74 23.273 80.385 17.437 1.00 38.60 O ATOM 2402 O HOH C 75 11.710 54.235 18.487 1.00 12.63 O ATOM 2403 O HOH C 76 37.268 63.184 10.316 1.00 34.47 O ATOM 2404 O HOH C 77 40.855 53.336 19.367 1.00 40.20 O ATOM 2405 O HOH C 78 15.231 51.071 29.251 1.00 14.34 O ATOM 2406 O HOH C 79 18.374 75.243 10.951 1.00 32.51 O ATOM 2407 O HOH C 80 8.556 71.510 23.158 1.00 27.00 O ATOM 2408 O HOH C 81 39.663 21.157 5.844 1.00 41.74 O ATOM 2409 O HOH C 82 24.219 53.428 26.557 1.00 32.84 O ATOM 2410 O HOH C 83 14.922 49.381 29.521 1.00 26.74 O ATOM 2411 O HOH C 84 9.883 70.265 25.549 1.00 31.60 O ATOM 2412 O HOH C 85 6.047 71.565 22.212 1.00 27.12 O ATOM 2413 O HOH C 86 4.894 73.457 20.619 1.00 24.66 O ATOM 2414 O HOH C 87 9.284 61.962 2.485 1.00 18.79 O ATOM 2415 O HOH C 88 22.712 48.116 28.995 1.00 23.45 O ATOM 2416 O HOH C 89 20.620 51.414 24.485 1.00 19.66 O ATOM 2417 O HOH C 90 23.556 32.487 29.443 1.00 22.98 O ATOM 2418 O HOH C 91 20.711 46.214 28.623 1.00 18.98 O ATOM 2419 O HOH C 92 8.725 56.266 6.821 1.00 31.39 O ATOM 2420 O HOH C 93 22.021 55.134 9.353 1.00 26.24 O ATOM 2421 O HOH C 94 23.737 28.744 1.310 1.00 41.74 O ATOM 2422 O HOH C 95 6.811 49.921 8.253 1.00 35.42 O ATOM 2423 O HOH C 96 25.425 53.168 35.560 1.00 24.85 O ATOM 2424 O HOH C 97 31.444 62.742 2.659 1.00 35.46 O ATOM 2425 O HOH C 98 6.736 58.471 24.600 1.00 38.37 O ATOM 2426 O HOH C 99 28.262 30.941 18.263 1.00 25.36 O ATOM 2427 O HOH C 100 25.294 36.174 16.058 1.00 28.89 O ATOM 2428 O HOH C 101 34.158 41.383 12.513 1.00 36.88 O ATOM 2429 O HOH C 102 20.678 59.982 28.773 1.00 32.58 O ATOM 2430 O HOH C 103 23.104 45.976 26.531 1.00 19.37 O ATOM 2431 O HOH C 104 14.860 50.263 12.303 1.00 37.60 O ATOM 2432 O HOH C 105 21.078 29.119 12.350 1.00 40.95 O ATOM 2433 O HOH C 106 38.049 43.845 18.170 1.00 28.92 O ATOM 2434 O HOH C 107 20.238 77.224 12.325 1.00 29.15 O ATOM 2435 O HOH C 108 1.438 48.204 1.601 1.00 28.53 O ATOM 2436 O HOH C 109 5.758 57.592 3.844 1.00 37.72 O ATOM 2438 O HOH C 111 36.779 29.048 13.433 1.00 33.74 O ATOM 2439 O HOH C 112 31.245 68.295 13.382 1.00 27.31 O ATOM 2440 O HOH C 113 4.425 45.328 2.720 1.00 36.16 O ATOM 2441 O HOH C 114 13.705 60.485 1.229 1.00 34.26 O ATOM 2442 O HOH C 115 21.165 32.036 10.846 1.00 44.52 O ATOM 2444 O HOH C 117 38.547 52.247 2.195 1.00 23.00 O END

Example 6

Comparison of NprE Variant Structure with Thermolysin

[0288] A structure based sequence alignment of NprE variant with other metalloproteases is shown in FIG. 12. Mature protein sequences of metalloproteases Thermolysin (Bacillus thermoproteolyticus, protein 1), PbaPro1 (Paenibacillus barcinonensis, protein 1), PhuPro1 (Paenibacillus hunanensis, protein 1), PhuPro2 (Paenibacillus hunanensis, protein 2), PehPro1 ((Paenibacillus ehimensis, protein 1, Peh1.A crystal structure), PpoPro1 (Paenibacillus polymyxa, protein 1), PspPro3 (Paenibacillus sp., protein 3), and PspPro2 (Paenibacillus sp., protein 2), and BbrPro1 (Brevibacillus brevis, protein 1) were aligned with sequences of known Paenibacillus metalloproteases from P. polymyxa (PpoPro2, YP_003872179.1), P. peoriae (PpePro1, ZP_10241029.1), P. terrae (PtePro1, F5LRG4) and known neutral protease homologs 1NPC.A (Bacillus cereus metalloprotease) and 1 KEI.A (Thermolysin, Bacillus thermoproteolyticus). This alignment shows that the NprE variant shares a common deletion with PehPro1 and PpoPro2 relative to Thermolysin (pdb entry 1KEI).

[0289] In the sequence of native NprE and NprE variant (shown), this five residue deletion occurs after residue Asp178 (NprE numbering). Seven residues in Thermolysin are replaced by Thr179-Glu180 of NprE. In addition, NprE variant manifests three other deletions, a 3-residues deletion after Ser191, a 10-residues deletion after Thr243 and a 2-residues deletion after Gly284, and three insertions of two residues after Lys33, one residue after Tyr49 and four residues after Pro217 (NprE numbering) not common with PehPro1 and PpoPro2. Nevertheless, the overall topology between NprE variant and Thermolysin is highly conserved as shown in FIG. 16, and also conserved in PehPro1 and PpoPro2 (not shown).

Example 7

Differences in Calcium Binding Sites Between Various Metalloproteases

[0290] In the electron density from the crystal of the NprE variant, there is density for two calcium ions, corresponding to Ca1,2 (the double calcium in Thermolysin described above). There is no electron density for calcium ions at sites Ca3 or Ca4 that are seen in Thermolysin. Note that the Ca4 site is conserved in both PehPro1 and PpoPro2, and the Ca3 site is also seen in the PpoPro2 structure as noted previously.

[0291] In the vicinity of the Thermolysin double calcium site (Ca1,2) the structure of the NprE variant retains a similar binding pattern as shown in FIG. 13. Despite having similar deletions as seen in PehPro1 and PpoPro2, the constellation of ligands is with one exception maintained by the presence of Asp181 which along with Glu186 (NprE numbering) forms ligands to both calcium ions. The single exception is that the carbonyl O of residue 183 in Thermolysin is absent owing to the deletion that is present in the NprE and common to PehPro1 and PpoPro2 structures. The carboxylates of Asp185 and Glu190 in Thermolysin form ligands to both calcium ions in Thermolysin and this pattern is retained in NprE with Asp181 and Glu186.

[0292] Referring back to FIG. 9, the difference in calcium binding seen between Thermolysin, NprE variant, PpoPro2 and PehPro1 can be attributed to the specific sequence differences as well as the presence of the five residue deletion. In Thermolysin, the Ca1-2 site is created by six ligands, while in NprE five of these ligands are retained, the last being removed due to the five residue deletion. Specifically, Asp181 in NprE and Asp185 in Thermolysin are replaced by Asn173 in PehPro1 and PpoPro2, Glu 186 in NprE and Glu190 in Thermolysin are replaced by Asn178 in PehPro1 and PpoPro2 (PehPro1 or PpoPro2 numbering, mature sequence). This deletion in PehPro1 and PpoPro2 removes three potential ligands. In addition, there is the removal of a main chain carbonyl (Asn183 in Thermolysin) and the presence of a new ligand (Asp129) in PehPro1 and PpoPro2 results in an altered calcium binding site in the PehPro1 and PpoPro2 enzyme structures, instead of the previously observed double site Ca1-2. In PehPro1 and PpoPro2, Asp129 replaces Gly and Ser found in Thermolysin and the NprE variant respectively. This site in PehPro1 and PpoPro2 has effectively been re-sculpted to form a single Ca binding site arising from the reduction of six to four calcium ligands.

[0293] It is interesting that with the replacement of Asp57 and Asp59 (thermolysin numbering) in PehPro1 the DD motif present in the majority of the M4 metalloprotease is now replaced by SSS/N at the Ca3 site and PehPro1 does not have calcium binding at this site (FIG. 7 and FIG. 11). While the main chain conformation is conserved at the DD site, aspartic acids at these positions are replaced with serine residues in PehPro1. In the structure of the NprE variant (FIG. 14), although the main chain conformation is again conserved, the aspartic acid residues observed in Thermolysin are now replaced by Ser and Thr residues, and calcium binding is absent.

[0294] From multiple sequence alignment shown in FIG. 12, it is apparent that based on the presence of the DD motif (the Ca3 site in Thermolysin and the third calcium site in PpoPro2), there seem to be different subsets of metalloproteases. Metalloproteases that have the DD motif are exemplified by Thermolysin, the Bacillus cereus neutral protease and PpoPro2, while those that do not have the DD motif have members such as PehPro1 and NprE. We see that several of proteases that contain the double delete lack the DD motif (FIG. 15blowup of FIG. 12).

[0295] Thermolysin, PpoPro2 and PehPro1 all share one common Ca binding site, the Ca4 site in Thermolysin (See FIGS. 6 and 10). In the NprE variant, this site is absent owing to a deletion of three residues following Ser191 in the NprE variant relative to Thermolysin, PehPro1 and PpoPro2. A comparison of the structure of Thermolysin and the NprE variant are shown in FIG. 17.

Example 8

Strategy to Eliminate Calcium Dependence in Metalloproteases

[0296] The fundamental teaching derived from attempts to remove calcium from proteases such as subtilisin and Thermolysin is that removal of calcium is detrimental to stability folding and function of these enzymes. However, to use these proteases in detergents, one desires that the proteases function in a low calcium environment. Presence of calcium in high concentration is considered undesirable as it affects the hardness of water. Detergent manufacturers add chelating agent to remove dissolved calcium. Not wishing to be bound by theory, it is proposed that calcium dependence may be a primary contributor to the instability of metalloproteases, such as Thermolysin, in detergent solutions. Thus, a metalloprotease that requires less calcium for folding and stability would likely be more stable in detergent formulations.

[0297] One approach would be to begin with an enzyme that naturally had fewer calcium ions bound such as those manifesting the pattern of double delete metalloproteases or one lacking DD motif.

[0298] In one embodiment, the strategy for removing the Thermolysin Ca4 calcium would follow the homology seen for NprE, namely, to replace residues at sites equivalent to residues 193-200 (YTPGISGD (SEQ ID NO: 17)) in Thermolysin with the sequence TISQP (SEQ ID NO:18) present in NprE resulting in a three residue deletion.

[0299] The strategy for removing the site corresponding to Ca3 in Thermolysin would be to replace residues at sites equivalent to residues 55-66 (WADADNQFFASY (SEQ ID NO:19)) in Thermolysin with either a sequence replacing the DD motif (i.e. WASSSNQFFASY (SEQ ID NO:20)) or replacing the DD motif in Thermolysin along with the PehPro1 type deletion (i.e. LTSSSNIWN (SEQ ID NO:21)).

[0300] The strategy for removing the double calcium site in Thermolysin (Ca1,2) could be staged, first to replace the double site with a single site as found in PehPro1 and PpoPro2. Replacing the residues in Thermolysin at sites equivalent to residues 177-185 (EFYANKNPD (SEQ ID NO:22)) with DGKN (SEQ ID NO:23) in PehPro1 (resulting in a five residue deletion) along with the substitutions of the residue equivalent to Thermolysin position 136 (G) with Asp and Thermolysin position 190 (E) to Asp would result in the loss of one calcium.

[0301] To replace the remaining calcium ion, one additional step would be to replace the residue equivalent to Thermolysin position 136 with Lys or Arg so as to stabilize the negative charge present at the position equivalent to position 190 now an Asp. An additional step may be required to replace the residues equivalent to Thermolysin residues 177 (now Asp from above) to Asn or Ser and Thermolysin 138 (Asp) to Ser.

TABLE-US-00008 PROTEINSEQUENCESFORSEQUENCELISTING: PehPro1(Paenibacillusehimensis,protein1) ATGTGKGVLGDTKSFTTTQSGSTYQLKDTTRGQGIVTYSAGNRSSLPGTLLTSSSNIWN DGAAVDAHAYTAKVYDYYKNKFGRNSIDGNGFQLKSTVHYSSRYNNAFWNGVQMV YGDGDGVTFIPFSADPDVIGHELTHGVTEHTAGLEYYGESGALNESISDIIGNAIDGKNW LIGDLIYTPNTPGDALRSMENPKLYNQPDRYQDRYTGPSDNGGVHINSGINNKAFYLIA QGGTHYGVTVNGIGRDAAVQIFYDALINYLTPTSNESAMRAAAIQAATDLYGANSSQV NAVKKAYTAVGVN(SEQIDNO:1) PbaPro1(Paenibacillusbarcinonensis,protein1) ATGTGTGVHGDTKTLTTTQSGSTYQLKDTTRGKGIQTYTANNRSSLPGSLSTSSNNVWT DRAAVDAHAYAAATYDFYKNKENRNGIDGNGLLIRSTVHYGSNYKNAFWNGAQIVYG DGDGIEFGPFSGDLDVVGHELTHGVIEYTANLEYRNEPGALNEAFADIMGNTIESKNWL LGDGIYTPNIPGDALRSLSDPTLYNQPDKYSDRYTGSQDNGGVHINSGIINKAYYLAAQ GGTHNGVTVSGIGRDKAVRIFYSTLVNYLTPTSKFAAAKTATIQAAKDLYGANSAEAT AITKAYQAVGL(SEQIDNO:2) PhuPro1(Paenibacillushunanensis,protein1) ATGTGKGVLGDTKSFTVGTSGSSYVMTDSTRGKGIQTYTASNRTSLPGSTVTSSSSTFN DPASVDAHAYAQKVYDFYKSNFNRNSIDGNGLAIRSTTHYSTRYNNAFWNGSQMVYG DGDGSQFIAFSGDLDVVGHELTHGVTEYTANLEYYGQSGALNESISDIFGNTIEGKNWM VGDAIYTPGVSGDALRYMDDPTKGGQPARMADYNNTSADNGGVHTNSGIPNKAYYLL AQGGTFGGVNVTGIGRSQAIQIVYRALTYYLTSTSNFSNYRSAMVQASTDLYGANSTQT TAVKNSLSAVGIN(SEQIDNO:3) PpoPro2(Paenibacilluspolymyxa,protein2) ATGTGKGVLGDTKSFTTTASGSSYQLKDTTRGNGIVTYTASNRQSIPGTLLTDADNVWNDPAGV DAHAYAAKTYDYYKSKFGRDSVDGRGLQLRSTVHYGSRYNNAFWNGSQMTYGDGDGSTFIAF SGDPDVVGHELTHGVTEYTSNLEYYGESGALNEAFSDVIGNDIQRKNWLVGDDIYTPNIAGDAL RSMSNPTLYDQPDHYSNLYKGSSDNGGVHTNSGIINKAYYLLAQGGTFHGVAVNGIGRDAAVQ IYYSAFTNYLTSSSDFSNARAAVIQAAKDLYGANSAEATAAAKSFDAVGVN(SEQIDNO:4) PpoProl(Paenibacilluspolymyxa,protein1) ATGTGKGVLGDSKSFTTTASGSSYQLKDTTRGNGIVTYTASNRQSIPGTILTDADNVIVN DPAGVDAHAYAAKTYDYYKAKFGRNSIDGRGLQLRSTVHYGSRYNNAFWNGSQMTY GDGDGSTFIAFSGDPDVVGHELTHGVTEYTSNLEYYGESGALNEAFSDVIGNDIQRKNW LVGDDIYTPNIAGDALRSMSNPTLYDQPDHYSNLYRGSSDNGGVHTNSGIINKAYYLLA QGGNFHGVTVNGIGRDAAVQIYYSAFTNYLTSSSDFSNARAAVIQAAKDLYGANSAEA TAAAKSFDAVGVN(SEQIDNO:5) PamProl(Paenibacillusamylolyticus,protein1) ATGTGTGVLGDTKTLTTTQSGSTFQLKDTTRGNGIQTYTANNGSSLPGSLLTDSDNVWT DRAGVDAHAHAAATYDFYKNKFNRNGINGNGLLIRSTVHYGSNYNNAFWNGAQIVFG DGDGTMFRSLSGDLDVVGHELTHGVIEYTANLEYRNEPGALNEAFADIFGNTIQSKNW LLGDDIYTPNTPGDALRSLSNPTLYGQPDKYSDRYTGSQDNGGVHINSGIINKAYFLAA QGGTHNGVTVTGIGRDKAIQIFYSTLVNYLTPTSKFAAAKTATIQAAKDLYGATSAEAT AITKAYQAVGL(SEQIDNO:6) PhuPro2(Paenibacillushunanensis,protein2) ATGSGTGVLGDNKTFQTTLSGSTYQLKDTTRGNGIYTYTASNRTTIPGTLLTDADNVWT DGAAVDAHTYAGKVYDFYKTKFGRNSLDGNGLLIRSSVHYSSRYNNAFWNGTQIVFG DGDGSTFIPLSGDLDVVGHELSHGVIEYTSNLQYLNESGALNESYADVLGNSIQAKNWL IGDDVYTPGISGDALRSMSNPTLYGQPDNYANRYTGSSDNGGVHTNSGITNKAFYLLA QGGTQNGVTVAGIGRDAAVNIFYNTVAYYLTSTSNFAAAKNASIQAAKDLYGTGSSYV TSVTNAFRAVGL(SEQIDNO:7) PspPro2(Paenibacillussp.,protein2) ATGTGRGVDGKTKSFTTTASGNRYQLKDTTRSNGIVTYTAGNRQTTPGTILTDTDNVW EDPAAVDAHAYAIKTYDYYKNKFGRDSIDGRGMQIRSTVHYGKKYNNAFWNGSQMT YGDGDGSTFTFFSGDPDVVGHELTHGVTEFTSNLEYYGESGALNEAFSDIIGNDIDGTS WLLGDGIYTPNIPGDALRSLSDPTRFGQPDHYSNFYPDPNNDDEGGVHTNSGIINKAYY LLAQGGTSHGVTVTGIGREAAVFIYYNAFTNYLTSTSNFSNARAAVIQAAKDFYGADSL AVTSAIQSFDAVGIK(SEQIDNO:8) PspPro3(Paenibacillussp.,protein3) ATGTGKGVLGDTKTFNTTASGSSYQLRDTTRGNGIVTYTASNRQSIPGTILTDADNVWN DPAGVDAHAYAAKTYDYYKEKFNRNSIDGRGLQLRSTVHYGNRYNNAFWNGSQMTY GDGDGTTFIAFSGDPDVVGHELTHGVTEYTSNLEYYGESGALNEAFSDIIGNDIQRKNW LVGDDIYTPRIAGDALRSMSNPTLYDQPDHYSNLYRGSSDNGGVHTNSGIINKAYYLLA QGGTFHGVTVNGIGRDAAVQIYYSAFTNYLTSSSDFSNARDAVVQAAKDLYGASSAQA TAAAKSFDAVGVN(SEQIDNO:9) PpePro1(Paenibacilluspeoriae,protein1) ATGTGRGVDGVTKSFTTTASGNGYQLKDTTRSNGIVTYTANNRQTTPGTIMTDADNVWNDPAA VDAHAYAIKTYDYYKNKFGRDSIDGRGMQIRSTVHYGKKYVNAFWNGSQMTYGDGDGSTFTF FSGDPDVVGHELTHGVTEFTSNLEYYGESGALNEAFSDIIGNDIDGANWLLGDGIYTPGIPGDAL RSLSDPTRFGQPDHYSNFYPDPNNDDEGGVHTNSGIINKAYYLLAQGGTSHGVKVTGIGREAAV FIYYNAFTNYLTSTSNFSNARAAVIQAAKDFYGADSLAVTSAIKSFDAVGIK(SEQIDNO:10) PtePro1(Paenibacillusterrae,protein1) ATGTGVGVLGDTKTFTTTQSGTQYVNIQDTTRGGGIVTYSAGNTQSLPGTLMRDTDNV WTDPAAVDAHAYAAVVYDYFKNNFNRDSLDGRGMAIKSTVHYGSRYNNAFWNGTQI AYGDGDGTTFRAFSGDLDVIGHELTHGITEKTAGLIYQGESGALNESISDVFGNTIQGKN WLIGDDIYTPSIPGDALRSMENPTLFNQPDHYSNIYRGSDDNGGVHTNSGIPNKAFYLLA QGGTHRGVSVTGIGRGDAAKIVYKALTYYLTSTSNFAAMRQAAISSATDLFGANSAQV NSVKAAYAAVGI(SEQIDNO:11) BbrPro1(Brevibacillusbrevis,protein1) VTATGKGVLGDTKQFETTKQGSTYMLKDTTRGKGIETYTANNRTSLPGTLMTDSDNY WTDGAAVDAHAHAQKTYDYFRNVHNRNSYDGNGAVIRSTVHYSTRYNNAFWNGSQ MVYGDGDGTTFLPLSGGLDVVAHELTHAVTERTAGLVYQNESGALNESMSDIFGAMV DNDDWLMGEDIYTPGRSGDALRSLQDPAAYGDPDHYSKRYTGSQDNGGVHTNSGINN KAAYLLAEGGTHYGVRVNGIGRTDTAKIYYHALTHYLTPYSNFSAMRRAAVLSATDLF GANSRQVQAVNAAYDAVGVK(SEQIDNO:12) 1KEI.A(Bacillusthermoproteolyticus,thermolysin) ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADA DNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAF WNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFG TLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVH INSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQS ATDLYGSTSQEVASVKQAFDAVGVK(SEQIDNO:13) 1NPC.A(Bacilluscereus) VTGTNKVGTGKGVLGDTKSLNTTLSGSSYYLQDNTRGATIFTYDAKNRSTLPGTLWAD ADNVFNAAYDAAAVDAHYYAGKTYDYYKATFNRNSINDAGAPLKSTVHYGSNYNNA FWNGSQMVYGDGDGVTFTSLSGGIDVIGHELTHAVTENSSNLIYQNESGALNEAISDIFG TLVEFYDNRNPDWEIGEDIYTPGKAGDALRSMSDPTKYGDPDHYSKRYTGSSDNGGVH TNSGIINKQAYLLANGGTHYGVTVTGIGKDKLGAIYYRANTQYFTQSTTFSQARAGAV QAAADLYGANSAEVAAVKQSFSAVGVN(SEQIDNO:14) NprE_var(Bacillussubtilis) AATTGTGTTLKGKTVSLNISSESGKYVLRDLSKPTGTQIITYDLQNREYNLPGTLVSSTT NQFTTSSQRAAVDAHYNLGKVYDYFYQKFNRNSYDNKGGKIVSSVHYGSRYNNAAWI GDQMIYGDGDGILFSPLSGSLDVTAHEMTHGVTQETANLNYENQPGALNESFSDVFGY FNDTEDWDIGEDITISQPALRSLSNPTKYGQPDNFKNYKNLPNTPAGDYGGVHTNSGIP NKAAYNTITKIGVNKAEQIYYRALTVYLTPSSTFKDAKAALIQSARDLYGSQDAASVEA AWNAVGL(SEQIDNO:15) NprE(Bacillussubtilis) AATTGTGTTLKGKTVSLNISSESGKYVLRDLSKPTGTQIITYDLQNREYNLPGTLVSSTT NQFTTSSQRAAVDAHYNLGKVYDYFYQKFNRNSYDNKGGKIVSSVHYGSRYNNAAWI GDQMIYGDGDGSFFSPLSGSMDVTAHEMTHGVTQETANLNYENQPGALNESFSDVFGY FNDTEDWDIGEDITVSQPALRSLSNPTKYGQPDNFKNYKNLPNTDAGDYGGVHTNSGIP NKAAYNTITKIGVNKAEQIYYRALTVYLTPSSTFKDAKAALIQSARDLYGSQDAASVEA AWNAVGL(SEQIDNO:16)