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Title:
HEPATITIS C VIRUS HELICASE CRYSTALS, CRYSTALLOGRAPHIC STRUCTURE AND METHODS
Document Type and Number:
WIPO Patent Application WO/2001/088113
Kind Code:
A2
Abstract:
Hepatitis C virus helicase has been crystallized as tetragonal and orthorhombic crystals, and the structure of the crystals has been solved. The structure coordinates of the crystal structures are useful for solving the structures of other molecules or molecular complexes.

Inventors:
FINZEL BARRY C (US)
HARRIS MELISSA S (US)
BALDWIN ERIC (US)
Application Number:
PCT/US2001/014233
Publication Date:
November 22, 2001
Filing Date:
May 02, 2001
Export Citation:
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Assignee:
UPJOHN CO (US)
FINZEL BARRY C (US)
HARRIS MELISSA S (US)
BALDWIN ERIC (US)
International Classes:
C12N9/90; G01N23/20; G01N25/14; G16B15/30; (IPC1-7): C12N9/90; A61K9/00; G06F19/00; G01N23/20; C30B29/50
Domestic Patent References:
WO1999009148A11999-02-25
Other References:
YAO ET AL: "Structure of the hepatitis C virus RNA helicase domain" NATURE STRUCTURAL BIOLOGY, NEW YORK, NY, US, vol. 4, no. 6, 1 June 1997 (1997-06-01), pages 463-467, XP002085175 ISSN: 1072-8368
CHO ET AL: "Crystal structure of RNA helicase from genotype 1b hepatitis C virus" JOURNAL OF BIOLOGICAL CHEMISTRY, AMERICAN SOCIETY OF BIOLOGICAL CHEMISTS, BALTIMORE, MD, US, vol. 273, no. 24, 12 June 1998 (1998-06-12), pages 15045-15052, XP002085177 ISSN: 0021-9258
Attorney, Agent or Firm:
Sandberg, Victoria A. (Raasch & Gebhardt P.A. P.O. Box 581415 Minneapolis, MN, US)
Perry, Robert E. (Gill Jennings & Every Broadgate House 7 Eldon Street London EC2M 7HL, GB)
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Claims:
What is claimed is:
1. A molecule or molecular complex comprising at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicaselike domain 1/domain 2 interface, wherein the domain 1/domain 2 interface comprises amino acids 205209,232238,415420 and 460 467, the domain 1/domain 2 interface being defined by a set of points having a root mean square deviation of less than about 1.5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCVA, UHCVB, or UHHO as listed in Tables 1, 2, or 3 respectively.
2. A molecule or molecular complex comprising at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicaselike oligonucleotide binding site, wherein the oligonucleotide binding site comprises amino acids selected from the group consisting of (1) domain 1 oligonucleotide binding site amino acids 230232,255,269, and 270272, and (2) domain 2 oligonucleotide binding site amino acids 391393,411413,415,416 and 460 ; the oligonucleotide binding site being defined by a set of points having a root mean square deviation of less than about 1.5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCVA, UHCVB, or UHHO as listed in Tables 1,2, or 3 respectively.
3. A Hepatitis C virus helicase molecule or molecular complex comprising at least a first and a second oligonucleotide binding site, wherein the distance between the first and the second oligonucleotide binding sites is less than about 21 angstroms.
4. The Hepatitis C virus helicase molecule or molecular complex of claim 3, wherein the distance between the first and the second oligonucleotide binding sites is about 18.8 to about 19.5 angstroms.
5. A molecule or molecular complex that is structurally homologous to a Hepatitis C virus helicase molecule or molecular complex, wherein the Hepatitis C virus helicase molecule or molecular complex is represented by at least a portion of the structure coordinates listed in Tables 1,2, or 3.
6. A scalable threedimensional configuration of points, at least a portion of said points derived from structure coordinates of at least a portion of a Hepatitis C virus helicase molecule or molecular complex as listed in Tables 1,2, or 3 and comprising at least one of a Hepatitis C virus helicase or Hepatitis C virus helicaselike domain 1/domain 2 interface, domain 1 oligonucleotide binding site, or domain 2 oligonucleotide binding site.
7. The scalable threedimensional configuration of points of claim 6, wherein substantially all of said points are derived from structure coordinates of a Hepatitis C virus helicase molecule or molecular complex as listed in Tables 1,2, or 3.
8. The scalable threedimensional configuration of points of claim 6 wherein at least a portion of the points derived from the Hepatitis C virus helicase structure coordinates are derived from structure coordinates representing the locations of at least the backbone atoms of amino acids selected from the group consisting of (1) domain 1/domain 2 interface amino acids 205209,232238,415420 and 460467, (2) domain 1 oligonucleotide binding site amino acids 230232, 255, 269, and 270272, and (3) domain 2 oligonucleotide binding site amino acids 391393, 411413,415,416 and 460; as represented by structure coordinates of UHCVA, UHCVB, or UHHO in Tables 1,2, and 3 respectively.
9. The scalable threedimensional configuration of points of claim 6 displayed as a holographic image, a stereodiagram, a model or a computerdisplayed image.
10. A scalable threedimensional configuration of points, at least a portion of the points derived from structure coordinates of at least a portion of a molecule or a molecular complex that is structurally homologous to a Hepatitis C virus helicase molecule or molecular complex and comprises at least one of a Hepatitis C virus helicase or Hepatitis C virus helicaselike domain 1/domain 2 interface, domain 1 oligonucleotide binding site, or domain 2 oligonucleotide binding site.
11. The scalable threedimensional configuration of points of claim 10 displayed as a holographic image, a stereodiagram, a model or a computerdisplayed image.
12. A machinereadable data storage medium comprising a data storage material encoded with machine readable data which, when using a machine programmed with instructions for using said data, is capable of displaying a graphical threedimensional representation of at least one molecule or molecular complex selected from the group consisting of : (i) a molecule or molecular complex comprising at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicaselike domain 1/domain 2 interface, wherein the domain 1/domain 2 interface comprises amino acids 205209,232238,415420 and 460 467, the domain 1/domain 2 interface being defined by a set of points having a root mean square deviation of less than about 1.5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCVA, UHCVB, or UHHO as listed in Tables 1, 2, or 3 respectively; (ii) a molecule or molecular complex comprising at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicaselike oligonucleotide binding site, wherein the oligonucleotide binding site comprises amino acids selected from the group consisting of (1) domain 1 oligonucleotide binding site amino acids 230232,255,269, and 270272, and (2) domain 2 oligonucleotide binding site amino acids 391393, 411413,415,416 and 460; the oligonucleotide binding site being defined by a set of points having a root mean square deviation of less than about 1. 5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCVA, UHCVB, or UHHO as listed in Tables 1, 2, or 3 respectively ; (iii) a Hepatitis C virus helicase molecule or molecular complex comprising at least a first and a second oligonucleotide binding site, wherein the distance between the first and the second oligonucleotide binding sites is less than about 21 angstroms; and (iv) a molecule or molecular complex that is structurally homologous to a Hepatitis C virus helicase molecule or molecular complex, wherein the Hepatitis C virus helicase molecule or molecular complex is represented by at least a portion of the structure coordinates listed in Tables 1,2, or 3.
13. A machinereadable data storage medium comprising a data storage material encoded with a first set of machine readable data which, when combined with a second set of machine readable data, using a machine programmed with instructions for using said first set of data and said second set of data, can determine at least a portion of the structure coordinates corresponding to the second set of machine readable data, wherein said first set of data comprises a Fourier transform of at least a portion of the structure coordinates for Hepatitis C virus helicase listed in Tables 1,2, or 3; and said second set of data comprises an xray diffraction pattern of a molecule or molecular complex of unknown structure.
14. A method for obtaining structural information about a molecule or a molecular complex of unknown structure comprising: crystallizing the molecule or molecular complex ; generating an xray diffraction pattern from the crystallized molecule or molecular complex; applying at least a portion of the structure coordinates set forth in Tables 1, 2, or 3 to the xray diffraction pattern to generate a threedimensional electron density map of at least a portion of the molecule or molecular complex whose structure is unknown.
15. A method for homology modeling a Hepatitis C virus helicase homolog comprising: aligning the amino acid sequence of a Hepatitis C virus helicase homolog with an amino acid sequence of Hepatitis C virus helicase (SEQ ID NO: 1) and incorporating the sequence of the Hepatitis C virus helicase homolog into a model of Hepatitis C virus helicase derived from structure coordinates set forth in Tables 1, 2, or 3 to yield a preliminary model of the Hepatitis C virus helicase homolog; subjecting the preliminary model to energy minimization to yield an energy minimized model ; remodeling regions of the energy minimized model where stereochemistry restraints are violated to yield a final model of the Hepatitis C virus helicase homolog.
16. A computerassisted method for identifying an inhibitor of Hepatitis C virus helicase activitycomprising: supplying a computer modeling application with a set of structure coordinates for at least a portion of at least one molecule or molecular complex selected from the group consisting of : (i) a molecule or molecular complex comprising at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicaselike domain 1/domain 2 interface, wherein the domain 1/domain 2 interface comprises amino acids 205209,232238,415420 and 460 467, the domain 1/domain 2 interface being defined by a set of points having a root mean square deviation of less than about 1.5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCVA, UHCVB, or UHHO as listed in Tables 1, 2, or 3 respectively; (ii) a molecule or molecular complex comprising at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicaselike oligonucleotide binding site, wherein the oligonucleotide binding site comprises amino acids selected from the group consisting of (1) domain 1 oligonucleotide binding site amino acids 230232,255,269, and 270272, and (2) domain 2 oligonucleotide binding site amino acids 391393, 411413,415,416 and 460; the oligonucleotide binding site being defined by a set of points having a root mean square deviation of less than about 1.5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCVA, UHCVB, or UHHO as listed in Tables 1, 2, or 3 respectively; (iii) a Hepatitis C virus helicase molecule or molecular complex comprising at least a first and a second oligonucleotide binding site, wherein the distance between the first and the second oligonucleotide binding sites is less than about 21 angstroms ; and (iv) a molecule or molecular complex that is structurally homologous to a Hepatitis C virus helicase molecule or molecular complex, wherein the Hepatitis C virus helicase molecule or molecular complex is represented by at least a portion of the structure coordinates listed in Tables 1,2, or 3; wherein said portion of the molecule comprises at least one HCV binding site selected from the group consisting of an oligonucleotide binding site on domain 1, an oligonucleotide binding site on domain 2, an NTP binding site, and a domain 1/domain 2 interface; supplying the computer modeling application with a set of structure coordinates of a chemical entity; and determining whether the chemical entity is expected to bind to or interfere with the molecule or molecular complex.
17. The method of claim 16 wherein determining whether the chemical entity is expected to bind to or interfere with the molecule or molecular complex comprises performing a fitting operation between the chemical entity and a binding site of the molecule or molecular complex, followed by computationally analyzing the results of the fitting operation to quantify the association between the chemical entity and the binding site.
18. The method of claim 16 further comprising screening a library of chemical entities.
19. A computerassisted method for designing an inhibitor of Hepatitis C virus helicase activity comprising: supplying a computer modeling application with a set of structure coordinates of at least a portion of at least one molecule or molecular complex selected from the group consisting of : (i) a molecule or molecular complex comprising at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicaselike domain 1/domain 2 interface, wherein the domain 1/domain 2 interface comprises amino acids 205209,232238,415420 and 460 467, the domain 1/domain 2 interface being defined by a set of points having a root mean square deviation of less than about 1. 5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCVA, UHCVB, or UHHO as listed in Tables 1, 2, or 3 respectively; (ii) a molecule or molecular complex comprising at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicaselike oligonucleotide binding site, wherein the oligonucleotide binding site comprises amino acids selected from the group consisting of (1) domain 1 oligonucleotide binding site amino acids 230232,255,269, and 270272, and (2) domain 2 oligonucleotide binding site amino acids 391393, 411413,415,416 and 460; the oligonucleotide binding site being defined by a set of points having a root mean square deviation of less than about 1. 5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCVA, UHCVB, or UHHO as listed in Tables 1,2, or 3 respectively; (iii) a Hepatitis C virus helicase molecule or molecular complex comprising at least a first and a second oligonucleotide binding site, wherein the distance between the first and the second oligonucleotide binding sites is less than about 21 angstroms; and (iv) a molecule or molecular complex that is structurally homologous to a Hepatitis C virus helicase molecule or molecular complex, wherein the Hepatitis C virus helicase molecule or molecular complex is represented by at least a portion of the structure coordinates listed in Tables 1,2, or 3; wherein said portion of the molecule comprises at least one HCV binding site selected from the group consisting of an oligonucleotide binding site on domain 1, an oligonucleotide binding site on domain 2, an NTP binding site, and a domain 1/domain 2 interface; supplying the computer modeling application with a set of structure coordinates for a chemical entity; evaluating the potential binding interactions between the chemical entity and substrate binding site of the molecule or molecular complex; structurally modifying the chemical entity to yield a set of structure coordinates for a modified chemical entity; and determining whether the modified chemical entity is an inhibitor expected to bind to or interfere with the molecule or molecular complex, wherein binding to or interfering with the molecule or molecular complex is indicative of potential inhibition of Hepatitis C virus helicase activity.
20. The method of claim 19 wherein determining whether the modified chemical entity is an inhibitor expected to bind to or interfere with the molecule or molecular complex comprises performing a fitting operation between the chemical entity and a binding site of the molecule or molecular complex, followed by computationally analyzing the results of the fitting operation to quantify the association between the chemical entity and the binding site.
21. The method of claim 19 wherein the set of structure coordinates for the chemical entity is obtained from a chemical fragment library.
22. A computerassisted method for designing an inhibitor of Hepatitis C virus helicase activity de novo comprising: supplying a computer modeling application with a set of structure coordinates of at least a portion of at least one molecule or molecular complex selected from the group consistingof : (i) a molecule or molecular complex comprising at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicaselike domain 1/domain 2 interface, wherein the domain 1/domain 2 interface comprises amino acids 205209,232238,415420 and 460 467, the domain 1/domain 2 interface being defined by a set of points having a root mean square deviation of less than about 1. 5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCVA, UHCVB, or UHHO as listed in Tables 1,2, or 3 respectively; (ii) a molecule or molecular complex comprising at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicaselike oligonucleotide binding site, wherein the oligonucleotide binding site comprises amino acids selected from the group consisting of (1) domain 1 oligonucleotide binding site amino acids 230232,255,269, and 270272, and (2) domain 2 oligonucleotide binding site amino acids 391393,411413,415,416 and 460; the oligonucleotide binding site being defined by a set of points having a root mean square deviation of less than about 1. 5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCVA, UHCVB, or UHHO as listed in Tables 1, 2, or 3 respectively; (iii) a Hepatitis C virus helicase molecule or molecular complex comprising at least a first and a second oligonucleotide binding site, wherein the distance between the first and the second oligonucleotide binding sites is less than about 21 angstroms; and (iv) a molecule or molecular complex that is structurally homologous to a Hepatitis C virus helicase molecule or molecular complex, wherein the Hepatitis C virus helicase molecule or molecular complex is represented by at least a portion of the structure coordinates listed in Tables 1, 2, or 3; wherein said portion of the molecule comprises at least one HCV binding site selected from the group consisting of an oligonucleotide binding site on domain 1, an oligonucleotide binding site on domain 2, an NTP binding site, and a domain 1/domain 2 interface; computationally building a chemical entity represented by set of structure coordinates; and determining whether the chemical entity is an inhibitor expected to bind to or interfere with the molecule or molecular complex, wherein binding to or interfering with the molecule or molecular complex is indicative of potential inhibition of Hepatitis C virus helicase activity.
23. The method of claim 22 wherein determining whether the chemical entity is an inhibitor expected to bind to or interfere with the molecule or molecular complex comprises performing a fitting operation between the chemical entity and a binding site of the molecule or molecular complex, followed by computationally analyzing the results of the fitting operation to quantify the association between the chemical entity and the binding site.
24. The method of any of claims 16,19, or 22 further comprising supplying or synthesizing the potential inhibitor, then assaying the potential inhibitor to determine whether it inhibits Hepatitis C virus helicase activity.
25. A method for making an inhibitor of Hepatitis C virus helicase activity, the method comprising chemically or enzymatically synthesizing a chemical entity to yield an inhibitor of Hepatitis C virus helicase activity, the chemical entity having been identified during a computerassisted process comprising supplying a computer modeling application with a set of structure coordinates of a molecule or molecular complex, the molecule or molecular complex comprising at least a portion of at least one of a Hepatitis C virus helicase or Hepatitis C virus helicaselike binding site; supplying the computer modeling application with a set of structure coordinates of a chemical entity; and determining whether the chemical entity is expected to bind to or interfere with the molecule or molecular complex at a binding site, wherein binding to or interfering with the molecule or molecular complex is indicative of potential inhibition of Hepatitis C virus helicase activity.
26. A method for making an inhibitor of Hepatitis C virus helicase activity, the method comprising chemically or enzymatically synthesizing a chemical entity to yield an inhibitor of Hepatitis C virus helicase activity, the chemical entity having been designed during a computerassisted process comprising supplying a computer modeling application with a set of structure coordinates of a molecule or molecular complex, the molecule or molecular complex comprising at least a portion of at least one of a Hepatitis C virus helicase or Hepatitis C virus helicaselike binding site; supplying the computer modeling application with a set of structure coordinates for a chemical entity; evaluating the potential binding interactions between the chemical entity and a binding site of the molecule or molecular complex; structurally modifying the chemical entity to yield a set of structure coordinates for a modified chemical entity; and determining whether the chemical entity is expected to bind to or interfere with the molecule or molecular complex at the binding site, wherein binding to or interfering with the molecule or molecular complex is indicative of potential inhibition of Hepatitis C virus helicase activity.
27. A method for making an inhibitor of Hepatitis C virus helicase activity, the method comprising chemically or enzymatically synthesizing a chemical entity to yield an inhibitor of Hepatitis C virus helicase activity, the chemical entity having been designed during a computerassisted process comprising supplying a computer modeling application with a set of structure coordinates of a molecule or molecular complex, the molecule or molecular complex comprising at least a portion of at least one of a Hepatitis C virus helicase or Hepatitis C virus helicaselike binding site; computationally building a chemical entity represented by set of structure coordinates; and determining whether the chemical entity is expected to bind to or interfere with the molecule or molecular complex at a binding site, wherein binding to or interfering with the molecule or molecular complex is indicative of potential inhibition of Hepatitis C virus helicase activity.
28. An inhibitor of Hepatitis C virus helicase activity identified, designed or made according to the method of any of the claims 16,19,22,25,26, and 27.
29. A composition comprising an inhibitor of Hepatitis C virus helicase activity identified or designed according to the method of any of the claims 16,19,22,25,26, and 27.
30. A pharmaceutical composition comprising an inhibitor of Hepatitis C virus helicase activity identified or designed according to the method of any of the 16,19,22,25,26, and 27 or a salt thereof, and pharmaceutically acceptable carrier.
31. A method for crystallizing a Hepatitis C virus helicase molecule or molecular complex comprising growing a crystal from a precipitant solution comprising purified Hepatitis C virus helicase, about 3% by weight to about 14% by weight PEG, about 5% by weight to about 15% by weight DMSO, and about 0. 05M to about 0.07M potassium phosphate.
32. A method for cocrystallizing a Hepatitis C virus helicase molecule and a ligand to yield a molecular complex, comprising : exchanging purified Hepatitis C virus helicase into a solution comprising HEPES, EDTA, and dithiothreitol; concentrating the Hepatitis C virus helicase to a concentration of about 12 16mg/mL ; combining concentrated Hepatitis C virus helicase with the ligand in a mixture comprising about 4% by weight to about 14% by weight PEG and about 5% by weight to about 15% by weight DMSO; and growing a cocrystal by vapor diffusion.
33. The method of claim 32 wherein combining the concentrated Hepatitis C virus helicase with the ligand in a mixture comprising PEG and DMSO and growing the co crystal are performed in the absence of potassium phosphate.
34. The method of claim 32 wherein the ligand binds to an NTP binding site on the Hepatitis C virus helicase.
35. A method for crystallizing a Hepatitis C virus helicase molecule or molecular complex comprising growing a crystal by vapor diffusion with macroseeding from a precipitant solution comprising purified Hepatitis C virus helicase, HEPES, and about 4% by weight to about 14% by weight monoalkyl ether of PEG.
36. A method for cocrystallizing a Hepatitis C virus helicase molecule and a ligand to yield a molecular complex, comprising growing a crystal by vapor diffusion with macro seeding from a precipitant solution comprising purified HCV helicase, HEPES, about 4% by weight to about 14% by weight monoalkyl ether of PEG, and the ligand, wherein the ligand binds to at least one oligonucleotide binding site on the Hepatitis C virus helicase.
37. The method of claims 3136 wherein the amino acid sequence of the Hepatitis C virus helicase is SEQ ID NO : 1.
38. Crystalline Hepatitis C virus helicase comprising a tetragonal crystal having unit cell dimensions ofa=b= 109 A3A ; c=84A2A ; a=p=y= 90° ; and space group P41 ; the unit cell containing two molecules in an asymmetric unit.
39. The crystalline Hepatitis C virus helicase of claim 38 wherein the amino acid sequence of Hepatitis C virus helicase is SEQ ID NO : 1.
40. Crystalline Hepatitis C virus helicase comprising an orthorhombic crystal characterized by unit cell dimensions ofa=66A2A ; b=110A3A ; c==64A2A ; a = ß = y = 90° ; and a space group P21212 ; the unit cell containing one molecule in the asymmetric unit.
41. The crystalline Hepatitis C virus helicase of claim 40 wherein the amino acid sequence of Hepatitis C virus helicase is SEQ ID NO : 1.
42. Crystalline Hepatitis C virus helicase having an amino acid sequence is SEQ ID NO : 1.
43. A composition comprising crystalline Hepatitis C virus helicase of any of claims 38 42.
44. A method for solving a crystal structure of a crystal of Hepatitis C virus helicase having unit cell dimensions of a = b = l09 A A 3 A ; c = 84 A i 2 A ; α = ß = γ = 90° ; and space group P41, the unit cell containing two molecules in an asymmetric unit, the method comprising: generating an xray diffraction pattern from the crystal, collecting diffraction data, and analyzing the data to generate the structure coordinates for the Hepatitis C virus helicase.
45. A method for solving a crystal structure of a crystal of Hepatitis C virus helicase having unit cell dimensions ofa=66A2A ; b=110A3A ; c=64A2A ; a=p=y = 90° ; and a space group P2, 212, the unit cell containing one molecule in an asymmetric unit, the method comprising: generating an xray diffraction pattern from the crystal, collecting diffraction data, and analyzing the data to generate the structure coordinates for the Hepatitis C virus helicase.
46. The method of claims 44 or 45 wherein the amino acid sequence of the Hepatitis C virus helicase is SEQ ID NO : 1.
47. A method for incorporating a chemical entity in a crystal comprising placing a tetragonal crystal of Hepatitis C virus helicase having unit cell dimensions of a = b =109 Å ~ 3 Å; c = 84 Å ~ 2 Å; α = ß = γ = 90° ; and space group P4, in an aqueous solution comprising about 1mM to about lOmM chemical entity, and 0% by weight to about 15% by weight DMSO.
48. A method for incorporating a chemical entity in a crystal comprising placing an orthorhombic crystal of Hepatitis C virus helicase having unit cell dimensions of a = 66 A <BR> <BR> ; b = 110 Å ~ 3 Å; c = 64 Å ~ 2 Å; α = ß = γ = 90°; and a space group P21212 in an aqueous solution comprising about 1mM to about lOmM chemical entity, and 0% by weight to about 15% by weight DMSO.
Description:
HEPATITIS C VIRUS HELICASE CRYSTALS, CRYSTALLOGRAPHIC STRUCTURE AND METHODS This application claims the benefit of U. S. Provisional Application Serial No.

60/201,598, filed 3 May 2000, which is incorporated herein by reference in its entirety.

FIELD OF THE INVENTION The invention relates to the crystallization and structure determination of Hepatitis C virus helicase.

BACKGROUND OF THE INVENTION The Hepatitis C virus (HCV) genome is translated as a large polyprotein of approximately 3000 amino acids that must be processed proteolytically to generate mature viral proteins, including coat (C) and envelope (E) proteins, and several non-structural (NS) enzymes necessary for viral replication (Figure 1). Nonstructural protein three, NS3, is a bi-functional enzyme possessing both a serine protease activity, and an RNA helicase activity. Separate activities have been isolated on the N-terminal third and C-terminal two-thirds of the NS3 polypeptide. Both serine protease and helicase fragments have shown independent activity when expressed as isolated fragments in vitro, and both activities are required for viral replication, making this protein an attractive target for drug development.

HCV NS3 helicase is an NTP-dependent enzyme that unwinds duplex RNA and RNA: DNA hybrid substrates during viral replication. Several laboratories have reported structures of this enzyme in different crystal forms (Yao et al., Nat. Struct. Biol., 4: 463- 77 (1997); Cho et al., J ; Biol. Chem., 273: 15045-52 (1998)), including one complex with bound single-stranded DNA (Kim et al., Structure, 6: 89-100 (1998)). HCV NS3 helicase was found to include three domains. Two of these domains (dl and d2) include homologous oligonucleotide-binding motifs conserved across helicase superfamilies (Korolev et al., Protein Science, 7: 605-10 (1998)) that are thought to bind to individual phosphates along the backbone of the oligonucleotide substrate (Kim et al., Structure, 6: 89-100 (1998)).

Although the above crystal structures have provided structural details for the enzyme in specific crystal forms, it would be desirable to have structures for additional crystal forms for comparison purposes. Such comparisons could be useful in helping to understand the protein structures by separating structural details that are merely a consequence of the environment of molecules in one crystal form from structural details that are independent of the crystal environment. Moreover, such comparisons might provide information applicable to better understanding the solution structure of the enzyme.

Multiple crystal forms can also be important for drug design processes. Structure- based drug design is dependent on the ability to produce crystalline complexes of enzyme and inhibitor, so that the interactions that make inhibitor-binding possible can be exploited in further chemical synthesis of analogs. While structures of native (uninhibited) enzyme are a necessary prerequisite to modeling studies, modeling alone can rarely predict correctly the bound geometry and orientation of even a very potent inhibitor. Weak inhibitors, such as preliminary lead compounds pose an even bigger problem for modeling. Structural data from analysis of a complex co-crystal is often the only way to probe molecular binding, and the only way to rationally move forward with a directed chemical analog program.

One common method for generating co-crystal structures is to soak an inhibitor into an existing native crystal form. However, problems frequently arise when intermolecular interactions that stabilize one particular crystal form are incompatible with ligand binding. The protein may be locked in a conformation that does not support binding, or the packing of protein molecules in the crystalline array may physically block access to a particular binding site. Alternatively, suitable solutions for growing protein crystals may not be optimized for inhibitor solubility. For example, the presence of salts in high concentrations may actually compete for inhibitor binding sites. These problems are sometimes alleviated by using alternate crystal forms.

SUMMARY OF THE INVENTION Two new crystal forms of Hepatitis C Virus NS3 helicase have been prepared.

The crystal forms include a tetragonal form with two molecules in the crystallographic asymmetric unit (UHCV-A and UHCV-B), and an orthorhombic form (UHHO). Analysis of X-ray diffraction data from both forms confirms the overall three-domain structure of the enzyme reported by others in the study of different helicase crystal forms. The two new helicase structures differ from those previously reported in the packing relationship between molecules and in regard to the position of domain 2. Domain 2 is free to move in and out about a centrally located hinge, and different crystal forms trap the hinge motion in different conformational states. Comparison of the position of this domain in each of the available crystal structures reveals that the tetragonal form described herein represents the most closed conformational state of the hinge thusfar observed.

In one aspect, the present invention provides a molecule or molecular complex. In one embodiment, the molecule or molecular complex includes at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicase-like domain 1/domain 2 interface, wherein the domain 1/domain 2 interface includes amino acids 205-209,232-238,415- 420 and 460-467, the domain 1/domain 2 interface being defined by a set of points having a root mean square deviation of less than about 1. 5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCV-A, UHCV-B, or UHHO as listed in Tables 1,2, or 3 respectively. In another embodiment, the molecule or molecular complex includes at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicase-like oligonucleotide binding site, wherein the oligonucleotide binding site includes amino acids selected from the group consisting of (1) domain 1 oligonucleotide binding site amino acids 230-232,255,269, and 270-272, and (2) domain 2 oligonucleotide binding site amino acids 391-393,411-413,415,416 and 460; the oligonucleotide binding site being defined by a set of points having a root mean square deviation of less than about 1.5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCV-A, UHCV-B, or UHHO as listed in Tables 1,2, or 3 respectively.

TABLE 1 : UHCV-A Atomic coordinates ATOM RESIDUE X Y Z Q B 1 N ASP A 186-37.219 69. 418 66. 294 1.00 42.22 2 CA ASP A 186-38.043 69. 779 65. 109 1.00 42.61 3 CB ASP A 186-38.600 68. 508 64. 474 1.00 42.44 4 C ASP A 186-39.103 70. 789 65. 512 1.00 42.79 5 O ASP A 186-39.444 70. 920 66. 714 1.00 42.49 6 N ASN A 187-39.587 71. 541 64. 508 1.00 43.26 7 CA ASN A 187-40.640 72. 533 64. 817 1.00 43.45 8 CB ASN A 187-40.194 73. 517 65. 891 1.00 42.71 9 C ASN A 187-41.149 73. 268 63. 596 1.00 43.68 10 O ASN A 187-40.539 73. 285 62. 535 1.00 43.13 11 N SER A 188-42. 311 73. 850 63. 815 1. 00 44.26 12 CA SER A 188-43.014 74. 698 62. 829 1.00 45.12 13 CB SER A 188-44.510 74. 536 62. 884 1.00 45.94 14 OG SER A 188-44.957 74. 935 64. 209 1.00 47.20 15 C SER A 188-42. 623 76. 143 63. 268 1. 00 45.56 160SERA 188-42.421 76. 996 62. 428 1.00 45.92 17 N SER A 189-42.523 76. 294 64. 558 1.00 46.00 18 CA SER A 189-42.120 77. 497 65. 338 1.00 46.12 19 CB SER A 189-42.555 77. 302 66. 767 1.00 47.11 20OSERA 189-42.305 78. 273 67. 743 1.00 47.58 21 C SER A 189-40.605 77. 699 65. 102 1.00 45.88 220SERA 189-39.817 76. 717 65. 031 1.00 46.14 23 N PRO A 190-40.193 78. 951 64. 866 1.00 45.50 24 CA PRO A 190-38.835 79. 394 64. 532 1.00 45.15 25 CB PRO A 190-38.946 80. 909 64. 312 1.00 45.36 26 CG PRO A 190-40.347 81. 316 64. 623 1.00 45.68 27 CD PRO A 190-41.156 80. 096 64. 918 1.00 45.65 28 C PRO A 190-37.706 79. 065 65. 464 1.00 44.25 29 0 PRO A 190-37.616 79. 621 66. 573 1.00 44.44 30 N PRO A 191-36.755 78. 237 65. 033 1.00 43.59 31 CD PRO A 191-36.779 77. 612 63. 681 1.00 43.41 32 CA PRO A 191-35.659 77. 756 65. 806 1.00 43.44 33 CB PRO A 191-34.801 76. 867 64. 922 1.00 43.27 34 CG PRO A 191-35.482 76. 848 63. 591 1.00 43.42 35 C PRO A 191-35. 102 78. 258 67. 062 1. 00 43.13 36 0 PRO A 191-34. 564 77. 354 67. 826 1. 00 43.46 37 N VAL A 192-35. 098 79. 494 67. 466 1. 00 42.67 38 CA VAL A 192-34.572 79. 962 68. 775 1.00 41.77 39 CB VAL A 192-35.568 79. 512 69. 863 1.00 42.28 40 CG1 VAL A 192-35.132 79. 618 71. 306 1.00 42.18 41 CG2 VAL A 192-36.823 80. 444 69. 729 1.00 42.49 42 C VAL A 192-33. 104 79. 836 69. 018 1. 00 40.85 43 0 VAL A 192-32. 578 78. 812 69. 528 1. 00 41.11 44 N VAL A 193-32.374 80. 897 68. 726 1.00 39.54 45 CA VAL A 193-30.928 81. 007 68. 841 1.00 38.30 46 CB VAL A 193-30.395 82. 370 68. 358 1.00 38.15 47 CG1 VAL A 193-28.877 82. 460 68. 459 1.00 38.17 48 CG2 VAL A 193-30.844 82. 799 67. 000 1.00 38.59 49 C VAL A 193 -30.405 80.623 70.222 1. 00 36.97 50 O VAL A 193-30.515 81. 396 71. 189 1.00 36.81 51 N PRO A 194-29.796 79. 459 70. 272 1.00 36.08 52 CD PRO A 194-29.624 78. 535 69. 131 1.00 35.59 53 CA PRO A 194-29.187 78. 913 71. 497 1.00 35.36 54 CB PRO A 194-28.869 77. 466 71. 093 1.00 35.47 55 CG PRO A 194-28.457 77. 674 69. 637 1.00 35.37 56 C PRO A 194-27.888 79. 656 71. 826 1. 00 34.95 57 O PRO A 194-27.388 80. 481 71. 055 1. 00 34.98 58 N GLN A 195-27.362 79. 333 72. 978 1. 00 34.54 59 CA GLN A 195-26.130 79. 958 73. 530 1. 00 34.62 60 CB GLN A 195-26.226 79. 908 75. 080 1. 00 34.62 61 C GLN A 195-24.913 79. 173 73. 025 1. 00 34.46 62 0 GLN A 195-23.804 79. 657 72. 762 1. 00 33.95 63 N SER A 196-25. 245 77.900 72.827 1.00 34. 26 64 CA SER A 196-24.271 76. 870 72. 365 1. 00 34.49 65 CB SER A 196-24.447 75. 745 73. 395 1. 00 35.26 66OSERA 196-23.648 74. 615 73. 241 1. 00 36.59 67 C SER A 196-24.559 76. 475 70. 928 1. 00 33.95 68 O SER A 196-25.748 76. 531 70. 484 1. 00 34.44 69 N PHE A 197-23.516 76. 106 70. 172 1. 00 33.16 70 CA PHE A 197-23.703 75. 706 68. 769 1. 00 32.34 71 CB PHE A 197-22.414 75. 206 68. 092 1. 00 32.31 72 CG PHE A 197-22. 756 74. 677 66. 714 1. 00 32. 21 73 CD1 PHE A 197-22.920 75. 560 65. 653 1. 00 32.33 74 CD2 PHE A 197-22.994 73. 325 66. 528 1. 00 31.88 75 CE1 PHE A 197-23.273 75. 097 64. 389 1. 00 31.91 76 CE2 PHE A 197-23.326 72. 830 65. 267 1. 00 32.13 77 CZ PHE A 197-23.482 73. 734 64. 199 1. 00 32.34 78 C PHE A 197-24.785 74. 636 68. 675 1. 00 32.04 79 0 PHE A 197-24.770 73. 648 69. 462 1. 00 31.90 80 N GLN A 198-25.675 74. 820 67. 680 1. 00 31.40 81 CA GLN A 198-26. 759 73. 803 67. 572 1. 00 30. 58 82 CB GLN A 198-27.850 74. 252 68. 584 1. 00 31.87 83 CG GLN A 198-29.123 73. 432 68. 513 1. 00 33.85 84 CD GLN A 198-30. 150 73. 965 69. 506 1. 00 35. 23 85 OE1 GLN A 198-29.853 74. 022 70. 712 1. 00 35.92 86 NE2 GLN A 198-31. 297 74. 391 68. 998 1. 00 35. 90 87 C GLN A 198-27. 407 73. 618 66. 230 1. 00 29. 54 88 O GLN A 198 -27.837 74.632 65.608 1.00 29. 86 89 N VAL A 199-27. 556 72. 363 65. 839 1. 00 28. 00 90 CA VAL A 199-28.248 72. 051 64. 560 1. 00 26.88 91 CB VAL A 199-27. 595 70. 841 63. 893 1. 00 25. 68 92 CG1 VAL A 199-28.346 70. 409 62. 645 1. 00 23.93 93 CG2 VAL A 199-26.145 71. 218 63. 489 1. 00 24.65 94 C VAL A 199-29.728 71. 825 64. 893 1. 00 26.70 95 O VAL A 199-30. 038 71. 012 65. 778 1. 00 26. 70 96 N ALA A 200-30.604 72. 503 64. 188 1. 00 26.25 97 CA ALA A 200-32.049 72. 365 64. 449 1. 00 25.36 98 CB ALA A 200-32.501 73. 668 65. 138 1. 00 25.58 99 C ALA A 200-32. 768 72. 153 63. 117 1. 00 24. 61 1000ALA A 200-32.296 72. 553 62. 047 1. 00 23.69 101 N HIS A 201-33.959 71. 546 63. 233 1. 00 23.87 102 CA HIS A 201-34.804 71. 299 62. 078 1. 00 23.00 103 CB HIS A 201-35.415 69. 873 62. 011 1. 00 21.94 104 CG HIS A 201-34. 300 68. 894 61. 798 1. 00 21. 20 105 CD2 HIS A 201-33. 442 68.353 62.680 1.00 21.57 106 ND1 HIS A 201-33.937 68. 451 60. 566 1. 00 21.81 107 CE1 HIS A 201-32.866 67. 670 60. 699 1. 00 22.02 108 NE2 HIS A 201-32. 541 67. 622 61. 960 1. 00 21. 87 109 C HIS A 201-35. 987 72. 237 62. 051 1. 00 23. 43 110 O HIS A 201-36.556 72. 581 63. 124 1. 00 23. 82 111 N LEU A 202 -36.379 72.593 60.675 1.00 23. 31 112 CA LEU A 202 -37.515 73.427 60.629 1.00 24. 81 113 CB LEU A 202-37.115 74. 886 60. 291 1. 00 24.69 114 CG LEU A 202-38.389 75. 758 60. 232 1. 00 24.20 115 CD1 LEU A 202-39.014 75. 717 61. 641 1. 00 23.72 116 CD2 LEU A 202-38.035 77. 139 59. 769 1. 00 24.30 117 C LEU A 202-38.389 72. 829 59. 510 1. 00 25.75 118 0 LEU A 202-38.294 73. 253 58. 360 1. 00 25.68 119 N HIS A 203-39.249 71. 919 59. 944 1. 00 26.74 120 CA HIS A 203-40.212 71. 255 59. 027 1. 00 26.88 121 CB HIS A 203-40.464 69. 819 59. 440 1. 00 25.69 122 CG HIS A 203-39.227 68. 985 59. 564 1. 00 25.19 123 CD2 HIS A 203-38.046 69. 051 58. 927 1. 00 24.86 124 ND1 HIS A 203-39.082 67. 962 60. 449 1. 00 26.04 125 CE1 HIS A 203-37.860 67. 415 60. 319 1. 00 26.21 126 NE2 HIS A 203-37.199 68. 064 59. 439 1. 00 24.92 127 C HIS A 203-41.472 72. 133 59. 001 1. 00 27.60 128 0 HIS A 203-42.276 72. 101 59. 953 1. 00 28.19 129 N ALA A 204-41.603 72. 953 57. 982 1. 00 27.76 130 CA ALA A 204-42.706 73. 910 57. 824 1. 00 28.29 131 CB ALA A 204-42.388 75. 189 58. 591 1. 00 27.52 132 C ALA A 204-42.939 74. 150 56. 362 1. 00 29.49 133 0 ALA A 204-42.164 73. 690 55. 522 1. 00 29.75 134 N PRO A 205-44.006 74. 873 56. 028 1. 00 30.83 135 CA PRO A 205-44.406 75. 134 54. 659 1. 00 31.43 136 CB PRO A 205-45.902 75. 350 54. 748 1. 00 31.29 137 CG PRO A 205-46.130 75. 935 56. 109 1. 00 31.24 138 CD PRO A 205-44.937 75. 496 56. 981 1. 00 31.31 139 C PRO A 205-43.615 76. 150 53. 888 1. 00 32.09 140 O PRO A 205-43. 141 77. 193 54. 362 1. 00 32. 73 141 N THR A 206-43.534 75. 858 52. 583 1. 00 32.38 142 CA THR A 206-42.757 76. 676 51. 644 1. 00 33.01 143 CB THR A 206-42.210 75. 832 50. 413 1. 00 33.81 144 OG1 THR A 206-41.287 76. 737 49. 689 1. 00 35.38 145 CG2 THR A 206-43.341 75. 408 49. 437 1. 00 33.95 146 C THR A 206-43.622 77. 825 51. 130 1. 00 32.55 147 0 THR A 206-44.840 77. 780 51. 255 1. 00 32.40 148 N GLY A 207-42. 904 78. 769 50. 545 1. 00 32. 05 149 CA GLY A 207-43. 500 79. 963 49. 954 1. 00 31. 80 150 C GLY A 207-42.572 81. 157 50. 188 1. 00 31.45 151 0 GLY A 207-41. 732 81. 091 51. 100 1. 00 31. 21 152 N SER A 208-42.755 82. 152 49. 326 1. 00 31.19 153 CA SER A 208-41.939 83. 373 49. 467 1. 00 31.15 154 CB SER A 208-42.303 84. 430 48. 480 1. 00 31.29 155 OG SER A 208-42. 080 84. 103 47. 156 1. 00 32. 46 156 C SER A 208-42.152 83. 923 50. 884 1. 00 30.98 157 0 SER A 208-41.212 84. 388 51. 518 1. 00 31.53 158 N GLY A 209-43.404 83. 888 51. 306 1. 00 30.43 159 CA GLY A 209-43.847 84. 393 52. 569 1. 00 29.61 160 C GLY A 209-43.297 83. 682 53. 784 1. 00 29.19 160 O GLY A 209-42.769 84. 369 54. 684 1. 00 28.83 162 N LYS A 210-43.435 82. 384 53. 821 1. 00 28.73 163 CA LYS A 210-43.057 81. 458 54. 830 1. 00 28.89 164 CB LYS A 210-43.641 80. 039 54. 492 1. 00 30.64 165 CG LYS A 210-45.158 79. 962 54. 547 1. 00 31.79 166 CD LYS A 210-45.702 79. 952 55. 939 1. 00 32.25 167 CE LYS A 210-47.200 80. 107 56. 064 1. 00 32.63 168 NZ LYS A 210-47.601 81. 502 55. 639 1. 00 33.08 169 C LYS A 210-41. 562 81. 248 54. 943 1. 00 28. 73 1700LYS A 210-41.080 80. 924 56. 049 1.00 28.29 171 N SER A 211-40.897 81. 396 53. 798 1.00 28.78 172 CA SER A 211-39.456 81. 223 53. 708 1.00 29.10 173 CB SER A 211-38.901 80. 999 52. 287 1.00 29.32 174 OG SER A 211-39.314 79. 892 51. 644 1.00 30.44 175 C SER A 211-38.667 82. 476 54. 167 1.00 29.05 176 0 SER A 211-37.643 82. 266 54. 822 1.00 29.74 177 N THR A 212-39.097 83. 599 53. 652 1.00 28.46 178 CA THR A 212-38.476 84. 885 53. 884 1.00 28.05 179 CB THR A 212-38.866 85. 926 52. 781 1.00 28.43 180 OG1 THR A 212-40. 313 86.064 52.843 1. 00 27.76 181 CG2 THR A 212-38.460 85. 481 51. 359 1.00 27.84 182 C THR A 212-38.668 85. 374 55. 290 1.00 27.59 183 0 THR A 212-37.879 86. 174 55. 817 1.00 27.35 184 N LYS A 213-39. 709 84.840 55.909 1. 00 27.33 185 CA LYS A 213-40.099 85. 146 57. 271 1.00 26.71 186 CB LYS A 213-41.352 84. 349 57. 636 1.00 27.59 187 CG LYS A 213-41.847 84. 633 59. 054 1.00 28.42 188 CD LYS A 213-43.017 83. 707 59. 389 1.00 29.08 189 CE LYS A 213-43.551 84. 062 60. 779 1.00 30.09 190LYS A 213-44.711 83. 195 61. 121 1.00 30.30 191 C LYS A 213-39.048 84. 858 58. 331 1.00 26.21 1920LYS A 213-38.785 85. 714 59. 222 1.00 26.18 193 N VAL A 214-38.460 83. 699 58. 290 1.00 25.35 194 CA VAL A 214-37.473 83. 208 59. 244 1.00 24.74 195 CB VAL A 214-37.265 81. 681 59. 045 1.00 25.03 196 CG1 VAL A 214-36.400 81. 086 60. 146 1.00 24. 26 197 CG2 VAL A 214-38.598 80. 935 58. 918 1.00 24.47 198 C VAL A 214-36.137 83. 928 59. 332 1.00 24.52 199 O VAL A 214-35. 624 84.075 60.462 1. 00 23.99 200 N PRO A 215-35.562 84. 189 58. 171 1.00 24.68 201 CD PRO A 215-36. 101 83. 950 56. 827 1. 00 24.59 202 CA PRO A 215-34.260 84. 879 58. 084 1.00 25.19 203 CB PRO A 215-33.840 84. 781 56. 629 1.00 24.85 204 CG PRO A 215-34.875 83. 938 55. 934 1.00 24.61 205 C PRO A 215-34.530 86. 329 58. 528 1.00 25.77 206 0 PRO A 215-33.780 86. 920 59. 303 1.00 25.93 207 N ALA A 216-35.603 86. 870 57. 939 1.00 26.13 208 CA ALA A 216-35.998 88. 248 58. 257 1.00 26.37 209 CB ALA A 216-37. 295 88.599 57.569 1. 00 26.78 210 C ALA A 216-36. 139 88. 395 59. 783 1. 00 26.81 211 0 ALA A 216-35.694 89. 422 60. 331 1.00 27.05 212 N ALA A 217-36.718 87. 416 60. 417 1.00 26. 70 213 CA ALA A 217-36.983 87. 420 61. 837 1.00 27.32 214 CB ALA A 217-38.046 86. 458 62. 362 1.00 27.44 215 C ALA A 217-35.701 87. 391 62. 609 1.00 27.21 216 O ALA A 217-35.651 88. 081 63. 629 1.00 27.86 217 N TYR A 218-34.723 86. 658 62. 132 1.00 27.02 218 CA TYR A 218-33.438 86. 555 62. 777 1.00 27.13 219 CB TYR A 218-32.546 85. 360 62. 484 1.00 25.61 220 CG TYR A 218-33.044 83. 982 62. 831 1.00 25.18 221 CD1 TYR A 218-33.289 83. 012 61. 849 1.00 25.49 222 CE1 TYR A 218-33.714 81. 716 62. 180 1.00 25.16 223 CD2 TYR A 218-33.239 83. 598 64. 141 1.00 25.01 224 CE2 TYR A 218-33.682 82. 316 64. 517 1.00 24.71 225 CZ TYR A 218-33.925 81. 391 63. 513 1.00 25.85 226 OH TYR A 218-34. 306 80. 138 63. 899 1. 00 27.79 227 C TYR A 218-32.650 87. 864 62. 575 1.00 27.22 228 0 TYR A 218-31.901 88. 147 63. 538 1.00 27.97 229 N ALA A 219-32.801 88. 542 61. 487 1.00 26.99 230 CA ALA A 219-32.041 89. 785 61. 248 1.00 27.60 231 CB ALA A 219-32.244 90. 220 59. 805 1.00 27.92 232 C ALA A 219-32.434 90. 896 62. 213 1.00 28.06 233 O ALA A 219-31.606 91. 740 62. 670 1.00 28.31 234 N ALA A 220-33.752 90. 932 62. 453 1.00 27.84 235 CA ALA A 220-34.300 91. 955 63. 376 1.00 27.82 236 CB ALA A 220-35. 814 91.975 63.227 1. 00 27.27 237 C ALA A 220-33. 868 91. 670 64. 805 1. 00 28.14 238 0 ALA A 220-33.842 92. 599 65. 621 1.00 28. 01 239 N GLN A 221-33.562 90. 425 65. 088 1.00 28.35 240 CA GLN A 221-33.155 89. 850 66. 393 1.00 28.74 241 CB GLN A 221-33.692 88. 460 66. 491 1.00 30.66 242 CG GLN A 221-33.598 87. 514 67. 643 1.00 32.83 243 CD GLN A 221-34.283 86. 185 67. 367 1.00 34.50 244 OE1 GLN A 221-34.764 85. 975 66. 255 1.00 35.87 245 NE2 GLN A 221-34. 357 85.265 68.321 1. 00 35.40 246 C GLN A 221-31. 657 90. 072 66. 629 1. 00 28.77 247 0 GLN A 221-31. 024 89. 781 67. 673 1. 00 29.00 248 N GLY A 222-31.050 90. 731 65. 634 1.00 27.70 249 CA GLY A 222-29.746 91. 151 65. 440 1.00 26.47 250 C GLY A 222-28.695 90. 348 64. 747 1.00 25.28 251 0 GLY A 222-27.544 90. 824 64. 592 1.00 24.99 252 N TYR A 223-29.009 89. 174 64. 261 1.00 24.26 253 CA TYR A 223-28.118 88. 227 63. 617 1.00 22.76 254 CB TYR A 223-28.749 86. 833 63. 933 1.00 23.77 255 CG TYR A 223-28. 967 86.521 65.377 1. 00 24.75 256 CD1 TYR A 223-30. 268 86. 433 65. 909 1. 00 24.45 257 CE1 TYR A 223-30.491 86. 128 67. 255 1.00 24.66 258 CD2 TYR A 223-27.895 86. 280 66. 240 1.00 25.63 259 CE2 TYR A 223-28.103 85. 955 67. 584 1.00 25.61 260 CZ TYR A 223-29. 403 85. 895 68. 082 1. 00 24.93 261 OH TYR A 223-29.559 85. 556 69. 407 1.00 24.27 262 C TYR A 223-27.718 88. 347 62. 201 1.00 21.45 263 O TYR A 223-28.349 88. 993 61. 356 1.00 20.85 264 N LYS A 224-26.504 87. 774 61. 877 1.00 21.03 265 CA LYS A 224-26.059 87. 792 60. 416 1.00 20.00 266 CB LYS A 224-24.580 87. 907 60. 289 1.00 20.36 267 CG LYS A 224-24.053 89. 213 60. 904 1.00 22.24 268 CD LYS A 224-22.572 89. 315 60. 945 1.00 24.15 269 CE LYS A 224-21.818 88. 294 61. 738 1.00 24.54 270LYS A 224-22.166 88. 189 63. 138 1.00 25.10 271 C LYS A 224-26.559 86. 392 59. 961 1.00 19.40 272 0 LYS A 224-26.432 85. 457 60. 769 1.00 20.05 273 N VAL A 225-27.185 86. 318 58. 832 1.00 18. 78 274 CA VAL A 225-27.798 85. 102 58. 329 1.00 17.05 275 CB VAL A 225-29.366 85. 303 58. 405 1.00 16.52 276 CG1 VAL A 225-30.040 83. 946 58. 028 1.00 15.02 277 CG2 VAL A 225-29.857 85. 687 59. 743 1.00 16.52 278 C VAL A 225-27.440 84. 737 56. 908 1.00 16.36 279 O VAL A 225-27.577 85. 514 55. 946 1.00 17.44 280 N LEU A 226-27.137 83. 455 56. 729 1.00 15.65 281 CA LEU A 226-26.857 82. 918 55. 396 1.00 15.41 282 CB LEU A 226-25.538 82. 109 55. 443 1.00 12.86 283 CG LEU A 226-25.121 81. 557 54. 117 1.00 12.34 284 CD1 LEU A 226-24.928 82. 593 53. 049 1.00 13.41 285 CD2 LEU A 226-23.815 80. 747 54. 288 1.00 12.60 286 C LEU A 226-28.031 82. 005 55. 019 1.00 15.55 287 0 LEU A 226-28.286 81. 113 55. 821 1.00 15.93 288 N VAL A 227-28.613 82. 238 53. 863 1.00 16.50 289 CA VAL A 227-29. 744 81. 368 53. 424 1. 00 16.16 290 CB VAL A 227-31.034 82. 198 53. 343 1.00 15.00 291 CG1 VAL A 227-32.188 81. 183 53. 097 1.00 14.84 292 CG2 VAL A 227-31.298 83. 017 54. 577 1.00 13.21 293 C VAL A 227-29.376 80. 580 52. 202 1.00 15.49 294 O VAL A 227-29.181 81. 166 51. 125 1.00 16.49 295 N LEU A 228-29.384 79. 250 52. 264 1.00 15.06 296 CA LEU A 228-28.990 78. 469 51. 050 1.00 14.89 297 CB LEU A 228-27.900 77. 552 51. 604 1.00 14.84 298 CG LEU A 228-26.698 78. 024 52. 315 1.00 15.05 299 CD1 LEU A 228-25. 821 76.920 52.829 1. 00 12. 57 300 CD2 LEU A 228-25.921 78. 947 51. 346 1.00 14.80 301 C LEU A 228-30.167 77. 637 50. 479 1.00 14.84 3020 LEU A 228-30.831 76. 975 51. 236 1.00 13.76 303 N ASN A 229-30.238 77. 575 49. 170 1.00 15.66 304 CA ASN A 229-31.186 76. 887 48. 342 1.00 15.79 305 CB ASN A 229-32.297 77. 882 47. 833 1.00 18.28 306 CG ASN A 229-33.031 78. 549 48. 972 1.00 19.81 307 OD1 ASN A 229-32.527 79. 489 49. 613 1.00 20.85 308 ND2 ASN A 229-34.292 78. 090'49. 082 1.00 21.40 309 C ASN A 229-30. 553 76. 326 47. 067 1. 00 15.58 310 0 ASN A 229-29.663 76. 933 46. 477 1.00 16.31 311 N PRO A 230-31. 127 75.244 46.564 1. 00 15.32 312 CD PRO A 230-32.179 74. 434 47. 188 1.00 15.00 313 CA PRO A 230-30.644 74. 648 45. 323 1.00 15.45 314 CB PRO A 230-31.555 73. 462 45. 111 1.00 14.87 315 CG PRO A 230-32.049 73. 056 46. 487 1.00 14.12 316 C PRO A 230-30.571 75. 556 44. 106 1.00 15.97 317 0 PRO A 230-29.546 75. 618 43. 431 1.00 15.48 318 N SER A 231-31.654 76. 164 43. 670 1.00 16.97 319 CA SER A 231-31. 862 76.903 42.488 1. 00 18.17 320 CB SER A 231-33.442 77. 135 42. 356 1.00 19.08 321 OG SER A 231-34. 041 75. 872 42. 497 1. 00 22.83 322 C SER A 231-31.414 78. 370 42. 544 1.00 19.03 323 0 SER A 231-31. 584 78. 932 43. 639 1. 00 18.66 324 N VAL A 232-31.090 78. 839 41. 372 1.00 19.82 325 CA VAL A 232-30. 729 80.261 41.226 1. 00 21.99 326 CB VAL A 232-30.076 80. 566 39. 875 1.00 23.71 327 CG1 VAL A 232-30. 003 82.090 39.625 1. 00 25.04 328 CG2 VAL A 232-28.594 80. 084 39. 847 1.00 24.60 329 C VAL A 232-32.072 81. 042 41. 345 1.00 22.74 330 O VAL A 232-32. 053 82. 146 41. 833 1. 00 22.92 331 N ALA A 233-33. 116 80.401 40.876 1. 00 23.30 332 CA ALA A 233-34.475 80. 882 40. 818 1.00 22.74 333 CB ALA A 233-35.319 79. 922 40. 001 1.00 24.96 334 C ALA A 233-35.156 81. 017 42. 151 1.00 22.61 335 0 ALA A 233-36.152 81. 778 42. 273 1.00 23.64 336 N ALA A 234-34.845 80. 212 43. 096 1.00 21.99 337 CA ALA A 234-35.342 80. 260 44. 459 1.00 21.45 338 CB ALA A 234-34.914 79. 006 45. 234 1.00 22.65 339 C ALA A 234-34.567 81. 482 45. 085 1.00 20.58 340 0 ALA A 234-35.151 82. 447 45. 524 1.00 20.78 341 N THR A 235-33.269 81. 365 45. 023 1.00 19.26 342 CA THR A 235-32.374 82. 365 45. 578 1.00 18.50 343 CB THR A 235-30.840 81. 936 45. 210 1.00 16.33 344 OG1 THR A 235-30.795 80. 664 45. 885 1.00 13.82 345 CG2 THR A 235-29.828 82. 949 45. 761 1.00 13.12 346 C THR A 235-32. 569 83. 773 45. 106 1. 00 18.53 347 0 THR A 235-32.461 84. 665 45. 960 1.00 19.87 348 N LEU A 236-32.925 83. 945 43. 872 1.00 18.74 349 CA LEU A 236-33.027 85. 299 43. 260 1.00 18.94 350 CB LEU A 236-32.715 84. 920 41. 792 1.00 18.22 351 CG LEU A 236-31.904 85. 956 40. 949 1.00 18.07 352 CD1 LEU A 236-30.495 86. 069 41. 523 1.00 16.94 353 CD2 LEU A 236-31.770 85. 238 39. 572 1.00 18.96 354 C LEU A 236-34.421 85. 842 43. 544 1.00 19.11 355 O LEU A 236-34.670 87. 038 43. 717 1.00 18.15 356 N GLY A 237-35.348 84. 904 43. 592 1.00 19.63 357 CA GLY A 237-36.766 85. 199 43. 835 1.00 20.28 358 C GLY A 237-37.059 85. 428 45. 310 1.00 21.01 359 0 GLY A 237-38.009 86. 244 45. 579 1.00 21.14 360 N PHE A 238-36. 396 84. 735 46. 196 1. 00 20.79 361 CA PHE A 238-36.541 84. 886 47. 645 1.00 20.99 362 CB PHE A 238-36.075 83. 783 48. 490 1.00 20.28 363 CG PHE A 238-36.767 82. 438 48. 464 1.00 21.27 364 CD1 PHE A 238-36.003 81. 279 48. 627 1.00 20.67 365 CD2 PHE A 238-38.112 82. 358 48. 209 1.00 21.25 366 CE1 PHE A 238-36.615 80. 037 48. 608 1.00 21.46 367 CE2 PHE A 238-38.777 81. 074 48. 172 1.00 22.04 368 CZ PHE A 238-37.993 79. 954 48. 419 1.00 21.61 369 C PHE A 238-35.904 86. 220 48. 111 1.00 21.90 370 O PHE A 238-36.352 86. 890 49. 059 1.00 22.17 371 N GLY A 239-34.842 86. 545 47. 436 1.00 23.19 372 CA GLY A 239-34.063 87. 801 47. 719 1.00 24.00 373 C GLY A 239-34.800 89. 004 47. 172 1.00 24.65 374 0 GLY A 239-34.640 90. 154 47. 646 1.00 25.18 375 N ALA A 240-35.539 88. 795 46. 093 1.00 25.20 376 CA ALA A 240-36.311 89. 880 45. 454 1.00 25.19 377 CB ALA A 240-36.639 89. 541 44. 003 1.00 24.99 378 C ALA A 240-37.604 90. 129 46. 231 1.00 26. 11 379 0 ALA A 240-38.192 91. 235 46. 175 1.00 25.81 380 N TYR A 241-38.045 89. 060 46. 902 1.00 26.27 381 CA TYR A 241-39.266 89. 140 47. 716 1.00 26.48 382 CB TYR A 241-39.888 87. 749 47. 892 1.00 27.43 383 CG TYR A 241-41.153 87. 763 48. 726 1.00 27.77 384 CD1 TYR A 241-41.108 87. 635 50. 112 1.00 27.84 385 CE1 TYR A 241-42.281 87. 636 50. 870 1.00 27.05 386 CD2 TYR A 241-42.392 87. 927 48. 101 1.00 27.54 387 CE2 TYR A 241-43.571 87. 905 48. 853 1.00 26.94 388 CZ TYR A 241-43.504 87. 783 50. 214 1.00 26.93 389 OH TYR A 241-44.686 87. 792 50. 926 1.00 28.06 390 C TYR A 241-38.907 89. 810 49. 045 1.00 26.24 391 O TYR A 241-39.654 90. 620 49. 592 1.00 26.05 392 N MET A 242-37.713 89. 481 49. 531 1.00 26.49 393 CA MET A 242-37.173 90. 081 50. 758 1.00 26.15 394 CB MET A 242-35.781 89. 616 51. 086 1.00 24.67 395 CG MET A 242-35.368 90. 159 52. 420 1.00 23.33 396 SD MET A 242-36.003 89. 298 53. 792 1.00 22.80 397 CE MET A 242-35.298 87. 690 53. 844 1.00 24.19 398 C MET A 242-37.109 91. 606 50. 525 1.00 26.98 399 O MET A 242-37.244 92. 354 51. 500 1.00 27.37 400 N SER A 243-36.862 92. 043 49. 301 1.00 28.10 401 CA SER A 243-36.806 93. 433 48. 951 1.00 29.42 402 CB SER A 243-36.050 93. 895 47. 709 1.00 30.10 403 OG SER A 243-34.646 93. 675 47. 795 1.00 30.61 404 C SER A 243-38.174 94. 122 48. 902 1.00 30.07 405 O SER A 243-38.323 95. 084 49. 680 1.00 30.80 406 N LYS A 244-39.045 93. 710 48. 004 1.00 30.10 407 CA LYS A 244-40.345 94. 323 47. 761 1.00 30.31 408 CB LYS A 244-41.015 93. 751 46. 480 1.00 32.23 409 CG LYS A 244-40.130 93. 536 45. 310 1.00 34.61 410 CD LYS A 244-39.264 94. 558 44. 712 1.00 36.60 411 CE LYS A 244-39.836 95. 723 43. 973 1.00 37.95 412 NZ LYS A 244-38.789 96. 713 43. 556 1.00 38.35 413 C LYS A 244-41.382 94. 163 48. 857 1.00 29.60 4140 LYS A 244-42.362 94. 957 48. 893 1.00 29.53 415 N ALA A 245-41.181 93. 233 49. 762 1.00 29.14 416 CA ALA A 245-42.122 92. 941 50. 845 1.00 28.83 417 CB ALA A 245-42.738 91. 545 50. 619 1.00 29.07 418 C ALA A 245-41. 597 93. 026 52. 248 1. 00 28. 07 419 O ALA A 245-42.404 93. 171 53. 167 1.00 28.40 420 N HIS A 246-40.315 92. 869 52. 462 1.00 27.62 421 CA HIS A 246-39.749 92. 942 53. 782 1.00 27.24 422 CB HIS A 246-39.012 91. 749 54. 308 1.00 25.11 423 CG HIS A 246-39. 788 90.535 54.637 1. 00 22.85 424 CD2 HIS A 246-39.972 89. 984 55. 857 1.00 22.65 425 ND1 HIS A 246-40.334 89. 703 53. 699 1.00 22.24 426 CE1 HIS A 246-40.841 88. 649 54. 354 1.00 22.88 427 NE2 HIS A 246-40.662 88. 777 55. 651 1.00 23.33 428 C HIS A 246-38.871 94. 186 53. 944 1.00 27.85 429 O HIS A 246-38.369 94. 381 55. 061 1.00 28.42 430 N GLY A 247-38. 645 94.888 52.869 1. 00 28.68 431 CA GLY A 247-37.783 96. 100 52. 953 1.00 29.24 432 C GLY A 247-36.364 95. 752 53. 376 1.00 29.84 433 0 GLY A 247-35.683 96. 584 54. 054 1.00 31.05 434 N ILE A 248-35.891 94. 617 52. 978 1.00 29.20 435 CA ILE A 248-34.523 94. 137 53. 228 1.00 28.87 436 CB ILE A 248-34.390 92. 971 54. 221 1.00 28. 74 437 CG2 ILE A 248-32.906 92. 549 54. 472 1.00 29.86 438 CG1 ILE A 248-35.040 93. 372 55. 566 1.00 29.49 439 CD1 ILE A 248-34.943 92. 270 56. 668 1.00 30.44 440 C ILE A 248-33.929 93. 756 51. 853 1.00 28.76 441 O ILE A 248-34.516 92. 970 51. 090 1.00 28.97 442 N ASP A 249-32.862 94. 463 51. 550 1.00 28.45 443 CA ASP A 249-32.083 94. 241 50. 305 1.00 27.70 444 CB ASP A 249-31.757 95. 496 49. 557 1.00 29.95 445 CG ASP A 249-32.931 96. 273 49. 012 1.00 32. 44 446 OD1 ASP A 249-33.290 95. 990 47. 831 1.00 33.66 447 OD2 ASP A 249-33.474 97. 135 49. 710 1.00 33.79 448 C ASP A 249-30.842 93. 453 50. 790 1.00 26.00 449 O ASP A 249-29.885 94. 065 51. 229 1.00 25.73 450 N PRO A 250-30.967 92. 146 50. 720 1.00 24.54 451 CD PRO A 250-32.127 91. 381 50. 208 1.00 24.54 452 CA PRO A 250-29.891 91. 260 51. 174 1.00 23.63 453 CB PRO A 250-30.692 89. 940 51. 445 1.00 23.50 454 CG PRO A 250-31.684 89. 937 50. 340 1.00 23.94 455 C PRO A 250-28.892 91. 029 50. 064 1.00 22.29 456 0 PRO A 250-29.144 91. 471 48. 926 1.00 22.37 457 N ASN A 251-27.796 90. 352 50. 396 1.00 21.21 458 CA ASN A 251-26. 826 90. 006 49. 333 1. 00 20.17 459 CB ASN A 251-25.503 89. 559 50. 023 1.00 20.52 460 CG ASN A 251-25.069 90. 702 50. 945 1.00 21.89 461 OD1 ASN A 251-24.358 91. 574 50. 466 1.00 22.78 462 ND2 ASN A 251-25.590 90. 700 52. 175 1.00 21.42 463 C ASN A 251-27.512 88. 808 48. 626 1.00 19.41 464 0 ASN A 251-28.135 88. 104 49. 365 1.00 17.06 465 N ILE A 252-27.310 88. 644 47. 362 1.00 20.23 466 CA ILE A 252-27.839 87. 623 46. 487 1.00 20.74 467 CB ILE A 252-28.992 88. 212 45. 568 1.00 21.31 468 CG2 ILE A 252-29.663 87. 184 44. 651 1.00 19.81 469 CG1 ILE A 252-30.054 88. 929 46. 434 1.00 22.38 470 CD1 ILE A 252-31.213 89. 567 45. 623 1.00 22.52 471 C ILE A 252-26.649 87. 122 45. 631 1.00 21.78 4720 ILE A 252-26.124 87. 886 44. 770 1.00 23.16 473 N ARG A 253-26. 176 85. 959 45. 946 1. 00 21.38 474 CA ARG A 253-25. 045 85. 292 45. 276 1. 00 21.92 475 CB ARG A 253-24. 037 84. 886 46. 375 1. 00 20. 92 476 CG ARG A 253-23. 660 86. 063 47. 291 1. 00 21.33 477 CD ARG A 253-22. 541 85. 615 48. 205 1. 00 22.06 478 NE ARG A 253-21. 325 85. 401 47. 482 1. 00 22.79 479 CZ ARG A 253-20. 570 86. 300 46. 875 1. 00 23.93 480 NH1 ARG A 253-20.872 87. 603 46. 900 1.00 24.32 481 NH2 ARG A 253-19.441 85. 927 46. 261 1.00 24.24 482 C ARG A 253-25.423 84. 036 44. 525 1.00 22.47 483 0 ARG A 253-25.657 82. 975 45. 125 1.00 22.45 484 N THR A 254-25.427 84. 107 43. 219 1.00 23.47 485 CA THR A 254-25.714 83. 038 42. 291 1.00 23.74 486 CB THR A 254-26.960 83. 290 41. 410 1.00 23.06 487 OG1 THR A 254-26.519 84. 245 40. 407 1.00 24.84 488 CG2 THR A 254-28.098 83. 863 42. 281 1.00 22.35 489 C THR A 254-24.435 82. 872 41. 425 1.00 24.79 490 O THR A 254-23.583 83. 760 41. 497 1.00 25.37 491 N GLY A 255-24.352 81. 796 40. 708 1.00 25.13 492 CA GLY A 255-23.159 81. 470 39. 921 1.00 26.77 493 C GLY A 255-23.099 82. 293 38. 656 1.00 27.88 494 0 GLY A 255-22.122 82. 139 37. 926 1.00 28.75 495 N VAL A 256-24.129 83. 058 38. 382 1.00 28.60 496 CA VAL A 256-24.159 83. 888 37. 145 1.00 29.10 497 CB VAL A 256-25.314 83. 375 36. 293 1.00 30.12 498 CG1 VAL A 256-26.664 83. 655 36. 923 1.00 30.86 499 CG2 VAL A 256-25.176 83. 793 34. 856 1.00 30.77 500 C VAL A 256-24.143 85. 353 37. 449 1.00 28.85 501 0 VAL A 256-23.645 86. 121 36. 603 1.00 29.48 502 N ARG A 257-24.701 85. 810 38. 562 1.00 28.96 503 CA ARG A 257-24.646 87. 228 38. 947 1.00 29.19 504 CB ARG A 257-25.642 88. 186 38. 307 1.00 29.56 505 CG ARG A 257-26.982 88. 153 38. 940 1.00 30.83 506 CD ARG A 257-27.872 89. 271 38. 687 1.00 32.08 507 NE ARG A 257-28.664 89. 477 37. 513 1.00 33.41 508 CZ ARG A 257-29.488 88. 466 37. 106 1.00 34.29 509 NH1 ARG A 257-29.498 87. 256 37. 687 1.00 35.55 510 NH2 ARG A 257-30.364 88. 689 36. 126 1.00 35.24 511 C ARG A 257-24.851 87. 318 40. 476 1.00 29.02 512 O ARG A 257-25.636 86. 591 41. 088 1.00 29.57 513 N THR A 258-24. 140 88. 159 41. 092 1. 00 29.09 514 CA THR A 258-24. 031 88. 539 42. 483 1. 00 29.32 515 CB THR A 258-22. 524 88. 491 42. 992 1. 00 29.29 516 OG1 THR A 258-22.163 87. 097 42. 872 1.00 30.94 517 CG2 THR A 258-22. 319 89. 024 44. 407 1. 00 29.49 518 C THR A 258-24.459 90. 032 42. 609 1.00 29.11 519 0 THR A 258-24.090 90. 885 41. 782 1.00 28.73 520 N ILE A 259-25.229 90. 221 43. 643 1.00 29.11 521 CA ILE A 259-25.761 91. 558 44. 004 1.00 28.62 522 CB ILE A 259-27.301 91. 619 43. 836 1.00 28.86 523 CG2 ILE A 259-27.868 92. 943 44. 397 1.00 29.38 524 CG1 ILE A 259-27.720 91. 410 42. 351 1.00 29.11 525 CD1 ILE A 259-29.275 91. 445 42. 191 1.00 29.61 526 C ILE A 259-25.371 91. 723 45. 478 1.00 28.36 527 O ILE A 259-25.917 91. 039 46. 322 1.00 27.77 528 N THR A 260-24.465 92. 643 45. 688 1.00 28.41 529 CA THR A 260-23.965 92. 916 47. 055 1.00 28.03 530 CB THR A 260-22.382 92. 892 47. 000 1.00 28. 35 531 OG1 THR A 260-22.045 91. 702 46. 225 1.00 29.23 532 CG2 THR A 260-21.750 92. 829 48. 403 1.00 28.85 533 C THR A 260-24.48594. 29247. 5001.00 27.51 534 0 THR A 260-24.366 95. 293 46. 756 1.00 26.55 535 N THR A 261-25. 060 94. 275 48. 731 1. 00 27.15 536 CA THR A 261-25.578 95. 511 49. 270 1.00 27.15 537 CB THR A 261-27.164 95. 599 49. 318 1.00 25.52 538 OG1 THR A 261-27. 516 94.703 50.378 1. 00 25.13 539 CG2 THR A 261-27.826 95. 201 47. 969 1.00 25.37 540 C THR A 261-25.051 95. 819 50. 662 1.00 27.48 541 O THR A 261-25. 256 97.014 51.048 1. 00 28.48 542 N GLY A 262-24.487 94. 899 51. 389 1.00 27.12 543 CA GLY A 262-23.992 95. 137 52. 741 1.00 26.68 544 C GLY A 262-24.815 94. 578 53. 854 1.00 27.08 545 0 GLY A 262-24.364 94. 612 55. 034 1.00 27.85 546 N SER A 263-25.982 94. 024 53. 579 1.00 27.17 547 CA SER A 263-26.929 93. 434 54. 533 1.00 26.66 548 CB SER A 263-28.173 92. 920 53. 769 1.00 27.19 549 OG SER A 263-29.153 92. 509 54. 752 1.00 26.05 550 C SER A 263-26.384 92. 300 55. 355 1.00 26.18 551 O SER A 263-25.469 91. 600 54. 892 1.00 27.10 552 N PRO A 264-26.907 92. 098 56. 549 1.00 25.46 553 CD PRO A 264-27.988 92. 899 57. 184 1.00 25.41 554 CA PRO A 264-26.465 91. 025 57. 448 1.00 24.90 555 CB PRO A 264-26.947 91. 500 58. 824 1.00 25.04 556 CG PRO A 264-28.246 92. 198 58. 504 1.00 24.90 557 C PRO A 264-27.139 89. 710 57. 058 1.00 23.39 558 0 PRO A 264-27.030 88. 704 57. 771 1.00 23.61 559 N ILE A 265-27.874 89. 798 55. 985 1.00 22.63 560 CA ILE A 265-28.583 88. 632 55. 412 1.00 21.22 561 CB ILE A 265-30.136 88. 785 55. 338 1.00 20.23 562 CG2 ILE A 265-30.770 87. 421 54. 808 1.00 18.51 563 CG1 ILE A 265-30.768 89. 140 56. 704 1.00 20.88 564 CD1 ILE A 265-32.290 89. 537 56. 478 1.00 20.35 565 C ILE A 265-28.131 88. 467 53. 932 1.00 20.13 5660 ILE A 265-28.390 89. 381 53. 101 1.00 20.18 567 N THR A 266-27.667 87. 241 53. 682 1.00 18.48 568 CA THR A 266-27. 252 86. 823 52. 353 1. 00 16.31 569 CB THR A 266-25. 677 86. 503 52. 323 1. 00 14. 55 570 OG1 THR A 266-24. 986 87. 705 52. 728 1. 00 13. 19 571 CG2 THR A 266-25.223 86. 102 50. 918 1. 00 13.66 572 C THR A 266-27.900 85. 507 51. 857 1. 00 15.69 573 0 THR A 266-27.839 84. 455 52. 520 1. 00 15.13 574 N TYR A 267-28.412 85. 604 50. 640 1. 00 15.59 575 CA TYR A 267-28.989 84. 455 49. 926 1. 00 15.65 576 CB TYR A 267-30.275 84. 779 49. 194 1. 00 16.78 577 CG TYR A 267-31. 500 84.914 50.041 1.00 17. 20 578 CD1 TYR A 267-31.762 86. 018 50. 808 1. 00 18.67 579 CE1 TYR A 267-32.923 86. 100 51. 576 1. 00 19.15 580 CD2 TYR A 267-32.354 83. 800 50. 131 1. 00 17.44 581 CE2 TYR A 267 -33.514 83.869 50.893 1.00 18. 28 582 CZ TYR A 267-33.781 84. 991 51. 626 1. 00 18.64 583 OH TYR A 267-34.910 85. 008 52. 375 1. 00 19.98 584 C TYR A 267-27.922 83. 991 48. 907 1. 00 14.55 585 O TYR A 267-27.362 84. 837 48. 208 1. 00 14.58 586 N SER A 268-27.667 82. 716 48. 917 1. 00 13.93 587 CA SER A 268-26.652 82. 101 48. 013 1. 00 12.89 588 CB SER A 268-25. 404 81. 715 48. 866 1. 00 13. 29 589 OG SER A 268-24.517 81. 169 47. 846 1. 00 14.13 590 C SER A 268-27. 260 80. 697 47. 633 1. 00 12. 99 591 0 SER A 268-28.074 80. 253 48. 391 1. 00 12.19 592 N THR A 269-26. 730 80. 155 46. 592 1. 00 13. 40 593 CA THR A 269-27.125 78. 857 46. 069 1. 00 12.83 594 CB THR A 269-27.133 78. 783 44. 528 1. 00 12.59 595 OG1 THR A 269-25.775 78. 892 44. 042 1. 00 14.95 596 CG2 THR A 269-28.061 79. 672 43. 716 1. 00 9.48 597 C THR A 269-26.113 77. 980 46. 779 1. 00 14.15 598 0 THR A 269-25.160 78. 580 47. 374 1. 00 14.26 599 N TYR A 270-26.344 76. 701 46. 827 1. 00 14.69 600 CA TYR A 270-25.505 75. 729 47. 451 1. 00 15.12 601 CB TYR A 270-26. 101 74. 327 47. 677 1. 00 13. 90 602 CG TYR A 270-27.096 74. 192 48. 811 1. 00 13.75 603 CD1 TYR A 270-28. 461 73. 940 48. 551 1. 00 14. 45 604 CE1 TYR A 270-29.388 73. 801 49. 595 1. 00 12.74 605 CD2 TYR A 270-26.656 74. 282 50. 124 1. 00 13.26 606 CE2 TYR A 270-27.574 74. 095 51. 185 1. 00 14.13 607 CZ TYR A 270-28.930 73. 910 50. 893 1. 00 13.74 608 OH TYR A 270-29.781 73. 891 51. 940 1. 00 15.51 609 C TYR A 270-24.187 75. 632 46. 645 1. 00 16.10 610 O TYR A 270-23.130 75. 571 47. 251 1. 00 17.51 611 N GLY A 271-24. 355 75. 651 45. 329 1. 00 15. 54 612 CA GLY A 271-23. 287 75. 594 44. 374 1. 00 15. 59 613 C GLY A 271-22. 372 76. 820 44. 557 1. 00 15. 46 614 0 GLY A 271-21. 160 76. 607 44. 673 1. 00 16. 21 615 N LYS A 272-22.948 77. 944 44. 580 1. 00 15.40 616 CA LYS A 272-22.234 79. 238 44. 766 1. 00 14.97 617 CB LYS A 272-23.157 80. 356 44. 385 1. 00 14.10 618 CG LYS A 272-22.544 81. 795 44. 679 1. 00 14.16 619 CD LYS A 272-21.353 81. 926 43. 734 1. 00 14.59 620 CE LYS A 272-20.843 83. 386 43. 651 1. 00 14.15 621LYS A 272-19.574 83. 283 42. 819 1. 00 15.87 622 C LYS A 272-21.574 79. 344 46. 089 1. 00 16.28 6230LYS A 272-20.471 80. 033 46. 184 1. 00 18.51 624 N PHE A 273-22. 037 78. 778 47. 164 1. 00 16. 23 625 CA PHE A 273-21. 465 78. 746 48. 520 1. 00 16. 28 626 CB PHE A 273-22.456 77. 956 49. 463 1.00 15.41 627 CG PHE A 273-21.927 77. 625 50. 824 1.00 15.07 628 CDI PHE A 273-21.633 78. 618 51. 767 1.00 14.99 629 CD2 PHE A 273-21.785 76. 311 51. 212 1.00 15.87 630 CE1 PHE A 273-21. 189 78. 305 53. 018 1. 00 15.39 631 CE2 PHE A 273-21.304 75. 934 52. 473 1.00 15.16 632 CZ PHE A 273-21.005 76. 977 53. 379 1.00 15.30 633 C PHE A 273-20.169 77. 907 48. 484 1.00 17.16 634 0 PHE A 273-19.185 78. 099 49. 192 1.00 16.84 635 N LEU A 274-20. 338 76. 865 47. 672 1. 00 17.66 636 CA LEU A 274-19. 249 75. 824 47. 505 1. 00 17.45 637 CB LEU A 274-20. 100 74. 675 46. 960 1. 00 16.51 638 CG LEU A 274-19. 787 73. 251 47. 265 1. 00 14.89 639 CD1 LEU A 274-19. 658 73.124 48.799 1. 00 13.80 640 CD2 LEU A 274-21.096 72. 436 46. 904 1.00 15.22 641 C LEU A 274-18.197 76. 480 46. 633 1.00 17. 87 642 0 LEU A 274-16.979 76. 385 46. 931 1.00 18.57 643 N ALA A 275-18.633 77. 143 45. 583 1.00 17.81 644 CA ALA A 275-17.722 77. 845 44. 676 1.00 18.90 645 CB ALA A 275-18. 400 78. 289 43. 437 1. 00 17.99 646 C ALA A 275-16.930 78. 867 45. 494 1.00 20.43 647 0 ALA A 275-15.702 79. 083 45. 281 1.00 20.94 648 N ASP A 276-17.513 79. 439 46. 530 1.00 20.50 649 CA ASP A 276-16.944 80. 411 47. 418 1.00 21.29 650 CB ASP A 276-18.007 81. 341 48. 038 1.00 23.14 651 CG ASP A 276-18.643 82. 259 47. 044 1.00 24.46 652 OD1 ASP A 276-19.779 82. 745 47. 252 1.00 25.31 653 OD2 ASP A 276-17.977 82. 554 46. 021 1.00 25.11 654 C ASP A 276-15.966 79. 900 48. 465 1.00 21.28 6550ASP A 276-15.343 80. 767 49. 145 1.00 21.35 656 N GLY A 277-15.831 78. 593 48. 623 1.00 20.57 657 CA GLY A 277-14.898 78. 054 49. 632 1.00 20.26 658 C GLY A 277-15.564 77. 656 50. 910 1.00 20.30 659 O GLY A 277-14.869 77. 440 51. 940 1.00 20.54 660 N GLY A 278-16.904 77. 600 50. 922 1.00 20.00 661 CA GLY A 278-17.554 77. 188 52. 223 1.00 20.17 662 C GLY A 278-17.633 78. 405 53. 164 1.00 20.31 663 O GLY A 278-17.759 79. 516 52. 727 1.00 19.76 664 N CYS A 279-17.573 78. 118 54. 455 1.00 21.59 665 CA CYS A 279-17.658 79. 020 55. 568 1.00 23.16 666 CB CYS A 279-18.18178. 35656. 8471.00 23.32 667 SG CYS A 279-19.851 77. 583 56. 864 1.00 23.91 668 C CYS A 279-16.331 79. 750 55. 853 1.00 24.21 669 0 CYS A 279-15.206 79. 227 55. 800 1.00 24.21 670 N SER A 280-16.520 81. 018 56. 178 1.00 25.34 671 CA SER A 280-15.422 81. 920 56. 574 1.00 26.15 672 CB SER A 280-14.924 82. 814 55. 553 1.00 28.26 673 OG SER A 280-15.715 83. 698 54. 880 1.00 28.85 674 C SER A 280-15.640 82. 369 58. 006 1.00 26.20 675 0 SER A 280-16.788 82. 385 58. 523 1.00 26.28 676 N GLY A 281-14.534 82. 572 58. 714 1.00 25.70 677 CA GLY A 281-14.523 82. 904 60. 133 1.00 25.02 678 C GLY A 281-15.424 84. 045 60. 518 1.00 24.57 679 O GLY A 281-15.303 85. 155 59. 962 1.00 25.21 680 N GLY A 282-16.275 83. 793 61. 481 1.00 23.94 681 CA GLY A 282-17.246 84. 673 62. 071 1.00 23.76 682 C GLY A 282-18.112 85. 504 61. 186 1.00 23.38 683 0 GLY A 282-18.608 86. 597 61. 594 1.00 23.66 684 N ALA A 283-18. 408 85. 018 59. 992 1. 00 22.70 685 CA ALA A 283-19.245 85. 682 59. 023 1.00 21.25 686 CB ALA A 283-18.978 85. 133 57. 616 1.00 21.20 687 C ALA A 283-20.720 85. 662 59. 276 1.00 20.89 688 0 ALA A 283-21.391 86. 638 58. 826 1.00 21.18 689 N TYR A 284-21.273 84. 649 59. 919 1.00 20.24 690 CA TYR A 284-22.723 84. 540 60. 158 1.00 18.98 691 CB TYR A 284-23.325 83. 413 59. 169 1.00 16.87 692 CG TYR A 284-23.203 83. 974 57. 785 1.00 15.28 693 CD1 TYR A 284-22.239 83. 529 56. 908 1.00 15.19 694 CE1 TYR A 284-22.145 84. 126 55. 628 1.00 15.20 695 CD2 TYR A 284-24.037 85. 004 57. 393 1.00 14.59 696 CE2 TYR A 284-23. 929 85.658 56.168 1. 00 13.82 697 CZ TYR A 284-22.969 85. 182 55. 283 1.00 14.85 698 OH TYR A 284-22.892 85. 743 54. 043 1.00 15.95 699 C TYR A 284-23.027 83. 932 61. 515 1.00 18.72 700 0 TYR A 284-22.247 83. 133 62. 018 1.00 18.85 701 N ASP A 285-24.191 84. 345 61. 995 1.00 19.34 702 CA ASP A 285-24.607 83. 777 63. 321 1.00 19.39 703 CB ASP A 285-25.443 84. 816 64. 031 1.00 20.24 704 CG ASP A 285-24.531 85. 981 64. 454 1.00 20.32 705 OD1 ASP A 285-24.742 87. 065 64. 025 1.00 20.62 706 OD2 ASP A 285-23. 699 85. 556 65. 315 1. 00 21.48 707 C ASP A 285-25.449 82. 526 63. 015 1.00 19.05 708 0 ASP A 285-25.361 81. 556 63. 766 1.00 19.50 709 N ILE A 286-26.230 82. 687 61. 958 1.00 18.54 710 CA ILE A 286-27.151 81. 569 61. 625 1.00 18.29 711 CB ILE A 286-28.650 82. 142 61. 617 1.00 18.69 712 CG2 ILE A 286-29.604 80. 892 61. 690 1.00 18.30 713 CG1 ILE A 286-29.012 83. 077 62. 751 1.00 19.56 714 CD1 ILE A 286-29.039 82. 554 64. 171 1.00 20.26 715 C ILE A 286-26.934 81. 142 60. 161 1.00 17.55 716 0 ILE A 286-26.775 82. 022 59. 333 1.00 17.54 717 N ILE A 287-27.079 79. 851 59. 918 1.00 17.30 718 CA ILE A 287-27.012 79. 375 58. 504 1.00 16.90 719 CB ILE A 287-25.733 78. 625 58. 111 1.00 16.86 720 CG2 ILE A 287-25.750 78. 057 56. 621 1.00 15.99 721 CG1 ILE A 287-24.469 79. 475 58. 365 1.00 16.19 722 CD1 ILE A 287-23.193 78. 624 58. 179 1.00 16.46 723 C ILE A 287-28. 260 78. 455 58. 330 1. 00 16.57 7240ILE A 287-28.428 77. 464 59. 006 1.00 16.56 725 N ILE A 288-29.140 78. 924 57. 466 1.00 16.81 726 CA ILE A 288-30.360 78. 158 57. 145 1.00 17.50 727 CB ILE A 288-31.532 79. 202 56. 897 1.00 17.33 728 CG2 ILE A 288-32.839 78. 483 56. 412 1.00 17.05 729 CG1 ILE A 288-31.790 79. 968 58. 238 1.00 16.40 730 CD1 ILE A 288-32.920 81. 043 58. 002 1.00 17.58 731 C ILE A 288-30.061 77. 401 55. 836 1.00 17.41 732 0 ILE A 288-29.807 78. 084 54. 832 1.00 17.80 733 N CYS A 289-30.153 76. 128 55. 870 1.00 18.00 734 CA CYS A 289-29.942 75. 251 54. 680 1.00 17.56 735 CB CYS A 289-29.146 74. 070 55. 005 1.00 17.39 736 SG CYS A 289-27.465 74. 043 55. 617 1.00 17.70 737 C CYS A 289-31.383 74. 915 54. 239 1.00 17.81 738 0 CYS A 289-32.013 73. 940 54. 737 1.00 17.88 739 N ASP A 290-31.913 75. 737 53. 383 1.00 17.54 740 CA ASP A 290-33.294 75. 642 52. 887 1. 00 17.85 741 CB ASP A 290-33.874 76. 980 52. 515 1. 00 16.44 742 CG ASP A 290-35.369 77. 029 52. 277 1. 00 17.04 743 OD1 ASP A 290-36.175 76. 393 52. 955 1. 00 16.22 744 OD2 ASP A 290-35.809 77. 714 51. 305 1. 00 17.19 745 C ASP A 290-33. 425 74. 494 51. 869 1. 00 17. 97 746 0 ASP A 290-32. 464 74. 065 51. 220 1. 00 18. 01 747 N GLU A 291-34. 648 73. 988 51. 811 1. 00 16. 95 748 CA GLU A 291-35. 061 72. 890 50. 958 1. 00 16. 07 749 CB GLU A 291-35. 020 73. 368 49. 491 1. 00 15. 20 750 CG GLU A 291-36. 003 74. 469 49. 126 1. 00 15. 21 751 CD GLU A 291-35.986 74. 891 47. 713 1. 00 17.68 752 OE1 GLU A 291-35.507 75. 943 47. 288 1. 00 17.49 753 OE2 GLU A 291-36.502 74. 016 46. 967 1. 00 18.79 754 C GLU A 291-34. 074 71. 754 51. 116 1. 00 15. 78 755 O GLU A 291-33. 651 71. 236 50. 091 1. 00 15. 69 756 N CYS A 292-33.790 71. 362 52. 341 1. 00 15.88 757 CA CYS A 292-32.883 70. 421 52. 809 1. 00 16.25 758 CB CYS A 292-32.468 70. 578 54. 276 1. 00 18.23 759 SG CYS A 292-33.665 69. 981 55. 491 1. 00 18.08 760 C CYS A 292-33.086 68. 950 52. 488 1. 00 16.10 761 O CYS A 292-32.161 68. 119 52. 750 1. 00 15.52 762 N HIS A 293-34.190 68. 658 51. 924 1. 00 15.62 763 CA HIS A 293-34.507 67. 232 51. 493 1. 00 15.77 764 CB HIS A 293-36.064 67. 180 51. 455 1. 00 15.36 765 CG HIS A 293-36.593 68. 234 50. 530 1. 00 15.79 766 CD2 HIS A 293-36.918 68. 123 49. 211 1. 00 15.45 767 ND1 HIS A 293-36. 791 69. 577 50. 859 1. 00 14. 79 768 CE1 HIS A 293-37.193 70. 207 49. 797 1. 00 13.76 769 NE2 HIS A 293-37.274 69. 374 48. 797.1.00 15.49 770 C HIS A 293-33.923 67. 037 50. 121 1. 00 16.61 771 O HIS A 293-33.999 65. 963 49. 520 1. 00 17.49 772 N SER A 294-33.281 68. 073 49. 545 1. 00 16.70 773 CA SER A 294-32.717 68. 041 48. 207 1. 00 17.48 774 CB SER A 294-32.271 69. 366 47. 644 1. 00 18.22 775 OG SER A 294-33.427 70. 229 47. 512 1. 00 18.84 776 C SER A 294-31.622 66. 998 48. 127 1. 00 17.99 777 O SER A 294-30.709 67. 008 48. 950 1. 00 17.68 778 N THR A 295-31.772 66. 136 47. 114 1. 00 18.28 779 CA THR A 295-30.810 65. 058 46. 931 1. 00 17.55 780 CB THR A 295-31.468 63. 630 47. 100 1. 00 16.93 781 OG1 THR A 295-32.393 63. 513 46. 003 1. 00 18.42 782 CG2 THR A 295-32.282 63. 555 48. 428 1. 00 17.59 783 C THR A 295-29.926 65. 224 45. 732 1. 00 17.49 784 O THR A 295-29.358 64. 254 45. 185 1. 00 18.08 785 N ASP A 296-29.744 66. 447 45. 283 1. 00 17.72 786 CA ASP A 296-28.778 66. 718 44. 183 1. 00 17.08 787 CB ASP A 296-29.108 67. 837 43. 302 1. 00 20.60 788 CG ASP A 296-29.516 69. 082 44. 040 1. 00 23.43 789 OD1 ASP A 296-28.718 69. 998 44. 282 1. 00 22.80 790 OD2 ASP A 296-30.740 69. 057 44. 355 1. 00 26.01 791 C ASP A 296-27.413 66. 797 44, 935 1. 00 15.42 7920ASP A 296-27.393 66. 974 46. 172 1. 00 15.23 793 N ALA A 297-26.383 66. 561 44. 174 1. 00 13.26 794 CA ALA A 297-25.040 66. 491 44. 666 1. 00 11.98 795 CB ALA A 297-24.198 65. 809 43. 600 1. 00 9.70 796 C ALA A 297-24.562 67. 790 45. 264 1. 00 12.29 797 O ALA A 297-23. 969 67. 793 46. 362 1. 00 12. 42 798 N THR A 298-24. 898 68. 905 44. 679 1. 00 12. 88 799 CA THR A 298-24. 509 70. 269 45. 185 1. 00 12. 82 800 CB THR A 298-24. 945 71. 350 44. 100 1. 00 12. 53 801 OG1 THR A 298-24. 276 70. 869 42. 891 1. 00 13. 88 802 CG2 THR A 298-24. 298 72. 778 44. 329 1. 00 12. 77 803 C THR A 298-25. 129 70. 518 46. 552 1. 00 13. 59 804 O THR A 298-24. 395 70. 894 47. 495 1. 00 13. 22 805 N SER A 299-26. 426 70. 162 46. 726 1. 00 14. 25 806 CA SER A 299-27. 112 70. 394 48. 011 1. 00 14. 13 807 CB SER A 299-28. 623 70. 206 47. 938 1. 00 13. 68 808 OG SER A 299 -29.079 70,907 46.777 1.00 14. 90 809 C SER A 299-26. 578 69. 522 49. 092 1. 00 14. 79 810 O SER A 299-26. 441 69. 977 50. 243 1. 00 15. 23 811 N ILE A 300-26. 306 68. 228 48. 775 1. 00 16. 26 <BR> <BR> 812 CA ILE A 300-25. 756 67. 298 49. 755 1. 00 15. 78 813 CB ILE A 300-25. 806 65. 818 49. 243 1. 00 18. 58 814 CG2 ILE A 300-24. 933 64. 816 50. 018 1. 00 18. 70 815 CG1 ILE A 300 -27.281 65.339 49.107 1.00 19. 15 816 CD1 ILE A 300-27. 532 63. 872 48. 637 1. 00 20. 35 817 C ILE A 300 -24.370 67.808 50.161 1.00 16. 67 818 O ILE A 300-24. 065 67. 837 51. 385 1. 00 16. 55 819 N LEU A 301-23. 521 68. 081 49. 171 1. 00 15. 97 820 CA LEU A 301-22. 169 68. 599 49. 413 1. 00 16. 31 821 CB LEU A 301-21. 389 68. 537 48. 111 1. 00 17. 13 822 CG LEU A 301 -19.870 68.757 48.164 1.00 16. 81 823 CD1 LEU A 301 -19.309 67.860 49.268 1.00 17. 77 824 CD2 LEU A 301-19. 285 68. 247 46. 819 1. 00 16. 99 825 C LEU A 301-22. 225 69. 934 50. 124 1. 00 16. 80 8260 LEU A301-21. 46970. 09251. 1231. 0017. 41 827 N GLY A 302-23. 151 70. 806 49. 746 1. 00 16. 25 828 CA GLY A 302-23. 330 72. 119 50. 386 1. 00 17. 36 829 C GLY A 302 -23.701 72.002 51.852 1.00 17. 38 830 O GLY A 302-23. 075 72. 593 52. 765 1. 00 18. 20 831 N ILE A 303-24. 720 71. 280 52. 171 1. 00 16. 92 832 CA ILE A 303-25. 250 70. 999 53. 499 1. 00 16. 60 833 CB ILE A 303 -26.517 70.115 53.404 1.00 15. 14 834 CG2 ILE A 303-26. 976 69. 543 54. 778 1. 00 15. 13 835 CG1 ILE A 303-27. 678 70. 819 52. 677 1. 00 15. 06 836 CD1 ILE A 303-28. 944 69. 878 52. 636 1. 00 17. 16 837 C ILE A 303-24. 179 70. 383 54. 372 1. 00 16. 56 <BR> <BR> 838 O ILE A 303-24. 050 70. 857 55. 501 1. 00 17. 08 839 N GLY A 304-23. 537 69. 335 53. 906 1. 00 16. 72 840 CA GLY A 304 -22.459 68.672 54.705 1.00 17. 01 841 C GLY A 304 -21.327 69.643 55.043 1.00 17. 96 842 0 GLY A 304-20. 639 69. 518 56. 085 1. 00 17. 15 843 N THR A 305-21. 015 70. 521 54. 051 1. 00 18. 12 844 CA THR A 305-19. 927 71. 493 54. 294 1. 00 19. 09 845 CB THR A 305-19. 676 72. 359 53. 000 1. 00 17. 89 846 OG1 THR A 305-19. 277 71. 411 51. 941 1. 00 16. 67 847 CG2 THR A 305-18. 576 73. 414 53. 234 1. 00 18. 68 848 C THR A 305-20. 343 72. 334 55. 502 1. 00 19. 94 849 O THR A 305-19. 557 72. 495 56. 472 1. 00 21. 48 850 N VAL A 306-21. 552 72. 824 55. 455 1. 00 19. 51 851 CA VAL A 306-22. 122 73. 632 56. 515 1. 00 19. 28 852 CB VAL A 306 -23.550 74.087 56.209 1.00 18. 61 853 CG1 VAL A 306 -24.178 74.825 57.421 1.00 19. 01 854 CG2 VAL A 306-23.707 74. 923 54. 971 1.00 17.91 855 C VAL A 306-21.985 72. 929 57. 855 1.00 19.54 8560 VAL A 306-21.526 73. 558 58. 833 1.00 20.04 857 N LEU A 307-22.465 71. 711 57. 899 1.00 19.46 858 CA LEU A 307-22.547 70. 904 59. 107 1.00 19.77 859 CB LEU A 307-23. 447 69.699 58.902 1. 00 19.33 860 CG LEU A 307-24.919 69. 888 58. 583 1.00 19.59 861 CD1 LEU A 307-25.604 68. 529 58. 209 1.00 18.76 862 CD2 LEU A 307-25.631 70. 304 59. 898 1.00 19.71 863 C LEU A 307-21.160 70. 701 59. 675 1.00 20.64 8640 LEU A 307-21.020 70. 769 60. 923 1.00 20.74 865 N ASP A 308-20.209 70. 561 58. 801 1.00 20.69 866 CA ASP A 308-18.798 70. 378 59. 248 1.00 21.96 867 CB ASP A 308-17. 999 69. 691 58. 114 1. 00 22.14 868 CG ASP A 308-16.536 69. 508 58. 509 1.00 23.36 869 OD1 ASP A 308-16.230 68. 842 59. 509 1.00 23.62 870 OD2 ASP A 308-15.692 70. 048 57. 776 1.00 23.54 871 C ASP A 308-18. 081 71. 655 59. 642 1. 00 22.23 872 O ASP A 308-17.204 71. 558 60. 524 1.00 22.92 873 N GLN A 309-18.368 72. 785 59. 003 1.00 22.47 874 CA GLN A 309-17.597 73. 982 59. 346 1.00 22.49 875 CB GLN A 309-17.144 74. 686 58. 071 1.00 22.13 876 CG GLN A 309-16.394 73. 882 57. 086 1.00 21.92 877 CD GLN A 309-16.101 74. 595 55. 804 1.00 20.76 878 OE1 GLN A 309-15.189 74. 183 55. 079 1.00 21.74 879 NE2 GLN A 309-16.885 75. 615 55. 460 1.00 19.60 880 C GLN A 309-18.305 75. 038 60. 148 1.00 22.92 881 0 GLN A 309-17.528 75. 988 60. 489 1.00 23.78 882 N ALA A 310-19.604 75. 013 60. 312 1.00 22.59 883 CA ALA A 310-20.351 76. 040 60. 971 1.00 22.93 884 CB ALA A 310-21.822 75. 951 60. 702 1.00 22.69 885 C ALA A 310-19.937 76. 362 62. 373 1.00 23.53 8860 ALA A 310-19.761 77. 559 62. 686 1.00 23.78 887 N GLU A 311-19.669 75. 379 63. 180 1.00 24.18 888 CA GLU A 311-19.270 75. 612 64. 578 1.00 25. 27 889 CB GLU A 311-19.308 74. 374 65. 421 1.00 26.64 890 CG GLU A 311-19.286 74. 527 66. 926 1.00 28.37 891 CD GLU A 311-19.285 73. 301 67. 771 1.00 29.53 892 OE1 GLU A 311-19.360 72. 141 67. 404 1.00 30.73 893 OE2 GLU A 311-19.158 73. 535 68. 985 1.00 30.52 894 C GLU A 311-17. 909 76. 273 64. 591 1. 00 25.62 895 O GLU A 311-17.714 77. 299 65. 311 1.00 26.43 896 N THR A 312-16. 989 75. 745 63. 819 1. 00 25.21 897 CA THR A 312-15.635 76. 305 63. 721 1.00 24.68 898 CB THR A 312-14.697 75. 465 62. 796 1.00 24.13 899 OG1 THR A 312-14.707 74. 118 63. 334 1.00 22.97 900 CG2 THR A 312-13.221 75. 953 62. 752 1.00 24.39 901 C THR A 312-15.759 77. 765 63. 329 1.00 24.55 902 O THR A 312-15.191 78. 638 63. 987 1.00 25.46 903 N ALA A 313-16.526 78. 073 62. 327 1.00 24.10 904 CA ALA A 313-16.784 79. 365 61. 782 1.00 23.78 905 CB ALA A 313-17.571 79. 256 60. 463 1.00 23.93 906 C ALA A 313-17.442 80. 401 62. 657 1.00 23.57 907 O ALA A 313-17.649 81. 540 62. 130 1.00 23.04 908 N GLY A 314-17.778 80. 077 63. 867 1.00 24.19 909 CA GLY A 314-18.445 81. 003 64. 771 1.00 24.62 910 C GLY A 314-19.946 81. 090 64. 661 1.00 24.62 911 0 GLY A 314-20.526 82. 033 65. 193 1.00 24.05 912 N ALA A 315-20.595 80. 123 64. 019 1.00 25.15 913 CA ALA A 315-22.035 80. 003 63. 868 1.00 25.07 914 CB ALA A 315-22.370 79. 003 62. 740 1.00 24.43 915 C ALA A 315-22.630 79. 427 65. 169 1.00 25.17 916 O ALA A 315-22.041 78. 526 65. 770 1.00 25.38 917 N ARG A 316-23.784 79. 917 65. 543 1.00 25.29 918 CA ARG A 316-24.556 79. 537 66. 704 1.00 26.59 919 CB ARG A 316-25.028 80. 828 67. 467 1.00 30.30 920 CG ARG A 316-23.779 81. 530 68. 008 1.00 33.91 921 CD ARG A 316-23.858 82. 934 68. 399 1.00 36.15 922 NE ARG A 316-24.805 83. 213 69. 443 1.00 38.82 923 CZ ARG A 316-25.040 84. 396 70. 013 1.00 39.43 924 NH1 ARG A 316-24.380 85. 500 69. 687 1.00 39.48 925 NH2 ARG A 316-26.032 84. 400 70. 921 1.00 40.14 926 C ARG A 316-25.732 78. 625 66. 377 1.00 26.02 927 O ARG A 316-26.232 77. 902 67. 250 1.00 26.15 928 N LEU A 317-26. 161 78.645 65.119 1. 00 24.89 929 CA LEU A 317-27.261 77. 771 64. 703 1.00 23.99 930 CB LEU A 317-28.571 78. 504 65. 116 1.00 22.93 931 CG LEU A 317-29.876 77. 786 64. 841 1.00 21.33 932 CD1 LEU A 317-30. 074 76. 509 65. 666 1. 00 20.43 933 CD2 LEU A 317-30.994 78. 786 65. 086 1.00 21.25 934 C LEU A 317-27.239 77. 469 63. 224 1.00 23.94 935 0 LEU A 317-27.056 78. 372 62. 377 1.00 23.82 936 N VAL A 318-27.482 76. 206 62. 970 1.00 24.31 937 CA VAL A 318-27.671 75. 568 61. 675 1.00 23.55 938 CB VAL A 318-26.697 74. 442 61. 364 1. 00 24.27 939 CG1 VAL A 318-27.048 73. 707 60. 041 1.00 24.28 940 CG2 VAL A 318-25.228 74. 799 61. 284 1.00 23.76 941 C VAL A 318-29.142 75. 056 61. 648 1.00 23.30 942 O VAL A 318-29.548 74. 129 62. 374 1.00 22.78 943 N VAL A 319-29.920 75. 649 60. 772 1.00 23.02 944 CA VAL A 319-31.332 75. 243 60. 604 1.00 22.35 945 CB VAL A 319-32.230 76. 482 60. 541 1.00 22.78 946 CG1 VAL A 319-33.703 76. 126 60. 254 1.00 22.09 947 CG2 VAL A 319-32.157 77. 307 61. 822 1.00 23.42 948 C VAL A 319-31.468 74. 391 59. 327 1.00 21.'66 949 O VAL A 319-31.174 74. 907 58. 243 1.00 21.72 950 N LEU A 320-31.940 73. 170 59. 492 1.00 20.78 951 CA LEU A 320-32.152 72. 326 58. 259 1.00 20.40 952 CB LEU A 320-31.620 70. 974 58. 656 1.00 19.45 953 CG LEU A 320-30.242 70. 890 59. 225 1.00 19.50 954 CD1 LEU A 320-29.965 69. 476 59. 707 1.00 20.10 955 CD2 LEU A 320-29.210 71. 225 58. 142 1.00 18.41 956 C LEU A 320-33.670 72. 434 58. 021 1.00 20.27 9570 LEU A 320-34.452 71. 790 58. 760 1.00 20.68 958 N ALA A 321-34.060 73. 260 57. 115 1.00 19.63 959 CA ALA A 321-35.436 73. 584 56. 758 1.00 19.60 960 CB ALA A 321-35.444 75. 110 56. 504 1.00 19.18 961 C ALA A 321-35.950 72. 921 55. 504 1.00 20.25 962 0 ALA A 321-35.290 72. 954 54. 476 1.00 19.74 963 N THR A 322-37.107 72. 235 55. 589 1.00 21.34 964 CA THR A 322-37.746 71. 576 54. 448 1.00 20.83 965 CB THR A 322-37.332 70. 077 54. 245 1.00 19.77 966 OG1 THR A 322-38.087 69. 680 53. 054 1.00 18.04 967 CG2 THR A 322-37.543 69. 183 55. 441 1.00 18.07 968 C THR A 322-39.256 71. 593 54. 680 1. 00 21.77 969 O THR A 322-39.648 71. 763 55. 848 1. 00 23.38 970 N ALA A 323-40.031 71. 403 53. 662 1. 00 22.09 971 CA ALA A 323-41.500 71. 362 53. 769 1. 00 22.33 972 CB ALA A 323-42.124 72. 118 52. 602 1. 00 22.28 973 C ALA A 323-41.913 69. 885 53. 640 1. 00 23.22 974 O ALA A 323-43.038 69. 448 54. 004 1. 00 24.39 975 N THR A 324-40. 980 69. 137 53. 090 1. 00 22. 57 976 CA THR A 324-41.131 67. 743 52. 819 1. 00 22.66 977 CB THR A 324-41.384 67. 533 51. 283 1. 00 22.42 978 OG1 THR A 324-40.211 68. 147 50. 656 1. 00 24.65 979 CG2 THR A 324-42.611 68. 304 50. 746 1. 00 20.99 980 C THR A 324-40.031 66. 891 53. 389 1. 00 23.23 981 O THR A 324-39.242 66. 336 52. 663 1. 00 23.20 982 N PRO A 325-40.035 66. 762 54. 711 1. 00 24.42 983 CA PRO A 325-39.121 65. 939 55. 439 1. 00 25.27 984 CB PRO A 325-39.605 66. 015 56. 891 1. 00 25.14 985 CG PRO A 325-40.751 66. 939 56. 958 1. 00 25.08 986 CD PRO A 325-41.017 67. 452 55. 603 1. 00 25.06 987 C PRO A 325-39.223 64. 450 54. 992 1. 00 26.29 988 O PRO A 325-40.290 63. 990 54. 546 1. 00 26.68 989 N PRO A 326-38.153 63. 736 55. 227 1. 00 26.78 990 CA PRO A 326-38.033 62. 319 54. 945 1. 00 27.74 991 CB PRO A 326-36.842 61. 883 55. 800 1. 00 27.44 992 CG PRO A 326-36.002 63. 101 55. 956 1. 00 27.72 993 CD PRO A 326-36.897 64. 288 55. 809 1. 00 27.45 994 C PRO A 326-39.283 61. 567 55. 480 1. 00 28.85 995 O PRO A 326-39.691 61. 757 56. 633 1. 00 29.01 996 N GLY A 327-39.855 60. 753 54. 631 1. 00 29.47 997 CA GLY A 327-41.052 59. 968 55. 008 1. 00 30.26 998 C GLY A 327-42.268 60. 859 55. 002 1. 00 30.77 999 0 GLY A 327-43.178 60. 693 55. 849 1. 00 31.23 1000 N SER A 328-42.251 61. 837 54. 081 1. 00 31.04 1001 CA SER A 328-43.457 62. 721 54. 007 1. 00 31.14 1002 CB SER A 328-43.131 64. 144 53. 568 1. 00 31.60 1003 OG SER A 328-42.775 64. 106 52. 185 1. 00 31.84 1004 C SER A 328-44.292 62. 064 52. 868 1. 00 30.75 1005 O SER A 328-43.757 61. 190 52. 178 1. 00 30.49 1006 N VAL A 329-45.492 62. 537 52. 746 1. 00 30.87 1007 CA VAL A 329-46.454 62. 106 51. 709 1. 00 31.10 1008 CB VAL A 329-47.283 60. 925 52. 273 1. 00 32.28 1009 CG1 VAL A 329-46. 516 59. 620 52. 314 1. 00 32. 50 1010 CG2 VAL A 329-47.621 61. 338 53. 747 1. 00 32.05 1011 C VAL A 329-47.340 63. 347 51. 522 1. 00 31.07 1012 0 VAL A 329-47.500 64. 010 52. 564 1. 00 31.58 1013 N THR A 330-47.870 63. 548 50. 386 1. 00 31. 02 1014 CA THR A 330-48.717 64. 656 50. 022 1. 00 31.60 1015 CB THR A 330-48.974 64. 696 48. 450 1. 00 32.08 1016 OG1 THR A 330-47.711 64. 385 47. 789 1. 00 32.85 1017 CG2 THR A 330-49.367 66. 126 47. 993 1. 00 32.46 1018 C THR A 330-50.105 64. 551 50. 701 1. 00 31.63 1019 0 THR A 330-50.820 63. 539 50. 626 1. 00 31.72 1020 N VAL A 331-50.488 65. 632 51. 273 1. 00 31.32 1021 CA VAL A 331-51.69265. 96952. 0181. 0030. 93 1022 CB VAL A 331-51. 160 66.597 53.354 1.00 32.31 1023 CG1 VAL A 331-52.206 67. 107 54. 326 1. 00 33. 60 1024 CG2 VAL A 331-50.262 65. 582 54. 037 1. 00 32.89 1025 C VAL A 331-52.500 66. 977 51. 220 1. 00 30.36 1026 0 VAL A 331-51.936 67. 848 50. 528 1. 00 30.08 1027 N PRO A 332-53.820 66. 866 51. 336 1. 00 30.02 1028 CA PRO A 332-54.758 67. 781 50. 663 1. 00 29.35 1029 CB PRO A 332-56.127 67. 344 51. 143 1. 00 29.66 1030 CG PRO A 332-55.846 66. 633 52. 444 1. 00 30.06 1031 CD PRO A 332-54.538 65. 858 52. 158 1. 00 29.94 1032 C PRO A 332-54.407 69. 228 51. 013 1. 00 28.65 1033 0 PRO A 332-54.084 69. 526 52. 178 1. 00 29.51 1034 N HIS A 333-54.492 70. 076 50. 047 1. 00 27.07 1035 CA HIS A 333-54.200 71. 535 50. 106 1. 00 25.93 1036HIS A 333-53.481 71. 883 48. 782 1. 00 25.76 1037 CG HIS A 333-52.730 73. 165 48. 717 1. 00 24.82 1038 ND1 HIS A 333-53.186 74. 416 48. 589 1. 00 23.94 1039 CE1 HIS A 333-52.187 75. 266 48. 515 1. 00 24.04 1040 NE2 HIS A 333-51.052 74. 579 48. 583 1. 00 24.80 1041 CD2 HIS A 333-51.347 73. 259 48. 718 1. 00 25.39 1042 C HIS A 333-55. 588 72.171 50.018 1.00 25. 46 10430HIS A 333-56.480 71. 477 49. 458 1. 00 25.39 1044 N PRO A 334-55.763 73. 327 50. 590 1. 00 25.39 1045 CA PRO A 334-57.035 74. 036 50. 619 1. 00 25.13 1046 CB PRO A 334-56.894 75. 056 51. 742 1. 00 25.17 1047 CG PRO A 334-55.506 74. 993 52. 234 1. 00 25.24 1048 CD PRO A 334-54.708 74. 107 51. 301 1. 00 25.49 1049 C PRO A 334-57.421 74. 715 49. 335 1. 00 25.14 10500PRO A 334-58.625 74. 975 49. 132 1. 00 25.67 1051 N ASN A 335-56.442 75. 051 48. 484 1. 00 24.94 1052 CA ASN A 335-56.759 75. 727 47. 210 1. 00 24.24 1053 CB ASN A 335-55.831 76. 942 47. 018 1. 00 26.61 1054 CG ASN A 335-55.873 78. 014 48. 080 1. 00 26.93 1055 OD1 ASN A 335-56.978 78. 511 48. 418 1. 00 29.04 1056 ND2 ASN A 335-54.709 78. 387 48. 592 1. 00 26.30 1057 C ASN A 335-56.644 74. 810 46. 009 1. 00 23.32 1058 O ASN A 335-57.110 75. 249 44. 910 1. 00 23.36 1059 N ILE A 336-56.022 73. 675 46. 152 1. 00 22.69 1060 CA ILE A 336-55.859 72. 711 45. 040 1. 00 22. 24 1061 CB ILE A 336-54.356 72. 203 45. 050 1. 00 19. 26 1062 CG1 ILE A 336-53.369 73. 392 45. 006 1. 00 16.70 1063 CD1 ILE A 336-51.850 72. 936 44. 977 1. 00 15.27 1064 CG2 ILE A 336-54.061 71. 254 43. 847 1. 00 18.80 1065 C ILE A 336-56.807 71. 535 44. 969 1. 00 23.11 1066 0 ILE A 336-56.791 70. 541 45. 732 1. 00 22.61 1067 N GLU A 337-57.579 71. 528 43. 883 1. 00 24.58 1068 CA GLU A 337-58.537 70. 436 43. 571 1. 00 25.79 1069 CB GLU A 337-59.815 70. 888 42. 907 1. 00 28.03 1070 CG GLU A 337-59.785 71. 713 41. 630 1. 00 31.76 1071 CD GLU A 337-61.040 72. 034 40. 893 1. 00 33.54 1072 OE1 GLU A 337-61.817 71. 236 40. 373 1. 00 33.23 1073 OE2 GLU A 337-61.227 73. 293 40. 843 1. 00 35.28 1074 C GLU A 337-57.865 69. 421 42. 631 1. 00 25.47 1075 0 GLU A 337-57.802 69. 729 41. 430 1. 00 25.28 1076 N GLU A 338-57.464 68. 290 43. 139 1. 00 25.46 1077 CA GLU A 338-56. 771 67. 215 42. 453 1. 00 25. 77 1078 CB GLU A 338-55.887 66. 493 43. 491 1. 00 26.93 1079 CG GLU A 338-54.897 67. 308 44. 316 1. 00 27.34 1080 CD GLU A 338-54.104 66. 603 45. 338 1. 00 28.75 1081 OE1 GLU A 338-53.171 65. 839 45. 092 1. 00 30.65 1082 OE2 GLUA 338-54.385 66. 797 46. 561 1.00 29.19 1083 C GLU A 338-57.557 66. 215 41. 661 1.00 25.68 1084 0 GLU A 338-57.930 65. 097 42. 092 1.00 25.62 1085 N VAL A 339-57.767 66. 481 40. 377 1.00 25.21 1086 CA VAL A 339-58.554 65. 724 39. 416 1.00 25. 03 1087 CB VAL A 339-59.257 66. 853 38. 540 1.00 24.28 1088 CG1 VAL A 339-60. 076 66. 377 37. 408 1. 00 24.54 1089 CG2 VAL A 339-59.927 67. 809 39. 447 1.00 24.15 1090 C VAL A 339-57. 915 64. 726 38. 520 1. 00 25.40 1091 0 VAL A 339-57.351 65. 154 37. 475 1.00 25.71 1092 N ALA A 340-58.091 63. 431 38. 787 1.00 24. 95 1093 CA ALA A 340-57.514 62. 371 37. 976 1.00 24.74 1094 CB ALA A 340-58.028 60. 973 38. 407 1.00 23.42 1095 C ALA A 340-57.903 62. 466 36. 504 1.00 25.08 1096 0 ALA A 340-59.127 62. 560 36. 249 1.00 25.71 1097 N LEU A 341-56.938 62. 365 35. 628 1.00 24.30 1098 CA LEU A 341-57.167 62. 328 34. 189 1.00 24.30 1099 CB LEU A 341-55.843 62. 466 33. 436 1.00 23.66 1100 CG LEU A 341-55.054 63. 726 33. 336 1.00 22. 90 1101 CD1 LEU A 341-53.929 63. 606 32. 354 1.00 21. 03 1102 CD2 LEU A 341-56.022 64. 839 32. 896 1.00 22.52 1103 C LEU A 341-57.807 60. 936 33. 845 1.00 24.45 1104 0 LEU A 341-57.442 59. 963 34. 539 1.00 24.44 1105 N SER A 342-58.583 60. 899 32. 792 1.00 24. 87 1106 CA SER A 342-59.183 59. 570 32. 393 1.00 25. 92 1107 CB SER A 342-60.719 59. 765 32. 409 1.00 25. 91 1108 OG SER A 342-60.957 60. 614 31. 280 1.00 27.77 1109 C SER A 342-58.751 59. 314 30. 952 1.00 26.18 1110 O SER A 342-57.832 59. 998 30. 493 1.00 25.82 1111 N THR A 343-59.415 58. 377 30. 249 1.00 26.59 1112 CA THR A 343-59.039 58. 100 28. 848 1.00 26.87 1113 CB THR A 343-59.106 56. 565 28. 463 1.00 27.33 1114 OG1 THR A 343-60.506 56. 194 28. 720 1.00 27.21 1115 CG2 THR A 343-58.150 55. 680 29. 246 1.00 27.21 1116 C THR A 343-59.714 58. 968 27. 828 1.00 26.47 1117 0 THR A 343-59.435 58. 889 26. 601 1.00 26.40 1118 N THR A 344-60.583 59. 874 28. 284 1.00 26.24 1119 CA THR A 344-61.300 60. 753 27. 375 1.00 25.63 1120 CB THR A 344-62.792 61. 034 27. 891 1.00 26. 10 1121 OG1 THR A 344-63.435 59. 717 28. 142 1.00 25.63 1122 CG2 THR A 344-63.561 61. 761 26. 781 1.00 25.88 1123 C THR A 344-60.558 62. 096 27. 265 1.00 25.55 1124 Q THR A 344-60.205 62. 668 28. 312 1.00 24.45 1125 N GLY A 345-60.357 62. 499 26. 031 1.00 25.76 1126 CA GLY A 345-59.667 63. 770 25. 687 1.00 26.27 1127 C GLY A 345-59. 052 63. 575 24. 296 1. 00 26. 98 1128 O GLY A 345 -58.849 62.428 23.868 1. 00 27. 05 1129 N GLU A 346-58.778 64. 652 23. 620 1.00 27.79 1130 CA GLU A 346-58.211 64. 740 22. 307 1.00 28. 06 1131 CB GLU A 346-58.119 66. 194 21. 779 1.00 29.28 1132 CG GLU A 346-59.360 66. 977 21. 479 1.00 30.62 1133 CD GLU A 346-60.371 67. 093 22. 562 1.00 30.26 1134 OE1 GLU A 346-60.335 66. 651 23. 689 1.00 28.92 1135 OE2 GLU A 346-61.373 67. 734 22. 129 1.00 32.76 1136 C GLU A 346-56.714 64. 383 22. 322 1.00 28.22 1137 0 GLU A 346-56.220 64. 087 21. 218 1.00 28.94 1138 N ILE A 347-56.102 64. 499 23. 479 1.00 27.61 1139 CA ILE A 347-54.655 64. 269 23. 589 1.00 27.12 1140 CB ILE A 347-54.106 65. 633 24. 252 1.00 28.35 1141 CG1 ILE A 347-54.591 66. 770 23. 335 1.00 28.34 1142 CD1 ILE A 347-54.43268. 19223. 9011.. 00 28.85 1143 CG2 ILE A 347-52.552 65. 592 24. 361 1.00 28.71 1144 C ILE A 347-54.218 63. 110 24. 397 1.00 26.49 1145 O ILE A 347-54.389 63. 109 25. 666 1.00 26.72 1146 N PRO A 348-53.629 62. 118 23. 747 1.00 25.89 1147 CA PRO A 348-53.053 60. 945 24. 427 1.00 25.22 1148 CB PRO A 348-52.379 60. 155 23. 281 1.00 26.06 1149 CG PRO A 348-52.979 60. 667 22. 022 1.00 26.29 1150 CD PRO A 348-53.364 62. 101 22. 290 1.00 26.26 1151 C PRO A 348-51.966 61. 508 25. 360 1.00 24.16 1152 0 PRO A 348-51.218 62. 417 24. 879 1.00 24.41 1153 N PHE A 349-51.912 61. 071 26. 584 1.00 22.61 1154 CA PHE A 349-50.945 61. 590 27. 586 1.00 21.14 1155 CB PHE A 349-51.465 62. 897 28. 252 1.00 20.31 1156 CG PHE A 349-50.593 63. 506 29. 323 1.00 19.70 1157 CD1 PHE A 349-49.406 64. 181 28. 906 1.00 18.59 1158 CE1 PHE A 349-48.568 64. 775 29. 850 1.00 17.05 1159 CZ PHE A 349-48.894 64. 737 31. 186 1.00 16.99 1160 CE2 PHE A 349-50.061 64. 032 31. 615 1.00 18.58 1161 CD2 PHE A 349-50.889 63. 426 30. 662 1.00 18.28 1162 C PHE A 349-50.708 60. 528 28. 655 1.00 20.76 1163 O PHE A 349-51.546 60. 314 29. 555 1.00 21.00 1164 N TYP A 350-49.570 59. 854 28. 554 1.00 19.87 1165 CA TYR A 350-49.126 58. 859 29. 496 1.00 19.41 1166 CB TYR A 350-48.549 59. 466 30. 785 1.00 17.31 1167 CG TYR A 350-47.269 60. 273 30. 469 1.00 17.52 1168 CD1 TYR A 350-46.011 59. 723 30. 687 1.00 16.47 1169 CE1 TYR A 350-44.848 60. 370 30. 344 1.00 15.65 1170 CZ TYR A 350-44.965 61. 667 29. 811 1.00 16.92 1171 OH TYR A 350-43.869 62. 365 29. 465 1.00 17.73 1172 CE2 TYR A 350-46.192 62. 243 29. 563 1.00 17.95 1173 CD2 TYR A 350-47.363 61. 513 29. 900 1.00 17.27 1174 C TYR A 350-50.130 57. 770 29. 825 1.00 19.69 1175 0 TYR A 350-50.073 57. 282 31. 000 1.00 19.98 1176 N GLY A 351-50.865 57. 355 28. 831 1.00 19.71 1177 CA GLY A 351-51.856 56. 262 29. 054 1.00 20.70 1178 C GLY A 351 -53.245 56.819 29.228 1. 00 21.17 1179 0 GLY A 351-54.217 56. 073 29. 043 1.00 22.51 1180 N LYS A 352-53.349 58. 077 29. 570 1.00 21.40 1181 CA LYS A 352-54.659 58. 742 29. 800 1.00 21.30 1182LYS A 352-54.589 59. 419 31. 162 1.00 22.37 1183 CG LYS A 352-54.246 58. 517 32. 295 1.00 21.59 1184 CD LYS A 352-55. 334 57.513 32.664 1. 00 22.80 1185 CE LYS A 352-54.830 56. 612 33. 765 1.00 23.63 1186LYS A 352-55.816 55. 656 34. 262 1.00 24.62 1187 C LYS A 352-54. 819 59. 762 28. 712 1. 00 20.95 1188 O LYS A 352-54.195 59. 579 27. 621 1.00 21.12 1189 N ALA A 353-55.606 60. 793 28. 959 1.00 20.81 1190 CA ALA A 353-55.722 61. 818 27. 858 1.00 20.93 1191 CB ALA A 353-56.891 61. 418 26. 971 1.00 22.15 1192 C ALA A 353-56. 005 63.183 28.484 1. 00 20.90 1193 0 ALA A 353-56.442 63. 255 29. 620 1.00 21.31 1194 N ILE A 354-55.82864. 20127. 6951.00 21.07 1195 CA ILE A 354-56.050 65. 592 28. 072 1.00 19.89 1196 CB ILE A 354-54.673 66. 398 27. 996 1.00 18.31 1197 CG1 ILE A 354-53.608 65. 845 28. 997 1.00 16.81 1198 CD1 ILE A 354-52.278 66. 642 28. 946 1.00 12.97 1199 CG2 ILE A 354-54.878 67. 912 28. 206 1.00 17.75 1200 C ILE A 354-57.100 66. 157 27. 136 1.00 20.33 1201 0 ILE A 354-56.861 66. 250 25. 922 1.00 21.25 1202 N PRO A 355-58.250 66. 528 27. 665 1.00 20.84 1203 CA PRO A 355-59.331 67. 126 26. 863 1.00 21.33 1204PRO A 355-60.464 67. 327 27. 883 1.00 21.38 1205PRO A 355-60.081 66. 640 29. 131 1.00 21.24 1206 CD PRO A 355-58.600 66. 407 29. 093 1.00 21.36 1207 C PRO A 355-58.840 68. 514 26. 462 1.00 22.18 1208 0 PRO A 355-58.340 69. 192 27. 395 1.00 22.20 1209 N LEU A 356-59.004 68. 936 25. 261 1.00 23.12 1210 CA LEU A 356-58. 553 70. 288 24. 884 1. 00 24.49 1211LEU A 356-58.671 70. 360 23. 364 1.00 26.37 1212 CG LEU A 356-58.347 71. 670 22. 667 1.00 27.79 1213 CD1 LEU A 356-58.377 71. 469 21. 141 1.00 27.55 1214 CD2 LEU A 356-59.452 72. 684 23. 018 1.00 28.36 1215 C LEU A 356-59.224 71. 382 25. 685 1.00 25.62 12160LEU A 356-58.639 72. 468 25. 982 1.00 25.50 1217 N GLU A 357-60.514 71. 225 26. 021 1.00 26.08 1218 CA GLU A 357-61.159 72. 339 26. 729 1.00 26.20 1219 CB GLU A 357-62.652 72. 396 26. 706 1.00 28.92 1220 CG GLU A 357-63.574 71. 376 27. 206 1.00 30.72 1221 CD GLU A 357-63.595 70. 906 28. 608 1.00 32.59 1222 OE1 GLU A 357-63.922 69. 725 28. 883 1.00 34.28 1223 OE2 GLU A 357-63.336 71. 731 29. 512 1.00 32.48 1224 C GLU A 357-60.555 72. 632 28. 076 1.00 25.22 12250GLU A 357-60.900 73. 713 28. 622 1.00 25.51 1226 N VAL A 358-59.679 71. 754 28. 606 1.00 23.72 1227 CA VAL A 358-59.138 72. 023 29. 944 1.00 22.85 1228VAL A 358-58.970 70. 851 30. 861 1.00 20. 68 1229 CG1 VAL A 358-60.194 69. 990 31. 152 1.00 19.60 1230 CG2 VAL A 358-57.745 69. 967 30. 646 1.00 18.83 1231 C VAL A 358-57.965 72. 989 29. 899 1.00 23.16 12320VAL A 358-57.666 73. 594 30. 934 1.00 23.52 1233 N ILE A 359-57.371 73. 157 28. 765 1.00 23.60 1234 CA ILE A 359-56.212 73. 975 28. 488 1.00 24.34 1235 CB ILE A 359-54.972 73. 023 28. 195 1.00 23.56 1236 CG1 ILE A 359-55.235 72. 263 26. 863 1.00 23.57 1237 CD1 ILE A 359-54.077 71. 311 26. 493 1.00 23.59 1238 CG2 ILE A 359-54.709 72. 022 29. 326 1.00 22.70 1239 C ILE A 359-56.430 74. 928 27. 335 1.00 25.11 1240 O ILE A 359-55.458 75. 598 26. 947 1.00 25.18 1241 N LYS A 360-57.666 75. 065 26. 852 1.00 25.94 1242 CA LYS A 360-57.917 75. 973 25. 722 1.00 26.94 1243 CB LYS A 360-59.222 75. 669 24. 984 1.00 29.44 1244 CG LYS A 360-59.312 76. 363 23. 650 1.00 31.14 1245 CD LYS A 360-60.669 76. 281 22. 930 1.00 31.93 1246 CE LYS A 360-60.532 76. 768 21. 486 1.00 32.06 1247 NZ LYS A 360-59.934 78. 130 21. 372 1.00 31.19 1248 C LYS A 360-57.795 77. 439 26. 054 1.00 27.13 1249 O LYS A 360-57.468 78. 254 25. 116 1.00 28.19 1250 N GLY A 361-57. 97977. 84827. 2911. 00 25.79 1251 CA GLY A 361-57.802 79. 291 27. 668 1.00 23.75 1252 C GLY A 361-57.109 79. 255 29. 024 1.00 22.15 1253 0 GLY A 361-57.048 78. 151 29. 573 1.00 22.70 1254 N GLY A 362-56.610 80. 380 29. 521 1.00 21.34 1255 CA GLY A 362-55.935 80. 347 30. 871 1.00 20.09 1256 C GLY A 362-54.472 79. 999 30. 644 1.00 19.10 1257 0 GLY A 362-54.077 79. 910 29. 471 1.00 20.04 1258 N ARG A 363-53.702 79. 840 31. 676 1.00 18.25 1259 CA ARG A 363-52.271 79. 544 31. 699 1.00 16.70 1260 CB ARG A 363-51.566 80. 677 32. 532 1.00 15.73 1261 CG ARG A 363-51.750 82. 031 31. 806 1.00 16.77 1262 CD ARG A 363-51.146 83. 065 32. 687 1.00 17.01 1263 NE ARG A 363-49.776 82. 969 33. 004 1.00 17.78 1264 CZ ARG A 363-48.710 83. 249 32. 230 1.00 18.72 1265 NH1 ARG A 363-48.765 83. 638 30. 987 1.00 18.89 1266 NH2 ARG A 363-47.525 83. 301 32. 879 1.00 20.38 1267 C ARG A 363-52.037 78. 263 32. 464 1.00 16.12 1268 O ARG A 363-52.264 78. 214 33. 679 1.00 17.23 1269 N HIS A 364-51.639 77. 201 31. 774 1.00 15.25 1270 CA HIS A 364-51.467 75. 896 32. 424 1.00 13.09 1271 CB HIS A 364-52.493 74. 859 31. 718 1.00 12.93 1272 CG HIS A 364-53.910 75. 503 31. 707 1.00 12.28 1273 ND1 HIS A 364-54.751 75. 414 32. 721 1.00 11.74 1274 CE1 HIS A 364-55.862 76. 101 32. 407 1.00 13.83 1275 NE2 HIS A 364-55.757 76. 586 31. 166 1.00 13.25 1276 CD2 HIS A 364-54.472 76. 185 30. 751 1.00 12.57 1277 C HIS A 364-50.065 75. 391 32. 128 1.00 12.44 1278 0 HIS A 364-49.466 75. 710 31. 094 1.00 13.98 1279 N, LEU A 365-49.510 74. 610 32. 978 1.00 12.22 1280 CA LEU A 365-48.227 73. 943 32. 945 1.00 10.88 1281 CB LEU A 365-47.462 74. 253 34. 204 1.00 11.91 1282 CG LEU A 365-46.261 73. 380 34. 603 1.00 13.51 1283 CD1 LEU A 365-45.227 73. 242 33. 516 1.00 12.69 1284 CD2 LEU A 365-45.620 73. 966 35. 836 1.00 14.58 1285 C LEU A 365-48.527 72. 393 32. 923 1.00 11.01 1286 O LEU A 365-49.157 71. 930 33. 862 1.00 11.18 1287 N ILE A 366-47.803 71. 748 32. 018 1.00 10.86 1288 CA ILE A 366-47.944 70. 237 31. 930 1.00 10.37 1289 CB ILE A 366-48. 492 69. 938 30. 487 1. 00 5.83 1290 CG1 ILE A 366-49.855 70. 729 30. 267 1.00 4.79 1291 CD1 ILE A 366-50.332 70. 320 28. 801 1.00 4.71 1292 CG2 ILE A 366-48.813 68. 381 30. 316 1.00 6.30 1293 C ILE A 366-46.483 69. 775 32. 154 1.00 11.27 12940 ILE A 366-45.618 70. 320 31. 441 1.00 10.79 1295 N PHE A 367-46.290 68. 815 33. 009 1.00 12.11 1296 CA PHE A 367-44.974 68. 233 33. 319 1.00 12.37 1297 CB PHE A 367-44.683 68. 009 34. 797 1.00 12.56 1298 CG PHE A 367-44.324 69. 166 35. 676 1.00 14.01 1299 CD1 PHE A 367-45.249 69. 809 36. 498 1.00 16.42 1300 CE1 PHE A 367-44.899 70. 926 37. 258 1.00 16.25 1301 CZ PHE A 367-43.567 71. 365 37. 229 1.00 14.43 1302 CE2 PHE A 367-42.637 70. 820 36. 361 1.00 13.44 1303 CD2 PHE A 367-43.055 69. 690 35. 596 1.00 14.13 1304 C PHE A 367-44.748 66. 985 32. 488 1.00 12.54 1305 O PHE A 367-45.585 66. 048 32. 630 1.00 11.43 1306 N CYS A 368-43.581 66. 918 31. 813 1.00 12.47 1307 CA CYS A 368-43.298 65. 696 30. 984 1.00 12. 57 1308 CB CYS A 368-43.362 66. 075 29. 547 1.00 12.81 1309 SG CYS A 368-44.845 66. 450 28. 680 1.00 14.25 1310 C CYS A 368-41.950 65. 075 31. 418 1. 00 12.63 1311 O CYS A 368-41.161 65. 847 32. 027 1. 00 12.16 1312 N HIS A 369-41.792 63. 783 31. 295 1. 00 12.30 1313 CA HIS A 369-40.540 63. 076 31. 748 1. 00 12.07 1314 CB HIS A 369-40.735 61. 492 31. 788 1. 00 11.73 1315 CG HIS A 369-40.585 60. 761 30. 487 1. 00 11.45 1316 ND1 HIS A 369-41.422 60. 610 29. 434 1. 00 12.21 1317 CE1 HIS A 369-40.826 59. 986 28. 429 1. 00 11.49 1318 NE2 HIS A 369-39.614 59. 605 28. 831 1. 00 10.68 1319 CD2 HIS A 369-39.480 60. 049 30. 105 1. 00 11.34 1320 C HIS A 369-39.327 63. 386 30. 879 1. 00 13.10 1321 O HIS A 369-38.116 63. 038 31. 266 1. 00 14.49 1322 N SER A 370-39.451 63. 926 29. 710 1. 00 13.07 1323 CA SER A 370-38.396 64. 194 28. 772 1. 00 13.34 1324 CB SER A 370-38.038 63. 028 27. 868 1. 00 11.92 1325 OG SER A 370-38.963 62. 823 26. 875 1. 00 12.51 1326 C SER A 370-38.587 65. 424 27. 911 1. 00 13.59 1327 O SER A 370-39.720 65. 928 27. 608 1. 00 13.54 1328 N LYS A 371-37.448 65. 901 27. 433 1. 00 13.46 1329 CA LYS A 371-37.380 67. 056 26. 550 1. 00 13.32 1330LYS A 371-36.090 67. 695 26. 316 1. 00 15.56 1331 CG LYS A 371-34.998 67. 087 25. 459 1. 00 17.90 1332 CD LYS A 371-33.851 68. 122 25. 354 1. 00 19.14 1333 CE LYS A 371-32.722 67. 707 24. 434 1. 00 21.96 1334 NZ LYS A 371-31.551 68. 665 24. 619 1. 00 21.68 1335 C LYS A 371-38. 064 66. 692 25. 240 1. 00 13. 75 13360LYS A 371-38.878 67. 480 24. 686 1. 00 13.17 1337 N LYS A 372-37.880 65. 466 24. 775 1. 00 14.02 1338 CA LYS A 372-38.490 65. 004 23. 527 1. 00 13.84 1339 CB LYS A 372-37.964 63. 713 22. 971 1. 00 15.98 1340 CG LYS A 372-36.529 63. 574 22. 683 1. 00 18.07 1341 CD LYS A 372-35.802 64. 461 21. 784 1. 00 20.81 1342 CE LYS A 372-36.167 64. 641 20. 365 1. 00 23.26 1343 NZ LYS A 372-35.082 65. 378 19. 609 1. 00 25.18 1344 C LYS A 372-40.011 65. 002 23. 543 1. 00 13.24 1345 O LYS A 372-40.609 65. 321 22. 545 1. 00 13.24 1346 N LYS A 373-40.566 64. 606 24. 623 1. 00 14.16 1347 CA LYS A 373-41.998 64. 458 24. 935 1. 00 15.26 1348 CB LYS A 373-42.167 63. 904 26. 360 1. 00 17.61 1349 CG LYS A 373-43.459 63. 117 26. 513 1. 00 18.76 1350 CD LYS A 373-44.710 63. 771 25. 964 1. 00 22.40 1351 CE LYS A 373-45.739 62. 597 25. 772 1. 00 23.75 1352LYS A 373-44.889 61. 536 25. 061 1. 00 24.85 1353 C LYS A 373-42.523 65. 886 24. 944 1. 00 14.55 1354 O LYS A 373-43.570 66. 215 24. 374 1. 00 16.19 1355 N CYS A 374-41.757 66. 741 25. 624 1. 00 13.67 1356 CA CYS A 374-42.051 68. 154 25. 657 1. 00 13.51 1357 CB CYS A 374-41.117 69. 072 26. 410 1. 00 9.91 1358 SG CYS A 374-41.127 68. 827 28. 095 1. 00 11.30 1359 C CYS A 374-42.248 68. 639 24. 231 1. 00 13.22 1360 O CYS A 374-43.258 69. 256 23. 910 1. 00 12.76 1361 N ASP A 375-41. 265 68. 365 23. 401 1. 00 14. 41 1362 CA ASP A 375-41. 294 68. 788 22. 010 1. 00 15. 71 1363 CB ASP A 375-40. 121 68. 409 21. 141 1. 00 16. 65 1364 CG ASP A 375-38. 790 68. 949 21. 545 1. 00 17. 99 1365 OD1 ASP A 375-37.772 68. 372 21. 170 1. 00 18.05 1366 OD2 ASP A 375-38.774 69. 927 22. 365 1. 00 18.59 1367 C ASP A 375-42.563 68. 291 21. 293 1.00 16.93 1368 O ASP A 375-43.109 69. 036 20. 494 1.00 16.66 1369 N GLU A 376-42.760 66. 975 21. 472 1.00 17.92 1370 CA GLU A 376-43.891 66. 354 20. 749 1.00 19.39 1371 CB GLU A 376-43.975 64. 847 20. 998 1.00 22.81 1372 CG GLUA 376-45.163 64. 237 20. 207 1.00 28.03 1373 CD GLU A 376-45.439 62. 819 20. 585 1.00 31.76 1374 OE1 GLU A 376 -46.511 62.403 20.977 1. 00 33.50 1375 OE2 GLU A 376-44. 392 62. 120 20. 476 1. 00 33.87 1376 C GLU A 376-45.228 66. 934 21. 161 1.00 19.31 1377 O GLU A 376-46. 087 67. 178 20. 298 1. 00 19.36 1378 N LEU A 377-45.396 67. 077 22. 474 1.00 18.78 1379 CA LEU A 377-46.634 67. 622 23. 021 1.00 18.42 1380 CB LEU A 377-46.771 67. 154 24. 479 1.00 18.99 1381 CG LEUA 377-48.028 67. 694 25. 174 1.00 19.70 1382 CD1 LEU A 377-49. 243 67. 242 24. 364 1. 00 19.88 1383 CD2 LEU A 377-48. 022 67. 159 26. 577 1. 00 19.99 1384 C LEU A 377-46.893 69. 026 22. 671 1.00 18.09 1385 O LEU A 377-48.041 69. 327 22. 259 1.00 19.22 1386 N ALA A 378-45.967 69. 975 22. 757 1.00 17.02 1387 CA ALA A 378-46. 173 71. 369 22. 427 1. 00 16.57 1388 CB ALA A 378 -45.029 72.261 22.825 1. 00 15.78 1389 CALA A 378-46.517 71. 565 20. 964 1.00 16.72 1390 O ALA A 378-47.332 72. 445 20. 650 1.00 17.20 1391 N ALA A 379-45.931 70. 821 20. 080 1.00 17.15 1392 CA ALA A 379-46. 182 70. 867 18. 652 1. 00 17.52 1393 CB ALA A 379-45. 125 70. 008 17. 969 1. 00 18.77 1394 CALA A 379-47.611 70. 382 18. 381 1.00 18.53 1395 O ALA A 379-48. 245 70.905 17.469 1. 00 18.45 1396 N LYS A 380-48.134 69. 457 19. 193 1.00 19.97 1397 CA LYS A 380-49.540 69. 004 18. 988 1.00 20.81 1398 CB LYS A 380-49.851 67. 630 19. 557 1.00 23.76 1399 CG LYS A 380-51.352 67. 210 19. 153 1.00 26.28 1400 CD LYS A 380-51.343 67. 338 17. 604 1.00 28.02 1401 CE LYS A 380-52.634 67. 176 16. 879 1.00 29.64 1402 NZ LYS A 380-53.227 65. 824 17. 085 1.00 30.71 1403 C LYS A 380-50.511 70. 074 19. 405 1.00 20.88 14040LYS A 380-51.565 70. 370 18. 730 1.00 21.08 1405 N LEU A 381-50.211 70. 732 20. 508 1.00 20.58 1406 CA LEU A 381-51.072 71. 823 21. 011 1.00 20.15 1407 CB LEU A 381-50.652 72. 228 22. 416 1.00 18.83 1408 CG LEU A 381-50.715 71. 106 23. 456 1.00 17.77 1409 CD1 LEU A 381-50. 238 71. 566 24. 816 1. 00 17.33 1410 CD2 LEU A 381-52. 102 70. 555 23. 463 1. 00 19.63 1411 C LEU A 381-51.034 72. 897 19. 952 1.00 20.91 1412 O LEU A 381-52.087 73. 497 19. 615 1.00 21.73 1413 N VAL A 382-49.852 73. 167 19. 455 1.00 20.58 1414 CA VAL A 382-49.667 74. 191 18. 421 1.00 20.50 1415 CB VAL A 382-48.211 74. 580 18. 200 1.00 19.13 1416 CG1 VAL A 382 -47.993 75.434 16.963 1. 00 18.55 1417 CG2 VAL A 382-47. 509 75. 187 19. 387 1. 00 17.01 1418 C VAL A 382-50.482 73. 836 17. 194 1.00 21.29 1419 O VAL A 382-51.069 74. 733 16. 568 1.00 21.90 1420 N ALA A 383-50. 525 72.588 16.813 1. 00 22.11 1421 CA ALA A 383-51. 292 72. 177 15. 605 1. 00 23.11 1422 CB ALA A 383-50. 804 70. 810 15. 212 1. 00 23.28 1423 C ALA A 383-52.775 72. 379 15. 842 1.00 23.84 14240 ALA A 383-53.580 72. 666 14. 907 1. 00 24.47 1425 N LEU A 384-53.234 72. 211 17. 062 1. 00 23.69 1426 CA LEU A 384-54.604 72. 377 17. 494 1. 00 23.06 1427 CB LEU A 384-54.819 71. 485 18. 730 1. 00 23.10 1428 CG LEU A 384-54.729 69. 994 18. 510 1. 00 22.36 1429 CD1 LEU A 384-54.736 69. 162 19. 757 1. 00 21.53 1430 CD2 LEU A 384-55.811 69. 635 17. 503 1. 00 22.20 1431 C LEU A 384-54.921 73. 822 17. 780 1. 00 23.69 1432 O LEU A 384-56.040 74. 068 18. 287 1. 00 24.31 1433 N GLY A 385-54.018 74. 776 17. 547 1. 00 23.44 1434 CA GLY A 385-54.416 76. 175 17. 847 1. 00 22.69 1435 C GLY A 385-54.220 76. 702 19. 213 1. 00 22.49 1436 O GLY A 385-54.652 77. 869 19. 518 1. 00 22.93 1437 N ILE A 386-53.549 75. 994 20. 098 1. 00 22.01 1438 CA ILE A 386-53.213 76. 440 21. 446 1. 00 21.87 1439 CB ILE A 386-53.294 75. 190 22. 392 1. 00 23.58 1440 CG1 ILE A 386-54.701 74. 573 22. 292 1. 00 24.30 1441 CD1 ILE A 386-54.927 73. 240 23. 042 1. 00 25.20 1442 CG2 ILE A 386-52.754 75. 429 23. 799 1. 00 23.19 1443 C ILE A 386-51. 805 77. 061 21. 462 1. 00 21. 59 1444 0 ILE A 386-50.833 76. 620 20. 798 1. 00 20.73 1445 N ASN A 387-51.713 78. 158 22. 208 1. 00 21.77 1446 CA ASN A 387-50.386 78. 825 22. 361 1. 00 21.26 1447 CB ASN A 387-50.610 80. 211 23. 007 1. 00 22.95 1448 CG ASN A 387-49.284 80. 961 23. 098 1. 00 23.29 1449 OD1 ASN A 387-48.430 80. 757 22. 213 1. 00 23.86 1450 ND2 ASN A 387-49. 124 81.835 24.073 1.00 23. 33 1451 C ASN A 387-49.654 77. 940 23. 372 1. 00 20.73 1452 O ASN A 387-49.923 78. 125 24. 551 1. 00 20.94 1453 N ALA A 388-48. 769 77.095 22.887 1.00 19. 68 1454 CA ALA A 388-47. 979 76. 189 23. 685 1. 00 18. 49 1455 CB ALA A 388-48.448 74. 738 23. 475 1. 00 16.27 1456 C ALA A 388-46.499 76. 407 23. 402 1. 00 17.11 1457 O ALA A 388-46.031 76. 735 22. 279 1. 00 17.64 1458 N VAL A 389-45.701 76. 292 24. 449 1. 00 16.51 1459 CA VAL A 389-44.270 76. 400 24. 462 1. 00 14.49 1460 CB VAL A 389-43. 684 77.748 24.904 1.00 13. 74 1461 CG1 VAL A 389-43. 81878. 82023. 9171. 0015. 31 1462 CG2 VAL A 389 -44.053 78.095 26.349 1.00 12. 94 1463 C VAL A 389-43.610 75. 283 25. 305 1. 00 14.55 1464 O VAL A 389-44. 066 75. 109 26. 404 1. 00 14. 75 1465 N ALA A 390-42.570 74. 716 24. 775 1. 00 13.96 1466 CA ALA A 390 -41.846 73.671 25.558 1.00 13. 77 1467 CB ALA A 390-41.570 72. 469 24. 714 1. 00 13.33 1468 C ALA A 390-40.656 74. 316 26. 197 1. 00 13.73 14690 ALA A 390-39.967 75. 114 25. 504 1. 00 13.72 1470 N TYR A 391-40.447 74. 046 27. 479 1. 00 14.18 1471 CA TYR A 391-39.217 74. 578 28. 172 1. 00 14.96 1472 CB TYR A 391-39.567 75. 719 29. 141 1. 00 16.69 1473 CG TYR A 391-38.390 76. 105 30. 012 1. 00 17.60 1474 CD1 TYR A 391-37.394 76. 967 29. 537 1. 00 18.66 1475 CE1 TYR A 391-36.293 77. 273 30. 354 1. 00 19.78 1476 CZ TYR A 391-36.211 76. 744 31. 629 1. 00 20.93 1477 OH TYR A 391 -35.115 76.995 32.475 1.00 22. 05 1478 CE2 TYR A 391-37.199 75. 884 32. 109 1. 00 18.60 1479 CD2 TYR A 391-38. 277 75. 580 31. 290 1. 00 18. 22 1480 C TYR A 391-38.526 73. 467 28. 913 1. 00 14.56 1481 O TYR A 391-39.156 72. 602 29. 548 1. 00 15.35 1482 N TYR A 392-37.171 73. 484 28. 846 1. 00 13.79 1483 CA TYR A 392-36.311 72. 532 29. 537 1. 00 13.05 1484 CB TYR A 392-36.295 71. 139 28. 893 1. 00 10.41 1485 CG TYR A 392-36.240 71. 131 27. 392 1. 00 9.07 1486 CD1 TYR A 392-35. 188 71.258 26.556 1.00 3. 82 1487 CE1 TYR A 392-35.329 71. 207 25. 199 1. 00 6.53 1488 CZ TYR A 392-36.580 70. 983 24. 615 1. 00 8.28 1489 OH TYR A 392-36.746 70. 806 23. 273 1. 00 10.87 1490 CE2 TYR A 392-37.677 70. 757 25. 416 1. 00 8.63 1491 CD2 TYR A 392-37.564 70. 844 26. 802 1. 00 8.35 1492 C TYR A 392-34.887 73. 034 29. 596 1. 00 13.25 1493 O TYR A 392-34.584 74. 062 29. 028 1. 00 12.60 1494 N ARG A 393-34.030 72. 174 30. 184 1. 00 13.65 1495 CA ARG A 393-32.616 72. 555 30. 281 1. 00 13.97 1496 CB ARG A 393-31.767 71. 472 30. 902 1. 00 17.17 1497 CG ARG A 393-30.309 71. 836 31. 000 1. 00 22.51 1498 CD ARG A 393-29.548 70. 668 31. 529 1. 00 26.79 1499 NE ARG A 393-28.141 70. 890 31. 602 1. 00 31.15 1500 CZ ARG A 393-27.300 70. 000 32. 148 1. 00 34.23 1501 NH1 ARG A 393-27.702 68. 873 32. 719 1. 00 35.20 1502 NH2 ARG A 393-25.977 70. 202 32. 002 1. 00 36.17 1503 C ARG A 393-31.966 72. 939 28. 979 1. 00 13.26 1504 0 ARG A 393-32. 064 72. 306 27. 913 1. 00 12. 65 1505 N GLY A 394-31.283 74. 089 29. 059 1. 00 13.67 1506 CA GLY A 394-30.569 74. 634 27. 876 1. 00 14.00 1507 C GLY A 394-31.290 75. 749 27. 175 1. 00 14.80 1508 O GLY A 394-30.656 76. 505 26. 369 1. 00 15.74 1509 N LEU A 395-32.578 75. 910 27. 435 1. 00 14.06 1510 CA LEU A 395-33.344 77. 026 26. 811 1. 00 13.87 1511 CB LEU A 395-34.714 76. 417 26. 340 1. 00 11.13 1512 CG LEU A 395-34.654 75. 268 25. 397 1. 00 10.45 1513 CD1 LEU A 395-36.049 74. 868 24. 841 1. 00 8.24 1514 CD2 LEU A 395-33.808 75. 525 24. 127 1. 00 11.81 1515 C LEU A 395-33.391 78. 140 27. 806 1. 00 14.19 1516 O LEU A 395-32.940 78. 015 28. 986 1. 00 13.94 1517 N ASP A 396-33.880 79. 284 27. 371 1. 00 15.56 1518 CA ASP A 396-34.017 80. 534 28. 163 1. 00 15.98 1519 CB ASP A 396-33.818 81. 691 27. 161 1. 00 17.27 1520 CG ASP A 396-33.686 83. 030 27. 837 1. 00 19.64 1521 OD1 ASP A 396-34.026 83. 143 29. 027 1. 00 20.72 1522 OD2 ASP A 396-33. 324 83.983 27.128 1.00 21. 44 1523 C ASP A 396-35.453 80. 564 28. 730 1. 00 17.04 1524 0 ASP A 396-36.394 80. 326 27. 981 1. 00 17.57 1525 N VAL A 397-35. 596 80.808 29.985 1.00 17. 82 1526 CA VAL A 397-36.838 80. 887 30. 715 1. 00 18.49 1527 CB VAL A 397-36. 694 80. 913 32. 222 1. 00 21. 42 1528 CG1 VAL A 397-36.048 82. 157 32. 817 1. 00 23.37 1529 CG2 VAL A 397-37.969 80. 548 32. 924 1. 00 23.29 1530 C VAL A 397-37.738 81. 963 30. 105 1. 00 17.93 1531 0 VAL A 397-38. 955 81. 827 30. 266 1. 00 18. 16 1532 N SER A 398-37.168 82. 933 29. 444 1. 00 16.91 1533 CA SER A 398-37. 799 84. 037 28. 799 1. 00 15. 61 1534 CB SER A 398-36.947 85. 168 28. 327 1. 00 15.72 1535 OG SER A 398-36.154 85. 777 29. 328 1. 00 16.27 1536 C SER A 398-38.756 83. 594 27. 698 1. 00 15.16 1537 0 SER A 398-39. 540 84. 456 27. 261 1. 00 14-85 1538 N VAL A 399-38.725 82. 321 27. 313 1.00 15.19 1539 CA VAL A 399-39.626 81. 741 26. 337 1.00 14.98 1540VAL A 399-39.209 80. 419 25. 745 1.00 16.57 1541 CG1 VAL A 399-37.888 80. 487 24. 926 1.00 15.18 1542 CG2 VAL A 399-38.973 79. 278 26. 759 1.00 16.84 1543 C VAL A 399-41.060 81. 684 26. 956 1.00 15.77 1544 0 VAL A 399-42.024 81. 607 26. 166 1.00 15.44 1545 N ILE A 400-41.133 81. 584 28. 248 1.00 16.58 1546 CA ILE A 400-42.502 81. 575 28. 884 1.00 18.41 1547 CB ILE A 400-42.344 80. 952 30. 330 1.00 18.62 1548 CG1 ILE A 400-41.619 79. 601 30. 223 1.00 16.95 1549 CD1 ILE A 400-41.204 78. 909 31. 549 1.00 14.47 1550 CG2 ILE A 400-43.727 80. 780 31. 022 1.00 20. 00 1551 C ILE A 400-42. 916 83. 026 28. 993 1. 00 20.07 15520ILE A 400-42.242 83. 841 29. 639 1.00 20.70 1553 N PRO A 401-43.989 83. 387 28. 295 1.00 21.30 1554 CA PRO A 401-44.560 84. 739 28. 348 1.00 21.34 1555 CB PRO A 401-45.649 84. 678 27. 287 1.00 21.08 1556 CG PRO A 401-46.094 83. 250 27. 351 1.00 21.20 1557 CD PRO A 401-44.808 82. 449 27. 474 1.00 21.34 1558 C PRO A 401-45.091 84. 906 29. 752 1.00 22.15 1559 O PRO A 401-45.685 83. 956 30. 354 1.00 22.72 1560 N THR A 402-44.905 86. 055 30. 370 1.00 22. 62 1561 CA THR A 402-45.387 86. 275 31. 739 1.00 22.69 1562 CB THR A 402-44.425 87. 009 32. 699 1.00 24.48 1563 OG1 THR A 402-43.927 88. 200 31. 965 1.00 24.93 1564 CG2 THR A 402-43.246 86. 108 33. 197 1.00 24.97 1565 C THR A 402-46.863 86. 560 31. 820 1.00 22.47 1566 0 THR A 402-47.440 86. 457 32. 940 1.00 22.74 1567 N SER A 403-47.462 86. 802 30. 676 1.00 22.38 1568 CA SER A 403-48.914 87. 049 30. 565 1.00 22.68 1569 CB SER A 403-49.110 88. 595 30. 574 1.00 24.96 1570 OG SER A 403-48.317 89. 057 29. 481 1.00 27.96 1571 C SER A 403-49.470 86. 493 29. 258 1.00 21.80 1572 0 SER A 403-48.788 86. 208 28. 276 1.00 21.40 1573 N GLY A 404-50.809 86. 325 29. 281 1.00 21.24 1574 CA GLY A 404-51.596 85. 789 28. 172 1.00 20.00 1575 C GLY A 404-51.861 84. 311 28. 438 1.00 19.46 1576 0 GLY A 404-51.203 83. 760 29. 346 1.00 20.70 1577 N ASP A 405-52.725 83. 719 27. 682 1.00 18.49 1578 CA ASP A 405-53.032 82. 280 27. 779 1.00 18.27 1579 CB ASP A 405-54.138 81. 928 26. 757 1.00 19.47 1580 CG ASP A 405-55.457 82. 602 27. 164 1.00 20.87 1581 OD1 ASP A 405-55.729 82. 909 28. 297 1.00 20.42 1582 OD2 ASP A 405-56.179 82. 869 26. 184 1.00 23.07 1583 C ASP A 405-51.728 81. 574 27. 272 1.00 17.37 1584 0 ASP A 405-51.173 82. 167 26. 387 1.00 16.19 1585 N VAL A 406-51.415 80. 430 27. 847 1.00 17.57 1586 CA VAL A 406-50.226 79. 684 27. 375 1.00 17.61 1587 CB VAL A 406-48.863 80. 280 27. 692 1.00 19.89 1588 CG1 VAL A 406-48.498 80. 258 29. 191 1.00 19.98 1589 CG2 VAL A 406-47.708 79. 682 26. 864 1.00 20.19 1590 C VAL A 406-50.380 78. 304 28. 087 1.00 17.24 1591 0 VAL A 406-51.046 78. 244 29. 094 1.00 16.86 1592 N VAL A 407-49.749 77. 371 27. 415 1.00 16.09 1593 CA VAL A 407-49.647 76. 013 27. 939 1.00 15.67 1594 CB VAL A 407-50.509 75. 033 27. 116 1.00 14.74 1595 CG1 VAL A 407-50.459 73. 605 27. 635 1.00 14.28 1596 CG2 VAL A 407-51.999 75. 469 27. 184 1.00 14.02 1597 C VAL A 407-48.106 75. 787 27. 769 1.00 15.45 1598 0 VAL A 407-47.661 75. 803 26. 641 1.00 14.87 1599 N VAL A 408-47.450 75. 789 28. 901 1.00 15.51 1600 CA VAL A 408-45.958 75. 507 28. 863 1.00 14.72 1601VAL A 408-45.381 76. 198 30. 118 1.00 16.14 1602 CG1 VAL A 408-43.948 75. 899 30. 375 1.00 16.92 1603 CG2 VAL A 408-45.586 77. 724 29. 935 1.00 17.61 1604 C VAL A 408-45.911 73. 979 29. 070 1.00 13.33 1605 O VAL A 408-46.597 73. 575 29. 963 1.00 12.16 1606 N VAL A 409-44.963 73. 351 28. 348 1.00 12.62 1607 CA VAL A 409-44.761 71. 897 28. 419 1.00 11.26 1608VAL A 409-45.101 71. 347 27. 020 1.00 9.92 1609 CG1 VAL A 409-45.186 69. 814 27. 020 1.00 10.21 1610 CG2 VAL A 409-46.554 71. 766 26. 595 1.00 9.14 1611 C VAL A 409-43.238 71. 793 28. 792 1.00 11.05 1612 0 VAL A 409-42.449 72. 215 27. 953 1.00 9.47 1613 N ALA A 410-43.018 71. 345 30. 019 1.00 10.61 1614 CA ALA A 410-41.683 71. 251 30. 571 1.00 11.40 1615 CB ALA A 410-41.582 72. 615 31. 406 1.00 11.39 1616 C ALA A 410-41.280 70. 115 31. 421 1.00 10.69 1617 0 ALA A 410-42.067 69. 222 31. 892 1.00 10.72 1618 N THR A 411-39.967 69. 887 31. 580 1.00 10.58 1619 CA THR A 411-39.396 68. 874 32. 417 1.00 11.28 1620 CB THR A 411-37.946 68. 386 31. 941 1.00 10.89 1621 OG1 THR A 411-37.250 69. 692 31. 856 1.00 12.26 1622 CG2 THR A 411-37.967 67. 637 30. 627 1.00 7.89 1623 C THR A 411-39.222 69. 608 33. 778 1.00 11.46 1624 0 THR A 411-39.691 70. 729 33. 772 1.00 10.69 1625 N ASP A 412-38.718 68. 906 34. 791 1.00 11.94 1626 CA ASP A 412-38. 546 69. 478 36. 089 1. 00 13.01 1627ASP A 412-38.072 68. 587 37. 228 1.00 14.41 1628 CG ASP A 412-39.095 67. 415 37. 461 1.00 15.72 1629 OD1 ASP A 412-38.647 66. 401 37. 939 1.00 16.46 1630 OD2 ASP A 412-40.247 67. 739 37. 244 1.00 16.23 1631 C ASP A 412-37.613 70. 729 36. 061 1.00 13.86 16320ASP A 412-37.601 71. 332 37. 133 1.00 12.61 1633 N ALA A 413-36.874 70. 921 34. 991 1.00 15.32 1634 CA ALA A 413-35.996 72. 117 34. 919 1.00 16.12 1635 CB ALA A 413-35.189 72. 132 33. 642 1.00 17.60 1636 C ALA A 413-36.814 73. 374 35. 061 1.00 17.14 1637 O ALA A 413-36.258 74. 481 35. 331 1.00 18.36 1638 N LEU A 414-38.109 73. 332 34. 827 1.00 17.24 1639 CA LEU A 414-39.018 74. 474 35. 008 1.00 17.29 1640LEU A 414-40.442 74. 011 34. 773 1.00 17.94 1641 CG LEU A 414-41.637 74. 915 35. 050 1.00 18.77 1642 CD1 LEU A 414-41.787 75. 365 36. 482 1.00 17.29 1643 CD2 LEU A 414-41.543 76. 084 34. 091 1.00 18.83 1644 C LEU A 414-38.878 74. 987 36. 479 1.00 16.94 16450LEU A 414-38.716 76. 216 36. 741 1.00 16.02 1646 N MET A 415-38.970 74. 076 37. 382 1.00 16.33 1647 CA MET A 415-38.916 74. 314 38. 815 1.00 17.73 1648 CB MET A 415-39.292 73. 062 39. 615 1.00 18.42 1649 CG MET A 415-40.766 72. 714 39. 342 1.00 18.08 1650MET A 415-41. 213 71. 315 40. 430 1. 00 18.52 1651 CE MET A 415-40.183 69. 992 39. 909 1.00 16.29 1652 C MET A 415-37. 634 74. 971 39. 259 1. 00 19.04 1653 0 MET A 415-37. 614 75. 743 40. 233 1. 00 18.96 1654 N THR A 416-36. 519 74. 618 38. 591 1. 00 19.83 1655 CA THR A 416-35. 230 75. 238 38. 976 1. 00 19.75 1656 CB THR A 416-34. 041 74. 233 38. 898 1. 00 19.89 1657 OG1 THR A 416-33. 714 73. 973 37. 518 1. 00 20.01 1658 CG2 THR A 416-34. 456 72. 849 39. 481 1. 00 20.00 1659 C THR A 416-35. 079 76. 612 38. 386 1. 00 19.67 1660 0 THR A 416-34. 412 77. 499 38. 991 1. 00 20.37 1661 N GLY A 417-35. 656 76. 948 37. 229 1. 00 18.90 1662 CA GLY A 417-35. 545 78. 210 36. 618 1. 00 18.95 1663 C GLY A 417-36. 677 79. 201 36. 584 1. 00 18.70 1664 O GLY A 417-36. 394 80. 380 36. 235 1. 00 17.80 1665 N TYR A 418-37. 893 78. 743 36. 820 1. 00 17.26 1666 CA TYR A 418-39. 063 79. 675 36. 701 1. 00 17.98 1667 CB TYR A 418-39. 894 79. 287 35. 501 1. 00 16.72 1668 CG TYR A 418-41. 168 80. 049 35. 275 1. 00 17.44 1669 CD1 TYR A 418-42. 411 79. 582 35. 668 1. 00 17.40 1670 CE1 TYR A 418-43. 578 80. 330 35. 385 1. 00 18.84 1671 CZ TYR A 418-43. 457 81. 548 34. 718 1. 00 18.65 1672 OH TYR A 418-44. 510 82. 312 34. 378 1. 00 21.07 1673 CE2 TYR A 418-42. 228 81. 983 34. 230 1. 00 18. 52 1674 CD2 TYR A 418-41. 098 81. 226 34. 542 1. 00 18.40 1675 C TYR A 418-39. 736 79. 837 38. 016 1. 00 18.65 1676 O TYR A 418-39. 784 78. 863 38. 776 1. 00 18.73 1677 N THR A 419-40. 145 81. 093 38. 340 1. 00 20.10 1678 CA THR A 419-40. 744 81. 309 39. 657 1. 00 20.89 1679 CB THR A 419-40. 069 82. 505 40. 483 1. 00 21.69 1680 OG1 THR A 419-40. 387 83. 732 39. 806 1. 00 23.37 1681 CG2 THR A 419-38. 535 82. 336 40. 590 1. 00 20.18 1682 C THR A 419-42. 236 81. 408 39. 702 1. 00 21.02 1683 O THR A 419-42. 747 81. 453 40. 858 1. 00 21.80 1684 N GLY A 420 -42.907 81.477 38.587 1. 00 20.17 1685 CA GLY A 420-44. 320 81. 582 38. 463 1. 00 19.84 1686 C GLY A 420-45. 118 80. 265 38. 652 1. 00 19.79 1687 0 GLY A 420-44. 602 79. 147 38. 555 1. 00 18.72 1688 N ASP A 421-46. 402 80. 565 38. 851 1. 00 19.61 1689 CA ASP A 421-47. 469 79. 603 39. 061 1. 00 20.26 1690 CB ASP A 421-48. 069 79. 683 40. 431 1. 00 21.77 1691 CG ASP A 421-48. 672 81. 055 40. 732 1. 00 23.24 1692 OD1 ASP A 421-49. 277 81. 707 39. 889 1. 00 24.34 1693 OD2 ASP A 421-48. 460 81. 424 41. 906 1. 00 25.02 1694 C ASP A 421-48. 470 79. 632 37. 907 1. 00 19.24 1695 0 ASP A 421-48. 434 80. 506 37. 016 1. 00 19.47 1696 N PHE A 422-49. 340 78. 602 37. 912 1. 00 17.98 1697 CA PHE A 422-50. 323 78. 516 36. 807 1. 00 17.09 1698 CB PHE A 422-49. 826 77. 531 35. 789 1. 00 16.45 1699 CG PHE A 422-48. 416 77. 714 35. 284 1. 00 15.37 1700 CD1 PHE A 422-48. 238 78. 332 34. 048 1. 00 16.08 1701 CE1 PHE A 422-46. 953 78. 483 33. 506 1. 00 15.47 1702 CZ PHE A 422-45. 864 78. 070 34. 290 1. 00 14.60 1703 CE2 PHE A 422-46. 036 77. 547 35. 569 1. 00 15.56 1704 CD2 PHE A 422-47. 348 77. 340 36. 055 1. 00 14.30 1705 C PHE A 422-51. 720 78. 154 37. 360 1. 00 16.33 1706 O PHE A 422-51. 828 77. 795 38. 525 1. 00 17.00 1707 N ASP A 423-52. 683 78. 228 36. 501 1. 00 15.96 1708 CA ASP A 423-54. 109 77. 961 36. 689 1. 00 15.53 1709 CB ASP A 423-54.917 78. 368 35. 467 1. 00 16.79 1710 CG ASP A 423-54.957 79. 843 35. 201 1. 00 18.30 1711 OD1 ASP A 423-55.265 80. 379 34. 121 1. 00 19.17 1712 OD2 ASP A 423-54.612 80. 431 36. 242 1. 00 19.04 1713 C ASP A 423-54.325 76. 451 36. 993 1. 00 15.50 1714 O ASP A 423-55.177 76. 177 37. 841 1. 00 15.09 1715 N SER A 424-53.523 75. 627 36. 287 1. 00 13.50 1716 CA SER A 424-53.612 74. 172 36. 537 1. 00 13.94 1717 CB SER A 424-54.537 73. 438 35. 639 1. 00 13.22 1718 OG SER A 424-54.233 73. 628 34. 274 1. 00 15.52 1719 C SER A 424-52.193 73. 614 36. 256 1. 00 14.28 17200 SERA 424-51.465 74. 314 35. 569 1. 00 15.04 1721 N VAL A 425-51.964 72. 490 36. 817 1. 00 14.03 1722 CA VAL A 425-50.697 71. 727 36. 608 1. 00 12.98 1723 CB VAL A 425-49.923 71. 722 37. 929 1. 00 10.91 1724 CG1 VAL A 425-48.773 70. 709 37. 880 1. 00 10.37 1725 CG2 VAL A 425-49.273 73. 102 38. 190 1. 00 11.71 1726 C VAL A 425-51.145 70. 280 36. 247 1. 00 13.78 1727 0 VAL A 425-51.851 69. 680 37. 064 1. 00 13.91 1728 N ILE A 426-50.768 69. 847 35. 053 1. 00 14.12 1729 CA ILE A 426-51.110 68. 418 34. 677 1. 00 13.13 1730 CB ILE A 426-51.540 68. 439 33. 162 1. 00 11.37 1731 CG1 ILE A 426-52.616 69. 492 32. 897 1. 00 10.60 1732 CD1 ILE A 426-53.149 69. 553 31. 448 1. 00 10.71 1733 CG2 ILE A 426-52.039 66. 986 32. 749 1. 00 9.82 1734 C ILE A 426-49.798 67. 633 34. 875 1. 00 13.29 17350 ILE A 426-48.797 67. 942 34. 198 1. 00 13.40 1736 N ASP A 427-49.747 66. 612 35. 686 1. 00 13.57 1737 CA ASP A 427-48.509 65. 854 35. 937 1. 00 14.02 1738 CB ASP A 427-48.428 65. 854 37. 503 1. 00 12.65 1739 CG ASP A 427-47.091 65. 328 37. 934 1. 00 12.88 1740 OD1 ASP A 427-46.390 64. 884 37. 030 1. 00 14.27 1741 OD2 ASP A 427-46.750 65. 248 39. 147 1. 00 14.16 1742 C ASP A 427-48.470 64. 491 35. 261 1. 00 14.92 1743 O ASP A 427-49.471 63. 764 35. 289 1. 00 14.38 1744 N CYS A 428-47.323 64. 076 34. 648 1. 00 15.86 1745 CA CYS A 428-47.243 62. 725 34. 031 1. 00 15.87 1746 CB CYS A 428-46.203 62. 643 32. 913 1. 00 16.84 1747 SG CYS A 428-44.540 63. 029 33. 476 1. 00 13.86 1748 C CYS A 428-46.967 61. 726 35. 113 1. 00 17.26 1749 0 CYS A 428-47.076 60. 484 34. 880 1. 00 17.54 1750 N ASN A 429-46.638 62. 215 36. 300 1. 00 17.36 1751 CA ASN A 429-46.389 61. 335 37. 444 1. 00 18. 48 1752 CB ASN A 429-47.697 60. 532 37. 694 1. 00 17.57 1753 CG ASN A 429-48.859 61. 376 38. 142 1. 00 15.98 1754 OD1 ASN A 429-49. 856 61. 585 37. 453 1. 00 16. 66 1755 ND2 ASN A 429-48.728 62. 070 39. 270 1. 00 18.38 1756 C ASN A 429-45.202 60. 417 37. 246 1. 00 19.75 1757 0 ASN A 429-45.092 59. 392 37. 952 1. 00 19.75 1758 N THR A 430-44.392 60. 741 36. 300 1. 00 20.88 1759 CA THR A 430-43.165 59. 973 35. 966 1. 00 21. 94 1760 CB THR A 430-43.224 59. 476 34. 480 1. 00 22.99 1761 OG1 THR A 430-44.369 58. 592 34. 332 1. 00 24.55 1762 CG2 THR A 430-41.980 58. 729 34. 042 1. 00 23.29 1763 C THR A 430-41.954 60. 880 36. 152 1. 00 22.50 1764 O THR A 430-42.013 62. 091 35. 888 1. 00 21.70 1765 N CYS A 431-40.872 60. 293 36. 637 1. 00 23.69 1766 CA CYS A 431-39.617 61. 010 36. 860 1.00 24.37 1767 CB CYS A 431-39.411 61. 177 38. 400 1.00 27.36 1768 SG CYS A 431-40.839 61. 889 39. 181 1.00 30.48 1769 C CYS A 431-38.423 60. 092 36. 484 1.00 23.87 1770 O CYS A 431-38.384 59. 006 37. 015 1.00 23.76 1771 N VAL A 432-37.558 60. 631 35. 674 1.00 23.77 1772 CA VAL A 432-36.333 59. 847 35. 287 1.00 23.62 1773 CB VAL A 432-35.924 60. 292 33. 877 1.00 22.72 1774 CG1 VAL A 432-34. 634 59. 548 33. 503 1. 00 22.95 1775 CG2 VAL A 432-37.004 59. 933 32. 891 1.00 20.72 1776 C VAL A 432-35.281 60. 099 36. 355 1.00 23.19 1777 O VAL A 432-35.272 61. 214 36. 925 1.00 22.83 1778 N THR A 433-34.429 59. 124 36. 624 1.00 23.22 1779 CA THR A 433-33.406 59. 370 37. 672 1.00 23.20 1780 CB THR A 433-34.105 59. 074 39. 072 1.00 23.59 1781 OG1 THR A 433-33.155 59. 674 40. 004 1.00 25.41 1782 CG2 THR A 433-34.273 57. 586 39. 379 1.00 22.78 1783 C THR A 433-32.149 58. 547 37. 427 1.00 22.23 1784 O THR A 433-32.201 57. 565 36. 703 1.00 21.62 1785 N GLN A 434-31.038 58. 924 38. 026 1.00 22.37 1786 CA GLN A 434-29.753 58. 208 37. 833 1.00 21.83 1787 CB GLN A 434-28.492 58. 999 37. 742 1.00 23.21 1788 CG GLN A 434-28.088 59. 911 36. 667 1.00 24.32 1789 CD GLN A 434-26.578 60. 198 36. 803 1.00 23.56 1790 OE1 GLN A 434-25.941 60. 126 35. 801 1.00 23.41 1791 NE2 GLN A 434-26.126 60. 552 37. 998 1.00 24.63 1792 C GLN A 434-29.501 57. 123 38. 870 1.00 21.48 1793 0 GLN A 434-29.701 57. 432 40. 060 1.00 22.03 1794 N THR A 435-28.880 56. 019 38. 400 1.00 20.51 1795 CA THR A 435-28.533 54. 890 39. 277 1.00 19.28 1796 CB THR A 435-29.555 53. 645 39. 275 1.00 18.60 1797 OG1 THR A 435-29.624 53. 203 37. 865 1.00 18.37 1798 CG2 THR A 435-30.996 53. 937 39. 716 1.00 18.84 1799 C THR A 435-27.129 54. 390 38. 934 1.00 18.62 1800 O THR A 435-26.655 54. 619 37. 795 1.00 19.98 1801 N VAL A 436-26.435 53. 773 39. 833 1.00 17.80 1802 CA VAL A 436-25.132 53. 155 39. 580 1.00 17.17 1803 CB VAL A 436-24.097 53. 076 40. 668 1.00 14.96 1804 CG1 VAL A 436-22.768 52. 580 40. 115 1.00 14.17 1805 CG2 VAL A 436-23.963 53. 853 41. 895 1.00 15.93 1806 C VAL A 436-25.574 51. 576 39. 588 1.00 17.76 1807 0 VAL A 436-26.232 51. 259 40. 533 1.00 18.13 1808 N ASP A 437-25.136 50. 899 38. 605 1.00 18.82 1809 CA ASP A 437-25.411 49. 409 38. 651 1.00 20.23 1810 CB ASP A 437-25.975 48. 862 37. 367 1.00 22.33 1811 CG ASP A 437-26.325 47. 373 37. 501 1.00 23.44 1812 OD1 ASP A 437-26.850 46. 820 36. 535 1.00 25.84 1813 OD2 ASP A 437-26. 086 46.787 38.561 1. 00 24.17 1814 C ASP A 437-23.986 48. 864 38. 932 1.00 19.75 1815 0 ASP A 437-23.094 49. 198 38. 116 1.00 19.85 1816 N PHE A 438-23.861 48. 148 40. 030 1.00 20. 09 1817 CA PHE A 438-22. 453 47. 573 40. 260 1. 00 20.46 1818 CB PHE A 438-22.121 47. 391 41. 706 1.00 20.17 1819 CG PHE A 438-22.054 48. 624 42. 548 1.00 21.42 1820 CD1 PHE A 438-21.041 49. 567 42. 252 1.00 21.55 1821 CE1 PHE A 438-20.938 50. 737 42. 982 1.00 21.62 1822 CZ PHE A 438-21.861 51. 006 43. 989 1.00 21.52 1823 CE2 PHE A 438-22.880 50. 099 44. 283 1. 00 23.08 1824 CD2 PHE A 438-22.964 48. 896 43. 536 1. 00 21.45 1825 C PHE A 438-22.417 46. 314 39. 390 1. 00 21.51 1826 O PHE A 438-22.634 45. 175 39. 857 1. 00 21.81 1827 N SER A 439-22.216 46. 464 38. 126 1. 00 21.81 1828 CA SER A 439-22.189 45. 496 37. 083 1. 00 23.16 1829 CB SER A 439-22.170 46. 339 35. 746 1. 00 24.39 1830 OG SER A 439-23.361 47. 083 35. 782 1. 00 26.03 1831 C SER A 439-21.110 44. 443 36. 983 1. 00 23.78 1832 O SER A 439-21.430 43. 306 36. 588 1. 00 23.67 1833 N LEU A 440-19.873 44. 793 37. 269 1. 00 24.12 1834 CA LEU A 440-18.727 43. 869 37. 179 1. 00 24.51 1835 CB LEU A 440-18.955 42. 728 38. 153 1. 00 24.58 1836 CG LEU A 440-18.947 43. 170 39. 621 1. 00 25.27 1837 CD1 LEU A 440-19.251 42. 050 40. 583 1. 00 24.52 1838 CD2 LEU A 440-17.563 43. 726 39. 925 1. 00 26.94 1839 C LEU A 440-18.420 43. 573 35. 753 1. 00 24.61 18400 LEUA 440-17.668 42. 625 35. 422 1. 00 25.61 1841 N ASP A 441-18.847 44. 432 34. 846 1. 00 24. 68 1842 CA ASP A 441-18.611 44. 305 33. 418 1. 00 24.77 1843 CB ASP A 441-19.962 44. 117 32. 700 1. 00 25.18 1844 CG ASP A 441-20.880 45. 336 32. 952 1. 00 25.57 1845 OD1 ASP A 441-20.519 46. 310 33. 642 1. 00 24.02 1846 OD2 ASP A 441-22.012 45. 201 32. 438 1. 00 26.45 1847 C ASP A 441-17.765 45. 339 32. 719 1. 00 24.75 1848 O ASP A 441-18.213 45. 869 31. 656 1. 00 25.45 1849 N PRO A 442-16.561 45. 681 33. 136 1. 00 24.12 1850 CA PRO A 442-15.889 45. 127 34. 288 1. 00 23.74 1851 CB PRO A 442-14.418 45. 328 33. 929 1. 00 23.73 1852 CG PRO A 442-14.360 46. 508 33. 041 1. 00 23.93 1853 CD PRO A 442-15.732 46. 639 32. 397 1. 00 23.94 1854 C PRO A 442-16.180 45. 764 35. 608 1. 00 23.52 1855 0 PRO A 442-16.083 45. 028 36. 611 1. 00 24.01 1856 N THR A 443-16.477 47. 080 35. 620 1. 00 22.01 1857 CA THR A 443-16.712 47. 746 36. 913 1. 00 20.65 1858 CB THR A 443-15.626 48. 916 37. 021 1. 00 19.14 1859 OG1 THR A 443-15.734 49. 620 35. 745 1. 00 18.65 1860 CG2 THR A 443-14.181 48. 400 37. 227 1. 00 18.06 1861 C THR A 443-18.108 48. 073 37. 319 1. 00 20.36 1862 O THR A 443-18.788 47. 355 38. 084 1. 00 19.61 1863 N PHE A 444-18.578 49. 279 36. 953 1. 00 20.25 1864 CA PHE A 444-19.911 49. 779 37. 263 1. 00 19.16 1865 CB PHE A 444-20.169 50. 592 38. 541 1. 00 18.83 1866 CG PHE A 444-19.326 51. 831 38. 584 1. 00 19.07 1867 CD1 PHE A 444-19.745 53. 017 37. 991 1. 00 19.17 1868 CE1 PHE A 444-18.970 54. 160 37. 972 1. 00 18.18 1869 CZ PHE A 444-17.678 54. 103 38. 609 1. 00 18.64 1870 CE2 PHE A 444-17.227 52. 930 39. 179 1. 00 17.66 1871 CD2 PHE A 444-18.066 51. 795 39. 190 1. 00 19.14 1872 C PHE A 444-20.467 50. 494 36. 039 1. 00 19.03 1873 0 PHE A 444-19.765 50. 768 35. 056 1. 00 19.13 1874 N THR A 445-21.762 50. 815 36. 246 1. 00 18.84 1875 CA THR A 445-22.487 51. 509 35. 155 1. 00 19.46 1876 CB THR A 445-23.629 50. 467 34. 638 1. 00 20.26 1877 OG1 THR A 445-22.860 49. 340 34. 187 1. 00 21.66 1878 CG2 THR A 445-24.562 51. 114 33. 660 1. 00 19.40 1879 C THR A 445-23. 319 52. 648 35. 730 1. 00 19. 23 1880 0 THR A 445-24. 004 52. 384 36. 736 1. 00 19. 27 1881 N ILE A 446-23.253 53. 767 35. 070 1. 00 19.41 1882 CA ILE A 446-24.114 54. 883 35. 481 1. 00 19.19 1883 CB ILE A 446-23.386 56. 238 35. 692 1. 00 16.05 1884 CG1 ILE A 446-22.235 56. 027 36. 741 1. 00 14.21 1885 CD1 ILE A 446-22.695 55. 660 38. 132 1. 00 15.05 1886 CG2 ILE A 446-24.424 57. 244 36. 306 1. 00 15.25 1887 C ILE A 446-25.250 54. 960 34. 474 1. 00 20.15 1888 0 ILE A 446-24.990 55. 110 33. 257 1. 00 20.61 1889 N GLU A 447-26.449 54. 932 34. 968 1. 00 21.55 1890 CA GLU A 447-27.652 55. 008 34. 161 1. 00 22.96 1891 CB GLU A 447-28.373 53. 606 34. 165 1. 00 25.21 1892 CG GLU A 447-27.806 52. 592 33. 272 1. 00 27.96 1893 CD GLU A 447-28. 485 51.227 33.347 1.00 29. 17 1894 OE1 GLU A 447-29.125 50. 894 34. 334 1. 00 29.08 1895 OE2 GLU A 447 -28.105 50.647 32.309 1.00 28. 80 1896 C GLU A 447-28.809 55. 815 34. 735 1. 00 23.18 1897 0 GLU A 447-28.898 56. 071 35. 904 1. 00 22.33 1898 N THR A 448-29.772 55. 926 33. 802 1. 00 24.57 1899 CA THR A 448-31.056 56. 584 34. 117 1. 00 26.33 1900 CB THR A 448-31.372 57. 797 33. 218 1. 00 27.14 1901 OG1 THR A 448-31.539 57. 208 31. 900 1. 00 28.71 1902 CG2 THR A 448-30.212 58. 799 33. 135 1. 00 27.31 1903 C THR A 448-32.129 55. 485 34. 128 1. 00 27.63 1904 O THR A 448-32.045 54. 409 33. 521 1. 00 28.14 1905 N ILE A 449-33.143 55. 763 34. 887 1. 00 28.37 1906 CA ILE A 449-34. 277 54.876 35.129 1.00 29. 26 1907 CB ILE A 449-33.838 53. 981 36. 369 1. 00 29.67 1908 CG1 ILE A 449-32.757 53. 015 35. 792 1. 00 30.83 1909 CD1 ILE A 449-32.193 51. 993 36. 806 1. 00 31.58 1910 CG2 ILE A 449-34.960 53. 320 37. 110 1. 00 29.95 1911 C ILE A 449-35.515 55. 683 35. 438 1. 00 29.83 19120 ILE A 449-35.394 56. 723 36. 108 1. 00 30.40 1913 N THR A 450-36.622 55. 198 34. 950 1. 00 29.75 1914 CA THR A 450-37.916 55. 780 35. 162 1. 00 30.32 1915 CB THR A 450-38.801 55. 860 33. 869 1. 00 30.27 1916 OG1 THR A 450-38. 147 56. 742 32. 914 1. 00 30. 92 1917 CG2 THR A 450-40.169 56. 502 34. 207 1. 00 31.35 <BR> <BR> 1918 C THR A 450-38. 617 54. 994 36. 252 1. 00 30. 86 1919 0 THR A 450-39.226 53. 934 36. 006 1. 00 31.74 1920 N LEU A 451-38.546 55. 488 37. 450 1. 00 30.77 1921 CA LEU A 451 -39.157 54.921 38.661 1.00 30. 44 1922 CB LEU A 451-38.148 55. 133 39. 797 1. 00 30.91 1923 CG LEU A 451-36.784 54. 517 39. 635 1. 00 31. 84 1924 CD1 LEU A 451-35. 917 54.804 40.856 1.00 31. 96 1925 CD2 LEU A 451-37.020 52. 984 39. 604 1. 00 32.41 1926 C LEU A 451-40.426 55. 798 38. 917 1. 00 29.84 19270 LEUA 451-40.597 56. 815 38. 231 1. 00 29.73 1928 N PRO A 452-41.241 55. 293 39. 829 1. 00 29.29 1929 CA PRO A 452-42. 480 55.999 40.203 1.00 28. 60 1930 CB PRO A 452-43.167 55. 083 41. 227 1. 00 28.96 1931 CG PRO A 452-42.003 54. 362 41. 858 1. 00 29.55 1932 CD PRO A 452-41.047 54. 104 40. 657 1. 00 29.51 1933 C PRO A 452-42. 051 57. 280 40. 963 1. 00 27. 27 1934 0 PRO A 452-41.013 57. 275 41. 612 1. 00 27.48 1935 N GLN A 453-42.943 58. 201 40. 892 1. 00 25.56 1936 CA GLN A 453-42.784 59. 543 41. 531 1. 00 24.82 1937 CB GLN A 453-43.888 60. 377 40. 833 1.00 21.56 1938 CG GLN A 453-44.199 61. 644 41. 436 1.00 19.59 1939 CD GLN A 453-45.344 62. 439 40. 888 1.00 17.38 1940 OE1 GLN A 453-46.503 62. 052 40. 951 1.00 17.82 1941 NE2 GLN A 453-44.979 63. 585 40. 351 1.00 13.61 1942 C GLN A 453-42.832 59. 429 43. 018 1.00 24.66 1943 0 GLN A 453-43.605 58. 585 43. 535 1.00 25.85 1944 N ASP A 454-42.008 60. 159 43. 768 1.00 23.39 1945 CA ASP A 454-41.964 60. 109 45. 235 1.00 22.47 1946ASP A 454-40.576 60. 053 45. 812 1.00 22.21 1947 CG ASP A 454-39.790 61. 343 45. 685 1.00 21.02 1948 OD1 ASP A 454-40.211 62. 277 45. 004 1.00 20.96 1949 OD2 ASP A 454-38.788 61. 435 46. 386 1.00 19.79 1950 C ASP A 454-42.802 61. 300 45. 732 1.00 22.19 1951 O ASP A 454-43.162 62. 109 44. 883 1.00 21.83 1952 N ALA A 455-43.049 61. 415 46. 992 1.00 21.97 1953 CA ALA A 455-43.852 62. 467 47. 589 1.00 21.73 1954 CB ALA A 455-44.053 62. 154 49. 055 1.00 21.93 1955 C ALA A 455-43.337 63. 859 47. 317 1.00 21.48 1956 0 ALA A 455-44.147 64. 807 47. 064 1.00 21.78 1957 N VAL A 456-42.045 64. 032 47. 356 1.00 21.09 1958 CA VAL A 456-41.403 65. 333 47. 083 1.00 19.97 1959 CB VAL A 456-39.892 65. 246 47. 390 1.00 20.13 1960 CG1 VAL A 456-39.208 66. 517 46. 785 1.00 19.41 1961 CG2 VAL A 456-39.650 65. 254 48. 865 1.00 20.03 1962 C VAL A 456-41.658 65. 836 45. 679 1.00 19.65 1963 O VAL A 456-41.764 67. 074 45. 514 1.00 21.13 1964 N SER A 457-41.590 65. 037 44. 684 1.00 18.95 1965 CA SER A 457-41.879 65. 403 43. 291 1.00 18.66 1966 CB SER A 457-41.555 64. 269 42. 355 1.00 16.97 1967 OG SER A 457-42.049 64. 365 41. 068 1.00 15.03 1968 C SER A 457-43.346 65. 783 43. 110 1.00 18.92 1969 0 SER A 457-43.583 66. 718 42. 355 1.00 19.32 1970 N ARG A 458-44.248 65. 025 43. 758 1.00 19.76 1971 CA ARG A 458-45.702 65. 276 43. 585 1.00 20.17 1972ARG A 458-46.581 64. 144 44. 254 1.00 20.82 1973 CG ARG A 458-48.004 64. 118 43. 683 1.00 21.24 1974 CD ARG A 458-48.864 63. 108 44. 311 1.00 21.63 1975 NE ARG A 458-50. 061 62. 790 43. 596 1. 00 21.26 1976 CZ ARG A 458-50.153 61. 941 42. 583 1.00 20.98 1977 NH1 ARG A 458-49.106 61. 172 42. 172 1.00 21.30 1978 NH2 ARG A 458-51.228 61. 975 41. 857 1.00 20.72' 1979 C ARG A 458-46.077 66. 569 44. 267 1.00 20.52 1980 0 ARG A 458-47.000 67. 297 43. 836 1.00 20.94 1981 N THR A 459-45.402 66. 814 45. 391 1.00 20.70 1982 CA THR A 459-45.663 68. 051 46. 179 1.00 20.38 1983 CB THR A 459-44.851 68. 004 47. 514 1.00 23.42 1984 OG1 THR A 459-45.230 66. 777 48. 212 1.00 25.66 1985 CG2 THR A 459-45.123 69. 205 48. 466 1.00 23.04 1986 C THR A 459-45.166 69. 276 45. 383 1.00 19.79 1987 0 THR A 459-45.861 70. 253 45. 223 1.00 19.59 1988 N GLN A 460-43.910 69. 125 44. 923 1.00 19.49 1989 CA GLN A 460-43.276 70. 213 44. 197 1.00 19.35 1990 CB GLN A 460-41.760 70. 114 44. 105 1.00 21.09 1991 CG GLN A 460-41.079 70. 038 45. 508 1.00 23.65 1992 CD GLN A 460-39.619 69. 878 45. 267 1.00 27.06 1993 OE1 GLN A 460-38.778 69. 425 46. 032 1.00 28. 97 1994 NE2 GLN A 460-39.236 70. 317 44. 047 1.00 28.54 1995 C GLN A 460-43.927 70. 492 42. 890 1.00 18.40 1996 0 GLN A 460-43.981 71. 689 42. 533 1.00 19.88 1997 N ARG A 461-44.332 69. 499 42. 147 1.00 17.60 1998 CA ARG A 461-44.997 69. 723 40. 838 1.00 16.58 1999 CB ARG A 461-45.018 68. 467 39. 969 1.00 13.54 2000 CG ARG A 461-43.613 67. 924 39. 587 1.00 11.74 2001 CD ARG A 461-43.821 66. 791 38. 628 1.00 11.77 2002 NE ARG A 461-42.637 66. 344 37. 930 1.00 13.62 2003 CZ ARG A 461-42.439 65. 304 37. 177 1.00 15.96 2004 NH1 ARG A 461-43.419 64. 385 36. 970 1.00 16.98 2005 NH2 ARG A 461-41.224 64. 999 36. 652 1.00 17.04 2006 C ARG A 461-46.403 70. 281 41. 039 1.00 16.31 2007 0 ARG A 461-46.756 71. 210 40. 287 1.00 16.12 2008 N ARG A 462-47.189 69. 729 41. 937 1.00 16.52 2009 CA ARG A 462-48. 610 70. 252 42. 167 1. 00 16.89 2010 CB ARG A 462-49.228 69. 417 43. 314 1.00 18.26 2011 CG ARG A 462-50.689 69. 727 43. 628 1.00 19.33 2012 CD ARG A 462-51.120 68. 989 44. 854 1.00 20.59 2013 NE ARG A 462-50.345 69. 532 46. 032 1.00 22.64 2014 CZ ARG A 462-50.601 69. 063 47. 253 1.00 24.56 2015 NH1 ARG A 462-51.503 68. 073 47. 449 1.00 26.76 2016 NH2 ARG A 462-50.059 69. 536 48. 352 1.00 24.82 2017 C ARG A 462-48. 610 71. 692 42. 684 1. 00 17.31 20180ARG A 462-49.570 72. 521 42. 554 1.00 16.67 2019 N GLY A 463-47.566 71. 999 43. 363 1.00 18.16 2020 CA GLY A 463-47.220 73. 265 44. 011 1.00 18.67 2021 C GLY A 463-47.056 74. 449 43. 114 1.00 18.87 2022 0 GLY A 463-46.843 75. 575 43. 666 1.00 20.03 2023 N ARG A 464-47.135 74. 324 41. 821 1.00 18.44 2024 CA ARG A 464-47.035 75. 365 40. 842 1.00 18.43 2025 CB ARG A 464-46.510 75. 128 39. 460 1.00 19.36 2026 CG ARG A 464-45.132 74. 777 39. 173 1.00 20.06 2027 CD ARG A 464-44.025 75. 374 39. 848 1.00 20.84 2028 NE ARG A 464-43.596 74. 729 41. 039 1.00 22.19 2029 CZ ARG A 464-42.432 74. 941 41. 680 1.00 23.40 2030 NH1 ARG A 464-41.535 75. 883 41. 298 1.00 23.19 2031 NH2 ARG A 464-42.068 74. 130 42. 669 1.00 22.35 2032 C ARG A 464-48.426 75. 933 40. 582 1.00 18.42 2033 0 ARG A 464-48.539 76. 777 39. 718 1.00 17.26 2034 N THR A 465-49.371 75. 306 41. 317 1.00 18. 70 2035 CA THR A 465-50.758 75. 835 41. 188 1.00 18. 17 2036 CB THR A 465-51.675 74. 937 40. 271 1.00 18.54 2037 OG1 THR A 465-52.919 75. 680 40. 134 1.00 19.05 2038 CG2 THR A 465-51.960 73. 549 40. 817 1.00 16.61 2039 C THR A 465-51.320 76. 068 42. 577 1.00 18.52 2040 0 THR A 465-50.719 75. 669 43. 609 1.00 19.02 2041 N GLY A 466-52.437 76. 719 42. 675 1.00 18.83 2042 CA GLY A 466-53.151 77. 010 43. 921 1.00 20.11 2043 C GLY A 466-52.488 77. 968 44. 863 1.00 21.55 2044 O GLY A 466-52.908 78. 084 46. 047 1.00 21.89 2045 N ARG A 467-51.434 78. 640 44. 429 1.00 22.27 2046 CA ARG A 467-50.692 79. 583 45. 235 1.00 23.22 2047 CB ARG A 467-49.428 80. 124 44. 500 1.00 24.92 2048 CG ARG A 467-48.330 79. 094 44. 470 1.00 26.65 2049 CD ARG A 467-47.081 79. 345 43. 718 1.00 28.34 2050 NE ARG A 467-46.093 78. 271 43. 998 1.00 28.94 2051 CZ ARG A 467-44.958 78. 053 43. 334 1.00 30.44 2052 NH1 ARG A 467-44.539 78. 731 42. 276 1.00 30.82 2053 NH2 ARG A 467-44.077 77. 089 43. 764 1.00 30.28 2054 C ARG A 467-51.542 80. 757 45. 693 1.00 23.51 2055 0 ARG A 467-51.574 81. 804 44. 993 1.00 23.20 2056 N GLY A 468-52.158 80. 580 46. 835 1.00 23.39 2057 CA GLY A 468-52.975 81. 611 47. 472 1.00 23.67 2058 C GLY A 468-54.166 82. 026 46. 689 1.00 23.75 2059 0 GLY A 468-54.590 83. 221 46. 786 1.00 24.78 2060 N LYS A 469-54.701 81. 158 45. 911 1.00 23.36 2061 CA LYS A 469-55.895 81. 284 45. 058 1.00 23.41 2062LYS A 469-55.637 82. 102 43. 827 1.00 24.71 2063 CG LYS A 469-54.436 81. 515 43. 028 1.00 25.93 2064 CD LYS A 469-54.390 82. 146 41. 667 1.00 26.20 2065 CE LYS A 469-54.090 83. 598 41. 604 1.00 27.58 2066LYS A 469-54.122 83. 995 40. 147 1.00 28.60 2067 C LYS A 469-56.196 79. 829 44. 652 1.00 23.61 2068 0 LYS A 469-55.289 79. 026 44. 906 1.00 24.38 2069 N PRO A 470-57.332 79. 509 44. 107 1.00 23.33 2070 CA PRO A 470-57.676 78. 143 43. 727 1.00 22.89 2071 CB PRO A 470-59.146 78. 185 43. 283 1.00 23.13 2072PRO A 470-59.671 79. 530 43. 800 1.00 23.98 2073 CD PRO A 470-58.436 80. 467 43. 837 1.00 23.86 2074 C PRO A 470-56.852 77. 637 42. 539 1.00 21.90 2075 0 PRO A 470-56.581 78. 428 41. 627 1.00 21.83 2076 N GLY A 471-56.605 76. 305 42. 569 1.00 20.21 2077 CA GLY A 471-55.840 75. 769 41. 366 1.00 18.89 2078 C GLY A 471-56.362 74. 294 41. 230 1.00 17.74 2079 0 GLY A 471-56.874 73. 818 42. 215 1.00 17.58 2080 N ILE A 472-56. 073 73.737 40.115 1. 00 15.86 2081 CA ILE A 472-56.447 72. 392 39. 764 1.00 15.22 2082 CB ILE A 472-57.266 72. 464 38. 420 1.00 13.47 2083 CG1 ILE A 472-58.564 73. 290 38. 595 1.00 11.99 2084 CD1 ILE A 472-59.255 73. 614 37. 259 1.00 12.19 2085 CG2 ILE A 472-57.627 70. 974 37. 971 1.00 14.25 2086 C ILE A 472-55.148 71. 611 39. 411 1.00 15.68 2087 0 ILE A 472-54.432 72. 139 38. 600 1.00 15.50 2088 N TYR A 473-55.061 70. 424 39. 901 1.00 16.50 2089 CA TYR A 473-53.976 69. 482 39. 637 1.00 16.47 2090 CB TYR A 473-53.231 69. 242 40. 947 1.00 15.40 2091 CG TYR A 473-52.129 68. 192 40. 910 1.00 16.16 2092 CD1 TYR A 473-52.420 66. 872 41. 301 1.00 14.40 2093 CE1 TYR A 473-51.456 65. 879 41. 283 1.00 15.56 2094 CZ TYR A 473-50.185 66. 166 40. 880 1.00 15.79 2095 OH TYR A 473-49.169 65. 247 40. 854 1.00 16.19 2096 CE2 TYR A 473-49.866 67. 481 40. 507 1.00 16.13 2097 CD2 TYR A 473-50.870 68. 466 40. 500 1.00 15.46 2098 C TYR A 473-54.491 68. 220 38. 989 1.00 17.21 2099 O TYR A 473-55.144 67. 365 39. 613 1.00 17.87 2100 N ARG A 474-54.192 68. 015 37. 699 1.00 17.56 2101 CA ARG A 474-54.671 66. 758 37. 011 1.00 17.39 2102 CB ARG A 474-55.089 67. 165 35. 624 1.00 16.56 2103 CG ARG A 474-56.254 68. 239 35. 672 1.00 17.23 2104 CD ARG A 474-56.537 68. 568 34. 255 1.00 17.84 2105 NE ARG A 474-57.390 69. 754 34. 128 1.00 19.84 2106 CZ ARG A 474-58.611 69. 918 34. 597 1.00 20.11 2107 NH1 ARG A 474-59.248 68. 943 35. 284 1.00 19.40 2108 NH2 ARG A 474-59. 168 71. 139 34. 511 1. 00 19. 71 2109 C ARG A 474-53. 592 65. 724 36. 988 1. 00 18. 45 2110 0 ARG A 474-52. 451 66. 127 36. 743 1. 00 19. 09 2111 N PHE A 475-53. 879 64. 410 37. 162 1. 00 18. 72 2112 CA PHE A 475-52. 870 63. 393 37. 178 1. 00 19. 55 2113 CB PHE A 475-52. 437 63. 030 38. 614 1. 00 18. 24 2114 CG PHE A 475-53. 552 62. 628 39. 524 1. 00 19. 67 2115 CD1 PHE A 475-53. 830 61. 258 39. 721 1. 00 19. 61 2116 CE1 PHE A 475-54. 862 60. 866 40. 538 1. 00 19. 80 2117 CZ PHE A 475-55. 644 61. 823 41. 200 1. 00 18. 57 2118 CE2 PHE A 475-55. 383 63. 176 41. 003 1. 00 19. 89 2119 CD2 PHE A 475-54. 370 63. 590 40. 132 1. 00 19. 30 2120 C PHE A 475-53. 186 62. 139 36. 392 1. 00 20. 72 2121 0 PHE A 475-54. 366 61. 787 36. 251 1. 00 21. 05 2122 N VAL A 476-52. 110 61. 462 36. 012 1. 00 21. 26 2123 CA VAL A 476-52. 224 60. 204 35. 294 1. 00 21. 62 2124 CB VAL A 476-51. 156 59. 899 34. 249 1. 00 19. 34 2125 CG1 VAL A 476-50. 941 60. 988 33. 207 1. 00 17. 57 2126 CG2 VAL A 476-49. 894 59. 368 34. 863 1. 00 19. 19 2127 C VAL A 476-52. 326 59. 083 36. 330 1. 00 22. 95 21280 VAL A476-53. 02558. 12436. 0841. 0023. 47 2129 N ALA A 477-51. 610 59. 218 37. 431 1. 00 24. 31 2130 CA ALA A 477-51. 607 58. 188 38. 467 1. 00 24. 97 2131 CB ALA A 477-50. 316 57. 355 38. 358 1. 00 25. 05 2132 C ALA A 477-51. 731 58. 659 39. 890 1. 00 26. 21 2133 0 ALA A 477-51. 069 59. 598 40. 334 1. 00 25. 96 2134 N PRO A 478-52. 572 57. 951 40. 631 1. 00 27. 34 2135 CA PRO A 478-52. 750 58. 206 42. 068 1. 00 28. 50 2136 CB PRO A 478-54. 050 57. 416 42. 370 1. 00 28. 42 2137 CG PRO A 478-53. 906 56. 187 41. 478 1. 00 28. 01 2138 CD PRO A 478-53. 395 56. 779 40. 171 1. 00 28. 11 2139 C PRO A 478-51. 539 57. 532 42. 721 1. 00 29. 84 2140 0 PRO A 478-51. 033 56. 539 42. 125 1. 00 30. 01 2141 N GLY A 479-51. 052 58. 059 43. 828 1. 00 31. 15 2142 CA GLY A 479-49. 937 57. 334 44. 486 1. 00 32. 59 2143 C GLY A 479-48. 552 57. 785 44. 137 1. 00 33. 43 2144 0 GLY A 479-48. 101 57. 966 42. 985 1. 00 34. 10 2145 N GLU A 480-47. 829 57. 937 45. 242 1. 00 33. 64 2146 CA GLU A 480-46. 440 58. 396 45. 266 1. 00 33. 54 2147 CB GLU A 480-46. 442 59. 797 45. 947 1. 00 34. 43 <BR> <BR> <BR> 2148 CG GLU A 480-47. 085 59. 704 47. 360 1. 00 35. 26 2149 CD GLU A 480-47. 189 61. 055 48. 013 1. 00 34. 65 2150 OE1 GLU A 480-47. 085 62. 071 47. 361 1. 00 35. 15 2151 OE2 GLU A 480-47. 391 60. 916 49. 239 1. 00 34. 49 2152 C GLU A 480-45. 650 57. 476 46. 192 1. 00 33. 06 2153 0 GLU A 480-46. 183 56. 954 47. 170 1. 00 33. 24 2154 N ARG A 481-44. 434 57. 298 45. 816 1. 00 32. 24 2155 CA ARG A 481-43. 433 56. 484 46. 592 1. 00 31. 95 2156 CB ARG A 481-42. 340 56. 317 45. 606 1. 00 32. 71 2157 CG ARG A 481-41. 024 55. 684 45. 556 1. 00 32. 92 2158 CD ARG A 481-40. 343 56. 260 44. 301 1. 00 33. 32 2159 NE ARG A 481-38. 962 55. 900 44. 234 1. 00 34. 09 2160 CZ ARG A 481-38. 062 56. 069 45. 196 1. 00 34. 94 2161 NH1 ARG A 481-38. 286 56. 605 46. 400 1. 00 34. 52 <BR> <BR> 2162 NH2 ARG A 481-36. 836 55. 544 44. 976 1. 00 35. 73 2163 C ARG A 481-42. 966 57. 464 47. 707 1. 00 31. 55 2164 0 ARG A 481-43. 028 58. 695 47. 529 1. 00 31. 05 2165 N PRO A 482-42.544 56. 910 48. 814 1.00 31.49 2166 CA PRO A 482-42.047 57. 699 49. 959 1.00 30.97 2167 CB PRO A 482-41.850 56. 654 51. 035 1.00 31.16 2168PRO A 482-41.410 55. 423 50. 227 1.00 31.31 2169 CD PRO A 482-42.439 55. 450 49. 082 1.00 31.73 2170 C PRO A 482-40.712 58. 345 49. 570 1.00 30.26 2171 O PRO A 482-39.884 57. 776 48. 846 1.00 30.45 2172 N SER A 483-40.536 59. 524 50. 115 1.00 29.72 2173 CA SER A 483-39.350 60. 372 49. 901 1.00 29.05 2174 CB SER A 483-39.821 61. 838 49. 985 1.00 27.83 2175 OG SER A 483-40.271 62. 089 51. 317 1.00 27.65 2176 C SER A 483-38.391 60. 150 51,. 066 1.00 28.54 2177 0 SER A 483-38.798 59. 512 52. 073 1.00 28.81 2178 N GLY A 484-37.168 60. 651 50. 896 1.00 27. 85 2179 CA GLY A 484-36.161 60. 540 51. 943 1.00 26.64 2180 C GLY A 484-34.988 59. 669 51. 655 1.00 26.20 2181 0 GLY A 484-34.162 59. 492 52. 587 1.00 25.85 2182 N MET A 485-34.877 59. 108 50. 464 1.00 26.29 2183 CA MET A 485-33. 708 58. 239 50. 180 1. 00 26.48 2184 CB MET A 485-33.916 56. 829 50. 641 1.00 30.11 2185 CG MET A 485-32.842 55. 873 50. 224 1.00 34.36 2186MET A 485-33.099 54. 207 50. 939 1.00 38.75 2187 CE MET A 485-34.895 54. 074 50. 655 1.00 37.77 2188 C MET A 485-33.110 58. 586 48. 858 1.00 25.35 2189 O MET A 485-33.815 59. 023 47. 943 1.00 25.28 2190 N PHE A 486-31.783 58. 453 48. 754 1.00 24.04 2191 CA PHE A 486-31.083 58. 750 47. 489 1.00 22.13 2192 CB PHE A 486-30.498 60. 144 47. 420 1.00 21.84 2193 CG PHE A 486-29. 412 60. 483 48. 415 1. 00 22.17 2194 CD1 PHE A 486-29.740 61. 003 49. 662 1.00 21.70 2195 CD2 PHE A 486-28.091 60. 192 48. 118 1.00 21.55 2196 CE1 PHE A 486-28. 743 61. 286 50. 587 1. 00 20.56 2197 CE2 PHE A 486-27.057 60. 466 49. 031 1.00 21.05 2198 CZ PHE A 486-27.405 61. 025 50. 258 1.00 20.53 2199 C PHE A 486-30.135 57. 598 47. 157 1.00 21.04 2200 O PHE A 486-29. 719 56. 778 48. 017 1. 00 19.39 2201 N ASP A 487-29.843 57. 551 45. 856 1.00 20.39 2202 CA ASP A 487-28. 997 56. 571 45. 229 1. 00 19.86 2203ASP A 487-29.282 56. 387 43. 738 1.00 18.60 2204 CG ASP A 487-28.618 55. 155 43. 153 1.00 18.91 2205 OD1 ASP A 487-27. 551 55. 136 42. 626 1. 00 17.98 2206 OD2 ASP A 487-29.299 54. 083 43. 175 1.00 20.99 2207 C ASP A 487-27.525 56. 874 45. 475 1.00 20.24 2208 O ASP A 487-27.135 58. 041 45. 547 1.00 20.93 2209 N SER A 488-26.773 55. 805 45. 493 1.00 19.76 2210 CA SER A 488-25. 324 55. 787 45. 679 1. 00 19.94 2211 CB SER A 488-24.838 54. 354 45. 872 1.00 21.51 2212 OG SER A 488-23.420 54. 232 45. 768 1.00 21.20 2213 C SER A 488-24.601 56. 554 44. 605 1.00 18.93 22140SERA 488-23.533 57. 103 44. 825 1.00 18.67 2215 N SER A 489-25.132 56. 630 43. 415 1.00 18.83 2216 CA SER A 489-24.470 57. 404 42. 313 1.00 17.96 2217 CB SER A 489-25.090 57. 168 40. 980 1.00 18.54 2218 OG SER A 489-26.475 57. 583 41. 106 1.00 19. 01 2219 C SER A 489-24.424 58. 857 42. 715 1.00 17.77 22200SERA 489-23.605 59. 562 42. 137 1.00 18.48 2221 N VAL A 490-25.305 59. 329 43. 593 1.00 18.04 2222 CA VAL A 490-25.308 60. 733 44. 034 1.00 18.28 2223 CB VAL A 490-26. 584 61.148 44.805 1. 00 18.18 2224 CG1 VAL A 490-26.639 62. 611 45. 164 1.00 16.10 2225 CG2 VAL A 490-27.809 60. 642 44. 097 1.00 17.43 2226 C VAL A 490-24.038 60. 999 44. 810 1.00 18.74 22270 VAL A 490-23. 564 62.153 44.705 1. 00 19.49 2228 N LEU A 491-23.540 59. 994 45. 510 1.00 18.33 2229 CA LEU A 491-22.260 60. 085 46. 267 1.00 18.07 2230 CB LEU A 491-22.068 58. 843 47. 194 1.00 17.65 2231 CG LEU A 491-23.160 58. 674 48. 229 1.00 18.05 2232 CD1 LEU A 491-23.014 57. 405 49. 084 1.00 18.43 2233 CD2 LEU A 491-23.160 59. 912 49. 131 1.00 18.79 2234 C LEU A 491-21.161 60. 242 45. 228 1.00 17.37 22350 LEU A 491-20.301 61. 128 45. 303 1.00 17.76 2236 N CYS A 492-21.212 59. 398 44. 219 1.00 16.42 2237 CA CYS A 492-20.322 59. 446 43. 085 1.00 15.74 2238 CB CYS A 492-20.838 58. 494 41. 985 1.00 16.31 2239 SG CYS A 492-19.663 58. 447 40. 590 1.00 16.33 2240 C CYS A 492-20.319 60. 898 42. 556 1.00 15.94 2241 0 CYS A 492-19.274 61. 490 42. 478 1.00 16.03 2242 N GLU A 493-21.493 61. 453 42. 268 1.00 16.42 2243 CA GLU A 493-21. 648 62.808 41.792 1. 00 16.10 2244 CB GLU A 493-23.084 63. 254 41. 568 1.00 18.16 2245 CG GLU A 493-23.847 62. 567 40. 418 1.00 18.28 2246 CD GLU A 493-25.268 63. 029 40. 339 1.00 19.98 2247 OE1 GLU A 493-26.100 62. 842 41. 194 1.00 19.37 2248 OE2 GLU A 493-25.458 63. 686 39. 304 1.00 22.17 2249 C GLU A 493-20. 991 63. 836 42. 695 1. 00 16.02 2250 O GLU A 493-20. 529 64.831 42.172 1. 00 16.71 2251 N CYS A 494-21.021 63. 647 43. 985 1.00 16.48 2252 CA CYS A 494-20.420 64. 443 45. 007 1.00 16.30 2253 CB CYS A 494-20.826 64. 091 46. 435 1.00 14.94 2254 SG CYS A 494-22.500 64. 473 46. 723 1.00 18.21 2255 C CYS A 494-18.892 64. 376 44. 867 1.00 16.56 2256 0 CYS A 494-18.273 65. 451 44. 904 1.00 15.66 2257 N TYR A 495-18. 362 63.144 44.723 1. 00 16.82 2258 CA TYR A 495-16.953 63. 005 44. 517 1.00 16. 43 2259 CB TYR A 495-16.181 61. 684 44. 720 1.00 17.18 2260 CG TYR A 495-16.278 61. 211 46. 152 1.00 17.78 2261 CD1 TYR A 495-17.414 60. 505 46. 535 1.00 16.64 2262 CE1 TYR A 495-17.570 60. 084 47. 850 1.00 17.60 2263 CD2 TYR A 495-15.283 61. 481 47. 091 1.00 17.70 2264 CE2 TYR A 495-15.437 61. 029 48. 406 1.00 18. 58 2265 CZ TYR A 495-16.599 60. 393 48. 793 1.00 17.16 2266 OH TYR A 495-16.726 59. 964 50. 085 1.00 18. 10 2267 C TYR A 495-16.562 63. 606 43. 168 1.00 16.85 2268 O TYR A 495-15.466 64. 159 43. 157 1.00 17. 30 2269 N ASP A 496-17.330 63. 537 42. 119 1.00 17.26 2270 CA ASP A 496-16. 889 64.116 40.805 1. 00 17.64 2271 CB ASP A 496-17.822 63. 457 39. 749 1.00 18.55 2272 CG ASP A 496-17.444 63. 637 38. 325 1.00 18.24 2273 OD1 ASP A 496-17.081 62. 672 37. 642 1.00 17.17 2274 OD2 ASP A 496-17.451 64. 789 37. 823 1.00 19. 06 2275 C ASP A 496-16.828 65. 612 40. 833 1.00 18. 79 2276 0 ASP A 496-16.002 66. 289 40. 136 1.00 19.06 2277 N ALA A 497-17.668 66. 273 41. 584 1.00 19.40 2278 CA ALA A 497-17.810 67. 701 41. 763 1.00 19. 00 2279 CB ALA A 497-19. 148 68. 091 42. 290 1. 00 18. 46 2280 C ALA A 497-16.705 68. 276 42. 643 1. 00 19.21 2281 0 ALA A 497-16.173 69. 350 42. 257 1. 00 19.35 2282 N GLY A 498-16.456 67. 669 43. 761 1. 00 18. 90.

2283 CA GLY A 498-15.340 68. 176 44. 635 1. 00 18.98 2284 C GLY A 498-14.117 68. 257 43. 720 1. 00 19.20 2285 O GLY A 498-13.354 69. 269 43. 695 1. 00 19.01 2286 N CYS A 499-13.926 67. 198 42. 945 1. 00 19.88 2287 CA CYS A 499-12.865 67. 016 41. 994 1. 00 20.17 2288 CB CYS A 499-12.673 65. 603 41. 439 1. 00 21. 21 2289 SG CYS A 499-12.022 64. 360 42. 554 1. 00 21.55 2290 C CYS A 499-12.849 67. 963 40. 809 1. 00 20.42 2291 0 CYS A 499-11.821 68. 579 40. 539 1. 00 20.41 2292 N ALA A 500-13.963 68. 082 40. 110 1. 00 20.40 2293 CA ALA A 500-14.038 68. 897 38. 908 1. 00 20.25 2294 CB ALA A 500-15.144 68. 335 37. 991 1. 00 18. 86 2295 C ALA A 500-14.320 70. 365 39. 139 1. 00 19.72 2296 O ALA A 500-13.958 71. 210 38. 323 1. 00 20.24 2297 N TRP A 501-15. 015 70. 624 40. 215 1. 00 19. 24 2298 CA TRP A 501-15. 469 71. 903 40. 583 1. 00 19. 18 2299 CB TRP A 501-16. 999 71. 964 40. 579 1. 00 18. 45 2300 CG TRP A 501-17.612 71. 744 39. 247 1. 00 18.83 2301 CD2 TRP A 501-17.693 72. 705 38. 178 1. 00 19.32 2302 CE2 TRP A 501-18.350 72. 089 37. 111 1. 00 19.58 2303 CE3 TRP A 501-17.235 74. 022 38. 042 1. 00 19.13 2304 CD1 TRP A 501-18.197 70. 609 38. 780 1. 00 18.93 2305 NE1 TRP A 501-18.651 70. 806 37. 482 1. 00 18.94 2306 CZ2 TRP A 501-18.580 72. 746 35. 912 1. 00 20.44 2307 CZ3 TRP A 501-17.490 74. 688 36. 874 1. 00 19.32 2308 CH2 TRP A 501-18.124 74. 044 35. 790 1. 00 20.70 2309 C TRP A 501-14.876 72. 565 41. 773 1. 00 19.93 2310 0 TRP A 501-14.579 73. 780 41. 572 1. 00 21.00 2311 N TYR A 502-14.746 71. 884 42. 902 1. 00 19.69 2312 CA TYR A 502-14. 284 72.641 44.078 1.00 20. 11 2313 CB TYR A 502-15.374 72. 469 45. 180 1. 00 18.50 2314 CG TYR A 502-16.737 72. 658 44. 568 1. 00 17.19 2315 CD1 TYR A 502-17.121 73. 922 44. 117 1. 00 17.14 2316 CE1 TYR A 502-18.329 74. 170 43. 501 1. 00 15.52 2317 CD2 TYR A 502-17.654 71. 644 44. 462 1. 00 17.29 2318 CE2 TYR A 502-18.942 71. 892 43. 900 1. 00 17.03 2319 CZ TYR A 502-19.255 73. 112 43. 406 1. 00 15.60 2320 OH TYR A 502-20.514 73. 369 42. 897 1. 00 15.57 2321 C TYR A 502-12.969 72. 279 44. 632 1. 00 21.44 2322 0 TYR A 502-12.808 72. 519 45. 856 1. 00 21.93 2323 N GLU A 503-12.081 71. 809 43. 810 1. 00 22.65 2324 CA GLU A 503-10.713 71. 434 44. 293 1. 00 24.17 2325 CB GLU A 503-9.858 72. 676 44. 390 1. 00 27.62 2326 CG GLU A 503-9.339 73. 520 43. 278 1. 00 31.98 2327 CD GLU A 503-8.215 73. 007 42. 420 1. 00 35.11 2328 OE1 GLU A 503-7.298 73. 746 42. 033 1. 00 36.32 2329 OE2 GLU A 503-8.271 71. 761 42. 223 1. 00 36.16 2330 C GLU A 503-10.785 70. 822 45. 680 1. 00 23.86 2331 O GLU A 503 -10.215 71.341 46.648 1.00 23. 46 2332 N LEU A 504-11-464 69. 682 45. 810 1. 00 23. 89 2333 CA LEU A 504-11. 557 68. 969 47. 082 1. 00 23. 45 2334 CB LEU A 504-13. 018 68. 832 47. 491 1. 00 22. 48 2335 CG LEU A 504-13.866 70. 033 47. 753 1. 00 21.38 2336 CD1 LEU A 504-15.284 69. 522 48. 136 1. 00 20.75 2337 CD2 LEU A 504-13.259 70. 839 48. 906 1. 00 20.96 2338 C LEU A 504-10. 949 67. 564 46. 802 1. 00 23. 91 2339 O LEU A 504-11.244 67. 016 45. 772 1. 00 23.40 2340 N THR A 505-10.087 67. 147 47. 729 1. 00 24.25 2341 CA THR A 505-9.497 65. 796 47. 494 1. 00 24.33 2342 CB THR A 505-8.228 65. 652 48. 408 1. 00 24.43 2343 OG1 THR A 505-8.698 65. 752 49. 791 1. 00 25.59 2344 CG2 THR A 505-7.205 66. 792 48. 195 1. 00 23.29 2345 C THR A 505-10.633 64. 857 47. 889 1. 00 24.14 2346 0 THR A 505-11.513 65. 261 48. 671 1. 00 24.64 2347 N PRO A 506-10.636 63. 681 47. 329 1. 00 23.51 2348 CD PRO A 506-9.687 63. 182 46. 314 1. 00 22.90 2349 CA PRO A 506-11.677 62. 687 47. 693 1. 00 22.88 2350 CB PRO A 506-11.111 61. 425 47. 101 1. 00 22.58 2351 CG PRO A 506-10.387 61. 842 45. 879 1. 00 22.07 2352 C PRO A 506-11.781 62. 614 49. 215 1. 00 23.48 2353 O PRO A 506-12.845 62. 274 49. 776 1. 00 23.02 2354 N ALA A 507-10.653 62. 893 49. 909 1. 00 23.59 2355 CA ALA A 507-10.667 62. 806 51. 387 1. 00 23.47 2356 CB ALA A 507-9.276 62. 593 51. 944 1. 00 23.89 2357 C ALA A 507-11.431 63. 937 52. 019 1. 00 23.50 2358 O ALA A 507-12.187 63. 722 52. 983 1. 00 23.41 2359 N GLU A 508-11.326 65. 136 51. 487 1. 00 24.10 2360 CA GLU A 508-12.040 66. 296 52. 000 1. 00 24.67 2361 CB GLU A 508-11.590 67. 633 51. 404 1. 00 28.22 2362 CG GLU A 508-12.342 68. 886 52. 005 1. 00 30.63 2363 CD GLU A 508-12. 099 69. 136 53. 464 1. 00 32. 52 2364 OE1 GLU A 508-11. 168 68. 660 54. 128 1. 00 34. 28 2365 OE2 GLU A 508-12.919 69. 913 53. 996 1. 00 32.64 2366 C GLU A 508-13.528 66. 144 51. 690 1. 00 24.23 23670 GLU A 508-14.360 66. 655 52. 450 1. 00 24.37 2368 N THR A 509-13.847 65. 492 50. 574 1. 00 23.05 2369 CA THR A 509-15.281 65. 329 50. 218 1. 00 21. 82 2370 CB THR A 509-15.479 64. 875 48. 730 1. 00 20.50 2371 OG1 THR A 509-14.963 65. 900 47. 822 1. 00 18.98 2372 CG2 THR A 509-16.899 64. 399 48. 453 1. 00 19.26 2373 C THR A 509-15.917 64. 401 51. 236 1. 00 21.81 2374 0 THR A 509-17.042 64. 611 51. 686 1. 00 21.72 2375 N THR A 510-15.161 63. 403 51. 678 1. 00 21.62 2376 CA THR A 510-15.572 62. 425 52. 666 1. 00 21.42 2377 CB THR A 510-14.508 61. 249 52. 828 1. 00 21.89 2378 OG1 THR A 510-14.441 60. 555 51. 571 1. 00 22.15 2379 CG2 THR A 510-14.786 60. 304 54. 011 1. 00 21.53 2380 C THR A 510-15.935 63. 039 54. 006 1. 00 21.50 2381 0 THR A 510-16.884 62. 588 54. 638 1. 00 21.16 2382 N VAL A 511-15.151 64. 007 54. 475 1. 00 21.33 2383 CA VAL A 511-15.323 64. 725 55. 721 1. 00 21.02 2384 CB VAL A 511-14.203 65. 777 55. 964 1. 00 20.85 2385 CG1 VAL A 511-14.456 66. 564 57. 238 1. 00 20.34 2386 CG2 VAL A 511-12. 825 65. 176 55. 997 1. 00 19. 68 2387 C VAL A 511-16.689 65. 445 55. 723 1. 00 20.95 23880 VAL A 511-17.398 65. 469 56. 694 1. 00 21.53 2389 N ARG A 512-16.946 66. 081 54. 596 1. 00 20.49 2390 CA ARG A 512-18.182 66. 838 54. 405 1. 00 19.97 2391 CB ARG A 512-18.006 67. 709 53. 165 1. 00 20.65 2392 CG ARG A 512-16.706 68. 532 53. 205 1. 00 20.75 2393 CD ARG A 512-16.651 69. 532 52. 133 1. 00 21.44 2394 NE ARG A 512-15.469 70. 407 52. 194 1. 00 23.32 2395 CZ ARG A 512-15.530 71. 601 51. 540 1. 00 23.75 2396 NH1 ARG A 512-16.607 72. 026 50. 894 1. 00 21.96 2397 NH2 ARG A 512-14.448 72. 380 51. 525 1. 00 24.49 2398 C ARG A 512-19.351 65. 883 54. 372 1. 00 20.10 2399 0 ARG A 512-20.352 66. 150 55. 093 1. 00 21.14 2400 N LEU A 513-19.306 64. 837 53. 599 1. 00 19.81 2401 CA LEU A 513-20.331 63. 811 53. 457 1. 00 20.47 2402LEU A 513-20.100 62. 910 52. 256 1. 00 17.39 2403 CG LEU A 513-20.019 63. 349 50. 854 1. 00 15.77 2404 CD1 LEU A 513-19.830 62. 258 49. 821 1. 00 14.25 2405 CD2 LEU A 513-21.158 64. 256 50. 465 1. 00 15.38 2406 C LEU A 513-20.580 63. 058 54. 771 1. 00 22.08 2407 O LEU A 513-21.761 62. 776 55. 104 1. 00 23.38 2408 N ARG A 514-19.515 62. 674 55. 450 1. 00 23.00 2409 CA ARG A 514-19.639 61. 965 56. 748 1. 00 23.93 2410 CB ARG A 514-18.228 61. 710 57. 297 1. 00 26.29 2411 CG ARG A 514-18.145 61. 037 58. 682 1. 00 27.09 2412 CD ARG A 514-18.963 59. 798 58. 653 1. 00 28.34 2413 NE ARG A 514-18.493 58. 765 57. 738 1. 00 28.57 2414 CZ ARG A 514-19.363 57. 824 57. 319 1. 00 30.18 2415 NH1 ARG A 514-20.676 57. 863 57. 637 1. 00 31.21 2416 NH2 ARG A 514-18.941 56. 792 56. 601 1. 00 30.11 2417 C ARG A 514-20.444 62. 850 57. 666 1. 00 24.77 2418 0 ARG A 514-21.313 62. 445 58. 501 1. 00 25.57 2419 N ALA A 515-20.179 64. 145 57. 493 1. 00 24.51 2420 CA ALA A 515-20.834 65. 158 58. 344 1. 00 24.76 2421 CB ALA A 515-20.163 66. 506 58. 264 1. 00 24.23 2422 C ALA A 515-22.318 65. 097 58. 107 1. 00 24.57 2423 0 ALA A 515-23.070 65. 091 59. 083 1. 00 25.39 2424 N TYR A 516-22.728 65. 049 56. 880 1. 00 24.28 2425 CA TYR A 516-24.123 64. 986 56. 421 1. 00 24.30 2426 CB TYR A 516-24.173 65. 048 54. 875 1. 00 21.75 2427 CG TYR A 516-25.511 65. 007 54. 227 1. 00 20.92 2428 CD1 TYR A 516-26.154 66. 164 53. 805 1. 00 19.91 2429 CE1 TYR A 516-27.427 66. 141 53. 179 1. 00 18.86 2430 CD2 TYR A 516-26.175 63. 785 54. 009 1. 00 19.70 2431 CE2 TYR A 516-27.427 63. 762 53. 381 1. 00 17.85 2432 CZ TYR A 516-28.037 64. 912 52. 994 1. 00 18.64 2433 OH TYR A 516-29.245 64. 856 52. 326 1. 00 17.73 2434 C TYR A 516-24. 753 63. 643 56. 870 1. 00 25. 10 2435 0 TYR A 516-25.911 63. 667 57. 313 1. 00 25.02 2436 N MET A 517-24.009 62. 587 56. 748 1. 00 25.65 2437 CA MET A 517-24.343 61. 222 57. 104 1. 00 27.59 2438 CB MET A 517-23.233 60. 251 56. 799 1. 00 29.66 2439 CG MET A 517-22.598 59. 854 55. 638 1. 00 32.06 2440MET A 517-23.459 58. 826 54. 442 1. 00 35.11 2441 CE MET A 517-24.881 59. 869 54. 091 1. 00 34.41 2442 C MET A 517-24.595 61. 031 58. 627 1. 00 28.19 2443 0 MET A 517-25.380 60. 106 58. 981 1. 00 28.58 2444 N ASN A 518-23.851 61. 740 59. 448 1. 00 28.12 2445 CA ASN A 518-23.966 61. 610 60. 903 1. 00 28.18 2446 CB ASN A 518-22.625 61. 990 61. 602 1. 00 27.63 2447 CG ASN A 518-21.516 61. 058 61. 221 1. 00 27.28 2448 OD1 ASN A 518-21.814 59. 859 60. 982 1. 00 28.89 2449 ND2 ASN A 518-20.277 61. 498 61. 261 1. 00 27.16 2450 C ASN A 518-25.062 62. 477 61. 482 1.00 28.37 2451 0 ASN A 518-25.223 62. 480 62. 714 1.00 28.64 2452 N THR A 519-25.752 63. 155 60. 616 1.00 28.65 2453 CA THR A 519-26.820 64. 077 61. 016 1.00 28.82 2454 CB THR A 519-26.610 65. 491 60. 299 1.00 28.08 2455 OG1 THR A 519-25.329 65. 948 60. 783 1.00 27.63 2456 CG2 THR A 519-27.789 66. 426 60. 638 1.00 28.14 2457 C THR A 519-28.189 63. 523 60. 694 1.00 29.28 2458 0 THR A 519-28.516 63. 371 59. 511 1.00 29.74 2459 N PRO A 520-28.952 63. 306 61. 748 1.00 29.31 2460 CD PRO A 520-28.528 63. 459 63. 165 1.00 29.33 2461 CA PRO A 520-30.306 62. 736 61. 670 1.00 28.47 2462 CB PRO A 520-30.516 62. 077 63. 026 1.00 28.97 2463PRO A 520-29.224 62. 199 63. 772 1.00 29.43 2464 C PRO A 520-31.371 63. 746 61. 304 1.00 27.24 2465 0 PRO A 520-31.256 64. 995 61. 537 1.00 26.52 2466 N GLY A 521-32.373 63. 233 60. 636 1.00 25.95 2467 CA GLY A 521-33.525 63. 972 60. 114 1.00 25.46 2468 C GLY A 521-33.306 64. 391 58. 665 1.00 25.00 2469 0 GLY A 521-34.105 65. 171 58. 099 1.00 25.24 2470 N LEU A 522-32.317 63. 795 58. 040 1.00 25.41 2471 CA LEU A 522-31.980 64. 198 56. 607 1.00 24.80 2472 CB LEU A 522-30.566 64. 765 56. 890 1.00 26.40 2473 CG LEU A 522-30.002 65. 881 56. 049 1.00 26.25 2474 CD1 LEU A 522-30.926 67. 111 56. 165 1.00 26.36 2475 CD2 LEU A 522-28.694 66. 232 56. 783 1.00 26.63 2476 C LEU A 522-32.000 62. 986 55. 708 1.00 24.06 2477 0 LEU A 522-31.763 61. 870 56. 185 1.00 24.38 2478 N PRO A 523-32.234 63. 171 54. 415 1.00 22.83 2479 CD PRO A 523-32.575 64. 475 53. 796 1.00 22.01 2480 CA PRO A 523-32.274 62. 075 53. 426 1.00 22.34 2481 CB PRO A 523-32.122 62. 872 52. 111 1.00 21.40 2482 CG PRO A 523-33.009 64. 066 52. 388 1.00 21.08 2483 C PRO A 523-31.129 61. 106 53. 656 1.00 23.00 2484 O PRO A 523-30.061 61. 520 54. 126 1.00 22.76 2485 N VAL A 524-31.335 59. 839 53. 370 1.00 23.71 2486 CA VAL A 524-30.375 58. 761 53. 574 1.00 24.41 2487 CB VAL A 524-30.829 57. 793 54. 697 1.00 25.40 2488 CG1 VAL A 524-30.983 58. 502 56. 037 1.00 25. 79 2489 CG2 VAL A 524-32.152 57. 140 54. 307 1.00 26.90 2490 C VAL A 524-30.034 57. 993 52. 310 1.00 23.84 2491 0 VAL A 524-30.797 57. 761 51. 417 1.00 23.26 2492 N CYS A 525-28.825 57. 499 52. 336 1.00 24.88 2493 CA CYS A 525-28.132 56. 778 51. 293 1.00 26.23 2494 CB CYS A 525-27.181 57. 819 50. 641 1.00 28.59 2495 SG CYS A 525-26.255 57. 319 49. 190 1.00 33.87 2496 C CYS A 525-27.269 55. 700 52. 005 1.00 26.27 2497 0 CYS A 525-27.033 55. 681 53. 207 1.00 25.29 2498 N GLN A 526-26.831 54. 850 51. 145 1.00 27.09 2499 CA GLN A 526-25.952 53. 669 51. 486 1.00 28.12 2500 CB GLN A 526-26.204 52. 665 50. 425 1.00 29.80 2501 CG GLN A 526-25.701 51. 305 50. 288 1.00 31.15 2502 CD GLN A 526-26.393 50. 435 49. 289 1.00 32.26 2503 OE1 GLN A 526-26. 666 49. 246 49. 540 1. 00 33.44 2504 NE2 GLN A 526-26.712 50. 996 48. 115 1.00 31.93 2505 C GLN A 526-24.616 54. 283 51. 799 1.00 28. 67 2506 0 GLN A 526-24.212 55. 285 51. 167 1.00 28.67 2507 N ASP A 527-23.939 53. 775 52. 835 1.00 29.57 2508 CA ASP A 527-22.639 54. 312 53. 248 1.00 30.13 2509ASP A 527-22.253 54. 177 54. 687 1.00 32.12 2510 CG ASP A 527-21.020 54. 883 55. 186 1.00 33.90 2511 OD1 ASP A 527-21.124 55. 654 56. 190 1.00 34.82 2512 OD2 ASP A 527-19.894 54. 764 54. 668 1.00 34.49 2513 C ASP A 527-21.592 53. 728 52. 283 1.00 30.08 2514 0 ASP A 527-21.046 52. 635 52. 538 1.00 30.43 2515 N HIS A 528-21.425 54. 496 51. 224 1.00 29.24 2516 CA HIS A 528-20.442 54. 173 50. 203 1.00 28.30 2517 CB HIS A 528-20.843 53. 947 48. 745 1.00 26.06 2518 CG HIS A 528-21.738 52. 798 48. 530 1.00 24.44 2519 CD2 HIS A 528-21.847 51. 638 49. 250 1.00 23. 98 2520 ND1 HIS A 528-22.673 52. 701 47. 548 1.00 24.92 2521 CE1 HIS A 528-23.294 51. 527 47. 619 1.00 24. 22 2522 NE2 HIS A 528-22. 823 50. 902 48. 670 1. 00 23.90 2523 C HIS A 528-19.321 55. 202 50. 225 1.00 27.94 2524 O HIS A 528-18. 600 55. 244 49. 220 1. 00 28.44 2525 N LEU A 529-19.188 55. 934 51. 338 1.00 27. 81 2526 CA LEU A 529-18.122 56. 916 51. 409 1.00 27.36 2527 CB LEU A 529-18.073 57. 716 52. 723 1.00 26.09 2528 CG LEU A 529-19.370 58. 486 53. 012 1.00 25.92 2529 CD1 LEU A 529-19.132 59. 607 54. 012 1.00 25.31 2530 CD2 LEU A 529-19.995 58. 885 51. 729 1.00 25.67 2531 C LEU A 529-16.791 56. 333 50. 971 1.00 27.32 2532 0 LEU A 529-16.107 56. 850 50. 087 1.00 26.65 2533 N GLU A 530-16.491 55. 221 51. 592 1.00 28.06 2534 CA GLU A 530-15.226 54. 479 51. 437 1.00 28.46 2535 CB GLU A 530-15.161 53. 405 52. 499 1.00 31.12 2536 CG GLU A 530-13.975 52. 499 52. 743 1.00 33.75 2537 CD GLU A 530-14.187 51. 561 53. 945 1.00 34.89 2538 OE1 GLU A 530-14.879 51. 872 54. 900 1.00 34.84 2539 OE2 GLU A 530-13.620 50. 477 53. 775 1.00 35.71 2540 C GLU A 530-14.946 53. 991 50. 065 1.00 28. 22 2541 0 GLU A 530-13.762 54. 009 49. 623 1.00 29.27 2542 N PHE A 531-15. 957 53. 515 49. 365 1. 00 27.43 2543 CA PHE A 531-15.869 53. 004 48. 008 1.00 26.26 2544 CB PHE A 531-17.062 52. 139 47. 575 1.00 25.80 2545 CG PHE A 531-16.994 51. 833 46. 094 1.00 27.34 2546 CD1 PHE A 531-16.058 50. 938 45. 594 1.00 27.08 2547 CD2 PHE A 531-17.876 52. 453 45. 208 1.00 26.33 2548 CE1 PHE A 531-15.951 50. 724 44. 223 1.00 27.66 2549 CE2 PHE A 531-17.803 52. 240 43. 847 1.00 26.27 2550 CZ PHE A 531-16.816 51. 376 43. 349 1.00 27.42 2551 C PHE A 531-15.502 54. 149 47. 068 1.00 25.31 2552 0 PHE A 531-14.418 54. 126 46. 483 1.00 24.90 2553 N TRP A 532-16.371 55. 124 46. 921 1.00 24.11 2554 CA TRP A 532-16.230 56. 262 46. 042 1.00 23.03 2555 CB TRP A 532-17.481 57. 097 46. 019 1.00 20.31 2556 CG TRP A 532-18.720 56. 420 45. 506 1.00 18.54 2557 CD2 TRP A 532-18.881 55. 905 44. 165 1.00 17.00 2558 CE2 TRP A 532-20.189 55. 443 44. 052 1.00 17.29 2559 CE3 TRP A 532-18.036 55. 852 43. 066 1.00 16.63 2560 CD1 TRP A 532-19.890 56. 216 46. 153 1.00 17.43 2561 NE1 TRP A 532-20.803 55. 618 45. 277 1.00 18.64 2562 CZ2 TRP A 532-20.697 54. 903 42. 888 1.00 16.32 2563 CZ3 TRP A 532-18.514 55. 282 41. 897 1.00 16.41 2564 CH2 TRP A 532-19. 841 54. 814 41. 815 1. 00 17.14 2565 C TRP A 532-14. 996 57. 098 46. 244 1. 00 23.06 2566 0 TRP A 532-14. 453 57. 708 45. 257 1. 00 23.50 2567 N GLU A 533-14. 644 57. 262 47. 511 1. 00 23.00 2568 CA GLU A 533-13. 422 58. 080 47. 794 1. 00 22.41 2569 CB GLU A 533-13. 126 58. 176 49. 277 1. 00 21.65 2570 CG GLU A 533-11. 884 59. 078 49. 598 1. 00 21.27 2571 CD GLU A 533-11. 469 58. 989 51. 016 1. 00 22.53 2572 OE1 GLU A 533-12. 232 59. 024 51. 938 1. 00 22.99 2573 OE2 GLU A 533-10. 216 58. 824 51. 174 1. 00 24.34 2574 C GLU A 533-12. 259 57. 250 47. 195 1. 00 22.36 2575 0 GLU A 533-11. 277 57. 688 46. 614 1. 00 21.94 2576 N GLY A 534-12. 454 55. 949 47. 411 1. 00 22.99 2577 CA GLY A 534-11. 464 54. 957 46. 931 1. 00 22.82 2578 C GLY A 534-11. 322 55. 064 45. 432 1. 00 23.14 2579 O GLY A 534-10. 182 54. 991 44. 942 1. 00 23.74 2580 N VAL A 535-12. 407 55. 144 44. 684 1. 00 22.93 2581 CA VAL A 535-12. 330 55. 215 43. 222 1. 00 22.74 2582 CB VAL A 535-13. 672 54. 842 42. 576 1. 00 23.10 2583 CG1 VAL A 535-14. 795 55. 677 43. 210 1. 00 25.74 2584 CG2 VAL A 535-13. 778 55. 072 41. 097 1. 00 24.38 2585 C VAL A 535 -11.627 56.469 42.748 1. 00 22.34 25860 VAL A535-10. 70456. 35241. 9331. 00 21.98 2587 N PHE A 536-12. 074 57. 624 43. 175 1. 00 22.40 2588 CA PHE A 536-11. 589 58. 942 42. 776 1. 00 21.83 2589 CB PHE A 536-12. 534 60. 076 43. 245 1. 00 20.51 2590 CG PHE A 536-13. 830 60. 083 42. 480 1. 00 18.12 2591 CD1 PHE A 536-13. 889 60. 813 41. 290 1. 00 16.79 2592 CD2 PHE A 536-14. 912 59. 310 42. 860 1. 00 17.83 2593 CE1 PHE A 536-15. 040 60. 828 40. 532 1. 00 17.13 2594 CE2 PHE A 536-16. 091 59. 297 42. 088 1. 00 16.75 2595 CZ PHE A 536-16. 158 60. 077 40. 924 1. 00 16.33 2596 C PHE A 536-10. 137 59. 137 43. 146 1. 00 22.56 2597 0 PHE A 536-9. 404 59. 943 42. 517 1. 00 22.71 2598 N THR A 537-9. 726 58. 428 44. 171 1. 00 22.79 2599 CA THR A 537-8. 378 58. 495 44. 687 1. 00 22.99 2600 CB THR A 537-8. 168 57. 917 46. 119 1. 00 23.03 2601 OG1 THR A 537-9. 047 58. 614 47. 009 1. 00 21.98 2602 CG2 THR A 537-6. 695 58. 054 46. 596 1. 00 22.46 2603 C THR A 537-7. 327 58. 027 43. 701 1. 00 22.96 2604 0 THR A 537-6. 244 58. 682 43. 751 1. 00 23.33 2605 N GLY A 538-7. 603 57. 095 42. 834 1. 00 22.35 2606 CA GLY A 538-6. 597 56. 593 41. 872 1. 00 22.25 2607 C GLY A 538-6. 699 57. 181 40. 497 1. 00 22.83 2608 O GLY A 538-5. 997 56. 833 39. 534 1. 00 23.03 2609 N LEU A 539 -7.658 58.109 40.326 1. 00 23.15 2610 CA LEU A 539-7. 895 58. 765 39. 043 1. 00 23.48 2611 CB LEU A 539-9. 377 59. 034 38. 871 1. 00 23.03 2612 CG LEU A 539-10. 369 57. 897 38. 910 1. 00 23.41 2613 CD1 LEU A 539-11. 769 58. 479 38. 717 1. 00 23.85 2614 CD2 LEU A 539-10. 045 56. 917 37. 785 1. 00 22.52 2615 C LEU A 539-7. 033 60. 053 39. 015 1. 00 23.88 2616 0 LEU A 539-7. 613 61. 110 38. 805 1. 00 24.78 2617 N THR A 540-5. 757 59. 883 39. 151 1. 00 23.95 2618 CA THR A 540-4. 815 61. 035 39. 184 1. 00 24.39 2619 CB THR A 540-3. 625 60. 613 40. 167 1. 00 23.89 2620 OG1 THR A 540-3. 125 59. 331 39. 572 1. 00 23.87 2621 CG2 THR A 540-4.173 60. 382 41. 561 1.00 23.60 2622 C THR A 540-4.347 61. 412 37. 826 1.00 24.31 2623 O THR A 540-4.510 60. 691 36. 850 1.00 24.23 2624 N HIS A 541-3.768 62. 566 37. 728 1.00 25.38 2625 CA HIS A 541-3.208 63. 211 36. 553 1.00 26.29 2626 CB HIS A 541-1.870 62. 581 36. 137 1.00 28.70 2627 CG HIS A 541-0.859 62. 571 37. 248 1.00 30.87 2628 CD2 HIS A 541-0.131 61. 528 37. 744 1.00 31.74 2629 ND1 HIS A 541-0.389 63. 707 37. 879 1.00 31.56 2630 CE1 HIS A 541 0. 519 63. 366 38. 772 1. 00 32.25 2631 NE2 HIS A 541 0. 696 62. 068 38. 704 1. 00 32.57 2632 C HIS A 541-4.172 63. 322 35. 400 1.00 26.56 2633 O HIS A 541-3.841 62. 999 34. 235 1.00 27. 38 2634 N ILE A 542-5. 370 63. 824 35. 664 1. 00 26.25 2635 CA ILE A 542-6.349 63. 955 34. 548 1.00 26.24 2636 CB ILE A 542-7.751 64. 273 35. 194 1.00 25.12 2637 CG2 ILE A 542-7.714 65. 639 35. 918 1.00 25.05 2638 CG1 ILE A 542-8.802 64. 233 34. 058 1.00 23.44 2639 CD1 ILE A 542-10.267 64. 254 34. 554 1.00 23.68 2640 C ILE A 542-5.839 64. 931 33. 517 1.00 26.80 2641 O ILE A 542-4. 879 65.692 33.721 1. 00 27.07 2642 N ASP A 543-6.414 64. 903 32. 316 1.00 26.96 2643 CA ASP A 543-6.059 65. 819 31. 239 1.00 27.06 2644 CB ASP A 543-6.348 65. 286 29. 850 1.00 26.51 2645 CG ASP A 543-5.886 66. 298 28. 821 1.00 27.92 2646 OD1 ASP A 543-4.876 66. 031 28. 179 1.00 29.19 2647 OD2 ASP A 543-6.534 67. 376 28. 737 1.00 28.26 2648 C ASP A 543-6.906 67. 085 31. 554 1.00 27.54 2649 O ASP A 543-8.110 67. 028 31. 578 1.00 27.05 2650 N ALA A 544-6. 175 68.153 31.768 1. 00 28.69 2651 CA ALA A 544-6.732 69. 460 32. 112 1.00 29. 03 2652 CB ALA A 544-5.564 70. 380 32. 435 1.00 29.56 2653 C ALA A 544-7.655 70. 069 31. 087 1.00 29.09 2654 O ALA A 544-8.533 70. 884 31. 464 1.00 29. 52 2655 N HIS A 545-7.415 69. 801 29. 810 1.00 28.88 2656 CA HIS A 545-8.264 70. 379 28. 759 1.00 28.22 2657 CB HIS A 545-7.712 70. 701 27. 359 1.00 28.99 2658 CG HIS A 545-6.754 71. 845 27. 491 1.00 29.95 2659 ND1 HIS A 545-5.406 71. 700 27. 655 1.00 30.66 2660 CE1 HIS A 545-4.863 72. 905 27. 822 1.00 30.69 2661 NE2 HIS A 545-5.804 73. 808 27. 791 1.00 29.79 2662 CD2 HIS A 545-7.024 73. 167 27. 583 1.00 30.23 2663 C HIS A 545-9.540 69. 571 28. 642 1.00 27.19 2664 O HIS A 545-10.579 70. 136 28. 300 1.00 27.41 2665 N PHE A 546-9.390 68. 302 28. 862 1.00 25.84 2666 CA PHE A 546-10.499 67. 362 28. 815 1.00 24.63 2667 CB PHE A 546-10.063 65. 930 28. 797 1.00 21.67 2668 CG PHE A 546-9.302 65. 551 27. 564 1.00 20.65 2669 CD1 PHE A 546-9.493 66. 308 26. 414 1.00 20.23 2670 CD2 PHE A 546-8.589 64. 339 27. 516 1.00 20.19 2671 CE1 PHE A 546-8.861 65. 961 25. 220 1.00 20.47 2672 CE2 PHE A 546-7.963 63. 966 26. 324 1.00 19.60 2673 CZ PHE A 546-8.145 64. 765 25. 191 1.00 19.34 2674 C PHE A 546-11.571 67. 669 29. 875 1.00 24.36 2675 O PHE A 546-12.759 67. 557 29. 558 1.00 24.65 2676 N LEU A 547-11.130 67. 978 31. 042 1.00 23.96 2677 CA LEU A 547-11.983 68. 282 32. 194 1.00 24.28 2678 CB LEU A 547-11.080 68. 301 33. 437 1.00 21.15 2679 CG LEU A 547-11.776 68. 601 34. 743 1.00 20.04 2680 CD1 LEU A 547-12.919 67. 528 34. 917 1.00 18.30 2681 CD2 LEU A 547-10.763 68. 361 35. 847 1.00 19.71 2682 C LEU A 547-12.702 69. 615 32. 000 1.00 25.16 26830LEU A 547-13.826 69. 836 32. 490 1.00 26.14 2684 N SER A 548-11.972 70. 498 31. 378 1.00 25.80 2685 CA SER A 548-12.452 71. 871 31. 070 1.00 26.10 2686 CB SER A 548-11.333 72. 610 30. 362 1.00 27.58 2687 OG SER A 548-11.672 73. 877 29. 934 1.00 29.49 2688 C SER A 548-13.661 71. 768 30. 167 1.00 26.29 2689 O SER A 548-14.722 72. 348 30. 476 1.00 26.52 2690 N GLN A 549-13.478 71. 036 29. 086 1.00 26.15 2691 CA GLN A 549-14.523 70. 835 28. 100 1.00 26.55 2692 CB GLN A 549-14.292 70. 239 26. 815 1.00 27.00 2693 CG GLN A 549-13.672 70. 372 25. 562 1.00 27.77 2694 CD GLN A 549-12.172 70. 539 25. 632 1.00 28.53 2695 OE1 GLN A 549-11.731 71. 274 26. 515 1.00 29.49 2696 NE2 GLN A 549-11.528 69. 887 24. 685 1.00 28.30 2697 C GLN A 549-15.696 70. 032 28. 706 1.00 26.67 2698 0 GLN A 549-16.792 70. 297 28. 225 1.00 27.81 2699 N THR A 550-15.422 69. 033 29. 494 1.00 26.55 2700 CA THR A 550-16.544 68. 233 30. 022 1.00 26.37 2701 CB THR A 550-16.196 66. 797 30. 443 1.00 25.96 2702 OG1 THR A 550-15.159 66. 966 31. 459 1.00 26.69 2703 CG2 THR A 550-15.632 65. 927 29. 314 1.00 25.63 2704 C THR A 550-17.329 69. 068 31. 002 1.00 26.64 2705 0 THR A 550-18.551 68. 865 31. 044 1.00 26.12 2706 N LYS A 551-16.595 69. 991 31. 644 1.00 26.97 2707 CA LYS A 551-17.258 70. 902 32. 610 1.00 27.02 2708LYS A 551-16.300 71. 528 33. 564 1.00 24.08 2709 CG LYS A 551-15. 620 70. 655 34. 553 1. 00 23.40 2710 CD LYS A 551-14.434 71. 326 35. 229 1.00 22.81 2711 CE LYS A 551-14. 741 72. 622 35. 889 1. 00 23.18 2712LYS A 551-13.563 73. 115 36. 658 1.00 23.28 2713 C LYS A 551-18.005 71. 938 31. 786 1.00 28.58 27140LYS A 551-19.159 72. 293 32. 136 1.00 28.70 2715 N GLN A 552-17.387 72. 389 30. 699 1.00 29.73 2716 CA GLN A 552-18.042 73. 386 29. 822 1.00 31.24 2717 CB GLN A 552-17.099 74. 092 28. 849 1.00 33.56 2718 CG GLN A 552-15.964 74. 846 29. 564 1.00 36.82 2719 CD GLN A 552-15.031 75. 573 28. 629 1.00 38. 83 2720 OE1 GLN A 552-15.290 76. 733 28. 270 1.00 40.97 2721 NE2 GLN A 552-13.926 74. 943 28. 206 1.00 38.95 2722 C GLN A 552-19.268 72. 873 29. 104 1.00 31.76 2723 O GLN A 552-20.245 73. 661 28. 889 1.00 31.88 2724 N SER A 553-19.307 71. 617 28. 673 1.00 31.91 2725 CA SER A 553-20.451 71. 063 27. 958 1.00 32.36 2726 CB SER A 553-20.038 69. 877 27. 114 1.00 33.66 2727 OG SER A 553-19.609 68. 812 28. 001 1.00 34.82 2728 C SER A 553-21.621 70. 718 28. 860 1.00 32.90 2729 O SER A 553-22.652 70. 169 28. 408 1.00 33. 35 2730 N GLY A 554-21.535 70. 968 30. 134 1.00 33.05 2731 CA GLY A 554-22.607 70. 719 31. 103 1.00 33.33 2732 C GLY A 554-22.990 69. 250 31. 158 1.00 33.34 2733 O GLY A 554-24.163 68. 846 31. 241 1.00 33.92 2734 N GLU A 555-21.975 68. 413 31. 179 1.00 33.21 2735 CA GLU A 555-22.238 66. 966 31. 213 1.00 32.32 2736 CB GLU A 555-21.369 66. 257 30. 251 1.00 35.15 2737 CG GLU A 555-21.869 64. 810 29. 924 1.00 35.95 2738 CD GLU A 555-21.100 64. 337 28. 731 1.00 36.92 2739 OE1 GLU A 555-21.623 64. 014 27. 691 1.00 37.75 2740 OE2 GLU A 555-19.888 64. 466 28. 982 1.00 38. 15 2741 C GLU A 555-22.364 66. 441 32. 604 1.00 30.71 27420 GLU A 555-21.911 67. 108 33. 556 1.00 30.31 2743 N ASN A 556-22.970 65. 234 32. 789 1.00 29.34 2744 CA ASN A 556-23.236 64. 730 34. 113 1.00 28.44 2745 CB ASN A 556-24.441 63. 793 34. 268 1.00 29.01 2746 CG ASN A 556-24.918 63. 803 35. 703 1.00 30.61 2747 OD1 ASN A 556-25.772 64. 650 36. 122 1.00 31.51 2748 ND2 ASN A 556-24.445 62. 889 36. 534 1.00 31.02 2749 C ASN A 556-22.066 64. 279 34. 953 1.00 27.13 2750 0 ASN A 556-22.243 64. 392 36. 206 1.00 28. 62 2751 N LEU A 557-21.038 63. 721 34. 393 1.00 24.49 2752 CA LEU A 557-19.906 63. 314 35. 297 1.00 21.86 2753 CB LEU A 557-19.987 61. 834 35. 601 1.00 19.84 2754 CG LEU A 557-21.095 61. 461 36. 550 1.00 20.11 2755 CD1 LEU A 557-21.351 59. 969 36. 675 1.00 19.26 2756 CD2 LEU A 557-20.628 61. 868 37. 972 1.00 19.96 2757 C LEU A 557-18. 671 63. 730 34. 522 1. 00 20.37 2758 0 LEU A 557-18.120 62. 858 33. 893 1.00 19.58 2759 N PRO A 558-18.440 65. 043 34. 563 1.00 19.78 2760 CD-PRO A 558-19.150 66. 046 35. 389 1.00 19.17 2761 CA PRO A 558-17.310 65. 605 33. 847 1.00 19.32 2762 CB PRO A 558-17.427 67. 104 34. 074 1.00 19.08 2763 CG PRO A 558-18.325 67. 313 35. 238 1.00 19.20 2764 C PRO A 558-15.973 65. 031 34. 272 1.00 18.90 2765 0 PRO A 558-15.028 64. 994 33. 462 1.00 19.13 2766 N TYR A 559-15.899 64. 593 35. 532 1.00 18.95 2767 CA TYR A 559-14.594 64. 086 36. 010 1.00 18.80 2768 CB TYR A 559-14.435 64. 044 37. 532 1.00 19.00 2769 CG TYR A 559-12.981 63. 930 37. 932 1.00 18.84 2770 CD1 TYR A 559-12.210 65. 105 37. 876 1.00 17.93 2771 CE1 TYR A 559-10.869 65. 100 38. 173 1.00 18.83 2772 CD2 TYR A 559-12.337 62. 745 38. 228 1.00 19.36 2773 CE2 TYR A 559-10.970 62. 702 38. 500 1.00 19.24 2774 CZ TYR A 559-10.241 63. 889 38. 449 1.00 19.82 2775 OH TYR A 559-8.899 63. 854 38. 722 1.00 20. 98 2776 C TYR A 559-14.410 62. 729 35. 354 1.00 18.33 2777 O TYR A 559-13.440 62. 549 34. 634 1.00 18.70 2778 N LEU A 560-15.381 61. 865 35. 625 1.00 17.65 2779 CA LEU A 560-15.297 60. 512 35. 050 1.00 17.81 2780 CB LEU A 560-16.268 59. 612 35. 684 1.00 15.14 2781 CG LEU A 560-16.246 59. 316 37. 168 1.00 14.25 2782 CD1 LEU A 560-17.305 58. 169 37. 396 1.00 12.67 2783 CD2 LEU A 560-14.880 58. 720 37. 522 1.00 13.42 2784 C LEU A 560-15.231 60. 571 33. 549 1.00 18.43 2785 0 LEU A 560-14.501 59. 751 32. 931 1.00 19.16 2786 N VAL A 561-16.000 61. 482 32. 952 1.00 18.36 2787 CA VAL A 561-15.943 61. 613 31. 502 1.00 18.56 2788 CB VAL A 561-17.089 62. 489 30. 969 1.00 17.35 2789 CG1 VAL A 561-16.969 62. 681 29. 455 1.00 16.76 2790 CG2 VAL A 561-18.398 61. 743 31. 291 1.00 16. 29 2791 C VAL A 561-14.561 62. 018 31. 041 1.00 19.25 2792 0 VAL A 561-13.987 61. 336 30. 157 1. 00 19.84 2793 N ALA A 562-13.966 63. 076 31. 569 1. 00 19.39 2794 CA ALA A 562-12.661 63. 539 31. 132 1. 00 19.53 2795 CB ALA A 562-12.371 64. 930 31. 624 1. 00 18.89 2796 C ALA A 562-11.562 62. 529 31. 428 1. 00 19.88 2797 0 ALA A 562-10.642 62. 378 30. 649 1. 00 20.09 2798 N TYR A 563-11.708 61. 795 32. 523 1. 00 20.84 2799 CA TYR A 563-10.724 60. 791 32. 941 1. 00 20.97 2800 CB TYR A 563-10.926 60. 401 34. 416 1. 00 20.16 2801 CG TYR A 563-9.630 59. 739 34. 898 1. 00 19.75 2802 CD1 TYR A 563-8.636 60. 623 35. 349 1. 00 19.23 2803 CE1 TYR A 563-7.390 60. 154 35. 746 1. 00 18.52 2804 CD2 TYR A 563-9.325 58. 393 34. 831 1f. 00 19.17 2805 CE2 TYR A 563-8.084 57. 918 35. 246 1. 00 19.04 2806 CZ TYR A 563-7.106 58. 812 35. 655 1. 00 19.82 2807 OH TYR A 563-5.888 58. 340 36. 099 1. 00 20.13 2808 C TYR A 563-10.675 59. 590 32. 002 1. 00 21.52 2809 0 TYR A 563-9.572 59. 133 31. 613 1. 00 22.12 2810 N GLN A 564-11.827 59. 070 31. 601 1. 00 21.51 2811 CA GLN A 564-11.909 57. 955 30. 612 1. 00 21.39 2812 CB GLN A 564-13.352 57. 547 30. 357 1. 00 19.77 2813 CG GLN A 564-13.575 56. 509 29. 251 1. 00 18.27 2814 CD GLN A 564-13.048 55. 134 29. 477 1. 00 16.19 2815 OE1 GLN A 564-13.687 54. 328 30. 154 1. 00 14.94 2816 NE2 GLN A 564-11.860 54. 789 28. 944 1. 00 16.77 2817 C GLN A 564-11.294 58. 445 29. 293 1. 00 21.88 2818 O GLN A 564-10.729 57. 677 28. 496 1. 00 23.13 2819 N ALA A 565-11.367 59. 710 29. 041 1. 00 21.77 2820 CA ALA A 565-10.902 60. 452 27. 893 1. 00 22.09 2821 CB ALA A 565-11.582 61. 775 27. 723 1. 00 22.42 2822 C ALA A 565-9.366 60. 589 27. 945 1. 00 22.01 28230 ALA A 565-8.741 60. 412 26. 912 1. 00 21.52 2824 N THR A 566-8.877 60. 824 29. 147 1. 00 22.44 2825 CA THR A 566-7.441 60. 902 29. 426 1. 00 22.82 2826 CB THR A 566-7.132 61. 407 30. 899 1. 00 22.48 2827 OG1 THR A 566-7.825 62. 666 30. 941 1. 00 22.74 2828 CG2 THR A 566-5.615 61. 711 31. 132 1. 00 21.99 2829 C THR A 566-6.769 59. 557 29. 152 1. 00 23.39 2830 0 THR A 566-5.802 59. 441 28. 391 1. 00 23.74 2831 N VAL A 567-7.329 58. 507 29. 758 1. 00 24.20 2832 CA VAL A 567-6.820 57. 154 29. 568 1. 00 24.11 2833 CB VAL A 567-7.692 56. 135 30. 357 1. 00 24.19 2834 CG1 VAL A 567-7.252 54. 739 30. 046 1. 00 23.57 2835 CG2 VAL A 567-7.569 56. 431 31. 849 1. 00 24.75 2836 C VAL A 567-6.795 56. 827 28. 078 1. 00 24.11 2837 0 VAL A 567-5.863 56. 138 27. 666 1. 00 23.90 2838 N CYS A 568-7.844 57. 236 27. 343 1. 00 24.06 2839 CA CYS A 568-7.935 56. 969 25. 915 1. 00 24.04 2840 CB CYS A 568-9.297 57. 301 25. 293 1. 00 21.95 2841 SG CYS A 568-10. 571 56. 143 25. 833 1. 00 19. 41 2842 C CYS A 568-6.812 57. 618 25. 143 1. 00 25.27 2843 0 CYS A 568-6.014 56. 942 24. 485 1. 00 26.06 2844 N ALA A 569-6.765 58. 947 25. 293 1. 00 25.45 2845 CA ALA A 569-5. 767 59. 772 24. 646 1. 00 26. 16 2846 CB ALA A 569-5-851 61. 195 25. 192 1. 00 25. 64 2847 C ALA A 569-4. 348 59. 260 24. 946 1. 00 27. 13 2848 O ALA A 569 -3.495 59.463 24.049 1.00 27. 65 2849 N ARG A 570-4.119 58. 726 26. 137 1.00 27.46 2850 CA ARG A 570-2.771 58. 240 26. 512 1.00 27.89 2851 CB ARG A 570-2. 363 58. 384 27. 986 1. 00 27.58 2852ARG A 570-2.223 59. 840 28. 406 1.00 27.82 2853 CD ARG A 570-2.144 60. 030 29. 878 1.00 29.05 2854 NE ARG A 570-2.210 61. 520 30. 078 1.00 29.89 2855 CZ ARG A 570-2.329 62. 033 31. 293 1.00 30.40 2856 NH1 ARG A 570-2.373 61. 198 32. 355 1.00 30.32 2857 NH2 ARG A 570-2.541 63. 359 31. 357 1.00 29.14 2858 C ARG A 570-2.508 56. 786 26. 158 1.00 28.20 2859 0 ARG A 570-1.405 56. 294 26. 510 1.00 28.37 2860 N ALA A 571-3.442 56. 134 25. 561 1.00 28.50 2861 CA ALA A 571-3.274 54. 713 25. 157 1.00 28.97 2862 CB ALA A 571-4.266 53. 876 25. 931 1.00 29.23 2863 C ALA A 571-3.542 54. 715 23. 659 1.00 29.93 28640ALA A 571-3.655 53. 666 23. 016 1.00 30.38 2865 N GLN A 572-3. 619 55. 943 23. 134 1. 00 30.05 2866 CA GLN A 572-3.924 56. 159 21. 719 1.00 30.25 2867 CB GLN A 572-2.740 55. 996 20. 810 1.00 32.93 2868 CG GLN A 572-1.552 56. 899 21. 036 1.00 35.95 2869 CD GLN A 572-0.500 56. 678 19. 964 1.00 38.40 2870 OE1 GLN A 572-0.836 56. 310 18. 819 1.00 39.92 2871 NE2 GLN A 572 0. 754 56. 885 20. 323 1. 00 38.77 2872 C GLN A 572-5.054 55. 197 21. 279 1.00 29.60 2873 O GLN A 572-5.006 54. 710 20. 129 1.00 29.91 2874 N ALA A 573-6.011 55. 009 22. 148 1.00 28.58 2875 CA ALA A 573-7.186 54. 144 21. 885 1.00 27.68 2876 CB ALA A 573-7. 335 53. 066 22. 931 1. 00 26.71 2877 C ALA A 573-8.424 55. 026 21. 790 1.00 27.12 2878 O ALA A 573-8.451 56. 166 22. 317 1.00 26.79 2879 N PRO A 574-9.430 54. 500 21. 114 1.00 26.32 2880 CD PRO A 574-9.429 53. 162 20. 469 1.00 26.37 2881 CA PRO A 574-10.693 55. 188 20. 865 1.00 25.62 2882PRO A 574-11.343 54. 346 19. 739 1.00 26.06 2883 CG PRO A 574-10.233 53. 481 19. 193 1.00 26.27 2884 C PRO A 574-11.602 55. 211 22. 074 1.00 24.72 2885 0 PRO A 574-11.481 54. 359 22. 956 1.00 25. 10 2886 N PRO A 575-12.506 56. 175 22. 093 1.00 24.09 2887 CD PRO A 575-12.660 57. 242 21. 080 1.00 23. 93 2888 CA PRO A 575-13.481 56. 321 23. 197 1.00 23. 32 2889 CB PRO A 575-14.127 57. 665 22. 949 1.00 23.47 2890PRO A 575-13.883 58. 008 21. 512 1.00 23. 64 2891 C PRO A 575-14.476 55. 169 22. 961 1.00 23.09 2892 0 PRO A 575-14.435 54. 688 21. 824 1.00 23.84 2893 N PRO A 576-15.278 54. 875 23. 944 1.00 22.55 2894 CD PRO A 576-15.217 55. 514 25. 296 1.00 21.86 2895 CA PRO A 576-16.248 53. 778 23. 921 1.00 21.99 2896PRO A 576-16.909 53. 827 25. 279 1.00 21.42 2897 CG PRO A 576-15.941 54. 518 26. 162 1.00 21.52 2898 C PRO A 576-17.195 53. 804 22. 765 1.00 22.43 2899 0 PRO A 576-17.632 52. 727 22. 320 1.00 22.69 2900 N SER A 577-17.488 54. 977 22. 260 1.00 22.27 2901 CA SER A 577-18.339 55. 261 21. 113 1.00 22.30 2902 CB SER A 577-19.823 55. 142 21. 438 1.00 21. 14 2903 OG SER A 577-20.143 56. 027 22. 507 1.00 20.33 2904 C SER A 577-18.069 56. 732 20. 727 1.00 22.78 2905 0 SER A 577-17.352 57. 445 21. 427 1.00 23.40 2906 N TRP A 578-18.688 57. 178 19. 663 1.00 23.37 2907 CA TRP A 578-18.560 58. 541 19. 182 1.00 23.42 2908 CB TRP A 578-17.886 58. 734 17. 861 1.00 23.28 2909 CG TRP A 578-16.424 58. 400 17. 737 1.00 23.77 2910 CD2 TRP A 578-15.352 59. 313 18. 140 1.00 23.65 2911 CE2 TRP A 578-14.125 58. 640 17. 895 1.00 23.61 2912 CE3 TRP A 578-15.336 60. 580 18. 696 1.00 23.80 2913 CD1 TRP A 578-15.813 57. 278 17. 308 1.00 23.80 2914 NE1 TRP A 578-14.425 57. 409 17. 384 1.00 23.85 2915 CZ2 TRP A 578-12.914 59. 230 18. 191 1.00 23.60 2916 CZ3 TRP A 578-14.132 61. 179 18. 982 1.00 23.46 2917 CH2 TRP A 578-12. 925 60. 500 18. 736 1. 00 23.62 2918 C TRP A 578-19.795 59. 362 19. 553 1.00 24.03 2919 O TRP A 578-20.161 60. 279 18. 819 1.00 23.96 2920 N ASP A 579-20.387 59. 071 20. 690 1.00 24.60 2921 CA ASP A 579-21.531 59. 827 21. 264 1.00 24.88 2922 CB ASP A 579-22.082 59. 195 22. 515 1.00 26.67 2923 CG ASP A 579-23.235 59. 818 23. 257 1.00 27.75 2924 ou1 ASP A 579-24.436 59. 514 22. 961 1.00 29.13 2925 OD2 ASP A 579-23.044 60. 616 24. 219 1.00 27.51 2926 C ASP A 579-20.902 61. 224 21. 552 1.00 24.89 2927 0 ASP A 579-19.693 61. 304 21. 666 1.00 23.89 2928 N GLN A 580-21. 790 62. 219 21. 636 1. 00 25.07 2929 CA GLN A 580-21.293 63. 594 21. 909 1.00 25.48 2930 CB GLN A 580-22.464 64. 572 21. 818 1.00 29.48 2931 CG GLN A 580-23. 461 64. 358 22. 963 1. 00 33.78 2932 CD GLN A 580-24.760 65. 099 22. 770 1.00 36.97 2933 OE1 GLN A 580-24.878 66. 171 22. 152 1.00 38.74 2934 NE2 GLN A 580-25.832 64. 454 23. 252 1.00 37.52 2935 C GLN A 580-20.636 63. 649 23. 280 1.00 24.36 2936 0 GLN A 580-20.049 64. 700 23. 638 1.00 24.40 2937 N MET A 581-20.747 62. 610 24. 053 1.00 23.91 2938 CA MET A 581-20.143 62. 524 25. 411 1.00 23.72 2939 CB MET A 581-20. 622 61. 300 26. 159 1. 00 22.54 2940 CG MET A 581-19.878 61. 078 27. 438 1.00 21.52 2941 SD MET A 581-20.613 59. 696 28. 381 1.00 20.60 2942 CE MET A 581-22.111 60. 361 29. 005 1.00 18.94 2943 C MET A 581-18.629 62. 577 25. 336 1.00 23.68 2944 0 MET A 581-17.901 63. 101 26. 205 1.00 24.45 2945 N TRP A 582-18.160 62. 084 24. 211 1.00 23.28 2946 CA TRP A 582-16.705 61. 971 23. 969 1.00 22.35 2947 CB TRP A 582-16.471 60. 517 23. 561 1.00 17.71 2948 CG TRP A 582-17.019 59. 478 24. 474 1.00 15.38 2949 CD2 TRP A 582-16.641 59. 171 25. 812 1.00 13.25 2950 CE2 TRP A 582-17.468 58. 106 26. 250 1.00 13.55 2951 CE3 TRP A 582-15.699 59. 678 26. 695 1.00 11.93 2952 CD1 TRP A 582-18.045 58. 617 24. 159 1.00 13.48 2953 NE1 TRP A 582-18.301 57. 783 25. 208 1.00 13.90 2954 CZ2 TRP A 582-17.374 57. 577 27. 535 1.00 11.77 2955 CZ3 TRP A 582-15.639 59. 217 27. 963 1.00 10.82 2956 CH2 TRP A 582-16.456 58. 130 28. 399 1.00 11.48 2957 C TRP A 582-16.157 62. 939 22. 982 1.00 23.08 2958 O TRP A 582-15.087 62. 658 22. 367 1.00 23.74 2959 N LYS A 583-16.837 64. 048 22. 754 1.00 24.21 2960 CA LYS A 583-16.383 65. 025 21. 753 1.00 24.98 2961 CB LYS A 583-17.478 66. 012 21. 335 1.00 26.40 2962 CG LYS A 583-18.031 66. 770 22. 537 1.00 27.90 2963 CD LYS A 583-19.147 67. 714 22. 258 1.00 28.94 2964 CE LYS A 583-19.633 68. 339 23. 554 1.00 30.58 2965LYS A 583-20. 735 69. 290 23. 293 1. 00 31.99 2966 C LYS A 583-15.049 65. 653 22. 014 1.00 24.98 2967 0 LYS A 583-14.425 66. 198 21. 064 1.00 24.93 2968 N CYS A 584-14.505 65. 518 23. 224 1.00 25.06 2969 CA CYS A 584-13.198 66. 127 23. 525 1.00 25.07 2970 CB CYS A 584-12.862 66. 224 24. 991 1.00 24.53 2971 SG CYS A 584-12.723 64. 689 25. 922 1.00 23.91 2972 C CYS A 584-12.101 65. 439 22. 715 1.00 25.54 2973 0 CYS A 584-11.035 66. 049 22. 573 1.00 25.30 2974 N LEU A 585-12.422 64. 232 22. 219 1.00 25.95 2975 CA LEU A 585-11.451 63. 450 21. 472 1.00 27.05 2976 CB LEU A 585-11.489 61. 985 21. 950 1.00 25.82 2977 CG LEU A 585-11.182 61. 646 23. 384 1.00 24.20 2978 CD1 LEU A 585-11.315 60. 170 23. 675 1.00 22. 94 2979 CD2 LEU A 585-9. 798 62. 145 23. 770 1. 00 22.09 2980 C LEU A 585-11.503 63. 597 19. 974 1.00 28. 39 2981 O LEU A 585-10.630 62. 984 19. 295 1.00 29.44 2982 N ILE A 586-12.405 64. 385 19. 456 1.00 29.15 2983 CA ILE A 586-12.569 64. 622 18. 017 1.00 29.93 2984 CB ILE A 586-13.846 65. 461 17. 721 1.00 31.07 2985 CG1 ILE A 586-15.101 64. 610 18. 098 1.00 31.64 2986 CD1 ILE A 586-16.449 65. 322 17. 785 1.00 32.32 2987 CG2 ILE A 586-13.968 65. 976-16. 263 1.00 31.03 2988 C ILE A 586-11. 313 64. 969 17. 251 1. 00 29.98 2989 0 ILE A 586-10.954 64. 217 16. 303 1.00 29.53 2990 N ARG A 587-10.608 66. 036 17. 598 1.00 29.93 2991 CA ARG A 587-9. 378 66. 425 16. 933 1. 00 30.27 2992ARG A 587-8.638 67. 607 17. 515 1.00 30.19 2993 CG ARG A 587-8.078 67. 589 18. 911 1.00 30.34 2994 CD ARG A 587-7.319 68. 832 19. 237 1.00 30.49 2995 NE ARG A 587-6.841 68. 985 20. 574 1.00 31.20 2996 CZ ARG A 587-7.470 69. 054 21. 751 1.00 32.67 2997 NH1 ARG A 587-6. 784 69.262 22.912 1. 00 31.74 2998 NH2 ARG A 587-8.815 68. 894 21. 888 1.00 33.00 2999 C ARG A 587-8.390 65. 240 16. 819 1.00 30.39 30000ARG A 587-7.642 65. 219 15. 826 1.00 30.52 3001 N LEU A 588-8.353 64. 356 17. 777 1.00 30.26 3002 CA LEU A 588-7.455 63. 209 17. 784 1.00 30.51 3003 CB LEU A 588-7.222 62. 734 19. 256 1.00 28. 88 3004 CG LEU A 588-6.370 63. 579 20. 150 1. 00 27.90 3005 CD1 LEU A 588-6.408 62. 986 21. 571 1.00 28.13 3006 CD2 LEU A 588-4.913 63. 336 19. 662 1.00 28.60 3007 C LEU A 588-8.016 61. 975 17. 105 1.00 30.96 30080LEU A 588-7. 325 60. 946 17. 136 1. 00 31.15 3009 N LYS A 589-9.241 62. 073 16. 661 1.00 31.76 3010 CA LYS A 589-9.957 60. 968 16. 081 1.00 32.57 3011 CB LYS A 589-11.252 61. 333 15. 396 1.00 32.97 3012 CG LYS A 589-11.985 60. 028 15. 012 1.00 33.32 3013 CD LYS A 589-13.325 60. 299 14. 417 1.00 33.37 3014 CE LYS A 589-14.030 58. 931 14. 207 1.00 34.24 3015LYS A 589-15.404 59. 254 13. 779 1.00 34.82 3016 C LYS A 589-9.168 59. 935 15. 340 1.00 33.49 30170LYS A 589-9.129 58. 764 15. 814 1.00 34.00 3018 N PRO A 590-8.558 60. 262 14. 229 1.00 34.00 3019 CD PRO A 590-8.579 61. 620 13. 636 1.00 34.39 3020 CA PRO A 590-7.780 59. 342 13. 412 1.00 34.63 3021 CB PRO A 590-7.303 60. 163 12. 218 1.00 34.62 3022 CG PRO A 590-7.388 61. 588 12. 665 1.00 34.55 3023 C PRO A 590-6.592 58. 654 14. 061 1.00 35.04 3024 0 PRO A 590-6.139 57. 583 13. 564 1.00 35.53 3025 N THR A 591-6.076 59. 199 15. 098 1.00 34.59 3026 CA THR A 591-4.919 58. 765 15. 881 1.00 34.26 3027 CB THR A 591-4.526 60. 099 16. 695 1.00 35.49 3028 OG1 THR A 591-4.294 61. 073 15. 596 1.00 35.94 3029 CG2 THR A 591-3.443 60. 003 17. 706 1.00 35.93 3030 C THR A 591-5.238 57. 604 16. 796 1.00 33.42 3031 O THR A 591-4.388 56. 776 17. 146 1.00 33.57 3032 N LEU A 592-6.507 57. 528 17. 141 1.00 32.48 3033 CA LEU A 592-7.090 56. 539 18. 060 1.00 31.35 3034 CB LEU A 592-8.254 57. 319 18. 720 1.00 28. 86 3035 CG LEU A 592-7.846 58. 723 19. 199 1.00 27.61 3036 CD1 LEU A 592-9.029 59. 396 19. 848 1.00 26.80 3037 CD2 LEU A 592-6.632 58. 659 20. 091 1.00 25.70 3038 C LEU A 592-7.448 55. 272 17. 328 1.00 31.43 30390 LEU A 592-8.171 55. 306 16. 309 1.00 31.68 3040 N HIS A 593-6.931 54. 156 17. 841 1.00 31.74 3041 CA HIS A 593-7.140 52. 829 17. 215 1.00 31.60 3042 CB HIS A 593-5.967 52. 442 16. 245 1.00 34.00 3043 CG HIS A 593-5.705 53. 498 15. 221 1.00 35.72 3044 CD2 HIS A 593-6.129 53. 647 13. 944 1.00 36.50 3045 ND1 HIS A 593-4.845 54. 555 15. 480 1.00 36.05 3046 CE1 HIS A 593-4.761 55. 306 14. 398 1.00 36.54 3047 NE2 HIS A 593-5.536 54. 798 13. 456 1.00 36.60 3048 C HIS A 593-7.082 51. 768 18. 303 1.00 30.98 3049 0 HIS A 593-6.475 52. 025 19. 363 1.00 31.14 3050 N GLY A 594-7.656 50. 619 17. 971 1.00 30.44 3051 CA GLY A 594-7.727 49. 498 18. 889 1.00 29.64 3052 C GLY A 594-8.943 49. 513 19. 805 1.00 29.32 3053 O GLY A 594-9.920 50. 296 19. 680 1.00 29.55 3054 N PRO A 595-8.897 48. 574 20. 764 1.00 28.41 3055 CD PRO A 595-7.780 47. 618 20. 926 1.00 27.97 3056 CA PRO A 595-9.943 48. 402 21. 771 1.00 28.02 3057 CB PRO A 595-9.627 47. 006 22. 354 1.00 28.10 3058 CG PRO A 595-8.184 46. 803 22. 119 1.00 28. 09 3059 C PRO A 595-9.876 49. 408 22. 903 1.00 27.36 3060 0 PRO A 595-8.790 49. 659 23. 458 1.00 29.11 3061 N THR A 596-10.976 49. 958 23. 349 1.00 25.92 3062 CA THR A 596-11.048 50. 915 24. 439 1.00 23.74 3063 CB THR A 596-12.551 51. 463 24. 573 1.00 21.32 3064 OG1 THR A 596-12.795 52. 077 23. 309 1.00 21.19 3065 CG2 THR A 596-12.702 52. 376 25. 785 1.00 19.69 3066 C THR A 596-10.714 50. 272 25. 773 1.00 22.94 3067 0 THR A 596-11.300 49. 219 26. 101 1.00 23.28 3068 N PRO A 597-9.907 50. 937 26. 516 1.00 22.46 3069 CD PRO A 597-9.205 52. 197 26. 173 1.00 22.83 3070 CA PRO A 597-9.551 50. 491 27. 908 1.00 22.19 3071 CB PRO A 597-8.221 51. 145 28. 101 1.00 22.11 3072 CG PRO A 597-8.012 52. 188 27. 061 1.00 21. 87 3073 C PRO A 597-10.670 51. 100 28. 795 1.00 21.82 3074 0 PRO A 597-10.595 52. 207 29. 340 1.00 20.98 3075 N LEU A 598-11.720 50. 317 28. 949 1.00 20.99 3076 CA LEU A 598-12.968 50. 652 29. 643 1.00 19.68 3077 CB LEU A 598-14.102 49. 714 29. 128 1.00 19.38 3078 CG LEU A 598-15.513 50. 009 29. 627 1.00 19.96 3079 CD1 LEU A 598-16.019 51. 321 29. 033 1.00 19.54 3080 CD2 LEU A 598-16.442 48. 888 29. 307 1.00 19.16 3081 C LEU A 598-12.746 50. 645 31. 115 1.00 18.56 30820 LEU A 598-12.218 49. 642 31. 658 1.00 19.11 3083 N LEU A 599-13.112 51. 771 31. 754 1.00 16.24 3084 CA LEU A 599-12.912 51. 898 33. 195 1.00 15.42 3085 CB LEU A 599-12. 493 53.397 33.429 1. 00 14.52 3086 CG LEU A 599-11. 263 53.905 32.826 1. 00 14.37 3087 CD1 LEU A 599-10.908 55. 362 33. 080 1.00 13.54 3088 CD2 LEU A 599-10.077 53. 025 33. 323 1.00 14.83 3089 C LEU A 599-14.243 51. 711 33. 929 1.00 14.79 3090 0 LEU A 599-14.328 51. 306 35. 087 1.00 15.00 3091 N TYR A 600-15.239 52. 139 33. 176 1.00 14.32 3092 CA TYR A 600-16.634 52. 091 33. 686 1.00 14.81 3093 CB TYR A 600-16. 689 52.892 35.007 1. 00 10.88 3094 CG TYR A 600-15.906 54. 220 34. 837 1.00 9.67 3095 CD1 TYR A 600-16.116 55. 035 33. 742 1.00 8.17 3096 CE1 TYR A 600-15.418 56. 215 33. 579 1.00 8.55 3097 CD2 TYR A 600-15.079 54. 606 35. 839 1.00 8.78 3098 CE2 TYR A 600-14.352 55. 839 35. 702 1.00 7.18 3099 CZ TYR A 600-14.496 56. 556 34. 574 1.00 8.46 3100 OH TYR A 600-13.811 57. 793 34. 479 1.00 11.04 3101 C TYR A 600-17.573 52. 420 32. 568 1.00 15.46 3102 0 TYR A 600-17.116 52. 866 31. 483 1.00 15.72 3103 N ARG A 601-18.830 52. 209 32. 821 1.00 16.75 3104 CA ARG A 601-19.877 52. 478 31. 777 1.00 17.19 3105 CB ARG A 601-20.644 51. 157 31. 595 1.00 18.54 3106 CG ARG A 601-19.906 50. 030 30. 872 1.00 21.05 3107 CD ARG A 601-20.654 48. 719 30. 926 1.00 21.82 3108 NE ARG A 601-19.978 47. 618 30. 293 1.00 22.91 3109 CZ ARG A 601-19.907 47. 280 29. 012 1.00 23.92 3110 NH1 ARG A 601-20.575 47. 913 28. 067 1.00 22.75 3111 NH2 ARG A 601-19.052 46. 319 28. 591 1.00 25.08 3112 C ARG A 601-20.727 53. 655 32. 126 1.00 17.61 3113 O ARG A 601-21.293 53. 723 33. 211 1.00 17.59 3114 N LEU A 602-20.785 54. 633 31. 204 1.00 18.35 3115 CA LEU A 602-21.547 55. 843 31. 278 1.00 17.87 3116 CB LEU A 602-20. 552 57. 033 31. 255 1. 00 16.76 3117 CG LEU A 602-19.434 57. 054 32. 267 1.00 15.27 3118 CD1 LEU A 602-18.613 58. 316 32. 150 1.00 15.62 3119 CD2 LEU A 602-19.935 56. 782 33. 661 1.00 15.60 3120 C LEU A 602-22.583 55. 983 30. 163 1.00 18.40 3121 O LEU A 602-23.390 56. 881 30. 212 1.00 18.82 3122 N GLY A 603-22.588 55. 144 29. 152 1.00 19.35 3123 CA GLY A 603-23. 416 55.069 27.996 1. 00 19.50 3124 C GLY A 603-23.149 53. 764 27. 223 1.00 20.47 31250 GLYA 603-22.394 52. 888 27. 671 1.00 21.19 3126 N ALA A 604-23.799 53. 666 26. 078 1.00 20.17 3127 CA ALA A 604-23.612 52. 541 25. 143 1.00 19.70 3128 CB ALA A 604-24.480 52. 827 23. 911 1.00 18. 09 3129 C ALA A 604-22.118 52. 584 24. 749 1.00 19.65 31300 ALA A 604-21.514 53. 689 24. 611 1.00 20.23 3131 N VAL A 605-21.517 51. 472 24. 668 1.00 19.56 3132 CA VAL A 605-20.167 51. 117 24. 314 1.00 19.03 3133 CB VAL A 605-19.519 50. 347 25. 472 1. 00 18.57 3134 CG1 VAL A 605-18. 103 49. 843 25. 138 1. 00 17.38 3135 CG2 VAL A 605-19. 411 51. 104 26. 792 1. 00 17.40 3136 C VAL A 605-20. 191 50. 396 22. 976 1. 00 19.65 3137 0 VAL A 605-20. 734 49. 214 22. 928 1. 00 20.29 3138 N GLN A 606-19. 635 50. 869 21. 910 1. 00 19.86 3139 CA GLN A 606-19. 626 50. 296 20. 596 1. 00 21.46 3141 CB GLN A 606 -20.119 51.198 19.427 1. 00 21.32 3141 C GLN A 606-18. 256 49. 817 20. 089 1. 00 22.82 3142 O GLN A 606 -18.259 49.071 19.088 1. 00 23.03 3143 N ASN A 607-17. 203 50. 313 20. 686 1. 00 24.11 3144 CA ASN A 607-15. 843 49. 885 20. 209 1. 00 25.15 3145 CB ASN A 607-14. 884 51. 059 20. 317 1. 00 26.26 3146 CG ASN A 607-13. 537 50. 679 19. 708 1. 00 27.95 3147 OD1 ASN A 607-13. 568 50. 147 18. 601 1. 00 27.48 3148 ND2 ASN A 607-12. 458 50. 978 20. 402 1. 00 28. 85 3149 C ASN A 607-15. 468 48. 681 21. 078 1. 00 25.43 3150 O ASN A 607-16. 024 48. 485 22. 155 1. 00 24.98 3151 N GLU A 608-14. 479 47. 940 20. 567 1. 00 26.27 3152 CA GLU A 608-13. 998 46. 762 21. 302 1. 00 27.03 3153 CB GLU A 608-12. 941 45. 978 20. 514 1. 00 29.79 3154 CG GLU A 608-12. 425 44. 757 21. 318 1. 00 32.76 3155 CD GLU A 608-11. 263 44. 019 20. 712 1. 00 34.91 3156 OE1 GLU A 608-10. 770 44. 351 19. 638 1. 00 35.54 3157 OE2 GLU A 608 -10.877 43.081 21.465 1. 00 36.19 3158 C GLU A 608-13. 364 47. 259 22. 600 1. 00 26.85 3159 0 GLU A 608-12. 906 48. 415 22. 606 1. 00 26.95 3160 N ILE A 609-13. 356 46. 458 23. 634 1. 00 26.70 3161 CA ILE A 609-12. 798 46. 856 24. 924 1. 00 27.34 3162 CB ILE A 609-13. 945 47. 076 25. 997 1. 00 26.42 3163 CG1 ILE A 609-14. 661 45. 730 26. 219 1. 00 24.58 3164 CD1 ILE A 609 -15.800 45.777 27.287 1. 00 24.89 3165 CG2 ILE A 609-14. 960 48. 168 25. 473 1. 00 26.24 3166 C ILE A 609-11. 809 45. 823 25. 492 1. 00 27.95 3167 O ILE A 609-11. 936 44. 585 25. 375 1. 00 27.45 3168 N THR A 610-10. 867 46. 425 26. 172 1. 00 28.39 3169 CA THR A 610-9. 779 45. 724 26. 899 1. 00 29.15 3170 CB THR A 610-8. 359 46. 203 26. 473 1. 00 30.61 3171 OG1 THR A 610-8. 354 47. 667 26. 718 1. 00 31.84 3172 CG2 THR A 610-7. 955 45. 939 25. 034 1. 00 31.26 3173 C THR A 610-10. 052 46. 067 28. 386 1. 00 29.33 3174 O THR A 610-10. 330 47. 257 28. 708 1. 00 29.30 3175 N LEU A 611-9. 927 45. 039 29. 201 1. 00 28.36 3176 CA LEU A 611-10. 180 45. 181 30. 634 1. 00 28.14 3177 CB LEU A 611-10. 919 43. 847 30. 927 1. 00 27.07 3178 CG LEU A 611-12. 036 43. 486 29. 951 1. 00 26.16 3179 CD1 LEU A 611-12. 615 42. 137 30. 414 1. 00 26.03 3180 CD2 LEU A 611-13. 105 44. 533 29. 914 1. 00 25.97 3181 C LEU A 611-8. 943 45. 214 31. 514 1. 00 28.28 3182 0 LEU A 611-9-128 45. 159 32. 758 1. 00 29.12 3183 N THR A 612-7. 781 45. 236 30. 946 1. 00 27.92 3184 CA THR A 612-6. 513 45. 170 31. 622 1. 00 27.67 3185 CB THR A 612-5. 589 44. 102 30. 855 1. 00 27.55 3186 OG1 THR A 612-5. 462 44. 686 29. 537 1. 00 28.34 3187 CG2 THR A 612 -6.293 42.729 30.879 1. 00 28.34 3188 C THR A 612-5. 708 46. 453 31. 759 1. 00 26.98 3189 0 THR A 612-4. 449 46. 342 31. 841 1. 00 27.65 3190 N HIS A 613-6. 378 47. 558 31. 727 1. 00 25.32 3191 CA HIS A 613-5.612 48. 839 31. 942 1. 00 24.34 3192 CB HIS A 613-6.470 50. 031 31. 493 1. 00 21.99 3193 CG HIS A 613-5.706 51. 332 31. 479 1. 00 19.87 3194 CD2 HIS A 613-5.030 51. 887 30. 467 1. 00 19.09 3195 ND1 HIS A 613-5.475 52. 089 32. 562 1. 00 18.57 3196 CE1 HIS A 613-4.754 53. 140 32. 216 1. 00 18.49 3197 NE2 HIS A 613-4.474 53. 092 30. 940 1. 00 19.11 3198 C HIS A 613-5.559 48. 787 33. 509 1. 00 24.37 3199 0 HIS A 613-6. 527 48. 308 34. 129 1. 00 24. 32 3200 N PRO A 614-4.459 49. 231 34. 073 1. 00 23.85 3201 CD PRO A 614-3.295 49. 729 33. 317 1. 00 24.64 3202 CA PRO A 614-4.266 49. 292 35. 483 1. 00 23.64 3203 CB PRO A 614-3.011 50. 185 35. 673 1. 00 24.45 3204 CG PRO A 614-2.427 50. 390 34. 353 1. 00 24.80 3205 C PRO A 614-5.402 50. 058 36. 197 1. 00 23.08 3206 0 PRO A 614-5.720 49. 748 37. 347 1. 00 22. 83 3207 N VAL A 615-5.829 51. 106 35. 514 1. 00 23.16 3208 CA VAL A 615-6.935 51. 943 36. 155 1. 00 22.95 3209 CB VAL A 615-7.165 53. 223 35. 357 1. 00 22.61 3210 CG1 VAL A 615-8.329 54. 011 36. 011 1. 00 21.81 3211 CG2 VAL A 615-5.940 54. 112 35. 341 1. 00 21.71 3212 C VAL A 615-8.165 51. 040 36. 240 1. 00 22.91 32130 VAL A 615-8.814 51. 036 37. 280 1. 00 22.98 3214 N THR A 616-8.353 50. 293 35. 135 1. 00 23.29 3215 CA THR A 616-9.516 49. 361 35. 130 1. 00 23.34 3216 CB THR A 616-9.739 48. 575 33. 815 1. 00 22.15 3217 OG1 THR A 616-9.837 49. 437 32. 694 1. 00 21.24 3218 CG2 THR A 616-10.998.47.663 33. 893 1. 00 20.65 3219 C THR A 616-9.322 48. 404 36. 309 1. 00 24.06 3220 0 THR A 616-10.197 48. 291 37. 173 1. 00 24.08 3221 N LYS A 617-8. 111 47. 812 36. 363 1. 00 25. 06 3222 CA LYS A 617-7.816 46. 872 37. 486 1. 00 25.50 3223 CB LYS A 617-6.402 46. 302 37. 270 1. 00 28.52 3224 CG LYS A 617-6.474 45. 365 36. 065 1. 00 30.94 3225 CD LYS A 617-5.250 44. 785 35. 550 1. 00 34.03 3226 CE LYS A 617-4.348 43. 884 36. 307 1. 00 35.16 3227 NZ LYS A 617-3.201 43. 440 35. 397 1. 00 36.97 3228 C LYS A 617-8.023 47. 439 38. 846 1. 00 25.17 32290 LYS A 617-8.561 46. 759 39. 792 1. 00 25.47 3230 N TYR A 618-7.582 48. 682 39. 044 1. 00 23.42 3231 CA TYR A 618-7.725 49. 348 40. 350 1. 00 22.46 3232 CB TYR A 618-6.907 50. 685 40. 312 1. 00 21.00 3233 CG TYR A 618-7.182 51. 508 41. 559 1. 00 21.81 3234 CD1 TYR A 618-6. 424 51.404 42.709 1.00 21. 74 3235 CE1 TYR A 618-6.735 52. 109 43. 859 1. 00 21.68 3236 CZ TYR A 618-7.814 52. 989 43. 857 1. 00 22.09 3237 OH TYR A 618-8.130 53. 720 44. 972 1. 00 22.57 3238 CE2 TYR A 618-8.594 53. 113 42. 713 1. 00 21.29 3239 CD2 TYR A 618-8.280 52. 390 41. 576 1. 00 21.07 3240 C TYR A 618-9.160 49. 514 40. 766 1. 00 21.92 3241 0 TYR A 618-9.546 49. 306 41. 952 1. 00 22.35 3242 N ILE A 619-10. 007 49. 921 39. 813 1. 00 21. 56 3243 CA ILE A 619-11.447 50. 115 40. 238 1. 00 20.95 3244 CB ILE A 619-12.174 50. 929 39. 153 1. 00 19.45 3245 CG2 ILE A 619-13.656 51. 116 39. 528 1. 00 17.58 3246 CG1 ILE A 619-11.465 52. 270 38. 860 1. 00 19.29 3247 CD1 ILE A 619-12.163 53. 081 37. 748 1. 00 19. 08 3248 C ILE A 619-12.026 48. 768 40. 611 1. 00 21.71 3249 0 ILE A 619-12.816 48. 622 41. 555 1. 00 22.09 3250 N MET A 620-11.606 47. 717 39. 935 1. 00 23.20 3251 CA MET A 620-12.071 46. 314 40. 200 1. 00 23.89 3252MET A 620-11.533 45. 358 39. 152 1. 00 23.30 3253 CG MET A 620-12. 120 45. 675 37. 790 1. 00 22. 83 3254 SD MET A 620-11. 318 44.597 36.530 1.00 23. 24 3255 CE MET A 620-11.729 42. 994 37. 228 1. 00 23.14 3256 C MET A 620-11.729 45. 980 41. 629 1. 00 25.11 3257 O MET A 620-12.514 45. 453 42. 420 1. 00 25.18 3258 N THR A 621-10.555 46. 429 42. 044 1. 00 26.58 3259 CA THR A 621-10. 023 46.245 43.399 1.00 28.18 3260 CB THR A 621-8.522 46. 664 43. 518 1. 00 30.16 3261 OG1 THR A 621-7.723 45. 734 42. 713 1. 00 30.57 3262 CG2 THR A 621-7.964 46. 888 44. 916 1. 00 30.86 3263 C THR A 621-10.872 46. 954 44. 441 1. 00 28.88 3264 0 THR A 621-11.152 46. 347 45. 497 1. 00 29.58 3265 N CYS A 622-11.257 48. 190 44. 210 1. 00 29.01 3266 CA CYS A 622-12.047 48. 957 45. 156 1. 00 29.92 3267 CB CYS A 622-12.246 50. 404 44. 719 1. 00 28.46 3268 SG CYS A 622-10. 831 51.393 44.374 1.00 28. 87 3269 C CYS A 622-13.400 48. 332 45. 436 1. 00 31.19 3270 O CYS A 622-13.981 48. 628 46. 530 1. 00 31.67 3271 N MET A 623-13.933 47. 563 44. 490 1. 00 32.05 3272 CA MET A 623-15.259 46. 971 44. 644 1. 00 34.07 3273 CB MET A 623-15.887 46. 614 43. 283 1. 00 34.62 3274 CG MET A 623-15.861 47. 846 42. 426 1. 00 34.88 3275 SD MET A 623-16.897 47. 658 40. 941 1. 00 35.42 3276 CE MET A 623-16.514 49. 280 40. 212 1. 00 35.85 3277 C MET A 623-15. 302 45.823 45.642 1.00 35. 61 3278 0 MET A 623-16. 339 45.561 46.298 1.00 36. 19 3279 N SER A 624-14. 185 45.191 45.785 1.00 36. 78 3280 CA SER A 624-13.840 44. 077 46. 637 1. 00 38.66 3281 CB SER A 624-12.424 43. 552 46. 279 1. 00 39.12 3282 OG SER A 624-12.337 43. 176 44. 924 1. 00 39.26 3283 C SER A 624-13.819 44. 470 48. 118 1. 00 39.78 32840SERA 624-14.150 43. 622 48. 980 1. 00 40.33 3285 N ALA A 625-13.397 45. 693 48. 412 1. 00 40.41 3286 CA ALA A 625-13.324 46. 185 49. 790 1. 00 40.60 3287 CB ALA A 625-12.037 46. 915 50. 058 1. 00 40.37 3288 C ALA A 625-14.564 47. 020 50. 151 1. 00 41.32 3289 0 ALA A 625-15. 415 46. 398 50. 907 1. 00 41. 86 6579 O HOH A 701-27.247 74. 874 43. 828 0. 80 15.27 6580 O HOH A 702-13.680 74. 948 47. 565 0. 80 23.09 6581 O HOH A 703-18.108 51. 903 51. 421 0. 80 26.50 6582 O HOH A 704-4.882 54. 692 40. 126 0. 60 22.25 6583 O HOH A 705-8. 441 68. 270 39. 147 0. 40 18. 96 6584 0 HOH A 706-20.744 68. 699 37. 291 0. 80 14.80 6585 O HOH A 707-4.462 51. 815 21. 073 0. 60 27.47 6586 O HOH A 708-19.892 55. 002 26. 488 0. 80 18.94 6587 0 HOH A 709-9.993 49. 962 16. 032 0. 80 31.79 6588 O HOH A 710 -10.084 56.750 16.003 0.80 33. 58 6589 O HOH A 711-15.909 65. 460 25. 593 1. 00 23.39 6590 O HOH A 712-16.870 67. 511 26. 228 0. 60 21.05 6591 O HOH A 713-8. 911 42. 667 27. 673 0. 60 20. 03 6592 O HOH A 714-3.619 55. 530 29. 358 0. 80 20.25 6593 0 HOH A 715-18.407 48. 401 33. 886 0. 80 19.43 6594 0 HOH A 716-22.082 61. 768 32. 391 0.40 18.58 6595 0 HOH A 717-22.590 50. 180 28. 165 0.80 18.03 6596 0 HOH A 718-23.703 47. 313 32. 016 0.80 23.31 6597 0 HOH A 719-27. 825 56.051 30.018 0. 60 19.10 6598 O HOH A 720-26.633 47. 923 42. 631 0.80 33.65 6599 O HOH A 721-26.301 51. 212 45. 365 0.60 19.88 6600 O HOH A 722-27.517 52. 961 46. 333 0.80 22.78 6601 O HOH A 723-32.831 55. 172 42. 880 0.60 12.66 6602 O HOH A 724-16.387 55. 263 30. 090 1.00 14.82 6603 O HOH A 725-19.153 54. 259 28. 769 1.00 21.71 6604 O HOH A 726-8.441 59. 733 49. 842 1.00 22.89 6605 O HOH A 727-38.108 64. 057 35. 232 0.80 31.77 6606 0 HOH A 728-39.097 65. 794 33. 989 0.60 17.08 6607 O HOH A 729-34.629 69. 503 31. 285 1.00 14.05 6608 O HOH A 730-60.650 64. 752 32. 708 0.60 16.76 6609 O HOH A 801 -30.589 93.245 47.228 1. 00 20.06 6610 O HOH A 802-30.156 67. 051 51. 424 1.00 15.59 6611 O HOH A 803-35.184 69. 063 58. 454 0.80 24.31 6612 0 HOH A 804-50.531 57. 599 25. 831 0.80 20.68 6613 0 HOH A 805-54.181 78. 137 27. 009 1.00 25.01 6614 O HOH A 806-35.167 68. 826 21. 995 1.00 21.35 6615 O HOH A 807-34.364 79. 639 24. 799 1.00 16.55 6616 0 HOH A 808-31.220 89. 856 70. 106 1.00 33.07 6617 O HOH A 809-38.291 58. 586 27. 175 1.00 21.00 6618 O HOH A 810-34.001 85. 451"30. 319 1.00 18.88 6619 O HOH A 811-24.063 94. 461 43. 475 1.00 25.92 6620 0 HOH A 812-22.779 96. 254 44. 568 1.00 28.08 6621 O HOH A 813-13.714 81. 445 64. 356 1.00 36.09 6622 O HOH A 814-62.511 57. 123 30. 038 1.00 33.99 6623 O HOH A 815-55.758 59. 278 36. 354 1.00 21.36 6624 O HOH A 816-36.956 82. 869 62. 423 0.80 23.66 6625 O HOH A 817-27.342 70. 275 67. 345 0.80 27.81 6626 0 HOH A 818-34.716 67. 023 56. 723 0.80 23.67 6627 O HOH A 819-39.701 73. 567 47. 726 0.60 21.96 6628 0 HOH A 820-22.925 42. 493 34. 932 0.80 25.75 6629 0 HOH A 821-32.661 87. 112 70. 496 0.80 30.32 6630 O HOH A 822-20. 605 86. 011 63. 694 0. 80 27.35 6631 O HOH A 823-19.888 81. 593 60. 792 0.80 18.99 6632 O HOH A 824-30.958 81. 162 48. 755 0.60 17.67 6633 O HOH A 825-27.879 72. 485 44. 833 1.00 14.25 6634 O HOH A 826-33. 216 92.127 46.250 0.80 26.37 6635 O HOH A 827-12.966 42. 592 25. 466 0.80 27.54 6636 O HOH A 828-39.793 92. 254 57. 430 0.80 22.87 6637 O HOH A 829-25.262 78. 936 41. 514 0.80 22.31 6638 O HOH A 830-22.000 82. 158 49. 501 0.80 24.56 6639 O HOH A 831-15.985 74. 330 49. 285 0.80 22.74 6640 O HOH A 832-13.774 77. 581 54. 164 0.80 22.87 6641 O HOH A 833-9.293 68. 942 50. 227 0.80 28.90 6642 0 HOH A 834-19.182 81. 892 55. 209 0.80 24.75 6643 0 HOH A 835-16. 291 87. 599 56. 447 0. 80 23.44 6644 O HOH A 836-19.58981. 26658. 3920.80 25.44 6645 O HOH A 837-21.289 83. 602 51. 490 0.80 28.03 6646 O HOH A 838-22. 207 88.639 51.896 0.80 15.96 6647 O HOH A 839-35.910 63. 449 50. 211 0.80 26.13 6648 O HOH A 840-34.822 66. 633 45. 638 0.80 29.21 6649 O HOH A 841-31.411 59. 547 43. 971 1.00 19.77 6650 O HOH A 842-26.849 66. 452 40. 688 0.80 15.49 6651 0 HOH A 843-25.627 68. 703 41. 437 0.80 14.10 6652 0 HOH A 844-27.238 60. 405 40. 509 1.00 21.82 6653 0 HOH A 845-20.442 72. 280 62. 710 0.60 23.24 6654 0 HOH A 846-16.852 72. 686 62. 657 0.60 21.82 6655 0 HOH A 847-19.661 78. 350 66. 777 0.60 24.66 6656 0 HOH A 848-34.920 70. 387 65. 816 0.80 27.15 6657 0 HOH A 849-48.409 73. 520 47. 251 0.80 18.45 6658 0 HOH A 850-48.084 70. 982 46. 399 0.80 19.64 6659 0 HOH A 851-49.30276. 06945. 9600.80 18.17 6660 0 HOH A 852-52.266 79. 174 48. 855 0.60 22.73 6661 O HOH A A 853-58. 799 63. 420 43. 330 0. 60 23.64 6662 0 HOH A 854-58.981 63. 447 30. 410 0.80 20.83 6663 0 HOH A 855-59.305 57. 472 35. 735 0.80 21.94 6664 0 HOH A 856-55.27365. 42918. 2830.60 28.49 6665 0 HOH A 857-49.272 59. 609 24. 940 0.80 23.51 6666 0 HOH A 858-64.907 69. 365 31. 036 1.00 31.91 6667 0 HOH A 859-50.214 82. 031 35. 864 0.80 21.12 6668 0 HOH A 860-57.326 77. 350 37. 700 0.80 19.88 6669 0 HOH A 861-51.661 82. 607 37. 872 0.80 24.54 6670 O HOH A A 862-53.676 79. 057 40. 709 1.00 19.28 6671 0 HOH A 863-57.754 79. 956 38. 171 0.80 20.95 6672 0 HOH A 864-58.529 73. 514 33. 718 0.80 19.76 6673 0 HOH A 865-31.702 69. 575 27. 590 0.80 20.28 6674 0 HOH A 866-62.924 68. 557 41. 031 0.80 25.28 6675 0 HOH A 867-60.255 71. 245 46. 000 0.80 18.96 6676 O HOH A 868 -60.606 69.353 45.360 0. 80 14.42 6677 0 HOH A 869-46.371 66. 621 17. 751 0.80 17.54 6678 O HOH A 870-47.425 67. 423 15. 428 0.60 15.48 6679 O HOH A 871-53.931 75. 990 13. 833 0.80 28.69 6680 O HOH A 872-48.094 79. 792 18. 410 0.80 19.66 6681 0 HOH A 873-44.067 75. 508 20. 595 1.00 15.38 66820HOH A 874-44.151 73. 437 18. 588 1.00 17.65 6683 O HOH A 875-48.089 73. 895 13. 943 0.80 21.05 6684 O HOH A 876-34.032 68. 031 29. 153 0.80 20.65 6685 0 HOH A 877-33.174 68. 885 33. 334 1.00 20.58 6686 0 HOH A 878-31.160 67. 541 32. 883 0.80 15.92 6687 O HOH A 879-32.627 71. 527 37. 091 0.80 23.00 6688 O HOH A 880-31.868 71. 153 34. 793 0.80 25.28 6689 O HOH A 881-29.909 79. 465 26. 820 0.80 19.38 6690 O HOH A 882-36. 020 84.189 37.581 0. 80 28.32 6691 0 HOH A 883-54.222 85. 891 25. 966 0.80 20.24 6692 0 HOH A 884-32. 683 74. 189 33. 533 1. 00 30.90 6693 O HOH A 885-38.648 83. 356 36. 705 0.80 24.32 6694 O HOH A 886-43.499 55. 779 35. 125 0.80 26.86 6695 O HOH A 887-51.072 83. 073 42. 602 1.00 24.22 6696 0 HOH A 888-51.425 53. 647 38. 234 0.80 30.09 6697 0 HOH A 889-19.059 67. 245 38. 560 0.80 18.42 6698 O HOH A 890-11.657 71. 252 41. 155 0.80 23.17 6699 O HOH A 891-11.325 73. 267 39. 832 0.80 29.54 6700 0 HOH A 892-9.708 73. 288 48. 410 0.60 21.16 6701 0 HOH A 893-7.572 62. 155 49. 190 1.00 22.50 6702 0 HOH A 894-15.028 59. 357 57. 323 0.80 28.79 6703 O HOH A 895-9.812 59. 707 54. 387 0.80 27.97 6704 O HOH A 896-8.106 62. 403 42. 567 0.80 19.18 6705 O HOH A 897-3.060 68. 824 32. 137 0.80 31.92 6706 O HOH A 898-24.695 62. 560 25. 911 0.80 30.37 6707 O HOH A 899-4.821 67. 621 19. 874 0.80 23.38 6708 O HOH A 900-17. 676 46. 033 23. 169 0. 80 27. 61 6709 O HOH A 901-18. 863 45. 514 25. 346 0. 80 28. 22 6710 O HOH A 902-8. 089 44. 049 39. 818 0. 80 21. 93 6711 O HOH A 903 -51.243 81.808 19.588 0.80 24. 68 6712 O HOH A 904-41. 864 77. 592 39. 457 0. 60 16. 35 6713 O HOH A 905 -39.722 77.803 40.962 0.60 20. 14 6714 0 HOH A 906-42. 157 61. 887 22. 263 0. 80 18. 89 6715 0 HOH A 907-23. 873 90. 166 36. 153 0. 60 17. 30 6716 0 HOH A 908-59. 740 76. 627 39. 657 0. 60 12. 98 6717 0 HOH A 909-51. 326 85. 494 41. 351 0. 60 16. 38 6718 0 HOH A 910-2. 571 63. 785 26. 960 0. 40 16. 49 6719 0 HOH A 911-6. 865 74. 209 24. 615 0. 60 19. 72 6720 O HOH A 912-16. 762 72. 497 21. 995 0. 60 21. 54 6721 O HOH A 913-8. 588 71. 186 24. 488 0. 40 23. 51 6722 O HOH A 914-41. 750 67. 103 17. 680 0. 60 19. 91 6723 0 HOH A 915-46. 059 82. 294 21. 465 0. 60 19. 56 6724 O HOH A 916-19. 466 47. 926 46. 718 0. 60 15. 60 6725 O HOH A 917 -20.848 46.368 48.419 0.60 18. 19 6726 O HOH A 918 -25.456 54.077 31.046 0.60 17. 80 6727 O HOH A 919 -23.279 59.964 33.210 0.60 17. 32 6728 O HOH A 920 -12.144 67.806 19.735 0.60 24. 55 6729 O HOH A 921 -24.003 62.093 20.205 0.60 18. 18 6730 O HOH A 922 -28.853 66.976 39.699 0.60 15. 22 6731 O HOH A 923-14. 688 75. 008 32. 192 0. 60 22. 34 6732 O HOH A 924-22. 642 46. 698 50. 272 0. 60 21. 53 6733 O HOH A 925 -28.425 61.468 56.065 0.60 22. 28 6734 0 HOH A 926-6. 740 66. 093 51. 422 0. 60 26. 62 6735 0 HOH A 927-11. 020 73. 159 34. 407 0. 40 15. 24 6736 O HOH A 928 -6.178 62.363 46.140 0.40 22. 19 6737 O HOH A 929 -21.715 71.654 41.803 0.60 14. 77 6738 O HOH A 930 -33.608 58.132 43.758 0.60 16. 52 6739 0 HOH A 931-39. 506 65. 631 40. 403 0. 60 15. 02 6740 O HOH A 932 -38.339 66.653 42.421 0.60 17. 17 6741 O HOH A 933 -36.344 62.733 46.996 0.60 17. 73 6742 O HOH A 934 -35.860 68.891 45.286 0.60 23. 97 6743 O HOH A 935 -34.963 70.899 45.658 0.60 20. 28 6744 O HOH A 936 -31.492 51.316 30.723 0.40 19. 35 6745 O HOH A 937 -26.685 52.615 30.004 0.40 17. 11 6746 O HOH A 938-50. 604 55. 272 33. 182 0. 40 18. 75 6747 0 HOH A 939-48. 187 56. 093 35. 486 0. 40 14. 27 6748 O HOH A 940 -53.792 79.480 23.608 0.40 21. 23 <BR> <BR> <BR> 6749 0 HOH A 941-47. 050 72. 077 15. 274 0. 60 16. 18 6750 O HOH A 942 -57.189 57.556 25.480 0.40 19. 14 6751 O HOH A 943 -62.381 63.454 33.821 0.40 17. 70 6752 0 HOH A 944-55. 387 69. 299 47. 372 0. 60 21. 98 6753 0 HOH A 945-52. 848 63. 775 48. 454 0. 60 19. 51 6754 0 HOH A 946-39. 291 77. 214 55. 513 0. 60 22. 66 6755 O HOH A 947 -30.055 63.775 42.523 0.40 13. 00 6756 0 HOH A 948-34. 759 80. 329 51. 807 0. 60 17. 65 <BR> <BR> 6757 O HOH A 949-30. 396 94. 640 55. 390 0. 60 20. 88 6758 O HOH A 950 -28.460 97.234 53.199 0.40 15. 49 6759 0 HOH A 951-21. 291 81. 107 35. 059 0. 40 18. 84 6760 0 HOH A 952-33. 664 91. 746 43. 699 0. 60 19. 27 6761 0 HOH A 953-14. 889 41. 553 36. 690 0. 40 21. 12 6762 O HOH A 954 -36.321 86.880 40.737 0.60 20. 89 6763 O HOH A 955 -34.434 75.608 44.551 0.60 17. 99 6764 O HOH A 956 -41.361 79.325 57.669 0.60 22. 42 6765 O HOH A 957-42.508 85.286 25.048 0.60 15.00 TABLE 2 : UHCV-B Atomic coordinates ATOM RESIDUE X Y Z Q B 3290 CB PRO B 190 34. 413 80. 208 19. 549 1. 00 37. 89 3291 C PRO B 190 36. 361 79. 796 21. 129 1. 00 37. 83 3292 O PRO B 190 37. 544 79. 855 20. 710 1. 00 38. 40 3293 N PRO B 190 34. 348 78. 398 21. 067 1. 00 37. 73 3294 CA PRO B 190 35. 271 79. 191 20. 285 1. 00 37. 73 3295 N PRO B 191 35. 997 80. 236 22. 322 1. 00 37. 49 <BR> <BR> 3296 CD PRO B 191 34. 642 80. 173 22. 904 1. 00 37. 22 3297 CA PRO B 191 36.981 80.842 23.250 1.00 37. 11 3298 CB PRO B 191 36.128 81.163 24.482 1.00 37. 13 3299 CG PRO B 191 34. 711 81. 242 23. 979 1. 00 36. 96 3300 C PRO B 191 38.126 79.875 23.525 1.00 36. 72 3301 O PRO B 191 37. 895 78. 671 23. 810 1. 00 36. 42 3302 N VAL B 192 39. 354 80. 380 23. 455 1. 00 36. 37 3303 CA VAL B 192 40. 528 79. 471 23. 740 1. 00 36. 35 3304 CB VAL B 192 41. 739 80. 120 23. 008 1. 00 35. 91 3305 CG1 VAL B 192 43. 044 79. 419 23. 334 1. 00 35. 76 3306 CG2 VAL B 192 41. 491 80. 144 21. 514 1. 00 35. 47 3307 C VAL B 192 40. 717 79. 324 25. 235 1. 00 36. 10 33080 VAL B 192 40. 262 80. 273 25. 942 1. 00 36. 78 3309 N VAL B 193 41.444 78.325 25.720 1.00 35. 20 3310 CA VAL B 193 41. 614 78. 154 27. 200 1. 00 34. 29 3311 CB VAL B 193 41. 444 76. 645 27. 498 1. 00 32. 97 3312 CG1 VAL B 193 41. 303 76. 297 28. 969 1. 00 32. 17 3313 CG2 VAL B 193 40. 388 76. 035 26. 612 1. 00 32. 57 3314 C VAL B 193 42. 965 78. 663 27. 660 1. 00 34. 39 3315 O VAL B 193 43.998 78.074 27.264 1.00 35. 20 3316 N PRO B 194 42. 982 79. 662 28. 503 1. 00 33. 82 3317 CD PRO B 194 41. 760 80. 371 28. 980 1. 00 33. 81 3318 CA PRO B 194 44. 208 80. 253 29. 035 1. 00 33. 66 3319 CB PRO B 194 43. 676 81. 559 29. 700 1. 00 33. 53 3320 CG PRO B 194 42. 322 81. 126 30. 194 1. 00 33. 76 3321 C PRO B 194 44. 842 79. 417 30. 119 1. 00 33. 60 3322 O PRO B 194 44.257 78.423 30.562 1.00 34. 07 3323 N GLN B 195 46.016 79.855 30.575 1.00 33. 48 3324 CA GLN B 195 46. 758 79. 186 31. 653 1. 00 32. 46 3325 CB GLN B 195 48. 277 79. 426 31. 716 1. 00 32. 62 3326 CG GLN B 195 49.139 78.755 30.655 1.00 32. 12 3327 CD GLN B 195 48. 934 77. 236 30. 750 1. 00 32. 67 3328 OE1 GLN B 195 49.022 76.674 31.842 1.00 32. 69 3329 NE2 GLN B 195 48.607 76.653 29.592 1.00 32. 19 3330 C GLN B 195 46. 211 79. 740 32. 982 1. 00 31. 81 3331 O GLN B 195 46. 504 79. 121 34. 013 1. 00 32. 81 3332 N SER B 196 45. 568 80. 867 32. 899 1. 00 30. 71 3333 CA SER B 196 45. 011 81. 586 34. 061 1. 00 29. 30 3334 CB SER B 196 45.190 83.099 33.753 1.00 29. 34 3335 OG SER B 196 44. 662 83. 876 34. 816 1. 00 29. 28 3336 C SER B 196 43. 611 81. 207 34. 486 1. 00 27. 95 3337 O SER B 196 43. 372 80. 172 35. 222 1. 00 28. 68 3338 N PHE B 197 42. 625 81. 999 34. 200 1. 00 25. 32 3339 CA PHE B 197 41. 209 81. 823 34. 493 1. 00 22. 37 3340 CB PHE B 197 40.78 81.873 35.967 1.00 17. 11 3341 CG PHE B 197 39. 196 81. 926 36. 006 1. 00 12. 53 3342 CD1 PHE B 197 38. 456 80. 717 35. 926 1. 00 11. 54 3343 CD2 PHE B 197 38. 510 83. 107 35. 959 1. 00 10. 94 3344 CE1 PHE B 197 37. 095 80. 779 35. 798 1. 00 9. 90 3345 CE2 PHE B 197 37. 110 83. 197 35. 955 1. 00 9.24 3346 CZ PHE B 197 36. 370 81. 944 35. 880 1. 00 8.97 3347 C PHE B 197 40. 506 82. 968 33. 732 1. 00 21.44 3348 0 PHE B 197 40. 923 84. 082 34. 056 1. 00 21.47 3349 N GLN B 198 39. 560 82. 632 32. 875 1. 00 21.69 3350 CA GLN B 198 38. 846 83. 800 32. 294 1. 00 21.46 3351 CB GLN B 198 39.699 84.558 31.409 1. 00 24.70 3352 CG GLN B 198 40. 415 83. 942 30. 229 1. 00 27.88 3353 CD GLN B 198 41. 414 85. 076 29. 808 1. 00 30.19 3354 OE1 GLN B 198 42. 193 85. 407 30. 719 1. 00 31.56 3355 NE2 GLN B 198 41. 188 85. 543 28. 630 1. 00 30.49 3356 C GLN B 198 37. 424 83. 583 31. 919 1. 00 20.87 3357 O GLN B 198 36. 974 82. 457 31. 808 1. 00 20.94 3358 N VAL B 199 36. 727 84. 716 31. 790 1. 00 20.06 3359 CA VAL B 199 35. 297 84. 672 31. 342 1. 00 19.63 3360 CB VAL B 199 34. 425 85. 499 32. 284 1. 00 19.15 3361 CG1 VAL B 199 32. 946 85. 553 31. 848 1. 00 18.85 3362 CG2 VAL B 199 34. 465 85. 040 33. 733 1. 00 18.58 3363 C VAL B 199 35. 293 85. 194 29. 894 1. 00 19.20 3364 0 VAL B 199 35. 767 86. 334 29. 675 1. 00 19.03 3365 N ALA B 200 34. 804 84. 454 28. 978 1. 00 18.65 3366 CA ALA B 200 34. 686 84. 781 27. 558 1. 00 18.76 3367 CB ALA B 200 35. 514 83. 828 26. 700 1. 00 19.24 3368 C ALA B 200 33. 209 84. 557 27. 180 1. 00 18.43 3369 O ALA B 200 32.543 83.781 27.813 1. 00 18.55 3370 N HIS B 201 32. 778 85. 218 26. 191 1. 00 18.88 3371 CA HIS B 201 31. 555 85. 389 25. 492 1. 00 19.00 3372 CB HIS B 201 31. 316 86. 940 25. 190 1. 00 18.23 3373 CG HIS B 201 31. 136 87. 629 26. 500 1. 00 17.00 3374 CD2 HIS B 201 32. 009 88. 262 27. 309 1. 00 17.28 3375 ND1 HIS B 201 29. 897 87. 721 27. 137 1. 00 16.25 3376 CE1 HIS B 201 30.032 88.355 28.269 1. 00 14.32 3377 NE2 HIS B 201 31. 269 88. 678 28. 412 1. 00 15.73 3378 C HIS B 201 31. 610 84. 715 24. 145 1. 00 20.31 3379 O HIS B 201 32. 615 84. 769 23. 404 1. 00 21.04 3380 N LEU B 202 30. 564 83. 959 23. 886 1. 00 21.25 3381 CA LEU B 202 30.398 83.215 22.664 1. 00 21.87 3382 CB LEU B 202 30. 272 81. 705 22. 905 1. 00 19.70 3383 CG LEU B 202 30. 078 80. 952 21. 550 1. 00 19.51 3384 CD1 LEU B 202 31. 250 81. 207 20. 644 1. 00 19.61 3385 CD2 LEU B 202 29. 966 79. 454 21. 850 1. 00 19.05 3386 C LEU B 202 29. 152 83. 797 22. 024 1. 00 23.56 3387 O LEU B 202 28. 094 83. 337 22. 425 1. 00 24.63 3388 N HIS B 203 29. 331 84. 746 21. 154 1. 00 25.68 3389 CA HIS B 203 28.105 85.314 20.464 1. 00 27.46 3390 CB HIS B 203 28. 180 86. 829 20. 284 1. 00 26.58 3391 CG HIS B 203 28. 350 87. 513 21. 616 1. 00 25.39 3392 CD2 HIS B 203 28. 919 88. 675 21. 951 1. 00 24.85 3393 ND1 HIS B 203 27. 721 87. 022 22. 766 1. 00 24.98 3394 CE1 HIS B 203 28. 019 87. 830 23. 748 1. 00 25.07 3395 NE2 HIS B 203 28. 715 88. 847 23. 302 1. 00 24.17 3396 C HIS B 203 28. 088 84. 602 19. 117 1. 00 29.56 3397 0 HIS B 203 28. 959 84. 851 18. 276 1. 00 29.61 3398 N ALA B 204 27.147 83.707 18.993 1. 00 32.11 3399 CA ALA B 204 27. 046 82. 931 17. 748 1. 00 35.46 3400 CB ALA B 204 28. 288 82. 106 17. 558 1. 00 36.45 3401 C ALA B 204 25. 726 82. 195 17. 819 1. 00 37.93 3402 0 ALA B 204 25. 308 81. 814 18. 930 1. 00 38.63 3403 N PRO B 205 25. 118 82. 052 16. 673 1. 00 39.69 3404 CD PRO B 205 25. 675 82. 515 15. 356 1. 00 40.25 3405 CA PRO B 205 23. 844 81. 434 16. 463 1. 00 41.20 3406 CB PRO B 205 23. 935 80. 864 15. 020 1. 00 40.99 3407 CG PRO B 205 25. 170 81. 450 14. 408 1. 00 40.70 3408 C PRO B 205 23. 458 80. 279 17. 370 1. 00 42.59 3409 O PRO B 205 24.205 79.753 18.207 1. 00 43.13 3410 N THR B 206 22. 157 79. 978 17. 179 1. 00 43.36 3411 CA THR B 206 21. 559 78. 808 17. 880 1. 00 44.13 3412 CB THR B 206 20. 155 78. 896 18. 503 1. 00 43.97 3413 OG1 THR B 206 20. 186 79. 859 19. 625 1. 00 42.81 3414 CG2 THR B 206 19. 571 77. 552 19. 032 1. 00 43.75 3415 C THR B 206 21. 695 77. 761 16. 720 1. 00 44.50 3416 O THR B 206 20. 788 77. 521 15. 929 1. 00 44.55 3417 N GLY B 207 22. 966 77. 382 16. 651 1. 00 44.55 3418 CA GLY B 207 23. 444 76. 434 15. 644 1. 00 44.49 3419 C GLY B 207 24. 933 76. 663 15. 376 1. 00 44.19 3420 O GLY B 207 25. 423 76. 120 14. 374 1. 00 44.26 3421 N SER B 208 25. 582 77. 501 16. 191 1. 00 43.88 3422 CA SER B 208 27. 053 77. 691 15. 985 1. 00 43.19 3423 CB SER B 208 27. 777 78. 271 17. 210 1. 00 43.34 3424 OG SER B 208 29. 218 78. 069 16. 990 1. 00 43.14 3425 C SER B 208 27. 541 76. 191 15. 932 1. 00 42.40 3426 O SER B 208 28. 045 75. 659 14. 981 1. 00 42.70 3427 N GLY B 209 27. 205 75. 637 17. 050 1. 00 41.34 3428 CA GLY B 209 27. 371 74. 306 17. 586 1. 00 39.35 3429 C GLY B 209 27. 801 74. 570 19. 060 1. 00 37.77 3430 O GLY B 209 28.460 73.745 19.685 1. 00 37.15 3431 N LYS B 210 27. 393 75. 742 19. 512 1. 00 36.47 3432 CA LYS B 210 27. 671 76. 324 20. 782 1. 00 34.90 3433 CB LYS B 210 27. 032 77. 682 21. 045 1. 00 34.27 3434 CG LYS B 210 25. 559 77. 626 21. 186 1. 00 34.66 3435 CD LYS B 210 24. 815 78. 924 21. 487 1. 00 33.47 3436 CE LYS B 210 23. 364 78. 481 21. 710 1. 00 32.88 3437 NZ LYS B 210 22. 541 79. 549 22. 175 1. 00 33.29 3438 C LYS B 210 27. 553 75. 407 21. 966 1. 00 33.88 3439 0 ZYS B 210 28. 346 75. 541 22. 921 1. 00 33.75 3440 N SER B 211 26. 609 74. 501 21. 937 1. 00 33.40 3441 CA SER B 211 26. 494 73. 551 23. 098 1. 00 32.56 3442 CB SER B 211 25. 122 73. 784 23. 712 1. 00 32.84 3443 OG SER B 211 24. 228 73. 680 22. 593 1. 00 33.42 3444 C SER B 211 26. 621 72. 146 22. 579 1. 00 32.19 3445 O SER B 211 26. 224 71. 232 23. 326 1. 00 32.06 3446 N THR B 212 27. 146 72. 001 21. 355 1. 00 31.96 3447 CA THR B 212 27. 298 70. 650 20. 742 1. 00 30.98 3448 CB THR B 212 26. 337 70. 465 19. 506 1. 00 30.11 3449 OG1 THR B 212 26. 844 71. 465 18. 544 1. 00 30.34 3450 CG2 THR B 212 24. 860 70. 675 19. 751 1. 00 28.86 3451 C THR B 212 28. 749 70. 503 20. 259 1. 00 30.58 3452 0 THR B 212 29. 532 69. 763 20. 856 1. 00 30.47 3453 N LYS B 213 29. 068 71. 250 19. 213 1. 00 30.44 3454 CA LYS B 213 30. 386 71. 253 18. 590 1. 00 29.86 3455 CB LYS B 213 30. 423 71. 947 17. 224 1. 00 31.59 3456 CG LYS B 213 29. 363 71. 460 16. 240 1. 00 33.18 3457 CD LYS B 213 29. 512 72. 128 14. 882 1. 00 34.62 3458 CE LYS B 213 28. 374 71. 735 13. 951 1. 00 35.83 3459 NZ LYS B 213 27. 087 72. 329 14. 476 1. 00 36.45 3460 C LYS B 213 31. 426 71. 934 19. 471 1. 00 28.73 3461 0 LYS B 213 32. 601 71. 567 19. 453 1. 00 28.15 3462 N VAL B 214 30. 953 72. 948 20. 199 1. 00 27.54 3463 CA VAL B 214 31. 876 73. 656 21. 108 1. 00 26.12 3464 CB VAL B 214 31. 595 75. 101 21. 349 1. 00 23.82 3465 CG1 VAL B 214 32. 606 75. 739 22. 324 1. 00 22.85 3466 CG2 VAL B 214 31. 685 75. 948 20. 056 1. 00 22.17 3467 C VAL B 214 32. 339 72. 701 22. 186 1. 00 25.88 3468 0 VAL B 214 33. 553 72. 445 22. 290 1. 00 25.30 3469 N PRO B 215 31. 402 72. 146 22. 938 1. 00 26.20 3470 CD PRO B 215 29. 977 72. 408 22. 913 1. 00 26.50 3471 CA PRO B 215 31. 749 71. 157 23. 977 1. 00 26.52 3472 CB PRO B 215 30. 441 70. 709 24. 552 1. 00 26.35 3473 CG PRO B 215 29. 398 71. 623 24. 071 1. 00 26.36 3474 C PRO B 215 32. 598 70. 033 23. 376 1. 00 26.95 3475 0 PRO B 215 33. 635 69. 696 23. 944 1. 00 27.32 3476 N ALA B 216 32. 186 69. 478 22. 250 1. 00 26.99 3477 CA ALA B 216 32. 901 68. 376 21. 577 1. 00 27.25 3478 CB ALA B 216 32. 059 67. 929 20. 377 1. 00 26.72 3479 C ALA B 216 34. 340 68. 652 21. 226 1. 00 27.15 3480 O ALA B 216 35. 270 67. 836 21. 439 1. 00 27.03 3481 N ALA B 217 34. 581 69. 806 20. 661 1. 00 27.30 3482 CA ALA B 217 35. 906 70. 259 20. 253 1. 00 27.65 3483 CB ALA B 217 35. 735 71. 509 19. 406 1. 00 28.56 3484 C ALA B 217 36. 834 70. 421 21. 424 1. 00 28.19 3485 O ALA B 217 38.077 70.269 21.265 1. 00 28.95 3486 N TYR B 218 36.304 70.746 22.592 1. 00 28.22 3487 CA TYR B 218 37. 061 70. 932 23. 831 1. 00 27.67 3488 CB TYR B 218 36. 457 71. 819 24. 898 1. 00 27.86 3489 CG TYR B 218 36. 297 73. 308 24. 776 1. 00 27.00 3490 CD1 TYR B 218 35. 092 73. 973 25. 002 1. 00 27.12 3491 CEl TYR B 18 34. 984 75. 364 24. 906 1. 00 27.42 3492 CD2 TYR B 218 37. 399 74. 093 24. 447 1. 00 26.98 3493 CE2 TYR B 218 37. 295 75. 474 24. 338 1. 00 26.68 3494 CZ TYR B 218 36. 109 76. 110 24. 566 1. 00 26.90 3495 OH TYR B 218 36. 091 77. 468 24. 408 1. 00 27.78 3496 C TYR B 218 37. 393 69. 559 24. 459 1. 00 27.15 3497 0 TYR B 218 38. 518 69. 320 24. 912 1. 00 26.74 3498 N ALA B 219 36.381 68.715 24.464 1. 00 27.12 3499 CA ALA B 219 36. 501 67. 359 25. 025 1. 00 27.74 3500 CB ALA B 219 35. 234 66. 576 24. 871 1. 00 27.19 3501 C ALA B 219 37. 716 66. 665 24. 383 1. 00 28.32 3502 0 ALA B 219 38. 479 65. 976 25. 045 1. 00 28.79 3503 N ALA B 220 37. 874 66. 958 23. 131 1. 00 2'8. 83 3504 CA ALA B 220 38. 919 66. 456 22. 251 1. 00 29.31 3505 CB ALA B 220 38. 567 66. 710 20. 795 1. 00 28.63 3506 C ALA B 220 40. 290 66. 937 22. 667 1. 00 29.44 3507 0 ALA B 220 41. 265 66. 151 22. 533 1. 00 29.47 3508 N GLN B 221 40.386 68.196 23.114 1. 00 28.87 3509 CA GLN B 221 41. 688 68. 703 23. 593 1. 00 27.90 3510 CB GLN B 221 41. 756 70. 213 23. 709 1. 00 30.04 3511 CG GLN B 221 41.498 70.965 22.401 1. 00 31.83 3512 CD GLN B 221 41. 822 72. 448 22. 597 1. 00 33.19 3513 OE1 GLN B 221 40.953 73.311 22.789 1. 00 34.79 3514 NE2 GLN B 221 43. 143 72. 716 22. 710 1. 00 32.37 3515 C GLN B 221 41. 936 68. 121 24. 990 1. 00 26.70 3516 0 GLN B 221 42. 910 68. 512 25. 671 1. 00 26.57 3517 N GLY B 222 41. 054 67. 248 25. 411 1. 00 25.68 3518 CA GLY B 222 41. 164 66. 594 26. 729 1. 00 24.24 3519 C GLY B 222 40. 662 67. 407 27. 888 1. 00 23.69 35200GLY B 222 41. 182 67. 265 29. 021 1. 00 23.56 3521 N TYR B 223 39. 648 68. 266 27. 640 1. 00 22.06 3522 CA TYR B 223 39. 114 69. 059 28. 756 1. 00 20.59 3523 CB TYR B 223 39. 084 70. 546 28. 511 1. 00 19.45 3524 CG TYR B 223 40. 333 71. 338 28. 211 1. 00 19.26 3525 CD1 TYR B 223 40. 643 71. 797 26. 918 1. 00 19.45 3526 CE1 TYR B 223 41. 756 72. 605 26. 680 1. 00 19.53 3527 CD2 TYR B 223 41. 213 71. 674 29. 211 1. 00 19.28 3528 CE2 TYR B 223 42. 358 72. 453 28. 974 1. 00 20.58 3529 CZ TYR B 223 42. 624 72. 873 27. 686 1. 00 20.53 3530 OH TYR B 223 43. 843 73. 548 27. 519 1. 00 22.14 3531 C TYR B 223 37. 793 68. 451 29. 204 1. 00 19.99 3532 0 TYR B 223 37. 086 67. 723 28. 464 1. 00 20.11 3533 N LYS B 224 37. 409 68. 771 30. 411 1. 00 19.44 3534 CA LYS B 224 36. 139 68. 370 31. 076 1. 00 18.14 3535 CB LYS B 224 36. 304 67. 900 32. 488 1. 00 17.10 3536 CG LYS B 224 37. 089 66. 573 32. 628 1. 00 16.63 3537 CD LYS B 224 37. 383 66. 221 34. 065 1. 00 16.04 3538 CE LYS B 224 38.300 67.243 34.702 1. 00 14.29 3539 NZ LYS B 224 38. 444 66. 963 36. 170 1. 00 14.42 3540 C LYS B 224 35. 250 69. 652 31. 011 1. 00 17.85 3541 0 LYS B 224 35. 679 70. 743 31. 441 1. 00 17.40 3542 N VAL B 225 34. 119 69. 460 30. 421 1. 00 17.58 3543 CA VAL B 225 33. 124 70. 486 30. 143 1. 00 17.35 3544 CB VAL B 225 33. 056 70. 645 28. 602 1. 00 17.95 3545 CG1 VAL B 225 32. 267 71. 912 28. 253 1. 00 19.47 3546 CG2 VAL B 225 34. 404 70. 659 27. 903 1. 00 19.12 3547 C VAL B 225 31. 757 70. 279 30. 742 1. 00 16.85 3548 0 VAL B 225 31. 158 69. 187 30. 661 1. 00 17.43 3549 N LEU B 226 31. 207 71. 355 31. 351 1. 00 15.91 3550 CA LEU B 226 29. 874 71. 426 31. 918 1. 00 14.78 3551 CB LEU B 226 29. 824 71. 865 33. 368 1. 00 11.98 3552LEU B 226 28. 520 72. 114 34. 102 1. 00 8. 69 3553 CD1 LEU B 226 27. 768 70. 777 34. 315 1. 00 8.50 3554 CD2 LEU B 226 28. 836 72. 744 35. 441 1. 00 5.94 3555 C LEU B 226 29. 094 72. 449 31. 063 1. 00 15.24 3556 0 LEU B 226 29. 568 73. 590 30. 897 1. 00 15.55 3557 N VAL B 227 27. 987 72. 024 30. 578 1. 00 15.07 3558 CA VAL B 227 27. 068 72. 859 29. 776 1. 00 15.37 3559 CB VAL B 227 26. 855 72. 288 28. 382 1. 00 15.21 3560 CG1 VAL B 227 25. 931 73. 158 27. 513 1. 00 14.95 3561 CG2 VAL B 227 28. 117 71. 900 27. 635 1. 00 13.52 3562 C VAL B 227 25. 769 72. 899 30. 597 1. 00 16.21 35630VAL B 227 25. 086 71. 873 30. 893 1. 00 17.23 3564 N LEU B 228 25. 441 74. 107 30. 965 1. 00 16.94 3565 CA LEU B 228 24. 266 74. 556 31. 670 1. 00 17.09 3566LEU B 228 24. 687 75. 537 32. 791 1. 00 15.83 3567LEU B 228 25. 606 75. 011 33. 878 1. 00 14.03 3568 CD1 LEU B 228 25. 800 76. 092 34. 973 1. 00 12.73 3569 CD2 LEU B 228 24. 943 73. 812 34. 527 1. 00 12.04 3570 C LEU B 228 23. 332 75. 225 30. 617 1. 00 17.20 3571 0 LEU B 228 23. 707 76. 149 29. 879 1. 00 17.26 3572 N ASN B 229 22. 087 74. 902 30. 736 1. 00 17.61 3573 CA ASN B 229 20. 978 75. 371 29. 857 1. 00 18. 28 3574 CB ASN B 229 20. 834 74. 176 28. 832 1. 00 19. 79 3575 CG ASN B 229 20. 059 74. 480 27. 600 1. 00 20. 64 3576 OD1 ASN B 229 18. 855 74. 336 27. 508 1. 00 22. 91 3577 ND2 ASN B 229 20. 754 74. 954 26. 548 1. 00 20. 70 3578 C ASN B 229 19.778 75.461 30.796 1.00 18. 80 3579 O ASN B 229 19. 675 74. 724 31. 798 1. 00 18. 47 3580 N PRO B 230 18. 857 76. 363 30. 481 1. 00 19. 83 3581 CD PRO B 230 18. 873 77. 271 29. 368 1. 00 19. 88 3582 CA PRO B 230 17. 674 76. 518 31. 331 1. 00 20. 79 3583 CB PRO B 230 17. 207 77. 927 31. 001 1. 00 20. 77 3584 CG PRO B 230 17. 610 78. 110 29. 574 1. 00 20. 91 3585 C PRO B 230 16. 609 75. 492 31. 060 1. 00 21. 62 35860PRO B 230 15. 610 75. 527 31. 811 1. 00 22. 71 3587 N SER B 231 16. 728 74. 682 30. 067 1. 00 22. 53 3588 CA SER B 231 15. 681 73. 700 29. 684 1. 00 23. 15 3589 CB SER B 231 15. 496 73. 860 28. 195 1. 00 23. 93 3590 OG SER B 231 14. 535 73. 052 27. 595 1. 00 25. 44 3591 C SER B 231 16. 036 72. 271 30. 041 1. 00 23. 71 3592 O SER B 231 17. 167 71. 869 29. 761 1. 00 24. 06 3593 N VAL B 232 15. 096 71. 592 30. 644 1. 00 23. 60 3594 CA VAL B 232 15.044 70.216 31.069 1.00 23. 88 3595 CB VAL B 232 14. 068 69. 752 32. 130 1. 00 22. 92 3596 CG1 VAL B 232 13. 889 68. 185 32. 126 1. 00 22. 53 3597 CG2 VAL B 232 14. 431 70. 095 33. 562 1. 00 21. 45 3598 C VAL B 232 14. 946 69. 320 29. 814 1. 00 24. 47 35990VAL B 232 15. 704 68. 345 29. 742 1. 00 24. 78 3600 N ALA B 233 14. 063 69. 731 28. 934 1. 00 24. 77 3601 CA ALA B 233 13. 875 69. 005 27. 643 1. 00 24. 43 3602 CB ALA B 233 12. 632 69. 572 26. 947 1. 00 23. 95 3603 C ALA B 233 15. 055 69. 293 26. 722 1. 00 23. 94 3604 0 ALA B 233 15. 333 68. 481 25. 874 1. 00 23. 86 3605 N ALA B 234 15. 626 70. 465 26. 779 1. 00 24. 70 3606 CA ALA B 234 16. 779 70. 852 25. 964 1. 00 24. 94 3607 CB ALA B 234 17. 040 72. 325 25. 910 1. 00 24. 82 3608 C ALA B 234 18. 005 70. 063 26. 424 1. 00 25. 28 3609 O ALA B 234 18. 817 69. 631 25. 583 1. 00 26. 15 3610 N THR B 235 18. 200 69. 945 27. 718 1. 00 25. 16 3611 CA THR B 235 19. 285 69. 193 28. 330 1. 00 25. 35 3612 CB THR B 235 19. 353 69. 517 29. 873 1. 00 24. 57 3613 OG1 THR B 235 19. 763 70. 905 29. 961 1. 00 22. 63 3614 CG2 THR B 235 20. 151 68. 522 30. 694 1. 00 24. 64 3615 C THR B 235 19. 093 67. 692 28. 102 1. 00 26. 45 3616 0 THR B 235 20. 032 67. 046 27. 646 1. 00 27. 14 3617 N LEU B 236 17. 923 67. 143 28. 436 1. 00 26. 91 3618 CA LEU B 236 17. 717 65. 706 28. 185 1. 00 27. 94 3619 CB LEU B 236 16. 341 65. 246 28. 618 1. 00 26. 37 3620LEU B 236 15. 923 65. 200 30. 049 1. 00 26. 11 3621 CD1 LEU B 236 14. 443 64. 732 30. 113 1. 00 25. 41 3622 CD2 LEU B 236 16. 839 64. 273 30. 831 1. 00 25. 03 3623 C LEU B 236 17. 999 65. 340 26. 734 1. 00 28. 52 36240LEU B 236 18. 325 64. 161 26. 490 1. 00 29. 58 3625 N GLY B 237 17. 812 66. 192 25. 790 1. 00 29. 44 3626 CA GLY B 237 17. 968 66. 057 24. 388 1. 00 30. 15 3627 C GLY B 237 19. 306 66. 210 23. 731 1. 00 30. 91 3628 O GLY B 237 19. 400 66. 277 22. 462 1. 00 30. 61 3629 N PHE B 238 20. 355 66. 324 24. 520 1. 00 31. 94 3630 CA PHE B 238 21. 728 66. 477 24. 020 1. 00 32.83 3631 CB PHE B 238 22. 578 67. 554 24. 587 1. 00 32.37 3632 CG PHE B 238 22. 268 68. 976 24. 364 1. 00 31.82 3633 CD1 PHE B 238 21. 714 69. 753 25. 401 1. 00 31.88 3634 CD2 PHE B 238 22. 508 69. 554 23. 119 1. 00 31.47 3635 CE1 PHE B 238 21. 442 71. 093 25. 193 1. 00 31.37 3636 CE2 PHE B 238 22. 242 70. 910 22. 913 1. 00 31.85 3637 CZ PHE B 238 21. 701 71. 675 23. 950 1. 00 31. 39 3638 C PHE B 238 22. 487 65. 154 24. 110 1. 00 33.83 3639 0 PHE B 238 23. 544 65. 021 23. 444 1. 00 34.67 3640 N GLY B 239 21. 995 64. 299 24. 962 1. 00 34.34 3641 CA GLY B 239 22. 696 62. 976 25. 092 1. 00 35.54 3642 C GLY B 239 22. 455 62. 290 23. 714 1. 00 36.06 3643 O GLY B 239 23. 348 61. 617 23. 194 1. 00 36.74 3644 N ALA B 240 21. 257 62. 499 23. 214 1. 00 36.22 3645 CA ALA B 240 20. 839 61. 897 21. 927 1. 00 36.66 3646 CB ALA B 240 19. 331 61. 830 21. 841 1. 00 36.82 3647 C ALA B 240 21. 496 62. 623 20. 772 1. 00 36.86 3648 O ALA B 240 22. 222 61. 997 19. 938 1. 00 37.29 3649 N TYR B 241 21. 270 63. 933 20. 706 1. 00 37.11 3650 CA TYR B 241 21. 904 64. 701 19. 630 1. 00 37.05 3651 CB TYR B 241 21. 796 66. 229 19. 641 1. 00 37.99 3652 CG TYR B 241 22. 559 66. 749 18. 414 1. 00 38.47 3653 CD1 TYR B 241 23. 922 66. 997 18. 463 1. 00 39.62 3654 CE1 TYR B 241 24. 627 67. 387 17. 321 1. 00 40.19 3655 CD2 TYR B 241 21. 913 66. 824 17. 190 1. 00 39.04 3656 CE2 TYR B 241 22. 591 67. 243 16. 046 1. 00 40.04 3657 CZ TYR B 241 23. 946 67. 526 16. 112 1. 00 40.30 3658 OH TYR B 241 24. 582 67. 885 14. 951 1. 00 41.24 3659 C TYR B 241 23. 386 64. 273 19. 647 1. 00 37.09 3660 O TYR B 241 23. 916 63. 956 18. 581 1. 00 37.46 3661 N MET B 242 23. 994 64. 242 20. 830 1. 00 36.73 3662 CA MET B 242 25. 361 63. 899 20. 957 1. 00 36.67 3663MET B 242 26. 206 64. 685 21. 954 1. 00 36.88 3664MET B 242 26. 291 66. 047 21. 259 1. 00 36.80 3665MET B 242 27. 496 67. 103 21. 853 1. 00 36.27 3666 CE MET B 242 29. 100 66. 424 21. 663 1. 00 36.21 3667 C MET B 242 25. 852 62. 542 20. 583 1. 00 36.62 3668 0 MET B 242 26. 828 62. 433 19. 834 1. 00 35.86 3669 N SER B 243 25. 208 61. 547 21. 146 1. 00 37.05 3670 CA SER B 243 25. 575 60. 134 20. 893 1. 00 37.91 3671 CB SER B 243 24. 623 59. 238 21. 619 1. 00 38.03 3672 OG SER B 243 24. 531 59. 585 23. 015 1. 00 38.40 3673 C SER B 243 25. 586 60. 011 19. 364 1. 00 38.34 3674 O SER B 243 26. 580 59. 572 18. 793 1. 00 38.75 3675 N LYS B 244 24. 505 60. 491 18. 755 1. 00 38.51 3676 CA LYS B 244 24. 303 60. 516 17. 353 1. 00 38.78 3677 CB LYS B 244 22. 923 60. 544 16. 764 1. 00 40.42 3678 CG LYS B 244 22. 038 59. 381 16. 771 1. 00 42.17 3679 CD LYS B 244 21. 319 58. 802 17. 913 1. 00 43.74 3680 CE LYS B 244 20. 194 59. 651 18. 507 1. 00 44.52 3681LYS B 244 19. 403 58. 857 19. 503 1. 00 44.65 3682 C LYS B 244 25. 152 61. 415 16. 491 1. 00 38.73 36830LYS B 244 25. 410 60. 968 15. 331 1. 00 39.20 3684 N ALA B 245 25. 566 62. 585 16. 926 1. 00 37.98 3685 CA ALA B 245 26. 350 63. 428 16. 025 1. 00 37.33 3686 CB ALA B 245 25. 527 64. 634 15. 628 1. 00 36.50 3687 C ALA B 245 27. 753 63. 780 16. 327 1. 00 37.08 3688 0 ALA B 245 28. 307 64. 532 15. 444 1. 00 37.62 3689 N HIS B 246 28. 332 63. 359 17. 421 1. 00 36.50 3690 CA HIS B 246 29. 722 63. 723 17. 769 1. 00 36.43 3691 CB HIS B 246 29. 891 64. 976 18. 660 1. 00 34.42 3692 CG HIS B 246 29. 371 66. 209 17. 981 1. 00 32.60 3693 CD2 HIS B 246 28. 103 66. 677 17. 891 1. 00 32.25 3694 ND1 HIS B 246 30. 171 67. 088 17. 295 1. 00 31.40 3695 CE1 HIS B 246 29. 413 68. 040 16. 778 1. 00 31.57 3696 NE2 HIS B 246 28. 160 67. 835 17. 120 1. 00 31.38 3697 C HIS B 246 30. 466 62. 532 18. 343 1. 00 36.42 3698 0 HIS B 246 31. 702 62. 585 18. 555 1. 00 36.89 3699 N GLY B 247 29. 719 61. 482 18. 586 1. 00 36.27 3700 CA GLY B 247 30. 263 60. 223 19. 112 1. 00 36.22 3701 C GLY B 247 29. 910 59. 936 20. 542 1. 00 35.81 37020 GLY B 247 29. 510 58. 802 20. 903 1. 00 36.22 3703 N ILE B 248 29. 906 60. 951 21. 340 1. 00 35.22 3704 CA ILE B 248 29. 674 61. 111 22. 744 1. 00 34.22 3705 CB ILE B 248 29. 984 62. 693 22. 965 1. 00 33.00 3706 CG2 ILE B 248 30. 034 63. 021 24. 458 1. 00 32.69 3707 CG1 ILE B 248 31. 294 62. 990 22. 216 1. 00 33.07 3708 CD1 ILE B 248 31. 775 64. 467 22. 204 1. 00 33.63 3709 C ILE B 248 28. 302 60. 882 23. 347 1. 00 33.84 3710 O ILE B 248 27. 266 61. 326 22. 837 1. 00 34.18 3711 N ASP B 249 28. 306 60. 233 24. 487 1. 00 33.58 3712 CA ASP B 249 27. 203 59. 929 25. 400 1. 00 33.15 3713 CB ASP B 249 27. 033 58. 463 25. 763 1. 00 37.01 3714 CG ASP B 249 26. 771 57. 573 24. 581 1. 00 40.62 3715 OD1 ASP B 249 25. 793 57. 825 23. 858 1. 00 42.82 3716 OD2 ASP B 249 27. 554 56. 601 24. 414 1. 00 42.23 3717 C ASP B 249 27. 664 60. 662 26. 743 1. 00 31.20 3718 O ASP B 249 28. 432 60. 096 27. 507 1. 00 31.17 3719 N PRO B 250 27. 134 61. 859 26. 891 1. 00 29.45 3720 CD PRO B 250 26. 207 62. 533 25. 976 1. 00 28.64 3721 CA PRO B 250 27. 520 62. 687 28. 036 1. 00 27.70 3722 CB PRO B 250 27. 245 64. 092 27. 508 1. 00 27.67 3723 CG PRO B 250 26. 333 63. 985 26. 360 1. 00 28.39 3724 C PRO B 250 26. 749 62. 341 29. 289 1. 00 26.00 3725 O PRO B 250 25. 817 61. 546 29. 207 1. 00 26.32 3726 N ASN B 251 27. 139 62. 934 30. 393 1. 00 23.99 3727 CA ASN B 251 26. 458 62. 783 31. 704 1. 00 22.57 3728 CB ASN B 251 27. 316 63. 130 32. 854 1. 00 20.54 3729 CG ASN B 251 28. 648 62. 361 32. 898 1. 00 19.63 3730 OD1 ASN B 251 28. 667 61. 225 33. 375 1. 00 21.09 3731 ND2 ASN B 251 29. 732 62. 979 32. 548 1. 00 19.00 3732 C ASN B 251 25. 241 63. 735 31. 498 1. 00 22.04 3733 O ASN B 251 25. 426 64. 654 30. 682 1. 00 21.74 3734 N ILE B 252 24. 132 63. 408 32. 025 1. 00 21.71 3735 CA ILE B 252 22. 921 64. 243 31. 842 1. 00 21.53 3736 CB ILE B 252 21. 840 63. 568 30. 965 1. 00 20.72 3737 CG1 ILE B 252 22. 241 63. 458 29. 506 1. 00 21.24 3738 CD1 ILE B 252 22. 508 64. 763 28. 692 1. 00 21.52 3739 CG2 ILE B 252 20. 457 64. 312 31. 121 1. 00 20.19 3740 C ILE B 252 22. 412 64. 527 33. 225 1. 00 21. 73 37410 ILE B 252 22. 174 63. 505 33. 910 1. 00 22.33 3742 N ARG B 253 22. 284 65. 791 33. 608 1. 00 21.28 3743 CA ARG B 253 21. 773 66. 045 34. 973 1. 00 21.15 3744 CB ARG B 253 22. 897 66. 469 35. 890 1. 00 21. 08 3745 CG ARG B 253 24. 125 65. 593 35. 939 1. 00 20. 97 3746 CD ARG B 253 25. 131 66. 168 36. 891 1. 00 20. 34 3747 NE ARG B 253 24. 780 66. 086 38. 256 1. 00 19. 37 3748 CZ ARG B 253 24. 757 65. 033 39. 049 1. 00 21. 20 3749 NH1 ARG B 253 25. 138 63. 789 38. 695 1. 00 22. 97 3750 NH2 ARG B 253 24. 281 65. 200 40. 298 1. 00 20. 50 3751 C ARG B 253 20. 645 67. 062 34. 953 1. 00 21. 74 3752 0 ARG B 253 20. 906 68. 273 34. 703 1. 00 21. 05 3753 N THR B 254 19. 482 66. 610 35. 335 1. 00 22. 94 3754 CA THR B 254 18. 266 67. 463 35. 403 1. 00 24. 30 3755 CB THR B 254 17. 355 67. 210 34. 151 1. 00 25. 14 3756 OG1 THR B 254 16. 745 65. 921 34. 403 1. 00 24. 82 3757 CG2 THR B 254 18. 104 67. 104 32. 806 1. 00 24. 41 3758 C THR B 254 17. 544 67. 019 36. 689 1. 00 25. 73 3759 O THR B 254 18. 005 66. 079 37. 364 1. 00 25. 85 3760 N GLY B 255 16. 458 67. 688 37. 051 1. 00 26. 65 3761 CA GLY B 255 15. 738 67. 381 38. 285 1. 00 27. 79 3762 C GLY B 255 15. 094 65. 981 38. 225 1. 00 29. 05 37630 GLY B 255 14. 969 65. 301 39. 226 1. 00 28. 41 3764 N VAL B 256 14. 724 65. 658 37. 008 1. 00 30. 73 3765 CA VAL B 256 14. 032 64. 422 36. 636 1. 00 32. 65 3766 CB VAL B 256 13. 270 64. 557 35. 312 1. 00 32. 82 3767 CG1 VAL B 256 12. 139 65. 610 35. 345 1. 00 32. 68 3768 CG2 VAL B 256 14. 081 64. 780 34. 062 1. 00 32. 51 3769 C VAL B 256 14. 889 63. 216 36. 861 1. 00 33. 64 3770 O VAL B 256 14. 607 62. 388 37. 756 1. 00 35. 07 3771 N ARG B 257 15. 950 63. 096 36. 076 1. 00 33. 65 3772 CA ARG B 257 16. 880 61. 977 36. 164 1. 00 32. 81 3773 CB ARG B 257 16. 518 60. 823 35. 241 1. 00 35. 27 3774 CG ARG B 257 16. 684 61. 063 33. 745 1. 00 37. 22 3775 CD ARG B 257 16. 178 59. 822 33. 014 1. 00 39. 52 3776 NE ARG B 257 14. 701 59. 752 33. 227 1. 00 41. 56 3777 CZ ARG B 257 13. 929 60. 707 32. 679 1. 00 42. 81 3778 NH1 ARG B 257 14. 518 61. 644 31. 915 1. 00 43. 47 3779 NH2 ARG B 257 12. 632 60. 775 32. 957 1. 00 43. 07 3780 C ARG B 257 18. 296 62. 430 35. 739 1. 00 31. 32 3781 O ARG B 257 18. 491 63. 228 34. 851 1. 00 30. 34 3782 N THR B 258 19. 205 61. 726 36. 420 1. 00 30. 47 3783 CA THR B 258 20. 652 61. 895 36. 182 1. 00 28. 88 3784 CB THR B 258 21. 357 62. 038 37. 586 1. 00 27. 94 3785 OG1 THR B 258 20. 814 63. 237 38. 147 1. 00 27. 03 3786 CG2 THR B 258 22. 853 61. 965 37. 629 1. 00 27. 73 3787 C THR B 258 21. 130 60. 635 35. 455 1. 00 27. 84 3788 o THR B 258 20. 627 59. 543 35. 748 1. 00 27. 20 3789 N ILE B 259 22. 084 60. 845 34. 582 1. 00 26. 97 3790 CA ILE B 259 22. 738 59. 787 33. 819 1. 00 26. 52 3791 CB ILE B 259 22. 192 59. 773 32. 323 1. 00 25. 99 3792 CG2 ILE B 259 22. 949 58. 794 31. 443 1. 00 25. 70 3793 CG1 ILE B 259 20. 659 59. 541 32. 413 1. 00 25. 39 3794 CD1 ILE B 259 19. 903 59. 808 31. 080 1. 00 25. 01 3795c ILE B 259 24. 233 60. 032 33. 773 1. 00 26. 25 3796 O ILE B 259 24. 635 60. 945 33. 024 1. 00 26. 85 3797 N THR B 260 24. 989 59. 266 34. 499 1. 00 26. 11 3798 CA THR B 260 26. 436 59. 324 34. 561 1. 00 26. 22 3799 CB THR B 260 27. 080 59. 236 35. 985 1. 00 25. 97 3800 OG1 THR B 260 26. 567 60. 324 36. 801 1. 00 26. 04 3801 CG2 THR B 260 28. 611 59. 257 35. 995 1. 00 24. 63 3802 C THR B 260 27. 021 58. 193 33. 681 1. 00 26. 59 3803 0 THR B 260 26. 736 56. 992 33. 880 1. 00 26. 15 3804 N THR B 261 27. 829 58. 649 32. 736 1. 00 26. 80 3805 CA THR B 261 28. 506 57. 807 31. 771 1. 00 26. 56 3806 CB THR B 261 28. 225 58. 234 30. 290 1. 00 26. 56 3807 OG1 THR B 261 28. 995 59. 411 29. 941 1. 00 27. 75 3808 CG2 THR B 261 26. 717 58. 511 30. 117 1. 00 26. 35 3809 C THR B 261 30. 002 57. 766 32. 029 1. 00 26. 60 3810 O THR B 261 30. 607 56. 710 31. 734 1. 00 27. 57 3811 N GLY B 262 30. 547 58. 849 32. 535 1. 00 25. 20 3812 CA GLY B 262 31. 955 58. 999 32. 834 1. 00 23. 70 3813 C GLY B 262 32. 659 59. 799 31. 747 1. 00 22. 69 3814 O GLY B 262 33. 888 59. 818 31. 627 1. 00 22. 80 3815 N SER B 263 31. 842 60. 419 30. 914 1. 00 21. 57 3816 CA SER B 263 32. 298 61. 241 29. 777 1. 00 20. 60 3817 CB SER B 263 30.986 61.688 29.056 1.00 20. 81 3818 OG SER B 263 31.218 62.465 27.927 1.00 21. 03 3819 C SER B 263 32. 861 62. 541 30. 376 1. 00 20. 15 3820 O SER B 263 32. 333 62. 921 31. 445 1. 00 20. 62 3821 N PRO B 264 33. 732 63. 184 29. 657 1. 00 19. 35 3822 CD PRO B 264 34. 323 62. 720 28. 383 1. 00 19. 37 3823 CA PRO B 264 34. 293 64. 475 30. 082 1. 00 18. 71 3824 CB PRO B 264 35. 559 64. 576 29. 254 1. 00 18. 60 3825 CG PRO B 264 35. 198 63. 884 27. 942 1. 00 18. 77 3826 C PRO B 264 33. 313 65. 623 29. 858 1. 00 18. 57 3827 0 PRO B 264 33. 611 66. 821 30. 167 1. 00 18. 62 3828 N ILE B 265 32. 177 65. 363 29. 280 1. 00 18. 56 3829 CA ILE B 265 31. 088 66. 269 28. 981 1. 00 17. 67 3830 CB ILE B 265 30. 608 66. 390 27. 504 1. 00 17. 08 3831 CG2 ILE B 265 29. 480 67. 494 27. 339 1. 00 14. 05 3832 CG1 ILE B 265 31. 785 66. 855 26. 542 1. 00 17. 73 3833 CD1 ILE B 265 31.216 66.813 25.063 1.00 17. 96 3834 C ILE B 265 29. 897 66. 005 29. 867 1. 00 17. 86 38350 ILE B 265 29. 388 64. 882 29. 921 1. 00 18. 08 3836 N THR B 266 29.387 67.089 30.481 1.00 18. 17 3837 CA THR B 266 28. 211 67. 004 31. 305 1. 00 18. 19 3838 CB THR B 266 28. 424 67. 143 32. 852 1. 00 16. 89 3839 OG1 THR B 266 29. 416 66. 237 33. 300 1. 00 16. 49 3840 CG2 THR B 266 27. 117 67. 082 33. 660 1. 00 14. 94 3841 C THR B 266 27. 230 68. 128 30. 927 1. 00 19. 19 3842 0 THR B 266 27. 677 69. 317 30. 942 1. 00 20. 45 3843 N TYR B 267 26. 021 67. 742 30. 684 1. 00 19. 47 3844 CA TYR B 267 24. 865 68. 620 30. 438 1. 00 18. 54 3845 CB TYR B 267 24. 007 68. 071 29. 279 1. 00 19. 26 3846 CG TYR B 267 24. 714 68. 262 27. 984 1. 00 19. 09 3847 CD1 TYR B 267 25. 508 67. 234 27. 407 1. 00 20. 50 3848 CE1 TYR B 267 26. 174 67. 456 26. 200 1. 00 20. 11 3849 CD2 TYR B 267 24. 651 69. 468 27. 352 1. 00 18. 89 3850 CE2 TYR B 267 25. 345 69. 723 26. 174 1. 00 18. 94 3851 CZ TYR B 267 26. 070 68. 699 25. 594 1. 00 20. 35 3852 OH TYR B 267 26. 714 68. 978 24. 418 1. 00 21. 52 3853 C TYR B 267 23. 999 68. 646 31. 689 1. 00 17. 72 3854 0 TYR B 267 3. 606 67. 583 32. 164 1. 00 16. 96 3855 N SER B 268 23. 787 69. 845 32. 251 1. 00 17. 21 3856 CA SER B 268 22. 940 70. 030 33. 443 1. 00 16. 24 3857 CB SER B 268 23. 753 70. 170 34. 734 1. 00 16. 69 3858 OG SER B 268 22. 741 70. 377 35. 780 1. 00 16. 23 3859 C SER B 268 22. 024 71. 201 33. 307 1. 00 15. 94 3860 0 SER B 268 22. 454 72. 166 32. 586 1. 00 16. 79 3861 N THR B 269 20. 841 71. 234 33. 894 1. 00 15. 59 3862 CA THR B 269 19. 985 72. 436 33. 803 1. 00 15. 79 3863 CB THR B 269 18. 458 72. 209 34. 040 1. 00 15. 30 3864 OG1 THR B 269 18. 375 71. 707 35. 397 1. 00 16. 63 3865 CG2 THR B 269 17. 754 71. 169 33. 127 1. 00 15. 13 3866 C THR B 269 20. 539 73. 411 34. 887 1. 00 15. 45 3867 0 THR B 269 21. 368 72. 978 35. 734 1. 00 15. 05 3868 N TYR B 270 20. 154 74. 666 34. 868 1. 00 16. 06 3869 CA TYR B 270 20. 660 75. 595 35. 926 1. 00 15. 71 3870 CB TYR B 270 20. 532 77. 071 35. 675 1. 00 15. 42 3871 CG TYR B 270 21. 300 77. 703 34. 533 1. 00 14. 13 3872 CD1 TYR B 270 20. 696 77. 923 33. 296 1. 00 14. 12 3873 CE1 TYR B 270 21. 383 78. 488 32. 202 1. 00 14. 42 3874 CD2 TYR B 270 22. 635 77. 990 34. 652 1. 00 14. 11 3875 CE2 TYR B 270 23. 333 78. 558 33. 605 1. 00 14. 32 3876 CZ TYR B 270 22. 749 78. 771 32. 408 1. 00 14. 44 3877 OH TYR B 270 23. 501 79. 272 31. 381 1. 00 15. 73 3878 C TYR B 270 20. 142 75. 159 37. 289 1. 00 15. 56 3879 O TYR B 270 20. 878 75. 096 38. 274 1. 00 15. 74 3880 N GLY B 271 18. 831 74. 880 37. 442 1. 00 15. 53 3881 CA GLY B 271 18. 254 74. 460 38. 705 1. 00 15. 39 3882 C GLY B 271 18. 862 73. 220 39. 341 1. 00 15. 58 38830 GLY B 271 18. 903 73. 075 40. 579 1. 00 15. 31 3884 N LYS B 272 19. 371 72. 336 38. 524 1. 00 16. 43 3885 CA LYS B 272 19. 962 71. 005 39. 038 1. 00 15. 46 3886 CB LYS B 272 19. 824 70. 082 37. 864 1. 00 14. 80 3887 CG LYS B 272 19. 708 68. 619 38. 202 1. 00 16. 61 3888 CD LYS B 272 20. 829 67. 951 38. 851 1. 00 16. 07 3889 CE LYS B 272 20. 684 66. 593 39. 416 1. 00 17. 16 3890 NZ LYS B 272 20. 096 66. 490 40. 764 1. 00 17. 98 3891 C LYS B 272 21. 349 71. 279 39. 543 1. 00 15. 39 3892 0 LYS B 272 21. 882 70. 729 40. 569 1. 00 15. 43 3893 N PHE B 273 21. 987 72. 218 38. 888 1. 00 15. 30 3894 CA PHE B 273 23. 335 72. 758 39. 216 1. 00 14. 39 3895 CB PHE B 273 23. 946 73. 595 38. 149 1. 00 14. 48 3896 CG PHE B 273 25. 160 74. 412 38. 512 1. 00 15. 05 3897 CD1 PHE B 273 26. 435 73. 930 38. 384 1. 00 15. 15 3898 CD2 PHE B 273 24. 956 75. 718 39. 012 1. 00 14. 38 3899 CE1 PHE B 273 27. 550 74. 675 38. 740 1. 00 14. 17 3900 CE2 PHE B 273 26. 039 76. 502 39. 398 1. 00 13. 82 3901 CZ PHE B 273 27. 337 75. 959 39. 246 1. 00 13. 73 3902 C PHE B 273 23. 209 73. 407 40. 592 1. 00 13. 45 3903 0 PHE B 273 23. 980 73. 140 41. 506 1. 00 12. 70 3904 N LEU B 274 22. 121 74. 180 40. 763 1. 00 13. 35 3905 CA LEU B 274 21. 893 74. 846 42. 044 1. 00 12. 14 3906 CB LEU B 274 20. 860 75. 961 41. 826 1. 00 14. 00 3907 CG LEU B 274 21. 309 77. 133 40. 957 1. 00 13. 54 3908 CD1 LEU B 274 20. 193 78. 123 40. 804 1. 00 14. 16 3909 CD2 LEU B 274 22. 517 77. 766 41. 696 1. 00 14. 69 3910 C LEU B 274 21. 550 73. 852 43. 135 1. 00 12. 43 39110 LEU B 274 22. 006 73. 992 44. 282 1. 00 12. 99 3912 N ALA B 275 20. 790 72. 838 42. 818 1. 00 12. 68 3913 CA ALA B 275 20. 356 71. 793 43. 726 1. 00 13. 72 3914 CB ALA B 275 19. 292 70. 860 43. 187 1. 00 13. 79 3915 C ALA B 275 21. 539 70. 958 44. 231 1. 00 14.20 3916 O ALA B 275 21. 452 70. 394 45. 301 1. 00 13.43 3917 N ASP B 276 22. 544 70. 909 43. 341 1. 00 14.25 3918 CA ASP B 276 23. 783 70. 218 43. 592 1. 00 14.29 3919 CB ASP B 276 24.380 69.668 42.292 1. 00 14.79 3920 CG ASP B 276 23. 569 68. 597 41. 586 1. 00 16.42 3921 OD1 ASP B 276 23. 577 68. 393 40. 325 1. 00 16.84 3922 OD2 ASP B 276 22. 806 67. 912 42. 257 1. 00 18.21 3923 C ASP B 276 24. 765 71. 078 44. 361 1. 00 14.48 3924 O ASP B 276 25. 897 70. 501 44. 596 1. 00 14.99 3925 N GLY B 277 24. 482 72. 249 44. 786 1. 00 13.93 3926 CA GLY B 277 25. 436 73. 096 45. 538 1. 00 13.89 3927 C GLY B 277 26. 351 73. 916 44. 675 1. 00 14.89 3928 0 GLY B 277 27.350 74.530 45.207 1. 00 15.38 3929 N GLY B 278 26. 137 73. 893 43. 344 1. 00 14.12 3930 CA GLY B 278 27. 028 74. 725 42. 485 1. 00 13.64 3931 C GLY B 278 28. 271 73. 901 42. 108 1. 00 12.94 3932 O GLY B 278 28. 109 72. 757 41. 752 1. 00 11.72 3933 N CYS B 279 29. 416 74. 592 42. 093 1. 00 12.38 3934 CA CYS B 279 30. 670 73. 904 41. 662 1. 00 12.87 3935 CB CYS B 279 31. 662 75. 014 41. 214 1. 00 15.75 3936 SG CYS B 279 31. 204 75. 948 39. 768 1. 00 17.23 3937 C CYS B 279 31. 332 73. 050 42. 731 1. 00 13.52 3938 0 CYS B 279 31. 451 73. 555 43. 867 1. 00 13.94 3939 N SER B 280 31. 648 71. 784 42. 420 1. 00 13.53 3940 CA SER B 280 32. 439 70. 939 43. 359 1. 00 14.17 3941 CB SER B 280 32. 092 69. 511 43. 600 1. 00 14.57 3942 OG SER B 280 32. 315 68. 642 42. 519 1. 00 13.89 3943 C SER B 280 33. 871 71. 132 42. 847 1. 00 15.13 3944 O SER B 280 34. 129'71. 695 41. 695 1. 00 16.70 3945 N GLY B 281 34. 856 70. 947 43. 673 1. 00 15.59 3946 CA GLY B 281 36. 255 71. 125 43. 354 1. 00 14.07 3947 C GLY B 281 36. 763 70. 141 42. 292 1. 00 14.24 3948 O GLY B 281 36.713 68.902 42.327 1. 00 13.49 3949 N GLY B 282 37. 334 70. 770 41. 291 1. 00 13.43 3950 CA GLY B 282 38. 037 70. 343 40. 145 1. 00 13.10 3951 C GLY B 282 37. 398 69. 472 39. 129 1. 00 13.02 39520GLY B 282 38. 127 68. 851 38. 336 1. 00 12.85 3953 N ALA B 283 36. 076 69. 484 39. 119 1. 00 12.91 3954 CA ALA B 283 35. 246 68. 683 38. 272 1. 00 13.22 3955 CB ALA B 283 33. 826 68. 652 38. 836 1. 00 14.03 3956 C ALA B 283 35. 287 69. 071 36. 826 1. 00 14.13 3957 O ALA B 283 35. 205 68. 181 35. 994 1. 00 13.59 3958 N TYR B 284 35. 336 70. 378 36. 521 1. 00 14.59 3959 CA TYR B 284 35. 344 70. 858 35. 147 1. 00 15.21 3960 CB TYR B 284 33.951 71.585 34.841 1. 00 15.00 3961 CG TYR B 284 32. 875 70. 541 35. 056 1. 00 14.95 3962 CD1 TYR B 284 32. 133 70. 474 36. 192 1. 00 15.09 3963 CE1 TYR B 284 31. 213 69. 450 36. 382 1. 00 15.04 3964 CD2 TYR B 284 32. 706 69. 567 34. 076 1. 00 15.15 3965 CE2 TYR B 284 31. 765 68. 556 34. 218 1. 00 15.49 3966 CZ TYR B 284 31. 026 68. 516 35. 384 1. 00 15.13 3967 OH TYR B 284 30.141 67.479 35.501 1. 00 16.10 3968 C TYR B 284 36. 435 71. 900 34. 902 1. 00 15.48 3969 O TYR B 284 36. 858 72. 646 35. 789 1. 00 15.96 3970 N ASP B 285 36.872 71.958 33.677 1. 00 16.28 3971 CA ASP B 285 37.931 72.863 33.207 1. 00 16.37 3972 CB ASP B 285 38. 869 72. 227 32. 159 1. 00 16. 66 3973 CG ASP B 285 39. 666 71. 029 32. 651 1. 00 16. 77 3974 OD1 ASP B 285 39. 481 69. 908 32. 182 1. 00 17. 69 3975 OD2 ASP B 285 40. 473 71. 205 33. 568 1. 00 16. 32 3976 C ASP B 285 37. 265 74. 098 32. 598 1. 00 16. 57 3977 O ASP B 285 37. 807 75. 207 32. 781 1. 00 17. 73 3978 N ILE B 286 36. 191 73. 857 31. 922 1. 00 16. 74 3979 CA ILE B 286 35. 363 74. 807 31. 219 1. 00 17. 07 3980 CB ILE B 286 35. 434 74. 463 29. 658 1. 00 17. 45 3981 CG2 ILE B 286 34. 584 75. 401 28. 780 1. 00 17. 34 3982 CG1 ILE B 286 36. 944 74. 462 29. 306 1. 00 16. 97 3983 CD1 ILE B 286 37. 290 74. 250 27. 858 1. 00 16. 07 3984 C ILE B 286 33. 903 74. 625 31. 625 1. 00 17. 45 39850 ILE B 286 33. 398 73. 510 31. 750 1. 00 18. 09 3986 N ILE B 287 33. 259 75. 787 31. 863 1. 00 17. 34 3987 CA ILE B 287 31. 845 75. 795 32. 214 1. 00 15. 91 3988 CB ILE B 287 31. 618 76. 284 33. 663 1. 00 13. 93 3989 CG2 ILE B 287 30.098 76.183 33.991 1.00 13. 67 3990 CG1 ILE B 287 32. 513 75. 466 34. 634 1. 00 13. 70 3991 CD1 ILE B 287 32.430 75.928 36.121 1.00 12. 20 3992 C ILE B 287 31. 150 76. 697 31. 179 1. 00 15. 99 39930 ILE B 287 31. 504 77. 894 31. 093 1. 00 16. 06 3994 N ILE B 288 30. 264 76. 116 30. 416 1. 00 15. 68 3995 CA ILE B 288 29. 588 76. 964 29. 368 1. 00 15. 38 3996 CB ILE B 288 29.429 76.162 28.040 1.00 15. 08 3997 CG2 ILE B 288 28.608 76.889 26.936 1.00 15. 07 3998 CG1 ILE B 288 30. 864 75. 885 27. 529 1. 00 15. 01 3999 CD1 ILE B 288 30. 860 75. 082 26. 191 1. 00 14. 54 4000 C ILE B 288 28. 218 77. 276 29. 960 1. 00 16. 14 4001 0 ILE B 288 27. 555 76. 285 30. 288 1-. 00 15. 88 4002 N CYS B 289 27. 981 78. 566 30. 061 1. 00 16. 09 4003 CA CYS B 289 26.616 78.985 30.563 1.00 16. 58 4004 CB CYS B 289 26. 768 80. 213 31. 469 1. 00 14. 23 4005 SG CYS B 289 27. 510 79. 842 33. 025 1. 00 12. 94 4006 C CYS B 289 25. 835 79. 264 29. 287 1. 00 17. 76 4007 O CYS B 289 26. 004 80. 280 28. 677 1. 00 17. 33 4008 N ASP B 290 25. 029 78. 280 28. 886 1. 00 19. 01 4009 CA ASP B 290 24. 295 78. 363 27. 619 1. 00 20. 56 4010 CB ASP B 290 24. 107 76. 939 27. 123 1. 00 22. 00 4011 CG ASP B 290 23. 637 76. 768 25. 739 1. 00 24. 04 4012 OD1 ASP B 290 24. 009 77. 512 24. 819 1. 00 26. 10 4013 OD2 ASP B 290 22.875 75.773 25.525 1.00 25. 49 4014 C ASP B 290 23. 069 79. 245 27. 801 1. 00 20. 95 4015 O ASP B 290 22. 551 79. 364 28. 908 1. 00 20. 08 4016 N GLU B 291 22. 683 79. 886 26. 689 1. 00 22. 20 4017 CA GLU B 291 21. 508 80. 818 26. 779 1. 00 23. 39 4018 CB GLU B 291 20. 251 80. 025 26. 500 1. 00 26. 49 4019 CG GLU B 291 20. 337 79. 766 24. 917 1. 00 29. 87 4020 CD GLU B 291 19. 482 78. 692 24. 430 1. 00 32. 36 4021 OE1 GLU B 291 18. 575 78. 194 25. 100 1. 00 35. 11 4022 OE2 GLU B 291 19. 835 78. 262 23. 305 1. 00 32. 92 4023 C GLU B 291 21. 623 81. 753 27. 930 1. 00 23. 15 40240 GLU B 291 20. 813 81. 857 28. 870 1. 00 24. 11 4025 N CYS B 292 22. 709 82. 541 27. 863 1. 00 22. 02 4026 CA CYS B 292 23. 087 83. 469 28. 923 1. 00 21. 93 4027 CB CYS B 292 24. 562 83. 712 29. 000 1. 00 20. 67 4028 SG CYS B 292 25. 239 84. 524 27. 588 1. 00 22. 43 4029 C CYS B 292 22. 211 84. 707 28. 923 1. 00 21. 58 4030 O CYS B 292 22. 339 85. 496 29. 871 1. 00 22. 25 4031 N HIS B 293 21. 350 84. 807 27. 933 1. 00 20. 75 4032 CA HIS B 293 20. 456 85. 982 27. 862 1. 00 20. 83 4033 CB HIS B 293 20. 026 86. 254 26. 374 1. 00 20. 03 4034 CG HIS B 293 19. 313 84. 997 25. 876 1. 00 20. 28 4035 CD2 HIS B 293 18. 027 84. 643 25. 994 1. 00 20. 71 4036 ND1 HIS B 293 19. 946 83. 940 25. 282 1. 00 19. 58 4037 CE1 HIS B 293 19. 063 83. 004 25. 052 1. 00 20. 24 4038 NE2 HIS B 293 17. 880 83. 386 25. 501 1. 00 21. 27 4039 C HIS B 293 19. 270 85. 688 28. 714 1. 00 20. 44 4040 O HIS B 293 18. 399 86. 539 28. 871 1. 00 20. 71 4041 N SER B 294 19. 186 84. 437 29. 222 1. 00 20. 33 4042 CA SER B 294 18. 011 84. 065 30. 030 1. 00 19. 11 4043 CB SER B 294 18. 076 82. 564 30. 426 1. 00 19. 40 4044 OG SER B 294 18. 465 81. 904 29. 230 1. 00 20. 16 4045 C SER B 294 17. 941 84. 919 31. 270 1. 00 18. 49 4046 O SER B 294 18. 942 85. 099 31. 952 1. 00 18. 50 4047 N THR B 295 16. 692 85. 372 31. 604 1. 00 17. 61 4048 CA THR B 295 16. 502 86. 183 32. 760 1. 00 16. 49 4049 CB THR B 295 16. 438 87. 736 32. 544 1. 00 15. 21 4050 OG1 THR B 295 15. 251 87. 969 31. 660 1. 00 16. 66 4051 CG2 THR B 295 17. 626 88. 359 31. 820 1. 00 13. 59 4052 C THR B 295 15. 580 85. 612 33. 777 1. 00 16. 05 4053 O THR B 295 15. 174 86. 406 34.. 638 1. 00 16. 17 4054 N ASP B 296 15. 269 84. 297 33. 715 1. 00 15. 56 4055 CA ASP B 296 14. 407 83. 730 34. 786 1. 00 15. 07 4056 CB ASP B 296 13. 988 82. 303 34. 325 1. 00 15. 27 4057 CG ASP B 296 15. 147 81. 420 34. 014 1. 00 16. 43 4058 OD1 ASP B 296 15. 634 80. 674 34. 887 1. 00 17. 16 4059 OD2 ASP B 296 15. 701 81. 365 32. 906 1. 00 17. 10 4060 C ASP B 296 15. 340 83. 671 36. 006 1. 00 14. 53 4061 O ASP B 296 16. 537 83. 460 35. 704 1. 00 15. 19 4062 N ALA B 297 14. 906 83. 727 37. 219 1. 00 13. 70 4063 CA ALA B 297 15. 718 83. 697 38. 401 1. 00 13. 36 4064 CB ALA B 297 14. 970 83. 493 39. 693 1. 00 11. 97 4065 C ALA B 297 16. 832 82. 616 38. 435 1. 00 13. 94 4066 0 ALA B 97 17. 867 82. 787 38. 987 1. 00 13. 25 4067 N THR B 298 16. 379 81. 372 38. 133 1. 00 14. 42 4068 CA THR B 298 17. 251 80. 214 38. 130 1. 00 15. 19 4069 CB THR B 298 16. 427 78. 881 37. 893 1. 00 14. 64 4070 OG1 THR B 298 15. 453 78. 927 38. 969 1. 00 14. 42 4071 CG2 THR B 298 17. 423 77. 725 38. 268 1. 00 14. 10 4072 C THR B 298 18.515 80.313 37.350 1.00 15. 50 4073 O THR B 298 19. 603 79. 839 37. 831 1. 00 17. 07 4074 N SER B 299 18. 472 80. 899 36. 142 1. 00 15. 34 4075 CA SER B 299 19. 563 81. 159 35. 262 1. 00 13. 69 4076 CB SER B 299 19. 055 81. 594 33. 868 1. 00 14. 75 4077 OG SER B 299 18. 256 80. 565 33. 241 1. 00 14. 12 4078 C SER B 299 20. 479 82. 233 35. 812 1. 00 14. 13 4079 O SER B 299 21. 714 82. 180 35. 701 1. 00 14. 29 4080 N ILE B 300 19. 895 83. 334 36. 236 1. 00 13. 93 4081 CA ILE B 300 20. 660 84. 474 36. 824 1. 00 13. 53 4082 CB ILE B 300 19. 631 85. 655 37. 024 1. 00 13. 55 4083 CG1 ILE B 300 19. 271 86. 211 35. 627 1. 00 12. 64 4084 CD1 ILE B 300 18. 081 87. 226 35. 646 1. 00 14. 21 4085 CG2 ILE B 300 20. 205 86. 797 37. 949 1. 00 12. 02 4086 C ILE B 300 21. 380 83. 927 38. 034 1. 00 13.70 4087 0 ILE B 300 22. 611 84. 046 38. 184 1. 00 13.26 4088 N LEU B 301 20. 697 83. 322 38. 963 1. 00 14.68 4089 CA LEU B 301 21. 374 82. 731 40. 137 1. 00 15.00 4090 CB LEU B 301 20. 237 82. 331 41. 123 1. 00 16.36 4091 CG LEU B 301 20. 834 82. 011 42. 498 1. 00 16.01 4092 CD1 LEU B 301 21. 559 83. 276 43. 037 1. 00 16.31 4093 CD2 LEU B 301 19. 670 81. 679 43. 419 1. 00 16.86 4094 C LEU B 301 22.356 81.658 39.768 1. 00 15.36 4095 0 LEU B 301 23. 471 81. 601 40. 376 1. 00 15.80 4096 N GLY B 302 22. 129 80. 820 38. 790 1. 00 14.60 4097 CA GLY B 302 23. 055 79. 758 38. 386 1. 00 14.24 4098 C GLY B 302 24. 290 80. 327 37. 765 1. 00 14.35 4099 O GLY B 302 25. 417 79. 846 38. 079 1. 00 14.65 4100 N ILE B 303 24. 170 81. 280 36. 871 1. 00 14.53 4101 CA ILE B 303 25. 285 81. 979 36. 206 1. 00 14.18 4102 CB ILE B 303 24. 739 82. 900 35. 035 1. 00 14.88 4103 CG2 ILE B 303 25.813 83.882 34.509 1. 00 15.49 4104 CG1 ILE B 303 24. 148 82. 049 33. 904 1. 00 13.09 4105 CD1 ILE B 303 23. 586 82. 860 32. 707 1. 00 12.85 4106 C ILE B 303 26. 108 82. 721 37. 232 1. 00 14.29 41070 ILE B 303 27. 362 82. 675 37. 236 1. 00 14.22 4108 N GLY B 304 25. 507 83. 398 38. 164 1. 00 13.55 4109 CA GLY B 304 26. 136 84. 145 39. 241 1. 00 12.44 4110 C GLY B 304 26. 921 83. 183 40. 116 1. 00 12.32 4111 O GLY B 304 28. 015 83. 518 40. 550 1. 00 12.58 4112 N THR B 305 26. 321 81. 998 40. 375 1. 00 12.13 4113 CA THR B 305 27.036 80.958 41.156 1. 00 11.06 4114 CB THR B 305 26. 083 79. 731 41. 479 1. 00 10.56 4115 OG1 THR B 305 24.932 80.298 42.256 1. 00 11.63 4116 CG2 THR B 305 26. 714 78. 642 42. 286 1. 00 8.08 4117 C THR B 305 28. 260 80. 499 40. 383 1. 00 10.46 4118 0 THR B 305 29. 275 80. 103 41. 010 1. 00 10.39 4119 N VAL B 306 28. 159 80. 310 39. 084 1. 00 10.62 4120 CA VAL B 306 29. 313 79. 913 38. 263 1. 00 9.49 4121 CB VAL B 306 28. 991 79. 669 36. 814 1. 00 7.83 4122 CG1 VAL B 306 30. 245 79. 540 35. 914 1. 00 5.75 4123 CG2 VAL B 306 28. 246 78. 299 36. 713 1. 00 5.45 4124 C VAL B 306 30. 390 80. 983 38. 381 1. 00 10.74 4125 0 VAL B 306 31. 551 80. 605 38. 678 1. 00 11.16 4126 N LEU B 307 30. 021 82. 225 38. 163 1. 00 10.55 4127 CA LEU B 307 30.962 83.384 38.228 1. 00 10.30 4128 CB LEU B 307 30.166 84.552 37.597 1. 00 7.20 4129 CG LEU B 307 29. 711 84. 514 36. 244 1. 00 6.51 4130 CD1 LEU B 307 28. 695 85. 593 35. 786 1. 00 7.51 4131 CD2 LEU B 307 30. 754 84. 444 35. 153 1. 00 5.80 4132 C LEU B 307 31. 653 83. 609 39. 500 1. 00 11.37 4133 O LEU B 30732. 92183. 94039. 6201. 00 11.88 4134 N ASP B 308 31.015 83.329 40.608 1. 00 11.99 4135 CA ASP B 308 31. 562 83. 430 41. 949 1. 00 12.74 4136 CB ASP B 308 30. 458 83. 654 42. 958 1. 00 14.01 4137 CG ASP B 308 30. 903 83. 605 44. 402 1. 00 14.46 4138 OD1 ASP B 308 31. 540 84. 575 44. 875 1. 00 14.63 4139 OD2 ASP B 308 30. 564 82. 667 45. 096 1. 00 13.26 4140 C ASP B 308 32. 455 82. 255 42. 306 1. 00 13.50 4141 0 ASP B 308 33. 426 82. 457 43. 079 1. 00 14.07 4142 N GLN B 309 32. 135 81. 058 41. 866 1. 00 12.67 4143 CA GLN B 309 32. 884 79. 862 42. 198 1. 00 11.85 4144 CB GLN B 309 31. 847 78. 711 42. 478 1. 00 10.78 4145 CG GLN B 309 30. 964 79. 102 43. 673 1. 00 10.26 4146 CD GLN B 309 29. 897 78. 049 43. 927 1. 00 12.93 4147 OE1 GLN B 309 29. 172 78. 215 44. 932 1. 00 15.59 4148 NE2 GLN B 309 29. 707 77. 159 42. 975 1. 00 10.75 4149 C GLN B 309 33. 894 79. 288 41. 228 1. 00 11.96 4150 O GLN B 309 34. 896 78. 741 41. 721 1. 00 12.24 4151 N ALA B 310 33. 681 79. 333 39. 980 1. 00 11.88 4152 CA ALA B 310 34. 533 78. 745 38. 958 1. 00 13.01 4153 CB ALA B 310 34. 152 79. 325 37. 613 1. 00 12.75 4154 C ALA B 310 35. 976 78. 710 39. 261 1. 00 13.67 4155 O ALA B 310 36.612 77.627 39.268 1. 00 15.01 4156 N GLU B 311 36. 613 79. 851 39. 470 1. 00 14.15 4157 CA GLU B 311 38. 065 79. 960 39. 679 1. 00 14.78 4158 CB GLU B 311 38. 601 81. 375 39. 566 1. 00 15.29 4159 CG GLU B 311 40. 118 81. 526 39. 556 1. 00 17.87 4160 CD GLU B 311 40. 609 82. 948 39. 622 1. 00 20.19 4161 OE1 GLU B 311 39. 836 83. 861 39. 804 1. 00 21.59 4162 OE2 GLU B 311 41. 835 83. 092 39. 554 1. 00 21.08 4163 C GLU B 311 38. 462 79. 291 40. 942 1. 00 14.59 4164 O GLU B 311 39. 533 78. 674 41. 053 1. 00 14.93 4165 N THR B 312 37. 551 79. 331 41. 928 1. 00 14.73 4166 CA THR B 312 37. 727 78. 648 43. 193 1. 00 14.53 4167 CB THR B 312 36. 810 79. 058 44. 390 1. 00 15.28 4168 OG1 THR B 312 37. 228 80. 417 44. 701 1. 00 13.35 4169 CG2 THR B 312 37. 005 78. 132 45. 627 1. 00 16.24 4170 C THR B 312 37. 732 77. 147 42. 977 1. 00 14.99 4171 O THR B 312 38. 759 76. 552 43. 406 1. 00 15.39 4172 N ALA B 313 36. 781 76. 597 42. 213 1. 00 13.64 4173 CA ALA B 313 36. 785 75. 164 41. 982 1. 00 13.34 4174 CB ALA B 313 35. 378 74. 669 41. 654 1. 00 12.79 4175 C ALA B 313 37. 786 74. 612 40. 956 1. 00 12.96 4176 O ALA B 313 37. 632 73. 404 40. 524 1. 00 12.14 4177 N GLY B 314 38. 668 75. 348 40. 458 1. 00 13.13 4178 CA GLY B 314 39. 684 75. 067 39. 492 1. 00 14.10 4179 C GLY B 314 39. 332 75. 170 38. 048 1. 00 14.46 41800GLY B 314 40. 188 74. 721 37. 181 1. 00 14.49 4181 N ALA B 315 38. 240 75. 774 37. 646 1. 00 14.70 4182 CA ALA B 315 37. 950 75. 898 36. 200 1. 00 15.38 4183 CB ALA B 315 36. 506 76. 364 35. 967 1. 00 13.93 4184 C ALA B 315 38. 934 76. 939 35. 651 1. 00 16.65 4185 O ALA B 315 39. 446 77. 780 36. 434 1. 00 16.93 4186 N ARG B 316 39. 199 76. 858 34. 375 1. 00 17.82 4187 CA ARG B 316 40. 048 77. 760 33. 642 1. 00 19.20 4188 CB ARG B 316 41. 318 77. 264 33. 003 1. 00 23.49 4189 CG ARG B 316 42. 555 77. 142 33. 932 1. 00 27.21 4190 CD ARG B 316 43. 716 76. 607 33. 098 1. 00 29.85 4191 NE ARG B 316 43. 499 75. 207 32. 821 1. 00 32.61 4192 CZ ARG B 316 44. 117 74. 475 31. 885 1. 00 34.90 4193 NH1 ARG B 316 44. 958 74. 960 30. 986 1. 00 34.93 4194 NH2 ARG B 316 43. 924 73. 123 31. 952 1. 00 36.33 4195 C ARG B 316 39. 302 78. 714 32. 702 1. 00 18.19 41960ARG B 316 39.818 79.802 32.363 1. 00 18.08 4197 N LEU B 317 38. 113 78. 308 32. 333 1. 00 16.91 4198 CA LEU B 317 37. 289 79. 076 31. 419 1. 00 15.94 4199 CB LEU B 317 37. 697 78. 529 30. 003 1. 00 14.44 4200 CG LEU B 317 37. 023 79. 132 28. 805 1. 00 13. 05 4201 CD1 LEU B 317 37. 326 80. 612 28. 597 1. 00 13. 78 4202 CD2 LEU B 317 37. 334 78. 370 27. 546 1. 00 12. 62 4203 C LEU B 317 35. 803 78. 927 31. 644 1. 00 15. 42 42040 LEU B 317 35. 309 77. 817 31. 816 1. 00 15. 70 4205 N VAL B 318 35. 097 80. 038 31. 725 1. 00 15. 63 4206 CA VAL B 318 33. 652 80. 182 31. 811 1. 00 15. 45 4207 CB VAL B 318 33. 056 81. 017 32. 942 1. 00 13. 20 4208 CG1 VAL B 318 31. 584 81. 382 32. 798 1. 00 12. 71 4209 CG2 VAL B 318 33. 315 80. 440 34. 343 1. 00 11. 68 4210 C VAL B 318 33. 335 80. 903 30. 473 1. 00 16. 07 4211 O VAL B 318 33. 943 81. 965 30. 267 1. 00 17. 76 4212 N VAL B 319 32. 486 80. 418 29. 684 1. 00 16. 55 4213 CA VAL B 319 31.982 80.884 28.424 1.00 16. 98 4214 CB VAL B 319 32. 055 79. 735 27. 358 1. 00 18. 35 4215 CG1 VAL B 319 31. 441 80. 193 26. 043 1. 00 17. 63 4216 CG2 VAL B 319 33. 456 79. 230 27. 149 1. 00 19. 36 4217 C VAL B 319 30. 486 81. 246 28. 648 1. 00 17. 01 4218 O VAL B 319 29. 741 80. 302 29. 062 1. 00 16. 87 4219 N LEU B 320 30. 145 82. 429 28. 311 1. 00 16. 63 4220 CA LEU B 320 28.794 82.999 28.405 1.00 17. 18 4221 CB LEU B 320 28. 957 84. 434 29. 003 1. 00 15. 08 4222 CG LEU B 320 29. 617 84. 449 30. 373 1. 00 13. 62 4223 CD1 LEU B 320 29. 853 85. 848 30. 870 1. 00 14. 16 4224 CD2 LEU B 320 28. 547 83. 734 31. 298 1. 00 12. 63 4225 C LEU B 320 28. 316 82. 989 26. 965 1. 00 18. 13 4226 O LEU B 320 28. 834 83. 795 26. 200 1. 00 19. 28 4227 N ALA B 321 27. 438 82. 066 26. 635 1. 00 18. 77 4228 CA ALA B 321 26. 935 81. 813 25. 294 1. 00 18. 46 4229 CB ALA B 321 27. 175'80. 319 25. 010 1. 00 18. 54 4230 C ALA B 321 25. 481 82. 114 25. 039 1. 00 18. 41 4231 0 ALA B 321 24. 598 81. 764 25. 791 1. 00 17. 94 4232 N THR B 322 25.268 82.842 23.919 1.00 19. 33 4233 CA THR B 322 23. 895 83. 215 23. 520 1. 00 19. 16 4234 CB THR B 322 23. 260 84. 365 24. 380 1. 00 19. 34 4235 OG1 THR B 322 21. 900 84. 561 23. 783 1. 00 18. 41 4236 CG2 THR B 322 24. 045 85. 637 24. 527 1. 00 17. 03 4237 C THR B 322 23. 847 83. 584 22. 064 1. 00 20. 02 4238 O THR B 322 24.869 84.060 21.536 1.00 20. 46 4239 N ALA B 323 22. 671 83. 398 21. 450 1. 00 21. 08 4240 CA ALA B 323 22. 601 83. 812 20. 018 1. 00 21. 28 4241 CB ALA B 323 21. 805 82. 924 19. 158 1. 00 22. 52 4242 C ALA B 323 22. 175 85. 276 20. 013 1. 00 21. 51 42430 ALA B 323 22. 298 85. 902 18. 960 1. 00 22. 31 4244 N THR B 324 21. 736 85. 755 21. 152 1. 00 21. 32 4245 CA THR B 324 21. 260 87. 114 21. 374 1. 00 21. 44 4246 CB THR B 324 19. 661 87. 031 21. 486 1. 00 21. 60 4247 OG1 THR B 324 19. 448 86. 082 22. 587 1. 00 22. 46 4248 CG2 THR B 324 19. 053 86. 505 20. 191 1. 00 22. 35 4249 C THR B 324 21. 750 87. 845 22. 615 1. 00 21. 75 4250 0 THR B 324 20.977 87.910 23.588 1.00 22. 03 4251 N PRO B 325 22. 957 88. 418 22. 590 1. 00 21. 61 4252 CA PRO B 325 23. 533 89. 152 23. 704 1. 00 22. 15 4253 CB PRO B 325 25.003 89.343 23.328 1.00 21.87 4254 CG PRO B 325 25. 023 89. 241 21. 835 1. 00 22. 04 4255 CD PRO B 325 23. 885 88. 300' 21. 462 1. 00 21. 70 4256 C PRO B 325 22. 882 90. 541 23. 862 1. 00 22. 69 4257 0 PRO B 325 22. 321 91. 055 22. 885 1. 00 23. 43 4258 N PRO B 326 23. 015 91. 103 25. 010 1. 00 22. 82 4259 CA PRO B 326 22. 443 92. 429 25. 341 1. 00 23. 30 4260PRO B 326 23. 110 92. 767 26. 676 1. 00 23. 22 4261PRO B 326 23. 062 91. 380 27. 326 1. 00 23. 30 4262 CD PRO B 326 23. 704 90. 521 26. 201 1. 00 23. 13 4263 C PRO B 326 22. 817 93. 394 24. 236 1. 00 23. 62 4264 O PRO B 326 23. 980 93. 391 23. 788 1. 00 24. 25 4265 N GLY B 327 21. 838 94. 114 23. 727 1. 00 23. 14 4266 CA GLY B 327 22. 074 95. 067 22. 640 1. 00 22. 98 4267 C GLY B 327 21. 923 94. 430 21. 289 1. 00 22. 68 4268 0 GLY B 327 22. 227 95. 053 20. 257 1. 00 23. 53 4269 N SER B 328 21. 479 93. 199 21. 217 1. 00 22. 12 4270 CA SER B 328 21. 254 92. 536 19. 934 1. 00 21. 07 4271 CB SER B 328 20. 974 91. 012 20. 082 1. 00 20. 98 4272 OG SER B 328 22. 237 90. 462 20. 226 1. 00 23. 47 4273 C SER B 328 20. 010 93. 150 19. 289 1. 00 19. 88 4274 0 SER B 328 19. 177 93. 540 20. 060 1. 00 19. 89 4275 N VAL B 329 20. 006 93. 073 17. 971 1. 00 19. 58 4276 CA VAL B 329 18. 856 93. 523 17. 161 1. 00 19. 05 4277 CB VAL B 329 19. 269 94. 724 16. 285 1. 00 21. 08 4278 CG1 VAL B 329 18. 072 95. 142 15. 394 1. 00 22. 12 4279 CG2 VAL B 329 19. 660 95. 925 17. 146 1. 00 20. 50 4280 C VAL B 329 18. 511 92. 314 16. 258 1. 00 19. 22 4281 0 VAL B 329 19. 444 91. 525 15. 986 1. 00 19. 14 4282 N THR B 330 17. 284 92. 199 15. 847 1. 00 19. 82 4283 CA THR B 330 16. 838 91. 094 14. 954 1. 00 20. 13 4284 CB THR B 330 15. 253 90. 978 14. 981 1. 00 18. 41 4285 OG1 THR B 330 14. 873 90. 882 16. 385 1. 00 18. 16 4286 CG2 THR B 330 14. 736 89. 764 14. 199 1. 00 18. 58 4287 C THR B 330 17. 260 91. 510 13. 520 1. 00 21. 11 4288 0 THR B 330 17. 035 92. 698 13. 148 1. 00 20. 46 4289 N VAL B 331 17. 907 90. 568 12. 850 1. 00 21. 75 4290 CA VAL B 331 18. 370 90. 817 11. 448 1. 00 22. 50 4291 CB VAL B 331 19. 917 90. 760 11. 397 1. 00 22. 99 4292 CG1 VAL B 331 20. 590 91. 788 12. 259 1. 00 23. 40 , 4293 CG2 VAL B 331 20. 373 89. 362 11. 877 1. 00 23. 33 4294 C VAL B 331 17. 814 89. 672 10. 602 1. 00 23. 06 42950VAL B 331 17. 434 88. 642 11. 155 1. 00 22. 42 4296 N PRO B 332 17. 809 89. 907 9. 314 1. 00 24. 92 4297 CA PRO B 332 17. 320 88. 906 8. 335 1. 00 25. 65 4298 CB PRO B 332 17. 466 89. 598 6. 994 1. 00 25. 57 4299 CG PRO B 332 17. 400 91. 053 7. 328 1. 00 24. 90 4300 CD PRO B 332 18. 294 91. 121 8. 606 1. 00 24. 94 4301 C PRO B 332 18. 018 87. 605 8. 523 1. 00 27. 20 4302 0 PRO B 332 19. 237 87. 519 8. 777 1. 00 27. 76 4303 N HIS B 333 17. 222 86. 521 8. 465 1. 00 28. 57 4304 CA HIS B 333 17. 790 85. 167 8. 680 1. 00 29. 93 4305HIS B 333 17. 061 84. 383 9. 771 1. 00 31. 26 4306HIS B 333 17. 661 83. 147 10. 299 1. 00 31. 82 4307 ND1 HIS B 333 18. 446 83. 116 11. 442 1. 00 32. 52 4308 CE1 HIS B 333 18. 880 81. 904 11. 668 1. 00 32. 15 4309 NE2 HIS B 333 18. 360 81. 103 10. 767 1. 00 32. 76 4310 CD2 HIS B 333 17. 601 81. 856 9. 897 1. 00 32. 75 4311 C HIS B 333 17. 588 84. 426 7. 356 1. 00 30. 63 43120HIS B 333 16. 612 84. 685 6. 646 1. 00 30. 97 4313 N PRO B 334 18. 579 83. 619 7. 055 1. 00 30. 98 4314 CA PRO B 334 18. 538 82. 854 5. 809 1. 00 31. 05 4315 CB PRO B 334 19. 946 82. 201 5. 727 1. 00 31. 28 4316 CG PRO B 334 20. 794 83. 014 6. 662 1. 00 31. 16 4317 CD PRO B 334 19. 808 83. 311 7. 818 1. 00 31. 13 4318 C PRO B 334 17. 525 81. 750 6. 162 1. 00 30. 86 4319 0 PRO B 334 17.599 81.198 7.280 1.00 31. 29 4320 N ASN B 335 16. 628 81. 563 5. 271 1. 00 30. 36 4321 CA ASN B 335 15. 639 80. 467 5. 370 1. 00 30. 40 4322 CB ASN B 335 16. 500 79. 281 5. 875 1. 00 30. 06 4323 CG ASN B 335 16. 106 78. 029 5. 080 1. 00 30. 47 4324 OD1 ASN B 335 16. 121 76. 893 5. 553 1. 00 31. 25 4325 ND2 ASN B 335 15. 894 78. 337 3. 784 1. 00 28. 95 4326 C ASN B 335 14. 402 80. 835 6. 143 1. 00 30. 19 4327 O ASN B 335 13. 631 79. 944 6. 612 1. 00 30. 63 4328 N ILE B 336 14. 113 82. 127 6. 275 1. 00 29. 63 4329 CA ILE B 336 12. 912 82. 609 6. 969 1. 00 28. 82 4330 CB ILE B 336 13. 179 82. 973 8. 472 1. 00 27. 65 4331 CG1 ILE B 336 13.751 81.807 9.250 1.00 25. 58 4332 CD1 ILE B 336 14.188 82.104 10.691 1.00 24. 29 4333 CG2 ILE B 336 11. 849 83. 514 9. 133 1. 00 27. 98 4334 C ILE B 336 12. 356 83. 820 6. 216 1. 00 28. 93 4335 O ILE B 336 13.027 84.888 6.178 1.00 29. 01 4336 N GLU B 337 11. 162 83. 634 5. 611 1. 00 28. 39 4337 CA GLU B 337 10. 593 84. 790 4. 913 1. 00 27. 98 4338 CB GLU B 337 9. 912 84. 741 3. 600 1. 00 30. 24 4339 CG GLU B 337 8.657 84.023 3.205 1.00 32. 43 4340 CD GLU B 337 7. 906 84. 361 1. 974 1. 00 34. 42 4341 OE1 GLU B 337 8. 278 84. 398 0. 811 1. 00 36. 28 4342 OE2 GLU B 337 6. 682 84. 670 2. 142 1. 00 35. 07 4343 C GLU B 337 9. 604 85. 378 5. 957 1. 00 26. 96 4344 O GLU B 337 8. 850 84. 606 6. 551 1. 00 26. 56 4345 N GLU B 338 9. 726 86. 634 6. 200 1. 00 26. 62 4346 CA GLU B 338 8. 920 87. 438 7. 113 1. 00 26. 30 4347 CB GLU B 338 9.790 88.427 7.876 1.00 25. 34 4348 CG GLU B 338 10. 893 87. 713 8. 710 1. 00 23. 74 4349 CD GLU B 338 11. 713 88. 647 9. 532 1. 00 23. 30 4350 OE1 GLU B 338 11.170 89.604 10.035 1.00 21. 98 4351 OE2 GLU B 338 12.906 88.324 9.670 1.00 22. 61 4352 C GLU B 338 7. 839 88. 181 6. 353 1. 00 26. 59 4353 O GLU B 338 8. 111 89. 033 5. 464 1. 00 26. 64 4354 N VAL B 339 6. 604 87. 908 6. 809 1. 00 25. 96 4355 CA VAL B 339 5.368 88.440 6.199 1.00 24. 96 4356 CB VAL B 339 4. 671 87. 193 5. 568 1. 00 24. 53 4357 CG1 VAL B 339 3. 337 87. 497 4. 913 1. 00 25. 92 4358 CG2 VAL B 339 5.562 86.451 4.625 1.00 25. 45 4359 C VAL B 339 4. 445 89. 063 7. 272 1. 00 24. 50 43600 VAL B 339 3. 977 88. 370 8. 188 1. 00 24. 07 4361 N ALA B 340 4.167 90.349 7.093 1.00 23. 97 4362 CA ALA B 340 3. 296 91. 048 8. 072 1. 00 23. 90 4363 CB ALA B 340 3.301 92.521 7.717 1.00 23. 46 4364 C ALA B 340 1.904 90.483 7.978 1.00 23. 92 43650 ALAB 3401. 53890. 1616. 8041. 0024. 21 4366 N LEU B 341 1.185 90.367 9.077 1.00 23. 60 4367 CA LEU B 341-0.244 89. 884 8. 980 1. 00 22.73 4368 CB LEU B 341-0.730 89. 309 10. 268 1. 00 21.92 4369 CG LEU B 341-0. 265 88.028 10.954 1.00 21. 29 4370 CD1 LEU B 341-1.040 87. 884 12. 250 1. 00 19.21 4371 CD2 LEU B 341-0.672 86. 856 10. 021 1.00 20.83 4372 C LEU B 341-1.035 91. 169 8. 594 1.00 22.82 4373 0 LEU B 341-0.534 92. 255 8. 897 1.00 22.67 4374 N SER B 342-2.188 90. 970 7. 951 1.00 22.67 4375 CA SER B 342-3.017 92. 144 7. 594 1.00 22.87 4376 CB SER B 342-3.444 92. 390 6. 194 1.00 24.16 4377 OG SER B 342-4.571 91. 618 5. 804 1.00 26.24 4378 C SER B 342-4.316 91. 932 8. 429 1.00 22.49 4379 0 SER B 342-4.317 91. 002 9. 239 1.00 21.92 4380 N THR B 343-5.313 92. 742 8. 112 1.00 22.98 4381 CA THR B 343-6.593 92. 630 8. 827 1.00 23.88 4382 CB THR B 343-7.290 94. 003 9. 029 1.00 24.77 4383 OG1 THR B 343-7.474 94. 381 7. 595 1.00 27.11 4384 CG2 THR B 343-6.418 95. 087 9. 687 1.00 24.63 4385 C THR B 343-7.535 91. 654 8. 095 1.00 23.75 43860THR B 343-8.691 91. 467 8. 527 1.00 23.67 4387 N THR B 344-7.016 91. 039 7. 078 1.00 23.53 4388 CA THR B 344-7.736 90. 042 6. 260 1.00 23.39 4389 CB THR B 344-7.419 90. 237 4. 745 1.00 24.64 4390 OG1 THR B 344-7.943 91. 590 4. 443 1.00 26.14 4391 CG2 THR B 344-7.977 89. 236 3. 741 1.00 24.65 4392 C THR B 344-7.412 88. 663 6. 800 1.00 23.21 4393 O THR B 344-6.237 88. 260 6. 934 1.00 23.14 4394 N GLY B 345-8.457 87. 929 7. 177 1.00 22.87 4395 CA GLY B 345-8.262 86. 584 7. 729 1.00 21.98 4396 C GLY B 345-9.498 86. 167 8. 488 1.00 21.85 4397 0 GLY B 345-10.305 87. 025 8. 907 1.00 22.65 4398 N GLU B 346--9. 643 84. 856 8. 569 1. 00 20.90 4399 CA GLU B 346-10.736 84. 187 9. 227 1.00 20.06 4400GLU B 346-10.860 82. 692 8. 882 1.00 21.68 4401 CG GLU B 346-11.190 82. 329 7. 458 1.00 23.99 4402 CD GLU B 346-10.297 82. 606 6. 326 1.00 25.58 4403 OE1 GLU B 346-9.099 82. 924 6. 341 1.00 25.66 4404 OE2 GLU B 346-10.883 82. 452 5. 219 1.00 26.42 4405 C GLU B 346-10.553 84. 164 10. 721 1.00 18.23 44060GLU B 346-11.532 83. 861 11. 366 1.00 18.62 4407 N ILE B 347-9.282 84. 312 11. 142 1.00 16.92 4408 CA ILE B 347-8.940 84. 204 12. 566 1.00 14.53 4409 CB ILE B 347-7.835 83. 065 12. 629 1.00 14.80 4410 CG1 ILE B 347-8.445 81. 761 12. 086 1.00 14.31 4411 CD1 ILE B 347-7.361 80. 802 11. 489 1.00 13.93 4412 CG2 ILE B 347-7.163 82. 936 14. 008 1.00 14.46 4413 C ILE B 347-8.338 85. 502 13. 093 1.00 13.65 4414 0 ILE B 347-7.191 85. 786 12. 792 1.00 12.93 4415 N PRO B 348-9.118 86. 204 13. 878 1.00 12.50 4416 CA PRO B 348-8.692 87. 457 14. 526 1.00 11.72 4417 CB PRO B 348-9.958 87. 698 15. 449 1.00 10.53 4418 CG PRO B 348-10.982 87. 428 14. 331 1.00 10.76 4419 CD PRO B 348-10.573 85. 879 14. 228 1.00 11.49 4420 C PRO B 348-7.477 87. 174 15. 367 1.00 11.64 4421 0 PRO B 348-7.479 86. 227 16. 127 1.00 10.40 4422 N PHE B 349-6.456 88. 080 15. 332 1.00 10.98 4423 CA PHE B 349-5.246 87. 777 16. 110 1.00 10.38 4424 CB PHE B 349-4.232 86. 979 15. 200 1.00 9.74 4425 CG PHE B 349-3.050 86. 471 15. 985 1.00 9.69 4426 CD1 PHE B 349-3.285 85. 544 17. 014 1.00 10.20 4427 CE1 PHE B 349-2.195 85. 046 17. 752 1.00 11.36 4428 CZ PHE B 349-0.908 85. 463 17. 424 1.00 10.56 4429 CE2 PHE B 349-0.648 86. 319 16. 389 1.00 9.76 4430 CD2 PHE B 349-1.755 86. 824 15. 643 1.00 11.28 4431 C PHE B 349-4.589 89. 105 16. 500 1.00 11.55 4432 0 PHE B 349-4.080 89. 702 15. 584 1.00 11.69 4433 N TYR B 350-4.732 89. 507 17. 715 1.00 13.12 4434 CA TYR B 350-4.052 90. 731 18. 179 1.00 14.36 4435 CB TYR B 350-2.542 90. 349 18. 389 1.00 10.99 4436 CG TYR B 350-2.363 89. 432 19. 561 1.00 10.16 4437 CD1 TYR B 350-2.069 89. 917 20. 831 1.00 9.53 4438 CE1 TYR B 350-1.858 89. 078 21. 931 1.00 9.74 4439 CZ TYR B 350-2.096 87. 684 21. 722 1.00 11.02 4440 OH TYR B 350-1.990 86. 842 22. 794 1.00 13.63 4441 CE2 TYR B 350-2.334 87. 186 20. 499 1.00 9.87 4442 CD2 TYR B 350-2.449 88. 028 19. 386 1.00 9.92 4443 C TYR B 350-4.156 91. 927 17. 291 1.00 15.31 4444 0 TYR B 350-3.137 92. 647 17. 153 1.00 17.30 4445 N GLY B 351-5.267 92. 272 16. 744 1.00 15.64 4446 CA GLY B 351-5.586 93. 400 15. 918 1.00 15.60 4447 C GLY B 351-5.411 93. 167 14. 457 1.00 15.46 4448 O GLY B 351-5.637 94. 102 13. 634 1.00 15.06 4449 N LYS B 352-4.867 92. 002 14. 138 1.00 15.19 4450 CA LYS B 352-4.633 91. 535 12. 764 1.00 15.08 4451 CB LYS B 352-3.179 91. 266 12. 454 1.00 16.02 4452 CG LYS B 352-2.239 92. 477 12. 478 1.00 18.10 4453 CD LYS B 352-2.662 93. 431 11. 359 1.00 19.76 4454 CE LYS B 352-1.722 94. 576 11. 086 1.00 19.19 4455 NZ LYS B 352-1.710 95. 453 12. 276 1.00 20.59 4456 C LYS B 352-5.491 90. 245 12. 630 1.00 15.01 4457 O LYS B 352-6.385 90. 085 13. 494 1.00 15.71 4458 N ALA B 353-5.318 89. 485 11. 622 1.00 14.75 4459 CA ALA B 353-6.039 88. 198 11. 449 1.00 15.41 4460 CB ALA B 353-7.304 88. 454 10. 634 1.00 14.30 4461 C ALA B 353-5.081 87. 248 10. 730 1.00 15.98 4462 0 ALA B 353-4.117 87. 687 10. 074 1.00 16.18 4463 N ILE B 354-5.378 85. 965 10. 821 1.00 16.67 4464 CA ILE B 354-4.585 84. 976 10. 061 1.00 17.28 4465 CB ILE B 354-4.141 83. 808 11. 111 1.00 16.73 4466 CG1 ILE B 354-3.420 84. 444 12. 286 1.00 16.18 4467 CD1 ILE B 354-3.219 83. 694 13. 587 1.00 15.89 4468 CG2 ILE B 354-3.298 82. 791 10. 325 1.00 18.32 4469 C ILE B 354-5.572 84. 299 9. 095 1.00 17.60 44700ILE B 354-6.624 83. 878 9. 565 1.00 17.15 4471 N PRO B 355-5.191 84. 187 7. 863 1.00 18.58 4472 CA PRO B 355-6.036 83. 439 6. 878 1.00 19.64 4473 CB PRO B 355-5.407 83. 790 5. 536 1.00 19.63 4474 CG PRO B 355-4.689 85. 105 5. 818 1.00 19.55 4475 CD PRO B 355-4.035 84. 810 7. 215 1.00 19.26 4476 C PRO B 355-5.908 81. 966 7. 212 1.00 20.76 4477 O PRO B 355-4. 760 81. 421 7. 449 1. 00 22.16 4478 N LEU B 356-6.946 81. 199 7. 224 1.00 21.33 4479 CA LEU B 356-6.955 79. 778 7. 507 1.00 21.27 4480LEU B 356-8.414 79. 325 7. 267 1.00 21.67 4481 CG LEU B 356-8.736 77. 902 7. 637 1.00 21.36 4482 CD1 LEU B 356-8.715 77. 790 9. 114 1.00 20.61 4483 CD2 LEU B 356-10.096 77. 491 7. 038 1.00 22.90 4484 C LEU B 356-5.986 78. 993 6. 581 1.00 21.95 4485 0 LEU B 356-5.451 77. 950 6. 973 1.00 21.62 4486 N GLU B 357-5.850 79. 431 5. 359 1.00 22.96 4487 CA GLU B 357-5.038 78. 771 4. 329 1.00 24.25 4488 CB GLU B 357-5.188 79. 424 2. 960 1.00 27.89 4489 CG GLU B 357-4.881 80. 902 2. 855 1.00 33.05 4490 CD GLU B 357-4.836 81. 668 1. 593 1.00 35.95 4491 OE1 GLU B 357-3.973 82. 478 1. 235 1.00 36.89 4492 OE2 GLU B 357-5.815 81. 485 0. 834 1.00 38.86 4493 C GLU B 357-3.601 78. 568 4. 744 1.00 23.96 4494 O GLU B 357-2.911 77. 549 4. 413 1.00 23.72 4495 N VAL B 358-3.110 79. 475 5. 570 1.00 23.40 4496 CA VAL B 358-1.727 79. 459 6. 062 1.00 22.72 4497 CB VAL B 358-1.324 80. 930 6. 319 1.00 22.11 4498 CG1 VAL B 358-1.827 81. 769 5. 133 1.00 21.95 4499 CG2 VAL B 358-1.738 81. 500 7. 630 1.00 21.45 4500 C VAL B 358-1.420 78. 486 7. 170 1.00 21.78 4501 O VAL B 358-0.211 78. 243 7. 410 1.00 21.16 4502 N ILE B 359-2.367 77. 915 7. 858 1.00 21.53 4503 CA ILE B 359-2.153 76. 981 8. 922 1.00 21.46 4504 CB ILE B 359-2.397 77. 592 10. 338 1.00 20.28 4505 CG1 ILE B 359-3.849 78. 150 10. 457 1.00 18.54 4506 CD1 ILE B 359-4.106 78. 728 11. 879 1.00 20.92 4507 CG2 ILE B 359-1.319 78. 611 10. 758 1.00 17.63 4508 C ILE B 359-2.868 75. 653 8. 743 1.00 23.01 4509 0 ILE B 359-2.772 74. 761 9. 628 1.00 22.56 4510 N LYS B 360-3.609 75. 581 7. 640 1.00 24.78 4511 CA LYS B 360-4.374 74. 316 7. 348 1.00 26.20 4512LYS B 360-5.491 74. 628 6. 334 1.00 28.97 4513 CG LYS B 360-6.434 73. 455 6. 191 1.00 31.91 4514 CD LYS B 360-7. 625 73.689 5.278 1. 00 34.16 4515 CE LYS B 360-8.385 72. 374 5. 054 1.00 35.44 4516LYS B 360-9.566 72. 604 4. 163 1.00 37.30 4517 C LYS B 360-3.355 73. 388 6. 637 1.00 26.28 4518 O LYS B 360-2.994 73. 733 5. 519 1.00 26.12 4519 N GLY B 361-2.950 72. 340 7. 336 1.00 26.16 4520 CA GLY B 361-1.913 71. 444 6. 669 1.00 26.60 4521 C GLY B 361-0.555 72. 144 6. 992 1.00 26.72 4522 O GLY B 361-0.374 73. 307 6. 695 1.00 26.55 4523 N GLY B 362 0. 286 71. 378 7. 647 1. 00 26.70 4524 CA GLY B 362 1.617 71.787 8.089 1. 00 25.38 4525 C GLY B 362 1. 599 71. 656 9. 614 1. 00 24.93 4526 O GLY B 362 0. 543 71. 284 10. 194 1. 00 25.52 4527 N ARG B 363 2.713 72.018 10.195 1. 00 23.44 4528 CA ARG B 363 2. 964 72. 043 11. 654 1. 00 21.95 4529ARG B 363 4. 098 71. 100 11. 987 1. 00 23.20 4530ARG B 363 3. 792 69. 603 11. 627 1. 00 22.27 4531 CD ARG B 363 4. 970 68. 793 11. 960 1. 00 23.32 4532 NE ARG B 363 5.418 68.927 13.338 1. 00 24.39 4533 CZ ARG B 363 4. 777 68. 462 14. 388 1. 00 24.60 4534 NH1 ARG B 363 3. 642 67. 784 14. 204 1. 00 26.18 4535 NH2 ARG B 363 5. 249 68. 647 15. 597 1. 00 24.21 4536 C ARG B 363 3. 368 73. 534 11. 862 1. 00 20.45 4537 O ARG B 363 4. 196 74. 013 11. 128 1. 00 20.10 4538 N HIS B 364 2. 565 74. 215 12. 658 1. 00 19.55 4539 CA HIS B 364 2. 741 75. 672 12. 866 1. 00 17.35 4540HIS B 364 1. 622 76. 437 12. 092 1. 00 17.28 4541 CG HIS B 364 1. 662 76. 072 10. 645 1. 00 17.40 4542 ND1 HIS B 364 2. 392 76. 725 9. 696 1. 00 17.60 4543 CE1 HIS B 364 2. 181 76. 214 8. 500 1. 00 17.31 4544 NE2 HIS B 364 1. 290 75. 231 8. 663 1. 00 18.94 4545 CD2 HIS B 364 0. 938 75. 182 9. 972 1. 00 18.09 4546 C HIS B 364 2. 669 76. 039 14. 303 1. 00 16.25 4547 0 HIS B 364 2. 089 75. 316 15. 117 1. 00 15.78 4548 N LEU B 365 3. 359 77. 157 14. 626 1. 00 15.25 4549 CA LEU B 365 3. 437 77. 652 16. 005 1. 00 15.27 4550LEU B 365 4. 867 77. 515 16. 566 1. 00 15.44 4551 CG LEU B 365 5. 233 78. 086 17. 920 1. 00 12.88 4552 CD1 LEU B 365 4. 443 77. 407 19. 025 1. 00 11.44 4553 CD2 LEU B 365 6. 744 77. 729 18. 147 1. 00 12.81 4554 C LEU B 365 3. 029 79. 162 15. 972 1. 00 14.67 4555 O LEU B 365 3. 479 79. 878 15. 120 1. 00 13.86 4556 N ILE B 366 2. 165 79. 413 16. 932 1. 00 14.92 4557 CA ILE B 366 1. 552 80. 713 17. 169 1. 00 14.24 4558 CB ILE B 366-0.011 80. 616 16. 979 1.00 13.77 4559 CG1 ILE B 366-0.338 80. 076 15. 541 1.00 14.07 4560 CD1 ILE B 366-1.881 79. 935 15. 265 1.00 12.04 4561 CG2 ILE B 366-0.660 81. 975 17. 281 1.00 12.25 4562 C ILE B 366 1. 885 81. 165 18. 582 1. 00 13.90 4563 O ILE B 366 1. 491 80. 479 19. 477 1. 00 13.91 4564 N PHE B 367 2. 601 82. 267 18. 720 1. 00 14.95 4565 CA PHE B 367 2. 901 82. 671 20. 134 1. 00 15.31 4566 CB PHE B 367 4. 283 83. 028 20. 419 1. 00 14.91 4567 CG PHE B 367 5. 406 82. 020 20. 322 1. 00 15.16 4568 CD1 PHE B 367 6. 183 81. 922 19. 156 1. 00 14.17 4569 CE1 PHE B 367 7. 285 81. 047 19. 121 1. 00 13.55 4570 CZ PHE B 367 7. 634 80. 330 20. 241 1. 00 11.66 4571 CE2 PHE B 367 6. 921 80. 489 21. 440 1. 00 11.23 4572 CD2 PHE B 367 5. 777 81. 306 21. 437 1. 00 13.93 4573 C PHE B 367 1. 744 83. 524 20. 623 1. 00 15.68 4574 0 PHE B 367 1. 327 84. 391 19. 863 1. 00 16.53 4575 N CYS B 368 1. 197 83. 260 21. 761 1. 00 16.46 4576 CA CYS B 368 0. 130 83. 969 22. 439 1. 00 17.62 4577 CB CYS B 368-1.186 83. 314 22. 559 1.00 17.42 4578 SG CYS B 368-2.101 82. 821 21. 112 1.00 19.07 4579 C CYS B 368 0. 729 84. 520 23. 732 1. 00 18.26 4580 O CYS B 368 1. 794 83. 930 24. 131 1. 00 19.67 4581 N HIS B 369 0. 243 85. 558 24. 370 1. 00 18.07 4582 CA HIS B 369 0. 861 86. 092 25. 579 1. 00 18.25 4583 CB HIS B 369 0. 908 87. 638 25. 677 1. 00 17.90 4584 CG HIS B 369-0.466 88. 194 26. 019 1.00 16.91 4585 ND1 HIS B 369-1.509 88. 139 25. 224 1.00 17.71 4586 CE1 HIS B 369-2.605 88. 583 25. 931 1.00 18.24 4587 NE2 HIS B 369-2.215 88. 963 27. 131 1.00 18.62 4588 CD2 HIS B 369-0.852 88. 729 27. 218 1.00 17.63 4589 C HIS B 369 0. 341 85. 508 26. 871 1. 00 19.37 45900HIS B 369 1. 078 85. 670 27. 899 1. 00 20.45 4591 N SER B 370-0.756 84. 772 26. 915 1.00 19.11 4592 CA SER B 370-1.282 84. 181 28. 174 1.00 18.53 4593 CB SER B 370-2.320 85. 102 28. 778 1.00 18.54 4594 OG SER B 370-3.329 85. 348 27. 852 1.00 16.17 4595 C SER B 370-1. 922 82.846 27.904 1. 00 19.03 4596 0 SER B 370-2.183 82. 566 26. 733 1.00 19.92 4597 N LYS B 371-2.191 82. 057 28. 933 1.00 19.52 4598 CA LYS B 371-2.773 80. 723 28. 756 1.00 20.48 4599 CB LYS B 371-3. 186 80. 033 30. 016 1. 00 22.49 4600 CG LYS B 371-2.447 80. 030 31. 316 1.00 24.97 4601 CD LYS B 371-3.070 78. 929 32. 206 1.00 26.85 4602 CE LYS B 371-4.590 78. 907 32. 223 1.00 27.94 4603LYS B 371-5.086 77. 759 33. 065 1.00 27.86 4604 C LYS B 371-4.180 80. 939 28. 093 1.00 20.59 46050LYS B 371-4.588 80. 134 27. 311 1.00 21.52 4606 N LYS B 372-4.847 81. 904 28. 645 1.00 20.90 4607 CA LYS B 372-6.237 82. 275 28. 258 1.00 21.22 4608LYS B 372-6.820 83. 142 29. 261 1.00 24.96 4609 CG LYS B 372-8.229 83. 672 29. 328 1.00 28.67 4610 CD LYS B 372-8.423 83. 925 30. 863 1.00 31.93 4611 CE LYS B 372-7.276 84. 762 31. 402 1.00 34.56 4612LYS B 372-7.225 84. 653 32. 900 1.00 36.95 4613 C LYS B 372-6.346 82. 581 26. 827 1.00 20.64 4614 0 LYS B 372-7.372 82. 199 26. 202 1.00 20.97 4615 N LYS B 373-5.405 83. 331 26. 261 1.00 19.86 4616 CA LYS B 373-5.409 83. 620 24. 832 1.00 19.52 4617 CB LYS B 373-4.453 84. 693 24. 413 1.00 19.86 4618 CG LYS B 373-4.818 86. 008 25. 211 1.00 21.86 4619 CD LYS B 373-6.243 86. 354 24. 877 1.00 23.55 4620 CE LYS B 373-6.838 87. 557 25. 533 1.00 25.05 4621LYS B 373-8.124 87. 881 24. 809 1.00 24.01 4622 C LYS B 373-5.161 82. 311 24. 073 1.00 19.34 4623 0 LYS B 373-5.767 82. 127 23. 031 1.00 19.08 4624 N CYS B 374-4.340 81. 422 24. 630 1.00 19.00 4625 CA CYS B 374-3.997 80. 148 24. 044 1.00 18.72 4626 CB CYS B 374-2.886 79. 412 24. 794 1.00 18.31 4627 SG CYS B 374-1.298 80. 249 24. 753 1.00 17.68 4628 C CYS B 374-5.190 79. 200 23. 925 1.00 18.35 46290CYS B 374-5.410 78. 588 22. 897 1.00 18.01 4630 N ASP B 375-5.878 79. 079 25. 033 1.00 19.07 4631 CA ASP B 375-7.076 78. 254 25. 153 1.00 18.81 4632ASP B 375-7.542 78. 096 26. 569 1.00 19.89 4633 CG ASP B 375-6.705 77. 395 27. 581 1.00 21.54 4634 OD1 ASP B 375-6.883 77. 620 28. 825 1.00 22.41 4635 OD2 ASP B 375-5. 808 76.589 27.211 1. 00 21.98 4636 C ASP B 375-8.113 78. 805 24. 167 1.00 18.90 46370ASP B 375-8.730 78. 037 23. 445 1.00 18. 63 4638 N GLU B 376-8.323 80. 118 24. 161 1.00 19.29 4639 CA GLU B 376-9.297 80. 747 23. 265 1.00 19.72 4640GLU B 376-9.448 82. 223 23. 514 1.00 22.76 4641 CG GLU B 376-9.896 82. 730 24. 864 1.00 26.51 4642 CD GLU B 376-10.262 84. 209 24. 877 1.00 28.42 4643 OE1 GLU B 376-9.948 84. 936 23. 934 1.00 28.94 4644 OE2 GLU B 376-10.973 84. 497 25. 871 1.00 28.71 4645 C GLU B 376-9.058 80. 470 21. 798 1.00 19.55 46460GLU B 376-10.010 80. 082 21. 057 1.00 19.82 4647 N LEU B 377-7.850 80. 656 21. 297 1.00 18.70 4648 CA LEU B 377-7.447 80. 441 19. 914 1.00 18.14 4649 CB LEU B 377-6.136 81. 199 19. 639 1. 00 17.64 4650LEU B 377-5.661 81. 175 18. 209 1.00 15.08 4651 CD1 LEU B 377-6.588 81. 852 17. 224 1.00 15.02 4652 CD2 LEU B 377-4.252 81. 638 18. 102 1.00 16.92 4653 C LEU B 377-7.471 78. 977 19. 540 1.00 18.48 4654 O LEU B 377-7. 972 78.634 18.429 1. 00 19. 18 4655 N ALA B 378-7.009 78. 099 20. 425 1.00 18.07 4656 CA ALA B 378-7.049 76. 647 20. 140 1. 00 17.91 4657 CB ALA B 378-6.426 75. 825 21. 251 1. 00 16.71 4658 C ALA B 378-8.460 76. 215 19. 850 1. 00 17.72 4659 O ALA B 378-8.655 75. 495 18. 848 1. 00 18.68 4660 N ALA B 379-9.404 76. 610 20. 690 1. 00 17.84 4661 CA ALA B 379-10.814 76. 256 20. 491 1. 00 18.38 4662 CB ALA B 379-11.729 76. 580 21. 664 1. 00 18.46 4663 C ALA B 379-11.315 76. 903 19. 208 1. 00 18.93 4664 O ALA B 379-12.022 76. 256 18. 422 1. 00 20.19 4665 N LYS B 380-10. 901 78.109 18.918 1.00 19. 12 4666 CA LYS B 380-11.308 78. 841 17. 729 1. 00 18.77 4667 CB LYS B 380-10.546 80. 157 17. 502 1. 00 19.83 4668 CG LYS B 380-11.355 81. 246 16. 785 1. 00 19.60 4669 CD LYS B 380-11.915 80. 966 15. 469 1. 00 22.04 4670 CE LYS B 380-12.978 81. 940 14. 949 1. 00 21.99 4671 NZ LYS B 380-13.646 81. 327 13. 726 1. 00 21.95 4672 C LYS B 380-10.881 77. 974 16. 552 1. 00 18.79 4673 O LYS B 380-11.611 77. 748 15. 596 1. 00 19.32 4674 N LEU B 381-9.589 77. 606 16. 605 1. 00 18.67 4675 CA LEU B 381-8.983 76. 820 15. 512 1. 00 18.54 4676 CB LEU B 381-7.464 76. 856 15. 604 1. 00 17.27 4677 CG LEU B 381-6.756 78. 223 15. 481 1. 00 16.44 4678 CD1 LEU B 381-5.261 78. 106 15. 704 1. 00 15.73 4679 CD2 LEU B 381-7.014 78. 637 14. 023 1. 00 15.11 4680 C LEU B 381-9. 593 75.418 15.466 1.00 19. 46 4681 O LEU B 381-9.731 74. 961 14. 319 1. 00 20.92 4682 N VAL B 382-9.926 74. 823 16. 582 1. 00 19.73 4683 CA VAL B 382-10.538 73. 478 16. 592 1. 00 20.39 4684 CB VAL B 382-10.505 72. 706 17. 900 1. 00 19.75 4685 CG1 VAL B 382-11.231 71. 344 17. 853 1. 00 18.69 4686 CG2 VAL B 382-9.026 72. 346 18. 272 1. 00 21.61 4687 C VAL B 382-11.873 73. 484 15. 877 1. 00 21.15 4688 0 VAL B 382-12. 208 72.434 15.252 1.00 21. 64 4689 N ALA B 383-12.650 74. 560 15. 958 1. 00 21.46 4690 CA ALA B 383-13.926 74. 668 15. 270 1. 00 21.45 4691 CB ALA B 383-14.873 75. 661 15. 952 1. 00 19.44 4692 C ALA B 383-13.810 74. 846 13. 792 1. 00 22.12 4693 O ALA B 383-14.791 74. 573 12. 997 1. 00 23.21 4694 N LEU B 384-12.704 75. 346 13. 319 1. 00 22.03 4695 CA LEU B 384-12.306 75. 567 11. 965 1. 00 21.94 4696 CB LEU B 384-11.439 76. 808 11. 836 1. 00 22.00 4697 CG LEU B 384-11.976 78. 183 11. 967 1. 00 22.01 4698 CD1 LEU B 384-10. 837 79.258 11.993 1.00 21. 79 4699 CD2 LEU B 384-12.774 78. 530 10. 676 1. 00 21.57 4700 C LEU B 384-11.719 74. 289 11. 332 1. 00 21.93 4701 O LEU B 384-11.236 74. 305 10. 189 1. 00 21.60 4702 N GLY B 385-11.799 73. 177 12. 052 1. 00 22.25 4703 CA GLY B 385-11. 316 71. 885 11. 672 1. 00 23. 09 4704 C GLY B 385-9.804 71. 699 11. 637 1. 00 23.53 47050 GLY B 385-9.281 70. 878 10. 860 1. 00 24.02 4706 N ILE B 386-9. 092 72.361 12.503 1.00 23. 82 4707 CA ILE B 386-7.668 72. 361 12. 649 1. 00 24.14 4708 CB ILE B 386 -7.139 73.837 12.624 1.00 25. 25 4709 CG1 ILE B 386-7. 380 74.396 11.213 1.00 26. 64 4710 CD1 ILE B 386-6.960 75. 858 11. 038 1. 00 28.05 4711 CG2 ILE B 386-5.669 74. 032 13. 093 1. 00 25.11 4712 C ILE B 386-7. 214 71.591 13.858 1.00 23. 97 47130 ILE B 386-7.901 71. 617 14. 874 1. 00 23.85 4714 N ASN B 387-6.061 70. 919 13. 703 1. 00 24.34 4715 CA ASN B 387-5.523 70. 147 14. 836 1. 00 24.46 4716 CB ASN B 387-4.839 68. 836 14. 486 1. 00 25.75 4717 CG ASN B 387-4.424 68. 065 15. 727 1. 00 25.32 4718 OD1 ASN B 387-4.985 68. 274 16. 820 1. 00 26.47 4719 ND2 ASN B 387-3.410 67. 208 15. 628 1. 00 25.90 4720 C ASN B 387-4.615 71. 133 15. 601 1. 00 24.64 4721 O ASN B 387-3.394 71. 184 15. 367 1. 00 24.04 4722 N ALA B 388-5.271 71. 801 16. 517 1. 00 24.20 4723 CA ALA B 388-4.700 72. 819 17. 389 1. 00 23.86 4724 CB ALA B 388-5.576 74. 079 17. 207 1. 00 23.44 4725 C ALA B 388-4.698 72. 387 18. 839 1. 00 23.83 47260 ALA B 388-5.730 71. 911 19. 383 1. 00 25. 28 4727 N VAL B 389-3.546 72. 532 19. 457 1. 00 23.31 4728 CA VAL B 389-3.323 72. 194 20. 884 1. 00 22.78 4729 CB VAL B 389-2.582 70. 845 20. 927 1. 00 22.90 4730 CG1 VAL B 389-1.260 70. 868 20. 156 1. 00 21.72 4731 CG2 VAL B 389-2. 348 70.405 22.361 1.00 24. 18 4732 C VAL B 389-2.609 73. 328 21. 565 1. 00 22.46 4733 O VAL B 389-1.717 73. 870 20. 888 1. 00 21.86 4734 N ALA B 390-2.969 73. 670 22. 795 1. 00 22.57 4735 CA ALA B 390-2.318 74. 767 23. 542 1. 00 22.40 4736 CB ALA B 390-3.331 75. 605 24. 350 1. 00 21.38 4737 C ALA B 390-1.306 74. 237 24. 564 1. 00 22.69 4738 O ALA B 390-1.612 73. 285 25. 310 1. 00 22.52 4739 N TYR B 391-0.166 74. 891 24. 622 1. 00 22.71 4740 CA TYR B 391 0. 926 74. 587 25. 533 1. 00 22. 86 4741 CB TYR B 391 2. 115 73. 888 24. 784 1. 00 24. 16 4742 CG TYR B 391 3. 217 73. 605 25. 824 1. 00 25. 69 4743 CD1 TYR B 391 3. 154 72. 499 26. 673 1. 00 26. 36 4744 CE1 TYR B 391 4. 093 72. 299 27. 681 1. 00 27. 11 4745 CZ TYR B 391 5. 139 73. 230 27. 801 1. 00 27. 52 4746 OH TYR B 391 6. 123 73. 086 28. 740 1. 00 29. 91 4747 CE2 TYR B 391 5. 227 74. 297 26. 939 1. 00 26. 35 4748 CD2 TYR B 391 4.281 74.483 25.953 1.00 26. 22 4749 C TYR B 391 1. 383 75. 823 26. 302 1. 00 23. 24 4750 0 TYR B 391 1. 643 76. 884 25. 696 1. 00 23. 51 4751 N TYR B 392 1. 493 75. 774 27. 576 1. 00 23. 23 4752 CA TYR B 392 1. 879 76. 778 28. 527 1. 00 25. 17 4753 CB TYR B 392 0. 766 77. 778 28. 792 1. 00 24. 70 4754 CG TYR B 392-0.618 77. 196 28. 960 1. 00 24.52 4755 CD1 TYR B 392-1.093 76. 553 30. 113 1. 00 25.41 4756 CE1 TYR B 392-2.412 76. 112 30. 179 1. 00 25.20 4757 CZ TYR B 392-3.273 76. 334 29. 124 1. 00 25.61 4758 OH TYR B 392-4.624 76. 006 29. 138 1. 00 25.53 4759 CE2 TYR B 392-2.823 76. 999 28. 005 1. 00 24.11 4760 CD2 TYR B 392-1.520 77. 411 27. 931 1. 00 23.32 4761 C TYR B 392 2. 371 76. 116 29. 818 1. 00 26. 58 4762 0 TYR B 392 2. 216 74. 895 29. 926 1. 00 27. 22 4763 N ARG B 393 2. 894 76. 879 30. 738 1. 00 27. 35 4764 CA ARG B 393 3. 444 76. 243 31. 975 1. 00 28. 56 4765 CB ARG B 393 4. 098 77. 292 32. 826 1. 00 31. 49 4766 CG ARG B 393 5. 072 76. 860 33. 938 1. 00 35. 42 4767 CD ARG B 393 5. 542 78. 160 34. 606 1. 00 37. 86 4768 NE ARG B 393 4. 589 78. 596 35. 639 1. 00 39. 60 4769 CZ ARG B 393 4.699 77.989 36.861 1.00 41. 64 4770 NH1 ARG B 393 5. 659 77. 089 37. 129 1. 00 41. 41 4771 NH2 ARG B 393 3. 802 78. 286 37. 816 1. 00 42. 14 4772 C ARG B 393 2. 293 75. 612 32. 730 1. 00 29. 06 4773 0 ARG B 393 1. 215 76. 204 32. 793 1. 00 28. 17 4774 N GLY B 394 2. 570 74. 465 33. 319 1. 00 30. 33 4775 CA GLY B 394 1. 568 73. 728 34. 099 1. 00 31. 60 4776 C GLY B 394 1. 027 72. 543 33. 314 1. 00 32. 68 4777 O GLY B 394 0. 379 71. 666 33. 913 1. 00 32. 26 4778 N LEU B 395 1. 330 72. 515 32. 025 1. 00 34. 20 4779 CA LEU B 395 0. 899 71. 455 31. 115 1. 00 35. 64 4780LEU B 395 0. 334 71. 993 29. 808 1. 00 36. 20 4781 CG LEU B 395-0.773 72. 942 29. 667 1. 00 36.39 4782 CD1 LEU B 395-1.202 73. 057 28. 204 1. 00 35.84 4783 CD2 LEU B 395-1.957 72. 652 30. 572 1. 00 36.80 4784 C LEU B 395 2.020 70.461 30.772 1.00 36. 45 4785 0 LEU B 395 3. 228 70. 809 30. 783 1. 00 36. 63 4786 N ASP B 396 1.538 69.288 30.337 1.00 36. 75 4787 CA ASP B 396 2. 504 68. 221 29. 962 1. 00 36. 91 4788 CB ASP B 396 2. 014 66. 863 30. 460 1. 00 38. 64 4789 CG ASP B 396 3. 175 65. 854 30. 365 1. 00 40. 00 4790 OD1 ASP B 396 3. 627 65. 659 29. 219 1. 00 40. 30 4791 OD2 ASP B 396 3. 644 65. 386 31. 407 1. 00 40. 34 4792 C ASP B 396 2. 835 68. 313 28. 485 1. 00 36. 78 4793 O ASP B 396 1. 969 68. 202 27. 604 1. 00 36. 92 4794 N VAL B 397 4. 124 68. 484 28. 187 1. 00 36. 34 4795 CA VAL B 397 4. 626 68. 642 26. 839 1. 00 35. 57 4796VAL B 397 6. 172 68. 716 26. 858 1. 00 36. 19 4797 CG1 VAL B 397 6. 681 69. 758 27. 827 1. 00 36. 68 4798 CG2 VAL B 397 6. 796 67. 347 27. 067 1. 00 35. 78 4799 C VAL B 397 4. 145'67. 623 25. 832 1. 00 35. 03 4800 O VAL B 397 4. 319 67. 814 24. 615 1. 00 34. 25 4801 N SER B 398 3. 597 66. 536 26. 323 1. 00 35. 16 4802 CA SER B 398 3. 123 65. 413 25. 483 1. 00 34. 40 4803 CB SER B 398 2. 984 64. 155 26. 315 1. 00 34. 33 4804 OG SER B 398 2. 183 64. 441 27. 465 1. 00 36. 04 4805 C SER B 398 1. 874 65. 756 24. 717 1. 00 34. 11 4806 O SER B 398 1. 490 65. 050 23. 751 1. 00 34. 04 4807 N VAL B 399 1. 294 66. 864 25. 175 1. 00 33. 61 4808 CA VAL B 399 0. 051 67. 357 24. 502 1. 00 32. 71 4809VAL B 399-0.548 68. 425 25. 384 1. 00 32.02 4810 CG1 VAL B 399-0.994 67. 936 26. 773 1. 00 31.51 4811 CG2 VAL B 399 0. 345 69. 650 25. 540 1. 00 30. 57 4812 C VAL B 399 0. 429 67. 626 23. 063 1. 00 32. 43 48130VAL B 399-0.312 67. 288 22. 146 1. 00 32.61 4814 N ILE B 400 1. 644 68. 143 22. 851 1. 00 32. 05 4815 CA ILE B 400 2. 158 68. 456 21. 512 1. 00 31. 22 4816 CB ILE B 400 3. 480 69. 315 21. 593 1. 00 29. 72 4817 CG1 ILE B 400 3. 316 70. 561 22. 501 1. 00 30. 21 4818 CD1 ILE B 400 4. 617 71. 398 22. 620 1. 00 28. 76 4819 CG2 ILE B 400 3.988 69.670 20.184 1.00 28. 45 4820 C ILE B 400 2. 549 67. 132 20. 835 1. 00 31. 66 4821 O ILE B 400 3. 406 66. 394 21. 406 1. 00 32. 20 4822 N PRO B 401 1. 984 66. 905 19. 683 1. 00 31. 63 4823 CA PRO B 401 2. 277 65. 668 18. 921 1. 00 31. 77 4824PRO B 401 1. 195 65. 678 17. 822 1. 00 31. 57 4825PRO B 401 1.026 67.158 17.570 1.00 31. 48 4826 CD PRO B 401 0. 984 67. 735 18. 991 1. 00 31. 63 4827 C PRO B 401 3. 647 65. 838 18. 273 1. 00 31.68 4828 0 PRO B 401 3. 961 66. 941 17. 822 1. 00 31.31 4829 N THR B 402 4. 361 64. 721 18. 135 1. 00 31.86 4830 CA THR B 402 5. 663 64. 652 17. 521 1. 00 31.63 4831 CB THR B 402 6. 416 63. 283 17. 873 1. 00 31.72 4832 OG1 THR B 402 6. 517 63. 224 19. 305 1. 00 32.23 4833 CG2 THR B 402 7. 793 63. 245 17. 185 1. 00 32.95 4834 C THR B 402 5. 642 64. 770 16. 006 1. 00 31.37 4835 0 THR B 402 6. 601 65. 360 15. 441 1. 00 31.42 4836 N SER B 403 4. 637 64. 171 15. 369 1. 00 31.11 4837 CA SER B 403 4. 530 64. 246 13. 894 1. 00 30.71 4838 CB SER B 403 5. 140 63. 132 13. 110 1. 00 32.21 4839 OG SER B 403 4. 503 61. 884 13. 402 1. 00 34.92 4840 C SER B 403 3. 069 64. 541 13. 576 1. 00 30.00 4841 0 SER B 403 2. 316 64. 700 14. 533 1. 00 29.86 4842 N GLY B 404 2. 735 64. 655 12. 307 1. 00 29.81 4843 CA GLY B 404 1. 339 64. 949 11. 924 1. 00 29.91 4844 C GLY B 404 1. 091 66. 461 11. 897 1. 00 29.96 4845 0 GLY B 404 1.985 67.262 12.307 1. 00 29.97 4846 N ASP B 405-0.091 66. 793 11. 349 1.00 28.97 4847 CA ASP B 405-0.408 68. 240 11. 262 1.00 28.19 4848 CB ASP B 405-1.212 68. 631 10. 072 1.00 29.34 4849 CG ASP B 405-0.578 68. 266 8. 751 1.00 30.37 4850 OD1 ASP B 405 0. 603 67. 883 8. 727 1. 00 30.86 4851 OD2 ASP B 405-1.331 68. 398 7. 758 1.00 31.41 4852 C ASP B 405-0.822 68. 718 12. 629 1.00 26.76 4853 O ASP B 405-1.388 67. 984 13. 458 1.00 26.97 4854 N VAL B 406-0.441 69. 969 12. 911 1.00 25.48 4855 CA VAL B 406-0.660 70. 693 14. 087 1.00 23.77 4856VAL B 406-0.139 70. 320 15. 464 1.00 24.60 4857 CG1 VAL B 406-0.840 69. 312 16. 291 1.00 25.06 4858 CG2 VAL B 406 1. 393 70. 178 15. 425 1. 00 23.83 4859 C VAL B 406-0.370 72. 206 13. 971 1.00 22.12 48600VAL B 406 0. 337 72. 679 13. 141 1. 00 21.30 4861 N VAL B 407-1.048 72. 796 14. 982 1.00 21.52 4862 CA VAL B 407-0.927 74. 240 15. 238 1.00 20.14 4863VAL B 407-1.973 75. 108 14. 619 1.00 19.63 4864 CG1 VAL B 407-1.765 76. 625 14. 837 1.00 18. 52 4865 CG2 VAL B 407-2.137 74. 872 13. 131 1.00 20.02 4866 C VAL B 407-0.766 74. 315 16. 767 1.00 19.76 48670VAL B 407-1.733 74. 054 17. 476 1.00 19.90 4868 N VAL B 408 0. 464 74. 440 17. 209 1. 00 19.65 4869 CA VAL B 408 0. 699 74. 547 18. 686 1. 00 19.41 4870VAL B 408 2. 058 74. 006 19. 093 1. 00 19.54 4871 CG1 VAL B 408 2. 345 74. 116 20. 605 1. 00 19.13 4872 CG2 VAL B 408 2. 246 72. 539 18. 684 1. 00 18.73 4873 C VAL B 408 0. 454 76. 068 18. 944 1. 00 19.05 4874 0 VAL B 408 0. 950 76. 857 18. 166 1. 00 19.10 4875 N VAL B 409-0.353 76. 356 19. 901 1.00 18.47 4876 CA VAL B 409-0.739 77. 662 20. 376 1.00 17.68 4877 CB VAL B 409-2.213 77. 974 20. 208 1.00 15.73 4878 CG1 VAL B 409-2.471 79. 441 20. 505 1.00 17.15 4879 CG2 VAL B 409-2.786 77. 437 18. 911 1.00 15.60 4880 C VAL B 409-0.231 77. 741 21. 811 1.00 18.19 4881 0 VAL B 409-0.738 77. 117 22. 732 1.00 19.34 4882 N ALA B 410 0. 851 78. 495 21. 957 1. 00 18.56 4883 CA ALA B 410 1. 540 78. 592 23. 245 1. 00 19.24 4884 CB ALA B 410 2. 765 77. 623 23. 057 1. 00 18. 65 4885 C ALA B 410 2. 130 79. 915 23. 657 1. 00 19. 65 4886 0 ALA B 410 2. 209 80. 903 22. 939 1. 00 19. 39 4887 N THR B 411 2. 658 79. 796 24. 893 1. 00 20. 40 4888 CA THR B 411 3. 353 80. 858 25. 592 1. 00 20. 09 4889 CB THR B 411 3. 004 80. 932 27. 124 1. 00 20. 00 4890 OG1 THR B 411 3. 500 79. 702 27. 705 1. 00 19. 55 4891 CG2 THR B 411 1. 563 81. 185 27. 530 1. 00 19. 24 4892 C THR B 411 4. 861 80. 624 25. 377 1. 00 20. 66 4893 O THR B 411 5. 278 79. 673 24. 734 1. 00 19. 92 4894 N ASP B 412 5. 646 81. 587 25. 859 1. 00 21. 28 4895 CA ASP B 412 7. 100 81. 543 25. 789 1. 00 22. 03 4896ASP B 412 7. 722 82. 808 26. 396 1. 00 20. 54 4897 CG ASP B 412 7. 610 83. 947 25. 445 1. 00 19. 93 4898 OD1 ASP B 412 7. 708 85. 122 25. 806 1. 00 21. 29 4899 OD2 ASP B 412 7. 503 83. 571 24. 263 1. 00 19. 70 4900 C ASP B 412 7. 602 80. 311 26. 559 1. 00 23. 34 4901 0 ASP B 412 8. 774 79. 954 26. 511 1. 00 23. 73 4902 N ALA B 413 6. 618 79. 772 27. 267 1. 00 24. 21 4903 CA ALA B 413 6. 845 78. 545 28. 071 1. 00 24. 92 4904 CB ALA B 413 5. 559 78. 174 28. 752 1. 00 24. 71 4905 C ALA B 413 7. 360 77. 446 27. 200 1. 00 25. 53 4906 0 ALA B 413 8. 099 76. 556 27. 677 1. 00 26. 08 4907 N LEU B 414 6. 983 77. 461 25. 936 1. 00 26. 29 4908 CA LEU B 414 7. 361 76. 491 24. 946 1. 00 27. 51 4909LEU B 414 6. 527 76. 680 23. 677 1. 00 27. 82 4910LEU B 414 6. 895 75. 762 22. 501 1. 00 27. 75 4911 CD1 LEU B 414 5. 809 75. 788 21. 452 1. 00 27. 84 4912 CD2 LEU B 414 8. 102 76. 410 21. 767 1. 00 28. 72 4913 C LEU B 414 8. 849 76. 447 24. 667 1. 00 28. 65 4914 O LEU B 414 9. 388 75. 373 24. 345 1. 00 29. 49 4915 N MET B 415 9. 469 77. 604 24. 656 1. 00 29. 61 4916 CA MET B 415 10. 899 77. 685 24. 315 1. 00 31. 37 4917 CB MET B 415 11. 304 79. 114 23. 995 1. 00 33. 74 4918 CG MET B 415 10. 416 79. 452 22. 767 1. 00 35. 31 4919 SD MET B 415 11. 062 80. 957 22. 171 1. 00 37. 68 4920 CE MET B 415 10. 893 82. 081 23. 575 1. 00 37. 57 4921 C MET B 415 11. 774 76. 972 25. 294 1. 00 31. 64 4922 0 MET B 415 12. 846 76. 451 24. 921 1. 00 31. 86 4923 N THR B 416 11. 278 76. 905 26. 513 1. 00 32. 12 4924 CA THR B 416 12. 126 76. 210 27. 564 1. 00 32. 88 4925 CB THR B 416 11. 915 77. 055 28. 872 1. 00 33. 04 4926 OG1 THR B 416 13. 140 76. 953 29. 653 1. 00 33. 69 4927 CG2 THR B 416 10. 703 76. 568 29. 694 1. 00 32. 78 4928 C THR B 416 11. 637 74. 773 27. 559 1. 00 33. 26 4929 0 THR B 416 12. 354 73. 755 27. 742 1. 00 33. 02 4930 N GLY B 417 10. 352 74. 636 27. 218 1. 00 33. 21 4931 CA GLY B 417 9. 644 73. 388 27. 143 1. 00 33. 87 4932 C GLY B 417 9. 920 72. 395 26. 062 1. 00 34. 34 4933 0 GLY B 417 10. 331 71. 225 26. 313 1. 00 35. 39 4934 N TYR B 418 9. 717 72. 758 24. 834 1. 00 33. 68 4935 CA TYR B 418 9. 852 71. 891 23. 632 1. 00 33. 05 4936 CB TYR B 418 8. 417 72. 090 22. 994 1. 00 30. 89 4937 CG TYR B 418 8. 160 71. 329 21. 736 1. 00 29. 71 4938 CD1 TYR B 418 8. 357 71. 883 20. 478 1. 00 28. 83 4939 CE1 TYR B 418 8. 173 71. 155 19. 321 1. 00 29. 46 4940 CZ TYR B 418 7. 770 69. 821 19. 414 1. 00 29. 85 4941 OH TYR B 418 7. 576 69. 057 18. 311 1. 00 31.17 4942 CE2 TYR B 418 7. 538 69. 244 20. 644 1. 00 30.26 4943 CD2 TYR B 418 7. 742 70. 001 21. 804 1. 00 29.90 4944 C TYR B 418 11. 011 72. 304 22. 798 1. 00 33.57 4945 0 TYR B 418 11. 375 73. 517 22. 783 1. 00 33.99 4946 N THR B 419 11. 689 71. 369 22. 099 1. 00 33.68 4947 CA THR B 419 12. 859 71. 687 21. 281 1. 00 33.48 4948 CB THR B 419 14. 128 70. 789 21. 668 1. 00 33.44 4949 OG1 THR B 419 13. 708 69. 403 21. 377 1. 00 34.56 4950 CG2 THR B 419 14. 590 70. 943 23. 098 1. 00 32.81 4951 C THR B 419 12. 662 71. 587 19. 772 1. 00 33.25 4952 O THR B 419 13. 675 71. 779 19. 041 1. 00 33.29 4953 N GLY B 420 11. 476 71. 232 19. 313 1. 00 32.19 4954 CA GLY B 420 11. 221 71. 084 17. 882 1. 00 31.59 4955 C GLY B 420 10. 976 72. 397 17. 154 1. 00 31.34 49560GLY B 420 10. 739 73. 467 17. 732 1. 00 31.65 4957 N ASP B 421 10. 975 72. 304 15. 842 1. 00 30.71 4958 CA ASP B 421 10. 759 73. 294 14. 856 1. 00 29.77 4959 CB ASP B 421 11. 845 73. 374 13. 790 1. 00 34.30 4960 CG ASP B 421 13. 148 73. 988 14. 276 1. 00 38.28 4961 OD1 ASP B 421 13. 523 73. 981 15. 479 1. 00 39.58 4962 OD2 ASP B 421 13. 729 74. 602 13. 332 1. 00 39.88 4963 C ASP B 421 9. 376 73. 155 14. 188 1. 00 28.00 4964 O ASP B 421 8. 719 72. 105 14. 278 1. 00 27.96 4965 N PHE B 422 9. 070 74. 215 13. 453 1. 00 25.51 4966 CA PHE B 422 7. 816 74. 390 12. 750 1. 00 22.91 4967 CB PHE B 422 6. 906 75. 303 13. 640 1. 00 20.75 4968 CG PHE B 422 6. 683 74. 753 15. 003 1. 00 19.92 4969 CD1 PHE B 422 5. 572 73. 893 15. 219 1. 00 19.93 4970 CE1 PHE B 422 5.348 73.373 16.490 1. 00 19.73 4971 CZ PHE B 422 6. 210 73. 607 17. 517 1. 00 20.32 4972 CE2 PHE B 422 7. 361 74. 448 17. 315 1. 00 19.79 4973 CD2 PHE B 422 7. 522 75. 002 16. 059 1. 00 19.71 4974 C PHE B 422 7. 986 74. 970 11. 372 1. 00 22.14 4975 0 PHE B 422 8. 933 75. 712 11. 078 1. 00 22. 52 4976 N ASP B 423 6. 951 74. 815 10. 546 1. 00 21.59 4977 CA ASP B 423 6. 894 75. 290 9. 180 1. 00 21.07 4978 CB ASP B 423 5. 862 74. 596 8. 330 1. 00 23.40 4979 CG ASP B 423 5. 875 73. 103 8. 163 1. 00 24.72 4980 OD1 ASP B 423 4. 876 72. 580 7. 641 1. 00 24.43 4981 OD2 ASP B 423 6. 896 72. 442 8. 548 1. 00 26.05 4982 C ASP B 423 6. 783 76. 804 9. 123 1. 00 19.86 4983 0 ASP B 423 7. 288 77. 425 8. 191 1. 00 19.99 4984 N SER B 424 6. 078 77. 355 10. 107 1. 00 18.97 4985 CA SER B 424 5. 920 78. 830 10. 178 1. 00 16.66 4986 CB SER B 424 4. 727 79. 379 9. 431 1. 00 18.00 4987 OG SER B 424 3. 518 79. 033 10. 133 1. 00 17.43 4988 C SER B 424 5. 740 79. 099 11. 696 1. 00 15.44 4989 O SER B 424 5. 344 78. 195 12. 401 1. 00 14.32 4990 N VAL B 425 6. 085 80. 298 12. 050 1. 00 14.61 4991 CA VAL B 425 5. 956 80. 888 13. 391 1. 00 14.87 4992VAL B 425 7. 306 81. 311 13. 999 1. 00 15.73 4993 CG1 VAL B 425 7. 110 82. 237 15. 258 1. 00 16.67 4994 CG2 VAL B 425 8. 033 80. 100 14. 578 1. 00 15.23 4995 C VAL Bk425 4. 985 82. 097 13. 268 1. 00 13.93 49960VAL B 425 5. 092 82. 807 12. 259 1. 00 12.83 4997 N ILE B 426 3. 998 82. 168 14. 181 1. 00 14.09 4998 CA ILE B 426 3. 056 83. 286 14. 146 1. 00 14.73 4999 CB ILE B 426 1. 576 82. 977 13. 779 1. 00 16.08 5000 CG1 ILE B 426 1. 497 82. 256 12. 427 1. 00 16.46 5001 CD1 ILE B 426 0. 059 82. 091 11. 876 1. 00 14.54 5002 CG2 ILE B 426 0. 755 84. 315 13. 678 1. 00 15.49 5003 C ILE B 426 3. 206 84. 018 15. 477 1. 00 14.71 50040ILE B 4263. 01583. 41416. 5221. 00 15.66 5005 N ASP B 427 3. 591 85. 274 15. 419 1. 00 14.89 5006 CA ASP B 427 3. 877 85. 958 16. 722 1. 00 14.53 5007ASP B 427 5. 364 86. 210 16. 618 1. 00 14.50 5008 CG ASP B 427 6. 026 86. 740 17. 874 1. 00 14.46 5009 OD1 ASP B 427 5. 463 86. 711 18. 957 1. 00 13.77 5010 OD2 ASP B 427 7. 193 87. 127 17. 685 1. 00 14.75 5011 C ASP B 427 2. 962 87. 142 17. 003 1. 00 14.79 5012 0 ASP B 427 2. 760 88. 073 16. 194 1. 00 13.76 5013 N CYS B 428 2. 598 87. 214 18. 247 1. 00 14.94 5014 CA CYS B 428 1. 726 88. 225 18. 841 1. 00 14.98 5015 CB CYS B 428 1. 061 87. 756 20. 122 1. 00 13.28 5016 SG CYS B 428 2. 009 87. 433 21. 551 1. 00 12.71 5017 C CYS B 428 2. 522 89. 500 19. 129 1. 00 15.55 5018 0 CYS B 428 1. 932 90. 532 19. 304 1. 00 15.28 5019 N ASN B 429 3. 843 89. 363 19. 154 1. 00 16.07 5020 CA ASN B 429 4. 819 90. 384 19. 388 1. 00 16.27 5021 CB ASN B 429 4. 936 91. 331 18. 216 1. 00 16.04 5022 CG ASN B 429 5. 189 90. 622 16. 904 1. 00 15.13 5023 OD1 ASN B 429 4. 296 90. 765 15. 943 1. 00 14.11 5024 ND2 ASN B 429 6. 218 90. 015 16. 729 1. 00 15.64 5025 C ASN B 429-4. 654 91. 069 20. 741 1. 00 17.11 5026 0 ASN B 429 5. 082 92. 214 20. 876 1. 00 17.86 5027 N THR B 430 4. 080 90. 387 21. 667 1. 00 17.69 5028 CA THR B 430 3. 806 90. 766 23. 034 1. 00 20. 27 5029 CB THR B 430 2. 246 90. 933 23. 243 1. 00 20.18 5030 OG1 THR B 430 1. 861 91. 981 22. 355 1. 00 21.67 5031 CG2 THR B 430 1. 747 91. 092 24. 613 1. 00 22.31 5032 C THR B 430 4. 312 89. 726 24. 049 1. 00 22.02 5033 0 THR B 430 4. 259 88. 496 23. 905 1. 00 22.22 5034 N CYS B 431 4. 772 90. 300 25. 137 1. 00 24.01 5035 CA CYS B 431 5. 315 89. 574 26. 285 1. 00 25.91 5036 CB CYS B 431 6. 797 89. 822 26. 286 1. 00 29.39 5037 SG CYS B 431 7. 770 88. 935 27. 515 1. 00 36.14 5038 C CYS B 431 4. 521 89. 941 27. 536 1. 00 26.34 5039 0 CYS B 431 3. 694 90. 937 27. 548 1. 00 26.73 5040 N VAL B 432 4. 615 89. 076 28. 501 1. 00 26. 13 5041 CA VAL B 432 3. 969 89. 273 29. 853 1. 00 25.97 5042VAL B 432 2. 850 88. 269 30. 050 1. 00 26.32 5043 CG1 VAL B 432 3. 260 86. 796 30. 020 1. 00 27.27 5044 CG2 VAL B 432 1. 987 88. 463 31. 276 1. 00 26.56 5045 C VAL B 432 5. 228 89. 228 30. 752 1. 00 25.57 5046 0 VAL B 432 6. 102 88. 376 30. 495 1. 00 25.01 5047 N THR B 433 5. 381 90. 178 31. 637 1. 00 25.70 5048 CA THR B 433 6. 550 90. 236 32. 547 1. 00 25.56 5049 CB THR B 433 7. 483 91. 407 31. 963 1. 00 27.63 5050 OG1 THR B 433 8. 682 91. 411 32. 794 1. 00 28.39 5051 CG2 THR B 433 6. 753 92. 754 32. 066 1. 00 27.99 5052 C THR B 433 6. 102 90. 646 33. 945 1. 00 24.70 5053 O THR B 433 5. 116 91. 381 34. 053 1. 00 24.41 5054 N GLN B 434 6. 819 90. 236 34. 974 1. 00 23.94 5055 CA GLN B 434 6. 544 90. 650 36. 347 1. 00 23. 47 5056 CB GLN B 434 6. 719 89. 760 37. 526 1. 00 23. 92 5057 CG GLN B 434 5. 821 88. 648 37. 915 1. 00 24. 59 5058 CD GLN B 434 6. 159 87. 90539. 1611. 00 25. 70 5059 OE1 GLN B 434 5. 324 87. 466 39.971 1.00 26. 37 5060 NE2 GLN B 434 7. 481 87. 705 39. 397 1. 00 25. 00 5061C GLN B 434 7. 344 91. 966 36.574 1.00 22. 88 5062 O GLN B 434 8. 492 92. 07936. 1371. 00 22. 85 5063 N THR B 435 6. 727 92. 881 37. 247 1. 00 22. 38 5064 CA THR B 435 7. 360 94. 192 37. 560 1. 00 21. 55 5065 CB THR B 435 6. 708 95. 343 36.705 1. 00 22. 86 5066 OG1 THR B 435 7. 505 96. 555 36. 889 1. 00 25. 74 5067 CG2 THR B 435 5. 309 95. 670 37. 210 1. 00 22. 42 5068 C THR B 435 7. 096 94. 43139. 0481. 00 21. 02 5069 O THR B 435 6. 061 93. 99039. 5701. 00 20. 69 5070 N VAL B 436 7. 987 95. 194 39. 651 1. 00 20. 46 5071 CA VAL B 436 7. 860 95. 51741. 0891. 00 19. 97 5072 CB VAL B 436 9. 212 95. 205 41. 755 1. 00 17. 84 5073 CG1 VAL B 436 10. 306 96. 131 41. 214 1. 00 18. 60 5074 CG2 VAL B 436 9. 162 95. 168 43. 236 1. 00 18. 49 5075 C VAL B 436 7. 491 96. 998 41. 112 1. 00 20. 77 50760 VAL B 436 7. 966 97. 672 40. 172 1. 00 21. 46 5077 N ASP B 437 6. 628 97. 360 42.023 1. 00 20. 68 5078 CA ASP B 437 6. 232 98. 772 42. 158 1. 00 21. 19 5079 CB ASP B 4374. 816 99. 017 41.707 1. 00 24. 22 5080 CG ASP B 437 4. 279 100. 398 41. 820 1. 00 26. 77 5081 OD1 ASP B 437 3. 055 100. 565 41. 994 1. 00 28. 98 5082OD2 ASP B 437 5. 024 101. 416 41. 742 1. 00 28. 15 5083 C ASP B 437 6. 486 99. 127 43.621 1. 00 20. 49 50840 ASP B 437 5. 875 98. 410 44.468 1. 00 20. 66 5085 N PHE B 438 7. 306 100. 107 43. 882 1. 00 20. 05 5086 CA PHE B 438 7. 502 100. 446 45. 339 1. 00 20. 10 5087 CB PHE B 4388. 838 101. 137 45. 618 1. 00 19. 85 5088 CG PHE B 438 9. 935 100. 211 45. 132 1. 00 20. 07 5089 CD1 PHE B 438 10. 032 98. 93645. 7501. 00 20. 05 5090 CE1 PHE B 438 11. 025 98. 058 45.328 1. 00 18. 80 5091 CZ PHE B 438 11. 844 98. 421 44. 299 1. 00 18. 97 5092 CE2 PHE B 438 11. 753 99. 669 43. 659 1. 00 19. 27 5093 CD2 PHE B 438 10. 743 100. 566 44. 090 1. 00 20. 54 5094 C PHE B 438 6. 353 101. 465 45. 570 1. 00 20. 32 50950 PHE B 4386. 627 102. 659 45.507 1. 00 19. 93 5096 N SER B 439 5. 207 100. 913 45.761 1. 00 20. 35 5097 CA SER B 439 3. 963 101. 691 45. 917 1. 00 20. 46 5093 CB SER B 439 2. 908 100. 801 45. 300 1. 00 20. 21 5099 OG SER B 439 2. 895 99. 555 45.968 1. 00 19. 09 5100 C SER B 439 3. 700 102. 247 47.264 1. 00 21. 24 51010 SER B 439 2. 777 103. 131 47.509 1. 00 22. 04 5102N LEU B 440 4. 412 101. 808 48.269 1. 00 20. 73 5103 CA LEU B 4404. 337 102. 267 49. 644 1. 00 20. 94 5014 CB LEU B 440 4. 821 103. 766 49. 594 1. 00 21. 57 5105 CG LEU B 440 6. 096 104. 020 48. 830 1. 00 20. 97 5106 CD1 LEU B 440 6. 392 105. 551 48. 832 1. 00 21. 69 5107CD2 LEU B 440 7. 215 103. 317 49. 575 1. 00 21. 52 5108C LEU B 440 2. 927 102. 208 50.179 1. 00 21. 19 5109 O LEU B 440 2. 525 103. 067 50.980 1. 00 21. 26 5110 N ASP B 441 2. 194 101. 146 49. 822 1. 00 21. 57 5111 CA ASP B 441 0. 822 100. 953 50. 285 1. 00 20. 98 5112 CB ASP B 441-0.102 101. 161 49. 003 1.00 21.96 5113 CG ASP B 441 0. 288 100. 148 47. 937 1. 00 23.63 5114 OD1 ASP B 441 1. 115 99. 217 48. 184 1. 00 22.51 5115 OD2 ASP B 441-0.215 100. 291 46. 801 1.00 24.28 5116 C ASP B 441 0. 552 99. 567 50. 837 1. 00 20.17 5117 0 ASP B 441-0.358 98. 951 50. 263 1.00 20.50 5118 N PRO B 442 1. 199 99. 073 51. 853 1. 00 19.54 5119 CA PRO B 442 2. 247 99. 762 52. 622 1. 00 19.37 5120 CB PRO B 442 2. 083 99. 102 53. 997 1. 00 18.64 5121 CG PRO B 442 1. 714 97. 682 53. 675 1. 00 18.79 5122 CD PRO B 442 0. 882 97. 758 52. 396 1. 00 18.84 5123 C PRO B 442 3. 671 99. 712 52. 145 1. 00 19.32 5124 O PRO B 442 4. 491 100. 666 52. 398 1. 00 19.74 5125 N THR B 443 4. 043 98. 668 51. 425 1. 00 18.85 5126 CA THR B 443 5. 43 98. 521 50. 948 1. 00 16.97 5127 CB THR B 443 6. 007 97. 284 51. 767 1. 00 16.58 5128 OG1 THR B 443 5. 131 96. 198 51. 409 1. 00 17.24 5129 CG2 THR B 443 5. 869 97. 518 53. 290 1. 00 15.96 5130 C THR B 443 5. 604 98. 426 49. 468 1. 00 16.43 5131 O THR B 443 5. 885 99. 406 48. 749 1. 00 15.41 5132 N PHE B 444 5. 495 97. 185 48. 931 1. 00 15.91 5133 CA PHE B 444 5. 711 96. 985 47. 487 1. 00 15.58 5134 CB PHE B 444 7. 131 96. 535 47. 068 1. 00 14.45 5135 CG PHE B 444 7. 587 95. 225 47. 688 1. 00 13.40 5136 CD1 PHE B 444 7. 353 93. 997 47. 040 1. 00 12.69 5137 CE1 PHE B 444 7. 621 92. 779 47. 653 1. 00 10.04 5138 CZ PHE B 444 8.198 92.791 48.939 1. 00 10.77 5139 CE2 PHE B 444 8. 528 94. 001 49. 578 1. 00 12.17 5140 CD2 PHE B 444 8. 198 95. 192 48. 936 1. 00 13.65 5141 C PHE B 444 4.596 96.086 46.937 1. 00 15.19 5142 0 PHE B 444 3. 942 95. 409 47. 669 1. 00 14.52 5143 N THR B 445 4. 474 96. 214 45. 613 1. 00 16.43 5144 CA THR B 445 3. 494 95. 425 44. 853 1. 00 17.84 5145 CB THR B 445 2. 540 96. 444 44. 062 1. 00 17.45 5146 OG1 THR B 445 1. 892 97. 261 45. 063 1. 00 16.49 5147 CG2 THR B 445 1. 444 95. 743 43. 211 1. 00 17.30 5148 C THR B 445 4. 277 94. 651 43. 782 1. 00 18.44 5149 O THR B 445 5. 069 95. 302 43. 099 1. 00 18.75 5150 N ILE B 446 3. 963 93. 401 43. 605 1. 00 19.79 5151 CA ILE B 446 4. 568 92. 594 42. 498 1. 00 20.89 5152 CB ILE B 446 5. 249 91. 310 43. 038 1. 00 19.35 5153 CG1 ILE B 446 6. 528 91. 765 43. 750 1. 00 20.58 5154 CD1 ILE B 446 7. 325 90. 777 44. 524 1. 00 19.09 5155 CG2 ILE B 446 5. 460 90. 261 41. 905 1. 00 20.14 5156 C ILE B 446 3. 442 92. 233 41. 548 1. 00 22.29 51570 ILE B 446 2. 481 91. 576 42. 045 1. 00 22.72 5158 N GLU B 447 3. 511 92. 632 40. 318 1. 00 23.43 5159 CA GLU B 447 2. 416 92. 299 39. 391 1. 00 25.11 5160 CB GLU B 447 1. 210 93. 187 39. 400 1. 00 29.30 5161 CG GLU B 447 0. 237 93. 171 40. 657 1. 00 33.64 5162 CD GLU B 447-0.950 94. 082 40. 554 1.00 35.51 5163 OE1 GLU B 447-0.997 95. 289 40. 799 1.00 36.18 5164 OE2 GLU B 447-1.999 93. 476 40. 142 1.00 36.50 5165C GLU B 447 2. 924 92. 030 38. 001 1. 00 24.69 51660 GLU B 447 4. 071 92. 326 37. 676 1. 00 24.59 5167 N THR B 448 2. 067 91. 402 37. 243 1. 00 24.71 5168 CA THR B 448 2. 329 91. 024 35. 851 1. 00 25.22 5169 CB THR B 448 1. 723 89. 591 35. 667 1. 00 25. 71 5170 OG1 THR B 448 2. 507 88. 727 36. 601 1. 00 26. 44 5171 CG2 THR B 448 1. 724 88. 978 34. 290 1. 00 25. 62 5172 C THR B 448 1. 760 92. 115 34. 965 1. 00 25. 93 5173 O THR B 448 0. 670 92. 633 35. 246 1. 00 26. 50 5174 N ILE B 449 2. 497 92. 468 33. 969 1. 00 26. 14 5175 CA ILE B 449 2. 191 93. 463 32. 945 1. 00 26. 35 5176 CB ILE B 449 3. 130 94. 708 33. 161 1. 00 27. 78 5177 CG1 ILE B 449 2. 683 95. 436 34. 440 1. 00 29. 25 5178 CDI ILE B 449 3. 537 96. 701 34. 715 1. 00 31. 07 5179 CG2 ILE B 449 3. 243 95. 674 31. 988 1. 00 29. 58 5180 C ILE B 449 2. 499 92. 834 31. 582 1. 00 25. 93 5181 O ILE B 449 3. 387 91. 966 31. 458 1. 00 25. 12 5182 N THR B 450 1. 794 93. 342 30. 594 1. 00 26. 02 5183 CA THR B 450 2. 038 92. 917 29. 203 1. 00 26. 03 5184 CB THR B 450 0. 679 92. 865 28. 419 1. 00 24. 71 5185 OG1 THR B 450-0.176 92. 043 29. 231 1. 00 23.24 5186 CG2 THR B 450 0. 950 92. 322 27. 012 1. 00 24. 89 5187 C THR B 450 2. 963 93. 919 28. 552 1. 00 26. 89 5188 O THR B 450 2. 774 95. 147 28. 813 1. 00 27. 66 5189 N LEU B 451 3. 964 93. 489 27. 818 1. 00 27. 15 5190 CA LEU B 451 4. 839 94. 493 27. 181 1. 00 27. 66 5191 CB LEU B 451 6. 154 94. 550 27. 936 1. 00 29. 81 5192 CG LEU B 451 6. 159 94. 934 29. 385 1. 00 31. 11 5193 CD1 LEU B 451 7. 567 94. 888 29. 971 1. 00 30. 30 5194 CD2 LEU B 451 5. 616 96. 358 29. 535 1. 00 31. 63 5195 C LEU B 451 5. 075 94. 111 25. 720 1. 00 27. 99 5196 O LEU B 451 4. 876 92. 944 25. 369 1. 00 28. 27 5197 N PRO B 452 5. 517 95. 108 24. 983 1. 00 28. 09 5198 CA PRO B 4525. 90694. 92923. 5651. 0027. 99 5199 CB PRO B 452 6. 307 96. 353 23. 136 1. 00 27. 94 5200 CG PRO B 452 5. 567 97. 246 24. 110 1. 00 28. 14 5201 CD PRO B 452 5. 735 96. 506 25. 429 1. 00 28. 08 5202 C PRO B 452 7. 150 94. 014 23. 718 1. 00 27. 93 5203 O PRO B 452 7. 692 94. 031 24. 858 1. 00 29. 22 5204 N GLN B 453 7. 548 93. 266 22. 722 1. 00 26. 82 5205 CA GLN B 453 8. 689 92. 328 22. 917 1. 00 25. 78 5206 CB GLN B 453 8. 543 91. 059 22. 062 1. 00 24. 96 5207 CG GLN B 453 8. 750 91. 333 20. 586 1. 00 23. 35 5208 CD GLN B 453 8. 444 90. 118 19. 734 1. 00 21. 25 5209 OE1 GLN B 453 8. 048 90. 459 18. 532 1. 00 19. 89 5210 NE2 GLN B 453 8. 472 88. 977 20. 154 1. 00 19. 97 5211 C GLN B 453 9. 994 93. 013 22. 533 1. 00 24. 95 52120 GLN B 453 9. 950 93. 994 21. 795 1. 00 24. 99 5213 N ASP B 454 11. 075 92. 412 23. 013 1. 00 24. 21 5214 CA ASP B 454 12. 405 92. 971 22. 721 1. 00 23. 37 5215 CB ASP B 454 13. 211 93. 193 24. 009 1. 00 24. 21 5216 CG ASP B 454 13. 579 91. 899 24. 687 1. 00 24. 70 5217 OD1 ASP B 454 13. 374 90. 831 24. 086 1. 00 23. 50 5218 OD2 ASP B 454 14. 097 91. 939 25. 828 1. 00 26. 04 5219 C ASP B 454 13. 036 92. 134 21. 653 1. 00 22. 28 5220 O ASP B 454 12. 415 91. 150 21. 213 1. 00 22. 52 5221 N ALA B 455 14. 184 92. 582 21. 186 1. 00 22. 32 5222 CA ALA B 455 14. 975 91. 919 20. 142 1. 00 21. 33 5223 CB ALA B 455 16. 219 92. 660 19. 856 1. 00 21. 02 5224C ALAB 45515. 25590. 47620. 5271. 0021. 18 52250 ALAB 45515. 24489. 59819. 6241. 0021. 46 5226 N VAL B 456 15. 449 90. 201 21. 788 1. 00 20. 74 5227 CA VAL B 456 15. 707 88. 787 22. 221 1. 00 19. 49 5228 CB VAL B 456 16. 144 88. 784 23. 684 1. 00 18. 35 5229 CG1 VAL B 456 16. 181 87. 383 24. 291 1. 00 17. 80 5230 CG2 VAL B 456 17. 484 89. 451 23. 842 1. 00 18. 07 5231 C VAL B 456 14. 499 87. 937 21. 951 1. 00 19. 47 5232 O VAL B 456 14. 609 86. 853 21. 342 1. 00 20. 06 5233 N SER B 457 13. 340 88. 423 22. 417 1. 00 18. 97 5234 CA SER B 457 12. 097 87. 671 22. 210 1. 00 17. 74 5235 CB SER B 457 10. 932 88. 273 23. 013 1. 00 17. 76 5236 OG SER B 457 9. 717 87. 777 22. 562 1. 00 15. 36 5237 C SER B 457 11. 751 87. 471 20. 781 1. 00 17. 75 5238 0 SER B 457 11. 292 86. 335 20. 445 1. 00 18. 45 5239 N ARG B 458 11. 903 88. 430 19. 924 1. 00 17. 21 5240 CA ARG B 458 11. 588 88. 431 18. 531 1. 00 17. 48 5241 CB ARG B 458 11. 815 89. 839 17. 898 1. 00 16. 33 5242 CG ARG B 458 11. 087 89. 978 16. 578 1. 00 15. 25 5243 CD ARG B 458 11. 248 91. 232 15. 855 1. 00 14. 65 5244 NE ARG B 458 10. 488 91. 432 14. 643 1. 00 13. 91 5245 CZ ARG B 458 9. 268 91. 738 14. 359 1. 00 12. 95 5246 NH1 ARG B 458 8. 807 91. 807 13. 111 1. 00 12. 97 5247 NH2 ARG B 458 8. 350 92. 185 15. 226 1. 00 13. 56 5248 C ARG B 458 12. 403 87. 370 17. 772 1. 00 18. 02 5249 0 ARG B 458 11. 940 86. 567 16. 966 1. 00 18. 56 5250 N THR B 459 13. 663 87. 360 18. 112 1. 00 18. 13 5251 CA THR B 459 14. 682 86. 436 17. 552 1. 00 17. 94 5252 CB THR B 459 16. 139 86. 978 17. 777 1. 00 17. 58 5253 OG1 THR B 459 16. 232 88. 196 16. 973 1. 00 17. 27 5254 CG2 THR B 459 17. 245 85. 968 17. 459 1. 00 17. 96 5255 C THR B 459 14. 458 85. 006 17. 957 1. 00 18. 21 5256 0 THR B 459 14. 446 84. 168 17. 011 1. 00 18. 14 5257 N GLN B 460 14. 318 84. 737 19. 222 1. 00 18. 69 5258 CA GLN B 460 14. 101 83. 430 19. 825 1. 00 19. 32 5259 CB GLN B 460 14.144 83.392 21.323 1.00 21. 25 5260 CG GLN B 460 15.372 83.747 22.084 1.00 22. 53 5261 CD GLN B 460 16. 580 82. 866 21. 985 1. 00 24. 10 5262 OE1 GLN B 460 17.718 83.269 21.829 1.00 24. 57 5263 NE2 GLN B 460 16. 367 81. 541 22. 185 1. 00 25. 68 5264 C GLN B 460 12. 841 82. 782 19. 296 1. 00 19. 68 52650 GLN B 460 12. 861 81. 633 18. 867 1. 00 19. 80 5266 N ARG B 461 11. 735 83. 540 19. 338 1. 00 19. 34 5267 CA ARG B 461 10. 476 83. 103 18. 799 1. 00 19. 39 5268 CB ARG B 461 9.365 84.086 19.090 1.00 18. 73 5269 CG ARG B 461 8. 853 84. 192 20. 496 1. 00 17. 97 5270 CD ARG B 461 7.615 85.100 20.508 1.00 17. 34 5271 NE ARG B 461 7. 178 85. 194 21. 898 1. 00 18. 49 5272 CZ ARG B 461 6.443 86.147 22.403 1.00 18. 81 5273 NH1 ARG B 461 6. 052 87. 157 21. 652 1. 00 20. 96 5274 NH2 ARG B 461 6. 207 86. 245 23. 722 1. 00 19. 54 5275 C ARG B 461 10.532 82.738 17.322 1.00 19. 64 5276 O ARG B 461 10.083 81.643 16.886 1.00 20. 21 5277 N ARG B 462 11. 035 83. 626 16. 508 1. 00 19. 86 5278 CA ARG B 462 11. 216 83. 476 15. 082 1. 00 20. 52 5279 CB ARG B 462 11. 777 84. 730 14. 402 1. 00 20. 66 5280 CG ARG B 462 11. 872 84. 628 12. 906 1. 00 20. 31 5281 CD ARG B 462 12. 624 85. 753 12. 293 1. 00 19. 81 5282 NE ARG B 462 14. 004 85. 748 12. 663 1. 00 19. 31 5283 CZ ARG B 462 14. 927 86. 653 12. 307 1. 00 20.03 5284 NH1 ARG B 462 14. 695 87. 690 11. 549 1. 00 20.83 5285 NH2 ARG B 462 16. 194 86. 498 12. 713 1. 00 19.86 5286 C ARG B 462 12. 212 82. 313 14. 824 1. 00 21.74 52870ARG B 462 12. 082 81. 629 13. 802 1. 00 22.01 5288 N GLY B 463 13. 134 82. 137 15. 749 1. 00 21.98 5289 CA GLY B 463 14. 129 81. 060 15. 604 1. 00 23.74 5290 C GLY B 463 13. 440 79. 720 15. 680 1. 00 24.89 5291 0 GLY B 463 14. 125 78. 671 15. 616 1. 00 25.84 5292 N ARG B 464 12. 116 79. 695 15. 858 1. 00 24.81 5293 CA ARG B 464 11. 430 78. 384 15. 959 1. 00 24.48 5294 CB ARG B 464 10. 447 78. 272 17. 097 1. 00 25.74 5295 CG ARG B 464 11. 198 78. 412 18. 486 1. 00 28.19 5296 CD ARG B 464 12. 107 77. 232 18. 520 1. 00 29.84 5297 NE ARG B 464 11. 307 75. 998 18. 751 1. 00 31.84 5298 CZ ARG B 464 11. 190 75. 564 20. 023 1. 00 32.79 5299 NH1 ARG B 464 11. 873 76. 213 20. 970 1. 00 33.10 5300 NH2 ARG B 464 10. 436 74. 519 20. 305 1. 00 32.80 5301 C ARG B 464 11. 082 77. 799 14. 642 1. 00 24.28 5302 0 ARG B 464 10. 542 76. 673 14. 558 1. 00 24.27 5303 N THR B 465 11. 378 78. 460 13. 563 1. 00 24.52 5304 CA THR B 465 11. 116 77. 959 12. 196 1. 00 25.02 5305 CB THR B 465 9. 973 78. 762 11. 468 1. 00 21.60 5306 OG1 THR B 465 9. 801 78. 055 10. 197 1. 00 21.52 5307 CG2 THR B 465 10. 358 80. 227 11. 153 1. 00 21.18 5308 C THR B 465 12. 434 78. 199 11. 424 1. 00 26.71 5309 O THR B 465 13. 276 78. 906 11. 998 1. 00 26.54 5310 N GLY B 466-12.544 77. 647 10. 242 1.00 28.60 5311 CA GLY B 466 13. 751 77. 842 9. 437 1. 00 31.99 5312 C GLY B 466 14. 884 76. 858 9. 532 1. 00 34.04 5313 O GLY B 466 15. 922 77. 123 8. 847 1. 00 34.50 5314 N ARG B 467 14. 781 75. 789 10. 284 1. 00 35.78 5315 CA ARG B 467 15. 847 74. 763 10. 363 1. 00 37.40 5316ARG B 467 15. 859 73. 973 11. 671 1. 00 40.48 5317 CG ARG B 467 17. 030 72. 940 11. 710 1. 00 43.27 5318 CD ARG B 467 16. 855 72. 006 12. 875 1. 00 44.98 5319 NE ARG B 467 15. 754 71. 113 12. 690 1. 00 47.51 5320 CZ ARG B 467 15. 544 70. 036 11. 958 1. 00 48.81 5321 NH1 ARG B 467 16. 446 69. 411 11. 192 1. 00 49.31 5322 NH2 ARG B 467 14. 266 69. 563 11. 863 1. 00 49.21 5323 C ARG B 467 15. 467 73. 693 9. 280 1. 00 37.83 5324 0 ARG B 467 14. 332 73. 174 9. 298 1. 00 38.32 5325 N GLY B 468 16. 425 73. 375 8. 441 1. 00 37.53 5326 CA GLY B 468 16. 196 72. 365 7. 363 1. 00 36.57 5327 C GLY B 468 15. 606 73. 136 6. 172 1. 00 35.86 53280GLY B 468 16. 352 73. 578 5. 274 1. 00 36.41 5329 N LYS B 469 14. 319 73. 354 6. 252 1. 00 34.15 5330 CA LYS B 469 13. 532 74. 070 5. 272 1. 00 32.80 5331 CB LYS B 469 12. 022 73. 722 5. 645 1. 00 32.19 5332 CG LYS B 469 11. 715 72. 249 5. 432 1. 00 31.96 5333 CD LYS B 469 10. 367 71. 711 5. 782 1. 00 31.00 5334 CE LYS B 469 9. 123 72. 315 5. 152 1. 00 29.77 5335 NZ LYS B 469 7. 947 71. 377 5. 479 1. 00 29.55 5336 C LYS B 469 13. 501 75. 599 5. 450 1. 00 31.81 53370LYS B 469 13. 656 76. 110 6. 538 1. 00 31.70 5338 N PRO B 470 13. 184 76. 256 4. 336 1. 00 31.05 5339 CA PRO B 470 12. 980 77. 731 4. 324 1. 00 30.26 5340PRO B 470 12. 748 78. 072 2. 858 1. 00 29.62 5341 CG PRO B 470 13. 073 76. 868 2. 077 1. 00 29.84 5342 CD PRO B 470 12. 957 75. 668 2. 997 1. 00 30.23 5343 C PRO B 470 11. 635 77. 891 5. 088 1. 00 30.00 5344 0 PRO B 470 10. 613 77. 295 4. 642 1. 00 30.67 5345 N GLY B 471 11. 676 78. 617 6. 179 1. 00 29.27 5346 CA GLY B 471 10. 449 78. 790 7. 033 1. 00 27.23 5347 C GLY B 471 9. 789 80. 116 6. 803 1. 00 25.75 5348 0 GLY B 471 10. 134 80. 816 5. 867 1. 00 25.95 5349 N ILE B 472 8. 788 80. 422 7. 655 1. 00 24.17 5350 CA ILE B 472 8. 021 81. 685 7. 506 1. 00 21.81 5351 CB ILE B 472 6. 722 81. 453 6. 668 1. 00 22.49 5352 CG1 ILE B 472 7. 077 80. 820 5. 316 1. 00 21.06 5353 CD1 ILE B 472 5. 856 80. 547 4. 434 1. 00 22.72 5354 CG2 ILE B 472 5. 892 82. 773 6. 419 1. 00 21.97 5355 C ILE B 472 7. 704 82. 207 8. 889 1. 00 20.09 5356 0 ILE B 472 7. 379 81. 442 9. 774 1. 00 19.34 5357 N TYR B 473 7. 844 83. 512 9. 002 1. 00 19.75 5358 CA TYR B 473 7. 564 84. 225 10. 272 1. 00 19.10 5359 CB TYR B 473 8. 840 84. 916 10. 750 1. 00 18.57 5360 CG TYR B 473 8. 702 85. 719 12. 013 1. 00 16.95 5361 CD1 TYR B 473 8. 830 87. 088 11. 961 1. 00 17.59 5362 CE1 TYR B 473 8. 644 87. 875 13. 106 1. 00 16.52 5363 CZ TYR B 473 8. 275 87. 296 14. 275 1. 00 15.77 5364 OH TYR B 473 8. 064 88. 050 15. 410 1. 00 15.60 5365 CE2 TYR B 473 8. 060 85. 915 14. 357 1. 00 15.90 5366 CD2 TYR B 473 8. 285 85. 152 13. 205 1. 00 16.87 5367 C TYR B 473 6. 483 85. 282 9. 968 1. 00 18.69 5368 0 TYR B 473 6. 749 86. 151 9. 173 1. 00 18.74 5369 N ARG B 474 5. 338 85. 163 10. 653 1. 00 18.48 5370 CA ARG B 474 4. 232 86. 119 10. 446 1. 00 17.35 5371 CB ARG B 474 2. 889 85. 426 10. 121 1. 00 18.16 5372ARG B 474 3. 021 84. 445 8. 959 1. 00 18.30 5373 CD ARG B 474 1. 703 83. 854 8. 589 1. 00 18.53 5374 NE ARG B 474 1. 817 82. 860 7. 598 1. 00 19.47 5375 CZ ARG B 474 2. 106 82. 946 6. 307 1. 00 20.41 5376 NH1 ARG B 474 2. 277 84. 040 5. 601 1. 00 20.27 5377 NH2 ARG B 474 2. 336 81. 797 5. 671 1. 00 20. 14 5378 C ARG B 474 4. 160 86. 997 11. 645 1. 00 16.65 5379 0 ARG B 474 4. 379 86. 478 12. 727 1. 00 17.30 5380 N PHE B 475 3. 816 88. 244 11. 507 1. 00 17.03 5381 CA PHE B 475 3. 866 89. 167 12. 655 1. 00 16.93 5382 CB PHE B 475 5. 289 89. 741 12. 752 1. 00 16.12 5383 CG PHE B 475 5. 686 90. 631 11. 609 1. 00 16.12 5384 CD1 PHE B 475 5. 282 91. 971 11. 614 1. 00 15.11 5385 CE1 PHE B 475 5. 582 92. 806 10. 553 1. 00 13.82 5386 CZ PHE B 475 6. 293 92. 351 9. 488 1. 00 15.32 5387 CE2 PHE B 475 6. 731 90. 986 9. 456 1. 00 15.19 5388 CD2 PHE B 475 6. 388 90. 158 10. 518 1. 00 15.33 5389 C PHE B 475 2. 757 90. 195 12. 589 1. 00 16.68 5390 0 PHE B 475 2. 235 90. 447 11. 532 1. 00 16.15 5391 N VAL B 476 2. 427 90. 697 13. 803 1. 00 17.03 5392 CA VAL B 476 1. 312 91. 703 13. 851 1. 00 17.65 5393 CB VAL B 476 0. 376 91. 484 15. 033 1. 00 17.23 5394 CG1 VAL B 476-0.286 90. 109 15. 089 1.00 16.81 5395 CG2 VAL B 476 1. 005 91. 750 16. 375 1. 00 18.49 5396 C VAL B 476 2.077 93.038 13.952 1. 00 18.08 5397 0 VAL B 476 1. 524 93. 976 13. 453 1. 00 18.33 5398 N ALA B 477 3. 266 93. 047 14. 570 1. 00 18.03 5399 CA ALA B 477 3. 934 94. 399 14. 650 1. 00 18.71 5400 CB ALA B 477 3. 783 94. 907 16. 080 1. 00 18.54 5401 C ALA B 477 5. 356 94. 398 14. 217 1. 00 20.21 5402 0 ALA B 477 6. 115 93. 505 14. 580 1. 00 19.39 5403 N PRO B 478 5. 722 95. 447 13. 460 1. 00 22.08 5404 CA PRO B 478 7. 046 95. 615 12. 960 1. 00 23.44 5405PRO B 478 6. 997 96. 682 11. 860 1. 00 22.85 5406PRO B 478 5. 874 97. 562 12. 369 1. 00 22.30 5407 CD PRO B 478 4. 876 96. 577 13. 013 1. 00 21.83 5408 C PRO B 478 8. 158 95. 741 13. 922 1. 00 25.35 5409 O PRO B 478 9. 278 95. 422 13. 351 1. 00 25.84 5410 N GLY B 479 8. 097 96. 079 15. 202 1. 00 26.57 5411 CA GLY B 479 9. 468 96. 086 15. 869 1. 00 27.99 5412 C GLY B 479 9. 488 95. 483 17. 248 1. 00 29.01 5413 0 GLY B 479 8. 512 94. 925 17. 800 1. 00 29.40 5414 N GLU B 480 10. 658 95. 692 17. 845 1. 00 29.56 5415 CA GLU B 480 11. 101 95. 237 19. 158 1. 00 29.65 5416GLU B 480 12. 329 94. 277 18. 768 1. 00 30.41 5417 CG GLU B 480 13. 302 95. 112 17. 930 1. 00 32.28 5418 CD GLU B 480 14. 407 94. 472 17. 173 1. 00 33.52 5419 OE1 GLU B 480 14. 396 93. 296 16. 853 1. 00 32.47 5420 OE2 GLU B 480 15. 285 95. 314 16. 822 1. 00 34.08 5421 C GLU B 480 11. 715 96. 315 20. 019 1. 00 29.79 54220GLU B 480 12. 325 97. 301 19. 569 1. 00 29.77 5423 N ARG B 481 11. 501 96. 184 21. 322 1. 00 30.23 5424 CA ARG B 481 12. 078 97. 112 22. 327 1. 00 30.70 5425ARG B 481 11. 442 97. 136 23. 635 1. 00 33.62 5426ARG B 481 9. 949'97. 424 23. 785 1. 00 37.04 5427 CD ARG B 481 9. 681 97. 311 25. 293 1. 00 40.92 5428 NE ARG B 481 10. 570 96. 212 25. 742 1. 00 43.94 5429 CZ ARG B 481 10. 580 95. 543 26. 866 1. 00 45.59 5430 NH1 ARG B 481 9. 690 95. 660 27. 859 1. 00 46.60 5431 NH2 ARG B 481 11. 624 94. 729 27. 115 1. 00 46.39 5432 C ARG B 481 13. 543 96. 617 22. 347 1. 00 30.48 5433 0 ARG B 481 13. 836 95. 683 21. 588 1. 00 30.71 5434 N PRO B 482 14. 379 97. 241 23. 131 1. 00 30.22 5435 CA PRO B 482 15. 790 96. 912 23. 207 1. 00 29.45 5436PRO B 482 16. 453 98. 175 23. 750 1. 00 29.84 5437 CG PRO B 482 15. 363 99. 108 24. 191 1. 00 30.16 5438 CD PRO B 482 14. 050 98. 361 24. 035 1. 00 30.49 5439 C PRO B 482 16. 120 95. 729 24. 107 1. 00 28. 56 5440 O PRO B 482 15. 659 95. 685 25. 262 1. 00 28.49 5441 N SER B 483 16. 975 94. 847 23. 530 1. 00 26.92 5442 CA SER B 483 17. 423 93. 691 24. 340 1. 00 25.68 5443 CB SER B 483 18. 163 92. 727 23. 432 1. 00 24. 02 5444 OG SER B 483 19. 167 93. 452 22. 800 1. 00 22.90 5445 C SER B 483 18. 373 94. 183 25. 453 1. 00 25.56 5446 0 SER B 483 18. 816 95. 320 25. 519 1. 00 25.48 5447 N GLY B 484 18. 604 93. 282 26. 403 1. 00 25.28 5448 CA GLY B 484 19. 434 93. 406 27. 524 1. 00 24.85 5449 C GLY B 484 19. 085 93. 949 28. 837 1. 00 23.96 5450 O GLY B 484 20. 035 94. 295 29. 580 1. 00 23.58 5451 N MET B 485 17. 831 94. 068 29. 221 1. 00 24.33 5452 CA MET B 48517. 38294. 58630. 4861. 00 24.10 5453 CB MET B 485 16. 729 95. 937 30. 435 1. 00 29.43 5454 CG MET B 485 17. 187 97. 125 29. 850 1. 00 34. 37 5455 SD MET B 485 16. 936 97. 738 28. 196 1. 00 39. 17 5456 CE MET B 485 15. 247 98. 370 28. 301 1. 00 38. 54 5457 C MET B 485 16. 503 93. 526 31. 173 1. 00 22. 59 5458 O MET B 485 15. 986 92. 577 30. 506 1. 00 22. 70 5459 N PHE B 486 16. 364 93. 646 32. 485 1. 00 19. 85 5460 CA PHE B 486 15. 514 92. 768 33. 275 1. 00 18. 08 5461 CB PHE B 486 15. 913 91. 351 33. 542 1. 00 15. 40 5462 CG PHE B 486 17. 134 91. 164 34. 438 1. 00 12. 44 5463 CD1 PHE B 486 18. 392 91. 213 33. 932 1. 00 12. 66 5464 CD2 PHE B 486 16. 982 90. 957 35. 775 1. 00 11. 51 5465 CE1 PHE B 486 19. 496 91. 016 34. 727 1. 00 10. 72 5466 CE2 PHE B 486 18. 047 90. 760 36. 655 1. 00 11. 37 5467 CZ PHE B 486 19. 357 90. 767 36. 056 1. 00 10. 67 5468 C PHE B 486 15. 085 93. 577 34. 511 1. 00 17. 76 5469 0 PHE B 486 15. 839 94. 475 34. 915 1. 00 17. 26 5470 N ASP B 487 13. 896 93. 241 35. 029 1. 00 16. 09 5471 CA ASP B 487 13. 288 93. 822 36. 150 1. 00 15. 27 5472 CB ASP B 487 11. 720 93. 755 35. 980 1. 00 15. 73 5473 CG ASP B 487 10. 945 94. 683 36. 854 1. 00 15. 82 5474 OD1 ASP B 487 10. 307 94. 461 37. 902 1. 00 16. 19 5475 OD2 ASP B 487 11. 051 95. 906 36. 548 1. 00 16. 53 5476 C ASP B 487 13. 825 93. 441 37. 499 1. 00 14. 99 5477 0 ASP B 487 14. 118 92. 297 37. 882 1. 00 14. 78 5478 N SER B 488 13. 857 94. 443 38. 378 1. 00 14. 23 5479 CA SER B 488 14. 223 94. 354 39. 776 1. 00 13. 36 5480 CB SER B 488 13. 895 95. 597 40. 590 1. 00 8. 42 5481 OG SER B 488 14. 145 95. 403 41. 962 1. 00 5. 81 5482 C SER B 488 13. 368 93. 243 40. 424 1. 00 13. 82 5483 0 SER B 48 13. 759 92. 43 41. 474 1. 00 13. 56 5484 N SER B 489 12. 191 92. 966 39. 849 1. 00 15. 20 5485 CA SER B 489 11. 354 91. 872 40. 484 1. 00 14. 77 5486 CB SER B 489 9. 963 91. 829 39. 908 1. 00 14. 89 5487 OG SER B 489 10. 067 91. 612 38. 486 1. 00 16. 57 5488 C SER B 489 12. 048 90. 548 40. 343 1. 00 14. 62 5489 0 SER B 489 11. 770 89. 563 41. 109 1. 00 14. 51 5490 N VAL B 490 12. 920 90. 375 39. 338 1. 00 13. 92 5491 CA VAL B 490 13. 689 89. 212 39. 116 1. 00 12. 31 5492 CB VAL B 490 14. 440 89. 155 37. 758 1. 00 11. 67 5493 CG1 VAL B 490 15. 227 87. 874 37. 685 1. 00 11. 42 5494 CG2 VAL B 490 13. 447 89. 146 36. 596 1. 00 12. 10 5495 C VAL B 490 14. 651 88. 864 40. 272 1. 00 11. 84 5496 O VAL B 490 14. 760 87. 669 40. 624 1. 00 10. 11 5497 N LEU B 491 15. 346 89. 834 40. 851 1. 00 9. 62 5498 CA LEU B 491 16. 243 89. 676 41. 984 1. 00 7. 78 5499 CB LEU B 491 16. 771 91. 176 42. 271 1. 00 4. 26 5500 CG LEU B 491 17. 455 91. 697 41. 098 1. 00 4. 78 5501 CD1 LEU B 491 18. 003 93. 143 41. 480 1. 00 2. 18 5502 CD2 LEU B 491 18. 741 90. 781 41. 017 1. 00 3. 42 5503 C LEU B 491 15. 521 89. 277 43. 244 1. 00 8. 50 5504 O 1EU B 491 15. 887 88. 560 44. 173 1. 00 8. 44 5505 N CYS B 492 14. 256 89. 889 43. 298 1. 00 7. 58 5506 CA CYS B 492 13. 393 89. 556 44. 407 1. 00 7. 82 5507 CB CYS B 492 11. 972 90. 245 44. 225 1. 00 8. 14 5508 SG CYS B 492 10. 889 89. 453 45. 564 1. 00 12. 53 5509 C CYS B 492 13. 127 88. 046 44. 297 1. 00 9. 40 5510 O CYS B 492 12. 958 87. 458 45. 318 1. 00 11. 07 5511 N GLU B 493 12. 967 87. 554 43. 101 1. 00 11. 38 5512 CA GLU B 493 12. 724 86. 117 42. 857 1. 00 12. 58 5513 CB GLU B 493 12. 276 85. 810 41. 498 1. 00 15. 58 5514 CG GLU B 493 11. 078 86. 408 40. 815 1. 00 17. 69 5515 CD GLU B 493 10. 904 85. 623 39. 526 1. 00 19. 65 5516 OE1 GLU B 493 11. 382 86. 040 38. 507 1. 00 16. 78 5517 OE2 GLU B 493 10. 416 84. 463 39. 689 1. 00 23. 68 5518 C GLU B 493 13. 976 85. 279 43. 114 1. 00 13. 17 55190GLU B 493 13. 820 84. 091 43. 487 1. 00 14. 67 5520 N CYS B 494 15. 143 85. 788 42. 905 1. 00 13. 49 5521 CA CYS B 494 16. 441 85. 111 43. 225 1. 00 12. 59 5522 CB CYS B 494 17. 591 85. 939 42. 713 1. 00 11. 96 5523 SG CYS B 494 17. 717 85. 962 40. 896 1. 00 14. 69 5524 C CYS B 494 16. 503 84. 855 44. 720 1. 00 12. 62 5525 O CYS B 494 16. 889 83. 750 45. 192 1. 00 13. 87 5526 N TYR B 495 16. 296 85. 894 45. 516 1. 00 11. 97 5527 CA TYR B 495 16. 226 85. 811 46. 961 1. 00 11. 82 5528 CB TYR B 495 16. 110 87. 130 47. 730 1. 00 10. 44 5529 CG TYR B 495 17. 331 87. 983 47. 526 1. 00 8. 90 5530 CD1 TYR B 495 17. 481 88. 839 46. 469 1. 00 8. 68 5531 CE1 TYR B 495 18. 550 89. 712 46. 353 1. 00 7. 77 5532 CD2 TYR B 495 18. 435 87. 795 48. 383 1. 00 9. 82 5533 CE2 TYR B 495 19. 599 88. 567 48. 192 1. 00 8. 36 5534 CZ TYR B 495 19. 673 89. 466 47. 167 1. 00 9. 53 5535 OH TYR B 495 20. 817 90. 174 47. 015 1. 00 8. 75 5536 C. TYR B 495 15. 162 84. 784 47. 340 1. 00 12. 65 5537 O TYR B 495 15. 414 83. 960 48. 250 1. 00 12. 68 5538 N ASP B 496 14. 010 84. 833 46. 690 1. 00 13. 49 5539 CA ASP B 496 12. 963 83. 813 47. 074 1. 00 15. 45 5540ASP B 496 11. 706 84. 180 46. 318 1. 00 16. 21 5541 CG ASP B 496 10. 435 83. 590 46. 802 1. 00 15. 60 5542 OD1 ASP B 496 9. 710 84. 385 47. 438 1. 00 15. 97 5543 OD2 ASP B 496 10. 119 82. 411 46. 453 1. 00 14. 22 5544 C ASP B 496 13. 462 82. 415 46. 850 1. 00 16. 90 5545 O ASP B 496 13. 220 81. 558 47. 750 1. 00 18. 23 5546 N ALA B 497 14. 086 82. 094 45. 719 1. 00 16. 34 5547 CA ALA B 497 14. 551 80. 740 45. 388 1. 00 15. 74 5548 CB ALA B 497 14. 932 80. 649 43. 917 1. 00 14. 34 5549 C ALA B 497 15. 738 80. 325 46. 251 1. 00 15. 97 5550 O ALA B 497 15. 773 79. 166 46. 725 1. 00 15. 95 5551 N GLY B 498 16. 661 81. 256 46. 489 1. 00 15. 15 5552 CA GLY B 498 17. 776 80. 854 47. 370 1. 00 16. 90 5553 C GLY B 498 17. 155 80. 359 48. 677 1. 00 18. 28 5554 O GLY B 498 17. 505 79. 286 49. 181 1. 00 19. 90 5555 N CYS B 499 16. 250 81. 144 49. 251 1. 00 18. 11 5556 CA CYS B 499 15. 624 80. 911 50. 529 1. 00 18. 54 5557 CB CYS B 499 14. 898 82. 072 51. 142 1. 00 14. 81 5558 SG CYS B 499 15. 800 83. 496 51. 667 1. 00 16. 18 5559 C CYS B 499 14. 757 79. 641 50. 614 1. 00 19. 48 5560 O CYS B 499 14. 801 78. 942 51. 624 1. 00 19. 85 5561 N ALA B 500 13. 955 79. 476 49. 592 1. 00 20. 45 5562 CA ALA B 500 13. 022 78. 405 49. 432 1. 00 20. 97 5563 CB ALA B 500 11. 968 78. 882 48. 377 1. 00 20. 59 5564 C ALA B 500 13. 636 77. 122 48. 925 1. 00 21. 93 5565 O ALA B 500 13. 367 76. 010 49. 421 1. 00 21. 99 5566 N TRP B 501 14. 406 77. 261 47. 852 1. 00 22. 22 5567 CA TRP B 501 14. 979 76. 093 47. 181 1. 00 22. 57 5568 CB TRP B 501 14. 690 76. 182 45. 693 1. 00 21. 47 5569 CG TRP B 501 13. 320 76. 036 45. 246 1. 00 22. 11 5570 CD2 TRP B 501 12. 593 74. 779 45. 249 1. 00 22. 85 5571 CE2 TRP B 501 11. 308 75. 034 44. 748 1. 00 22. 46 5572 CE3 TRP B 501 12. 938 73. 500 45. 678 1. 00 23. 07 5573 CD1 TRP B 501 12. 428 76. 977 44. 760 1. 00 21. 39 5574 NE1 TRP B 501 11. 244 76. 372 44. 432 1. 00 23. 20 5575 CZ2 TRP B 501 10. 395 74. 024 44. 609 1. 00 23. 39 5576 CZ3 TRP B 501 12. 004 72. 490 45. 552 1. 00 22. 83 5577 CH2 TRP B 501 10. 738 72. 775 45. 040 1. 00 22. 61 5578 C TRP B 501 16. 380 75. 656 47. 411 1. 00 22. 61 5579 O TRP B 501 16. 583 74. 434 47. 627 1. 00 23. 61 5580 N TYR B 502 17. 357 76. 502 47. 360 1. 00 22. 45 5581 CA TYR B 502 18. 780 76. 199 47. 440 1. 00 22. 05 5582 CB TYR B 502 19. 479 77. 039 46. 323 1. 00 20. 82 5583 CG TYR B 502 18. 738 76. 718 45. 054 1. 00 20. 56 5584 CD1 TYR B 502 18. 543 75. 395 44. 656 1. 00 19. 66 5585 CE1 TYR B 502,17.836 75. 104 43. 475 1. 00 19.33 5586 CD2 TYR B 502 18. 204 77. 751 44. 273 1. 00 20. 76 5587 CE2 TYR B 502 17. 540 77. 441 43. 094 1. 00 20. 36 5588 CZ TYR B 502 17. 412 76. 146 42. 677 1. 00 19. 34 5589 OH TYR B 502 16. 714 75. 940 41. 529 1. 00 20. 57 5590 C TYR B 502 19. 503 76. 364 48. 690 1. 00 23. 03 5591 O TYR B 502 20. 755 76. 158 48. 774 1. 00 23. 16 5592 N GLU B 50318. 76476. 74549. 7151. 0023. 57 5593 CA GLU B 503 19. 311 76. 935 51. 027 1. 00 23. 78 5594 CB GLU B 503 20. 085 75. 650 51. 444 1. 00 26. 97 5595 CG GLU B 503 19.254 74.472 51.927 1.00 28. 62 5596 CD GLU B 503 18. 484 74. 924 53. 143 1. 00 29. 43 5597 OE1 GLU B 503 18. 899 74. 443 54. 167 1. 00 30. 65 5598 OE2 GLU B 503 17. 574 75. 718 53. 073 1. 00 31. 85 5599 C GLU B 503 20. 302 78. 038 51. 183 1. 00 23. 05 56000 GLU B 503 21. 171 77. 781 52. 025 1. 00 23. 61 5601 N LEU B 504 20.196 79.138 50.484 1.00 21. 85 5602 CA LEU B 504 21.209 80.243 50.605 1.00 20. 07 5603 CB LEU B 504 21. 124 80. 822 49. 126 1. 00 17. 69 5604 CG LEU B 504 21. 608 79. 889 48. 057 1. 00 18. 18 5605 CD1 LEU B 504 21. 458 80. 456 46. 673 1. 00 17. 31 5606 CD2 LEU B 504 23. 114 79. 679 48. 366 1. 00 16. 55 5607 C LEU B 504 20. 647 81. 324 51. 525 1. 00 20. 20 56080 LEU B 504 19. 456 81. 554 51. 334 1. 00 19. 67 5609 N THR B 505 21.424 81.929 52.391 1.00 20. 18 5610 CA THR B 505 20. 914 83. 030 53. 225 1. 00 19. 47 5611 CB THR B 505 21. 924 83. 348 54. 409 1. 00 20. 54 5612 OG1 THR B 505 23. 262 83. 481 53. 823 1. 00 22. 11 5613 CG2 THR B 505 22. 035 82. 332 55. 542 1. 00 21. 88 5614 C THR B 505 20. 887 84. 238 52. 257 1. 00 18. 47 5615 O THR B 505 21. 507 84. 215 51. 202 1. 00 18. 21 5616 N PRO B 506 20. 100 85. 230 52. 599 1. 00 17. 99 5617 CD PRO B 506 19. 203 85. 338 53. 745 1. 00 17. 47 5618 CA PRO B 506 20. 045 86. 455 51. 722 1. 00 17. 35 5619 CB PRO B 506 19. 276 87. 403 52. 655 1. 00 17. 54 5620 CG PRO B 506 18. 261 86. 443 53. 306 1. 00 17. 74 5621 C PRO B 506 21. 480 86. 909 51. 461 1. 00 17. 25 5622 O PRO B 506 21. 859 87. 312 50. 307 1. 00 17. 40 5623 N ALA B 507 22.324 86.823 52.500 1.00 16. 49 5624 CA ALA B 507 23. 720 87. 258 52. 378 1. 00 16. 31 5625 CB ALA B 507 24.371 87.574 53.704 1.00 14. 63 5626 C ALA B 507 24. 486 86. 394 51. 400 1. 00 15. 65 5627 O ALA B 507 25. 312 86. 964 50. 626 1. 00 15. 06 5628 N GLU B 508 24. 173 85. 113 51. 289 1. 00 15. 90 5629 CA GLU B 508 24. 868 84. 241 50. 305 1. 00 16. 30 5630 CB GLU B 508 24.874 82.753 50.761 1.00 18. 50 5631 CG GLU B 508 25. 533 82. 526 52. 108 1. 00 22. 36 5632 CD GLU B 508 25. 402 81. 161 52. 746 1. 00 25. 71 5633 OE1 GLU B 508 24. 367 80. 829 53. 292 1. 00 26. 64 5634 OE2 GLU B 508 26. 354 80. 395 52. 641 1. 00 26. 84 5635 C GLU B 508 24. 339 84. 447 48. 931 1. 00 15. 53 56360 GLU B 508 25. 068 84. 428 47. 895 1. 00 15. 70 5637 N THR B 509 23. 024 84. 756 48. 790 1. 00 14. 21 5638 CA THR B 509 22. 448 84. 997 47. 498 1. 00 12. 34 5639 CB THR B 509 20. 882 85. 186 47. 414 1. 00 11. 32 5640 OG1 THR B 509 20.223 84.033 47.987 1.00 10. 07 5641 CG2 THR B 509 20. 409 85. 448 46. 003 1. 00 12. 16 5642 C THR B 509 23. 132 86. 271 46. 990 1. 00 11. 98 5643 0 THR B 509 23. 439 86. 365 45. 853 1. 00 12. 03 5644 N THR B 510 23. 263 87. 257 47. 853 1. 00 13. 08 5645 CA THR B 510 23. 898 88. 532 47. 441 1. 00 12. 34 5646 CB THR B 510 23. 927 89. 563 48. 594 1. 00 13. 05 5647 OG1 THR B 510 22. 602 90. 017 48. 966 1. 00 13. 99 5648 CG2 THR B 510 24.809 90.794 48.215 1.00 13. 57 5649 C THR B 510 25. 170 88. 374 46. 696 1. 00 12. 54 5650 O THR B 510 25. 470 89. 085 45. 658 1. 00 13. 35 5651 N VAL B 511 26. 134 87. 619 47. 203 1. 00 12. 60 5652 CA VAL B 511 27.451 87.325 46.682 1.00 12. 84 5653 CB VAL B 511 28. 275 86. 414 47. 614 1. 00 12. 94 5654 CG1 VAL B 511 29. 630 85. 963 46. 989 1. 00 12. 29 5655 CG2 VAL B 511 28. 600 87. 090 48. 936 1. 00 12. 23 5656 C VAL B 511 27. 456 86. 817 45. 254 1. 00 13. 40 56570 VAL B 511 28. 313 87. 259 44. 420 1. 00 13. 73 5658 N ARG B 512 26. 549 85. 897 45. 024 1. 00 13. 42 5659 CA ARG B 512 26.368 85.282 43.708 1.00 13. 60 5660 CB ARG B 512 25. 459 84. 086 43. 826 1. 00 13. 81 5661 CG ARG B 512 25.981 83.149 44.942 1.00 16. 31 5662 CD ARG B 512 25. 283 81. 834 44. 844 1. 00 18. 56 5663 NE ARG B 512 25. 922 80. 917 45. 888 1. 00 20. 20 5664 CZ ARG B 512 25. 694 79. 616 45. 772 1. 00 19. 65 5665 NH1 ARG B 512 24. 947 79. 206 44. 763 1. 00 19. 32 5666 NH2 ARG B 512 26. 264 78. 790 46. 656 1. 00 21. 78 5667 C ARG B 512 25. 751 86. 272 42. 745 1. 00 12. 90 5668 0 ARG B 512 26. 151 86. 313 41. 580 1. 00 13. 22 5669 N LEU B 513 24.736 87.071 43.224 1.00 11. 59 5670 CA LEU B 513 24. 149 88. 049 42. 273 1. 00 10. 71 5671 CB LEU B 513 22. 768 88. 456 42. 811 1. 00 8. 26 5672 CG LEU B 513 21. 724 87. 397 42. 987 1. 00 9. 17 5673 CD1 LEU B 513 20. 397 87. 982 43. 594 1. 00 7. 50 5674 CD2 LEU B 513 21. 354 86. 808 41. 641 1. 00 4. 87 5675 C LEU B 513 25. 147 89. 175 42. 043 1. 00 10. 69 56760 LEU B 513 25. 241 89. 768 40. 938 1. 00 11. 59 5677 N ARG B 514 25. 926 89. 497 43. 064 1. 00 10. 62 5678 CA ARG B 514 26. 978 90. 552 42. 833 1. 00 11. 66 5679 CB ARG B 514 27. 751 90. 791 44. 153 1. 00 13. 79 5680 CG ARG B 514 28. 826 91. 875 44. 085 1. 00 15. 28 5681 CD ARG B 514 28. 242 93. 104 43. 499 1. 00 17. 37 5682 NE ARG B 514 27. 215 93. 743 44. 307 1. 00 18. 94 5683 CZ ARG B 514 26. 386 94. 665 43. 805 1. 00 21. 34 5684 NH1 ARG B 514 26. 340 94. 995 42. 513 1. 00 21. 54 5685 NH2 ARG B 514 25. 775 95. 516 44. 643 1. 00 22. 74 5686 C ARG B 514 27. 920 90. 078 41. 729 1. 00 11. 86 5687 0 ARG B 514 28. 349 90. 863 40. 849 1. 00 12. 19 5688 N ALA B 515 28. 237 88. 823 41. 618 1. 00 12. 42 5689 CA ALA B 515 29. 192 88. 256 40. 591 1. 00 12. 88 5690 CB ALA B 515 29. 566 86. 851 40. 941 1. 00 13. 68 5691 C ALA B 515 28. 603 88. 425 39. 233 1. 00 13. 12 5692 O ALA B 515 29. 179 88. 908 38. 260 1. 00 13. 00 5693 N TYR B 516 27. 282 88. 129 39. 211 1. 00 14. 63 5694 CA TYR B 516 26. 434 88. 262 38. 045 1. 00 14. 74 5695 CB TYR B 516 25. 017 87. 610 38. 278 1. 00 15. 00 5696 CG TYR B 516 24. 165 87. 685 37. 042 1. 00 14. 87 5697 CD1 TYR B 516 23. 999 86. 580 36. 190 1. 00 13. 94 5698 CE1 TYR B 516 23. 280 86. 694 35. 002 1. 00 12. 62 5699 CD2 TYR B 516 23. 597 88. 898 36. 630 1. 00 14. 99 5700 CE2 TYR B 516 22. 904 89. 002 35. 428 1. 00 14. 70 5701 CZ TYR B 516 22. 744 87. 876 34. 629 1. 00 13. 39 5702 OH TYR B 516 22. 003 88. 029 33. 463 1. 00 12. 94 5703 C TYR B 516 26. 391 89. 675 37. 522 1. 00 15. 71 5704 O TYR B 516 26. 626 89. 994 36. 316 1. 00 14. 23 5705 N MET B 517 26. 030 90. 582 38. 417 1. 00 17. 40 5706 CA MET B 517 25. 805 92. 008 38. 204 1. 00 17. 11 5707MET B 517 25. 209 92. 537 39. 510 1. 00 20. 14 5708MET B 517 23. 893 92. 069 39. 925 1. 00 21. 48 5709MET B 517 22. 498 92. 898 39. 122 1. 00 27. 54 5710 CE MET B 517 22. 554 94. 465 40. 015 1. 00 26. 53 5711 C MET B 517 26. 983 92. 802 37. 759 1. 00 17. 74 57120MET B 517 26. 841 93. 826 37. 023 1. 00 18. 09 5713 N ASN B 518 28. 158 92. 460 38. 202 1. 00 16. 86 5714 CA ASN B 518 29. 426 93. 004 37. 978 1. 00 17. 38 5715 CB ASN B 518 30. 318 93. 234 39. 260 1. 00 17. 69 5716 CG ASN B 518 29. 737 94. 305 40. 156 1. 00 17. 43 5717 OD1 ASN B 518 28. 550 94. 733 39. 979 1. 00 16. 37 5718 ND2 ASN B 518 30. 414 94. 720 41. 209 1. 00 16. 97 5719 C ASN B 518 30. 245 92. 419 36. 835 1. 00 16. 67 57200ASN B 518 31. 207 93. 135 36. 486 1. 00 17. 51 5721 N THR B 519 29. 878 91. 352 36. 201 1. 00 15. 22 5722 CA THR B 519 30. 685 90. 760 35. 072 1. 00 14. 13 5723 CB THR B 519 30. 424 89. 165 34. 997 1. 00 10. 91 5724 OG1 THR B 519 30. 808 88. 642 36. 300 1. 00 9. 65 5725 CG2 THR B 519 31. 213 88. 443 33. 917 1. 00 10. 68 5726 C THR B 519 30. 121 91. 412 33. 804 1. 00 15. 64 5727 O THR B 519 28. 873 91. 480 33. 653 1. 00 15. 46 5728 N PRO B 520 31. 009 91. 901 32. 944 1. 00 15. 81 5729 CD PRO B 520 32. 478 91. 935 33. 141 1. 00 16. 31 5730 CA PRO B 520 30. 633 92. 584 31. 739 1. 00 16. 35 5731 CB PRO B 520 31. 949 93. 173 31. 171 1. 00 16. 07 5732PRO B 520 32. 864 93. 208 32. 392 1. 00 16. 46 5733 C PRO B 520 29. 933 91. 700 30. 749 1. 00 15. 95 5734 O PRO B 520 30. 075 90. 465 30. 747 1. 00 17. 66 5735 N GLY B 521 29. 107 92. 292 29. 911 1. 00 14. 86 5736 CA GLY B 521 28. 349 91. 769 28. 867 1. 00 14. 37 5737 C GLY B 521 27. 189 90. 879 29. 099 1. 00 14. 00 5738 0 GLY B 521 26. 931 90. 023 28. 223 1. 00 15. 11 5739 N LEU B 522 26. 488 91. 011 30. 218 1. 00 12.49 5740 CA LEU B 522 25. 345 90. 245 30. 588 1. 00 12.21 5741 CB LEU B 522 25. 518 89. 477 31. 918 1. 00 8.70 5742LEU B 522 26. 564 88. 345 31. 977 1. 00 9.22 5743 CD1 LEU B 522 26. 771 87. 920 33. 462 1. 00 7.79 5744 CD2 LEU B 522 25. 955 87. 097 31. 334 1. 00 7.26 5745 C LEU B 522 24. 134 91. 273 30. 689 1. 00 12.51 57460LEU B 522 24. 383 92. 459 30. 860 1. 00 12.99 5747 N PRO B 523 22. 990 90. 728 30. 627 1. 00 12.54 5748 CD PRO B 523 22. 701 89. 280 30. 349 1. 00 12.44 5749 CA PRO B 523 21. 739 91. 532 30. 758 1. 00 12.97 5750PRO B 523 20. 632 90. 480 30. 797 1. 00 12.80 5751 CG PRO B 523 21. 209 89. 269 30. 157 1. 00 13.02 5752 C PRO B 523 21. 900 92. 290 32. 044 1. 00 13.95 5753 0 PRO B 523 22. 485 91. 785 33. 027 1. 00 15.91 5754 N VAL B 524 21. 250 93. 435 32. 190 1. 00 14.00 5755 CA VAL B 524 21. 353 94. 308 33. 308 1. 00 13.04 5756VAL B 524 22. 177 95. 554 32. 905 1. 00 13.22 5757 CG1 VAL B 524 23. 656 95. 264 32. 668 1. 00 13.19 5758 CG2 VAL B 524 21. 646 96. 205 31. 639 1. 00 14.39 5759 C VAL B 524 20. 072 94. 664 34. 009 1. 00 12.29 5760 0 VAL B 524 19. 038 94. 826 33. 322 1. 00 12.03 5761 N CYS B 525 20. 272 94. 925 35. 283 1. 00 12.34 5762 CA CYS B 525 19. 103 95. 306 36. 117 1. 00 13.19 5763 CB CYS B 525 18. 758 93. 988 36. 990 1. 00 13.68 5764 SG CYS B 525 17. 358 94. 454 37. 983 1. 00 16.53 5765 C CYS B 525 19. 440 96. 393 37. 111 1. 00 13.99 5766 0 CYS B 525 20. 601 96. 568 37. 454 1. 00 13.29 5767 N GLN B 526 18. 420 97. 127 37. 597 1. 00 13.08 5768 CA GLN B 526 18. 729 98. 167 38. 626 1. 00 14.33 5769 CB GLN B 526 17. 473 98. 965 39. 020 1. 00 13.18 5770 CG GLN B 526 17. 030 99. 813 37. 825 1. 00 10.30 5771 CD GLN B 526 17. 935 100. 910 37. 374 1. 00 9.92 5772 OE1 GLN B 526 18. 115 101. 162 36. 168 1. 00 10.98 5773 NE2 GLN B 526 18. 445 101. 679 38. 273 1. 00 9.45 5774 C GLN B 526 19. 254 97. 362 39. 784 1. 00 15.82 5775 0 GLN B 526 18. 724 96. 255 40. 080 1. 00 17.76 5776 N ASP B 527 20. 257 97. 895 40. 432 1. 00 16.22 5777 CA ASP B 527 20. 889 97. 183 41. 542 1. 00 16.34 5778 CB ASP B 527 22. 383 97. 520 41. 640 1. 00 18.72 5779 CG ASP B 527 23. 105 96. 877 42. 794 1. 00 22.19 5780 OD1 ASP B 527 24. 366 96. 956 42. 898 1. 00 22.73 5781 OD2 ASP B 527 22. 482 96. 206 43. 643 1. 00 22.33 5782 C ASP B 527 20. 175 97. 439 42. 846 1. 00 15.03 5783 0 ASP B 527 20. 491 98. 434 43. 547 1. 00 15.00 5784 N HIS B 528 19. 414 96. 476 43. 248 1. 00 14.07 5785 CA HIS B 528 18.635 96.475 44.452 1. 00 13.48 5786HIS B 528 17. 111 96. 465 44. 258 1. 00 12.26 5787 CG HIS B 528 16. 590 97. 606 43. 403 1. 00 11.56 5788 CD2 HIS B 528 16. 939 98. 919 43. 451 1. 00 11.25 5789 ND1 HIS B 528 15. 601 97. 519 42. 473 1. 00 8.83 5790 CE1 HIS B 528 15. 552 98. 724 41. 862 1. 00 10.48 5791 NE2 HIS B 528 16. 291 99. 537 42. 453 1. 00 9.64 5792 C HIS B 528 19. 036 95. 269 45. 326 1. 00 13.10 5793 O HIS B 528 18. 210 94. 933 46. 134 1. 00 13.92 5794 N LEU B 529 20. 186 94. 694 45. 199 1. 00 12.82 5795 CA LEU B 529 20. 649 93. 578 45. 998 1. 00 12.35 5796 CB LEU B 529 22. 107 93. 216 45. 583 1. 00 9. 37 5797 CG LEU B 529 22. 537 92. 900 44. 200 1. 00 6. 91 5798 CD1 LEU B 529 24. 049 92. 425 44. 316 1. 00 7. 04 5799 CD2 LEU B 529 21. 798 91. 595 43. 725 1. 00 6. 15 5800 C LEU B 529 20.546 93.880 47.487 1.00 12. 81 58010 LEU B 529 19. 952 93. 100 48. 291 1. 00 12. 29 5802 N GLU B 530 21. 102 95. 005 47. 933 1. 00 12. 74 5803 CA GLU B 530 21. 032 95. 331 49. 400 1. 00 14. 22 5804 CB GLU B 530 21. 897 96. 606 49. 684 1. 00 19. 20 5805 CG GLU B 530 22. 036 96. 881 51. 196 1. 00 24. 47 5806 CD GLU B 530 23. 125 97. 849 51. 611 1. 00 28. 07 5807 OE1 GLU B 530 23. 316 98. 758 50. 777 1. 00 30. 51 5808 OE2 GLU B 530 23. 798 97. 730 52. 632 1. 00 28. 92 5809 C GLU B 530 19. 630 95. 532 49. 866 1. 00 13. 19 58100 GLU B 530 19. 187 95. 162 50. 987 1. 00 13. 48 5811 N PHE B 531 18. 805 96. 115 49. 010 1. 00 13. 47 5812 CA PHE B 531 17. 364 96. 312 49. 284 1. 00 12. 89 5813 CB PHE B 531 16. 617 97. 187 48. 254 1. 00 13. 03 5814 CG PHE B 531 15. 131 97. 130 48. 494 1. 00 13. 46 5815 CD1 PHE B 531 14. 570 97. 668 49. 630 1. 00 13. 74 5816 CD2 PHE B 531 14. 350 96. 285 47. 663 1. 00 12. 76 5817 CE1 PHE B 531 13. 198 97. 478 49. 863 1. 00 13. 77 5818 CE2 PHE B 531 13. 024 96. 112 47. 896 1. 00 12. 42 5819 CZ PHE B 531 12. 428 96. 700 49. 009 1. 00 12. 37 5820 C PHE B 531 16. 722 94. 922 49. 460 1. 00 13. 11 58210. PHE B 531 16. 263 94. 626 50. 557 1. 00 13. 29 5822 N TRP B 532 16. 675 94. 072 48. 455 1. 00 13. 99 5823 CA TRP B 532 16. 113 92. 724 48. 538 1. 00 13. 81 5824 CB TRP B 532 16. 055 92. 036 47. 149 1. 00 13. 63 5825 CG TRP B 532 15. 144 92. 674 46. 138 1. 00 11. 83 5826 CD2 TRP B 532 13. 710 92. 844 46. 320 1. 00 11. 49 5827 CE2 TRP B 532 13. 245 93. 615 45. 263 1. 00 11. 07 5828 CE3 TRP B 532 12. 816 92. 467 47. 335 1. 00 10. 54 5829 CD1 TRP B 532 15. 458 93. 380 45. 009 1. 00 10. 44 5830 NE1 TRP B 532 14. 269 93. 944 44. 443 1. 00 10. 95 5831 CZ2 TRP B 532 11. 861 93. 855 45. 093 1. 00 11. 63 5832 CZ3 TRP B 532 11. 502 92. 684 47. 181 1. 00 10. 08 5833 CH2 TRP B 532 11. 009 93. 415 46. 081 1. 00 8. 47 5834 C TRP B 532 16. 740 91. 864 49. 605 1. 00 14. 87 5835 0 TRP B 532 16. 047 91. 005 50. 259 1. 00 16. 03 5836 N GLU B 533 18. 028 91. 952 49. 867 1. 00 14. 49 5837 CA GLU B 533 18.666 91.143 50.927 1.00 14. 72 5838 CB GLU B 533 20. 129 91. 195 50. 954 1. 00 13. 48 5839 CG GLU B 533 20. 897 90. 494 52. 107 1. 00 14. 77 5840 CD GLU B 533 22. 344 90. 925 52. 097 1. 00 15. 50 5841 OE1 GLU B 533 22. 952 91. 273 51. 131 1. 00 16. 96 5842 OE2 GLU B 533 22. 883 90. 822 53. 197 1. 00 16. 53 5843 C GLU B 533 18. 077 91. 574 52. 262 1. 00 15. 01 58440 GLU B 533 17. 725 90. 709 53. 034 1. 00 15. 27 5845 N GLY B 534 18. 037 92. 864 52. 561 1. 00 15. 37 5846 CA GLY B 534 17. 441 93. 358 53. 828 1. 00 16. 06 5847 C GLY B 534 16. 044 92. 793 54. 128 1. 00 16. 55 5848 GLY B 534 15. 751 92. 337 55. 244 1. 00 16. 87 5849 N VAL B 535 15. 179 92. 776 53. 168 1. 00 16. 58 5850 CA VAL B 535 13. 809 92. 297 53. 188 1. 00 16. 27 5851 CB VAL B 535 13. 098 92. 381 51. 830 1. 00 15. 27 5852 CG1 VAL B 535 11. 716 91. 688 51. 870 1. 00 16. 10 5853 CG2 VAL B 535 13. 023 93. 723 51. 273 1. 00 15.85 5854 C VAL B 535 13.737 90.849 53.670 1. 00 16.01 5855 0 VAL B 535 13. 075 90. 619 54. 651 1. 00 16.49 5856 N PHE B 536 14. 284 89. 977 52. 825 1. 00 15.90 5857 CA PHE B 536 14. 290 88. 554 53. 151 1. 00 16.40 5858 CB PHE B 536 14. 826 87. 654 52. 009 1. 00 15.97 5859 CG PHE B 536 13.864 87.596 50.850 1. 00 14.01 5860 CD1 PHE B 536 13. 048 86. 498 50. 646 1. 00 15.04 5861 CD2 PHE B 536 13.777 88.691 49.991 1. 00 13.15 5862 CE1 PHE B 53612. 17486. 44449. 5981. 00 13.98 5863 CE2 PHE B 536 12. 916 88. 637 48. 901 1. 00 13.21 5864 CZ PHE B 536 12. 107 87. 519 48. 702 1. 00 12.38 5865 C PHE B 536 15. 064 88. 285 54. 422 1. 00 17.54 5866 O PHE B 536 14. 824 87. 256 55. 054 1. 00 18.23 5867 N THR B 537 16. 039 89. 136 54. 747 1. 00 17.73 5868 CA THR B 537 16. 831 88. 860 55. 980 1. 00 18.71 5869 CB THR B 537 18. 020 89. 862 56. 152 1. 00 18.02 5870 OG1 THR B 537 18.948 89.684 55.021 1. 00 17.18 5871 CG2 THR B 537 18. 718 89. 725 57. 520 1. 00 19.24 5872 C THR B 537 15. 832 88. 942 57. 164 1. 00 19.98 5873 0 THR B 537 15. 801 88. 155 58. 130 1. 00 19.74 5874 N GLY B 538 15. 002 89. 984 57. 029 1. 00 20. 13 5875 CA GLY B 538 13. 978 90. 231 58. 037 1. 00 20.89 5876 C GLY B 538 12. 815 89. 302 57. 974 1. 00 20.61 5877 O GLY B 538 11. 944 89. 484 58. 853 1. 00 21.22 5878 N LEU B 539 12. 720 88. 361 57. 088 1. 00 20.36 5879 CA LEU B 539 11. 630 87. 417 56. 982 1. 00 20.89 5880 CB LEU B 539 11.381 87.022 55.512 1. 00 18.46 5881 CG LEU B 539 10. 763 88. 104 54. 657 1. 00 17.10 5882 CD1 LEU B 539 10. 474 87. 630 53. 268 1. 00 16.75 5883 CD2 LEU B 539 9. 569 88. 678 55. 383 1. 00 16.55 5884 C LEU B 539 11. 863 86. 175 57. 816 1. 00 22.86 5885 O LEU B 539 12. 050 85. 110 57. 182 1. 00 23. 04 5886 N THR B 540 11. 736 86. 319 59. 118 1. 00 24.30 5887 CA THR B 540 12. 030 85. 215 60. 037 1. 00 26.25 5888 CB THR B 540 12.730 85.789 61.348 1. 00 27.24 5889 OG1 THR B 540 11. 664 86. 625 61. 950 1. 00 29.52 5890 CG2 THR B 540 13. 939 86. 675 61. 029 1. 00 28.16 5891 C THR B 540 10. 885 84. 334 60. 525 1. 00 27.22 5892 O THR B 540 9. 713 84. 679 60. 619 1. 00 26.74 5893 N HIS B 541 11. 340 83. 163 60. 933 1. 00 27.53 5894 CA HIS B 541 10.609 82.053 61.468 1. 00 28.23 5895 CB HIS B 541 10.145 82.194 62.910 1. 00 28.39 5896HIS B 541 11.186 82.465 63.917 1. 00 28.76 5897 CD2 HIS B 541 11.394 83.571 64.668 1. 00 29.34 5898 ND1 HIS B 541 12. 106 81. 550 64. 365 1. 00 29.41 5899 CE1 HIS B 541 12. 871 82. 081 65. 300 1. 00 28.69 5900 NE2 HIS B 541 12. 465 83. 316 65. 484 1. 00 29.72 5901 C HIS B 541 9. 369 81. 790 60. 615 1. 00 28.75 5902 0 HIS B 541 8. 256 81. 837 61. 153 1. 00 28.98 5903 N ILE B 542 9. 638 81. 557 59. 364 1. 00 29.59 5904 CA ILE B 542 8. 568 81. 227 58. 381 1. 00 29.84 5905 CB ILE B 542 9. 128 81. 121 56. 939 1. 00 29.15 5906 CG2 ILE B 542 10. 039 79. 867 56. 766 1. 00 30.44 5907 CG1 ILE B 542 7. 957 81. 007 55. 919 1. 00 28. 23 5908 CD1 ILE B 542 8. 432 80. 983 54. 442 1. 00 26.71 5909 C ILE B 542 8. 054 79. 857 58. 869 1. 00 30.44 5910 O ILE B 542 8. 761 79. 206 59. 640 1. 00 30.60 5911 N ASP B 543 6. 896 79. 484 58. 391 1. 00 31.02 5912 CA ASP B 543 6. 290 78. 189 58. 762 1. 00 31.78 5913 CB ASP B 543 4. 759 78. 378 58. 856 1. 00 33.48 5914 CG ASP B 543 4. 069 77. 053 59. 166 1. 00 34.91 5915 OD1 ASP B 543 4. 281 76. 471 60. 235 1. 00 35.58 5916 OD2 ASP B 543 3. 296 76. 596 58. 313 1. 00 36.06 5917 C ASP B 543 6. 715 77. 161 57. 726 1. 00 31.45 5918 0 ASP B 543 6. 494 77. 493 56. 538 1. 00 31.65 5919 N AZA B 544 7. 249 76. 034 58. 125 1. 00 31.39 5920 CA ALA B 544 7. 687 75. 037 57. 138 1. 00 31.90 5921 CB ALA B 544 8. 789 74. 190 57. 702 1. 00 31.93 5922 C ALA B 544 6. 611 74. 288 56. 416 1. 00 32.66 5923 O ALA B 544 6. 801 73. 762 55. 251 1. 00 32.94 5924 N HIS B 545 5. 431 74. 202 57. 012 1. 00 32.70 5925 CA HIS B 545 4. 298 73. 480 56. 375 1. 00 32.66 5926 CB HIS B 545 3. 158 73. 252 57. 375 1. 00 35.89 5927 CG HIS B 545 2. 000 72. 480 56. 842 1. 00 38.25 5928 ND1 HIS B 545 1. 747 71. 162 57. 116 1. 00 39.28 5929 CE1 HIS B 545 0. 632 70. 787 56. 496 1. 00 40.03 5930 NE2 HIS B 545 0. 173 71. 813 55. 792 1. 00 39.93 5931 CD2 HIS B 545 1. 002 72. 882 56. 013 1. 00 39.37 5932 C HIS B 545 3. 789 74. 333 55. 213 1. 00 32.04 5933 O HIS B 545 3. 412 73. 774 54. 162 1. 00 32.39 5934 N PHE B 546 3. 719 75. 658 55. 447 1. 00 30.90 5935 CA PHE B 546 3.251 76.582 54.422 1. 00 29.57 5936 CB PHE B 546 2. 783 77. 936 54. 859 1. 00 29.04 5937 CG PHE B 546 -1.649 77.954 55.831 1. 00 28.87 5938 CD1 PHE B 546 0. 629 76. 993 55. 712 1. 00 29.13 5939 CD2 PHE B 546 1. 520 78. 969 56. 757 1. 00 29.36 5940 CE1 PHE B 546-0. 430 76. 973 56. 601 1. 00 28.42 5941 CE2 PHE B 546 0. 433 78. 993 57. 643 1. 00 28.93 5942 CZ PHE B 546-0. 538 77. 973 57. 539 1. 00 28.59 5943 C PHE B 546 4. 256 76. 672 53. 277 1. 00 29.02 5944 O PHE B 546 3. 814 76. 845 52. 143 1. 00 29.20 5945 N LEU B 547 5. 545 76. 596 53. 600 1. 00 28.45 5946 CA LEU B 547 6. 558 76. 689 52. 556 1. 00 27.46 5947 CB LEU B 547 7. 939 76. 947 53. 157 1. 00 24.24 5948 CG LEU B 547 9. 098 77. 023 52. 120 1. 00 20.60 5949 CD1 LEU B 547 8.871 78.160 51.166 1. 00 19.97 5950 CD2 LEU B 547 10.379 77.116 52.879 1. 00 19.04 5951 C LEU B 547 6. 514 75. 539 51. 573 1. 00 27.83 5952 0 LEU B 547 6. 685 75. 753 50. 360 1. 00 27.81 5953 N SER B 548 6. 273 74. 353 52. 096 1. 00 28.69 5954 CA SER B 548 6. 274 73. 104 51. 294 1. 00 28.83 5955 CB SER B 548 6. 326 71. 905 52. 216 1. 00 30.70 5956 OG SER B 548 6. 573 70. 647 51. 557 1. 00 30.75 5957 C SER B 548 5. 222 73. 147 50. 240 1. 00 28. 76 5958 O SER B 548 5. 486 72. 848 49. 047 1. 00 29.02 5959 N GLN B 549 4.033 73.596 50.569 1. 00 28.59 5960 CA GLN B 549 2. 885 73. 738 49. 745 1. 00 29.18 5961 CB GLN B 549 1. 600 74. 113 50. 553 1. 00 31.59 5962 CG GLN B 549 1.097 73.017 51.437 1. 00 33.53 5963 CD GLN B 549 0.008 73.408 52.385 1. 00 35.55 5964 OE1 GLN B 549 0.059 72.983 53.550 1. 00 37.69 5965 NE2 GLN B 549-0. 955 74. 203 51. 972 1. 00 36.23 5966 C GLN B 549 2. 983 74. 772 48. 639 1. 00 28.99 5967 O GLN B 549 2. 291 74. 676 47. 626 1. 00 29.42 5968 N THR B 550 3. 700 75. 845 48. 964 1. 00 28.73 5969 CA THR B 550 3. 917 76. 951 48. 045 1. 00 27.27 5970 CB THR B 550 4.163 78.319 48.716 1. 00 25.52 5971 OG1 THR B 550 5. 325 78. 253 49. 590 1. 00 26.77 5972 CG2 THR B 550 2. 960 78. 863 49. 513 1. 00 23.79 5973 C THR B 550 4. 963 76. 461 47. 045 1. 00 27.42 5974 O THR B 550 4. 867 76. 747 45. 852 1. 00 26.95 5975 N LYS B 551 5. 879 75. 681 47. 593 1. 00 28.02 5976 CA LYS B 551 6.956 75.122 46.764 1. 00 29.00 5977 CB LYS B 551 8. 251 74. 999 47. 348 1. 00 28.80 5978 CG LYS B 551 8. 882 74. 397 48. 490 1. 00 29.26 5979 CD LYS B 551 10. 404 74. 651 48. 590 1. 00 29.67 5980 CE LYS B 551 10. 984 73. 793 49. 692 1. 00 30.54 5981 NZ LYS B 551 12.445 73.777 49.778 1. 00 29.77 5982 C LYS B 551 6. 409 74. 097 45. 812 1. 00 30.33 5983 O LYS B 551 6. 639 74. 128 44. 589 1. 00 30.58 5984 N GLY B 552 5.572 73.208 46.335 1. 00 31.24 5985 CA GLN B 552 4. 973 72. 141 45. 534 1. 00 32.06 5986 CB GLN B 552 4.605 70.968 46.482 1. 00 34.33 5987 CG GLN B 552 5.859 70.640 47.324 1. 00 36.80 5988 CD GLN B 552 7. 133 70. 382 46. 592 1. 00 38.87 5989 OE1 GLN B 552 8. 262 70. 551 47. 144 1. 00 39.91 5990 NE2 GLN B 552 7. 045 69. 972 45. 315 1. 00 39.10 5991 C GLN B 552 3.907 72.599 44.623 1. 00 31.74 5992 O GLN B 552 3. 698 71. 913 43. 587 1. 00 32.35 5993 N SER B 553 3. 242 73. 698 44. 895 1. 00 31.75 5994 CA SER B 553 2. 169 74. 217 44. 026 1. 00 32.09 5995 CB SER B 553 1. 207 75. 162 44. 678 1. 00 33.42 5996 OG SER B 553 1. 692 76. 494 44. 791 1. 00 34.38 5997 C SER B 553 2. 785 74. 905 42. 782 1. 00 32.04 5998 O SER B 553 2. 083 75. 406 41. 895 1. 00 32.15 5999 N GLY B 554 4. 086 74. 993 42. 746 1. 00 32.09 6000 CA GLY B 554 4. 936 75. 551 41. 717 1. 00 31.53 6001 C GLY B 554 4.731 76.954 41.303 1. 00 31.22 6002 0 GLY B 554 5. 237 77. 396 40. 212 1. 00 32.58 6003 N GLU B 555 4. 157 77. 768 42. 159 1. 00 30.37 6004 CA GLU B 555 3. 851 79. 178 41. 845 1. 00 28.97 6005 CB GLU B 555 2.676 79.652 42.703 1. 00 30.16 6006 CG GLU B 555 1. 732 80. 585 41. 815 1. 00 32.20 6007 CD GLU B 555 0. 886 81. 413 42. 758 1. 00 33.48 6008 OE1 GLU B 555 0.266 80.975 43.707 1. 00 34.13 6009 OE2 GLU B 555 1. 113 82. 619 42. 419 1. 00 33.44 6010 C GLU B 555 5. 044 80. 098 42. 116 1. 00 27.24 6011 O GLU B 555 6. 072 79. 725 42. 712 1. 00 26.88 6012 N ASN B 556 4. 906 81. 315 41. 613 1. 00 25.82 6013 CA ASN B 556 5. 922 82. 376 41. 750 1. 00 24.65 6014 CB ASN B 556 5.778 83.465 40.754 1. 00 25.81 6015 CG ASN B 556 6. 101 83. 311 39. 321 1. 00 27.43 6016 OD1 ASN B 556 5.230 83.299 38.437 1. 00 28.60 6017 ND2 ASN B 556 7. 431 83. 232 38. 962 1. 00 27.35 6018 C ASN B 556 5. 981 82. 835 43. 204 1. 00 24.15 6019 O ASN B 556 4. 905 83. 035 43. 820 1. 00 25.16 6020 N LEU B 557 7. 172 82. 961 43. 777 1. 00 22.81 6021 CA LEU B 557 7. 362 83. 431 45. 141 1. 00 21.55 6022 CB LEU B 557 6. 874 84. 947 45. 180 1. 00 18.89 6023 CG LEU B 557 7. 530 85. 753 44. 117 1. 00 17.84 6024 CD1 LEU B 557 7. 210 87. 205 43. 964 1. 00 20. 53 6025 CD2 LEU B 557 9. 087 85. 639 44. 326 1. 00 18. 14 6026 C LEU B 557 6. 780 82. 576 46. 228 1. 00 21. 44 60270 LEU B 557 6. 004 83. 089 47. 074 1. 00 22. 14 6028 N PRO B 558 7. 145 81. 311 46. 259 1. 00 19. 79 6029 CD PRO B 558 8. 028 80. 676 45. 241 1. 00 19. 33 6030 CA PRO B 558 6. 709 80. 348 47. 271 1. 00 19. 78 6031 CB PRO B 558 7. 645 79. 144 47. 003 1. 00 19. 78 6032 CG PRO B 558 8. 755 79. 663 46. 154 1. 00 19. 27 6033 C PRO B 558 7. 060 80. 904 48. 641 1. 00 19. 99 6034 0 PRO B 558 6. 396 80. 712 49. 681 1. 00 20. 73 6035 N TYR B 559 8. 237 81. 546 48. 656 1. 00 19. 26 6036 CA TYR B 559 8. 698 82. 111 49. 930 1. 00 18. 06 6037 CB TYR B 559 10. 228 82. 251 49. 915 1. 00 17. 21 6038 CG TYR B 559 10. 764 82. 269 51. 339 1. 00 16. 39 6039 CD1 TYR B 559 11. 263 81. 066 51. 885 1. 00 16. 58 6040 CE1 TYR B 559 11. 780 81. 032 53. 173 1. 00 16. 44 6041 CD2 TYR B 559 10. 804 83. 435 52. 107 1. 00 14. 75 6042 CE2 TYR B 559 11. 251 83. 356 53. 403 1. 00 15. 95 6043 CZ TYR B 559 11. 767 82. 193 53. 931 1. 00 16. 28 6044 OH TYR B 559 12. 241 82. 225 55. 231 1. 00 18. 90 6045 C TYR B 559 7. 865 83. 243 50. 402 1. 00 18. 02 6046 O TYR B 559 7. 445 83. 254 51. 605 1. 00 18. 56 6047 N LEU B 560 7. 571 84. 284 49. 611 1. 00 17. 73 6048 CA LEU B 560 6. 790 85. 422 50. 005 1. 00 16. 96 6049 CB LEU B 560 6. 836 86. 546 48. 977 1. 00 14. 65 6050 CG LEU B 560 8. 240 87. 153 48. 784'1. 00 12. 79 6051 CD1 LEU B 560 8. 090 88. 340 47. 897 1. 00 10. 59 6052 CD2 LEU B 560 8. 822 87. 399 50. 156 1. 00 12. 18 6053 C LEU B 5605. 34485. 04950. 2951. 0017. 33 60540 LEU B 560 4. 716 85. 710 51. 154 1. 00 17. 94 6055 N VAL B 561 4. 823 84. 193 49. 444 1. 00 16. 97 6056 CA VAL B 561 3. 469 83. 675 49. 548 1. 00 16. 91 6057 CB VAL B 561 3.088 82.768 48.364 1.00 16. 94 6058 CG1 VAL B 561 1. 678 82. 161 48. 496 1. 00 17. 35 6059 CG2 VAL B 561 3. 153 83. 394 47. 006 1. 00 15. 59 6060 C VAL B 561 3. 409 82. 966 50. 909 1. 00 17. 36 6061 0 VAL B 561 2. 519 83. 246 51. 701 1. 00 17. 48 6062 N ALA B 562 4. 371 82. 068 51. 156 1. 00 18. 06 6063 CA ALA B 562 4. 383 81. 291 52. 370 1. 00 17. 38 6064 CB ALA B 562 5. 127 79. 999 52. 368 1. 00 19. 37 6065 C ALA B 562 4. 605 82. 121 53. 606 1. 00 17. 61 60660 ALA B 562 4. 168 81. 646 54. 693 1. 00 17. 99 6067 N TYR B 563 5. 247 83. 275 53. 447 1. 00 16. 51 6068 CA TYR B 563 5. 530 84. 135 54. 592 1. 00 16. 43 6069 CB TYR B 563 6. 772 85. 046 54. 329 1. 00 13. 51 6070 CG TYR B 563 7. 276 85. 454 55. 713 1. 00 12. 59 6071 CD1 TYR B 563 8. 059 84. 555 56. 443 1. 00 11. 47 6072 CE1 TYR B 563 8. 416 84. 894 57. 776 1. 00 11. 98 6073 CD2 TYR B 563 6. 967 86. 662 56. 239 1. 00 12. 46 6074 CE2 TYR B 563 7. 347 87. 051 57. 540 1. 00 12. 92 6075 CZ TYR B 563 8. 126 86. 129 58. 271 1. 00 13. 34 6076 OH TYR B 563 8.512 86.587 49.L485 1.00 15. 46 6077 C TYR B 563 4. 274 84. 908 55. 012 1. 00 16. 87 6078 O TYR B 563 3. 885 84. 934 56. 156 1. 00 16. 63 6079 N GLN B 564 3. 692 85. 547 54. 001 1. 00 17. 86 6080 CA GLN B 564 2. 420 86. 291 54. 235 1. 00 19. 13 6081 CB GLN B 564 1. 836 86. 772 52. 911 1. 00 19. 28 6082 CG GLN B 564 0. 513 87. 494 53. 067 1. 00 19. 18 6083 CD GLN B 564 0. 571 88. 752 53. 882 1. 00 18. 26 6084 OE1 GLN B 564 0. 674 89. 845 53. 337 1. 00 18. 98 6085 NE2 GLN B 564 0. 388 88. 589 55. 158 1. 00 17. 06 6086 C GLN B 564 1. 502 85. 328 54. 964 1. 00 19. 33 6087 0 GLN B 564 1. 031 85. 631 56. 045 1. 00 20. 05 6088 N ALA B 565 1. 300 84. 116 54. 437 1. 00 19. 96 6089 CA ALA B 565 0. 464 83. 085 55. 014 1. 00 20. 00 6090 CB ALA B 565 0. 338 81. 885 54. 057 1. 00 19. 93 6091 C ALA B 565 0. 820 82. 674 56. 403 1. 00 21. 31 6092 0 ALA B 565-0.010 82. 040 57. 124 1. 00 22.19 6093 N THR B 566 2. 096 82. 844 56. 801 1. 00 21. 30 6094 CA THR B 566 2. 554 82. 512 58. 160 1. 00 21. 01 6095 CB THR B 566 4. 111 82. 428 58. 279 1. 00 20. 27 6096 OG1 THR B 566 4. 607 81. 386 57. 422 1. 00 20. 09 6097 CG2 THR B 566 4. 593 82. 443 59. 719 1. 00 19. 41 6098 C THR B 566 2. 025 83. 594 59. 119 1. 00 21. 46 6099 0 THR B 566 1. 584 83. 315 60. 228 1. 00 22. 03 6100 N VAL B 567 2. 184 84. 820 58. 664 1. 00 21. 32 6101 CA VAL B 567 1. 746 86. 025 59. 328 1. 00 21. 91 6102VAL B 567 2. 429 87. 282 58. 777 1. 00 20. 97 6103 CG1 VAL B 567 1. 768 88. 524 59. 358 1. 00 20. 88 6104 CG2 VAL B 567 3. 922 87. 313 59. 145 1. 00 19. 41 6105 C VAL B 567 0. 236 86. 073 59. 441 1. 00 22. 69 6106 0. VAL B 567-0.269 86. 508 60. 484 1. 00 22.43 6107 N CYS B 568-0.454 85. 538 58. 420 1. 00 23.68 6108 CA CYS B 568-1.929 85. 483 58. 435 1. 00 24.74 6109 CB CYS B 568-2.589 85. 384 57. 074 1. 00 22.88 6110 SG CYS B 568-2.397 86. 749 55. 923 1. 00 24.98 6111 C CYS B 568-2.394 84. 446 59. 451 1. 00 25.32 6112 0 CYS B 568-3.250 84. 725 60. 319 1. 00 26.20 6113 N ALA B 569-1.870 83. 262 59. 373 1. 00 25.81 6114 CA ALA B 569-2.205 82. 144 60. 249 1. 00 26.55 6115 CB ALA B 569-1.441 80. 910 59. 802 1. 00 25.30 6116 C ALA B 569-1.882 82. 414 61. 704 1. 00 27.73 6117 0 ALA B 569-2.525 81. 771 62. 551 1. 00 28.63 6118 N ARG B 570-0'897 83. 255 61. 996 1. 00 28. 14 6119 CA ARG B 570-0.495 83. 548 63. 357 1. 00 29.29 6120ARG B 570 1. 040 83. 657 63. 549 1. 00 29. 95 6121ARG B 570 1. 810 82. 497 63. 108 1. 00 31. 06 6122 CD ARG B 570 3. 163 82. 110 63. 285 1. 00 31. 78 6123 NE ARG B 570 4. 277 82. 966 63. 014 1. 00 32. 88 6124 CZ ARG B 570 5. 537 82. 503 62. 816 1. 00 33. 05 6125 NH1 ARG B 570 5. 795 81. 194 62. 803 1. 00 32. 86 6126 NH2 ARG B 570 6. 503 83. 399 62. 594 1. 00 32. 89 6127 C ARG B 570-1.226 84. 735 63. 950 1. 00 29.67 6128 0 ARG B 570-1.004 85. 177 65. 084 1. 00 30.83 6129 N ALA B 571-2.149 85. 282 63. 195 1. 00 29.45 6130 CA ALA B 571-2.965 86. 443 63. 551 1. 00 28.58 6131 CB ALA B 571-2.470 87. 603 62. 689 1. 00 27.81 6132 C ALA B 571-4.435 86. 067 63. 372 1. 00 28.22 6133 0 ALA B 571-5.380 86. 873 63. 532 1. 00 27.45 6134 N GLN B 572-4.587 84. 762 63. 098 1. 00 27.91 6135 CA GLN B 572-5.879 84. 142 62. 816 1. 00 27.44 6136 CB GLN B 572-6.665 83. 618 63. 950 1. 00 29.13 6137 CG GLN B 572-6.139 82. 389 64. 670 1. 00 30.40 6138 CD GLN B 572-6.088 81. 179 63. 740 1. 00 32.20 6139 OE1 GLN B 572-7.095 80. 575 63. 355 1. 00 31.96 6140 NE2 GLN B 572-4.850 80. 754 63. 371 1. 00 32.19 6141 C GLN B 572-6.623 85. 027 61. 830 1. 00 26.87 6142 0 GLN B 572-7.815 85. 232 61. 947 1. 00 27.20 6143 N ALA B 573-5.856 85. 583 60. 896 1. 00 26.15 6144 CA ALA B 573-6.408 86. 492 59. 865 1. 00 25.18 6145 CB ALA B 573-5.599 87. 790 59. 926 1. 00 24.30 6146 C ALA B 573-6.371 85. 799 58. 518 1. 00 24.91 6147 O ALA B 573-5.526 84. 900 58. 283 1. 00 25.01 6148 N PRO B 574-7.274 86. 167 57. 637 1. 00 24.24 6149 CD PRO B 574-8.321 87. 199 57. 836 1. 00 23.99 6150 CA PRO B 574-7.375 85. 579 56. 297 1. 00 23.38 6151 CB PRO B 574-8.760 86. 037 55. 788 1. 00 23.39 6152PRO B 574-9.452 86. 573 56. 999 1. 00 23.51 6153 C PRO B 574-6.330 86. 213 55. 416 1. 00 23.57 6154 O PRO B 574-5.852 87. 334 55. 720 1. 00 24.09 6155 N PRO B 575-6.036 85. 523 54. 318 1. 00 22.68 6156 CD PRO B 575-6.558 84. 216 53. 949 1. 00 21.80 6157 CA PRO B 575-5.075 86. 035 53. 323 1. 00 22.01 6158 CB PRO B 575-4.902 84. 838 52. 354 1. 00 22.09 6159 CG PRO B 575-6.240 84. 123 52. 434 1. 00 21.56 6160 C PRO B 575-5.686 87. 209 52. 598 1. 00 22.40 6161 0 PRO B 575-6.904 87. 456 52. 739 1. 00 22.21 6162 N PRO B 576-4. 853 87. 925 51. 842 1. 00 22. 46 6163 CD PRO B 576-3.402 87. 658 51. 738 1. 00 22.36 6164 CA PRO B 576-5.265 89. 108 51. 083 1. 00 22.97 6165 CB PRO B 576-4.036 89. 452 50. 235 1. 00 22.32 6166PRO B 576-2.856 88. 804 50. 901 1. 00 22.55 6167 C PRO B 576-6.488 89. 001 50. 201 1. 00 23.57 6168 O PRO B 576-7.140 90. 013 49. 878 1. 00 24.03 6169 N SER B 577-6.811 87. 822 49. 712 1. 00 23.99 6170 CA SER B 577-7. 888 87.415 48.882 1.00 24. 42 6171 CB SER B 577-7.938 87. 867 47. 451 1. 00 24.26 6172 OG SER B 577-6.921 87. 340 46. 661 1. 00 25.06 6173 C SER B 577-7.904 85. 858 48. 914 1. 00 25.19 6174 O SER B 577-6.976 85. 222 49. 453 1. 00 25.75 6175 N TRP B 578-8.918 85. 297 48. 327 1. 00 25.40 6176 CA TRP B 578-9.057 83. 844 48. 244 1. 00 25.71 6177 CB TRP B 578-10.240 83. 268 48. 934 1. 00 24.14 6178 CG TRP B 578-10.259 83. 287 50. 424 1. 00 22.61 6179 CD2 TRP B 578-9.471 82. 408 51. 282 1. 00 21.74 6180 CE2 TRP B 578-9.757 82. 777 52. 621 1. 00 20.85 6181 CE3 TRP B 578-8.584 81. 371 51. 025 1. 00 21.17 6182 CD1 TRP B 578-10.938 84. 111 51. 257 1. 00 21.85 6183 NE1 TRP B 578-10.671 83. 800 52. 567 1. 00 21.32 6184 CZ2 TRP B 578-9.190 82. 154 53. 710 1. 00 20.31 6185 CZ3 TRP B 578-8. 027 80. 736 52. 106 1. 00 21. 40 6186 CH2 TRP B 578-8.288 81. 126 53. 429 1. 00 20.46 6187 C TRP B 578-8.529 83. 292 46. 953 1. 00 27.00 6188 O TRP B 578-8.696 82. 097 46. 641 1. 00 27.91 6189 N ASP B 579-7.817 84. 116 46. 173 1. 00 28.06 6190 CA ASP B 579-7.184 83. 697 44. 918 1. 00 28.65 6191 CB ASP B 579-6.523 84. 814 44. 126 1. 00 31.14 6192 CG ASP B 579-7.535 85. 766 43. 494 1. 00 33.51 6193 OD1 ASP B 579-7.261 86. 846 42. 880 1. 00 35.03 6194 OD2 ASP B 579-8.728 85. 370 43. 571 1. 00 34.37 6195 C ASP B 579-6.381 82. 439 45. 119 1.00 28.47 6196 0 ASP B 579-5.922 82. 191 46. 236 1.00 28.19 6197 N GLN B 580-6.236 81. 636 44. 075 1.00 28.57 6198 CA GLN B 580-5.485 80. 396 44. 025 1.00 28.39 6199 CB GLN B 580-5.118 80. 047 42. 554 1.00 31.41 6200 CG GLN B 580-6.242 79. 812 41. 603 1.00 34.89 6201 CD GLN B 580-5.849 79. 586 40. 141 1.00 36. 84 6202 OE1 GLN B 580-4.719 79. 747 39. 703 1.00 37.47 6203 NE2 GLN B 580-6.863 79. 259 39. 324 1.00 37.60 6204 C GLN B 580-4. 169 80. 393 44. 803 1. 00 27.32 62050GLN B 580-3.761 79. 357 45. 344 1.00 27.37 6206 N MET B 581-3.435 81. 471 44. 718 1.00 26.40 6207 CA MET B 581-2.155 81. 748 45. 367 1.00 25.00 6208MET B 581-1. 865 83. 247 45. 160 1. 00 26.01 6209MET B 581-0.817 83. 770 46. 076 1.00 25.95 6210MET B 581-0.414 85. 440 45. 578 1.00 27.34 6211 CE MET B 581-1.951 86. 314 45. 590 1.00 28.65 6212 C MET B 581-2.148 81. 398 46. 844 1.00 24.23 6213 0 MET B 581-1.206 80. 794 47. 365 1.00 23.51 6214 N TRP B 582-3.247 81. 809 47. 508 1.00 23.50 6215 CA TRP B 582-3. 382 81. 583 48. 934 1. 00 23.44 6216 CB TRP B 582-4.318 82. 741 49. 507 1.00 20.35 6217 CG TRP B 582-3.725 84. 046 49. 081 1.00 17.04 6218 CD2 TRP B 582-2.421 84. 516 49. 458 1.00 16.14 6219 CE2 TRP B 582-2.223 85. 751 48. 789 1.00 15.97 6220 CE3 TRP B 582-1.442 84. 074 50. 335 1.00 16.11 6221 CD1 TRP B 582-4.229 84. 910 48. 194 1.00 15.50 6222 NE1 TRP B 582-3. 376 86. 015 48. 057 1. 00 16.36 6223 CZ2 TRP B 582-1.092 86. 524 48. 943 1.00 15.00 6224 CZ3 TRP B 582-0.274 84. 836 50. 466 1.00 15.56 6225 CH2 TRP B 582-0.137 86. 058 49. 838 1.00 14.68 6226 C TRP B 582-4.007 80. 256 49. 267 1.00 24.82 6227 O TRP B 582-4.464 80. 165 50. 430 1.00 25.49 6228 N LYS B 583-4.104 79. 286 48. 367 1.00 25.83 6229 CA LYS B 583-4.768 78. 028 48. 690 1.00 26.72 6230LYS B 583-5.248 77. 152 47. 603 1.00 29.35 6231 CG LYS B 583-4.298 76. 602 46. 543 1.00 32.31 6232 CD LYS B 583-5.174 75. 910 45. 434 1.00 34.41 6233 CE LYS B 583-6.182 76. 928 44. 888 1.00 36.07 6234 NZ LYS B 583-6.939 76. 443 43. 724 1.00 37.28 6235 C LYS B 583-4.202 77. 307 49. 857 1.00 27.24 62360LYS B 583-4.847 76. 303 50. 269 1.00 27.41 6237 N CYS B 584-3.061 77. 747 50. 399 1.00 27.26 6238 CA CYS B 584-2.443 77. 072 51. 526 1.00 27.86 6239 CB CYS B 584-0.972 77. 281 51. 761 1.00 28.05 6240 SG CYS B 584-0.347 78. 879 52. 320 1.00 27.52 6241 C CYS B 584-3.245 77. 334 52. 815 1.00 28.04 6242 0 CYS B 584-3.099 76. 554 53. 752 1.00 28.25 6243 N LEU B 585-4.050 78. 400 52. 801 1.00 27.84 6244 CA LEU B 585-4.817 78. 709 54. 044 1.00 27.52 6245 CB LEU B 585-4.645 80. 196 54. 248 1.00 25.64 6246LEU B 585-3.307 80. 792 54. 632 1.00 23.67 6247 CD1 LEU B 585-3.361 82. 308 54. 585 1.00 24.44 6248 CD2 LEU B 585-3.071 80. 418 56. 118 1.00 23.13 6249 C LEU B 585-6.271 78. 262 53. 948 1.00 28.12 62500LEU B 585-7.092 78. 676 54. 772 1.00 28.87 6251 N ILE B 586-6.583 77. 493 52. 945 1.00 28.10 6252 CA ILE B 586-7.920 76. 974 52. 653 1.00 27.81 6253 CB ILE B 586-7.906 76. 283 51. 250 1.00 27.03 6254 CG1 ILE B 586-9.341 75. 878 50. 880 1.00 26.52 6255 CD1 ILE B 586-10.348 77. 052 50. 763 1.00 26.45 6256 CG2 ILE B 586-6.991 75. 012 51. 242 1.00 27.29 6257 C ILE B 586-8.517 76. 194 53. 790 1.00 28.22 6258 0 ILE B 586-9.638 76. 479 54. 215 1.00 27.93 6259 N ARG B 587-7.794 75. 261 54. 389 1.00 28.70 6260 CA ARG B 587-8.161 74. 444 55. 491 1.00 29.26 6261ARG B 587-7.415 73. 180 55. 772 1.00 32.50 6262ARG B 587-7.332 72. 057 54. 734 1.00 36.27 6263 CD ARG B 587-6.766 70. 832 55. 418 1.00 39.37 6264 NE ARG B 587-6.502 69. 737 54. 505 1.00 42.16 6265 CZ ARG B 587-6.033 68. 544 54. 865 1.00 43.94 6266 NH1 ARG B 587-5. 741 67. 576 53. 976 1. 00 44.24 6267 NH2 ARG B 587-5.904 68. 238 56. 158 1.00 45.05 6268 C ARG B 587-8.289 75. 263 56. 780 1.00 29.10 6269 0 ARG B 587-8.742 74. 676 57. 804 1.00 29.47 6270 N LEU B 588-7. 885 76. 495 56. 796 1. 00 28.55 6271 CA LEU B 588-8.010 77. 352 57. 983 1.00 28.49 6272LEU B 588-6.678 78. 020 58. 313 1.00 28.75 6273 CG LEU B 588-5.471 77. 321 58. 792 1.00 28.23 6274 CD1 LEU B 588-4. 258 78. 273 58. 819 1. 00 28.08 6275 CD2 LEU B 588-5.692 76. 939 60. 278 1.00 28.88 6276 C LEU B 588-9.056 78. 442 57. 689 1.00 28.06 6277 0 LEU B 588-9.204 79. 355 58. 519 1.00 28.54 6278 N LYS B 589-9.666 78. 376 56. 536 1.00 27.71 6279 CA LYS B 589-10.658 79. 382 56. 122 1.00 27.23 6280 CB LYS B 589-11.152 79. 214 54. 730 1.00 26.73 6281 CG LYS B 589-12.146 80. 282 54. 281 1.00 27.02 6282 CD LYS B 589-12.497 80. 083 52. 822 1.00 27.65 6283 CE LYS B 589-13.319 81. 247 52. 319 1.00 27.15 6284LYS B 589-13.412 81. 183 50. 861 1.00 28.97 6285 C LYS B 589-11.744 79. 676 57. 129 1.00 27.36 6286 0 LYS B 589-12.082 80. 853 57. 388 1.00 27.10 6287 N PRO B 590-12.314 78. 647 57. 726 1.00 27.54 6288 CD PRO B 590-11.986 77. 223 57. 401 1.00 27.57 6289 CA PRO B 590-13.356 78. 749 58. 729 1.00 27.73 6290PRO B 590-13.637 77. 267 59. 088 1.00 27.50 6291 CG PRO B 590-13.268 76. 538 57. 810 1.00 27.80 6292 C PRO B 590-12.970 79. 453 60. 036 1.00 27.65 6293 0 PRO B 590-13.833 79. 982 60. 758 1.00 27.42 6294 N THR B 591-11.667 79. 357 60. 364 1.00 28.19 6295 CA THR B 591-11.175 79. 938 61. 628 1.00 28.02 6296 CB THR B 591-10.081 79. 042 62. 359 1.00 28.40 6297 OG1 THR B 591-8.793 79. 258 61. 705 1.00 29.77 6298 CG2 THR B 591-10.377 77. 533 62. 227 1.00 27.78 6299 C THR B 591-10.660 81. 340 61. 454 1.00 27.40 6300 0 THR B 591-10.613 82. 048 62. 453 1.00 27.82 6301 N LEU B 592-10.320 81. 730 60. 233 1.00 27.01 6302 CA LEU B 592-9.767 83. 049 59. 950 1.00 26.33 6303LEU B 592-8.857 82. 939 58. 721 1.00 26.46 6304 CG LEU B 592-7.779 81. 909 58. 605 1.00 26.30 6305 CD1 LEU B 592-6.935 82. 165 57. 339 1.00 27.03 6306 CD2 LEU B 592-6.868 81. 803 59. 797 1.00 26.88 6307 C LEU B 592-10.793 84. 171 59. 873 1.00 26.41 6308 0 LEU B 592-11.842 84. 183 59. 213 1.00 25.80 6309 N HIS B 593-10.400 85. 256 60. 546 1.00 26.67 6310 CA HIS B 593-11.193 86. 486 60. 634 1.00 27.07 6311 CB HIS B 593-12.206 86. 410 61. 842 1.00 28.88 6312HIS B 593-11.460 86. 163 63. 122 1.00 31.09 6313 CD2 HIS B 593-10.969 85. 000 63. 635 1.00 31.97 6314 ND1 HIS B 593-11.057 87. 145 64. 005 1.00 31.81 6315 CE1 HIS B 593-10.369 86. 595 64. 989 1.00 31.68 6316 NE2 HIS B 593-10.306 85. 293 64. 798 1.00 32.09 6317 C HIS B 593-10.256 87. 672 60. 934 1.00 26.20 6318 0 HIS B 593-9.205 87. 497 61. 597 1.00 25.87 6319 N GLY B 594-10.710 88. 799 60. 463 1.00 25.31 6320 CA GLY B 594-10.050 90. 076 60. 663 1.00 24.70 6321 C GLY B 594-9.485 90. 689 59. 411 1.00 23. 76 63220GLY B 594-9.631 90. 098 58. 347 1.00 24.23 6323 N PRO B 595-8.887 91. 872 59. 591 1.00 23.06 6324 CD PRO B 595-8.683 92. 567 60. 871 1.00 22. 82 6325 CA PRO B 595-8.223 92. 598 58. 485 1.00 22.18 6326PRO B 595-7.978 93. 983 59. 060 1.00 22.32 6327PRO B 595-7.841 93. 765 60. 545 1.00 22.41 6328 C PRO B 595-6.912 91. 835 58. 258 1.00 21.41 6329 0 PRO B 595-6.455 91. 184 59. 236 1.00 21.52 6330 N THR B 596-6.393 91. 885 57. 040 1.00 20.79 6331 CA THR B 596-5.110 91. 119 56. 824 1.00 19.12 6332 CB THR B 596-4.982 90. 750 55. 281 1.00 19.43 6333 OG1 THR B 596-6.061 89. 828 54. 959 1.00 19.54 6334 CG2 THR B 596-3.629 90. 120 54. 889 1.00 18. 18 6335 C THR B 596-3.940 92. 001 57. 211 1.00 18.56 6336 O THR B 596-3.840 93. 160 56. 792 1.00 18.06 6337 N PRO B 597-2.998 91. 399 57. 906 1.00 18. 35 6338 CD PRO B 597-2.925 90. 074 58. 452 1.00 17.68 6339 CA PRO B 597-1.752 92. 189 58. 259 1.00 18.25 6340PRO B 597-1.308 91. 514 59. 510 1.00 18.39 6341 CG PRO B 597-2.044 90. 203 59. 670 1.00 18.12 6342 C PRO B 597-0.921 92. 037 56. 980 1.00 18.28 6343 O PRO B 597-0.260 91. 020 56. 888 1.00 17.75 6344 N LEU B 598-1.087 93. 018 56. 060 1.00 18.04 6345 CA LEU B 598-0.453 92. 966 54. 764 1.00 17.40 6346LEU B 598-1.273 93. 737 53. 745 1.00 14.77 6347 CG LEU B 598-1.165 93. 787 52. 295 1.00 12.66 6348 CD1 LEU B 598-1.743 92. 602 51. 474 1.00 13.38 6349 CD2 LEU B 598-1.525 95. 053 51. 598 1.00 10.53 6350 C LEU B 598 1. 015 93. 341 54. 806 1. 00 17.85 6351 O LEU B 598 1. 392 94. 454 55. 275 1. 00 17.80 6352 N LEU B 599 1. 823 92. 479 54. 163 1. 00 17.76 6353 CA LEU B 599 3. 280 92. 681 54. 122 1. 00 17.31 6354 CB LEU B 599 3. 884 91. 244 54. 262 1. 00 17.23 6355 CG LEU B 599 3. 591 90. 503 55. 523 1. 00 17.76 6356 CD1 LEU B 599 4. 354 89. 193 55. 558 1. 00 18. 95 6357 CD2 LEU B 599 3. 922 91. 262 56. 768 1. 00 17.31 6358 C LEU B 599 3. 771 93. 365 52. 882 1. 00 17.12 6359 O LEU B 599 4. 769 94. 116 52. 780 1. 00 16.49 6360 N TYR B 600 3. 073 93. 006 51. 804 1. 00 16. 83 6361 CA TYR B 600 3. 325 93. 430 50. 438 1. 00 16.78 6362 CB TYR B 600 4. 655 92. 773 49. 946 1. 00 14.38 6363 CG TYR B 600 4. 962 91. 430 50. 595 1. 00 13.01 6364 CD1 TYR B 600 4. 271 90. 270 50. 266 1. 00 13.20 6365 CE1 TYR B 600 4. 601 89. 060 50. 911 1. 00 13.29 6366 CD2 TYR B 600 6. 051 91. 309 51. 442 1. 00 11.31 6367 CE2 TYR B 600 6. 412 90. 109 52. 077 1. 00 11.88 6368 CZ TYR B 600 5. 663 88. 987 51. 771 1. 00 12.66 6369 OH TYR B 600 5. 941 87. 809 52. 415 1. 00 14.64 6370 C TYR B 600 2. 154 93. 034 49. 598 1. 00 17.46 6371 O TYR B 600 1. 480 92. 105 50. 099 1. 00 17.90 6372 N ARG B 601 2. 030 93. 582 48. 430 1. 00 17.85 6373 CA ARG B 601 0. 927 93. 170 47. 501 1. 00 18.49 6374 CB ARG B 601 0. 292 94. 370 46. 890 1. 00 18.20 6375 CG ARG B 601-0. 540 95. 218 47. 873 1. 00 18. 97 6376 CD ARG B 601-0. 556 96. 625 47. 285 1. 00 19.54 6377 NE ARG B 601-1. 300 97. 485 48. 228 1. 00 20.91 6378 CZ ARG B 601-2. 619 97. 277 48. 436 1. 00 21.54 6379 NH1 ARG B 601-3. 301 96. 320 47. 807 1. 00 21.43 6380 NH2 ARG B 601-3. 216 98. 054 49. 315 1. 00 21.54 6381 C ARG B 601 1. 485 92. 221 46. 443 1. 00 19.26 6382 O ARG B 601 2. 381 92. 570 45. 647 1. 00 18.56 6383 N LEU B 602 0. 931 91. 031 46. 436 1. 00 19.75 6384 CA LEU B 602 1. 245 89. 939 45. 541 1. 00 20.73 6385 CB LEU B 602 1. 701 88. 683 46. 241 1. 00 16.96 6386 CG LEU B 602 2.927 88.654 47.136 1. 00 13.74 6387 CD1 LEU B 602 3. 234 87. 256 47. 521 1. 00 14.13 6388 CD2 LEU B 602 4. 081 89. 446 46. 532 1. 00 12.01 6389 C LEU B 602 0. 120 89. 640 44. 532 1. 00 22.56 6390 O LEU B 602 0. 260 88. 672 43. 738 1. 00 24.05 6391 N GLY B 603-0. 933 90. 341 44. 496 1. 00 23.40 6392 CA GLY B 603-2. 011 90. 160 43. 495 1. 00 24.41 6393 C GLY B 603-2. 999 91. 248 43. 920 1. 00 25.76 6394 O GLY B 603-2. 541 92. 224 44. 542 1. 00 26.42 6395 N ALA B 604-4. 240 91. 020 43. 608 1. 00 26.35 6396 CA ALA B 604-5. 317 91. 943 44. 029 1. 00 26.56 6397 CB ALA B 604-6. 562 91. 638 43. 227 1. 00 26.72 6398 C ALA B 604-5. 588 91. 600 45. 515 1. 00 26.86 6399 O ALA B 604-5. 446 90. 458 45. 938 1. 00 26.71 6400 N VAL B 605-6. 006 92. 640 46. 197 1. 00 27.37 6401 CA VAL B 605-6. 351 92. 572 47. 614 1. 00 27.75 6402 CB VAL B 605-5. 455 93. 536 48. 405 1. 00 26.65 6403 CG1 VAL B 605-5. 814 93. 511 49. 900 1. 00 26.58 6404 CG2 VAL B 605-3. 999 93. 196 48. 210 1. 00 24.34 6405 C VAL B 605-7. 847 92. 749 47. 736 1. 00 28.82 6406 O VAL B 605-8. 438 93. 618 47. 056 1. 00 29.15 6407 N GLN B 606-8. 480 91. 894 48. 500 1. 00 29.79 6408 CA GLN B 606-9. 930 91. 900 48. 700 1. 00 30.15 6409 CB GLN B 606-10. 705 90. 742 48. 132 1. 00 32.36 6410 CG GLN B 606-10. 997 90. 512 46. 783 1. 00 34.10 6411 CD GLN B 606-10. 402 90. 301 45. 503 1. 00 35.65 6412 OE1 GLN B 606-10. 612 89. 238 44. 849 1. 00 36.17 6413 NE2 GLN B 606-9. 705 91. 278 44. 888 1. 00 36.07 6414 C GLN B 606 -10.305 92.114 50.145 1. 00 29.70 6415 O GLN B 606-11. 337 92. 773 50. 356 1. 00 30.03 6416 N ASN B 607-9. 566 91. 496 51. 040 1. 00 29.17 6417 CA ASN B 607-9. 853 91. 636 52. 471 1. 00 28.97 6418 CB ASN B 607-9. 076 90. 546 53. 279 1. 00 27.61 6419 CG ASN B 607-9. 582 90. 582 54. 711 1. 00 26.97 6420 OD1 ASN B 607-10. 680 91. 185 54. 861 1. 00 27.78 6421 ND2 ASN B 607-8. 945 90. 033 55. 699 1. 00 25.69 6422 C ASN B 607-9. 450 93. 047 52. 915 1. 00 29.30 6423 O ASN B 607-8.685 93. 701 52. 177 1.00 29.02 6424 N GLU B 608-9.990 93. 473 54. 036 1.00 30.00 6425 CA GLU B 608-9.610 94. 794 54. 651 1.00 30.73 6426 CB GLU B 608-10.424 95. 004 55. 926 1.00 33.68 6427 CG GLU B 608-10.197 96. 137 56. 890 1.00 37.16 6428 CD GLU B 608-11.037 96. 260 58. 124 1.00 39.94 6429 OE1 GLU B 608-11.854 95. 422 58. 526 1.00 41.60 6430 OE2 GLU B 608-10.868 97. 334 58. 770 1.00 40.65 6431 C GLU B 608-8.155 94. 551 55. 149 1.00 30.37 6432 0 GLU B 608-7.811 93. 338 55. 364 1.00 29.96 6433 N ILE B 609-7.432 95. 615 55. 378 1.00 29.97 6434 CA ILE B 609-6.051 95. 439 55. 884 1.00 29.99 6435 CB ILE B 609-5.062 95. 679 54. 703 1.00 29.11 6436 CG1 ILE B 609-5.282 97. 106 54. 147 1.00 30.32 6437 CD1 ILE B 609-4.324 97. 442 52. 953 1.00 30.75 6438 CG2 ILE B 609-5.302 94. 654 53. 540 1.00 28.52 6439 C ILE B 609-5.736 96. 201 57. 149 1.00 30.38 6440 O ILE B 609-6.423 97. 138 57. 609 1.00 30.46 6441 N THR B 610-4.692 95. 746 57. 826 1.00 30.16 6442 CA THR B 610-4.059 96. 248 58. 992 1.00 31.12 6443 CB THR B 610-3.998 95. 716 60. 411 1.00 31.85 6444 OG1 THR B 610-3.513 94. 350 60. 410 1.00 34.50 6445 CG2 THR B 610-4. 825 96. 141 61. 534 1. 00 32.39 6446 C THR B 610-2.512 96. 338 58. 605 1.00 31.43 6447 0 THR B 610-1.968 95. 263 58. 379 1.00 31.06 6448 N LEU B 611-2.044 97. 560 58. 696 1.00 31.49 6449 CA LEU B 611-0.637 97. 825 58. 355 1.00 31.78 6450 CB LEU B 611-0.690 99. 186 57. 570 1.00 32.34 6451 CG LEU B 611-1.622 99. 253 56. 392 1.00 32.45 6452 CD1 LEU B 611-1. 544 100. 658 55. 766 1. 00 31.93 6453 CD2 LEU B 611-1.195 98. 203 55. 367 1.00 32.85 6454 C LEU B 611 0. 238 98. 033 59. 560 1. 00 31.74 64550 LEU B 611 1. 175 98. 869 59. 413 1. 00 32.18 6456 N THR B 612 0. 048 97. 360 60. 656 1. 00 31.79 6457 CA THR B 612 0. 888 97. 628 61. 832 1. 00 31.56 6458 CB THR B 612-0.041 98. 102 63. 060 1.00 31.78 6459 OG1 THR B 612-0.628 96. 883 63. 628 1.00 31.09 6460 CG2 THR B 612-1.109 99. 108 62. 619 1.00 31.86 6461 C THR B 612 1. 665 96. 431 62. 315 1. 00 31.30 6462 O THR B 612 2. 035 96. 494 63. 507 1. 00 31.10 6463 N HIS B 613 1. 833 95. 409 61. 527 1. 00 30.83 6464 CA HIS B 613 2. 586 94. 176 61. 969 1. 00 30.10 6465 CB HIS B 613 2. 195 92. 981 61. 064 1. 00 29.01 6466 CG HIS B 613 2. 813 91. 684 61. 469 1. 00 27.96 6467 CD2 HIS B 613 2. 252 90. 592 62. 020 1. 00 27. 65 6468 ND1 HIS B 613 4. 136 91. 384 61. 317 1. 00 28.06 6469 CE1 HIS B 613 4. 379 90. 164 61. 776 1. 00 27.98 6470 NE2 HIS B 613 3. 234 89. 655 62. 198 1. 00 28.25 6471 C HIS B 613 4. 055 94. 556 61. 844 1. 00 29.86 6472 O HIS B 613 4. 393 95. 311 60. 908 1. 00 30.32 6473 N PRO B 614 4. 887 94. 105 62. 751 1. 00 29.62 6474 CD PRO B 614 4. 537 93. 253 63. 894 1. 00 29.61 6475 CA PRO B 614 6. 315 94. 443 62. 777 1. 00 29.46 6476 CB PRO B 614 6. 912 93. 664 63. 945 1. 00 29.48 6477 CG PRO B 614 5. 871 92. 692 64. 354 1. 00 29.47 6478 C PRO B 614 7. 008 94. 226 61. 454 1. 00 28.78 6479 O PRO B 614 7. 797 95. 110 60. 993 1. 00 28.74 6480 N VAL B 615 6. 748 93.094 60. 843 1.00 28.29 6481 CA VAL B 615 7. 371 92.804 59. 531 1.00 27.57 6482 CB VAL B 615 7. 298 91.350 59. 119 1.00 27.94 6483 CG1 VAL B 615 7. 886 91.068 57. 750 1.00 28.18 6484 CG2 VAL B 615 7. 863 90.405 60. 147 1.00 27.24 6485 C VAL B 615 6. 961 93.865 58. 546 1.00 26.54 6486 O VAL B 615 7. 850 94.250 57. 768 1.00 26.55 6487 N THR B 616 5. 718 94.364 58. 580 1.00 26.48 6488 CA THR B 616 5. 320 95.406 57. 606 1.00 25.53 6489 CB THR B 616 3. 827 95.850 57. 751 1.00 24.36 6490 OG1 THR B 616 3. 032 94.639 57. 692 1.00 23.84 6491 CG2 THR B 616 3. 438 96.829 56. 657 1.00 23.27 6492 C THR B 616 6. 225 96.644 57. 792 1.00 25.87 6493 O THR B 616 6. 740 97.288 56. 851 1.00 25.48 6494 N LYS B 617 6. 282 97.011 59. 055 1.00 26.37 6495 CA LYS B 617 7. 150 98.126 59. 481 1.00 27.08 6496 CB LYS B 617 6. 981 98.416 60. 952 1.00 29.45 6497 CG LYS B 617 5. 544 98.977 61. 171 1.00 31.51 6498 CD LYS B 617 5. 568 99.590 62. 576 1.00 33.42 6499 CE LYS B 617 4. 360 100.517 62. 704 1.00 34.50 6500 NZ LYS B 617 4. 491 101.248 64. 006 1.00 35.56 6501 C LYS B 617 8. 588 97.851 59. 119 1.00 26.88 6502 O LYS B 617 9. 274 98.769 58. 550 1.00 28.26 6503 N TYR B 618 9. 052 96.660 59. 370 1.00 26.52 6504 CA TYR B 618 10. 469 96.311 58. 972 1.00 26.49 6505 CB TYR B 618 10. 783 94.893 59. 393 1.00 25.20 6506 CG TYR B 618 12. 165 94.450 58. 928 1.00 24.64 6507 CD1 TYR B 618 13. 319 94.761 59. 639 1.00 24.04 6508 CE1 TYR B 618 14. 565 94.361 59. 186 1.00 24.11 6509 CZ TYR B 618 14. 668 93.637 57. 998 1.00 23.33 6510 OH TYR B 618 15. 896 93.229 57. 505 1.00 22.39 6511 CE2 TYR B 618 13. 544 93.353 57. 267 1.00 24.24 6512 CD2 TYR B 618 12. 281 93.739 57. 729 1.00 24.51 6513 C TYR B 618 10. 653 96.58157. 4821.00 26.56 6514 O TYR B 618 11. 531 97.361 57. 033 1.00 26.67 6515 N ILE B 619 9. 780 95.954 56. 670 1.00 26.58 6516 CA ILE B 619 9. 848 96.178 55. 194 1.00 26.13 6517 CB ILE B 619 8. 893 95.196 54. 448 1.00 24.28 6518 CG2 ILE B 619 9. 157 95.162 52. 920 1.00 23.33 6519 CG1 ILE B 619 9. 124 93.730 54. 985 1.00 23.55 6520 CD1 ILE B 619 8. 244 92.664 54. 342 1.00 22.34 6521 C ILE B 619 9. 837 97.638 54. 848 1.00 26.43 65220 ILE B 619 10. 592 98.124 53. 967 1.00 26.62 6523 N MET B 620 9. 003 98.437 55. 520 1.00 27.19 6524 CA MET B 620 8. 927 99.919 55. 265 1.00 27.67 6525 CB MET B 620 7. 856 100.471 56. 182 1.00 28.83 6526 CG MET B 620 6. 509 99.930 55. 640 1.00 29.64 6527 SD MET B 620 5. 247 100.430 56. 856 1.00 31.72 6528 CE MET B 620 5. 535 102.224 56. 825 1.00 31.99 6529 C MET B 620 10. 288 100.527 55. 519 1.00 27.80 6530 O MET B 620 10. 823 101.344 54. 749 1.00 27.63 6531 N THR B 621 10. 832 100.094 56. 645 1.00 28.57 6532 CA THR B 621 12. 207 100.518 57. 030 1.00 29.67 6533 CB THR B 621 12. 591 99.725 58. 343 1.00 31.61 6534 OG1 THR B 621 11. 838 100.417 59. 403 1.00 33.09 6535 CG2 THR B 621 14. 039 99.459 58. 601 1.00 32.71 6536 C THR B 621 13. 193 100.334 55. 917 1.00 29.40 6537 0 THR B 621 13. 900 101.274 55. 519 1.00 29.70 6538 N CYS B 622 13. 257 99.118 55. 369 1.00 29.50 6539 CA CYS B 622 14. 190 98.783 54. 277 1.00 28.47 6540 CB CYS B 622 13. 926 97.334 53. 816 1.00 28.31 6541 SG CYS B 622 14. 246 96.094 55. 073 1.00 27.74 6542 C CYS B 622 14. 095 99.658 53. 053 1. 00 27.96 6543 0 CYS B 622 15. 110 99.839 52. 347 1.00 28.02 6544 N MET B 623 12. 891 100.052 52. 728 1.00 28.25 6545 CA MET B 623 12. 668 100.902 51. 530 1.00 28.85 6546MET B 623 11. 197 100.991 51. 172 1.00 27.80 6547 CG MET B 623 10. 771 99.578 50. 749 1.00 27.18 6548 SD MET B 623 9. 043 99.586 50. 397 1.00 26.21 6549 CE MET B 623 8. 876 100.600 48. 979 1.00 23.59 6550 C MET B 623 13. 359 102.242 51. 667 1.00 29.40 6551 0 MET B 623 14. 116 102.646 50. 765 1.00 30.55 6552 N SER B 624 13. 132 102.907 52. 765 1.00 29.81 6553 CA SER B 624 13. 726 104.217 53. 066 1.00 30.32 6554 CB SER B 624 13. 439 104.549 54. 543 1.00 30.76 6555 OG SER B 624 12. 044 104.499 54. 797 1.00 30.46 6556 C SER B 624 15. 251 104.154 52. 947 1.00 30.41 6557 0 SER B 624 15. 891 105.043 52. 340 1.00 31.27 6558 N ALA B 625 15. 822 103.166 53. 589 1.00 30.27 6559 CA ALA B 625 17. 254 102.950 53. 652 1.00 30.21 6560 CB ALA B 625 17. 486 101.650 54. 479 1.00 30.59 6561 C ALA B 625 17. 936 102.780 52. 320 1.00 30.66 6562 0 ALA B 625 18. 810 103.553 51. 854 1.00 30.74 6563 N ASP B 626 17. 554 101.682 51. 688 1.00 31.33 6564 CA ASP B 626 18. 096 101.197 50. 444 1.00 31.94 6565ASP B 626 18. 506 99.728 50. 514 1.00 34.65 6566 CG ASP B 626 19. 677 99.518 51. 471 1.00 37.38 6567 OD1 ASP B 626 20. 858 99.544 50. 996 1.00 38.32 6568 OD2 ASP B 626 19. 424 99.389 52. 683 1.00 37.69 6569 C ASP B 626 17. 512 101.637 49. 159 1.00 31.41 65700ASP B 626 18. 216 101.435 48. 145 1.00 31.74 6571 N LEU B 627 16. 324 102.226 49. 216 1.00 31.11 6572 CA LEU B 627 15. 763 102.718 47. 908 1.00 30.64 6573 CB LEU B 627 14. 476 102.039 47. 637 1.00 28.22 6574 CG LEU B 627 14. 340 100.543 47. 550 1.00 26.09 6575 CD1 LEU B 627 12. 883 100.245 47. 255 1.00 26.33 6576 CD2 LEU B 627 15. 208 99.946 46. 462 1.00 25.43 6577 C LEU B 627 15. 797 104.265 47. 998 1.00 30.66 6578 0 LEU B 627 15. 468 104.758 49. 113 1.00 30.98 6766 0 HOH B 701 17. 103 75.469 34. 923 1.00 13.81 6767 0 HOH B 702 22. 719 75.626 47. 698 0.80 21.81 6768 0 HOH B 703 19. 876 97.853 47. 062 1.00 14.58 6769 O HOH B 704 11. 451 91.259 61. 277 0.80 26.89 6770 O HOH B 705 13. 841 79.178 56. 038 0.80 28.17 6771 0 HOH B 706 9. 703 79.044 42. 664 0.80 23.96 6772 0 HOH B 707-7.480 88.062 63. 303 0.80 25.70 6773 0 HOH B 708-3.037 88.688 47. 136 0.80 24.61 6774 O HOH B 709-12.900 88.777 58. 633 0. 80 28.28 6775 0 HOH B 710-11.790 83. 086 56. 757 0. 80 26.93 6776 0 HOH B 711-0.961 78.694 48. 745 0.80 21.21 O HOH B 712-0.027 77.694 46. 599 0.60 22.48 6778 0 HOH B 713-3.298 99.961 60. 012 0.80 26.23 6779 O HOH B 714 3. 445 87.353 63. 624 0.80 29.84 6780 O HOH B 715 2. 307 97.550 49. 343 0.80 20.72 6781 0 HOH B 717-2. 719 94. 905 45. 011 1. 00 27. 85 6782 0 HOH B 718-0.207 98. 524 44. 373 0. 60 17.06 6783 0 HOH B 716 2. 580 84. 539 43. 162 0. 40 22. 49 6784 0 HOH B 719-0.666 90. 595 39. 154 0. 60 18.87 6785 0 HOH B 720 9. 712 100. 399 40. 734 1. 00 39. 63 6786 0 HOH B 721 12. 949 99. 181 39. 424 0. 60 17. 70 6787 0 HOH B 722 13.802 97.248 37.723 1.00 16. 39 6788 O HOH B 723 10.187 96.027 32.782 0.40 19. 15 6789 0 HOH B 724 0. 513 89. 660 50. 354 0. 80 15. 84 6790 O HOH B 725-1.090 90. 270 48. 267 0. 80 21.88 6791 0 HOH B 726 21. 280 89. 235 55. 412 0. 60 17. 54 6792 0 HOH B 727 5. 395 86. 164 27. 423 0. 60 24. 72 6793 O HOH B 728 4. 369 84. 459 26. 378 0. 80 22. 68 6794 O HOH B 729 3. 092 79. 548 30. 029 0. 80 18. 95 6795 O HOH B 730-1.248 88. 195 5. 478 1. 00 25.06 6796 0 HOH B 801 27. 892 90. 252 25. 453 1. 00 23. 73 6797 0 HOH B 802 37.672 66.893 40.924 1.00 17. 69 6798 0 HOH B 803 22. 819 71. 570 29. 275 1. 00 20. 44 6799 0 HOH B 804 25. 973 63. 027 36. 316 1. 00 20. 78 6800 O HOH B 805 23. 612 60. 310 28. 015 1. 00 28. 28 6801 0 HOH B 806 16. 973 77. 969 34. 396 1. 00 14. 65 6802 O HOH B 807 28. 351 70. 184 42. 604 1. 00 18. 19 6803 0 HOH B 808 33. 271 72. 285 39. 243 1. 00 19. 47 6804 0 HOH B 809 31. 073 70. 973 39. 634 1. 00 13. 86 6805 0 HOH B 810 21. 383 86. 129 32. 050 1. 00 12. 09 6806 O HOH B 811 35. 345 82. 780 39. 593 1. 00 10. 74 6807 O HOH B 812 41.100 78.204 38.350 1.00 23. 29 6808 0 HOH B 813 18. 370 88. 155 14. 654 1. 00 21. 85 6809 0 HOH B 814 14. 564 87. 046 8. 051 1. 00 26. 33 6830 O HOH B 815-3. 256 88.232 7.461 1.00 15. 53 6811 O HOH B 816-2.265 72. 134 10. 297 1. 00 21.19 68120HOH B 817-0.475 83. 267 31. 386 0. 80 19.74 6813 0 HOH B 818-6.479 87. 850 19. 789 1. 00 21.66 6814 0 HOH B 819-5. 484 72.574 24.044 1.00 20. 59 6815 0 HOH B 820 5. 300 71. 879 31. 182 1. 00 36. 68 6816 O HOH B 821 5. 203 66. 567 23. 068 0. 80 33. 36 6817 0 HOH B 822 8. 357 87. 566 34. 263 0. 60 19. 35 6818 0 HOH B 823 15. 991 96. 966 35. 926 1. 00 13. 36 6819 0 HOH B 824 30.627 88.277 44.509 1.00 19 66 6820 0 HOH B 825 27. 980 93. 547 46. 883 1. 00 27. 27 6821 O HOH B 826 24. 822 92. 089 34. 706 1. 00 17. 10 6822 O HOH B 827 26. 809 93. 042 32. 887 1. 00 16. 84 6823 O HOH B 828 23. 614 97. 411 38. 403 0. 80 10. 89 6824 O HOH B 829 22. 454 97. 206 46. 233 1. 00 20. 20 6825 O HOH B 830 20. 593 94. 462 53. 817 1. 00 18. 90 6826 O HOH B 831 34. 340 67. 576 42. 912 1. 00 10. 74 6827 O HOH B 832 10. 198 86. 303 67. 113 0. 60 31. 02 6828 0 HOH B 833-12.421 75. 171 54. 019 0. 80 22.84 6829 0 HOH B 834-12.606 86. 987 54. 285 0. 60 29.04 6830 O HOH B 835-8.575 98. 222 54. 608 0. 80 30.21 6831 O HOH B 836 29.959 62.968 36.839 0.80 20. 78 6832 0 HOH B 837 36. 292 64. 867 37. 443 1. 00 17. 84 6833 0 HOH B 838 33. 929 65. 625 35. 857 1. 00 19. 27 6834 0 HOH B 839 34. 674 81. 277 45. 627 0. 80 14. 71 6835 O HOH B 840 39. 197 82. 938 25. 612 0. 80 31. 68 6836 O HOH B 841 35.375 87.404 25.304 0.80 28.L 90 6837 0 HOH B 842 36. 051 81. 796 41. 902 0. 80 15. 81 6838 0 HOH B 843 37. 125 84. 702 39. 592 0. 80 15.52 6839 O HOH B 84438. 42483. 40642. 8360. 80 25.52 6840 O HOH B 845 27.769 86.325 25.828 0. 80 22.35 6841 0 HOH B 846 20. 404 81. 426 22. 089 0. 80 28.32 6842 0 HOH B 847 32. 844 69. 803 16. 994 0. 80 31.17 6843 0 HOH B 848 40.195 75.724 21.526 0. 80 33.39 6844 0 HOH B 849 14. 951 74. 115 35. 731 0. 80 21.14 6845 0 HOH B 850 13. 686 66. 228 25. 328 0. 60 24.88 6846 0 HOH B 851 18. 783 62. 222 27. 487 0. 80 26.48 6847 O HOH B 852 20. 135 60. 106 26. 568 0. 40 25.14 6848 0 HOH B 853 24. 384 69. 476 38. 081 0. 80 21.02 6849 0 HOH B 854 27. 198 69. 679 38. 015 1. 00 16.72 6850 O HOH B 855 28. 562 71. 251 39. 082 1. 00 15.11 6851 0 HOH B 856 28. 414 67. 555 37. 233 0. 80 17.31 6852 O HOH B 857 23. 444 76. 101 45. 406 1. 00 21.08 6853 O HOH B 858 30. 200 67. 973 39. 748 0. 80 13.60 6854 O HOH B 859 16. 960 98. 313 33. 333 1. 00 28.75 6855 0 HOH B 860 13. 943 84. 470 30. 070 0. 80 22.69 6856 0 HOH B 861 35. 730 72. 881 38. 252 1. 00 18.13 6857 0 HOH B 862 26. 892 92. 336 24. 573 1. 00 23.53 6858 0 HOH B 863 30. 492 91. 262 25. 556 0. 80 21.19 6859 0 HOH B 864 20. 530 86. 137 10. 625 0. 60 27.70 686- O HOH B 865 11. 656 90. 649 12. 186 0. 60 16.29 6861 O HOH B 866 15. 668 83. 676 15. 036 0. 80 21.78 6862 0 HOH B 867 12. 006 88. 642 5. 054 0. 80 30.61 6863 0 HOH B 868 1. 499 86. 925 7. 137 0. 80 21.70 6864 0 HOH B 869 1. 686 80. 335 8. 745 0. 80 18.24 6865 0 HOH B 870-7.483 81. 661 4. 050 0.80 20.16 6866 O HOH B 881 21. 137 100. 776 39. 921 1. 00 17.59 6867 O HOH B 882 7. 249 70. 278 12. 601 0. 80 24.96 6868 0 HOH B 883-4.089 83. 754 31. 808 0.80 27.84 6869 0 HOH B 884-8.438 78. 992 29. 794 0.80 24.23 6870 O HOH B 885-7.766 84. 939 20. 972 0.60 24.66 6871 0 HOH B 886-9. 328 83. 688 19. 315 1. 00 20.44 6872 O HOH B 887-12.679 80. 501 21. 696 1.00 16.80 6873 O HOH B 888-13.778 74. 192 19. 548 0.80 20.95 6874 0 HOH B 889-15. 239 72. 772 18. 231 0. 80 19.13 6875 0 HOH B 890-14.162 82. 289 11. 146 0.80 20.35 6876 0 HOH B 891 34. 678 94. 410 29. 422 0. 80 26.67 6877 O HOH B 892-4. 002 70. 854 11. 266 0. 60 23.04 6878 O HOH B 893-3.416 71. 284 25. 598 0.80 23.80 6879 0 HOH B 894 7. 832 75. 187 31. 081 0. 60 21.46 6880 O HOH B 895 0. 677 80. 376 31. 684 0. 80 22.10 6881 O HOH B 896-2.557 66. 375 20. 539 0.60 26.53 6882 0 HOH B 897-2.473 64. 792 16. 813 0.80 22.02 6883 O HOH B 898 6. 223 95. 302 19. 396 0. 60 28.20 6884 O HOH B 899 2. 595 88. 459 39. 252 0. 80 25.04 6885 0 HOH B 900 16. 523 91. 074 26. 987 1. 00 24.97 6886 0 HOH B 901 13. 180 89. 610 31. 895 0. 80 17.15 6887 O HOH B 902 11. 121 82. 485 42. 340 0. 60 21.76 6888 O HOH B 903 11. 815 80. 965 39. 737 0. 60 22.77 6889 0 HOH B 904 18. 540 84. 138 49. 546 0. 80 10.02 6890 O HOH B 905 17. 410 78. 613 53. 668 1. 00 30.33 6891 0 HOH B 906 27. 130 82. 380 48. 602 0. 80 22.57 6892 0 HOH B 907 32. 294 90. 032 42. 451 0. 80 17.82 6893 O HOH B 908 26. 531 97. 291 40. 983 0. 60 21.10 6894 O HOH B 909 33. 091 87. 973 35. 862 0. 80 20.88 6895 0 HOH B 910 16. 956 96. 326 53. 028 0. 80 20.01 6896 O HOH B 911 34. 926 89. 166 34. 333 1. 00 25.85 6897 0 HOH B 912 28. 373 95. 132 30. 082 1. 00 14.28 6898 0 HOH B 913 24. 937 95. 895 36. 914 1. 00 14.21 6899 0 HOH B 914-10. 824 86.922 47.067 0. 80 31.00 6900 0 HOH B 915-3. 760 86.923 43.757 0. 80 32.35 6901 0 HOH B 916-10.709 74. 546 60. 011 0.80 26.72 6902 O HOH B 917-2.599 97. 052 43. 709 0.80 25.62 6903 0 HOH B 918 11. 182 104. 558 56. 977 0. 40 18.75 6904 O HOH B 919-9.280 95. 892 45. 265 0.40 21. 26 6905 O HOH B 920-9.476 87. 023 51. 888 0.60 15.67 6906 O HOH B 921 11. 429 80. 805 44. 745 0. 60 17.69 69070HOH B 922 8. 632 76. 200 43. 041 0. 60 23.56 6908 O HOH B 923 20. 013 101. 989 42. 070 0. 60 18.76 6909 O HOH B 924 25. 361 87. 698 27. 261 0. 60 17.19 6910 O HOH B 925 31. 442 89. 667 46. 660 0. 60 15.35 6911 0 HOH B 92626. 89889. 38751. 2720. 60 14.47 69120HOH B 927 17. 572 80. 905 53. 709 0. 60 22.05 6913 O HOH B 928 18. 896 99. 278 33. 304 0. 80 20.85 6914 0 HOH B 929-13.212 87. 013 6. 640 0.60 17.88 6915 0 HOH B 930 20. 399 89. 454 26. 309 0. 60 19.43 6916 O HOH B 931 12. 319 96. 934 33. 434 0. 60 20.35 6917 O HOH B 932 1. 975 84. 899 2. 601 0. 60 17.30 6918 O HOH B 933 16. 853 83. 080 3. 334 0. 60 20.05 6919 0 HOH B 934 9. 839 85. 456 24. 268 0. 40 14.66 6920 O HOH B 935 14. 016 89. 374 27. 420 0. 40 18.29 6921 O HOH B 936 18. 547 89. 854 27. 344 0. 60 19.61 6922 O HOH B 937 5. 959 81. 235 31. 432 0. 60 17.25 6923 O HOH B 938 10. 253 68. 103 24. 474 0. 60 18.05 6924 O HOH B 939 2. 923 62. 228 17. 739 0. 60 20.98 6925 O HOH B 940-6.915 71. 798 21. 665 0.60 25.82 6926 0 HOH B 941-8.908 75. 323 24. 332 0.60 14.61 6927 0 HOH B 942 29.308 96.312 45.866 0. 60 15.40 6928 O HOH B 943-13.605 78. 796 7. 412 0.40 15.26 6929 O HOH B 944-10.569 82. 235 28. 025 0.40 21.21 6930 O HOH B 945-14.739 82. 676 5. 370 0.60 19.04 6931 O HOH B 946 8. 679 91. 531 6. 186 0. 40 19.97 6932 0 HOH B 947 42. 985 79. 109 37. 096 0. 60 21.28 6933 0 HOH B 948 28. 567 67. 945 41. 541 0. 60 15.40 6934 O HOH B 949 31. 598 65. 685 39. 623 0. 80 16.16 6935 O HOH B 950 27. 264 66. 232 40. 866 0. 60 17.02 69360HOH B 951 19. 788 71. 457 48. 569 0. 40 17.67 6937 O HOH B 952 16. 193 69. 350 41. 645 0. 60 19.07 6938 0 HOH B 953 33. 654 62. 243 33. 970 0. 60 18.13 6939 O HOH B 954 31. 753 60. 835 35. 092 0. 60 17.42 6940 O HOH B 955 22. 912 56. 700 36. 203 0. 40 16.47 6941 0 HOH B 956 26. 190 64. 617 44. 084 0. 40 16.11 6942 O HOH B 957 38. 207 87. 304 32. 417 0. 60 16.71 6943 0 HOH B 958 45. 873 86. 226 37. 886 0. 40 15.27 6944 O HOH B 959 19. 520 105. 049 49. 557 0. 40 19.95 6945 O HOH B 960-2.811 91. 712 29. 033 0.60 19.92 TABLE 3 : UHHO Atomic coordinates ATOMRESIDUEXYZQ B 1 C SER 189 29. 357-9.421 6. 417 1.00 33.22 2 O SER 189 29. 284-8.166 6. 494 1.00 34.67 3 N PRO 190 28. 793-10.160 7. 366 1.00 32.21 4 CA PRO 190 27. 860-9. 606 8. 318 1. 00 30.94 5 C PRO 190 28. 563-8.714 9. 327 1.00 29.18 6 0 PRO 190 29. 757-8.882 9. 612 1.00 30.42 7 CB PRO 190 27. 284-10.805 9. 063 1.00 31.38 8 CG PRO 190 28. 115-11.956 8.717 1. 00 31.99 9 CD PRO 190 28. 789-11.640 7. 406 1.00 32.72 10 N PRO 191 27. 799-7.816 9. 918 1.00 26.39 11 CA PRO 191 28. 374-6.945 10. 949 1.00 23.80 12 CB PRO 191 27. 264-5.913 11. 153 1.00 24.63 13 CG PRO 191 25. 988-6.594 10. 766 1.00 24.46 14 CD PRO 191 26. 367-7.575 9. 698 1.00 25.42 15 C PRO 191 28. 600-7.795 12. 195 1.00 20.84 16 0 PRO 191 27. 947-8.825 12. 363 1.00 20.32 17 N VAL 192 29. 534-7.351 13. 064 1.00 17.58 18 CA VAL 192 29. 793-8.035 14. 309 1.00 13.88 19 CB VAL 192 31. 326-8.142 14. 617 1.00 13.57 20 CG1 VAL 192 31. 571-8.889 15. 920 1.00 13.54 21 CG2 VAL 192 32. 080-8.824 13. 503 1.00 13.69 22 C VAL 192 29. 216-7.176 15. 442 1.00 11.06 23 O VAL 192 29. 453-5.990 15. 500 1.00 9.74 24 N VAL 193 28. 460-7.813 16. 328 1.00 11.25 25 CA-VAL 193 27. 943-7.129 17. 518 1.00 10.00 26 CB VAL 193 26. 538-7.596 17. 911 1.00 10.31 27 CG1 VAL 193 26. 064-6.954 19. 205 1.00 9.97 28 CG2 VAL 193 25. 577-7.292 16. 749 1.00 10.56 29 C VAL 193 28. 981-7.388 18. 605 1.00 10.00 30 O VAL 193 29. 331-8.534 18. 840 1.00 9.79 31 N PRO 194 29. 531-6.345 19. 241 1.00 10.31 32 CD PRO 194 29. 149-4.931 19. 008 1.00 9.02 33 CA PRO 194 30. 516-6. 491 20.284 1. 00 10.07 34 CB PRO 194 30. 922-5. 027 20. 595 1. 00 9.66 35 CG PRO 194 29. 624-4.294 20. 305 1.00 9.19 36 C PRO 194 30. 060-7.157 21. 544 1.00 10.94 37 0 PRO 194 28. 881-7.287 21. 961 1.00 11.62 38 N GLN 195 31. 044-7.621 22. 334 1.00 11.01 39 CA GLN 195 30. 726-8.306 23. 584 1.00 11.77 40 CB GLN 195 32. 030-8.949 24. 087 1.00 12.49 41 CG GLN 195 32. 091-9.652 25. 353 1.00 14.75 42 CD GLN 195 32. 165-8.901 26. 655 1.00 16.55 43 OE1 GLN 195 32. 777-7.811 26. 753 1.00 16.40 44 NE2 GLN 195 31. 704-9.553 27. 735 1.00 18.09 45 C GLN 195 30. 125-7.374 24. 620 1.00 12.32 46 0 GLN 195 29. 363-7.722 25. 503 1.00 11.32 47 N SER 196 30. 496-6.109 24. 467 1.00 12.02 48 CA SER 196 30. 115-5.091 25. 445 1.00 12.51 49 CB SER 196 31. 597-4.873 25. 974 1.00 14. 95 50 OG SER 196 31. 576-4. 119 27.089 1. 00 19.16 51 C SER 196 29. 611-3.846 24. 725 1.00 10.38 52 O SER 196 29. 885-3.731 23. 557 1.00 8.61 53 N PHE 197 28. 847-2.999 25. 456 1.00 9.94 54 CA PHE 197 28.285 -1.813 24.828 1. 00 8.47 55 CB PHE 197 27. 457-1.005 25. 864 1. 00 7.58 56 CG PHE 197 26. 870 0. 233 25. 209 1. 00 8. 49 57 CD1 PHE 197 25. 759 0. 124 24. 407 1. 00 10. 30 58 CD2 PHE 197 27. 523 1. 452 25. 299 1. 00 10. 27 59 CE1 PHE 197 25. 226 1. 185 23. 731 1. 00 10. 85 60 CE2 PHE 197 27. 013 2. 557 24. 652 1. 00 12. 19 61 CZ PHE 197 25. 857 2. 454 23. 880 1. 00 12. 39 62 C PHE 197 29. 275-0.901 24. 135 1. 00 7.31 63 O PHE 197 30. 320-0.564 24. 689 1. 00 8.99 64 N GLN 198 28. 975-0.512 22. 926 1. 00 6.87 65 CA GLN 198 29. 751 0. 381 22. 121 1. 00 7. 70 66 CB GLN 198 31. 054-0.197 21. 770 1. 00 11.12 67 CG GLN 198 31. 591-1.378 21. 405 1. 00 11.82 68 CD GLN 198 32. 829-2.079 20. 994 1. 00 8.02 69 OE1 GLN 198 33. 646-2.531 21. 761 1. 00 8.11 70 NE2 GLN 198 32. 952-2.141 19. 670 1. 00 8.83 71 C GLN 198 29. 019 1. 279 21. 177 1. 00 7. 39 72 0 GLN 198 27. 850 1. 045 20. 811 1. 00 6. 88 73 N VAL 199 29. 659 2. 404 20. 805 1. 00 6. 77 74 CA VAL 199 29. 119 3. 371 19. 883 1. 00 7. 17 75 CB VAL 199 29.051 4.821 20.465 1.00 7. 48 76 CG1 VAL 199 28. 448 5. 786 19. 447 1. 00 6. 62 77 CG2 VAL 199 28. 336 4. 829 21. 789 1. 00 9. 11 78 C VAL 199 29. 906 3. 359 18. 617 1. 00 7. 60 79 O VAL 199 31. 131 3. 658 18. 720 1. 00 8. 39 80 N ALA 200 29. 370 2. 994 17. 462 1. 00 6. 77 81 CA ALA 200 30. 096 2. 965 16. 225 1. 00 7. 55 82 CB ALA 200 30.218 1.590 15.566 1.00 7. 66 83 C ALA 200 29.527 3. 928 15. 198 1. 00 8.04 84 0 ALA 200 28. 387 4. 432 15. 330 1. 00 7. 84 5 N HIS 201 30. 354 4. 317 14. 258 1. 00 7. 61 86 CA HIS 201 30. 019 5. 211 13. 170 1. 00 7. 48 87 CB HIS 201 30. 986 6. 398 13. 007 1. 00 6. 52 88 CG HIS 201 30.869 7.322 14.208 1.00 5. 56 89 CD2 HIS 201 31. 267 7. 254 15. 472 1. 00 6. 93 90 ND1 HIS 201 30. 162 8. 502 14. 071 1. 00 5. 79 91 CE1 HIS 201 30. 147 9. 128 15. 211 1. 00 6. 96 92 NE2 HIS 201 30.817 8.391 16.118 1.00 7. 09 93 C HIS 201 29. 957 4. 462 11. 849 1. 00 9. 36 94 O HIS 201 30.815 3.659 11.476 1.00 11. 01 95 N LEU 202 28. 892 4. 709 11. 117 1. 00 8. 85 96 CA LEU 202 28. 677 4. 132 9. 820 1. 00 9. 52 97 CB LEU 202 27.367 3.297 9.78 1.00 8. 12 98 CG LEU 202 27.010 2.664 8.431 1.00 8. 03 99 CD1 LEU 202 28. 169 1. 799 7. 903 1. 00 7. 69 100 CD2 LEU 202 25. 797 1. 702 8. 652 1. 00 7. 64 101 C LEU 202 28. 679 5. 251 8. 793 1. 00 10. 44 102 0 LEU 202 27. 689 5. 982 8. 659 1. 00 9. 59 103 N HIS 203 29. 791 5. 400 8. 061 1. 00 11. 43 104 CA HIS 203 29. 854 6. 411 7. 011 1. 00 13. 28 105 CB HIS 203 31. 091 7. 279 7. 033 1. 00 13. 75 106 CG HIS 203 31. 280 8. 011 8. 331 1. 00 15. 20 107 CD2 HIS 203 30.439 8.290 9.354 1.00 14. 54 108 ND1 HIS 203 32. 528 8. 418 8. 741 1. 00 17. 68 109 CE1 HIS 203 32.417 9.042 9.922 1.00 15. 89 110 NE2 HIS 203 31. 162 8. 972 10. 310 1. 00 14. 00 111 C HIS 203 29.711 5.728 5.648 1.00 14. 64 1120HIS20330. 5934. 9925. 2271. 00 15.73 113 N ALA 204 28. 597 5. 936 4. 976 1. 00 15.12 114 CA ALA 204 28.407 5.253 3.669 1. 00 15.52 115 CB ALA 204 27. 956 3. 820 3. 956 1. 00 14.48 116 C ALA 204 27. 457 6. 053 2. 842 1. 00 15. 91 117 0 ALA 204 26. 616 6. 798 3. 386 1. 00 17.00 118 N PRO 205 27. 534 5. 984 1. 527 1. 00 16.59 119 CA PRO 205 26. 692 6. 729 0. 648 1. 00 17.75 120 CB PRO 205 27. 251 6. 477-0.748 1.00 18.19 121 CG PRO 205 28. 501 5. 688-0.580 1.00 18.15 122 CD PRO 205 28. 510 5. 114 0. 801 1. 00 17.20 123 C PRO 205 25. 205 6. 393 0. 673 1. 00 18.28 124 O PRO 205 24. 712 5. 332 1. 062 1. 00 18.17 125 N THR 206 24. 456 7. 391 0. 264 1. 00 18.73 126 CA THR 206 22. 993 7. 285 0. 129 1. 00 18.77 127 CB THR 206 22. 466 8. 520-0.632 1.00 18.61 128 OG1 THR 206 22. 923 9. 659 0. 084 1. 00 20.08 129 CG2 THR 206 20. 967 8. 515-0.787 1.00 19.09 130 C THR 206 22. 796 6. 132-0.902 1.00 19.07 131 O THR 206 23. 599 6. 042-1.846 1.00 18.59 132 N GLY 207 21. 758 5. 375-0.651 1.00 19.34 133 CA GLY 207 21. 447 4. 263-1.529 1.00 19.45 134 C GLY 207 22. 324 3. 101-1.171 1.00 19.87 135 O GLY 207 22. 270 2. 096-1.889 1.00 21.48 136 N SER 208 23. 124 3. 154-0.095 1.00 19.52 137 CA SER 208 23. 968 1. 968 0. 157 1. 00 19.44 138 CB SER 208 25. 371 2. 310 0. 588 1. 00 20.12 139 OG SER 208 25. 392 2. 960 1. 831 1. 00 19.89 140 C SER 208 23. 317 0. 975 1. 091 1. 00 19.26 141 O SER 208 23. 906-0. 108 1. 258 1. 00 21.57 142 N GLY 209 22.190 1.265 1.728 1. 00 17.60 143 CA GLY 209 21. 524 0. 317 2. 602 1. 00 15.72 144 C GLY 209 21. 697 0. 567 4. 072 1. 00 14.77 145 O GLY 209 21. 474-0.306 4. 935 1.00 14.71 146 N LYS 210 22. 180 1. 765 4. 438 1. 00 13.96 147 CA LYS 210 22. 376 2. 071 5. 844 1. 00 13.31 148 CB LYS 210 22. 771 3. 561 6. 075 1. 00 14.15 149 CG LYS 210 24. 157 3. 890 5. 552 1. 00 14.73 150 CD LYS 210 24.601 5.305 5.766 1. 00 14.53 151 CE LYS 210 23. 796 6. 345 5. 073 1. 00 14.39 152 NZ LYS 210 23. 785 6. 266 3. 604 1. 00 15.55 153 C LYS 210 21. 118 1. 787 6. 648 1. 00 12.47 154 0 LYS 210 21. 199 1. 337 7. 778 1. 00 11.23 155 N SER 211 19. 955 2. 160 6. 082 1. 00 13.02 156 CA SER 211 18. 705 1. 992 6. 808 1. 00 13.99 157 CB SER 211 17. 869 3. 295 6. 596 1. 00 16.47 158 OG SER 211 17. 887 3. 470 5. 145 1. 00 20.35 159 C SER 211 17. 861 0. 804 6. 393 1. 00 13.97 160 0 SER 211 16. 761 0. 650 6. 897 1. 00 14.25 161 N THR 212 18. 378-0.044 5. 505 1.00 13.03 162 CA THR 212 17. 623-1.201 5. 013 1.00 12.75 163 CB THR 212 17. 113-0.912 3. 586 1.00 13.47 164 OG1 THR 212 18. 187-0.555 2. 710 1.00 14. 52 165 CG2 THR 212 16. 116 0. 269 3. 590 1. 00 13.75 166 C THR 212 18. 438-2.480 5. 116 1.00 12.68 167 0 THR 212 18. 131-3.351 5. 908 1.00 11.40 168 N LYS 213 19. 502-2.572 4. 319 1.00 13.08 169 CA LYS 213 20. 396-3.733 4. 330 1. 00 13.25 170 CB LYS 213 21. 451-3.566 3. 307 1. 00 17. 28 171 CG LYS 213 21. 398-3.638 1. 865 1. 00 21.71 172 CD LYS 213 22. 656-3.146 1. 215 1. 00 25.12 173 CE LYS 213 23. 968-3.749 1. 640 1. 00 26.32 174 NZ LYS 213 25. 072-2.939 0. 920 1. 00 28.47 175 C LYS 213 21. 077-3.906 5. 691 1. 00 11.52 1760LYS21321. 155-5.043 6. 148 1. 00 10. 66 177 N VAL 214 21. 590-2.838 6. 306 1. 00 9.94 178 CA VAL 214 22. 222-2.941 7. 613 1. 00 9.49 179 CB VAL 214 22. 924-1.657 8. 033 1. 00 9.23 180 CG1 VAL 214 23. 576-1.791 9. 425 1. 00 10.28 181 CG2 VAL 214 24. 023-1.329 7. 017 1. 00 11.28 182 C VAL 214 21. 328-3.509 8. 696 1. 00 8.94 183 0 VAL 214 21. 663-4.508 9. 344 1. 00 8.29 184 N PRO 215 20. 173-2.906 8. 972 1. 00 7.98 185 CD PRO 215 19. 691-1.681 8. 296 1. 00 8.67 186 CA PRO 215 19. 237-3.430 9. 936 1. 00 8.38 187 CB PRO 215 18. 021-2.506 9. 865 1. 00 8.60 188 CG PRO 215 18. 337-1.462 8. 912 1. 00 9.12 189 C PRO 215 18. 803-4.873 9. 542 1. 00 7.93 1900PRO21518. 612-5.663 10. 491 1. 00 8.91 191 N ALA 216 18. 676-5.173 8. 272 1. 00 8.61 192 CA ALA 216 18. 247-6.541 7. 933 1. 00 10.10 193 CB ALA 216 17. 833-6.692 6. 515 1. 00 9.72 194 C ALA 216 19. 347-7.521 8. 362 1. 00 12.46 195 0 ALA 216 19. 086-8.597 8. 891 1. 00 13.41 196 N ALA 217 20. 591-7.100 8. 124 1. 00 11.62 197 CA ALA 217 21. 733-7.934 8. 473 1. 00 12.53 198 CB ALA 217 23. 002-7.318 7. 906 1. 00 12.28 199 C ALA 217 21. 794-8.225 9. 942 1. 00 12.47 200 O ALA 217 22. 107-9.375 10. 297 1. 00 13.77 201 N TYR 218 21. 641-7.262 10. 840 1. 00 11.78 202 CA TYR 218 21. 665-7.514 12. 257 1. 00 12.24 203 CB TYR 218 21. 621-6.238 13. 097 1. 00 12.19 204 CG TYR 218 22. 840-5.344 13. 016 1. 00 12.75 205 CD1 TYR 218 22. 841-4.126 12. 368 1. 00 12.09 206 CE1 TYR 218 23. 992-3.328 12. 399 1. 00 13.42 207 CD2 TYR 218 23. 972-5.744 13. 730 1. 00 14.03 208 CE2 TYR 218 25. 121-4.957 13. 746 1. 00 13.85 209 CZ TYR 218 25. 114-3.751 13. 058 1. 00 14.20 210 OH TYR 218 26. 272-3.026 13. 055 1. 00 15.50 211 C TYR 218 20. 467-8.375 12. 702 1. 00 13.11 212 0 TYR 218 20. 583-9.133 13. 638 1. 00 13.27 213 N ALA 219 19. 326-8.180 12. 010 1. 00 14.42 214 CA ALA 219 18. 130-8.949 12. 418 1. 00 14.95 215 CB ALA 219 16. 857-8.439 11. 798 1. 00 13.81 216 C ALA 219 18. 374-10.424 12. 087 1. 00 14.59 217 O ALA 219 17. 950-11.253 12. 873 1. 00 15.36 218 N ALA 220 19. 028-10.694 10. 990 1. 00 15.44 219 CA ALA 220 19. 349-12.054 10. 533 1. 00 14.86 220 CB ALA 220 20. 103-11.938 9. 201 1. 00 13.62 221 C ALA 220 20. 162-12.829 11. 540 1. 00 15.86 222 O ALA 220 20. 203-14.066 11. 616 1. 00 16.20 223 N GLN 221 20.788 - 12.113 12.441 1.00 15. 36 224 CA GLN 221 21. 638-12.672 13. 502 1. 00 16.28 225 CB GLN 221 22. 854-11.787 13. 336 1. 00 18.56 226 CG GLN 221 24. 150-11.878 13. 884 1. 00 20.71 227 CD GLN 221 25. 241-10.948 13. 356 1. 00 19.81 228 OE1 GLN 221 25. 215-10.254 12. 347 1. 00 19.37 229 NE2 GLN 221 26. 336-11.034 14. 098 1. 00 20.65 230 C GLN 221 20. 887-12.815 14. 785 1. 00 14.99 231 0 GLN 221 21. 369-13.228 15. 849 1. 00 15.23 232 N GLY 222 19. 564-12.515 14. 770 1. 00 13.19 233 CA GLY 222 18. 720-12.648 15. 929 1. 00 12.35 234 C GLY 222 18. 606-11.448 16. 830 1. 00 13.10 235 O GLY 222 17. 975-11.516 17. 900 1. 00 14.16 236 N TYR 223 19. 131-10.270 16. 409 1. 00 12.03 237 CA TYR 223 19. 002-9.096 17. 272 1. 00 11.23 238 CB TYR 223 20. 251-8.174 17. 085 1. 00 10.33 239 CG TYR 223 21. 527-8.893 17. 501 1. 00 10.23 240 CD1 TYR 223 22. 405-9.398 16. 574 1. 00 12.20 241 CE1 TYR 223 23. 567-10.060 16. 981 1. 00 13.94 242 CD2 TYR 223 21. 762-9.097 18. 844 1. 00 13.12 243 CE2 TYR 223 22. 916-9.775 19. 267 1. 00 14.57 244 CZ TYR 223 23. 808-10.225 18. 321 1. 00 15.12 245 OH TYR 223 24. 951-10.879 18. 759 1. 00 16.59 246 C TYR 223 17. 758-8.236 16. 939 1. 00 9.49 247 0 TYR 223 17. 254-8.258 15. 835 1. 00 9.16 248 N LYS 224 17. 380-7.479 17. 954 1. 00 10.65 249 CA LYS 224 16 255-6.526 17. 848 1. 00 10.64 250 CB LYS 224 15. 536-6.390 19. 160 1. 00 11.74 251 CG LYS 224 15. 051-7.773 19. 694 1. 00 15.18 252 CD LYS 224 14. 351-7.684 20. 967 1. 00 17.55 253 CE LYS 224 14.823 - 7.265 22.267 1.00 19. 97 254 NZ LYS 224 15. 813-7.949 23. 092 1. 00 21.23 255 C LYS 224 16. 898-5.182 17. 465 1. 00 10.06 256 O LYS 224 17. 821-4.748 18. 138 1. 00 10.35 257 N VAL 225 16. 445-4.585 16. 391 1. 00 10.06 258 CA VAL 225 16. 938-3.377 15. 837 1. 00 8.59 259 CB VAL 225 17. 491-3.561 14. 387 1. 00 9.70 260 CG1 VAL 225 18. 263-2.320 13. 991 1. 00 8.88 261 CG2 VAL 225 18. 335-4.823 14. 269 1. 00 10.86 262 C VAL 225 15. 939-2.198 15. 771 1. 00 8.10 263 O VAL 225 14. 887-2. 283 15.188 1.00 8. 59 264 N LEU 226 16. 437-1.078 16. 335 1. 00 7.34 265 CA LEU 226 15. 649 0.186 16. 262 1. 00 6.39 266 CB LEU 226 15. 520 0.824 17. 615 1. 00 5.76 267 CG LEU 226 14. 860 2. 242 17. 624 1. 00 6. 55 268 CD1 LEU 226 13. 430 2.110 17. 045 1. 00 7.13 269 CD2 LEU 226 14. 889 2.790 19. 032 1. 00 7.15 270 C LEU 226 16. 352 1.110 15. 258 1. 00 6.25 271 0 LEU 226 17. 575 1.338 15. 426 1. 00 6.91 272 N VAL 227 15. 688 1.586 14. 244 1. 00 4.45 273 CA VAL 227 16. 215 2.478 13. 223 1. 00 4.83 274 CB VAL 227 16. 117 1.902 11. 820 1. 00 4.96 275 CG1 VAL 227 16. 772 2.841 10. 788 1. 00 7.25 276 CG2 VAL 227 16. 718 0.484 11. 709 1. 00 4.61 277 C VAL 227 15. 559 3.863 13. 361 1. 00 6.89 278 O VAL 227 14. 340 4.027 13. 171 1. 00 6.46 279 N LEU 228 16. 392 4.887 13. 716 1. 00 6. 98 280 CA LEU 228 15. 823 6.244 13. 899 1. 00 6.72 281 CB LEU 228 16. 254 6.819 15. 233 1. 00 7.17 282 CG LEU 228 15. 877 6.032 16. 497 1. 00 6.37 283 CD1 LEU 228 16.431 6.686 17.748 1.00 6. 51 284 CD2 LEU 228 14. 355 5. 918 16. 625 1. 00 5. 63 285 C LEU 228 16.038 7.166 12.736 1.00 5.] 94 286 0 LEU 228 17. 134 7. 093 12. 142 1. 00 6. 33 287 N ASN 229 15. 116 8. 053 12. 391 1. 00 6. 04 288 CA ASN 229 15. 266 8. 962 11. 253 1. 00 6. 73 289 CB ASN 229 14. 739 8. 238 10. 043 1. 00 10. 26 290 CG ASN 229 15. 093 8. 787 8. 702 1. 00 13. 30 291 OD1 ASN 229 14. 481 9. 789 8. 277 1. 00 15. 80 <BR> <BR> 292 ND2 ASN 229 16. 143 8. 258 8. 077 1. 00 13. 21 293 C ASN 229 14. 515 10. 275 11. 507 1. 00 7. 24 294 0 ASN 229 13. 544 10. 302 12. 253 1. 00 5. 83 295 N PRO 230 14. 980 11. 379 10. 976 1. 00 8. 89 296 CD PRO 230 16. 175 11. 568 10. 113 1. 00 8. 55 297 CA PRO 230 14. 330 12. 657 11. 200 1. 00 10. 04 298 CB PRO 230 15.377 13.705 10.801 1.00 10. 52 299 CG PRO 230 16. 615 12. 963 10. 512 1. 00 9. 54 300 C PRO 230 13. 015 12. 805 10. 479 1. 00 11. 24 301 O PRO 230 12.108 13.495 11.008 1.00 14. 55 302 N SER 231 12. 766 12. 167 9. 393 1. 00 11. 59 303 CA SER 231 11. 556 12. 256 8. 599 1. 00 12. 70 304 CB SER 231 12.037 12.217 7.150 1.00 13. 86 305 OG SER 231 11. 024 12. 052 6. 233 1. 00 18. 13 306 C SER 231 10. 489 11. 203 8. 813 1. 00 13. 30 307 O SER 231 10. 779 10. 020 8. 827 1. 00 11. 58 308 N VAL 232 9. 233 11. 687 8. 946 1. 00 13. 14 309 CA VAL 232 8. 055 10. 821 9. 086 1. 00 12. 69 310 CB'VAZ 232 6. 765 11. 623 9. 348 1. 00 13. 10 311 CG1 VAL 232 5.476 10.827 9.191 1.00 12. 92 312 CG2 VAL 232 6. 797 12. 151 10. 776 1. 00 14. 63 <BR> <BR> 313 C VAL 232 7. 898 10. 078 7. 746 1. 00 12. 01 314 O VAL 232 7. 752 8. 886 7. 694 1. 00 10. 30 315 N ALA 233 8. 047 10. 871 6. 674 1. 00 13. 23 316 CA ALA 233 7. 965 10. 352 5. 330 1. 00 13. 52 317 CB ALA 233 8. 073 11. 476 4. 348 1. 00 13. 68 318 C ALA 233 8. 962 9. 230 5. 066 1. 00 14. 41 319 O ALA 233 8. 559 8. 187 4. 521 1. 00 14. 75 320 N ALA 234 10. 201 9. 400 5. 487 1. 00 14. 37 321 CA ALA 234 11.228 8.365 5.283 1.00 14. 53 322 CB ALA 234 12.640 8.900 5.461 1.00 14. 13 323 C ALA 234 10. 974 7. 165 6. 168 1. 00 13. 71 324 O ALA 234 11. 089 6. 031 5. 700 1. 00 15. 57 325 N THR 235 10. 584 7. 375 7. 403 1. 00 12. 88 326 CA THR 235 10.293 6.308 8.357 1.00 12. 47 327 CB THR 235 9.945 6.871 9.723 1.00 11. 16 328 OG1 THR 235 11. 035 7. 637 10. 274 1. 00 10. 91 329 CG2 THR 235 9. 500 5. 820 10. 731 1. 00 8. 84 330 C THR 235 9. 146 5. 426 7. 842 1. 00 13. 71 331 0 THR 235 9. 275 4. 212 7. 815 1. 00 13. 96 332 N LEU 236 8. 063 6. 044 7. 377 1. 00 14. 31 333 CA LEU 236 6. 912 5. 349 6. 846 1. 00 15. 70 334 CB LEU 236 5. 770 6. 282 6. 530 1. 00 14. 95 335 CG LEU 236 5. 068 7. 084 7. 629 1. 00 14. 18 336 CD1 LEU 236 4. 059 8. 031 6. 975 1. 00 14. 44 337 CD2 LEU 236 4. 313 6. 087 8. 540 1. 00 13. 95 338 C LEU 236 7.303 4.585 5.566 1.00 17. 44 339 O LEU 236 6. 817 3. 474 5. 332 1. 00 17. 72 340 N GLY 237 8. 151 5. 218 4. 774 1. 00 18.54 341 CA BLY 237 8.648 4.676 3.536 1. 00 20.53 342 C GLY 237 9.496 3.444 3.685 1. 00 22.53 343 O GLY 237 9. 405 2. 534 2. 850 1. 00 23.43 344 N PHE 238 10. 299 3. 358 4. 749 1. 00 24.36 345 CA PHE 238 11. 144 2. 188 4. 950 1. 00 27.06 346 CB PHE 238 12. 103 2. 275 6. 131 1. 00 26.30 347 CG PHE 238 13. 084 3. 384 6. 050 1. 00 25. 77 348 CD1 PHE 238 14. 041 3. 429 5. 055 1. 00 25. 30 349 CE1 PHE 238 14. 937 4. 482 4. 994 1. 00 25.49 350 CZ PHE 238 14. 924 5. 467 5. 957 1. 00 24.58 351 CE2 PHE 238 14. 010 5. 404 6. 980 1. 00 24.30 352 CD2 PHE 238 13.108 4.362 7.040 1. 00 25.11 353 C PHE 238 10. 351 0. 894 5. 102 1. 00 28.51 354 0 PHE 238 10. 790-0.151 4. 595 1.00 29.05 355 N GLY 239 9. 231 0. 975 5. 812 1. 00 29.21 356 CA GLY 239 8. 398-0.188 6. 054 1.00 29.71 357 C GLY 239 7. 829-0.762 4. 788 1.00 30.59 358 O GLY 239 7. 688-1. 990 4. 605 1. 00 30.69 359 N ALA 240 7. 492 0. 155 3. 872 1. 00 30.87 360 CA ALA 240 6. 942-0.320 2. 586 1.00 31.00 361 CB ALA 240 6. 207 0. 817 1. 902 1. 00 32.65 362 C ALA 240 8. 084-0.879 1. 751 1.00 30.75 3630ALA2407. 959-1.877 1. 036 1.00 30.41 364 N TYR 241 9. 250-0.217 1. 843 1.00 30.02 365 CA TYR 241 10. 410-0.690 1. 095 1.00 29.80 366 CB TYR 241 11. 534 0. 354 1. 222 1. 00 31.01 367 CG TYR 241 12. 775-0.057 0. 452 1.00 32.76 368 CD1 TYR 241 13. 714-0.919 1. 002 1.00 33.77 369 CE1 TYR 241 14. 820-1.315 0. 289 1.00 34.21 370 CD2 TYR 241 13. 012 0. 442-0.816 1.00 34.17 371 CE2 TYR 241 14. 139 0. 080-1.529 1.00 34.77 372 CZ TYR 241 15. 024-0.809-0.976 1.00 35.19 373 OH TYR 241 16. 137-1.196-1.687 1.00 37.11 374 C TYR 241 10. 915-2.043 1. 586 1.00 29.11 375 O TYR 241 11. 316-2.873 0. 776 1.00 29.50 376 N MET 242 11. 018-2.248 2. 899 1.00 28.46 377 CA MET 242 11. 503-3.475 3. 485 1.00 28.33 378 CB MET 242 11. 721-3.323 5. 012 1.00 24.22 379 CG MET 242 12. 860-2.389 5. 349 1.00 20.64 380 SD MET 242 14. 545-3.007 5. 005 1.00 18.76 381 CE MET 242 14. 811-4.062 6. 393 1.00 16.18 382 C MET 242 10. 780-4.754 3. 119 1.00 30.41 383 0 MET 242 11. 395-5.851 3. 123 1.00 30.32 384 N SER 243 9. 481-4.691 2. 807 1.00 32.11 385 CA SER 243 8. 744-5.900 2. 414 1.00 34.82 386 CB SER 243 7. 245-5.629 2. 273 1.00 35.03 387 OG ER 243 6.687 -5.109 3.474 1. 00 35.04 388 C SER 243 9. 231-6.308 1. 007 1.00 36.59 389 O SER 243 9. 700-7.407 0. 738 1.00 36.87 390 N LYS 244 9. 096-5.307 0. 119 1.00 38.09 391 CA LYS 244 9. 467-5.479-1.278 1.00 38.74 392 CB LYS 244 8. 803-4.357-2.141 1.00 41.08 393 CG LYS 244 8. 928-4.642-3.612 1.00 44.30 394 CD LYS 244 8. 420-3.687-4.628 1.00 46.62 395 CE LYS 244 8. 684-4.248-6.051 1.00 47.99 396 NZ LYS 244 8. 136-3.290-7.069 1.00 49.16 397 C LYS 244 10. 953-5.498-1.495 1.00 38.12 398 O LYS 244 11. 400-5.306-2.624 1.00 39.32 399 N ALA 245 11. 781-5.692-0.477 1.00 37.24 400 CA ALA 245 13. 241-5.709-0.723 1.00 36.59 401 CB ALA 245 13. 876-4.429-0.283 1.00 36.60 402 C ALA 245 13. 837-6.904 0. 011 1.00 36.51 403 O ALA 245 14. 424-7.778-0.603 1.00 37.84 404 N HIS 246 13. 580-6.967 1. 301 1.00 35.40 405 CA HIS 246 14. 033-8. 022 2. 180 1. 00 34.62 406 CB HIS 246 14. 745-7.283 3. 356 1.00 34.72 407 CG HIS 246 15. 842-6.403 2. 795 1.00 35.06 408 CD2 HIS 246 17. 173-6.589 2. 668 1.00 35.64 409 ND1 HIS 246 15. 574-5.141 2. 300 1.00 35.19 410 CE1 HIS 246 16. 698-4.589 1. 871 1.00 35.32 411 NE2 HIS 246 17. 679-5.433 2. 086 1.00 36.17 412 C HIS 246 12. 870-8.847 2. 714 1.00 34.08 413 O HIS 246 13. 028-9.543 3. 724 1.00 34.39 414 N GLY 247 11. 696-8.771 2. 078 1.00 33.05 415 CA GLY 247 10. 531-9.522 2. 576 1.00 32.04 416 C GLY 247 10. 255-9.323 4. 055 1.00 30.89 417 O GLY 247 9. 740-10.234 4. 760 1.00 31.83 418 N ILE 248 10. 569-8.138 4. 593 1.00 28.30 419 CA ILE 248 10. 364-7.851 5. 999 1.00 25.08 420 CB ILE 248 11. 675-7.281 6. 601 1.00 24.79 421 CG2 ILE 248 11. 524-6.859 8. 053 1.00 23.10 422 CG1 ILE 248 12. 795-8.341 6. 474 1.00 25.39 423 CD1 ILE 248 14. 164-7.788 6. 823 1.00 25.35 424 C ILE 248 9. 267-6.788 6. 180 1.00 22.85 425 O ILE 248 9. 266-5.806 5. 485 1.00 22.16 426 N ASP 249 8. 362-7.040 7. 084 1.00 21.59 427 CA ASP 249 7. 315-6.094 7. 460 1.00 20.40 428 CB ASP 249 5. 875-6.621 7. 376 1.00 25.12 429 CG ASP 249 5. 528-6.695 5. 894 1.00 29.56 430 OD1 ASP 249 4. 906-5.704 5. 424 1.00 32.83 431 OD2 ASP 249 5. 968-7.636 5. 218 1.00 32.70 432 C ASP 249 7. 634-5.650 8. 889 1.00 16.59 433 O ASP 249 7. 301-6.314 9. 859 1.00 16.89 434 N PRO 250 8. 387-4.562 8. 983 1.00 14.94 435 CD PRO 250 8. 834-3. 714 7. 854 1. 00 14.03 436 CA PRO 250 8. 800-4.047 10. 267 1.00 14.20 437 CB PRO 250 9. 946-3.105 9. 879 1.00 13.72 438 CG PRO 250 9. 553-2.581 8. 547 1.00 14.02 439 C PRO 250 7. 727-3.219 10. 972 1.00 13.55 4400PRO2506. 750-2.806 10. 337 1.00 13.75 441 N ASN 251 7. 997-2.990 12. 236 1.00 12.02 442 CA ASN 251 7. 115-2.105 13. 048 1.00 11.69 443 CB ASN 251 7. 431-2.273 14. 496 1.00 11.59 444 CG ASN 251 7. 328-3.714 14. 974 1.00 12.78 445 OD1 ASN 251 6. 239-4.248 15. 104 1.00 14.31 446 ND2 ASN 251 8. 484-4.276 15. 351 1.00 11.64 447 C ASN 251 7. 549-0.664 12. 633 1.00 11.98 448 O ASN 251 8. 719-0.477 12. 299 1.00 10.90 449 N ILE 252 6.602 0.205 12.550 1. 00 11.24 450 CA ILE 252 6. 813 1. 597 12. 126 1. 00 11.14 451 CB ILE 252 6. 184 1. 796 10. 735 1. 00 13.40 452 CG2 ILE 252 6. 366 3. 231 10. 213 1. 00 13.45 453 CG1 ILE 252 6.788 0.784 9.764 1. 00 13.79 454 CD1 ILE 252 6. 305 0. 763 8. 387 1. 00 15.55 455 C ILE 252 6. 164 2. 502 13. 146 1. 00 11.21 456 0 ILE 252 4. 985 2. 259 13. 511 1. 00 10.22 457 N ARG 253 6. 909 3. 508 13. 644 1. 00 9.89 458 CA ARG 253 6. 325 4. 390 14. 634 1. 00 9.03 459 CB ARG 253 6. 865 4. 116 16. 038 1. 00 9.12 460 CG ARG 253 6. 741 2. 637 16. 484 1. 00 8.88 461 CD ARG 253 7. 156 2. 444 17. 896 1. 00 11.14 462 NE ARG 253 6. 379 3. 137 18. 894 1. 00 11.54 463 CZ ARG 253 5. 117 2. 862 19. 194 1. 00 13.00 464 NH1 ARG 253 4. 502 1. 845 18. 569 1. 00 14.31 465 NH2 ARG 253 4. 477 3. 578 20. 086 1. 00 12.29 466 C ARG 253 6. 547 5. 859 14. 249 1. 00 9.82 467 O ARG 253 7. 688 6. 302 14. 037 1. 00 9.84 468 N THR 254 5. 492 6. 593 14. 019 1. 00 10.00 469 CA THR 254 5. 505 8. 007 13. 711 1. 00 10.46 470 CB THR 254 5. 295 8. 452 12. 278 1. 00 9.80 471 OG1 THR 254 3. 950 8. 101 11. 865 1. 00 10.23 472 CG2 THR 254 6. 297 7. 870 11. 282 1. 00 8.76 473 C THR 254 4. 402 8. 652 14. 584 1. 00 10.81 474 0 THR 254 3. 510 8. 010 15. 179 1. 00 10.16 475 N GLY 255 4. 485 9. 977 14. 710 1. 00 11.68 476 CA GLY 255 3. 462 10. 647 15. 536 1. 00 12.93 477 C GLY 255 2. 107 10. 522 14. 843 1. 00 13.02 478 O GLY 255 1. 144 10. 576 15. 586 1. 00 14.78 479 N VAL 256 2. 004 10. 326 13. 567 1. 00 13.36 480 CA VAL 256 0. 779 10. 230 12. 814 1. 00 14.38 481 CB VAL 256 1. 016 10. 817 11. 403 1. 00 15.31 482 CG1 VAL 256 2. 060 10. 071 10. 596 1. 00 16.24 483 CG2 VAL 256-0. 260'10. 854 10. 571 1. 00 19.85 484 C VAL 256 0. 205 8. 818 12. 662 1. 00 14.11 485 O VAL 256 -1.008 8.592 12.508 1. 00 14.42 486 N ARG 257 1. 094 7. 842 12. 660 1. 00 12.62 487 CA ARG 257 0. 680 6. 458 12. 442 1. 00 13.01 488 CB ARG 257 0. 737 6. 316 10. 899 1. 00 16.71 489 CG ARG 257 0. 251 5. 034 10. 289 1. 00 19.17 490 CD ARG 257 0. 519 5. 065 8. 793 1. 00 23.26 491 NE ARG 257 0. 006 3. 949 8. 044 1. 00 26.93 492 CZ ARG 257-1. 276 3. 657 7. 781 1. 00 29.04 493 NH1 ARG 257-2. 287 4. 414 8. 177 1. 00 27.10 494 NH2 ARG 257-1. 555 2. 561 7. 062 1. 00 30.91 495 C ARG 257 1. 720 5. 493 12. 999 1. 00 12.15 496 0 ARG 257 2. 953 5. 738 12. 818 1. 00 11.55 497 N THR 258 1. 251 4. 440 13. 620 1. 00 11.61 498 CA THR 258 2. 174 3. 402 14. 116 1. 00 12.62 499 CB THR 258 2. 397 3. 306 15. 599 1. 00 13.29 500 OG1 THR 258 1. 188 2. 985 16. 267 1. 00 17.13 501 CG2 THR 258 3. 011 4. 541 16. 210 1. 00 11.63 502 C THR 258 1. 670 2. 054 13. 560 1. 00 12.86 503 O THR 258 0. 475 1. 820 13. 507 1. 00 13.06 05 N ILE 259 2.563 1.224 13.108 1. 00 12.80 505 CA ILE 259 2. 314-0.101 12. 551 1.00 11.76 506 CB ILE 259 2. 683-0.138 11. 084 1.00 10.24 507 CG2 ILE 259 2. 441-1.502 10. 420 1.00 10.56 508 CG1 ILE 259 1.908 0.959 10.325 1. 00 8.87 509 CD1 ILE 259 2.437 1.129 8.916 1. 00 10.18 510 C ILE 259 3. 128-1.085 13. 416 1.00 13.50 511 ILE2594. 340-0.908 13. 673 1. 00 12.95 512 N THR 260 2. 448-2.074 13. 969 1. 00 13.40 513 CA THR 260 3. 039-3.092 14. 827 1. 00 13.22 514 CB THR 260 2. 513-3. 017 16. 244 1. 00 13. 53 515 OG1 THR 260 2. 692-1.695 16. 803 1. 00 15.31 516 CG2 THR 260 3. 172-4.001 17. 180 1. 00 13.40 517 C THR 260 2. 757-4.479 14. 247 1. 00 14. 19 518 0 THR 260 1. 628-4.878 13. 996 1. 00 14.34 519 N THR 261 3. 841-5. 203 13. 98) 1. 00 14. 55 520 CA THR 261 3. 807-6.534 13. 392 1. 00 15.22 521 CB THR 261 4. 546-6.517 12. 030 1. 00 15.05 522 OG1 THR 261 5. 924-6.146 12. 303 1. 00 15.56 523 CG2 THR 261 3. 969-5.479 11. 100 1. 00 14.97 524 C THR 261 4. 551-7.558 14. 241 1. 00 16.20 525 THR2614. 463-8.749 13. 951 1. 00 17.39 526 N GLY 262 5. 248-7.112 15. 274 1. 00 15.99 527 CA GLY 262 6. 053-7.955 16. 109 1. 00 16.57 528 C GLY 262 7. 440-8.226 15. 489 1. 00 15.78 529 O GLY 262 8. 139-9.032 16. 083 1. 00 17.55 530 N SER 263 7. 767-7.690 14. 354 1. 00 14. 91 531 CA SER 263 9. 087-7.842 13. 713 1. 00 14.29 532 CB SER 263 9. 168-6.895 12. 511 1. 00 13.31 533 OG SER 263 10. 477-6.875 11. 932 1. 00 13.43 534 C SER 263 10. 187-7.432 14. 679 1. 00 13.48 535 O SER 263 9. 925-6.616 15. 555 1. 00 13.28 536 N PRO 264 11. 403-7.996 14. 572 1. 00 13.05 537 CD PRO 264 11. 752-9.013 13. 547 1. 00 13.34 538 CA PRO 264 12. 513-7.634 15. 400 1. 00 12.59 539 CB PRO 264 13. 606-8.674 15. 042 1. 00 12.77 540 CG PRO 264 13. 262-9.132 13. 663 1. 00 12.97 541 C PRO 264 13. 075-6.250 14. 990 1. 00 12.27 542 PRO26413. 966-5.704 15. 647 1. 00 12.05 543 N ILE 265 12. 601-5.740 13. 866 1. 00 11.95 544 CA ILE 265 12. 993-4.463 13. 326 1. 00 10.32 545 CB ILE 265 13. 429-4. 520 11. 865 1. 00 9. 76 546 CG2 ILE 265 13. 875-3.091 11. 434 1. 00 10.69 547 CG1 ILE 265 14. 615-5.485 11. 655 1. 00 9.09 548 CD1 ILE 265 14. 962-5.708 10. 191 1. 00 9.02 549 C ILE 265 11. 877-3.412 13. 497 1. 00 9.80 550 ILE26510. 735-3.635 13. 147 1. 00 9.74 551 N THR 266 12. 285-2.240 13. 982 1. 00 9.55 552 CA THR 266 11. 406-1.121 14. 246 1. 00 8.02 553 CB THR 266 11. 130-0.921 15. 717 1. 00 6.49 554 OG1 THR 266 10. 606-2.076 16. 388 1. 00 7.49 555 CG2 THR 266 10. 199 0. 292 16. 020 1. 00 4. 42 556 C THR 266 12. 017 0. 164 13. 663 1. 00 8. 61 557 O THR 266 13.166 0.462 13.924 1.00 6. 93 558 N TYR 267 11. 218 0. 874 12. 886 1. 00 8. 60 559 CA TYR 267 11. 549 2. 150 12. 292 1. 00 8. 92 560 CB TYR 267 11.283 2.267 10.816 1.00 8. 03 <BR> <BR> 561 CG TYR 267 12. 198 1. 414 9. 956 1. 00 9. 48 562 CD1 TYR 267 11. 943 0. 088 9. 660 1. 00 8. 79 563 CE1 TYR 267 12. 792-0.630 8. 845 1. 00 10.60 564 CD2 TYR 267 13. 386 1. 993 9. 470 1. 00 9. 05 565 CE2 TYR 267 14. 255 1. 252 8. 701 1. 00 9. 00 566 CZ TYR 267 13. 977-0.061 8. 398 1. 00 10.14 567 OH TYR 267 14. 842-0.788 7. 613 1. 00 11.14 568 C TYR 267 10. 734 3. 231 13. 014 1. 00 11. 08 569 O TYR 267 9.505 2.082 13.150 1.00 11. 62 570 N SER 268 11. 407 4. 259 13. 519 1. 00 9. 16 571 CA SER 268 10. 706 5. 319 14. 207 1. 00 8. 68 572 CB SER 268 10.837 5.162 15.731 1.00 9. 52 573 OG SER 268 10. 219 6. 202 16. 462 1. 00 10. 15 574 C SER 268 11. 359 6. 662 13. 869 1. 00 8. 76 575 O SER 268 12. 505 6. 697 13. 475 1. 00 7. 73 576 NTHR 269 10.561 7.731 14.097 1.00 7. 89 577 CA THR 269 11. 186 9. 057 13. 930 1. 00 6. 34 578 CB THR 269 10. 103 10. 165 13. 657 1. 00 5. 69 579 OG1 THR 269 9. 153 10. 051 14. 734 1. 00 6. 02 580 CG2 THR 269 9. 486 10. 030 12. 315 1. 00 5. 30 581 C THR 269 11. 828 9. 329 15. 260 1. 00 4. 86 582 O THR 269 11. 552 8. 656 16. 274 1. 00 4. 46 583 N TYR 270 12.828 10.238 15.316 1.00 5. 81 584 CA TYR 270 13. 400 10. 618 16. 581 1. 00 5. 84 585 CB TYR 270 14. 526 11. 665 16. 448 1. 00 6. 65 586 CG TYR 270 15. 774 11. 105 15. 773 1. 00 5. 03 587 CD1 TYR 270 16. 026 11. 306 14. 430 1. 00 5. 67 588 CE1 TYR 270 17.185 10.768 13.851 1.00 5. 60 589 CD2 TYR 270 16. 619 10. 312 16. 532 1. 00 4. 28 590 CE2 TYR 270 17. 776 9. 791 15. 972 1. 00 3. 44 591 CZ TYR 270 18. 012 10. 003 14. 630 1. 00 4. 61 592 OH TYR 270 19. 171 9. 501 14.. 089 1. 00 5. 46 593 C TYR 270 12.282 11262 17.468 1.00 5. 35 594 O TYR 270 12. 303 11. 052 18. 642 1. 00 4. 95 595 N GLY 271N11.367 12.006 16.858 1.00 6. 84 596 CA GLY 271 10. 281 12. 651 17. 606 1. 00 6. 43 597 C GLY 271 9.355 11.644 18.372 1.00 5. 35 598 O GLY 271 9. 066 11. 807 19. 516 1. 00 4. 63 599 N LYS 272 8. 979 10. 628 17. 582 1. 00 6. 44 600 CA LYS 272 8. 143 9. 519 18. 118 1. 00 6. 07 601 CB LYS 272 7.625 8.646 16.985 1.00 5. 72 602 CG LYS 272 6. 693 7. 519 17. 391 1. 00 8. 96 603 CD LYS 272 5.493 8.093 18.193 1.00 10. 53 604 CE LYS 272 4. 497 6. 949 18. 381 1. 00 11. 33 605NZ LYS 272 3.441 7.300 19.298 1.00 12. 93 606 C LYS 272 8. 889 8. 743 19. 183 1. 00 5. 81 6070LYS2728. 3348. 42820. 2091. 007. 03 608 N PHE 273 10. 183 8. 473 18. 976 1. 00 5. 59 609 CA PHE 273 11. 017 7. 768 19. 954 1. 00 5. 19 <BR> <BR> 610 CB PHE 273 12. 456 7. 661 19. 270 1. 00 3. 96 611 CG PHE 273 13. 492 7. 236 20. 265 1. 00 5. 55 612 CD1 PHE 273 13. 567 5. 923 20. 699 1. 00 6. 22 613 CD2 PHE 273 14. 418 8. 153 20. 783 1. 00 6. 50 614 CE1 PHE 273 14. 478 5. 511 21. 632 1. 00 6. 20 615 CE2 PHE 273 15.356 7.728 21.725 1.00 6. 91 616 CZ PHE 273 15. 394 6. 403 22. 148 1. 00 5. 82 617 C PHE 273 11. 043 8. 484 21. 271 1. 00 4. 70 618 O PHE 273 10. 917 8. 022 22. 400 1. 00 4. 41 <BR> <BR> 619 N LEU 274 11. 148 9. 834 21. 157 1. 00 5. 85 620 CA LEU 274 11. 195 10. 734 22. 355 1. 00 7. 16 621 CB LEU 274 11. 894 11. 898 21. 746 1. 00 9. 00 622 CG LEU 274 12. 913 12. 878 22. 197 1. 00 8. 88 623 CDl LEU 274 14. 090 12. 224 22. 938 1. 00 6. 56 624 CD2 LEU 274 13. 417 13. 688 20. 999 1. 00 5. 80 625 C LEU 274 9. 799 10. 769 22. 979 1. 00 7. 44 626 O LEU 274 9.629 10.643 24.190 1.00 8. 58 627 N ALA 275 8. 750 10. 859 22. 219 1. 00 7. 77 628 CA ALA 275 7. 352 10. 851 22. 722 1. 00 8. 60 629 CB ALA 275 6. 412 11. 089 21. 566 1. 00 4. 05 630 C ALA 275 7. 096 9. 511 23. 421 1. 00 9. 82 631 0 ALA 275 6. 452 9. 492 24. 488 1. 00 11. 21 632 N ASP 276 7. 587 8. 421 22. 894 1. 00 9. 86 633 CA ASP 276 7. 497 7. 108 23. 490 1. 00 11. 02 634 CB ASP 276 7. 875 5. 998 22. 481 1. 00 12. 50 635 CG ASP 276 6. 867 5. 766 21. 396 1. 00 11. 46 636 OD1 ASP 276 7. 165 5. 238 20. 309 1. 00 11. 51 637 OD2 ASP 276 5. 673 6. 112 21. 719 1. 00 13. 06 638 C ASP 276 8. 313 6. 917 24. 745 1. 00 12. 12 639 0 ASP 276 8. 278 5. 828 25. 391 1. 00 14. 09 640 N GLY 277 9.116 7.845 25.214 1.00 11. 36 <BR> <BR> <BR> 641 CA GLY 277 9. 894 7. 724 26. 412 1. 00 11. 86 642 C GLY 277 11. 358 7. 356 26. 277 1. 00 11. 45 643 O GLY 277 12.004 7.028 27.261 1.00 12. 08 644 N GLY 278 11.904 7.398 25.060 1.00 11. 58 645 CA GLY 278 13. 335 7. 057 24. 894 1. 00 10. 82 646 C GLY 278 13. 499 5. 515 24. 953 1. 00 10. 81 647 O GLY 278 12. 660 4. 802 24. 458 1. 00 11. 18 648 N CYS 279 14.594 5.049 25.489 1.00 10. 84 649 CA CYS 279 14.924 3.641 25.551 1.00 13. 51 650 CB CYS 279 16.426 3.410 25.827 1.00 10. 89 651 SG CYS 279 17. 454 3. 962 24. 477 1. 00 12. 00 652 C CYS 279 14.124 2.888 26.599 1.00 17. 26 653 O CYS 279 14. 151 3. 306 27. 735 1. 00 18. 27 654 N SER 280 13.465 1.826 26.148 1.00 20. 22 655 CA SER 280 12. 658 1. 016 27. 093 1. 00 23. 45 656 CB SER 280 11. 360 0. 603 26. 384 1. 00 26. 30 657 OG SER 280 10. 611 1. 755 25. 930 1. 00 29. 15 658 C SER 280 13. 489-0.228 27. 471 1. 00 23.67 659 O SER 280 14. 067-0.881 26. 588 1. 00 23.40 660 N GLY 281 13. 568-0.514 28. 758 1. 00 24.11 661 CA GLY 281 14. 326-1. 638 29. 262 1. 00 24. 67 662 C GLY 281 14. 321-2.852 28. 366 1. 00 25.23 663 O GLY 281 13. 257-3.355 27. 970 1. 00 25.13 664 N GLY 282 15. 510-3.401 28. 066 1. 00 25.47 665 CA GLY 282 15. 640-4.581 27. 231 1. 00 24.84 666 C GLY 282 14. 892-4.573 25. 927 1. 00 24.58 667 O GLY 282 14. 752-5.634 25. 270 1. 00 25.38 668 N ALA 283 14. 420-3.435 25. 412 1. 00 23.26 669 CA ALA 283 13. 682-3.442 24. 156 1. 00 21.72 670 CB ALA 283 12. 755-2.228 24. 110 1. 00 20.92 671 C ALA 283 14. 532-3.648 22. 936 1. 00 20. 92 672 0 ALA 283 14. 099-4.362 21. 974 1. 00 21.30 673 N TYR 284 15.727 -3.045 22.805 1.00 19. 67 674 CA TYR 284 16. 513-3.283 21. 598 1. 00 17.39 675 CE TYR 284 16.644 -2.088 20.640 1.00 17. 06 676 CG TYR 284 15. 264-1.602 20. 254 1. 00 16.82 677 CD1 TYR 284 14. 690-0.617 21. 056 1. 00 17.15 678 CE1 TYR 284 13. 422-0. 163 20. 757 1. 00 18. 69 679 CD2 TYR 284 14.575 -2.132 19.198 1.00 15. 79 680 CE2 TYR 284 13. 316-1.641 18. 875 1. 00 18.96 681 CZ TYR 284 12. 728-0.686 19. 667 1. 00 18.29 682 OH TYR 284 11. 496-0. 173 19. 411 1. 00 18. 56 683 C TYR 284 17. 961-3.651 21. 954 1. 00 15.77 684 0 TYR 284 18. 419-3.290 23. 011 1. 00 17.35 685 N ASP 285 18. 552-4.349 21. 037 1. 00 13.61 686 CA ASP 285 19. 938-4.773 21. 083 1. 00 11.55 687 CB ASP 285 20.117 -6.114 20.371 1.00 12. 75 688 CG ASP 285 19. 365-7.241 21. 078 1. 00 12.96 689 OD1 ASP 285 18. 514-7.873 20. 487 1. 00 14.76 690 OD2 ASP 285 19. 623-7. 428 22.280 1.00 14. 87 691 C ASP 285 20. 766-3.733 20. 272 1. 00 10.12 692 0 ASP 285 21-827-3. 353 20. 725 1. 00 9. 88 693 N ILE 286 20. 236-3.334 19. 110 1. 00 8.90 694 CA ILE 286 21. 001-2. 393 18. 268 1. 00 7. 91 695 CB ILE 286 21. 303-2.938 16. 854 1. 00 5.84 696 CG2 ILE 286 22. 321-2.047 16. 158 1. 00 5.01 697 CG1 ILE 286 21. 724-4.394 16. 840 1. 00 6.79 698 CD1 ILE 286 22. 852-4.835 17. 698 1. 00 8.37 699 C ILE 286 20. 114-1.160 17. 981 1. 00 7.15 700 O ILE 286 18. 952-1.326 17. 741 1. 00 6.00 701 N ILE 287 20. 753 0. 014 18. 032 1. 00 7. 29 702 CB ILE 287 20.007 1.249 17.738 1.00 6. 30 703 CB ILE 287 19. 763 2. 104 18. 993 1. 00 6. 52 704 CG2 ILE 287 19.019 3.405 18.578 1.00 5. 15 705 CG1 ILE 287 18. 996 1. 304 20. 018 1. 00 6. 95 706 CD1 ILE 287 18. 890 1. 822 21. 410 1. 00 11. 24 707 C ILE 287 20. 802 1. 974 16. 664 1. 00 5. 56 708 O ILE 287 21. 945 2. 347 16. 856 1. 00 6. 13 709 N ILE 288 20.196 2.126 15.514 1.00 5. 45 710 CA ILE 288 20. 759 2. 775 14. 370 1. 00 5. 75 711 CB ILE 288 20. 565 2. 034 13. 050 1. 00 7. 02 712 CG2 ILE 288 21. 213 2. 854 11. 918 1. 00 5. 87 713 CG1 ILE 288 21. 169 0. 631 13. 127 1. 00 6. 25 714 CD1 ILE 288 20. 845-0. 269 11. 941 1. 00 8. 27 715 C ILE 288 20. 126 4. 181 14. 290 1. 00 6. 32 716 O ILE 288 18.923 4.355 14.090 1.00 6. 43 717 N CYS 289 21. 018 5. 144 14. 523 1. 00 5. 86 718 CA CYS 289 20.625 6.566 14.421 1.00 6. 47 719 CB CYS 289 21. 247 7. 362 15. 546 1. 00 4. 34 720 SG CYS 289 20. 910 7. 096 17. 210 1. 00 6. 54 721 C CYS 289 21. 023 7. 072 13. 036 1. 00 6. 90 722 O CYS 289 22.169 7.529 12.775 1.00 6. 61 723 N ASP 290 20. 074 7. 036 12. 113 1. 00 7. 14 724 CA ASP 290 20. 283 7. 438 10. 724 1. 00 9. 53 725 CB ASP 290 19.332 6.665 9.841 1.00 14. 43 726 CG ASP 290 19. 597 6. 672 8. 385 1. 00 16. 40 727 OD1 ASP 290 20. 763 6. 718 7. 922 1. 00 15. 98 728 OD2 ASP 290 18. 523 6. 614 7. 710 1. 00 19. 45 729 C ASP 290 20. 176 8. 949 10. 508 1. 00 8. 37 730 O ASP 290 19. 472 9. 605 11. 294 1. 00 8. 21 731 N GLU 291 20. 918 9. 414 9. 523 1. 00 7. 20 732 CA GLU 291 20. 970 10. 914 9. 332 1. 00 8. 12 <BR> <BR> 733 CB GLU 291 19. 518 11. 285 9. 002 1. 00 11. 61 734 CG GLU 291 19.105 11.263 7.603 1.00 14. 82 <BR> <BR> 735 CD GLU 291 19. 728 10. 469 6. 524 1. 00 15-91 736 OE1 GLU 291 19. 173 9. 781 5. 667 1. 00 16. 90 737 OE2 GLU 291 20. 977 10. 735 6. 310 1. 00 16. 77 738 C GLU 291 21.538 11.527 10.572 1.00 6. 06 739 0 GLU 291 21. 142 12. 611 11. 040 1. 00 6. 10 740 N CYS 292 22.587 10.880 11.184 1.00 5. 04 741 CA CYS 292 23. 107 11. 394 12. 439 1. 00 3. 77 742 CB CYS 292 24. 000 10. 337 13. 149 1. 00 5. 93 743 SG CYS 292 25. 550 10. 129 12. 275 1. 00 6. 46 744 C CYS 292 23. 835 12. 744 12. 340 1. 00 3. 25 745 O CYS 292 24. 259 13. 281 13. 371 1. 00 3. 77 746 N HIS 293 23. 962 13. 298 11. 169 1. 00 4. 46 747 CA HIS 293 24. 593 14. 626 11. 001 1. 00 5. 90 748 CB HIS 293 25. 122 14. 713 9. 540 1. 00 5. 38 749 CG HIS 293 23. 951 14. 653 8. 572 1. 00 8. 01 750 CD2 HIS 293 23. 188 15. 631 7. 989 1. 00 7. 24 751 ND1 HIS 293 23. 406 13. 450 8. 190 1. 00 6. 74 752 CE1 HIS 293 22. 371 13. 704 7. 400 1. 00 7. 12 753 NE2 HIS 293 22. 214 14. 992 7. 289 1. 00 8. 05 754 C HIS 293 23. 507 15. 715 11. 186 1. 00 6. 19 755 0 HIS 293 23. 816 16. 900 11. 180 1. 00 6. 48 756 N SER 294 22. 238 15. 315 11. 325 1. 00 6. 11 757 CA SER 294 21. 148 16. 275 11. 492 1. 00 6. 85 758 CB SER 294 19. 769 15. 506 11. 458 1. 00 4. 78 759 OG SER 294 19. 733 14. 858 10. 225 1. 00 9. 31 760 C SER 294 21. 235 17. 115 12. 737 1. 00 6. 21 761 O SER 294 21. 408 16. 684 13. 877 1. 00 6. 64 762 N THR 295 21. 050 18. 463 12. 535 1. 00 7. 34 763 CA THR 295 21. 161 19. 390 13. 614 1. 00 8. 30 764 CB THR 295 22. 337 20. 391 13. 444 1. 00 8. 12 765 OG1 THR 295 22. 138 21. 130 12. 243'1. 00 10. 33 766 CG2 THR 295 23. 649 19. 627 13. 309 1. 00 8. 89 767 C THR 295 19. 873 20. 038 14. 029 1. 00 8. 71 768 0 THR 295 19. 856 21. 028 14. 739 1. 00 8. 97 769 N ASP 296 18. 721 19. 442 13. 617 1. 00 8. 34 770 CA ASP 296 17. 448 20. 012 14. 120 1. 00 8. 05 771 CB ASP 296 16. 226 19. 518 13. 379 1. 00 9. 39 772 CG ASP 296 16. 082 18. 018 13. 497 1. 00 8. 94 773 OD1 ASP 296 15. 216 17. 553 14. 251 1. 00 9. 43 774 OD2 ASP 296 16. 896 17. 373 12. 792 1. 00 12. 03 775 C ASP 296 17. 411 19. 584 15. 607 1. 00 7. 22 776 0 ASP 296 18. 034 18. 539 15. 946 1. 00 7. 46 777 N ALA 297 16. 710 20. 295 16. 443 1. 00 5. 63 778 CA ALA 297 16. 690 19. 996 17. 851 1. 00 5. 06 <BR> <BR> 779 CB ALA 297 15. 996 21. 145 18. 632 1. 00 3. 83 780 C ALA 297 16.188 18.608 18.184 1.00 4. 03 781 O ALA 297 16. 648 18. 004 19. 135 1. 00 3. 92 782 N THR 298 15. 173 18. 113 17. 515 1. 00 7. 20 783 CA THR 298 14. 598 16. 784 17. 753 1. 00 7. 15 784 CB THR 298 13. 332 16. 548 16. 899 1. 00 7. 88 785 OG1 THR 298 12. 444 17. 646 17. 224 1. 00 10. 29 786 CG2 THR 298 12. 649 15. 256 17. 404 1. 00 7. 86 787 C THR 298 15. 641 15. 689 17. 470 1. 00 5. 90 788 O THR 298 15. 748 14. 768 18. 276 1. 00 5. 86 789 N SER 299 16. 369 15. 782 16. 381 1. 00 5. 05 790 CA SER 299 17. 411 14. 785 16. 098 1. 00 6. 01 791 CB SER 299 18. 006 14. 992 14. 736 1. 00 5. 70 792 OG SER 299 17.107 14.881 13.652 1.00 7. 24 793 C SER 299 18. 485 14. 770 17. 181 1. 00 6. 00 794 O SER 299 18.871 13.717 17.699 1.00 5. 20 795 N IZE 300 19. 021 15. 941 17. 561 1. 00 6. 86 796 CA ILE 300 20.003 16.077 18.618 1.00 4. 91 797 CB ILE 300 20. 458 17. 585 18. 727 1. 00 3. 73 798 CG2 ILE 300 21. 248 17. 773 20. 000 1. 00 2. 00 799 CG1 ILE 300 21. 191 17. 940 17. 441 1. 00 4. 49 800 CD1 ILE 300 21. 415 19. 435 17. 237 1. 00 6. 17 801 C ILE 300 19. 557 15. 547 19. 941 1. 00 3. 81 802 0 ILE 300 20. 237 14. 750 20. 639 1. 00 4. 08 803 N LEU 301 18. 277 15. 925 20. 346 1. 00 2. 55 804 CA LEU 301 17. 761 15. 433 21. 583 1. 00 2. 00 805 CB LEU 301 16. 535 16. 222 22. 008 1. 00 4. 58 806 CG LEU 301 15. 947 15. 936 23. 410 1. 00 4. 87 807 CD1 LEU 301 16.924 16.222 24.524 1.00 5. 46 808 CD2 LEU 301 14. 655 16. 775 23. 539 1. 00 6. 89 809 C LEU 301 17. 525 13. 911 21. 467 1. 00 2. 13 810 O LEU 301 17.796 13.251 22.468 1.00 2. 52 811 N GLY 302 17. 135 13. 450 20. 291 1. 00 3. 98 812 CA GLY 302 16. 886 11. 992 20. 145 1. 00 4. 61 813 C GLY 302 18. 203 11. 205 20. 258 1. 00 4. 26 814 0 GLY 302 18. 245 10. 229 20. 970 1. 00 4. 20 815 N ILE 303 19.181 11.678 19.511 1.00 5. 61 816 CA ILE 303 20. 538 11. 064 19. 544 1. 00 4. 12 817 CB ILE 303 21. 431 11. 635 18. 426 1. 00 5. 93 818 CG2 ILE 303 22. 868 11. 080 18. 653 1. 00 4. 60 819 CG1 ILE 303 20. 880 11. 293 17. 075 1. 00 6. 29 820 CD1 ILE 303 21. 430 11. 896 15. 801 1. 00 7. 46 821 C ILE 303 21. 115 11. 106 20. 911 1. 00 3. 89 8220ILE30321. 60710. 06321. 4101. 002. 64 823 N GLY 304 21. 043 12. 247 21. 640 1. 00 3. 32 824 CA GLY 304 21. 495 12. 393 22. 996 1. 00 4. 10 825 C GLY 304 20. 852 11. 397 23. 941 1. 00 6. 24 826 O GLY 304 21. 486 10. 794 24. 801 1. 00 5. 98 827 N THR 305 19. 530 11. 182 23. 752 1. 00 6. 01 828 CA THR 305 18. 764 10. 245 24. 586 1. 00 5. 33 829 CB THR 305 17. 262 10. 359 24. 247 1. 00 4. 71 830 OG1 THR 305 16. 863 11. 730 24. 487 1. 00 4. 81 831 CG2 THR 305 16. 418 9. 394 25. 052 1. 00 4. 36 832 C THR 305 19. 276 8. 789 24. 349 1. 00 3. 40 833 O THR 305 19.504 8.082 25.305 1.00 4. 86 834 N VAL 306 19. 451 8. 412 23. 145 1. 00 3. 09 835 CA VAL 306 19. 970 7. 115 22. 746 1. 00 4. 90 836 CB VAL 306 20. 105 6. 926 21. 233 1. 00 3. 07 837 CG1 VAL 306 20. 823 5. 599 20. 887 1. 00 2. 00 838 CG2 VAL 306 18.685 6.788 20.594 1.00 4. 78 839 C VAL 306 21. 320 6. 880 23. 477 1. 00 4. 93 840 O VAL 306 21.545 5.905 24.172 1.00 4. 27 841 N LEU 307 22.169 7.855 23.296 1.00 4. 54 842 CA LEU 307 23. 548 7. 789 23. 839 1. 00 5. 17 843 CB LEU 307 2.403 8.882 23.225 1.00 2. 31 844 CG LEU 307 24. 657 8. 894 21. 741 1. 00 3. 96 845 CD1 LEU 307 25. 232 10. 241 21. 318 1. 00 4. 53 846 CD2 LEU 307 25. 743 7. 789 21. 413 1. 00 5. 53 847 C LEU 307 23. 569 7. 739 25. 328 1. 00 4. 93 848 0 LEU 307 24. 339 6. 998 25. 964 1. 00 7. 22 849 N ASP 308 22. 676 8. 470 25. 985 1. 00 6. 12 850 CA ASP 308 22. 623 8. 453 27. 411 1. 00 7. 28 851 CB ASP 308 21. 963 9. 753 27. 938 1. 00 7. 90 852 CG ASP 308 22. 172 9. 872 29. 410 1. 00 8. 50 853 OD1 ASP 308 23. 294 10. 026 29. 965 1. 00 8.73 854 OD2 ASP 308 21. 140 9. 755 30. 089 1. 00 11.97 855 C ASP 308 21.928 7.229 28.007 1. 00 8.42 856 0 ASP 308 22. 299 6. 848 29. 136 1. 00 10.53 857 N GLN 309 20. 994 6. 608 27. 306 1. 00 7.94 858 CA GLN 309 20. 244 5. 513 27. 870 1. 00 8.32 859 CB GLN 309 18. 736 5. 845 27. 683 1. 00 7.05 860 CG GLN 309 18. 283 7. 179 28. 264 1. 00 7.60 861 CD GLN 309 16.806 7.470 8.059 1. 00 8.96 862 OE1 GLN 309 16.145 6.827 27.245 1. 00 8.40 863 NE2 GLN 309 16.283 8.497 28.722 1. 00 9.57 864 C GLN 309 20. 410 4. 121 27. 298 1. 00 9.55 865 O GLN 309 19. 941 3. 193 28. 003 1. 00 10.72 866 N ALA 310 20.967 3.928 26.123 1. 00 8.89 867 CA ALA 310 21.062 2.616 25.509 1. 00 9.02 868 CB ALA 310 21. 580 2. 739 24. 081 1. 00 8.06 869 C ALA 310 21. 743 1. 540 26. 334 1. 00 9.68 870 O ALA 310 21.218 0.401 26.472 1. 00 9.28 871 N GLU 311 22. 927 1. 802 26. 841 1. 00 9.70 872 CA GLU 311 23. 648 0. 836 27. 638 1. 00 10.98 873 CB GLU 311 25.003 1.382 28.075 1. 00 12.55 874 CG GLU 311 25. 791 0. 328 28. 857 1. 00 14.51 875 CD GLU 311 27. 227 0. 724 29. 062 1. 00 16.94 876 OE1 GLU 311 27.635 1.862 28.779 1. 00 15.76 877 OE2 GLU 311 27. 998-0.167 29. 508 1.00 19.80 878 C. GLU 311 22. 822 0. 390 28. 830 1. 00 12.08 879 0 GLU 311 22. 802-0.810 29. 137 1.00 12.07 880 N THR 312 22.205 1.341 29.532 1. 00 11.98 881 CA THR 312 21.376 1. 051 30. 691 1.00 12.48 882 CB THR 312 20. 977 2. 325 31. 430 1. 00 12.71 883 OG1 THR 312 22. 169 2. 885 31. 972 1. 00 15.31 884 CG2 THR 312 20. 008 2. 076 32. 559 1. 00 15.25 885 C THR 312 20. 171 0. 238 30. 303 1. 00 11.45 886 O THR 312 19. 785-0.631 31. 079 1.00 13.15 887 N ALA 313 19.589 0.484 29.167 1. 00 10.64 888 CA ALA 313 18. 459-0.217 28. 625 1.00 11.64 889 CB ALA 313 17.743 0.590 27.524 1. 00 9.84 890 C ALA 313 18. 861-1.575 28. 047 1.00 11.93 891 O ALA 313 18. 068-2.192 27. 329 1.00 14.84 892 N GLY 314 20. 097-2.000 28. 251 1.00 11.94 893 CA GLY 314 20. 597-3.269 27. 794 1.00 10.57 894 C GLY 314 20. 925-3.444 26. 369 1.00 10.22 895 O GLY 314 21. 086-4.597 25. 872 1.00 10.52 896 N ALA 315 21. 143-2.345 25. 633 1.00 8. 85 897 CA ALA 315 21. 520-2. 436 24.236 1. 00 9.14 898 CB ALA 315 21. 317-1.135 23. 485 1.00 8.39 899 C ALA 315 23. 046-2.756 24. 213 1.00 9.51 900 0 ALA 315 23. 724-2.547 25. 210 1.00 11.18 901 N ARG 316 23. 470-3.328 23. 124 1.00 9.21 902 CA ARG 316 24. 871-3.645 22. 913 1.00 11.34 903 CB ARG 316 25. 065-5.134 22. 598 1.00 14.23 904 CG ARG 316 25. 239-5.876 23. 984 1.00 18.17 905 CD ARG 316 25. 239-7.377 23. 735 1.00 20.89 906 NE ARG 316 23. 856-7.778 23. 412 1.00 23.00 907 CZ ARG 316 23. 527-9.001 23. 012 1.00 23.98 908 NH1 ARG 316 24. 519-9.871 22. 801 1.00 24.09 909 NH2 ARG 316 22. 264-9.382 22. 958 1.00 22.75 910 C ARG 316 25. 584-2.754 21. 930 1. 00 9.58 911 0 ARG 316 26. 827-2.634 21. 921 1. 00 9.92 912 N LEU 317 24. 809-2.110 21. 060 1. 00 8.07 913 CA LEU 317 25. 392-1.285 20. 037 1. 00 6.76 914 CB LEU 317 25. 721-2.178 18. 795 1. 00 6.65 915 CG LEU 317 26. 368-1.552 17. 610 1. 00 5.91 916 CD1 LEU 317 27. 796-1.095 17. 989 1. 00 3.78 917 CD2 LEU 317 26. 420-2.397 16. 352 1. 00 9.24 918 C LEU 317 24. 514-0.126 19. 552 1. 00 7.77 919 O LEU 317 23. 363-0.253 19. 211 1. 00 8.25 920 N VAL 318 25.181 1.004 19.425 1.00 6. 96 921 CA VAL 318 24. 623 2. 235 18. 849 1. 00 7. 08 922 CB VAL 318 24. 585 3. 452 19. 775 1. 00 6. 82 923 CG1 VAL 318 24. 156 4. 680 18. 979 1. 00 6. 67 924 CG2 VAL 318 23. 577 3. 217 20. 912 1. 00 6. 74 925 C VAL 318 25.434 2.554 17.601 1.00 6. 63 926 O VAL 318 26.675 2.589 17.667 1.00 6. 95 927 N VAL 319 24. 789 2. 680 16. 474 1. 00 5. 67 928 CA VAL 319 25. 354 2. 988 15. 217 1. 00 6. 45 929 CB VAL 319 25. 098 2. 012 14. 068 1. 00 5. 81 930 CG1 VAL 319 25. 751 2. 382 12. 739 1. 00 4. 73 931 CG2 VAL 319 25. 428 0. 585 14. 424 1. 00 6. 68 932 C VAL 319 24. 890 4. 402 14. 781 1. 00 7. 56 933 0 VAL 319 23. 709 4. 635 14. 473 1. 00 7. 32 934 N LEU 320 25. 918 5. 254 14. 662 1. 00 5. 98 935 CA LEU 320 25. 626 6. 635 14. 164 1. 00 5. 31 936 CB LEU 320 26.522 7.599 14.964 1.00 4. 09 937 CG LEU 320 26. 348 7. 459 16. 483 1. 00 4. 67 938 CD1 LEU 320 27.31 8.315 17.249 1.00 5. 71 939 CD2 LEU 320 24. 942 7. 910 16. 911 1. 00 2. 08 940 C LEU 320 25.846 6.636 12.701 1.00 5. 48 941 O LEU 320 26. 989 6. 671 12. 197 1. 00 6. 96 942 N ALA 321 24. 773 6. 640 11. 879 1. 00 6. 33 943 CA ALA 321 24.883 6.564 10.428 1.00 5. 97 944 CB ALA 321 24.009 5.354 9.988 1.00 4. 65 945 C ALA 321 24.549 7.794 9.638 1.00 7. 15 946 O ALA 321 23.538 8.487 9.829 1.00 6. 63 947 N THR 322 25. 406 8. 076 8. 634 1. 00 8. 02 948 CA THR 322 25. 268 9. 211 7. 770 1. 00 8. 73 949 CB THR 322 25. 695 10. 576 8. 451 1. 00 6. 23 950 OG1 THR 322 25. 399 11. 633 7. 540 1. 00 7. 59 951 CG2 THR 322 27. 143 10. 593 8. 848 1. 00 5. 49 952 C THR 322 26. 138 9. 054 6. 514 1. 00 9. 50 953 O THR 322 27.184 8.381 6.565 1.00 9. 87 954 N ALA 323 25. 732 9. 748 5. 474 1. 00 9. 48 955 CA ALA 323 26. 500 9. 779 4. 233 1. 00 10. 68 956 CB ALA 323 25. 633 9. 834 2. 994 1. 00 9. 86 957 C ALA 323 27. 370 11. 084 4. 257 1. 00 11. 75 958 0 ALA 323 28. 261 11. 219 3. 415 1. 00 11. 77 959 N THR 324 27. 073 11. 944 5. 187 1. 00 10. 60 960 CA THR 324 27. 754 13. 233 5. 253 1. 00 11. 98 961 CB THR 324 26. 804 14. 318 4. 700 1. 00 13. 59 962 OG1 THR 324 25.577 14.173 5.402 1.00 12. 36 963 CG2 THR 324 26. 617 14. 193 3. 218 1. 00 14. 75 964 C THR 324 28. 175 13. 613 6. 648 1. 00 11. 66 965 O THR 324 27. 541 14. 424 7. 288 1. 00 11. 69 966 N PRO 325 29. 262 12. 996 7. 112 1. 00 12. 36 967 CA PRO 325 29.801 13.271 8.427 1. 00 12.49 968 CB PRO 325 30. 696 12. 096 8. 678 1. 00 12.15 969 CG PRO 325 31. 093 11. 554 7. 353 1. 00 10.87 970 CD PRO 325 30. 052 11. 990 6. 374 1. 00 12.13 971 C PRO 325 30. 458 14. 653 8. 513 1. 00 12.24 9720PRO32530. 75815. 3117. 5251. 00 12.41 973 N PRO 326 30. 643 15. 123 9. 718 1. 00 14.00 974 CA PRO 326 31. 268 16. 422 10. 011 1. 00 14.90 975 CB PRO 326 31. 500 16. 400 11. 503 1. 00 13.93 976 CG PRO 326 30. 400 15. 547 12. 025 1. 00 13.72 977 CD PRO 326 30. 367 14. 401 11. 006 1. 00 13.76 978 C PRO 326 32. 569 16. 542 9. 228 1. 00 17.61 979 O PRO 326 33. 338 15. 577 9. 117 1. 00 18.63 980 N GLY 327 32.755 17.703 8.639 1. 00 19.57 981 CA GLY 327 33. 886 18. 010 7. 811 1. 00 22.16 982 C GLY 327 33. 556 17. 755 6. 340 1. 00 23. 94 983 O GLY 327 34. 396 17. 955 5. 465 1. 00 25. 03 984 N SER 328 32. 324 17. 293 6. 053 1. 00 23.98 985 CA SER 328 31. 958 17. 027 4. 678 1. 00 24.01 986 CB SER 328 30. 558 16. 366 4. 552 1. 00 23.43 987 OG SER 328 30. 641 15. 020 5. 009 1. 00 20.07 988 C SER 328 32. 005 18. 259 3. 784 1. 00 23.80 989 O SER 328 31. 762 19. 387 4. 213 1. 00 24.04 990 N VAL 329 32. 364 17. 998 2. 535 1. 00 24.10 991 CA VAL 329 32.417 18.959 1.472 1. 00 23.96 992 CB VAL 329 33. 768 19. 582 1. 114 1. 00 25.69 993 CG1 VAL 329 34. 322 20. 444 2. 247 1. 00 25.30 994 CG2 VAL 329 34. 769 18. 478 0. 753 1. 00 26.03 995 c VAL 329 31. 832 18. 286 0. 212 1. 00 22.98 996 O VAL 329 31. 927 17. 101 0. 041 1. 00 21.99 997 N THR 330 31. 173 19. 079-0.590 1.00 23.51 998 CA THR 330 30. 567 18. 615-1.819 1.00 23.91 999 CB THR 330 29. 597 19. 704-2.335 1.00 21.69 1000 OG1 THR 330 28. 686 19. 943-1.236 1.00 21. 60 1001 CG2 THR 330 28. 837 19. 249-3.544 1.00 22.50 1002 C THR 330 31. 644 18. 331-2.866 1.00 25.09 1003 O THR 330 32. 592 19. 091-3.026 1.00 25.37 1004 N VAL 331 31. 480 17. 202-3.540 1.00 25.34 1005 CA VAL 331 32. 396 16. 763-4.590 1.00 26.56 1006 CB VAL 331 32. 974 15. 365-4.327 1.00 27.18 1007 CG1 VAL 331 33. 773 15. 371-3.028 1.00 28.56 1008 CG2 VAL 331 31. 906 14. 282-4.229 1.00 26.92 1009 C VAL 331 31. 633 16. 744-5.929 1.00 26.87 1010 O VAL 331 30. 397 16. 620-5.970 1.00 25.73 1011 N PRO 332 32. 357 16. 905-7.009 1.00 27.39 1012 CA PRO 332 31.788 16. 914-8.344 1.00 26.93 1013 CB PRO 332 33. 010 17. 026-9.246 1.00 27.20 1014 CG PRO 332 34. 043 17. 693-8.401 1.00 27.04 1015 CD PRO 332 33. 846 17. 123-7.014 1.00 27.59 1016 C PRO 332 31. 052 15. 592-8.594 1.00 26.68 10170 PRO 332 31. 417 14. 560-8.075 1.00 26.75 1018 N HIS 333 29. 998 15. 683-9.376 1.00 26.70 1019 CA HIS 333 29. 166 14. 550-9.782 1.00 26.98 1020 CB HIS 333 27,728 14.795 -9.369 1. 00 28.13 1021 CG HIS 333 26. 830 13. 621-9.614 1.00 29.92 1022 ND1 HIS 333 26. 562 13. 116-10.882 1.00 29.69 1023 CE1 HIS 333 25. 691 12. 137-10.759 1.00 30.33 1024 NE2 HIS 333 25. 374 11. 984-9.485 1. 00 30.06 1025 CD2 HIS 333 26. 081 12. 897-8.735 1. 00 29.95 1026 C HIS 333 29. 276 14. 470-11.320 1. 00 26.52 1027 0 HIS 333 29. 134 15. 463-12.032 1. 00 26.06 1028 N PRO 334 29. 595 13. 301-11.830 1. 00 26.93 1029 CA PRO 334 29. 773 13. 065-13.243 1. 00 26.44 1030 CB PRO 334 30. 273 11. 615-13.312 1. 00 27.24 1031 CG PRO 334 30. 462 11. 142-11.920 1. 00 26.77 1032 CD PRO 334 29. 738 12. 054-11.006 1. 00 26.53 1033 C PRO 334 28. 589 13. 250-14.155 1. 00 25.37 1034 O PRO 334 28. 744 13. 522-15.360 1. 00 24.64 1035 N ASN 335 27. 385 13. 109-13.627 1. 00 25.14 1036 CA ASN 335 26. 176 13. 225-14.476 1. 00 24.12 1037 CB ASN 335 25. 333 11. 991-14.079 1. 00 25.13 1038 CG ASN 335 24. 361 11. 591-15.169 1. 00 26.63 1039 OD1 ASN 335 24. 806 11. 546-16.338 1. 00 26.69 1040 ND2 ASN 335 23. 118 11. 321-14.843 1. 00 26.90 1041 C ASN 335 25. 476 14. 544-14.280 1. 00 23.20 1042 0 ASN 335 24. 384 14. 815-14.780 1. 00 22.66 1043 N ILE 336 26. 131 15. 477-13.549 1. 00 22.56 1044 CA ILE 336 25.569 16. 788-13.289 1. 00 21.47 1045 CB ILE 336 25. 226 17. 011-11.788 1. 00 18.38 1046 CG1 ILE 336 24. 365 15. 914-11.186 1. 00 16.88 1047 CD1 ILE 336 24. 019 16. 054-9.712 1. 00 15.87 1048 CG2 ILE 336 24. 448 18. 344-11.670 1. 00 17.56 1049 C ILE 336 26.529 17. 924-13.692 1. 00 22.12 1050 O ILE 336 27. 618 18. 078-13.110 1. 00 21.60 1051 N GLU 337 26. 081 18. 762-14.631 1. 00 23.57 1052 CA GLU 337 26. 925 19. 892-15.011 1. 00 24.96 1053 CB GLU 337 26. 891'20. 312-16.457 1. 00 26.68 1054 CG GLU 337 25. 581 20. 827-16.954 1. 00 29.17 1055 CD GLU 337 25. 565 21. 452-18.330 1. 00 30.71 1056 OE1 GLU 337 26. 217 22. 512-18.540 1. 00 30.48 1057 OE2 GLU 337 24. 855 20. 872-19.210 1. 00 29.40 1058 C GLU 337 26. 497 21. 073-14.119 1. 00 25.14 1059 O GLU 337 25. 317 21. 406-14.079 1. 00 25.68 1060 N GLU 338 27. 462 21. 678-13.440 1. 00 25.33 1061 CA GLU 338 27. 155 22. 822-12. 566 1. 00 24. 82 1062 CB GLU 338 27. 948 22. 688-11.260 1. 00 24.33 1063 CG GLU 338 27. 610 21. 344-10.613 1. 00 23.98 1064 CD GLU 338 28. 179 21. 163-9.256 1. 00 25.68 1065 OE1 GLU 338 28. 060 22. 102-8. 426 1. 00 27. 78 1066 OE2 GLU 338 28. 705 20. 081-8.922 1. 00 25.92 1067 C GLU 338 27. 378 24. 140-13.272 1. 00 24.46 1068 0 GLU 338 28. 481 24. 437-13.708 1. 00 24.55 1069 N VAL 339 26. 346 24. 954-13.413 1. 00 25.12 1070 CA VAL 339 26. 459 26. 225-14.107 1. 00 26.36 1071 CB VAL 339 25. 529 26. 237-15.356 1. 00 27.72 1072 CG1 VAL 339 25. 807 27. 475-16.192 1. 00 28.55 1073 CG2 VAL 339 25. 617 24. 951-16.132 1. 00 29.01 1074 C VAL 339 26. 071 27. 434-13.271 1. 00 26.16 1075 o VAL 339 24. 927 27. 582-12.834 1. 00 25.73 1076 N ALA 340 26. 994 28. 375-13.103 1. 00 26.86 1077 CA ALA 340 26.679 29.590 -12.355 1.00 27. 03 1078 CB ALA 340 27. 957 30. 438-12.209 1. 00 27.29 1079 C ALA 340 25. 625 30. 405-13.073 1. 00 27.36 1080 O ALA 340 25. 635 30. 534-14.309 1. 00 29.06 1081 N LEU 341 24.628 30. 925-12.389 1. 00 27.40 1082 CA LEU 341 23. 629 31. 781-13. 016 1. 00 28. 60 1083 CB LEU 341 22. 610 32. 187-11.931 1. 00 26.97 1084 CG LEU 341 21. 633 31. 079-11.523 1. 00 25.02 1085 CD1 LEU 341 20.902 31. 449-10.254 1. 00 23.99 1086 CD2 LEU 341 20. 621 30. 914-12.674 1. 00 24.13 1087 C LEU 341 24. 295 33. 074-13.515 1. 00 30.42 1088 O LEU 341 25.491 33.261 -13.369 1.00 30. 76 1089 N SER 342 23. 497 33. 958-14.097 1. 00 31.78 1090 CA SER 342 23. 968 35. 247-14.572 1. 00 32.81 1091 CB SER 342 24. 244 35. 423-16.034 1. 00 32.64 1092 OG SER 342 25. 342 34. 688-16. 535 1. 00 32. 70 1093 C SER 342 23. 014 36. 331-14.065 1. 00 34.24 1094 O SER 342 22. 132 36. 055-13.228 1. 00 33.78 1095 N THR 343 23. 228 37. 543-14.588 1. 00 35.82 1096 CA THR 343 22. 384 38. 652-14.150 1. 00 37.45 1097 C THR 343 21. 373 39. 066-15.193 1. 00 38.30 1098 O THR 343 20. 578 39. 985-14.935 1. 00 39.04 1099 CB THR 343 23. 201 39. 823-13.600 1. 00 38.35 1100 N THR 344 21. 356 38. 409-16.349 1. 00 38.38 1101 CA THR 344 20. 379 38. 729-17.399 1. 00 37.75 1102 C THR 344 19. 246 37. 704-17.363 1. 00 37.56 1103 O THR 344 19. 456 36. 546-17.760 1. 00 38.39 1104 N GLY 345 18. 071 38. 081-16.905 1. 00 37.08 1105 CA GLY 345 16. 918 37. 203-16.829 1. 00 36.52 1106 C GLY 345 15. 674 37. 897-16.299 1. 00 35.87 1107 0 GLY 345 15. 716 38. 955-15.652 1. 00 36.29 1108 N GLU 346 14.519 37. 316-16.533 1. 00 35.17 1109 CA GLU 346 13.228 37. 832-16.121 1. 00 34.33 1110 C GLU 346 12. 844 37. 583-14.681 1. 00 32.89 1111 O GLU 346 11.989 38. 311-14.141 1. 00 32.31 1112 N ILE 347 13. 467 36. 591-14.032 1. 00 31.73 1113 CA ILE 347 13. 096 36. 346-12.618 1. 00 30.36 1114 C ILE 347 14. 218 36. 796-11.704 1. 00 29.15 1115 0 ILE 347 15. 379 36. 418-11.902 1. 00 28.94 1116 CB ILE 347 12. 875 34. 823-12. 434 1. 00 31. 52 1117 CG1 ILE 347 11. 788 34. 415-13.423 1. 00 33.19 1118 CG2 ILE 347 12. 477 34. 515-10.995 1. 00 30.69 1119 CD1 ILE 347 11.527 32. 946-13.604 1. 00 34.58 1120 N PRO 348 13. 855 37. 610-10.706 1. 00 27.98 1121 CA PRO 348 14. 850 38. 082-9.739 1. 00 27.43 1122 CB PRO 348 14. 143 39. 147-8.951 1. 00 26.99 1123 CG PRO 348 12. 684 38. 864-9.119 1. 00 27.21 1124 CD PRO 348 12. 506 38. 068-10.397 1. 00 27.33 1125 C PRO 348 15. 304 36. 885-8.895 1. 00 27.30 1126 0 PRO 348 14. 485 36. 210-8.232 1. 00 26.11 1127 N PHE 349 16. 632 36. 623-8.966 1. 00 27.49 1128 CA PHE 349 17. 148 35. 505-8. 217 1. 00 26. 86 1129 CB PHE 349 17. 317 34. 234-9. 086 1.00 25. 53 1130 CG PHE 349 17. 438 33. 011-8.197 1. 00 23.55 1131 CD1 PHE 349 16. 321 32. 587-7.481 1. 00 23.51 1132 CE1 PHE 349 16. 373 31. 464-6.657 1. 00 23. 18 1133 CZ PHE 349 17. 560 30. 756-6.573 1. 00 21.88 1134 CE2 PHE 349 18. 653 31. 155-7.300 1. 00 21.19 1135 CD2 PHE 349 18. 594 32. 282-8.098 1. 00 22.21 1136 C PHE 349 18. 440 35. 785-7.477 1. 00 27. 01 1137 0 PHE 349 19. 552 35. 657-7.950 1. 00 27.12 1138 N TYR 350 18. 245 36. 137-6.208 1. 00 28.18 1139 CA TYR 350 19. 369 36. 357-5.295 1. 00 28.48 1140 CB TYR 350 19. 755 34. 965-4. 736 1.00 25. 32 1141 CG TYR 350 18. 625 34. 396-3.895 1. 00 22.77 1142 CD1 TYR 350 18. 640 34. 622-2.529 1. 00 22.41 1143 CE1 TYR 350 17. 634 34. 157-1.712 1. 00 22.29 1144 CZ TYR 350 16. 580 33. 438-2.278 1. 00 20.85 1145 OH TYR 350 15. 603 32. 972-1.438 1. 00 22.28 1146 CE2 TYR 350 16. 558 33. 197-3. 618 1.00 20. 37 1147 CD2 TYR 350 17. 567 33. 682-4.434 1. 00 20.49 1148 C TYR 350 20. 535 37. 110-5.860 1. 00 29.90 1149 O TYR 350 21. 707 36. 707-5.853 1. 00 30.45 1150 N GLY 351 20. 211 38. 321-6.358 1. 00 30.59 1151 CA GLY 351 21. 208 39. 205-6.922 1. 00 31.22 1152 C GLY 351 21. 640 38. 712-8.275 1. 00 32.14 1153 O GLY 351 22. 645 39. 190-8.816 1. 00 32.90 1154 N LYS 352 20.916 37. 712-8.786 1. 00 31.83 1155 CA LYS 352 21. 238 37. 187-10.139 1. 00 32.13 1156 CB LYS 352 21. 879 35. 826-10.105 1. 00 33.79 1157 CG LYS 352 23.184 35. 611-9.419 1. 00 34.38 1158 CD LYS 352 24. 338 36. 348-10.054 1. 00 35.61 1159 CE LYS 352 25. 649 36. 005-9.338 1. 00 35.81 1160 NZ LYS 352 26.808 36. 703-9.998 1. 00 37.47 1161 C LYS 352 19. 868 37. 072-10.851 1. 00 31.54 1162 O LYS 352 18.854 37. 525-10.288 1. 00 30.45 1163 N ALA 353 19. 879 36. 419-12.011 1. 00 31.51 1164 CA ALA 353 18. 630 36. 253-12.727 1. 00 31.68 1165 CB ALA 353 18. 440 37. 370-13.768 1. 00 31.42 1166 C ALA 353 18. 439 34. 909-13.426 1. 00 31. 23 1167 O ALA 353 19. 336 34. 243-13.913 1. 00 30.92 1168 N ILE 354 17.125 34. 592-13.477 1. 00 31.06 1169 CA ILE 354 16. 682 33. 363-14.132 1. 00 30.49 1170 CB ILE 354 15.801 32. 492-13.209 1. 00 27.53 1171 CG1 ILE 354 16. 659 32. 066-12.008 1. 00 25.49 1172 CD1 ILE 354 16. 054 31. 228-10.956 1. 00 23.92 1173 CG2 ILE 354 15. 237 31. 291-13.959 1. 00 27.50 1174 C ILE 354 16. 001 33. 665-15.465 1. 00 31.83 1175 O ILE 354 14. 882 34. 185-15.500 1. 00 31.89 1176 N PRO 355 16.726 33. 366-16.549 1. 00 32.61 1177 CA PRO 355 16. 237 33. 503-17.911 1. 00 33.38 1178 CB PRO 355 17. 355 32. 965-18.798 1. 00 33.08 1179 CG PRO 355 18. 518 32. 741-17.932 1. 00 33.12 1180 CD PRO 355 18. 072 32. 738-16.510 1. 00 32.68 1181 C PRO 355 15. 059 32. 501-18.063 1. 00 34.36 1182 O PRO 355 15. 248 31. 301-18.204 1. 00 34.12 1183 N LEU 356 13.876 33. 053-17.998 1. 00 34.63 1184 CA LEU 356 12. 602 32. 377-18. 067 1. 00 34. 79 1185 CB LEU 356 11.599 33. 461-18.493 1. 00 36. 88 1186 CG LEU 356 10. 127 33. 158-18.241 1. 00 38.07 1187 CD1 LEU 356 9. 941 33. 013-16.706 1. 00 39.51 1188 CD2 LEU 356 9. 263 34. 326-18.714 1. 00 38.23 1189 C LEU 356 12.560 31. 182-18.998 1. 00 34.28 1190 O LEU 356 11. 718 30. 273-18.926 1. 00 33.48 1191 N GLU 357 13. 480 31. 165-19.949 1. 00 34.27 1192 CA GLU 357 13.665 30. 121-20.926 1. 00 34.09 1193 CB GLU 357 14. 763 30. 578-21.957 1. 00 35.09 1194 CG GLU 357 16.063 30. 885-21.288 1. 00 36.45 1195 CD GLU 357 17. 219 31. 510-21.972 1. 00 37.61 1196 OE1 GLU 357 18. 314 30. 878-22.109 1. 00 38.18 1197 OE2 GLU 357 17.161 32. 727-22.341 1. 00 38.28 1198 C GLU 357 14. 130 28. 847-20.241 1. 00 33.24 1199 0 GLU 357 13. 765 27. 760-20.690 1. 00 33.38 1200 N VAL 358 14. 894 28. 952-19.148 1. 00 33.16 1201 CA VAL 358 15. 430 27. 750-18.504 1. 00 32.57 1202 CB VAL 358 16. 806 27. 958-17.850 1. 00 33.15 1203 CG1 VAL 358 17. 824 28. 404-18.895 1. 00 33.28 1204 CG2 VAL 358 16. 769 28. 938-16.702 1. 00 33.09 1205 C VAL 358 14. 504 26. 959-17.624 1. 00 31.84 1206 0 VAL 358 14. 835 25. 869-17.125 1. 00 30.79 1207 N ILE 359 13. 283 27. 466-17.429 1. 00 31.93 1208 CA ILE 359 12. 306 26. 786-16.612 1. 00 31.25 1209 CB ILE 359 12. 191 27. 452-15.223 1. 00 29.83 1210 CG1 ILE 359 11. 854 28. 932-15.431 1. 00 29.27 1211 CD1 ILE 359 11. 520 29. 681-14.175 1. 00 29.67 1212 CG2 ILE 359 13. 469 27. 199-14.448 1. 00 29.16 1213 C ILE 359 10. 931 26. 706-17.253 1. 00 31.80 1214 0 ILE 359 10. 165 25. 833-16.765 1. 00 32.60 1215 N GLY 362 9. 436 22. 305-18.884 1. 00 26. 26 1216 CA GLY 362 9. 817 20. 987-18.320 1. 00 23.95 1217 C GLY 362 9. 604 20. 934-16.807 1. 00 22.67 1218 0 GLY 362 8. 771 21. 663-16.259 1. 00 22.25 1219 N ARG 363 10.362 20.060 -16.137 1.00 22. 09 1220 CA ARG 363 10. 262 19. 905-14.686 1. 00 21.72 1221 CB ARG 363 9. 881 18. 491-14.273 1. 00 21.69 1222 CG ARG 363 8.493 18. 061-14.738 1. 00 22.86 1223 CD ARG 363 8.136 16. 653-14.322 1. 00 22.01 1224 NE ARG 363 7.892 16. 372-12.938 1. 00 21.62 1225 CZ ARG 363 6. 817 16. 617-12.212 1. 00 22.79 1226 NH1 ARG 363 5. 734 17. 148-12.777 1. 00 25.41 1227 NH2 ARG 363 6. 794 16. 395-10.900 1. 00 23.11 1228 C ARG 363 11.516 20. 424-13.964 1. 00 20.49 1229 O ARG 363 12.610 19. 883-14.061 1. 00 19.60 1230 N HIS 364 11. 319 21. 515-13.219 1. 00 19.52 1231 CA HIS 364 12. 393 22. 178-12.533 1. 00 19.04 1232 CB HIS 364 12. 653 23. 577-13.214 1. 00 19.49 1233 CG HIS 364 12. 966 23. 303-14.657 1. 00 19.46 1234 ND1 HIS 364 14. 191 22. 848-15.048 1. 00 21.02 1235 CE1 HIS 364 14. 167 22. 648-16.368 1. 00 22.20 1236 NE2 HIS 364 12. 964 22. 939-16. 809 1.00 21. 60 1237 CD2 HIS 364 12. 179 23. 349-15.758 1. 00 20.60 1238 C HIS 364 12. 189 22. 428-11.070 1. 00 17.44 1239 0 HIS 364 11. 082 22. 492-10.574 1. 00 18.37 1240 N LEU 365 13. 316 22. 510-10.352 1. 00 16.59 1241 CA LEU 365 13. 312 22. 751-8.928 1. 00 15.58 1242 CB LEU 365 13. 686 21. 539-8.094 1. 00 13.09 1243 CG LEU 365 13. 853 21. 636-6.606 1. 00 10.94 1244 CD1 LEU 365 12.599 22. 133-5.862 1. 00 10.74 1245 CD2 LEU 365 14. 270 20. 283-6.033 1. 00 12.59 1246 C LEU 365 14. 185 23. 966-8.551 1. 00 15.89 1247 0 LEU 365 15. 366 23. 989-8.777 1. 00 14.95 1248 N ILE 366 13. 520 24. 927-7.897 1. 00 16.40 1249 CA ILE 366 14. 249 26. 112-7.427 1. 00 16.73 1250 CB ILE 366 13. 698 27. 432-7.995 1. 00 16.05 1251 CG1 ILE 366 13. 601 27. 348-9.507 1. 00 16.63 1252 CD1 ILE 366 12. 894 28. 564-10.118 1.00 15.97 1253 CG2 ILE 366 14. 687 28. 557-7.643 1.00 18.10 1254 C ILE 366 14. 199 26. 175-5.898 1.00 16.02 1255 O ILE 366 13. 171 26. 050-5.239 1.00 16.66 1256 N PHE 367 15. 397 26. 318-5.306 1.00 15.73 1257 CA PHE 367 15. 581 26. 443-3.903 1.00 16.16 1258 CB PHE 367 16. 623 25. 545-3.272 1.00 14.42 1259 CG PHE 367 16. 360 24. 069-3.279 1.00 13.91 1260 CD1 PHE 367 16. 953 23. 239-4.203 1.00 13.31 1261 CE1 PHE 367 16. 705 21. 870-4.183 1.00 14.10 1262 CZ PHE 367 15. 879 21. 312-3.198 1.00 13.86 1263 CE2 PHE 367 15. 306 22. 151-2.238 1.00 15.72 1264 CD2 PHE 367 15. 547 23. 519-2.292 1.00 14.82 1265 C PHE 367 15. 851 27. 926-3.526 1.00 18.03 1266 O PHE 367 16.739 28. 577-4.040 1.00 16.55 1267 N CYS 368 15. 004 28. 384-2.623 1.00 20.00 1268 CA CYS 368 14. 965 29. 683-2.023 1.00 21.76 1269 CB CYS 368 13. 599 30. 363-2. 261 1. 00 21.99 1270 SG CYS 368 13. 319 30. 764-3.976 1.00 24.61 1271 C CYS 368 15. 260 29. 638-0.532 1.00 22.91 1272 0 CYS 368 14. 978 28. 600 0. 088 1. 00 23.80 1273 N HIS 369 15. 790 30. 719 0. 059 1. 00 23.93 1274 CA HIS 369 16. 153 30. 677 1. 466 1. 00 26.13 1275 CB HIS 369 17. 179 31. 740 1. 887 1. 00 26.38 1276 CG HIS 369 16.603 33.123 1.932 1. 00 27.61 1277 ND1 HIS 369 16. 177 33. 828 0. 840 1. 00 27.76 1278 CE1 HIS 369 15. 775 35. 028 1. 175 1. 00 28.28 1279 NE2 HIS 369 15. 910 35. 122 2. 503 1. 00 28.13 1280 CD2 HIS 369 16. 437 33. 962 2. 981 1. 00 27.72 1281 C HIS 369 15. 014 30. 642 2. 463 1. 00 27.88 1282 0 HIS 369 15. 232 30. 096 3. 571 1. 00 28.82 1283 N SER 370 13. 826 31. 146 2. 167 1. 00 29.67 1284 CA SER 370 12. 751 31. 076 3. 154 1. 00 31.32 1285 C SER 370 11. 423 30. 614 2. 554 1. 00 32.90 1286 0 SER 370 11. 180 30. 678 1. 349 1. 00 33.73 1287 CB SER 370 12.507 32.459 3.791 1. 00 30.98 1288 OG SER 370 12. 080 33. 381 2. 774 1. 00 31.16 1289 N LYS 371 10. 530 30. 234 3. 489 1. 00 33.55 1290 CA LYS 371 9. 181 29. 771 3. 077 1. 00 33.84 1291 CB LYS 371 8. 426 29. 395 4. 352 1. 00 33.64 1292 CG LYS 371 9. 114 28. 465 5. 307 1. 00 34.04 1293 CD LYS 371 9. 469 27. 087 4. 823 1. 00 33.76 1294 CE LYS 371 10. 090 26. 231 5. 929 1. 00 34.39 1295 NZ LYS 371 10. 400 24. 840 5. 441 1. 00 33.93 1296 C LYS 371 8. 453 30. 906 2. 343 1. 00 33.97 1297 O LYS 371 7.769 30.726 1.355 1. 00 34.43 1298 N LYS 372 8. 637 32. 122 2. 833 1. 00 34.21 1299 CA LYS 372 8. 079 33. 341 2. 331 1. 00 34.06 1300 CB LYS 372 8. 438 34. 527 3. 276 1. 00 36.36 1301 CG LYS 372 7. 900 35. 852 2. 745 1. 00 38.40 1302 CD LYS 372 8. 278 37. 052 3. 600 1. 00 39.46 1303 CE LYS 372 7. 768 38. 318 2. 899 1. 00 40.94 1304 NZ LYS 372 8.133 39.567 3.629 1. 00 42. 30 1305 C LYS 372 8. 508 33. 654 0. 908 1. 00 32.73 1306 LYS3727. 66233. 9230. 0761. 00 32.11 1307 N LYS 373 9. 797 33. 584 0. 632 1. 00 32.72 1308 CA LYS 373 10. 335 33. 844-0.720 1.00 32.34 1309 CB LYS 373 11. 877 33. 768-0.601 1.00 32.38 1310 CG LYS 373 12. 657 33. 931-1.849 1.00 32.09 1311 CD LYS 373 12. 702 35. 236-2.555 1.00 31.79 1312 CE LYS 373 13. 499 36. 284-1.775 1.00 33.22 1313 NZ LYS 373 13. 761 37. 512-2.601 1.00 33.32 1314 C LYS 373 9.868 32. 746-1.695 1.00 32. 08 1315 0 LYS 373 9. 823 32. 877-2.913 1.00 31.08 1316 N CYS 374 9. 570 31. 570-1.108 1.00 32.64 1317 CA CYS 374 9. 093 30. 455-1.935 1.00 32.33 1318 CB CYS 374 8. 997 29. 152-1.185 1.00 32.58 1319 SG CYS 374 10. 489 28. 351-0.585 1.00 30.35 1320 C CYS 374 7. 716 30. 875-2.487 1.00 32.59 1321 O CYS 374 7. 506 30. 905-3.697 1.00 31.98 1322 N ASP 375 6. 831 31. 259-1.549 1.00 32.66 1323 CA ASP 375 5. 489 31. 683-1.941 1.00 32.76 1324 CB ASP 375 4. 590 31. 965-0.730 1.00 35.59 1325 CG ASP 375 4. 307 30. 629-0.037 1.00 38.09 1326 OD1 ASP 375 5. 250 29. 820 0. 064 1. 00 39.50 1327 OD2 ASP 375 3. 169 30. 352 0. 317 1. 00 39.61 1328 C ASP 375 5. 477 32. 865-2.883 1.00 31.41 1329 O ASP 375 4. 717 32. 890-3.841 1.00 30.04 1330 N GLU 376 6. 376 33. 786-2.599 1.00 31.23 1331 CA GLU 376 6. 509 34. 983-3.418 1.00 31.29 1332 CB GLU 376 7. 502 35. 970-2.792 1.00 34.96 1333 CG GLU 376 7. 627 37. 271-3.607 1.00 39.53 1334 CD GLU 376 8. 559 38. 264-2.935 1.00 42.46 1335 OE1 GLU 376 9. 364 38. 922-3.626 1.00 42.89 1336 OE2 GLU 376 8. 473 38. 360-1.677 1.00 44.53 1337 C GLU 376 6. 874 34. 582-4.835 1.00 28.83 1338 O GLU 376 6. 157 34. 888-5.766 1.00 26.95 1339 N LEU 377 7. 922 33. 750-4.943 1.00 29.17 1340 CA LEU 377 8. 419 33. 325-6.254 1.00 27.74 1341 CB LEU 377 9.831 32. 746-6.165 1.00 29.21 1342 CG LEU 377 10.525 32. 384-7.484 1.00 28.78 1343 CD1 LEU 377 10. 627 33. 573-8. 375 1. 00 27.85 1344 CD2 LEU 377 11. 912 31. 776-7.253 1.00 30.35 1345 C LEU 377 7. 453 32. 490-7.044 1.00 26.55 13460LEU3777. 35632. 630-8.280 1.00 25.07 1347 N ALA 378 6. 760 31. 583-6.345 1.00 26.41 1348 CA ALA 378 5. 770 30. 767-7.089 1.00 26.12 1349 CB ALA 378 5. 201 29. 693-6.160 1.00 26.40 1350 C ALA 378 4. 641 31. 708-7.542 1.00 25.76 1351 0 ALA 378 4. 152 31. 612-8.662 1.00 25.17 1352 N ALA 379 4. 246 32. 619-6.619 1.00 25.60 1353 CA ALA 379 3. 164 33. 553-6.975 1.00 24.86 1354 CB ALA 379 2. 803 34. 428-5.809 1.00 24.23 1355 C ALA 379 3. 580 34. 371-8.197 1.00 25.15 1356 O ALA 379 2. 742 34. 677-9. 053 1.00 24.56 1357 N LYS 380 4.901 34. 701-8.299 1.00 25.16 1358 CA LYS 380 5.287 35. 459-9.461 1.00 24.78 1359 CB LYS 380 6.608 36. 159-9.539 1.00 26. 85 1360 CG LYS 380 6. 987 37. 141-8.503 1.00 29.71 1361 CD LYS 380 7. 878 36. 657-7.390 1.00 31.79 1362 CE LYS 380 9.304 36. 617-8.047 1.00 34.18 1363 NZ LYS 380 9.621 38.019 -8.513 1. 00 35.02 1364 C LYS 380 5.159 34. 634-10.753 1.00 23.81 1365 O LYS 380 4.745 35.161 -11.782 1. 00 22.40 1366 N LEU 381 5.581 33.367 -10.617 1. 00 23.77 1367 CA LEU 381 5.593 32.460 -11.757 1. 00 22.87 1368 CB LEU 381 6.349 31.173 -11.378 1. 00 23.11 1369 CG LEU 381 7. 854 31. 382-11.085 1.00 23.16 1370 CD1 LEU 381 8.508 30.137 -10.520 1. 00 23.39 1371 CD2 LEU 381 8.591 31.778 -12.384 1. 00 23.14 1372 C LEU 381 4.252 32.244 -12.403 1. 00 22.47 1373 O LEU 381 4.057 32.336 -13.633 1. 00 22.14 1374 N VAL 382 3.291 31.934 -11.549 1. 00 22.34 1375 CA VAL 382 1.902 31.38 -11.977 1. 00 22.12 1376 CB VAL 382 1.032 31.405 -10.741 1. 00 21.91 1377 CG1 VAL 382 -0.462 31.467 -11.044 1. 00 20.99 1378 CG2 VAL 382 1. 434 29. 962-10.334 1.00 20.39 1379 C VAL 382 1.416 32. 988-12.689 1.00 21.34 1380 O VAL 382 0. 798 32. 848-13.729 1.00 21.59 1381 N ALA 383 1. 719 34. 158-12.124 1.00 21.50 1382 CA ALA 383 1. 333 35. 450-12.700 1.00 21.64 1383 CB ALA 383 1. 831 36. 541-11.743 1.00 18.69 1384 C ALA 383 1. 933 35. 650-14.103 1.00 22.70 1385 0 ALA 383 1. 429 36. 399-14.956 1.00 22.46 1386 N LEU 384 3. 064 34. 992-14.351 1.00 22.34 1387 CA LEU 384 3. 781 35. 019-15.609 1.00 23.61 1388 CB LEU 384 5. 295 34. 853-15.363 1.00 25.91 1389 CG LEU 384 6. 011 35. 952-14.578 1.00 27.33 1390 CD1 LEU 384 7.308 35. 507-13.936 1.00 26.85 1391 CD2 LEU 384 6. 382 37. 087-15.568 1.00 28.95 1392 C LEU 384 3.279 33. 816-16.430 1.00 23. 56 1393 0 LEU 384 3. 800 33. 517-17.488 1.00 24.78 1394 N GLY 385 2. 279 33. 107-15.904 1.00 22.81 1395 CA GLY 385 1. 688 31. 993-16.582 1.00 22.86 1396 C GLY 385 2. 434 30. 688-16.526 1.00 23.11 1397 O GLY 385 2. 246 29. 844-17.423 1.00 22.48 1398 N ILE 386 3. 300 30. 537-15.531 1.00 23.35 1399 CA ILE 386 4. 057 29. 276-15.397 1.00 24.33 1400 CB ILE 386 5. 563 29. 538-15. 270 1. 00 25.84 1401 CG1 ILE 386 6. 102 30. 129-16.583 1.00 28.49 1402 CD1 ILE 386 7. 572 30. 481-16.605 1.00 29.23 1403 CG2 ILE 386 6. 359 28. 316-14.837 1.00 25.75 1404 C ILE 386 3. 469 28. 531-14.209 1.00 25.10 1405 O ILE 386 3.214 29. 145-13.160 1.00 25.67 1406 N ASN 387 3. 190 27. 238-14.400 1.00 25.32 1407 CA ASN 387 2. 642 26. 451-13.298 1.00 25.99 1408 CB ASN 387 2. 246 25. 065-13. 860 1. 00 25.90 1409 CG ASN 387 1. 312 24. 363-12.894 1.00 27.74 1410 OD1 ASN 387 0. 837 24. 914-11.888 1.00 28.56 1411 ND2 ASN 387 0. 943 23. 146-13.249 1.00 29.68 1412 C ASN 387 3. 746 26. 236-12.239 1.00 26.82 1413 0 ASN 387 4. 606 25. 353-12.429 1.00 27.65 1414 N ALA 388 3. 730 27. 027-11.176 1.00 26.87 1415 CA ALA 388 4. 675 26. 910-10.088 1. 00 27.19 1416 CB ALA 388 5.463 28.172 -9.883 1. 00 26.67 1417 C ALA 388 3. 954 26. 489-8.795 1.00 28.18 1418 O ALA 388 2.790 26.870 -8.550 1. 00 27.67 1419 N VAL 389 4.638 25. 683-7.990 1.00 28.38 1420 CA VAL 389 4.117 25.171 -6.736 1. 00 29.24 1421 CB VAL 389 4. 161 23. 613-6.702 1.00 30.91 1422 CG1 VAL 389 3.310 23.079 -5.584 1. 00 31.83 1423 CG2 VAL 389 3. 985 22. 975-8.020 1.00 32.68 1424 C VAL 389 5. 142 25. 518-5.611 1.00 29.07 1425 O VAL 389 6. 342 25. 317-5.846 1.00 28.41 1426 N ALA 390 4. 677 25. 966-4.463 1.00 28.70 1427 CA ALA 390 5.595 26. 239-3.360 1.00 29.81 1428 CB ALA 390 5. 254 27. 489-2. 574 1. 00 30.18 1429 C ALA 390 5.525 25. 028-2.409 1.00 30.88 1430 O ALA 390 4. 402 24. 548-2. 117 1. 00 30.61 1431 N TYR 391 6. 664 24. 548-1.954 1.00 31.50 1432 CA TYR 391 6. 620 23. 409-1.034 1.00 33.61 1433 CB TYR 391 6. 962 22. 089-1.712 1.00 35.20 1434 CG TYR 391 6. 914 20. 947-0.695 1.00 37.04 1435 CD1 TYR 391 5. 724 20. 284-0.445 1.00 38.58 1436 CE1 TYR 391 5. 672 19. 281 0. 506 1. 00 39.62 1437 CZ TYR 391 6.792 18.923 1.209 1. 00 39.48 1438 OH TYR 391 6. 724 17. 920 2. 142 1. 00 40.09 1439 CE2 TYR 391 7. 972 19. 592 0. 984 1. 00 39.19 1440 CD2 TYR 391 8. 029 20. 589 0. 031 1. 00 38. 03 1441 C TYR 391 7. 519 23. 675 0. 163 1. 00 34. 62 1442 0 TYR 391 8. 590 24. 284 0. 043 1. 00 34.22 1443 N TYR 392 7. 112 23. 182 1. 320 1. 00 35.83 1444 CA TYR 392 7. 813 23. 295 2. 562 1. 00 37.58 1445 CB TYR 392 8. 157 24. 749 2. 940 1. 00 39.16 1446 CG TYR 392 6. 981 25. 643 2. 606 1. 00 41.13 1447 CD1 TYR 392 5. 702 25. 396 3. 066 1. 00 42.36 1448 CE1 TYR 392 4.640 26.188 2.654 1. 00 43.63 1449 CZ TYR 392 4. 881 27. 269 1. 812 1. 00 43.37 1450 OH TYR 392 3. 831 28. 076 1. 458 1. 00 43.73 1451 CE2 TYR 392 6. 156 27. 517 1. 347 1. 00 42.54 1452 CD2 TYR 392 7. 204 26. 713 1. 728 1. 00 41.64 1453 C TYR 392 7. 125 22. 624 3. 757 1. 00 38.15 1454 O TYR 392 6. 413 21. 648 3. 573 1. 00 38. 55 1455 N VAL 397 2. 290 18. 131 0. 285 1. 00 42.28 1456 CA VAL 397 3. 211 17. 653-0.781 1.00 41.89 1457 C VAL 397 2.329 17. 268-1.965 1.00 41.82 1458 O VAL 397 2. 734 16. 964-3.073 1.00 41.34 1459 CB VAL 397 4.023 16. 455-0.301 1.00 43.04 1460 CG1 VAL 397 3. 168 15. 203-0.109 1.00 43.49 1461 CG2 VAL 397 5. 243 16. 190-1.147 1.00 42.97 1462 N SER 398 1. 032 17. 308-1. 650 1. 00 41.64 1463 CA SER 398-0. 041 16. 996-2.584 1.00 40.81 1464 C SER 398 0. 106 18. 023-3.732 1.00 39.55 1465 O SER 398-0. 174 17. 793-4.876 1.00 39.03 1466 CB SER 398-1. 355 17. 466-1.859 1.00 42.17 1467 OG SER 398-1. 310 17. 042-0.495 1.00 43.07 1468 N VAL 399 0. 543 19. 201-3.267 1.00 38.82 1469 CA VAL 399 0. 733 20. 359-4.126 1.00 37.69 1470 C VAL 399 1. 644 20. 134-5.290 1.00 37.19 1471 O VAL 399 1. 456 20. 679-6.391 1.00 37.05 1472 CB VAL 399 1. 188 21. 542-3.243 1.00 37.91 1473 CG1 VAL 399 0. 102 21. 739-2.172 1.00 38.49 1474 CG2 VAL 399 2. 505 21. 253-2.554 1.00 37.54 1475 N ILE 400 2.700 19. 333-5.075 1.00 37.24 1476 CA ILE 400 3. 628 19. 034-6.169 1.00 36.07 1477 CB ILE 400 5. 071 18. 908-5. 759 1. 00 36.08 1478 CG1 ILE 400 5. 931 18. 292-6.877 1.00 35.47 1479 CD1 ILE 400 7. 413 18. 404-6.494 1.00 37.42 1480 CG2 ILE 400 5. 318 18. 283-4.406 1. 00 36.43 1481 C ILE 400 3.090 17. 957-7.089 1. 00 35.06 1482 O ILE 400 2. 833 16. 819-6.708 1. 00 35.15 1483 N PRO 401 2. 879 18. 336-8.343 1. 00 34.58 1484 CA PRO 401 2. 384 17. 447-9.374 1. 00 34.50 1485 C PRO 401 3. 459 16. 392-9.660 1. 00 34.76 1486 PRO4014. 65516. 667-9.608 1. 00 33.72 1487 CB PRO 401 2. 121 18. 349-10.556 1. 00 34.40 1488 CG PRO 401 3. 031 19. 509-10.371 1. 00 34.34 1489 CD PRO 401 3. 183 19. 688-8.885 1. 00 34.57 1490 N THR 402 2. 990 15. 171-9.925 1. 00 35.21 1491 CA THR 402 3. 906 14. 052-10.157 1. 00 35.14 1492 CB THR 402 3. 273 12. 761-9.587 1. 00 35.96 1493 OG1 THR 402 2. 075 12. 444-10.309 1. 00 36.78 1494 CG2 THR 402 2. 912 12. 996-8.113 1. 00 34.95 1495 C THR 402 4. 204 13. 895-11.633 1. 00 34.66 1496 0 THR 402 5. 119 13. 188-12.037 1. 00 34.52 1497 N SER 403 3. 425 14. 637-12.427 1. 00 34.15 1498 CA SER 403 3. 547 14. 593-13.867 1. 00 33.47 1499 CB SER 403 2. 435 13. 604-14.331 1. 00 33.98 1500 OG SER 403 2. 458 13. 473-15.726 1. 00 34.94 1501 C SER 403 3. 313 15. 943-14.540 1. 00 33.27 1502 O SER 403 2. 641 16. 841-14. 032 1. 00 33. 01 1503 N GLY 404 3. 873 16. 113-15.734 1. 00 33.08 1504 CA GLY 404 3. 748 17. 292-16. 527 1. 00 32. 68 1505 C GLY 404 4. 738 18. 407-16.282 1. 00 32.45 1506 O GLY 404 5. 796 18. 248-15.697 1. 00 32.28 1507 N ASP 405 4.388 19. 608-16.751 1. 00 31.81 1508 CA ASP 405 5. 240 20. 757-16.578 1. 00 31.23 1509 CB ASP 405 5. 065 21. 796-17.653 1. 00 33.51 1510 CG ASP 405 5.476 21. 268-19.020 1. 00 37.37 1511 OD1 ASP 405 6. 392 20. 403-19.054 1. 00 38.11 1512 OD2 ASP 405 4. 859 21. 753-20.011 1. 00 39.62 1513 C ASP 405 5. 053 21. 390-15.213 1. 00 29.96 1514 O ASP 405 3.935 21. 537-14.710 1. 00 30.36 1515 N VAL 406 6. 224 21. 762-14.635 1. 00 28.06 1516 CA VAL 406 6. 156 22. 419-13.348 1. 00 26.40 1517 CB VAL 3406 5.596 21. 482-12.259 1. 00 26.44 1518 CG1 VAL 406 6.608 20. 370-11.999 1. 00 26.44 1519 CG2 VAL 406 5. 114 22. 216-11.049 1. 00 25.05 1520 C VAL 406 7.522 22. 952-12.910 1. 00 25. 55 1521 0 VAL 406 8. 593 22. 479-13.261 1. 00 24.90 1522 N VAL 407 7.387 24. 028-12.142 1. 00 24.76 1523 CA VAL 407 8.498 24. 705-11.507 1. 00 22.86 1524 CB VAL 407 8.819 26. 112-11.982 1. 00 21.56 1525 CG1 VAL 407 10.003 26. 696-11.201 1. 00 19.62 1526 CG2 VAL 407 9.190 26. 114-13.465 1. 00 20.87 1527 c VAL 407 8. 149 24. 640-10.010 1. 00 22. 26 1528 VAL4077. 15725. 178-9. 483 1.00 22. 95 1529 N VAL 408 8. 957 23. 832-9.319 1. 00 21.00 1530 CA VAL 408 8.748 23. 691-7.868 1. 00 20.28 1531 CB VAL 408 8.898 22. 287-7.352 1. 00 18.06 1532CG1 VAL4088. 52722. 150-5.884 1. 00 16.22 1533 CG2 VAL 408 8.123 21. 294-8.206 1. 00 17.28 1534 C VAL 408 9. 732 24. 710-7. 248 1. 00 21. 18 1535 O VAL 408 10.856 24.843 -7.667 1.00 20. 02 1536 N VAL 409 9. 184 25. 501-6. 356 1. 00 23. 10 1537 CA VAL 409 9.880 26. 538-5.610 1. 00 24.14 1538 CB VAL 409 9.313 27. 952-5.801 1. 00 24.42 1539 CG1 VAL 409 10. 163 28. 945-4.991 1. 00 24.72 1540 CG2 VAL 409 9.318 28. 372-7.258 1. 00 24.33 1541 C VAL 409 9. 775 26. 115-4.148 1. 00 25.02 1542 0 VAL 409 8. 706 26. 210-3.514 1. 00 27.02 1543 N ALA 410 10. 838 25. 559-3.597 1. 00 24.70 1544 CA ALA 410 10.791 25. 073-2.229 1. 00 25.57 1545 CB ALA 410 10. 764 23. 519-2.306 1. 00 23. 83 1546 C ALA 410 11.922 25. 486-1.317 1. 00 26.96 1547 O ALA 410 12. 855 26. 190-1.613 1. 00 26.84 1548 N THR 411 11. 835 24. 952-0.104 1. 00 29.64 1549 CA THR 411 12. 776 25. 081 0. 969 1. 00 31. 00 1550 CB THR 411 12. 117 25. 501 2. 302 1. 00 31. 74 1551 OG1 THR 411 11. 215 24. 483 2. 753 1. 00 33. 12 1552 CG2 THR 411 11. 398 26. 823 2. 113 1. 00 30. 46 1553 C THR 411 13. 326 23. 654 1. 157 1. 00 32. 08 1554 O THR 411 12. 863 22. 736 0. 469 1. 00 32. 40 1555 N ASP 412 14. 213 23. 464 2. 098 1. 00 32. 95 1556 CA ASP 412 14. 790 22. 146 2. 357 1. 00 33. 56 1557 CB ASP 412 15. 973 22. 341 3. 332 1. 00 33. 03 1558 CG ASP 412 16. 948 23. 292 2. 597 1. 00 31. 74 1559 OD1 ASP 412 17. 490 22. 785 1. 591 1. 00 30. 55 1560 OD2 ASP 412 17. 017 24. 443 3. 036 1. 00 30. 30 1561 C ASP 412 13. 815 21. 132 2. 898 1. 00 34. 02 1562 0 ASP 412 14. 173 19. 976 3. 142 1. 00 34. 05 1563 N ALA 413 12.583 21.566 3.051 1.00 34. 97 1564 CA ALA 413 11. 449 20. 784 3. 528 1. 00 35. 57 1565 CB ALA 413 10.319 21.712 3.921 1.00 35. 85 1566 C ALA 413 11. 020 19. 819 2. 423 1. 00 35. 85 1567 O ALA 413 10. 405 18. 781 2. 680 1. 00 36. 55 1568 N LEU 414 11. 423 20. 154 1. 207 1. 00 35. 10 1569 CA LEU 414 11. 152 19. 319 0. 034 1. 00 35. 22 1570 CB LEU 414 11. 682 20. 022-1.202 1. 00 34.30 1571 CG LEU 414 11. 709 19. 499-2.610 1. 00 33.97 1572 CD1 LEU 414 12. 644 18. 316-2.837 1. 00 33.13 1573 CD2 LEU 414 10. 311 19. 171-3.118 1. 00 33.15 1574 C LEU 414 11. 794 17. 955 0. 181 1. 00 35. 59 1575 0 LEU 414 11. 286 16. 918-0.217 1. 00 36.08 1576 N MET 415 12. 974 17. 949 0. 785 1. 00 36. 04 1577 CA MET 415 13. 739 16. 696 0. 911 1. 00 36. 27 1578 CB MET 415 15. 214 17. 157 1. 000 1. 00 36. 78 1579 CG MET 415 15. 395 18. 093-0.239 1. 00 36.20 1580 SD MET 415 16. 918 18. 827-0.501 1. 00 35.49 1581 CE MET 415 17. 327 19. 689 0. 983 1. 00 34. 88 1582 C MET 415 13. 260 15. 810 2. 006 1. 00 36. 38 1583 O MET 415 13. 273 14. 579 1. 845 1. 00 37. 18 1584 N THR 416 12. 782 16. 415 3. 097 1. 00 35. 81 1585 CA THR 416 12.261 15.632 4.223 1.00 35. 01 1586 CB THR 416 12. 315 16. 446 5. 506 1. 00 35. 38 1587 OG1 THR 416 11. 772 15. 684 6. 595 1. 00 37. 40 1588 CG2 THR 416 11. 541 17. 746 5. 418 1. 00 36. 06 1589 C THR 416 10. 866 15. 113 3. 883 1. 00 34. 25 1590 0 THR 416 10. 431 14. 037 4. 316 1. 00 32. 05 1591 N GLY 417 10.145 15.865 3.016 1.00 34. 09 1592 CA GLY 417 8. 836 15. 468 2. 620 1. 00 34. 31 1593 C GLY 417 8. 599 15. 006 1. 212 1. 00 34. 46 1594 0 GLY 417 7. 603 14. 272 1. 010 1. 00 35. 03 1595 N TYR 418 9. 395 15. 349 0. 228 1. 00 33. 75 1596 CA TYR 418 9. 117 14. 929-1.158 1. 00 33.38 1597 CB TYR 418 8. 910 16. 207-1.976 1. 00 32.39 1598 CG TYR 418 8. 639 15. 935-3.435 1. 00 31.06 1599 CD1 TYR 418 9. 662 16. 029-4.365 1. 00 29.98 1600 CE1 TYR 418 9. 425 15. 757-5.696 1. 00 30.29 1601 CZ TYR 418 8. 175 15. 340-6.101 1. 00 30.24 1602 OH TYR 418 7. 929 15. 116-7.440 1. 00 29.25 1603 CE2 TYR 418 7. 151 15. 242-5. 190 1. 00 30. 42 1604 CD2 TYR 418 7. 385 15. 516-3.854 1. 00 30.73 1605 C TYR 418 10. 152 14. 012-1.754 1. 00 34.09 1606 0 TYR 418 11. 361 14. 136-1.445 1. 00 34.13 1607 N THR 419 9. 773 13. 110-2.672 1. 00 33.40 1608 CA THR 419 10. 673 12. 152-3.250 1. 00 33.27 1609 CB THR 419 9. 851 10. 804-3.250 1. 00 35.14 1610 OG1 THR 419 10. 679 9. 748-3.702 1. 00 36.06 1611 CG2 THR 419 8. 686 11. 034-4.233 1. 00 36.32 1612 C THR 419 11. 345 12. 308-4.571 1. 00 32.84 1613 0 THR 419 12. 574 11. 927-4.696 1. 00 33.76 1614 N GLY 420 10. 778 12. 780-5.656 1. 00 31.19 1615 CA GLY 420 11. 313 12. 930-6.945 1. 00 28.55 1616 C GLY 420 12. 457 13. 810-7.354 1. 00 27.27 1617 0 GLY 420 13. 098 14. 617-6.652 1. 00 26.52 1618 N ASP 421 12. 782 13. 672-8. 668 1.00 25. 53 1619 CA ASP 421 13. 860 14. 395-9. 303 1.00 24.28 1620 CB ASP 421 14. 994 13. 468-9.682 1. 00 25.88 1621 CG ASP 421 15. 583 12. 688-8.514 1. 00 26.91 1622 OD1 ASP 421 15. 870 13. 204-7.428 1. 00 25. 89 1623 OD2 ASP 421 15. 756 11. 447-8.708 1. 00 28.33 1624 C ASP 421 13. 406 15. 307-10.434 1. 00 22.06 16250ASP42112. 29115. 230-10.964 1. 00 22.07 1626 N PHE 422 14. 299 16. 197-10.863 1. 00 19.58 1627 CA PHE 422 14. 000 17. 209-11.845 1. 00 18. 52 1628 CB PHE 422 13.896 18. 538-11.001 1. 00 16.35 1629 CG PHE 422 12. 806 18. 451-9.971 1. 00 15.95 1630 CD1 PHE 422 11. 499 18. 851-10.310 1. 00 14.91 1631 CE1 PHE 422 10. 491 18. 791-9.374 1. 00 14.96 1632 CZ PHE 422 10. 711 18. 262-8.122 1. 00 15.19 1633 CE2 PHE 422 12. 001 17. 862-7.774 1. 00 15.76 1634 CD2 PHE 422 13.024 17. 958-8.702 1. 00 15.05 1635 C PHE 422 14. 994 17. 374-12.958 1. 00 18.76 1636 O PHE 422 16. 116 16. 855-12.864 1. 00 18.26 1637 N ASP 423 14. 606 18. 092-14.021 1. 00 19.22 1638 CA ASP 423 15. 514 18. 308-15.159 1. 00 20.75 1639 CB ASP 423 14. 753 18. 885-16. 349 1. 00 23. 11 1640 CG ASP 423 13. 663 17. 916-16.808 1. 00 24.67 1641 OD1 ASP 423 12. 629 18. 362-17. 315 1. 00 24. 65 1642 OD2 ASP 423 13. 871 16. 687-16.621 1. 00 25.69 1643 C ASP 423 16. 696 19. 198-14.785 1. 00 20. 75 1644 0 ASP 423 17. 834 19. 057-15.247 1. 00 21.55 1645 N SER 424 16.429 20. 118-13.862 1. 00 20.40 1646 CA SER 424 17.434 21. 011-13.350 1. 00 19.35 1647 CB SER 424 17. 664 22. 263-14.209 1. 00 19.35 1648 OG SER 424 16. 529 23. 119-14.091 1. 00 20.04 1649 C SER 424 17. 026 21. 439-11. 928 1.00 18. 01 1650 0 SER 424 15. 906 21. 297-11.456 1. 00 17.69 1651 N VAL 425 18.041 21. 904-11.231 1. 00 17.74 1652 CA VAL 425 18. 022 22. 446-9.910 1. 00 16.44 1653 CB VAL 425 18. 660 21. 633-8.788 1. 00 15.18 1654 CG1 VAL 425 18. 800 22. 404-7. 483 1. 00 12. 91 1655 CG2 VAL 425 17. 791 20. 376-8.508 1. 00 13.86 1656 C VAL 425 18. 751 23. 834-10. 000 1. 00 16. 39 1657 O VAL 425 19.857 23. 919-10.505 1. 00 16.92 1658 N ILE 426 18. 017 24. 810-9.475 1. 00 15.43 1659 CA ILE 426 18. 618 26. 164-9.419 1. 00 14.97 1660 CB ILE 426 17. 828 27. 197-10.197 1. 00 15.96 1661 CG1 ILE 426 17. 595 26. 739-11.633 1. 00 17.09 1662 CD1 ILE 426 16. 735 27. 715-12.419 1. 00 18.66 1663 CG2 ILE 426 18.647 28. 533-10.249 1. 00 17.07 1664 C ILE 426 18. 640 26. 426-7.899 1. 00 13.64 1665 0 ILE 426 17. 624 26. 306-7.194 1. 00 13.18 1666 N ASP 427 19. 807 26. 727-7.382 1. 00 12.95 1667 CA ASP 427 19. 958 26. 926-5.946 1. 00 12.20 1668 CB ASP 427 20. 927 25. 791-5.519 1. 00 11.50 1669 CG ASP 427 21. 187 25. 640-4.084 1. 00 11.56 1670 OD1 ASP 427 20. 715 26. 405-3.239 1. 00 10.01 1671 OD2 ASP 427 21. 912 24. 648-3.717 1. 00 12.57 1672 C ASP 427 20.488 28. 303-5.570 1. 00 12.15 1673 0 ASP 427 21. 458 28. 838-6.106 1. 00 11.70 1674 N CYS 428 19. 817 28. 894-4.568 1. 00 12.18 1675 CA CYS 428 20.174 30. 212-4.073 1. 00 11. 98 1676 CB CYS 428 19.037 30. 771-3.212 1. 00 10.15 1677 SG CYS 428 18. 691 30. 068-1.638 1. 00 10.90 1678 C CYS 428 21. 446 30. 092-3. 240 1.00 11.85 1679 0 CYS 428 22. 067 31. 096-2.917 1. 00 12.82 1680 N ASN 429 21. 775 28. 882-2.805 1. 00 11.65 1681 CA ASN 429 22. 960 28. 590-2.022 1. 00 11.49 1682 CB ASN 429 24. 287 28. 962-2.756 1. 00 11.25 1683 CG ASN 429 24. 414 28. 325-4.095 1. 00 10.53 1684 OD1 ASN 429 24. 423 29. 016-5.090 1. 00 13.33 1685 ND2 ASN 429 24. 407 26. 991-4. 246 1.00 10. 35 1686 C ASN 429 22. 992 29. 196-0.634 1. 00 11.98 1687 O ASN 429 24.029 29.346 0.009 1.00 11. 55 1688 N THR 430 21. 843 29. 568-0.121 1. 00 12.43 1689 CA THR 430 21. 600 30. 145 1. 138 1. 00 14. 18 1690 CB THR 430 21. 377 31. 671 1. 125 1. 00 14. 47 1691 OG1 THR 430 20. 273 32. 092 0. 320 1. 00 16. 21 1692 CG2 THR 430 22. 635 32. 373 0. 672 1. 00 13. 93 1693 C THR 430 20. 440 29. 461 1. 876 1. 00 15. 46 1694 0 THR 430 19. 615 28. 741 1. 353 1. 00 14. 51 <BR> <BR> 1695 N CYS 431 20. 451 29. 692 3. 184 1. 00 18. 63 1696 CA CYS 431 19. 431 29. 125 4. 047 1. 00 21. 11 <BR> <BR> 1697 CB CYS 431 19. 844 27. 742 4. 560 1. 00 24. 83 1698 SG CYS 431 21. 195 27. 783 5. 711 1. 00 29. 98 1699 C CYS 431 19.205 30.056 5.251 1.00 21.04 1700 O CYS 431 20.041 30.846 5.678 1.00 21.46 <BR> <BR> 1701 N VAL 432 18. 015 29. 932 5. 783 1. 00 21. 17 1702 CA VAL 432 17.597 30.684 6.958 1.00 20. 82 1703 CB VAL 432 16. 126 31. 132 6. 818 1. 00 21. 73 1704 CG1 VAL 432 15. 649 31. 740 8. 111 1. 00 21. 07 1705 CG2 VAL 432 16. 057 32. 178 5. 686 1. 00 20. 94 1706 C VAL 432 17.736 29.783 8.175 1.00 20. 06 1707 o VAL 432 17. 220 28. 672 8. 197 1. 00 20. 30 1708 N THR 433 18. 435 30. 279 9. 165 1. 00 19.71 1709 CA THR 433 18. 636 29. 513 10. 399 1. 00 20.25 1710 CB THR 433 20. 084 28. 979 10. 386 1. 00 21.18 1711 OG1 THR 433 20. 327 28. 170 11. 531 1. 00 23.49 1712 CG2 THR 433 21. 079 30. 139 10. 364 1. 00 20.53 1713 C THR 433 18. 421 30. 488 11. 562 1. 00 19.17 1714 O THR 433 18. 227 31. 684 11. 299 1. 00 19.85 1715 N GLN 434 18. 429 30. 027 12. 762 1. 00 18.67 1716 CA GLN 434 18. 304 30. 868 13. 940 1. 00 18.14 1717 CB GLN 434 17. 310 30. 363 14. 949 1. 00 22.44 1718 CG GLN 434 15. 826 30. 381 14. 684 1. 00 26.73 1719 CD GLN 434 15. 051 29. 638 15. 774 1. 00 30.67 1720 OE1 GLN 434 14. 046 30. 096 16. 357 1. 00 32.86 1721 NE2 GLN 434 15. 469 28. 393 16. 071 1. 00 30.28 1722 C GLN 434 19. 693 30. 987 14. 602 1. 00 16.57 1723 0 GLN 434 20. 589 30. 114 14. 490 1. 00 15.53 1724 N THR 435 19. 881 32. 082 15. 292 1. 00 15.09 1725 CA THR 435 21. 068 32. 365 16. 041 1. 00 14.55 1726 CB THR 435 22. 102 33. 188 15. 258 1. 00 15.40 1727 OG1 THR 435 23. 328 33. 110 16. 013 1. 00 17.59 1728 CG2 THR 435 21. 710 34. 653 15. 165 1. 00 15.33 1729 C THR 435 20. 664 33. 051 17. 354 1. 00 14.21 1730 O THR 435 19.551 33.621 17.463 1. 00 14.69 1731 N VAL 436 21. 476 32. 917 18. 384 1. 00 13.72 1732 CA VAL 436 21. 259 33. 541 19. 661 1. 00 14.00 1733 CB VAL 436 21. 261 32. 630 20. 883 1. 00 13.16 1734 CG1 VAL 436 22. 530 31. 806 21. 042 1. 00 13.54 1735 CG2 VAL 436 21. 054 33. 472 22. 173 1. 00 14.08 1736 C VAL 436 22. 226 34. 724 19. 827 1. 00 14.34 1737 O VAL 436 23. 415 34. 634 19. 533 1. 00 14.69 1738 N ASP 437 21. 693 35. 868 20. 256 1. 00 13.14 1739 CA ASP 437 22. 543 37. 055 20. 492 1. 00 14.05 1740 CB ASP 437 22. 148 38. 177 19. 564 1. 00 17.69 1741 CG ASP 437 22. 889 39. 470 19. 719 1. 00 21.64 1742 OD1 ASP 437 22. 506 40. 473 19. 017 1. 00 24.58 1743 OD2 ASP 437 23. 892 39. 576 20. 487 1. 00 21.54 1744 C ASP 437 22. 429 37. 374 21. 963 1. 00 12.97 1745 0 ASP 437 21. 304 37. 586 22. 423 1. 00 12.36 1746 N PHE 438 23. 493 37. 309 22. 728 1. 00 12.77 1747 CA PHE 438 23.449 37.622 24.153 1. 00 14.00 1748 CB PHE 438 24. 547 36. 915 24. 933 1. 00 15.14 1749 CG PHE 438 24. 410 35. 410 24. 789 1. 00 17.42 1750 CD1 PHE 438 23. 284 34. 767 25. 294 1. 00 17. 92 1751 CE1 PHE 438 23. 121 33. 396 25. 134 1. 00 17.26 1752 CZ PHE 438 24. 095 32. 665 24. 520 1. 00 19.22 1753 CE2 PHE 438 25. 218 33. 291 24. 008 1. 00 20.03 1754 CD2 PHE 438 25. 377 34. 660 24. 154 1. 00 18.74 1755 C PHE 438 23. 500 39. 153 24. 275 1. 00 14.82 1756 0 PHE 438 24. 490 39. 778 24. 681 1. 00 15.45 1757 N SER 439 22. 403 39. 779 23. 861 1. 00 14.09 1758 CA SER 439 22. 163 41. 159 23. 754 1. 00 13.60 1759 CB SER 439 21. 081 41. 376 22. 659 1. 00 13.74 1760 OG SER 439 19. 880 40. 716 23. 008 1. 00 14.41 1761 C SER 439 21. 961 41. 997 24. 963 1. 00 15.21 1762 O SER 439 22.056 43.261 24.829 1. 00 17.00 1763 N LEU 440 21. 702 41. 475 26. 140 1. 00 14.29 1764 CA LEU 440 21. 528 42. 152 27. 388 1. 00 14.94 1765 CB LEU 440 22. 918 42. 737 27. 819 1. 00 16.73 1766 CG LEU 440 23. 961 41. 616 27. 877 1. 00 17.02 1767 CD1 LEU 440 25. 342 42. 232 28. 018 1. 00 19.63 1768 CD2 LEU 440 23. 623 40. 662 29. 019 1. 00 17.27 1769 C LEU 440 20. 526 43. 276 27. 304 1. 00 15.12 1770 O LEU 440 20. 675 44. 314 27. 969 1. 00 17.12 1771 N ASP 441 19. 459 43. 055 26. 554 1. 00 14.20 1772 CA ASP 441 18. 441 44. 092 26. 404 1. 00 13.49 1773 CB ASP 441 18. 678 44. 670 24. 974 1. 00 13.04 1774 CG ASP 441 18. 552 43. 665 23. 891 1. 00 14.73 1775 OD1 ASP 441 18. 450 42. 441 24. 235 1. 00 14.84 1776 OD2 ASP 441 18. 472 44. 031 22. 690 1. 00 15.43 1777 C ASP 441 16. 996 43. 676 26. 594 1. 00 11.54 1778 O ASP 441 16. 151 43. 950 25. 739 1. 00 11.51 1779 N PRO 442 16. 686 43. 081 27. 733 1. 00 11.09 1780 CA PRO 442 17. 570 42. 814 28. 798 1. 00 11.12 1781 CB PRO 442 16. 606 42. 905 30. 023 1. 00 11.27 1782 CG PRO 442 15. 319 42. 404 29. 504 1. 00 10.59 1783 CD PRO 442 15. 273 42. 649 28. 059 1. 00 11.06 1784 C PRO 442 18. 306 41. 496 28. 942 1. 00 11.43 1785 Q PRO 442 19. 177 41. 375 29. 816 1. 00 11.27 1786 N THR 443 17.903 40.498 24.168 1. 00 11.46 1787 CA THR 443 18. 534 39. 170 28. 299 1. 00 10.94 1788 CB THR 443 17. 477 38. 160 28. 821 1. 00 9.86 1789 OG1 THR 443 16. 359 38. 178 27. 945 1. 00 8.64 1790 CG2 THR 443 16.970 38.473 30.202 1. 00 8.06 1791 C THR 443 19. 179 38. 723 27. 010 1. 00 11.12 1792 O THR 443 20. 315 39. 110 26. 695 1. 00 11.59 1793 N PHE 444 18. 495 37. 888 26. 229 1. 00 10.25 1794 CA PHE 444 18. 995 37. 371 24. 987 1. 00 9.16 1795 CB PHE 444 19. 430 35. 892 25. 147 1. 00 6.85 1796 CG PHE 444 18. 284 34. 965 25. 500 1. 00 7.09 1797 CD1 PHE 444 17. 521 34. 416 24. 466 1. 00 6.78 1798 CE1 PHE 444 16. 463 33. 570 24. 779 1. 00 7.99 1799 CZ PHE 444 16. 160 33. 269 26. 092 1. 00 6.32 1800 CE2 PHE 444 16. 933 33. 797 27. 106 1. 00 6.12 1801 CD2 PHE 444 18. 009 34. 627 26. 813 1. 00 5.30 1802 C PHE 444 17. 987 37. 583 23. 891 1. 00 7.57 1803 O PHE 444 16. 799 37. 899 24. 133 1. 00 7.16 1804 N THR 445 18. 389 37. 400 22. 639 1. 00 8.25 1805 CA THR 445 17. 565 37. 552 21. 476 1. 00 8.94 1806 CB THR 445 18. 009 38. 763 20. 584 1. 00 9.79 1807 OG1 THR 445 18. 084 39. 968 21. 299 1. 00 10.72 1808 CG2 THR 445 17. 088 38. 935 19. 398 1. 00 10.17 1809 C THR 445 17. 711 36. 307 20. 597 1. 00 10.79 1810 O THR 445 18. 836 35. 840 20. 387 1. 00 11.17 1811 N ILE 446 16. 599 35. 726 20. 197 1. 00 12.51 1812 CA ILE 446 16. 610 34. 591 19. 256 1. 00 13.95 1813 CB IZE 446 15. 625 33. 451 19. 554 1. 00 13.14 1814 CG1 ILE 446 15. 905 32. 904 20. 974 1. 00 11.57 1815 CD1 ILE 446 17. 297 32. 357 21. 217 1. 00 8.99 1816 CG2 ILE 446 15.684 32.334 18.483 1. 00 10.38 1817 C ILE 446 16. 283 35. 254 17. 903 1. 00 15.37 1818 O ILE 446 15. 221 35. 848 17. 784 1. 00 16.02 1819 N GLU 447 17. 214 35. 222 16. 962 1. 00 16.86 1820 CA GLU 447 17. 047 35. 840 15. 683 1. 00 19. 17 1821 CB GLU 447 18.283 36.788 15.429 1. 00 22.43 1822 CG GLU 447 18. 494 37. 718 16. 578 1. 00 28.30 1823 CD GLU 447 19. 747 38. 547 16. 547 1. 00 31.65 1824 OE1 GLU 447 20.783 38.064 16.032 1. 00 32.89 1825 OE2 GLU 447 19. 689 39. 695 17. 092 1. 00 34.11 1826 C GLU 447 17. 168 34. 863 14. 485 1. 00 19.06 1827 O GLU 447 17. 890 33. 891 14. 490 1. 00 17.60 1828 N THR 448 16. 473 35. 258 13. 450 1. 00 19.86 1829 CA THR 448 16. 506 34. 510 12. 191 1. 00 22.02 1830 CB THR 448 15. 148 34. 540 11. 499 1. 00 24.73 1831 OG1 THR 448 14.208 33.0757 12.266 1. 00 27.92 1832 CG2 THR 448 15. 223 34. 133 10. 072 1. 00 24.29 1833 C THR 448 17. 549 35. 215 11. 336 1. 00 22.21 1834 0 THR 448 17. 388 36. 439 11. 195 1. 00 22.62 1835 N ILE 449 18. 564 34. 491 10. 907 1. 00 21.67 1836 CA ILE 449 19. 597 35. 093 10. 064 1. 00 21.24 1837 CB ILE 449 20.962 35.198 10.704 1. 00 21.68 1838 CG1 ILE 449 21. 532 33. 817 11. 048 1. 00 22.47 1839 CD1 ILE 449 22.948 33.859 11.569 1. 00 22.61 1840 CG2 ILE 449 20. 879 36. 071 11. 950 1. 00 24.24 1841 C ILE 449 19. 685 34. 252 8. 770 1. 00 20.55 1842 0 ILE 449 19. 203 33. 119 8. 744 1. 00 20.17 1843 N THR 450 20. 218 34. 820 7. 736 1. 00 20.02 1844 CA THR 450 20. 404 34. 146 6. 451 1. 00 20.40 1845 CB THR 450 19. 959 34. 898 5. 219 1. 00 21.10 1846 OG1 THR 450 18. 536 35. 151 5. 219 1. 00 22.48 1847 CG2 THR 450 20. 235 34. 199 3. 894 1. 00 21.05 1848 C THR 450 21. 911 33. 838 6. 406 1. 00 20.84 1849 O THR 450 22. 750 34. 685 6. 758 1. 00 21.43 1850 N LEU 451 22. 212 32. 597 6. 102 1. 00 19.94 1851 CA LEU 451 23. 555 32. 102 5. 996 1. 00 18.72 1852 CB LEU 451 23.952 31.124 7.101 1. 00 17.30 1853 CG LEU 451 24.085 31.529 8.539 1. 00 16.70 1854 CD1 LEU 451 24.472 30.337 9.405 1. 00 16. 72 1855 CD2 LEU 451 25.128 32.647 8.701 1. 00 16. 33 1856 C LEU 451 23. 757 31. 311 4. 680 1. 00 17.02 1857 O LEU 451 22. 847 30. 752 4. 102 1. 00 16. 13 1858 N PRO 452 25. 033 31. 255 4. 298 1. 00 17.03 1859 CA PRO 452 25. 420 30. 458 3. 162 1. 00 16.83 1860 CB PRO 452 26.908 30.662 3.031 1. 00 16.89 1861 CG PRO 452 27. 260 31. 826 3. 884 1. 00 17.21 1862 CD PRO 452 26. 193 31. 897 4. 946 1. 00 17.71 1863 C PRO 452 25. 109 28. 994 3. 564 1. 00 16.91 1864 O PRO 452 25. 228 28. 584 4. 728 1. 00 17.39 1865 N GLN 453 24. 651 28. 251 2. 606 1. 00 16.08 1866 CA GLN 453 24.323 26.814 2.809 1. 00 15.75 1867 CB GLN 453 24. 026 26. 373 1. 414 1. 00 16.34 1868 CG GLN 453 23. 826 25. 154 0. 745 1. 00 16.98 1869 CD GLN 453 23. 637 25. 227-0.767 1.00 13. 90 1870 OE1 GLN 453 24. 484 25. 714-1.509 1.00 14.47 1871 NE2 GLN 453 22. 515 24. 708-1.173 1.00 14.14 1872 C GLN 453 25. 567 26. 036 3. 303 1. 00 14. 94 1873 o GLN 453 26. 691 26. 386 2. 977 1. 00 14.25 1874 N ASP 454 25. 290 24. 919 4. 022 1. 00 13.92 1875 CA ASP 454 26. 450 24. 101 4. 441 1. 00 13.29 1876 CB ASP 454 26. 271 23. 535 5. 820 1. 00 14.12 1877 CG ASP 454 25. 317 22. 418 6. 057 1. 00 14.53 1878 OD1 ASP 454 24. 515 21. 916 5. 257 1. 00 15.10 1879 OD2 ASP 454 25. 403 21. 881 7. 204 1. 00 16.35 1880 C ASP 454 26. 643 23. 007 3. 378 1. 00 11.85 1881 O ASP 454 25. 797 22. 883 2. 484 1. 00 11.90 1882 N ALA 455 27.710 22.214 3.422 1. 00 11.13 1883 CA ALA 455 27.925 21.148 2.463 1. 00 11.01 1884 CB ALA 455 29. 261 20. 457 2. 783 1. 00 10.55 1885 C ALA 455 26. 830 20. 112 2. 356 1. 00 11.80 1886 O ALA 455 26. 602 19. 560 1. 286 1. 00 12.20 1887 N VAL 456 26. 129 19. 792 3. 448 1. 00 13.02 1888 CA VAL 456 25. 039 18. 793 3. 377 1. 00 13.42 1889 CB VAL 456 24. 568 18. 357 4. 761 1. 00 14.94 1890 CG1 VAL 456 23. 465 17. 282 4. 616 1. 00 14.88 1891 CG2 VAL 456 25. 755 17. 858 5. 564 1. 00 14.31 1892 C VAL 456 23. 910 19. 361 2. 551 1. 00 13.16 1893 O VAL 456 23. 370 18. 678 1. 688 1. 00 14.45 1894 N SER 457 23.606 20.653 2.776 1. 00 12.62 1895 CA SER 457 22. 601 21. 304 1. 965 1. 00 12.65 1896 CB SER 457 22. 337 22. 735 2. 495 1. 00 13.54 1897 OG SER 457 21. 401 23. 366 1. 594 1. 00 14.07 1898 C SER 457 22. 945 21. 337 0. 503 1. 00 12.86 1899 O SER 457 22. 135 20. 954-0.363 1.00 13.56 1900 N ARG 458 24. 183 21. 741 0. 151 1. 00 13.36 1901 CA ARG 458 24. 563 21. 832-1. 238 1. 00 13.07 1902 CB ARG 458 25. 983 22. 361-1.396 1.00 14.47 1903 CG ARG 458 26. 222 22. 891-2.830 1.00 15.06 1904 CD ARG 458 27. 686 23. 297-2.983 1.00 16.33 1905 NE ARG 458 27. 874 23. 985-4.288 1.00 17.11 1906 CZ ARG 458 27. 596 25. 264-4.497 1.00 16.66 1907 NH1 ARG 458 27. 181 26. 057-3.523 1.00 16.40 1908 NH2 ARG 458 27. 767 25. 763-5.720 1.00 17.91 1909 C ARG 458 24. 458 20. 455-1.928 1.00 12.29 1910 O ARG 458 23. 982 20. 345-3.051 1.00 11.72 1911 N THR 459 24. 945 19. 443-1.214 1.00 11.83 1912 CA THR 459 24. 878 18. 082-1.780 1.00 11.81 1913 CB THR 459 25. 768 17. 155-0.959 1.00 11.27 1914 OG1 THR 459 27. 119 17. 513-1.313 1.00 13.22 1915 CG2 THR 459 25. 524 15. 698-1.155 1.00 10.39 1916 C THR 459 23. 440 17. 608-1.976 1.00 10.93 1917 O THR 459 23. 115 17. 106-3.051 1.00 11.11 1918 N GLN 460 22. 581 17. 811-0.968 1.00 12.06 1919 CA GLN 460 21. 195 17. 373-1.088 1.00 14.22 1920 CB GLN 460 20. 491 17. 291 0. 247 1. 00 17.33 1921 CG GLN 460 21.019 16.227 1.199 1. 00 22.20 1922 CD GLN 460 20. 360 16. 273 2. 556 1. 00 25.37 1923 OE1 GLN 460 20.910 15.724 3.530 1. 00 27.66 1924 NE2 GLN 460 19.218 16.915 2.748 1. 00 27.50 1925 C GLN 460 20.390 18.147 -3.099 1. 00 13.58 1926 O GLN 460 19. 576 17. 546-2.797 1.00 13.96 1927 N ARG 461 20. 556 19. 490-2.144 1.00 13.56 1928 CA ARG 461 19. 796 20. 238-3.160 1.00 12.12 1929 CB ARG 461 19. 963 21. 736-2.923 1.00 11.11 1930 CG ARG 461 19. 264 22. 248-1.662 1.00 10.11 1931 CD ARG 461 19. 489 23. 742-1.534 1.00 12.77 1932 NE ARG 461 18. 853 24. 331-0.364 1.00 12.91 1933 CZ ARG 461 18. 996 25. 609-0.027 1.00 13.36 1934 NH1 ARG 461 19. 749 26. 431-0.735 1.00 12.45 1935 NH2 ARG 461 18. 398 26. 021 1. 076 1. 00 17.41 1936 C ARG 461 20. 230 19. 856-4.558 1. 00 11.74 1937 O ARG 461 19. 403 19. 635-5.466 1. 00 11.08 1938 N ARG 462 21. 570 19. 776-4.767 1. 00 11.73 1939 CA ARG 462 22. 053 19. 450-6.109 1. 00 12.31 1940 CB ARG 462 23. 618 19. 503-6.096 1. 00 14.50 1941 CG ARG 462 24. 173 19. 271-7.514 1. 00 15.33 1942 CD ARG 462 25. 688 19. 091-7.522 1. 00 15.71 1943 NE ARG 462 26. 059 17. 939-6.654 1. 00 16.34 1944 CZ ARG 462 27. 302 17. 587-6.390 1. 00 17.87 1945 NH1 ARG 462 28. 313 18. 279-6.965 1. 00 19.30 1946 NH2 ARG 462 27. 581 16. 625-5.521 1. 00 16.46 1947 C ARG 462 21. 596 18. 045-6.521 1. 00 12.16 1948 O ARG 462 21. 323 17. 774-7.675 1. 00 13.11 1949 N GLY 463 21. 495 17. 180-5.517 1. 00 12.84 1950 CA GLY 463 21. 160 15. 786-5.748 1. 00 13.65 1951 C GLY 463 19. 800 15. 515-6.308 1. 00 15.71 1952 O GLY 463 19.481 14. 358-6.649 1. 00 16. 83 1953 N ARG 464 18. 943 16. 508-6.406 1. 00 15.62 1954 CA ARG 464 17. 588 16. 369-6.954 1. 00 16.48 1955 CB ARG 464 16. 764 17. 534-6.348 1. 00 17.56 1956 CG ARG 464 16. 634 17. 284-4.813 1. 00 19.66 1957 CD ARG 464 15. 593 16. 171-4.686 1. 00 23.37 1958 NE ARG 464 15. 341 15. 748-3.334 1. 00 26.82 1959 CZ ARG 464 14. 234 15. 127-2.917 1. 00 28.21 1960 NH1 ARG 464 13. 218 14. 886-3.739 1. 00 28.64 1961 NH2 ARG 464 14. 194 14. 809-1. 616 1. 00 29. 64 1962 C ARG 464 17. 567 16. 288-8.434 1. 00 16.33 1963 O ARG 464 16.527 16. 174-9.086 1. 00 17.31 1964 N THR 465 18. 741 16. 381-9.071 1. 00 16.12 1965 CA THR 465 18. 865 16. 282-10.522 1. 00 17.08 1966 CB THR 465 19. 062 17. 634-11.214 1. 00 17.26 1967 OG1 THR 465 18. 900 17. 559-12.654 1. 00 17.74 1968 CG2 THR 465 20. 463 18. 221-10.955 1. 00 15.24 1969 C THR 465 20. 015 15. 296-10. 805 1.00 17. 93 1970 O THR 465 20. 746 14. 888-9.897 1. 00 17.35 1971 N GLY 466 20. 171 14. 874-12.046 1. 00 20.12 1972 CA GLY 466 21. 219 13. 998-12.493 1. 00 22.07 1973 C GLY 466 21. 079 12. 529-12.336 1. 00 24.24 1974 O GLY 466 22. 059 11. 801-12.563 1. 00 25.39 1975 N ARG 467 19. 923 12. 031-11.896 1. 00 25.37 1976 CA ARG 467 19. 709 10. 562-11.745 1. 00 25.66 1977 CB ARG 467 18. 830 10. 292-10.549 1. 00 25.18 1978 C ARG 467 19. 036 10. 164-13. 068 1.00 25. 61 1979 O ARG 467 18. 005 10. 772-13.409 1. 00 26.24 1980 N GLY 468 19. 600 9. 236-13.800 1. 00 25.77 1981 CA GLY 468 18. 917 8. 942-15.111 1. 00 26.28 1982 C GLY 468 19. 520 9. 949-16.100 1. 00 26.61 1983 O GLY 468 20. 752 9. 889-16.316 1. 00 27.87 1984 N LYS 469 18. 735 10. 877-16.634 1. 00 25. 00 1985 CA LYS 469 19. 349 11. 804-17.597 1. 00 24.73 1986 CB LYS 469 18.256 12.495. -18.407 1.00 24.12 1987 C LYS 469 20. 311 12. 772-16.932 1. 00 24.27 1988 O LYS 469 20. 172 13. 136-15.762 1. 00 22.64 1989 N PRO 470 21.322 13.195 -17.694 1.00 24. 75 1990 CA PRO 470 22. 313 14. 166-17. 180 1. 00 24. 51 1991 CB PRO 470 22. 995 14. 632-18.470 1. 00 25.16 1992 CG PRO 470 22. 930 13. 449-19.397 1. 00 25.15 1993 CD PRO 470 21. 574 12. 835-19.097 1. 00 25.23 1994 C PRO 470 21. 566 15. 340-16.543 1. 00 23.98 1995 0 PRO 470 20. 590 15. 813-17.165 1. 00 24.65 1996 N GLY 471 21-973 15. 821-15.387 1. 00 22.80 1997 CA GLY 471 21. 268 16. 922-14.745 1. 00 22.38 1998 C GLY 471 21. 968 18. 264-14.894 1. 00 21. 78 1999 0 GLY 471 23. 131 18. 343-15.329 1. 00 21.87 2000 N ILE 472 21. 244 19. 314-14.516 1. 00 21.07 2001 CA ILE 472 21. 811 20. 664-14.561 1. 00 21.12 2002 CB ILE 472 21. 146 21. 587-15.598 1. 00 23.10 2003 CG1 ILE 472 21. 192 20. 955-16.980 1. 00 24.46 2004 CD1 ILE 472 20. 394 21. 735-18.022 1. 00 26.55 2005 CG2 ILE 472 21. 890 22. 946-15.633 1. 00 22.61 2006 C ILE 472 21.565 21. 308-13.171 1. 00 20.21 2007 0 ILE 472 20. 440 21. 343-12.682 1. 00 19.00 2008 N TYR 473 22. 657 21. 776-12.610 1. 00 19.67 2009 CA TYR 473 22. 674 22. 456-11.340 1. 00 19.18 2010 CB TYR 473 23. 617 21. 818-10.345 1. 00 16.89 2011 CG TYR 473 23. 739 22. 495-8.997 1. 00 16.40 2012 CD1 TYR 473 24. 906 23. 144-8.600 1. 00 15.46 2013 CE1 TYR 473 25. 004 23. 729-7.353 1. 00 14.66 2014 CZ TYR 473 23. 935 23. 687-6.491 1. 00 12.77 2015 OH TYR 473 24. 010 24. 221-5.229 1. 00 12.62 2016 CE2 TYR 473 22. 762 23. 033-6.866 1. 00 14.03 2017 CD2 TYR 473 22. 665 22. 455-8.106 1. 00 13.95 2018 C TYR 473 23. 136 23. 914-11.552 1. 00 19.78 2019 O TYR 473 24. 343 24. 106-11.781 1. 00 20.21 2020 N ARG 474 22. 175 24. 820-11.474 1. 00 19.25 2021 CA ARG 474 22. 550 26. 252-11.631 1. 00 19.53 2022 CB ARG 474 21. 416 26. 981-12. 390 1. 00 21. 50 2023 CG ARG 474 21. 095 26. 252-13.702 1. 00 23.53 2024 CD ARG 474 19. 991 26. 974-14.449 1. 00 26.34 2025 NE ARG 474 19. 592 26. 297-15.662 1. 00 28.73 2026 CZ ARG 474 20. 344 25. 946-16.691 1. 00 30.07 2027 NH1 ARG 474 21. 644 26. 201-16.715 1. 00 31.36 2028 NH2 ARG 474 19. 768 25. 268-17.693 1. 00 30.66 2029 C ARG 474 22. 689 26. 856-10.237 1. 00 18.01 2030 0 ARG 474 21. 836 26. 606-9.364 1. 00 16.48 2031 N PHE 475 23. 734 27. 659-10.003 1. 00 18.43 2032 CA PHE 475 23. 915 28. 240-8.687 1. 00 18.38 2033 CB PHE 475 24. 992 27. 443-7.882 1. 00 19.87 2034 CG PHE 475 26. 316 27. 450-8.601 1. 00 21.60 2035 CD1 PHE 475 27. 233 28. 474-8.413 1. 00 21.98 2036 CE1 PHE 475 28. 420 28. 499-9.119 1. 00 21.39 2037 CZ PHE 475 28. 701 27. 492-10.014 1. 00 22.18 2038 CE2 PHE 475 27. 800 26. 454-10.219 1. 00 21.87 2039 CD2 PHE 475 26. 616 26. 440-9.516 1. 00 22.10 2040 C PHE 475 24. 247 29. 721-8.646 1. 00 17.57 2041 0 PHE 475 24. 785 30. 298-9.589 1. 00 18.41 2042 N VAL 476 23. 939 30. 336-7.526 1. 00 16.75 2043 CA VAL 476 24. 222 31. 744-7.251 1. 00 17.51 2044 CB VAL 476 23. 275 32. 316-6.182 1. 00 16.02 2045 CG1 VAL 476 23. 743 33. 669-5.647 1. 00 18.12 2046 CG2 VAL 476 21. 870 32. 511-6.759 1. 00 16.02 2047 C VAL 476 25. 669 31. 953-6.784 1. 00 18.09 2048 O VAL 476 26. 344 32. 894-7.191 1. 00 18.46 2049 N ALA 477 26.126 31. 115-5.858 1. 00 18.66 2050 CA ALA 477 27. 448 31. 228-5.270 1. 00 19.01 2051 CB ALA 477 27. 257 31. 718-3.823 1. 00 18.89 2052 C ALA 477 28. 191 29. 908-5.306 1. 00 19.61 2053 0 ALA 477 27. 635 28. 864-5.014 1. 00 19.21 2054 N PRO 478 29.468 29.952 -5.667 1.00 20. 93 2055 CA PRO 478 30. 282 28. 772-5.788 1. 00 22.12 2056 CB PRO 478 31. 530 29. 263-6.516 1. 00 21.83 2057 CG PRO 478 31. 619 30. 708-6.161 1. 00 21.39 2058 CD PRO 478 30. 204 31. 197-6.015 1. 00 21.13 2059 C PRO 478 30. 648 28. 144-4.462 1. 00 23.50 2060 0 PRO 478 31. 019 26. 945-4.440 1. 00 24.86 2061 N GLY 479 30. 543 28. 908-3.378 1. 00 23.68 2062 CA GLY 479 30. 933 28. 352-2.111 1. 00 24.62 2063 C GLY 479 29. 891 27. 732-1.225 1. 00 23.81 2064 0 GLY 479 28. 693 27. 949-1.329 1. 00 23.35 2065 N GLU 480 30. 414 26. 959-0.280 1. 00 24.48 2066 CA GLU 480 29. 676 26. 297 0. 775 1. 00 24. 17 2067 CB GLU 480 29. 360 24. 811 0. 535 1. 00 24. 40 2068 CG GLU 480 30. 636 23. 977 0. 452 1. 00 24. 02 2069 CD GLU 480 30. 407 22. 544 0. 045 1. 00 23. 95 2070 OE1 GLU 480 29. 274 22. 215-0.318 1. 00 23.91 2071 OE2 GLU 480 31. 386 21. 753 0. 086 1. 00 25. 10 2072 C GLU 480 30. 540 26. 330 2. 077 1. 00 22. 95 2073 0 GLU 480 31. 766 26. 315 2. 116 1. 00 23. 17 2074 N ARG 481 29. 799 26. 371 3. 134 1. 00 21. 60 2075 CA ARG 481 30. 440 26. 367 4. 493 1. 00 21. 18 2076 CB ARG 481 29. 478 27. 200 5. 233 1. 00 23. 14 2077 CG ARG 481 29. 199 27. 647 6. 561 1. 00 23. 93 2078 CD ARG 481 27. 677 28. 156 6. 437 1. 00 26. 32 2079 NE ARG 481 27.111 27.672 7.684 1.00 26. 95 2080 CZ ARG 481 25. 867 27. 323 7. 904 1. 00 27. 05 2081 NH1 ARG 481 24. 867 27. 371 7. 059 1. 00 25. 48 2082 NH2 ARG 481 25. 707 26. 625 9. 050 1. 00 28. 53 2083 C ARG 481 30. 451 24. 876 4. 843 1. 00 19. 84 2084 0 ARG 481 29. 525 24. 113 4. 484 1. 00 18. 93 2085 N PRO 482 31. 515 24. 402 5. 451 1. 00 19. 41 2086 CA PRO 482 31. 593 23. 006 5. 851 1. 00 19. 37 2087 CB PRO 482 32. 984 22. 876 6. 454 1. 00 18. 84 2088 CG PRO 482 33. 441 24. 224 6. 780 1. 00 18. 94 2089 CD PRO 482 32.672 25.212 5.924 1.00 19. 49 2090 C PRO 482 30. 521 22. 678 6. 917 1. 00 19. 22 2091 0 PRO 482 30. 116 23. 525 7. 734 1. 00 19. 34 2092 N SER 483 30. 105 21. 430 6. 911 1. 00 19. 39 2093 CA SER 483 29. 128 20. 964 7. 934 1. 00 18. 73 2094 CB SER 483 28. 323 19. 799 7. 366 1. 00 15. 95 2095 OG SER 483 29. 124 18. 675 7. 154 1. 00 15. 08 2096 C SER 483 29. 874 20. 510 9. 194 1. 00 18. 37 2097 O SER 483 31. 099 20. 236 9. 173 1. 00 18. 38 2098 N GLY 484 29. 155 20. 419 10. 335 1. 00 17. 59 2099 CA GLY 484 29. 850 19. 934 11. 525 1. 00 17. 63 <BR> <BR> 2100 C GLY 484 29. 719 20. 793 12. 741 1. 00 17. 06 2101 O GLY 484 30. 153 20. 364 13. 809 1. 00 16. 72 2102 N MET 485 29.171 22.008 12.555 1.00 16. 92 2103 CA MET 485 29. 022 22. 905 13. 751 1. 00 16. 87 2104 CB MET 485 30. 203 23. 813 13. 692 1. 00 21. 78 2105 CG MET 485 30. 772 24. 705 14. 711 1. 00 26. 86 2106 SD MET 485 32. 544 25. 254 14. 366 1. 00 31. 84 2107 CE MET 485 32. 250 26. 191 12. 864 1. 00 31. 96 2108 C MET 485 27. 587 23. 409 13. 751 1. 00 14. 92 2109 0 MET 485 26. 958 23. 496 12. 679 1. 00 16. 03 2110 N PHE 486 26. 960 23. 648 14. 864 1. 00 12. 40 2111 CA PHE 486 25. 591 24. 164 14. 950 1. 00 11. 54 2112 CB PHE 486 24. 531 23. 108 15. 152 1. 00 8. 60 2113 CG PHE 486 24. 574 22. 302 16. 386 1. 00 7. 54 2114 CD1 PRE 486 25. 323 21. 115 16. 407 1. 00 7. 69 2115 CD2 PRE 486 23. 856 22. 627 17. 523 1. 00 8. 32 2116 CE1 PHE 486 25. 356 20. 304 17. 519 1. 00 7. 73 2117 CE2 PHE 486 23. 864 21. 812 18. 654 1. 00 8. 35 2118 CZ PHE 486 24.658 20.641 18.659 1.00 7. 65 2119 C PHE 486 25. 570 25. 238 16. 038 1. 00 11. 16 2120 0 PHE 486 26. 415 25. 292 16. 934 1. 00 11. 56 2121 N ASP 487 24. 524 26. 083 16. 029 1. 00 11. 48 2122 CA ASP 487 24. 345 27. 173 16. 926 1. 00 10. 95 2123 CB ASP 487 23. 374 28. 213 16. 220 1. 00 10. 24 2124 CG ASP 487 23. 429 29. 562 16. 846 1. 00 11. 65 2125 OD1 ASP 487 22. 704 29. 999 17. 742 1. 00 12. 90 2126 OD2 ASP 487 24. 227 30. 391 16. 331 1. 00 13. 09 2127 C ASP 487 23. 748 26. 840 18. 280 1. 00 11. 39 2128 O ASP 487 23.002 25.895 18.461 1.00 11. 70 2129 N SER 488 24. 071 27. 669 19. 272 1. 00 11. 06 2130 CA SER 488 23. 606 27. 601 20. 636 1. 00 10. 39 2131 CB SER 488 24.237 28.694 21.467 1.00 9. 66 2132 OG SER 488 23. 928 28. 687 22. 845 1. 00 10. 83 2133 C SER 488 22. 073 27. 685 20. 699 1. 00 10. 72 2134 0 SER 488 21. 454 27. 073 21. 583 1. 00 10. 77 2135 N SER 489 21. 494 28. 438 19. 786 1. 00 10. 72 2136 CA SER 489 20. 020 28. 559 19. 758 1. 00 10. 96 2137 CB SER 489 19. 574 29. 466 18. 614 1. 00 11. 44 2138 OG SER 489 19. 885 28. 935 17. 352 1. 00 11. 33 2139 C SER 489 19. 413 27. 148 19. 570 1. 00 9. 35 2140 O SER 489 18. 265 26. 961 19. 963 1. 00 9. 19 2141 N VAL 490 20. 135 26. 225 18. 938 1. 00 8. 08 2142 CA VAL 490 19.631 24.867 18.805 1.00 8. 79 2143 CB VAL 490 20.482 23.952 17.904 1.00 8. 04 2144 CG1 VAL 490 19. 954 22. 491 17. 885 1. 00 8. 29 2145 CG2 VAL 490 20. 492 24. 530 16. 515 1. 00 8. 17 2146 C VAL 490 19.497 24.262 20.207 1.00 7. 98 2147 O VAL 490 18. 534 23. 528 20. 450 1. 00 8. 37 2148 N LEU 491 20. 453 24. 525 21. 079 1. 00 6. 86 2149 CA LEU 491 20. 365 24. 013 22. 455 1. 00 7. 24 2150 CB LEU 491 21. 640 24. 330 23. 201 1. 00 6. 53 2151 CG LEU 491 22. 943 23. 829 22. 629 1. 00 6. 92 2152 CD1 LEU 491 24. 158 24. 243 23. 497 1. 00 6. 17 2153 CD2 LEU 491 22. 992 22. 296 22. 478 1. 00 6. 46 2154 C LEU 491 19. 109 24. 523 23. 186 1. 00 6. 75 2155 0 LEU 491 18. 414 23. 772 23. 865 1. 00 5. 10 2156 N CYS 492 18. 884 25. 821 23. 041 1. 00 7. 27 2157 CA CYS 492 17. 684 26. 455 23. 594 1. 00 7. 16 2158 CB CYS 492 17. 664 27. 923 23. 218 1. 00 8. 00 2159 SG CYS 492 16. 132 28. 834 23. 709 1. 00 9. 05 2160 C CYS 492 16. 489 25. 671 23. 046 1. 00 6. 01 <BR> <BR> 2161 0 CYS 492 15. 606 25. 317 23. 834 1. 00 7. 01 2162 N GLU 493 16. 443 25. 334 21. 756 1. 00 6. 70 2163 CA GLU 493 15.314 24.594 21.223 1.00 6. 86 2164 CB GLU 493 15. 340 24. 519 19. 720 1. 00 10.54 2165 CG GLU 493 15. 455 25. 907 19. 058 1. 00 13.91 2166 CD GLU 493 15. 467 25. 663 17. 580 1. 00 19. 10 2167 OE1 GLU 493 16. 360 24. 957 17. 070 1. 00 18.86 2168 OE2 GLU 493 14. 439 26. 119 17. 013 1. 00 25.62 2169 C GLU 493 15.170 23.205 21.825 1. 00 5.83 2170 O GLU 493 14. 049 22. 743 21. 937 1. 00 6.74 2171 N CYS 494 16. 251 22. 513 22. 157 1. 00 5.51 2172 CA CYS 494 16. 197 21. 222 22. 803 1. 00 6.61 2173 CB CYS 494 17. 589 20. 551 22. 936 1. 00 6.68 2174 SG CYS 494 18. 368 20. 154 21. 355 1. 00 5.99 2175 C CYS 494 15. 523 21. 326 24. 157 1. 00 5.50 2176 0 CYS 494 14. 719 20. 488 24. 549 1. 00 6.39 2177 N TYR 495 15. 841 22. 350 24. 943 1. 00 5.71 2178 CA TYR 495 15. 238 22. 621 26. 220 1. 00 5.22 2179 CB TYR 495 15. 950 23. 635 27. 103 1. 00 5.21 2180 CG TYR 495 17. 278 23. 105 27. 646 1. 00 5.60 2181 CD1 TYR 495 18. 437 23. 359 26. 938 1. 00 5.68 2182 CE1 TYR 495 19. 673 22. 874 27. 395 1. 00 5.51 2183 CD2 TYR 495 17. 342 22. 403 28. 833 1. 00 4.43 2184 CE2 TYR 495 18. 582 21. 952 29. 294 1. 00 4.71 2185 CZ TYR 495 19. 730 22. 189 28. 589 1. 00 6.10 2186 OH TYR 495 20. 931 21. 723 29. 064 1. 00 6.39 2187 C TYR 495 13. 759 22. 991 26. 076 1. 00 5.70 2188 0 TYR 495 12. 925 22. 541 26. 843 1. 00 5.02 2189 N ASP 496 13. 464 23. 724 25. 005 1. 00 5.88 2190 CA ASP 496 12. 068 24. 116 24. 758 1. 00 5.43 2191 CB ASP 496 12. 091 25. 194 23. 674 1. 00 6.41 2192 CG ASP 496 10. 736 25. 896 23. 517 1. 00 4.55 2193 OD1 ASP 496 10. 680 27. 046 23. 921 1. 00 4.54 2194 OD2 ASP 496 9. 824 25. 287 22. 990 1. 00 6.40 2195 C ASP 496 11. 235 22. 892 24. 433 1. 00 4.95 2196 0 ASP 496 10. 156 22. 702 24. 980 1. 00 3.57 2197 N ALA 497 11. 750 21. 990 23. 616 1. 00 5.97 2198 CA ALA 497 11. 114 20. 736 23. 233 1. 00 6.59 2199 CB ALA 497 11. 842 20. 132 22. 049 1. 00 7.30 2200 C ALA 497 10. 983 19. 776 24. 375 1. 00 7.21 2201 0 ALA 497 9. 959 19. 054 24. 484 1. 00 8.72 2202 N GLY 498 11. 992 19. 673 25. 264 1. 00 5.84 2203 CA GLY 498 11. 932 18. 781 26. 421 1. 00 7.00 2204 C GLY 498 10. 755 19. 181 27. 322 1. 00 7.22 2205 0 GLY 498 9. 963 18. 395 27. 823 1. 00 7.21 2206 N CYS 499 10. 705 20. 498 27. 566 1. 00 6.79 2207 CA CYS 499 9. 651 21. 089 28. 380 1. 00 7.19 2208 CB CYS 499 9. 991 22. 530 28. 766 1. 00 6.96 2209 SG CYS 499 11. 369 22. 746 29. 878 1. 00 8.78 2210 C CYS 499 8. 294 21. 047 27. 658 1. 00 7.99 2211 0 CYS 499 7. 332 20. 677 28. 358 1. 00 9.60 2212 N ALA 500 8. 210 21. 418 26. 387 1. 00 8.26 2213 CA ALA 500 6. 903 21. 467 25. 720 1. 00 9.27 2214 CB ALA 500 6. 970 22. 460 24. 541 1. 00 10.45 2215 C ALA 500 6. 266 20. 172 25. 308 1. 00 10.71 2216 O ALA 500 5. 015 19. 955 25. 428 1. 00 10.51 2217 N TRP 501 7. 034 19. 168 24. 880 1. 00 9.56 2218 CA TRP 501 6. 524 17. 912 24. 419 1. 00 10.25 2219 CB TRP 501 7. 129 17. 730 22. 991 1. 00 9.38 2220 CG TRP 501 6. 605 18. 747 22. 014 1. 00 11.52 2221 CD2 TRP 501 5. 274 18. 719 21. 435 1. 00 12.96 2222 CE2 TRP 501 5. 176 19. 842 20. 602 1. 00 12.98 2223 CE3 TRP 501 4. 165 17. 860 21. 589 1. 00 11.73 2224 CD1 TRP 501 7. 212 19. 850 21. 520 1. 00 10.99 2225 NE1 TRP 501 6. 385 20. 509 20. 661 1. 00 13.57 2226 CZ2 TRP 501 4. 016 20. 123 19. 870 1. 00 13.92 2227 CZ3 TRP 501 3. 023 18. 164 20. 863 1. 00 12.05 2228 CH2 TRP 501 2. 967 19. 279 20. 006 1. 00 12.65 2229 C TRP 501 6. 903 16. 631 25. 139 1. 00 11.04 2230 O TRP 501 6. 164 15. 617 25. 028 1. 00 11.83 2231 N TYR 502 8. 070 16. 620 25. 795 1. 00 10.32 2232 CA TYR 502 8. 566 15. 392 26. 383 1. 00 9.42 2233 CB TYR 502 9. 957 15. 066 25. 721 1. 00 8.75 2234 CG TYR 502 9. 876 15. 121 24. 217 1. 00 8.86 2235 CD1 TYR 502 9. 010 14. 312 23. 484 1. 00 9.28 2236 CE1 TYR 502 8. 943 14. 408 22. 118 1. 00 9.58 2237 CD2 TYR 502 10. 719 15. 991 23. 522 1. 00 7.70 2238 CE2 TYR 502 10. 652 16. 123 22. 159 1. 00 6.86 2239 CZ TYR 502 9. 762 15. 330 21. 451 1. 00 8.12 2240 OH TYR 502 9. 722 15. 405 20. 103 1. 00 7.93 2241 C TYR 502 8.598 15.278 27.844 1. 00 9.28 2242 0 TYR 502 9. 151 14. 304 28. 373 1. 00 10.12 2243 N GLU 503 7. 973 16. 190 28. 597 1. 00 9.36 2244 CA GLU 503 7. 967 16. 131 30. 033 1. 00 11.34 2245 CB GLU 503 7. 039 14. 986 30. 498 1. 00 16.55 2246 CG GLU 503 5.602 15.233 30.020 1. 00 20.15 2247 CD GLU 503 4.697 14.328 30.865 1. 00 25.68 2248 OE1 GLU 503 4. 214 13. 344 30. 346 1. 00 26.72 2249 OE2 GLU 503 4. 555 14. 664 32. 092 1. 00 29.22 2250 C GLU 503 9. 332 15. 985 30. 652 1. 00 10.63 2251 O GLU 503 9.519 15.331 31.697 1. 00 9.93 2252 N LEU 504 10. 341 16. 635 30. 055 1. 00 8.97 2253 CA LEU 504 11. 675 16. 536 30. 653 1. 00 9.41 2254 CB LEU 504 12. 740 16. 474 29. 568 1. 00 10.16 2255 CG LEU 504 12. 608 15. 330 28. 549 1. 00 11.32 2256 CD1 LEU 504 13. 736 15. 509 27. 533 1. 00 10.92 2257 CD2 LEU 504 12. 633 13. 997 29. 264 1. 00 10.07 2258 C LEU 504 11. 984 17. 811 31. 460 1. 00 9.32 2259 0 LEU 504 11. 743 18. 894 30. 992 1. 00 8.44 2260 N THR 505 12. 516 17. 560 32. 613 1. 00 10.59 2261 CA THR 505 12. 934 18. 719 33. 457 1. 00 10.87 2262 CB THR 505 13. 304 18. 235 34. 842 1. 00 11.01 2263 OG1 THR 505 14. 520 17. 460 34. 822 1. 00 12.78 2264 CG2 THR 505 12. 175 17. 493 35. 515 1. 00 10.97 2265 C THR 505 14. 207 19. 196 32. 755 1. 00 9.46 2266 O THR 505 14. 813 18. 413 31. 984 1. 00 8.64 2267 N PRO 506 14. 536 20. 434 32. 915 1. 00 8.60 2268 CD PRO 506 13. 830 21. 474 33. 678 1. 00 8.39 2269 CA PRO 506 15. 784 20. 961 32. 285 1. 00 8.20 2270 CB PRO 506 15. 809 22. 407 32. 829 1. 00 8.51 2271 CG PRO 506 14. 306 22. 712 32. 885 1. 00 7.86 2272 C PRO 506 16. 996 20. 124 32. 673 1. 00 7.85 2273 O PRO 506 17. 804 19. 852 31. 765 1. 00 7.74 2274 N ALA 507 17. 141 19. 616 33. 899 1. 00 8.40 2275 CA ALA 507 18. 306 18. 769 34. 236 1. 00 8.87 2276 CB ALA 507 18. 344 18. 470 35. 732 1. 00 8.60 2277 C ALA 507 18. 298 17. 478 33. 438 1. 00 8.36 2278 O ALA 507 19. 347 16. 946 33. 059 1. 00 8. 30 2279 N GLU 508 17.129 16.908 33.200 1.00 8. 43 2280 CA GLU 508 16. 982 15. 700 32. 394 1. 00 7. 93 <BR> <BR> 2281 CB GLU 508 15. 556 15. 172 32. 412 1. 00 9. 87 2282 CG GLU 508 15. 156 14. 640 33. 784 1. 00 13. 00 2283 CD GLU 508 13. 743 14. 249 34. 002 1. 00 15. 97 2284 OE1 GLU 508 12.815 14.619 33.246 1.00 14. 91 2285 OE2 GLU 508 13.487 13.572 35.067 1.00 19. 65 2286 C GLU 508 17. 434 15. 994 30. 983 1. 00 7. 18 2287 O GLU 508 18. 149 15. 179 30. 374 1. 00 7. 95 2288 N THR 509 17. 089 17. 161 30. 393 1. 00 6. 34 2289 CA THR 509 17. 560 17. 459 29. 048 1. 00 5. 31 2290 CB THR 509 16. 917 18. 766 28. 491 1. 00 5. 86 2291 OG1 THR 509 15.522 18.508 28.431 1.00 6. 04 2292 CG2 THR 509 17. 434 19. 242 27. 149 1. 00 5. 91 2293 C THR 509 19. 092 17. 566 29. 035 1. 00 4. 44 2294 O THR 509 19. 705 17. 124 28. 055 1. 00 3. 49 2295 N THR 510 19. 633 18. 172 30. 023 1. 00 5. 32 2296 CA THR 510 21. 087 18. 373 30. 118 1. 00 7. 03 2297 CB THR 510 21. 470 19. 151 31. 384 1. 00 7. 45 <BR> <BR> 2298 OG1 THR 510 20. 866 20. 461 31. 256 1. 00 10. 36 2299 CG2 THR 510 22. 991 19. 361 31. 473 1. 00 7. 90 2300 C THR 510 21. 817 17. 046 30. 061 1. 00 6. 52 2301 O THR 510 22. 792 16. 954 29. 302 1. 00 5. 63 2302 N VAL 511 21. 383 16. 059 30. 831 1. 00 7. 17 2303 CA VAL 511 22. 063 14. 733 30. 793 1. 00 6. 39 2304 CB VAL 511 21. 334 13. 742 31. 732 1. 00 8. 71 2305 CG1 VAL 511 22. 148 12. 439 31. 814 1. 00 11. 35 2306 CG2 VAL 511 21.291 14.278 33.161 1.00 11. 21 2307 C VAL 511 22. 135 14. 161 29. 406 1. 00 5. 70 2308 O VAL 511 23.094 13.524 28.950 1.00 5. 37 2309 N ARG 512 21. 038 14. 238 28. 607 1. 00 4. 66 2310 CA ARG 512 20. 952 13. 789 27. 258 1. 00 4. 56 2311 CB ARG 512 19. 443 13. 839 26. 817 1. 00 5. 34 2312 CG ARG 512 18. 569 13. 063 27. 845 1. 00 4. 54 2313 CD ARG 512 17. 068 13. 297 27. 406 1. 00 5. 63 2314 NE ARG 512 16. 294 12. 329 28. 186 1. 00 6. 55 2315 CZ ARG 512 15. 159 11. 773 27. 869 1. 00 7. 94 2316 NH1 ARG 512 14. 549 11. 936 26. 696 1. 00 8. 13 2317 NH2 ARG 512 14. 513 11. 103 28. 853 1. 00 9. 75 2318 C ARG 512 21. 836 14. 566 26. 295 1. 00 4. 41 2319 O ARG 512 22. 477 14. 012 25. 395 1. 00 4. 57 2320 N LEU 513 21. 968 15. 880 26. 452 1. 00 3. 51 2321 CA LEU 513 22. 811 16. 743 25. 677 1. 00 3. 00 2322 CB LEU 513 22.358 18.177 25.729 1.00 2. 99 2323 CG LEU 513 20.891 18.444 25.253 1.00 2. 43 2324 CD1 LEU 513 20. 649 19. 977 25. 382 1. 00 4. 58 2325 CD2 LEU 513 20. 689 17. 993 23. 833 1. 00 5. 38 2326 C LEU 513 24. 289 16. 526 26. 054 1. 00 4. 16 2327 0 LEU 513 25. 136 16. 622 25. 162 1. 00 4. 98 , 2328 N ARG 514 24. 557 16. 231 27. 306 1. 00 4. 59 2329 CA ARG 514 25. 937 15. 911 27. 725 1. 00 4. 22 2330 CB ARG 514 26. 061 15. 693 29. 211 1. 00 5. 35 2331 CG ARG 514 25. 977 16. 904 30. 148 1. 00 4. 60 2332 CD ARG 514 27. 184 17. 819 29. 907 1. 00 4. 15 2333 NE ARG 514 27. 127 18. 935 30. 876 1. 00 7. 82 2334 CZ ARG 514 27. 925 20. 020 30. 765 1. 00 8. 84 2335 NH1 ARG 514 28. 761 20. 185 29. 760 1. 00 9. 46 2336 NH2 ARG 514 27. 881 20. 919 31. 773 1. 00 10. 54 2337 C ARG 514 26. 438 14. 679 26. 959 1. 00 5. 00 2338 0 ARG 514 27. 573 14. 645 26. 396 1. 00 4. 68 2339 N ALA 515 25. 564 13. 677 26. 909 1. 00 5. 80 2340 CA ALA 515 25. 855 12. 422 26. 184 1. 00 5. 87 2341 CB ALA 515 24. 646 11. 491 26. 284 1. 00 6. 08 2342 C ALA 515 26. 173 12. 678 24. 732 1. 00 5. 61 2343 O ALA 515 27. 140 12. 135 24. 198 1. 00 6. 74 2344 N TYR 516 25. 406 13. 464 23. 990 1. 00 4. 81 2345 CA TYR 516 25. 584 13. 857 22. 648 1. 00 4. 49 2346 CB TYR 516 24. 420 14. 812 22. 174 1. 00 4. 92 <BR> <BR> 2347 CG TYR 516 24. 513 15. 244 20. 739 1. 00 5. 73<BR> <BR> <BR> <BR> <BR> 2348 CD1 TYR 516 23. 745 14. 634 19. 758 1. 00 6. 26 2349 CE1 TYR 516 23. 820 14. 993 18. 429 1. 00 4. 69 2350 CD2 TYR 516 25. 348 16. 324 20. 342 1. 00 5. 39 2351 CE2 TYR 516 25. 458 16. 688 19. 026 1. 00 5. 85 2352 CZ TYR 516 24. 669 16. 050 18. 065 1. 00 4. 88 2353 OH TYR 516 24. 785 16. 437 16. 788 1. 00 4. 60 2354 C TYR 516 26. 928 14. 659 22. 476 1. 00 3. 84 2355 0 TYR 516 27. 686 14. 293 21. 600 1. 00 3. 88 2356 N MET 517 27. 150 15. 595 23. 383 1. 00 3. 68 2357 CA MET 517 28. 350 16. 416 23. 261 1. 00 5. 14 2358 CB MET 517 28. 223 17. 746 23. 992 1. 00 6. 77 2359 CG MET 517 27. 061 18. 640 23. 614 1. 00 8. 84 2360 SD MET 517 27. 095 20. 280 24. 391 1. 00 12. 08 2361 CE MET 517 28. 562 20. 984 23. 666 1. 00 9. 69 2362 C MET 517 29. 612 15. 659 23. 627 1. 00 5. 82 2363 O MET 517 30. 696 16. 142 23. 276 1. 00 7. 19 2364 N ASN 518 29.519 14.527 24.306 1.00 6. 21 2365 CA ASN 518 30. 694 13. 723 24. 680 1. 00 6. 26 2366 CB ASN 518 30.527 13.174 26.102 1.00 6. 44 2367 CG ASN 518 31.801 12.562 26.694 1.00 7. 38 2368 OD1 ASN 518 32. 895 13. 092 26. 434 1. 00 5. 49 2369 ND2 ASN 518 31. 655 11. 510 27. 468 1. 00 8. 26 2370 C ASN 518 30. 889 12. 577 23. 673 1. 00 6. 41 2371 O ASN 518 31. 690 11. 631 23. 885 1. 00 7. 03 2372 N THR 519 30. 266 12. 623 22. 519 1. 00 6. 15 2373 CA THR 519 30. 380 11. 601 21. 480 1. 00 6. 38 2374 CB THR 519 28. 950 11. 010 21. 142 1. 00 3. 99 2375 OG1 THR 519 28. 425 10. 488 22. 358 1. 00 6. 17 2376 CG2 THR 519 29. 099 9. 842 20. 173 1. 00 4. 00 2377 C THR 519 31. 099 12. 057 20. 257 1. 00 6. 70 2378 O THR 519 30. 629 12. 915 19. 464 1. 00 7. 85 2379 N PRO 520 32. 383 11. 631 20. 078 1. 00 7. 29 2380 CD PRO 520 33. 082 10. 685 20. 975 1. 00 7. 71 2381 CA PRO 520 33. 201 12. 004 18. 943 1. 00 8. 17 2382 CB PRO 520 34. 522 11. 248 19. 163 1. 00 8. 49 2383 CG PRO 520 34. 546 11. 030 20. 681 1. 00 9. 66 2384 C PRO 520 32. 567 11. 604 17. 623 1. 00 7. 53 2385 o PRO 520 31. 788 10. 619 17. 549 1. 00 10. 57 2386 N GLY 521 32. 734 12. 328 16. 55g 1. 00 6. 33 2387 CA GLY 521 32. 194 12. 105 15. 283 1. 00 6. 71 2388 C GLY 521 30. 835 12. 711 14. 994 1. 00 7. 73 2389 O GLY 521 30.284 12.452 13.938 1.00 9. 45 2390 N LEU 522 30.305 13.519 15.907 1.00 7. 99 2391 CA LEU 522 29. 023 14. 206 15. 703 1. 00 8. 13 2392 CB LEU 522 28. 065 13. 959 16. 880 1. 00 7. 76 2393 CG LEU 522 27.418 12.565 16.999 1.00 9. 15 2394 CD1 LEU 522 26.705 12.382 18.315 1.00 9. 31 2395 CD2 LEU 522 26. 435 12. 319 15. 825 1. 00 7. 85 2396 C LEU 522 29. 261 15. 719 15. 582 1. 00 8. 19 2397 O LEU 522 30. 316 16. 193 16. 024 1. 00 7. 33 2398 N PRO 523 28. 274 16. 411 15. 000 1. 00 8. 67 2399 CD PRO 523 27. 069 15. 840 14. 366 1. 00 8. 01 2400 CA PRO 523 28. 300 17. 869 14. 890 1. 00 7. 67 2401 CB PRO 523 26.970 18.272 14.327 1.00 8. 61 2402 CG PRO 523 26. 381 17. 023 13. 727 1. 00 8. 95 2403 C PRO 523 28. 544 18. 447 16. 278 1. 00 6. 70 2404 O PRO 523 28. 127 17. 885 17. 290 1. 00 7. 17 2405 N VAL 524 29. 249 19. 581 16. 352 1. 00 7. 33 2406 CA VAL 524 29. 633 20. 220 17. 559 1. 00 7. 89 2407 CB VAL 524 31.189 20.288 17.792 1.00 9. 48 2408 CG1 VAL 524 31. 833 18. 893 17. 834 1. 00 12. 94 2409 CG2 VAL 524 31. 918 21. 204 16. 887 1. 00 10. 36 2410 C VAL 524 29.064 21.629 17.773 1.00 7. 52 2411 O VAL 524 28.840 22.360 16.831 1.00 8. 82 2412 N CYS 525 28. 833 21. 979 19. 004 1. 00 8. 78 2413 CA CYS 525 28. 323 23. 291 19. 389 1. 00 10. 81 2414 CB CYS 525 26. 808 23. 259 19. 731 1. 00 12. 78 2415 SG CYS 525 26.478 22.079 21.069 1.00 19. 26 2416 C CYS 525 29. 064 23. 725 20. 669 1. 00 11. 03 2417 O CYS 525 29. 720 22. 926 21. 347 1. 00 10. 93 2418 N GLN 526 28. 938 25. 012 21. 003 1. 00 10. 86 2419 CA GLN 526 29. 524 25. 543 22. 189 1. 00 10. 78 242, 0 CB GLN 526 29. 325 27. 071 22. 253 1. 00 14. 97 2421 CG GLN 526 29.985 27.861 21.129 1.00 18. 80 2422 CD GLN 526 29. 732 29. 353 21. 346 1. 00 23. 43 2423 OE1 GLN 526 30.390 29.993 22.164 1.00 25. 70 2424 NE2 GLN 526 28. 707 29. 870 20. 687 1. 00 25. 08 2425 C GLN 526 28.817 24.968 23.401 1.00 9. 87 2426 O GLN 526 27. 598 24. 687 23. 367 1. 00 9. 79 2427 N ASP 527 29. 553 24. 782 24. 481 1. 00 9. 34 2428 CA ASP 527 29. 000 24. 319 25. 735 1. 00 8. 75 <BR> <BR> 2429 CB ASP 527 29. 956 23. 560 26. 592 1. 00 6. 83 2430 CG ASP 527 29. 424 23. 025 27. 867 1. 00 8. 25 <BR> <BR> 2431 OD1 ASP 527 30. 234 22. 466 28. 669 1. 00 7. 82 2432 OD2 ASP 527 28. 189 23. 100 28. 172 1. 00 8. 59 2433 C ASP 527 28. 276 25. 437 26. 514 1. 00 8. 54 2434 ASP52728. 82126. 12627. 3691. 008. 43 2435 N HIS 528 26. 969 25. 564 26. 240 1. 00 8. 33 2436 CA HIS 528 26. 114 26. 501 26. 917 1. 00 7. 88 2437 CB HIS 528 25. 515 27. 559 26. 015 1. 00 8. 49 2438 CG HIS 528 26. 434 28. 521 25. 350 1. 00 10. 58 2439 CD2 HIS 528 27. 652 28. 983 25. 745 1. 00 12. 19 <BR> <BR> 2440 ND1 HIS 528 26. 222 29. 050 24. 117 1. 00 11. 19 2441 CE1 HIS 528 27. 206 29. 880 23. 803 1. 00 11. 81 <BR> <BR> 2442 NE2 HIS 528 28. 127 29. 794 24. 737 1. 00 11. 11 2443 C HIS 528 24. 987 25. 767 27. 642 1. 00 8. 02 2444 O HIS 528 23. 927 26. 335 27. 890 1. 00 8. 25 2445 N LEU 529 25. 240 24. 522 28. 048 1. 00 8. 42 2446 CA LEU 529 24.235 23.741 28.739 1.00 7.37 2447 CB LEU 529 24. 691 22. 260 28. 855 1. 00 7. 87 2448 CG LEU 529 24.988 21.530 27.545 1.00 6. 08 2449 CD1 LEU 529 25. 238 20. 035 27. 904 1. 00 4. 09 2450 CD2 LEU 529 23. 837 21. 667 26. 568 1. 00 6. 00 2451 C LEU 529 23. 833 24. 273 30. 080 1. 00 7. 26 2452 O LEU 529 22. 650 24. 298 30. 387 1. 00 7. 16 2453 N GLU 530 24. 774 24. 689 30. 930 1. 00 6. 85 2454 CA GLU 530 24. 478 25. 213 32. 249 1. 00 7. 91 2455 CB GLU 530 25. 751 25. 555 33. 040 1. 00 8. 68 2456 CG GLU 530 26.665 24.337 33.216 1.00 11. 33 2457 CD GLU 530 26. 018 23. 267 34. 036 1. 00 13. 56 2458 OE1 GLU 530 25. 325 23. 608 35. 025 1. 00 15. 71 <BR> <BR> 2459 OE2 GLU 530 26. 153 22. 074 33. 709 1. 00 16. 38 2460 C GLU 530 23. 600 26. 472 32. 108 1. 00 6. 81 2461 O GLU 530 22. 717 26. 596 32. 941 1. 00 8. 63 2462 N PHE 531 23. 876 27. 310 31. 151 1. 00 7. 22 2463 CA PHE 531 23. 115 28. 510 30. 881 1. 00 7. 31 2464 CB PHE 531 23. 718 29. 420 29. 775 1. 00 7. 96 2465 CG PHE 531 22. 781 30. 565 29. 393 1. 00 7. 32 2466 CD1 PHE 531 22. 520 31. 576 30. 320 1. 00 9. 09 2467 CD2 PHE 531 22. 154 30. 564 28. 160 1. 00 7. 43 2468 CE1 PHE 531 21. 614 32. 569 30. 000 1. 00 9. 04 2469 CE2 PHE 531 21. 302 31. 615 27. 797 1. 00 7. 80 2470 CZ PHE 531 21. 031 32. 618 28. 736 1. 00 6. 90 2471 C PHE 531 21. 648 28. 189 30. 527 1. 00 6. 65 2472 O PHE 531 20.777 28.687 31.227 1.00 6. 17 2473 N TRP 532 21. 470 27. 471 29. 452 1. 00 6. 00 2474 CA TRP 532 20. 127 27. 082 29. 010 1. 00 6. 69 2475 CB TRP 532 20. 151 26. 436 27. 660 1. 00 6. 05 2476 CG TRP 532 20. 561 27. 293 26. 505 1. 00 6. 27 2477 CD2 TRP 532 19. 893 28. 521 26. 088 1. 00 7. 30 2478 CE2 TRP 532 20. 592 29. 020 24. 988 1. 00 8. 48 2479 CE3 TRP 532 18. 740 29. 180 26. 530 1. 00 5. 46 2480 CD1 TRP 532 21. 629 27. 151 25. 681 1. 00 5. 29 2481 NE1 TRP 532 21. 647 28. 142 24. 733 1. 00 9. 71 2482 CZ2 TRP 532 20. 244 30. 187 24. 315 1. 00 8. 41 2483 CZ3 TRP 532 18. 358 30. 322 25. 822 1. 00 4. 97 2484 CH2 TRP 532 19. 103 30. 824 24. 762 1. 00 6. 33 2485 C TRP 532 19. 360 26. 333 30. 059 1. 00 6. 84 2486 0 TRP 532 18. 154 26. 544 30. 249 1. 00 6. 35 2487 N GLU 533 19. 995 25. 376 30. 755 1. 00 6. 94 2488 CA GLU 533 19. 333 24. 653 31. 805 1. 00 7. 55 2489 CB GLU 533 20. 223 23. 604 32. 493 1. 00 6. 99 2490 CG GLU 533 19. 428 22. 834 33. 546 1. 00 8. 31 2491 CD GLU 533 20. 227 21. 880 34. 356 1. 00 10. 51 2492 OE1 GLU 533 21. 119 21. 189 33. 799 1. 00 12. 17 2493 OE2 GLU 533 20.046 21.793 35.567 1.00 10. 85 2494 C GLU 533 18. 844 25. 673 32. 858 1. 00 8. 56 2495 0 GLU 533 17. 672 25. 612 33. 277 1. 00 9. 42 2496 N GLY 534 19.685 26.587 33.269 1.00 7. 54 2497 CA GLY 534 19. 359 27. 627 34. 240 1. 00 6. 84 2498 C GLY 534 18. 141 28. 436 33. 764 1. 00 6. 21 2499 O GLY 534 17. 188 28. 545 34. 516 1. 00 7. 01 2500 N VAL 535 18. 157 28. 873 32. 530 1. 00 6. 55 2501 CA VAL 535 17. 024 29. 602 31. 965 1. 00 8. 34 2502 CB VAL 535 17. 270 30. 032 30. 516 1. 00 9. 42 2503 CG1 VAL 535 16. 091 30. 669 29. 778 1. 00 6. 56 2504 CG2 VAL 535 18. 467 30. 987 30. 470 1. 00 8. 97 2505 C VAL 535 15. 720 28. 798 32. 065 1. 00 9. 65 2506 O VAL 535 14.749 29.368 32.616 1.00 10. 50 2507 N PHE 536 15. 644 27. 606 31. 519 1. 00 8. 05 2508 CA PHE 536 14. 425 26. 835 31. 550 1. 00 8. 55 2509 CB PHE 536 14. 429 25. 688 30. 532 1. 00 6. 73 2510 CG PHE 536 14.267 26.163 29.094 1.00 6. 13 2511 CD1 PHE 536 12. 999 26. 178 28. 511 1. 00 5. 82 2512 CD2 PHE 536 15. 308 26. 744 28. 409 1. 00 4. 23 2513 CE1 PHE 536 12. 821 26. 668 27. 217 1. 00 5. 65 2514 CE2 PHE 536 15. 187 27. 221 27. 140 1. 00 5. 18 2515 CZ PHE 536 13. 916 27. 159 26. 533 1. 00 7. 61 2516 C PHE 536 13. 983 26. 526 32. 944 1. 00 8. 35 2517 O PHE 536 12. 771 26. 510 33. 220 1. 00 9. 08 2518 N THR 537 14. 881 26. 356 33. 897 1. 00 8. 37 2519 CA THR 537 14. 626 26. 090 35. 278 1. 00 10. 07 2520 CB THR 537 15. 898 25. 742 36. 078 1. 00 8. 98 2521 OG1 THR 537 16. 449 24. 543 35. 449 1. 00 11. 40 2522 CG2 THR 537 15. 623 25. 358 37. 511 1. 00 8. 50 2523 C THR 537 13. 809 27. 191 35. 948 1. 00 10. 66 2524 O THR 537 12. 958 26. 875 36. 811 1. 00 12. 47 2525 N GLY 538 13. 956 28. 417 35. 539 1. 00 10. 15 2526 CA GLY 538 13. 209 29. 535 36. 057 1. 00 9. 56 2527 C GLY 538 11. 854 29. 714 35. 414 1. 00 10. 26 2528 0 GLY 538 11. 047 30. 514 35. 956 1. 00 11. 12 2529 N LEU 539 11. 482 28. 985 34. 364 1. 00 8. 87 2530 CA LEU 539 10. 184 29. 195 33. 699 1. 00 9. 11 2531 CB LEU 539 10. 363 28. 966 32. 200 1. 00 8. 03 2532 CG LEU 539 11. 505 29. 729 31. 503 1. 00 7. 68 2533 CD1 LEU 539 11. 546 29. 445 30. 006 1. 00 7. 15 2534 CD2 LEU 539 11. 487 31. 255 31. 743 1. 00 6. 73 2535 C LEU 539 9. 120 28. 311 34. 309 1. 00 10. 41 2536 0 LEU 539 8. 675 27. 338 33. 698 1. 00 11. 94 2537 N THR 540 8. 685 28. 626 35. 530 1. 00 10. 69 2538 CA THR 540 7. 716 27. 870 36. 268 1. 00 11. 18 2539 CB THR 540 8. 061 27. 841 37. 773 1. 00 13. 16 2540 OG1 THR 540 8. 144 29. 193 38. 224 1. 00 13. 69 2541 CG2 THR 540 9. 397 27. 156 38. 065 1. 00 13. 59 2542 C THR 540 6. 280 28. 376 36. 144 1. 00 11. 51 2543 0 THR 540 6. 007 29. 559 35. 975 1. 00 11. 40 2544 N HIS 541 5. 341 27. 426 36. 328 1. 00 11. 14 2545 CA HIS 541 3. 931 27. 728 36. 251 1. 00 11. 46 2546 CB HIS 541 3. 475 28. 594 37. 427 1. 00 15. 80 2547 CG HIS 541 3. 827 27. 949 38. 726 1. 00 19. 19 2548 CD2 HIS 541 4. 635 28. 331 39. 737 1. 00 20. 81 2549 ND1 HIS 541 3. 316 26. 712 39. 098 1. 00 22. 15 2550 CE1 HIS 541 3. 813 26. 377 40. 273 1. 00 21. 59 <BR> <BR> 2551 NE2 HIS 541 4. 601 27. 342 40. 678 1. 00 21. 85 2552 C HIS 541 3. 448 28. 316 34. 933 1. 00 10. 25 2553 0 HIS 541 2. 709 29. 320 34. 916 1. 00 9. 90 2554 N ILE 542 3. 844 27. 721 33. 813 1. 00 8. 53 2555 CA ILE 542 3. 400 28. 146 32. 511 1. 00 8. 25 2556 CB ILE 542 4. 084 27. 385 31. 361 1. 00 7. 96 2557 CG2 ILE 542 3.662 25.908 31.321 1.00 7. 52 2558 CG1 ILE 542 3. 910 28. 052 30. 010 1. 00 5. 98 2559 CD1 ILE 542 4. 899 27. 582 28. 922 1. 00 3. 75 2560 C ILE 542 1. 861 27. 834 32. 494 1. 00 8. 71 2561 0 IZE 542 1. 431 26. 959 33. 241 1. 00 7. 29 2562 N ASP 543 1. 147 28. 600 31. 686 1. 00 8. 70 2563 CA ASP 543-0. 295 28. 362 31. 573 1. 00 8. 97 2564 CB ASP 543-0. 997 29. 626 31. 062 1. 00 9. 45 2565 CG ASP 543-2. 514 29. 459 30. 834 1. 00 8. 01 2566 OD1 ASP 543-3. 236 29. 484 31. 821 1. 00 11. 20 2567 OD2 ASP 543-2. 907 29. 335 29. 667 1. 00 11. 21 2568 C ASP 543-0. 465 27. 230 30. 544 1. 00 8. 87 2569 0 ASP 543-0. 007 27. 318 29. 399 1. 00 9. 90 2570 N ALA 544-1. 127 26. 202 30. 980 1. 00 10. 26 2571 CA ALA 544-1. 412 25. 020 30. 160 1. 00 10. 45 2572 CB ALA 544 -2.238 24.041 31.015 1.00 10. 74 2573 C ALA 544-2. 136 25. 374 28. 898 1. 00 10. 06 2574 O ALA 544-1. 849 24. 905 27. 807 1. 00 9. 69 2575 N HIS 545-3. 228 26. 149 29. 067 1. 00 10. 04 2576 CA HIS 545-4. 007 26. 610 27. 899 1. 00 9. 51 2577 CB HIS 545-5. 115 27. 555 28. 505 1. 00 13. 19 2578 CG HIS 545-5. 893 28. 224 27. 425 1. 00 16. 63 2579 ND1 HIS 545-6. 906 27. 607 26. 706 1. 00 18. 75 2580 CE1 HIS 545-7. 369 28. 449 25. 802 1. 00 19. 88 2581 NE2 HIS 545-6. 657 29. 579 25. 877 1. 00 20. 70 2582 CD2 HIS 545-5. 752 29. 459 26. 892 1. 00 18. 88 2583 C HIS 545-3. 217 27. 291 26. 844 1. 00 8. 15 2584 O HIS 545 -3.373 26.967 25.669 1.00 8. 14 2585 N PHE 546-2. 322 28. 267 27. 160 1. 00 9. 17 2586 CA PHE 546-1. 507 28. 951 26. 170 1. 00 9. 15 2587 CB PHE 546-0. 822 30. 230 26. 692 1. 00 10. 63 2588 CG PHE 546-1. 831 31. 281 27. 115 1. 00 11. 60 2589 CD1 PHE 546-2. 843 31. 682 26. 259 1. 00 11. 81 2590 CD2 PHE 546-1. 698 31. 868 28. 355 1. 00 11. 57 2591 CE1 PHE 546-3. 752 32. 641 26. 698 1. 00 12. 77 2592 CE2 PHE 546-2. 635 32. 822 28. 795 1. 00 11. 68 2593 CZ PHE 546-3. 664 33. 163 27. 977 1. 00 11. 62 2594 C PHE 546-0. 443 28. 047 25. 523 1. 00 9. 65 2595 0 PHE 546-0. 174 28. 200 24. 334 1. 00 9. 83 2596 N LEU 547 0. 172 27. 171 26. 328 1. 00 10. 38 2597 CA LEU 547 1. 151 26. 213 25. 783 1. 00 9. 50 2598 CB LEU 547 1. 817 25. 438 26. 927 1. 00 7. 82 2599 CG LEU 547 2. 832 24. 361 26. 510 1. 00 7. 09 2600 CD1 LEU 547 3. 965 25. 018 25. 699 1. 00 8. 06 2601 CD2 LEU 547 3. 385 23. 633 27. 714 1. 00 5. 06 2602 C LEU 547 0. 497 25. 257 24. 784 1. 00 10. 47 2603 O LEU 547 1. 037 24. 944 23. 731 1. 00 9. 56 2604 N SER 548-0. 769 24. 858 25. 094 1. 00 12. 30 2605 CA SER 548-1. 543 24. 017 24. 193 1. 00 13. 08 2606 CB SER 548-2. 966 23. 738 24. 666 1. 00 14. 63 2607 OG SER 548-2. 928 23. 071 25. 933 1. 00 18. 22 2608 C SER 548-1. 667 24. 688 22. 839 1. 00 13. 29 2609 0 SER 548-1. 569 24. 052 21. 798 1. 00 14. 72 2610 N GLN 549-1. 837 26. 001 22. 846 1. 00 13. 05 2611 CA GLN 549-1. 978 26. 776 21. 642 1. 00 14. 18 2612 CB GLN 549-2. 140 28. 278 22. 012 1. 00 18. 67 2613 CG GLN 549-3. 021 28. 716 23. 044 1. 00 22. 48 2614 CD GLN 549 -4.500 28.553 22.924 1.00 25. 55 2615 OE1 GLN 549-5. 211 29. 423 23. 490 1. 00 27. 43 2616 NE2 GLN 549 -4.975 27.555 22.221 1.00 26. 35 2617 C GLN 549-0.695 26. 844 20. 787 1. 00 13.51 2618 0 GLN 549-0. 732 26. 687 19. 574 1. 00 14. 24 2619 N THR 550 0. 388 27. 261 21. 454 1. 00 12. 40 2620 CA THR 550 1. 656 27. 430 20. 766 1. 00 12.74 2621 CB THR 550 2. 757 28. 130 21. 588 1. 00 10.13 2622 OG1 THR 550 3.044 27.459 22.810 1. 00 10. 98 2623 CG2 THR 550 2.298 29.542 21.978 1. 00 10.68 2624 C THR 550 2. 068 26. 094 20. 186 1. 00 12.34 2625 0 THR 550 2. 516 26. 034 19. 066 1. 00 12.80 2626 N LYS 551 1.908 25.032 20.989 1. 00 14.50 2627 CA LYS 551 2. 241 23. 676 20. 530 1. 00 15.11 2628 CB LYS 551 2. 066 22. 660 21. 646 1. 00 14.02 2629 CG LYS 551 3. 143 22. 683 22. 712 1. 00 10.58 2630 CD LYS 551 2. 901 21. 760 23. 855 1. 00 7.95 2631 CE LYS 551 2. 622 20. 313 23. 466 1. 00 6.88 2632 NZ LYS 551 2. 367 19. 455 24. 647 1. 00 9.60 2633 C LYS 551 1. 385 23. 280 19. 337 1. 00 18.00 2634 0 LYS 551 1. 898 22. 883 18. 289 1. 00 18.23 2635 N GLN 552 0. 056 23. 479 19. 476 1. 00 19.71 2636 CA GLN 552-0. 881 23. 186 18. 419 1. 00 22.03 2637 CB GLN 552-2. 348 23. 279 18. 797 1. 00 24.65 2638 CG GLN 552 -2.850 22.272 19.809 1. 00 28.46 2639 CD GLN 552-4. 346 22. 381 20. 079 1. 00 31.04 2640 OE1 GLN 552-5. 153 21. 669 19. 447 1. 00 34.02 2641 NE2 GLN 552-4. 756 23. 249 20. 996 1. 00 30.17 2642 C GLN 552-0. 622 24. 021 17. 179 1. 00 21.92 2643 O GLN 552 -0.919 23.528 16.104 1. 00 23.48 2644 N SER 553-0. 065 25. 208 17. 286 1. 00 21.31 2645 CA SER 553 0. 199 26. 039 16. 147 1. 00 22.36 2646 CB SER 553 0. 336 27. 530 16. 534 1. 00 23.76 2647 OG SER 553 1. 577 27. 690 17. 215 1. 00 25.22 2648 C SER 553 1. 479 25. 666 15. 398 1. 00 23. 12 2649 O SER 553 1.694 26.281 14.342 1.00 23.97 2650 N GLY 554 2.308 24.740 15.863 1. 00 22.73 2651 CA GLY 554 3. 508 24. 437 15. 075 1. 00 23.80 2652 C GLY 554 4. 576 25. 513 15. 139 1. 00 24.01 2653 0 GLY 554 5. 633 25. 459 14. 491 1. 00 25.14 2654 N GLU 555 4. 379 26. 492 15. 967 1. 00 23.60 2655 CA GLU 555 5. 282 27. 586 16. 235 1. 00 23.69 2656 CB GLU 555 4. 528 28. 481 17. 216 1. 00 26.10 2657 CG GLU 555 5. 346 29. 667 17. 744 1. 00 29.38 2658 CD GLU 555 4. 302 30. 815 17. 834 1. 00 30.80 2659 OE1 GLU 555 4. 437 31. 626 16. 864 1. 00 32.63 2660 OE2 GLU 555 3. 398 30. 774 18. 646 1. 00 29.97 2661 C GLU 555 6. 646 27. 184 16. 751 1. 00 21.67 2662 0 GLU 555 6. 807 26. 197 17. 497 1. 00 19.96 2663 N ASN 556 7. 664 27. 985 16. 401 1. 00 19.76 2664 CA ASN 556 9. 023 27. 661 16. 873 1. 00 18.50 2665 CB ASN 556 10. 102 28. 405 16. 084 1. 00 22.32 2666 CG ASN 556 11. 398 27. 620 16. 066 1. 00 26.45 2667 OD1 ASN 556 11. 543 26. 829 15. 083 1. 00 30.32 2668 ND2 ASN 556 12. 350 27. 690 16. 944 1. 00 27.61 2669 C ASN 556 9. 071 28. 108 18. 346 1. 00 14.81 2670 O ASN 556 8.433 29.162 18.644 1. 00 15.46 2671 N LEU 557 9. 765 27. 412 19-188 1. 00 10.52 2672 CA LEU 557 9. 877 27. 740 20. 590 1. 00 8.71 2673 CB LEU 557 10. 815 28. 953 20. 818 1. 00 8.61 2674 CG LEU 557 12. 256 28. 747 20. 362 1. 00 7.25 2675 CD1 LEU 557 13. 017 30. 080 20. 391 1. 00 8.59 2676 CD2 LEU 557 12. 970 27. 788 21. 348 1. 00 9.29 2677 C LEU 557 8. 548 27. 958 21. 279 1. 00 7. 24 2678 0 LEU 557 8. 341 29. 032 21. 900 1. 00 5. 66 2679 N PRO 558 7. 675 26. 970 21. 229 1. 00 7. 39 2680 CD PRO 558 7. 889 25. 673 20. 501 1. 00 6. 26 2681 CA PRO 558 6. 352 27. 013 21. 828 1. 00 7. 11 2682 CB PRO 558 5. 689 25. 658 21. 452 1. 00 7. 77 2683 CG PRO 558 6. 869 24. 760 21. 167 1. 00 7. 01 2684 C PRO 558 6. 357 27. 260 23. 303 1. 00 6. 43 2685 0 PRO 558 5. 460 27. 970 23. 791 1. 00 6. 54 2686 N TYR 559 7. 370 26. 754 24. 045 1. 00 5. 53 2687 CA TYR 559 7. 476 26. 948 25. 448 1. 00 5. 66 2688 CB TYR 559 8. 492 26. 027 26. 130 1. 00 7. 67 2689 CG TYR 559 8. 209 25. 753 27. 599 1. 00 7. 39 2690 CD1 TYR 559 7. 192 24. 792 27. 860 1. 00 8. 05 2691 CE1 TYR 559 6. 862 24. 460 29. 147 1. 00 9. 09 2692 CD2 TYR 559 8. 819 26. 380 28. 653 1. 00 7. 92 2693 CE2 TYR 559 8. 487 26. 073 29. 965 1. 00 8. 81 2694 CZ TYR 559 7. 517 25. 089 30. 193 1. 00 9. 16 2695 OH TYR 559 7. 196 24. 751 31. 478 1. 00 10. 11 2696 C TYR 559 7. 817 28. 432 25. 736 1. 00 6. 25 2697 0 TYR 559 7. 154 29. 046 26. 577 1. 00 6. 22 2698 N LEU 560 8. 834 28. 952 25. 099 1. 00 6. 93 2699 CA LEU 560 9. 223 30. 353 25. 291 1. 00 7. 81 2700 CB LEU 560 10.550 30.712 24.661 1.00 7. 24 2701 CG LEU 560 11. 826 30. 025 25. 179 1. 00 6. 74 2702 CD1 LEU 560 13. 017 30. 800 24. 583 1. 00 6. 22 2703 CD2 LEU 560 11. 886 30. 014 26. 699 1. 00 6. 99 2704 C LEU 560 8. 123 31. 328 24. 837 1. 00 6. 86 2705 O LEU 560 7.945 32.371 25.524 1.00 6. 84 2706 N VAL 561 7. 447 30. 992 23. 779 1. 00 5. 45 2707 CA VAL 561 6. 351 31. 871 23. 298 1. 00 6. 98 2708 CB VAL 561 5.918 31.547 21.897 1.00 5. 73 2709 CG1 VAL 561 4. 716 32. 417 21. 467 1. 00 7. 05 2710 CG2 VAL 561 7. 031 31. 718 20. 834 1. 00 7. 24 2711 C VAL 561 5.222 31.820 24.313 1.00 7. 19 27120VAL5614. 70432. 87624. 7431. 006. 07 2713 N ALA 562 4. 776 30. 631 24. 721 1. 00 5. 94 2714 CA ALA 562 3. 704 30. 490 25. 685 1. 00 7. 32 2715 CB ALA 562 3. 287 29. 006 25. 815 1. 00 5. 71 2716 C ALA 562 4. 061 31. 069 27. 039 1. 00 6. 75 2717 0 ALA 562 3. 194 31. 553 27. 779 1. 00 6. 79 2718 N TYR 563 5. 347 31. 104 27. 433 1. 00 6. 75 2719 CA TYR 563 5. 733 31. 614 28. 714 1. 00 5. 71 2720 CB TYR 563 7. 142 31. 187 29. 154 1. 00 5. 27 2721 CG TYR 563 7. 230 31. 298 30. 675 1. 00 4. 76 2722 CD1 TYR 563 6. 718 30. 255 31. 460 1. 00 4. 44 2723 CE1 TYR 563 6. 769 30. 305 32. 839 1. 00 3. 34 2724 CD2 TYR 563 7.696 32.433 31.320 1.00 5. 62 2725 CD2 TYR 563 70697 32.484 32.685 1.00 3. 46 2726 CZ TYR 563 7. 223 31. 441 33. 450 1. 00 4. 91 2727 OH TYR 563 7. 236 31. 555 34. 820 1. 00 6. 12 2728 C TYR 563 5. 609 33. 171 28. 714 1. 00 5. 77 2729 O TYR 563 5. 079 33. 697 29. 710 1. 00 5. 91 2730 N GLN 564 6. 056 33. 749 27. 648 1. 00 5. 04 2731 CA GLN 564 5.944 35.214 27.522 1.00 7. 24 2732 CB GLN 564 6.618 35.718 26.268 1.00 6. 54 2733 CG GLN 564 6. 510 37. 254 26. 053 1. 00 7. 38 2734 CD GLN 564 7.247 38.086 27.079 1.00 8. 49 2735 OE1 GLN 564 8.490 38.303 26.955 1.00 8. 19 2736 NE2 GLN 564 6. 551 38. 559 28. 116 1. 00 8. 93 2737 C GZN 564 4. 419 35. 564 27. 520 1. 00 6. 84 2738 O GLN 564 4.030 36.491 28.221 1.00 6. 56 2739 N ALA 565 3. 645 34. 842 26. 765 1. 00 7. 51 2740 CA ALA 565 2. 194 35. 016 26. 687 1. 00 8. 39 2741 CB ALA 565 1. 611 33. 978 25. 711 1. 00 7. 90 2742 C ALA 565 1.521 34.899 28.034 1.00 9. 12 2743 0 ALA 565 0. 584 35. 644 28. 334 1. 00 8. 85 2744 N THR 566 1. 898 33. 880 28. 818 1. 00 8. 96 2745 CA THR 566 1. 396 33. 611 30. 149 1. 00 8. 57 2746 CB THR 566 2. 047 32. 357 30. 778 1. 00 9. 52 2747 OG1 THR 566 1. 693 31. 177 30. 059 1. 00 9. 05 2748 CG2 THR 566 1. 682 32. 148 32. 239 1. 00 9. 06 2749 C THR 566 1. 692 34. 835 31. 052 1. 00 8. 15 2750 O THR 566 0.838 35.325 31.731 1.00 6. 65 2751 N VAL 567 2. 946 35. 294 31. 054 1. 00 7. 34 2752 CA VAL 567 3.353 36.450 31.815 1.00 6. 96 2753 CB VAL 567 4.895 36.699 31.686 1.00 4. 40 2754 CG1 VAL 567 5.259 38.110 32.106 1.00 5. 55 2755 CG2 VAL 567 5.594 35.690 32.629 1.00 4. 61 2756 C VAL 567 2.526 37.685 31.424 1.00 6. 84 2757 0 VAL 567 2. 126 38. 435 32. 287 1. 00 7. 80 2758 N CYS 568 2. 297 37. 917 30. 142 1. 00 7. 80 2759 CA CYS 568 1. 521 39. 013 29. 632 1. 00 7. 41 2760 CB CYS 568 1.597 39.158 28.122 1.00 6. 19 2761 SG CYS 568 3. 200 39. 571 27. 419 1. 00 7. 44 2762 C CYS 568 0. 044 38. 919 30. 052 1. 00 7. 61 2763 O CYS 568-0. 511 39. 912 30. 501 1. 00 7. 59 2764 N ALA 569-0. 561 37. 751 29. 876 1. 00 7. 46 2765 CA ALA 569 -2.005 37.623 30.275 1.00 6. 35 2766 CB ALA 569-2. 474 36. 211 29. 862 1. 00 6. 05 2767 C ALA 569-2. 172 37. 874 31. 733 1. 00 6. 13 2768 O ALA 569-3. 128 38. 564 32. 174 1. 00 6. 25 2769 N ARG 570-1. 252 37. 401 32. 580 1. 00 6. 14 2770 CA ARG 570-1. 276 37. 561 34. 013 1. 00 5. 97 <BR> <BR> 2771 CB ARG 570-0. 322 36. 644 34. 754 1. 00 5. 02 2772 CG ARG 570-0. 649 35. 173 34. 678 1. 00 4. 81 2773 CD ARG 570 0. 402 34. 293 35. 369 1. 00 6. 06 2774 NE ARG 570-0. 036 32. 891 35. 279 1. 00 6. 08 2775 CZ ARG 570 0. 693 31. 810 35. 419 1. 00 6. 34 2776 NH1 ARG 570 1. 997 31. 949 35. 658 1. 00 6. 07 2777 NH2 ARG 570 0. 140 30. 605 35. 230 1. 00 7. 68 2778 C ARG 570-1. 068 39. 023 34. 423 1. 00 6. 41 2779 O ARG 570 -1.664 39.482 35.401 1.00 6. 75 <BR> <BR> 2780 N ALA 571-0. 333 39. 759 33. 618 1. 00 6. 62 2781 CA ALA 571-0. 155 41. 193 33. 955 1. 00 8. 73 2782 CB ALA 571 1. 231 41. 700 33. 585 1. 00 9. 80 2785 C ALA 571-1. 170 42. 066 33. 231 1. 00 7. 25 2786 O ALA 571-1. 101 43. 281 33. 392 1. 00 7. 21 2787 N GLN 572 -2.001 41.489 32.415 1.00 7. 88 2788 CA GLN 572 -2.947 42.141 31.560 1.00 9. 20 2789 CB GLN 572 -4.141 42.814 32.210 1.00 8. 14 2790 CG GLN 572 -5.033 41.877 33.008 1.00 8. 33 2791 CD GLN 572-6. 274 42. 574 33. 555 1. 00 8. 76 2792 OE1 GLN 572 -6.110 43.275 34.567 1.00 9. 63 2793 NE2 GLN 572-7. 416 42. 391 32. 915 1. 00 7. 87 2794 C GZN 572-2. 163 43. 152 30. 666 1. 00 9. 98 2795 0 GLN 572-2. 623 44. 271 30. 411 1. 00 9. 48 2796 N ALA 573-1. 006 42. 686 30. 203 1. 00 9. 09 2797 CA ALA 573-0. 098 43. 458 29. 385 1. 00 8. 93 2798 CB ALA 573 1. 323 43. 500 29. 986 1. 00 10. 06 2799 C ALA 573-0. 049 42. 932 27. 986 1. 00 8. 99 2800 O ALA 573-0. 274 41. 729 27. 672 1. 00 6. 78 2801 N PRO 574 0. 258 43. 814 27. 039 1. 00 10. 56 2802 CD PRO 574 0. 537 45. 262 27. 194 1. 00 10. 36 2803 CA PRO 574 0. 304 43. 405 25. 655 1. 00 11. 03 2804 CB PRO 574 0. 309 44. 706 24. 863 1. 00 11. 45 2805 CG PRO 574 0. 062 45. 776 25. 849 1. 00 10. 38 2806 C PRO 574 1. 585 42. 575 25. 402 1. 00 10. 27 2807 O PRO 574 2. 534 42. 691 26. 151 1. 00 10. 25 2808 N PRO 575 1. 498 41. 749 24. 393 1. 00 10. 25 2809 CD PRO 575 0. 339 41. 586 23. 499 1. 00 10. 55 2810 CA PRO 575 2. 675 40. 989 23. 946 1. 00 11. 46 2811 CB PRO 575 2. 149 40. 087 22. 865 1. 00 11. 38 2812 CG PRO 575 0. 780 40. 555 22. 498 1. 00 11. 76 2813 C PRO 575 3. 643 42. 012 23. 321 1. 00 13. 21 2814 O PRO 575 3. 260 43. 146 23. 008 1. 00 13. 02 2815 N PRO 576 4. 888 41. 598 23. 079 1. 00 13. 60 2816 CD PRO 576 5. 400 40. 245 23. 444 1. 00 13. 11 2817 CA PRO 576 5. 910 42. 460 22. 516 1. 00 14. 03 2818 CB PRO 576 7. 128 41. 529 22. 363 1. 00 13. 50 2819 CG PRO 576 6. 901 40. 449 23. 343 1. 00 13. 29 2820 C PRO 576 5. 499 43. 074 21. 194 1. 00 14. 66 2821 0 PRO 576 5. 953 44. 170 20. 856 1. 00 16. 56 2822 N SER 577 4. 659 42. 381 20. 434 1. 00 15. 17 2823 CA SER 577 4. 144 42. 893 19. 173 1. 00 14. 94 2824 CB SER 577 5. 116 42. 752 18. 023 1. 00 16. 23 2825 OG SER 577 5. 298 41. 385 17. 666 1. 00 17. 32 2826 C SER 577 2. 850 42. 145 18. 860 1. 00 14. 86 2827 O SER 577 2. 446 41. 282 19. 640 1. 00 14. 44 2828 N TRP 578 2. 217 42. 449 17. 757 1. 00 15. 59 2829 CA TRP 578 1.037 41.817 17.256 1.00 16. 68 2830 CB TRP 578-0. 199 42. 690 17. 056 1. 00 15. 52 2831 CG TRP 578-0. 716 43. 144 18. 407 1. 00 14. 70 2832 CD2 TRP 578-1. 366 42. 279 19. 359 1. 00 15. 34 2833 CE2 TRP 578-1. 614 43. 046 20. 508 1. 00 15. 21 2834 CE3 TRP 578-1. 746 40. 915 19. 335 1. 00 13. 89 2835 CD1 TRP 578-0. 606 44. 347 18. 997 1. 00 15. 57 2836 NE1 TRP 578-1. 161 44. 311 20. 259 1. 00 16. 14 2837 CZ2 TRP 578-2. 284 42. 538 21. 635 1. 00 14. 84 2838 CZ3 TRP 578-2. 352 40. 418 20. 470 1. 00 12. 91 2839 CH2 TRP 578-2. 630 41. 189 21. 575 1. 00 12. 33 2840 C TRP 578 1. 357 40. 870 16. 103 1. 00 18. 38 2841 0 TRP 578 0. 499 40. 431 15. 312 1. 00 19. 19 2842 N ASP 579 2. 652 40. 490 16. 055 1. 00 19. 10 2843 CA ASP 579 3. 129 39. 505 15. 093 1. 00 19. 25 2844 CB ASP 579 4. 571 39. 035 15. 488 1. 00 22. 79 2845 CG ASP 579 5. 132 38. 069 14. 447 1. 00 25. 67 2846 OD1 ASP 579 5. 271 38. 590 13. 290 1. 00 28. 68 2847 OD2 ASP 579 5. 396 36. 863 14. 609 1. 00 24. 13 2848 C ASP 579 2. 280 38. 250 15. 341 1. 00 18. 28 2849 O ASP 579 1. 905 38. 044 16. 488 1. 00 17. 81 2850 N GLN 580 2.103 37.418 14.345 1.00 19. 29 2851 CA GLN 580 1. 313 36. 205 14. 497 1. 00 20. 01 2852 CB GLN 580 1. 107 35. 518 13. 154 1. 00 24. 61 2853 CG GLN 580 2.365 35.128 12.430 1.00 30. 70 2854 CD GLN 580 2. 189 34. 315 11. 150 1. 00 34. 29 2855 OE1 GLN 580 1. 212 33. 577 10. 944 1. 00 36. 22 2856 NE2 GLN 580 3. 182 34. 410 10. 259 1. 00 34. 91 2857 C GLN 580 1. 830 35. 286 15. 581 1. 00 18. 84 2858 O GLN 580 1. 086 34. 434 16. 072 1. 00 17. 93 2859 N MET 581 3. 087 35. 387 15. 992 1. 00 17. 73 2860 CA MET 581 3. 618 34. 559 17. 085 1. 00 16. 55 2861 CB MET 581 5. 018 35. 128 17. 400 1. 00 16. 65 2862 CG MET 581 5. 748 34. 545 18. 560 1. 00 17. 20 2863 SD MET 581 7.438 35.224 18.688 1.00 15. 83 2864 CE MET 581 8. 111 34. 686 17. 128 1. 00 15. 55 2865 C MET 581 2.788 34.698 18.360 1.00 15. 99 2866 O MET 581 2.643 33.838 19.196 1.00 15. 53 2867 N TRP 582 2. 219 35. 902 18. 511 1. 00 15. 89 2868 CA TRP 582 1. 426 36. 258 19. 678 1. 00 15. 82 2869 CB TRP 582 1. 854 37. 702 20. 054 1. 00 13. 54 2870 CG TRP 582 3.347 37.869 20.208 1.00 11. 71 2871 CD2 TRP 582 4. 208 37. 177 21. 122 1. 00 10. 64 2872 CE2 TRP 582 5. 497 37. 655 20. 920 1. 00 11. 02 2873 CE3 TRP 582 3. 989 36. 239 22. 140 1. 00 10. 77 2874 CD1 TRP 582 4.148 38.655 19.430 1.00 11. 15 2875 NE1 TRP 582 5. 427 38. 559 19. 883 1. 00 13. 03 2876 CZ2 TRP 582 6. 597 37. 176 21. 637 1. 00 10. 19 2877 CZ3 TRP 582 5. 075 35. 793 22. 893 1. 00 11. 27 2878 CH2 TRP 582 6. 372 36. 249 22. 598 1. 00 9. 97 2879 C TRP 582-0. 078 36. 207 19. 455 1. 00 15. 67 2880 O TRP 582-0. 852 36. 871 20. 165 1. 00 15. 26 2881 N LYS 583 -0.532 35.385 18.529 1.00 16. 09 2882 CA LYS 583-1. 939 35. 277 18. 197 1. 00 16. 91 2883 CB LYS 583-2. 126 34. 437 16. 914 1. 00 18. 82 2884 CG LYS 583-1. 735 32. 961 17. 089 1. 00 20. 15 2885 CD LYS 583-1. 974 32. 231 15. 779 1. 00 22. 14 2886 CE LYS 583 -1.647 30.754 15.909 1.00 24. 40 2887 NZ LYS 583-1. 779 30. 066 14. 602 1. 00 25. 95 2888 C LYS 583 -2.834 34.776 19.292 1.00 16. 66 2889 O LYS 583-4. 047 35. 079 19. 354 1. 00 17. 10 2890 N CYS 584-2. 314 33. 994 20. 213 1. 00 16. 78 2891 CA CYS 584-3. 052 33. 436 21. 318 1. 00 15. 74 2892 CB CYS 584-2. 243 32. 382 22. 070 1. 00 16. 03 2893 SG CYS 584-0. 741 32. 973 22. 889 1. 00 15. 96 2894 C CYS 584-3. 551 34. 555 22. 233 1. 00 15. 78 2895 O CYS 584-4. 419 34. 324 23. 068 1. 00 16. 95 2896 N LEU 585-3. 032 35. 791 22. 036 1. 00 14. 33 2897 CA LEU 585-3. 486 36. 894 22. 853 1. 00 12. 46 2898 CB LEU 585-2. 322 37. 662 23. 459 1. 00 10. 23 2899 CG LEU 585-1. 459 36. 905 24. 472 1. 00 9. 30 2900 CD1 LEU 585-0. 326 37. 822 24. 944 1. 00 9. 39 2901 CD2 LEU 585 -2.254 36.350 25.629 1.00 9. 57 2902 C LEU 585-4. 401 37. 866 22. 121 1. 00 12. 65 2903 0 LEU 585-4. 911 38. 741 22. 759 1. 00 12. 36 2904 N ILE 586 -4.592 37.679 20.837 1.00 15. 23 2905 CA ILE 586-5. 409 38. 529 19. 997 1. 00 17. 07 2906 CB ILE 586 -5.468 38.042 18.528 1.00 17.75 2907 CG1 ILE 586-4. 117 38. 174 17. 850 1. 00 18. 31 2908 CD1 ILE 586-3. 909 37. 691 16. 437 1. 00 17. 13 2909 CG2 ILE 586 -6.584 38.745 17.758 1.00 18.50 2910 C ILE 586 -6.790 38.716 20.619 1.00 17. 48 2911 O ILE 586-7. 240 39. 852 20. 725 1. 00 18. 42 2912 N ARG 587-7. 443 37. 650 21. 036 1. 00 18. 10 2913 CA ARG 587-8. 759 37. 775 21. 649 1. 00 19. 24 2914 CB ARG 587-9. 295 36. 373 22. 017 1. 00 22. 94 2915 CG ARG 587-8. 274 35. 539 22. 809 1. 00 26. 78 2916 CD ARG 587-8. 884 34. 237 23. 312 1. 00 29. 07 2917 NE ARG 587-7. 894 33. 331 23. 905 1. 00 30. 47 2918 CZ ARG 587-6. 988 32. 584 23. 263 1. 00 27. 92 2919 NH1 ARG 587-6. 925 32. 539 21. 955 1. 00 25. 15 2920 NH2 ARG 587-6. 117 31. 897 23. 995 1. 00 26. 44 2921 C ARG 587-8. 826 38. 753 22. 795 1. 00 18. 42 2922 O ARG 587 -9.861 39.428 23.028 1.00 17. 41 2923 N LEU 588-7. 746 38. 941 23. 557 1. 00 16. 96 2924 CA LEU 588-7. 664 39. 798 24. 690 1. 00 15. 27 2925 CB LEU 588-6. 587 39. 217 25. 668 1. 00 14. 08 2926 CG LEU 588-6. 904 37. 854 26. 232 1. 00 12. 91 2927 CD1 LEU 588 -5.728 37.359 27.087 1.00 13. 11 2928 CD2 LEU 588-8. 136 38. 017 27. 122 1. 00 12. 19 2929 C LEU 588-7. 183 41. 223 24. 450 1. 00 15. 63 2930 O LEU 588-7. 102 41. 997 25. 402 1. 00 15. 79 2931 N LYS 589-6. 850 41. 550 23. 252 1. 00 15. 99 2932 CA LYS 589-6. 309 42. 850 22. 891 1. 00 16. 64 2933 CB LYS 589-6. 174 42. 866 21. 396 1. 00 17. 89 2934 CG LYS 589 -5.463 43.982 20.651 1.00 19. 53 2935 CD LYS 589-5. 454 43. 484 19. 192 1. 00 21. 26 2936 CE LYS 589-4. 694 44. 293 18. 220 1. 00 23. 05 2937 NZ LYS 589-4. 895 43. 796 16. 826 1. 00 22. 66 2938 C LYS 589 -6.935 44.049 23.524 1.00 16. 88 2939 O LYS 589-6. 252 44. 935 24. 068 1. 00 16. 14 2940 N PRO 590-8. 272 44. 173 23. 512 1. 00 17. 44 2941 CD PRO 590-9. 181 43. 184 22. 893 1. 00 17. 07 2942 CA PRO 590-8. 942 45. 311 24. 071 1. 00 17. 84 2943 CB PRO 590-10. 435 44. 963 23. 849 1. 00 18. 34 2944 CG PRO 590 -10.404 44.015 22.701 1.00 18. 62 2945 C PRO 590-8. 712 45. 533 25. 545 1. 00 17. 05 2946 O PRO 590-8. 962 46. 607 26. 062 1. 00 18. 00 <BR> <BR> 2947 N THR 591-8. 300 44. 488 26. 251 1. 00 16. 29 2948 CA THR 591-8. 096 44. 492 27. 677 1. 00 14. 40 2949 CB THR 591-8. 662 43. 197 28. 347 1. 00 14. 79 2950 OG1 THR 591-7. 875 42. 017 28. 056 1. 00 15. 45 2951 CG2 THR 591-10. 031 42. 855 27. 751 1. 00 15. 48 <BR> <BR> 2952 C THR 591-6. 613 44. 572 28. 061 1. 00 12. 84 2953 O THR 591-6. 411 44. 564 29. 266 1. 00 14. 17 2954 N LEU 592-5. 689 44. 572 27. 125 1. 00 11. 81 2955 CA LEU 592-4. 262 44. 583 27. 454 1. 00 11. 79 2956 CB LEU 592-3. 442 43. 613 26. 611 1. 00 11. 37 2957 CG LEU 592-3. 883 42. 154 26. 635 1. 00 11. 47 2958 CD1 LEU 592-3. 123 41. 247 25. 678 1. 00 10. 75 2959 CD2 LEU 592-3. 878 41. 623 28. 057 1. 00 9. 30 2960 C LEU 592-3. 708 45. 981 27. 285 1. 00 12. 08 2961 0 LEU 592-3. 931 46. 623 26. 250 1. 00 13. 49 2962 N HIS 593-3. 044 46. 449 28. 319 1. 00 12. 67 2963 CA HIS 593-2. 527 47. 830 28. 299 1. 00 12. 63 2964 CB HIS 593-3. 518 48. 682 29. 154 1. 00 15. 41 2965 CG HIS 593-4. 944 48. 587 28. 733 1. 00 19. 77 2966 CD2 HIS 593-5. 636 49. 063 27. 662 1. 00 22. 08 2967 ND1 HIS 593-5. 873 47. 837 29. 434 1. 00 20. 42 2968 CE1 HIS 593-7. 074 47. 910 28. 851 1. 00 20. 29 2969 NE2 HIS 593-6. 945 48. 631 27. 773 1. 00 21. 41 2970 C HIS 593-1. 181 47. 875 29. 012 1. 00 11. 26 2971 0 HIS 593-0. 878 47. 038 29. 850 1. 00 10. 45 2972 N GLY 594-0. 405 48. 917 28. 735 1. 00 12. 06 2973 CA GLY 594 0. 867 49. 157 29. 363 1. 00 11. 34 2974 C GLY 594 2. 038 48. 522 28. 636 1. 00 11. 06 2975 O GLY 594 1. 879 47. 993 27. 532 1. 00 12. 01 2976 N PRO 595 3. 201 48. 590 29. 239 1. 00 12. 05 2977 CD PRO 595 3. 447 49. 175 30. 578 1. 00 11. 76 2978 CA PRO 595 4. 419 48. 005 28. 676 1. 00 11. 53 2979 CB PRO 595 5. 524 48. 621 29. 541 1. 00 12. 01 2980 CG PRO 595 4. 887 48. 830 30. 853 1. 00 12. 34 2981 C PRO 595 4. 480 46. 480 28. 860 1. 00 11. 60 2982 O PRO 595 3. 920 45. 864 29. 770 1. 00 11. 73 2983 N THR 596 5. 248 45. 865 27. 967 1. 00 11. 81 2984 CA THR 596 5. 426 44. 395 28. 025 1. 00 11. 75 2985 CB THR 596 5. 766 43. 855 26. 637 1. 00 10. 87 2986 OG1 THR 596 4.765 44.191 25.667 1.00 11. 28 2987 CG2 THR 596 6. 065 42. 371 26. 620 1. 00 11. 93 2988 C THR 596 6. 528 44. 064 29. 037 1. 00 9. 78 2989 O THR 596 7. 608 44. 628 28. 987 1. 00 10. 19 2990 N PRO 597 6.248 43.136 29.931 1.00 9. 56 2991 CD PRO 597 4. 954 42. 436 30. 128 1. 00 7. 98 2992 CA PRO 597 7. 254 42. 654 30. 904 1. 00 8. 95 2993 CB PRO 597 6. 471 41. 957 31. 961 1. 00 7. 76 2994 CG PRO 597 5. 032 42. 062 31. 557 1. 00 8. 80 2995 C PRO 597 8. 100 41. 716 30. 013 1. 00 9. 73 2996 O PRO 597 7.757 40.541 29.865 1.00 10. 60 2997 N LEU 598 9. 141 42. 291 29. 394 1. 00 9. 56 2998 CA LEU 598 9. 933 41. 530 28. 436 1. 00 10. 05 2999 CB LEU 598 10.608 42.505 27.442 1.00 10. 67 3000 CG LEU 598 11. 168 41. 888 26. 172 1. 00 10. 26 <BR> <BR> 3001 CD1 LEU 598 10. 066 41. 390 25. 265 1. 00 10. 08 3002 CD2 LEU 598 12. 112 42. 864 25. 457 1. 00 11. 44 3003 C LEU 598 10.927 40.588 29.053 1.00 9. 38 3004 0 LEU 598 11. 837 41. 006 29. 756 1. 00 9. 62 3005 N LEU 599 10. 817 39. 285 28. 697 1. 00 8. 66 3006 CA LEU 599 11. 668 38. 271 29. 275 1. 00 7. 96 3007 CB LEU 599 10. 865 36. 951 29. 369 1. 00 5. 69 3008 CG LEU 599 9. 506 37. 023 30. 065 1. 00 4. 72 3009 CD1 LEU 599 8. 849 35. 636 30. 115 1. 00 3. 72 3010 CD2 LEU 599 9. 607 37. 640 31. 450 1. 00 4. 98 3011 C LEU 599 12. 933 37. 961 28. 466 1. 00 7. 98 3012 0 LEU 599 13. 948 37. 614 29. 066 1. 00 8. 48 3013 N TYR 600 12. 828 38. 109 27. 207 1. 00 8. 45 3014 CA TYR 600 13. 769 37. 846 26. 142 1. 00 9. 29 3015 CB TYR 600 14. 161 36. 329 26. 103 1. 00 7. 89 3016 CG TYR 600 12. 950 35. 419 26. 373 1. 00 5. 37 3017 CD1 TYR 600 11. 900 35. 324 25. 504 1. 00 5. 39 3018 CE1 TYR 600 10. 783 34. 532 25. 845 1. 00 5. 30 3019 CD2 TYR 600 12. 940 34. 688 27. 568 1. 00 5. 69 3020 CE2 TYR 600 11. 860 33. 881 27. 880 1. 00 4. 94 3021 CZ TYR 600 10. 778 33. 819 26. 983 1. 00 3.67 3022 OH TYR 600 9. 720 33. 029 27. 378 1. 00 4.83 3023 C TYR 600 13. 123 38. 306 24. 854 1. 00 9.72 3024 0 TYR 600 11. 912 38. 658 24. 841 1. 00 8.74 3025 N ARG 601 13. 870 38. 376 23. 761 1. 00 9.35 3026 CA ARG 601 13. 386 38. 799 22. 464 1. 00 9.49 3027 CB ARG 601 14. 270 39. 942 21. 935 1. 00 11.09 3028 CG ARG 601 14. 153 41. 230 22. 786 1. 00 10.63 3029 CD ARG 601 15. 315 42. 164 22. 455 1. 00 12.58 3030 NE ARG 601 15. 303 43. 437 23. 082 1. 00 11.89 3031 CZ ARG 601 14. 675 44. 561 22. 745 1. 00 11.82 3032 NH1 ARG 601 14.036 44.625 21.625 1. 00 12.90 3033 NH2 ARG 601 14. 687 45. 565 23. 648 1. 00 11.64 3034 C ARG 601 13. 341 37. 663 21. 450 1. 00 10.82 3035 O ARG 601 14. 350 36. 991 21. 146 1. 00 10. 93 3036 N LEU 602 12. 178 37. 407 20. 877 1. 00 10.63 3037 CA LEU 602 11. 988 36. 366 19. 871 1. 00 11.35 3038 CB LEU 602 10. 919 35. 420 20. 402 1. 00 10.19 3039 CG LEU 602 11. 220 34. 773 21. 762 1. 00 10.45 3040 CD1 LEU 602 10.003 33.962 22.207 1. 00 12.14 3041 CD2 LEU 602 12. 453 33. 873 21. 686 1. 00 10.56 3042 C LEU 602 11. 647 36. 914 18. 512 1. 00 12.72 3043 0 LEU 602 11. 457 36. 193 17. 520 1. 00 14.31 3044 N GLY 603 11. 566 38. 208 18. 359 1. 00 15.64 3045 CA GLY 603 11. 276 38. 929 17. 119 1. 00 16.52 3046 C GLY 603 11. 376 40. 437 17. 413 1. 00 17.05 3047 O GLY 603 11. 945 40. 808 18. 453 1. 00 16.85 3048 N ALA 604 10. 785 41. 259 16. 560 1. 00 17.47 3049 CA ALA 604. 10.829 42. 712 16. 806 1.00 18.97 3050 CB ALA 604 10. 375 43. 501 15. 589 1. 00 19.06 3051 C ALA 604 9.926 43.047 18.002 1. 00 19.41 3052 O AZA 604 8. 897 42. 402 18. 183 1. 00 20.23 3053 N VAL 605 10. 363 44. 002 18. 789 1. 00 19.20 3054 CA VAL 605 9. 604 44. 448 19. 966 1. 00 19.41 3055 CB VAL 605 10. 440 44. 547 21. 223 1. 00 18.00 3056 CG1 VAL 605 9. 678 45. 133 22. 419 1. 00 18.61 3057 CG2 VAL 605 11. 057 43. 210 21. 610 1. 00 17.14 3058 C VAL 605 8. 969 45. 780 19. 579 1. 00 20.88 30590VAL6059. 69046. 76819. 3321. 00 21. 55 3060 N GLN 606 7. 650 45. 791 19. 411 1. 00 21.05 3061 CA GLN 606 7. 004 47. 038 19. 025 1. 00 22.57 3062 CB GLN 606 6.252 46.847 17.707 1. 00 25.69 3063 CG GLN 606 7. 359 46. 527 16. 671 1. 00 29.82 3064 CD GLN 606 6.868 46.273 15.289 1. 00 33.87 3065 OE1 GLN 606 7.404 46.842 14.316 1. 00 37.11 3066 NE2 GLN 606 5. 869 45. 403 15. 144 1. 00 33.72 3067 C GLN 606 6.313 47.784 20.105 1. 00 22.75 3068 O GLN 606 5. 928 48. 954 19. 903 1. 00 24.79 3069 N ASN 607 6. 190 47. 253 21. 311 1. 00 20.65 3070 CA ASN 607 5. 510 47. 933 22. 406 1. 00 18.78 3071 CB ASN 607 4. 657 46. 817 23. 139 1. 00 18.60 3072 CG ASN 607 3. 845 47. 412 24. 266 1. 00 18.39 3073 OD1 ASN 607 3. 612 48. 630 24. 286 1. 00 18.72 3074 ND2 ASN 607 3. 428 46. 626 25. 243 1. 00 16.09 3075 C ASN 607 6. 541 48. 424 23. 393 1. 00 17.38 3076 0 ASN 607 7. 676 47. 959 23. 287 1. 00 16.82 3077 N GLU 608 6. 178 49. 335 24. 293 1. 00 16.62 3078 CA GLU 608 7. 075 49. 786 25. 347 1. 00 16. 42 3079 CB GLU 608 6. 323 50. 822 26. 189 1. 00 21. 06 3080 CG GLU 608 7. 050 51. 409 27. 336 1. 00 27. 74 3081 CD GLU 608 6. 296 52. 361 28. 250 1. 00 31. 95 3082 OE1 GLU 608 5. 071 52. 618 28. 152 1. 00 33. 50 3083 OE2 GLU 608 6.989 52.867 29.164 1.00 33. 88 3084 C GLU 608 7. 353 48. 582 26. 276 1. 00 15. 23 3085 O GLU 608 6. 494 47. 720 26. 410 1. 00 14. 73 3086 N ILE 609 8. 462 48. 548 26. 980 1. 00 13. 83 3087 CA ILE 609 8. 751 47. 433 27. 873 1. 00 13. 45 3088 CB ILE 609 9.865 46.520 27.276 1.00 12. 99 3089 CG1 ILE 609 11. 195 47. 272 27. 157 1. 00 13. 70 3090 CD1 IvE 609 12. 379 46. 437 26. 673 1. 00 13. 53 3091 CG2 ILE 609 9.409 46.093 25.859 1.00 14. 12 3092 C ILE 609 9. 165 47. 807 29. 265 1. 00 12. 83 3093 O ILE 609 9.585 48.912 29.638 1.00 13. 84 3094 N THR 610 9. 125 46. 796 30. 111 1. 00 12. 05 3095 CA THR 610 9. 565 46. 925 31. 501 1. 00 12. 88 3096 CB THR 610 8. 402 47. 002 32. 479 1. 00 13. 29 3097 OG1 THR 610 8. 956 47. 153 33. 796 1. 00 16. 84 3098 CG2 THR 610 7. 527 45. 784 32. 429 1. 00 10. 56 3099 C THR 610 10. 530 45. 758 31. 701 1. 00 13. 34 3100 O THR 610 10. 321 44. 714 31. 016 1. 00 12. 93 3101 N LEU 611 11. 523 45. 909 32. 548 1. 00 13. 64 3102 CA LEU 611 12. 533 44. 876 32. 721 1. 00 14. 53 3103 CB LEU 611 13. 907 45. 541 32. 404 1. 00 15. 28 3104 CG LEU 611 13. 959 46. 358 31. 124 1. 00 14. 83 3105 CD1 LEU 611 15. 304 47. 053 30. 986 1. 00 15. 65 3106 CD2 LEU 611 13. 564 45. 606 29. 875 1. 00 14. 88 3107 C LEU 611 12. 622 44. 365 34. 140 1. 00 14. 46 3108 0 LEU 611 13. 591 43. 630 34. 460 1. 00 16. 26 3109 N THR 612 11. 665 44. 668 34. 965 1. 00 13. 88 3110 CA THR 612 11. 621 44. 256 36. 342 1. 00 15. 24 3111 CB THR 612 11. 130 45. 430 37. 246 1. 00 17. 61 3112 OG1 THR 612 9. 909 45. 970 36. 713 1. 00 19. 40 3113 CG2 THR 612 12. 196 46. 522 37. 178 1. 00 18. 56 3114 C THR 612 10. 913 42. 995 36. 690 1. 00 14. 98 3115 0 THR 612 10. 873 42. 684 37. 891 1. 00 15. 57 3116 N HIS 613 10. 322 42. 267 35. 712 1. 00 14. 23 3117 CA HIS 613 9. 644 41. 004 36. 061 1. 00 11. 56 <BR> <BR> 3118 CB HIS 613 9. 066 40. 359 34. 787 1. 00 12. 29 3119 CG HIS 613 8. 094 39. 266 35. 093 1. 00 11. 72 3120 CD2 HIS 613 6. 735 39. 343 35. 257 1. 00 13. 33 3121 ND1 HIS 613 8. 437 37. 992 35. 369 1. 00 11. 75 3122 CE1 HIS 613 7. 383 37. 262 35. 688 1. 00 13. 73 3123 NE2 HIS 613 6. 333 38. 089 35. 648 1. 00 14. 15 3124 C HIS 613 10. 686 40. 072 36. 655 1. 00 10. 97 3125 O HIS 613 11. 835 40. 028 36. 213 1. 00 10. 80 <BR> <BR> 3126 N PRO 614 10. 336 39. 345 37. 694 1. 00 11. 02 3127 CD PRO 614 8. 975 39. 383 38. 317 1. 00 11. 32 3128 CA PRO 614 11. 187 38. 414 38. 365 1. 00 10. 45 3129 CB PRO 614 10. 292 37. 696 39. 376 1. 00 11. 26 3130 CG PRO 614 9. 113 38. 602 39. 528 1. 00 11. 78 3131 C PRO 614 11. 836 37. 448 37. 401 1. 00 9. 19 3132 0 PRO 614 12. 983 37. 119 37. 619 1. 00 9. 16 3133 N VAL 615 11. 130 37. 013 36. 378 1. 00 10. 01 3134 CA VAL 615 11. 737 36. 076 35. 404 1. 00 9. 23 3135 CB VAL 615 10. 656 35. 415 34. 541 1. 00 7.75 3136 CG1 VAL 615 11. 222 34. 562 33. 407 1. 00 7.80 3137 CG2 VAL 615 9. 768 34. 558 35. 426 1. 00 9.04 3138 C VAL 615 12. 824 36. 760 34. 601 1. 00 8.70 3139 0 VAL 615 13. 883 36. 186 34. 336 1. 00 8.20 3140 N THR 616 12. 605 38. 021 34. 212 1. 00 9.64 3141 CA THR 616 13. 597 38. 796 33. 482 1. 00 10.04 3142 CB THR 616 13. 101 40. 214 33. 186 1. 00 9.06 3143 OG1 THR 616 11. 892 40. 070 32. 445 1. 00 8.82 3144 CG2 THR 616 14. 151 40. 954 32. 324 1. 00 9.33 3145 C THR 616 14. 916 38. 871 34. 287 1. 00 11.18 3146 O THR 616 15. 996 38. 588 33. 781 1. 00 10.45 3147 N LYS 617 14. 804 39. 230 35. 548 1. 00 12.50 3148 CA LYS 617 15. 883 39. 370 36. 493 1. 00 12.81 3149 CB LYS 617 15. 286 39. 872 37. 833 1. 00 15.61 3150 CG LYS 617 14. 678 41. 298 37. 542 1. 00 18.86 3151 CD LYS 617 13. 997 41. 813 38. 792 1. 00 22.12 3152 CE LYS 617 14.988 41.940 39.931 1. 00 25.82 3153 NZ LYS 617 14. 383 42. 446 41. 195 1. 00 28.02 3154 C LYS 617 16. 625 38. 072 36. 714 1. 00 12.23 3155 O LYS 617 17. 818 38. 016 36. 770 1. 00 11.67 3156 N TYR 618 15. 831 37. 007 36. 842 1. 00 12.60 3157 CA TYR 618 16. 367 35. 659 37. 018 1. 00 12.04 3158 CB TYR 618 15.195 34.676 37.217 1. 00 12.63 3159 CG TYR 618 15. 755 33. 252 37. 189 1. 00 13.71 3160 CD1 TYR 618 16. 424 32. 752 38. 267 1. 00 13.69 3161 CE1 TYR 618 16. 954 31. 449 38. 222 1. 00 14.25 3162 CZ TYR 618 16. 820 30. 717 37. 042 1. 00 13.01 3163 OH TYR 618 17. 384 29. 478 37. 031 1. 00 13.52 3164 CE2 TYR 618 16. 180'31. 219 35. 950 1. 00 12.41 3165 CD2 TYR 618 15.605 32.486 36.023 1. 00 14.07 3166 C TYR 618 17. 216 35. 287 35. 812 1. 00 11.88 3167 0 TYR 618 18. 345 34. 804 35. 988 1. 00 12.67 3168 N ILE 619 16. 702 35. 566 34. 603 1. 00 10.90 3169 CA ILE 619 17. 439 35. 262 33. 386 1. 00 11.06 3170 CB ILE 619 16.624 35.329 32.105 1. 00 10.54 3171 CG2 ILE 619 17. 447 35. 020 30. 847 1. 00 10.55 3172 CG1 ILE 619 15. 407 34. 343 32. 174 1. 00 8.77 3173 CD1 ILE 619 14. 469 34. 460 31. 047 1. 00 5.30 3174 C ILE 619 18. 709 36. 070 33. 338 1. 00 11.87 3175 O ILE 619 19. 771 35. 585 32. 874 1. 00 11.27 3176 N MET 620 18. 622 37. 341 33. 796 1. 00 12.46 3177 CA MET 620 19. 868 38. 173 33. 811 1. 00 13.27 3178 CB MET 620 19. 467 39. 593 34. 250 1. 00 13.55 3179 CG MET 620 18. 632 40. 289 33. 185 1. 00 15.32 3180 SD MET 620 17. 841 41. 829 33. 765 1. 00 18. 98 3181 CE MET 620 19. 235 42. 712 34. 455 1. 00 19.13 3182 C MET 620 20. 907 37. 558 34. 719 1. 00 12.97 3183 0 MET 620 22. 113 37. 596 34. 425 1. 00 13.65 3184 N THR 621 20. 524 36. 985 35. 828 1. 00 12.92 3185 CA THR 621 21. 383 36. 338 36. 784 1. 00 13.16 3186 CB THR 621 20. 590 35. 827 37. 999 1. 00 13.90 3187 OG1 THR 621'19. 920 36. 949 38. 613 1. 00 17.11 3188 CG2 THR 621 21. 458 35. 280 39. 103 1. 00 16.49 3189 C THR 621 22. 038 35. 118 36. 119 1. 00 13.77 3190 O THR 621 23. 193 34. 820 36. 399 1. 00 14.19 3191 N CYS 622 21. 286 34. 419 35. 284 1. 00 13.74 3192 CA CYS 622 21. 809 33. 236 34. 616 1. 00 13. 37 3193 CB CYS 622 20. 740 32. 388 33. 931 1. 00 14. 33 3194 SG CYS 622 19. 500 31. 655 34. 955 1. 00 14. 84 3195 C CYS 622 22. 891 33. 629 33. 628 1. 00 12. 97 3196 0 CYS 622 23. 940 32. 968 33. 562 1. 00 13. 28 3197 N MET 623 22. 656 34. 698 32. 910 1. 00 12. 20 3198 CA MET 623 23. 636 35. 208 31. 957 1. 00 14. 16 3199 CB MET 623 23. 073 36. 419 31. 189 1. 00 14. 10 3200 CG MET 623 21. 861 35. 983 30. 362 1. 00 14. 92 3201 SD MET 623 21. 290 37. 147 29. 185 1. 00 14. 71 3202 CE MET 623 22. 678 37. 313 28. 036 1. 00 16. 15 3203 C MET 623 24. 962 35. 580 32. 606 1. 00 14. 44 3204 O MET 623 26. 032 35. 323 32. 043 1. 00 13. 99 3205 N SER 624 24. 855 36. 227 33. 771 1. 00 15. 39 3206 CA SER 624 25. 996 36. 655 34. 525 1. 00 16. 27 3207 CB SER 624 25. 572 37. 568 35. 706 1. 00 16. 66 3208 OG SER 624 24.924 38.698 35.058 1.00 19. 94 3209 C SER 624 26. 795 35. 497 35. 099 1. 00 17. 38 3210 O SER 624 28.045 35.541 35.046 1.00 17. 75 3211 N ALA 625 26. 112 34. 501 35. 659 1. 00 16. 94 3212 CA ALA 625 26. 823 33. 394 36. 243 1. 00 17. 06 3213 CB ALA 625 25.955 32.731 37.328 1.00 18. 19 3214 C ALA 625 27. 240 32. 309 35. 272 1. 00 16. 77 3215 0 ALA 625 28. 309 31. 713 35. 520 1. 00 18. 28 3216 N ASP 626 26. 534 32. 104 34. 186 1. 00 15. 25 3217 CA ASP 626 26. 831 30. 993 33. 291 1. 00 14. 65 3218 CB ASP 626 25. 501 30. 237 32. 988 1. 00 13. 40 3219 CG ASP 626 24. 803 29. 778 34. 220 1. 00 13. 04 3220 OD1 ASP 626 25. 429 29. 573 35. 289 1. 00 15. 10 3221 OD2 ASP 626 23. 557 29. 659 34. 164 1. 00 14. 68 3222 C ASP 626 27. 440 31. 322 31. 972 1. 00 14. 54 3223 O ASP 626 27.725 30.393 31.209 1.00 14. 92 3224 N LEU 627 27.574 32.599 31.663 1.00 15. 19 3225 CA LEU 627 28. 164 33. 003 30. 383 1. 00 15. 28 3226 CB LEU 627 27. 158 33. 704 29. 487 1. 00 14. 82 3227 CG LEU 627 25. 865 32. 985 29. 083 1. 00 14. 61 3228 CD1 LEU 627 24.949 33.884 28.269 1.00 14. 54 3229 CD2 LEU 627 26. 170 31. 751 28. 182 1. 00 14. 46 3230 C LEU 627 29. 372 33. 917 30. 758 1. 00 16. 97 3231 O LEU 627 30.334 33.737 29.926 1.00 20. 00 3232 P P04 685 20. 882 4. 398 2. 640 1. 00 18. 76 3233 01 P04 685 22. 394 4. 254 2. 815 1. 00 18. 42 3234 02 P04 685 20. 540 5. 660 1. 822 1. 00 19. 86 3235 O3 PO4 685 20.412 3.205 1.758 1.00 20. 18 3236 04 P04 685 20. 026 4. 319 4. 034 1. 00 19. 32 3237 0 WAT 701 11. 980 13. 310 14. 337 1. 00 9. 00 3238 0 WAT 702 5. 236-3.167 8. 352 0. 80 20.24 3239 O WAT 703 28.871 9.080 11.724 1.00 10. 46 3240 O WAT 704 9.309 37.722 24.229 1.00 8. 73 3241 O WAT 705 9. 857 38. 972 21. 454 1. 00 11. 96 3242 O WAT 706 28.326 12.058 12.026 1.00 14. 81 3243 0 WAT 707 17. 263-2.223 25. 022 1. 00 18.78 3244 O WAT 708 13.211 5.409 10.665 1.00 13. 26 <BR> <BR> 3245 0 WAT 709 14. 344 14. 685 13. 948 1. 00 5. 28 3246 O WAT 710 6. 926 12. 403 14. 522 1. 00 14. 56 3247 O WAT 711 9. 426 4. 963 18. 974 1. 00 14. 28 3248 O WAT 712 11.799 10.995 26.104 1.00 9. 04 3249 O WAT 713 11.111 4.179 29.213 0. 80 19.93 3250 O WAT 714 13. 176 1. 433 23. 323 0. 60 20.21 3251 O WAT 715 15. 724 0. 306 24. 485 1. 00 15.49 3252 O WAT 716 10. 777 3. 171 20. 362 1. 00 18.47 3253 O WAT 717 26.005 18.242 10.095 1. 00 9.88 3254 O WAT 718 20.184 19.405 9.947 1. 00 12.88 3255 O WAT 719 24.361 4.339 26.816 1. 00 8.71 3256 O WAT 720 24. 137-2.772 27. 784 1.00 14.90 3257 O WAT 721 18. 373 42. 407 20. 362 1. 00 13.31 3258 O WAT 722 16.621 40.631 25.386 1. 00 7.95 3259 O WAT 723 26. 712 29. 164 19. 143 1. 00 16.95 3260 O WAT 724 9.622 22.991 21.357 1. 00 8.56 3261 O WAT 725 8. 256 22. 458 19. 023 0. 80 10.68 3262 O WAT 726 6. 120 18. 192 28. 283 1. 00 10.66 3263 O WAT 727 3.464 17.285 27.878 0. 80 21.84 3264 O WAT 728 10. 632 24. 476 34. 754 1. 00 15.19 3265 O WAT 729 2.805 38.618 34.918 1. 00 13.79 3266 O WAT 730-2. 136 26. 055 33. 692 0. 80 15.31 3267 O WAT 731 8. 470 39. 951 19. 565 1. 00 17.93 3268 O WAT 732 10. 334 48. 811 22. 891 1. 00 19.97 3269 O WAT 733 12. 754 47. 703 22. 348 0. 80 18.95 3270 O WAT 734 31. 272-1.749 17. 599 1.00 11.34 3271 O WAT 735 33. 970-7.278 21. 555 1.00 11.59 3272 O WAT 736 32.669 5.817 18.049 1. 00 7.04 3273 O WAT 737 31. 876 3. 672 8. 111 1. 00 16.65 3274 O WAT 738 12. 745 16. 569 11. 599 1. 00 26.23 3275 O WAT 739 8.975 14.768 8.947 1. 00 16.74 3276 O WAT 740 7. 953-9.594 8. 932 1.00 22.73 3277 O WAT 741 5. 112-0.307 16. 438 1.00 16. 95 3278 O WAT 742 27.936 16.963 9.099 1. 00 12.85 3279 O WAT 743 26. 626 20. 256 11. 316 0. 60 13.99 3280 O WAT 744 23.135 10.603 5.078 0. 80 13.92 3281 O WAT 745 22. 625 25. 767 13. 855 1. 00 10.47 3282 O WAT 746 28.921 16.457 19.529 1. 00 11.45 3283 O WAT 747 13.694 20.425 29.324 1. 00 5.30 3284 O WAT 748 16.940 12.363 31.160 0. 80 13.99 3285 O WAT 749 25.321 20.235 35.404 1. 00 16.07 3286 O WAT 750 29. 397 16. 544 27. 075 1. 00 8.97 3287 O WAT 751 28.961 19.163 27.014 1. 00 6.62 3288 O WAT 752 30. 062 22. 427 31. 552 1. 00 13.60 3289 O WAT 753 26.125 18.362 33.482 1. 00 9.55 3290 O WAT 754-5. 224 38. 862 30. 343 1. 00 5.50 3291 O WAT 755 13.835 42.790 19.294 1. 00 12.37 3292 O WAT 756 10.178 42.399 32.842 1. 00 11.55 3293 O WAT 757 28. 087-10.738 19. 733 1.00 16.48 3294 O WAT 758 27. 159-4.173 27. 629 0.60 18.60 3295 O WAT 759 31. 738-4.368 16. 532 1.00 12.32 3296 O WAT 760 31.358 2.412 3.032 0. 60 28.92 3297 O WAT 761 23. 126 15. 032 15. 154 1. 00 7.74 3298 O WAT 762 13.214 19.597 15.649 0. 80 13.46 3299 O WAT 763 17.907 3.337 29.830 1. 00 13.40 3300 O WAT 764 24. 669 0. 319 32. 596 0. 60 32.16 3301 O WAT 765 30. 335 27. 288-13.554 0.60 29.12 3302 O WAT 766 26. 274 31. 863 20. 533 0. 80 24.18 3303 O WAT 767 25.866 37.360 21.468 1. 00 18.79 3304 O WAT 78 16.674 41.228 16.275 0. 60 21.37 3305 O WAT 769 18. 335 14. 558-14.661 1.00 22. 06 3306 0 WAT 770 23. 085 28. 868-15.427 0. 60 30.21 3307 0 WAT 771 27. 506 26. 579 19. 269 0. 80 16. 03 3308 0 WAT 772 7. 233 14. 715 18. 804 0. 60 12. 98 3309 0 WAT 773 14. 947 16. 177 37. 119 0. 60 14. 78 3310 O WAT 774 21.869 16.921 34.663 1.00 12.60 3311 O WAT 775 22.565 19.575 35.363 1.00 12. 68 3312 O WAT 776 24.121 16.424 33.203 1.00 9. 22 3313 0 WAT 777 31. 293 15. 563 19. 732 0. 80 13. 39 3314 O WAT 778 32.403 16.532 14.623 1.00 14. 17 3315 0 WAT 779 32. 277 25. 286 24. 610 0. 80 20. 26 3316 0 WAT 780 30. 912 25. 781 29. 346 1. 00 9. 26 3317 0 WAT 781 27. 681-10.533 15. 841 1. 00 11.51 3318 0 WAT 782 12. 399-3.766 17. 042 0. 80 13.92 3319 O WAT 783 10. 847-6.249 18. 308 0. 80 20.31 3320 O WAT 784 20. 159 16. 871 6. 381 0. 80 15. 53 3321 O WAT 785 18.504 15.667 8.189 0.60 12. 26 3322 O WAT 786 26.643 27.371 29.899 1.00 7. 92 3323 O WAT 787 27.683 24.770 30.305 1.00 8. 65 3324 0 WAT 788 22. 373 25. 714 35. 472 0. 80 16. 99 3325 O WAT 789 0.424 27.546 36.230 0.80 15. 65 3326 O WAT 790 -4.660 26.989 31.521 1.00 11. 72 3327 0 WAT 791 11. 612 25. 322 18. 677 0. 80 18. 04 3328 O WAT 792 3.593 36.770 36.361 1.00 13. 49 3329 0 WAT 793 3. 771 34. 072 36. 294 1. 00 13. 33 3330 O WAT 794 32.895 22.003 24.943 1.00 11. 20 3331 0 WAT 795 31. 430 19. 803 25. 819 1. 00 9. 81 3332 O WAT 796 -4.055 44.411 35.730 1.00 10. 02 <BR> <BR> 3333 O WAT 797 11. 988 48. 437 33. 945 1. 00 13. 67 3334 O WAT 798 14.077 37.298 40.056 0.80 10. 83 3335 O WAT 799 1. 205 5. 648 18. 914 0. 60 19. 90 3336 0 WAT 800 20. 418 34. 762 0. 485 0. 80 18. 83 3337 0 WAT 801 33. 505-5.277 23. 153 0. 80 12.24 3338 0 WAT 802 35. 559-4. 225 25.246 0.60 18. 00 3339 O WAT 803 7.984 13.796 6.323 0.80 18. 47 3340 O WAT 804 6.408 7.888 3.066 0.80 14. 97 3341 O WAT 805 23.327 13.120 4.174 0.80 12.35 3342 0 WAT 806 19. 834 13. 598 5. 047 0. 80 22. 87 3343 O WAT 807 9.382 14. 883-9.425 0. 80 21.21 3344 O WAT 808 4.223 37. 239-5.238 0. 80 24.23 3345 O WAT 809 26.029 33. 159-0.346 0. 60 19.63 3346 0 WAT 810 17. 514 22. 284 36. 741 0. 80 12. 49 3347 O WAT 811-4. 257 25. 631 35. 047 0. 60 13. 40 3348 O WAT 812 4. 934 24. 476 18. 142 0. 80 15. 11 3349 O WAT 813 33.845 15.469 26.863 0.80 12. 92 3350 O WAT 814 8.020 38.273 17.593 0.60 18. 79 3351 O WAT 815 12.702 45.338 17.961 0.60 15. 56 3352 0 WAT 816 14. 697 38. 343 16. 499 0. 60 16. 66 3353 O WAT 817 10.090 50.985 26.750 0.80 13. 23 3354 O WAT 818 16.630 46.462 35.095 0.60 16. 50 3355 0 WAT 819 24. 693 15. 959-5.252 0. 80 12.28 3356 0 WAT 820 31. 645 11. 142 11. 838 1. 00 11. 29 3357 O WAT 821 -7.322 40.648 30.608 1.00 10. 45 3358 0 WAT 822 12. 066 23. 134 20. 132 0. 80 12. 33 3359 O WAT 823 15.786 20.710 36.277 1.00 10. 38 3360 O WAT 824 29.764 8.377 23.834 0.80 17. 50 3361 0 WAT 825 2. 009-8. 014 16. 293 0. 80 24. 14 3362 O WAT 826 17.478 -10.409 20.648 0.60 19. 32 3363 O WAT 827 28. 917-3.956 13. 757 0. 80 11.77 3364 O WAT 828 18.434 9.884 30.291 0.60 11. 95 3365 0 WAT 829 13. 665 35. 140-5.528 0. 60 20.58 3366 O WAT 830 29. 055 0. 226 12. 711 0. 80 18. 84 3367 0 WAT 831 9. 910 20. 459 32. 112 0. 80 11. 54 3368 0 WAT 832 33. 298 3. 903 14. 341 0. 80 13. 96 3369 0 WAT 833 14. 498 17. 128-20. 512 0.60 31.58 3370 O WAT 834 20.070 8.296 3.735 0.60 15. 86 <BR> <BR> 3371 0 WAT 835 32. 467 17. 597 25. 057 0. 80 13. 65 3372 0 WAT 836 10. 568-8.744 10. 429 0. 80 19.99 3373 0 WAT 837 6. 956 32. 119 14. 844 0. 60 26. 53 3374 0 WAT 838 22. 348 33. 880-2.497 0. 60 16. 72 3375 O WAT 839 6.197 25.979 33.828 1.00 13.30 <BR> <BR> <BR> 3376 0 WAT 840 29. 264 19. 309 20. 837 0. 80 11. 22 3377 0 WAT 841 21. 033 15. 745 36. 947 0. 80 13. 67 3378 0 WAT 842-0. 443 22. 558 27. 723 0. 80 13. 91 3379 0 WAT 843 22. 277 8. 595 2. 919 0. 60 13. 92 3380 O WAT 844 31.886 21.637 22.391 0.80 13. 06 3381 O WAT 845 23. 734 39. 613 32. 897 0. 60 14. 87 3382 O WAT 846 20.391 6.527 5.473 0.80 17. 90 3383 O WAT 847 10.038 14.910 14.987 0.60 15.70 3384 O WAT 848 1. 752 26. 682-4.299 0. 80 22. 42 3385 0 WAT 849 21. 758 18. 980 7. 667 0. 80 16. 45 3386 O WAT 850 0. 340 7. 347 16. 778 0. 80 24. 77 3387 O WAT 851 7. 397 20. 444 31. 018 0. 80 12. 80 3388 O WAT 852 4. 398 29. 301-19.493 0. 60 17. 57 3389 O WAT 853 23.018 4.038 29.558 1.00 12. 56 3390 O WAT 854 20.316 27.491 14.668 0.80 17. 39 3391 O WAT 855 -3.121 10.204 11.879 0.60 17. 19 3392 O WAT 856 1.108 1.933 19.870 0.60 19.02 3393 O WAT 857 21.823 31.513 38.364 0.60 28. 27 3394 0 WAT 858 16. 590 42. 986 18. 781 0. 60 13. 39 3395 0 WAT 859 15. 689 22. 686 15. 158 1. 00 13. 42 3396 O WAT 860 2.911 19.795 28.093 0.60 22. 77 3397 O WAT 861 -6.174 24.267 23.402 0.60 27. 53 3398 O WAT 862 29. 802 13. 001-6.921 0. 60 28.24 3399 0 WAT 863 19. 056 40. 684 37. 618 0. 80 13. 13 3400 O WAT 864 35.507 21.358 24.664 0.60 13. 23 3401 O WAT 865 1.512 38. 026-17.103 0. 60 17.35 3402 O WAT 866-6. 379 34. 955 20. 636 0. 60 18. 66 3403 O WAT 867 15.200 12.033 36.465 0.60 24. 88 3404 O WAT 868 31. 843-1.450 26. 436 0. 80 13.35 3405 O WAT 869 3.848 7.564 22.582 0.60 17. 28 3406 O WAT 870 28. 991 26. 919 16. 901 0. 60 20. 72 3407 O WAT 871 12.452 34.116 16.613 0.60 20. 01 3408 O WAT 872 24.553 35.588 38.471 0.80 15. 53 3409 O WAT 873 10.387 17.954 19.148 0.80 12. 65 3410 O WAT 874 5.440 13.731 23.201 0.60 12. 44 3411 O WAT 875 22. 253 35. 883 1. 904 0. 60 19. 08 3412 O WAT 876 11.787 20.477 12.934 0.60 21. 12 3413 O WAT 877 -0.488 29. 999-19.128 0. 60 17.93 3414 O WAT 878 10.492 15. 167-12.877 0. 60 17.77 3415 O WAT 879 -3.691 45.579 23.581 0.80 16. 32 3416 O WAT 880 27.494 6.986 25.127 0.60 14. 97 3417 O WAT 881 6.301 31.212 38.800 0.60 13. 60 3418 O WAT 882 12.410 21.733 17.900 0.60 18. 83 3419 O WAT 883 -4.943 48.865 24.760 0.60 22. 11 3420 0 WAT 884 15. 646 44. 222 36. 041 0. 60 16. 53 3421 0 WAT 885 31. 045 17. 801-12.984 0. 60 24.68 3422 0 WAT 886 33. 332 14. 920 21. 537 0. 80 18. 43 3423 0 WAT 887 30. 177-12.082 15. 262 0. 60 17.33 3424 0 WAT 888 12. 325 15. 241-14.958 0. 60 21.58 3425 0 WAT 889 18. 271-8.518 24. 230 0. 60 15.44 3426 O WAT 890 15. 206 11. 791 6. 908 0. 80 15. 92 3427 0 WAT 891 12. 112 11. 891 32. 422 0. 60 17. 71 3428 0 WAT 892-0. 190 49. 535 25. 137 0. 60 24. 87 3429 0 WAT 893-0. 359 30. 191 19. 404 0. 80 13. 17 3430 O WAT 894 12.792 38.976 41.476 0.80 12. 75 3431 0 WAT 895-1. 837 46. 567 21. 881 0. 80 16. 65 3432 0 WAT 896 28. 006-7.266 28. 127 0. 60 18.28 3433 0 WAT 897 29. 585-1.337 14. 661 0. 80 15.20 3434 0 WAT 898 6. 233-2.243 18. 563 0. 60 19.59 3435 0 WAT 899 10. 606 36. 292 14. 925 0. 60 18. 52 3436 O WAT 900-11. 561 48. 424 25. 677 0. 60 20. 41 3437 0 WAT 901 24. 250-10.784 9. 367 0. 80 17.35 3438 0 WAT 902 18. 965 14. 796-2.469 0. 60 17.37 3439 O WAT 903 4.499 2.305 6.220 0.80 16. 37 3440 O WAT 904 22.665 45.993 25.414 0.60 18. 85 3441 O WAT 905 12. 122 42. 772 43. 022 0. 60 20. 37 3442 O WAT 906 14.569 48.600 34.917 0.60 13. 98 3443 O WAT 907 6.056 22.311 18.001 0.60 14. 90 3444 0 WAT 908 21. 559-6.351 23. 734 0. 80 17.53 3445 O WAT 909 32.133 8.098 19.094 0.60 9.24 3446 O WAT 910 11.006 32.068 16.815 0.60 21. 19 3447 O WAT 911 11.744 32.986 38.011 0.60 23. 03 3448 O WAT 912 18.661 36.814 0.583 0.60 19. 75 3449 0 WAT 913 2. 049 3. 509 6. 243 0. 80 20. 31 3450 O WAT 914 35.135 23.320 3.571 0.60 24. 82 3451 O WAT 915 -10.851 40.817 25.264 0.60 13. 97 3452 O WAT 916 31. 596-5.165 11. 647 0. 60 21.84 3453 O WAT 917 24.215 27.580 12.489 0.60 16. 89 3454 0 WAT 918 19. 895-9.667 5. 461 0. 60 16.96 3455 0 WAT 919 21. 145 23. 733 12. 894 0. 80 11. 76 3456 O WAT 920 26.745 30.286 -0.429 0.60 16. 45 3457 O WAT 921 18.785 23.578 13.398 0.80 14. 82 3458 O WAT 922 34.617 25.706 2.628 0.80 22. 84 3459 O WAT 923 22.104 21.306 5.772 0.80 17. 81 3460 0 WAT 924 20. 277 37. 557 8. 142 0. 60 16. 44 3461 0 WAT 925 24. 310 19. 788 8. 231 0. 60 12. 33 3462 O WAT 926 -5.064 25.402 19.070 0.60 27. 40 3463 O WAT 927 2.406 25. 726-1.175 0. 60 26.64 3464 O WAT 928 32.051 1.906 25.006 0.60 14. 27 3465 O WAT 929 7.347 2.199 22.382 0.60 15. 27 3466 0 WAT 930-7. 596 45. 948 31. 253 0. 60 19. 23 3467 O WAT 931 14.410 37.525 13.817 0.60 18. 04 3468 O WAT 932 23.751 13.401 1.327 0.60 16. 06 3469 0 WAT 933-2. 788 47. 082 35. 410 0. 60 15. 61 3470 O WAT 934 27. 456-13.369 11. 840 0. 60 20.99 3471 O WAT 935 20.785 43.322 30.959 0.60 12. 18 3472 0 WAT 936 9. 610 20. 160 18. 516 0. 60 12. 00 3473 O WAT 937 2.636 46.661 19.816 0.60 21. 91 3474 O WAT 938 6.440 52.059 21.726 0.60 24. 01 3475 O WAT 939 25.829 12. 025-0.197 0. 60 18.52 3476 O WAT 940 26. 686-1.153 10. 929 0. 60 16.20 3477 0 WAT 941 16. 058-10.673 14. 868 0. 60 10.55 3478 O WAT 942 4.444 9.892 3.675 0.60 13. 47 3479 0 WAT 943 4. 236-0.496 6. 363 0. 60 16.01 3480 O WAT 944 18. 198-5.949 25. 756 0. 60 12.72 3481 0 WAT 945 27. 074 4. 273 27. 836 0. 60 9. 32 3482 0 WAT 946 28. 735 5. 415 26. 456 0. 60 14. 80 3483 0 WAT 947 23. 343-6.260 27. 108 0. 60 16.53 3484 O WAT 948 29.006 15. 698-2.613 0. 60 13.19 3485 0 WAT 949 28. 921 17. 872-10.369 0. 60 22.76 3486 0 WAT 950 23. 345 18. 454-18.472 0. 60 22.49 3487 O WAT 951 30. 161 20. 192-13.513 0. 60 23.20 3488 0 WAT 952 19. 767 20. 076 4. 121 0. 60 19-19 3489 0 WAT 953 21. 911 38. 074 3. 454 0. 60 21. 15 3490 O WAT 954 34.086 14.688 13.634 0.60 13. 01 3491 O WAT 955 17. 407 22. 640 39. 585 0. 60 16. 75 3492 O WAT 956 22.578 28.167 36.141 0.60 15. 99 3493 0 WAT 957 12. 233 24. 976 38. 516 0. 60 19. 51 3494 O WAT 958 6.128 24.921 37.102 0.60 11. 22 3495 O WAT 959 0.063 20.833 26.142 0.60 14. 56 3496 O WAT 960 7.384 35.004 38.639 0.60 13. 35 3497 0 WAT 961-1. 276 46. 080 32. 717 0. 60 11. 98 3498 0 WAT 962-4. 514 46. 751 31. 689 0. 60 19. 04 3499 O WAT 963 1.876 44.666 21.347 0.60 18. 52 3500 O WAT 964 3.012 45.306 16.642 0.60 16. 96 3501 0 WAT 965 18. 507-2.578 0. 265 0. 60 12.83 3502 O WAT 966 2.710 45.967 32.280 0.60 16. 22 3503 O WAT 967 1.557 25.091 37.418 0.60 20. 75 3504 O WAT 968 22.841 24.840 5.191 0.60 10. 39 3505 0 WAT 969 35. 156 19. 446-3.419 0. 60 27.52 3506 0 WAT 970 3. 095 51. 287 26. 995 0. 60 27. 69 3507 0 WAT 971 32. 535 15. 441 17. 472 0. 60 12. 27 3508 O WAT 972 17.394 18.167 10.164 0.60 13. 35 3509 O WAT 973 26. 396-2.561 31. 809 0. 60 26.57 3510 O WAT 974 25.837 0.888 4.220 0.60 19. 32 3511 0 WAT 975 6. 277 12. 168-2.745 0. 60 25.54 3512 0 WAT 976 26. 514 9. 572-0. 722 0. 60 20. 40 3513 O WAT 977 11. 984 5. 547 3. 042 0. 60 16. 91 3514 0 WAT 978 18. 026 26. 620 14. 393 0. 60 18. 74 3515 O WAT 979 9.835 12.734 12.494 0.60 18. 01 3516 O WAT 980-0. 376 39. 540 12. 842 0. 60 21. 61 3517 0 WAT 981 0. 756 32. 942 20. 501 0. 60 16. 27 3518 O WAT 982 15. 618 27. 140 1. 778 0. 60 23. 43 3519 O WAT 983 10.103 23.928 39.565 0.60 20. 19 3520 0 WAT 984 8. 044 17. 727 33. 875 0. 60 29. 13 3521 0 WAT 985 23. 017 39. 568 37. 570 0. 60 22. 57 in another aspect, the present invention provides a Hepatitis C virus helicase molecule or molecular complex that includes at least a first and a second oligonucleotide binding site. In one embodiment, the distance between the first and the second oligonucleotide binding sites is less than about 21 angstroms. In another embodiment, the distance between the first and the second oligonucleotide binding sites is about 18.8 to about 19.5 angstroms.

In another aspect, the present invention provides a molecule or molecular complex that is structurally homologous to a Hepatitis C virus helicase molecule or molecular complex, wherein the Hepatitis C virus helicase molecule or molecular complex is represented by at least a portion of the structure coordinates listed in Tables 1,2, or 3.

In another aspect, the present invention provides a scalable three-dimensional configuration of points, at least a portion of said points derived from structure coordinates of at least a portion of a Hepatitis C virus helicase molecule or molecular complex as listed in Tables 1,2, or 3 and including at least one of a Hepatitis C virus helicase or Hepatitis C virus helicase-like domain 1/domain 2 interface, domain 1 oligonucleotide binding site, or domain 2 oligonucleotide binding site. Preferably, substantially all of the points are derived from structure coordinates of a Hepatitis C virus helicase molecule or molecular complex as listed in Tables 1,2, or 3. Preferably, at least a portion of the points derived from the Hepatitis C virus helicase structure coordinates are derived from structure coordinates representing the locations of at least the backbone atoms of amino acids selected from the group consisting of (1) domain 1/domain 2 interface amino acids 205-209,232-238,415-420 and 460-467, (2) domain 1 oligonucleotide binding site amino acids 230-232,255,269, and 270-272, and (3) domain 2 oligonucleotide binding site amino acids 391-393,411-413,415,416 and 460; as represented by structure coordinates of UHCV-A, UHCV-B, or UHHO in Tables 1, 2, and 3 respectively. The scalable three- dimensional configuration of points may optionally be displayed as a holographic image, a stereodiagram, a model or a computer-displayed image.

In another aspect, the present invention provides a scalable three-dimensional configuration of points, at least a portion of the points derived from structure coordinates of at least a portion of a molecule or a molecular complex that is structurally homologous to a Hepatitis C virus helicase molecule or molecular complex and includes at least one of a Hepatitis C virus helicase or Hepatitis C virus helicase-like domain 1/domain 2 interface, domain 1 oligonucleotide binding site, or domain 2 oligonucleotide binding site.

In another aspect, the present invention provides a machine-readable data storage medium including a data storage material encoded with machine readable data which, when using a machine programmed with instructions for using said data, is capable of displaying a graphical three-dimensional representation of at least one molecule or molecular complex selected from the group consisting of (i) a molecule or molecular complex including at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicase-like domain 1/domain 2 interface, wherein the domain 1/domain 2 interface includes amino acids 205-209, 232-238,415-420 and 460-467, the domain 1/domain 2 interface being defined by a set of points having a root mean square deviation of less than about 1.5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCV-A, UHCV-B, or UHHO as listed in Tables 1,2, or 3 respectively; (ii) a molecule or molecular complex including at least a portion of a Hepatitis C virus helicase or Hepatitis C virus helicase-like oligonucleotide binding site, wherein the oligonucleotide binding site includes amino acids selected from the group consisting of (1) domain 1 oligonucleotide binding site amino acids 230-232, 255, 269, and 270-272, and (2) domain 2 oligonucleotide binding site amino acids 391- 393,411-413,415,416 and 460; the oligonucleotide binding site being defined by a set of points having a root mean square deviation of less than about 1.5A from points representing the backbone atoms of said amino acids as represented by the structure coordinates of UHCV-A, UHCV-B, or UHHO as listed in Tables 1,2, or 3 respectively ; (iii) a Hepatitis C virus helicase molecule or molecular complex including at least a first and a second oligonucleotide binding site, wherein the distance between the first and the second oligonucleotide binding sites is less than about 21 angstroms ; and (iv) a molecule or molecular complex that is structurally homologous to a Hepatitis C virus helicase molecule or molecular complex, wherein the Hepatitis C virus helicase molecule or molecular complex is represented by at least a portion of the structure coordinates listed in Tables 1,2, or 3.

In another aspect, the present invention provides a machine-readable data storage medium including a data storage material encoded with a first set of machine readable data which, when combined with a second set of machine readable data, using a machine programmed with instructions for using said first set of data and said second set of data, can determine at least a portion of the structure coordinates corresponding to the second set of machine readable data, wherein said first set of data includes a Fourier transform of at least a portion of the structure coordinates for Hepatitis C virus helicase listed in Tables 1,2, or 3; and said second set of data includes an x-ray diffraction pattern of a molecule or molecular complex of unknown structure.

In another aspect, the present invention provides a method for obtaining structural information about a molecule or a molecular complex of unknown structure. The method includes crystallizing the molecule or molecular complex; generating an x-ray diffraction pattern from the crystallized molecule or molecular complex; and applying at least a portion of the structure coordinates set forth in Tables 1, 2, or 3 to the x-ray diffraction pattern to generate a three-dimensional electron density map of at least a portion of the molecule or molecular complex whose structure is unknown.

In another aspect, the present invention provides a method for homology modeling a Hepatitis C virus helicase homolog. The method includes aligning the amino acid sequence of a Hepatitis C virus helicase homolog with an amino acid sequence of Hepatitis C virus helicase (SEQ ID NO: 1) and incorporating the sequence of the Hepatitis C virus helicase homolog into a model of Hepatitis C virus helicase derived from structure coordinates set forth in Tables 1,2, or 3 to yield a preliminary model of the Hepatitis C virus helicase homolog; subjecting the preliminary model to energy minimization to yield an energy minimized model; remodeling regions of the energy minimized model where stereochemistry restraints are violated to yield a final model of the Hepatitis C virus helicase homolog.

In anther aspect, the present invention provides a computer-assisted method for identifying, designing, and making inhibitors of Hepatitis C virus helicase activity.

Preferably the invention provides compositions, more preferably pharmaceutical compositions, including such inhibotors.

In another aspect, the present invention provides a method for crystallizing a Hepatitis C virus helicase molecule or molecular complex including growing a crystal from a precipitant solution including purified Hepatitis C virus helicase, about 3% by weight to about 14% by weight PEG, about 5% by weight to about 15% by weight DMSO, and about 0. 05M to about 0.07M potassium phosphate.

In another aspect, the present invention provides a method for co-crystallizing a Hepatitis C virus helicase molecule and a ligand to yield a molecular complex, including exchanging purified Hepatitis C virus helicase into a solution including HEPES, EDTA, and dithiothreitol ; concentrating the Hepatitis C virus helicase to a concentration of about 12-16mg/mL ; combining concentrated Hepatitis C virus helicase with the ligand in a mixture including about 4% by weight to about 14% by weight PEG and about 5% by weight to about 15% by weight DMSO; and growing a co-crystal by vapor diffusion.

In another aspect, the present invention provides a method for crystallizing a Hepatitis C virus helicase molecule or molecular complex including growing a crystal by vapor diffusion with macro-seeding from a precipitant solution including purified Hepatitis C virus helicase, HEPES, and about 4% by weight to about 14% by weight mono-alkyl ether of PEG.

In another aspect, the present invention provides a method for co-crystallizing a Hepatitis C virus helicase molecule and a ligand to yield a molecular complex, including growing a crystal by vapor diffusion with macro-seeding from a precipitant solution including purified HCV helicase, HEPES, about 4% by weight to about 14% by weight mono-alkyl ether of PEG, and the ligand, wherein the ligand binds to at least one oligonucleotide binding site on the Hepatitis C virus helicase.

In another aspect, the present invention provides crystalline Hepatitis C virus helicase including a tetragonal crystal having unit cell dimensions of a = b = 109 A 3 A ; c=84A2A ; a=p==y= 90° ; and space group P41 ; the unit cell containing two molecules in an asymmetric unit. Preferably, the invention provides a method for solving the structure of such crystals. Preferably, the invention provides methods for incorporating chemical entities in such crystals.

In another aspect, the present invention provides crystalline Hepatitis C virus helicase including an orthorhombic crystal characterized by unit cell dimensions of a = 66 Ai2A ; b = 110 Å ~ 3 Å; c = 64 Å ~ 2 Å ; a=ß=y=90o ; andaspace groupP21212 ; the unit cell containing one molecule in the asymmetric unit. Preferably, the invention provides a method for solving the structure of such crystals. Preferably, the invention provides methods for incorporating chemical entities in such crystals.

Hepatitis C virus helicase crystals having orthorhombic crystal forms have been found to be surprisingly useful for incorporating chemical entities through crystal soaking methods. For example, the aqueous solubility of poorly soluble chemical entities is frequently enhanced by the addition of dimethylsulfoxide (DMSO) to the aqueous solution. The orthorhombic crystals of Hepatitis C virus helicase show unexpected stability upon immersion in such DMSO-containing aqueous solutions, resulting in the potential for increased effectiveness in the incorporation of chemical entities.

Hepatitis C virus helicase crystals having tetragonal crystal forms have also been found to be surprisingly useful for incorporating chemical entities through crystal soaking methods. For example, chemical entities which interact with the domain 1/domain 2 interface or span oligonucleotide binding sites in domain 1 and domain 2 may be incorporated through crystal soaking methods. The use of tetragonal crystals of Hepatitis C virus helicase in such soaking methods may lead to a better understanding of the binding interactions of Hepatitis C virus helicase with chemical entities.

Tables 1,2, and 3 list the atomic structure coordinates for Hepatitis C virus helicase as derived by x-ray diffraction from crystals of UHCV-A, UHCV-B, and UHHO, respectively. Column 1 lists a number for the atom in the structure. Column 2 lists the element whose coordinates are measured. The first letter in the column defines the element. Column 3 lists the type of amino acid. Column 4 lists a number for the amino acid in the structure. Columns 5-7 list the crystallographic coordinates X, Y, and Z respectively. The crystallographic coordinates define the atomic position of the element measured. Column 8 lists an occupancy factor that refers to the fraction of the molecules in which each atom occupies the position specified by the coordinates. A value of"1" indicates that each atom has the same conformation, i. e., the same position, in all molecules of the crystal. Column 9 lists a thermal factor"B"that measures movement of the atom around its atomic center.

ABBREVIATIONS The following abbreviations are used throughout this disclosure: Hepatitis C virus (HCV) Dimethyl sulfoxide (DMSO) Polyethylene glycol (PEG) Polyethylene glycol mono-methyl ether (PEGMME) Dithiothreitol (DTT) Multiple anomalous dispersion (MAD) Root mean square (r. m. s.) Root mean square deviation (r. m. s. d.) The following abbreviations are used for amino acids throughout this disclosure: A = Ala = Alanine T = Thr = Threonine V = Val = Valine C = Cys = Cysteine L = Leu = Leucine Y = Tyr = Tyrosine I = He = Isoleucine N = Asn = Asparagine P = Pro = Proline Q = Gln = Glutamine F = Phe = Phenylalanine D = Asp = Aspartic Acid W = Trp = TryptophanE = Glu = Glutamic Acid M = Met = Methionine K = Lys = Lysine G = Gly = Glycine R = Arg = Arginine S = Ser = Serine H = His = Histidine BRIEF DESCRIPTION OF THE FIGURES Figure 1 is a schematic of the hepatitis C virus polyprotein organization; the C- terminal two-thirds of NS3 contains RNA helicaselNTPase activity.

Figure 2 depicts the amino acid sequence of the HCV-1 genotype 1 a construct used in this work ; sequence motifs conserved (Gorbalenya et al., Current Opin. in Struct.

Biol., 3: 419-29 (1993)) in helicase are highlighted ; secondary structure assignments are shown across the top, with alpha helices identified by solid bars and beta strands by hatched bars.

Figure 3 is a ribbon drawing depicting the three-domain structure of the HCV helicase ; the NTP-binding site is located on the surface of domain 1 that is closest to domain 2.

Figure 4 shows a comparison of all the available crystal structures of HCV helicase with common domains 1 and 3 superimposed ; different crystal structures show variability in the position of domain 2.

Figure 5 shows a comparison of the positions of domain 2 for UHCV-A and the prior art structure 80HM, which represent extremes of motion in domain 2 of available structures; common domains 1 and 3 have been overlaid. The motion of domain 2 can be envisioned as rotation about a hinge axis (solid black line). In view (a), the hinge axis (solid black line) is oriented vertically in the plane of the paper (similar to the orientation of Figure 3); in view (b), the hinge axis (solid black line) is roughly perpendicular to the plane of the paper; in both (a) and (b), the V-shaped pair of vectors (solid black lines) illustrates the range of motion of centers of mass of the rotating domain (domain 2).

Figure 6 shows a comparison of the conformation of the conserved NTP-binding loop (Walker motif A; residues 205-213 ; PTGSGKSTK; SEQ ID NO : 2) in the orthorhombic crystal form UHHO (a) and the tetragonal crystal form molecule A, UHCV- A (b); a single inorganic phosphate is bound at this site in UHHO.

DETAILED DESCRIPTION OF THE INVENTION CRYSTALLINE FORMS OF HCVHELICASE AND METHOD OF MAKING Applicants have produced crystals comprising HCV helicase which are suitable for X-ray crystallographic analysis. Thus, one embodiment of the invention provides a tetragonal crystal form of an HCV helicase characterized by unit cell dimensions of a = b =109 A i 3 A ; c = 84 A i 2 A, a = p = y = 90° and space group P41, with two molecules in the asymmetric unit. Another embodiment of the invention provides an orthorhombic crystal form of an HCV helicase contains characterized by unit cell dimensions of a = <BR> <BR> <BR> 66 ; b=llOAi3A ; c=64Ai2A, a=, B=Y=90°andspacegroupP2l2l2 with only one molecule in the asymmetric unit.

Accordingly, one aspect of the invention provides a Hepatitis C virus helicase or Hepatitis C virus helicase/ligand crystal. Native Hepatitis C virus helicase crystals may be prepared by methods described herein. In one embodiment, Hepatitis C virus helicase crystals may be grown from a precipitant solution including purified Hepatitis C virus helicase, about 3% by weight to about 14% by weight PEG, about 5% by weight to about 15% by weight DMSO, and about 0. 05M to about 0.07M potassium phosphate.

Preferably the DMSO concentration is about 7% by weight to about 12% by weight and PEG has a molecular weight of about 2,000 to 20,000 daltons. In another embodiment, Hepatitis C virus helicase crystals may be grown by vapor diffusion with macro-seeding from a precipitant solution comprising purified Hepatitis C virus helicase, HEPES, and about 4% by weight to about 14% by weight mono-alkyl ether of PEG. Preferably the mono-alkyl ether of PEG is a mono-methyl ether of PEG. Preferably the PEG has a molecular weight of about 2,000 to 20,000 daltons.

In addition, Hepatitis C virus helicase/ligand crystals may be prepared by methods including soaking existing native crystals in a solution containing the ligand, or by growing crystals under conditions similar to the crystallization conditions for the native crystals but in the presence of chemical entities. Variation in buffer and buffer pH as well as other additives such as PEG is apparent to those skilled in the art and may result in similar crystals.

X-RAY CRYSTALLOGRAPHIC ANALYSIS Using high resolution X-ray crystallography, the three-dimensional structures of two unique crystal forms of the HCV helicase (genotype-1, strain 1A) have been solved.

These new crystal forms are identified herein as UHCV and UHHO. The constituent amino acids of both UHCV and UHHO are defined by a set of structure coordinates as set forth in Tables 1,2, and 3. The term"structure coordinates"refers to Cartesian coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of x-rays by the atoms (scattering centers) of an HCV helicase in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are then used to establish the positions of the individual atoms of the HCV helicase protein or protein/ligand complex.

It will be understood by one of skill in the art that slight variations in structure coordinates can be generated by mathematically manipulating the HCV helicase structure coordinates. For example, the structure coordinates set forth in Tables 1,2, and 3 could be manipulated by crystallographic permutations of the structure coordinates, fractionalization of the structure coordinates, integer additions or subtractions to sets of the structure coordinates, inversion of the structure coordinates or any combination of the above. Alternatively, modifications in the crystal structure due to mutations, additions, substitutions, and/or deletions of amino acids, or other changes in any of the components that make up the crystal, could also yield variations in structure coordinates. Such slight variations in the individual coordinates will have little effect on overall shape. If such variations are within an acceptable standard error as compared to the original coordinates, the resulting three-dimensional shape is considered to be"structurally equivalent." Structural equivalence is described in more detail below.

It should be noted that slight variations in individual structure coordinates of the HCV helicase, as defined above, would not be expected to significantly alter the nature of the chemical entities that could associate with the binding sites. Thus, for example, a ligand that bound to an oligonucleotide binding site of HCV helicase would also be expected to bind to another binding site whose structure coordinates define a shape that falls within the acceptable error.

Both crystal forms of HCV helicase (UHCV and UHHO) arise from crystallization trials with a helicase fragment consisting of NS3 residues 166-631 as defined in Figure 2, (polyprotein residues 1192-1657) (Jin et al., Arch. Biochem. Biophys., 323: 47-53 (1995)) including a C-terminal SH6-tag to facilitate purification from a recombinant system. A tetragonal crystal form and an orthorhombic crystal form were characterized at high resolution. The tetragonal form, characterized by unit cell a = b = 109 A, c = 84 A and space group P41, has two molecules in the asymmetric unit. This structure has been solved by molecular replacement and refined at 2.0 A resolution (R=0.228). The orthorhombic form, with intermolecular interactions unrelated to the tetragonal form, is orthorhombic, space group P21212 (a = 66 A, b = 110 A, c = 64 A), with only one molecule in the asymmetric unit. This structure has been refined against 1.8 A data (R=0. 206). Both structures confirm the overall structural topology previously described by others. Secondary structure assignments are summarized in Figure 2. The enzyme has a structure composed of three domains, each of roughly 140 amino acids (Figure 3).

Domains 1 and 2 share a similar alpha-beta fold with a centralized parallel beta sheet surrounded by helices. Domain 3 adopts a different alpha-helical fold.

The two crystal structure determinations result in three crystallographically independent observations of the helicase enzyme structure (two from the tetragonal form crystals and one from the orthorhombic form). These structures, identified herein as UHCV-A, UHCV-B (tetragonal form molecules A and B) and UHHO (orthorhombic form), can be compared to helicase structures available from analysis of other crystal forms 1HEI-A, 1HEI-B, lAlV and 80HM (See Table 6 in Example in for identification and references). These structures have been superimposed in a variety of different ways, and the r. m. s. differences in structure are summarized in Table 6. Differences in all Ca positions after superposition are 0.89 A (UHCV-A vs. UHCV-B), and 1.52 A (UHCV-A vs. UHHO). The overall structures of individual domains (e. g., domain 3 vs. domain 3, or domain 2 vs. domain 2) are closely conserved in all the crystal forms.

There is an extensive and rigid interface between domains 1 and 3 formed by hydrophobic complementarity of domain 1 helix a4 with domain 3 helices a5 and a6 ; these two domains have the same fixed relationship to each other in all reported crystal structures. (Compare r. m. s. differences in position of Table 6 based on superimpositions with combined dl/d3 to those of dl or d3 individually). In contrast, domain 2 is only loosely associated with domain 1, and the interface to domain 3 is limited to contacts on the extreme end of a long beta hairpin that extends downward to lie against the back of domain 3 (Figure 3). Significant variation in the position of domain 2 has been reported with respect to the fixed domains 1 and 3, and this has been likened to rotation of the domain about a centrally located hinge (Cho et al., J Biol. Chem., 273: 15045-52 (1998)).

This rotation is readily apparent when all domains 1 and 3 are superimposed (Figure 4).

The most striking difference in enzyme structure observed upon comparison of these new crystal forms with known crystal forms is the position of domain 2 with respect to domain 1 about the centrally located hinge. Without intending to be bound by theory or mechanism, it is believed that the in-and-out movement of domain 2 relative to fixed domains 1 and 3 may play a role in deforming and translocating oligonucleotide substrates during catalysis. Conserved sequence motifs in domain 1 define the site of NTP binding and hydrolysis near the dl/d2 interface, so reaction with the NTP co-factor may be necessary to facilitate this conformational change.

The rotation of domain 2 around the centrally located hinge was quantitated for five known helicase crystal forms using the analytical method of Wriggers & Schulten (Proteins : Structure, Function, and Genetics, 29: 1-14 (1997)) (Table 7). Motion of domain 2 can be described as rotation around a vertical hinge axis near residue 484. Data for UHCV-B is not shown since, by this analysis, the angle of rotation differentiating UHCV-A and UHCV-B is small (2.8°). A similar rotation angle was noted by Yao et al.

(Nat. Struct. Biol., 4: 463-77 (1997)) in their comparison of the two molecules in their crystal form (1HEI-A vs 1HEI-B) ; these trivial comparisons have been omitted from the tabulation. The tetragonal crystal form UHCV-A serves as a convenient reference state, because it represents the most closed state of the hinge. 80HM, with domain 2 rotated 32.3°, represents the opposite extreme (Figure 5). Models 1HEI and lAlV are similar to each other, and represent intermediate hinge states of 14.2° and 9.5° rotations from UHCV-A, respectively. Together, these structures appear to define a continuum of domain rotations about the same vertical hinge axis. As a consequence of these movements, the distance between the oligonucleotide binding sites changes (Table 7).

The hinge motion impacts the enzyme structure at two important catalytic sites, the NTP-binding site and the oligonucleotide-binding sites. The NTP-binding site, identified by the conserved tri-phosphate binding Motif I (Walker Motif"A" ; Walker et al., EMBO J., 1: 945-51 (1982)) lies on the surface of domain 1 facing the broad gap between domains 1 and 2. While the gap between domains is not closed in any of the available crystal forms (it is smallest in UHCV-A), one can imagine an extreme hinge conformation, perhaps induced by binding or hydrolysis of ATP in domain 1, that brings domain 2 into direct contact with domain 1. Conserved sequence motif VI (residues Q46oRxGRxGR467 where x represents unconserved amino acids within the motif ; SEQ ID NO : 3) on domain 2 has been suggested as an important mediator of this allosteric effect (Kim et al., Structure, 6: 89-100 (1998)).

Based on the structural analysis of a helicase/single-stranded DNA co-crystal, Kim et al. (Structure, 6: 89-100 (1998)) have identified oligonucleotide binding sites on both domains 1 and 2. The distance between these two sites (defined by residues G255 and T269 in dl, and R393 and Tam in d2), changes by as much as 8 A when domain 2 swings from one extreme state (e. g., UHCV-A) to the other (80HM). A single oligonucleotide held at both sites must either undergo a large conformational change or dissociate (and re- associate) at one end or the other as the enzyme undergoes a hinge-state change. Either action might be utilized effectively during processive substrate strand separation.

Because the hinge domain (domain 2) of the helicase is further toward a closed position in the tetragonal form structures UHCV-A and UHCV-B than in any other crystal structure reported to date, this crystal form is particularly well-suited for the characterization of inhibitors that span the two oligonucleotide-binding sites of the enzyme, or compounds that interfere with allosteric motions of domain 2 by binding across the dl/d2 interface. It may be less well suited for studying inhibitors that bind at the NTP-binding site, as access to this site is blocked in one of the two molecules in the asymmetric unit by intermolecular contacts introduced from crystal symmetry.

The orthorhombic form of UHHO represents a conformational intermediate that is not easily modeled as a hinge, but appears as a conformation intermediate between the extreme positions of domain 2. The fact that the orthorhombic crystal form UHHO has an accessible NTP-binding site occupied by inorganic phosphate in the native crystal form suggests that it may be uniquely suited for the study of inhibitors or co-factors that bind at the NTP-binding site. This crystal form is also desirable in the study of cofactors becasue it grows from solutions that contain significant quantities of DMSO, which is often required to bring marginally soluble chemical entities into solution with HCV helicase.

Beyond the domain 2 position, notable structural differences in the HCV helicase crystal forms are isolated in only a few areas. The NTP-binding loop (conserved Motif I ; residues 205-214) appears to be quite flexible, and the exact conformation of this loop varies from structure to structure. The presence or absence of bound cation co-factor (Mg+2), or counter-anion (So4~2 or po4~2) affects the geometry, as does the crystal environment. The structure of this loop in the orthorhombic form UHHO may be most representative of the active enzyme. In this structure, each of the four oxygen atoms of the phosphate ion is bound and held through hydrogen bonds to backbone amides of G207, G209 and K210, Oy of S211 and Nz of K210 (Figure 6a). This inorganic phosphate occupies a position taken by the beta-phosphate of nucleoside tri-phosphates in other NTP-binding enzymes that share this sequence motif (Pai et al., EMBO J., 9: 2351 (1990); Tari et al., Nat. Struct. Biol., 3: 355 (1996)). In contrast to molecule A of the tetragonal form (UHCV-A), this loop adopts a different geometry (Figure 6b), in which the loop is collapsed on itself, making only intramolecular H-bonds. This presumably inactive conformation is apparently stabilized through contacts with a crystallographically related molecule. In UHCV-B, the loop adopts a geometry more similar to the consensus geometry represented by UHHO.

CONFORMATIONAL STATES AND BINDING SITES Applicants'invention has provided, for the first time, information about extent of the relative motion of domain 2 relative to domain 1 in HCV helicase. In particular, the identification of a substantially"closed"conformation, represented by the UHCV structure, that affects access to the NTP binding site on domain 1 and alters the relative locations of the oligonucleotide binding sites on domains 1 and 2 has far reaching ramifications for drug discovery and design.

It is well known that structural information about protein binding sites is of significant utility in fields such as drug discovery. The association of natural ligands, substrates, cofactors and the like with binding sites on enzymes or receptors is the basis of many biological mechanisms of action. Similarly, many drugs exert their biological effects through association with the binding sites of receptors and enzymes. Such associations may occur with all or any parts of the binding site. An understanding of such associations helps lead to the design of drugs having more favorable associations with their target, and thus improved biological effects. Therefore, this information is valuable in designing potential inhibitors of HCV helicase-like binding sites, as discussed in more detail below.

The term"binding site"as used herein refers to a region of a molecule or molecular complex, that, as a result of its shape, favorably associates with another chemical entity. A"chemical entity,"as that term is used herein, includes chemical compounds, complexes of two or more chemical compounds, and fragments of such compounds or complexes. Chemical entities that are determined to associate with HCV helicase are potential drug candidates. The term"HCV helicase-like binding site"refers to a portion of a molecule or molecular complex whose shape is sufficiently similar to at least a portion of a binding site of HCV helicase as to be expected to bind related ligands.

The term"associating with"refers to a condition of proximity between a chemical entity, or portions thereof, and an HCV helicase molecule or portions thereof. The association may be non-covalent, wherein the juxtaposition is energetically favored by hydrogen bonding, van der Waals forces, or electrostatic interactions, or it may be covalent.

In the present invention, four different binding sites for HCV helicase are identified. First, an NTP binding site is present on the surface of domain 1 of HCV helicase. As noted above, the NTP-binding site is identified by the conserved tri- phosphate binding Motif I (Walker Motif"A" ; Walker et al., EMBO J., 1: 945-51 (1982)) that lies on the surface of domain 1 facing the broad gap between domains 1 and 2. HCV helicase also includes two oligonucleotide binding sites, one on domain 1 and the other on domain 2. The two oligonucleotide sites can also be defined in relation to each other.

The distance (defined as the distance between the side chain oxygen of T269 and the side chain oxygen of T4n) between these sites (defined by residues G255 and T269 in domain 1, and R393 and T411 in domain 2) changes by as much as 8 A when domain 2 swings from one extreme state (e. g., UHCV-A) to the other (80HM). The distance between the two oligonucleotide binding sites preferably is less than about 21 angstroms and more preferably is about 18.8 to about 19.5 angstroms.

HCV helicase also possesses an allosteric binding site at the interface between domains 1 and 2. Conserved sequence motif VI (residues Q46oRxGRxGR467 where x represents unconserved amino acids within the motif; SEQ ID NO : 3) on domain 2 has been suggested as an important mediator of this allosteric effect (Kim et al., Structure, 6: 89-100 (1998)).

In one aspect, the binding sites of HCV helicase include the set of structure coordinates of all atoms in their respective constituent amino acids; in another aspect, the binding sites include the set of structure coordinates of just the backbone atoms of their respective constituent atoms. It will be readily apparent to those of skill in the art that the numbering of amino acids in other isoforms of HCV helicase may be different than that of other HCV helicase isoforms.

THREE-DIMENSIONALCONFIGURATIONS The structure coordinates listed in Tables 1,2, or 3 for the tetragonal and orthorhombic crystal forms of HCV helicase, or for a domain thereof or a portion of a domain, such as for one of the binding sites of HCV helicase, define a unique, scalable configuration of points in space. Those of skill in the art understand that a set of structure coordinates for protein or an protein/ligand complex, or a portion thereof, defines a relative set of spatially distributed points that, in turn, defines a configuration in three dimensions. A similar or identical configuration can be defined by an entirely different set of coordinates, provided the distances and angles between the points defined by the coordinates remain essentially the same. It will be further understood that this three dimensional configuration is scalable ; that is, smaller and larger configurations are uniquely defined by the relative distances between and among the points, and the angles defined by any three points.

The present invention thus includes a scalable three-dimensional configuration of points defined by the structure coordinates of at least a portion of an HCV helicase molecule, as shown in Tables 1,2, or 3, as well as structurally equivalent configurations, as described below. A"scalable three-dimensional configuration"that is defined by a set of structure coordinates includes not just the particular configuration defined by the set of structure coordinates but also those scaled configurations defined by the relative distances between and among the points defined by the structure coordinates, and the angles defined by any three points. It will be understood that slight variations in the positions of one or more points will not substantially alter the three-dimensional configuration defined by a set of structure coordinates, and configurations including such slight variations are included in this embodiment of the invention. Such a slight variation in position is preferably less than about 1.5A, more preferably less than about 1. OA, between the point with the varied position and the point nearest to it.

Preferably, the three-dimensional configuration includes points defined by structure coordinates representing the locations of a plurality of the amino acids defining an HCV helicase binding site. More preferably, the three dimensional configuration includes points defined by structure coordinates representing locations of a plurality of amino acids defining domain 2 of HCV helicase and, optionally, at least a portion of domain 1. In one aspect, the three-dimensional configuration includes points defined by structure coordinates representing the locations of just the backbone atoms of the plurality of amino acids. Preferably, the backbone atoms include the backbone atoms of amino acids selected from the group consisting of (1) domain 1/domain 2 interface amino acids 205-209,232-238,415-420 and 460-467, (2) domain 1 oligonucleotide binding site amino acids 230-232,255,269, and 270-272, and (3) domain 2 oligonucleotide binding site amino acids 391-393,411-413,415,416 and 460; in another aspect, the three-dimensional configuration includes points defined by structure coordinates representing the locations of the side chain and the backbone atoms (other than hydrogens) of the plurality of amino acids. Preferably, the side chain and backbone atoms include the side chain and backbone atoms amino acids selected from the group consisting of (1) domain 1/domain 2 interface amino acids 205-209,232-238,415-420 and 460-467, (2) domain 1 oligonucleotide binding site amino acids 230-232,255,269, and 270-272, and (3) domain 2 oligonucleotide binding site amino acids 391-393,411-413,415,416 and 460. In yet another aspect, the three-dimensional configuration includes points defined by structure coordinates representing the locations the backbone atoms of at least 30 amino acids that are contiguous in the amino acid sequence of HCV helicase (SEQ ID NO : 1). In still another aspect, the three-dimensional configuration includes points defined by structure coordinates representing the locations the side chain atoms and the backbone atoms of at least 30 amino acids that are contiguous in the amino acid sequence of HCV helicase (SEQ ID NO : 1).

Likewise, the invention also includes a three-dimensional configuration of points defined by structure coordinates of molecules or molecular complexes that are structurally homologous to HCV helicase, as well as structurally equivalent configurations.

Structurally homologous molecules or molecular complexes are defined below.

Advantageously, structurally homologous molecules can be identified using the structure coordinates of HCV helicase (Tables 1,2, and 3) according to a method of the invention.

The configurations of points in space defined by structure coordinates according to the invention can be visualized as, for example, a holographic image, a stereodiagram, a model or a computer-displayed image, and the invention thus includes such images, diagrams or models.

STRUCTURAL EQUI-VALENCE "Structural equivalence,"as the term is used herein, describes a relationship between the three-dimensional structures of two molecules or portions thereof, e. g., two crystal structures. Various computational analyses can be used to determine whether a molecule or portion thereof is"structurally equivalent"to all or part of an HCV helicase such as UHCV-A, UHCV-B, or UHHO represented by the structure coordinates in Tables 1,2, or 3. Such analyses may be carried out in current software applications, such as the Molecular Similarity application of QUANTA (Molecular Simulations Inc., San Diego, CA) version 4.1, and as described in the accompanying User's Guide.

The Molecular Similarity application permits comparisons between different structures, different conformations of the same structure, and different parts of the same structure. The procedure used in Molecular Similarity to compare structures is divided into four steps: (1) load the structures to be compared ; (2) define the atom equivalences in these structures ; (3) perform a fitting operation ; and (4) analyze the results.

Each structure is identified by a name. One structure is identified as the target (i. e., the fixed structure) ; all remaining structures are working structures (i. e., moving structures). Since atom equivalency within QUANTA is defined by user input, for the purpose of this invention equivalent atoms are defined as protein backbone atoms (N, Ca, C, and O) for all conserved residues between the two structures being compared. A conserved residue is defined as a residue that is structurally or functionally equivalent.

Only rigid fitting operations are considered.

When a rigid fitting method is used, the working structure is translated and rotated to obtain an optimum fit with the target structure. The fitting operation uses an algorithm that computes the optimum translation and rotation to be applied to the moving structure, such that the root mean square difference of the fit over the specified pairs of equivalent atom is an absolute minimum. This number, given in angstroms, is reported by QUANTA.

For the purpose of this invention, any molecule or molecular complex or binding site thereof, or any portion thereof, that has a root mean square deviation of conserved residue backbone atoms (N, Ca, C, O) of less than 1.5A, when superimposed on the relevant backbone atoms described by the reference structure coordinates listed in Tables 1,2, or 3, is considered"structurally equivalent"to the reference molecule. That is to say, the crystal structures of those portions of the two molecules are substantially identical, within acceptable error. Particularly preferred structurally equivalent molecules or molecular complexes are those that are defined by the entire set of structure coordinates in Tables 1,2, or 3,"a root mean square deviation from the conserved backbone atoms of those amino acids of not more than 1.5A. More preferably, the root mean square deviation is less than about 1. 0A.

The term"root mean square deviation"means the square root of the arithmetic mean of the squares of the deviations. It is a way to express the deviation or variation from a trend or object. For purposes of this invention, the"root mean square deviation" defines the variation in the backbone of a protein from the backbone of HCV helicase or a binding site portion thereof, as defined by the structure coordinates of HCV helicase described herein.

MACHINE READABLE STORAGE MEDIA Transformation of the structure coordinates for all or a portion of Hepatitis C virus helicase or the Hepatitis C virus helicase/ligand complex or one of its binding sites, for structurally homologous molecules as defined below, or for the structural equivalents of any of these molecules or molecular complexes as defined above, into three-dimensional graphical representations of the molecule or complex can be conveniently achieved through the use of commercially-available software.

The invention thus further provides a machine-readable storage medium comprising a data storage material encoded with machine readable data which, when using a machine programmed with instructions for using said data, is capable of displaying a graphical three-dimensional representation of any of the molecule or molecular complexes of this invention that have been described above. In a preferred embodiment, the machine-readable data storage medium comprises a data storage material encoded with machine readable data which, when using a machine programmed with instructions for using said data, is capable of displaying a graphical three- dimensional representation of a molecule or molecular complex comprising all or any parts of a Hepatitis C virus helicase binding site or a Hepatitis C virus helicase-like binding site, as defined above. In another preferred embodiment, the machine-readable data storage medium is capable of displaying a graphical three-dimensional representation of a molecule or molecular complex defined by the structure coordinates of all of the amino acids in Tables 1,2, or 3, i a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 A.

In an alternative embodiment, the machine-readable data storage medium comprises a data storage material encoded with a first set of machine readable data which comprises the Fourier transform of the structure coordinates set forth in Tables 1,2, or 3, and which, when using a machine programmed with instructions for using said data, can be combined with a second set of machine readable data comprising the x-ray diffraction pattern of a molecule or molecular complex to determine at least a portion of the structure coordinates corresponding to the second set of machine readable data.

For example, a system for reading a data storage medium may include a computer comprising a central processing unit ("CPU"), a working memory which may be, e. g., RAM (random access memory) or"core"memory, mass storage memory (such as one or more disk drives or CD-ROM drives), one or more display devices (e. g., cathode-ray tube ("CRT") displays, light emitting diode ("LED") displays, liquid cyrstal displays ("LCDs"), electroluminescent displays, vacuum fluorescent displays, field emission displays ("FEDs"), plasma displays, projection panels, etc.), one or more user input devices (e. g., keyboards, microphones, mice, touch screens, etc.), one or more input lines, and one or more output lines, all of which are interconnected by a conventional bidirectional system bus. The system may be a stand-alone computer, or may be networked (e. g., through local area networks, wide area networks, intrants, extranets, or the internet) to other systems (e. g., computers, hosts, servers, etc.). The system may also include additional computer controlled devices such as consumer electronics and appliances.

Input hardware may be coupled to the computer by input lines and may be implemented in a variety of ways. Machine-readable data of this invention may be inputted via the use of a modem or modems connected by a telephone line or dedicated data line. Alternatively or additionally, the input hardware may comprise CD-ROM drives or disk drives. In conjunction with a display terminal, a keyboard may also be used as an input device.

Output hardware may be coupled to the computer by output lines and may similarly be implemented by conventional devices. By way of example, the output hardware may include a display device for displaying a graphical representation of a binding site of this invention using a program such as QUANTA as described herein.

Output hardware might also include a printer, so that hard copy output may be produced, or a disk drive, to store system output for later use.

In operation, a CPU coordinates the use of the various input and output devices, coordinates data accesses from mass storage devices, accesses to and from working memory, and determines the sequence of data processing steps. A number of programs may be used to process the machine-readable data of this invention. Such programs are discussed in reference to the computational methods of drug discovery as described herein. References to components of the hardware system are included as appropriate throughout the following description of the data storage medium.

Machine-readable storage devices useful in the present invention include, but are not limited to, magnetic devices, electrical devices, optical devices, and combinations thereof. Examples of such data storage devices include, but are not limited to, hard disk devices, CD devices, digital video disk devices, floppy disk devices, removable hard disk devices, magneto-optic disk devices, magnetic tape devices, flash memory devices, bubble memory devices, holographic storage devices, and any other mass storage peripheral device. It should be understood that these storage devices include necessary hardware (e. g., drives, controllers, power supplies, etc.) as well as any necessary media (e. g., disks, flash cards, etc.) to enable the storage of data. <BR> <BR> <BR> <BR> <BR> <BR> <P>STRUCTURALLYHOMOLOGOUSMOLECULES, MOLECULAR COMPLEXES, AND CRYSTALSTRUCTURES The structure coordinates set forth in Tables 1,2, or 3 can be used to aid in obtaining structural information about another crystallized molecule or molecular complex. A"molecular complex"means a protein in covalent or non-covalent association with a chemical entity or compound. The method of the invention allows determination of at least a portion of the three-dimensional structure of molecules or molecular complexes which contain one or more structural features that are similar to structural features of Hepatitis C virus helicase. These molecules are referred to herein as "structurally homologous"to Hepatitis C virus helicase. Similar structural features can include, for example, regions of amino acid identity, conserved active site or binding site motifs, and similarly arranged secondary structural elements (e. g., a helices and p sheets) and the assembly of these elements into domains. Optionally, structural homology is determined by aligning the residues of the two amino acid sequences to optimize the number of identical amino acids along the lengths of their sequences; gaps in either or both sequences are permitted in making the alignment in order to optimize the number of identical amino acids, although the amino acids in each sequence must nonetheless remain in their proper order. Preferably, two amino acid sequences are compared using the Blastp program, version 2.0.9, of the BLAST 2 search algorithm, as described by Tatusova et al., FEMSMicrobiol Lett., 174: 247-50 (1999), and available at http://www. ncbi. nhn. nih. gov/gorf/bl2. html. Preferably, the default values for all BLAST 2 search parameters are used, including matrix = BLOSUM62 ; open gap penalty = 11, extension gap penalty = 1, gap x_dropoff= 50, expect = 10, wordsize = 3, and filter on.

In the comparison of two amino acid sequences using the BLAST search algorithm, structural similarity is referred to as"identity."Preferably, a structurally homologous molecule is a protein that has an amino acid sequence sharing at least 65% identity with the amino acid sequence of Hepatitis C virus helicase (SEQ ID NO: 1). More preferably, a protein that is structurally homologous to Hepatitis C virus helicase includes at least one contiguous stretch of at least 50 amino acids that shares at least 80% amino acid sequence identity with the analogous portion of Hepatitis C virus helicase. Methods for generating structural information about the structurally homologous molecule or molecular complex are well-known and include, for example, molecular replacement techniques.

Therefore, in another embodiment this invention provides a method of utilizing molecular replacement to obtain structural information about a molecule or molecular complex whose structure is unknown comprising the steps of : (a) crystallizing the molecule or molecular complex of unknown structure; (b) generating an x-ray diffraction pattern from said crystallized molecule or molecular complex; and (c) applying at least a portion of the structure coordinates set forth in Tables 1,2, or 3 to the x-ray diffraction pattern to generate a three-dimensional electron density map of the molecule or molecular complex whose structure is unknown.

By using molecular replacement, all or part of the structure coordinates of Hepatitis C virus helicase or the Hepatitis C virus helicase/ligand complex as provided by this invention (and set forth in Tables 1,2, or 3) can be used to determine the structure of a crystallized molecule or molecular complex whose structure is unknown more quickly and efficiently than attempting to determine such information ab initio.

Molecular replacement provides an accurate estimation of the phases for an unknown structure. Phases are a factor in equations used to solve crystal structures that cannot be determined directly. Obtaining accurate values for the phases, by methods other than molecular replacement, is a time-consuming process that involves iterative cycles of approximations and refinements and greatly hinders the solution of crystal structures. However, when the crystal structure of a protein containing at least a structurally homologous portion has been solved, the phases from the known structure provide a satisfactory estimate of the phases for the unknown structure.

Thus, this method involves generating a preliminary model of a molecule or molecular complex whose structure coordinates are unknown, by orienting and positioning the relevant portion of Hepatitis C virus helicase or the Hepatitis C virus helicase/ligand complex according to Tables 1,2, or 3 within the unit cell of the crystal of the unknown molecule or molecular complex so as best to account for the observed x-ray diffraction pattern of the crystal of the molecule or molecular complex whose structure is unknown. Phases can then be calculated from this model and combined with the observed x-ray diffraction pattern amplitudes to generate an electron density map of the structure whose coordinates are unknown. This, in turn, can be subjected to any well- known model building and structure refinement techniques to provide a final, accurate structure of the unknown crystallized molecule or molecular complex (E. Lattman,"Use of the Rotation and Translation Functions,"in Meth. Enzymol., 115: 55-77 (1985); M. G.

Rossman, ed.,"The Molecular Replacement Method,"Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York (1972)).

Structural information about a portion of any crystallized molecule or molecular complex that is sufficiently structurally homologous to a portion of Hepatitis C virus helicase can be resolved by this method. In addition to a molecule that shares one or more structural features with Hepatitis C virus helicase as described above, a molecule that has similar bioactivity, such as the same catalytic activity, substrate specificity or ligand binding activity as Hepatitis C virus helicase, may also be sufficiently structurally homologous to Hepatitis C virus helicase to permit use of the structure coordinates of Hepatitis C virus helicase to solve its crystal structure.

In a preferred embodiment, the method of molecular replacement is utilized to obtain structural information about a molecule or molecular complex, wherein the molecule or molecular complex comprises at least one Hepatitis C virus helicase subunit or homolog. A"subunit"of Hepatitis C virus helicase is a Hepatitis C virus helicase molecule that has been truncated at the N-terminus or the C-terminus, or both. In the context of the present invention, a"homolog"of Hepatitis C virus helicase is a protein that contains one or more amino acid substitutions, deletions, additions, or rearrangements with respect to the amino acid sequence of Hepatitis C virus helicase, but that, when folded into its native conformation, exhibits or is reasonably expected to exhibit at least a portion of the tertiary (three-dimensional) structure of Hepatitis C virus helicase. For example, structurally homologous molecules can contain deletions or additions of one or more contiguous or noncontiguous amino acids, such as a loop or a domain. Structurally homologous molecules also include"modified"Hepatitis C virus helicase molecules that have been chemically or enzymatically derivatized at one or more constituent amino acid, including side chain modifications, backbone modifications, and N-and C-terminal modifications including acetylation, hydroxylation, methylation, amidation, and the attachment of carbohydrate or lipid moieties, cofactors, and the like.

A heavy atom derivative of Hepatitis C virus helicase is also included as a Hepatitis C virus helicase homolog. The term"heavy atom derivative"refers to derivatives of Hepatitis C virus helicase produced by chemically modifying a crystal of Hepatitis C virus helicase. In practice, a crystal is soaked in a solution containing heavy metal atom salts, or organometallic compounds, e. g., lead chloride, gold thiomalate, thiomersal or uranyl acetate, which can diffuse through the crystal and bind to the surface of the protein. The location (s) of the bound heavy metal atom (s) can be determined by x- ray diffraction analysis of the soaked crystal. This information, in turn, is used to generate the phase information used to construct three-dimensional structure of the protein (T. L.

Blundell and N. L. Johnson, Protein Crystallography, Academic Press (1976)).

Because Hepatitis C virus helicase can crystallize in more than one crystal form, the structure coordinates of Hepatitis C virus helicase as provided by this invention are particularly useful in solving the structure of other crystal forms of Hepatitis C virus helicase or Hepatitis C virus helicase complexes.

The structure coordinates of HCV helicase as provided by this invention are particularly useful in solving the structure of HCV helicase mutants. Mutants may be prepared, for example, by expression of HCV helicase cDNA previously altered in its coding sequence by oligonucleotide-directed mutagenesis. Mutants may also be generated by site-specific incorporation of unnatural amino acids into HCV helicase proteins using the general biosynthetic method of C. J. Noren et al., Science, 244: 182-188 (1989). In this method, the codon encoding the amino acid of interest in wild-type HCV helicase is replaced by a"blank"nonsense codon, TAG, using oligonucleotide-directed mutagenesis. A suppressor tRNA directed against this codon is then chemically aminoacylated in vitro with the desired unnatural amino acid. The aminoacylated tRNA is then added to an in vitro translation system to yield a mutant HCV helicase with the site-specific incorporated unnatural amino acid.

Selenocysteine or selenomethionine may be incorporated into wild-type or mutant HCV helicase by expression of HCV helicase-encoding cDNAs in auxotrophic E. coli strains (Hendrickson et al., EMBO J., 9 (5): 1665-72 (1990)). In this method, the wild-type or mutagenized HCV helicase cDNA may be expressed in a host organism on a growth medium depleted of either natural cysteine or methionin (or both) but enriched in selenocysteine or selenomethionine (or both).

The structure coordinates of Hepatitis C virus helicase in Tables 1, 2, or 3 are also particularly useful to solve the structure of crystals of Hepatitis C virus helicase, Hepatitis C virus helicase mutants or Hepatitis C virus helicase homologs co-complexed with a variety of chemical entities. This approach enables the determination of the optimal sites for interaction between chemical entities, including candidate Hepatitis C virus helicase inhibitors and Hepatitis C virus helicase. Potential sites for modification within the various binding site of the molecule can also be identified. This information provides an additional tool for determining the most efficient binding interactions, for example, increased hydrophobic interactions, between Hepatitis C virus helicase and a chemical entity. For example, high resolution x-ray diffraction data collected from crystals exposed to different types of solvent allows the determination of where each type of solvent molecule resides. Small molecules that bind tightly to those sites can then be designed and synthesized and tested for their Hepatitis C virus helicase inhibition activity.

All of the complexes referred to above may be studied using well-known x-ray diffraction techniques and may be refined versus 1.5-3 A resolution x-ray data to an R value of about 0.20 or less using computer software, such as X-PLOR (Yale University, 1992, distributed by Molecular Simulations, Inc. ; see, e. g., Blundell & Johnson, supra ; Meth. Enzymol., Vol. 114 & 115, H. W. Wyckoff et al., eds., Academic Press (1985)).

This information may thus be used to optimize known Hepatitis C virus helicase inhibitors, and more importantly, to design new Hepatitis C virus helicase inhibitors.

The invention also includes the unique three-dimensional configuration defined by a set of points defined by the structure coordinates for a molecule or molecular complex structurally homologous to Hepatitis C virus helicase as determined using the method of the present invention, structurally equivalent configurations, and magnetic storage media comprising such set of structure coordinates.

Further, the invention includes structurally homologous molecules as identified using the method of the invention.

HOMOLOGYMODELING Using homology modeling, a computer model of a Hepatitis C virus helicase homolog can be built or refined without crystallizing the homolog. First, a preliminary model of the Hepatitis C virus helicase homolog is created by sequence alignment with Hepatitis C virus helicase, secondary structure prediction, the screening of structural libraries, or any combination of those techniques. Computational software may be used to carry out the sequence alignments and the secondary structure predictions. Structural incoherences, e. g., structural fragments around insertions and deletions, can be modeled by screening a structural library for peptides of the desired length and with a suitable conformation. For prediction of the side chain conformation, a side chain rotamer library may be employed. Where the Hepatitis C virus helicase homolog has been crystallized, the final homology model can be used to solve the crystal structure of the homolog by molecular replacement, as described above. Next, the preliminary model is subjected to energy minimization to yield an energy minimized model. The energy minimized model may contain regions where stereochemistry restraints are violated, in which case such regions are remodeled to obtain a final homology model. The homology model is positioned according to the results of molecular replacement, and subjected to further refinement comprising molecular dynamics calculations.

RATIONAL DRUG DESIGN Computational techniques can be used to screen, identify, select and design chemical entities capable of associating with Hepatitis C virus helicase or structurally homologous molecules. Such ligands can include, for example, (a) inhibitors of HCV helicase that bind to at least one of the oligonucleotide binding sites of HCV helicase ; (b) compounds that interfere with the allosteric motion of domain 2 of HCV helicase by binding at the interface between domain 1 and domain 2 of HCV helicase; and (c) inhibitors or cofactors that bind to the NTP binding site on domain 1 of HCV helicase.

Computational techniques can be used to screen, identify, select and design chemical entities capable of associating with HCV helicase or structurally homologous molecules.

Knowledge of the structure coordinates for the two new crystal forms of HCV helicase permits the design and/or identification of natural of synthetic compounds that have a shape complementary to the conformation of one or more of the four HCV helicase binding sites identified herein. In particular, computational techniques can be used to identify or design chemical entities, such as inhibitors, cofactors, allosteric effectors, agonists and antagonists, that associate with an HCV helicase binding site or an HCV helicase-like binding site. Inhibitors may bind to all or a portion of a binding site of HCV helicase, and can be competitive, non-competitive, or uncompetitive inhibitors; or interfere with dimerization by binding at the interface between the two monomers. Once identified and screened for biological activity, these chemical entities may be used therapeutically or prophylactically to block HCV helicase activity and, thus, to treat Hepatitis C virus infection. Structure-activity data for analogs of ligands bind to HCV helicase or HCV helicase-like binding sites can also be obtained computationally.

The term"chemical entity,"as used herein, refers to chemical compounds, complexes of two or more chemical compounds, and fragments of such compounds or complexes. Chemical entities that are determined to associate with Hepatitis C virus helicase are potential drug candidates. Data stored in a machine-readable storage medium that is capable of displaying a graphical three-dimensional representation of the structure of Hepatitis C virus helicase or a structurally homologous molecule, as identified herein, or portions thereof may thus be advantageously used for drug discovery. The structure coordinates of the chemical entity are used to generate a three-dimensional image that can be computationally fit to the three-dimensional image of Hepatitis C virus helicase or a structurally homologous molecule. The three-dimensional molecular structure encoded by the data in the data storage medium can then be computationally evaluated for its ability to associate with chemical entities. When the molecular structures encoded by the data is displayed in a graphical three-dimensional representation on a computer screen, the protein structure can also be visually inspected for potential association with chemical entities.

One embodiment of the method of drug design involves evaluating the potential association of a known chemical entity with Hepatitis C virus helicase or a structurally homologous molecule, particularly with a Hepatitis C virus helicase binding site or Hepatitis C virus helicase-like binding site. The method of drug design thus includes computationally evaluating the potential of a selected chemical entity to associate with any of the molecules or molecular complexes set forth above. This method comprises the steps of : (a) employing computational means to perform a fitting operation between the selected chemical entity and a binding site of the molecule or molecular complex ; and (b) analyzing the results of said fitting operation to quantify the association between the chemical entity and the binding site.

In another embodiment, the method of drug design involves computer-assisted design of chemical entities that associate with Hepatitis C virus helicase, its homologs, or portions thereof. Chemical entities can be designed in a step-wise fashion, one fragment at a time, or may be designed as a whole or"de novo." To be a viable drug candidate, the chemical entity identified or designed according to the method must be capable of structurally associating with at least part of a Hepatitis C virus helicase or Hepatitis C virus helicase-like binding sites, and must be able, sterically and energetically, to assume a conformation that allows it to associate with the Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site. Non-covalent molecular interactions important in this association include hydrogen bonding, van der Waals interactions, hydrophobic interactions, and electrostatic interactions.

Conformational considerations include the overall three-dimensional structure and orientation of the chemical entity in relation to the binding site, and the spacing between various functional groups of an entity that directly interact with the Hepatitis C virus helicase-like binding site or homologs thereof.

Optionally, the potential binding of a chemical entity to a Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site is analyzed using computer modeling techniques prior to the actual synthesis and testing of the chemical entity. If these computational experiments suggest insufficient interaction and association between it and the Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site, testing of the entity is obviated. However, if computer modeling indicates a strong interaction, the molecule may then be synthesized and tested for its ability to bind to or interfere with a Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site. Binding assays to determine if a compound actually binds to Hepatitis C virus helicase can also be performed and are well known in the art. Binding assays may employ kinetic or thermodynamic methodology using a wide variety of techniques including, but not limited to, microcalorimetry, circular dichroism, capillary zone electrophoresis, nuclear magnetic resonance spectroscopy, fluorescence spectroscopy, and combinations thereof.

One skilled in the art may use one of several methods to screen chemical entities or fragments for their ability to associate with a Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site. This process may begin by visual inspection of, for example, a Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site on the computer screen based on the Hepatitis C virus helicase structure coordinates in Tables 1, 2, or 3 or other coordinates which define a similar shape generated from the machine- readable storage medium. Selected fragments or chemical entities may then be positioned in a variety of orientations, or docked, within the binding site. Docking may be accomplished using software such as QUANTA and SYBYL, followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARMM and AMBER.

Specialized computer programs may also assist in the process of selecting fragments or chemical entities. Examples include GRID (Goodford, J. Med. Chem., 28: 849-57 (1985) ; available from Oxford University, Oxford, UK); MCSS (Miranker et al., Proteins : Struct. Funct. Gen., 11: 29-34 (1991) ; available from Molecular Simulations, San Diego, CA); AUTODOCK (Goodsell et al., Proteins : Struct. Funct. Genet., 8: 195- 202 (1990); available from Scripps Research Institute, La Jolla, CA); and DOCK (Kuntz et al., J Mol. Biol., 161: 269-88 (1982); available from University of California, San Francisco, CA).

Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound or complex. Assembly may be preceded by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of Hepatitis C virus helicase. This would be followed by manual model building using software such as QUANTA or SYBYL (Tripos Associates, St. Louis, MO).

Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include, without limitation, CAVEAT (P. A. Bartlett et al., in Molecular Recognition in Chemical and Biological Problems, Special Publ., Royal Chem. Soc., 78: 182-96 (1989); Lauri et al., J : Comput. Aided Mol. Des., 8: 51-66 (1994); available from the University of California, Berkeley, CA); 3D database systems such as ISIS (available from MDL Information Systems, San Leandro, CA; reviewed in Martin, J Med. Chem. 35: 2145-54 (1992)); and HOOK (Eisen et al., Proteins : Struc., Funct., Genet, 19: 199-221 (1994); available from Molecular Simulations, San Diego, CA).

Hepatitis C virus helicase binding compounds may be designed"de novo"using either an empty binding site or optionally including some portion (s) of a known inhibitor (s). There are many de novo ligand design methods including, without limitation, LUDI (Bohm, J Comp. Aid. Molec. Design., 6: 61-78 (1992); available from Molecular Simulations Inc., San Diego, CA); LEGEND (Nishibata et al., Tetrahedron, 47: 8985 (1991) ; available from Molecular Simulations Inc., San Diego, CA); LeapFrog (available from Tripos Associates, St. Louis, MO); and SPROUT (Gillet et al., J. Comput. Aided Mol. Design, 7 : 127-53 (1993); available from the University of Leeds, UK).

Once a compound has been designed or selected by the above methods, the efficiency with which that entity may bind to or interfere with a Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site may be tested and optimized by computational evaluation. For example, an effective Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site inhibitor must preferably demonstrate a relatively small difference in energy between its bound and free states (i. e., a small deformation energy of binding). Thus, the most efficient Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site inhibitors should preferably be designed with a deformation energy of binding of not greater than about 10 kcal/mole ; more preferably, not greater than 7 kcal/mole. Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site inhibitors may interact with the binding site in more than one conformation that is similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free entity and the average energy of the conformations observed when the inhibitor binds to the protein.

An entity designed or selected as binding to or interfering with a Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site may be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target enzyme and with the surrounding water molecules. Such non- complementary electrostatic interactions include repulsive charge-charge, dipole-dipole, and charge-dipole interactions.

Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interactions. Examples of programs designed for such uses include: Gaussian 94, revision C (M. J. Frisch, Gaussian, Inc., Pittsburgh, PA (1995)); AMBER, version 4.1 (P. A. Kollman, University of California at San Francisco, (1995)); QUANTA/CHARMM (Molecular Simulations, Inc., San Diego, CA (1995)); Insight IIlDiscover (Molecular Simulations, Inc., San Diego, CA (1995)); DelPhi (Molecular Simulations, Inc., San Diego, CA (1995)); and AMSOL (Quantum Chemistry Program Exchange, Indiana University). These programs may be implemented, for instance, using a Silicon Graphics workstation such as an Indigo2 with"IMPACT" graphics. Other hardware systems and software packages will be known to those skilled in the art.

Another approach encompassed by this invention is the computational screening of small molecule databases for chemical entities or compounds that can bind in whole, or in part, to a Hepatitis C virus helicase or Hepatitis C virus helicase-like binding site. In this screening, the quality of fit of such entities to the binding site may be judged either by shape complementarity or by estimated interaction energy (Meng et al., J Comp. Chem., 13: 505-24 (1992)).

Yet another approach to rational drug design involves an iterative process to identify inhibitors of HCV helicase. Iterative drug design is a method for optimizing associations between a protein and a compound by determining and evaluating the three- dimensional structures of successive sets of protein/compound complexes. In iterative drug design, crystals of a series of protein/compound complexes are obtained and then the three-dimensional structures of each complex is solved. Such an approach provides insight into the association between the proteins and compounds of each complex. This is accomplished by selecting compounds with inhibitory activity, obtaining crystals of this new protein/compound complex, solving the three dimensional structure of the complex, and comparing the associations between the new protein/compound complex and previously solved protein/compound complexes. By observing how changes in the compound affected the protein/compound associations, these associations may be optimized.

PHA. RMACEUTICAL COMPOSITIONS Pharmaceutical compositions of this invention comprise an inhibitor of Hepatitis C virus helicase activity identified according to the invention, or a pharmaceutically acceptable salt thereof, and a pharmaceutically acceptable carrier, adjuvant, or vehicle.

The term"pharmaceutically acceptable carrier"refers to a carrier (s) that is"acceptable"in the sense of being compatible with the other ingredients of a composition and not deleterious to the recipient thereof. Optionally, the pH of the formulation is adjusted with pharmaceutically acceptable acids, bases, or buffers to enhance the stability of the formulated compound or its delivery form.

Methods of making and using such pharmaceutical compositions are also included in the invention. The pharmaceutical compositions of the invention can be administered orally, parenterally, by inhalation spray, topically, rectally, nasally, buccally, vaginally, or via an implanted reservoir. Oral administration or administration by injection is preferred. The term parenteral as used herein includes subcutaneous, intracutaneous, intravenous, intramuscular, intra-articular, intrasynovial, intrasternal, intrathecal, intralesional, and intracranial injection or infusion techniques.

Dosage levels of between about 0.01 and about 100 mg/kg body weight per day, preferably between about 0.5 and about 75 mg/kg body weight per day of the Hepatitis C virus helicase inhibitory compounds described herein are useful for the prevention and treatment of Hepatitis C virus helicase mediated disease. Typically, the pharmaceutical compositions of this invention will be administered from about 1 to about 5 times per day or alternatively, as a continuous infusion. Such administration can be used as a chronic or acute therapy. The amount of active ingredient that may be combined with the carrier materials to produce a single dosage form will vary depending upon the host treated and the particular mode of administration. A typical preparation will contain from about 5% to about 95% active compound (w/w). Preferably, such preparations contain from about 20% to about 80% active compound.

In order that this invention be more fully understood, the following examples are set forth. These examples are for the purpose of illustration only and are not to be construed as limiting the scope of the invention in any way.

EXAMPLES EXAMPLE 1 : CRYSTAL PREPARATIONAND DATA COLLECTION MATERIALSAND METHODS The HCV helicase is expressed in the yeast S. cerevisiae. The plasmid pd. hell was constructed by ligating the following fragments: a) a 1365 bp BamHI-HindE fragment from plasmid pPGAP/AG containing the ADH2/GAPDH promoter sequences; b) a 1424 bp HindE-SalI fragment generated by PCR, encoding HCV-1 helicase (aa 1193-1658) followed by a stop codon; and c) a 13.1 kbp BamHI-SalI fragment from the yeast/bacterial shuttle vector pBS24.1 which contains pBR322 sequences, leu2 gene, URA3 gene, 2-micron sequences, and the alpha-factor terminator. The plasmid pd. hell. His was constructed from pd. hell by the addition of oligonucleotides which created 6 histidine codons at the 3'end of the helicase sequence.

The plasmid pd. hell. His was transformed into an S. cerevisiae strain AD3 (Chiron), using a lithium acetate protocol. Transformants were selected on ura-plates.

Single colonies were patched onto leu-plates. Starter cultures were grown in leu-8% glucose media and then inoculated into YEPD (about 1% yeast extract; about 2% peptone; about 2% glucose). The induction of helicase expression occurs after the glucose is depleted from the YEPD media.

PURIFICATION Yeast cells (160 gram) were broken using the Dynomill in the following buffer: 50mM TRIS HCl pH 8.0/O. 1M NaCl/0. 1% octyl-glucoside. The lysate was centrifuged 25000x g for 1 hour and the pellet discarded. The supernatant was diluted with 25mM TRIS HCl pH 8.0; 0.1% octyl-glucoside to a conductivity below 3.3 mS/cm. A 1 liter TMAE Fractogel column was equilibrated with 50mM TRIS HCl pH 8.0; 0.1% octyl- glucoside. The supernatant was loaded onto the column at a linear flow rate of 39 cm/hr.

The column was washed to baseline with equilibration buffer. The protein was eluted with a 10 column volume gradient from 0 M NaCl to 0.3 M NaCl in equilibration buffer.

A Ni Chelating Sepharose Fast Flow column was equilibrated with 20mM TRIS Cl pH 7.9 0. 5M NaCl 5 mM Imidazole 0.1% octyl-glucoside. Five hundred mM NaCl and 5mM imidazole was added to the TMAE pool and loaded onto the column at a linear flow rate of 238 cm/hr. The column was washed to baseline with equilibration buffer made 60mM Imidazole. The column was eluted with a 15 column volume gradient from 60mM to 350mM Imidazole in equilibration buffer. The HCV Helicase was exchanged into the following buffer: 50mM TRIS-HCl pH 8.0/0.5M NaCl/l 0% Glycerol/0.1% octyl- glucoside/5mM BME. The concentration and buffer exchange was done using an Amicon stirred cell with 30K cut off membrane. The complete sequence of the HCV-1 genotype la construct used is shown in Figure 2.

CRYSTALLIZATION Crystals having a morphology of tetragonal bipyramids were grown by vapor diffusion with extensive macro-seeding from precipitant solutions of 6-12% PEG 5000MME (Fluka, Sigma-Aldrich Co., Inc., Milwaukee, WI) and lOmM HEPES pH 7.5 (Sigma, Sigma-Aldrich Co., Inc., Milwaukee, WI). Orthorhombic crystals were grown from 3.0-7% PEG4000; 10% DMSO; 0.06M K2P04 solutions by vapor diffusion utilizing extensive macro-seeding.

An HCV helicase crystal grown from 12.08 mg/ml protein in l OmM Na HEPES pH 7.5; 1mM EDTA; 5 mM DTT with 8% PEG5000 MME on a sitting drop bridge was mounted at room temperature in a glass capillary for diffraction data collection. The crystal was about 0.12 x 0.12 x 0.05 mm in size. The data were collected on the single Siemens Hi-Star proportional counter mounted on the two-theta arm of a Siemens four- circle goniostat, positioned 14 cm from the crystal at an angle of 10° from the incident beam (Bruker AXS, Madison, WI). A Siemens rotating anode X-Ray generator operated at 5.0 kW and equipped with graphite monochromator served as the source of CuKa X- Rays. Data were collected in four 60° scans through omega, with each image recording intensities through a 0.25° rotation. This data set is identified as"ux0723". Data were integrated and scaled with XENGEN v2.1 software (Howard et al., J. Appl. Cryst., 20: 383-87 (1987)). Observed unit cell parameters for this and other crystals described herein are shown in Table 4, along with other parameters that are measures of the quality of the diffraction data. This data was used for initial molecular replacement toward the solution of this structure, but was later superceded by higher resolution data collected at beamline 17-ID of the Advanced Photon Source (APS) at Argonne National Labs (aps026).

A superior HCV helicase crystal was grown from 3 microliters of 9.13 mg/ml protein in lOmM Na HEPES 7.5; 1mM EDTA ; 5 mM DTT mixed with 3 microliters ofl4% PEG5000 MME on a sitting drop bridge seeded with a dilute microseed stock (after 1 hour pre-equilibration). The crystal appeared after about 1 week. A final size of about. 4 x. 4 x. 2 mm was observed. The crystal was transferred into a cryogenic solution [0.8ml of (10% glycerol, 10% PEG5000 MME, l00mM Na HEPES pH 7.5) mixed with 0.2 ml glycerol] and equilibrated for 35 minutes. The crystal was then plunged into liquid propane and the frozen crystal transferred to APS in liquid nitrogen for data collection.

The synchrotron data were collected with the sample under a dry liquid-N2-controlled cold stream (Oxford CryoSystems) at 1 OOK. hicident radiation with wavelength B=l. 0000 A was used. All data were collected in a single 100° omega scan in 0.25° increments, and recorded on a Bruker CCD detector operated in binned (lk) mode. The crystal-to-detector distance was 15. 0 cm. Two-dimensional images were integrated and scaled with the SAINT (v 5) software system as implemented by staff of the Industrial Macromolecular Crystallography Association (IMCA). This crystal yielded 2.0 A diffraction data used in structural refinement of this crystal form. This data is identified as"apsO26"in Table 4.

Diffraction data from two crystals were used in the structure analysis. The crystal that ultimately gave rise to diffraction data identified as"ux0770"was transferred to successive 10 microliter drops containing increasing concentrations of cryogenic solution (0.06M potassium phosphate; 7% PEG8000; 10% DMSO; 25% Glycerol). Two minutes in 1 microliter cryogenic solution + 9 microliters well mix; two minutes in 2 microliters cryogenic solution + 8 microliters well mix; two minutes in 4 microliters cryogenic solution + 6 microliters well mix; two minutes in 6 microliters cryogenic solution + 4 microliters well mix; two minutes in 8 microliters cryogenic solution + 2 microliters well mix; and 10 microliters cryogenic solution for two minutes. The crystal was frozen in liquid nitrogen in a Hampton fiber loop and maintained at 100 K under a dry liquid-N2- controlled cold stream (Oxford Cryosystems, Oxford, U. K.) during diffraction data collection. Diffraction data were collected on the Single Hi-Star detector (Siemens) at a crystal-to-detector distance of 14 cm and 2 theta angle was 20°. In this configuration, the detector can acquire 2.2 A resolution data. Data were collected in 0.25° increments in seven 60° omega scans. The crystal was somewhat mosaic but gave very good diffraction.

Data were integrated and scaled with XENGEN v. 2.1 software (Howard et al., R Appl.

Cryst., 20: 383-87 (1987)).

Another crystal that ultimately gave rise to diffraction data identified as"ux0771" was transferred to successive 10 microliter drops containing increasing concentrations of cryogenic solution and frozen as described above. Data were collected at 100K on a Siemens Dual Hi-Star detector system mounted on a rotating anode X-ray source equipped with Göbel mirrors. The master detector was placed at a 2 theta angle 35° from the incident beam at distance of 15 cm from the crystal. The second (slave) detector is then at an effective 2 theta of-12.84° to intercept low resolution data. Diffraction data were measured to 1.8 A (Table 4).

TABLE 4: Diffraction data summary Tetragonal Form Orthorhombic Form Space Group P41 P21212 Data set ID ux0723 aps026 ux0770 ux0771 Cell Parameters a 112.34 A 109.57 A 66.14 A 66.21 A b 112.34 A 109.57 A 109.86 A 110.12 A c 87.37 A 84.08 A 63.87 A 64.21 A Resolution 3.4 A 2.0 A 2. 3 A 1.8 A No. Observations 31,652 302,188 104,158 167,634 No. Unique reflections 11,173 64,446 21,598 43,264 % Completeness 73% 96% 99% 96% RS, 0.097 0.082 0.043 0.055 EXAMPLE 2 : X-RAY CRYSTAL STRUCTURE SOLUTIONS TETRAGONAL FORM Crystals were assigned to one of the two enantiomorphic space groups P41 or P43 on the basis of scaling statistics and systematic absences in the diffraction data. The final choice (P41) was made on the basis of superior translation function results (described below). The volume of the asymmetric unit is large enough to accommodate two independent helicase molecules, although no particular noncrystallographic symmetry was evident from inspection of self-rotation functions with GLRF (Tong et al., Acta C7ystallogr., A46: 783-92 (1990)).

The structure was solved by application of molecular replacement methods as implemented in X-Plor v3.851 (Brünger, X-PLOR Manual. Version 3.1: A system for crystallography and NMR, New Haven, Yale University Press (1992)). An initial search model was constructed using atomic coordinates from an HCV genotype lb structure, which were later deposited in the Protein Data Bank as entry 80HM (Cho et al., J. Biol.

Chem., 273: 15045-52 (1998)). A rotation function was computed and peaks subjected to PC-refinement (Brunger, Acta C7ystallogr., A46: 46-57 (1990)) using 4-8 A diffraction data with Fobs 4op. The first rotation function searches and PC-refinement calculations conduced with this model (containing all three domains) yielded very poor Patterson correlations (0.03-0.05). In retrospect, as the"closed"form 80HM bears the least resemblance to the"open"form UHCV, it is apparent why the initial attempts to use the 80HM model for molecular replacement failed.

A second search model was constructed by applying the stereo figure reconstruction algorithm of Rossmann (formerly available from the Protein Data Bank) to Figure 1 of Yao et al. (Nat. Struct. Biol., 4: 463-77 (1997)) to deduce approximate coordinates for the 1HEI structure. The coordinates derived from this procedure were prone to large errors, but they were eventually sufficient to reveal a 15-20° difference in the position of domain 2 relative to 1HEI. A series of different models based on the initial coordinates of 80HM that sampled a range of motions of the hinge at 5° increments spanning the distribution represented by the two available structures (80HM and our modeled version of I IHEI) was constructed. These were subsequently used as a battery of different search models in molecular replacement. None of these models gave a statistically convincing solution. In hindsight, however, it was apparent that the range of hinge motions generated was not large enough to include the correct solution.

Nevertheless, the comparison of peak lists from many of the different hinge models helped identify two rotations that were present in search results with a number of different models. In addition, a subsequent search with a truncated model from which domain 2 had been removed altogether gave peaks in Patterson correlation filtering that were comparable to those found with any of the hinge models. This truncated model contained only domains 1 and 3 (residues 181-325 and 484-624). While the heights of these peaks were low (PC=0.045-0.050), their persistence in rotation functions with several different models made them stand out. Subsequent translation function searches carried out with any of the hinge models resulted in the same solution, but R-values varied, and the model with domain 2 removed gave the best statistics.

Two persistent and independent rotations identified by PC-filtering (with PC=0.0496 and 0.0449, respectively) were carried through the X-Plor translation functions, where two convincing solutions for both molecular positions (9s above background) were identified only for enantiomorphic space group P4l. This model consisting of two molecules (each with only two domains) resulted in an R-value of 0.405. Electron density computed with this model was sufficiently interpretable to allow approximate placement of the missing domain 2 (residues 326-483) of one molecule. A new model including all three domains was then reinserted as the search probe through all molecular replacement calculations, yielding universally more convincing results. The R- value after final rigid body refinement with both complete molecules was 0.343.

All subsequent work was conducted with synchrotron data set aps026. The molecular replacement procedures were repeated as described above using the last complete model.

This search against new data produced equivalent results, but with significantly better statistics. Refinement was initiated with X-Plor positional refinement, followed by a single round of X-Plor simulated-annealing refinement (Brünger, J Mol. Biol., 203: 803- 16 (1988)), using scripts generated automatically by Quanta (Molecular Simulations Inc.) for this purpose. The R-value was reduced to 0.269 for 10-2.0 A data, while the Rfee (cross-validation R based on an 8% random reflection sampling, Brünger, J : Mol. Biol., 203: 803-16 (1988)) was reduced from 0.410 to 0.353. Subsequent refinement was completed with constrained least-squares of PROFFT (Hendrickson et al.,"Incorporation of Stereochemical Information into Crystallographic Refinement"in Computing in Crystallography, (Diamond, R., Ramaseshan, S. and Ventkatesan, K.. eds.), Indian Academy of Sci, Bangalore, India. pp. 13. 01-13.25 (1980) ; Finzel, J : Appl. Cryst., 20: 53- 55 (1987)) interspersed with frequent model analysis, map interpretation and rebuilding conducted with the CHAIN (v7.1) modeling package (Sack, J Mol. Graphics, 6: 224-25 (1988)). During this rebuilding, the amino acid sequence represented by the model was corrected to reflect the HCV-1 strain la sequence of Figure 2. Final agreement factors and model geometry measures are summarized in Table 5.

ORTHORHOMBIC FORM Crystals were assigned to space group P2, 212 based on scaling statistics and systematic absences in the diffraction data. The asymmetric unit contained only one helicase molecule (Vm=2. 3) (Matthews, J Mol. Biol., 33: 491-97 (1968)). Molecular replacement was first attempted with X-Plor using the refined tetragonal form model (Molecule A) consisting of only domains 1 and 3. A single prominent rotation with PC=0. 135 was readily identified from a rotation function analysis of 4-8 A data of ux0770. A translation solution 8a above background was also identified. This model resulted in an R-value of 0.45 (8-3 A). Molecular replacement was repeated with this same model using the AMoRe program (Navaza, J Acta Crystallogr., A50 : 157-63 (1994)) of the CCP4 package (Collaborative Computational Project Number 4, Acta Cryst., D50: 760-63 (1994)), which gave an equivalent solution (but much more quickly).

An examination of molecular packing implicit in this solution led us to conclude that domain 2 could only be accommodated in an orientation roughly equivalent to its position in the tetragonal form crystals. Domain 2 was fit to poor density calculated from the AMoRe model, and the rotation/translation search repeated in AMoRe, resulting in a model with R=0.41 (8-4 A). The position of domains 1/3 and 2 were refined as rigid bodies with X-Plor, and then the model was subjected to constrained least-squares refinement of all positional parameters by PROFFT. Electron density defining large segments of domain 2 (initially examined at 2.3 A resolution) was initially poor, but was clarified somewhat by computation of"omit"maps in which all of domain 2 omitted from the model. Individual segments of domain 2 were repositioned manually as suggested by density throughout the refinement process, which was long and tedious, but gradually electron density maps improved. Diffraction data was superceded by higher resolution data of ux0771 following PROFFT cycle 32, and all 1. 8 A data was gradually included in the refinement. The final R-value is 0.206. Final agreement factors and model geometry measures are summarized in Table 5.

TABLE 5 : Refinement statistics Tetragonal Form Orthorhombic Form apsO26 ux0771 Final Reflection agreement Resolution of data used 10. 0 B 2.0 A 6.0 B 1.8 A (Fobs#4#F) (Fobs#4#F) Final R-value 0.228 0.206 No. of reflections used 55,087 33,899 Final model characteristics Protein atoms 6,578 3210 Solvent atoms 367 306 Mean Isotropic B 22.9 16.5 Model geometry conformity Rms deviation from ideality (Target o) Distances (A) 1-2 (Bond) 0.023 (0.030) 0.019 (0.030) 1-3 (Bond angle) 0.038 (0.040) 0.031 (0.040) 1-4 (Fixed torsion angle) 0.041 (0.050) 0.030 (0.050) Planes (A) Peptides 0.017 (0.030) 0.015 (0.030) Other 0.021 (0.030) 0.015 (0.030) Chiral Volumes (A3) 0.300 (0.300) 0.197 (0.250) Non-bonded contacts (A) 1-4 0.189 (0.400) 0.172 (0.300) Possible H-bonds 0.248 (0.400) 0.176 (0.300) Other 0.218 (0.400) 0.180 (0.300) Thermal Parameters (Mean AB ; A) 1-2 (Main-chain atoms) 0.957 (2.000) 1.200 (3.000) 1-2 (side-chain atoms) 1.043 (1.500) 1.266 (2.000) 1-3 1.625 (3.000) 1.909 (4.000) EXAMPLE3 : COMPARISONOFHCVHELICASESTRUCTURES Coordinates for 1HEI-A, 1HEI-B, 1AIV and 80HM were obtained from the Protein Data Bank. Atomic coordinates from different structures (including UHCV-A, UHCV-B and UHHO as described herein) were overlaid (Table 6) using a program that forces a superposition of all common atoms to requested pairs of residues in two structures using the methods of Kabsch (Acta Cryst., A34: 827-28 (1978)). Because the tetragonal form (UHCV-A) appears to represent an extreme closed conformation for domain 2, this model was chosen as the resting state for comparison to other geometries.

The root mean square distances given in Table 6 reflect the distances between alpha carbons following superposition of all atoms common to both structures.

TABLE 6: R. M. S. difference in alpha-carbon positions (A) after superposition of helicase coordinates from different crystal forms StructureH FragmentsI UHCV-B UHHO 1HEI-A 1HEI-B 1AAV 8OHM UHCV-A dl vs dl 1.13 1.02 1.15 1.41 1.47 0.98 d2 vs d2 0.57 0.93 1.36 1.58 0.77 0.89 d3 vs d3 0.50 0.57 0.85 0.90 0.38 0.68 dl/d3 vs dl/d3 0.90 0.90 1.02 1.20 1.08 0.87 all vs all 0.89 1.52 2.08 2.55 1.52 4.18 UHCV-B dl vs dl-0. 46 0.55 0.82 1.00 0.64 d2 vs d2-0. 85 1.35 1.60 0.84 0.90 d3 vs d3-0. 40 0.93 0.95 0.54 0.56 dl/d3 vs dl/d3-0. 55 0.85 0.98 0.88 0.67 all vs all-1.34 2.17 2.65 1.60 4.28 UHHO dl vs dl--0. 59 0.89 0.98 0.65 d2 vs d2--1. 53 1.79 1.08 1.02 d3 vs d3--0. 96 0.99 0.52 0.62 dl/d3 vsdl/d3--0. 91 1.09 0.82 0.69 all vs all--2.06 2.58 1.53 3.61 1HE1-A dl vs dl---0. 82 0.90 0.79 d2 vs d2---1. 16 1.00 1.01 d3 vs d3---0. 44 0.91 0.98 dl/d3 vs dl/d3---0. 67 0.93 0.91 all vs all---1.23 1.13 2.67 lAlV dl vs dl-----1. 17 d2 vs d2-----0. 66 d3 vs d3 73 d1/d3 vs d1/d3 - - - - - 0.99 all vs all - - - - - 3.11 HStructures UHCV-A Tetragonal form molecule A (described herein) LTHCV-B Tetragonal form molecule B (described herein) (space group P41 ; a=b=109. 57 A, c=84.08 A ; Z=2) UHHO Orthorhombic form (described herein); 360-361,393-396 missing (space group P2, 212 ; a=66. 14 A, b=109.57 A, c=63.87 A ; Z=1) 1HEI-A Schering-Plough (S-P) orthorhombic form molecule A (Yao et al., Nat. Struct. Biol., 4: 463-77 (1997)) 1HEI-B S-P orthorhombic form molecule B; 233-261 missing (Yao et al., Nat. Struct. Biol., 4: 463-77 (1997); space group P212121 ; a=81. 54 A, b=102.73 A, c=119. 50 A; Z=2) 80HM Pohang trigonal form; 417-420 missing (Cho et al., J. Biol. Chem., 273: 15045-52 (1998); space group P3, 2 1 ; a=b=93. 3 A, c=104.6 A) lAlV Vertex orthorhombic form; 415-417 missing (Kim et al., Structure, 6: 89-100 (1998) ; space group P21212 ; a=73. 10 A, b=117. 50 A, c=63.40 A) Fragments dl Domain 1; residues 192-326. d2 Domain 2; residues 327-483, excluding hairpin 435-446. d3 Domain 3; residues 484-624.

The movement of domain 2 results in a change in teh distance separating oligonucleotide binding sites in domain 1 and domain 2. The distance between these sites is defined as the distance between the side chain oxygen of T269 and the side chain oxygen ouf This and is tabulated for each structure in Table 7.

TABLE 7: Distances UHCV-A UHHO lAlV 1HEI-A 80HM (this report) (this report) (Vertex) (S-P) (Pohang) Distance between DNA binding motifs 19.3A 19.2A 21.5A 22.3A 26.8A of domain 1 and 2 EXAMPLE 4 : PREPARATION OFA HELICASElLIGAND COMPLEY (TETRAGONAL FORM) To prepare a co-crystalline complex of HCV helicase with a chemical entity, native tetrahedral crystals (UHCV) grown as described in Example 1 were transferred into a cryogenic solution [10% (v/v) glycerol, 10% PEG500OMME, lOmM HEPES (pH 7.5)] and stabilized overnight. This crystal was soaked in 88% cryogenic solution, 1mM MgCl2 and l OmM of the chemical entity for 2 days prior to being frozen in liquid nitrogen for data collection. The crystals had a dark orange appearance. Diffraction data were obtained at the Advanced Photon Source beam-line 17-ID as described in Example 1. Crystals diffracted to 2.0A. Analysis of this data revealed that the chemical entity is bound spanning the oligonucleotide binding sites, making interactions with G2ss and T269 on domain 1 ; and R393 and T411 on domain 2.

Similar treatment of orthorhombic form crystals (UHHO) with the same chemical entity resulted in no apparent formation of complex. This may be the result of the incorrect (suboptimal) spacing separating oligonucleotide-binding sites in the orthorhombic crystal form. The same result may be expected with other alternate crystal forms of HCV helicase. This result demonstrates the unique utility of the tetrahedral (UHCV) crystal form for studying some ligands that bind spanning the oligonucleotide binding sites EXAMPLE 5 : PREPARATION OFA HELICASE/LIGAND COMPLEX (ORTHORHOMBIC FORME To prepare a co-crystalline complex of HCV helicase with another ligand, native orthorhombic crystals (UHHO) grown as described in Example 1 were transferred into a stabilization solution of 7% PEG4000,5% DMSO, and l OxnM ligand. After a few hours the crystals were sequentially transferred (30 minutes each soak) into stabilization solutions containing progressively higher DMSO concentrations. The final concentration reached was 20% DMSO. The crystal was then frozen in liquid nitrogen. Diffraction data was obtained and analyzed as described in Example 1. Crystals diffracted to 1.8A.

Analysis of this data revealed that the ligand is bound in the NTP-binding site of HCV helicase.

Similar treatment of tetragonal form crystals (UHCV) with the same compound resulted in visible cracking of the crystals, and a complete loss of diffraction. This result demonstrates the unique utility of the orthorhombic crystal form (UHHO) for studying ligands that bind at the NTP-binding site, and the possible unsuitability of the tetragonal crystals for this purpose.

The complete disclosure of all patents, patent applications including provisional applications, and publications, and electronically available material (e. g., GenBank amino acid and nucleotide sequence submissions) cited herein are incorporated by reference.

The foregoing detailed description and examples have been given for clarity of understanding only. No unnecessary limitations are to be understood therefrom. The invention is not limited to the exact details shown and described; many variations will be apparent to one skilled in the art and are intended to be included within the invention defined by the claims.

SEQUENCE LISTING FREE TEXT SEQ ID NO: 1 Hepatitis C virus (HCV) NS3 helicase SEQ ID NO: 2 Conserved NTP-binding loop (Walker motif A) in Hepatitis C virus (HCV) NS3 helicase SEQ ID NO: 3 Conserved sequence motif VI in Hepatitis C virus (HCV) NS3 helicase




 
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