# Patent

## Title
Amyloid-beta peptide crystal structure

## Abstract

The invention relates provides a novel crystal structure of the fibrillogenic part of amyloid β-peptide (Aβ). More specifically the crystal structure is Aβ-IgNAR and, accordingly the present invention also relates to selecting and/or designing compounds that modulate amyloid β-peptide (Aβ) activity using techniques such as in silico screening and crystal soaking experiments. The invention further relates to compounds and methods for inhibiting interaction between amyloid β-peptide (Aβ) monomers, more particularly, inhibiting or disrupting amyloid β-peptide (Aβ) oligomer formation and toxic activity.

## Background
FILING DATA
This application is a §371 national stage of PCT International Application No. PCT/AU2009/001327, filed Oct. 6, 2009, claiming priority of Australian Patent Application Nos. 2008905174, filed Oct. 6, 2008 and 2008905176, filed Oct. 6, 2008, the contents of all of which are hereby incorporated by reference into this application.
REFERENCE TO SEQUENCE LISTING
This application incorporates-by-reference nucleotide and/or amino acid sequences which are present in the file named “130306—0687—82750_SEQUENCELISTING_REB.TXT”, which is 29.0 kilobytes in size, and which was created Mar. 6, 2013 in the IBM-PC machine format, having an operating system compatibility with MS-Windows, which is contained in the text file filed Mar. 6, 2013 as part of this application.
FIELD
The invention relates generally to a novel crystal structure of the fibrillogenic part of amyloid β-peptide (Aβ). More specifically the crystal structure is Aβ-IgNAR and, accordingly the present invention also relates to selecting and/or designing compounds that modulate amyloid β-peptide (Aβ) activity using techniques such as in silico screening and crystal soaking experiments. The invention further relates to compounds and methods for inhibiting interaction between amyloid β-peptide (Aβ) monomers, more particularly, inhibiting or disrupting amyloid β-peptide (Aβ) oligomer formation and toxic activity
BACKGROUND
Bibliographic details of the publications referred to by author in this specification are collected alphabetically at the end of the description. The disclosure of each reference referred to in this application is incorporated herein by reference.
Reference to any prior art in this specification is not, and should not be taken as, an acknowledgment or any form of suggestion that this prior art forms part of the common general knowledge in any country.
Alzheimer's disease (AD) is a progressive neurodegenerative disorder characterized by the presence of misfolded protein depositions or amyloid plaques Crouch, P. J., S.-M. E. Harding, et al. (2008). “Mechanisms of Aβ mediated neurodegeneration in Alzheimer's disease.” Int J Biochem Cell Biol 40(2): 181-198. Plaques consist predominantly of amyloid β-peptide (Aβ), which is produced by cleavage from the membrane-bound amyloid precursor protein (APP) via the β/γ secretase pathway. (The sequence of Aβ is set out in SEQ ID NO 1). However, the current view suggests that soluble Aβ oligomer intermediates, and not the plaque burden, may be the major drivers of Aβ-mediated neuronal dysfunction Walsh, D. M. and D. J. Selkoe (2007). “Aβ oligomers—a decade of discovery.” J. Neurochem. 101(5): 1172-1184. Shankar, G. M., S. Li, et al. (2008). “Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory.” Nat. Med. Frustratingly, obtaining atomic resolution information for Aβ and such oligomers has been a major challenge Kajava, A. V., J. M. Squire, et al. (2006). “β-structures in fibrous proteins.” Adv Protein Chem 73: 1-15. Nelson, R. and D. Eisenberg (2006). “Recent atomic models of amyloid fibril structure.” Curr Opin Struct Biol 16(2): 260-265. Nelson, R. and D. Eisenberg (2006). “Structural models of amyloid-like fibrils.” Adv Protein Chem 73: 235-282, due in part to the propensity of the peptide to form amyloidal fibrils and aggregates rather than form crystallographic lattices.
The present inventors have obtained a 2.2 Å resolution crystal structure of residues 18-41 of Aβ peptide constrained within the CDR3 loop region of a shark immunoglobulin new antigen receptor (IgNAR) single variable domain antibody Henderson, K. A., V. A. Streltsov, et al. (2007). “Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition.” Structure 15(11): 1452-66. The predominant oligomeric species is a tightly associated Aβ dimer, with paired dimers forming a tetramer which is caged within four IgNAR domains, preventing further uncontrolled amyloid formation. The results reveal unusual Aβ loop topologies and inter-peptide interactions, strikingly different from fibrillar models based on solid state NMR spectroscopy data Petkova, A. T., Y. Ishii, et al. (2002). “A structural model for Alzheimer's b-amyloid fibrils based on experimental constraints from solid state NMR.” Proc Natl Acad Sci USA 99(26): 16742-16747. Luhrs, T., C. Ritter, et al. (2005). “3D structure of Alzheimer's amyloid-β(1-42) fibrils.” Proc Natl Acad Sci USA 102(48): 17342-17347. Petkova, A. T., W. M. Yau, et al. (2006). “Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils.” Biochemistry 45(2): 498-512. Sato, T., P. Kienlen-Campard, et al. (2006). “Inhibitors of amyloid toxicity based on β-sheet packing of Aβ40 and Aβ42.” Biochemistry 45(17): 5503-5516, that describe Aβ residues 18-42 as forming parallel, in-register β-sheets. Notwithstanding, conserved elements can be identified within the structure consistent with residues and motifs previously identified as critical in Ap peptide folding and neurotoxicity. This crystallographic model suggests a novel paradigm for Aβ oligomer formation, and potentially provides a system for the testing of Aβ oligomer imaging reagents and Alzheimer's disease drug candidates.
SUMMARY OF THE INVENTION
In a first aspect the present invention provides a crystal of amyloid β-peptide (Aβ(18-41) as a fusion with IgNAR (Aβ-IgNAR). In a preferred embodiment the Aβ-IgNAR crystal substantially conforms to the atomic co-ordinates of Appendix I. Preferably at least 75% of the structure has the recited RMSD value, more preferably at least 90% of the structure has the recited RMSD value and most preferably about 100% of the structure has the recited RMSD value.
In a second aspect the present invention provides an Aβ-IgNAR molecule having the amino acid sequence of SEQ ID Nos 15 to 24.
In a third aspect the present invention provides a method of assessing the interaction of a compound with Aβ, the method comprising contacting the crystal of the present invention with the compound and measuring the level of binding of the compound to the Aβ crystal.
In a fourth aspect the present invention provides a method of selecting or designing a compound that interacts with Aβ protein, the method comprising (a) assessing the stereochemical complementarity between a compound and a topographic region of Aβ protein, wherein the protein comprises: (i) amino acids 18-41 of the Aβ protein positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å; or (ii) one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) obtaining a compound which possesses stereochemical complementarity to a topographic region of the Aβ protein; and (c) testing the compound for its ability to modulate an activity associated with the Aβ protein.
In a fifth aspect the present invention provides a method for identifying a potential modulator compound for Aβ protein which method comprises: (a) providing a three-dimensional structure of amino acids 18-41 of Aβ protein as defined by the atomic coordinates shown in Appendix I, or atomic coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) providing the three-dimensional structure of a candidate compound; and (c) assessing the stereochemical complementarity between the three-dimensional structure of step (b) and a topographic region of the three-dimensional structure of step (a).
In a sixth aspect the present invention provides a computer-assisted method for identifying potential compounds able to interact with Aβ protein and thereby modulate an activity mediated by Aβ protein, using a programmed computer comprising a processor, an input device, and an output device, comprising the steps of: (a) inputting into the programmed computer, through the input device, data comprising the atomic coordinates of amino acids 18-41 of Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) generating, using computer methods, a set of atomic coordinates of a structure that possesses stereochemical complementarity to the atomic coordinates of amino acids 18-41 of the Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations, thereby generating a criteria data set; (c) comparing, using the processor, the criteria data set to a computer database of chemical structures; (d) selecting from the database, using computer methods, chemical structures which are similar to a portion of said criteria data set; and (e) outputting, to the output device, the selected chemical structures which are complementary to or similar to a portion of the criteria data set.
In a seventh aspect the present invention provides a method for evaluating the ability of a chemical entity to interact with Aβ protein, said method comprising the steps of: (a) creating a computer model of amino acids 18-41 of Aβ protein using structure coordinates wherein the root mean square deviation between said structure coordinates and the structure coordinates of amino acids 18-41 of Aβ protein as set forth in Appendix I is not more than about 1.5 Å; (b) employing computational means to perform a fitting operation between the chemical entity and said computer model of the binding surface; and (c) analysing the results of said fitting operation to quantify the association between the chemical entity and the Aβ protein model.
In an eighth aspect the present invention provides a computer for producing a three-dimensional representation of a molecule or molecular complex, wherein the computer comprises: (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the machine readable data comprise the atomic coordinates of amino acids 18-41 of Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) a working memory for storing instructions for processing the machine-readable data; (c) a central-processing unit coupled to the working memory and to the machine-readable data storage medium, for processing the machine-readable data into the three dimensional representation; and (d) an output hardware coupled to the central processing unit, for receiving the three-dimensional representation.
In a ninth aspect the present invention provides a method of assessing the ability of a compound to affect the ability of Aβ to form dimers or tetramers, the method comprising assessing the level Aβ-IgNAR dimerisation or tetramerisation in the presence or absence of the compound.
In an embodiment of this aspect of the invention the Aβ-IgNAR has the amino acid sequence of any one of SEQ ID NOs: 2, 4-13, 15-24. In another embodiment the assessment of dimerisation or tetramerisation is made by SDS-PAGE or western blot.
In a tenth aspect the present invention provides a method of assessing the affect of a mutation in Aβ to affect the ability of Aβ to form dimers or tetramers, the method comprising assessing the level of dimerisation or tetramerisation of Aβ-IgNAR including the mutation, assessing the level of dimerisation or tetramerisation of Aβ-IgNAR without the mutation and comparing the two levels.
In an embodiment of this aspect of the invention the Aβ-IgNAR not including the mutation has the amino acid sequence of any one of SEQ ID NOs: 2, 4-6, 15-18. In another embodiment the assessment of dimerisation or tetramerisation is made by SDS-PAGE or western blot.
In a eleventh aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by N27, K28, I31 and L34 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
In an twelfth aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by G33, L34, M35 and V36 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
In a thirteenth aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by V18, F20, S26, K28, G29, I32, M35, V39 and I41 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
In a fourteenth aspect the present invention provides a compound for decreasing metal binding by amyloid β-peptide oligomers, wherein the compound interacts with the aligned E22 of the Aβ monomers in the Aβ oligomer.
In a fifteenth aspect the present invention provides the use of an Aβ-IgNAR molecule of any one SEQ ID NOs 2, 4, 5, 6, 13, 15, 16, 17 or 18 to raise antibodies against Aβ wherein the antibodies bind to residues 18 to 41 of SEQ ID NO 1 when presented in the Aβ-IgNAR molecule of any one of SEQ ID NOs 2, 4, 5, 6, 13, 15, 16, 17 or 18 but not to an isolated linear peptide having a sequence of residues 18 to 41 of SEQ ID NO 1.
In a sixteenth aspect the present invention provides an antibody which specifically binds to residues 18 to 41 of SEQ ID NO 1 when presented in the Aβ-IgNAR molecule of any one of SEQ ID NOs 2, 4, 5, 6, 13, 15, 16, 17 or 18 but not to an isolated linear peptide having the sequence of residues 18 to 41 of SEQ ID NO 1.



BRIEF DESCRIPTION OF THE FIGURES
FIG. 1 shows a schematic representation Aβ-IgNAR dimer, illustrating dimer (1), tetramer (2), and amyloid (3) interfaces.
FIG. 2 Aβ-IgNAR fusions form a stable dimer. a, Affinity purified Aβ-IgNAR-G1 elutes as a dimer by gel filtration (solid line) in comparison to 12Y-2 IgNAR monomer (dotted line), b, SDS-PAGE of affinity-purified Aβ-IgNAR-G1 under reducing (R) and non-reducing (U) conditions, illustrating formation of tetrameric (arrowed) species in the absence of heating/reducing agent.
FIG. 3 Representative electron density for Aβ-IgNAR-G1. Electron density 2F0-Fc for residues 18-41 of Aβ-IgNAR-G1 chain A. The map is contoured at 1.0σ.
FIG. 4 Aβ-IgNAR-G1 tetramer. Three aspects of the Aβ-IgNAR-G1 tetramer are shown, illustrating the axis of approximate symmetry through dimeric and tetrameric forms.
FIG. 5 Models of amyloid fibril formation. a, Construction of Aβ oligomer model based on the Aβ-IgNAR-G1 tetramer, incorporating six Aβ (1-41) metal-binding tetramers. The cartoon representation is overlayed with surfaces shaded by chains. Black spheres represent metals (Zn, Cu etc). b, As for a, represented as solubility surface (dark—hydrophilic; light—hydrophobic) c, View along the oligomer axis.
FIG. 6 In silico docking of ChemBridge 9124833 to the Aβ-IgNAR-G1 structure. The compound 3-methoxy-4-[2-(4-morpholinyl)-2-oxoethoxy]aniline (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).
FIG. 7 In silico docking of ChemBridge 7996209 to the Aβ-IgNAR-G1 structure. The compound N-[2-(4-methylphenyl)-2-oxoethyl]-1-oxo-3,4-dihydro-1H-isochromene-3-carboxamide (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).
FIG. 8 In silico docking of ChemBridge 7949851 to the Aβ-IgNAR-G1 structure. The compound methyl [3-(phenoxyacetyl)-1H-indol-1-yl]acetate (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).
FIG. 9 In silico docking of ChemBridge 7780327 to the Aβ-IgNAR-G1 structure. The compound 2-methyl-3-{[(3-methylphenoxy)acetyl]amino}benzoic acid (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).
FIG. 10 In silico docking of ChemBridge 7302096 to the Aβ-IgNAR-G1 structure. The compound 3-{[(2,5-dimethoxyphenyl)amino]carbonyl}-7-oxabicyclo[2.2.1]hept-5-ene-2-carboxylic acid (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).
FIG. 11 In silico docking of ChemBridge 5785027 to the Aβ-IgNAR-G1 structure. The compound 2-{2-[(2-hydroxyethyl)amino]-1H-benzimidazol-1-yl}-1-(1-naphthyl)ethanone hydrobromide (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).
FIG. 12 In silico docking of fenofibrate to the Aβ-IgNAR-G1 structure. Fenofibrate (dark shading) docked within the Aβ-IgNAR-G1 structure (wireframe).



DETAILED DESCRIPTION OF THE INVENTION
Definitions
The reference to residue numbers in respect of Aβ is to number residue as in the sequence of Aβ as provided in SEQ ID NO: 1. The residue number is not the number of the residue as it appears in the Aβ-IgNAR molecule.
As used herein, the term “atomic coordinates” refer to a set of values which define the position of one or more atoms with reference to a system of axes.
A structure that “substantially conforms” to a given set of atomic coordinates is a structure wherein at least about 50% of such structure has an RMSD of less than about 1.5 Å for the backbone atoms in secondary structure elements in each domain, and more preferably, less than about 1.3 Å for the backbone atoms in secondary structure elements in each domain, and, in increasing preference, less than about 1.0 Å, less than about 0.7 Å, less than about 0.5 Å, and most preferably, less than about 0.3 Å for the backbone atoms in secondary structure elements in each domain.
Preferably a structure that substantially conforms to a given set of atomic co-ordinates is a structure wherein at least about 75% of such structure has the recited RMSD value, more preferably at least about 90% of such structure has the recited RMSD value, and most preferably, about 100% of such structure has the recited RMSD value.
The above definition of “substantially conforms” can be extended to include atoms of amino acid side chains. As used herein, the phrase “common amino acid side chains” refers to amino acid side chains that are common to both the structure which substantially conforms to a given set of atomic coordinates and the structure that is actually represented by such atomic coordinates.
By the terms “modulate” or “modulating” it is meant that the compound changes an Aβmonomer, dimer, or tetramer by at least 10%. Suitably, a compound modulates Aβ monomer, dimer, or tetramer by decreasing oligomerization or toxicity.
By using the terms “inhibition”/“inhibiting” and/or “disruption”/“disrupting” it is intended to include the concept of “modulate” or “modulating.”
The phrase “decrease oligomerization or toxicity” is intended to encompass partial or complete inhibition of oligomerization or toxicity. The ability of a compound to increase or decrease activity can be assessed by any one of the Aβ oligomerization or toxicity assays described herein.
The term “antibody”, as used herein, broadly refers to any immunoglobulin (Ig) molecule comprised of four polypeptide chains, two heavy (H) chains and two light (L) chains, or any functional fragment, mutant, variant, or derivation thereof, which retains the essential epitope binding features of an Ig molecule. Such mutant, variant, or derivative antibody formats are known in the art. Non-limiting embodiments of which are discussed below.
In a full-length antibody, each heavy chain is comprised of a heavy chain variable region (abbreviated herein as HCVR or VH) and a heavy chain constant region. The heavy chain constant region is comprised of three domains, CH1, CH2 and CH3. Each light chain is comprised of a light chain variable region (abbreviated herein as LCVR or VL) and a light chain constant region. The light chain constant region is comprised of one domain, CL. The VH and VL regions can be further subdivided into regions of hypervariability, termed complementarity determining regions (CDR), interspersed with regions that are more conserved, termed framework regions (FR). Each VH and VL is composed of three CDRs and four FRs, arranged from amino-terminus to carboxy-terminus in the following order: FR1, CDR1, FR2, CDR2, FR3, CDR3, FR4. Immunoglobulin molecules can be of any type (e.g., IgG, IgE, IgM, IgD, IgA and IgY), class (e.g., IgG1, IgG2, IgG 3, IgG4, IgA1 and IgA2) or subclass.
The term “antigen binding domain” or “antigen binding portion” of an antibody, as used herein, refers to one or more fragments of an antibody or protein that retain the ability to specifically bind to an antigen (e.g., IL-12). It has been shown that the antigen-binding function of an antibody can be performed by fragments of a full-length antibody. Such antibody embodiments may also be bispecific, dual specific, or multi-specific formats; specifically binding to two or more different antigens. Examples of binding fragments encompassed within the term “antigen-binding portion” of an antibody include (i) a Fab fragment, a monovalent fragment consisting of the VL, VH, CL and CH1 domains; (ii) a F(ab′)2 fragment, a bivalent fragment comprising two Fab fragments linked by a disulfide bridge at the hinge region; (iii) a Fd fragment consisting of the VH and CH1 domains; (iv) a Fv fragment consisting of the VL and VH domains of a single arm of an antibody, (v) a dAb fragment (Ward et al. 1989 Nature 341 544-6, Winter et al., PCT publication WO 90/05144 A1 herein incorporated by reference), which comprises a single variable domain; and (vi) an isolated complementarity determining region (CDR). Furthermore, although the two domains of the Fv fragment, VL and VH, are coded for by separate genes, they can be joined, using recombinant methods, by a synthetic linker that enables them to be made as a single protein chain in which the VL and VH regions pair to form monovalent molecules (known as single chain Fv (scFv); (see e.g., Bird et al. 1988 Science 242 423-6; Huston et al. 1988 Proc Natl Acad Sci USA 85 5879-83). Such single chain antibodies are also intended to be encompassed within the term “antigen-binding portion” of an antibody. Other forms of single chain antibodies, such as diabodies are also encompassed. Diabodies are bivalent, bispecific antibodies in which VH and VL domains are expressed on a single polypeptide chain, but using a linker that is too short to allow for pairing between the two domains on the same chain, thereby forcing the domains to pair with complementary domains of another chain and creating two antigen binding sites (see e.g., Holliger, P., et al., 1993, Proc. Natl. Acad. Sci. USA 90:6444-6448; Poljak, R. J., et al., 1994, Structure 2:1121-1123). Such antibody binding portions are known in the art (Kontermann and Dubel eds., Antibody Engineering 2001 Springer-Verlag. New York. 790 pp., ISBN 3-540-41354-5).
In a first aspect the present invention provides a crystal of amyloid β-peptide Aβ(18-41) as a fusion with IgNAR (Aβ-IgNAR). In a preferred embodiment the Aβ3-IgNAR crystal substantially conforms to the atomic co-ordinates of Appendix I. Preferably at least 75% of the structure has the recited RMSD value, more preferably at least 90% of the structure has the recited RMSD value and most preferably about 100% of the structure has the recited RMSD value.
In a second aspect the present invention provides an Aβ-IgNAR molecule having the amino acid sequence of SEQ ID Nos 15 to 24. SEQ ID Nos 15 to 24 set forth the amino acid sequences of the Aβ-IgNAR molecules described in Table 4, but without the 2× FLAG tag present in those molecules listed in Table 4. Thus, SEQ ID No:15 sets forth the amino acid sequence of a fusion of amyloid β-peptide Aβ(18-41) with IgNAR (Aβ-IgNAR); SEQ ID No.16 sets forth the amino acid sequence of a variant Aβ-IgNAR molecule containing the Gly3 mutation; SEQ ID No.17 sets forth the amino acid sequence of a variant Aβ-IgNAR molecule containing the Gly6 mutation; SEQ ID No.18 sets forth the amino acid sequence of a variant Aβ-IgNAR molecule containing the Gly2 mutation; SEQ ID No.19 sets forth the amino acid sequence of a variant Aβ-IgNAR molecule containing the Leu34Pro mutation; SEQ ID No.20 sets forth the amino acid sequence of a variant Aβ-IgNAR molecule containing the Asp23Asn mutation; SEQ ID No.21 sets forth the amino acid sequence of a variant Aβ-IgNAR molecule containing the Glu22Gln mutation; SEQ ID No.22 sets forth the amino acid sequence of a variant Aβ-IgNAR molecule containing the Ala21Gly mutation; SEQ ID No.23 sets forth the amino acid sequence of a variant Aβ-IgNAR molecule containing the ΔGlu22 mutation; and SEQ ID No.24 sets forth the amino acid sequence of a variant Aβ-IgNAR molecule containing the Ser26Cys mutation.
In a third aspect the present invention provides a method of assessing the interaction of a compound with Aβ, the method comprising contacting the crystal of the present invention with the compound and measuring the level of binding of the compound to the Aβ crystal.
In a fourth aspect the present invention provides a method of selecting or designing a compound that interacts with Aβ protein, the method comprising (a) assessing the stereochemical complementarity between a compound and a topographic region of Aβ protein, wherein the protein comprises: (i) amino acids 18-41 of the Aβ protein positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å; or (ii) one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) obtaining a compound which possesses stereochemical complementarity to a topographic region of the Aβ protein; and (c) testing the compound for its ability to modulate an activity associated with the Aβ protein.
In a fifth aspect the present invention provides a method for identifying a potential modulator compound for Aβ protein which method comprises: (a) providing a three-dimensional structure of amino acids 18-41 of Aβ protein as defined by the atomic coordinates shown in Appendix I, or atomic coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) providing the three-dimensional structure of a candidate compound; and (c) assessing the stereochemical complementarity between the three-dimensional structure of step (b) and a topographical region of the three-dimensional structure of step (a).
In a sixth aspect the present invention provides a computer-assisted method for identifying potential compounds able to interact with Aβ protein and thereby modulate an activity mediated by Aβ protein, using a programmed computer comprising a processor, an input device, and an output device, comprising the steps of: (a) inputting into the programmed computer, through the input device, data comprising the atomic coordinates of amino acids 18-41 of Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) generating, using computer methods, a set of atomic coordinates of a structure that possesses stereochemical complementarity to the atomic coordinates of amino acids 18-41 of the Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations, thereby generating a criteria data set; (c) comparing, using the processor, the criteria data set to a computer database of chemical structures; (d) selecting from the database, using computer methods, chemical structures which are similar to a portion of said criteria data set; and (e) outputting, to the output device, the selected chemical structures which are complementary to or similar to a portion of the criteria data set.
In a seventh aspect the present invention provides a method for evaluating the ability of a chemical entity to interact with Aβ protein, said method comprising the steps of: (a) creating a computer model of amino acids 18-41 of Aβ protein using structure coordinates wherein the root mean square deviation between said structure coordinates and the structure coordinates of amino acids 18-41 of Aβ protein as set forth in Appendix I is not more than about 1.5 Å; (b) employing computational means to perform a fitting operation between the chemical entity and said computer model of the binding surface; and (c) analysing the results of said fitting operation to quantify the association between the chemical entity and the Aβ protein model.
In an eighth aspect the present invention provides a computer for producing a three-dimensional representation of a molecule or molecular complex, wherein the computer comprises: (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the machine readable data comprise the atomic coordinates of amino acids 18-41 of Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å, or one or more subsets of said amino acids, or one or more subsets of said amino acids related to the coordinates shown in Appendix I by whole body translations and/or rotations; (b) a working memory for storing instructions for processing the machine-readable data; (c) a central-processing unit coupled to the working memory and to the machine-readable data storage medium, for processing the machine-readable data into the three dimensional representation; and (d) an output hardware coupled to the central processing unit, for receiving the three-dimensional representation.
The Aβ-IgNAR crystal may comprises an Aβ-IgNAR monomer, dimer or tetramer as described in more detail below.
In a preferred embodiment, an Aβ-IgNAR crystal of the invention has the atomic coordinates set forth in Appendix I. It will be understood by those skilled in the art that atomic coordinates may be varied, without affecting significantly the accuracy of models derived therefrom; thus, although the invention provides a very precise definition of a preferred atomic structure, it will be understood that minor variations are envisaged and the claims are intended to encompass such variations. Preferred are variants in which the root mean square deviation (RMSD) of the x, y and z co-ordinates for all backbone atoms other than hydrogen is less than 1.5 Å (preferably less than 1 Å, 0.7 Å or less than 0.3 Å) compared with the coordinates given in Appendix I. It will be readily appreciated by those skilled in the art that a 3D rigid body rotation and/or translation of the atomic coordinates does not alter the structure of the molecule concerned.
In a highly preferred embodiment, the crystal has the atomic coordinates as shown in Appendix I.
As used herein, the term “atomic coordinates” refer to a set of values which define the position of one or more atoms with reference to a system of axes.
The present invention also provides a crystal structure of an Aβ(18-41) polypeptide (monomer, dimer and tetramer), or a region thereof.
The atomic coordinates obtained experimentally for amino acids 18 to 41 of Aβ-IgNAR are shown in Appendix I. However, a person skilled in the art will appreciate that a set of atomic coordinates determined by X-ray crystallography is not without standard error. Accordingly, any set of structure coordinates for an Aβ-IgNAR polypeptide that has a root mean square deviation of protein backbone atoms of less than 1.5 Å when superimposed (using backbone atoms) on the atomic coordinates listed in Appendix I shall be considered identical.
The present invention also comprises the atomic coordinates of Aβ(18-41) polypeptide (monomer, dimer and tetramer) that substantially conform to the atomic coordinates listed in Appendix I.
A structure that “substantially conforms” to a given set of atomic coordinates is a structure wherein at least about 50% of such structure has an RMSD of less than about 1.5 Å for the backbone atoms in secondary structure elements in each domain, and more preferably, less than about 1.3 Å for the backbone atoms in secondary structure elements in each domain, and, in increasing preference, less than about 1.0 Å, less than about 0.7 Å, less than about 0.5 Å, and most preferably, less than about 0.3 Å for the backbone atoms in secondary structure elements in each domain.
In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of such structure has the recited RMSD value, and more preferably, at least about 90% of such structure has the recited RMSD value, and most preferably, about 100% of such structure has the recited RMSD value.
In an even more preferred embodiment, the above definition of “substantially conforms” can be extended to include atoms of amino acid side chains. As used herein, the phrase “common amino acid side chains” refers to amino acid side chains that are common to both the structure which substantially conforms to a given set of atomic coordinates and the structure that is actually represented by such atomic coordinates.
The variations in coordinates may be generated due to mathematical manipulations of the structure coordinates. For example, the structure coordinates set forth in Appendix I could be manipulated by crystallographic permutations of the structure coordinates, fractionalisation of the structure coordinates, integer additions or subtractions to sets of the structure coordinates, inversion of the structure coordinates, or any combination thereof.
Alternatively, modification 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 account for variations in structure coordinates.
Various computational analyses are used to determine whether a molecular complex or a portion thereof is sufficiently similar to all or parts of the structure of Aβ-IgNAR and Aβ monomer, dimer and tetramer described above. Such analyses may be carried out in current software applications, such as the Molecular Similarity program of QUANTA (Molecular Simulations Inc., San Diego, Calif.) version 4.1.
The Molecular Similarity program permits comparisons between different structures, different conformations of the same structure, and different parts of the same structure.
Comparisons typically involve calculation of the optimum translations and rotations required such that the root mean square difference of the fit over the specified pairs of equivalent atoms is an absolute minimum. This number is given in angstroms.
Accordingly, structural coordinates of Aβ-IgNAR or Aβ monomer, dimer or tetramer within the scope of the present invention include structural coordinates related to the atomic coordinates listed in Appendix I by whole body translations and/or rotations. Accordingly, RMSD values listed above assume that at least the backbone atoms of the structures are optimally superimposed which may require translation and/or rotation to achieve the required optimal fit from which to calculate the RMSD value.
A three dimensional structure of Aβ-IgNAR or Aβ monomer, dimer or tetramer or region thereof which substantially conforms to a specified set of atomic coordinates can be modelled by a suitable modeling computer program such as MODELER (Sali & Blundell, 1993), as implemented in the Insight II Homology software package (Insight II (97.0), MSI, San Diego), using information, for example, derived from the following data: (1) the amino acid sequence of the Aβ-IgNAR or Aβ monomer, dimer or tetramer polypeptide; (2) the amino acid sequence of the related portion(s) of the protein represented by the specified set of atomic coordinates having a three dimensional configuration; and, (3) the atomic coordinates of the specified three dimensional configuration. A three dimensional structure of Aβ-IgNAR or Aβ monomer, dimer or tetramer polypeptide which substantially conforms to a specified set of atomic coordinates can also be calculated by a method such as molecular replacement, which is described in detail below.
Structure coordinates/atomic coordinates are typically loaded onto a machine readable-medium for subsequent computational manipulation. Thus models and/or atomic coordinates are advantageously stored on machine-readable media, such as magnetic or optical media and random-access or read-only memory, including tapes, diskettes, hard disks, CD-ROMs and DVDs, flash memory cards or chips, servers and the internet. The machine is typically a computer.
The structure coordinates/atomic coordinates may be used in a computer to generate a representation, e.g. an image, of the three-dimensional structure of the Aβ-IgNAR or Aβ monomer, dimer or tetramer crystal which can be displayed by the computer and/or represented in an electronic file.
The structure coordinates/atomic coordinates and models derived therefrom may also be used for a variety of purposes such as drug discovery, biological reagent (binding protein) selection and X-ray crystallographic analysis of other protein crystals.
The three-dimensional structure of Aβ-IgNAR or Aβ monomer, dimer or tetramer provided by the present invention can be used to identify potential target binding sites on Aβ monomer, dimer or tetramers, or derived higher order multimers (i.e. to identify those regions of Aβ involved in oligomerization and/or toxicity and/or disease) as well as in methods for identifying or designing compounds which interact with potential target binding sites of Aβ, e.g. potential modulators/inhibitors of Aβ.
In one embodiment, the target binding site is a region of Aβ involved in oligermisation. Preferred target binding sites comprise one or more of the following domains: the dimerisation domain, the tetramerisation domain, the amyloid formation domain.
In a ninth aspect the present invention provides a method of assessing the ability of a compound to affect the ability of Aβ to form dimers or tetramers, the method comprising assessing the level Aβ-IgNAR dimerisation or tetramerisation in the presence or absence of the compound.
In an embodiment of this aspect of the invention the Aβ-IgNAR has the amino acid sequence of any one of SEQ ID NOs: 2, 4-13, 15-24. In another embodiment the assessment of dimerisation or tetramerisation is made by SDS-PAGE or western blot.
In a tenth aspect the present invention provides a method of assessing the affect of a mutation in Aβ to affect the ability of Aβ to form dimers or tetramers, the method comprising assessing the level of dimerisation or tetramerisation of Aβ-IgNAR including the mutation, assessing the level of dimerisation or tetramerisation of Aβ-IgNAR without the mutation and comparing the two levels.
In a eleventh aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by N27, K28, I31 and L34 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
In an embodiment of this aspect the region of Aβ-peptide is defined by F19, A21, G25, N27, K28, I31 and L34.
In an embodiment of this aspect of the invention the compound is the peptide 27-NKGAI-31 to compete with formation of the dimer.
In another embodiment of this aspect of the invention the compound is the peptide 27-NKxxIxxL-34 (wherein x is any amino acid) to compete with formation of the dimer with or with out flanking residues.
In another embodiment the compound is an antibody or an antigen binding region thereof which binds Aβ-peptide in the region defined by N27, K28, I31 and L34. The antibody or antigen binding region may bind the Aβ-peptide in the region defined by F19, A21, G25, N27, K28, I31 and L34.
In an twelfth aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by G33, L34, M35 and V36 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
In an embodiment of this aspect the region of Aβ-peptide is defined by I32, G33, L34, M35 and V36.
In an embodiment of this aspect of the invention the compound is the peptide 33-GLMV-36 to compete for tetramer with or without flanking residues
In another embodiment of this aspect of the invention the compound is the peptide 31-IIGLxV-36 (wherein x is any amino acid) to compete with the formation of the tetramer.
In another embodiment the compound is an antibody or an antigen binding region thereof which binds Aβ-peptide in the region defined by G33, L34, M35 and V36. The antibody or antigen binding region may bind the Aβ-peptide in the region defined by I32, G33, L34, M35 and V36.
In a thirteenth aspect the present invention provides a compound for inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, wherein the compound interacts with the region of Aβ-peptide defined by V18, F20, S26, K28, G29, I32, M35, V39 and I41 of Aβ-peptide wherein amino acids 18-41 of the Aβ protein are positioned at atomic coordinates as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
In an embodiment of this aspect the region of Aβ-peptide is defined by V18, F20, D23, S26, K28, G29, A30, I32, M35, G37, V39 and I41.
In an embodiment of this aspect of the invention the compound is the peptide selected from the group consisting of the peptides 26-SxKG-29, 18-VxF-20, 32-IxxM-35, and 39-VxI-41 each with or without flanking sequences; wherein the peptide competes for formation of amyloid.
In another embodiment the compound is an antibody or an antigen binding region thereof which binds Aβ-peptide in the region defined by V18, F20, S26, K28, G29, I32, M35, V39 and I41. The antibody or antigen binding region may bind the Aβ-peptide in the region defined by V18, F20, D23, S26, K28, G29, A30, I32, M35, G37, V39 and I41.
In a fourteenth aspect the present invention provides a compound for decreasing metal binding by amyloid β-peptide oligomers, wherein the compound interacts with the aligned E22 of the Aβ monomers in the Aβ oligomer.
The compounds of the present invention may also be foldamers or peptidomimetics including peptidomimetics based on β-peptides. More information these classes of compounds can be found in the following references, the disclosure of which is incorporated herein by reference.

    
    
        Ripka, Amy Sa; Rich, Daniel Ha. Peptidomimetic design. Current Opinion in Chemical Biology. Vol: 2, Issue: 4, 1998 441-452.
        Robinson J A, Demarco S, Gombert F, Moehle K, Obrecht D. The design, structures and therapeutic potential of protein epitope mimetics. Drug Discov Today. 2008 Sep. 10.
        Robinson J A. beta-Hairpin Peptidomimetics: Design, Structures and Biological Activities. Acc Chem. Res. 2008 Apr. 16.
        Appella, D. H.; Christianson, L. A.; Karle, I. L.; Powell, D. R.; Gellman, S. H. β-Peptide Foldamers: Robust Helix Formation in a New Family of -Amino Acid Oligomers J. Am. Chem. Soc.; (Communication); 1996; 118(51); 13071-13072.
        Gellman, S. H., “Foldamers: a manifesto”, Acc. Chem. Res 1998, 31(4): 173-180.
        Hill D J, Mio M J, Prince R B, Hughes T S, Moore J S, “A field guide to foldamers”, Chem. Rev. 2001, 101(12): 3893-4012.
    
    


In another aspect the present invention provides a method of inhibiting or disrupting amyloid β-peptide oligomer formation or toxic activity, the method comprising contacting the Aβ-peptide with a compound according to the present invention.
In another embodiment of the present invention the peptides have the same or a similar conformation as they do in the Aβ-peptide. This confirmation is provided by the coordinates amino acids 18-41 of the Aβ protein as shown in Appendix I, or structural coordinates having a root mean square deviation from the backbone atoms of said amino acids of not more than 1.5 Å.
The target or binding site is a region of Aβ involved in oligermisation. Preferred target or binding sites comprise one or more of the following domains: the dimerisation domain, the tetramerisation domain, the amyloid formation domain.
A schematic representation of Aβ-IgNAR dimer is shown in FIG. 1. The interfaces which may be targeted include:

    
    
        The dimer interface (1)
        The tetramer interface (2) and
        The amyloid interface (3)
    
    


Alternatively, the target binding site may comprise one or more amino acids from one or more of the following amino acid sequences:

    
    
        (i) amino acids V18-I41;
        (ii) amino acids F19, A21, G25, N27, K28, G29, I31, L34 (dimer interface)
        (iii) amino acids I32, G33, L34, M35, V36 (tetramer interface)
        (iv) amino acids V18, F20, D23, S26, K28, G29, A30, I32, M35, G37, V39, I41 (amyloid interface)
    
    


A compound may interact with a specified region of Aβ-IgNAR and Aβ monomer, dimer, or tetramer (e.g. an interface) by binding either directly or indirectly to that region. A compound which binds directly, binds to the specified region. A compound which binds indirectly, binds to a region in close proximity to or adjacent to the specified region with the result that it interferes with the ability of the specified region to oligomerise, either antagonistically or agonistically. Such interference may be steric, electrostatic, or allosteric. Preferably, a compound interacts with a specified region of the Aβ-IgNAR and Aβ monomer, dimer, or tetramer by binding directly to the specified region.
Binding can be either by covalent or non-covalent interactions, or both. Examples of non-covalent interactions include electrostatic interactions, van der Waals interactions, hydrophobic interactions and hydrophilic interactions.
When a compound interacts with Aβ-IgNAR and Aβ monomer, dimer, or tetramer, it preferably “modulates” Aβ-IgNAR and Aβ monomer, dimer, or tetramer activity respectively. By “modulate” we mean that the compound changes an activity of Aβ-IgNAR and Aβmonomer, dimer, or tetramer by at least 10%. Suitably, a compound modulates Aβ-IgNAR and Aβ monomer, dimer, or tetramer by decreasing oligomerization or toxicity. The phrase “decrease oligomerization or toxicity” is intended to encompass partial or complete inhibition of oligomerization or toxicity. The ability of a candidate compound to increase or decrease activity can be assessed by any one of the Aβ oligomerization or toxicity assays described herein.
As mentioned above one of the assay protocols involves assessment of binding using the actual crystal. Binding of chemical fragments/compounds is assessed by soaking or co-crystallizing such fragments/compounds into crystals provided by the invention and then subjecting these to an X-ray beam and obtaining diffraction data. Difference Fourier techniques are readily applied by those skilled in the art to determine the location within the Aβ-IgNAR and Aβ monomer, dimer, or tetramer structure at which these fragments/compounds bind.
Typically compounds derived from the various screening protocols described herein are subjected to biological testing. There are a number of such test and a useful review is provided in Rahimi, F., Shanmugam, A. & Bitan, G.; Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders. Current Alzheimer research 5, 319-341 (2008) The disclosure of which is incorporated herein by reference.
Other methods involving the use of the crystal or A3-IgNAR protein include:
Assays utilising the Aβ-IgNAR protein and crystals/structure:
Recombinant Protein Production and SDS-Page/Western Blot

    
    
        Assessment of dimerisation and tetramerisation of recombinant Aβ-IgNAR proteins.
        Analysis of affect of familial/in vitro determined/structurally predicted/experimentally derived mutations on Aβ-IgNAR folding, oligomerization, and toxicity.
        Analysis of action of peptides/compounds/fragments/metals/antibodies on oligomerization of Aβ peptide.
    
    


An example of this method is shown in FIG. 2a where the monomer-dimer ratio is used an assay tool ie using ability of compounds to disrupt formation of dimer, and assaying by SDS-PAGE and western blot.
Size Exclusion Chromatography

    
    
        Assessment of dimerisation and tetramerisation of recombinant Aβ-IgNAR proteins.
        Analysis of affect of familial/in vitro determined/structurally predicted/experimentally derived mutations on Aβ-IgNAR folding, oligomerization, and toxicity.
        Analysis of action of peptides/compounds/fragments/antibodies on dimerisation and tetramerisation of Aβ-IgNAR.
        Analysis of action of peptides/compounds/fragments/metals/antibodies on oligomerization of Aβ-IgNAR.
    
    


BIAcore Biosensor

    
    
        Determination of binding affinities for peptides/compounds/fragments/antibodies targeting the Aβ-IgNAR structure.
    
    


Protein Crystallography

    
    
        Analysis of affect of familial/in vitro determined/structurally predicted/experimentally derived mutations on Aβ-IgNAR structure and oligomerization.
        Determination of binding site of peptides/compounds/fragments/metals/antibodies in the Aβ-IgNAR structure.
    
    


X-Ray Absorption Spectrometry

    
    
        Determination of binding sites of metals, stoichiometry and oxidation state in the Aβ-IgNAR structure using X-ray Absorption Near-Edge Spectroscopy (XANES) and Extended X-ray Absorption Fine Structure (EXAFS) methods.
    
    


Assaying derived/selected peptides/compounds/fragments/antibodies for activity
Electron Microscopy

    
    
        Analysis of action of peptides/compounds/fragments/metals/antibodies on oligomerization of Aβ peptide.
    
    


Yeast Cell Toxicity Assays

    
    
        Analysis of affect of peptides/compounds/fragments/antibodies on oligomerization of Aβ peptide in yeast systems.
        Analysis of action of peptides/compounds/fragments/metals/antibodies in reducing Aβ-mediated cellular toxicity in yeast systems.
    
    


Neuronal Cell Toxicity Assays

    
    
        Analysis of action of peptides/compounds/fragments/metals/antibodies in reducing Aβ-mediated cellular toxicity in neuronal cell lines.
        In vitro neuroprotection (MTT) assay against oligomer-mediated toxicity
    
    


Animal Studies

    
    
        Analysis of action of peptides/compounds/fragments/metals/antibodies in reducing Aβ-mediated cellular toxicity in animal model systems.
    
    


Further information regarding these and other methods which may be usefully applied in the present invention is provided in the following references the disclosures of which is incorporated herein by reference

    
    
        Streltsov, V. A. (2008). “X-ray absorption and diffraction studies of the metal binding sites in amyloid β-peptide.” Eur Biophys J 37(3): 257-263.
        Streltsov, V. A. and J. N. Varghese (2008). “Substrate mediated reduction of copper-amyloid-β complex in Alzheimer's disease.” Chem Commun (Camb)(27): 3169-3171.
        Streltsov, V. A. Titmuss, S. J., Epa, V. C., Barnham, K. J., Masters, C. L., Varghese, J. N. (2008). “The structure of the Amyloid β-peptide high affinity Copper II binding site in Alzheimer's Disease.” Biophysical Journal. (2008) 95 (7) 3447-3456
        Caine, J., et al. Alzheimer's Ab fused to green fluorescent protein induces growth stress and a heat shock response. FEMS Yeast Res 7, 1230-1236 (2007).
        Bharadwaj, P., Waddington, L., Varghese, J. & Macreadie, I. G. A new method to measure cellular toxicity of non-fibrillar and fibrillar Alzheimer's Abeta using yeast. J Alzheimers Dis 13, 147-150 (2008).
        Mosmann, T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. Journal of immunological methods 65, 55-63 (1983).
        Maynard C J, Cappai R, Volitakis I, Cherny R A, Masters C L, Li Q X, Bush A I. Gender and genetic background effects on brain metal levels in APP transgenic and normal mice: implications for Alzheimer beta-amyloid pathology. J Inorg Biochem. 2006 May; 100(5-6):952-62.
        Gotz, J., et al. A decade of tau transgenic animal models and beyond. Brain pathology (Zurich, Switzerland) 17, 91-103 (2007).
    
    


Direct binding of compounds to Aβ-IgNAR and Aβ monomer, dimer, or tetramer can also be assessed by Surface Plasmon Resonance (BIAcore) (reviewed in Morton & Myszka, 1998). Here Aβ-IgNAR and Aβ monomer, dimer, or tetramer is immobilized on a CM5 or other sensor chip by either direct chemical coupling using amine or thiol-disulphide exchange coupling (Nice & Catimel, 1999) or by capturing as a fusion protein to an appropriately derivatised sensor surface (Morten & Myszka, 1998). The potential binding molecule (called an analyte) is passed over the sensor surface at an appropriate flow rate and a range of concentrations. The classical method of analysis is to collect responses for a wide range of analyte concentrations. A range of concentrations provides sufficient information about the reaction, and by using a fitting algorithm such as CLAMP (see Morton & Myszka, 1998), rate constants can be determined (Morton & Myszka, 1998; Nice & Catimel, 1999). Normally, the ligand surface is regenerated at the end of each analyte binding cycle. Surface regeneration ensures that the same number of ligand binding sites is accessible to the analyte at the beginning of each cycle.
Incubation periods are selected for optimum activity, but may also be optimized to facilitate rapid high-throughput screening. Normally, between 0.1 and 1 hour will be sufficient. In general, a plurality of assay mixtures is run in parallel with different test agent concentrations to obtain a differential response to these concentrations. Typically, one of these concentrations serves as a negative control, i.e. at zero concentration or below the level of detection.
The basic format of oligomerization and toxicity assays are as follows:

    
    
        (i) gel filtration; and western blot/SDS-PAGE
        (ii) cellular assays
        (iii) electron microscopy and oligomerization
        (iv) yeast assays
        (v) animal studies
    
    


The compounds/chemical entities of the present invention may be used to modulate Aβ oligomerization and/or toxicity in cells, by direct binding of the chemical entity to an interface or region of Aβ-IgNAR and Aβ monomer, dimer, or tetramer and/or by an allosteric interaction elsewhere.
Given that Aβ monomer, dimer, or tetramer or oligomerization activity and toxicity is implicated in neuronal disfunction and a range of disorders, the compounds of the present invention may also be used to treat, ameliorate or prevent disorders associated with Alzheimer's disease and/or other amyloidogenic neuropathies.
The compounds which interact with Aβ-IgNAR and Aβ monomer, dimer, or tetramer and in particular to interact with the target interfaces, are useful as agonists or antagonists against the action of Aβ on other yet to be identified ligands. The compounds are useful as assay reagents for identifying other useful ligands by, for example as research tools for further analysis of Aβ oligomerization and as potential therapeutics in pharmaceutical compositions.
Aβ-IgNAR and Aβ monomer, dimer, or tetramer antagonists provided by this invention are potentially useful as therapeutics. For example, compounds are potentially useful as treatments for Alzheimers disease. These antagonists may also be used to detect the presence of Ab dimers in biological samples in particular blood and CSF. In this regard the biological sample is contacted with the compound and the level of binding assessed.
As will be evident to the skilled person, the crystal structures presented herein have enabled, for the first time, the identification of critical regions and conformations of Aβ involved in folding, dimerisation, tetramerisation, and oligermisation leading to fibril formation and toxicity.
Using a variety of known modelling techniques, the crystal structure of the present invention can be used to produce a model for at least part of Aβ monomer, dimer, or tetramer, and higher order oligomers.
As used herein, the term “modelling” includes the quantitative and qualitative analysis of molecular structure and/or function based on atomic structural information and interaction models. The term “modelling” includes conventional numeric-based molecular dynamic and energy minimisation models, interactive computer graphic models, modified molecular mechanics models, distance geometry and other structure-based constraint models.
Molecular modelling techniques can be applied to the atomic coordinates of the Aβ-IgNAR and Aβ monomer, dimer, or tetramer or a region thereof to derive a range of 3D models and to investigate the structure of interfaces and binding sites, such as the binding sites of monoclonal antibodies, nonimmunoglobulin binding proteins and inhibitory peptides.
These techniques may also be used to screen for or design small and large chemical entities which are capable of binding Aβ-IgNAR and Aβ monomer, dimer, or tetramer, their respective interfaces, and affecting oligomerization and toxicity. The screen may employ a solid 3D screening system or a computational screening system.
Such modelling methods are to design or select chemical entities that possess stereochemical complementary to particular regions of Aβ-IgNAR and Aβ monomer, dimer, or tetramer. By “stereochemical complementarity” we mean that the compound or a portion thereof makes a sufficient number of energetically favourable contacts with Aβ as to have a net reduction of free energy on binding.
Such stereochemical complementarity is characteristic of a molecule that matches intra-site surface residues located at

    
    
        (i) amino acids V18-I41;
        (ii) amino acids N27, K28, I31, L34, (dimer interface)
        (iii) amino acids G33, L34, M35, V36; (tetramer interface)
        (iv) amino acids V18, F20, S26, K28, G29, I32, M35, V39, I41 (amyloid interface),
        Or combinations thereof.
    
    


Additional intra-site residues include:

    
    
        amino acids F19, A21, G25, N27, K28, G29, I31, L34 (dimer interface)
        amino acids I32, G33, L34, M35, V36 (tetramer interface)
        amino acids V18, F20, D23, S26, K28, A30, I32, M35, G37, V39, I41 (amyloid interface)
    
    


By “match” we mean that the identified portions interact with the surface residues, for example, via hydrogen bonding or by non-covalent Van der Waals and Coulomb interactions (with surface or residue) which promote desolvation of the molecule within the site, in such a way that retention of the molecule at the binding site is favoured energetically.
It is preferred that the stereochemical complementarity is such that the compound has a Kd for the site of less than 10−4M, more preferably less than 10−5M and more preferably 10−6M. In a most preferred embodiment, the Kd value is less than 10−8M and more preferably less than 10−9M.
Chemical entities which are complementary to the shape and electrostatics or chemistry of the sites characterised by amino acids positioned at atomic coordinates set out in Appendix I will be able to bind to the regions given above, either independently or in combination and when the binding is sufficiently strong, substantially inhibit oligomerization and/or toxicity.
It will be appreciated that it is not necessary that the complementarity between chemical entities and the site(s) extend over all residues of the site(s) in order to inhibit oligomerization and/or toxicity.
A number of methods may be used to identify chemical entities possessing stereo-complementarity to a region of the Aβ-IgNAR and Aβ monomer, dimer, or tetramer. For instance, the process may begin by visual inspection of potential interface sites, on the computer screen based on the Aβ-IgNAR and Aβ monomer, dimer, or tetramer structures, or region thereof, coordinates in Appendix I generated from the machine-readable storage medium. Alternatively, selected fragments or chemical entities may then be positioned in a variety of orientations, or docked, within an individual binding site of Aβ-IgNAR and Aβ monomer, dimer, or tetramer, as defined supra. Modelling software that is well known and available in the art may be used (Guida, 1994). These include QUANTA and InsightII [Molecular Simulations, Inc., San Diego, Calif., a division of Pharmacopiea, Inc., Princeton, N.J., 1992], SYBYL [Molecular Modeling Software, Tripos Associates, Inc., St. Louis, Mo., 1992]. This modelling step may be followed by energy minimization with standard molecular mechanics force fields such as AMBER (Weiner et al., 1984), and CHARMM (Brooks et al., 1983). In addition, there are a number of more specialized computer programs to assist in the process of selecting the binding moieties of this invention.
Specialised computer programs may also assist in the process of selecting fragments or chemical entities. These include, inter alia:
1. GRID (Goodford, 1985). GRID is available from Oxford University, Oxford, UK.
2. MCSS (MXXXanker & Karplus, 1991). MCSS is available from Molecular Simulations, Burlington, Mass.
3. AUTODOCK (Goodsell & Olsen, 1990). AUTODOCK is available from Scripps Research Institute, La Jolla, Calif.
4. DOCK (Kuntz et al., 1982). DOCK is available from University of California, San Francisco, Calif.
Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound. In one embodiment, assembly may proceed 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 Aβ-IgNAR and Aβ monomer, dimer, or tetramer. This is followed by manual model building using software such as Quanta or Sybyl. Alternatively, fragments may be joined to additional atoms using standard chemical geometry.
The above-described evaluation process for chemical entities may be performed in a similar fashion for chemical compounds.
Useful programs to aid one skilled in the art in connecting the individual chemical entities or fragments include:
1. CAVEAT (Bartlett et al., 1989). CAVEAT is available from the University of California, Berkeley, Calif.
2. 3D Database systems such as MACCS-3D (MDL Information Systems, San Leandro, Calif.). This area is reviewed in Martin (1992).
3. HOOK (available from Molecular Simulations, Burlington, Mass.).
Other molecular modeling techniques may also be employed in accordance with this invention, see, e.g., Cohen et al. (1990) and Navia & Murcko (1992).
There are two preferred approaches to designing a molecule, according to the present invention, that complement the stereochemistry of Aβ-IgNAR and Aβ monomer, dimer, or tetramer. The first approach is to in silico directly dock molecules from a three-dimensional structural database, to the interface site(s), using mostly, but not exclusively, geometric criteria to assess the goodness-of-fit of a particular molecule to the site. In this approach, the number of internal degrees of freedom (and the corresponding local minima in the molecular conformation space) is reduced by considering only the geometric (hard-sphere) interactions of two rigid bodies, where one body (the active site) contains “pockets” or “grooves” that form binding sites for the second body (the complementing molecule).
This approach is illustrated by Kuntz et al. (1982) and Ewing et al. (2001), the contents of which are hereby incorporated by reference, whose algorithm for ligand design is implemented in a commercial software package, DOCK version 4.0, distributed by the Regents of the University of California and further described in a document, provided by the distributor, which is entitled “Overview of the DOCK program suite” the contents of which are hereby incorporated by reference. Pursuant to the Kuntz algorithm, the shape of the interface represented by a site on the Aβ-IgNAR and Aβ monomer, dimer, or tetramer is defined as a series of overlapping spheres of different radii. One or more extant databases of crystallographic data, such as the Cambridge Structural Database System maintained by Cambridge University (University Chemical Laboratory, Lensfield Road, Cambridge, U.K.), the Protein Data Bank maintained by the Research Collaboratory for Structural Bioinformatics (Rutgers University, N.J., U.S.A.), LeadQuest (Tripos Associates, Inc., St. Louis, Mo.), Available Chemicals DXXXectory (Molecular Design Ltd., San Leandro, Calif.), and the NCI database (National Cancer Institute, U.S.A) is then searched for molecules which approximate the shape thus defined.
Molecules identified on the basis of geometric parameters, can then be modified to satisfy criteria associated with chemical complementarity, such as hydrogen bonding, ionic interactions and Van der Waals interactions. Different scoring functions can be employed to rank and select the best molecule from a database. See for example Bohm & Stahl (1999). The software package FlexX, marketed by Tripos Associates, Inc. (St. Louis, Mo.) is another program that can be used in this direct docking approach (see Rarey et al., 1996).
The second preferred approach entails an assessment of the interaction of respective chemical groups (“probes”) with the active site at sample positions within and around the site, resulting in an array of energy values from which three-dimensional contour surfaces at selected energy levels can be generated. The chemical-probe approach to ligand design is described, for example, by Goodford, (1985), the contents of which are hereby incorporated by reference, and is implemented in several commercial software packages, such as GRID (product of Molecular Discovery Ltd., West Way House, Elms Parade, Oxford OX2 9LL, U.K.).
Pursuant to this approach, the chemical prerequisites for a site-complementing molecule are identified at the outset, by probing the active site with different chemical probes, e.g., water, a methyl group, an amine nitrogen, a carboxyl oxygen, or a hydroxyl. Favoured sites for interaction between the active site and each probe are thus determined, and from the resulting three-dimensional pattern of such sites a putative complementary molecule can be generated. This may be done either by programs that can search three-dimensional databases to identify molecules incorporating desired pharmacophore patterns or by programs which use the favoured sites and probes as input to perform de novo design. Suitable programs for determining and designing pharmacophores include CATALYST (including HypoGen or HipHop) (Molecular Simulations, Inc), and CERIUS2, DISCO (Abbott Laboratories, Abbott Park, Ill.) and ChemDBS-3D (Chemical Design Ltd., Oxford, U.K.).
The pharmacophore can be used to screen in silico compound libraries/three-dimensional databases, using a program such as CATALYST (Molecular Simulations, Inc); MACCS-3D and ISIS/3D (Molecular Design Ltd., San Leandro, Calif.), ChemDBS-3D (Chemical Design Ltd., Oxford, U.K.), and Sybyl/3DB Unity (Tripos Associates, Inc., St. Louis, Mo.).
Databases of chemical structures are available from a number of sources including Cambridge Crystallographic Data Centre (Cambridge, U.K.), Molecular Design, Ltd., (San Leandro, Calif.), Tripos Associates, Inc. (St. Louis, Mo.), Chemical Abstracts Service (Columbus, Ohio), the Available Chemical DXXXectory (MDL Inc), the Derwent World Drug Index (WDI), BioByteMasterFile, the National Cancer Institute database (NCI), and the Maybridge catalogue.
De novo design programs include LUDI (Biosym Technologies Inc., San Diego, Calif.), Leapfrog (Tripos Associates, Inc.), Aladdin (Daylight Chemical Information Systems, Irvine, Calif.), and LigBuilder (Peking University, China).
Once an entity or compound has been designed or selected by the above methods, the efficiency with which that entity or compound may bind to Aβ-IgNAR and Aβ monomer, dimer, or tetramer can be tested and optimised by computational evaluation. An effective Aβ-IgNAR and Aβ monomer, dimer, or tetramer binding compound 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 Aβ-IgNAR and Aβ monomer, dimer, or tetramer binding compound should preferably be designed with a deformation energy of binding of not greater than about 10 kcal/mole, preferably, not greater than 7 kcal/mole. Binding compounds may interact with Aβ-IgNAR and Aβ monomer, dimer, or tetramer in more than one conformation that are 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 compound and the average energy of the conformations observed when the compound binds to the protein.
A compound designed or selected as binding to Aβ-IgNAR and Aβ monomer, dimer, or tetramer may be further computationally optimised so that in its bound state it would preferably lack repulsive electrostatic interaction with the target protein. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the compound and the protein when the compound is bound to Aβ-IgNAR and Aβ monomer, dimer, or tetramer, preferably make a neutral or favourable contribution to the enthalpy of binding.
Once an Aβ-IgNAR and Aβ monomer, dimer, or tetramer-binding compound has been optimally selected or designed, as described above, substitutions may then be made in some of its atoms or side groups to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation should be avoided. Such substituted chemical compounds may then be analysed for efficiency of fit to Aβ-IgNAR and Aβ monomer, dimer, or tetramer by the same computer methods described in detail above.
Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include: Gaussian 92, revision C (Frisch, Gaussian, Inc., Pittsburgh, Pa.); AMBER, version 4.0 (Kollman, University of California at San Francisco); QUANTA/CHARMM (Molecular Simulations, Inc., Burlington, Mass.); and Insight II/Discover (Biosysm Technologies Inc., San Diego, Calif.).
The screening/design methods may be implemented in hardware or software, or a combination of both. However, preferably, the methods are implemented in computer programs executing on programmable computers each comprising a processor, a data storage system (including volatile and non-volatile memory and/or storage elements), at least one input device, and at least one output device. Program code is applied to input data to perform the functions described above and generate output information. The output information is applied to one or more output devices, in known fashion. The computer may be, for example, a personal computer, microcomputer, or workstation of conventional design.
Each program is preferably implemented in a high level procedural or object-oriented programming language to communicate with a computer system. However, the programs can be implemented in assembly or machine language, if desired. In any case, the language may be compiled or interpreted language.
Each such computer program is preferably stored on a storage medium or device (e.g., ROM or magnetic diskette) readable by a general or special purpose programmable computer, for configuring and operating the computer when the storage media or device is read by the computer to perform the procedures described herein. The system may also be considered to be implemented as a computer-readable storage medium, configured with a computer program, where the storage medium so configured causes a computer to operate in a specific and predefined manner to perform the functions described herein.
Screening Assays and Confirmation of Binding and Biological Activity
Compounds selected or designed in accordance with the in silico methods of the invention may be subjected to further confirmation of binding to Aβ-IgNAR and Aβ monomer, dimer, or tetramer by cocrystallization of the compound with Aβ-IgNAR and Aβ monomer, dimer, or tetramer and structural determination, as described herein.
Libraries may be screened in solution by methods generally known in the art for determining whether ligands competitively bind at a common site. Such methods may include screening libraries in solution (e.g.; Houghten, 1992), or on beads (Lam, 1991), chips (Fodor, 1993), bacteria or spores (U.S. Pat. No. 5,223,409: Lardner), plasmids (Cull et al., 1992), or on phage (Scott & Smith, 1990; Devlin, 1990; CwXXXla et al., 1990; Felici, 1991; U.S. Pat. No. 5,223,409: Lardner).
Where the screening assay is a binding assay, Aβ-IgNAR and Aβ monomer, dimer, or tetramer may be joined to a label, where the label can directly or indirectly provide a detectable signal. Various labels include radioisotopes, fluorescent molecules, chemiluminescent molecules, enzymes, specific binding molecules, particles, e.g., magnetic particles, and the like. Specific binding molecules include pairs, such as biotin and streptavidin, digoxin and antidigoxin, etc. For the specific binding members, the complementary member would normally be labeled with a molecule that provides for detection, in accordance with known procedures.
A variety of other reagents may be included in the screening assay. These include reagents like salts, neutral proteins, e.g., albumin, detergents, etc., which are used to facilitate optimal protein-protein binding and/or reduce non-specific or background interactions. Reagents that improve the efficiency of the assay, such as protease inhibitors, nuclease inhibitors, antimicrobial agents, etc., may be used. The components are added in any order that produces the requisite binding. Incubations are performed at any temperature that facilitates optimal activity, typically between 4 and 40° C.
The Aβ-IgNAR molecule may be used in its own right as a sink or tool to mop up oligomers both in vivo and in vitro ie as a therapeutic.
The Aβ-IgNAR molecule of the present invention may also be used as an antigen to raise antibodies against Aβ.
In a fifteenth aspect the present invention provides the use of an Aβ-IgNAR molecule of any one SEQ ID NOs 2, 4, 5, 6, 13, 15, 16, 17 or 18 to raise antibodies against Aβ wherein the antibodies bind to residues 18 to 41 of SEQ ID NO 1 when presented in the Aβ-IgNAR molecule of any one of SEQ ID NOs 2, 4, 5, 6, 15, 16, 17 or 18 but not to an isolated linear peptide having a sequence of residues 18 to 41 of SEQ ID NO 1.
In a sixteenth aspect the present invention provides an antibody which specifically binds to residues antibodies bind to residues 18 to 41 of SEQ ID NO 1 when presented in the Aβ-IgNAR molecule of any one of SEQ ID NOs 2, 4, 5, 6, 13, 15, 16, 17 or 18 but not to an isolated linear peptide having a sequence of residues 18 to 41 of SEQ ID NO 1.
In a preferred embodiment the antibody is a monoclonal antibody.
As will be understood by persons skilled in the art the antibodies of the present invention are directed to conformational epitopes of 18-41 of Aβ which are presented when Aβ 18-41 is positioned within the Aβ-IgNAR molecule. Such conformational epitopes will not be present in the isolated linear Aβ 18-41 peptide.
In addition to therapeutic uses the antibodies of the present invention may also be used in diagnostic assays to detect the presence of Aβ dimers in biological samples in particular blood and CSF. In this regard the biological sample is contacted with the antibody and the level of binding assessed.
Throughout this specification the word “comprise”, or variations such as “comprises” or “comprising”, will be understood to imply the inclusion of a stated element, integer or step, or group of elements, integers or steps, but not the exclusion of any other element, integer or step, or group of elements, integers or steps.
All publications mentioned in this specification are herein incorporated by reference. Any discussion of documents, acts, materials, devices, articles or the like which has been included in the present specification is solely for the purpose of providing a context for the present invention. It is not to be taken as an admission that any or all of these matters form part of the prior art base or were common general knowledge in the field relevant to the present invention as it existed in Australia or elsewhere before the priority date of each claim of this application.
In order that the nature of the present invention may be more clearly understood, preferred forms thereof will now be described with reference to the following non-limiting examples.
EXAMPLE 1
Methods Summary
Construction of Aβ-IgNAR chimeras. Aβ-IgNAR-G1/G3/G6 and G1-Leu34Pro coding sequences were constructed by splice-overlap PCR using IgNAR 12Y-2 DNA template (Nuttall, Humberstone et al. 2004), cloned into E. coli periplasmic expression vector pGC, and verified by DNA sequencing.
Protein purification and crystallization. Recombinant proteins were expressed into the E. coli periplasmic space, purified by affinity chromatography through an anti-FLAG Ig/Sepharose column equilibrated in TBS, and collected as single peaks by gel filtration. Proteins ( ̃4-5 mg/ml in 20 mM Tris.HCl, pH 8.0) were set up as 0.4 μl sitting drops. Aβ-IgNAR-G1 (SEQ ID NO: 2) crystallised under a wide range of conditions (biased towards PEG 6000; PEG 3350; and PEG MME 2000 at neutral pH). Final crystallisation conditions were 0.2 M ammonium chloride, 20% polyethylene glycol (PEG) 6000, 0.1 M MES pH 6, with diffraction quality crystals (Space Group P32 and cell parameters a=b=79.40, c=84.89 Å) obtained after 9 days. No crystals were obtained for Aβ-IgNAR-G3 (SEQ ID NO: 4) or Aβ-IgNAR-G6 (SEQ ID NO: 5).
Structure determination. A full data set (93% completeness) was collected at the Australian Synchrotron 3-BM1 beam line to 2.2 Å resolution. Data were collected at −160° C. and processed using the HKL2000 suite (Otwinowski and Minor 1997). Diffraction data statistics are summarized in Table 1. The structure was solved by molecular replacement MOLREP (Vagin and Teplyakov 1997) using IgNAR 12Y-2 (PDB 1VES) minus CDR3 region as search template. Four independent molecules (A, B, C and D) were found in the asymmetric unit. The final refinement converged to R/Rfree values of 0.164/0.246. In total, 97.8% residues are in the most favoured regions of the Ramachandran plot, with 1.6% residues in the additionally allowed regions.







TABLE 1





X-ray refinement statistics


















Resolution (Å)
26.17-2.20



Rwork/Rfree
16.4/24.6



Number of




Protein amino acids
503



Water
394



B-factors




Overall
46.5



Protein
46.0



Water
51.7



R.m.s deviations




Bond lengths (Å)
0.019



Bond angles (°)
1.958










Results

The crystallographic structures of the IgNAR single variable domain antibody 12Y-2(Streltsov, Varghese et al. 2004) (PDB: 1VES) reveal self-stabilized extended β-hairpin CDR3 loop regions. We hypothesized that engineering the amyloidogenic component of Aβ peptide (residues Val17-Ala42) within this loop would (1) allow formation of an amyloid protofilament structure; while (2) preventing uncontrolled fibril formation and polymerisation by trapping the amyloid moiety in a cage of IgNAR domains that are amenable to crystallization. Three chimeric proteins were modelled based on existing NMR β-hairpin models of amyloid plaques (Luhrs, Ritter et al. 2005), incorporating variable N- and C-terminal glycine linkers to allow in-register transition from the immunoglobulin framework β-sheets to the Aβ peptide. These constructs, designated Aβ-IgNAR-G1 (SEQ ID NO. 2); Aβ-IgNAR-G3 (SEQ ID NO. 4); and Aβ-IgNAR-G6 (SEQ ID NO. 5), were expressed as recombinant proteins in E. coli and tested for oligomer formation. SDS and β-mercaptoethanol-stable dimers were observed in the bacterial periplasmic space by Western blot for all three chimeric proteins but not the unmodified IgNAR. The greater conformational flexibility for the glycine-3 and glycine-6 versions appeared to allow more rapid dimer formation, and protein induction at higher temperature tended to promote a higher dimer:monomer ratio. Upon affinity purification all 3 variants behaved as dimers, rather than the monomer observed for the wild type IgNAR, and tetrameric species were also apparent. (FIGS. 2a and 2b). Trigonal crystals of Aβ-IgNAR-G1 (SEQ ID NO: 2), but not the other two chimeric proteins, grew under a variety of conditions and diffracted to 2.2 Å resolution. The structure was solved by molecular replacement using IgNAR 12Y-2 (SEQ ID NO: 3) with removed CDR3 region as the search model, and refinement completed with R/Rfree factors of 16.4/24.6% (Table 1). Representative regions of electron density are shown in FIG. 3.
The Aβ-IgNAR-G1 (SEQ ID NO: 2) quaternary structure consists of four independent molecules (A, B, C and D) in the asymmetric unit (FIG. 4), which form a tight tetramer (dimer of dimers) through interactions predominantly mediated by the Aβ peptide component. The inter-chain association for each dimer (A-C and B-D) is extremely robust, as indicated by an average surface of interaction (buried surface) of 580 Å2 and an average shape correlation statistic (Lawrence and Colman 1993) (Sc)=0.64 (Tables 2 & 3). The dimer-dimer interaction (AC-BD) which forms the crystallographic tetramer is somewhat less extensive (buried surface of 546 Å2). The underlying IgNAR scaffold monomers are very closely overlaid with each-other and with the previously described 12Y-2 structure.







TABLE 2







Aβ-IgNAR-G1 buried surface areas1.














Chain
A
B
C
D
Total2







A
—
215.7
589.0
290.8
1095.5



B
215.7
—
254.9
563.8
1034.4



C
578.2
250.2
—
215.8
1044.2



D
296.5
569.6
221.5
—
1087.6



Average




1065.4







1For Aβ regions only.



2Area excluded on first molecule due to interaction with second (in Angstroms squared). Calculated using point density = 10 points/square Å; Probe sphere radius = 1.7 Å.













TABLE 3







Aβ-IgNAR-G1 shape complementarity statistics 1.











Sc
A
B
C
D














A
1
0.590
0.709
0.786


B

1
0.742
0.567


C


1
0.717


D



1





1Calculated using the Sc program with a 1.7 Å probe radius.






The Aβ-IgNAR-G1 structure reveals the Aβ peptide region (Val18-Ile41) as comprising two adjacent and connected loop motifs, rather than the expected extended β-hairpin structure. The first motif consists of residues Val18-Ile31 which adopt a 10-11 Å wide β-α structure, stabilised by intra-molecular and inter-molecular contacts and consisting of one β strand (Val18-Ala21) plus a 310-helical turn (Val24-Ser26)(chains A) and similar but distorted helix in chain B or an extended loop (chains C and D). The second motif consists of residues Ile32-Ile41 and is a β-hairpin consisting of two anti-parallel β-strands which form a 3-strand β-sheet with the parallel β-strand of the first loop motif. The overlaid Aβ loops have an average r.m.s.d.=1.19 Å2, and as can be seen from FIG. 2d the greatest divergence occurs between residues Val24-Asn27, where chains A and B adopt a different conformation from chains C and D. Consequently, for the A/B chain conformations the Lys28 side-chain is directed out of the plane of the loop and forms intramolecular contacts with Val24 (2.6 Å) and Asn27 (3.6 Å) (chain A) and helps maintain the helical conformation of Val24-Ser26. In contrast, for the C/D chains the Lys28 side chain is now directed internally and forms two intra-molecular contacts with the carbonyl oxygens of Asp23 (3.0 and 3.5 Å) and Ser26 (4.0 and 3.0 Å) and two inter-molecular contacts with carbonyl oxygens of chain A/B: Gly29 (2.6 and 3.3 Å) and Asn27 (2.8 and 3.6 Å). The transition between the two states for Lys28 appears pivotal to crystallisation, and may represent a vital mechanism (and energy minimum) for Aβ oligomer formation. In NMR-based structures of amyloid plaques, residues Leu17-Ala42 form parallel, in-register β-sheets (Petkova, Ishii et al. 2002; Luhrs, Ritter et al. 2005; Sato, Kienlen-Campard et al. 2006), with Lys28 facing outward in the first Aβ chain of the adjacently stacked peptides, while subsequent Aβ peptides have the Lys28 side-chain directed internally and forming intermolecular contacts (salt bridges) with residue Asp23 (Luhrs, Ritter et al. 2005; Petkova, Yau et al. 2006; Sato, Kienlen-Campard et al. 2006). Thus our structure is consistent with NMR data for this position.
Overall, the dimers (AC and BD), each related by an pseudo 2-fold axis running through the long axis of the tetramer, are stabilized around the Asp23-Ala30 loop by the carbonyl oxygen charges neutralizing the buried Lys28 amide group and by the amide group of Asp27 forming a hydrogen bonding network with the neighbouring dimer's carbonyl oxygen of Gly29 and carboxy oxygen of Asp27. The surface towards the tetramer interface is stabilized by the hydrophobic residues Ile31, Val40, and Leu34. The tetramer interface is stabilized by two 3-stranded β-sheets of the monomer forming a single 6-stranded β-sheet with a pseudo-2-fold axis running perpendicular to and through the centroid of the extended β-sheets. The Leu34 side-chains face each other: two from each side of the tetramer, rotated by  ̃90° (see later). Similarly, the respective Met35 side-chains are surrounded by hydrophobic residues Ile32, Val39 and Ile41. Intermolecular contacts seen by NMR such as Ala21/Val36 (Luhrs, Ritter et al. 2005) and Ile32/Leu34/Val36 (Petkova, Yau et al. 2006) are also observed for this motif. An earlier crystallographic structure of Aβ(28-42) fused C-terminally to Tk-RNase HII (Takano, Endo et al. 2006) also suggested formation of a limited β-hairpin conformation which partially overlaps with the Aβ-IgNAR-G1 β-hairpin motif (r.m.s.d.=1.9 Å for 13 atoms).
The tetrameric structure displays features described for various models of both Aβ protofilaments (Malinchik, Inouye et al. 1998; Losic, Martin et al. 2006) and soluble globulomers(Barghorn, Nimmrich et al. 2005) and shows strong correlation with other independently obtained structural data for Aβ fragments and fibrils(Rahimi, Shanmugam et al. 2008). The top and bottom of the tetramer is covered by a contiguous hydrophobic surface with a girdle of hydrophilic residues) (22EDVGSNKGA30) (SEQ ID NO:25) running along the sides. The wedged-shape interface visible in our structure also suggest a possible mechanism for membrane-spanning pore formation(Jang, Zheng et al. 2008). Thus, we hypothesised that the observed dimer or tetramer may be a common structural motif in Aβ oligomerization, and modelled the Aβ tetramers minus the IgNAR domain as a building block of high order oligomers. By aligning Aβ tetramers on top of each other along the polar axis, utilising the interaction pattern observed between parallel Aβ stacks by NMR structure(Petkova, Yau et al. 2006), a series of multimeric constructs were generated (FIG. 5a-c). Sequential tetramers in this model are rotated by  ̃30° along the oligomer axis creating a twisted (coiled) cylinder up to  ̃40 Å wide. While the N-terminal residue Val18 appears to be too close to the next tetramer in this configuration, this probably results from constraints imposed by the IgNAR scaffold, which would be absent in a soluble oligomeric form. Adding N-terminal Aβ peptides residues Ala1-Lys16, as described by XAFS data(Streltsov 2008), onto the crystallographic tetramer results in a model whereby this unstructured metal-binding fragment is ideally oriented to mediate reactive oxygen species toxicity. Mechanistically, neighbouring tetramers as shown in FIG. 3a-c align Glu22 and Asp23 side chains (from different tetramers) to form a belt of 4 potential metal-binding sites (Glu22-G1u22=10-12 Å; Asp23-Asp23=5.5-7 Å). With contributions from oxygen and nitrogens atoms this may conceivably produce one additional low affinity binding site per Ap monomer in the aggregate. Upon metal binding to the Aβ N-terminus (Asp1; Glu11; His6; His13; His14), the adjacent Val 18-Ala21 fragment should be stabilized, facilitating tetramer-tetramer interactions and accelerating oligomer (fibril) growth.
Familial and in vitro-generated mutations represent valuable tools for dissecting Aβ peptide function. For example the major pathogenic familial Aβ mutations (Walsh 2005), i.e. Ala21Gly (Flemish), Glu22Gly (Arctic), Glu22Lys (Italian) and Asp23Asn (Iowa) are localized within a β-turn stabilized by hydrogen bonds between Asp23 (OD1) and Ser26 (OG) (2.8 Å), and Asp23 (OD2) and Gly25 (N) (3.4 Å). Interactions with Phe20 also appear important for loop stability: Asp23 (OD1) is at 2.6 Å from an intra-loop water molecule which is at 3.1 Å from Phe20 (N), an interaction which FAD mutation Asp23 Asn is predicted break. Similarly, the “Wurth” mutations (Wurth, Guimard et al. 2002), derived in vitro from studies of the folding of Aβ(1-42)-GFP fusions (Wurth, Guimard et al. 2002), signpost residues important in aggregation. These mutations map into the surface residues of the monomer that interfere with formation of the dimer or tetramer interfaces and the amylogenic surface. For example mutation Leu34Pro is described to markedly decrease Aβ aggregation, both alone and in combination with other variants. Here, the four Leu34 side-chains form a universal type joint, leading to our prediction that a Leu34Pro substitution would here (1) disrupts the central hydrophobic core of the tetramer; and (2) break the β-sheets formed by residues Ile32-Val36 between adjacent dimers. To test this theory, we produced the variant Aβ-IgNAR-G1 (Leu34Pro) (SEQ ID NO. 7) and assessed the affect of this change on dimerisation. We observed marked reversion to monomeric form, of similar magnitude ( ̃30%) to that originally described for this mutation in vitro (Wurth, Guimard et al. 2002). Upon affinity purification, this variant tended toward dimerisation, but in contrast to the parental Aβ-IgNAR-G1 was not resistant to β-mercaptoethanol treatment and failed to crystallise, suggesting that the tetramer interface had indeed been compromised.
The mechanistic basis of Aβ-mediated toxicity remains controversial and unresolved. Currently popular candidate mechanisms include: neuronal damage mediated by reactive oxygen species (ROS)(Bush 2000; Streltsov 2008); membrane destabilisation and/or pore formation (Jang, Zheng et al. 2008); and activation or modification of the apotopic pathway (Culmsee and Landshamer 2006). Most probably the final disease aetiology will prove to be multi-factorial. By developing a crystallographic model for amyloidogenic Aβ, we hoped to devise a system to test such hypotheses. Surprisingly, our structures revealed not the expected β-turn-βextended loop, but rather an unusual and compact four-lobed cloverleaf structure, which may prove to be the proto-oligomeric building block. To the best of our knowledge, this “cloverleaf” model is the first full x-ray crystallographic structure of the amyloidogenic component of the Aβ peptide.
Simplistically, our structure can be envisaged as presenting three aspects, which we describe as the dimer interface, the tetramer interface, and the amyloid-extension face. Each potentially represents a viable target for interventionist agents aimed at disrupting oligomer formation and toxic activity. Such moieties may extend beyond imaging agents to novel chemical and biological entities, including chemical compounds and peptidomimetic constructs. In this sense, we believe our structure represents a possible novel paradigm for Aβ folding, which will engender testable hypotheses for the protein folding and toxicity of this medically important peptide and its associated forms.
EXAMPLE 2
Familial Mutations
A series of variants for Aβ-IgNAR-G1 were produced (Table 4), with the aim of determining the affect of so-called “familial mutations” upon the Aβ-IgNAR-G1 structure. All these mutation map to residues 21-23. All variants displayed the characteristic Aβ dimerization predicted from the structure.












TABLE 4





Protein
Description
Mutation
MW (Da)
Tag
SEQ ID NO:




















35A-1
Aβ-IgNAR
—
15,654
FLAG × 2
2


12Y-2
IgNAR wt
—
14,878
FLAG × 2
3


37A-1
Aβ-IgNAR
Gly3
15,953
FLAG × 2
4


37Q-6
Aβ-IgNAR
Gly6
16,123
FLAG × 2
5


37P-3
Aβ-IgNAR
Gly2
15,768
FLAG × 2
6


37D-4
Aβ-IgNAR
Leu34Pro
15,638
FLAG × 2
7


37F-2
Aβ-IgNAR
Asp23Asn
15,653
FLAG × 2
8


37K-1
Aβ-IgNAR
Glu22Gln
15,653
FLAG × 2
9


37L-2
Aβ-IgNAR
Ala21Gly
15,640
FLAG × 2
10


37R-1
Aβ-IgNAR
ΔGlu22
15,525
FLAG × 2
11


37M-4
Aβ-IgNAR
Ser26Cys
15,670
FLAG × 2
12


37V-2
Aβ-IgNAR
—
14,345
His
13


37Y-1
IgNAR wt
—
13,553
His
14









A Western blot showed the characteristic dimerization for the familial mutants compared to wild type Aβ-IgNAR-G1 (35A-1) and the non-dimerizing wild type IgNAR (12Y-2) and “Wurth” mutant 37D-4. Familial mutants of Aβ-IgNAR-G1 reveal the presence of dimeric species at  ̃30 kDa, in contrast to the wild type IgNAR (12Y-2) and the mutant Leu34Pro (37D-4)
EXAMPLE 3
In Silico Screening
The crystallographic structure co-ordinates were taken and screened in silico against a database of compounds.
The crystal structure of the tetramer was examined disregarding the IgNAR domains. A site (cavity) on the ‘amyloidogenic’ surface, bounded by residues (chain B and chain C and Aβ amino acid residue number within these chains) B18, B32, B33, B34, B35, B41, C18, C32, C33, C34, C35, and C41 was selected as the target for docking molecules from the chemical database. The ‘Clean lead-like’ subset (approx. 1136000 compounds) from the ZINC database (http://zinc.docking.org; J. J. Irwin and B. K. Shoichet, J. Chem. Inf. Model, (2005), 45, 177-182) was used for the virtual screening or docking.
First, the program DOCK v. 6.2 (Univ. of California at San Francisco, USA; T. J. A. Ewing et al., J. Comput.-Aided Molec. Design, (2001), 15, 411-428.) was used to dock a segment of approx. 25000 compounds (molecules) from the database to the selected docking site on the tetramer surface. The force-field grid energy (sum of van der Waals and Coulomb energies) was used as the primary scoring function while the Zou GB/SA score (H-Y. Liu et al., J. Phys. Chem. B, (2004), 108, 5453-5462)) was used as the secondary scoring function. The DOCK output .mol2 files for each compound, giving the scores (energies) and the docked poses, were then processed by the program Binding Response (S. Zhong and A. D. MacKerell, J. Chem. Inf. Model., (2007), 47, 2302-2315) to obtain n, the number of docked molecule atoms enclosed by the docking site. Sorting the output, a total of 361 compounds were chosen for the second stage of virtual screening on the basis of the highest grid score, GB/SA score, and n.
The second stage of virtual screening was done with the program Surflex-Dock v.2.3 (A. N. Jain, J. Comput.-Aided Mol. Design, (2007), 21, 281-306), within Sybyl v.8.1 (Tripos Inc., St. Louis, USA). In docking with this program, the GeomX docking option was used with the number of additional starting conformations per molecule increased to 10 and the soft grid treatment turned off. From the docked poses, the top scoring molecules (Total score greater than 4.0, ‘Crash’ component of the score greater than −1.0) were visually examined and 6 compounds available from ChemBridge Corp. (San Diego, USA) were selected for purchase. These compounds are set out in Table 5.









TABLE 5





Compound 

Molecular 


ID
Molecular Name
Weight







7996209
N-[2-(4-methylphenyl)-2-oxoethyl]-
323.3



1-oxo-3,4-dihydro-1H-isochromene-




3-carboxamide



7780327
2-methyl-3-{[(3-
299.2



methylphenoxy)acetyl]amino}benzoic




acid



7302096
3-{[(2,5-dimethoxyphenyl)
319.3



amino]carbony1}-7-




oxabicyclo[2.2.1]hept-5-ene-2-




carboxylic acid



5785027
2-{2-[(2-hydroxyethyl)amino]-1H-
426.3



benzimidazol-1-yl}-1-(1-




naphthyl)ethanone hydrobromide



9124833
3-methoxy-4-[2-(4-morpholinyl)-2-
266.3



oxoethoxy]aniline



7949851
methyl [3-(phenoxyacetyl)-1H-indol-
323.3



1-yl]acetate









Illustrations of these compounds binding to Ab-IgNAR structure are shown in FIGS. 6 to 11.
These 6 compounds were purchased and tested for binding to the Aβ-IgNAR-G1 dimer and IgNAR alone by BIAcore biosensor. No binding definitively above background was observed, perhaps due to the interface targeted ie dimer immobilized, but the cavity targeted was formed by the dimer-tetramer interface.
By way of comparison, docking performed for the anti-inflammatory drug fenofibrate which has been shown to bind Aβ (Kukar et al. Nature 453, 925-929 (2008) Substrate-targeting -secretase modulators). Docking experiments performed using the structure and a possible modelled solution presented in FIG. 12. No biochemical data for fenofibrate as soaking into crystals cracked the protein crystals, and the insolubility of fenofibrate precluded definitive biosensor experimentation.
It will be appreciated by persons skilled in the art that numerous variations and/or modifications may be made to the invention as shown in the specific embodiments without departing from the spirit or scope of the invention as broadly described. The present embodiments are, therefore, to be considered in all respects as illustrative and not restrictive.
References


    Barghorn, S., V. Nimmrich, et al. (2005). “Globular amyloid b-peptide oligomer—a homogenous and stable neuropathological protein in Alzheimer's disease.” J. Neurochem. 95β): 834-847.
    Bush, A. I. (2000). “Metals and neuroscience.” Curr Opin Chem Biol 4(2): 184-191.
    Crouch, P. J., S.-M. E. Harding, et al. (2008). “Mechanisms of Ab mediated neurodegeneration in Alzheimer's disease.” Int J Biochem Cell Biol 40(2): 181-198.
    Culmsee, C. and S. Landshamer (2006). “Molecular insights into mechanisms of the cell death program: role in the progression of neurodegenerative disorders.” Curr Alzheimer Res 3(4): 269-83.
    Henderson, K. A., V. A. Streltsov, et al. (2007). “Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition.” Structure 15(11): 1452-66.
    Jang, H., J. Zheng, et al. (2008). “New structures help the modeling of toxic amyloidbeta ion channels.” Trends Biochem Sci 33(2): 91-100.
    Kajava, A. V., J. M. Squire, et al. (2006). “b-structures in fibrous proteins.” Adv Protein Chem 73: 1-15.
    Lawrence, M. C. and P. M. Colman (1993). “Shape complementarity at protein/protein interfaces.” J Mol Biol 234(4): 946-950.
    Losic, D., L. L. Martin, et al. (2006). “High resolution scanning tunnelling microscopy of the b-amyloid protein (Ab1-40) of Alzheimer's disease suggests a novel mechanism of oligomer assembly.” Journal of Structural Biology 155(1): 104-110.
    Luhrs, T., C. Ritter, et al. (2005). “3D structure of Alzheimer's amyloid-b(1-42) fibrils.” Proc Natl Acad Sci USA 102(48): 17342-17347.
    Malinchik, S. B., H. Inouye, et al. (1998). “Structural analysis of Alzheimer's b(1-40) amyloid: protofilament assembly of tubular fibrils.” Biophys. J. 74(1): 537-745.
    Nelson, R. and D. Eisenberg (2006). “Recent atomic models of amyloid fibril structure.” Curr Opin Struct Biol 16(2): 260-265.
    Nelson, R. and D. Eisenberg (2006). “Structural models of amyloid-like fibrils.” Adv Protein Chem 73: 235-282.
    Nuttall, S. D., K. S. Humberstone, et al. (2004). “Selection and affinity maturation of IgNAR variable domains targeting Plasmodium falciparum AMA1.” Proteins 55(1): 187-97.
    Otwinowski, Z. and W. Minor (1997). “Processing of X-ray Diffraction Data Collected in Oscillation Mode.” Methods in Enzymology: 307-326.
    Petkova, A. T., Y. Ishii, et al. (2002). “A structural model for Alzheimer's b-amyloid fibrils based on experimental constraints from solid state NMR.” Proc Natl Acad Sci USA 99(26): 16742-16747.
    Petkova, A. T., W. M. Yau, et al. (2006). “Experimental constraints on quaternary structure in Alzheimer's b-amyloid fibrils.” Biochemistry 45(2): 498-512.
    Rahimi, F., A. Shanmugam, et al. (2008). “Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders.” Curr Alzheimer Res 5β): 319-41.
    Sato, T., P. Kienlen-Campard, et al. (2006). “Inhibitors of amyloid toxicity based on b-sheet packing of Ab40 and Ab42.” Biochemistry 45(17): 5503-5516.
    Shankar, G. M., S. Li, et al. (2008). “Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory.” Nat. Med. 
    Streltsov, V. (2008). “X-ray absorption and diffraction studies of the metal binding sites in amyloid b-peptide.” Eur Biophys J 37β): 257-263.
    Streltsov, V. A., J. N. Varghese, et al. (2004). “Structural evidence for evolution of shark Ig new antigen receptor variable domain antibodies from a cell-surface receptor.” Proc Natl Acad Sci USA 101(34): 12444-12449.
    Takano, K., S. Endo, et al. (2006). “Structure of amyloid-b fragments in aqueous environments.” Febs J 273(1): 150-158.
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    Walsh, D. M. (2005). “Disease-associated intra-Ab mutations.” Alzheimer Research Forum: Available at: http://www.alzgene.org.
    Walsh, D. M. and D. J. Selkoe (2007). “Ab oligomers—a decade of discovery.” J. Neurochem. 101(5): 1172-1184.
    Wurth, C., N. K. Guimard, et al. (2002). “Mutations that reduce aggregation of the Alzheimer's Ab42 peptide: an unbiased search for the sequence determinants of Ab amyloidogenesis.” J Mol Biol 319(5): 1279-1290.










APPENDIX I







HEADER
Ab-IgNAR









REMARK
3



REMARK
3
 REFINEMENT.










REMARK
3
 PROGRAM:
REFMAC 5.3.0040


REMARK
3









REMARK
3
  REFINEMENT TARGET:  MAXIMUM LIKELIHOOD


REMARK
3


REMARK
3
 DATA USED IN REFINEMENT.











REMARK
3
 RESOLUTION RANGE HIGH
(ANGSTROMS):
 2.20


REMARK
3
 RESOLUTION RANGE LOW
(ANGSTROMS):
 68.84












REMARK
3
 DATA CUTOFF
(SIGMA(F)):
NONE












REMARK
3
 COMPLETENESS FOR RANGE
(%):
 93.45










REMARK
3
 NUMBER OF REFLECTIONS:
 26860


REMARK
3









REMARK
3
 FIT TO DATA USED IN REFINEMENT.










REMARK
3
 CROSS-VALIDATION METHOD:
THROUGHOUT


REMARK
3
 FREE R VALUE TEST SET SELECTION:
RANDOM











REMARK
3
 R VALUE
(WORKING + TEST SET):
0.16841











REMARK
3
 R VALUE
(WORKING SET):
 0.16431










REMARK
3
 FREE R VALUE:
 0.24650











REMARK
3
 FREE R VALUE TEST SET SIZE
(%):
 5.1










REMARK
3
 FREE R VALUE TEST SET COUNT:
 1439


REMARK
3









REMARK
3
 FIT IN THE HIGHEST RESOLUTION BIN.










REMARK
3
 TOTAL NUMBER OF BINS USED:
    20


REMARK
3
 BIN RESOLUTION RANGE HIGH:
  2.202


REMARK
3
 BIN RESOLUTION RANGE LOW:
  2.260











REMARK
3
 REFLECTION IN BIN
(WORKING SET):
   1219












REMARK
3
 BIN COMPLETENESS
(WORKING + TEST) 
(%):
  56.98











REMARK
3
 BIN R VALUE
(WORKING SET):
  0.229










REMARK
3
 BIN FREE R VALUE SET COUNT:
     55










REMARK
3
 BIN FREE R VALUE:
  0.307


REMARK
3









REMARK
3
 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.










REMARK
3
 ALL ATOMS:
   4173


REMARK
3


REMARK
3
 B VALUES.











REMARK
3
 FROM WILSON PLOT
(A**2):
NULL











REMARK
3
 MEAN B VALUE
(OVERALL, A**2):
 46.544









REMARK
3
 OVERALL ANISOTROPIC B VALUE.











REMARK
3
  B11 (A**2):
0.05



REMARK
3
  B22 (A**2):
0.05


REMARK
3
  B33 (A**2):
−0.08


REMARK
3
  B12 (A**2):
0.03


REMARK
3
  B13 (A**2):
0.00


REMARK
3
  B23 (A**2):
0.00


REMARK
3









REMARK
3
 ESTIMATED OVERALL COORDINATE ERROR.











REMARK
3
 ESU BASED ON R VALUE
(A):
 0.241


REMARK
3
 ESU BASED ON FREE R VALUE
(A):
 0.223











REMARK
3
 ESU BASED ON MAXIMUM LIKELIHOOD
  (A):
 0.152











REMARK
3
 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD
(A**2):
 11.557


REMARK
3










REMARK
3
CORRELATION COEFFICIENTS.



REMARK
3
 CORRELATION COEFFICIENT FO-FC:
 0.968


REMARK
3
 CORRELATION COEFFICIENT FO-FC FREE:
 0.930


REMARK
3













REMARK
3
 RMS DEVIATIONS FROM IDEAL VALUES

COUNT
RMS
WEIGHT


REMARK
3
 BOND LENGTHS REFINED ATOMS
(A):
3835 ;
0.022 ;
 0.022


REMARK
3
 BOND ANGLES REFINED ATOMS
(DEGREES):
5173 ;
1.994 ;
 1.953


REMARK
3
 TORSION ANGLES, PERIOD 1
(DEGREES):
499 ;
7.067 ;
 5.000


REMARK
3
 TORSION ANGLES, PERIOD 2
(DEGREES):
152 ;
35.901 ;
23.947


REMARK
3
 TORSION ANGLES, PERIOD 3
(DEGREES):
664 ;
21.119 ;
15.000


REMARK
3
 TORSION ANGLES, PERIOD 4
(DEGREES):
24 ;
14.991 ;
15.000


REMARK
3
 CHIRAL-CENTER RESTRAINTS
(A**3):
591 ;
0.179 ;
 0.200


REMARK
3
 GENERAL PLANES REFINED ATOMS
(A):
2832 ;
0.008 ;
 0.020


REMARK
3
 NON-BONDED CONTACTS REFINED ATOMS
(A):
1537 ;
0.228 ;
 0.200


REMARK
3
 NON-BONDED TORSION REFINED ATOMS
(A):
2516 ;
0.311 ;
 0.200


REMARK
3
 H-BOND (X . . . Y) REFINED ATOMS
(A):
292 ;
0.240 ;
 0.200


REMARK
3
 SYMMETRY VDW REFINED ATOMS
(A):
52 ;
0.222 ;
 0.200


REMARK
3
 SYMMETRY H-BOND REFINED ATOMS
(A):
22 ;
0.298 ;
 0.200


REMARK
3


REMARK
3
 ISOTROPIC THERMAL FACTOR RESTRAINTS.

COUNT
RMS
WEIGHT


REMARK
3
 MAIN-CHAIN BOND REFINED ATOMS
(A**2):
2501 ;
1.051 ;
 1.500


REMARK
3
 MAIN-CHAIN ANGLE REFINED ATOMS
(A**2):
3921 ;
1.795 ;
 2.000


REMARK
3
 SIDE-CHAIN BOND REFINED ATOMS
(A**2):
1515 ;
3.032 ;
 3.000


REMARK
3
 SIDE-CHAIN ANGLE REFINED ATOMS
(A**2):
1252 ;
4.656 ;
 4.500


REMARK
3


REMARK
3
 NCS RESTRAINTS STATISTICS


REMARK
3
 NUMBER OF NCS GROUPS: NULL


REMARK
3


REMARK
3
 TLS DETAILS


REMARK
3
 NUMBER OF TLS GROUPS:    4









REMARK
3
 ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY


REMARK
3


REMARK
3
 TLS GROUP:   1


REMARK
3
  NUMBER OF COMPONENTS GROUP:  1













REMARK
3
  COMPONENTS
C SSSEQI
 TO C
SSSEQI



REMARK
3
  RESIDUE RANGE:
A
1
 A
126












REMARK
3
  ORIGIN FOR THE GROUP (A):
63.8110
  0.9650
−21.6740









REMARK
3
  T TENSOR













REMARK
3
   T11:
−0.1980
T22:
−0.2050



REMARK
3
   T33:
−0.1620
T12:
0.0369


REMARK
3
   T13:
0.0437
T23:
0.0680









REMARK
3
  L TENSOR













REMARK
3
   L11:
2.9649
L22:
2.1492



REMARK
3
   L33:
5.5016
L12:
1.6240


REMARK
3
   L13:
−3.1186
L23:
−1.7013









REMARK
3
  S TENSOR















REMARK
3
   S11:
−0.1563
S12:
0.1452
S13:
−0.2168



REMARK
3
   S21:
−0.3866
S22:
0.0489
S23:
−0.3471


REMARK
3
   S31:
0.2723
S32:
−0.1279
S33:
0.1075


REMARK
3









REMARK
3
 TLS GROUP:   2


REMARK
3
  NUMBER OF COMPONENTS GROUP:  1













REMARK
3
  COMPONENTS
C SSSEQI
 TO C
SSSEQI



REMARK
3
  RESIDUE RANGE:
B
1
 B
126












REMARK
3
  ORIGIN FOR THE GROUP (A):
22.5770
−14.1900
−12.2800


REMARK
3
  T TENSOR













REMARK
3
   T11:
−0.0751
T22:
−0.1155



REMARK
3
   T33:
−0.1816
T12:
−0.0421


REMARK
3
   T13:
−0.0399
T23:
−0.0558









REMARK
3
  L TENSOR













REMARK
3
   L11:
10.1470
L22:
1.3573



REMARK
3
   L33:
3.5880
L12:
1.6659


REMARK
3
   L13:
3.8599
L23:
0.8640









REMARK
3
  S TENSOR















REMARK
3
   S11:
0.2336
S12:
−0.7625
S13:
−0.3980



REMARK
3
   S21:
0.2329
S22:
−0.2032
S23:
−0.1926


REMARK
3
   S31:
0.0115
S32:
−0.2069
S33:
−0.0305


REMARK
3









REMARK
3
 TLS GROUP:   3


REMARK
3
  NUMBER OF COMPONENTS GROUP:  1













REMARK
3
  COMPONENTS
C SSSEQI
 TO C
SSSEQI



REMARK
3
  RESIDUE RANGE:
C
1
 C
126












REMARK
3
  ORIGIN FOR THE GROUP (A):
35.8140
 7.3450
 5.8670


REMARK
3
  T TENSOR













REMARK
3
   T11:
−0.1853
T22:
−0.1041



REMARK
3
   T33:
−0.2449
T12:
0.0111


REMARK
3
   T13:
−0.0203
T23:
−0.0062









REMARK
3
  L TENSOR













REMARK
3
   L11:
2.6982
L22:
1.5248



REMARK
3
   L33:
3.8494
L12:
−1.7131


REMARK
3
   L13:
−3.2164
L23:
2.1240









REMARK
3
  S TENSOR















REMARK
3
   S11:
−0.1201
S12:
−0.0335
S13:
0.0035



REMARK
3
   S21:
0.0881
S22:
−0.0407
S23:
0.0913


REMARK
3
   S31:
0.1124
S32:
0.0662
S33:
0.1608


REMARK
3









REMARK
3
 TLS GROUP:   4


REMARK
3
  NUMBER OF COMPONENTS GROUP:  1













REMARK
3
  COMPONENTS
C SSSEQI
 TO C
SSSEQI



REMARK
3
  RESIDUE RANGE:
D
1
 D
125












REMARK
3
  ORIGIN FOR THE GROUP (A):
59.5290
−29.2800
 −4.2380


REMARK
3
  T TENSOR













REMARK
3
   T11:
0.0220
T22:
−0.0010



REMARK
3
   T33:
−0.1489
T12:
0.0046


REMARK
3
   T13:
0.0795
T23:
0.0694









REMARK
3
  L TENSOR













REMARK
3
   L11:
2.7989
L22:
9.7864



REMARK
3
   L33:
4.7502
L12:
−4.5612


REMARK
3
   L13:
2.9365
L23:
−5.7275









REMARK
3
  S TENSOR















REMARK
3
   S11:
0.4188
S12:
0.4905
S13:
0.0482



REMARK
3
   S21:
−0.7846
S22:
−0.4194
S23:
0.2228


REMARK
3
   S31:
0.4959
S32:
0.5328
S33:
0.0006


REMARK
3









REMARK
3
 BULK SOLVENT MODELLING.


REMARK
3
 METHOD USED:  MASK


REMARK
3
 PARAMETERS FOR MASK CALCULATION


REMARK
3
 VDW PROBE RADIUS:   1.20


REMARK
3
 ION  PROBE RADIUS:   0.80


REMARK
3
 SHRINKAGE RADIUS:   0.80


REMARK
3


REMARK
3
 OTHER REFINEMENT REMARKS:


REMARK
3
 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS


REMARK
3

















SSBOND
1
CYS
A
22

CYS
A
83




SSBOND
2
CYS
B
22

CYS
B
83


SSBOND
3
CYS
C
22

CYS
C
83


SSBOND
4
CYS
D
22

CYS
D
83


CISPEP
1
THR
A
6

PRO
A
7

 0.00


CISPEP
2
THR
D
6

PRO
D
7

 0.00


CISPEP
3
THR
B
6

PRO
B
7

 0.00


CISPEP
4
THR
C
6

PRO
C
7

 0.00








CRYST1
  79.399   79.399    84.890    90.00  90.00  120.00 P 32


SCALE1
   0.012595   0.007272   0.000000         0.00000


SCALE2
   0.000000   0.014543   0.000000         0.00000


SCALE3
   0.000000   0.000000   0.011780         0.00000


















ATOM
1
N
ALA
A
1
61.749
8.643
−7.895
1.00
40.15
N


ATOM
2
CA
ALA
A
1
62.634
7.902
−8.884
1.00
40.18
C


ATOM
3
CB
ALA
A
1
62.339
6.518
−8.853
1.00
39.79
C


ATOM
4
C
ALA
A
1
62.285
8.403
−10.269
1.00
40.24
C


ATOM
5
O
ALA
A
1
61.183
8.874
−10.490
1.00
40.36
O


ATOM
6
N
TRP
A
2
63.195
8.273
−11.213
1.00
39.60
N


ATOM
7
CA
TRP
A
2
62.842
8.487
−12.631
1.00
39.57
C


ATOM
8
CB
TRP
A
2
62.870
9.972
−12.978
1.00
38.16
C


ATOM
9
CG
TRP
A
2
64.196
10.736
−12.660
1.00
37.18
C


ATOM
10
CD1
TRP
A
2
64.695
11.043
−11.419
1.00
36.93
C


ATOM
11
NE1
TRP
A
2
65.878
11.763
−11.534
1.00
39.31
N


ATOM
12
CE2
TRP
A
2
66.153
11.943
−12.869
1.00
37.67
C


ATOM
13
CD2
TRP
A
2
65.132
11.298
−13.609
1.00
36.59
C


ATOM
14
CE3
TRP
A
2
65.173
11.364
−15.011
1.00
37.43
C


ATOM
15
CZ3
TRP
A
2
66.223
12.030
−15.622
1.00
37.01
C


ATOM
16
CH2
TRP
A
2
67.259
12.614
−14.864
1.00
37.70
C


ATOM
17
CZ2
TRP
A
2
67.247
12.571
−13.485
1.00
38.75
C


ATOM
18
C
TRP
A
2
63.930
7.731
−13.337
1.00
40.62
C


ATOM
19
O
TRP
A
2
64.970
7.444
−12.740
1.00
41.17
O


ATOM
20
N
VAL
A
3
63.713
7.420
−14.598
1.00
41.79
N


ATOM
21
CA
VAL
A
3
64.712
6.737
−15.393
1.00
41.23
C


ATOM
22
CB
VAL
A
3
64.067
5.575
−16.107
1.00
42.49
C


ATOM
23
CG1
VAL
A
3
65.010
5.042
−17.208
1.00
41.14
C


ATOM
24
CG2
VAL
A
3
63.708
4.417
−15.072
1.00
42.49
C


ATOM
25
C
VAL
A
3
65.240
7.752
−16.400
1.00
42.26
C


ATOM
26
O
VAL
A
3
64.461
8.371
−17.135
1.00
39.69
O


ATOM
27
N
ASP
A
4
66.560
7.946
−16.388
1.00
42.27
N


ATOM
28
CA
ASP
A
4
67.259
8.833
−17.277
1.00
42.47
C


ATOM
29
CB
ASP
A
4
68.484
9.335
−16.509
1.00
44.28
C


ATOM
30
CG
ASP
A
4
69.123
10.573
−17.112
1.00
43.29
C


ATOM
31
OD1
ASP
A
4
68.608
11.128
−18.127
1.00
41.54
O


ATOM
32
OD2
ASP
A
4
70.150
10.991
−16.507
1.00
47.28
O


ATOM
33
C
ASP
A
4
67.725
8.103
−18.544
1.00
42.79
C


ATOM
34
O
ASP
A
4
68.709
7.350
−18.523
1.00
43.97
O


ATOM
35
N
GLN
A
5
67.048
8.361
−19.639
1.00
42.16
N


ATOM
36
CA
GLN
A
5
67.299
7.703
−20.903
1.00
43.25
C


ATOM
37
CB
GLN
A
5
65.983
7.258
−21.571
1.00
42.36
C


ATOM
38
CG
GLN
A
5
66.230
6.429
−22.844
1.00
43.49
C


ATOM
39
CD
GLN
A
5
64.959
5.836
−23.412
1.00
43.79
C


ATOM
40
OE1
GLN
A
5
63.975
5.772
−22.714
1.00
45.41
O


ATOM
41
NE2
GLN
A
5
64.976
5.402
−24.693
1.00
41.11
N


ATOM
42
C
GLN
A
5
68.052
8.629
−21.864
1.00
42.68
C


ATOM
43
O
GLN
A
5
67.584
9.724
−22.191
1.00
41.82
O


ATOM
44
N
THR
A
6
69.198
8.157
−22.354
1.00
42.97
N


ATOM
45
CA
THR
A
6
69.971
8.908
−23.364
1.00
42.86
C


ATOM
46
CB
THR
A
6
71.203
9.619
−22.713
1.00
43.54
C


ATOM
47
OG1
THR
A
6
71.985
8.617
−22.080
1.00
44.91
O


ATOM
48
CG2
THR
A
6
70.801
10.670
−21.649
1.00
41.18
C


ATOM
49
C
THR
A
6
70.442
8.007
−24.507
1.00
43.00
C


ATOM
50
O
THR
A
6
70.734
6.818
−24.262
1.00
44.11
O


ATOM
51
N
PRO
A
7
70.571
8.561
−25.757
1.00
42.63
N


ATOM
52
CA
PRO
A
7
70.323
9.961
−26.145
1.00
42.77
C


ATOM
53
CB
PRO
A
7
71.057
10.081
−27.477
1.00
41.46
C


ATOM
54
CG
PRO
A
7
70.903
8.752
−28.078
1.00
41.46
C


ATOM
55
CD
PRO
A
7
71.052
7.779
−26.918
1.00
43.08
C


ATOM
56
C
PRO
A
7
68.835
10.178
−26.359
1.00
43.23
C


ATOM
57
O
PRO
A
7
68.177
9.198
−26.651
1.00
44.91
O


ATOM
58
N
ARG
A
8
68.302
11.392
−26.222
1.00
43.41
N


ATOM
59
CA
ARG
A
8
66.868
11.625
−26.493
1.00
44.08
C


ATOM
60
CB
ARG
A
8
66.349
12.944
−25.869
1.00
43.76
C


ATOM
61
CG
ARG
A
8
64.763
13.006
−25.738
1.00
46.28
C


ATOM
62
CD
ARG
A
8
64.248
13.844
−24.561
1.00
48.21
C


ATOM
63
NE
ARG
A
8
64.530
13.270
−23.235
1.00
51.99
N


ATOM
64
CZ
ARG
A
8
64.574
13.982
−22.102
1.00
49.58
C


ATOM
65
NH1
ARG
A
8
64.388
15.306
−22.123
1.00
45.49
N


ATOM
66
NH2
ARG
A
8
64.817
13.367
−20.953
1.00
50.31
N


ATOM
67
C
ARG
A
8
66.538
11.587
−27.988
1.00
43.51
C


ATOM
68
O
ARG
A
8
65.418
11.284
−28.370
1.00
43.05
O


ATOM
69
N
THR
A
9
67.498
11.929
−28.846
1.00
42.86
N


ATOM
70
CA
THR
A
9
67.285
11.777
−30.274
1.00
43.57
C


ATOM
71
CB
THR
A
9
66.814
13.095
−30.939
1.00
43.56
C


ATOM
72
OG1
THR
A
9
67.858
14.036
−30.821
1.00
48.77
O


ATOM
73
CG2
THR
A
9
65.563
13.731
−30.225
1.00
43.75
C


ATOM
74
C
THR
A
9
68.564
11.279
−30.904
1.00
42.93
C


ATOM
75
O
THR
A
9
69.650
11.556
−30.398
1.00
43.89
O


ATOM
76
N
ALA
A
10
68.453
10.511
−31.978
1.00
42.78
N


ATOM
77
CA
ALA
A
10
69.619
9.970
−32.667
1.00
42.32
C


ATOM
78
CB
ALA
A
10
69.994
8.627
−32.086
1.00
42.83
C


ATOM
79
C
ALA
A
10
69.314
9.859
−34.149
1.00
43.20
C


ATOM
80
O
ALA
A
10
68.155
9.623
−34.518
1.00
43.17
O


ATOM
81
N
THR
A
11
70.318
10.143
−34.992
1.00
42.97
N


ATOM
82
CA
THR
A
11
70.225
9.915
−36.444
1.00
43.50
C


ATOM
83
CB
THR
A
11
70.189
11.203
−37.289
1.00
43.99
C


ATOM
84
OG1
THR
A
11
69.173
12.071
−36.792
1.00
46.81
O


ATOM
85
CG2
THR
A
11
69.888
10.919
−38.782
1.00
44.63
C


ATOM
86
C
THR
A
11
71.394
9.035
−36.818
1.00
42.68
C


ATOM
87
O
THR
A
11
72.527
9.265
−36.405
1.00
42.50
O


ATOM
88
N
LYS
A
12
71.095
7.988
−37.565
1.00
42.11
N


ATOM
89
CA
LYS
A
12
72.062
6.984
−37.863
1.00
41.61
C


ATOM
90
CB
LYS
A
12
71.742
5.752
−37.024
1.00
42.20
C


ATOM
91
CG
LYS
A
12
72.682
5.566
−35.832
1.00
42.69
C


ATOM
92
CD
LYS
A
12
72.462
6.488
−34.722
1.00
42.75
C


ATOM
93
CE
LYS
A
12
73.785
6.938
−34.193
1.00
45.64
C


ATOM
94
NZ
LYS
A
12
74.413
5.947
−33.372
1.00
45.06
N


ATOM
95
C
LYS
A
12
72.005
6.639
−39.319
1.00
41.13
C


ATOM
96
O
LYS
A
12
70.939
6.763
−39.917
1.00
40.78
O


ATOM
97
N
GLU
A
13
73.148
6.221
−39.886
1.00
41.13
N


ATOM
98
CA
GLU
A
13
73.217
5.639
−41.224
1.00
41.27
C


ATOM
99
CB
GLU
A
13
74.632
5.698
−41.828
1.00
42.20
C


ATOM
100
CG
GLU
A
13
75.229
7.083
−41.972
1.00
45.88
C


ATOM
101
CD
GLU
A
13
74.375
8.034
−42.822
1.00
46.51
C


ATOM
102
OE1
GLU
A
13
74.450
9.257
−42.598
1.00
46.46
O


ATOM
103
OE2
GLU
A
13
73.643
7.546
−43.710
1.00
49.37
O


ATOM
104
C
GLU
A
13
72.800
4.187
−41.192
1.00
40.83
C


ATOM
105
O
GLU
A
13
72.992
3.508
−40.169
1.00
41.54
O


ATOM
106
N
THR
A
14
72.215
3.721
−42.301
1.00
40.03
N


ATOM
107
CA
THR
A
14
71.940
2.318
−42.489
1.00
39.84
C


ATOM
108
CB
THR
A
14
71.377
2.042
−43.909
1.00
40.21
C


ATOM
109
OG1
THR
A
14
69.983
2.377
−43.955
1.00
37.92
O


ATOM
110
CG2
THR
A
14
71.526
0.563
−44.299
1.00
39.74
C


ATOM
111
C
THR
A
14
73.270
1.599
−42.243
1.00
40.13
C


ATOM
112
O
THR
A
14
74.324
2.000
−42.791
1.00
39.27
O


ATOM
113
N
GLY
A
15
73.233
0.613
−41.342
1.00
40.34
N


ATOM
114
CA
GLY
A
15
74.396
−0.218
−41.032
1.00
40.42
C


ATOM
115
C
GLY
A
15
75.117
0.128
−39.748
1.00
40.96
C


ATOM
116
O
GLY
A
15
75.788
−0.709
−39.224
1.00
41.04
O


ATOM
117
N
GLU
A
16
74.989
1.365
−39.256
1.00
41.99
N


ATOM
118
CA
GLU
A
16
75.598
1.850
−38.014
1.00
43.51
C


ATOM
119
CB
GLU
A
16
75.343
3.359
−37.860
1.00
43.93
C


ATOM
120
CG
GLU
A
16
76.304
4.377
−38.538
1.00
45.03
C


ATOM
121
CD
GLU
A
16
76.197
5.807
−37.839
1.00
46.94
C


ATOM
122
OE1
GLU
A
16
75.428
6.678
−38.323
1.00
43.22
O


ATOM
123
OE2
GLU
A
16
76.837
6.036
−36.754
1.00
52.94
O


ATOM
124
C
GLU
A
16
74.854
1.177
−36.872
1.00
43.56
C


ATOM
125
O
GLU
A
16
73.865
0.509
−37.092
1.00
43.77
O


ATOM
126
N
SER
A
17
75.282
1.388
−35.641
1.00
43.74
N


ATOM
127
CA
SER
A
17
74.492
0.923
−34.544
1.00
44.40
C


ATOM
128
CB
SER
A
17
75.215
−0.229
−33.873
1.00
44.97
C


ATOM
129
OG
SER
A
17
76.123
0.270
−32.945
1.00
50.00
O


ATOM
130
C
SER
A
17
74.111
2.054
−33.578
1.00
44.40
C


ATOM
131
O
SER
A
17
74.564
3.183
−33.740
1.00
43.42
O


ATOM
132
N
LEU
A
18
73.218
1.768
−32.623
1.00
44.29
N


ATOM
133
CA
LEU
A
18
72.750
2.743
−31.631
1.00
43.42
C


ATOM
134
CB
LEU
A
18
71.264
3.018
−31.857
1.00
44.02
C


ATOM
135
CG
LEU
A
18
70.458
4.188
−31.246
1.00
45.03
C


ATOM
136
CD1
LEU
A
18
69.189
3.777
−30.570
1.00
43.77
C


ATOM
137
CD2
LEU
A
18
71.201
5.339
−30.494
1.00
43.20
C


ATOM
138
C
LEU
A
18
72.893
2.116
−30.251
1.00
43.15
C


ATOM
139
O
LEU
A
18
72.533
0.967
−30.042
1.00
42.50
O


ATOM
140
N
THR
A
19
73.396
2.881
−29.305
1.00
42.18
N


ATOM
141
CA
THR
A
19
73.367
2.460
−27.919
1.00
42.94
C


ATOM
142
CB
THR
A
19
74.762
2.333
−27.352
1.00
41.91
C


ATOM
143
OG1
THR
A
19
75.459
1.366
−28.144
1.00
46.16
O


ATOM
144
CG2
THR
A
19
74.690
1.835
−25.920
1.00
43.14
C


ATOM
145
C
THR
A
19
72.566
3.445
−27.107
1.00
42.46
C


ATOM
146
O
THR
A
19
72.838
4.656
−27.120
1.00
42.53
O


ATOM
147
N
ILE
A
20
71.548
2.927
−26.451
1.00
42.31
N


ATOM
148
CA
ILE
A
20
70.689
3.706
−25.552
1.00
43.03
C


ATOM
149
CB
ILE
A
20
69.201
3.335
−25.767
1.00
43.33
C


ATOM
150
CG1
ILE
A
20
68.800
3.502
−27.256
1.00
44.11
C


ATOM
151
CD1
ILE
A
20
67.399
2.948
−27.600
1.00
44.88
C


ATOM
152
CG2
ILE
A
20
68.302
4.141
−24.822
1.00
42.84
C


ATOM
153
C
ILE
A
20
71.077
3.333
−24.134
1.00
42.61
C


ATOM
154
O
ILE
A
20
71.157
2.147
−23.843
1.00
41.82
O


ATOM
155
N
ASN
A
21
71.379
4.327
−23.294
1.00
43.17
N


ATOM
156
CA
ASN
A
21
71.708
4.102
−21.860
1.00
44.83
C


ATOM
157
CB
ASN
A
21
72.990
4.831
−21.455
1.00
44.74
C


ATOM
158
CG
ASN
A
21
74.197
4.409
−22.296
1.00
50.81
C


ATOM
159
OD1
ASN
A
21
74.786
3.335
−22.070
1.00
57.38
O


ATOM
160
ND2
ASN
A
21
74.594
5.257
−23.256
1.00
52.86
N


ATOM
161
C
ASN
A
21
70.569
4.588
−20.961
1.00
45.00
C


ATOM
162
O
ASN
A
21
70.033
5.670
−21.182
1.00
44.50
O


ATOM
163
N
CYS
A
22
70.208
3.816
−19.949
1.00
44.60
N


ATOM
164
CA
CYS
A
22
69.167
4.237
−19.029
1.00
45.32
C


ATOM
165
CB
CYS
A
22
67.909
3.372
−19.165
1.00
45.74
C


ATOM
166
SG
CYS
A
22
66.995
3.746
−20.639
1.00
54.23
S


ATOM
167
C
CYS
A
22
69.658
4.101
−17.624
1.00
44.15
C


ATOM
168
O
CYS
A
22
70.236
3.107
−17.289
1.00
43.54
O


ATOM
169
N
VAL
A
23
69.395
5.085
−16.785
1.00
43.49
N


ATOM
170
CA
VAL
A
23
69.643
4.909
−15.365
1.00
42.35
C


ATOM
171
CB
VAL
A
23
71.085
5.352
−14.883
1.00
43.00
C


ATOM
172
CG1
VAL
A
23
71.963
6.041
−15.953
1.00
41.73
C


ATOM
173
CG2
VAL
A
23
71.199
5.917
−13.413
1.00
42.45
C


ATOM
174
C
VAL
A
23
68.417
5.249
−14.481
1.00
42.71
C


ATOM
175
O
VAL
A
23
67.709
6.260
−14.671
1.00
41.74
O


ATOM
176
N
LEU
A
24
68.123
4.344
−13.563
1.00
42.36
N


ATOM
177
CA
LEU
A
24
67.057
4.563
−12.645
1.00
43.14
C


ATOM
178
CB
LEU
A
24
66.608
3.213
−12.068
1.00
43.10
C


ATOM
179
CG
LEU
A
24
65.662
3.260
−10.863
1.00
44.67
C


ATOM
180
CD1
LEU
A
24
64.281
3.811
−11.337
1.00
42.56
C


ATOM
181
CD2
LEU
A
24
65.508
1.885
−10.150
1.00
44.14
C


ATOM
182
C
LEU
A
24
67.691
5.476
−11.592
1.00
42.20
C


ATOM
183
O
LEU
A
24
68.575
5.053
−10.877
1.00
42.62
O


ATOM
184
N
ARG
A
25
67.261
6.734
−11.531
1.00
41.75
N


ATOM
185
CA
ARG
A
25
67.859
7.731
−10.598
1.00
40.94
C


ATOM
186
CB
ARG
A
25
68.196
9.032
−11.327
1.00
39.67
C


ATOM
187
CG
ARG
A
25
69.067
8.832
−12.554
1.00
39.63
C


ATOM
188
CD
ARG
A
25
69.891
10.080
−12.859
1.00
38.88
C


ATOM
189
NE
ARG
A
25
70.828
9.833
−13.950
1.00
44.89
N


ATOM
190
CZ
ARG
A
25
72.121
9.535
−13.783
1.00
47.29
C


ATOM
191
NH1
ARG
A
25
72.620
9.447
−12.539
1.00
46.01
N


ATOM
192
NH2
ARG
A
25
72.924
9.391
−14.850
1.00
43.92
N


ATOM
193
C
ARG
A
25
66.903
8.056
−9.468
1.00
41.31
C


ATOM
194
O
ARG
A
25
65.691
7.828
−9.600
1.00
39.67
O


ATOM
195
N
ASP
A
26
67.466
8.586
−8.375
1.00
41.32
N


ATOM
196
CA
ASP
A
26
66.756
8.989
−7.190
1.00
43.62
C


ATOM
197
CB
ASP
A
26
66.179
10.401
−7.349
1.00
45.00
C


ATOM
198
CG
ASP
A
26
67.224
11.395
−7.953
1.00
52.91
C


ATOM
199
OD1
ASP
A
26
66.854
12.215
−8.853
1.00
59.13
O


ATOM
200
OD2
ASP
A
26
68.436
11.347
−7.556
1.00
60.06
O


ATOM
201
C
ASP
A
26
65.732
7.986
−6.674
1.00
43.23
C


ATOM
202
O
ASP
A
26
64.635
8.350
−6.232
1.00
43.09
O


ATOM
203
N
ALA
A
27
66.114
6.708
−6.710
1.00
43.21
N


ATOM
204
CA
ALA
A
27
65.231
5.600
−6.311
1.00
42.66
C


ATOM
205
CB
ALA
A
27
65.081
4.609
−7.466
1.00
40.95
C


ATOM
206
C
ALA
A
27
65.800
4.898
−5.058
1.00
43.66
C


ATOM
207
O
ALA
A
27
66.997
4.563
−4.986
1.00
43.64
O


ATOM
208
N
SER
A
28
64.929
4.643
−4.097
1.00
44.63
N


ATOM
209
CA
SER
A
28
65.301
3.945
−2.860
1.00
46.25
C


ATOM
210
CB
SER
A
28
64.306
4.340
−1.793
1.00
46.62
C


ATOM
211
OG
SER
A
28
62.989
4.076
−2.343
1.00
51.66
O


ATOM
212
C
SER
A
28
65.244
2.424
−3.024
1.00
45.27
C


ATOM
213
O
SER
A
28
65.753
1.699
−2.204
1.00
45.50
O


ATOM
214
N
PHE
A
29
64.597
1.951
−4.080
1.00
44.65
N


ATOM
215
CA
PHE
A
29
64.428
0.515
−4.320
1.00
44.66
C


ATOM
216
CB
PHE
A
29
63.026
0.206
−4.853
1.00
44.20
C


ATOM
217
CG
PHE
A
29
62.491
1.236
−5.821
1.00
43.80
C


ATOM
218
CD1
PHE
A
29
61.557
2.181
−5.392
1.00
42.75
C


ATOM
219
CE1
PHE
A
29
61.055
3.155
−6.275
1.00
42.50
C


ATOM
220
CZ
PHE
A
29
61.457
3.156
−7.641
1.00
42.43
C


ATOM
221
CE2
PHE
A
29
62.376
2.202
−8.074
1.00
43.56
C


ATOM
222
CD2
PHE
A
29
62.895
1.243
−7.168
1.00
40.83
C


ATOM
223
C
PHE
A
29
65.444
0.022
−5.324
1.00
44.85
C


ATOM
224
O
PHE
A
29
66.046
0.816
−6.017
1.00
45.13
O


ATOM
225
N
GLU
A
30
65.606
−1.292
−5.428
1.00
44.65
N


ATOM
226
CA
GLU
A
30
66.616
−1.829
−6.302
1.00
45.34
C


ATOM
227
CB
GLU
A
30
67.141
−3.148
−5.719
1.00
46.03
C


ATOM
228
CG
GLU
A
30
67.484
−3.139
−4.182
1.00
51.87
C


ATOM
229
CD
GLU
A
30
68.905
−2.718
−3.833
1.00
61.36
C


ATOM
230
OE1
GLU
A
30
69.655
−3.533
−3.218
1.00
64.71
O


ATOM
231
OE2
GLU
A
30
69.283
−1.554
−4.132
1.00
66.90
O


ATOM
232
C
GLU
A
30
66.040
−2.045
−7.710
1.00
44.87
C


ATOM
233
O
GLU
A
30
64.804
−2.206
−7.902
1.00
43.77
O


ATOM
234
N
LEU
A
31
66.933
−2.100
−8.692
1.00
44.05
N


ATOM
235
CA
LEU
A
31
66.527
−2.480
−10.022
1.00
44.47
C


ATOM
236
CB
LEU
A
31
67.529
−1.966
−11.057
1.00
44.35
C


ATOM
237
CG
LEU
A
31
67.302
−2.279
−12.541
1.00
44.08
C


ATOM
238
CD1
LEU
A
31
68.569
−2.051
−13.351
1.00
41.58
C


ATOM
239
CD2
LEU
A
31
66.136
−1.523
−13.132
1.00
41.76
C


ATOM
240
C
LEU
A
31
66.373
−4.001
−10.047
1.00
45.45
C


ATOM
241
O
LEU
A
31
67.337
−4.736
−9.819
1.00
46.74
O


ATOM
242
N
LYS
A
32
65.139
−4.478
−10.238
1.00
45.05
N


ATOM
243
CA
LYS
A
32
64.876
−5.919
−10.271
1.00
44.49
C


ATOM
244
CB
LYS
A
32
63.509
−6.221
−9.649
1.00
44.92
C


ATOM
245
CG
LYS
A
32
63.393
−5.867
−8.121
1.00
46.76
C


ATOM
246
CD
LYS
A
32
64.441
−6.598
−7.239
1.00
46.19
C


ATOM
247
CE
LYS
A
32
63.953
−6.546
−5.816
1.00
50.58
C


ATOM
248
NZ
LYS
A
32
64.928
−7.103
−4.883
1.00
53.68
N


ATOM
249
C
LYS
A
32
64.934
−6.509
−11.676
1.00
44.11
C


ATOM
250
O
LYS
A
32
65.328
−7.643
−11.858
1.00
42.45
O


ATOM
251
N
ASP
A
33
64.509
−5.743
−12.676
1.00
44.84
N


ATOM
252
CA
ASP
A
33
64.436
−6.261
−14.076
1.00
44.80
C


ATOM
253
CB
ASP
A
33
63.261
−7.211
−14.233
1.00
45.40
C


ATOM
254
CG
ASP
A
33
63.419
−8.179
−15.400
1.00
49.24
C


ATOM
255
OD1
ASP
A
33
64.455
−8.192
−16.141
1.00
47.77
O


ATOM
256
OD2
ASP
A
33
62.433
−8.933
−15.577
1.00
55.63
O


ATOM
257
C
ASP
A
33
64.293
−5.127
−15.063
1.00
44.19
C


ATOM
258
O
ASP
A
33
64.063
−3.981
−14.671
1.00
42.88
O


ATOM
259
N
THR
A
34
64.481
−5.431
−16.348
1.00
43.32
N


ATOM
260
CA
THR
A
34
64.513
−4.362
−17.365
1.00
42.96
C


ATOM
261
CB
THR
A
34
65.977
−4.082
−17.816
1.00
43.35
C


ATOM
262
OG1
THR
A
34
66.616
−5.313
−18.245
1.00
46.20
O


ATOM
263
CG2
THR
A
34
66.799
−3.582
−16.631
1.00
42.87
C


ATOM
264
C
THR
A
34
63.634
−4.801
−18.566
1.00
42.17
C


ATOM
265
O
THR
A
34
63.395
−6.018
−18.771
1.00
40.33
O


ATOM
266
N
GLY
A
35
63.143
−3.820
−19.318
1.00
40.76
N


ATOM
267
CA
GLY
A
35
62.446
−4.100
−20.554
1.00
40.48
C


ATOM
268
C
GLY
A
35
62.659
−2.980
−21.531
1.00
40.71
C


ATOM
269
O
GLY
A
35
63.001
−1.868
−21.139
1.00
41.72
O


ATOM
270
N
TRP
A
36
62.465
−3.294
−22.815
1.00
40.28
N


ATOM
271
CA
TRP
A
36
62.674
−2.399
−23.935
1.00
40.14
C


ATOM
272
CB
TRP
A
36
63.993
−2.767
−24.656
1.00
38.78
C


ATOM
273
CG
TRP
A
36
65.201
−2.495
−23.763
1.00
37.14
C


ATOM
274
CD1
TRP
A
36
65.778
−3.349
−22.867
1.00
36.99
C


ATOM
275
NE1
TRP
A
36
66.846
−2.715
−22.216
1.00
37.64
N


ATOM
276
CE2
TRP
A
36
66.915
−1.410
−22.659
1.00
37.73
C


ATOM
277
CD2
TRP
A
36
65.912
−1.233
−23.632
1.00
35.75
C


ATOM
278
CE3
TRP
A
36
65.771
0.021
−24.231
1.00
38.30
C


ATOM
279
CZ3
TRP
A
36
66.662
1.028
−23.895
1.00
38.55
C


ATOM
280
CH2
TRP
A
36
67.669
0.808
−22.922
1.00
38.11
C


ATOM
281
CZ2
TRP
A
36
67.803
−0.388
−22.308
1.00
39.69
C


ATOM
282
C
TRP
A
36
61.462
−2.494
−24.882
1.00
40.45
C


ATOM
283
O
TRP
A
36
60.900
−3.575
−25.086
1.00
37.84
O


ATOM
284
N
TYR
A
37
61.082
−1.350
−25.466
1.00
40.70
N


ATOM
285
CA
TYR
A
37
59.866
−1.236
−26.308
1.00
41.93
C


ATOM
286
CB
TYR
A
37
58.685
−0.707
−25.468
1.00
42.76
C


ATOM
287
CG
TYR
A
37
58.563
−1.427
−24.194
1.00
42.14
C


ATOM
288
CD1
TYR
A
37
57.719
−2.520
−24.075
1.00
40.34
C


ATOM
289
CE1
TYR
A
37
57.646
−3.242
−22.868
1.00
41.85
C


ATOM
290
CZ
TYR
A
37
58.426
−2.826
−21.801
1.00
42.69
C


ATOM
291
OH
TYR
A
37
58.379
−3.479
−20.599
1.00
47.21
O


ATOM
292
CE2
TYR
A
37
59.238
−1.728
−21.895
1.00
42.12
C


ATOM
293
CD2
TYR
A
37
59.307
−1.027
−23.098
1.00
41.52
C


ATOM
294
C
TYR
A
37
60.081
−0.257
−27.427
1.00
42.18
C


ATOM
295
O
TYR
A
37
60.936
0.595
−27.346
1.00
41.61
O


ATOM
296
N
ARG
A
38
59.267
−0.357
−28.453
1.00
43.78
N


ATOM
297
CA
ARG
A
38
59.532
0.406
−29.648
1.00
46.16
C


ATOM
298
CB
ARG
A
38
60.599
−0.320
−30.467
1.00
45.76
C


ATOM
299
CG
ARG
A
38
60.521
−0.353
−31.940
1.00
49.53
C


ATOM
300
CD
ARG
A
38
61.333
−1.543
−32.436
1.00
50.13
C


ATOM
301
NE
ARG
A
38
60.989
−1.847
−33.794
1.00
52.73
N


ATOM
302
CZ
ARG
A
38
61.856
−1.891
−34.805
1.00
60.11
C


ATOM
303
NH1
ARG
A
38
61.402
−2.162
−36.023
1.00
59.27
N


ATOM
304
NH2
ARG
A
38
63.172
−1.662
−34.620
1.00
60.83
N


ATOM
305
C
ARG
A
38
58.216
0.686
−30.345
1.00
46.60
C


ATOM
306
O
ARG
A
38
57.320
−0.172
−30.373
1.00
46.42
O


ATOM
307
N
THR
A
39
58.077
1.929
−30.802
1.00
46.84
N


ATOM
308
CA
THR
A
39
56.980
2.339
−31.664
1.00
47.57
C


ATOM
309
CB
THR
A
39
56.261
3.586
−31.110
1.00
47.10
C


ATOM
310
OG1
THR
A
39
55.916
3.378
−29.750
1.00
50.61
O


ATOM
311
CG2
THR
A
39
54.999
3.839
−31.858
1.00
49.14
C


ATOM
312
C
THR
A
39
57.637
2.703
−32.961
1.00
47.84
C


ATOM
313
O
THR
A
39
58.482
3.618
−32.983
1.00
46.61
O


ATOM
314
N
LYS
A
40
57.283
1.980
−34.034
1.00
49.00
N


ATOM
315
CA
LYS
A
40
57.849
2.253
−35.349
1.00
51.32
C


ATOM
316
CB
LYS
A
40
57.656
1.095
−36.329
1.00
51.60
C


ATOM
317
CG
LYS
A
40
58.368
−0.180
−35.877
1.00
54.32
C


ATOM
318
CD
LYS
A
40
58.208
−1.327
−36.858
1.00
55.56
C


ATOM
319
CE
LYS
A
40
59.149
−1.119
−38.039
1.00
55.54
C


ATOM
320
NZ
LYS
A
40
59.491
−2.440
−38.640
1.00
58.58
N


ATOM
321
C
LYS
A
40
57.310
3.555
−35.909
1.00
51.81
C


ATOM
322
O
LYS
A
40
56.245
4.013
−35.513
1.00
51.60
O


ATOM
323
N
LEU
A
41
58.073
4.166
−36.805
1.00
53.16
N


ATOM
324
CA
LEU
A
41
57.623
5.383
−37.454
1.00
54.73
C


ATOM
325
CB
LEU
A
41
58.735
5.951
−38.319
1.00
55.27
C


ATOM
326
CG
LEU
A
41
58.569
7.373
−38.833
1.00
56.10
C


ATOM
327
CD1
LEU
A
41
59.828
7.743
−39.616
1.00
54.91
C


ATOM
328
CD2
LEU
A
41
58.320
8.338
−37.636
1.00
58.13
C


ATOM
329
C
LEU
A
41
56.385
5.086
−38.311
1.00
55.70
C


ATOM
330
O
LEU
A
41
56.424
4.238
−39.228
1.00
55.38
O


ATOM
331
N
GLY
A
42
55.290
5.778
−38.001
1.00
56.61
N


ATOM
332
CA
GLY
A
42
54.043
5.583
−38.715
1.00
57.83
C


ATOM
333
C
GLY
A
42
53.064
4.709
−37.968
1.00
59.16
C


ATOM
334
O
GLY
A
42
51.849
4.803
−38.199
1.00
59.45
O


ATOM
335
N
SER
A
43
53.587
3.873
−37.060
1.00
60.41
N


ATOM
336
CA
SER
A
43
52.775
2.988
−36.198
1.00
61.00
C


ATOM
337
CB
SER
A
43
53.550
1.722
−35.781
1.00
60.84
C


ATOM
338
OG
SER
A
43
53.706
0.833
−36.880
1.00
61.59
O


ATOM
339
C
SER
A
43
52.239
3.671
−34.956
1.00
61.22
C


ATOM
340
O
SER
A
43
52.845
4.581
−34.387
1.00
61.91
O


ATOM
341
N
THR
A
44
51.092
3.206
−34.507
1.00
61.44
N


ATOM
342
CA
THR
A
44
50.502
3.811
−33.352
1.00
61.38
C


ATOM
343
CB
THR
A
44
48.964
3.869
−33.493
1.00
61.80
C


ATOM
344
OG1
THR
A
44
48.650
4.479
−34.762
1.00
60.23
O


ATOM
345
CG2
THR
A
44
48.307
4.653
−32.316
1.00
59.36
C


ATOM
346
C
THR
A
44
50.973
3.105
−32.083
1.00
61.97
C


ATOM
347
O
THR
A
44
51.440
3.773
−31.146
1.00
62.38
O


ATOM
348
N
ASN
A
45
50.885
1.770
−32.064
1.00
61.54
N


ATOM
349
CA
ASN
A
45
51.100
1.020
−30.825
1.00
61.43
C


ATOM
350
CB
ASN
A
45
50.127
−0.173
−30.705
1.00
61.50
C


ATOM
351
CG
ASN
A
45
48.642
0.221
−30.958
1.00
62.37
C


ATOM
352
OD1
ASN
A
45
48.185
1.305
−30.582
1.00
62.72
O


ATOM
353
ND2
ASN
A
45
47.896
−0.683
−31.590
1.00
61.46
N


ATOM
354
C
ASN
A
45
52.560
0.609
−30.523
1.00
60.98
C


ATOM
355
O
ASN
A
45
53.299
0.149
−31.394
1.00
61.08
O


ATOM
356
N
GLU
A
46
52.938
0.823
−29.265
1.00
60.78
N


ATOM
357
CA
GLU
A
46
54.210
0.400
−28.672
1.00
60.71
C


ATOM
358
CB
GLU
A
46
54.284
0.954
−27.266
1.00
60.85
C


ATOM
359
CG
GLU
A
46
55.575
0.708
−26.576
1.00
63.83
C


ATOM
360
CD
GLU
A
46
55.497
1.029
−25.103
1.00
70.18
C


ATOM
361
OE1
GLU
A
46
54.694
0.349
−24.389
1.00
72.55
O


ATOM
362
OE2
GLU
A
46
56.254
1.940
−24.657
1.00
73.06
O


ATOM
363
C
GLU
A
46
54.333
−1.121
−28.614
1.00
59.83
C


ATOM
364
O
GLU
A
46
53.389
−1.791
−28.220
1.00
60.32
O


ATOM
365
N
GLN
A
47
55.485
−1.669
−29.007
1.00
58.86
N


ATOM
366
CA
GLN
A
47
55.685
−3.121
−28.999
1.00
57.92
C


ATOM
367
CB
GLN
A
47
55.601
−3.679
−30.411
1.00
58.34
C


ATOM
368
CG
GLN
A
47
56.948
−3.889
−31.081
1.00
61.68
C


ATOM
369
CD
GLN
A
47
56.886
−3.720
−32.595
1.00
68.07
C


ATOM
370
OE1
GLN
A
47
57.774
−3.090
−33.219
1.00
69.58
O


ATOM
371
NE2
GLN
A
47
55.838
−4.288
−33.204
1.00
69.32
N


ATOM
372
C
GLN
A
47
56.991
−3.546
−28.291
1.00
56.40
C


ATOM
373
O
GLN
A
47
57.991
−2.855
−28.403
1.00
56.16
O


ATOM
374
N
SER
A
48
56.973
−4.691
−27.599
1.00
53.86
N


ATOM
375
CA
SER
A
48
58.112
−5.136
−26.806
1.00
53.14
C


ATOM
376
CB
SER
A
48
57.759
−6.239
−25.793
1.00
52.59
C


ATOM
377
OG
SER
A
48
56.373
−6.331
−25.659
1.00
55.97
O


ATOM
378
C
SER
A
48
59.210
−5.658
−27.672
1.00
51.60
C


ATOM
379
O
SER
A
48
58.968
−6.329
−28.679
1.00
51.19
O


ATOM
380
N
ILE
A
49
60.433
−5.380
−27.229
1.00
50.47
N


ATOM
381
CA
ILE
A
49
61.627
−5.856
−27.920
1.00
49.33
C


ATOM
382
CB
ILE
A
49
62.710
−4.755
−28.005
1.00
48.45
C


ATOM
383
CG1
ILE
A
49
62.251
−3.636
−28.919
1.00
48.57
C


ATOM
384
CD1
ILE
A
49
62.995
−2.348
−28.670
1.00
47.03
C


ATOM
385
CG2
ILE
A
49
64.064
−5.362
−28.492
1.00
47.35
C


ATOM
386
C
ILE
A
49
62.198
−7.054
−27.160
1.00
48.70
C


ATOM
387
O
ILE
A
49
62.555
−6.911
−25.986
1.00
48.29
O


ATOM
388
N
SER
A
50
62.293
−8.198
−27.849
1.00
49.00
N


ATOM
389
CA
SER
A
50
62.998
−9.436
−27.400
1.00
49.52
C


ATOM
390
CB
SER
A
50
62.551
−10.647
−28.223
1.00
49.72
C


ATOM
391
OG
SER
A
50
61.213
−10.968
−27.948
1.00
52.50
O


ATOM
392
C
SER
A
50
64.507
−9.299
−27.621
1.00
48.65
C


ATOM
393
O
SER
A
50
64.944
−9.131
−28.735
1.00
48.05
O


ATOM
394
N
ILE
A
51
65.270
−9.397
−26.540
1.00
47.94
N


ATOM
395
CA
ILE
A
51
66.706
−9.224
−26.516
1.00
47.34
C


ATOM
396
CB
ILE
A
51
67.134
−9.131
−25.012
1.00
47.28
C


ATOM
397
CG1
ILE
A
51
66.616
−7.835
−24.342
1.00
47.48
C


ATOM
398
CD1
ILE
A
51
66.759
−6.511
−25.185
1.00
46.22
C


ATOM
399
CG2
ILE
A
51
68.618
−9.405
−24.815
1.00
49.45
C


ATOM
400
C
ILE
A
51
67.332
−10.427
−27.229
1.00
46.82
C


ATOM
401
O
ILE
A
51
66.976
−11.538
−26.927
1.00
46.57
O


ATOM
402
N
GLY
A
52
68.227
−10.219
−28.197
1.00
46.54
N


ATOM
403
CA
GLY
A
52
68.790
−11.324
−28.979
1.00
45.30
C


ATOM
404
C
GLY
A
52
69.129
−10.786
−30.354
1.00
46.43
C


ATOM
405
O
GLY
A
52
68.603
−9.736
−30.754
1.00
47.18
O


ATOM
406
N
GLY
A
53
70.047
−11.446
−31.054
1.00
45.33
N


ATOM
407
CA
GLY
A
53
70.408
−11.065
−32.399
1.00
45.72
C


ATOM
408
C
GLY
A
53
71.007
−9.680
−32.446
1.00
45.66
C


ATOM
409
O
GLY
A
53
72.039
−9.435
−31.823
1.00
46.03
O


ATOM
410
N
ARG
A
54
70.359
−8.794
−33.207
1.00
45.46
N


ATOM
411
CA
ARG
A
54
70.681
−7.360
−33.292
1.00
45.57
C


ATOM
412
CB
ARG
A
54
69.802
−6.697
−34.364
1.00
45.77
C


ATOM
413
CG
ARG
A
54
70.428
−6.723
−35.756
1.00
47.80
C


ATOM
414
CD
ARG
A
54
69.460
−6.515
−36.962
1.00
47.13
C


ATOM
415
NE
ARG
A
54
68.139
−5.901
−36.699
1.00
48.21
N


ATOM
416
CZ
ARG
A
54
67.854
−4.597
−36.739
1.00
48.23
C


ATOM
417
NH1
ARG
A
54
68.788
−3.680
−36.949
1.00
47.12
N


ATOM
418
NH2
ARG
A
54
66.614
−4.205
−36.539
1.00
47.74
N


ATOM
419
C
ARG
A
54
70.538
−6.549
−31.994
1.00
44.48
C


ATOM
420
O
ARG
A
54
71.102
−5.455
−31.899
1.00
45.01
O


ATOM
421
N
TYR
A
55
69.760
−7.042
−31.028
1.00
43.84
N


ATOM
422
CA
TYR
A
55
69.450
−6.305
−29.788
1.00
43.35
C


ATOM
423
CB
TYR
A
55
67.958
−6.426
−29.448
1.00
44.35
C


ATOM
424
CG
TYR
A
55
67.074
−5.915
−30.548
1.00
46.48
C


ATOM
425
CD1
TYR
A
55
66.572
−6.774
−31.512
1.00
49.83
C


ATOM
426
CE1
TYR
A
55
65.784
−6.314
−32.555
1.00
49.58
C


ATOM
427
CZ
TYR
A
55
65.477
−4.973
−32.627
1.00
50.34
C


ATOM
428
OH
TYR
A
55
64.687
−4.523
−33.663
1.00
50.81
O


ATOM
429
CE2
TYR
A
55
65.965
−4.079
−31.681
1.00
48.69
C


ATOM
430
CD2
TYR
A
55
66.772
−4.557
−30.655
1.00
48.63
C


ATOM
431
C
TYR
A
55
70.266
−6.876
−28.651
1.00
42.80
C


ATOM
432
O
TYR
A
55
69.952
−7.955
−28.191
1.00
42.93
O


ATOM
433
N
VAL
A
56
71.355
−6.232
−28.240
1.00
41.64
N


ATOM
434
CA
VAL
A
56
72.001
−6.733
−27.046
1.00
40.80
C


ATOM
435
CB
VAL
A
56
73.464
−7.357
−27.245
1.00
42.17
C


ATOM
436
CG1
VAL
A
56
73.841
−7.600
−28.748
1.00
38.54
C


ATOM
437
CG2
VAL
A
56
74.538
−6.558
−26.522
1.00
43.83
C


ATOM
438
C
VAL
A
56
71.827
−5.785
−25.862
1.00
41.18
C


ATOM
439
O
VAL
A
56
71.910
−4.546
−25.990
1.00
39.41
O


ATOM
440
N
GLU
A
57
71.512
−6.367
−24.712
1.00
40.70
N


ATOM
441
CA
GLU
A
57
71.286
−5.580
−23.520
1.00
41.90
C


ATOM
442
CB
GLU
A
57
69.900
−5.898
−22.929
1.00
42.24
C


ATOM
443
CG
GLU
A
57
69.600
−5.062
−21.704
1.00
42.95
C


ATOM
444
CD
GLU
A
57
68.308
−5.403
−20.974
1.00
42.25
C


ATOM
445
OE1
GLU
A
57
67.949
−6.577
−20.900
1.00
38.99
O


ATOM
446
OE2
GLU
A
57
67.670
−4.457
−20.460
1.00
44.79
O


ATOM
447
C
GLU
A
57
72.384
−5.881
−22.492
1.00
42.34
C


ATOM
448
O
GLU
A
57
72.798
−7.042
−22.344
1.00
42.11
O


ATOM
449
N
THR
A
58
72.877
−4.831
−21.831
1.00
42.68
N


ATOM
450
CA
THR
A
58
73.858
−4.957
−20.757
1.00
43.59
C


ATOM
451
CB
THR
A
58
75.189
−4.212
−21.077
1.00
43.40
C


ATOM
452
OG1
THR
A
58
75.624
−4.579
−22.385
1.00
46.66
O


ATOM
453
CG2
THR
A
58
76.359
−4.628
−20.109
1.00
43.34
C


ATOM
454
C
THR
A
58
73.158
−4.367
−19.552
1.00
44.00
C


ATOM
455
O
THR
A
58
72.617
−3.287
−19.658
1.00
44.75
O


ATOM
456
N
VAL
A
59
73.085
−5.096
−18.435
1.00
45.31
N


ATOM
457
CA
VAL
A
59
72.445
−4.573
−17.188
1.00
46.32
C


ATOM
458
CB
VAL
A
59
71.193
−5.433
−16.756
1.00
46.73
C


ATOM
459
CG1
VAL
A
59
70.611
−4.939
−15.416
1.00
45.96
C


ATOM
460
CG2
VAL
A
59
70.109
−5.392
−17.855
1.00
46.73
C


ATOM
461
C
VAL
A
59
73.470
−4.509
−16.019
1.00
46.15
C


ATOM
462
O
VAL
A
59
74.107
−5.492
−15.742
1.00
45.02
O


ATOM
463
N
ASN
A
60
73.646
−3.357
−15.368
1.00
46.21
N


ATOM
464
CA
ASN
A
60
74.410
−3.289
−14.091
1.00
47.08
C


ATOM
465
CB
ASN
A
60
75.582
−2.282
−14.177
1.00
46.82
C


ATOM
466
CG
ASN
A
60
76.468
−2.280
−12.923
1.00
49.00
C


ATOM
467
OD1
ASN
A
60
75.999
−2.345
−11.785
1.00
52.76
O


ATOM
468
ND2
ASN
A
60
77.757
−2.224
−13.138
1.00
49.31
N


ATOM
469
C
ASN
A
60
73.440
−2.923
−12.955
1.00
47.32
C


ATOM
470
O
ASN
A
60
73.134
−1.773
−12.726
1.00
46.07
O


ATOM
471
N
LYS
A
61
72.939
−3.925
−12.255
1.00
48.72
N


ATOM
472
CA
LYS
A
61
71.962
−3.707
−11.182
1.00
49.59
C


ATOM
473
CB
LYS
A
61
71.378
−5.055
−10.716
1.00
49.75
C


ATOM
474
CG
LYS
A
61
70.215
−5.564
−11.593
1.00
50.68
C


ATOM
475
CD
LYS
A
61
69.812
−6.983
−11.174
1.00
50.86
C


ATOM
476
CE
LYS
A
61
68.695
−7.504
−12.055
1.00
54.11
C


ATOM
477
NZ
LYS
A
61
68.044
−8.687
−11.416
1.00
56.87
N


ATOM
478
C
LYS
A
61
72.560
−2.919
−10.000
1.00
49.82
C


ATOM
479
O
LYS
A
61
71.854
−2.143
−9.371
1.00
50.15
O


ATOM
480
N
GLY
A
62
73.848
−3.134
−9.718
1.00
49.68
N


ATOM
481
CA
GLY
A
62
74.606
−2.382
−8.706
1.00
49.85
C


ATOM
482
C
GLY
A
62
74.552
−0.878
−8.922
1.00
49.84
C


ATOM
483
O
GLY
A
62
74.322
−0.121
−7.980
1.00
50.26
O


ATOM
484
N
SER
A
63
74.731
−0.433
−10.169
1.00
48.77
N


ATOM
485
CA
SER
A
63
74.577
0.986
−10.490
1.00
47.70
C


ATOM
486
CB
SER
A
63
75.754
1.436
−11.342
1.00
47.84
C


ATOM
487
OG
SER
A
63
75.593
0.909
−12.632
1.00
51.09
O


ATOM
488
C
SER
A
63
73.200
1.385
−11.111
1.00
46.97
C


ATOM
489
O
SER
A
63
73.043
2.490
−11.649
1.00
47.21
O


ATOM
490
N
LYS
A
64
72.209
0.497
−11.007
1.00
44.94
N


ATOM
491
CA
LYS
A
64
70.843
0.715
−11.475
1.00
44.84
C


ATOM
492
CB
LYS
A
64
70.057
1.625
−10.509
1.00
43.86
C


ATOM
493
CG
LYS
A
64
70.033
1.170
−9.029
1.00
47.25
C


ATOM
494
CD
LYS
A
64
69.005
2.001
−8.219
1.00
44.70
C


ATOM
495
CE
LYS
A
64
69.247
1.819
−6.729
1.00
44.99
C


ATOM
496
NZ
LYS
A
64
68.112
2.477
−6.068
1.00
44.40
N


ATOM
497
C
LYS
A
64
70.804
1.247
−12.917
1.00
44.07
C


ATOM
498
O
LYS
A
64
70.049
2.146
−13.280
1.00
43.97
O


ATOM
499
N
SER
A
65
71.587
0.626
−13.752
1.00
43.50
N


ATOM
500
CA
SER
A
65
71.940
1.168
−15.069
1.00
44.29
C


ATOM
501
CB
SER
A
65
73.362
1.691
−14.968
1.00
44.32
C


ATOM
502
OG
SER
A
65
73.875
1.947
−16.238
1.00
50.36
O


ATOM
503
C
SER
A
65
71.865
0.026
−16.097
1.00
43.54
C


ATOM
504
O
SER
A
65
72.276
−1.068
−15.818
1.00
44.78
O


ATOM
505
N
PHE
A
66
71.310
0.273
−17.268
1.00
43.55
N


ATOM
506
CA
PHE
A
66
71.086
−0.763
−18.282
1.00
42.34
C


ATOM
507
CB
PHE
A
66
69.779
−1.568
−18.040
1.00
41.29
C


ATOM
508
CG
PHE
A
66
68.550
−0.738
−17.764
1.00
43.12
C


ATOM
509
CD1
PHE
A
66
68.427
0.051
−16.599
1.00
42.71
C


ATOM
510
CE1
PHE
A
66
67.241
0.790
−16.358
1.00
44.02
C


ATOM
511
CZ
PHE
A
66
66.195
0.688
−17.257
1.00
45.56
C


ATOM
512
CE2
PHE
A
66
66.300
−0.135
−18.391
1.00
43.21
C


ATOM
513
CD2
PHE
A
66
67.444
−0.813
−18.639
1.00
43.36
C


ATOM
514
C
PHE
A
66
71.113
−0.110
−19.662
1.00
42.27
C


ATOM
515
O
PHE
A
66
70.725
1.063
−19.818
1.00
40.59
O


ATOM
516
N
SER
A
67
71.578
−0.848
−20.661
1.00
42.12
N


ATOM
517
CA
SER
A
67
71.575
−0.287
−22.008
1.00
42.94
C


ATOM
518
CB
SER
A
67
72.871
0.482
−22.245
1.00
44.09
C


ATOM
519
OG
SER
A
67
73.943
−0.414
−22.195
1.00
46.13
O


ATOM
520
C
SER
A
67
71.318
−1.326
−23.109
1.00
42.30
C


ATOM
521
O
SER
A
67
71.475
−2.518
−22.887
1.00
41.64
O


ATOM
522
N
LEU
A
68
70.843
−0.857
−24.259
1.00
42.72
N


ATOM
523
CA
LEU
A
68
70.479
−1.706
−25.376
1.00
42.24
C


ATOM
524
CB
LEU
A
68
69.032
−1.415
−25.795
1.00
42.06
C


ATOM
525
CG
LEU
A
68
68.062
−2.356
−26.561
1.00
42.82
C


ATOM
526
CD1
LEU
A
68
67.123
−1.619
−27.518
1.00
37.15
C


ATOM
527
CD2
LEU
A
68
68.630
−3.617
−27.193
1.00
45.54
C


ATOM
528
C
LEU
A
68
71.342
−1.215
−26.521
1.00
42.90
C


ATOM
529
O
LEU
A
68
71.347
−0.010
−26.820
1.00
41.46
O


ATOM
530
N
ARG
A
69
72.031
−2.141
−27.196
1.00
42.96
N


ATOM
531
CA
ARG
A
69
72.635
−1.810
−28.465
1.00
43.33
C


ATOM
532
CB
ARG
A
69
74.071
−2.295
−28.521
1.00
44.06
C


ATOM
533
CG
ARG
A
69
74.908
−1.467
−29.419
1.00
44.93
C


ATOM
534
CD
ARG
A
69
76.347
−1.648
−29.074
1.00
51.01
C


ATOM
535
NE
ARG
A
69
77.032
−2.495
−30.046
1.00
55.03
N


ATOM
536
CZ
ARG
A
69
77.938
−2.041
−30.924
1.00
59.47
C


ATOM
537
NH1
ARG
A
69
78.259
−0.733
−30.942
1.00
59.92
N


ATOM
538
NH2
ARG
A
69
78.520
−2.876
−31.794
1.00
52.94
N


ATOM
539
C
ARG
A
69
71.867
−2.458
−29.589
1.00
43.41
C


ATOM
540
O
ARG
A
69
71.684
−3.661
−29.590
1.00
42.37
O


ATOM
541
N
ILE
A
70
71.416
−1.646
−30.545
1.00
43.65
N


ATOM
542
CA
ILE
A
70
70.858
−2.153
−31.779
1.00
44.23
C


ATOM
543
CB
ILE
A
70
69.492
−1.515
−32.157
1.00
44.17
C


ATOM
544
CG1
ILE
A
70
68.603
−1.333
−30.942
1.00
45.74
C


ATOM
545
CD1
ILE
A
70
67.758
−0.131
−31.117
1.00
46.30
C


ATOM
546
CG2
ILE
A
70
68.756
−2.351
−33.172
1.00
43.47
C


ATOM
547
C
ILE
A
70
71.856
−1.934
−32.893
1.00
44.58
C


ATOM
548
O
ILE
A
70
72.153
−0.792
−33.282
1.00
45.70
O


ATOM
549
N
SER
A
71
72.376
−3.022
−33.425
1.00
45.40
N


ATOM
550
CA
SER
A
71
73.387
−2.879
−34.435
1.00
46.26
C


ATOM
551
CB
SER
A
71
74.597
−3.736
−34.104
1.00
46.66
C


ATOM
552
OG
SER
A
71
74.223
−5.080
−34.154
1.00
46.90
O


ATOM
553
C
SER
A
71
72.788
−3.238
−35.776
1.00
46.26
C


ATOM
554
O
SER
A
71
71.702
−3.811
−35.833
1.00
45.27
O


ATOM
555
N
ASP
A
72
73.491
−2.855
−36.845
1.00
47.04
N


ATOM
556
CA
ASP
A
72
73.083
−3.164
−38.220
1.00
47.40
C


ATOM
557
CB
ASP
A
72
73.125
−4.671
−38.470
1.00
47.74
C


ATOM
558
CG
ASP
A
72
73.180
−5.019
−39.934
1.00
51.59
C


ATOM
559
OD1
ASP
A
72
73.693
−4.202
−40.771
1.00
53.46
O


ATOM
560
OD2
ASP
A
72
72.705
−6.140
−40.238
1.00
56.93
O


ATOM
561
C
ASP
A
72
71.704
−2.556
−38.534
1.00
46.75
C


ATOM
562
O
ASP
A
72
70.796
−3.217
−39.079
1.00
46.48
O


ATOM
563
N
LEU
A
73
71.601
−1.275
−38.183
1.00
46.13
N


ATOM
564
CA
LEU
A
73
70.406
−0.467
−38.296
1.00
45.96
C


ATOM
565
CB
LEU
A
73
70.745
0.931
−37.780
1.00
45.33
C


ATOM
566
CG
LEU
A
73
70.287
1.479
−36.425
1.00
48.34
C


ATOM
567
CD1
LEU
A
73
69.586
0.448
−35.493
1.00
42.67
C


ATOM
568
CD2
LEU
A
73
71.423
2.297
−35.755
1.00
49.05
C


ATOM
569
C
LEU
A
73
69.946
−0.366
−39.742
1.00
46.10
C


ATOM
570
O
LEU
A
73
70.764
−0.352
−40.660
1.00
44.78
O


ATOM
571
N
ARG
A
74
68.631
−0.281
−39.934
1.00
46.57
N


ATOM
572
CA
ARG
A
74
68.040
−0.106
−41.264
1.00
47.37
C


ATOM
573
CB
ARG
A
74
67.637
−1.474
−41.849
1.00
46.77
C


ATOM
574
CG
ARG
A
74
66.719
−2.239
−40.899
1.00
49.24
C


ATOM
575
CD
ARG
A
74
66.663
−3.759
−41.079
1.00
50.32
C


ATOM
576
NE
ARG
A
74
67.971
−4.409
−40.931
1.00
53.80
N


ATOM
577
CZ
ARG
A
74
68.136
−5.671
−40.534
1.00
55.17
C


ATOM
578
NH1
ARG
A
74
67.079
−6.433
−40.214
1.00
53.89
N


ATOM
579
NH2
ARG
A
74
69.367
−6.169
−40.440
1.00
55.31
N


ATOM
580
C
ARG
A
74
66.851
0.854
−41.114
1.00
46.54
C


ATOM
581
O
ARG
A
74
66.367
1.069
−39.989
1.00
46.24
O


ATOM
582
N
VAL
A
75
66.407
1.456
−42.221
1.00
46.74
N


ATOM
583
CA
VAL
A
75
65.304
2.453
−42.211
1.00
47.37
C


ATOM
584
CB
VAL
A
75
64.850
2.870
−43.638
1.00
47.20
C


ATOM
585
CG1
VAL
A
75
63.727
3.897
−43.563
1.00
48.39
C


ATOM
586
CG2
VAL
A
75
65.979
3.477
−44.373
1.00
45.91
C


ATOM
587
C
VAL
A
75
64.073
2.053
−41.387
1.00
47.49
C


ATOM
588
O
VAL
A
75
63.434
2.919
−40.786
1.00
48.41
O


ATOM
589
N
GLU
A
76
63.774
0.748
−41.340
1.00
47.38
N


ATOM
590
CA
GLU
A
76
62.578
0.186
−40.682
1.00
47.03
C


ATOM
591
CB
GLU
A
76
62.327
−1.264
−41.122
1.00
46.90
C


ATOM
592
CG
GLU
A
76
62.075
−1.440
−42.631
1.00
50.85
C


ATOM
593
CD
GLU
A
76
63.370
−1.574
−43.459
1.00
56.49
C


ATOM
594
OE1
GLU
A
76
64.438
−1.844
−42.855
1.00
56.84
O


ATOM
595
OE2
GLU
A
76
63.321
−1.414
−44.721
1.00
60.06
O


ATOM
596
C
GLU
A
76
62.681
0.239
−39.173
1.00
46.09
C


ATOM
597
O
GLU
A
76
61.694
0.020
−38.485
1.00
46.19
O


ATOM
598
N
ASP
A
77
63.880
0.526
−38.662
1.00
45.73
N


ATOM
599
CA
ASP
A
77
64.123
0.677
−37.224
1.00
44.49
C


ATOM
600
CB
ASP
A
77
65.557
0.277
−36.855
1.00
44.34
C


ATOM
601
CG
ASP
A
77
65.839
−1.207
−37.086
1.00
47.06
C


ATOM
602
OD1
ASP
A
77
64.964
−2.086
−36.810
1.00
51.98
O


ATOM
603
OD2
ASP
A
77
66.959
−1.515
−37.546
1.00
50.67
O


ATOM
604
C
ASP
A
77
63.820
2.086
−36.705
1.00
44.17
C


ATOM
605
O
ASP
A
77
63.795
2.288
−35.501
1.00
43.66
O


ATOM
606
N
SER
A
78
63.606
3.056
−37.601
1.00
43.76
N


ATOM
607
CA
SER
A
78
63.254
4.403
−37.176
1.00
43.69
C


ATOM
608
CB
SER
A
78
62.975
5.334
−38.352
1.00
43.43
C


ATOM
609
OG
SER
A
78
64.074
5.409
−39.232
1.00
42.84
O


ATOM
610
C
SER
A
78
62.026
4.342
−36.304
1.00
44.36
C


ATOM
611
O
SER
A
78
61.112
3.604
−36.591
1.00
45.78
O


ATOM
612
N
GLY
A
79
62.009
5.134
−35.239
1.00
44.36
N


ATOM
613
CA
GLY
A
79
60.931
5.138
−34.284
1.00
43.30
C


ATOM
614
C
GLY
A
79
61.435
5.586
−32.936
1.00
43.00
C


ATOM
615
O
GLY
A
79
62.541
6.110
−32.830
1.00
43.25
O


ATOM
616
N
THR
A
80
60.585
5.415
−31.929
1.00
42.21
N


ATOM
617
CA
THR
A
80
60.837
5.861
−30.587
1.00
42.60
C


ATOM
618
CB
THR
A
80
59.658
6.697
−30.047
1.00
43.53
C


ATOM
619
OG1
THR
A
80
59.501
7.860
−30.873
1.00
45.61
O


ATOM
620
CG2
THR
A
80
59.869
7.123
−28.565
1.00
44.78
C


ATOM
621
C
THR
A
80
61.047
4.587
−29.775
1.00
42.21
C


ATOM
622
O
THR
A
80
60.308
3.637
−29.924
1.00
41.06
O


ATOM
623
N
TYR
A
81
62.115
4.578
−28.973
1.00
41.77
N


ATOM
624
CA
TYR
A
81
62.463
3.459
−28.122
1.00
40.78
C


ATOM
625
CB
TYR
A
81
63.891
2.998
−28.407
1.00
39.74
C


ATOM
626
CG
TYR
A
81
64.031
2.350
−29.774
1.00
40.54
C


ATOM
627
CD1
TYR
A
81
64.286
0.993
−29.909
1.00
38.77
C


ATOM
628
CE1
TYR
A
81
64.400
0.414
−31.226
1.00
42.36
C


ATOM
629
CZ
TYR
A
81
64.245
1.208
−32.347
1.00
37.03
C


ATOM
630
OH
TYR
A
81
64.353
0.685
−33.633
1.00
39.33
O


ATOM
631
CE2
TYR
A
81
63.975
2.523
−32.218
1.00
38.69
C


ATOM
632
CD2
TYR
A
81
63.891
3.106
−30.932
1.00
40.06
C


ATOM
633
C
TYR
A
81
62.382
3.935
−26.715
1.00
40.90
C


ATOM
634
O
TYR
A
81
62.766
5.033
−26.462
1.00
40.58
O


ATOM
635
N
LYS
A
82
61.896
3.088
−25.819
1.00
41.29
N


ATOM
636
CA
LYS
A
82
61.850
3.350
−24.388
1.00
42.71
C


ATOM
637
CB
LYS
A
82
60.422
3.634
−23.944
1.00
42.24
C


ATOM
638
CG
LYS
A
82
59.994
4.963
−24.379
1.00
44.27
C


ATOM
639
CD
LYS
A
82
58.731
5.424
−23.596
1.00
45.18
C


ATOM
640
CE
LYS
A
82
58.202
6.727
−24.265
1.00
46.00
C


ATOM
641
NZ
LYS
A
82
57.117
7.194
−23.357
1.00
56.94
N


ATOM
642
C
LYS
A
82
62.315
2.107
−23.650
1.00
42.18
C


ATOM
643
O
LYS
A
82
62.061
1.027
−24.094
1.00
40.76
O


ATOM
644
N
CYS
A
83
63.042
2.318
−22.560
1.00
43.46
N


ATOM
645
CA
CYS
A
83
63.439
1.309
−21.629
1.00
44.61
C


ATOM
646
CB
CYS
A
83
64.761
1.693
−20.986
1.00
45.96
C


ATOM
647
SG
CYS
A
83
64.973
3.375
−20.311
1.00
48.94
S


ATOM
648
C
CYS
A
83
62.409
1.325
−20.534
1.00
45.71
C


ATOM
649
O
CYS
A
83
61.631
2.271
−20.456
1.00
46.30
O


ATOM
650
N
GLN
A
84
62.385
0.287
−19.692
1.00
43.77
N


ATOM
651
CA
GLN
A
84
61.568
0.350
−18.534
1.00
42.92
C


ATOM
652
CB
GLN
A
84
60.203
−0.292
−18.790
1.00
42.16
C


ATOM
653
CG
GLN
A
84
59.330
−0.191
−17.551
1.00
43.09
C


ATOM
654
CD
GLN
A
84
57.821
−0.376
−17.766
1.00
46.36
C


ATOM
655
OE1
GLN
A
84
57.016
0.257
−17.094
1.00
50.63
O


ATOM
656
NE2
GLN
A
84
57.443
−1.260
−18.660
1.00
44.97
N


ATOM
657
C
GLN
A
84
62.286
−0.351
−17.413
1.00
42.33
C


ATOM
658
O
GLN
A
84
62.766
−1.454
−17.614
1.00
40.11
O


ATOM
659
N
ALA
A
85
62.403
0.310
−16.256
1.00
42.76
N


ATOM
660
CA
ALA
A
85
62.992
−0.323
−15.027
1.00
43.66
C


ATOM
661
CB
ALA
A
85
63.803
0.674
−14.213
1.00
42.44
C


ATOM
662
C
ALA
A
85
61.854
−0.875
−14.159
1.00
43.77
C


ATOM
663
O
ALA
A
85
60.904
−0.143
−13.877
1.00
42.85
O


ATOM
664
N
PHE
A
86
61.986
−2.140
−13.760
1.00
42.59
N


ATOM
665
CA
PHE
A
86
61.015
−2.843
−12.918
1.00
43.37
C


ATOM
666
CB
PHE
A
86
60.674
−4.222
−13.484
1.00
41.48
C


ATOM
667
CG
PHE
A
86
60.048
−4.178
−14.879
1.00
43.52
C


ATOM
668
CD1
PHE
A
86
58.751
−3.695
−15.063
1.00
40.20
C


ATOM
669
CE1
PHE
A
86
58.158
−3.672
−16.327
1.00
38.57
C


ATOM
670
CZ
PHE
A
86
58.871
−4.088
−17.428
1.00
42.08
C


ATOM
671
CE2
PHE
A
86
60.178
−4.538
−17.273
1.00
43.63
C


ATOM
672
CD2
PHE
A
86
60.765
−4.568
−15.998
1.00
42.39
C


ATOM
673
C
PHE
A
86
61.564
−2.990
−11.487
1.00
44.25
C


ATOM
674
O
PHE
A
86
62.745
−3.227
−11.275
1.00
45.17
O


ATOM
675
N
TYR
A
87
60.673
−2.891
−10.514
1.00
44.26
N


ATOM
676
CA
TYR
A
87
61.056
−2.955
−9.127
1.00
42.81
C


ATOM
677
CB
TYR
A
87
61.591
−1.595
−8.705
1.00
42.95
C


ATOM
678
CG
TYR
A
87
60.589
−0.506
−9.034
1.00
44.84
C


ATOM
679
CD1
TYR
A
87
60.593
0.094
−10.300
1.00
44.05
C


ATOM
680
CE1
TYR
A
87
59.685
1.047
−10.640
1.00
46.61
C


ATOM
681
CZ
TYR
A
87
58.730
1.425
−9.702
1.00
45.72
C


ATOM
682
OH
TYR
A
87
57.877
2.355
−10.081
1.00
48.88
O


ATOM
683
CE2
TYR
A
87
58.659
0.878
−8.442
1.00
45.57
C


ATOM
684
CD2
TYR
A
87
59.622
−0.126
−8.110
1.00
45.85
C


ATOM
685
C
TYR
A
87
59.820
−3.359
−8.308
1.00
42.27
C


ATOM
686
O
TYR
A
87
58.694
−3.482
−8.832
1.00
42.84
O


ATOM
687
N
VAL
A
88
60.017
−3.599
−7.022
1.00
41.80
N


ATOM
688
CA
VAL
A
88
58.912
−3.966
−6.147
1.00
40.05
C


ATOM
689
CB
VAL
A
88
59.180
−5.357
−5.568
1.00
40.65
C


ATOM
690
CG1
VAL
A
88
60.622
−5.432
−4.904
1.00
34.41
C


ATOM
691
CG2
VAL
A
88
59.093
−6.416
−6.658
1.00
36.97
C


ATOM
692
C
VAL
A
88
58.720
−2.893
−5.015
1.00
41.14
C


ATOM
693
O
VAL
A
88
59.646
−2.140
−4.619
1.00
42.19
O


ATOM
694
N
PHE
A
89
57.529
−2.846
−4.472
1.00
40.69
N


ATOM
695
CA
PHE
A
89
57.239
−1.957
−3.367
1.00
38.05
C


ATOM
696
CB
PHE
A
89
57.064
−0.483
−3.841
1.00
37.66
C


ATOM
697
CG
PHE
A
89
55.841
−0.218
−4.771
1.00
35.47
C


ATOM
698
CD1
PHE
A
89
55.948
−0.343
−6.141
1.00
34.15
C


ATOM
699
CE1
PHE
A
89
54.868
−0.074
−6.984
1.00
30.34
C


ATOM
700
CZ
PHE
A
89
53.716
0.379
−6.408
1.00
38.20
C


ATOM
701
CE2
PHE
A
89
53.627
0.586
−4.999
1.00
30.74
C


ATOM
702
CD2
PHE
A
89
54.662
0.290
−4.241
1.00
36.54
C


ATOM
703
C
PHE
A
89
56.012
−2.518
−2.694
1.00
39.07
C


ATOM
704
O
PHE
A
89
55.218
−3.234
−3.341
1.00
35.78
O


ATOM
705
N
PHE
A
90
55.886
−2.215
−1.394
1.00
38.51
N


ATOM
706
CA
PHE
A
90
54.693
−2.576
−0.621
1.00
39.88
C


ATOM
707
CB
PHE
A
90
54.993
−2.528
0.874
1.00
37.98
C


ATOM
708
CG
PHE
A
90
55.700
−3.740
1.386
1.00
37.62
C


ATOM
709
CD1
PHE
A
90
55.078
−5.003
1.336
1.00
35.79
C


ATOM
710
CE1
PHE
A
90
55.688
−6.126
1.895
1.00
37.83
C


ATOM
711
CZ
PHE
A
90
56.950
−6.030
2.476
1.00
38.12
C


ATOM
712
CE2
PHE
A
90
57.601
−4.739
2.526
1.00
38.60
C


ATOM
713
CD2
PHE
A
90
56.922
−3.620
1.998
1.00
37.29
C


ATOM
714
C
PHE
A
90
53.467
−1.698
−0.981
1.00
40.53
C


ATOM
715
O
PHE
A
90
53.605
−0.502
−1.196
1.00
40.32
O


ATOM
716
N
ALA
A
91
52.277
−2.306
−0.985
1.00
41.27
N


ATOM
717
CA
ALA
A
91
51.067
−1.617
−1.372
1.00
41.84
C


ATOM
718
CB
ALA
A
91
49.892
−2.513
−1.182
1.00
42.15
C


ATOM
719
C
ALA
A
91
50.860
−0.249
−0.668
1.00
43.70
C


ATOM
720
O
ALA
A
91
50.328
0.664
−1.280
1.00
43.35
O


ATOM
721
N
GLU
A
92
51.321
−0.091
0.581
1.00
44.95
N


ATOM
722
CA
GLU
A
92
51.195
1.188
1.293
1.00
45.93
C


ATOM
723
CB
GLU
A
92
50.780
0.942
2.711
1.00
46.65
C


ATOM
724
CG
GLU
A
92
49.555
0.079
2.779
1.00
48.11
C


ATOM
725
CD
GLU
A
92
48.913
0.127
4.131
1.00
57.18
C


ATOM
726
OE1
GLU
A
92
48.562
1.252
4.563
1.00
59.80
O


ATOM
727
OE2
GLU
A
92
48.750
−0.953
4.764
1.00
56.56
O


ATOM
728
C
GLU
A
92
52.446
2.067
1.252
1.00
47.30
C


ATOM
729
O
GLU
A
92
52.450
3.195
1.756
1.00
48.77
O


ATOM
730
N
ASP
A
93
53.503
1.616
0.598
1.00
46.55
N


ATOM
731
CA
ASP
A
93
54.636
2.501
0.483
1.00
46.41
C


ATOM
732
CB
ASP
A
93
55.884
1.692
0.182
1.00
45.51
C


ATOM
733
CG
ASP
A
93
57.082
2.561
−0.131
1.00
44.76
C


ATOM
734
OD1
ASP
A
93
58.026
2.046
−0.789
1.00
42.86
O


ATOM
735
OD2
ASP
A
93
57.072
3.754
0.253
1.00
42.99
O


ATOM
736
C
ASP
A
93
54.344
3.551
−0.605
1.00
46.69
C


ATOM
737
O
ASP
A
93
54.653
3.334
−1.774
1.00
46.46
O


ATOM
738
N
VAL
A
94
53.716
4.660
−0.218
1.00
46.68
N


ATOM
739
CA
VAL
A
94
53.276
5.672
−1.199
1.00
47.78
C


ATOM
740
CB
VAL
A
94
52.240
6.690
−0.629
1.00
47.50
C


ATOM
741
CG1
VAL
A
94
52.844
7.591
0.471
1.00
48.03
C


ATOM
742
CG2
VAL
A
94
51.023
5.941
−0.088
1.00
48.45
C


ATOM
743
C
VAL
A
94
54.439
6.375
−1.893
1.00
47.62
C


ATOM
744
O
VAL
A
94
54.323
6.822
−3.039
1.00
48.80
O


ATOM
745
N
GLY
A
95
55.577
6.444
−1.228
1.00
47.46
N


ATOM
746
CA
GLY
A
95
56.743
7.084
−1.829
1.00
46.54
C


ATOM
747
C
GLY
A
95
57.216
6.371
−3.077
1.00
46.80
C


ATOM
748
O
GLY
A
95
57.971
6.944
−3.858
1.00
48.77
O


ATOM
749
N
SER
A
96
56.789
5.125
−3.282
1.00
45.12
N


ATOM
750
CA
SER
A
96
57.316
4.299
−4.367
1.00
43.91
C


ATOM
751
CB
SER
A
96
57.806
2.951
−3.774
1.00
43.86
C


ATOM
752
OG
SER
A
96
59.082
3.050
−3.170
1.00
45.47
O


ATOM
753
C
SER
A
96
56.280
3.976
−5.464
1.00
43.04
C


ATOM
754
O
SER
A
96
56.556
3.141
−6.333
1.00
41.97
O


ATOM
755
N
ASN
A
97
55.083
4.582
−5.411
1.00
42.62
N


ATOM
756
CA
ASN
A
97
53.955
4.125
−6.262
1.00
41.42
C


ATOM
757
CB
ASN
A
97
52.664
3.995
−5.411
1.00
41.08
C


ATOM
758
CG
ASN
A
97
52.129
5.344
−4.941
1.00
42.94
C


ATOM
759
OD1
ASN
A
97
52.503
6.365
−5.465
1.00
46.83
O


ATOM
760
ND2
ASN
A
97
51.255
5.342
−3.965
1.00
40.83
N


ATOM
761
C
ASN
A
97
53.666
4.932
−7.525
1.00
42.28
C


ATOM
762
O
ASN
A
97
52.585
4.750
−8.141
1.00
41.82
O


ATOM
763
N
LYS
A
98
54.573
5.850
−7.915
1.00
42.02
N


ATOM
764
CA
LYS
A
98
54.248
6.732
−9.041
1.00
43.43
C


ATOM
765
CB
LYS
A
98
54.942
8.098
−8.900
1.00
44.23
C


ATOM
766
CG
LYS
A
98
55.210
8.508
−7.418
1.00
46.17
C


ATOM
767
CD
LYS
A
98
54.021
9.049
−6.764
1.00
48.50
C


ATOM
768
CE
LYS
A
98
54.408
9.875
−5.559
1.00
45.50
C


ATOM
769
NZ
LYS
A
98
54.697
8.979
−4.390
1.00
48.43
N


ATOM
770
C
LYS
A
98
54.460
6.112
−10.439
1.00
43.17
C


ATOM
771
O
LYS
A
98
54.025
6.663
−11.415
1.00
42.52
O


ATOM
772
N
GLY
A
99
55.057
4.929
−10.498
1.00
43.81
N


ATOM
773
CA
GLY
A
99
55.295
4.242
−11.742
1.00
43.60
C


ATOM
774
C
GLY
A
99
54.052
3.507
−12.181
1.00
42.19
C


ATOM
775
O
GLY
A
99
53.008
3.607
−11.544
1.00
42.85
O


ATOM
776
N
ALA
A
100
54.151
2.775
−13.283
1.00
40.39
N


ATOM
777
CA
ALA
A
100
53.014
1.974
−13.753
1.00
39.22
C


ATOM
778
CB
ALA
A
100
53.278
1.513
−15.205
1.00
36.47
C


ATOM
779
C
ALA
A
100
52.932
0.751
−12.819
1.00
38.50
C


ATOM
780
O
ALA
A
100
53.913
0.368
−12.262
1.00
38.16
O


ATOM
781
N
ILE
A
101
51.772
0.140
−12.652
1.00
38.62
N


ATOM
782
CA
ILE
A
101
51.638
−1.134
−11.945
1.00
38.55
C


ATOM
783
CB
ILE
A
101
50.190
−1.269
−11.405
1.00
40.06
C


ATOM
784
CG1
ILE
A
101
49.797
0.015
−10.598
1.00
42.79
C


ATOM
785
CD1
ILE
A
101
50.554
0.261
−9.310
1.00
39.48
C


ATOM
786
CG2
ILE
A
101
49.959
−2.667
−10.762
1.00
36.33
C


ATOM
787
C
ILE
A
101
51.767
−2.274
−12.951
1.00
39.19
C


ATOM
788
O
ILE
A
101
50.995
−2.357
−13.950
1.00
36.64
O


ATOM
789
N
ILE
A
102
52.677
−3.191
−12.663
1.00
39.81
N


ATOM
790
CA
ILE
A
102
52.909
−4.348
−13.578
1.00
39.64
C


ATOM
791
CB
ILE
A
102
54.454
−4.487
−13.734
1.00
39.59
C


ATOM
792
CG1
ILE
A
102
55.089
−3.117
−14.157
1.00
38.41
C


ATOM
793
CD1
ILE
A
102
54.460
−2.524
−15.511
1.00
33.86
C


ATOM
794
CG2
ILE
A
102
54.819
−5.583
−14.725
1.00
40.76
C


ATOM
795
C
ILE
A
102
52.195
−5.647
−13.073
1.00
39.13
C


ATOM
796
O
ILE
A
102
51.854
−6.530
−13.816
1.00
39.94
O


ATOM
797
N
GLY
A
103
52.050
−5.776
−11.775
1.00
39.01
N


ATOM
798
CA
GLY
A
103
51.334
−6.885
−11.213
1.00
38.49
C


ATOM
799
C
GLY
A
103
51.324
−6.752
−9.716
1.00
37.24
C


ATOM
800
O
GLY
A
103
51.882
−5.833
−9.130
1.00
36.17
O


ATOM
801
N
LEU
A
104
50.749
−7.742
−9.089
1.00
37.99
N


ATOM
802
CA
LEU
A
104
50.493
−7.683
−7.688
1.00
39.66
C


ATOM
803
CB
LEU
A
104
49.031
−7.210
−7.355
1.00
37.53
C


ATOM
804
CG
LEU
A
104
48.649
−7.290
−5.842
1.00
40.70
C


ATOM
805
CD1
LEU
A
104
47.171
−7.118
−5.505
1.00
39.27
C


ATOM
806
CD2
LEU
A
104
49.430
−6.275
−4.991
1.00
38.45
C


ATOM
807
C
LEU
A
104
50.744
−9.080
−7.236
1.00
40.91
C


ATOM
808
O
LEU
A
104
50.123
−10.019
−7.747
1.00
40.88
O


ATOM
809
N
MET
A
105
51.687
−9.213
−6.306
1.00
43.27
N


ATOM
810
CA
MET
A
105
51.982
−10.471
−5.649
1.00
45.57
C


ATOM
811
CB
MET
A
105
53.480
−10.581
−5.502
1.00
47.53
C


ATOM
812
CG
MET
A
105
54.143
−11.586
−6.445
1.00
56.01
C


ATOM
813
SD
MET
A
105
53.858
−11.477
−8.250
1.00
66.51
S


ATOM
814
CE
MET
A
105
54.839
−12.860
−8.841
1.00
57.93
C


ATOM
815
C
MET
A
105
51.291
−10.529
−4.289
1.00
44.27
C


ATOM
816
O
MET
A
105
51.143
−9.509
−3.650
1.00
43.68
O


ATOM
817
N
VAL
A
106
50.826
−11.700
−3.870
1.00
44.78
N


ATOM
818
CA
VAL
A
106
50.387
−11.916
−2.462
1.00
46.00
C


ATOM
819
CB
VAL
A
106
50.185
−13.396
−2.124
1.00
46.66
C


ATOM
820
CG1
VAL
A
106
51.551
−14.154
−2.328
1.00
47.69
C


ATOM
821
CG2
VAL
A
106
49.015
−13.959
−2.921
1.00
45.00
C


ATOM
822
C
VAL
A
106
51.431
−11.451
−1.442
1.00
46.49
C


ATOM
823
O
VAL
A
106
52.639
−11.733
−1.590
1.00
46.05
O


ATOM
824
N
GLY
A
107
50.942
−10.795
−0.390
1.00
45.74
N


ATOM
825
CA
GLY
A
107
51.799
−10.227
0.629
1.00
44.85
C


ATOM
826
C
GLY
A
107
51.784
−8.730
0.425
1.00
44.68
C


ATOM
827
O
GLY
A
107
52.526
−8.029
1.054
1.00
45.42
O


ATOM
828
N
GLY
A
108
50.939
−8.247
−0.480
1.00
43.98
N


ATOM
829
CA
GLY
A
108
50.840
−6.821
−0.790
1.00
43.08
C


ATOM
830
C
GLY
A
108
52.084
−6.255
−1.442
1.00
42.91
C


ATOM
831
O
GLY
A
108
52.434
−5.089
−1.242
1.00
42.44
O


ATOM
832
N
VAL
A
109
52.719
−7.046
−2.291
1.00
43.26
N


ATOM
833
CA
VAL
A
109
53.948
−6.599
−2.957
1.00
42.66
C


ATOM
834
CB
VAL
A
109
55.000
−7.751
−2.883
1.00
43.69
C


ATOM
835
CG1
VAL
A
109
56.193
−7.522
−3.854
1.00
42.19
C


ATOM
836
CG2
VAL
A
109
55.408
−8.004
−1.423
1.00
42.91
C


ATOM
837
C
VAL
A
109
53.554
−6.242
−4.387
1.00
42.97
C


ATOM
838
O
VAL
A
109
53.096
−7.113
−5.167
1.00
42.03
O


ATOM
839
N
VAL
A
110
53.665
−4.958
−4.723
1.00
42.17
N


ATOM
840
CA
VAL
A
110
53.415
−4.541
−6.054
1.00
40.80
C


ATOM
841
CB
VAL
A
110
52.310
−3.424
−6.153
1.00
44.02
C


ATOM
842
CG1
VAL
A
110
52.372
−2.549
−7.365
1.00
42.03
C


ATOM
843
CG2
VAL
A
110
51.848
−2.769
−4.779
1.00
41.33
C


ATOM
844
C
VAL
A
110
54.630
−4.554
−6.979
1.00
41.32
C


ATOM
845
O
VAL
A
110
55.745
−4.275
−6.542
1.00
41.11
O


ATOM
846
N
ILE
A
111
54.454
−4.937
−8.242
1.00
40.50
N


ATOM
847
CA
ILE
A
111
55.520
−4.758
−9.218
1.00
39.74
C


ATOM
848
CB
ILE
A
111
55.693
−6.002
−10.151
1.00
42.13
C


ATOM
849
CG1
ILE
A
111
55.947
−7.264
−9.286
1.00
44.65
C


ATOM
850
CD1
ILE
A
111
55.492
−8.577
−9.969
1.00
51.14
C


ATOM
851
CG2
ILE
A
111
56.814
−5.793
−11.241
1.00
39.84
C


ATOM
852
C
ILE
A
111
55.308
−3.462
−9.981
1.00
38.67
C


ATOM
853
O
ILE
A
111
54.231
−3.209
−10.519
1.00
39.08
O


ATOM
854
N
GLY
A
112
56.314
−2.594
−9.989
1.00
37.53
N


ATOM
855
CA
GLY
A
112
56.135
−1.251
−10.626
1.00
36.49
C


ATOM
856
C
GLY
A
112
57.100
−1.138
−11.758
1.00
37.46
C


ATOM
857
O
GLY
A
112
58.065
−1.929
−11.859
1.00
37.41
O


ATOM
858
N
GLY
A
113
56.787
−0.246
−12.688
1.00
38.41
N


ATOM
859
CA
GLY
A
113
57.674
0.011
−13.832
1.00
39.24
C


ATOM
860
C
GLY
A
113
57.818
1.473
−14.008
1.00
38.63
C


ATOM
861
O
GLY
A
113
56.810
2.152
−13.932
1.00
40.39
O


ATOM
862
N
GLU
A
114
59.046
1.981
−14.149
1.00
40.63
N


ATOM
863
CA
GLU
A
114
59.293
3.395
−14.613
1.00
42.64
C


ATOM
864
CB
GLU
A
114
60.340
4.176
−13.800
1.00
42.87
C


ATOM
865
CG
GLU
A
114
59.955
4.975
−12.595
1.00
50.17
C


ATOM
866
CD
GLU
A
114
58.981
6.134
−12.814
1.00
55.34
C


ATOM
867
OE1
GLU
A
114
59.160
6.926
−13.769
1.00
61.09
O


ATOM
868
OE2
GLU
A
114
58.080
6.310
−11.959
1.00
57.31
O


ATOM
869
C
GLU
A
114
59.949
3.324
−15.964
1.00
42.42
C


ATOM
870
O
GLU
A
114
60.953
2.626
−16.132
1.00
43.93
O


ATOM
871
N
LYS
A
115
59.503
4.152
−16.876
1.00
42.38
N


ATOM
872
CA
LYS
A
115
60.016
4.192
−18.240
1.00
42.73
C


ATOM
873
CB
LYS
A
115
58.829
4.219
−19.234
1.00
44.06
C


ATOM
874
CG
LYS
A
115
58.069
2.975
−19.365
1.00
47.53
C


ATOM
875
CD
LYS
A
115
57.203
3.006
−20.629
1.00
53.24
C


ATOM
876
CE
LYS
A
115
56.289
1.786
−20.589
1.00
54.45
C


ATOM
877
NZ
LYS
A
115
55.402
1.783
−21.803
1.00
61.37
N


ATOM
878
C
LYS
A
115
60.796
5.484
−18.507
1.00
41.16
C


ATOM
879
O
LYS
A
115
60.463
6.586
−18.007
1.00
40.33
O


ATOM
880
N
GLY
A
116
61.804
5.356
−19.341
1.00
40.59
N


ATOM
881
CA
GLY
A
116
62.579
6.518
−19.817
1.00
39.49
C


ATOM
882
C
GLY
A
116
61.717
7.400
−20.692
1.00
40.21
C


ATOM
883
O
GLY
A
116
60.615
6.997
−21.112
1.00
38.64
O


ATOM
884
N
ALA
A
117
62.212
8.605
−20.987
1.00
41.52
N


ATOM
885
CA
ALA
A
117
61.472
9.547
−21.817
1.00
42.80
C


ATOM
886
CB
ALA
A
117
62.048
10.974
−21.662
1.00
44.34
C


ATOM
887
C
ALA
A
117
61.451
9.187
−23.295
1.00
43.54
C


ATOM
888
O
ALA
A
117
60.687
9.767
−24.039
1.00
44.55
O


ATOM
889
N
GLY
A
118
62.303
8.280
−23.760
1.00
43.70
N


ATOM
890
CA
GLY
A
118
62.260
7.966
−25.184
1.00
41.16
C


ATOM
891
C
GLY
A
118
63.528
8.367
−25.883
1.00
41.11
C


ATOM
892
O
GLY
A
118
64.195
9.321
−25.473
1.00
41.17
O


ATOM
893
N
THR
A
119
63.870
7.617
−26.927
1.00
40.36
N


ATOM
894
CA
THR
A
119
64.921
7.982
−27.896
1.00
39.93
C


ATOM
895
CB
THR
A
119
66.082
6.926
−27.933
1.00
39.67
C


ATOM
896
OG1
THR
A
119
66.775
6.941
−26.682
1.00
36.77
O


ATOM
897
CG2
THR
A
119
67.130
7.237
−29.078
1.00
37.93
C


ATOM
898
C
THR
A
119
64.168
7.915
−29.198
1.00
40.54
C


ATOM
899
O
THR
A
119
63.610
6.841
−29.510
1.00
41.01
O


ATOM
900
N
ALA
A
120
64.042
9.058
−29.886
1.00
39.18
N


ATOM
901
CA
ALA
A
120
63.474
9.123
−31.240
1.00
39.16
C


ATOM
902
CB
ALA
A
120
62.887
10.544
−31.521
1.00
39.16
C


ATOM
903
C
ALA
A
120
64.617
8.819
−32.234
1.00
38.85
C


ATOM
904
O
ALA
A
120
65.576
9.562
−32.300
1.00
37.63
O


ATOM
905
N
LEU
A
121
64.560
7.680
−32.925
1.00
39.42
N


ATOM
906
CA
LEU
A
121
65.634
7.279
−33.798
1.00
39.83
C


ATOM
907
CB
LEU
A
121
66.049
5.819
−33.513
1.00
40.42
C


ATOM
908
CG
LEU
A
121
66.974
5.144
−34.569
1.00
40.59
C


ATOM
909
CD1
LEU
A
121
68.396
5.751
−34.587
1.00
38.95
C


ATOM
910
CD2
LEU
A
121
67.007
3.604
−34.288
1.00
41.03
C


ATOM
911
C
LEU
A
121
65.256
7.492
−35.280
1.00
40.22
C


ATOM
912
O
LEU
A
121
64.147
7.165
−35.705
1.00
39.00
O


ATOM
913
N
THR
A
122
66.171
8.081
−36.057
1.00
40.54
N


ATOM
914
CA
THR
A
122
65.968
8.199
−37.476
1.00
40.45
C


ATOM
915
CB
THR
A
122
65.896
9.701
−37.936
1.00
41.48
C


ATOM
916
OG1
THR
A
122
64.702
10.294
−37.406
1.00
44.87
O


ATOM
917
CG2
THR
A
122
65.878
9.852
−39.480
1.00
39.71
C


ATOM
918
C
THR
A
122
67.138
7.487
−38.092
1.00
40.29
C


ATOM
919
O
THR
A
122
68.279
7.874
−37.877
1.00
39.60
O


ATOM
920
N
VAL
A
123
66.875
6.408
−38.818
1.00
40.92
N


ATOM
921
CA
VAL
A
123
67.930
5.869
−39.707
1.00
41.20
C


ATOM
922
CB
VAL
A
123
68.359
4.405
−39.388
1.00
41.03
C


ATOM
923
CG1
VAL
A
123
67.511
3.799
−38.233
1.00
39.09
C


ATOM
924
CG2
VAL
A
123
68.518
3.549
−40.620
1.00
40.22
C


ATOM
925
C
VAL
A
123
67.788
6.260
−41.186
1.00
42.10
C


ATOM
926
O
VAL
A
123
66.767
6.047
−41.842
1.00
42.13
O


ATOM
927
N
LYS
A
124
68.836
6.892
−41.677
1.00
43.39
N


ATOM
928
CA
LYS
A
124
68.864
7.415
−43.030
1.00
44.97
C


ATOM
929
CB
LYS
A
124
70.047
8.388
−43.187
1.00
44.33
C


ATOM
930
CG
LYS
A
124
69.902
9.697
−42.471
1.00
43.86
C


ATOM
931
CD
LYS
A
124
71.265
10.355
−42.186
1.00
42.06
C


ATOM
932
CE
LYS
A
124
71.842
11.023
−43.404
1.00
46.07
C


ATOM
933
NZ
LYS
A
124
73.312
11.366
−43.269
1.00
46.30
N


ATOM
934
C
LYS
A
124
68.989
6.198
−43.984
1.00
45.36
C


ATOM
935
O
LYS
A
124
69.693
5.235
−43.663
1.00
45.33
O


ATOM
936
N
ALA
A
125
68.274
6.214
−45.110
1.00
46.08
N


ATOM
937
CA
ALA
A
125
68.489
5.175
−46.141
1.00
47.11
C


ATOM
938
CB
ALA
A
125
67.648
5.451
−47.384
1.00
46.76
C


ATOM
939
C
ALA
A
125
69.972
5.123
−46.500
1.00
47.33
C


ATOM
940
O
ALA
A
125
70.618
6.175
−46.508
1.00
47.44
O


ATOM
941
N
ALA
A
126
70.528
3.890
−46.738
1.00
48.74
N


ATOM
942
CA
ALA
A
126
71.863
3.817
−47.444
1.00
49.81
C


ATOM
943
CB
ALA
A
126
72.337
2.362
−47.714
1.00
49.59
C


ATOM
944
C
ALA
A
126
71.800
4.577
−48.758
1.00
49.59
C


ATOM
945
O
ALA
A
126
70.772
4.531
−49.478
1.00
51.31
O


ATOM
946
OXT
ALA
A
126
72.764
5.235
−49.161
1.00
51.16
O


ATOM
947
N
ALA
B
1
32.574
−25.808
−7.345
1.00
54.95
N


ATOM
948
CA
ALA
B
1
31.899
−24.453
−7.214
1.00
54.95
C


ATOM
949
CB
ALA
B
1
32.851
−23.438
−6.634
1.00
55.01
C


ATOM
950
C
ALA
B
1
31.283
−23.899
−8.498
1.00
54.51
C


ATOM
951
O
ALA
B
1
31.993
−23.349
−9.338
1.00
55.95
O


ATOM
952
N
TRP
B
2
29.963
−23.999
−8.630
1.00
53.08
N


ATOM
953
CA
TRP
B
2
29.268
−23.472
−9.820
1.00
50.94
C


ATOM
954
CB
TRP
B
2
29.049
−24.605
−10.808
1.00
51.28
C


ATOM
955
CG
TRP
B
2
28.244
−25.758
−10.275
1.00
51.82
C


ATOM
956
CD1
TRP
B
2
28.645
−26.700
−9.352
1.00
52.56
C


ATOM
957
NE1
TRP
B
2
27.625
−27.612
−9.141
1.00
53.31
N


ATOM
958
CE2
TRP
B
2
26.550
−27.281
−9.932
1.00
51.80
C


ATOM
959
CD2
TRP
B
2
26.903
−26.123
−10.670
1.00
51.84
C


ATOM
960
CE3
TRP
B
2
25.970
−25.573
−11.562
1.00
51.22
C


ATOM
961
CZ3
TRP
B
2
24.719
−26.207
−11.705
1.00
52.11
C


ATOM
962
CH2
TRP
B
2
24.404
−27.365
−10.954
1.00
52.45
C


ATOM
963
CZ2
TRP
B
2
25.303
−27.907
−10.064
1.00
51.92
C


ATOM
964
C
TRP
B
2
27.938
−22.763
−9.508
1.00
49.34
C


ATOM
965
O
TRP
B
2
27.440
−22.864
−8.388
1.00
48.53
O


ATOM
966
N
VAL
B
3
27.368
−22.056
−10.497
1.00
47.43
N


ATOM
967
CA
VAL
B
3
26.076
−21.354
−10.319
1.00
45.64
C


ATOM
968
CB
VAL
B
3
26.099
−19.865
−10.731
1.00
45.32
C


ATOM
969
CG1
VAL
B
3
24.721
−19.227
−10.539
1.00
42.93
C


ATOM
970
CG2
VAL
B
3
27.168
−19.097
−9.887
1.00
45.26
C


ATOM
971
C
VAL
B
3
24.945
−22.081
−11.021
1.00
45.65
C


ATOM
972
O
VAL
B
3
24.996
−22.334
−12.239
1.00
45.33
O


ATOM
973
N
ASP
B
4
23.951
−22.435
−10.211
1.00
44.65
N


ATOM
974
CA
ASP
B
4
22.792
−23.198
−10.608
1.00
44.39
C


ATOM
975
CB
ASP
B
4
22.440
−24.131
−9.458
1.00
44.31
C


ATOM
976
CG
ASP
B
4
21.422
−25.186
−9.834
1.00
48.07
C


ATOM
977
OD1
ASP
B
4
20.972
−25.212
−11.005
1.00
48.90
O


ATOM
978
OD2
ASP
B
4
21.052
−25.997
−8.932
1.00
51.27
O


ATOM
979
C
ASP
B
4
21.621
−22.242
−10.868
1.00
44.17
C


ATOM
980
O
ASP
B
4
20.926
−21.829
−9.913
1.00
45.13
O


ATOM
981
N
GLN
B
5
21.411
−21.881
−12.140
1.00
41.99
N


ATOM
982
CA
GLN
B
5
20.330
−20.945
−12.536
1.00
40.63
C


ATOM
983
CB
GLN
B
5
20.776
−20.017
−13.679
1.00
38.50
C


ATOM
984
CG
GLN
B
5
19.743
−18.908
−14.001
1.00
38.32
C


ATOM
985
CD
GLN
B
5
20.265
−17.971
−15.026
1.00
40.18
C


ATOM
986
OE1
GLN
B
5
21.484
−17.928
−15.203
1.00
40.72
O


ATOM
987
NE2
GLN
B
5
19.367
−17.207
−15.738
1.00
32.03
N


ATOM
988
C
GLN
B
5
19.078
−21.717
−12.978
1.00
40.31
C


ATOM
989
O
GLN
B
5
19.183
−22.575
−13.867
1.00
40.15
O


ATOM
990
N
THR
B
6
17.928
−21.407
−12.360
1.00
40.19
N


ATOM
991
CA
THR
B
6
16.597
−21.960
−12.747
1.00
41.32
C


ATOM
992
CB
THR
B
6
16.104
−23.106
−11.802
1.00
42.19
C


ATOM
993
OG1
THR
B
6
16.242
−22.695
−10.438
1.00
45.35
O


ATOM
994
CG2
THR
B
6
16.930
−24.421
−11.980
1.00
42.80
C


ATOM
995
C
THR
B
6
15.521
−20.844
−12.901
1.00
40.56
C


ATOM
996
O
THR
B
6
15.543
−19.855
−12.194
1.00
41.21
O


ATOM
997
N
PRO
B
7
14.605
−20.982
−13.859
1.00
40.24
N


ATOM
998
CA
PRO
B
7
14.476
−22.120
−14.793
1.00
39.70
C


ATOM
999
CB
PRO
B
7
13.018
−22.018
−15.237
1.00
38.51
C


ATOM
1000
CG
PRO
B
7
12.763
−20.573
−15.267
1.00
37.58
C


ATOM
1001
CD
PRO
B
7
13.570
−19.975
−14.102
1.00
39.88
C


ATOM
1002
C
PRO
B
7
15.428
−21.915
−15.952
1.00
39.21
C


ATOM
1003
O
PRO
B
7
15.772
−20.760
−16.237
1.00
40.93
O


ATOM
1004
N
ARG
B
8
15.863
−22.985
−16.598
1.00
39.22
N


ATOM
1005
CA
ARG
B
8
16.691
−22.864
−17.793
1.00
41.90
C


ATOM
1006
CB
ARG
B
8
17.582
−24.141
−17.979
1.00
40.92
C


ATOM
1007
CG
ARG
B
8
19.021
−23.843
−17.244
1.00
46.48
C


ATOM
1008
CD
ARG
B
8
20.003
−25.051
−17.078
1.00
49.30
C


ATOM
1009
NE
ARG
B
8
20.903
−25.344
−18.231
1.00
58.14
N


ATOM
1010
CZ
ARG
B
8
21.129
−24.550
−19.298
1.00
60.29
C


ATOM
1011
NH1
ARG
B
8
21.970
−24.991
−20.239
1.00
62.88
N


ATOM
1012
NH2
ARG
B
8
20.541
−23.343
−19.446
1.00
55.02
N


ATOM
1013
C
ARG
B
8
15.916
−22.266
−19.062
1.00
41.20
C


ATOM
1014
O
ARG
B
8
16.488
−21.531
−19.915
1.00
39.59
O


ATOM
1015
N
THR
B
9
14.594
−22.472
−19.057
1.00
40.29
N


ATOM
1016
CA
THR
B
9
13.687
−22.185
−20.154
1.00
41.50
C


ATOM
1017
CB
THR
B
9
13.369
−23.496
−20.870
1.00
41.08
C


ATOM
1018
OG1
THR
B
9
14.478
−23.831
−21.716
1.00
44.54
O


ATOM
1019
CG2
THR
B
9
12.186
−23.397
−21.691
1.00
44.46
C


ATOM
1020
C
THR
B
9
12.420
−21.625
−19.532
1.00
41.17
C


ATOM
1021
O
THR
B
9
11.988
−22.105
−18.486
1.00
42.29
O


ATOM
1022
N
ALA
B
10
11.863
−20.577
−20.120
1.00
39.83
N


ATOM
1023
CA
ALA
B
10
10.527
−20.109
−19.709
1.00
39.81
C


ATOM
1024
CB
ALA
B
10
10.636
−19.150
−18.520
1.00
39.10
C


ATOM
1025
C
ALA
B
10
9.708
−19.486
−20.865
1.00
39.00
C


ATOM
1026
O
ALA
B
10
10.218
−18.783
−21.709
1.00
37.05
O


ATOM
1027
N
THR
B
11
8.433
−19.807
−20.926
1.00
41.44
N


ATOM
1028
CA
THR
B
11
7.504
−19.035
−21.763
1.00
42.21
C


ATOM
1029
CB
THR
B
11
7.116
−19.744
−23.092
1.00
43.19
C


ATOM
1030
OG1
THR
B
11
5.708
−19.620
−23.359
1.00
45.57
O


ATOM
1031
CG2
THR
B
11
7.568
−21.172
−23.089
1.00
43.44
C


ATOM
1032
C
THR
B
11
6.410
−18.391
−20.904
1.00
43.25
C


ATOM
1033
O
THR
B
11
5.846
−19.026
−20.001
1.00
42.68
O


ATOM
1034
N
LYS
B
12
6.255
−17.074
−21.067
1.00
43.20
N


ATOM
1035
CA
LYS
B
12
5.257
−16.353
−20.305
1.00
43.24
C


ATOM
1036
CB
LYS
B
12
5.922
−15.425
−19.313
1.00
43.55
C


ATOM
1037
CG
LYS
B
12
6.850
−16.125
−18.282
1.00
43.71
C


ATOM
1038
CD
LYS
B
12
6.045
−16.918
−17.255
1.00
46.08
C


ATOM
1039
CE
LYS
B
12
6.956
−17.432
−16.177
1.00
46.77
C


ATOM
1040
NZ
LYS
B
12
6.207
−18.212
−15.178
1.00
48.14
N


ATOM
1041
C
LYS
B
12
4.323
−15.587
−21.224
1.00
43.67
C


ATOM
1042
O
LYS
B
12
4.603
−15.377
−22.399
1.00
43.55
O


ATOM
1043
N
GLU
B
13
3.196
−15.198
−20.670
1.00
44.88
N


ATOM
1044
CA
GLU
B
13
2.183
−14.407
−21.349
1.00
45.97
C


ATOM
1045
CB
GLU
B
13
0.819
−14.763
−20.763
1.00
45.50
C


ATOM
1046
CG
GLU
B
13
−0.252
−14.954
−21.805
1.00
51.14
C


ATOM
1047
CD
GLU
B
13
−1.672
−15.025
−21.223
1.00
52.49
C


ATOM
1048
OE1
GLU
B
13
−2.214
−13.977
−20.736
1.00
56.84
O


ATOM
1049
OE2
GLU
B
13
−2.268
−16.136
−21.318
1.00
61.96
O


ATOM
1050
C
GLU
B
13
2.512
−12.959
−21.020
1.00
43.04
C


ATOM
1051
O
GLU
B
13
3.028
−12.701
−19.945
1.00
41.31
O


ATOM
1052
N
THR
B
14
2.223
−12.015
−21.916
1.00
41.79
N


ATOM
1053
CA
THR
B
14
2.424
−10.600
−21.549
1.00
41.84
C


ATOM
1054
CB
THR
B
14
2.091
−9.590
−22.653
1.00
41.46
C


ATOM
1055
OG1
THR
B
14
0.695
−9.668
−22.914
1.00
46.96
O


ATOM
1056
CG2
THR
B
14
2.850
−9.885
−23.954
1.00
39.14
C


ATOM
1057
C
THR
B
14
1.601
−10.261
−20.284
1.00
41.06
C


ATOM
1058
O
THR
B
14
0.519
−10.798
−20.082
1.00
39.53
O


ATOM
1059
N
GLY
B
15
2.167
−9.424
−19.419
1.00
39.95
N


ATOM
1060
CA
GLY
B
15
1.531
−9.033
−18.178
1.00
39.59
C


ATOM
1061
C
GLY
B
15
1.928
−9.927
−17.032
1.00
39.94
C


ATOM
1062
O
GLY
B
15
1.745
−9.553
−15.861
1.00
40.01
O


ATOM
1063
N
GLU
B
16
2.448
−11.112
−17.347
1.00
40.07
N


ATOM
1064
CA
GLU
B
16
2.963
−12.013
−16.311
1.00
41.17
C


ATOM
1065
CB
GLU
B
16
3.024
−13.455
−16.850
1.00
40.57
C


ATOM
1066
CG
GLU
B
16
1.656
−14.146
−16.761
1.00
41.94
C


ATOM
1067
CD
GLU
B
16
1.562
−15.517
−17.442
1.00
43.73
C


ATOM
1068
OE1
GLU
B
16
2.530
−16.134
−17.948
1.00
43.61
O


ATOM
1069
OE2
GLU
B
16
0.432
−16.009
−17.477
1.00
54.01
O


ATOM
1070
C
GLU
B
16
4.321
−11.577
−15.715
1.00
40.58
C


ATOM
1071
O
GLU
B
16
4.936
−10.595
−16.140
1.00
41.16
O


ATOM
1072
N
SER
B
17
4.803
−12.311
−14.732
1.00
40.31
N


ATOM
1073
CA
SER
B
17
6.133
−12.054
−14.205
1.00
39.94
C


ATOM
1074
CB
SER
B
17
5.987
−11.519
−12.797
1.00
40.72
C


ATOM
1075
OG
SER
B
17
5.762
−12.588
−11.942
1.00
41.64
O


ATOM
1076
C
SER
B
17
7.004
−13.346
−14.277
1.00
39.37
C


ATOM
1077
O
SER
B
17
6.488
−14.426
−14.552
1.00
39.99
O


ATOM
1078
N
LEU
B
18
8.320
−13.220
−14.120
1.00
39.17
N


ATOM
1079
CA
LEU
B
18
9.270
−14.346
−14.176
1.00
39.40
C


ATOM
1080
CB
LEU
B
18
10.217
−14.269
−15.412
1.00
39.88
C


ATOM
1081
CG
LEU
B
18
10.975
−15.464
−16.093
1.00
39.25
C


ATOM
1082
CD1
LEU
B
18
12.361
−15.081
−16.621
1.00
36.41
C


ATOM
1083
CD2
LEU
B
18
11.031
−16.801
−15.375
1.00
36.79
C


ATOM
1084
C
LEU
B
18
10.151
−14.217
−12.952
1.00
39.21
C


ATOM
1085
O
LEU
B
18
10.648
−13.131
−12.684
1.00
38.56
O


ATOM
1086
N
THR
B
19
10.350
−15.309
−12.208
1.00
39.51
N


ATOM
1087
CA
THR
B
19
11.356
−15.331
−11.145
1.00
38.61
C


ATOM
1088
CB
THR
B
19
10.745
−15.681
−9.777
1.00
39.40
C


ATOM
1089
OG1
THR
B
19
9.596
−14.859
−9.569
1.00
40.21
O


ATOM
1090
CG2
THR
B
19
11.734
−15.391
−8.613
1.00
37.97
C


ATOM
1091
C
THR
B
19
12.481
−16.291
−11.544
1.00
39.08
C


ATOM
1092
O
THR
B
19
12.242
−17.425
−11.918
1.00
38.36
O


ATOM
1093
N
ILE
B
20
13.713
−15.795
−11.510
1.00
39.84
N


ATOM
1094
CA
ILE
B
20
14.881
−16.577
−11.832
1.00
40.37
C


ATOM
1095
CB
ILE
B
20
15.752
−15.886
−12.869
1.00
41.04
C


ATOM
1096
CG1
ILE
B
20
14.963
−15.656
−14.189
1.00
41.04
C


ATOM
1097
CD1
ILE
B
20
15.801
−14.744
−15.167
1.00
40.82
C


ATOM
1098
CG2
ILE
B
20
17.039
−16.690
−13.157
1.00
37.32
C


ATOM
1099
C
ILE
B
20
15.653
−16.721
−10.544
1.00
42.32
C


ATOM
1100
O
ILE
B
20
15.910
−15.743
−9.821
1.00
42.02
O


ATOM
1101
N
ASN
B
21
16.009
−17.959
−10.235
1.00
43.42
N


ATOM
1102
CA
ASN
B
21
16.750
−18.232
−9.028
1.00
44.99
C


ATOM
1103
CB
ASN
B
21
15.975
−19.274
−8.234
1.00
45.42
C


ATOM
1104
CG
ASN
B
21
14.760
−18.676
−7.544
1.00
49.78
C


ATOM
1105
OD1
ASN
B
21
14.911
−17.898
−6.575
1.00
55.43
O


ATOM
1106
ND2
ASN
B
21
13.546
−19.031
−8.021
1.00
48.66
N


ATOM
1107
C
ASN
B
21
18.162
−18.714
−9.316
1.00
45.15
C


ATOM
1108
O
ASN
B
21
18.355
−19.604
−10.139
1.00
46.04
O


ATOM
1109
N
CYS
B
22
19.145
−18.141
−8.642
1.00
45.51
N


ATOM
1110
CA
CYS
B
22
20.512
−18.645
−8.738
1.00
46.56
C


ATOM
1111
CB
CYS
B
22
21.398
−17.616
−9.407
1.00
46.01
C


ATOM
1112
SG
CYS
B
22
20.937
−17.240
−11.134
1.00
54.66
S


ATOM
1113
C
CYS
B
22
21.094
−19.006
−7.382
1.00
46.14
C


ATOM
1114
O
CYS
B
22
20.802
−18.342
−6.400
1.00
45.68
O


ATOM
1115
N
VAL
B
23
21.914
−20.064
−7.348
1.00
46.34
N


ATOM
1116
CA
VAL
B
23
22.574
−20.552
−6.137
1.00
45.67
C


ATOM
1117
CB
VAL
B
23
21.951
−21.906
−5.581
1.00
45.26
C


ATOM
1118
CG1
VAL
B
23
22.335
−22.151
−4.112
1.00
44.69
C


ATOM
1119
CG2
VAL
B
23
20.461
−21.936
−5.697
1.00
46.49
C


ATOM
1120
C
VAL
B
23
24.018
−20.856
−6.513
1.00
46.67
C


ATOM
1121
O
VAL
B
23
24.255
−21.594
−7.477
1.00
46.49
O


ATOM
1122
N
LEU
B
24
24.964
−20.275
−5.775
1.00
47.05
N


ATOM
1123
CA
LEU
B
24
26.379
−20.661
−5.783
1.00
49.11
C


ATOM
1124
CB
LEU
B
24
27.194
−19.589
−5.042
1.00
48.19
C


ATOM
1125
CG
LEU
B
24
28.539
−19.018
−5.483
1.00
50.04
C


ATOM
1126
CD1
LEU
B
24
29.178
−18.189
−4.317
1.00
47.71
C


ATOM
1127
CD2
LEU
B
24
29.500
−20.085
−5.957
1.00
51.22
C


ATOM
1128
C
LEU
B
24
26.508
−21.967
−4.994
1.00
50.50
C


ATOM
1129
O
LEU
B
24
26.243
−21.987
−3.785
1.00
50.47
O


ATOM
1130
N
ARG
B
25
26.902
−23.047
−5.670
1.00
52.28
N


ATOM
1131
CA
ARG
B
25
27.026
−24.372
−5.044
1.00
53.42
C


ATOM
1132
CB
ARG
B
25
26.429
−25.461
−5.933
1.00
53.07
C


ATOM
1133
CG
ARG
B
25
25.046
−25.141
−6.419
1.00
51.09
C


ATOM
1134
CD
ARG
B
25
24.139
−26.318
−6.287
1.00
51.67
C


ATOM
1135
NE
ARG
B
25
22.742
−25.901
−6.377
1.00
52.28
N


ATOM
1136
CZ
ARG
B
25
21.895
−25.907
−5.354
1.00
51.59
C


ATOM
1137
NH1
ARG
B
25
22.299
−26.334
−4.157
1.00
51.61
N


ATOM
1138
NH2
ARG
B
25
20.644
−25.498
−5.532
1.00
50.56
N


ATOM
1139
C
ARG
B
25
28.483
−24.685
−4.733
1.00
55.51
C


ATOM
1140
O
ARG
B
25
29.364
−23.827
−4.909
1.00
55.95
O


ATOM
1141
N
ASP
B
26
28.724
−25.902
−4.238
1.00
57.67
N


ATOM
1142
CA
ASP
B
26
30.064
−26.414
−3.891
1.00
59.47
C


ATOM
1143
CB
ASP
B
26
30.592
−27.321
−5.009
1.00
59.83
C


ATOM
1144
CG
ASP
B
26
29.669
−28.511
−5.285
1.00
61.62
C


ATOM
1145
OD1
ASP
B
26
28.795
−28.416
−6.198
1.00
62.14
O


ATOM
1146
OD2
ASP
B
26
29.814
−29.530
−4.572
1.00
62.86
O


ATOM
1147
C
ASP
B
26
31.052
−25.293
−3.599
1.00
60.27
C


ATOM
1148
O
ASP
B
26
32.103
−25.207
−4.225
1.00
60.76
O


ATOM
1149
N
ALA
B
27
30.693
−24.433
−2.646
1.00
61.28
N


ATOM
1150
CA
ALA
B
27
31.493
−23.273
−2.307
1.00
61.93
C


ATOM
1151
CB
ALA
B
27
30.784
−22.014
−2.708
1.00
61.89
C


ATOM
1152
C
ALA
B
27
31.863
−23.212
−0.829
1.00
62.84
C


ATOM
1153
O
ALA
B
27
30.991
−23.186
0.053
1.00
63.36
O


ATOM
1154
N
SER
B
28
33.171
−23.214
−0.581
1.00
63.10
N


ATOM
1155
CA
SER
B
28
33.737
−22.641
0.624
1.00
63.63
C


ATOM
1156
CB
SER
B
28
35.224
−22.968
0.718
1.00
63.90
C


ATOM
1157
OG
SER
B
28
35.570
−24.105
−0.058
1.00
64.95
O


ATOM
1158
C
SER
B
28
33.601
−21.129
0.427
1.00
63.77
C


ATOM
1159
O
SER
B
28
33.495
−20.363
1.393
1.00
64.47
O


ATOM
1160
N
PHE
B
29
33.625
−20.737
−0.852
1.00
63.20
N


ATOM
1161
CA
PHE
B
29
33.530
−19.355
−1.334
1.00
62.45
C


ATOM
1162
CB
PHE
B
29
33.358
−19.335
−2.872
1.00
62.20
C


ATOM
1163
CG
PHE
B
29
34.395
−20.140
−3.656
1.00
60.55
C


ATOM
1164
CD1
PHE
B
29
35.699
−20.308
−3.201
1.00
60.68
C


ATOM
1165
CE1
PHE
B
29
36.646
−21.025
−3.950
1.00
60.56
C


ATOM
1166
CZ
PHE
B
29
36.304
−21.564
−5.173
1.00
60.35
C


ATOM
1167
CE2
PHE
B
29
35.014
−21.392
−5.648
1.00
62.60
C


ATOM
1168
CD2
PHE
B
29
34.066
−20.671
−4.891
1.00
61.14
C


ATOM
1169
C
PHE
B
29
32.352
−18.604
−0.706
1.00
62.55
C


ATOM
1170
O
PHE
B
29
31.268
−19.188
−0.504
1.00
62.53
O


ATOM
1171
N
GLU
B
30
32.545
−17.315
−0.411
1.00
61.80
N


ATOM
1172
CA
GLU
B
30
31.445
−16.518
0.143
1.00
61.37
C


ATOM
1173
CB
GLU
B
30
31.797
−15.884
1.497
1.00
61.71
C


ATOM
1174
CG
GLU
B
30
32.680
−14.633
1.411
1.00
64.15
C


ATOM
1175
CD
GLU
B
30
32.153
−13.451
2.233
1.00
65.74
C


ATOM
1176
OE1
GLU
B
30
32.866
−13.015
3.168
1.00
63.81
O


ATOM
1177
OE2
GLU
B
30
31.033
−12.963
1.925
1.00
66.59
O


ATOM
1178
C
GLU
B
30
30.920
−15.470
−0.836
1.00
59.86
C


ATOM
1179
O
GLU
B
30
31.681
−14.655
−1.343
1.00
59.82
O


ATOM
1180
N
LEU
B
31
29.606
−15.497
−1.069
1.00
58.15
N


ATOM
1181
CA
LEU
B
31
28.946
−14.572
−1.982
1.00
56.44
C


ATOM
1182
CB
LEU
B
31
27.444
−14.831
−1.998
1.00
56.25
C


ATOM
1183
CG
LEU
B
31
26.669
−14.204
−3.148
1.00
54.16
C


ATOM
1184
CD1
LEU
B
31
27.090
−14.868
−4.401
1.00
51.33
C


ATOM
1185
CD2
LEU
B
31
25.183
−14.389
−2.910
1.00
53.29
C


ATOM
1186
C
LEU
B
31
29.187
−13.136
−1.575
1.00
55.70
C


ATOM
1187
O
LEU
B
31
28.791
−12.748
−0.489
1.00
55.50
O


ATOM
1188
N
LYS
B
32
29.831
−12.354
−2.436
1.00
54.55
N


ATOM
1189
CA
LYS
B
32
30.081
−10.963
−2.096
1.00
54.28
C


ATOM
1190
CB
LYS
B
32
31.576
−10.589
−2.202
1.00
54.33
C


ATOM
1191
CG
LYS
B
32
31.918
−9.629
−3.367
1.00
56.46
C


ATOM
1192
CD
LYS
B
32
33.271
−8.944
−3.278
1.00
55.97
C


ATOM
1193
CE
LYS
B
32
33.233
−7.762
−2.288
1.00
63.91
C


ATOM
1194
NZ
LYS
B
32
32.451
−6.536
−2.708
1.00
64.90
N


ATOM
1195
C
LYS
B
32
29.216
−10.009
−2.902
1.00
52.81
C


ATOM
1196
O
LYS
B
32
28.927
−8.898
−2.450
1.00
52.61
O


ATOM
1197
N
ASP
B
33
28.818
−10.438
−4.093
1.00
51.52
N


ATOM
1198
CA
ASP
B
33
28.077
−9.585
−5.000
1.00
50.34
C


ATOM
1199
CB
ASP
B
33
29.020
−8.581
−5.653
1.00
51.45
C


ATOM
1200
CG
ASP
B
33
28.458
−7.192
−5.654
1.00
54.79
C


ATOM
1201
OD1
ASP
B
33
29.150
−6.290
−5.130
1.00
60.70
O


ATOM
1202
OD2
ASP
B
33
27.308
−6.997
−6.126
1.00
60.01
O


ATOM
1203
C
ASP
B
33
27.349
−10.349
−6.103
1.00
48.37
C


ATOM
1204
O
ASP
B
33
27.618
−11.514
−6.338
1.00
47.51
O


ATOM
1205
N
THR
B
34
26.435
−9.656
−6.783
1.00
46.63
N


ATOM
1206
CA
THR
B
34
25.607
−10.230
−7.812
1.00
45.52
C


ATOM
1207
CB
THR
B
34
24.228
−10.594
−7.311
1.00
45.26
C


ATOM
1208
OG1
THR
B
34
23.507
−9.400
−7.005
1.00
44.94
O


ATOM
1209
CG2
THR
B
34
24.280
−11.520
−6.066
1.00
46.07
C


ATOM
1210
C
THR
B
34
25.396
−9.238
−8.924
1.00
45.83
C


ATOM
1211
O
THR
B
34
25.372
−8.017
−8.702
1.00
45.11
O


ATOM
1212
N
GLY
B
35
25.201
−9.773
−10.125
1.00
45.83
N


ATOM
1213
CA
GLY
B
35
24.725
−8.972
−11.249
1.00
44.82
C


ATOM
1214
C
GLY
B
35
23.816
−9.785
−12.153
1.00
43.28
C


ATOM
1215
O
GLY
B
35
23.801
−11.019
−12.111
1.00
42.32
O


ATOM
1216
N
TRP
B
36
23.074
−9.070
−12.992
1.00
42.69
N


ATOM
1217
CA
TRP
B
36
22.094
−9.665
−13.876
1.00
42.22
C


ATOM
1218
CB
TRP
B
36
20.695
−9.393
−13.321
1.00
41.99
C


ATOM
1219
CG
TRP
B
36
20.426
−10.204
−12.070
1.00
42.02
C


ATOM
1220
CD1
TRP
B
36
20.606
−9.809
−10.785
1.00
39.92
C


ATOM
1221
NE1
TRP
B
36
20.263
−10.839
−9.929
1.00
42.86
N


ATOM
1222
CE2
TRP
B
36
19.869
−11.931
−10.660
1.00
41.27
C


ATOM
1223
CD2
TRP
B
36
19.955
−11.571
−12.021
1.00
41.39
C


ATOM
1224
CE3
TRP
B
36
19.601
−12.520
−13.014
1.00
42.24
C


ATOM
1225
CZ3
TRP
B
36
19.161
−13.779
−12.616
1.00
42.06
C


ATOM
1226
CH2
TRP
B
36
19.077
−14.117
−11.226
1.00
42.99
C


ATOM
1227
CZ2
TRP
B
36
19.428
−13.199
−10.235
1.00
42.30
C


ATOM
1228
C
TRP
B
36
22.263
−9.062
−15.251
1.00
42.47
C


ATOM
1229
O
TRP
B
36
22.527
−7.848
−15.372
1.00
43.87
O


ATOM
1230
N
TYR
B
37
22.124
−9.884
−16.284
1.00
42.85
N


ATOM
1231
CA
TYR
B
37
22.396
−9.464
−17.688
1.00
44.60
C


ATOM
1232
CB
TYR
B
37
23.771
−9.983
−18.167
1.00
45.76
C


ATOM
1233
CG
TYR
B
37
24.857
−9.689
−17.146
1.00
47.71
C


ATOM
1234
CD1
TYR
B
37
25.524
−8.464
−17.117
1.00
50.27
C


ATOM
1235
CE1
TYR
B
37
26.524
−8.179
−16.125
1.00
51.99
C


ATOM
1236
CZ
TYR
B
37
26.825
−9.195
−15.183
1.00
53.06
C


ATOM
1237
OH
TYR
B
37
27.770
−9.042
−14.172
1.00
54.16
O


ATOM
1238
CE2
TYR
B
37
26.137
−10.395
−15.213
1.00
54.10
C


ATOM
1239
CD2
TYR
B
37
25.163
−10.627
−16.175
1.00
51.46
C


ATOM
1240
C
TYR
B
37
21.332
−10.026
−18.555
1.00
44.88
C


ATOM
1241
O
TYR
B
37
20.705
−11.043
−18.209
1.00
45.77
O


ATOM
1242
N
ARG
B
38
21.135
−9.388
−19.698
1.00
45.01
N


ATOM
1243
CA
ARG
B
38
20.136
−9.799
−20.689
1.00
44.85
C


ATOM
1244
CB
ARG
B
38
18.859
−8.971
−20.449
1.00
44.48
C


ATOM
1245
CG
ARG
B
38
17.818
−8.990
−21.512
1.00
49.57
C


ATOM
1246
CD
ARG
B
38
16.572
−8.154
−21.096
1.00
50.80
C


ATOM
1247
NE
ARG
B
38
16.808
−6.728
−20.931
1.00
59.29
N


ATOM
1248
CZ
ARG
B
38
16.791
−5.849
−21.929
1.00
65.43
C


ATOM
1249
NH1
ARG
B
38
16.570
−6.250
−23.196
1.00
68.18
N


ATOM
1250
NH2
ARG
B
38
17.020
−4.560
−21.670
1.00
66.70
N


ATOM
1251
C
ARG
B
38
20.678
−9.588
−22.100
1.00
43.70
C


ATOM
1252
O
ARG
B
38
21.291
−8.573
−22.413
1.00
43.08
O


ATOM
1253
N
THR
B
39
20.399
−10.551
−22.970
1.00
43.10
N


ATOM
1254
CA
THR
B
39
20.574
−10.401
−24.392
1.00
41.41
C


ATOM
1255
CB
THR
B
39
21.561
−11.463
−24.921
1.00
40.29
C


ATOM
1256
OG1
THR
B
39
22.780
−11.325
−24.192
1.00
44.60
O


ATOM
1257
CG2
THR
B
39
21.830
−11.278
−26.361
1.00
38.65
C


ATOM
1258
C
THR
B
39
19.209
−10.611
−25.023
1.00
40.66
C


ATOM
1259
O
THR
B
39
18.632
−11.718
−24.960
1.00
40.48
O


ATOM
1260
N
LYS
B
40
18.696
−9.575
−25.658
1.00
38.27
N


ATOM
1261
CA
LYS
B
40
17.420
−9.673
−26.286
1.00
40.05
C


ATOM
1262
CB
LYS
B
40
16.985
−8.329
−26.866
1.00
40.66
C


ATOM
1263
CG
LYS
B
40
18.180
−7.401
−27.336
1.00
46.79
C


ATOM
1264
CD
LYS
B
40
19.495
−7.235
−26.337
1.00
45.68
C


ATOM
1265
CE
LYS
B
40
20.177
−5.941
−26.663
1.00
47.93
C


ATOM
1266
NZ
LYS
B
40
19.625
−5.348
−28.020
1.00
50.16
N


ATOM
1267
C
LYS
B
40
17.399
−10.781
−27.346
1.00
39.05
C


ATOM
1268
O
LYS
B
40
18.428
−11.090
−27.963
1.00
38.47
O


ATOM
1269
N
LEU
B
41
16.231
−11.387
−27.526
1.00
37.38
N


ATOM
1270
CA
LEU
B
41
16.110
−12.482
−28.447
1.00
36.97
C


ATOM
1271
CB
LEU
B
41
14.693
−13.025
−28.410
1.00
35.93
C


ATOM
1272
CG
LEU
B
41
14.361
−14.498
−28.751
1.00
38.03
C


ATOM
1273
CD1
LEU
B
41
15.260
−15.201
−29.688
1.00
29.12
C


ATOM
1274
CD2
LEU
B
41
12.935
−14.628
−29.245
1.00
34.95
C


ATOM
1275
C
LEU
B
41
16.456
−12.015
−29.853
1.00
37.90
C


ATOM
1276
O
LEU
B
41
15.750
−11.171
−30.429
1.00
38.11
O


ATOM
1277
N
GLY
B
42
17.516
−12.596
−30.428
1.00
38.84
N


ATOM
1278
CA
GLY
B
42
17.894
−12.309
−31.828
1.00
39.84
C


ATOM
1279
C
GLY
B
42
19.138
−11.426
−31.882
1.00
41.12
C


ATOM
1280
O
GLY
B
42
19.889
−11.451
−32.845
1.00
40.47
O


ATOM
1281
N
SER
B
43
19.398
−10.703
−30.795
1.00
42.54
N


ATOM
1282
CA
SER
B
43
20.505
−9.752
−30.700
1.00
43.80
C


ATOM
1283
CB
SER
B
43
20.102
−8.627
−29.733
1.00
43.55
C


ATOM
1284
OG
SER
B
43
21.263
−8.058
−29.131
1.00
47.40
O


ATOM
1285
C
SER
B
43
21.837
−10.389
−30.246
1.00
44.08
C


ATOM
1286
O
SER
B
43
21.850
−11.442
−29.639
1.00
43.11
O


ATOM
1287
N
THR
B
44
22.950
−9.730
−30.556
1.00
46.01
N


ATOM
1288
CA
THR
B
44
24.284
−10.132
−30.088
1.00
49.08
C


ATOM
1289
CB
THR
B
44
25.386
−9.746
−31.113
1.00
49.56
C


ATOM
1290
OG1
THR
B
44
24.825
−8.862
−32.111
1.00
50.26
O


ATOM
1291
CG2
THR
B
44
25.951
−10.982
−31.782
1.00
51.25
C


ATOM
1292
C
THR
B
44
24.609
−9.414
−28.788
1.00
50.25
C


ATOM
1293
O
THR
B
44
25.441
−9.865
−27.991
1.00
51.27
O


ATOM
1294
N
ASN
B
45
23.915
−8.304
−28.560
1.00
51.11
N


ATOM
1295
CA
ASN
B
45
24.288
−7.373
−27.522
1.00
51.61
C


ATOM
1296
CB
ASN
B
45
23.900
−5.973
−27.975
1.00
51.54
C


ATOM
1297
CG
ASN
B
45
24.666
−5.532
−29.257
1.00
52.45
C


ATOM
1298
OD1
ASN
B
45
24.146
−4.760
−30.070
1.00
52.60
O


ATOM
1299
ND2
ASN
B
45
25.895
−6.033
−29.433
1.00
53.59
N


ATOM
1300
C
ASN
B
45
23.809
−7.699
−26.105
1.00
51.58
C


ATOM
1301
O
ASN
B
45
22.632
−7.837
−25.840
1.00
52.48
O


ATOM
1302
N
GLU
B
46
24.750
−7.844
−25.189
1.00
51.92
N


ATOM
1303
CA
GLU
B
46
24.414
−8.133
−23.821
1.00
52.44
C


ATOM
1304
CB
GLU
B
46
25.368
−9.161
−23.221
1.00
52.91
C


ATOM
1305
CG
GLU
B
46
24.884
−9.678
−21.894
1.00
58.15
C


ATOM
1306
CD
GLU
B
46
25.957
−10.405
−21.123
1.00
66.36
C


ATOM
1307
OE1
GLU
B
46
25.706
−11.582
−20.727
1.00
70.62
O


ATOM
1308
OE2
GLU
B
46
27.039
−9.793
−20.894
1.00
69.30
O


ATOM
1309
C
GLU
B
46
24.380
−6.860
−22.976
1.00
51.53
C


ATOM
1310
O
GLU
B
46
25.327
−6.088
−22.964
1.00
53.42
O


ATOM
1311
N
GLN
B
47
23.278
−6.642
−22.286
1.00
49.40
N


ATOM
1312
CA
GLN
B
47
23.107
−5.475
−21.450
1.00
48.39
C


ATOM
1313
CB
GLN
B
47
21.867
−4.713
−21.877
1.00
48.97
C


ATOM
1314
CG
GLN
B
47
21.851
−4.315
−23.390
1.00
54.17
C


ATOM
1315
CD
GLN
B
47
22.859
−3.187
−23.733
1.00
58.95
C


ATOM
1316
OE1
GLN
B
47
22.457
−2.123
−24.216
1.00
59.67
O


ATOM
1317
NE2
GLN
B
47
24.167
−3.430
−23.488
1.00
56.36
N


ATOM
1318
C
GLN
B
47
22.954
−5.913
−20.012
1.00
46.93
C


ATOM
1319
O
GLN
B
47
22.368
−6.955
−19.731
1.00
45.54
O


ATOM
1320
N
SER
B
48
23.510
−5.138
−19.103
1.00
45.48
N


ATOM
1321
CA
SER
B
48
23.310
−5.430
−17.703
1.00
45.97
C


ATOM
1322
CB
SER
B
48
24.518
−5.024
−16.823
1.00
44.83
C


ATOM
1323
OG
SER
B
48
24.567
−3.634
−16.677
1.00
48.28
O


ATOM
1324
C
SER
B
48
21.996
−4.775
−17.260
1.00
45.25
C


ATOM
1325
O
SER
B
48
21.625
−3.706
−17.747
1.00
44.79
O


ATOM
1326
N
ILE
B
49
21.310
−5.440
−16.336
1.00
44.46
N


ATOM
1327
CA
ILE
B
49
19.994
−5.034
−15.879
1.00
43.57
C


ATOM
1328
CB
ILE
B
49
19.191
−6.343
−15.528
1.00
43.55
C


ATOM
1329
CG1
ILE
B
49
18.786
−7.071
−16.799
1.00
41.77
C


ATOM
1330
CD1
ILE
B
49
18.315
−8.465
−16.522
1.00
45.18
C


ATOM
1331
CG2
ILE
B
49
17.998
−6.077
−14.627
1.00
42.15
C


ATOM
1332
C
ILE
B
49
20.202
−4.130
−14.678
1.00
43.36
C


ATOM
1333
O
ILE
B
49
20.937
−4.516
−13.800
1.00
43.25
O


ATOM
1334
N
SER
B
50
19.619
−2.910
−14.657
1.00
44.45
N


ATOM
1335
CA
SER
B
50
19.533
−2.085
−13.399
1.00
44.63
C


ATOM
1336
CB
SER
B
50
19.444
−0.561
−13.621
1.00
44.94
C


ATOM
1337
OG
SER
B
50
19.832
−0.190
−14.927
1.00
49.21
O


ATOM
1338
C
SER
B
50
18.328
−2.500
−12.603
1.00
43.86
C


ATOM
1339
O
SER
B
50
17.189
−2.461
−13.099
1.00
43.03
O


ATOM
1340
N
ILE
B
51
18.603
−2.881
−11.369
1.00
43.39
N


ATOM
1341
CA
ILE
B
51
17.624
−3.379
−10.447
1.00
43.30
C


ATOM
1342
CB
ILE
B
51
18.340
−3.979
−9.224
1.00
43.57
C


ATOM
1343
CG1
ILE
B
51
19.287
−5.151
−9.618
1.00
44.05
C


ATOM
1344
CD1
ILE
B
51
18.667
−6.326
−10.418
1.00
35.96
C


ATOM
1345
CG2
ILE
B
51
17.357
−4.242
−8.073
1.00
43.78
C


ATOM
1346
C
ILE
B
51
16.771
−2.224
−9.993
1.00
44.13
C


ATOM
1347
O
ILE
B
51
17.287
−1.167
−9.601
1.00
45.28
O


ATOM
1348
N
GLY
B
52
15.456
−2.413
−10.016
1.00
44.21
N


ATOM
1349
CA
GLY
B
52
14.540
−1.395
−9.504
1.00
43.63
C


ATOM
1350
C
GLY
B
52
13.381
−1.293
−10.469
1.00
43.28
C


ATOM
1351
O
GLY
B
52
13.460
−1.784
−11.585
1.00
43.58
O


ATOM
1352
N
GLY
B
53
12.310
−0.656
−10.035
1.00
43.27
N


ATOM
1353
CA
GLY
B
53
11.083
−0.560
−10.850
1.00
42.78
C


ATOM
1354
C
GLY
B
53
10.462
−2.015
−10.752
1.00
43.77
C


ATOM
1355
O
GLY
B
53
9.995
−2.673
−9.640
1.00
43.34
O


ATOM
1356
N
ARG
B
54
10.551
−2.654
−12.075
1.00
43.61
N


ATOM
1357
CA
ARG
B
54
9.886
−3.914
−12.251
1.00
42.86
C


ATOM
1358
CB
ARG
B
54
9.068
−3.913
−13.539
1.00
44.13
C


ATOM
1359
CG
ARG
B
54
9.889
−3.906
−14.830
1.00
42.33
C


ATOM
1360
CD
ARG
B
54
8.906
−3.835
−15.998
1.00
45.56
C


ATOM
1361
NE
ARG
B
54
9.580
−3.821
−17.288
1.00
47.32
N


ATOM
1362
CZ
ARG
B
54
9.650
−4.835
−18.148
1.00
47.04
C


ATOM
1363
NH1
ARG
B
54
9.064
−6.010
−17.908
1.00
50.81
N


ATOM
1364
NH2
ARG
B
54
10.306
−4.664
−19.280
1.00
46.49
N


ATOM
1365
C
ARG
B
54
10.892
−5.077
−12.274
1.00
44.33
C


ATOM
1366
O
ARG
B
54
10.498
−6.291
−12.483
1.00
44.77
O


ATOM
1367
N
TYR
B
55
12.186
−4.751
−12.152
1.00
43.57
N


ATOM
1368
CA
TYR
B
55
13.228
−5.749
−11.905
1.00
43.62
C


ATOM
1369
CB
TYR
B
55
14.498
−5.407
−12.673
1.00
44.46
C


ATOM
1370
CG
TYR
B
55
14.287
−5.318
−14.171
1.00
46.09
C


ATOM
1371
CD1
TYR
B
55
14.032
−4.088
−14.784
1.00
48.85
C


ATOM
1372
CE1
TYR
B
55
13.812
−3.998
−16.152
1.00
48.27
C


ATOM
1373
CZ
TYR
B
55
13.865
−5.144
−16.918
1.00
48.69
C


ATOM
1374
OH
TYR
B
55
13.655
−5.041
−18.268
1.00
47.96
O


ATOM
1375
CE2
TYR
B
55
14.087
−6.373
−16.336
1.00
48.31
C


ATOM
1376
CD2
TYR
B
55
14.296
−6.448
−14.959
1.00
45.72
C


ATOM
1377
C
TYR
B
55
13.511
−5.706
−10.398
1.00
43.55
C


ATOM
1378
O
TYR
B
55
14.064
−4.715
−9.878
1.00
42.28
O


ATOM
1379
N
VAL
B
56
13.071
−6.744
−9.689
1.00
43.19
N


ATOM
1380
CA
VAL
B
56
13.348
−6.837
−8.260
1.00
42.73
C


ATOM
1381
CB
VAL
B
56
12.127
−6.516
−7.293
1.00
42.21
C


ATOM
1382
CG1
VAL
B
56
10.841
−6.421
−7.968
1.00
44.06
C


ATOM
1383
CG2
VAL
B
56
12.051
−7.448
−6.048
1.00
45.27
C


ATOM
1384
C
VAL
B
56
14.263
−8.013
−7.898
1.00
42.60
C


ATOM
1385
O
VAL
B
56
13.991
−9.173
−8.224
1.00
41.88
O


ATOM
1386
N
GLU
B
57
15.388
−7.664
−7.277
1.00
42.73
N


ATOM
1387
CA
GLU
B
57
16.395
−8.617
−6.875
1.00
44.06
C


ATOM
1388
CB
GLU
B
57
17.815
−8.148
−7.214
1.00
42.94
C


ATOM
1389
CG
GLU
B
57
18.805
−9.083
−6.512
1.00
44.58
C


ATOM
1390
CD
GLU
B
57
20.228
−9.094
−7.028
1.00
48.71
C


ATOM
1391
OE1
GLU
B
57
20.904
−8.036
−7.062
1.00
49.40
O


ATOM
1392
OE2
GLU
B
57
20.704
−10.204
−7.334
1.00
49.94
O


ATOM
1393
C
GLU
B
57
16.271
−8.867
−5.374
1.00
44.37
C


ATOM
1394
O
GLU
B
57
16.096
−7.910
−4.621
1.00
43.80
O


ATOM
1395
N
THR
B
58
16.326
−10.154
−4.985
1.00
45.59
N


ATOM
1396
CA
THR
B
58
16.372
−10.633
−3.584
1.00
47.38
C


ATOM
1397
CB
THR
B
58
15.228
−11.630
−3.244
1.00
47.57
C


ATOM
1398
OG1
THR
B
58
13.968
−11.157
−3.752
1.00
48.77
O


ATOM
1399
CG2
THR
B
58
15.109
−11.859
−1.738
1.00
46.75
C


ATOM
1400
C
THR
B
58
17.694
−11.404
−3.420
1.00
48.37
C


ATOM
1401
O
THR
B
58
18.014
−12.246
−4.263
1.00
48.05
O


ATOM
1402
N
VAL
B
59
18.443
−11.121
−2.353
1.00
48.84
N


ATOM
1403
CA
VAL
B
59
19.708
−11.814
−2.089
1.00
50.27
C


ATOM
1404
CB
VAL
B
59
20.942
−10.858
−2.229
1.00
49.98
C


ATOM
1405
CG1
VAL
B
59
22.241
−11.607
−1.987
1.00
48.98
C


ATOM
1406
CG2
VAL
B
59
20.971
−10.233
−3.605
1.00
49.50
C


ATOM
1407
C
VAL
B
59
19.732
−12.503
−0.708
1.00
51.31
C


ATOM
1408
O
VAL
B
59
19.396
−11.889
0.306
1.00
51.41
O


ATOM
1409
N
ASN
B
60
20.110
−13.784
−0.692
1.00
52.16
N


ATOM
1410
CA
ASN
B
60
20.417
−14.503
0.550
1.00
52.82
C


ATOM
1411
CB
ASN
B
60
19.494
−15.713
0.703
1.00
52.46
C


ATOM
1412
CG
ASN
B
60
19.190
−16.052
2.165
1.00
53.85
C


ATOM
1413
OD1
ASN
B
60
18.162
−16.662
2.452
1.00
55.75
O


ATOM
1414
ND2
ASN
B
60
20.069
−15.657
3.083
1.00
51.06
N


ATOM
1415
C
ASN
B
60
21.917
−14.916
0.621
1.00
53.15
C


ATOM
1416
O
ASN
B
60
22.307
−16.018
0.189
1.00
53.51
O


ATOM
1417
N
LYS
B
61
22.758
−14.024
1.159
1.00
53.07
N


ATOM
1418
CA
LYS
B
61
24.188
−14.318
1.304
1.00
52.63
C


ATOM
1419
CB
LYS
B
61
24.962
−13.086
1.789
1.00
52.57
C


ATOM
1420
CG
LYS
B
61
25.168
−12.025
0.708
1.00
53.36
C


ATOM
1421
CD
LYS
B
61
25.866
−10.798
1.240
1.00
53.65
C


ATOM
1422
CE
LYS
B
61
26.365
−9.877
0.126
1.00
53.16
C


ATOM
1423
NZ
LYS
B
61
27.560
−9.116
0.657
1.00
54.11
N


ATOM
1424
C
LYS
B
61
24.443
−15.537
2.211
1.00
52.22
C


ATOM
1425
O
LYS
B
61
25.476
−16.199
2.070
1.00
52.39
O


ATOM
1426
N
GLY
B
62
23.489
−15.827
3.105
1.00
51.07
N


ATOM
1427
CA
GLY
B
62
23.513
−17.025
3.955
1.00
50.34
C


ATOM
1428
C
GLY
B
62
23.572
−18.280
3.105
1.00
49.30
C


ATOM
1429
O
GLY
B
62
24.571
−19.021
3.116
1.00
49.51
O


ATOM
1430
N
SER
B
63
22.498
−18.488
2.327
1.00
48.43
N


ATOM
1431
CA
SER
B
63
22.370
−19.683
1.482
1.00
47.02
C


ATOM
1432
CB
SER
B
63
20.884
−19.978
1.224
1.00
46.83
C


ATOM
1433
OG
SER
B
63
20.078
−19.136
2.232
1.00
47.96
O


ATOM
1434
C
SER
B
63
23.105
−19.552
0.135
1.00
45.91
C


ATOM
1435
O
SER
B
63
23.128
−20.499
−0.652
1.00
45.61
O


ATOM
1436
N
LYS
B
64
23.718
−18.402
−0.122
1.00
44.87
N


ATOM
1437
CA
LYS
B
64
24.410
−18.152
−1.417
1.00
44.92
C


ATOM
1438
CB
LYS
B
64
25.586
−19.115
−1.651
1.00
44.61
C


ATOM
1439
CG
LYS
B
64
26.660
−19.099
−0.554
1.00
45.05
C


ATOM
1440
CD
LYS
B
64
27.665
−20.213
−0.805
1.00
44.56
C


ATOM
1441
CE
LYS
B
64
28.244
−20.755
0.486
1.00
42.89
C


ATOM
1442
NZ
LYS
B
64
29.561
−20.185
0.780
1.00
41.38
N


ATOM
1443
C
LYS
B
64
23.429
−18.180
−2.601
1.00
44.11
C


ATOM
1444
O
LYS
B
64
23.754
−18.623
−3.704
1.00
44.27
O


ATOM
1445
N
SER
B
65
22.219
−17.710
−2.358
1.00
43.78
N


ATOM
1446
CA
SER
B
65
21.231
−17.677
−3.417
1.00
45.07
C


ATOM
1447
CB
SER
B
65
20.157
−18.737
−3.220
1.00
45.06
C


ATOM
1448
OG
SER
B
65
19.602
−18.635
−1.939
1.00
46.48
O


ATOM
1449
C
SER
B
65
20.654
−16.282
−3.598
1.00
44.87
C


ATOM
1450
O
SER
B
65
20.725
−15.444
−2.695
1.00
46.30
O


ATOM
1451
N
PHE
B
66
20.165
−16.024
−4.795
1.00
43.98
N


ATOM
1452
CA
PHE
B
66
19.662
−14.717
−5.174
1.00
43.45
C


ATOM
1453
CB
PHE
B
66
20.794
−13.716
−5.484
1.00
43.22
C


ATOM
1454
CG
PHE
B
66
21.805
−14.199
−6.486
1.00
42.41
C


ATOM
1455
CD1
PHE
B
66
22.667
−15.256
−6.188
1.00
41.96
C


ATOM
1456
CE1
PHE
B
66
23.629
−15.678
−7.083
1.00
40.78
C


ATOM
1457
CZ
PHE
B
66
23.745
−15.037
−8.303
1.00
43.25
C


ATOM
1458
CE2
PHE
B
66
22.909
−13.946
−8.609
1.00
42.43
C


ATOM
1459
CD2
PHE
B
66
21.955
−13.537
−7.693
1.00
42.09
C


ATOM
1460
C
PHE
B
66
18.748
−14.890
−6.362
1.00
43.59
C


ATOM
1461
O
PHE
B
66
18.876
−15.857
−7.112
1.00
43.27
O


ATOM
1462
N
SER
B
67
17.813
−13.966
−6.521
1.00
43.46
N


ATOM
1463
CA
SER
B
67
16.872
−14.080
−7.599
1.00
43.95
C


ATOM
1464
CB
SER
B
67
15.647
−14.891
−7.177
1.00
44.17
C


ATOM
1465
OG
SER
B
67
14.969
−14.198
−6.173
1.00
47.70
O


ATOM
1466
C
SER
B
67
16.442
−12.745
−8.140
1.00
43.18
C


ATOM
1467
O
SER
B
67
16.571
−11.715
−7.497
1.00
42.89
O


ATOM
1468
N
LEU
B
68
15.918
−12.787
−9.347
1.00
42.60
N


ATOM
1469
CA
LEU
B
68
15.432
−11.612
−10.012
1.00
42.76
C


ATOM
1470
CB
LEU
B
68
16.174
−11.461
−11.336
1.00
41.93
C


ATOM
1471
CG
LEU
B
68
16.515
−10.118
−11.984
1.00
45.17
C


ATOM
1472
CD1
LEU
B
68
16.440
−10.205
−13.537
1.00
43.08
C


ATOM
1473
CD2
LEU
B
68
15.823
−8.866
−11.437
1.00
43.46
C


ATOM
1474
C
LEU
B
68
13.988
−11.907
−10.355
1.00
42.62
C


ATOM
1475
O
LEU
B
68
13.711
−12.896
−11.018
1.00
42.63
O


ATOM
1476
N
ARG
B
69
13.075
−11.045
−9.973
1.00
42.71
N


ATOM
1477
CA
ARG
B
69
11.746
−11.161
−10.528
1.00
44.20
C


ATOM
1478
CB
ARG
B
69
10.715
−11.157
−9.418
1.00
43.82
C


ATOM
1479
CG
ARG
B
69
9.300
−11.193
−9.930
1.00
44.98
C


ATOM
1480
CD
ARG
B
69
8.390
−11.421
−8.752
1.00
50.13
C


ATOM
1481
NE
ARG
B
69
7.015
−11.124
−9.113
1.00
58.36
N


ATOM
1482
CZ
ARG
B
69
6.457
−9.914
−9.010
1.00
61.11
C


ATOM
1483
NH1
ARG
B
69
7.188
−8.871
−8.565
1.00
61.04
N


ATOM
1484
NH2
ARG
B
69
5.170
−9.750
−9.367
1.00
59.12
N


ATOM
1485
C
ARG
B
69
11.485
−10.025
−11.500
1.00
43.87
C


ATOM
1486
O
ARG
B
69
11.692
−8.876
−11.157
1.00
45.00
O


ATOM
1487
N
ILE
B
70
11.026
−10.355
−12.699
1.00
43.46
N


ATOM
1488
CA
ILE
B
70
10.727
−9.370
−13.697
1.00
43.63
C


ATOM
1489
CB
ILE
B
70
11.407
−9.689
−15.035
1.00
45.10
C


ATOM
1490
CG1
ILE
B
70
12.912
−9.941
−14.806
1.00
43.18
C


ATOM
1491
CD1
ILE
B
70
13.478
−10.890
−15.730
1.00
45.17
C


ATOM
1492
CG2
ILE
B
70
11.137
−8.524
−16.012
1.00
44.11
C


ATOM
1493
C
ILE
B
70
9.209
−9.326
−13.860
1.00
43.63
C


ATOM
1494
O
ILE
B
70
8.592
−10.314
−14.166
1.00
43.43
O


ATOM
1495
N
SER
B
71
8.610
−8.175
−13.579
1.00
44.13
N


ATOM
1496
CA
SER
B
71
7.177
−8.025
−13.678
1.00
44.47
C


ATOM
1497
CB
SER
B
71
6.659
−7.217
−12.519
1.00
43.71
C


ATOM
1498
OG
SER
B
71
6.974
−7.938
−11.370
1.00
45.34
O


ATOM
1499
C
SER
B
71
6.729
−7.397
−14.962
1.00
44.92
C


ATOM
1500
O
SER
B
71
7.546
−6.909
−15.731
1.00
43.62
O


ATOM
1501
N
ASP
B
72
5.398
−7.295
−15.068
1.00
46.93
N


ATOM
1502
CA
ASP
B
72
4.640
−7.266
−16.317
1.00
47.72
C


ATOM
1503
CB
ASP
B
72
3.574
−6.195
−16.338
1.00
49.50
C


ATOM
1504
CG
ASP
B
72
4.135
−4.834
−16.302
1.00
54.38
C


ATOM
1505
OD1
ASP
B
72
4.521
−4.403
−15.190
1.00
60.99
O


ATOM
1506
OD2
ASP
B
72
4.146
−4.186
−17.381
1.00
60.20
O


ATOM
1507
C
ASP
B
72
5.411
−7.335
−17.615
1.00
46.39
C


ATOM
1508
O
ASP
B
72
5.706
−6.316
−18.250
1.00
46.34
O


ATOM
1509
N
LEU
B
73
5.653
−8.569
−18.014
1.00
45.38
N


ATOM
1510
CA
LEU
B
73
6.476
−8.921
−19.147
1.00
44.12
C


ATOM
1511
CB
LEU
B
73
6.686
−10.447
−19.152
1.00
43.05
C


ATOM
1512
CG
LEU
B
73
7.513
−11.022
−17.984
1.00
42.55
C


ATOM
1513
CD1
LEU
B
73
7.264
−12.505
−17.805
1.00
37.65
C


ATOM
1514
CD2
LEU
B
73
9.037
−10.729
−18.116
1.00
40.53
C


ATOM
1515
C
LEU
B
73
5.861
−8.430
−20.443
1.00
44.58
C


ATOM
1516
O
LEU
B
73
4.637
−8.415
−20.594
1.00
44.57
O


ATOM
1517
N
ARG
B
74
6.712
−8.006
−21.370
1.00
44.91
N


ATOM
1518
CA
ARG
B
74
6.279
−7.680
−22.737
1.00
45.45
C


ATOM
1519
CB
ARG
B
74
6.565
−6.224
−23.047
1.00
45.64
C


ATOM
1520
CG
ARG
B
74
6.164
−5.286
−22.019
1.00
49.91
C


ATOM
1521
CD
ARG
B
74
7.106
−4.109
−22.126
1.00
57.66
C


ATOM
1522
NE
ARG
B
74
7.462
−3.603
−20.811
1.00
60.89
N


ATOM
1523
CZ
ARG
B
74
6.724
−2.746
−20.101
1.00
64.00
C


ATOM
1524
NH1
ARG
B
74
5.571
−2.278
−20.587
1.00
65.92
N


ATOM
1525
NH2
ARG
B
74
7.155
−2.334
−18.909
1.00
64.22
N


ATOM
1526
C
ARG
B
74
7.067
−8.497
−23.727
1.00
44.79
C


ATOM
1527
O
ARG
B
74
8.042
−9.136
−23.365
1.00
45.02
O


ATOM
1528
N
VAL
B
75
6.666
−8.466
−24.983
1.00
45.42
N


ATOM
1529
CA
VAL
B
75
7.276
−9.328
−26.006
1.00
45.62
C


ATOM
1530
CB
VAL
B
75
6.624
−9.140
−27.368
1.00
45.40
C


ATOM
1531
CG1
VAL
B
75
5.223
−9.671
−27.324
1.00
46.53
C


ATOM
1532
CG2
VAL
B
75
7.440
−9.851
−28.447
1.00
45.91
C


ATOM
1533
C
VAL
B
75
8.765
−9.030
−26.108
1.00
44.93
C


ATOM
1534
O
VAL
B
75
9.578
−9.937
−26.234
1.00
45.36
O


ATOM
1535
N
GLU
B
76
9.105
−7.760
−25.986
1.00
44.44
N


ATOM
1536
CA
GLU
B
76
10.458
−7.282
−26.127
1.00
44.58
C


ATOM
1537
CB
GLU
B
76
10.449
−5.771
−26.372
1.00
45.85
C


ATOM
1538
CG
GLU
B
76
9.328
−5.317
−27.417
1.00
51.77
C


ATOM
1539
CD
GLU
B
76
7.931
−5.030
−26.766
1.00
59.07
C


ATOM
1540
OE1
GLU
B
76
6.879
−5.154
−27.462
1.00
60.29
O


ATOM
1541
OE2
GLU
B
76
7.898
−4.661
−25.557
1.00
62.06
O


ATOM
1542
C
GLU
B
76
11.389
−7.671
−24.957
1.00
43.89
C


ATOM
1543
O
GLU
B
76
12.627
−7.513
−25.082
1.00
42.88
O


ATOM
1544
N
ASP
B
77
10.817
−8.202
−23.859
1.00
42.42
N


ATOM
1545
CA
ASP
B
77
11.618
−8.761
−22.766
1.00
41.98
C


ATOM
1546
CB
ASP
B
77
10.833
−8.835
−21.468
1.00
42.23
C


ATOM
1547
CG
ASP
B
77
10.458
−7.483
−20.905
1.00
44.50
C


ATOM
1548
OD1
ASP
B
77
11.179
−6.460
−21.084
1.00
48.11
O


ATOM
1549
OD2
ASP
B
77
9.417
−7.454
−20.227
1.00
47.95
O


ATOM
1550
C
ASP
B
77
12.117
−10.205
−23.101
1.00
42.26
C


ATOM
1551
O
ASP
B
77
12.839
−10.816
−22.314
1.00
42.73
O


ATOM
1552
N
SER
B
78
11.679
−10.742
−24.230
1.00
40.74
N


ATOM
1553
CA
SER
B
78
12.145
−12.007
−24.758
1.00
40.45
C


ATOM
1554
CB
SER
B
78
11.467
−12.307
−26.105
1.00
37.71
C


ATOM
1555
OG
SER
B
78
10.070
−12.574
−25.878
1.00
37.58
O


ATOM
1556
C
SER
B
78
13.660
−11.964
−24.910
1.00
40.32
C


ATOM
1557
O
SER
B
78
14.208
−11.100
−25.589
1.00
40.12
O


ATOM
1558
N
GLY
B
79
14.328
−12.910
−24.280
1.00
39.35
N


ATOM
1559
CA
GLY
B
79
15.758
−13.031
−24.490
1.00
39.80
C


ATOM
1560
C
GLY
B
79
16.392
−13.943
−23.466
1.00
38.99
C


ATOM
1561
O
GLY
B
79
15.697
−14.690
−22.788
1.00
39.42
O


ATOM
1562
N
THR
B
80
17.706
−13.880
−23.381
1.00
38.30
N


ATOM
1563
CA
THR
B
80
18.493
−14.660
−22.436
1.00
39.61
C


ATOM
1564
CB
THR
B
80
19.765
−15.195
−23.148
1.00
39.70
C


ATOM
1565
OG1
THR
B
80
19.339
−16.052
−24.190
1.00
38.59
O


ATOM
1566
CG2
THR
B
80
20.688
−15.994
−22.197
1.00
37.90
C


ATOM
1567
C
THR
B
80
18.929
−13.821
−21.246
1.00
40.30
C


ATOM
1568
O
THR
B
80
19.531
−12.776
−21.414
1.00
39.92
O


ATOM
1569
N
TYR
B
81
18.642
−14.329
−20.060
1.00
41.21
N


ATOM
1570
CA
TYR
B
81
18.921
−13.698
−18.817
1.00
41.29
C


ATOM
1571
CB
TYR
B
81
17.654
−13.633
−17.949
1.00
41.37
C


ATOM
1572
CG
TYR
B
81
16.647
−12.664
−18.510
1.00
41.48
C


ATOM
1573
CD1
TYR
B
81
16.562
−11.381
−18.023
1.00
40.06
C


ATOM
1574
CE1
TYR
B
81
15.644
−10.454
−18.583
1.00
44.06
C


ATOM
1575
CZ
TYR
B
81
14.846
−10.857
−19.675
1.00
43.01
C


ATOM
1576
OH
TYR
B
81
13.959
−9.992
−20.249
1.00
42.85
O


ATOM
1577
CE2
TYR
B
81
14.913
−12.137
−20.160
1.00
37.03
C


ATOM
1578
CD2
TYR
B
81
15.798
−13.043
−19.604
1.00
38.04
C


ATOM
1579
C
TYR
B
81
19.940
−14.563
−18.132
1.00
43.06
C


ATOM
1580
O
TYR
B
81
19.798
−15.785
−18.103
1.00
43.90
O


ATOM
1581
N
LYS
B
82
20.990
−13.924
−17.631
1.00
43.98
N


ATOM
1582
CA
LYS
B
82
22.054
−14.585
−16.866
1.00
45.48
C


ATOM
1583
CB
LYS
B
82
23.331
−14.667
−17.693
1.00
46.06
C


ATOM
1584
CG
LYS
B
82
23.440
−16.011
−18.369
1.00
48.70
C


ATOM
1585
CD
LYS
B
82
24.530
−16.006
−19.412
1.00
54.28
C


ATOM
1586
CE
LYS
B
82
24.476
−17.315
−20.209
1.00
53.81
C


ATOM
1587
NZ
LYS
B
82
25.735
−17.388
−20.957
1.00
57.58
N


ATOM
1588
C
LYS
B
82
22.308
−13.867
−15.552
1.00
44.33
C


ATOM
1589
O
LYS
B
82
22.201
−12.664
−15.484
1.00
44.79
O


ATOM
1590
N
CYS
B
83
22.566
−14.626
−14.507
1.00
43.87
N


ATOM
1591
CA
CYS
B
83
22.995
−14.054
−13.266
1.00
44.81
C


ATOM
1592
CB
CYS
B
83
22.327
−14.739
−12.098
1.00
44.27
C


ATOM
1593
SG
CYS
B
83
22.696
−16.465
−11.941
1.00
45.41
S


ATOM
1594
C
CYS
B
83
24.497
−14.258
−13.210
1.00
46.24
C


ATOM
1595
O
CYS
B
83
25.008
−15.105
−13.936
1.00
46.71
O


ATOM
1596
N
GLN
B
84
25.197
−13.440
−12.415
1.00
46.76
N


ATOM
1597
CA
GLN
B
84
26.617
−13.650
−12.077
1.00
46.51
C


ATOM
1598
CB
GLN
B
84
27.526
−12.679
−12.810
1.00
47.55
C


ATOM
1599
CG
GLN
B
84
29.032
−12.902
−12.495
1.00
50.71
C


ATOM
1600
CD
GLN
B
84
29.953
−12.348
−13.563
1.00
54.90
C


ATOM
1601
OE1
GLN
B
84
30.999
−12.943
−13.851
1.00
61.33
O


ATOM
1602
NE2
GLN
B
84
29.584
−11.212
−14.160
1.00
54.98
N


ATOM
1603
C
GLN
B
84
26.829
−13.518
−10.569
1.00
45.81
C


ATOM
1604
O
GLN
B
84
26.324
−12.604
−9.944
1.00
44.81
O


ATOM
1605
N
ALA
B
85
27.532
−14.488
−9.993
1.00
44.59
N


ATOM
1606
CA
ALA
B
85
27.840
−14.484
−8.590
1.00
43.83
C


ATOM
1607
CB
ALA
B
85
27.646
−15.884
−8.031
1.00
43.38
C


ATOM
1608
C
ALA
B
85
29.316
−14.014
−8.479
1.00
43.84
C


ATOM
1609
O
ALA
B
85
30.172
−14.539
−9.175
1.00
45.10
O


ATOM
1610
N
PHE
B
86
29.603
−12.990
−7.689
1.00
43.41
N


ATOM
1611
CA
PHE
B
86
30.985
−12.634
−7.399
1.00
43.48
C


ATOM
1612
CB
PHE
B
86
31.195
−11.139
−7.499
1.00
43.25
C


ATOM
1613
CG
PHE
B
86
30.922
−10.598
−8.863
1.00
45.60
C


ATOM
1614
CD1
PHE
B
86
29.695
−9.993
−9.153
1.00
46.99
C


ATOM
1615
CE1
PHE
B
86
29.434
−9.498
−10.461
1.00
49.94
C


ATOM
1616
CZ
PHE
B
86
30.427
−9.610
−11.452
1.00
47.51
C


ATOM
1617
CE2
PHE
B
86
31.649
−10.207
−11.143
1.00
46.33
C


ATOM
1618
CD2
PHE
B
86
31.874
−10.723
−9.877
1.00
43.78
C


ATOM
1619
C
PHE
B
86
31.291
−13.124
−6.015
1.00
44.35
C


ATOM
1620
O
PHE
B
86
30.508
−12.925
−5.066
1.00
44.86
O


ATOM
1621
N
TYR
B
87
32.427
−13.779
−5.866
1.00
43.59
N


ATOM
1622
CA
TYR
B
87
32.679
−14.421
−4.604
1.00
43.44
C


ATOM
1623
CB
TYR
B
87
32.251
−15.913
−4.633
1.00
43.50
C


ATOM
1624
CG
TYR
B
87
32.810
−16.691
−5.817
1.00
44.45
C


ATOM
1625
CD1
TYR
B
87
34.022
−17.351
−5.704
1.00
46.50
C


ATOM
1626
CE1
TYR
B
87
34.574
−18.044
−6.759
1.00
45.78
C


ATOM
1627
CZ
TYR
B
87
33.918
−18.111
−7.953
1.00
46.91
C


ATOM
1628
OH
TYR
B
87
34.547
−18.831
−8.957
1.00
48.61
O


ATOM
1629
CE2
TYR
B
87
32.684
−17.477
−8.120
1.00
45.59
C


ATOM
1630
CD2
TYR
B
87
32.130
−16.777
−7.031
1.00
43.90
C


ATOM
1631
C
TYR
B
87
34.139
−14.221
−4.248
1.00
42.55
C


ATOM
1632
O
TYR
B
87
34.935
−13.761
−5.046
1.00
42.89
O


ATOM
1633
N
VAL
B
88
34.468
−14.599
−3.037
1.00
41.90
N


ATOM
1634
CA
VAL
B
88
35.747
−14.320
−2.484
1.00
40.38
C


ATOM
1635
CB
VAL
B
88
35.563
−13.113
−1.524
1.00
41.09
C


ATOM
1636
CG1
VAL
B
88
36.089
−13.331
−0.157
1.00
39.39
C


ATOM
1637
CG2
VAL
B
88
36.117
−11.869
−2.206
1.00
41.64
C


ATOM
1638
C
VAL
B
88
36.321
−15.611
−1.910
1.00
39.32
C


ATOM
1639
O
VAL
B
88
35.617
−16.392
−1.274
1.00
39.48
O


ATOM
1640
N
PHE
B
89
37.584
−15.880
−2.214
1.00
38.33
N


ATOM
1641
CA
PHE
B
89
38.325
−16.946
−1.527
1.00
36.70
C


ATOM
1642
CB
PHE
B
89
38.362
−18.233
−2.346
1.00
35.81
C


ATOM
1643
CG
PHE
B
89
38.830
−18.069
−3.773
1.00
33.80
C


ATOM
1644
CD1
PHE
B
89
40.156
−18.343
−4.112
1.00
33.47
C


ATOM
1645
CE1
PHE
B
89
40.606
−18.225
−5.403
1.00
30.77
C


ATOM
1646
CZ
PHE
B
89
39.726
−17.835
−6.426
1.00
31.68
C


ATOM
1647
CE2
PHE
B
89
38.387
−17.583
−6.134
1.00
33.87
C


ATOM
1648
CD2
PHE
B
89
37.946
−17.711
−4.782
1.00
36.04
C


ATOM
1649
C
PHE
B
89
39.704
−16.451
−1.269
1.00
37.19
C


ATOM
1650
O
PHE
B
89
40.059
−15.356
−1.701
1.00
36.81
O


ATOM
1651
N
PHE
B
90
40.484
−17.258
−0.565
1.00
38.03
N


ATOM
1652
CA
PHE
B
90
41.842
−16.928
−0.180
1.00
38.04
C


ATOM
1653
CB
PHE
B
90
42.075
−17.297
1.280
1.00
39.75
C


ATOM
1654
CG
PHE
B
90
41.328
−16.416
2.209
1.00
43.37
C


ATOM
1655
CD1
PHE
B
90
39.930
−16.435
2.223
1.00
47.99
C


ATOM
1656
CE1
PHE
B
90
39.208
−15.584
3.055
1.00
50.22
C


ATOM
1657
CZ
PHE
B
90
39.893
−14.691
3.875
1.00
46.73
C


ATOM
1658
CE2
PHE
B
90
41.285
−14.653
3.848
1.00
49.56
C


ATOM
1659
CD2
PHE
B
90
41.992
−15.504
2.998
1.00
47.02
C


ATOM
1660
C
PHE
B
90
42.831
−17.568
−1.103
1.00
37.73
C


ATOM
1661
O
PHE
B
90
42.675
−18.723
−1.455
1.00
35.86
O


ATOM
1662
N
ALA
B
91
43.808
−16.766
−1.541
1.00
38.81
N


ATOM
1663
CA
ALA
B
91
44.880
−17.186
−2.450
1.00
41.01
C


ATOM
1664
CB
ALA
B
91
45.887
−16.050
−2.613
1.00
41.04
C


ATOM
1665
C
ALA
B
91
45.610
−18.459
−1.997
1.00
42.55
C


ATOM
1666
O
ALA
B
91
46.126
−19.208
−2.826
1.00
41.40
O


ATOM
1667
N
GLU
B
92
45.643
−18.675
−0.677
1.00
45.64
N


ATOM
1668
CA
GLU
B
92
46.278
−19.854
−0.067
1.00
49.34
C


ATOM
1669
CB
GLU
B
92
46.339
−19.765
1.468
1.00
49.34
C


ATOM
1670
CG
GLU
B
92
47.103
−18.578
2.047
1.00
53.21
C


ATOM
1671
CD
GLU
B
92
46.215
−17.331
2.266
1.00
57.21
C


ATOM
1672
OE1
GLU
B
92
45.848
−17.086
3.448
1.00
59.01
O


ATOM
1673
OE2
GLU
B
92
45.901
−16.599
1.280
1.00
55.91
O


ATOM
1674
C
GLU
B
92
45.529
−21.121
−0.433
1.00
50.92
C


ATOM
1675
O
GLU
B
92
46.163
−22.112
−0.803
1.00
51.36
O


ATOM
1676
N
ASP
B
93
44.198
−21.098
−0.315
1.00
52.93
N


ATOM
1677
CA
ASP
B
93
43.454
−22.356
−0.337
1.00
55.69
C


ATOM
1678
CB
ASP
B
93
41.992
−22.280
0.238
1.00
55.85
C


ATOM
1679
CG
ASP
B
93
40.982
−21.501
−0.651
1.00
58.02
C


ATOM
1680
OD1
ASP
B
93
40.972
−21.667
−1.896
1.00
60.03
O


ATOM
1681
OD2
ASP
B
93
40.134
−20.749
−0.080
1.00
58.21
O


ATOM
1682
C
ASP
B
93
43.647
−23.117
−1.659
1.00
57.09
C


ATOM
1683
O
ASP
B
93
43.222
−22.670
−2.731
1.00
56.60
O


ATOM
1684
N
VAL
B
94
44.381
−24.231
−1.542
1.00
59.08
N


ATOM
1685
CA
VAL
B
94
44.863
−25.029
−2.673
1.00
61.07
C


ATOM
1686
CB
VAL
B
94
46.088
−25.913
−2.271
1.00
61.32
C


ATOM
1687
CG1
VAL
B
94
46.489
−26.881
−3.404
1.00
61.77
C


ATOM
1688
CG2
VAL
B
94
47.300
−25.062
−1.795
1.00
61.40
C


ATOM
1689
C
VAL
B
94
43.755
−25.952
−3.125
1.00
62.29
C


ATOM
1690
O
VAL
B
94
42.925
−26.361
−2.312
1.00
62.77
O


ATOM
1691
N
GLY
B
95
43.738
−26.286
−4.410
1.00
63.72
N


ATOM
1692
CA
GLY
B
95
42.849
−27.341
−4.889
1.00
65.63
C


ATOM
1693
C
GLY
B
95
41.366
−26.996
−4.820
1.00
66.94
C


ATOM
1694
O
GLY
B
95
40.503
−27.897
−4.790
1.00
67.35
O


ATOM
1695
N
SER
B
96
41.082
−25.693
−4.764
1.00
67.66
N


ATOM
1696
CA
SER
B
96
39.752
−25.126
−5.019
1.00
68.33
C


ATOM
1697
CB
SER
B
96
38.719
−25.490
−3.934
1.00
68.30
C


ATOM
1698
OG
SER
B
96
39.096
−25.003
−2.655
1.00
69.15
O


ATOM
1699
C
SER
B
96
39.951
−23.610
−5.149
1.00
68.57
C


ATOM
1700
O
SER
B
96
40.232
−22.909
−4.161
1.00
68.47
O


ATOM
1701
N
ASN
B
97
39.872
−23.144
−6.399
1.00
68.54
N


ATOM
1702
CA
ASN
B
97
40.063
−21.737
−6.798
1.00
67.90
C


ATOM
1703
CB
ASN
B
97
41.539
−21.450
−7.190
1.00
67.64
C


ATOM
1704
CG
ASN
B
97
42.549
−21.839
−6.102
1.00
67.80
C


ATOM
1705
OD1
ASN
B
97
43.346
−21.010
−5.642
1.00
68.17
O


ATOM
1706
ND2
ASN
B
97
42.535
−23.103
−5.706
1.00
67.46
N


ATOM
1707
C
ASN
B
97
39.164
−21.548
−8.020
1.00
67.37
C


ATOM
1708
O
ASN
B
97
39.474
−20.763
−8.918
1.00
67.83
O


ATOM
1709
N
LYS
B
98
38.028
−22.246
−8.012
1.00
66.43
N


ATOM
1710
CA
LYS
B
98
37.501
−22.902
−9.221
1.00
65.41
C


ATOM
1711
CB
LYS
B
98
36.489
−24.003
−8.837
1.00
65.75
C


ATOM
1712
CG
LYS
B
98
37.167
−25.283
−8.285
1.00
67.70
C


ATOM
1713
CD
LYS
B
98
36.292
−26.019
−7.266
1.00
70.57
C


ATOM
1714
CE
LYS
B
98
36.108
−25.188
−5.992
1.00
71.50
C


ATOM
1715
NZ
LYS
B
98
35.816
−26.004
−4.778
1.00
71.51
N


ATOM
1716
C
LYS
B
98
37.036
−22.104
−10.467
1.00
64.00
C


ATOM
1717
O
LYS
B
98
37.100
−22.642
−11.587
1.00
64.50
O


ATOM
1718
N
GLY
B
99
36.583
−20.861
−10.313
1.00
61.92
N


ATOM
1719
CA
GLY
B
99
35.934
−20.173
−11.453
1.00
58.65
C


ATOM
1720
C
GLY
B
99
36.850
−19.277
−12.268
1.00
56.59
C


ATOM
1721
O
GLY
B
99
38.048
−19.538
−12.374
1.00
56.84
O


ATOM
1722
N
ALA
B
100
36.282
−18.223
−12.849
1.00
53.87
N


ATOM
1723
CA
ALA
B
100
37.065
−17.133
−13.429
1.00
51.62
C


ATOM
1724
CB
ALA
B
100
36.164
−16.245
−14.269
1.00
51.17
C


ATOM
1725
C
ALA
B
100
37.690
−16.294
−12.312
1.00
49.55
C


ATOM
1726
O
ALA
B
100
36.987
−15.896
−11.373
1.00
49.34
O


ATOM
1727
N
ILE
B
101
38.985
−16.005
−12.395
1.00
47.31
N


ATOM
1728
CA
ILE
B
101
39.533
−14.981
−11.484
1.00
45.25
C


ATOM
1729
CB
ILE
B
101
40.904
−15.345
−10.756
1.00
45.80
C


ATOM
1730
CG1
ILE
B
101
42.016
−14.358
−11.079
1.00
46.05
C


ATOM
1731
CD1
ILE
B
101
42.324
−13.495
−9.928
1.00
46.13
C


ATOM
1732
CG2
ILE
B
101
41.319
−16.849
−10.843
1.00
44.18
C


ATOM
1733
C
ILE
B
101
39.355
−13.542
−12.031
1.00
44.02
C


ATOM
1734
O
ILE
B
101
39.651
−13.227
−13.209
1.00
43.07
O


ATOM
1735
N
ILE
B
102
38.734
−12.724
−11.185
1.00
41.55
N


ATOM
1736
CA
ILE
B
102
38.307
−11.368
−11.482
1.00
40.42
C


ATOM
1737
CB
ILE
B
102
36.935
−11.028
−10.777
1.00
41.20
C


ATOM
1738
CG1
ILE
B
102
35.748
−11.863
−11.308
1.00
43.88
C


ATOM
1739
CD1
ILE
B
102
35.773
−12.274
−12.825
1.00
43.26
C


ATOM
1740
CG2
ILE
B
102
36.582
−9.531
−10.871
1.00
44.23
C


ATOM
1741
C
ILE
B
102
39.378
−10.376
−10.971
1.00
39.32
C


ATOM
1742
O
ILE
B
102
39.623
−9.342
−11.614
1.00
39.71
O


ATOM
1743
N
GLY
B
103
40.002
−10.670
−9.810
1.00
36.32
N


ATOM
1744
CA
GLY
B
103
41.079
−9.842
−9.312
1.00
32.38
C


ATOM
1745
C
GLY
B
103
41.673
−10.369
−8.038
1.00
31.16
C


ATOM
1746
O
GLY
B
103
41.199
−11.372
−7.457
1.00
31.39
O


ATOM
1747
N
LEU
B
104
42.706
−9.670
−7.578
1.00
29.03
N


ATOM
1748
CA
LEU
B
104
43.424
−10.049
−6.423
1.00
27.58
C


ATOM
1749
CB
LEU
B
104
44.839
−10.544
−6.818
1.00
26.53
C


ATOM
1750
CG
LEU
B
104
45.829
−10.943
−5.733
1.00
26.78
C


ATOM
1751
CD1
LEU
B
104
47.232
−11.015
−6.252
1.00
30.47
C


ATOM
1752
CD2
LEU
B
104
45.473
−12.251
−5.078
1.00
27.53
C


ATOM
1753
C
LEU
B
104
43.459
−8.841
−5.496
1.00
28.83
C


ATOM
1754
O
LEU
B
104
43.870
−7.752
−5.901
1.00
27.59
O


ATOM
1755
N
MET
B
105
43.067
−9.055
−4.233
1.00
29.96
N


ATOM
1756
CA
MET
B
105
43.136
−8.031
−3.177
1.00
31.39
C


ATOM
1757
CB
MET
B
105
41.918
−8.182
−2.270
1.00
33.00
C


ATOM
1758
CG
MET
B
105
41.063
−6.942
−2.145
1.00
38.80
C


ATOM
1759
SD
MET
B
105
40.356
−6.594
−3.753
1.00
41.80
S


ATOM
1760
CE
MET
B
105
39.143
−7.874
−3.693
1.00
49.56
C


ATOM
1761
C
MET
B
105
44.336
−8.189
−2.319
1.00
31.71
C


ATOM
1762
O
MET
B
105
44.667
−9.305
−1.911
1.00
31.15
O


ATOM
1763
N
VAL
B
106
44.991
−7.075
−2.006
1.00
31.47
N


ATOM
1764
CA
VAL
B
106
45.960
−7.056
−0.929
1.00
33.12
C


ATOM
1765
CB
VAL
B
106
46.528
−5.649
−0.736
1.00
32.05
C


ATOM
1766
CG1
VAL
B
106
47.526
−5.649
0.323
1.00
32.12
C


ATOM
1767
CG2
VAL
B
106
47.164
−5.186
−2.013
1.00
31.80
C


ATOM
1768
C
VAL
B
106
45.287
−7.601
0.368
1.00
34.62
C


ATOM
1769
O
VAL
B
106
44.032
−7.384
0.577
1.00
34.28
O


ATOM
1770
N
GLY
B
107
46.126
−8.309
1.212
1.00
34.95
N


ATOM
1771
CA
GLY
B
107
45.566
−9.209
2.267
1.00
34.64
C


ATOM
1772
C
GLY
B
107
45.048
−10.613
1.825
1.00
35.04
C


ATOM
1773
O
GLY
B
107
44.566
−11.404
2.676
1.00
36.55
O


ATOM
1774
N
GLY
B
108
45.122
−10.929
0.525
1.00
32.55
N


ATOM
1775
CA
GLY
B
108
45.225
−12.307
0.075
1.00
30.81
C


ATOM
1776
C
GLY
B
108
43.925
−12.886
−0.359
1.00
30.73
C


ATOM
1777
O
GLY
B
108
43.812
−14.091
−0.489
1.00
31.42
O


ATOM
1778
N
VAL
B
109
42.963
−12.006
−0.622
1.00
30.06
N


ATOM
1779
CA
VAL
B
109
41.610
−12.332
−1.113
1.00
29.98
C


ATOM
1780
CB
VAL
B
109
40.595
−11.330
−0.447
1.00
29.82
C


ATOM
1781
CG1
VAL
B
109
39.238
−11.415
−0.954
1.00
27.30
C


ATOM
1782
CG2
VAL
B
109
40.579
−11.519
1.073
1.00
31.58
C


ATOM
1783
C
VAL
B
109
41.576
−12.271
−2.652
1.00
30.22
C


ATOM
1784
O
VAL
B
109
41.988
−11.285
−3.280
1.00
29.55
O


ATOM
1785
N
VAL
B
110
41.103
−13.354
−3.257
1.00
31.00
N


ATOM
1786
CA
VAL
B
110
40.832
−13.376
−4.656
1.00
30.34
C


ATOM
1787
CB
VAL
B
110
41.760
−14.318
−5.501
1.00
30.78
C


ATOM
1788
CG1
VAL
B
110
41.079
−14.939
−6.663
1.00
27.57
C


ATOM
1789
CG2
VAL
B
110
42.605
−15.240
−4.676
1.00
28.92
C


ATOM
1790
C
VAL
B
110
39.376
−13.342
−4.934
1.00
32.42
C


ATOM
1791
O
VAL
B
110
38.617
−13.904
−4.193
1.00
32.63
O


ATOM
1792
N
ILE
B
111
38.986
−12.596
−5.962
1.00
34.25
N


ATOM
1793
CA
ILE
B
111
37.608
−12.418
−6.360
1.00
36.25
C


ATOM
1794
CB
ILE
B
111
37.377
−10.966
−6.834
1.00
37.63
C


ATOM
1795
CG1
ILE
B
111
38.177
−9.980
−5.960
1.00
39.86
C


ATOM
1796
CD1
ILE
B
111
37.582
−9.749
−4.568
1.00
44.15
C


ATOM
1797
CG2
ILE
B
111
35.871
−10.598
−6.970
1.00
35.86
C


ATOM
1798
C
ILE
B
111
37.401
−13.299
−7.581
1.00
37.45
C


ATOM
1799
O
ILE
B
111
38.116
−13.150
−8.569
1.00
38.10
O


ATOM
1800
N
GLY
B
112
36.478
−14.244
−7.487
1.00
37.85
N


ATOM
1801
CA
GLY
B
112
36.044
−15.026
−8.625
1.00
39.55
C


ATOM
1802
C
GLY
B
112
34.660
−14.536
−9.031
1.00
40.92
C


ATOM
1803
O
GLY
B
112
33.991
−13.833
−8.279
1.00
40.69
O


ATOM
1804
N
GLY
B
113
34.240
−14.877
−10.241
1.00
41.72
N


ATOM
1805
CA
GLY
B
113
32.878
−14.675
−10.631
1.00
42.68
C


ATOM
1806
C
GLY
B
113
32.526
−15.932
−11.369
1.00
44.53
C


ATOM
1807
O
GLY
B
113
33.385
−16.523
−12.033
1.00
45.28
O


ATOM
1808
N
GLU
B
114
31.281
−16.352
−11.230
1.00
45.00
N


ATOM
1809
CA
GLU
B
114
30.721
−17.475
−11.954
1.00
46.79
C


ATOM
1810
CB
GLU
B
114
30.486
−18.650
−11.003
1.00
47.57
C


ATOM
1811
CG
GLU
B
114
31.481
−19.777
−11.016
1.00
54.05
C


ATOM
1812
CD
GLU
B
114
31.681
−20.428
−12.384
1.00
60.74
C


ATOM
1813
OE1
GLU
B
114
32.730
−21.116
−12.540
1.00
65.24
O


ATOM
1814
OE2
GLU
B
114
30.834
−20.241
−13.294
1.00
62.06
O


ATOM
1815
C
GLU
B
114
29.349
−16.990
−12.451
1.00
46.24
C


ATOM
1816
O
GLU
B
114
28.600
−16.427
−11.683
1.00
45.45
O


ATOM
1817
N
LYS
B
115
29.048
−17.210
−13.730
1.00
47.57
N


ATOM
1818
CA
LYS
B
115
27.705
−16.986
−14.306
1.00
47.63
C


ATOM
1819
CB
LYS
B
115
27.868
−16.442
−15.716
1.00
49.05
C


ATOM
1820
CG
LYS
B
115
28.285
−14.990
−15.769
1.00
49.49
C


ATOM
1821
CD
LYS
B
115
28.457
−14.608
−17.209
1.00
58.06
C


ATOM
1822
CE
LYS
B
115
28.325
−13.100
−17.425
1.00
62.98
C


ATOM
1823
NZ
LYS
B
115
29.569
−12.371
−16.971
1.00
67.39
N


ATOM
1824
C
LYS
B
115
26.831
−18.235
−14.341
1.00
46.96
C


ATOM
1825
O
LYS
B
115
27.328
−19.359
−14.475
1.00
46.33
O


ATOM
1826
N
GLY
B
116
25.522
−18.055
−14.202
1.00
46.82
N


ATOM
1827
CA
GLY
B
116
24.551
−19.156
−14.429
1.00
45.94
C


ATOM
1828
C
GLY
B
116
24.477
−19.549
−15.896
1.00
46.06
C


ATOM
1829
O
GLY
B
116
24.948
−18.798
−16.764
1.00
46.74
O


ATOM
1830
N
ALA
B
117
23.929
−20.732
−16.203
1.00
44.78
N


ATOM
1831
CA
ALA
B
117
23.856
−21.181
−17.602
1.00
43.54
C


ATOM
1832
CB
ALA
B
117
23.609
−22.733
−17.710
1.00
42.15
C


ATOM
1833
C
ALA
B
117
22.804
−20.377
−18.395
1.00
43.36
C


ATOM
1834
O
ALA
B
117
22.765
−20.473
−19.619
1.00
44.57
O


ATOM
1835
N
GLY
B
118
22.009
−19.543
−17.711
1.00
42.01
N


ATOM
1836
CA
GLY
B
118
21.041
−18.672
−18.374
1.00
40.50
C


ATOM
1837
C
GLY
B
118
19.638
−19.226
−18.447
1.00
40.45
C


ATOM
1838
O
GLY
B
118
19.440
−20.454
−18.385
1.00
39.63
O


ATOM
1839
N
THR
B
119
18.689
−18.293
−18.609
1.00
39.73
N


ATOM
1840
CA
THR
B
119
17.267
−18.517
−18.728
1.00
39.06
C


ATOM
1841
CB
THR
B
119
16.494
−17.767
−17.648
1.00
39.37
C


ATOM
1842
OG1
THR
B
119
16.867
−18.298
−16.359
1.00
42.58
O


ATOM
1843
CG2
THR
B
119
14.985
−17.926
−17.817
1.00
36.37
C


ATOM
1844
C
THR
B
119
16.846
−18.000
−20.086
1.00
40.30
C


ATOM
1845
O
THR
B
119
17.046
−16.827
−20.386
1.00
40.23
O


ATOM
1846
N
ALA
B
120
16.306
−18.881
−20.930
1.00
40.46
N


ATOM
1847
CA
ALA
B
120
15.808
−18.450
−22.232
1.00
39.96
C


ATOM
1848
CB
ALA
B
120
16.032
−19.546
−23.327
1.00
38.10
C


ATOM
1849
C
ALA
B
120
14.333
−18.107
−22.056
1.00
39.39
C


ATOM
1850
O
ALA
B
120
13.514
−18.995
−21.874
1.00
39.29
O


ATOM
1851
N
LEU
B
121
14.018
−16.811
−22.058
1.00
38.26
N


ATOM
1852
CA
LEU
B
121
12.655
−16.366
−21.893
1.00
38.37
C


ATOM
1853
CB
LEU
B
121
12.552
−15.321
−20.816
1.00
37.24
C


ATOM
1854
CG
LEU
B
121
11.223
−14.563
−20.800
1.00
39.25
C


ATOM
1855
CD1
LEU
B
121
10.056
−15.389
−20.199
1.00
38.60
C


ATOM
1856
CD2
LEU
B
121
11.327
−13.202
−20.149
1.00
34.33
C


ATOM
1857
C
LEU
B
121
11.955
−15.883
−23.237
1.00
39.04
C


ATOM
1858
O
LEU
B
121
12.473
−15.020
−23.955
1.00
40.91
O


ATOM
1859
N
THR
B
122
10.811
−16.491
−23.548
1.00
38.34
N


ATOM
1860
CA
THR
B
122
9.930
−16.055
−24.614
1.00
39.43
C


ATOM
1861
CB
THR
B
122
9.552
−17.214
−25.559
1.00
39.02
C


ATOM
1862
OG1
THR
B
122
10.738
−17.917
−25.949
1.00
39.58
O


ATOM
1863
CG2
THR
B
122
8.846
−16.654
−26.785
1.00
40.51
C


ATOM
1864
C
THR
B
122
8.660
−15.512
−23.988
1.00
38.05
C


ATOM
1865
O
THR
B
122
8.034
−16.192
−23.186
1.00
38.30
O


ATOM
1866
N
VAL
B
123
8.343
−14.258
−24.283
1.00
38.09
N


ATOM
1867
CA
VAL
B
123
7.093
−13.650
−23.812
1.00
38.38
C


ATOM
1868
CB
VAL
B
123
7.274
−12.260
−23.225
1.00
37.30
C


ATOM
1869
CG1
VAL
B
123
5.940
−11.665
−22.754
1.00
38.24
C


ATOM
1870
CG2
VAL
B
123
8.307
−12.240
−22.120
1.00
35.68
C


ATOM
1871
C
VAL
B
123
6.172
−13.609
−25.055
1.00
40.09
C


ATOM
1872
O
VAL
B
123
6.580
−13.168
−26.152
1.00
38.15
O


ATOM
1873
N
LYS
B
124
4.948
−14.096
−24.870
1.00
42.46
N


ATOM
1874
CA
LYS
B
124
3.962
−14.184
−25.947
1.00
45.11
C


ATOM
1875
CB
LYS
B
124
3.596
−15.645
−26.162
1.00
44.65
C


ATOM
1876
CG
LYS
B
124
4.855
−16.487
−26.597
1.00
44.00
C


ATOM
1877
CD
LYS
B
124
4.562
−17.860
−27.095
1.00
41.77
C


ATOM
1878
CE
LYS
B
124
5.855
−18.519
−27.544
1.00
40.51
C


ATOM
1879
NZ
LYS
B
124
5.576
−19.819
−28.207
1.00
47.63
N


ATOM
1880
C
LYS
B
124
2.734
−13.382
−25.557
1.00
47.91
C


ATOM
1881
O
LYS
B
124
2.298
−13.441
−24.407
1.00
48.54
O


ATOM
1882
N
ALA
B
125
2.192
−12.603
−26.488
1.00
50.80
N


ATOM
1883
CA
ALA
B
125
0.849
−12.034
−26.276
1.00
53.80
C


ATOM
1884
CB
ALA
B
125
0.556
−10.903
−27.275
1.00
53.63
C


ATOM
1885
C
ALA
B
125
−0.163
−13.137
−26.440
1.00
55.22
C


ATOM
1886
O
ALA
B
125
−0.164
−13.791
−27.472
1.00
56.23
O


ATOM
1887
N
ALA
B
126
−1.002
−13.379
−25.438
1.00
57.49
N


ATOM
1888
CA
ALA
B
126
−2.254
−14.133
−25.698
1.00
59.24
C


ATOM
1889
CB
ALA
B
126
−3.063
−14.300
−24.393
1.00
59.45
C


ATOM
1890
C
ALA
B
126
−3.111
−13.414
−26.810
1.00
60.27
C


ATOM
1891
O
ALA
B
126
−3.505
−13.983
−27.865
1.00
59.50
O


ATOM
1892
OXT
ALA
B
126
−3.391
−12.183
−26.675
1.00
60.56
O


ATOM
1893
N
ALA
C
1
47.894
12.704
−2.969
1.00
49.41
N


ATOM
1894
CA
ALA
C
1
46.483
12.845
−2.525
1.00
48.69
C


ATOM
1895
CB
ALA
C
1
45.612
11.926
−3.320
1.00
49.22
C


ATOM
1896
C
ALA
C
1
46.345
12.555
−1.040
1.00
49.03
C


ATOM
1897
O
ALA
C
1
47.219
11.950
−0.422
1.00
48.45
O


ATOM
1898
N
TRP
C
2
45.241
12.989
−0.442
1.00
48.83
N


ATOM
1899
CA
TRP
C
2
45.029
12.703
0.970
1.00
47.92
C


ATOM
1900
CB
TRP
C
2
45.920
13.592
1.858
1.00
46.22
C


ATOM
1901
CG
TRP
C
2
45.728
15.092
1.734
1.00
46.85
C


ATOM
1902
CD1
TRP
C
2
46.068
15.895
0.653
1.00
46.02
C


ATOM
1903
NE1
TRP
C
2
45.753
17.216
0.924
1.00
45.63
N


ATOM
1904
CE2
TRP
C
2
45.233
17.303
2.191
1.00
46.81
C


ATOM
1905
CD2
TRP
C
2
45.200
15.983
2.737
1.00
47.63
C


ATOM
1906
CE3
TRP
C
2
44.719
15.802
4.053
1.00
46.87
C


ATOM
1907
CZ3
TRP
C
2
44.289
16.918
4.769
1.00
46.19
C


ATOM
1908
CH2
TRP
C
2
44.326
18.226
4.185
1.00
45.94
C


ATOM
1909
CZ2
TRP
C
2
44.781
18.428
2.907
1.00
46.39
C


ATOM
1910
C
TRP
C
2
43.560
12.862
1.314
1.00
48.15
C


ATOM
1911
O
TRP
C
2
42.877
13.673
0.702
1.00
47.92
O


ATOM
1912
N
VAL
C
3
43.077
12.104
2.304
1.00
48.14
N


ATOM
1913
CA
VAL
C
3
41.713
12.343
2.793
1.00
47.09
C


ATOM
1914
CB
VAL
C
3
40.905
11.060
3.039
1.00
46.72
C


ATOM
1915
CG1
VAL
C
3
39.538
11.402
3.680
1.00
44.65
C


ATOM
1916
CG2
VAL
C
3
40.706
10.367
1.753
1.00
46.02
C


ATOM
1917
C
VAL
C
3
41.738
13.261
3.993
1.00
46.31
C


ATOM
1918
O
VAL
C
3
42.494
13.073
4.925
1.00
48.10
O


ATOM
1919
N
ASP
C
4
40.937
14.303
3.930
1.00
46.31
N


ATOM
1920
CA
ASP
C
4
40.908
15.306
4.965
1.00
45.27
C


ATOM
1921
CB
ASP
C
4
40.916
16.681
4.312
1.00
45.16
C


ATOM
1922
CG
ASP
C
4
40.888
17.815
5.312
1.00
46.64
C


ATOM
1923
OD1
ASP
C
4
41.135
17.640
6.526
1.00
52.47
O


ATOM
1924
OD2
ASP
C
4
40.594
18.933
4.886
1.00
48.46
O


ATOM
1925
C
ASP
C
4
39.615
15.025
5.728
1.00
44.41
C


ATOM
1926
O
ASP
C
4
38.534
15.276
5.260
1.00
43.86
O


ATOM
1927
N
GLN
C
5
39.777
14.424
6.883
1.00
43.38
N


ATOM
1928
CA
GLN
C
5
38.699
14.020
7.725
1.00
42.49
C


ATOM
1929
CB
GLN
C
5
38.951
12.585
8.184
1.00
43.25
C


ATOM
1930
CG
GLN
C
5
37.964
12.087
9.266
1.00
42.78
C


ATOM
1931
CD
GLN
C
5
38.117
10.629
9.568
1.00
43.36
C


ATOM
1932
OE1
GLN
C
5
38.975
9.911
8.977
1.00
44.25
O


ATOM
1933
NE2
GLN
C
5
37.341
10.171
10.522
1.00
41.48
N


ATOM
1934
C
GLN
C
5
38.612
14.947
8.919
1.00
41.74
C


ATOM
1935
O
GLN
C
5
39.573
15.107
9.659
1.00
41.18
O


ATOM
1936
N
THR
C
6
37.434
15.557
9.077
1.00
42.37
N


ATOM
1937
CA
THR
C
6
37.127
16.448
10.187
1.00
42.38
C


ATOM
1938
CB
THR
C
6
37.134
17.922
9.730
1.00
43.81
C


ATOM
1939
OG1
THR
C
6
36.323
18.087
8.567
1.00
42.52
O


ATOM
1940
CG2
THR
C
6
38.614
18.342
9.375
1.00
41.50
C


ATOM
1941
C
THR
C
6
35.801
16.006
10.801
1.00
42.03
C


ATOM
1942
O
THR
C
6
34.967
15.469
10.102
1.00
42.87
O


ATOM
1943
N
PRO
C
7
35.654
16.121
12.134
1.00
41.26
N


ATOM
1944
CA
PRO
C
7
36.674
16.605
13.095
1.00
39.68
C


ATOM
1945
CB
PRO
C
7
35.847
17.012
14.318
1.00
38.19
C


ATOM
1946
CG
PRO
C
7
34.571
16.163
14.235
1.00
39.85
C


ATOM
1947
CD
PRO
C
7
34.370
15.774
12.795
1.00
41.08
C


ATOM
1948
C
PRO
C
7
37.674
15.539
13.526
1.00
40.17
C


ATOM
1949
O
PRO
C
7
37.376
14.341
13.492
1.00
40.26
O


ATOM
1950
N
ARG
C
8
38.833
15.968
14.000
1.00
39.86
N


ATOM
1951
CA
ARG
C
8
39.787
15.015
14.450
1.00
42.27
C


ATOM
1952
CB
ARG
C
8
41.170
15.678
14.495
1.00
43.98
C


ATOM
1953
CG
ARG
C
8
42.321
14.715
14.708
1.00
50.28
C


ATOM
1954
CD
ARG
C
8
42.501
13.799
13.469
1.00
56.99
C


ATOM
1955
NE
ARG
C
8
43.131
14.492
12.357
1.00
59.34
N


ATOM
1956
CZ
ARG
C
8
44.447
14.636
12.274
1.00
64.10
C


ATOM
1957
NH1
ARG
C
8
45.012
15.284
11.252
1.00
65.07
N


ATOM
1958
NH2
ARG
C
8
45.200
14.117
13.239
1.00
67.46
N


ATOM
1959
C
ARG
C
8
39.357
14.418
15.816
1.00
41.81
C


ATOM
1960
O
ARG
C
8
39.638
13.250
16.123
1.00
41.61
O


ATOM
1961
N
THR
C
9
38.647
15.208
16.622
1.00
41.23
N


ATOM
1962
CA
THR
C
9
38.189
14.769
17.918
1.00
41.41
C


ATOM
1963
CB
THR
C
9
39.112
15.257
19.097
1.00
42.45
C


ATOM
1964
OG1
THR
C
9
39.108
16.701
19.180
1.00
45.56
O


ATOM
1965
CG2
THR
C
9
40.515
14.757
18.961
1.00
40.73
C


ATOM
1966
C
THR
C
9
36.847
15.389
18.127
1.00
41.08
C


ATOM
1967
O
THR
C
9
36.648
16.543
17.778
1.00
42.09
O


ATOM
1968
N
ALA
C
10
35.932
14.635
18.707
1.00
40.39
N


ATOM
1969
CA
ALA
C
10
34.587
15.110
19.081
1.00
40.33
C


ATOM
1970
CB
ALA
C
10
33.522
14.620
18.072
1.00
38.32
C


ATOM
1971
C
ALA
C
10
34.259
14.568
20.473
1.00
41.20
C


ATOM
1972
O
ALA
C
10
34.525
13.384
20.784
1.00
40.94
O


ATOM
1973
N
THR
C
11
33.736
15.455
21.324
1.00
42.57
N


ATOM
1974
CA
THR
C
11
33.123
15.099
22.616
1.00
42.23
C


ATOM
1975
CB
THR
C
11
33.759
15.861
23.749
1.00
42.79
C


ATOM
1976
OG1
THR
C
11
35.145
15.491
23.827
1.00
46.26
O


ATOM
1977
CG2
THR
C
11
33.078
15.537
25.097
1.00
40.59
C


ATOM
1978
C
THR
C
11
31.633
15.460
22.493
1.00
42.65
C


ATOM
1979
O
THR
C
11
31.325
16.618
22.223
1.00
43.18
O


ATOM
1980
N
LYS
C
12
30.743
14.467
22.657
1.00
41.78
N


ATOM
1981
CA
LYS
C
12
29.339
14.597
22.369
1.00
41.37
C


ATOM
1982
CB
LYS
C
12
28.928
13.733
21.191
1.00
41.59
C


ATOM
1983
CG
LYS
C
12
29.465
14.167
19.826
1.00
41.91
C


ATOM
1984
CD
LYS
C
12
29.346
15.654
19.576
1.00
43.02
C


ATOM
1985
CE
LYS
C
12
28.977
15.936
18.151
1.00
46.80
C


ATOM
1986
NZ
LYS
C
12
29.307
17.320
17.716
1.00
49.30
N


ATOM
1987
C
LYS
C
12
28.579
14.096
23.536
1.00
42.56
C


ATOM
1988
O
LYS
C
12
29.097
13.230
24.256
1.00
43.65
O


ATOM
1989
N
GLU
C
13
27.341
14.602
23.726
1.00
41.23
N


ATOM
1990
CA
GLU
C
13
26.474
14.080
24.762
1.00
41.54
C


ATOM
1991
CB
GLU
C
13
25.675
15.232
25.379
1.00
41.00
C


ATOM
1992
CG
GLU
C
13
26.562
16.359
25.900
1.00
42.17
C


ATOM
1993
CD
GLU
C
13
25.723
17.635
26.233
1.00
46.00
C


ATOM
1994
OE1
GLU
C
13
26.311
18.695
26.591
1.00
47.15
O


ATOM
1995
OE2
GLU
C
13
24.466
17.550
26.116
1.00
48.60
O


ATOM
1996
C
GLU
C
13
25.563
13.073
24.149
1.00
40.75
C


ATOM
1997
O
GLU
C
13
25.335
13.105
22.910
1.00
42.27
O


ATOM
1998
N
THR
C
14
25.002
12.167
24.938
1.00
40.94
N


ATOM
1999
CA
THR
C
14
24.042
11.239
24.328
1.00
42.25
C


ATOM
2000
CB
THR
C
14
23.544
10.101
25.272
1.00
42.73
C


ATOM
2001
OG1
THR
C
14
22.715
10.665
26.243
1.00
48.01
O


ATOM
2002
CG2
THR
C
14
24.705
9.386
25.975
1.00
42.04
C


ATOM
2003
C
THR
C
14
22.861
12.015
23.700
1.00
40.89
C


ATOM
2004
O
THR
C
14
22.487
13.053
24.202
1.00
41.70
O


ATOM
2005
N
GLY
C
15
22.308
11.538
22.591
1.00
39.88
N


ATOM
2006
CA
GLY
C
15
21.224
12.239
21.898
1.00
38.62
C


ATOM
2007
C
GLY
C
15
21.690
13.211
20.812
1.00
38.27
C


ATOM
2008
O
GLY
C
15
20.912
13.537
19.886
1.00
39.29
O


ATOM
2009
N
GLU
C
16
22.921
13.685
20.902
1.00
36.77
N


ATOM
2010
CA
GLU
C
16
23.522
14.515
19.858
1.00
38.21
C


ATOM
2011
CB
GLU
C
16
24.766
15.286
20.373
1.00
37.37
C


ATOM
2012
CG
GLU
C
16
24.448
16.420
21.495
1.00
38.40
C


ATOM
2013
CD
GLU
C
16
25.627
17.359
21.780
1.00
38.50
C


ATOM
2014
OE1
GLU
C
16
26.733
16.846
21.984
1.00
40.44
O


ATOM
2015
OE2
GLU
C
16
25.489
18.609
21.757
1.00
38.88
O


ATOM
2016
C
GLU
C
16
23.874
13.652
18.635
1.00
40.24
C


ATOM
2017
O
GLU
C
16
23.852
12.414
18.745
1.00
42.05
O


ATOM
2018
N
SER
C
17
24.137
14.306
17.494
1.00
39.57
N


ATOM
2019
CA
SER
C
17
24.621
13.722
16.264
1.00
40.14
C


ATOM
2020
CB
SER
C
17
23.844
14.317
15.073
1.00
39.97
C


ATOM
2021
OG
SER
C
17
22.451
13.972
15.174
1.00
42.60
O


ATOM
2022
C
SER
C
17
26.094
14.113
16.057
1.00
40.75
C


ATOM
2023
O
SER
C
17
26.547
15.102
16.557
1.00
40.20
O


ATOM
2024
N
LEU
C
18
26.823
13.314
15.288
1.00
40.85
N


ATOM
2025
CA
LEU
C
18
28.139
13.643
14.874
1.00
41.38
C


ATOM
2026
CB
LEU
C
18
29.061
12.561
15.427
1.00
41.14
C


ATOM
2027
CG
LEU
C
18
30.600
12.596
15.451
1.00
44.10
C


ATOM
2028
CD1
LEU
C
18
31.251
11.259
14.907
1.00
38.99
C


ATOM
2029
CD2
LEU
C
18
31.291
13.933
15.015
1.00
41.87
C


ATOM
2030
C
LEU
C
18
28.102
13.544
13.321
1.00
41.20
C


ATOM
2031
O
LEU
C
18
27.616
12.564
12.803
1.00
39.57
O


ATOM
2032
N
THR
C
19
28.624
14.567
12.624
1.00
41.23
N


ATOM
2033
CA
THR
C
19
28.945
14.495
11.209
1.00
41.67
C


ATOM
2034
CB
THR
C
19
28.303
15.664
10.371
1.00
41.81
C


ATOM
2035
OG1
THR
C
19
26.939
15.741
10.732
1.00
41.36
O


ATOM
2036
CG2
THR
C
19
28.390
15.426
8.826
1.00
41.66
C


ATOM
2037
C
THR
C
19
30.442
14.493
11.061
1.00
41.89
C


ATOM
2038
O
THR
C
19
31.144
15.426
11.504
1.00
41.70
O


ATOM
2039
N
ILE
C
20
30.930
13.399
10.473
1.00
41.66
N


ATOM
2040
CA
ILE
C
20
32.321
13.291
10.062
1.00
42.12
C


ATOM
2041
CB
ILE
C
20
32.855
11.887
10.306
1.00
41.88
C


ATOM
2042
CG1
ILE
C
20
32.758
11.550
11.820
1.00
41.13
C


ATOM
2043
CD1
ILE
C
20
32.960
10.088
12.166
1.00
40.95
C


ATOM
2044
CG2
ILE
C
20
34.363
11.820
9.859
1.00
42.36
C


ATOM
2045
C
ILE
C
20
32.348
13.605
8.568
1.00
42.26
C


ATOM
2046
O
ILE
C
20
31.661
12.949
7.823
1.00
41.71
O


ATOM
2047
N
ASN
C
21
33.104
14.624
8.159
1.00
43.04
N


ATOM
2048
CA
ASN
C
21
33.313
14.925
6.762
1.00
45.16
C


ATOM
2049
CB
ASN
C
21
33.189
16.438
6.512
1.00
46.62
C


ATOM
2050
CG
ASN
C
21
31.762
16.957
6.721
1.00
49.24
C


ATOM
2051
OD1
ASN
C
21
30.831
16.593
5.972
1.00
56.70
O


ATOM
2052
ND2
ASN
C
21
31.582
17.830
7.730
1.00
49.52
N


ATOM
2053
C
ASN
C
21
34.686
14.471
6.266
1.00
45.75
C


ATOM
2054
O
ASN
C
21
35.684
14.670
6.944
1.00
46.28
O


ATOM
2055
N
CYS
C
22
34.723
13.897
5.073
1.00
46.82
N


ATOM
2056
CA
CYS
C
22
35.959
13.487
4.390
1.00
48.35
C


ATOM
2057
CB
CYS
C
22
36.085
11.967
4.403
1.00
49.01
C


ATOM
2058
SG
CYS
C
22
36.404
11.250
6.007
1.00
54.40
S


ATOM
2059
C
CYS
C
22
35.984
13.967
2.918
1.00
47.56
C


ATOM
2060
O
CYS
C
22
34.978
13.866
2.185
1.00
47.67
O


ATOM
2061
N
VAL
C
23
37.123
14.505
2.496
1.00
46.77
N


ATOM
2062
CA
VAL
C
23
37.304
14.992
1.118
1.00
44.55
C


ATOM
2063
CB
VAL
C
23
37.150
16.531
1.002
1.00
44.60
C


ATOM
2064
CG1
VAL
C
23
37.928
17.212
2.000
1.00
46.21
C


ATOM
2065
CG2
VAL
C
23
37.482
17.046
−0.374
1.00
41.80
C


ATOM
2066
C
VAL
C
23
38.626
14.498
0.625
1.00
44.64
C


ATOM
2067
O
VAL
C
23
39.675
14.683
1.266
1.00
43.95
O


ATOM
2068
N
LEU
C
24
38.574
13.824
−0.512
1.00
44.47
N


ATOM
2069
CA
LEU
C
24
39.784
13.393
−1.220
1.00
44.52
C


ATOM
2070
CB
LEU
C
24
39.348
12.419
−2.293
1.00
44.25
C


ATOM
2071
CG
LEU
C
24
40.109
11.175
−2.724
1.00
44.73
C


ATOM
2072
CD1
LEU
C
24
39.957
11.047
−4.204
1.00
40.23
C


ATOM
2073
CD2
LEU
C
24
41.538
11.066
−2.237
1.00
39.12
C


ATOM
2074
C
LEU
C
24
40.400
14.631
−1.912
1.00
44.53
C


ATOM
2075
O
LEU
C
24
39.900
15.064
−2.955
1.00
44.70
O


ATOM
2076
N
ARG
C
25
41.478
15.178
−1.362
1.00
44.03
N


ATOM
2077
CA
ARG
C
25
42.084
16.424
−1.857
1.00
44.69
C


ATOM
2078
CB
ARG
C
25
42.553
17.314
−0.692
1.00
44.52
C


ATOM
2079
CG
ARG
C
25
41.525
17.578
0.303
1.00
48.32
C


ATOM
2080
CD
ARG
C
25
41.769
18.944
0.893
1.00
55.19
C


ATOM
2081
NE
ARG
C
25
40.566
19.723
0.675
1.00
61.48
N


ATOM
2082
CZ
ARG
C
25
39.708
19.984
1.631
1.00
63.06
C


ATOM
2083
NH1
ARG
C
25
39.998
19.570
2.840
1.00
64.66
N


ATOM
2084
NH2
ARG
C
25
38.597
20.665
1.395
1.00
64.06
N


ATOM
2085
C
ARG
C
25
43.299
16.116
−2.694
1.00
44.89
C


ATOM
2086
O
ARG
C
25
43.971
15.093
−2.441
1.00
45.00
O


ATOM
2087
N
ASP
C
26
43.593
17.013
−3.647
1.00
44.78
N


ATOM
2088
CA
ASP
C
26
44.661
16.859
−4.650
1.00
45.57
C


ATOM
2089
CB
ASP
C
26
46.044
17.275
−4.103
1.00
46.72
C


ATOM
2090
CG
ASP
C
26
45.991
18.501
−3.221
1.00
50.19
C


ATOM
2091
OD1
ASP
C
26
45.405
19.537
−3.629
1.00
53.01
O


ATOM
2092
OD2
ASP
C
26
46.552
18.429
−2.099
1.00
56.34
O


ATOM
2093
C
ASP
C
26
44.784
15.464
−5.185
1.00
44.38
C


ATOM
2094
O
ASP
C
26
45.871
14.927
−5.215
1.00
43.71
O


ATOM
2095
N
ALA
C
27
43.679
14.845
−5.567
1.00
44.56
N


ATOM
2096
CA
ALA
C
27
43.757
13.530
−6.180
1.00
44.95
C


ATOM
2097
CB
ALA
C
27
42.740
12.552
−5.573
1.00
43.12
C


ATOM
2098
C
ALA
C
27
43.581
13.633
−7.690
1.00
46.25
C


ATOM
2099
O
ALA
C
27
42.797
14.464
−8.174
1.00
46.95
O


ATOM
2100
N
SER
C
28
44.294
12.777
−8.432
1.00
46.99
N


ATOM
2101
CA
SER
C
28
44.153
12.779
−9.869
1.00
48.62
C


ATOM
2102
CB
SER
C
28
45.480
12.479
−10.560
1.00
48.58
C


ATOM
2103
OG
SER
C
28
46.044
11.353
−9.990
1.00
52.33
O


ATOM
2104
C
SER
C
28
43.026
11.836
−10.303
1.00
48.24
C


ATOM
2105
O
SER
C
28
42.716
11.733
−11.473
1.00
49.15
O


ATOM
2106
N
PHE
C
29
42.370
11.220
−9.334
1.00
47.44
N


ATOM
2107
CA
PHE
C
29
41.340
10.221
−9.612
1.00
46.65
C


ATOM
2108
CB
PHE
C
29
41.726
8.894
−8.920
1.00
45.70
C


ATOM
2109
CG
PHE
C
29
43.158
8.502
−9.180
1.00
42.81
C


ATOM
2110
CD1
PHE
C
29
43.538
8.066
−10.448
1.00
36.25
C


ATOM
2111
CE1
PHE
C
29
44.850
7.768
−10.742
1.00
40.99
C


ATOM
2112
CZ
PHE
C
29
45.820
7.884
−9.731
1.00
43.75
C


ATOM
2113
CE2
PHE
C
29
45.441
8.337
−8.441
1.00
40.55
C


ATOM
2114
CD2
PHE
C
29
44.116
8.649
−8.189
1.00
40.78
C


ATOM
2115
C
PHE
C
29
39.958
10.697
−9.171
1.00
46.58
C


ATOM
2116
O
PHE
C
29
39.831
11.601
−8.317
1.00
46.70
O


ATOM
2117
N
GLU
C
30
38.942
10.067
−9.750
1.00
45.81
N


ATOM
2118
CA
GLU
C
30
37.563
10.269
−9.351
1.00
46.83
C


ATOM
2119
CB
GLU
C
30
36.632
9.980
−10.536
1.00
47.06
C


ATOM
2120
CG
GLU
C
30
36.882
10.950
−11.687
1.00
49.84
C


ATOM
2121
CD
GLU
C
30
36.469
12.382
−11.319
1.00
57.62
C


ATOM
2122
OE1
GLU
C
30
37.291
13.328
−11.489
1.00
60.20
O


ATOM
2123
OE2
GLU
C
30
35.322
12.553
−10.835
1.00
58.67
O


ATOM
2124
C
GLU
C
30
37.257
9.401
−8.127
1.00
46.19
C


ATOM
2125
O
GLU
C
30
37.833
8.321
−7.956
1.00
47.70
O


ATOM
2126
N
LEU
C
31
36.387
9.880
−7.259
1.00
45.21
N


ATOM
2127
CA
LEU
C
31
35.899
9.053
−6.142
1.00
44.93
C


ATOM
2128
CB
LEU
C
31
35.102
9.934
−5.217
1.00
43.15
C


ATOM
2129
CG
LEU
C
31
35.111
9.885
−3.699
1.00
44.69
C


ATOM
2130
CD1
LEU
C
31
33.683
10.296
−3.177
1.00
36.97
C


ATOM
2131
CD2
LEU
C
31
35.711
8.615
−3.022
1.00
38.29
C


ATOM
2132
C
LEU
C
31
34.937
7.956
−6.652
1.00
45.16
C


ATOM
2133
O
LEU
C
31
33.860
8.246
−7.196
1.00
44.80
O


ATOM
2134
N
LYS
C
32
35.286
6.701
−6.434
1.00
46.15
N


ATOM
2135
CA
LYS
C
32
34.505
5.608
−6.991
1.00
46.54
C


ATOM
2136
CB
LYS
C
32
35.461
4.506
−7.478
1.00
46.96
C


ATOM
2137
CG
LYS
C
32
34.801
3.264
−8.090
1.00
50.13
C


ATOM
2138
CD
LYS
C
32
33.911
3.610
−9.290
1.00
57.71
C


ATOM
2139
CE
LYS
C
32
33.263
2.363
−9.882
1.00
61.56
C


ATOM
2140
NZ
LYS
C
32
33.432
1.172
−8.953
1.00
64.12
N


ATOM
2141
C
LYS
C
32
33.606
5.063
−5.905
1.00
46.00
C


ATOM
2142
O
LYS
C
32
32.462
4.730
−6.158
1.00
46.13
O


ATOM
2143
N
ASP
C
33
34.149
4.969
−4.698
1.00
44.66
N


ATOM
2144
CA
ASP
C
33
33.519
4.229
−3.609
1.00
44.59
C


ATOM
2145
CB
ASP
C
33
33.969
2.787
−3.714
1.00
45.73
C


ATOM
2146
CG
ASP
C
33
32.854
1.826
−3.570
1.00
53.17
C


ATOM
2147
OD1
ASP
C
33
32.322
1.737
−2.442
1.00
60.90
O


ATOM
2148
OD2
ASP
C
33
32.510
1.158
−4.597
1.00
61.93
O


ATOM
2149
C
ASP
C
33
34.007
4.777
−2.272
1.00
42.39
C


ATOM
2150
O
ASP
C
33
35.028
5.440
−2.230
1.00
39.76
O


ATOM
2151
N
THR
C
34
33.338
4.398
−1.181
1.00
42.58
N


ATOM
2152
CA
THR
C
34
33.698
4.850
0.198
1.00
43.04
C


ATOM
2153
CB
THR
C
34
32.810
6.031
0.681
1.00
43.33
C


ATOM
2154
OG1
THR
C
34
31.451
5.618
0.749
1.00
45.15
O


ATOM
2155
CG2
THR
C
34
32.867
7.227
−0.263
1.00
43.17
C


ATOM
2156
C
THR
C
34
33.529
3.715
1.235
1.00
43.65
C


ATOM
2157
O
THR
C
34
32.668
2.867
1.082
1.00
44.87
O


ATOM
2158
N
GLY
C
35
34.384
3.686
2.256
1.00
43.02
N


ATOM
2159
CA
GLY
C
35
34.214
2.825
3.400
1.00
40.60
C


ATOM
2160
C
GLY
C
35
34.387
3.562
4.711
1.00
40.55
C


ATOM
2161
O
GLY
C
35
35.086
4.603
4.784
1.00
40.16
O


ATOM
2162
N
TRP
C
36
33.817
2.969
5.766
1.00
39.56
N


ATOM
2163
CA
TRP
C
36
33.800
3.546
7.094
1.00
39.04
C


ATOM
2164
CB
TRP
C
36
32.434
4.191
7.420
1.00
37.69
C


ATOM
2165
CG
TRP
C
36
32.204
5.462
6.649
1.00
36.88
C


ATOM
2166
CD1
TRP
C
36
31.534
5.601
5.445
1.00
37.03
C


ATOM
2167
NE1
TRP
C
36
31.582
6.905
5.028
1.00
39.08
N


ATOM
2168
CE2
TRP
C
36
32.299
7.641
5.951
1.00
36.41
C


ATOM
2169
CD2
TRP
C
36
32.682
6.771
6.993
1.00
35.39
C


ATOM
2170
CE3
TRP
C
36
33.372
7.289
8.105
1.00
39.61
C


ATOM
2171
CZ3
TRP
C
36
33.629
8.658
8.149
1.00
41.57
C


ATOM
2172
CH2
TRP
C
36
33.200
9.514
7.090
1.00
39.46
C


ATOM
2173
CZ2
TRP
C
36
32.533
9.007
5.998
1.00
38.02
C


ATOM
2174
C
TRP
C
36
34.152
2.464
8.081
1.00
39.80
C


ATOM
2175
O
TRP
C
36
33.630
1.365
7.971
1.00
39.62
O


ATOM
2176
N
TYR
C
37
35.047
2.780
9.028
1.00
39.72
N


ATOM
2177
CA
TYR
C
37
35.586
1.769
9.988
1.00
42.18
C


ATOM
2178
CB
TYR
C
37
37.003
1.298
9.614
1.00
42.50
C


ATOM
2179
CG
TYR
C
37
37.114
0.995
8.128
1.00
46.10
C


ATOM
2180
CD1
TYR
C
37
36.832
−0.275
7.647
1.00
46.08
C


ATOM
2181
CE1
TYR
C
37
36.869
−0.558
6.267
1.00
49.05
C


ATOM
2182
CZ
TYR
C
37
37.246
0.447
5.381
1.00
48.62
C


ATOM
2183
OH
TYR
C
37
37.305
0.146
4.032
1.00
51.96
O


ATOM
2184
CE2
TYR
C
37
37.562
1.732
5.836
1.00
48.05
C


ATOM
2185
CD2
TYR
C
37
37.495
2.009
7.191
1.00
46.46
C


ATOM
2186
C
TYR
C
37
35.599
2.413
11.358
1.00
41.82
C


ATOM
2187
O
TYR
C
37
35.694
3.624
11.464
1.00
41.95
O


ATOM
2188
N
ARG
C
38
35.544
1.586
12.381
1.00
42.36
N


ATOM
2189
CA
ARG
C
38
35.573
2.021
13.729
1.00
44.49
C


ATOM
2190
CB
ARG
C
38
34.144
2.242
14.237
1.00
43.43
C


ATOM
2191
CG
ARG
C
38
34.110
2.406
15.718
1.00
47.74
C


ATOM
2192
CD
ARG
C
38
32.742
2.530
16.225
1.00
51.14
C


ATOM
2193
NE
ARG
C
38
31.885
1.427
15.821
1.00
52.19
N


ATOM
2194
CZ
ARG
C
38
30.571
1.409
16.035
1.00
57.68
C


ATOM
2195
NH1
ARG
C
38
29.942
2.452
16.614
1.00
59.02
N


ATOM
2196
NH2
ARG
C
38
29.868
0.353
15.673
1.00
59.82
N


ATOM
2197
C
ARG
C
38
36.288
0.991
14.613
1.00
45.46
C


ATOM
2198
O
ARG
C
38
36.115
−0.222
14.456
1.00
46.19
O


ATOM
2199
N
THR
C
39
37.083
1.516
15.543
1.00
46.20
N


ATOM
2200
CA
THR
C
39
37.717
0.800
16.641
1.00
46.40
C


ATOM
2201
CB
THR
C
39
39.209
1.155
16.699
1.00
45.51
C


ATOM
2202
OG1
THR
C
39
39.825
0.817
15.455
1.00
49.49
O


ATOM
2203
CG2
THR
C
39
39.937
0.406
17.866
1.00
48.80
C


ATOM
2204
C
THR
C
39
36.992
1.338
17.885
1.00
47.15
C


ATOM
2205
O
THR
C
39
37.109
2.523
18.232
1.00
45.10
O


ATOM
2206
N
LYS
C
40
36.167
0.482
18.484
1.00
49.20
N


ATOM
2207
CA
LYS
C
40
35.389
0.844
19.650
1.00
51.33
C


ATOM
2208
CB
LYS
C
40
34.355
−0.221
19.990
1.00
51.30
C


ATOM
2209
CG
LYS
C
40
32.952
0.226
19.595
1.00
55.88
C


ATOM
2210
CD
LYS
C
40
31.926
−0.887
19.626
1.00
59.21
C


ATOM
2211
CE
LYS
C
40
31.099
−0.803
20.895
1.00
63.11
C


ATOM
2212
NZ
LYS
C
40
31.075
−2.176
21.526
1.00
61.59
N


ATOM
2213
C
LYS
C
40
36.333
1.157
20.816
1.00
52.57
C


ATOM
2214
O
LYS
C
40
37.423
0.611
20.886
1.00
50.99
O


ATOM
2215
N
LEU
C
41
35.938
2.114
21.659
1.00
54.39
N


ATOM
2216
CA
LEU
C
41
36.802
2.622
22.737
1.00
57.08
C


ATOM
2217
CB
LEU
C
41
36.066
3.736
23.533
1.00
57.10
C


ATOM
2218
CG
LEU
C
41
36.543
4.136
24.933
1.00
59.84
C


ATOM
2219
CD1
LEU
C
41
35.549
5.096
25.662
1.00
61.21
C


ATOM
2220
CD2
LEU
C
41
37.964
4.735
24.863
1.00
62.80
C


ATOM
2221
C
LEU
C
41
37.302
1.465
23.642
1.00
58.11
C


ATOM
2222
O
LEU
C
41
36.505
0.742
24.266
1.00
58.05
O


ATOM
2223
N
GLY
C
42
38.616
1.264
23.669
1.00
59.71
N


ATOM
2224
CA
GLY
C
42
39.187
0.174
24.457
1.00
61.51
C


ATOM
2225
C
GLY
C
42
39.653
−1.023
23.643
1.00
62.72
C


ATOM
2226
O
GLY
C
42
40.460
−1.830
24.139
1.00
63.71
O


ATOM
2227
N
SER
C
43
39.164
−1.138
22.404
1.00
62.76
N


ATOM
2228
CA
SER
C
43
39.511
−2.239
21.519
1.00
62.79
C


ATOM
2229
CB
SER
C
43
38.328
−2.559
20.602
1.00
62.63
C


ATOM
2230
OG
SER
C
43
38.301
−3.927
20.271
1.00
61.87
O


ATOM
2231
C
SER
C
43
40.742
−1.897
20.689
1.00
63.37
C


ATOM
2232
O
SER
C
43
41.116
−0.728
20.557
1.00
63.84
O


ATOM
2233
N
THR
C
44
41.394
−2.912
20.139
1.00
63.50
N


ATOM
2234
CA
THR
C
44
42.377
−2.657
19.070
1.00
64.33
C


ATOM
2235
CB
THR
C
44
43.793
−3.127
19.469
1.00
64.45
C


ATOM
2236
OG1
THR
C
44
43.781
−4.544
19.687
1.00
66.10
O


ATOM
2237
CG2
THR
C
44
44.238
−2.424
20.769
1.00
63.59
C


ATOM
2238
C
THR
C
44
41.890
−3.251
17.729
1.00
63.70
C


ATOM
2239
O
THR
C
44
42.568
−3.185
16.695
1.00
64.39
O


ATOM
2240
N
ASN
C
45
40.675
−3.793
17.782
1.00
63.29
N


ATOM
2241
CA
ASN
C
45
39.968
−4.421
16.665
1.00
63.06
C


ATOM
2242
CB
ASN
C
45
38.963
−5.407
17.285
1.00
63.41
C


ATOM
2243
CG
ASN
C
45
38.299
−6.286
16.258
1.00
64.24
C


ATOM
2244
OD1
ASN
C
45
38.944
−6.744
15.312
1.00
64.63
O


ATOM
2245
ND2
ASN
C
45
36.996
−6.530
16.436
1.00
64.01
N


ATOM
2246
C
ASN
C
45
39.202
−3.426
15.744
1.00
62.52
C


ATOM
2247
O
ASN
C
45
38.108
−2.951
16.115
1.00
62.14
O


ATOM
2248
N
GLU
C
46
39.763
−3.111
14.573
1.00
61.57
N


ATOM
2249
CA
GLU
C
46
39.080
−2.251
13.572
1.00
61.38
C


ATOM
2250
CB
GLU
C
46
40.062
−1.708
12.530
1.00
61.16
C


ATOM
2251
CG
GLU
C
46
39.403
−1.084
11.308
1.00
63.74
C


ATOM
2252
CD
GLU
C
46
40.014
0.267
10.932
1.00
66.98
C


ATOM
2253
OE1
GLU
C
46
39.729
1.274
11.635
1.00
69.02
O


ATOM
2254
OE2
GLU
C
46
40.770
0.320
9.935
1.00
67.74
O


ATOM
2255
C
GLU
C
46
37.917
−2.948
12.868
1.00
60.84
C


ATOM
2256
O
GLU
C
46
38.086
−4.018
12.322
1.00
61.63
O


ATOM
2257
N
GLN
C
47
36.748
−2.322
12.856
1.00
60.18
N


ATOM
2258
CA
GLN
C
47
35.542
−2.929
12.279
1.00
59.69
C


ATOM
2259
CB
GLN
C
47
34.492
−3.142
13.364
1.00
60.04
C


ATOM
2260
CG
GLN
C
47
34.685
−4.423
14.153
1.00
63.45
C


ATOM
2261
CD
GLN
C
47
33.988
−4.364
15.502
1.00
67.03
C


ATOM
2262
OE1
GLN
C
47
33.722
−5.409
16.101
1.00
69.04
O


ATOM
2263
NE2
GLN
C
47
33.687
−3.134
15.992
1.00
65.48
N


ATOM
2264
C
GLN
C
47
34.882
−2.103
11.188
1.00
57.90
C


ATOM
2265
O
GLN
C
47
34.807
−0.893
11.276
1.00
56.91
O


ATOM
2266
N
SER
C
48
34.333
−2.792
10.205
1.00
57.17
N


ATOM
2267
CA
SER
C
48
33.545
−2.155
9.151
1.00
57.02
C


ATOM
2268
CB
SER
C
48
33.367
−3.095
7.949
1.00
57.30
C


ATOM
2269
OG
SER
C
48
33.469
−2.341
6.749
1.00
59.39
O


ATOM
2270
C
SER
C
48
32.203
−1.664
9.682
1.00
55.73
C


ATOM
2271
O
SER
C
48
31.564
−2.325
10.497
1.00
55.50
O


ATOM
2272
N
ILE
C
49
31.823
−0.460
9.257
1.00
55.13
N


ATOM
2273
CA
ILE
C
49
30.555
0.176
9.651
1.00
54.08
C


ATOM
2274
CB
ILE
C
49
30.701
1.702
9.867
1.00
53.11
C


ATOM
2275
CG1
ILE
C
49
31.364
2.013
11.191
1.00
54.19
C


ATOM
2276
CD1
ILE
C
49
31.747
3.486
11.251
1.00
50.86
C


ATOM
2277
CG2
ILE
C
49
29.335
2.437
9.866
1.00
53.88
C


ATOM
2278
C
ILE
C
49
29.495
−0.094
8.577
1.00
53.70
C


ATOM
2279
O
ILE
C
49
29.695
0.176
7.389
1.00
54.09
O


ATOM
2280
N
SER
C
50
28.372
−0.637
9.027
1.00
53.80
N


ATOM
2281
CA
SER
C
50
27.170
−0.832
8.215
1.00
53.15
C


ATOM
2282
CB
SER
C
50
26.378
−2.049
8.731
1.00
53.47
C


ATOM
2283
OG
SER
C
50
27.216
−3.191
8.674
1.00
55.46
O


ATOM
2284
C
SER
C
50
26.299
0.421
8.248
1.00
51.25
C


ATOM
2285
O
SER
C
50
25.876
0.861
9.314
1.00
50.95
O


ATOM
2286
N
ILE
C
51
26.055
0.964
7.058
1.00
49.62
N


ATOM
2287
CA
ILE
C
51
25.252
2.177
6.854
1.00
47.96
C


ATOM
2288
CB
ILE
C
51
25.704
2.918
5.527
1.00
47.87
C


ATOM
2289
CG1
ILE
C
51
27.198
3.362
5.611
1.00
47.14
C


ATOM
2290
CD1
ILE
C
51
27.596
4.066
6.953
1.00
42.36
C


ATOM
2291
CG2
ILE
C
51
24.764
4.088
5.185
1.00
47.30
C


ATOM
2292
C
ILE
C
51
23.750
1.837
6.844
1.00
46.21
C


ATOM
2293
O
ILE
C
51
23.318
0.974
6.084
1.00
47.08
O


ATOM
2294
N
GLY
C
52
22.958
2.488
7.697
1.00
44.14
N


ATOM
2295
CA
GLY
C
52
21.505
2.239
7.784
1.00
41.65
C


ATOM
2296
C
GLY
C
52
21.099
2.653
9.184
1.00
40.74
C


ATOM
2297
O
GLY
C
52
21.943
2.713
10.069
1.00
40.48
O


ATOM
2298
N
GLY
C
53
19.822
2.961
9.391
1.00
38.99
N


ATOM
2299
CA
GLY
C
53
19.345
3.387
10.677
1.00
37.19
C


ATOM
2300
C
GLY
C
53
19.888
4.738
11.055
1.00
37.85
C


ATOM
2301
O
GLY
C
53
19.829
5.692
10.269
1.00
37.66
O


ATOM
2302
N
ARG
C
54
20.424
4.812
12.277
1.00
38.16
N


ATOM
2303
CA
ARG
C
54
21.107
5.990
12.806
1.00
36.67
C


ATOM
2304
CB
ARG
C
54
21.487
5.783
14.286
1.00
37.09
C


ATOM
2305
CG
ARG
C
54
20.294
5.610
15.167
1.00
36.01
C


ATOM
2306
CD
ARG
C
54
20.611
5.607
16.667
1.00
37.36
C


ATOM
2307
NE
ARG
C
54
21.596
4.563
16.963
1.00
39.11
N


ATOM
2308
CZ
ARG
C
54
22.885
4.774
17.227
1.00
39.90
C


ATOM
2309
NH1
ARG
C
54
23.418
6.002
17.263
1.00
35.96
N


ATOM
2310
NH2
ARG
C
54
23.645
3.734
17.490
1.00
38.73
N


ATOM
2311
C
ARG
C
54
22.310
6.430
12.016
1.00
37.64
C


ATOM
2312
O
ARG
C
54
22.696
7.611
12.105
1.00
38.33
O


ATOM
2313
N
TYR
C
55
22.927
5.527
11.242
1.00
38.47
N


ATOM
2314
CA
TYR
C
55
24.111
5.852
10.435
1.00
38.95
C


ATOM
2315
CB
TYR
C
55
25.104
4.647
10.444
1.00
41.10
C


ATOM
2316
CG
TYR
C
55
25.676
4.328
11.842
1.00
43.73
C


ATOM
2317
CD1
TYR
C
55
24.897
3.737
12.850
1.00
45.50
C


ATOM
2318
CE1
TYR
C
55
25.432
3.473
14.108
1.00
47.29
C


ATOM
2319
CZ
TYR
C
55
26.778
3.788
14.349
1.00
47.61
C


ATOM
2320
OH
TYR
C
55
27.392
3.558
15.581
1.00
49.34
O


ATOM
2321
CE2
TYR
C
55
27.541
4.359
13.367
1.00
44.66
C


ATOM
2322
CD2
TYR
C
55
27.001
4.622
12.141
1.00
44.65
C


ATOM
2323
C
TYR
C
55
23.703
6.228
8.973
1.00
38.22
C


ATOM
2324
O
TYR
C
55
23.137
5.426
8.270
1.00
38.89
O


ATOM
2325
N
VAL
C
56
24.009
7.436
8.522
1.00
37.84
N


ATOM
2326
CA
VAL
C
56
23.618
7.965
7.202
1.00
37.02
C


ATOM
2327
CB
VAL
C
56
22.603
9.173
7.358
1.00
37.86
C


ATOM
2328
CG1
VAL
C
56
22.116
9.728
5.981
1.00
36.06
C


ATOM
2329
CG2
VAL
C
56
21.430
8.757
8.169
1.00
36.23
C


ATOM
2330
C
VAL
C
56
24.901
8.476
6.531
1.00
38.69
C


ATOM
2331
O
VAL
C
56
25.605
9.334
7.094
1.00
37.27
O


ATOM
2332
N
GLU
C
57
25.230
7.898
5.369
1.00
39.95
N


ATOM
2333
CA
GLU
C
57
26.318
8.383
4.518
1.00
41.91
C


ATOM
2334
CB
GLU
C
57
27.001
7.223
3.793
1.00
42.73
C


ATOM
2335
CG
GLU
C
57
28.243
7.712
3.058
1.00
44.86
C


ATOM
2336
CD
GLU
C
57
29.213
6.641
2.626
1.00
46.27
C


ATOM
2337
OE1
GLU
C
57
30.406
6.928
2.665
1.00
51.32
O


ATOM
2338
OE2
GLU
C
57
28.819
5.529
2.281
1.00
45.88
O


ATOM
2339
C
GLU
C
57
25.772
9.321
3.461
1.00
42.24
C


ATOM
2340
O
GLU
C
57
24.679
9.095
2.933
1.00
42.46
O


ATOM
2341
N
THR
C
58
26.505
10.370
3.128
1.00
42.56
N


ATOM
2342
CA
THR
C
58
26.114
11.189
1.984
1.00
44.27
C


ATOM
2343
CB
THR
C
58
25.754
12.622
2.431
1.00
45.63
C


ATOM
2344
OG1
THR
C
58
24.690
12.556
3.388
1.00
44.93
O


ATOM
2345
CG2
THR
C
58
25.232
13.504
1.208
1.00
46.97
C


ATOM
2346
C
THR
C
58
27.348
11.189
1.130
1.00
44.50
C


ATOM
2347
O
THR
C
58
28.413
11.350
1.666
1.00
43.33
O


ATOM
2348
N
VAL
C
59
27.230
10.942
−0.176
1.00
45.04
N


ATOM
2349
CA
VAL
C
59
28.406
10.977
−1.063
1.00
45.53
C


ATOM
2350
CB
VAL
C
59
28.708
9.588
−1.708
1.00
46.05
C


ATOM
2351
CG1
VAL
C
59
29.915
9.649
−2.706
1.00
47.53
C


ATOM
2352
CG2
VAL
C
59
29.006
8.579
−0.643
1.00
45.51
C


ATOM
2353
C
VAL
C
59
28.206
12.053
−2.134
1.00
45.35
C


ATOM
2354
O
VAL
C
59
27.147
12.120
−2.743
1.00
44.02
O


ATOM
2355
N
ASN
C
60
29.203
12.919
−2.317
1.00
44.36
N


ATOM
2356
CA
ASN
C
60
29.194
13.869
−3.435
1.00
44.75
C


ATOM
2357
CB
ASN
C
60
29.177
15.316
−2.912
1.00
45.64
C


ATOM
2358
CG
ASN
C
60
28.884
16.325
−4.015
1.00
47.39
C


ATOM
2359
OD1
ASN
C
60
29.294
16.141
−5.154
1.00
49.89
O


ATOM
2360
ND2
ASN
C
60
28.148
17.385
−3.681
1.00
49.11
N


ATOM
2361
C
ASN
C
60
30.404
13.658
−4.329
1.00
44.46
C


ATOM
2362
O
ASN
C
60
31.482
14.175
−4.051
1.00
44.94
O


ATOM
2363
N
LYS
C
61
30.277
12.837
−5.357
1.00
43.78
N


ATOM
2364
CA
LYS
C
61
31.416
12.530
−6.207
1.00
43.85
C


ATOM
2365
CB
LYS
C
61
31.024
11.439
−7.200
1.00
45.23
C


ATOM
2366
CG
LYS
C
61
30.890
10.014
−6.579
1.00
46.82
C


ATOM
2367
CD
LYS
C
61
30.106
9.171
−7.582
1.00
50.75
C


ATOM
2368
CE
LYS
C
61
29.705
7.801
−7.064
1.00
54.46
C


ATOM
2369
NZ
LYS
C
61
30.794
6.802
−7.151
1.00
54.88
N


ATOM
2370
C
LYS
C
61
31.910
13.801
−6.932
1.00
43.81
C


ATOM
2371
O
LYS
C
61
33.080
13.971
−7.175
1.00
42.45
O


ATOM
2372
N
GLY
C
62
31.000
14.714
−7.249
1.00
44.61
N


ATOM
2373
CA
GLY
C
62
31.383
15.991
−7.859
1.00
45.46
C


ATOM
2374
C
GLY
C
62
32.487
16.728
−7.119
1.00
45.37
C


ATOM
2375
O
GLY
C
62
33.376
17.295
−7.727
1.00
45.73
O


ATOM
2376
N
SER
C
63
32.450
16.704
−5.792
1.00
45.46
N


ATOM
2377
CA
SER
C
63
33.420
17.441
−5.008
1.00
44.70
C


ATOM
2378
CB
SER
C
63
32.688
18.416
−4.091
1.00
45.19
C


ATOM
2379
OG
SER
C
63
31.893
17.677
−3.181
1.00
47.62
O


ATOM
2380
C
SER
C
63
34.264
16.451
−4.232
1.00
44.60
C


ATOM
2381
O
SER
C
63
34.979
16.823
−3.314
1.00
45.58
O


ATOM
2382
N
LYS
C
64
34.200
15.185
−4.631
1.00
43.31
N


ATOM
2383
CA
LYS
C
64
34.998
14.106
−4.028
1.00
42.72
C


ATOM
2384
CB
LYS
C
64
36.477
14.180
−4.442
1.00
43.43
C


ATOM
2385
CG
LYS
C
64
36.775
14.385
−5.937
1.00
42.33
C


ATOM
2386
CD
LYS
C
64
38.280
14.079
−6.230
1.00
41.50
C


ATOM
2387
CE
LYS
C
64
38.590
14.577
−7.695
1.00
39.78
C


ATOM
2388
NZ
LYS
C
64
39.915
14.109
−8.180
1.00
42.69
N


ATOM
2389
C
LYS
C
64
34.886
14.092
−2.496
1.00
43.21
C


ATOM
2390
O
LYS
C
64
35.878
13.779
−1.795
1.00
42.92
O


ATOM
2391
N
SER
C
65
33.699
14.441
−1.992
1.00
41.43
N


ATOM
2392
CA
SER
C
65
33.469
14.458
−0.580
1.00
42.62
C


ATOM
2393
CB
SER
C
65
33.231
15.866
−0.083
1.00
43.83
C


ATOM
2394
OG
SER
C
65
32.354
16.529
−0.959
1.00
45.50
O


ATOM
2395
C
SER
C
65
32.347
13.565
−0.135
1.00
42.45
C


ATOM
2396
O
SER
C
65
31.421
13.224
−0.874
1.00
40.59
O


ATOM
2397
N
PHE
C
66
32.466
13.139
1.103
1.00
42.45
N


ATOM
2398
CA
PHE
C
66
31.473
12.198
1.636
1.00
43.16
C


ATOM
2399
CB
PHE
C
66
31.730
10.756
1.181
1.00
42.27
C


ATOM
2400
CG
PHE
C
66
33.099
10.222
1.510
1.00
44.09
C


ATOM
2401
CD1
PHE
C
66
34.242
10.716
0.857
1.00
42.19
C


ATOM
2402
CE1
PHE
C
66
35.517
10.219
1.123
1.00
44.28
C


ATOM
2403
CZ
PHE
C
66
35.670
9.175
2.052
1.00
45.40
C


ATOM
2404
CE2
PHE
C
66
34.513
8.620
2.721
1.00
43.80
C


ATOM
2405
CD2
PHE
C
66
33.244
9.152
2.449
1.00
46.12
C


ATOM
2406
C
PHE
C
66
31.421
12.354
3.123
1.00
43.16
C


ATOM
2407
O
PHE
C
66
32.351
12.914
3.730
1.00
43.47
O


ATOM
2408
N
SER
C
67
30.295
12.004
3.716
1.00
43.08
N


ATOM
2409
CA
SER
C
67
30.192
12.283
5.145
1.00
43.78
C


ATOM
2410
CB
SER
C
67
29.498
13.599
5.348
1.00
42.88
C


ATOM
2411
OG
SER
C
67
28.148
13.307
5.122
1.00
50.83
O


ATOM
2412
C
SER
C
67
29.420
11.172
5.783
1.00
42.30
C


ATOM
2413
O
SER
C
67
28.653
10.502
5.119
1.00
42.27
O


ATOM
2414
N
LEU
C
68
29.704
10.935
7.050
1.00
40.76
N


ATOM
2415
CA
LEU
C
68
28.938
10.035
7.877
1.00
39.22
C


ATOM
2416
CB
LEU
C
68
29.870
9.117
8.675
1.00
39.26
C


ATOM
2417
CG
LEU
C
68
29.519
7.673
9.067
1.00
39.79
C


ATOM
2418
CD1
LEU
C
68
30.187
7.273
10.332
1.00
36.92
C


ATOM
2419
CD2
LEU
C
68
28.064
7.184
8.998
1.00
41.23
C


ATOM
2420
C
LEU
C
68
28.281
10.919
8.932
1.00
38.92
C


ATOM
2421
O
LEU
C
68
28.962
11.636
9.668
1.00
36.62
O


ATOM
2422
N
ARG
C
69
26.988
10.734
9.088
1.00
38.05
N


ATOM
2423
CA
ARG
C
69
26.216
11.297
10.182
1.00
38.81
C


ATOM
2424
CB
ARG
C
69
24.957
12.018
9.603
1.00
37.83
C


ATOM
2425
CG
ARG
C
69
24.394
12.996
10.666
1.00
42.79
C


ATOM
2426
CD
ARG
C
69
23.175
13.730
10.200
1.00
53.15
C


ATOM
2427
NE
ARG
C
69
23.050
14.889
11.076
1.00
60.64
N


ATOM
2428
CZ
ARG
C
69
22.234
14.973
12.136
1.00
64.79
C


ATOM
2429
NH1
ARG
C
69
21.415
13.954
12.452
1.00
64.71
N


ATOM
2430
NH2
ARG
C
69
22.227
16.089
12.882
1.00
64.93
N


ATOM
2431
C
ARG
C
69
25.714
10.174
11.063
1.00
38.49
C


ATOM
2432
O
ARG
C
69
25.016
9.296
10.576
1.00
38.05
O


ATOM
2433
N
ILE
C
70
26.036
10.204
12.355
1.00
38.71
N


ATOM
2434
CA
ILE
C
70
25.420
9.290
13.321
1.00
38.97
C


ATOM
2435
CB
ILE
C
70
26.478
8.582
14.218
1.00
39.33
C


ATOM
2436
CG1
ILE
C
70
27.623
8.001
13.370
1.00
41.07
C


ATOM
2437
CD1
ILE
C
70
28.826
7.749
14.203
1.00
42.56
C


ATOM
2438
CG2
ILE
C
70
25.853
7.519
15.050
1.00
36.50
C


ATOM
2439
C
ILE
C
70
24.425
10.106
14.188
1.00
38.51
C


ATOM
2440
O
ILE
C
70
24.863
10.970
14.928
1.00
38.32
O


ATOM
2441
N
SER
C
71
23.124
9.833
14.069
1.00
36.88
N


ATOM
2442
CA
SER
C
71
22.084
10.437
14.955
1.00
38.63
C


ATOM
2443
CB
SER
C
71
20.691
10.355
14.353
1.00
36.29
C


ATOM
2444
OG
SER
C
71
20.721
10.830
13.058
1.00
42.47
O


ATOM
2445
C
SER
C
71
21.938
9.783
16.308
1.00
37.24
C


ATOM
2446
O
SER
C
71
22.280
8.640
16.509
1.00
39.57
O


ATOM
2447
N
ASP
C
72
21.394
10.530
17.218
1.00
37.94
N


ATOM
2448
CA
ASP
C
72
21.064
10.056
18.525
1.00
38.88
C


ATOM
2449
CB
ASP
C
72
19.761
9.261
18.465
1.00
38.48
C


ATOM
2450
CG
ASP
C
72
19.127
9.150
19.805
1.00
40.88
C


ATOM
2451
OD1
ASP
C
72
19.397
10.036
20.649
1.00
41.95
O


ATOM
2452
OD2
ASP
C
72
18.355
8.204
20.029
1.00
46.35
O


ATOM
2453
C
ASP
C
72
22.192
9.248
19.194
1.00
39.02
C


ATOM
2454
O
ASP
C
72
21.996
8.088
19.548
1.00
40.28
O


ATOM
2455
N
LEU
C
73
23.354
9.857
19.369
1.00
38.81
N


ATOM
2456
CA
LEU
C
73
24.525
9.137
19.900
1.00
39.26
C


ATOM
2457
CB
LEU
C
73
25.754
10.076
20.004
1.00
38.40
C


ATOM
2458
CG
LEU
C
73
26.271
10.505
18.635
1.00
37.52
C


ATOM
2459
CD1
LEU
C
73
27.086
11.766
18.820
1.00
36.13
C


ATOM
2460
CD2
LEU
C
73
27.118
9.367
18.077
1.00
35.66
C


ATOM
2461
C
LEU
C
73
24.290
8.464
21.258
1.00
38.78
C


ATOM
2462
O
LEU
C
73
23.600
9.018
22.132
1.00
38.58
O


ATOM
2463
N
ARG
C
74
24.851
7.275
21.430
1.00
38.74
N


ATOM
2464
CA
ARG
C
74
24.881
6.575
22.744
1.00
40.73
C


ATOM
2465
CB
ARG
C
74
24.123
5.247
22.684
1.00
40.63
C


ATOM
2466
CG
ARG
C
74
23.674
4.750
21.330
1.00
44.45
C


ATOM
2467
CD
ARG
C
74
22.291
5.411
21.028
1.00
52.00
C


ATOM
2468
NE
ARG
C
74
21.296
4.424
20.582
1.00
57.73
N


ATOM
2469
CZ
ARG
C
74
20.034
4.701
20.272
1.00
54.39
C


ATOM
2470
NH1
ARG
C
74
19.236
3.719
19.917
1.00
55.75
N


ATOM
2471
NH2
ARG
C
74
19.588
5.942
20.292
1.00
49.28
N


ATOM
2472
C
ARG
C
74
26.351
6.305
23.159
1.00
41.08
C


ATOM
2473
O
ARG
C
74
27.223
6.297
22.283
1.00
39.54
O


ATOM
2474
N
VAL
C
75
26.629
6.061
24.453
1.00
41.83
N


ATOM
2475
CA
VAL
C
75
28.019
5.793
24.874
1.00
42.82
C


ATOM
2476
CB
VAL
C
75
28.167
5.434
26.383
1.00
42.84
C


ATOM
2477
CG1
VAL
C
75
27.517
6.484
27.263
1.00
42.05
C


ATOM
2478
CG2
VAL
C
75
27.552
4.094
26.683
1.00
44.76
C


ATOM
2479
C
VAL
C
75
28.658
4.705
24.017
1.00
43.85
C


ATOM
2480
O
VAL
C
75
29.833
4.797
23.665
1.00
44.32
O


ATOM
2481
N
GLU
C
76
27.888
3.668
23.662
1.00
44.43
N


ATOM
2482
CA
GLU
C
76
28.437
2.562
22.865
1.00
45.15
C


ATOM
2483
CB
GLU
C
76
27.474
1.346
22.799
1.00
46.21
C


ATOM
2484
CG
GLU
C
76
25.983
1.699
22.474
1.00
51.67
C


ATOM
2485
CD
GLU
C
76
25.070
1.966
23.696
1.00
56.22
C


ATOM
2486
OE1
GLU
C
76
23.911
1.494
23.654
1.00
60.97
O


ATOM
2487
OE2
GLU
C
76
25.456
2.651
24.684
1.00
58.26
O


ATOM
2488
C
GLU
C
76
28.927
3.022
21.474
1.00
44.53
C


ATOM
2489
O
GLU
C
76
29.708
2.291
20.812
1.00
43.93
O


ATOM
2490
N
ASP
C
77
28.535
4.236
21.040
1.00
42.84
N


ATOM
2491
CA
ASP
C
77
29.055
4.766
19.743
1.00
41.95
C


ATOM
2492
CB
ASP
C
77
28.118
5.832
19.168
1.00
42.62
C


ATOM
2493
CG
ASP
C
77
26.752
5.282
18.781
1.00
45.69
C


ATOM
2494
OD1
ASP
C
77
26.657
4.110
18.318
1.00
43.73
O


ATOM
2495
OD2
ASP
C
77
25.773
6.049
18.913
1.00
44.99
O


ATOM
2496
C
ASP
C
77
30.508
5.313
19.846
1.00
40.76
C


ATOM
2497
O
ASP
C
77
31.127
5.640
18.846
1.00
40.30
O


ATOM
2498
N
SER
C
78
31.024
5.464
21.061
1.00
40.14
N


ATOM
2499
CA
SER
C
78
32.383
5.978
21.240
1.00
40.43
C


ATOM
2500
CB
SER
C
78
32.751
6.039
22.716
1.00
38.77
C


ATOM
2501
OG
SER
C
78
31.800
6.795
23.385
1.00
40.31
O


ATOM
2502
C
SER
C
78
33.411
5.118
20.519
1.00
40.44
C


ATOM
2503
O
SER
C
78
33.259
3.898
20.413
1.00
41.58
O


ATOM
2504
N
GLY
C
79
34.456
5.763
20.014
1.00
39.91
N


ATOM
2505
CA
GLY
C
79
35.569
5.065
19.403
1.00
39.20
C


ATOM
2506
C
GLY
C
79
36.243
5.931
18.378
1.00
39.12
C


ATOM
2507
O
GLY
C
79
35.911
7.103
18.272
1.00
38.52
O


ATOM
2508
N
THR
C
80
37.125
5.335
17.584
1.00
39.32
N


ATOM
2509
CA
THR
C
80
37.814
6.062
16.539
1.00
40.74
C


ATOM
2510
CB
THR
C
80
39.345
5.858
16.627
1.00
40.22
C


ATOM
2511
OG1
THR
C
80
39.806
6.345
17.896
1.00
41.93
O


ATOM
2512
CG2
THR
C
80
40.088
6.585
15.475
1.00
39.67
C


ATOM
2513
C
THR
C
80
37.331
5.592
15.192
1.00
41.67
C


ATOM
2514
O
THR
C
80
37.464
4.406
14.867
1.00
42.93
O


ATOM
2515
N
TYR
C
81
36.797
6.532
14.413
1.00
41.16
N


ATOM
2516
CA
TYR
C
81
36.235
6.302
13.098
1.00
41.38
C


ATOM
2517
CB
TYR
C
81
34.934
7.118
12.928
1.00
41.71
C


ATOM
2518
CG
TYR
C
81
33.832
6.627
13.831
1.00
41.50
C


ATOM
2519
CD1
TYR
C
81
32.840
5.753
13.343
1.00
42.16
C


ATOM
2520
CE1
TYR
C
81
31.777
5.275
14.208
1.00
37.37
C


ATOM
2521
CZ
TYR
C
81
31.752
5.716
15.516
1.00
42.71
C


ATOM
2522
OH
TYR
C
81
30.763
5.238
16.353
1.00
44.53
O


ATOM
2523
CE2
TYR
C
81
32.747
6.575
16.023
1.00
41.06
C


ATOM
2524
CD2
TYR
C
81
33.763
7.031
15.181
1.00
40.89
C


ATOM
2525
C
TYR
C
81
37.221
6.760
12.031
1.00
41.95
C


ATOM
2526
O
TYR
C
81
37.878
7.771
12.247
1.00
42.20
O


ATOM
2527
N
LYS
C
82
37.373
5.968
10.947
1.00
41.37
N


ATOM
2528
CA
LYS
C
82
38.121
6.382
9.764
1.00
42.18
C


ATOM
2529
CB
LYS
C
82
39.448
5.632
9.579
1.00
41.37
C


ATOM
2530
CG
LYS
C
82
40.368
5.886
10.712
1.00
46.60
C


ATOM
2531
CD
LYS
C
82
41.821
5.742
10.339
1.00
52.93
C


ATOM
2532
CE
LYS
C
82
42.613
5.556
11.625
1.00
55.71
C


ATOM
2533
NZ
LYS
C
82
44.075
5.483
11.354
1.00
61.02
N


ATOM
2534
C
LYS
C
82
37.281
6.164
8.540
1.00
41.18
C


ATOM
2535
O
LYS
C
82
36.568
5.188
8.473
1.00
40.69
O


ATOM
2536
N
CYS
C
83
37.420
7.065
7.587
1.00
40.93
N


ATOM
2537
CA
CYS
C
83
36.864
6.904
6.294
1.00
44.17
C


ATOM
2538
CB
CYS
C
83
36.274
8.199
5.799
1.00
43.61
C


ATOM
2539
SG
CYS
C
83
37.465
9.490
5.676
1.00
48.89
S


ATOM
2540
C
CYS
C
83
37.964
6.491
5.319
1.00
45.48
C


ATOM
2541
O
CYS
C
83
39.145
6.776
5.525
1.00
46.68
O


ATOM
2542
N
GLN
C
84
37.567
5.801
4.258
1.00
45.72
N


ATOM
2543
CA
GLN
C
84
38.485
5.529
3.193
1.00
44.76
C


ATOM
2544
CB
GLN
C
84
38.975
4.074
3.282
1.00
44.52
C


ATOM
2545
CG
GLN
C
84
39.885
3.726
2.122
1.00
45.70
C


ATOM
2546
CD
GLN
C
84
40.912
2.652
2.388
1.00
49.09
C


ATOM
2547
OE1
GLN
C
84
42.083
2.752
1.918
1.00
52.22
O


ATOM
2548
NE2
GLN
C
84
40.512
1.628
3.106
1.00
43.81
N


ATOM
2549
C
GLN
C
84
37.809
5.818
1.886
1.00
44.70
C


ATOM
2550
O
GLN
C
84
36.677
5.362
1.628
1.00
45.18
O


ATOM
2551
N
ALA
C
85
38.503
6.588
1.058
1.00
44.54
N


ATOM
2552
CA
ALA
C
85
38.073
6.857
−0.324
1.00
43.12
C


ATOM
2553
CB
ALA
C
85
38.450
8.228
−0.717
1.00
41.23
C


ATOM
2554
C
ALA
C
85
38.750
5.826
−1.261
1.00
43.54
C


ATOM
2555
O
ALA
C
85
40.001
5.667
−1.262
1.00
42.69
O


ATOM
2556
N
PHE
C
86
37.919
5.123
−2.014
1.00
42.31
N


ATOM
2557
CA
PHE
C
86
38.354
4.226
−3.079
1.00
42.97
C


ATOM
2558
CB
PHE
C
86
37.549
2.932
−3.061
1.00
43.29
C


ATOM
2559
CG
PHE
C
86
37.713
2.185
−1.762
1.00
45.80
C


ATOM
2560
CD1
PHE
C
86
36.695
2.201
−0.782
1.00
42.22
C


ATOM
2561
CE1
PHE
C
86
36.905
1.563
0.421
1.00
42.36
C


ATOM
2562
CZ
PHE
C
86
38.101
0.899
0.668
1.00
42.36
C


ATOM
2563
CE2
PHE
C
86
39.105
0.869
−0.301
1.00
42.11
C


ATOM
2564
CD2
PHE
C
86
38.913
1.529
−1.489
1.00
43.32
C


ATOM
2565
C
PHE
C
86
38.206
4.860
−4.425
1.00
42.06
C


ATOM
2566
O
PHE
C
86
37.274
5.618
−4.692
1.00
41.81
O


ATOM
2567
N
TYR
C
87
39.169
4.558
−5.277
1.00
42.72
N


ATOM
2568
CA
TYR
C
87
39.184
5.052
−6.646
1.00
42.08
C


ATOM
2569
CB
TYR
C
87
39.938
6.398
−6.719
1.00
43.64
C


ATOM
2570
CG
TYR
C
87
41.182
6.458
−5.859
1.00
44.34
C


ATOM
2571
CD1
TYR
C
87
41.161
7.043
−4.589
1.00
46.58
C


ATOM
2572
CE1
TYR
C
87
42.332
7.098
−3.787
1.00
46.11
C


ATOM
2573
CZ
TYR
C
87
43.502
6.541
−4.268
1.00
47.59
C


ATOM
2574
OH
TYR
C
87
44.668
6.553
−3.504
1.00
48.00
O


ATOM
2575
CE2
TYR
C
87
43.538
5.961
−5.531
1.00
47.66
C


ATOM
2576
CD2
TYR
C
87
42.385
5.926
−6.320
1.00
48.34
C


ATOM
2577
C
TYR
C
87
39.850
3.971
−7.494
1.00
41.63
C


ATOM
2578
O
TYR
C
87
40.505
3.080
−6.962
1.00
40.18
O


ATOM
2579
N
VAL
C
88
39.649
4.060
−8.807
1.00
40.58
N


ATOM
2580
CA
VAL
C
88
40.190
3.116
−9.791
1.00
38.74
C


ATOM
2581
CB
VAL
C
88
39.090
2.177
−10.417
1.00
38.40
C


ATOM
2582
CG1
VAL
C
88
38.522
1.217
−9.367
1.00
35.07
C


ATOM
2583
CG2
VAL
C
88
37.906
2.991
−11.012
1.00
37.81
C


ATOM
2584
C
VAL
C
88
40.912
3.876
−10.888
1.00
38.92
C


ATOM
2585
O
VAL
C
88
40.597
5.063
−11.145
1.00
38.50
O


ATOM
2586
N
PHE
C
89
41.883
3.200
−11.534
1.00
37.31
N


ATOM
2587
CA
PHE
C
89
42.656
3.790
−12.610
1.00
36.15
C


ATOM
2588
CB
PHE
C
89
43.787
4.711
−12.062
1.00
36.75
C


ATOM
2589
CG
PHE
C
89
44.555
4.132
−10.846
1.00
36.77
C


ATOM
2590
CD1
PHE
C
89
44.066
4.284
−9.550
1.00
38.64
C


ATOM
2591
CE1
PHE
C
89
44.743
3.751
−8.429
1.00
36.48
C


ATOM
2592
CZ
PHE
C
89
45.932
3.067
−8.631
1.00
39.07
C


ATOM
2593
CE2
PHE
C
89
46.401
2.894
−9.914
1.00
37.47
C


ATOM
2594
CD2
PHE
C
89
45.720
3.431
−11.009
1.00
35.24
C


ATOM
2595
C
PHE
C
89
43.291
2.637
−13.345
1.00
37.04
C


ATOM
2596
O
PHE
C
89
43.464
1.544
−12.808
1.00
34.79
O


ATOM
2597
N
PHE
C
90
43.645
2.885
−14.591
1.00
36.52
N


ATOM
2598
CA
PHE
C
90
44.378
1.903
−15.331
1.00
37.25
C


ATOM
2599
CB
PHE
C
90
44.357
2.209
−16.812
1.00
36.55
C


ATOM
2600
CG
PHE
C
90
43.017
1.968
−17.458
1.00
35.98
C


ATOM
2601
CD1
PHE
C
90
42.555
0.662
−17.653
1.00
37.27
C


ATOM
2602
CE1
PHE
C
90
41.365
0.403
−18.313
1.00
35.06
C


ATOM
2603
CZ
PHE
C
90
40.588
1.508
−18.772
1.00
40.72
C


ATOM
2604
CE2
PHE
C
90
41.050
2.842
−18.572
1.00
35.96
C


ATOM
2605
CD2
PHE
C
90
42.266
3.045
−17.941
1.00
30.26
C


ATOM
2606
C
PHE
C
90
45.793
1.765
−14.824
1.00
38.44
C


ATOM
2607
O
PHE
C
90
46.373
2.754
−14.304
1.00
37.09
O


ATOM
2608
N
ALA
C
91
46.305
0.523
−14.949
1.00
38.72
N


ATOM
2609
CA
ALA
C
91
47.654
0.146
−14.505
1.00
40.42
C


ATOM
2610
CB
ALA
C
91
47.942
−1.248
−14.918
1.00
39.03
C


ATOM
2611
C
ALA
C
91
48.790
1.067
−14.986
1.00
41.68
C


ATOM
2612
O
ALA
C
91
49.730
1.312
−14.221
1.00
42.62
O


ATOM
2613
N
GLU
C
92
48.683
1.578
−16.211
1.00
42.40
N


ATOM
2614
CA
GLU
C
92
49.667
2.488
−16.825
1.00
45.96
C


ATOM
2615
CB
GLU
C
92
49.609
2.365
−18.350
1.00
46.83
C


ATOM
2616
CG
GLU
C
92
49.960
0.958
−18.882
1.00
54.78
C


ATOM
2617
CD
GLU
C
92
51.461
0.705
−19.228
1.00
65.73
C


ATOM
2618
OE1
GLU
C
92
51.753
0.838
−20.455
1.00
68.70
O


ATOM
2619
OE2
GLU
C
92
52.324
0.333
−18.328
1.00
67.00
O


ATOM
2620
C
GLU
C
92
49.561
3.991
−16.450
1.00
46.75
C


ATOM
2621
O
GLU
C
92
50.310
4.807
−16.965
1.00
47.85
O


ATOM
2622
N
ASP
C
93
48.622
4.360
−15.586
1.00
46.84
N


ATOM
2623
CA
ASP
C
93
48.578
5.692
−14.997
1.00
47.98
C


ATOM
2624
CB
ASP
C
93
47.402
5.780
−14.024
1.00
48.91
C


ATOM
2625
CG
ASP
C
93
47.048
7.201
−13.702
1.00
53.37
C


ATOM
2626
OD1
ASP
C
93
47.669
7.763
−12.756
1.00
59.02
O


ATOM
2627
OD2
ASP
C
93
46.171
7.745
−14.411
1.00
52.66
O


ATOM
2628
C
ASP
C
93
49.855
5.869
−14.185
1.00
46.99
C


ATOM
2629
O
ASP
C
93
50.113
5.046
−13.293
1.00
48.62
O


ATOM
2630
N
VAL
C
94
50.638
6.908
−14.499
1.00
43.77
N


ATOM
2631
CA
VAL
C
94
51.934
7.192
−13.906
1.00
40.69
C


ATOM
2632
CB
VAL
C
94
53.120
6.915
−14.893
1.00
40.79
C


ATOM
2633
CG1
VAL
C
94
52.921
7.686
−16.247
1.00
38.04
C


ATOM
2634
CG2
VAL
C
94
53.260
5.446
−15.184
1.00
38.24
C


ATOM
2635
C
VAL
C
94
51.966
8.674
−13.471
1.00
40.53
C


ATOM
2636
O
VAL
C
94
51.209
9.479
−13.973
1.00
39.56
O


ATOM
2637
N
GLY
C
95
52.867
9.022
−12.553
1.00
40.49
N


ATOM
2638
CA
GLY
C
95
53.050
10.415
−12.093
1.00
38.78
C


ATOM
2639
C
GLY
C
95
52.272
10.847
−10.852
1.00
38.81
C


ATOM
2640
O
GLY
C
95
52.535
11.890
−10.335
1.00
40.05
O


ATOM
2641
N
SER
C
96
51.312
10.069
−10.362
1.00
37.58
N


ATOM
2642
CA
SER
C
96
50.546
10.497
−9.227
1.00
39.65
C


ATOM
2643
CB
SER
C
96
49.053
10.780
−9.608
1.00
39.56
C


ATOM
2644
OG
SER
C
96
49.035
11.894
−10.504
1.00
43.48
O


ATOM
2645
C
SER
C
96
50.567
9.465
−8.136
1.00
39.35
C


ATOM
2646
O
SER
C
96
50.517
8.279
−8.401
1.00
39.38
O


ATOM
2647
N
ASN
C
97
50.640
9.963
−6.915
1.00
39.49
N


ATOM
2648
CA
ASN
C
97
50.421
9.178
−5.740
1.00
40.25
C


ATOM
2649
CB
ASN
C
97
50.339
10.076
−4.528
1.00
38.65
C


ATOM
2650
CG
ASN
C
97
50.340
9.274
−3.160
1.00
44.04
C


ATOM
2651
OD1
ASN
C
97
50.540
9.865
−2.086
1.00
43.90
O


ATOM
2652
ND2
ASN
C
97
50.135
7.962
−3.221
1.00
43.78
N


ATOM
2653
C
ASN
C
97
49.107
8.442
−5.898
1.00
38.81
C


ATOM
2654
O
ASN
C
97
48.018
9.028
−5.895
1.00
39.38
O


ATOM
2655
N
LYS
C
98
49.235
7.141
−5.999
1.00
38.34
N


ATOM
2656
CA
LYS
C
98
48.109
6.210
−6.077
1.00
37.85
C


ATOM
2657
CB
LYS
C
98
48.641
4.910
−6.704
1.00
37.89
C


ATOM
2658
CG
LYS
C
98
49.077
5.156
−8.197
1.00
34.79
C


ATOM
2659
CD
LYS
C
98
49.488
3.865
−8.838
1.00
40.63
C


ATOM
2660
CE
LYS
C
98
49.867
4.054
−10.316
1.00
40.81
C


ATOM
2661
NZ
LYS
C
98
51.073
4.918
−10.448
1.00
38.45
N


ATOM
2662
C
LYS
C
98
47.375
5.892
−4.755
1.00
39.19
C


ATOM
2663
O
LYS
C
98
46.408
5.154
−4.777
1.00
38.96
O


ATOM
2664
N
GLY
C
99
47.858
6.420
−3.636
1.00
38.59
N


ATOM
2665
CA
GLY
C
99
47.449
5.964
−2.296
1.00
40.76
C


ATOM
2666
C
GLY
C
99
47.880
4.530
−2.081
1.00
41.30
C


ATOM
2667
O
GLY
C
99
48.795
4.036
−2.767
1.00
43.80
O


ATOM
2668
N
ALA
C
100
47.248
3.856
−1.143
1.00
40.11
N


ATOM
2669
CA
ALA
C
100
47.560
2.475
−0.883
1.00
39.38
C


ATOM
2670
CB
ALA
C
100
46.860
2.024
0.434
1.00
39.23
C


ATOM
2671
C
ALA
C
100
46.989
1.713
−2.025
1.00
39.51
C


ATOM
2672
O
ALA
C
100
45.893
2.022
−2.468
1.00
39.92
O


ATOM
2673
N
ILE
C
101
47.710
0.705
−2.490
1.00
39.69
N


ATOM
2674
CA
ILE
C
101
47.214
−0.164
−3.542
1.00
39.24
C


ATOM
2675
CB
ILE
C
101
48.382
−0.869
−4.334
1.00
39.71
C


ATOM
2676
CG1
ILE
C
101
49.331
0.190
−5.017
1.00
39.84
C


ATOM
2677
CD1
ILE
C
101
48.627
1.159
−5.924
1.00
36.72
C


ATOM
2678
CG2
ILE
C
101
47.804
−1.860
−5.378
1.00
35.43
C


ATOM
2679
C
ILE
C
101
46.322
−1.192
−2.832
1.00
40.48
C


ATOM
2680
O
ILE
C
101
46.747
−1.835
−1.875
1.00
39.46
O


ATOM
2681
N
ILE
C
102
45.077
−1.290
−3.277
1.00
41.20
N


ATOM
2682
CA
ILE
C
102
44.077
−2.062
−2.594
1.00
42.13
C


ATOM
2683
CB
ILE
C
102
42.722
−1.275
−2.453
1.00
42.58
C


ATOM
2684
CG1
ILE
C
102
42.912
−0.020
−1.630
1.00
42.57
C


ATOM
2685
CD1
ILE
C
102
43.084
−0.204
−0.096
1.00
41.89
C


ATOM
2686
CG2
ILE
C
102
41.542
−2.148
−1.947
1.00
42.41
C


ATOM
2687
C
ILE
C
102
43.887
−3.331
−3.396
1.00
41.41
C


ATOM
2688
O
ILE
C
102
43.698
−4.376
−2.821
1.00
42.57
O


ATOM
2689
N
GLY
C
103
43.942
−3.261
−4.715
1.00
40.57
N


ATOM
2690
CA
GLY
C
103
43.742
−4.479
−5.498
1.00
38.60
C


ATOM
2691
C
GLY
C
103
44.033
−4.305
−6.974
1.00
37.22
C


ATOM
2692
O
GLY
C
103
44.253
−3.238
−7.441
1.00
37.08
O


ATOM
2693
N
LEU
C
104
44.060
−5.393
−7.704
1.00
38.36
N


ATOM
2694
CA
LEU
C
104
44.255
−5.381
−9.148
1.00
39.71
C


ATOM
2695
CB
LEU
C
104
45.653
−5.917
−9.493
1.00
39.02
C


ATOM
2696
CG
LEU
C
104
46.002
−6.069
−10.973
1.00
40.16
C


ATOM
2697
CD1
LEU
C
104
45.968
−4.664
−11.690
1.00
34.76
C


ATOM
2698
CD2
LEU
C
104
47.334
−6.727
−11.161
1.00
38.01
C


ATOM
2699
C
LEU
C
104
43.142
−6.283
−9.728
1.00
41.24
C


ATOM
2700
O
LEU
C
104
42.985
−7.408
−9.276
1.00
38.88
O


ATOM
2701
N
MET
C
105
42.368
−5.743
−10.678
1.00
43.67
N


ATOM
2702
CA
MET
C
105
41.297
−6.447
−11.366
1.00
47.58
C


ATOM
2703
CB
MET
C
105
40.101
−5.568
−11.687
1.00
47.39
C


ATOM
2704
CG
MET
C
105
39.496
−4.652
−10.666
1.00
50.10
C


ATOM
2705
SD
MET
C
105
37.752
−4.217
−11.239
1.00
57.87
S


ATOM
2706
CE
MET
C
105
37.532
−4.959
−12.846
1.00
54.27
C


ATOM
2707
C
MET
C
105
41.835
−6.794
−12.704
1.00
47.26
C


ATOM
2708
O
MET
C
105
42.684
−6.094
−13.231
1.00
47.11
O


ATOM
2709
N
VAL
C
106
41.329
−7.879
−13.266
1.00
48.20
N


ATOM
2710
CA
VAL
C
106
41.630
−8.250
−14.630
1.00
49.68
C


ATOM
2711
CB
VAL
C
106
41.031
−9.665
−14.914
1.00
50.52
C


ATOM
2712
CG1
VAL
C
106
41.298
−10.144
−16.355
1.00
51.88
C


ATOM
2713
CG2
VAL
C
106
41.664
−10.679
−13.916
1.00
51.57
C


ATOM
2714
C
VAL
C
106
41.214
−7.095
−15.602
1.00
48.70
C


ATOM
2715
O
VAL
C
106
40.269
−6.361
−15.355
1.00
49.46
O


ATOM
2716
N
GLY
C
107
42.012
−6.859
−16.629
1.00
48.36
N


ATOM
2717
CA
GLY
C
107
41.763
−5.713
−17.516
1.00
47.26
C


ATOM
2718
C
GLY
C
107
42.676
−4.536
−17.234
1.00
45.75
C


ATOM
2719
O
GLY
C
107
42.501
−3.459
−17.799
1.00
46.81
O


ATOM
2720
N
GLY
C
108
43.627
−4.736
−16.328
1.00
43.80
N


ATOM
2721
CA
GLY
C
108
44.597
−3.735
−15.974
1.00
42.42
C


ATOM
2722
C
GLY
C
108
44.050
−2.585
−15.171
1.00
41.50
C


ATOM
2723
O
GLY
C
108
44.487
−1.448
−15.371
1.00
43.12
O


ATOM
2724
N
VAL
C
109
43.083
−2.852
−14.304
1.00
39.69
N


ATOM
2725
CA
VAL
C
109
42.387
−1.806
−13.556
1.00
37.50
C


ATOM
2726
CB
VAL
C
109
40.845
−1.962
−13.644
1.00
37.78
C


ATOM
2727
CG1
VAL
C
109
40.292
−1.715
−15.041
1.00
32.98
C


ATOM
2728
CG2
VAL
C
109
40.105
−1.033
−12.610
1.00
35.07
C


ATOM
2729
C
VAL
C
109
42.802
−1.942
−12.103
1.00
38.36
C


ATOM
2730
O
VAL
C
109
42.639
−3.027
−11.512
1.00
36.60
O


ATOM
2731
N
VAL
C
110
43.336
−0.870
−11.513
1.00
37.27
N


ATOM
2732
CA
VAL
C
110
43.845
−0.955
−10.160
1.00
37.80
C


ATOM
2733
CB
VAL
C
110
45.245
−0.371
−10.070
1.00
38.39
C


ATOM
2734
CG1
VAL
C
110
46.115
−1.019
−11.123
1.00
35.91
C


ATOM
2735
CG2
VAL
C
110
45.851
−0.565
−8.672
1.00
34.68
C


ATOM
2736
C
VAL
C
110
42.897
−0.237
−9.248
1.00
39.02
C


ATOM
2737
O
VAL
C
110
42.247
0.697
−9.695
1.00
38.55
O


ATOM
2738
N
ILE
C
111
42.743
−0.718
−8.010
1.00
39.64
N


ATOM
2739
CA
ILE
C
111
41.985
−0.007
−6.976
1.00
40.38
C


ATOM
2740
CB
ILE
C
111
41.039
−0.966
−6.233
1.00
40.84
C


ATOM
2741
CG1
ILE
C
111
40.202
−1.806
−7.257
1.00
43.74
C


ATOM
2742
CD1
ILE
C
111
39.645
−3.116
−6.586
1.00
44.34
C


ATOM
2743
CG2
ILE
C
111
40.111
−0.240
−5.264
1.00
40.12
C


ATOM
2744
C
ILE
C
111
42.995
0.553
−6.005
1.00
40.90
C


ATOM
2745
O
ILE
C
111
43.911
−0.155
−5.522
1.00
40.15
O


ATOM
2746
N
GLY
C
112
42.870
1.839
−5.722
1.00
41.79
N


ATOM
2747
CA
GLY
C
112
43.727
2.465
−4.695
1.00
41.67
C


ATOM
2748
C
GLY
C
112
42.804
3.024
−3.631
1.00
42.53
C


ATOM
2749
O
GLY
C
112
41.599
3.097
−3.837
1.00
42.69
O


ATOM
2750
N
GLY
C
113
43.352
3.378
−2.479
1.00
42.32
N


ATOM
2751
CA
GLY
C
113
42.544
3.983
−1.444
1.00
42.68
C


ATOM
2752
C
GLY
C
113
43.431
4.872
−0.602
1.00
43.14
C


ATOM
2753
O
GLY
C
113
44.645
4.595
−0.482
1.00
42.77
O


ATOM
2754
N
GLU
C
114
42.829
5.961
−0.105
1.00
43.84
N


ATOM
2755
CA
GLU
C
114
43.389
6.874
0.895
1.00
45.57
C


ATOM
2756
CB
GLU
C
114
43.530
8.314
0.328
1.00
46.12
C


ATOM
2757
CG
GLU
C
114
44.677
8.540
−0.659
1.00
48.41
C


ATOM
2758
CD
GLU
C
114
46.012
8.648
0.104
1.00
53.32
C


ATOM
2759
OE1
GLU
C
114
45.961
8.894
1.318
1.00
54.08
O


ATOM
2760
OE2
GLU
C
114
47.105
8.460
−0.484
1.00
53.74
O


ATOM
2761
C
GLU
C
114
42.434
6.922
2.110
1.00
45.53
C


ATOM
2762
O
GLU
C
114
41.258
7.185
1.933
1.00
44.18
O


ATOM
2763
N
LYS
C
115
42.973
6.750
3.330
1.00
45.32
N


ATOM
2764
CA
LYS
C
115
42.202
6.844
4.591
1.00
44.84
C


ATOM
2765
CB
LYS
C
115
42.676
5.771
5.567
1.00
46.12
C


ATOM
2766
CG
LYS
C
115
42.435
4.362
5.125
1.00
51.00
C


ATOM
2767
CD
LYS
C
115
42.795
3.392
6.277
1.00
58.28
C


ATOM
2768
CE
LYS
C
115
41.567
2.885
7.055
1.00
57.90
C


ATOM
2769
NZ
LYS
C
115
41.949
1.742
8.016
1.00
54.76
N


ATOM
2770
C
LYS
C
115
42.365
8.197
5.290
1.00
44.22
C


ATOM
2771
O
LYS
C
115
43.431
8.823
5.252
1.00
43.62
O


ATOM
2772
N
GLY
C
116
41.305
8.645
5.954
1.00
43.05
N


ATOM
2773
CA
GLY
C
116
41.356
9.864
6.689
1.00
42.05
C


ATOM
2774
C
GLY
C
116
42.174
9.631
7.930
1.00
42.35
C


ATOM
2775
O
GLY
C
116
42.452
8.484
8.287
1.00
42.05
O


ATOM
2776
N
ALA
C
117
42.571
10.708
8.596
1.00
42.37
N


ATOM
2777
CA
ALA
C
117
43.399
10.550
9.757
1.00
43.05
C


ATOM
2778
CB
ALA
C
117
44.260
11.829
10.014
1.00
42.67
C


ATOM
2779
C
ALA
C
117
42.634
10.084
11.023
1.00
43.56
C


ATOM
2780
O
ALA
C
117
43.246
9.826
12.055
1.00
43.65
O


ATOM
2781
N
GLY
C
118
41.314
9.951
10.965
1.00
43.66
N


ATOM
2782
CA
GLY
C
118
40.611
9.472
12.152
1.00
42.79
C


ATOM
2783
C
GLY
C
118
39.896
10.562
12.934
1.00
41.73
C


ATOM
2784
O
GLY
C
118
40.354
11.701
12.976
1.00
40.92
O


ATOM
2785
N
THR
C
119
38.743
10.194
13.496
1.00
39.98
N


ATOM
2786
CA
THR
C
119
37.946
11.020
14.384
1.00
38.58
C


ATOM
2787
CB
THR
C
119
36.488
11.253
13.783
1.00
39.57
C


ATOM
2788
OG1
THR
C
119
36.588
12.076
12.602
1.00
38.54
O


ATOM
2789
CG2
THR
C
119
35.520
11.976
14.801
1.00
36.85
C


ATOM
2790
C
THR
C
119
37.848
10.245
15.679
1.00
38.20
C


ATOM
2791
O
THR
C
119
37.235
9.181
15.707
1.00
38.00
O


ATOM
2792
N
ALA
C
120
38.444
10.762
16.760
1.00
39.02
N


ATOM
2793
CA
ALA
C
120
38.267
10.190
18.104
1.00
38.01
C


ATOM
2794
CB
ALA
C
120
39.460
10.554
19.000
1.00
37.67
C


ATOM
2795
C
ALA
C
120
36.956
10.710
18.698
1.00
38.14
C


ATOM
2796
O
ALA
C
120
36.900
11.849
19.022
1.00
38.99
O


ATOM
2797
N
LEU
C
121
35.904
9.888
18.786
1.00
37.88
N


ATOM
2798
CA
LEU
C
121
34.606
10.267
19.338
1.00
37.54
C


ATOM
2799
CB
LEU
C
121
33.405
9.771
18.456
1.00
37.32
C


ATOM
2800
CG
LEU
C
121
32.005
9.892
19.096
1.00
36.95
C


ATOM
2801
CD1
LEU
C
121
31.645
11.412
19.345
1.00
30.48
C


ATOM
2802
CD2
LEU
C
121
30.953
9.178
18.323
1.00
36.88
C


ATOM
2803
C
LEU
C
121
34.449
9.684
20.736
1.00
39.77
C


ATOM
2804
O
LEU
C
121
34.550
8.474
20.921
1.00
39.94
O


ATOM
2805
N
THR
C
122
34.231
10.558
21.715
1.00
39.58
N


ATOM
2806
CA
THR
C
122
33.743
10.128
23.012
1.00
42.41
C


ATOM
2807
CB
THR
C
122
34.744
10.283
24.221
1.00
42.49
C


ATOM
2808
OG1
THR
C
122
34.066
10.807
25.351
1.00
47.39
O


ATOM
2809
CG2
THR
C
122
35.975
11.103
23.923
1.00
44.50
C


ATOM
2810
C
THR
C
122
32.368
10.695
23.269
1.00
41.60
C


ATOM
2811
O
THR
C
122
32.115
11.879
22.992
1.00
40.70
O


ATOM
2812
N
VAL
C
123
31.465
9.800
23.664
1.00
41.20
N


ATOM
2813
CA
VAL
C
123
30.065
10.141
23.928
1.00
41.97
C


ATOM
2814
CB
VAL
C
123
29.040
9.174
23.218
1.00
41.64
C


ATOM
2815
CG1
VAL
C
123
27.572
9.521
23.597
1.00
38.86
C


ATOM
2816
CG2
VAL
C
123
29.222
9.177
21.701
1.00
36.97
C


ATOM
2817
C
VAL
C
123
29.901
10.060
25.442
1.00
43.60
C


ATOM
2818
O
VAL
C
123
30.189
9.036
26.029
1.00
43.27
O


ATOM
2819
N
LYS
C
124
29.459
11.137
26.070
1.00
46.27
N


ATOM
2820
CA
LYS
C
124
29.335
11.162
27.519
1.00
50.07
C


ATOM
2821
CB
LYS
C
124
29.566
12.574
28.019
1.00
51.04
C


ATOM
2822
CG
LYS
C
124
30.992
13.088
27.721
1.00
55.46
C


ATOM
2823
CD
LYS
C
124
31.184
14.509
28.264
1.00
62.63
C


ATOM
2824
CE
LYS
C
124
30.287
15.512
27.491
1.00
64.83
C


ATOM
2825
NZ
LYS
C
124
30.202
16.850
28.169
1.00
67.51
N


ATOM
2826
C
LYS
C
124
27.960
10.729
27.900
1.00
51.41
C


ATOM
2827
O
LYS
C
124
27.006
11.094
27.223
1.00
53.12
O


ATOM
2828
N
ALA
C
125
27.857
9.965
28.982
1.00
53.39
N


ATOM
2829
CA
ALA
C
125
26.584
9.427
29.504
1.00
55.35
C


ATOM
2830
CB
ALA
C
125
26.828
8.627
30.778
1.00
54.28
C


ATOM
2831
C
ALA
C
125
25.485
10.460
29.739
1.00
57.36
C


ATOM
2832
O
ALA
C
125
25.745
11.656
29.989
1.00
56.29
O


ATOM
2833
N
ALA
C
126
24.240
9.987
29.654
1.00
60.08
N


ATOM
2834
CA
ALA
C
126
23.084
10.865
29.877
1.00
62.33
C


ATOM
2835
CB
ALA
C
126
21.766
10.076
29.780
1.00
62.64
C


ATOM
2836
C
ALA
C
126
23.246
11.540
31.244
1.00
63.68
C


ATOM
2837
O
ALA
C
126
23.436
10.871
32.272
1.00
64.15
O


ATOM
2838
OXT
ALA
C
126
23.253
12.783
31.350
1.00
65.04
O


ATOM
2839
N
ALA
D
1
46.173
−30.720
−12.181
1.00
52.41
N


ATOM
2840
CA
ALA
D
1
47.352
−29.997
−11.635
1.00
52.38
C


ATOM
2841
CB
ALA
D
1
47.073
−28.463
−11.586
1.00
52.73
C


ATOM
2842
C
ALA
D
1
47.756
−30.484
−10.247
1.00
52.06
C


ATOM
2843
O
ALA
D
1
47.324
−29.889
−9.245
1.00
52.92
O


ATOM
2844
N
TRP
D
2
48.618
−31.503
−10.174
1.00
50.77
N


ATOM
2845
CA
TRP
D
2
49.207
−31.901
−8.886
1.00
49.15
C


ATOM
2846
CB
TRP
D
2
48.379
−33.027
−8.243
1.00
49.04
C


ATOM
2847
CG
TRP
D
2
48.455
−34.342
−8.948
1.00
48.39
C


ATOM
2848
CD1
TRP
D
2
47.909
−34.665
−10.162
1.00
48.80
C


ATOM
2849
NE1
TRP
D
2
48.181
−35.993
−10.473
1.00
47.88
N


ATOM
2850
CE2
TRP
D
2
48.915
−36.540
−9.456
1.00
48.78
C


ATOM
2851
CD2
TRP
D
2
49.105
−35.532
−8.474
1.00
48.50
C


ATOM
2852
CE3
TRP
D
2
49.816
−35.851
−7.312
1.00
49.44
C


ATOM
2853
CZ3
TRP
D
2
50.318
−37.152
−7.169
1.00
48.14
C


ATOM
2854
CH2
TRP
D
2
50.130
−38.111
−8.167
1.00
48.46
C


ATOM
2855
CZ2
TRP
D
2
49.430
−37.833
−9.311
1.00
48.68
C


ATOM
2856
C
TRP
D
2
50.692
−32.283
−8.969
1.00
48.37
C


ATOM
2857
O
TRP
D
2
51.129
−32.808
−9.982
1.00
47.97
O


ATOM
2858
N
VAL
D
3
51.447
−32.014
−7.892
1.00
47.21
N


ATOM
2859
CA
VAL
D
3
52.880
−32.359
−7.783
1.00
46.09
C


ATOM
2860
CB
VAL
D
3
53.713
−31.248
−7.051
1.00
45.63
C


ATOM
2861
CG1
VAL
D
3
55.086
−31.739
−6.681
1.00
45.70
C


ATOM
2862
CG2
VAL
D
3
53.857
−30.036
−7.931
1.00
45.94
C


ATOM
2863
C
VAL
D
3
53.042
−33.724
−7.090
1.00
45.51
C


ATOM
2864
O
VAL
D
3
52.541
−33.953
−5.995
1.00
45.34
O


ATOM
2865
N
ASP
D
4
53.726
−34.629
−7.766
1.00
44.30
N


ATOM
2866
CA
ASP
D
4
53.861
−36.002
−7.344
1.00
43.85
C


ATOM
2867
CB
ASP
D
4
53.638
−36.897
−8.574
1.00
43.56
C


ATOM
2868
CG
ASP
D
4
53.731
−38.385
−8.283
1.00
46.38
C


ATOM
2869
OD1
ASP
D
4
53.456
−39.152
−9.224
1.00
48.84
O


ATOM
2870
OD2
ASP
D
4
54.085
−38.824
−7.165
1.00
49.73
O


ATOM
2871
C
ASP
D
4
55.282
−36.096
−6.773
1.00
42.85
C


ATOM
2872
O
ASP
D
4
56.260
−36.173
−7.527
1.00
43.36
O


ATOM
2873
N
GLN
D
5
55.399
−36.044
−5.450
1.00
40.53
N


ATOM
2874
CA
GLN
D
5
56.695
−36.068
−4.816
1.00
39.40
C


ATOM
2875
CB
GLN
D
5
56.769
−34.988
−3.723
1.00
38.84
C


ATOM
2876
CG
GLN
D
5
58.080
−34.973
−2.919
1.00
37.60
C


ATOM
2877
CD
GLN
D
5
58.067
−33.903
−1.836
1.00
40.37
C


ATOM
2878
OE1
GLN
D
5
57.169
−33.053
−1.805
1.00
39.68
O


ATOM
2879
NE2
GLN
D
5
59.067
−33.928
−0.944
1.00
37.57
N


ATOM
2880
C
GLN
D
5
56.978
−37.445
−4.208
1.00
39.58
C


ATOM
2881
O
GLN
D
5
56.165
−37.959
−3.443
1.00
39.26
O


ATOM
2882
N
THR
D
6
58.153
−37.997
−4.531
1.00
39.50
N


ATOM
2883
CA
THR
D
6
58.650
−39.281
−4.032
1.00
39.81
C


ATOM
2884
CB
THR
D
6
58.637
−40.379
−5.152
1.00
39.82
C


ATOM
2885
OG1
THR
D
6
59.280
−39.861
−6.318
1.00
41.35
O


ATOM
2886
CG2
THR
D
6
57.202
−40.812
−5.536
1.00
41.10
C


ATOM
2887
C
THR
D
6
60.103
−39.129
−3.536
1.00
39.11
C


ATOM
2888
O
THR
D
6
60.846
−38.306
−4.047
1.00
38.91
O


ATOM
2889
N
PRO
D
7
60.509
−39.925
−2.532
1.00
38.82
N


ATOM
2890
CA
PRO
D
7
59.674
−40.854
−1.771
1.00
38.84
C


ATOM
2891
CB
PRO
D
7
60.708
−41.859
−1.250
1.00
39.29
C


ATOM
2892
CG
PRO
D
7
61.982
−40.990
−1.047
1.00
38.10
C


ATOM
2893
CD
PRO
D
7
61.918
−39.932
−2.080
1.00
38.51
C


ATOM
2894
C
PRO
D
7
58.938
−40.128
−0.616
1.00
38.96
C


ATOM
2895
O
PRO
D
7
59.364
−39.093
−0.218
1.00
38.31
O


ATOM
2896
N
ARG
D
8
57.835
−40.664
−0.098
1.00
40.27
N


ATOM
2897
CA
ARG
D
8
57.128
−40.039
1.046
1.00
40.80
C


ATOM
2898
CB
ARG
D
8
55.743
−40.686
1.236
1.00
40.70
C


ATOM
2899
CG
ARG
D
8
54.775
−40.011
2.223
1.00
45.33
C


ATOM
2900
CD
ARG
D
8
54.283
−38.614
1.746
1.00
52.07
C


ATOM
2901
NE
ARG
D
8
54.080
−38.557
0.289
1.00
54.98
N


ATOM
2902
CZ
ARG
D
8
52.900
−38.616
−0.330
1.00
57.24
C


ATOM
2903
NH1
ARG
D
8
51.758
−38.714
0.359
1.00
56.56
N


ATOM
2904
NH2
ARG
D
8
52.862
−38.549
−1.658
1.00
58.04
N


ATOM
2905
C
ARG
D
8
57.977
−40.100
2.331
1.00
40.53
C


ATOM
2906
O
ARG
D
8
57.929
−39.207
3.158
1.00
40.81
O


ATOM
2907
N
THR
D
9
58.770
−41.153
2.475
1.00
40.47
N


ATOM
2908
CA
THR
D
9
59.629
−41.350
3.634
1.00
40.91
C


ATOM
2909
CB
THR
D
9
58.994
−42.340
4.695
1.00
41.45
C


ATOM
2910
OG1
THR
D
9
58.726
−43.600
4.084
1.00
41.04
O


ATOM
2911
CG2
THR
D
9
57.639
−41.805
5.351
1.00
41.38
C


ATOM
2912
C
THR
D
9
60.999
−41.914
3.169
1.00
41.67
C


ATOM
2913
O
THR
D
9
61.083
−42.696
2.225
1.00
40.23
O


ATOM
2914
N
ALA
D
10
62.064
−41.522
3.868
1.00
42.06
N


ATOM
2915
CA
ALA
D
10
63.392
−42.065
3.635
1.00
41.77
C


ATOM
2916
CB
ALA
D
10
64.160
−41.142
2.735
1.00
42.21
C


ATOM
2917
C
ALA
D
10
64.086
−42.181
4.998
1.00
42.56
C


ATOM
2918
O
ALA
D
10
63.811
−41.387
5.903
1.00
40.53
O


ATOM
2919
N
THR
D
11
64.914
−43.211
5.161
1.00
43.58
N


ATOM
2920
CA
THR
D
11
65.800
−43.354
6.320
1.00
45.06
C


ATOM
2921
CB
THR
D
11
65.427
−44.561
7.235
1.00
45.98
C


ATOM
2922
OG1
THR
D
11
64.100
−44.386
7.754
1.00
48.35
O


ATOM
2923
CG2
THR
D
11
66.423
−44.712
8.442
1.00
45.10
C


ATOM
2924
C
THR
D
11
67.177
−43.562
5.723
1.00
46.01
C


ATOM
2925
O
THR
D
11
67.379
−44.392
4.825
1.00
46.79
O


ATOM
2926
N
LYS
D
12
68.118
−42.766
6.193
1.00
46.59
N


ATOM
2927
CA
LYS
D
12
69.488
−42.806
5.725
1.00
46.11
C


ATOM
2928
CB
LYS
D
12
69.766
−41.586
4.863
1.00
45.49
C


ATOM
2929
CG
LYS
D
12
68.877
−41.544
3.598
1.00
44.78
C


ATOM
2930
CD
LYS
D
12
69.231
−42.666
2.588
1.00
40.67
C


ATOM
2931
CE
LYS
D
12
68.264
−42.658
1.445
1.00
42.32
C


ATOM
2932
NZ
LYS
D
12
68.712
−43.565
0.374
1.00
41.82
N


ATOM
2933
C
LYS
D
12
70.441
−42.847
6.903
1.00
47.39
C


ATOM
2934
O
LYS
D
12
70.080
−42.564
8.065
1.00
46.27
O


ATOM
2935
N
GLU
D
13
71.669
−43.213
6.583
1.00
48.57
N


ATOM
2936
CA
GLU
D
13
72.742
−43.190
7.538
1.00
49.48
C


ATOM
2937
CB
GLU
D
13
73.578
−44.461
7.335
1.00
50.69
C


ATOM
2938
CG
GLU
D
13
73.899
−45.243
8.610
1.00
53.61
C


ATOM
2939
CD
GLU
D
13
75.339
−45.752
8.601
1.00
59.15
C


ATOM
2940
OE1
GLU
D
13
75.609
−46.771
9.288
1.00
59.36
O


ATOM
2941
OE2
GLU
D
13
76.200
−45.139
7.892
1.00
59.86
O


ATOM
2942
C
GLU
D
13
73.534
−41.911
7.193
1.00
48.81
C


ATOM
2943
O
GLU
D
13
73.480
−41.453
6.043
1.00
48.11
O


ATOM
2944
N
THR
D
14
74.259
−41.324
8.155
1.00
48.09
N


ATOM
2945
CA
THR
D
14
75.143
−40.192
7.810
1.00
47.65
C


ATOM
2946
CB
THR
D
14
75.925
−39.621
9.031
1.00
47.59
C


ATOM
2947
OG1
THR
D
14
76.628
−40.678
9.687
1.00
48.03
O


ATOM
2948
CG2
THR
D
14
74.987
−38.998
10.048
1.00
47.29
C


ATOM
2949
C
THR
D
14
76.117
−40.593
6.681
1.00
47.56
C


ATOM
2950
O
THR
D
14
76.583
−41.748
6.620
1.00
47.03
O


ATOM
2951
N
GLY
D
15
76.414
−39.648
5.793
1.00
46.77
N


ATOM
2952
CA
GLY
D
15
77.304
−39.915
4.667
1.00
46.69
C


ATOM
2953
C
GLY
D
15
76.607
−40.296
3.367
1.00
46.34
C


ATOM
2954
O
GLY
D
15
77.083
−39.969
2.293
1.00
46.24
O


ATOM
2955
N
GLU
D
16
75.484
−40.998
3.474
1.00
46.52
N


ATOM
2956
CA
GLU
D
16
74.670
−41.389
2.327
1.00
46.87
C


ATOM
2957
CB
GLU
D
16
73.574
−42.384
2.757
1.00
46.63
C


ATOM
2958
CG
GLU
D
16
74.023
−43.586
3.578
1.00
46.69
C


ATOM
2959
CD
GLU
D
16
72.979
−44.733
3.575
1.00
48.35
C


ATOM
2960
OE1
GLU
D
16
73.193
−45.693
2.807
1.00
53.70
O


ATOM
2961
OE2
GLU
D
16
71.954
−44.705
4.299
1.00
48.55
O


ATOM
2962
C
GLU
D
16
74.003
−40.187
1.632
1.00
46.94
C


ATOM
2963
O
GLU
D
16
74.209
−39.019
1.977
1.00
46.67
O


ATOM
2964
N
SER
D
17
73.174
−40.471
0.637
1.00
47.38
N


ATOM
2965
CA
SER
D
17
72.518
−39.376
−0.056
1.00
47.46
C


ATOM
2966
CB
SER
D
17
73.184
−39.131
−1.410
1.00
48.28
C


ATOM
2967
OG
SER
D
17
72.749
−40.047
−2.416
1.00
52.49
O


ATOM
2968
C
SER
D
17
71.029
−39.642
−0.196
1.00
46.61
C


ATOM
2969
O
SER
D
17
70.588
−40.785
0.001
1.00
46.62
O


ATOM
2970
N
LEU
D
18
70.263
−38.583
−0.477
1.00
44.97
N


ATOM
2971
CA
LEU
D
18
68.829
−38.674
−0.742
1.00
43.88
C


ATOM
2972
CB
LEU
D
18
68.010
−37.924
0.319
1.00
44.17
C


ATOM
2973
CG
LEU
D
18
66.612
−38.336
0.802
1.00
44.22
C


ATOM
2974
CD1
LEU
D
18
65.730
−37.114
0.965
1.00
44.33
C


ATOM
2975
CD2
LEU
D
18
65.950
−39.375
−0.033
1.00
43.22
C


ATOM
2976
C
LEU
D
18
68.614
−37.943
−2.049
1.00
43.24
C


ATOM
2977
O
LEU
D
18
69.159
−36.865
−2.231
1.00
42.98
O


ATOM
2978
N
THR
D
19
67.817
−38.528
−2.936
1.00
42.05
N


ATOM
2979
CA
THR
D
19
67.259
−37.821
−4.062
1.00
41.13
C


ATOM
2980
CB
THR
D
19
67.673
−38.509
−5.373
1.00
41.27
C


ATOM
2981
OG1
THR
D
19
68.982
−39.032
−5.185
1.00
42.63
O


ATOM
2982
CG2
THR
D
19
67.703
−37.531
−6.542
1.00
39.59
C


ATOM
2983
C
THR
D
19
65.731
−37.751
−3.892
1.00
40.45
C


ATOM
2984
O
THR
D
19
65.055
−38.763
−3.753
1.00
40.58
O


ATOM
2985
N
ILE
D
20
65.207
−36.542
−3.859
1.00
39.89
N


ATOM
2986
CA
ILE
D
20
63.766
−36.329
−3.894
1.00
40.16
C


ATOM
2987
CB
ILE
D
20
63.326
−35.181
−2.940
1.00
40.54
C


ATOM
2988
CG1
ILE
D
20
63.757
−35.493
−1.505
1.00
41.28
C


ATOM
2989
CD1
ILE
D
20
63.883
−34.280
−0.649
1.00
41.55
C


ATOM
2990
CG2
ILE
D
20
61.799
−34.926
−3.043
1.00
39.20
C


ATOM
2991
C
ILE
D
20
63.383
−35.979
−5.323
1.00
39.22
C


ATOM
2992
O
ILE
D
20
64.012
−35.141
−5.904
1.00
38.55
O


ATOM
2993
N
ASN
D
21
62.358
−36.632
−5.859
1.00
39.57
N


ATOM
2994
CA
ASN
D
21
61.852
−36.370
−7.213
1.00
41.08
C


ATOM
2995
CB
ASN
D
21
61.773
−37.676
−7.967
1.00
41.24
C


ATOM
2996
CG
ASN
D
21
63.008
−37.956
−8.759
1.00
43.85
C


ATOM
2997
OD1
ASN
D
21
63.215
−37.323
−9.793
1.00
48.63
O


ATOM
2998
ND2
ASN
D
21
63.814
−38.942
−8.325
1.00
43.95
N


ATOM
2999
C
ASN
D
21
60.453
−35.779
−7.184
1.00
41.77
C


ATOM
3000
O
ASN
D
21
59.636
−36.200
−6.375
1.00
41.70
O


ATOM
3001
N
CYS
D
22
60.180
−34.794
−8.039
1.00
42.41
N


ATOM
3002
CA
CYS
D
22
58.840
−34.207
−8.137
1.00
43.48
C


ATOM
3003
CB
CYS
D
22
58.774
−32.833
−7.476
1.00
42.75
C


ATOM
3004
SG
CYS
D
22
59.105
−32.836
−5.677
1.00
49.46
S


ATOM
3005
C
CYS
D
22
58.428
−34.062
−9.580
1.00
43.16
C


ATOM
3006
O
CYS
D
22
59.168
−33.495
−10.359
1.00
43.59
O


ATOM
3007
N
VAL
D
23
57.228
−34.523
−9.918
1.00
43.81
N


ATOM
3008
CA
VAL
D
23
56.647
−34.300
−11.241
1.00
44.50
C


ATOM
3009
CB
VAL
D
23
56.382
−35.665
−11.979
1.00
44.28
C


ATOM
3010
CG1
VAL
D
23
55.931
−35.444
−13.468
1.00
44.41
C


ATOM
3011
CG2
VAL
D
23
57.614
−36.588
−11.902
1.00
42.56
C


ATOM
3012
C
VAL
D
23
55.358
−33.477
−11.126
1.00
45.73
C


ATOM
3013
O
VAL
D
23
54.510
−33.746
−10.265
1.00
45.32
O


ATOM
3014
N
LEU
D
24
55.224
−32.460
−11.986
1.00
47.64
N


ATOM
3015
CA
LEU
D
24
53.951
−31.724
−12.179
1.00
48.97
C


ATOM
3016
CB
LEU
D
24
54.214
−30.344
−12.795
1.00
48.56
C


ATOM
3017
CG
LEU
D
24
53.466
−29.079
−12.328
1.00
49.30
C


ATOM
3018
CD1
LEU
D
24
53.669
−27.924
−13.368
1.00
46.03
C


ATOM
3019
CD2
LEU
D
24
51.974
−29.319
−11.999
1.00
48.04
C


ATOM
3020
C
LEU
D
24
52.983
−32.521
−13.083
1.00
49.95
C


ATOM
3021
O
LEU
D
24
53.134
−32.529
−14.313
1.00
50.57
O


ATOM
3022
N
ARG
D
25
52.001
−33.195
−12.471
1.00
51.10
N


ATOM
3023
CA
ARG
D
25
51.019
−34.050
−13.192
1.00
51.64
C


ATOM
3024
CB
ARG
D
25
50.696
−35.313
−12.386
1.00
51.32
C


ATOM
3025
CG
ARG
D
25
51.863
−36.063
−11.871
1.00
49.97
C


ATOM
3026
CD
ARG
D
25
52.204
−37.166
−12.794
1.00
47.93
C


ATOM
3027
NE
ARG
D
25
53.274
−37.967
−12.225
1.00
47.52
N


ATOM
3028
CZ
ARG
D
25
53.981
−38.861
−12.909
1.00
47.68
C


ATOM
3029
NH1
ARG
D
25
53.741
−39.083
−14.202
1.00
46.46
N


ATOM
3030
NH2
ARG
D
25
54.941
−39.536
−12.298
1.00
48.61
N


ATOM
3031
C
ARG
D
25
49.699
−33.318
−13.473
1.00
52.55
C


ATOM
3032
O
ARG
D
25
49.412
−32.286
−12.847
1.00
52.60
O


ATOM
3033
N
ASP
D
26
48.891
−33.884
−14.386
1.00
53.55
N


ATOM
3034
CA
ASP
D
26
47.619
−33.276
−14.857
1.00
54.33
C


ATOM
3035
CB
ASP
D
26
46.477
−33.475
−13.843
1.00
54.58
C


ATOM
3036
CG
ASP
D
26
45.374
−34.384
−14.368
1.00
55.93
C


ATOM
3037
OD1
ASP
D
26
44.789
−34.090
−15.443
1.00
57.14
O


ATOM
3038
OD2
ASP
D
26
45.089
−35.398
−13.694
1.00
57.19
O


ATOM
3039
C
ASP
D
26
47.694
−31.801
−15.233
1.00
54.37
C


ATOM
3040
O
ASP
D
26
46.708
−31.085
−15.092
1.00
54.79
O


ATOM
3041
N
ALA
D
27
48.845
−31.346
−15.719
1.00
54.73
N


ATOM
3042
CA
ALA
D
27
49.050
−29.918
−15.985
1.00
54.79
C


ATOM
3043
CB
ALA
D
27
50.415
−29.475
−15.472
1.00
54.57
C


ATOM
3044
C
ALA
D
27
48.897
−29.583
−17.469
1.00
54.93
C


ATOM
3045
O
ALA
D
27
49.543
−30.202
−18.321
1.00
55.09
O


ATOM
3046
N
SER
D
28
48.038
−28.617
−17.781
1.00
54.75
N


ATOM
3047
CA
SER
D
28
47.935
−28.133
−19.152
1.00
54.93
C


ATOM
3048
CB
SER
D
28
46.488
−27.753
−19.510
1.00
55.22
C


ATOM
3049
OG
SER
D
28
46.074
−26.557
−18.862
1.00
55.13
O


ATOM
3050
C
SER
D
28
48.892
−26.952
−19.338
1.00
54.84
C


ATOM
3051
O
SER
D
28
49.138
−26.492
−20.463
1.00
54.36
O


ATOM
3052
N
PHE
D
29
49.413
−26.472
−18.209
1.00
54.77
N


ATOM
3053
CA
PHE
D
29
50.460
−25.448
−18.167
1.00
54.65
C


ATOM
3054
CB
PHE
D
29
50.152
−24.392
−17.096
1.00
55.22
C


ATOM
3055
CG
PHE
D
29
49.499
−24.951
−15.847
1.00
56.31
C


ATOM
3056
CD1
PHE
D
29
50.206
−25.806
−14.988
1.00
56.26
C


ATOM
3057
CE1
PHE
D
29
49.596
−26.332
−13.834
1.00
57.52
C


ATOM
3058
CZ
PHE
D
29
48.269
−25.993
−13.528
1.00
57.03
C


ATOM
3059
CE2
PHE
D
29
47.554
−25.124
−14.385
1.00
58.39
C


ATOM
3060
CD2
PHE
D
29
48.174
−24.614
−15.534
1.00
56.93
C


ATOM
3061
C
PHE
D
29
51.867
−26.058
−17.966
1.00
54.11
C


ATOM
3062
O
PHE
D
29
52.019
−27.269
−17.723
1.00
53.85
O


ATOM
3063
N
GLU
D
30
52.884
−25.210
−18.091
1.00
53.36
N


ATOM
3064
CA
GLU
D
30
54.270
−25.660
−18.088
1.00
52.94
C


ATOM
3065
CB
GLU
D
30
55.046
−25.061
−19.275
1.00
53.22
C


ATOM
3066
CG
GLU
D
30
54.424
−25.259
−20.663
1.00
54.41
C


ATOM
3067
CD
GLU
D
30
54.848
−26.554
−21.333
1.00
56.12
C


ATOM
3068
OE1
GLU
D
30
55.997
−27.002
−21.121
1.00
57.05
O


ATOM
3069
OE2
GLU
D
30
54.028
−27.124
−22.079
1.00
56.87
O


ATOM
3070
C
GLU
D
30
54.947
−25.262
−16.778
1.00
51.85
C


ATOM
3071
O
GLU
D
30
54.501
−24.352
−16.081
1.00
51.46
O


ATOM
3072
N
LEU
D
31
56.045
−25.942
−16.474
1.00
51.22
N


ATOM
3073
CA
LEU
D
31
56.825
−25.688
−15.275
1.00
49.86
C


ATOM
3074
CB
LEU
D
31
57.710
−26.901
−14.991
1.00
49.53
C


ATOM
3075
CG
LEU
D
31
58.340
−26.964
−13.595
1.00
48.63
C


ATOM
3076
CD1
LEU
D
31
57.315
−26.642
−12.490
1.00
43.48
C


ATOM
3077
CD2
LEU
D
31
58.957
−28.337
−13.398
1.00
46.35
C


ATOM
3078
C
LEU
D
31
57.695
−24.468
−15.489
1.00
49.34
C


ATOM
3079
O
LEU
D
31
58.652
−24.527
−16.250
1.00
49.11
O


ATOM
3080
N
LYS
D
32
57.362
−23.366
−14.838
1.00
49.24
N


ATOM
3081
CA
LYS
D
32
58.155
−22.156
−14.986
1.00
49.60
C


ATOM
3082
CB
LYS
D
32
57.325
−20.901
−14.692
1.00
49.77
C


ATOM
3083
CG
LYS
D
32
56.343
−20.516
−15.862
1.00
51.34
C


ATOM
3084
CD
LYS
D
32
56.909
−20.827
−17.265
1.00
50.23
C


ATOM
3085
CE
LYS
D
32
55.918
−20.497
−18.363
1.00
51.66
C


ATOM
3086
NZ
LYS
D
32
55.711
−21.653
−19.277
1.00
51.95
N


ATOM
3087
C
LYS
D
32
59.398
−22.205
−14.111
1.00
50.13
C


ATOM
3088
O
LYS
D
32
60.530
−22.068
−14.608
1.00
50.59
O


ATOM
3089
N
ASP
D
33
59.174
−22.422
−12.820
1.00
48.97
N


ATOM
3090
CA
ASP
D
33
60.207
−22.327
−11.799
1.00
49.30
C


ATOM
3091
CB
ASP
D
33
60.268
−20.869
−11.293
1.00
49.60
C


ATOM
3092
CG
ASP
D
33
61.514
−20.592
−10.464
1.00
54.11
C


ATOM
3093
OD1
ASP
D
33
62.644
−21.000
−10.869
1.00
55.49
O


ATOM
3094
OD2
ASP
D
33
61.356
−19.998
−9.367
1.00
59.32
O


ATOM
3095
C
ASP
D
33
59.965
−23.362
−10.629
1.00
47.92
C


ATOM
3096
O
ASP
D
33
58.887
−23.942
−10.506
1.00
47.18
O


ATOM
3097
N
THR
D
34
60.964
−23.576
−9.782
1.00
47.12
N


ATOM
3098
CA
THR
D
34
60.882
−24.571
−8.714
1.00
45.90
C


ATOM
3099
CB
THR
D
34
61.701
−25.848
−9.054
1.00
46.44
C


ATOM
3100
OG1
THR
D
34
63.095
−25.523
−9.217
1.00
43.45
O


ATOM
3101
CG2
THR
D
34
61.172
−26.526
−10.312
1.00
46.59
C


ATOM
3102
C
THR
D
34
61.449
−24.004
−7.427
1.00
46.20
C


ATOM
3103
O
THR
D
34
62.340
−23.122
−7.464
1.00
46.30
O


ATOM
3104
N
GLY
D
35
60.944
−24.509
−6.290
1.00
45.15
N


ATOM
3105
CA
GLY
D
35
61.530
−24.211
−4.995
1.00
44.20
C


ATOM
3106
C
GLY
D
35
61.560
−25.447
−4.130
1.00
44.10
C


ATOM
3107
O
GLY
D
35
60.734
−26.358
−4.309
1.00
43.01
O


ATOM
3108
N
TRP
D
36
62.497
−25.440
−3.172
1.00
43.91
N


ATOM
3109
CA
TRP
D
36
62.680
−26.524
−2.222
1.00
43.17
C


ATOM
3110
CB
TRP
D
36
63.989
−27.274
−2.505
1.00
42.16
C


ATOM
3111
CG
TRP
D
36
63.897
−28.084
−3.748
1.00
42.33
C


ATOM
3112
CD1
TRP
D
36
64.287
−27.709
−4.990
1.00
41.86
C


ATOM
3113
NE1
TRP
D
36
64.020
−28.710
−5.901
1.00
41.80
N


ATOM
3114
CE2
TRP
D
36
63.440
−29.761
−5.246
1.00
39.28
C


ATOM
3115
CD2
TRP
D
36
63.339
−29.404
−3.881
1.00
41.23
C


ATOM
3116
CE3
TRP
D
36
62.771
−30.315
−2.975
1.00
40.97
C


ATOM
3117
CZ3
TRP
D
36
62.320
−31.538
−3.462
1.00
41.67
C


ATOM
3118
CH2
TRP
D
36
62.442
−31.859
−4.835
1.00
42.09
C


ATOM
3119
CZ2
TRP
D
36
63.008
−30.988
−5.737
1.00
39.64
C


ATOM
3120
C
TRP
D
36
62.666
−25.949
−0.848
1.00
43.26
C


ATOM
3121
O
TRP
D
36
63.284
−24.931
−0.618
1.00
42.62
O


ATOM
3122
N
TYR
D
37
61.921
−26.603
0.042
1.00
43.77
N


ATOM
3123
CA
TYR
D
37
61.774
−26.215
1.445
1.00
44.44
C


ATOM
3124
CB
TYR
D
37
60.384
−25.667
1.724
1.00
45.80
C


ATOM
3125
CG
TYR
D
37
59.912
−24.825
0.615
1.00
50.24
C


ATOM
3126
CD1
TYR
D
37
60.243
−23.457
0.557
1.00
52.74
C


ATOM
3127
CE1
TYR
D
37
59.827
−22.661
−0.510
1.00
53.61
C


ATOM
3128
CZ
TYR
D
37
59.078
−23.238
−1.534
1.00
53.15
C


ATOM
3129
OH
TYR
D
37
58.677
−22.491
−2.597
1.00
53.11
O


ATOM
3130
CE2
TYR
D
37
58.744
−24.592
−1.499
1.00
53.55
C


ATOM
3131
CD2
TYR
D
37
59.167
−25.382
−0.419
1.00
51.12
C


ATOM
3132
C
TYR
D
37
61.987
−27.398
2.367
1.00
43.19
C


ATOM
3133
O
TYR
D
37
61.769
−28.539
1.964
1.00
41.62
O


ATOM
3134
N
ARG
D
38
62.305
−27.064
3.620
1.00
42.47
N


ATOM
3135
CA
ARG
D
38
62.552
−28.009
4.705
1.00
43.75
C


ATOM
3136
CB
ARG
D
38
64.045
−28.379
4.717
1.00
43.86
C


ATOM
3137
CG
ARG
D
38
64.576
−28.648
6.062
1.00
48.19
C


ATOM
3138
CD
ARG
D
38
65.373
−29.910
6.170
1.00
53.19
C


ATOM
3139
NE
ARG
D
38
66.808
−29.728
5.932
1.00
58.72
N


ATOM
3140
CZ
ARG
D
38
67.438
−28.558
5.839
1.00
57.26
C


ATOM
3141
NH1
ARG
D
38
66.768
−27.415
5.974
1.00
56.27
N


ATOM
3142
NH2
ARG
D
38
68.751
−28.546
5.624
1.00
57.23
N


ATOM
3143
C
ARG
D
38
62.090
−27.458
6.088
1.00
42.91
C


ATOM
3144
O
ARG
D
38
62.281
−26.267
6.405
1.00
42.55
O


ATOM
3145
N
THR
D
39
61.471
−28.341
6.874
1.00
42.58
N


ATOM
3146
CA
THR
D
39
61.179
−28.177
8.299
1.00
41.28
C


ATOM
3147
CB
THR
D
39
59.656
−28.312
8.600
1.00
41.27
C


ATOM
3148
OG1
THR
D
39
58.892
−27.440
7.743
1.00
43.39
O


ATOM
3149
CG2
THR
D
39
59.344
−27.965
10.027
1.00
42.59
C


ATOM
3150
C
THR
D
39
61.989
−29.229
9.060
1.00
41.19
C


ATOM
3151
O
THR
D
39
61.748
−30.449
8.968
1.00
40.45
O


ATOM
3152
N
LYS
D
40
62.968
−28.750
9.804
1.00
40.73
N


ATOM
3153
CA
LYS
D
40
63.868
−29.605
10.541
1.00
41.06
C


ATOM
3154
CB
LYS
D
40
64.893
−28.753
11.289
1.00
41.28
C


ATOM
3155
CG
LYS
D
40
66.298
−29.293
11.229
1.00
45.60
C


ATOM
3156
CD
LYS
D
40
67.141
−28.840
12.503
1.00
49.44
C


ATOM
3157
CE
LYS
D
40
68.173
−29.941
12.917
1.00
47.27
C


ATOM
3158
NZ
LYS
D
40
68.965
−29.678
14.177
1.00
50.09
N


ATOM
3159
C
LYS
D
40
63.075
−30.457
11.539
1.00
41.44
C


ATOM
3160
O
LYS
D
40
62.069
−30.038
12.073
1.00
40.57
O


ATOM
3161
N
LEU
D
41
63.524
−31.676
11.782
1.00
41.67
N


ATOM
3162
CA
LEU
D
41
62.755
−32.533
12.643
1.00
42.41
C


ATOM
3163
CB
LEU
D
41
63.321
−33.947
12.570
1.00
41.48
C


ATOM
3164
CG
LEU
D
41
62.834
−34.954
13.562
1.00
42.23
C


ATOM
3165
CD1
LEU
D
41
63.555
−36.244
13.284
1.00
38.77
C


ATOM
3166
CD2
LEU
D
41
61.360
−35.124
13.379
1.00
42.31
C


ATOM
3167
C
LEU
D
41
62.723
−31.942
14.067
1.00
42.92
C


ATOM
3168
O
LEU
D
41
63.747
−31.819
14.744
1.00
42.91
O


ATOM
3169
N
GLY
D
42
61.531
−31.532
14.484
1.00
43.29
N


ATOM
3170
CA
GLY
D
42
61.306
−31.127
15.848
1.00
44.22
C


ATOM
3171
C
GLY
D
42
61.080
−29.639
15.878
1.00
45.23
C


ATOM
3172
O
GLY
D
42
60.854
−29.079
16.923
1.00
45.24
O


ATOM
3173
N
SER
D
43
61.155
−29.018
14.704
1.00
46.01
N


ATOM
3174
CA
SER
D
43
60.973
−27.595
14.531
1.00
47.24
C


ATOM
3175
CB
SER
D
43
62.214
−27.065
13.803
1.00
46.38
C


ATOM
3176
OG
SER
D
43
61.967
−25.912
13.064
1.00
48.60
O


ATOM
3177
C
SER
D
43
59.635
−27.315
13.798
1.00
48.54
C


ATOM
3178
O
SER
D
43
59.126
−28.181
13.090
1.00
48.74
O


ATOM
3179
N
THR
D
44
59.057
−26.130
13.995
1.00
50.34
N


ATOM
3180
CA
THR
D
44
57.829
−25.713
13.289
1.00
52.56
C


ATOM
3181
CB
THR
D
44
56.759
−25.084
14.274
1.00
53.48
C


ATOM
3182
OG1
THR
D
44
56.875
−25.640
15.613
1.00
52.17
O


ATOM
3183
CG2
THR
D
44
55.331
−25.334
13.742
1.00
54.43
C


ATOM
3184
C
THR
D
44
58.044
−24.766
12.057
1.00
54.01
C


ATOM
3185
O
THR
D
44
57.128
−24.557
11.228
1.00
54.29
O


ATOM
3186
N
ASN
D
45
59.246
−24.208
11.908
1.00
54.74
N


ATOM
3187
CA
ASN
D
45
59.508
−23.303
10.784
1.00
55.53
C


ATOM
3188
CB
ASN
D
45
60.529
−22.227
11.169
1.00
56.24
C


ATOM
3189
CG
ASN
D
45
61.816
−22.827
11.744
1.00
59.18
C


ATOM
3190
OD1
ASN
D
45
62.441
−23.684
11.108
1.00
63.33
O


ATOM
3191
ND2
ASN
D
45
62.210
−22.391
12.954
1.00
59.01
N


ATOM
3192
C
ASN
D
45
59.965
−24.043
9.524
1.00
55.48
C


ATOM
3193
O
ASN
D
45
60.900
−24.875
9.572
1.00
55.04
O


ATOM
3194
N
GLU
D
46
59.292
−23.739
8.413
1.00
55.16
N


ATOM
3195
CA
GLU
D
46
59.654
−24.237
7.120
1.00
55.65
C


ATOM
3196
CB
GLU
D
46
58.413
−24.405
6.238
1.00
56.04
C


ATOM
3197
CG
GLU
D
46
58.708
−25.157
4.911
1.00
56.84
C


ATOM
3198
CD
GLU
D
46
57.527
−25.197
3.937
1.00
58.64
C


ATOM
3199
OE1
GLU
D
46
57.030
−26.309
3.624
1.00
64.99
O


ATOM
3200
OE2
GLU
D
46
57.106
−24.115
3.448
1.00
64.43
O


ATOM
3201
C
GLU
D
46
60.613
−23.246
6.494
1.00
54.79
C


ATOM
3202
O
GLU
D
46
60.260
−22.103
6.253
1.00
55.34
O


ATOM
3203
N
GLN
D
47
61.827
−23.695
6.233
1.00
53.79
N


ATOM
3204
CA
GLN
D
47
62.853
−22.868
5.641
1.00
52.99
C


ATOM
3205
CB
GLN
D
47
64.145
−23.017
6.442
1.00
53.28
C


ATOM
3206
CG
GLN
D
47
64.900
−21.697
6.634
1.00
57.45
C


ATOM
3207
CD
GLN
D
47
64.465
−20.874
7.888
1.00
59.69
C


ATOM
3208
OE1
GLN
D
47
65.207
−19.989
8.343
1.00
58.09
O


ATOM
3209
NE2
GLN
D
47
63.291
−21.193
8.452
1.00
61.05
N


ATOM
3210
C
GLN
D
47
63.105
−23.262
4.184
1.00
51.77
C


ATOM
3211
O
GLN
D
47
63.009
−24.438
3.832
1.00
50.62
O


ATOM
3212
N
SER
D
48
63.439
−22.274
3.341
1.00
50.27
N


ATOM
3213
CA
SER
D
48
63.767
−22.526
1.941
1.00
49.06
C


ATOM
3214
CB
SER
D
48
63.715
−21.209
1.153
1.00
50.37
C


ATOM
3215
OG
SER
D
48
62.799
−20.303
1.782
1.00
54.39
O


ATOM
3216
C
SER
D
48
65.158
−23.135
1.844
1.00
46.80
C


ATOM
3217
O
SER
D
48
66.000
−22.874
2.670
1.00
46.24
O


ATOM
3218
N
ILE
D
49
65.401
−23.952
0.838
1.00
46.02
N


ATOM
3219
CA
ILE
D
49
66.723
−24.566
0.630
1.00
45.76
C


ATOM
3220
CB
ILE
D
49
66.583
−26.054
0.296
1.00
45.49
C


ATOM
3221
CG1
ILE
D
49
66.175
−26.853
1.553
1.00
44.65
C


ATOM
3222
CD1
ILE
D
49
65.438
−28.191
1.239
1.00
45.72
C


ATOM
3223
CG2
ILE
D
49
67.837
−26.618
−0.311
1.00
45.66
C


ATOM
3224
C
ILE
D
49
67.497
−23.813
−0.475
1.00
46.86
C


ATOM
3225
O
ILE
D
49
66.993
−23.579
−1.580
1.00
46.20
O


ATOM
3226
N
SER
D
50
68.714
−23.400
−0.154
1.00
48.31
N


ATOM
3227
CA
SER
D
50
69.582
−22.795
−1.161
1.00
50.07
C


ATOM
3228
CB
SER
D
50
70.610
−21.875
−0.521
1.00
49.69
C


ATOM
3229
OG
SER
D
50
69.966
−20.656
−0.222
1.00
51.30
O


ATOM
3230
C
SER
D
50
70.259
−23.905
−1.918
1.00
50.54
C


ATOM
3231
O
SER
D
50
70.853
−24.804
−1.304
1.00
50.91
O


ATOM
3232
N
ILE
D
51
70.136
−23.854
−3.247
1.00
51.03
N


ATOM
3233
CA
ILE
D
51
70.803
−24.826
−4.120
1.00
50.47
C


ATOM
3234
CB
ILE
D
51
70.134
−24.926
−5.529
1.00
50.18
C


ATOM
3235
CG1
ILE
D
51
68.659
−25.348
−5.394
1.00
49.97
C


ATOM
3236
CD1
ILE
D
51
68.424
−26.692
−4.703
1.00
47.26
C


ATOM
3237
CG2
ILE
D
51
70.886
−25.890
−6.438
1.00
50.01
C


ATOM
3238
C
ILE
D
51
72.267
−24.464
−4.162
1.00
50.13
C


ATOM
3239
O
ILE
D
51
72.621
−23.304
−4.390
1.00
51.21
O


ATOM
3240
N
GLY
D
52
73.112
−25.450
−3.903
1.00
49.83
N


ATOM
3241
CA
GLY
D
52
74.537
−25.220
−3.804
1.00
49.62
C


ATOM
3242
C
GLY
D
52
75.198
−26.276
−2.957
1.00
49.66
C


ATOM
3243
O
GLY
D
52
74.639
−26.711
−1.948
1.00
50.36
O


ATOM
3244
N
GLY
D
53
76.371
−26.698
−3.407
1.00
49.38
N


ATOM
3245
CA
GLY
D
53
77.253
−27.612
−2.696
1.00
49.23
C


ATOM
3246
C
GLY
D
53
76.697
−29.008
−2.480
1.00
49.36
C


ATOM
3247
O
GLY
D
53
76.756
−29.935
−3.362
1.00
49.29
O


ATOM
3248
N
ARG
D
54
76.120
−29.151
−1.269
1.00
49.43
N


ATOM
3249
CA
ARG
D
54
75.465
−30.394
−0.907
1.00
49.74
C


ATOM
3250
CB
ARG
D
54
75.282
−30.480
0.624
1.00
49.32
C


ATOM
3251
CG
ARG
D
54
76.280
−31.418
1.274
1.00
50.69
C


ATOM
3252
CD
ARG
D
54
76.661
−31.101
2.722
1.00
50.07
C


ATOM
3253
NE
ARG
D
54
75.585
−30.643
3.597
1.00
48.37
N


ATOM
3254
CZ
ARG
D
54
74.591
−31.392
4.086
1.00
49.71
C


ATOM
3255
NH1
ARG
D
54
74.447
−32.683
3.773
1.00
49.71
N


ATOM
3256
NH2
ARG
D
54
73.710
−30.832
4.899
1.00
47.05
N


ATOM
3257
C
ARG
D
54
74.141
−30.581
−1.660
1.00
49.58
C


ATOM
3258
O
ARG
D
54
73.723
−31.708
−1.911
1.00
50.26
O


ATOM
3259
N
TYR
D
55
73.485
−29.486
−2.017
1.00
49.51
N


ATOM
3260
CA
TYR
D
55
72.126
−29.555
−2.579
1.00
49.79
C


ATOM
3261
CB
TYR
D
55
71.193
−28.546
−1.877
1.00
49.87
C


ATOM
3262
CG
TYR
D
55
71.207
−28.685
−0.366
1.00
50.16
C


ATOM
3263
CD1
TYR
D
55
72.286
−28.218
0.368
1.00
50.07
C


ATOM
3264
CE1
TYR
D
55
72.336
−28.353
1.725
1.00
51.90
C


ATOM
3265
CZ
TYR
D
55
71.290
−28.965
2.417
1.00
52.02
C


ATOM
3266
OH
TYR
D
55
71.409
−29.070
3.799
1.00
51.10
O


ATOM
3267
CE2
TYR
D
55
70.183
−29.449
1.720
1.00
50.23
C


ATOM
3268
CD2
TYR
D
55
70.158
−29.306
0.317
1.00
48.86
C


ATOM
3269
C
TYR
D
55
72.155
−29.335
−4.089
1.00
49.96
C


ATOM
3270
O
TYR
D
55
72.233
−28.193
−4.549
1.00
49.02
O


ATOM
3271
N
VAL
D
56
72.139
−30.445
−4.840
1.00
50.10
N


ATOM
3272
CA
VAL
D
56
72.158
−30.378
−6.319
1.00
50.02
C


ATOM
3273
CB
VAL
D
56
73.128
−31.484
−6.945
1.00
49.66
C


ATOM
3274
CG1
VAL
D
56
72.672
−31.803
−8.492
1.00
49.55
C


ATOM
3275
CG2
VAL
D
56
74.716
−31.073
−6.641
1.00
50.23
C


ATOM
3276
C
VAL
D
56
70.703
−30.509
−6.834
1.00
50.01
C


ATOM
3277
O
VAL
D
56
69.996
−31.474
−6.542
1.00
50.57
O


ATOM
3278
N
GLU
D
57
70.240
−29.514
−7.565
1.00
50.47
N


ATOM
3279
CA
GLU
D
57
68.959
−29.637
−8.261
1.00
50.96
C


ATOM
3280
CB
GLU
D
57
68.069
−28.432
−8.002
1.00
49.91
C


ATOM
3281
CG
GLU
D
57
66.785
−28.464
−8.792
1.00
48.91
C


ATOM
3282
CD
GLU
D
57
65.896
−27.281
−8.499
1.00
46.98
C


ATOM
3283
OE1
GLU
D
57
66.400
−26.213
−8.111
1.00
46.14
O


ATOM
3284
OE2
GLU
D
57
64.670
−27.425
−8.644
1.00
49.35
O


ATOM
3285
C
GLU
D
57
69.192
−29.777
−9.755
1.00
51.88
C


ATOM
3286
O
GLU
D
57
70.071
−29.125
−10.302
1.00
52.11
O


ATOM
3287
N
THR
D
58
68.414
−30.645
−10.396
1.00
53.11
N


ATOM
3288
CA
THR
D
58
68.383
−30.727
−11.854
1.00
54.42
C


ATOM
3289
CB
THR
D
58
69.137
−31.978
−12.403
1.00
54.38
C


ATOM
3290
OG1
THR
D
58
68.449
−33.205
−11.829
1.00
56.17
O


ATOM
3291
CG2
THR
D
58
70.734
−31.924
−12.037
1.00
55.32
C


ATOM
3292
C
THR
D
58
66.896
−30.691
−12.250
1.00
55.02
C


ATOM
3293
O
THR
D
58
66.072
−31.406
−11.670
1.00
55.11
O


ATOM
3294
N
VAL
D
59
66.577
−29.813
−13.219
1.00
55.68
N


ATOM
3295
CA
VAL
D
59
65.203
−29.468
−13.615
1.00
55.90
C


ATOM
3296
CB
VAL
D
59
64.926
−27.955
−13.378
1.00
55.61
C


ATOM
3297
CG1
VAL
D
59
64.629
−27.687
−11.961
1.00
55.58
C


ATOM
3298
CG2
VAL
D
59
66.144
−27.115
−13.745
1.00
57.13
C


ATOM
3299
C
VAL
D
59
64.991
−29.817
−15.100
1.00
56.39
C


ATOM
3300
O
VAL
D
59
65.863
−29.553
−15.950
1.00
55.93
O


ATOM
3301
N
ASN
D
60
63.840
−30.415
−15.410
1.00
56.80
N


ATOM
3302
CA
ASN
D
60
63.549
−30.882
−16.774
1.00
56.63
C


ATOM
3303
CB
ASN
D
60
63.691
−32.413
−16.873
1.00
56.38
C


ATOM
3304
CG
ASN
D
60
64.099
−32.854
−18.348
1.00
57.37
C


ATOM
3305
OD1
ASN
D
60
65.090
−33.646
−18.466
1.00
56.92
O


ATOM
3306
ND2
ASN
D
60
63.351
−32.354
−19.408
1.00
55.67
N


ATOM
3307
C
ASN
D
60
62.172
−30.461
−17.310
1.00
56.88
C


ATOM
3308
O
ASN
D
60
61.252
−31.423
−17.192
1.00
56.87
O


ATOM
3309
N
LYS
D
61
62.032
−28.997
−17.392
1.00
57.33
N


ATOM
3310
CA
LYS
D
61
60.747
−28.473
−17.883
1.00
57.81
C


ATOM
3311
CB
LYS
D
61
60.891
−26.968
−18.145
1.00
58.40
C


ATOM
3312
CG
LYS
D
61
59.597
−26.259
−18.597
1.00
59.54
C


ATOM
3313
CD
LYS
D
61
59.929
−25.060
−19.492
1.00
61.86
C


ATOM
3314
CE
LYS
D
61
58.690
−24.361
−20.096
1.00
61.96
C


ATOM
3315
NZ
LYS
D
61
58.446
−23.001
−19.525
1.00
62.65
N


ATOM
3316
C
LYS
D
61
60.212
−29.215
−19.141
1.00
57.89
C


ATOM
3317
O
LYS
D
61
58.997
−29.366
−19.309
1.00
58.21
O


ATOM
3318
N
GLY
D
62
61.122
−29.693
−20.002
1.00
57.58
N


ATOM
3319
CA
GLY
D
62
60.761
−30.486
−21.186
1.00
57.06
C


ATOM
3320
C
GLY
D
62
60.000
−31.791
−20.907
1.00
56.82
C


ATOM
3321
O
GLY
D
62
59.381
−32.386
−21.864
1.00
57.25
O


ATOM
3322
N
SER
D
63
60.060
−32.244
−19.594
1.00
55.97
N


ATOM
3323
CA
SER
D
63
59.302
−33.409
−19.125
1.00
54.90
C


ATOM
3324
CB
SER
D
63
60.272
−34.621
−18.908
1.00
55.09
C


ATOM
3325
OG
SER
D
63
60.645
−34.692
−17.338
1.00
54.74
O


ATOM
3326
C
SER
D
63
58.474
−33.104
−17.762
1.00
53.75
C


ATOM
3327
O
SER
D
63
57.786
−34.003
−17.034
1.00
53.64
O


ATOM
3328
N
LYS
D
64
58.533
−31.834
−17.394
1.00
52.95
N


ATOM
3329
CA
LYS
D
64
57.857
−31.310
−16.167
1.00
52.47
C


ATOM
3330
CB
LYS
D
64
56.344
−31.240
−16.372
1.00
52.40
C


ATOM
3331
CG
LYS
D
64
55.971
−29.890
−17.112
1.00
53.07
C


ATOM
3332
CD
LYS
D
64
54.977
−30.113
−18.294
1.00
53.84
C


ATOM
3333
CE
LYS
D
64
53.558
−30.322
−17.603
1.00
53.96
C


ATOM
3334
NZ
LYS
D
64
52.517
−30.001
−18.618
1.00
51.87
N


ATOM
3335
C
LYS
D
64
58.301
−31.907
−14.795
1.00
51.17
C


ATOM
3336
O
LYS
D
64
57.603
−31.826
−13.761
1.00
51.55
O


ATOM
3337
N
SER
D
65
59.517
−32.439
−14.827
1.00
49.79
N


ATOM
3338
CA
SER
D
65
60.167
−33.103
−13.708
1.00
49.92
C


ATOM
3339
CB
SER
D
65
60.834
−34.407
−14.213
1.00
49.55
C


ATOM
3340
OG
SER
D
65
61.759
−34.932
−13.248
1.00
53.24
O


ATOM
3341
C
SER
D
65
61.234
−32.168
−13.120
1.00
49.16
C


ATOM
3342
O
SER
D
65
61.838
−31.333
−13.866
1.00
48.96
O


ATOM
3343
N
PHE
D
66
61.437
−32.304
−11.802
1.00
47.24
N


ATOM
3344
CA
PHE
D
66
62.543
−31.670
−11.066
1.00
46.15
C


ATOM
3345
CB
PHE
D
66
62.277
−30.171
−10.826
1.00
44.90
C


ATOM
3346
CG
PHE
D
66
61.128
−29.867
−9.891
1.00
44.59
C


ATOM
3347
CD1
PHE
D
66
59.801
−29.989
−10.317
1.00
42.09
C


ATOM
3348
CE1
PHE
D
66
58.738
−29.686
−9.470
1.00
41.74
C


ATOM
3349
CZ
PHE
D
66
58.997
−29.224
−8.170
1.00
42.61
C


ATOM
3350
CE2
PHE
D
66
60.315
−29.087
−7.722
1.00
43.21
C


ATOM
3351
CD2
PHE
D
66
61.376
−29.410
−8.586
1.00
44.86
C


ATOM
3352
C
PHE
D
66
62.988
−32.439
−9.769
1.00
45.82
C


ATOM
3353
O
PHE
D
66
62.222
−33.197
−9.181
1.00
46.26
O


ATOM
3354
N
SER
D
67
64.238
−32.257
−9.351
1.00
45.70
N


ATOM
3355
CA
SER
D
67
64.862
−33.149
−8.367
1.00
45.45
C


ATOM
3356
CB
SER
D
67
65.603
−34.242
−9.113
1.00
45.90
C


ATOM
3357
OG
SER
D
67
64.734
−35.335
−9.256
1.00
47.19
O


ATOM
3358
C
SER
D
67
65.871
−32.497
−7.455
1.00
45.20
C


ATOM
3359
O
SER
D
67
66.655
−31.642
−7.902
1.00
46.01
O


ATOM
3360
N
LEU
D
68
65.872
−32.930
−6.196
1.00
44.54
N


ATOM
3361
CA
LEU
D
68
66.855
−32.507
−5.212
1.00
44.12
C


ATOM
3362
CB
LEU
D
68
66.203
−31.902
−3.968
1.00
43.76
C


ATOM
3363
CG
LEU
D
68
66.799
−30.640
−3.315
1.00
44.66
C


ATOM
3364
CD1
LEU
D
68
66.693
−30.684
−1.812
1.00
45.00
C


ATOM
3365
CD2
LEU
D
68
68.213
−30.336
−3.739
1.00
41.15
C


ATOM
3366
C
LEU
D
68
67.653
−33.717
−4.766
1.00
43.76
C


ATOM
3367
O
LEU
D
68
67.095
−34.701
−4.302
1.00
41.85
O


ATOM
3368
N
ARG
D
69
68.966
−33.629
−4.920
1.00
44.26
N


ATOM
3369
CA
ARG
D
69
69.873
−34.621
−4.383
1.00
45.51
C


ATOM
3370
CB
ARG
D
69
70.817
−35.147
−5.493
1.00
44.78
C


ATOM
3371
CG
ARG
D
69
71.578
−36.356
−5.011
1.00
47.38
C


ATOM
3372
CD
ARG
D
69
72.519
−36.978
−6.039
1.00
50.01
C


ATOM
3373
NE
ARG
D
69
73.038
−38.236
−5.447
1.00
64.56
N


ATOM
3374
CZ
ARG
D
69
74.278
−38.371
−4.916
1.00
70.54
C


ATOM
3375
NH1
ARG
D
69
75.200
−37.308
−4.958
1.00
70.65
N


ATOM
3376
NH2
ARG
D
69
74.628
−39.585
−4.368
1.00
70.40
N


ATOM
3377
C
ARG
D
69
70.647
−33.877
−3.316
1.00
44.18
C


ATOM
3378
O
ARG
D
69
71.228
−32.821
−3.583
1.00
45.88
O


ATOM
3379
N
ILE
D
70
70.611
−34.393
−2.100
1.00
44.15
N


ATOM
3380
CA
ILE
D
70
71.400
−33.865
−1.004
1.00
43.11
C


ATOM
3381
CB
ILE
D
70
70.560
−33.577
0.247
1.00
43.37
C


ATOM
3382
CG1
ILE
D
70
69.343
−32.713
−0.092
1.00
40.96
C


ATOM
3383
CD1
ILE
D
70
68.184
−33.028
0.730
1.00
43.95
C


ATOM
3384
CG2
ILE
D
70
71.443
−32.879
1.306
1.00
43.28
C


ATOM
3385
C
ILE
D
70
72.431
−34.947
−0.699
1.00
43.35
C


ATOM
3386
O
ILE
D
70
72.072
−36.079
−0.404
1.00
42.77
O


ATOM
3387
N
SER
D
71
73.707
−34.619
−0.851
1.00
43.10
N


ATOM
3388
CA
SER
D
71
74.735
−35.597
−0.571
1.00
43.65
C


ATOM
3389
CB
SER
D
71
75.794
−35.590
−1.669
1.00
43.42
C


ATOM
3390
OG
SER
D
71
76.168
−34.259
−1.929
1.00
44.36
O


ATOM
3391
C
SER
D
71
75.306
−35.317
0.817
1.00
43.63
C


ATOM
3392
O
SER
D
71
74.923
−34.309
1.447
1.00
44.14
O


ATOM
3393
N
ASP
D
72
76.156
−36.232
1.309
1.00
43.29
N


ATOM
3394
CA
ASP
D
72
76.858
−36.065
2.582
1.00
42.35
C


ATOM
3395
CB
ASP
D
72
77.912
−34.951
2.458
1.00
42.24
C


ATOM
3396
CG
ASP
D
72
78.973
−35.012
3.572
1.00
44.75
C


ATOM
3397
OD1
ASP
D
72
78.995
−36.012
4.344
1.00
42.13
O


ATOM
3398
OD2
ASP
D
72
79.800
−34.057
3.659
1.00
47.88
O


ATOM
3399
C
ASP
D
72
75.880
−35.777
3.746
1.00
41.01
C


ATOM
3400
O
ASP
D
72
75.935
−34.731
4.394
1.00
40.46
O


ATOM
3401
N
LEU
D
73
74.982
−36.713
4.003
1.00
40.43
N


ATOM
3402
CA
LEU
D
73
73.915
−36.470
4.965
1.00
39.98
C


ATOM
3403
CB
LEU
D
73
72.761
−37.447
4.752
1.00
40.03
C


ATOM
3404
CG
LEU
D
73
71.891
−37.260
3.493
1.00
38.61
C


ATOM
3405
CD1
LEU
D
73
70.971
−38.462
3.446
1.00
37.16
C


ATOM
3406
CD2
LEU
D
73
71.094
−36.006
3.576
1.00
38.44
C


ATOM
3407
C
LEU
D
73
74.409
−36.458
6.424
1.00
39.77
C


ATOM
3408
O
LEU
D
73
75.344
−37.149
6.802
1.00
38.86
O


ATOM
3409
N
ARG
D
74
73.784
−35.600
7.214
1.00
40.34
N


ATOM
3410
CA
ARG
D
74
74.125
−35.418
8.616
1.00
40.91
C


ATOM
3411
CB
ARG
D
74
74.711
−34.024
8.803
1.00
41.22
C


ATOM
3412
CG
ARG
D
74
75.561
−33.574
7.623
1.00
44.83
C


ATOM
3413
CD
ARG
D
74
76.259
−32.276
7.888
1.00
51.37
C


ATOM
3414
NE
ARG
D
74
75.309
−31.193
8.146
1.00
55.28
N


ATOM
3415
CZ
ARG
D
74
75.645
−30.008
8.662
1.00
56.79
C


ATOM
3416
NH1
ARG
D
74
76.913
−29.758
8.987
1.00
55.96
N


ATOM
3417
NH2
ARG
D
74
74.711
−29.079
8.868
1.00
56.56
N


ATOM
3418
C
ARG
D
74
72.820
−35.563
9.406
1.00
40.45
C


ATOM
3419
O
ARG
D
74
71.735
−35.292
8.851
1.00
40.13
O


ATOM
3420
N
VAL
D
75
72.901
−36.003
10.663
1.00
39.63
N


ATOM
3421
CA
VAL
D
75
71.700
−36.030
11.512
1.00
40.06
C


ATOM
3422
CB
VAL
D
75
71.970
−36.527
12.963
1.00
39.68
C


ATOM
3423
CG1
VAL
D
75
72.504
−37.923
12.939
1.00
37.56
C


ATOM
3424
CG2
VAL
D
75
72.893
−35.615
13.685
1.00
41.38
C


ATOM
3425
C
VAL
D
75
70.872
−34.702
11.509
1.00
40.03
C


ATOM
3426
O
VAL
D
75
69.652
−34.750
11.502
1.00
40.31
O


ATOM
3427
N
GLU
D
76
71.516
−33.534
11.474
1.00
39.38
N


ATOM
3428
CA
GLU
D
76
70.783
−32.267
11.413
1.00
38.58
C


ATOM
3429
CB
GLU
D
76
71.704
−31.072
11.643
1.00
39.43
C


ATOM
3430
CG
GLU
D
76
73.155
−31.300
11.253
1.00
43.81
C


ATOM
3431
CD
GLU
D
76
73.899
−32.091
12.300
1.00
49.07
C


ATOM
3432
OE1
GLU
D
76
74.410
−33.201
12.002
1.00
50.38
O


ATOM
3433
OE2
GLU
D
76
73.963
−31.604
13.445
1.00
53.73
O


ATOM
3434
C
GLU
D
76
70.012
−32.038
10.113
1.00
37.13
C


ATOM
3435
O
GLU
D
76
69.328
−31.018
9.981
1.00
36.46
O


ATOM
3436
N
ASP
D
77
70.139
−32.955
9.156
1.00
35.88
N


ATOM
3437
CA
ASP
D
77
69.302
−32.934
7.896
1.00
35.98
C


ATOM
3438
CB
ASP
D
77
69.995
−33.640
6.719
1.00
35.29
C


ATOM
3439
CG
ASP
D
77
71.259
−32.944
6.258
1.00
36.12
C


ATOM
3440
OD1
ASP
D
77
71.314
−31.707
6.247
1.00
34.87
O


ATOM
3441
OD2
ASP
D
77
72.200
−33.674
5.890
1.00
39.60
O


ATOM
3442
C
ASP
D
77
67.933
−33.626
8.022
1.00
35.40
C


ATOM
3443
O
ASP
D
77
67.106
−33.451
7.146
1.00
35.70
O


ATOM
3444
N
SER
D
78
67.740
−34.480
9.027
1.00
34.77
N


ATOM
3445
CA
SER
D
78
66.422
−34.981
9.345
1.00
35.45
C


ATOM
3446
CB
SER
D
78
66.473
−35.750
10.659
1.00
35.78
C


ATOM
3447
OG
SER
D
78
67.436
−36.770
10.546
1.00
36.74
O


ATOM
3448
C
SER
D
78
65.321
−33.899
9.393
1.00
35.23
C


ATOM
3449
O
SER
D
78
65.471
−32.828
10.038
1.00
35.34
O


ATOM
3450
N
GLY
D
79
64.210
−34.192
8.716
1.00
33.82
N


ATOM
3451
CA
GLY
D
79
63.078
−33.271
8.649
1.00
34.33
C


ATOM
3452
C
GLY
D
79
62.191
−33.603
7.481
1.00
35.45
C


ATOM
3453
O
GLY
D
79
62.404
−34.627
6.767
1.00
36.59
O


ATOM
3454
N
THR
D
80
61.239
−32.707
7.242
1.00
36.95
N


ATOM
3455
CA
THR
D
80
60.265
−32.773
6.142
1.00
37.81
C


ATOM
3456
CB
THR
D
80
58.812
−32.455
6.589
1.00
37.21
C


ATOM
3457
OG1
THR
D
80
58.540
−33.092
7.845
1.00
42.51
O


ATOM
3458
CG2
THR
D
80
57.794
−32.957
5.599
1.00
36.93
C


ATOM
3459
C
THR
D
80
60.658
−31.822
5.030
1.00
39.38
C


ATOM
3460
O
THR
D
80
60.734
−30.616
5.253
1.00
39.45
O


ATOM
3461
N
TYR
D
81
60.882
−32.394
3.835
1.00
39.69
N


ATOM
3462
CA
TYR
D
81
61.244
−31.683
2.641
1.00
40.11
C


ATOM
3463
CB
TYR
D
81
62.433
−32.367
1.967
1.00
40.22
C


ATOM
3464
CG
TYR
D
81
63.719
−32.354
2.802
1.00
39.55
C


ATOM
3465
CD1
TYR
D
81
64.755
−31.515
2.468
1.00
39.29
C


ATOM
3466
CE1
TYR
D
81
65.935
−31.489
3.213
1.00
39.91
C


ATOM
3467
CZ
TYR
D
81
66.087
−32.315
4.305
1.00
40.52
C


ATOM
3468
OH
TYR
D
81
67.291
−32.242
5.010
1.00
39.06
O


ATOM
3469
CE2
TYR
D
81
65.066
−33.175
4.655
1.00
37.99
C


ATOM
3470
CD2
TYR
D
81
63.892
−33.194
3.897
1.00
38.47
C


ATOM
3471
C
TYR
D
81
60.064
−31.621
1.693
1.00
40.88
C


ATOM
3472
O
TYR
D
81
59.242
−32.572
1.577
1.00
42.06
O


ATOM
3473
N
LYS
D
82
59.925
−30.469
1.063
1.00
41.23
N


ATOM
3474
CA
LYS
D
82
58.819
−30.189
0.172
1.00
41.95
C


ATOM
3475
CB
LYS
D
82
57.779
−29.315
0.863
1.00
42.23
C


ATOM
3476
CG
LYS
D
82
56.447
−30.008
1.156
1.00
46.06
C


ATOM
3477
CD
LYS
D
82
55.949
−29.607
2.549
1.00
53.37
C


ATOM
3478
CE
LYS
D
82
54.875
−30.528
3.091
1.00
51.30
C


ATOM
3479
NZ
LYS
D
82
53.540
−30.122
2.613
1.00
50.40
N


ATOM
3480
C
LYS
D
82
59.381
−29.472
−1.028
1.00
42.24
C


ATOM
3481
O
LYS
D
82
60.236
−28.607
−0.899
1.00
41.51
O


ATOM
3482
N
CYS
D
83
58.912
−29.863
−2.207
1.00
43.47
N


ATOM
3483
CA
CYS
D
83
59.163
−29.117
−3.400
1.00
44.82
C


ATOM
3484
CB
CYS
D
83
59.474
−30.038
−4.564
1.00
45.49
C


ATOM
3485
SG
CYS
D
83
58.161
−31.141
−4.953
1.00
44.99
S


ATOM
3486
C
CYS
D
83
57.923
−28.295
−3.711
1.00
45.88
C


ATOM
3487
O
CYS
D
83
56.827
−28.610
−3.259
1.00
46.33
O


ATOM
3488
N
GLN
D
84
58.132
−27.220
−4.465
1.00
46.29
N


ATOM
3489
CA
GLN
D
84
57.058
−26.400
−5.007
1.00
45.80
C


ATOM
3490
CB
GLN
D
84
56.949
−25.084
−4.280
1.00
46.07
C


ATOM
3491
CG
GLN
D
84
55.811
−24.290
−4.826
1.00
47.89
C


ATOM
3492
CD
GLN
D
84
55.202
−23.369
−3.835
1.00
50.52
C


ATOM
3493
OE1
GLN
D
84
54.030
−23.056
−3.953
1.00
54.26
O


ATOM
3494
NE2
GLN
D
84
55.991
−22.898
−2.861
1.00
50.71
N


ATOM
3495
C
GLN
D
84
57.352
−26.107
−6.466
1.00
44.92
C


ATOM
3496
O
GLN
D
84
58.466
−25.756
−6.822
1.00
44.76
O


ATOM
3497
N
ALA
D
85
56.328
−26.309
−7.271
1.00
44.45
N


ATOM
3498
CA
ALA
D
85
56.287
−26.074
−8.693
1.00
44.03
C


ATOM
3499
CB
ALA
D
85
55.513
−27.178
−9.330
1.00
43.73
C


ATOM
3500
C
ALA
D
85
55.581
−24.740
−8.953
1.00
44.64
C


ATOM
3501
O
ALA
D
85
54.506
−24.480
−8.398
1.00
45.56
O


ATOM
3502
N
PHE
D
86
56.179
−23.900
−9.797
1.00
44.70
N


ATOM
3503
CA
PHE
D
86
55.646
−22.570
−10.110
1.00
43.77
C


ATOM
3504
CB
PHE
D
86
56.662
−21.505
−9.755
1.00
43.68
C


ATOM
3505
CG
PHE
D
86
56.899
−21.325
−8.234
1.00
43.64
C


ATOM
3506
CD1
PHE
D
86
58.108
−21.734
−7.644
1.00
39.50
C


ATOM
3507
CE1
PHE
D
86
58.352
−21.536
−6.258
1.00
41.98
C


ATOM
3508
CZ
PHE
D
86
57.392
−20.906
−5.466
1.00
43.10
C


ATOM
3509
CE2
PHE
D
86
56.164
−20.469
−6.060
1.00
42.82
C


ATOM
3510
CD2
PHE
D
86
55.936
−20.693
−7.427
1.00
42.57
C


ATOM
3511
C
PHE
D
86
55.284
−22.518
−11.581
1.00
43.35
C


ATOM
3512
O
PHE
D
86
56.047
−22.948
−12.451
1.00
43.61
O


ATOM
3513
N
TYR
D
87
54.071
−22.067
−11.860
1.00
43.20
N


ATOM
3514
CA
TYR
D
87
53.528
−22.118
−13.225
1.00
42.85
C


ATOM
3515
CB
TYR
D
87
52.706
−23.392
−13.419
1.00
42.88
C


ATOM
3516
CG
TYR
D
87
51.616
−23.570
−12.381
1.00
43.24
C


ATOM
3517
CD1
TYR
D
87
50.361
−23.023
−12.574
1.00
41.66
C


ATOM
3518
CE1
TYR
D
87
49.378
−23.166
−11.626
1.00
43.81
C


ATOM
3519
CZ
TYR
D
87
49.645
−23.855
−10.456
1.00
42.83
C


ATOM
3520
OH
TYR
D
87
48.635
−23.981
−9.495
1.00
45.90
O


ATOM
3521
CE2
TYR
D
87
50.879
−24.412
−10.260
1.00
40.71
C


ATOM
3522
CD2
TYR
D
87
51.849
−24.270
−11.203
1.00
41.31
C


ATOM
3523
C
TYR
D
87
52.678
−20.887
−13.442
1.00
42.38
C


ATOM
3524
O
TYR
D
87
52.341
−20.184
−12.479
1.00
41.90
O


ATOM
3525
N
VAL
D
88
52.328
−20.625
−14.690
1.00
42.33
N


ATOM
3526
CA
VAL
D
88
51.484
−19.482
−15.014
1.00
42.91
C


ATOM
3527
CB
VAL
D
88
52.241
−18.322
−15.725
1.00
42.23
C


ATOM
3528
CG1
VAL
D
88
52.648
−18.693
−17.134
1.00
42.89
C


ATOM
3529
CG2
VAL
D
88
53.461
−17.852
−14.923
1.00
42.15
C


ATOM
3530
C
VAL
D
88
50.343
−20.009
−15.861
1.00
43.65
C


ATOM
3531
O
VAL
D
88
50.483
−21.016
−16.523
1.00
44.60
O


ATOM
3532
N
PHE
D
89
49.204
−19.351
−15.789
1.00
44.07
N


ATOM
3533
CA
PHE
D
89
48.019
−19.716
−16.558
1.00
44.21
C


ATOM
3534
CB
PHE
D
89
47.186
−20.807
−15.865
1.00
43.34
C


ATOM
3535
CG
PHE
D
89
46.719
−20.466
−14.459
1.00
42.59
C


ATOM
3536
CD1
PHE
D
89
45.427
−19.948
−14.236
1.00
42.34
C


ATOM
3537
CE1
PHE
D
89
44.978
−19.651
−12.942
1.00
41.00
C


ATOM
3538
CZ
PHE
D
89
45.828
−19.873
−11.839
1.00
41.21
C


ATOM
3539
CE2
PHE
D
89
47.115
−20.389
−12.048
1.00
40.99
C


ATOM
3540
CD2
PHE
D
89
47.547
−20.683
−13.358
1.00
39.83
C


ATOM
3541
C
PHE
D
89
47.258
−18.419
−16.699
1.00
45.29
C


ATOM
3542
O
PHE
D
89
47.586
−17.446
−16.012
1.00
44.92
O


ATOM
3543
N
PHE
D
90
46.278
−18.379
−17.594
1.00
46.60
N


ATOM
3544
CA
PHE
D
90
45.525
−17.166
−17.790
1.00
47.84
C


ATOM
3545
CB
PHE
D
90
45.113
−17.033
−19.229
1.00
49.12
C


ATOM
3546
CG
PHE
D
90
46.217
−16.590
−20.135
1.00
52.21
C


ATOM
3547
CD1
PHE
D
90
46.291
−15.259
−20.561
1.00
55.64
C


ATOM
3548
CE1
PHE
D
90
47.315
−14.828
−21.443
1.00
57.08
C


ATOM
3549
CZ
PHE
D
90
48.263
−15.751
−21.908
1.00
55.59
C


ATOM
3550
CE2
PHE
D
90
48.194
−17.095
−21.480
1.00
57.82
C


ATOM
3551
CD2
PHE
D
90
47.171
−17.503
−20.596
1.00
55.72
C


ATOM
3552
C
PHE
D
90
44.331
−17.079
−16.865
1.00
47.66
C


ATOM
3553
O
PHE
D
90
43.697
−18.071
−16.572
1.00
46.94
O


ATOM
3554
N
ALA
D
91
44.053
−15.867
−16.398
1.00
48.49
N


ATOM
3555
CA
ALA
D
91
42.982
−15.599
−15.447
1.00
49.73
C


ATOM
3556
CB
ALA
D
91
42.942
−14.112
−15.129
1.00
48.83
C


ATOM
3557
C
ALA
D
91
41.632
−16.093
−15.969
1.00
51.41
C


ATOM
3558
O
ALA
D
91
40.799
−16.593
−15.209
1.00
51.12
O


ATOM
3559
N
GLU
D
92
41.441
−15.964
−17.282
1.00
53.68
N


ATOM
3560
CA
GLU
D
92
40.229
−16.427
−17.962
1.00
56.07
C


ATOM
3561
CB
GLU
D
92
40.134
−15.798
−19.358
1.00
56.18
C


ATOM
3562
CG
GLU
D
92
40.983
−16.517
−20.403
1.00
57.25
C


ATOM
3563
CD
GLU
D
92
41.361
−15.626
−21.547
1.00
59.32
C


ATOM
3564
OE1
GLU
D
92
42.579
−15.479
−21.797
1.00
59.13
O


ATOM
3565
OE2
GLU
D
92
40.441
−15.065
−22.189
1.00
60.55
O


ATOM
3566
C
GLU
D
92
40.105
−17.952
−18.095
1.00
57.18
C


ATOM
3567
O
GLU
D
92
39.052
−18.416
−18.520
1.00
57.56
O


ATOM
3568
N
ASP
D
93
41.171
−18.709
−17.789
1.00
58.82
N


ATOM
3569
CA
ASP
D
93
41.110
−20.181
−17.684
1.00
60.41
C


ATOM
3570
CB
ASP
D
93
42.458
−20.800
−17.271
1.00
60.06
C


ATOM
3571
CG
ASP
D
93
42.370
−22.306
−16.993
1.00
62.32
C


ATOM
3572
OD1
ASP
D
93
43.088
−22.798
−16.075
1.00
63.69
O


ATOM
3573
OD2
ASP
D
93
41.580
−23.010
−17.680
1.00
63.08
O


ATOM
3574
C
ASP
D
93
39.992
−20.523
−16.698
1.00
61.55
C


ATOM
3575
O
ASP
D
93
40.234
−20.746
−15.495
1.00
61.84
O


ATOM
3576
N
VAL
D
94
38.775
−20.549
−17.266
1.00
62.79
N


ATOM
3577
CA
VAL
D
94
37.473
−20.563
−16.567
1.00
63.66
C


ATOM
3578
CB
VAL
D
94
36.302
−20.047
−17.526
1.00
63.67
C


ATOM
3579
CG1
VAL
D
94
35.125
−19.424
−16.748
1.00
63.68
C


ATOM
3580
CG2
VAL
D
94
35.843
−21.115
−18.522
1.00
63.79
C


ATOM
3581
C
VAL
D
94
37.238
−21.948
−15.970
1.00
64.13
C


ATOM
3582
O
VAL
D
94
38.119
−22.810
−16.078
1.00
64.47
O


ATOM
3583
N
GLY
D
95
36.089
−22.145
−15.317
1.00
64.40
N


ATOM
3584
CA
GLY
D
95
35.774
−23.376
−14.568
1.00
64.71
C


ATOM
3585
C
GLY
D
95
36.866
−24.412
−14.294
1.00
65.01
C


ATOM
3586
O
GLY
D
95
36.569
−25.624
−14.258
1.00
65.10
O


ATOM
3587
N
SER
D
96
38.110
−23.954
−14.083
1.00
65.03
N


ATOM
3588
CA
SER
D
96
39.264
−24.858
−13.891
1.00
65.03
C


ATOM
3589
CB
SER
D
96
40.390
−24.533
−14.887
1.00
65.25
C


ATOM
3590
OG
SER
D
96
41.339
−25.594
−14.955
1.00
64.98
O


ATOM
3591
C
SER
D
96
39.806
−24.852
−12.454
1.00
64.82
C


ATOM
3592
O
SER
D
96
40.023
−23.779
−11.867
1.00
65.31
O


ATOM
3593
N
ASN
D
97
40.052
−26.057
−11.928
1.00
63.87
N


ATOM
3594
CA
ASN
D
97
40.392
−26.313
−10.521
1.00
62.98
C


ATOM
3595
CB
ASN
D
97
39.702
−27.644
−10.104
1.00
63.42
C


ATOM
3596
CG
ASN
D
97
39.953
−28.045
−8.633
1.00
65.04
C


ATOM
3597
OD1
ASN
D
97
40.047
−27.190
−7.736
1.00
66.76
O


ATOM
3598
ND2
ASN
D
97
40.030
−29.363
−8.387
1.00
63.43
N


ATOM
3599
C
ASN
D
97
41.921
−26.317
−10.231
1.00
61.78
C


ATOM
3600
O
ASN
D
97
42.552
−27.385
−10.142
1.00
61.83
O


ATOM
3601
N
LYS
D
98
42.507
−25.129
−10.063
1.00
59.84
N


ATOM
3602
CA
LYS
D
98
43.970
−24.994
−9.904
1.00
58.24
C


ATOM
3603
CB
LYS
D
98
44.446
−23.620
−10.431
1.00
58.64
C


ATOM
3604
CG
LYS
D
98
44.251
−23.361
−11.938
1.00
57.61
C


ATOM
3605
CD
LYS
D
98
42.829
−22.926
−12.285
1.00
57.73
C


ATOM
3606
CE
LYS
D
98
42.248
−21.834
−11.301
1.00
59.29
C


ATOM
3607
NZ
LYS
D
98
41.046
−20.972
−12.134
1.00
57.74
N


ATOM
3608
C
LYS
D
98
44.493
−25.245
−8.461
1.00
57.13
C


ATOM
3609
O
LYS
D
98
43.767
−25.784
−7.606
1.00
57.08
O


ATOM
3610
N
GLY
D
99
45.767
−24.891
−8.225
1.00
55.60
N


ATOM
3611
CA
GLY
D
99
46.378
−24.754
−6.872
1.00
52.95
C


ATOM
3612
C
GLY
D
99
46.501
−23.279
−6.415
1.00
50.67
C


ATOM
3613
O
GLY
D
99
45.678
−22.440
−6.801
1.00
51.24
O


ATOM
3614
N
ALA
D
100
47.510
−22.956
−5.601
1.00
47.56
N


ATOM
3615
CA
ALA
D
100
47.594
−21.643
−4.932
1.00
44.47
C


ATOM
3616
CB
ALA
D
100
48.583
−21.700
−3.781
1.00
44.23
C


ATOM
3617
C
ALA
D
100
47.948
−20.493
−5.881
1.00
42.73
C


ATOM
3618
O
ALA
D
100
48.733
−20.692
−6.805
1.00
41.87
O


ATOM
3619
N
ILE
D
101
47.368
−19.313
−5.635
1.00
40.81
N


ATOM
3620
CA
ILE
D
101
47.614
−18.108
−6.395
1.00
40.35
C


ATOM
3621
CB
ILE
D
101
46.370
−17.176
−6.453
1.00
40.67
C


ATOM
3622
CG1
ILE
D
101
45.119
−17.901
−6.945
1.00
41.30
C


ATOM
3623
CD1
ILE
D
101
45.229
−18.533
−8.316
1.00
44.91
C


ATOM
3624
CG2
ILE
D
101
46.719
−15.835
−7.192
1.00
38.52
C


ATOM
3625
C
ILE
D
101
48.703
−17.316
−5.677
1.00
40.37
C


ATOM
3626
O
ILE
D
101
48.578
−17.042
−4.478
1.00
40.20
O


ATOM
3627
N
ILE
D
102
49.757
−16.950
−6.405
1.00
39.73
N


ATOM
3628
CA
ILE
D
102
50.891
−16.245
−5.850
1.00
38.51
C


ATOM
3629
CB
ILE
D
102
52.225
−16.834
−6.388
1.00
39.69
C


ATOM
3630
CG1
ILE
D
102
52.294
−18.341
−6.159
1.00
40.45
C


ATOM
3631
CD1
ILE
D
102
52.156
−18.810
−4.677
1.00
39.56
C


ATOM
3632
CG2
ILE
D
102
53.461
−16.084
−5.804
1.00
40.43
C


ATOM
3633
C
ILE
D
102
50.816
−14.788
−6.296
1.00
37.28
C


ATOM
3634
O
ILE
D
102
51.315
−13.893
−5.613
1.00
38.01
O


ATOM
3635
N
GLY
D
103
50.181
−14.539
−7.424
1.00
35.03
N


ATOM
3636
CA
GLY
D
103
50.172
−13.194
−7.991
1.00
33.31
C


ATOM
3637
C
GLY
D
103
49.411
−13.068
−9.275
1.00
32.34
C


ATOM
3638
O
GLY
D
103
49.072
−14.050
−9.924
1.00
31.10
O


ATOM
3639
N
LEU
D
104
49.098
−11.840
−9.621
1.00
32.17
N


ATOM
3640
CA
LEU
D
104
48.403
−11.557
−10.841
1.00
32.15
C


ATOM
3641
CB
LEU
D
104
46.965
−11.134
−10.534
1.00
33.36
C


ATOM
3642
CG
LEU
D
104
46.100
−10.577
−11.696
1.00
35.07
C


ATOM
3643
CD1
LEU
D
104
44.837
−9.947
−11.110
1.00
35.43
C


ATOM
3644
CD2
LEU
D
104
45.772
−11.706
−12.740
1.00
34.01
C


ATOM
3645
C
LEU
D
104
49.131
−10.472
−11.532
1.00
32.05
C


ATOM
3646
O
LEU
D
104
49.436
−9.462
−10.903
1.00
31.50
O


ATOM
3647
N
MET
D
105
49.419
−10.679
−12.826
1.00
31.71
N


ATOM
3648
CA
MET
D
105
50.112
−9.717
−13.682
1.00
31.42
C


ATOM
3649
CB
MET
D
105
51.206
−10.403
−14.533
1.00
31.83
C


ATOM
3650
CG
MET
D
105
52.155
−11.228
−13.703
1.00
36.87
C


ATOM
3651
SD
MET
D
105
53.267
−10.213
−12.674
1.00
43.45
S


ATOM
3652
CE
MET
D
105
54.104
−9.296
−13.942
1.00
32.92
C


ATOM
3653
C
MET
D
105
49.131
−9.055
−14.624
1.00
30.41
C


ATOM
3654
O
MET
D
105
48.154
−9.673
−15.072
1.00
29.25
O


ATOM
3655
N
VAL
D
106
49.362
−7.789
−14.917
1.00
29.43
N


ATOM
3656
CA
VAL
D
106
48.394
−7.148
−15.760
1.00
30.76
C


ATOM
3657
CB
VAL
D
106
48.317
−5.542
−15.699
1.00
30.85
C


ATOM
3658
CG1
VAL
D
106
48.876
−4.946
−14.421
1.00
28.68
C


ATOM
3659
CG2
VAL
D
106
48.867
−4.937
−16.875
1.00
27.85
C


ATOM
3660
C
VAL
D
106
48.670
−7.711
−17.170
1.00
31.76
C


ATOM
3661
O
VAL
D
106
49.843
−7.941
−17.524
1.00
32.26
O


ATOM
3662
N
GLY
D
107
47.590
−7.909
−17.944
1.00
31.86
N


ATOM
3663
CA
GLY
D
107
47.602
−8.730
−19.149
1.00
31.60
C


ATOM
3664
C
GLY
D
107
46.937
−10.076
−18.867
1.00
31.76
C


ATOM
3665
O
GLY
D
107
46.782
−10.884
−19.774
1.00
32.48
O


ATOM
3666
N
GLY
D
108
46.594
−10.347
−17.602
1.00
31.73
N


ATOM
3667
CA
GLY
D
108
45.845
−11.561
−17.219
1.00
30.76
C


ATOM
3668
C
GLY
D
108
46.575
−12.837
−16.858
1.00
30.68
C


ATOM
3669
O
GLY
D
108
45.940
−13.868
−16.709
1.00
31.60
O


ATOM
3670
N
VAL
D
109
47.894
−12.799
−16.705
1.00
31.23
N


ATOM
3671
CA
VAL
D
109
48.659
−14.009
−16.355
1.00
31.01
C


ATOM
3672
CB
VAL
D
109
50.115
−13.935
−16.919
1.00
31.60
C


ATOM
3673
CG1
VAL
D
109
50.128
−14.044
−18.453
1.00
30.53
C


ATOM
3674
CG2
VAL
D
109
50.988
−14.970
−16.332
1.00
28.81
C


ATOM
3675
C
VAL
D
109
48.653
−14.172
−14.835
1.00
32.20
C


ATOM
3676
O
VAL
D
109
48.994
−13.258
−14.125
1.00
32.24
O


ATOM
3677
N
VAL
D
110
48.207
−15.323
−14.332
1.00
33.52
N


ATOM
3678
CA
VAL
D
110
48.274
−15.592
−12.911
1.00
34.03
C


ATOM
3679
CB
VAL
D
110
46.863
−15.796
−12.233
1.00
34.35
C


ATOM
3680
CG1
VAL
D
110
46.831
−16.818
−11.135
1.00
33.72
C


ATOM
3681
CG2
VAL
D
110
45.754
−15.985
−13.234
1.00
34.18
C


ATOM
3682
C
VAL
D
110
49.389
−16.575
−12.582
1.00
35.97
C


ATOM
3683
O
VAL
D
110
49.627
−17.552
−13.306
1.00
35.08
O


ATOM
3684
N
ILE
D
111
50.130
−16.253
−11.526
1.00
38.15
N


ATOM
3685
CA
ILE
D
111
51.201
−17.117
−11.055
1.00
40.04
C


ATOM
3686
CB
ILE
D
111
52.441
−16.328
−10.556
1.00
39.96
C


ATOM
3687
CG1
ILE
D
111
53.021
−15.546
−11.706
1.00
40.77
C


ATOM
3688
CD1
ILE
D
111
52.827
−14.083
−11.586
1.00
42.20
C


ATOM
3689
CG2
ILE
D
111
53.550
−17.273
−10.029
1.00
40.87
C


ATOM
3690
C
ILE
D
111
50.628
−18.015
−10.003
1.00
40.99
C


ATOM
3691
O
ILE
D
111
50.059
−17.563
−8.987
1.00
41.58
O


ATOM
3692
N
GLY
D
112
50.722
−19.313
−10.257
1.00
42.26
N


ATOM
3693
CA
GLY
D
112
50.331
−20.269
−9.235
1.00
41.93
C


ATOM
3694
C
GLY
D
112
51.500
−21.086
−8.715
1.00
43.09
C


ATOM
3695
O
GLY
D
112
52.575
−21.142
−9.325
1.00
42.76
O


ATOM
3696
N
GLY
D
113
51.266
−21.778
−7.598
1.00
44.33
N


ATOM
3697
CA
GLY
D
113
52.260
−22.648
−7.011
1.00
45.49
C


ATOM
3698
C
GLY
D
113
51.626
−23.882
−6.435
1.00
47.03
C


ATOM
3699
O
GLY
D
113
50.533
−23.830
−5.852
1.00
47.41
O


ATOM
3700
N
GLU
D
114
52.319
−25.001
−6.599
1.00
47.97
N


ATOM
3701
CA
GLU
D
114
51.835
−26.273
−6.122
1.00
48.98
C


ATOM
3702
CB
GLU
D
114
51.275
−27.062
−7.304
1.00
49.06
C


ATOM
3703
CG
GLU
D
114
50.539
−28.280
−6.942
1.00
52.21
C


ATOM
3704
CD
GLU
D
114
49.046
−28.083
−6.856
1.00
56.29
C


ATOM
3705
OE1
GLU
D
114
48.457
−28.646
−5.897
1.00
58.05
O


ATOM
3706
OE2
GLU
D
114
48.462
−27.412
−7.753
1.00
57.66
O


ATOM
3707
C
GLU
D
114
52.968
−27.042
−5.375
1.00
49.12
C


ATOM
3708
O
GLU
D
114
54.066
−27.250
−5.899
1.00
48.87
O


ATOM
3709
N
LYS
D
115
52.678
−27.446
−4.147
1.00
48.78
N


ATOM
3710
CA
LYS
D
115
53.615
−28.192
−3.317
1.00
48.72
C


ATOM
3711
CB
LYS
D
115
53.481
−27.719
−1.866
1.00
49.82
C


ATOM
3712
CG
LYS
D
115
54.298
−26.510
−1.509
1.00
51.17
C


ATOM
3713
CD
LYS
D
115
54.010
−26.041
−0.090
1.00
56.06
C


ATOM
3714
CE
LYS
D
115
55.030
−24.958
0.334
1.00
62.44
C


ATOM
3715
NZ
LYS
D
115
54.544
−24.084
1.479
1.00
66.54
N


ATOM
3716
C
LYS
D
115
53.450
−29.733
−3.408
1.00
47.04
C


ATOM
3717
O
LYS
D
115
52.334
−30.258
−3.557
1.00
46.88
O


ATOM
3718
N
GLY
D
116
54.576
−30.441
−3.346
1.00
46.00
N


ATOM
3719
CA
GLY
D
116
54.576
−31.909
−3.157
1.00
44.67
C


ATOM
3720
C
GLY
D
116
54.109
−32.255
−1.746
1.00
44.37
C


ATOM
3721
O
GLY
D
116
54.088
−31.386
−0.850
1.00
44.53
O


ATOM
3722
N
ALA
D
117
53.718
−33.515
−1.544
1.00
43.07
N


ATOM
3723
CA
ALA
D
117
53.148
−33.918
−0.289
1.00
41.97
C


ATOM
3724
CB
ALA
D
117
52.397
−35.199
−0.448
1.00
41.67
C


ATOM
3725
C
ALA
D
117
54.208
−34.037
0.806
1.00
41.59
C


ATOM
3726
O
ALA
D
117
53.855
−34.218
1.958
1.00
42.73
O


ATOM
3727
N
GLY
D
118
55.487
−33.984
0.449
1.00
40.27
N


ATOM
3728
CA
GLY
D
118
56.542
−33.997
1.430
1.00
39.78
C


ATOM
3729
C
GLY
D
118
57.349
−35.274
1.452
1.00
41.03
C


ATOM
3730
O
GLY
D
118
56.891
−36.346
1.032
1.00
41.30
O


ATOM
3731
N
THR
D
119
58.575
−35.170
1.943
1.00
41.33
N


ATOM
3732
CA
THR
D
119
59.336
−36.361
2.271
1.00
41.15
C


ATOM
3733
CB
THR
D
119
60.404
−36.914
1.152
1.00
41.78
C


ATOM
3734
OG1
THR
D
119
61.763
−36.991
1.623
1.00
46.65
O


ATOM
3735
CG2
THR
D
119
60.283
−36.324
−0.201
1.00
36.84
C


ATOM
3736
C
THR
D
119
59.867
−36.263
3.698
1.00
40.96
C


ATOM
3737
O
THR
D
119
60.532
−35.282
4.053
1.00
40.91
O


ATOM
3738
N
ALA
D
120
59.514
−37.258
4.517
1.00
38.25
N


ATOM
3739
CA
ALA
D
120
60.005
−37.311
5.887
1.00
37.80
C


ATOM
3740
CB
ALA
D
120
58.969
−38.040
6.791
1.00
35.79
C


ATOM
3741
C
ALA
D
120
61.369
−38.034
5.933
1.00
37.39
C


ATOM
3742
O
ALA
D
120
61.421
−39.245
5.827
1.00
37.29
O


ATOM
3743
N
LEU
D
121
62.471
−37.298
6.048
1.00
37.88
N


ATOM
3744
CA
LEU
D
121
63.791
−37.950
6.023
1.00
37.30
C


ATOM
3745
CB
LEU
D
121
64.792
−37.133
5.216
1.00
37.16
C


ATOM
3746
CG
LEU
D
121
66.302
−37.438
5.387
1.00
36.66
C


ATOM
3747
CD1
LEU
D
121
66.766
−38.702
4.727
1.00
34.65
C


ATOM
3748
CD2
LEU
D
121
67.118
−36.308
4.863
1.00
34.00
C


ATOM
3749
C
LEU
D
121
64.286
−38.098
7.456
1.00
38.21
C


ATOM
3750
O
LEU
D
121
64.305
−37.112
8.182
1.00
37.52
O


ATOM
3751
N
THR
D
122
64.672
−39.322
7.853
1.00
39.39
N


ATOM
3752
CA
THR
D
122
65.420
−39.553
9.093
1.00
40.36
C


ATOM
3753
CB
THR
D
122
64.764
−40.661
9.897
1.00
41.03
C


ATOM
3754
OG1
THR
D
122
63.433
−40.254
10.264
1.00
40.03
O


ATOM
3755
CG2
THR
D
122
65.574
−41.056
11.168
1.00
41.88
C


ATOM
3756
C
THR
D
122
66.850
−39.909
8.706
1.00
41.03
C


ATOM
3757
O
THR
D
122
67.056
−40.848
7.985
1.00
40.84
O


ATOM
3758
N
VAL
D
123
67.835
−39.101
9.103
1.00
42.99
N


ATOM
3759
CA
VAL
D
123
69.234
−39.583
9.052
1.00
44.79
C


ATOM
3760
CB
VAL
D
123
70.202
−38.754
8.099
1.00
45.22
C


ATOM
3761
CG1
VAL
D
123
71.523
−38.462
8.713
1.00
44.87
C


ATOM
3762
CG2
VAL
D
123
69.528
−37.548
7.456
1.00
43.50
C


ATOM
3763
C
VAL
D
123
69.796
−40.080
10.409
1.00
46.99
C


ATOM
3764
O
VAL
D
123
69.848
−39.349
11.408
1.00
46.54
O


ATOM
3765
N
LYS
D
124
70.123
−41.378
10.437
1.00
49.38
N


ATOM
3766
CA
LYS
D
124
70.636
−42.039
11.647
1.00
50.47
C


ATOM
3767
CB
LYS
D
124
70.156
−43.525
11.743
1.00
49.98
C


ATOM
3768
CG
LYS
D
124
68.619
−43.748
12.007
1.00
50.05
C


ATOM
3769
CD
LYS
D
124
68.052
−43.043
13.279
1.00
49.05
C


ATOM
3770
CE
LYS
D
124
66.688
−43.609
13.767
1.00
48.44
C


ATOM
3771
NZ
LYS
D
124
65.834
−42.572
14.515
1.00
47.51
N


ATOM
3772
C
LYS
D
124
72.171
−41.904
11.655
1.00
50.68
C


ATOM
3773
O
LYS
D
124
72.808
−42.063
10.610
1.00
51.52
O


ATOM
3774
N
ALA
D
125
72.722
−41.535
12.816
1.00
51.34
N


ATOM
3775
CA
ALA
D
125
74.161
−41.416
13.055
1.00
52.01
C


ATOM
3776
CB
ALA
D
125
74.443
−41.064
14.528
1.00
51.75
C


ATOM
3777
C
ALA
D
125
74.834
−42.715
12.711
1.00
52.46
C


ATOM
3778
O
ALA
D
125
74.540
−43.751
13.329
1.00
52.80
O


ATOM
3779
OXT
ALA
D
125
75.650
−42.744
11.792
1.00
52.94
O


ATOM
3780
O
HOH
W
1
27.537
−6.895
−25.418
1.00
49.96
O


ATOM
3781
O
HOH
W
2
16.484
−15.501
−2.860
1.00
51.92
O


ATOM
3782
O
HOH
W
3
64.994
−13.128
−29.648
1.00
61.47
O


ATOM
3783
O
HOH
W
4
58.640
−8.263
−15.036
1.00
51.01
O


ATOM
3784
O
HOH
W
5
49.811
−21.870
−19.181
1.00
53.77
O


ATOM
3785
O
HOH
W
6
47.451
15.219
8.922
1.00
53.13
O


ATOM
3786
O
HOH
W
7
57.241
6.450
−33.199
1.00
67.49
O


ATOM
3787
O
HOH
W
8
55.602
−37.210
4.291
1.00
45.54
O


ATOM
3788
O
HOH
W
9
71.793
−8.853
−14.510
1.00
53.04
O


ATOM
3789
O
HOH
W
10
28.959
18.294
23.084
1.00
44.15
O


ATOM
3790
O
HOH
W
11
51.211
−1.996
−16.782
1.00
34.13
O


ATOM
3791
O
HOH
W
12
20.537
2.113
13.747
1.00
37.57
O


ATOM
3792
O
HOH
W
13
63.618
−7.963
−22.008
1.00
48.46
O


ATOM
3793
O
HOH
W
14
15.973
−5.480
−1.302
1.00
58.45
O


ATOM
3794
O
HOH
W
15
47.026
19.336
−8.349
1.00
45.60
O


ATOM
3795
O
HOH
W
16
38.870
18.600
16.145
1.00
48.41
O


ATOM
3796
O
HOH
W
17
55.643
−13.712
−15.385
1.00
53.69
O


ATOM
3797
O
HOH
W
18
29.523
17.221
14.352
1.00
33.22
O


ATOM
3798
O
HOH
W
19
74.183
−13.852
−32.153
1.00
45.21
O


ATOM
3799
O
HOH
W
20
51.603
5.048
−41.486
1.00
67.11
O


ATOM
3800
O
HOH
W
21
75.638
−22.627
9.738
1.00
66.50
O


ATOM
3801
O
HOH
W
22
16.178
1.770
−16.784
1.00
63.18
O


ATOM
3802
O
HOH
W
23
72.855
−27.072
5.746
1.00
46.62
O


ATOM
3803
O
HOH
W
24
28.469
17.946
−7.226
1.00
50.63
O


ATOM
3804
O
HOH
W
25
52.814
15.053
−42.546
1.00
68.81
O


ATOM
3805
O
HOH
W
26
54.094
10.191
−35.541
1.00
68.73
O


ATOM
3806
O
HOH
W
27
28.221
15.502
−7.510
1.00
61.71
O


ATOM
3807
O
HOH
W
28
29.651
−7.408
−0.031
1.00
77.42
O


ATOM
3808
O
HOH
W
29
55.208
−11.816
−1.694
1.00
65.92
O


ATOM
3809
O
HOH
W
30
65.842
−14.431
−7.424
1.00
62.18
O


ATOM
3810
O
HOH
W
31
86.092
−37.988
19.084
1.00
62.21
O


ATOM
3811
O
HOH
W
32
57.547
−17.020
−8.281
1.00
54.14
O


ATOM
3812
O
HOH
W
33
15.238
−25.319
−14.960
1.00
48.17
O


ATOM
3813
O
HOH
W
34
32.868
−10.730
−16.000
1.00
60.24
O


ATOM
3814
O
HOH
W
35
27.383
−23.747
−14.732
1.00
54.01
O


ATOM
3815
O
HOH
W
36
45.466
−36.429
−7.768
1.00
61.01
O


ATOM
3816
O
HOH
W
37
85.751
6.805
−23.803
1.00
63.72
O


ATOM
3817
O
HOH
W
38
64.003
−17.550
−25.097
1.00
52.50
O


ATOM
3818
O
HOH
W
39
18.054
10.470
11.460
1.00
31.24
O


ATOM
3819
O
HOH
W
40
3.495
−9.168
−13.711
1.00
46.96
O


ATOM
3820
O
HOH
W
41
41.882
−5.080
13.345
1.00
59.64
O


ATOM
3821
O
HOH
W
42
53.605
−40.677
−18.373
1.00
65.41
O


ATOM
3822
O
HOH
W
43
36.386
−1.428
−3.036
1.00
50.71
O


ATOM
3823
O
HOH
W
44
73.455
−43.317
−0.552
1.00
59.07
O


ATOM
3824
O
HOH
W
45
78.144
−43.753
12.847
1.00
65.80
O


ATOM
3825
O
HOH
W
46
57.888
−11.778
−11.462
1.00
57.52
O


ATOM
3826
O
HOH
W
47
45.202
−5.340
3.650
1.00
48.23
O


ATOM
3827
O
HOH
W
48
63.611
−10.382
−24.415
1.00
50.05
O


ATOM
3828
O
HOH
W
49
57.536
6.456
−7.141
1.00
28.46
O


ATOM
3829
O
HOH
W
50
58.272
−0.505
−0.424
1.00
30.38
O


ATOM
3830
O
HOH
W
51
46.690
−1.769
0.708
1.00
25.84
O


ATOM
3831
O
HOH
W
52
43.295
5.650
−15.284
1.00
31.89
O


ATOM
3832
O
HOH
W
53
64.526
9.634
−19.506
1.00
29.96
O


ATOM
3833
O
HOH
W
54
23.155
−22.622
−14.253
1.00
34.18
O


ATOM
3834
O
HOH
W
55
64.074
−2.755
−3.506
1.00
32.46
O


ATOM
3835
O
HOH
W
56
65.733
−39.979
14.780
1.00
50.48
O


ATOM
3836
O
HOH
W
57
25.603
12.096
6.016
1.00
29.23
O


ATOM
3837
O
HOH
W
58
16.263
−22.766
−25.732
1.00
37.53
O


ATOM
3838
O
HOH
W
59
51.239
2.681
−2.880
1.00
34.06
O


ATOM
3839
O
HOH
W
60
54.458
−2.187
−19.524
1.00
40.20
O


ATOM
3840
O
HOH
W
61
71.361
7.864
−19.372
1.00
37.66
O


ATOM
3841
O
HOH
W
62
56.520
7.752
−18.350
1.00
37.39
O


ATOM
3842
O
HOH
W
63
13.694
−9.946
−29.896
1.00
38.42
O


ATOM
3843
O
HOH
W
64
61.439
−41.245
8.021
1.00
41.37
O


ATOM
3844
O
HOH
W
65
39.971
3.043
13.470
1.00
51.30
O


ATOM
3845
O
HOH
W
66
28.958
15.268
1.059
1.00
43.67
O


ATOM
3846
O
HOH
W
67
30.104
2.750
2.608
1.00
40.29
O


ATOM
3847
O
HOH
W
68
69.821
−2.267
−8.072
1.00
33.11
O


ATOM
3848
O
HOH
W
69
52.286
−7.121
−16.541
1.00
38.11
O


ATOM
3849
O
HOH
W
70
58.487
−28.442
5.036
1.00
37.01
O


ATOM
3850
O
HOH
W
71
25.719
16.565
13.085
1.00
44.30
O


ATOM
3851
O
HOH
W
72
52.822
−11.013
−17.837
1.00
45.81
O


ATOM
3852
O
HOH
W
73
22.805
−12.848
−21.485
1.00
48.51
O


ATOM
3853
O
HOH
W
74
36.702
17.554
5.981
1.00
37.50
O


ATOM
3854
O
HOH
W
75
71.895
−9.443
−24.558
1.00
45.80
O


ATOM
3855
O
HOH
W
76
41.108
15.717
−5.487
1.00
39.02
O


ATOM
3856
O
HOH
W
77
18.799
8.481
10.303
1.00
46.57
O


ATOM
3857
O
HOH
W
78
61.610
7.007
−4.915
1.00
50.08
O


ATOM
3858
O
HOH
W
79
60.439
−0.706
−2.323
1.00
33.12
O


ATOM
3859
O
HOH
W
80
58.416
5.614
−9.104
1.00
39.99
O


ATOM
3860
O
HOH
W
81
55.764
−3.255
−35.605
1.00
54.28
O


ATOM
3861
O
HOH
W
82
42.688
13.409
7.580
1.00
32.60
O


ATOM
3862
O
HOH
W
83
56.203
7.504
−13.473
1.00
53.50
O


ATOM
3863
O
HOH
W
84
49.392
−17.628
−1.745
1.00
48.43
O


ATOM
3864
O
HOH
W
85
38.478
17.991
−4.303
1.00
51.79
O


ATOM
3865
O
HOH
W
86
27.380
11.533
−6.035
1.00
43.44
O


ATOM
3866
O
HOH
W
87
17.419
−2.527
−17.186
1.00
46.81
O


ATOM
3867
O
HOH
W
88
65.605
11.412
−34.743
1.00
39.99
O


ATOM
3868
O
HOH
W
89
22.567
−9.323
0.874
1.00
67.08
O


ATOM
3869
O
HOH
W
90
60.466
−7.608
−10.787
1.00
44.79
O


ATOM
3870
O
HOH
W
91
70.029
13.354
−25.195
1.00
48.65
O


ATOM
3871
O
HOH
W
92
27.738
−0.724
12.598
1.00
46.67
O


ATOM
3872
O
HOH
W
93
67.709
−9.736
−34.668
1.00
44.52
O


ATOM
3873
O
HOH
W
94
66.469
−42.220
−2.677
1.00
50.32
O


ATOM
3874
O
HOH
W
95
39.659
4.264
19.635
1.00
47.26
O


ATOM
3875
O
HOH
W
96
33.798
−0.629
0.634
1.00
57.82
O


ATOM
3876
O
HOH
W
97
68.516
5.533
−7.794
1.00
38.76
O


ATOM
3877
O
HOH
W
98
57.378
4.251
−27.603
1.00
49.36
O


ATOM
3878
O
HOH
W
99
45.738
12.067
6.077
1.00
40.86
O


ATOM
3879
O
HOH
W
100
72.260
−27.692
−8.666
1.00
69.19
O


ATOM
3880
O
HOH
W
101
74.870
5.332
−30.099
1.00
41.86
O


ATOM
3881
O
HOH
W
102
19.884
−13.568
−28.826
1.00
38.32
O


ATOM
3882
O
HOH
W
103
3.023
−14.597
−13.318
1.00
47.56
O


ATOM
3883
O
HOH
W
104
44.498
−8.083
−17.403
1.00
48.70
O


ATOM
3884
O
HOH
W
105
75.836
−5.431
−10.641
1.00
58.00
O


ATOM
3885
O
HOH
W
106
60.710
7.924
−15.560
1.00
30.19
O


ATOM
3886
O
HOH
W
107
40.439
−9.476
15.038
1.00
60.28
O


ATOM
3887
O
HOH
W
108
56.235
−30.734
8.744
1.00
53.65
O


ATOM
3888
O
HOH
W
109
63.101
−1.697
−1.511
1.00
31.65
O


ATOM
3889
O
HOH
W
110
56.808
5.705
−16.251
1.00
33.23
O


ATOM
3890
O
HOH
W
111
38.263
8.376
22.049
1.00
55.72
O


ATOM
3891
O
HOH
W
112
64.897
−23.439
−3.286
1.00
46.93
O


ATOM
3892
O
HOH
W
113
30.449
−20.129
−16.647
1.00
51.12
O


ATOM
3893
O
HOH
W
114
24.716
−6.274
−13.423
1.00
48.87
O


ATOM
3894
O
HOH
W
115
69.646
14.058
−27.887
1.00
43.33
O


ATOM
3895
O
HOH
W
116
74.378
8.019
−23.439
1.00
42.12
O


ATOM
3896
O
HOH
W
117
74.411
−6.755
−12.312
1.00
46.21
O


ATOM
3897
O
HOH
W
118
80.776
−40.223
6.131
1.00
51.98
O


ATOM
3898
O
HOH
W
119
16.271
−26.835
−20.387
1.00
53.48
O


ATOM
3899
O
HOH
W
120
45.888
8.444
12.000
1.00
56.59
O


ATOM
3900
O
HOH
W
121
69.004
−39.355
13.718
1.00
48.52
O


ATOM
3901
O
HOH
W
122
44.628
1.826
3.253
1.00
55.53
O


ATOM
3902
O
HOH
W
123
10.540
−21.289
−24.117
1.00
55.75
O


ATOM
3903
O
HOH
W
124
39.519
7.553
−11.796
1.00
42.99
O


ATOM
3904
O
HOH
W
125
17.953
2.631
6.934
1.00
46.87
O


ATOM
3905
O
HOH
W
126
59.706
−42.276
8.568
1.00
49.22
O


ATOM
3906
O
HOH
W
127
71.515
9.604
−9.652
1.00
51.76
O


ATOM
3907
O
HOH
W
128
22.711
−2.131
7.099
1.00
56.06
O


ATOM
3908
O
HOH
W
129
50.497
1.860
−26.962
1.00
48.49
O


ATOM
3909
O
HOH
W
130
13.213
−25.189
−17.571
1.00
47.33
O


ATOM
3910
O
HOH
W
131
36.422
−18.594
1.861
1.00
59.55
O


ATOM
3911
O
HOH
W
132
67.824
−18.443
8.774
1.00
64.42
O


ATOM
3912
O
HOH
W
133
38.702
9.149
25.860
1.00
63.04
O


ATOM
3913
O
HOH
W
134
26.829
−19.030
−19.104
1.00
49.31
O


ATOM
3914
O
HOH
W
135
59.736
−32.012
10.576
1.00
35.03
O


ATOM
3915
O
HOH
W
136
64.103
0.614
−0.340
1.00
40.32
O


ATOM
3916
O
HOH
W
137
68.933
−33.671
−8.563
1.00
47.24
O


ATOM
3917
O
HOH
W
138
30.091
−18.545
3.715
1.00
65.55
O


ATOM
3918
O
HOH
W
139
11.871
−19.774
−24.246
1.00
33.50
O


ATOM
3919
O
HOH
W
140
54.104
−8.838
−17.264
1.00
43.66
O


ATOM
3920
O
HOH
W
141
68.475
−6.296
−7.780
1.00
51.54
O


ATOM
3921
O
HOH
W
142
61.319
8.970
−35.221
1.00
63.08
O


ATOM
3922
O
HOH
W
143
5.216
−2.074
−13.989
1.00
53.77
O


ATOM
3923
O
HOH
W
144
77.471
−7.485
−20.605
1.00
62.28
O


ATOM
3924
O
HOH
W
145
22.942
−15.078
−26.211
1.00
45.04
O


ATOM
3925
O
HOH
W
146
62.912
−3.121
−6.057
1.00
35.08
O


ATOM
3926
O
HOH
W
147
60.466
−10.624
−21.327
1.00
50.25
O


ATOM
3927
O
HOH
W
148
49.218
8.905
−16.800
1.00
51.16
O


ATOM
3928
O
HOH
W
149
33.265
10.047
−10.678
1.00
48.18
O


ATOM
3929
O
HOH
W
150
58.095
9.361
−4.575
1.00
50.70
O


ATOM
3930
O
HOH
W
151
44.991
−5.664
−19.770
1.00
52.37
O


ATOM
3931
O
HOH
W
152
46.997
−10.249
−1.900
1.00
46.25
O


ATOM
3932
O
HOH
W
153
30.534
2.664
−1.760
1.00
51.90
O


ATOM
3933
O
HOH
W
154
75.688
−26.530
1.235
1.00
61.29
O


ATOM
3934
O
HOH
W
155
31.837
18.468
15.789
1.00
47.11
O


ATOM
3935
O
HOH
W
156
22.573
−6.055
−12.416
1.00
40.78
O


ATOM
3936
O
HOH
W
157
69.966
−24.619
2.582
1.00
51.01
O


ATOM
3937
O
HOH
W
158
7.080
−14.929
−10.596
1.00
46.45
O


ATOM
3938
O
HOH
W
159
30.087
19.609
−1.446
1.00
65.48
O


ATOM
3939
O
HOH
W
160
35.321
18.508
20.566
1.00
53.81
O


ATOM
3940
O
HOH
W
161
66.872
−33.922
14.718
1.00
52.80
O


ATOM
3941
O
HOH
W
162
19.048
−21.457
−21.483
1.00
49.57
O


ATOM
3942
O
HOH
W
163
55.940
2.690
−8.893
1.00
32.16
O


ATOM
3943
O
HOH
W
164
73.832
−5.186
−31.071
1.00
44.92
O


ATOM
3944
O
HOH
W
165
73.497
4.469
−51.566
1.00
49.98
O


ATOM
3945
O
HOH
W
166
46.143
−24.184
2.265
1.00
65.14
O


ATOM
3946
O
HOH
W
167
53.822
−6.318
−27.868
1.00
59.13
O


ATOM
3947
O
HOH
W
168
22.273
−7.060
−32.842
1.00
55.91
O


ATOM
3948
O
HOH
W
169
69.920
5.647
−54.927
1.00
52.38
O


ATOM
3949
O
HOH
W
170
75.276
−0.500
−18.493
1.00
56.03
O


ATOM
3950
O
HOH
W
171
74.355
−7.796
−18.378
1.00
51.15
O


ATOM
3951
O
HOH
W
172
49.846
7.730
−10.950
1.00
26.02
O


ATOM
3952
O
HOH
W
173
74.688
6.874
−18.930
1.00
59.05
O


ATOM
3953
O
HOH
W
174
8.532
−17.930
−12.696
1.00
46.51
O


ATOM
3954
O
HOH
W
175
65.329
10.399
−23.289
1.00
31.68
O


ATOM
3955
O
HOH
W
176
62.448
−6.262
−23.487
1.00
45.41
O


ATOM
3956
O
HOH
W
177
13.206
−11.211
−6.299
1.00
49.50
O


ATOM
3957
O
HOH
W
178
61.714
2.022
−1.453
1.00
36.23
O


ATOM
3958
O
HOH
W
179
46.778
11.434
−6.992
1.00
35.69
O


ATOM
3959
O
HOH
W
180
27.754
6.719
−4.382
1.00
58.45
O


ATOM
3960
O
HOH
W
181
15.241
−0.832
−13.316
1.00
42.58
O


ATOM
3961
O
HOH
W
182
58.699
9.096
−7.863
1.00
34.47
O


ATOM
3962
O
HOH
W
183
64.941
−16.861
0.001
1.00
64.80
O


ATOM
3963
O
HOH
W
184
77.519
−7.298
−17.771
1.00
59.86
O


ATOM
3964
O
HOH
W
185
61.404
−45.244
5.009
1.00
47.15
O


ATOM
3965
O
HOH
W
186
21.672
−2.040
−10.318
1.00
50.64
O


ATOM
3966
O
HOH
W
187
29.956
−0.092
−9.945
1.00
62.76
O


ATOM
3967
O
HOH
W
188
36.410
15.705
−10.591
1.00
55.05
O


ATOM
3968
O
HOH
W
189
77.269
−24.718
−6.307
1.00
58.93
O


ATOM
3969
O
HOH
W
190
53.639
−41.684
4.960
1.00
46.88
O


ATOM
3970
O
HOH
W
191
39.701
−8.194
−19.650
1.00
68.65
O


ATOM
3971
O
HOH
W
192
72.960
11.333
−30.255
1.00
57.07
O


ATOM
3972
O
HOH
W
193
69.245
−8.902
−20.463
1.00
59.91
O


ATOM
3973
O
HOH
W
194
25.519
2.766
−5.298
1.00
62.24
O


ATOM
3974
O
HOH
W
195
23.823
−18.240
−23.523
1.00
53.83
O


ATOM
3975
O
HOH
W
196
76.411
−10.927
−28.761
1.00
57.41
O


ATOM
3976
O
HOH
W
197
68.909
7.633
−3.751
1.00
54.97
O


ATOM
3977
O
HOH
W
198
68.238
4.063
−57.802
1.00
60.28
O


ATOM
3978
O
HOH
W
199
57.902
−43.905
0.785
1.00
47.08
O


ATOM
3979
O
HOH
W
200
26.387
1.586
19.253
1.00
57.98
O


ATOM
3980
O
HOH
W
201
37.729
12.225
22.176
1.00
36.41
O


ATOM
3981
O
HOH
W
202
52.534
7.353
−41.886
1.00
66.91
O


ATOM
3982
O
HOH
W
203
27.054
−0.735
4.862
1.00
51.36
O


ATOM
3983
O
HOH
W
204
42.236
−8.736
1.239
1.00
49.54
O


ATOM
3984
O
HOH
W
205
72.453
−49.755
2.535
1.00
57.88
O


ATOM
3985
O
HOH
W
206
21.715
13.751
27.357
1.00
63.70
O


ATOM
3986
O
HOH
W
207
72.850
11.054
−33.545
1.00
48.23
O


ATOM
3987
O
HOH
W
208
72.490
9.599
−53.823
1.00
63.34
O


ATOM
3988
O
HOH
W
209
62.543
16.639
−24.176
1.00
32.72
O


ATOM
3989
O
HOH
W
210
45.124
−6.604
−14.457
1.00
40.86
O


ATOM
3990
O
HOH
W
211
67.128
11.703
−20.217
1.00
33.12
O


ATOM
3991
O
HOH
W
212
71.826
−45.136
14.739
1.00
57.74
O


ATOM
3992
O
HOH
W
213
57.710
7.585
−21.003
1.00
45.04
O


ATOM
3993
O
HOH
W
214
38.961
−13.213
−15.679
1.00
47.33
O


ATOM
3994
O
HOH
W
215
44.800
6.821
8.691
1.00
43.90
O


ATOM
3995
O
HOH
W
216
52.098
−22.105
−2.209
1.00
58.29
O


ATOM
3996
O
HOH
W
217
59.838
−5.952
−22.966
1.00
42.78
O


ATOM
3997
O
HOH
W
218
18.495
−22.454
−8.937
1.00
43.08
O


ATOM
3998
O
HOH
W
219
41.438
−0.960
2.947
1.00
47.12
O


ATOM
3999
O
HOH
W
220
28.357
−12.574
2.320
1.00
67.42
O


ATOM
4000
O
HOH
W
221
31.534
1.142
5.187
1.00
52.28
O


ATOM
4001
O
HOH
W
222
52.061
−0.982
−33.448
1.00
66.10
O


ATOM
4002
O
HOH
W
223
70.684
−25.967
−10.607
1.00
59.78
O


ATOM
4003
O
HOH
W
224
24.630
−22.237
−21.050
1.00
62.09
O


ATOM
4004
O
HOH
W
225
42.829
−4.753
−0.058
1.00
47.47
O


ATOM
4005
O
HOH
W
226
70.534
13.938
−33.309
1.00
57.59
O


ATOM
4006
O
HOH
W
227
37.629
6.169
−9.632
1.00
35.87
O


ATOM
4007
O
HOH
W
228
39.050
−3.195
8.473
1.00
56.47
O


ATOM
4008
O
HOH
W
229
50.163
−25.989
−2.653
1.00
57.19
O


ATOM
4009
O
HOH
W
230
66.728
8.298
−2.609
1.00
53.22
O


ATOM
4010
O
HOH
W
231
46.144
4.981
2.915
1.00
49.44
O


ATOM
4011
O
HOH
W
232
64.030
15.931
−27.869
1.00
50.25
O


ATOM
4012
O
HOH
W
233
78.237
−11.718
−16.675
1.00
66.40
O


ATOM
4013
O
HOH
W
234
3.812
−6.905
−25.561
1.00
46.71
O


ATOM
4014
O
HOH
W
235
64.296
−9.563
−18.956
1.00
55.82
O


ATOM
4015
O
HOH
W
236
57.040
10.985
−10.979
1.00
33.38
O


ATOM
4016
O
HOH
W
237
68.114
0.724
−44.435
1.00
47.88
O


ATOM
4017
O
HOH
W
238
77.812
2.986
−35.556
1.00
54.12
O


ATOM
4018
O
HOH
W
239
68.542
13.125
−10.000
1.00
42.93
O


ATOM
4019
O
HOH
W
240
70.815
11.906
−8.762
1.00
61.18
O


ATOM
4020
O
HOH
W
241
59.743
−4.943
−32.625
1.00
68.83
O


ATOM
4021
O
HOH
W
242
53.599
−2.593
−24.738
1.00
57.17
O


ATOM
4022
O
HOH
W
243
28.804
−22.157
−13.530
1.00
66.00
O


ATOM
4023
O
HOH
W
244
12.528
−20.034
−9.931
1.00
54.81
O


ATOM
4024
O
HOH
W
245
18.999
−13.928
−26.454
1.00
37.34
O


ATOM
4025
O
HOH
W
246
9.399
−7.555
−10.236
1.00
51.74
O


ATOM
4026
O
HOH
W
247
9.422
−23.577
−21.883
1.00
51.71
O


ATOM
4027
O
HOH
W
248
48.989
16.285
−2.427
1.00
52.11
O


ATOM
4028
O
HOH
W
249
25.370
13.160
27.839
1.00
51.67
O


ATOM
4029
O
HOH
W
250
34.924
12.483
−8.217
1.00
36.25
O


ATOM
4030
O
HOH
W
251
55.418
−37.562
−1.079
1.00
39.90
O


ATOM
4031
O
HOH
W
252
65.053
−34.377
−13.229
1.00
61.20
O


ATOM
4032
O
HOH
W
253
65.103
−23.855
−7.015
1.00
61.09
O


ATOM
4033
O
HOH
W
254
59.191
−30.854
12.930
1.00
31.05
O


ATOM
4034
O
HOH
W
255
74.576
−21.281
−5.297
1.00
62.37
O


ATOM
4035
O
HOH
W
256
77.566
−33.129
5.274
1.00
55.66
O


ATOM
4036
O
HOH
W
257
53.903
−22.288
−17.014
1.00
50.27
O


ATOM
4037
O
HOH
W
258
45.037
−8.754
−15.227
1.00
49.48
O


ATOM
4038
O
HOH
W
259
22.148
10.033
10.947
1.00
39.41
O


ATOM
4039
O
HOH
W
260
65.185
−7.017
−20.794
1.00
45.24
O


ATOM
4040
O
HOH
W
261
35.881
−2.206
17.490
1.00
44.28
O


ATOM
4041
O
HOH
W
262
51.882
0.389
−39.836
1.00
67.72
O


ATOM
4042
O
HOH
W
263
31.840
18.088
10.972
1.00
46.55
O


ATOM
4043
O
HOH
W
264
0.515
−17.290
−27.161
1.00
54.35
O


ATOM
4044
O
HOH
W
265
69.618
−46.411
15.204
1.00
62.11
O


ATOM
4045
O
HOH
W
266
30.859
7.314
28.270
1.00
50.41
O


ATOM
4046
O
HOH
W
267
18.081
11.850
9.552
1.00
53.90
O


ATOM
4047
O
HOH
W
268
59.391
−23.586
16.532
1.00
66.97
O


ATOM
4048
O
HOH
W
269
35.395
5.989
−11.309
1.00
48.68
O


ATOM
4049
O
HOH
W
270
16.271
1.278
9.498
1.00
66.12
O


ATOM
4050
O
HOH
W
271
46.429
19.602
7.510
1.00
50.45
O


ATOM
4051
O
HOH
W
272
41.687
0.016
6.150
1.00
48.74
O


ATOM
4052
O
HOH
W
273
55.497
−10.087
2.040
1.00
52.80
O


ATOM
4053
O
HOH
W
274
11.272
−9.479
−30.539
1.00
38.85
O


ATOM
4054
O
HOH
W
275
54.397
−1.130
−21.031
1.00
54.26
O


ATOM
4055
O
HOH
W
276
12.883
−21.707
−24.390
1.00
53.71
O


ATOM
4056
O
HOH
W
277
18.287
−21.975
−25.586
1.00
45.47
O


ATOM
4057
O
HOH
W
278
46.785
0.418
−18.533
1.00
32.22
O


ATOM
4058
O
HOH
W
279
45.873
−0.317
−20.312
1.00
58.31
O


ATOM
4059
O
HOH
W
280
46.094
−1.639
−18.715
1.00
40.18
O


ATOM
4060
O
HOH
W
281
42.337
−11.592
−18.551
1.00
65.25
O


ATOM
4061
O
HOH
W
282
39.890
13.264
−12.839
1.00
51.77
O


ATOM
4062
O
HOH
W
283
44.794
10.396
3.595
1.00
40.28
O


ATOM
4063
O
HOH
W
284
39.618
18.733
13.341
1.00
51.45
O


ATOM
4064
O
HOH
W
285
53.173
−35.468
−3.845
1.00
38.36
O


ATOM
4065
O
HOH
W
286
17.906
−8.860
−0.520
1.00
47.10
O


ATOM
4066
O
HOH
W
287
67.074
−7.604
−16.718
1.00
36.14
O


ATOM
4067
O
HOH
W
288
12.354
−4.311
−22.662
1.00
46.21
O


ATOM
4068
O
HOH
W
289
74.559
−22.448
−0.574
1.00
63.95
O


ATOM
4069
O
HOH
W
290
24.579
9.857
−1.018
1.00
42.40
O


ATOM
4070
O
HOH
W
291
42.836
−14.137
−19.076
1.00
48.67
O


ATOM
4071
O
HOH
W
292
42.577
−32.888
−9.222
1.00
58.27
O


ATOM
4072
O
HOH
W
293
51.889
−30.288
0.706
1.00
47.73
O


ATOM
4073
O
HOH
W
294
58.591
9.524
−11.965
1.00
64.46
O


ATOM
4074
O
HOH
W
295
23.195
6.118
25.651
1.00
51.90
O


ATOM
4075
O
HOH
W
296
62.053
−7.731
−30.991
1.00
49.35
O


ATOM
4076
O
HOH
W
297
49.685
−0.059
−34.867
1.00
57.45
O


ATOM
4077
O
HOH
W
298
27.481
15.626
30.011
1.00
62.52
O


ATOM
4078
O
HOH
W
299
22.412
16.454
25.493
1.00
43.70
O


ATOM
4079
O
HOH
W
300
63.991
−24.156
−11.886
1.00
44.37
O


ATOM
4080
O
HOH
W
301
23.584
−2.108
−14.137
1.00
51.53
O


ATOM
4081
O
HOH
W
302
16.320
−11.014
1.961
1.00
61.11
O


ATOM
4082
O
HOH
W
303
21.217
−22.569
−24.840
1.00
58.72
O


ATOM
4083
O
HOH
W
304
41.646
17.848
−7.228
1.00
65.03
O


ATOM
4084
O
HOH
W
305
22.950
17.731
10.015
1.00
58.75
O


ATOM
4085
O
HOH
W
306
56.767
7.202
2.006
1.00
62.33
O


ATOM
4086
O
HOH
W
307
58.177
−38.332
−8.428
1.00
51.10
O


ATOM
4087
O
HOH
W
308
36.859
6.714
22.042
1.00
67.48
O


ATOM
4088
O
HOH
W
309
8.548
−9.082
−6.377
1.00
64.08
O


ATOM
4089
O
HOH
W
310
77.441
6.499
−18.901
1.00
53.22
O


ATOM
4090
O
HOH
W
311
50.214
−2.598
−28.240
1.00
65.39
O


ATOM
4091
O
HOH
W
312
67.157
−32.383
12.563
1.00
52.04
O


ATOM
4092
O
HOH
W
313
42.103
10.501
15.691
1.00
58.68
O


ATOM
4093
O
HOH
W
314
32.134
−22.541
−14.797
1.00
64.57
O


ATOM
4094
O
HOH
W
315
49.067
3.344
−37.222
1.00
67.11
O


ATOM
4095
O
HOH
W
316
61.987
−46.753
3.536
1.00
61.36
O


ATOM
4096
O
HOH
W
317
60.318
−9.489
−9.294
1.00
50.74
O


ATOM
4097
O
HOH
W
318
48.190
−10.315
0.317
1.00
44.60
O


ATOM
4098
O
HOH
W
319
50.098
−10.842
−18.057
1.00
53.04
O


ATOM
4099
O
HOH
W
320
46.094
9.952
6.886
1.00
54.78
O


ATOM
4100
O
HOH
W
321
74.455
7.920
−30.461
1.00
54.66
O


ATOM
4101
O
HOH
W
322
73.297
−11.177
−30.246
1.00
54.61
O


ATOM
4102
O
HOH
W
323
55.869
3.785
−16.712
1.00
47.04
O


ATOM
4103
O
HOH
W
324
17.752
−20.654
−6.176
1.00
66.30
O


ATOM
4104
O
HOH
W
325
19.223
−5.198
−23.515
1.00
66.40
O


ATOM
4105
O
HOH
W
326
14.416
−5.443
−29.063
1.00
58.70
O


ATOM
4106
O
HOH
W
327
20.794
−20.150
−22.576
1.00
47.38
O


ATOM
4107
O
HOH
W
328
46.970
9.591
−3.000
1.00
61.77
O


ATOM
4108
O
HOH
W
329
44.733
9.137
−4.905
1.00
58.82
O


ATOM
4109
O
HOH
W
330
44.656
15.089
8.206
1.00
62.37
O


ATOM
4110
O
HOH
W
331
41.354
13.880
11.375
1.00
49.54
O


ATOM
4111
O
HOH
W
332
37.483
14.530
22.480
1.00
53.31
O


ATOM
4112
O
HOH
W
333
41.722
19.379
−3.546
1.00
50.97
O


ATOM
4113
O
HOH
W
334
42.731
13.993
−12.884
1.00
72.77
O


ATOM
4114
O
HOH
W
335
23.790
0.599
10.614
1.00
45.38
O


ATOM
4115
O
HOH
W
336
59.513
−7.372
−13.143
1.00
61.55
O


ATOM
4116
O
HOH
W
337
56.314
9.708
−14.663
1.00
50.95
O


ATOM
4117
O
HOH
W
338
31.978
−18.528
−15.554
1.00
67.33
O


ATOM
4118
O
HOH
W
339
56.351
−11.784
−4.728
1.00
42.25
O


ATOM
4119
O
HOH
W
340
32.235
−7.490
−8.002
1.00
48.45
O


ATOM
4120
O
HOH
W
341
11.039
−11.212
−5.888
1.00
56.05
O


ATOM
4121
O
HOH
W
342
45.883
15.519
−9.499
1.00
60.90
O


ATOM
4122
O
HOH
W
343
42.607
11.894
21.114
1.00
59.64
O


ATOM
4123
O
HOH
W
344
64.897
−45.210
2.801
1.00
46.00
O


ATOM
4124
O
HOH
W
345
62.414
−44.124
9.836
1.00
54.24
O


ATOM
4125
O
HOH
W
346
66.607
−47.490
14.098
1.00
51.46
O


ATOM
4126
O
HOH
W
347
33.184
9.901
29.054
1.00
54.19
O


ATOM
4127
O
HOH
W
348
61.338
−8.260
−18.802
1.00
61.80
O


ATOM
4128
O
HOH
W
349
58.915
10.462
−1.335
1.00
59.07
O


ATOM
4129
O
HOH
W
350
72.985
11.119
−6.571
1.00
57.45
O


ATOM
4130
O
HOH
W
351
52.715
−5.406
−30.681
1.00
76.01
O


ATOM
4131
O
HOH
W
352
79.919
−27.316
−4.944
1.00
61.96
O


ATOM
4132
O
HOH
W
353
71.264
8.651
−47.201
1.00
49.44
O


ATOM
4133
O
HOH
W
354
22.664
12.842
33.813
1.00
49.23
O


ATOM
4134
O
HOH
W
355
27.068
20.483
22.480
1.00
39.84
O


ATOM
4135
O
HOH
W
356
31.821
−0.902
1.857
1.00
55.00
O


ATOM
4136
O
HOH
W
357
35.021
−1.745
3.155
1.00
59.58
O


ATOM
4137
O
HOH
W
358
39.467
2.391
21.237
1.00
73.05
O


ATOM
4138
O
HOH
W
359
35.690
−6.904
−2.480
1.00
64.18
O


ATOM
4139
O
HOH
W
360
38.038
−8.228
−14.500
1.00
64.77
O


ATOM
4140
O
HOH
W
361
56.585
−29.520
5.841
1.00
60.72
O


ATOM
4141
O
HOH
W
362
55.461
−35.538
5.382
1.00
54.96
O


ATOM
4142
O
HOH
W
363
62.048
−20.002
−5.479
1.00
55.47
O


ATOM
4143
O
HOH
W
364
65.219
−29.258
15.468
1.00
67.43
O


ATOM
4144
O
HOH
W
365
15.338
−5.304
−5.505
1.00
54.06
O


ATOM
4145
O
HOH
W
366
28.667
17.880
30.849
1.00
58.81
O


ATOM
4146
O
HOH
W
367
7.490
−4.018
−9.949
1.00
49.82
O


ATOM
4147
O
HOH
W
368
41.902
−0.891
15.421
1.00
58.16
O


ATOM
4148
O
HOH
W
369
23.205
−24.145
−0.987
1.00
49.15
O


ATOM
4149
O
HOH
W
370
46.687
7.432
6.640
1.00
58.62
O


ATOM
4150
O
HOH
W
371
47.413
16.850
−8.082
1.00
59.32
O


ATOM
4151
O
HOH
W
372
6.503
−2.107
−24.879
1.00
52.47
O


ATOM
4152
O
HOH
W
373
47.592
−16.616
−26.050
1.00
54.23
O


ATOM
4153
O
HOH
W
374
32.148
2.927
25.177
1.00
51.95
O


ATOM
4154
O
HOH
W
375
70.869
13.479
−15.671
1.00
61.78
O


ATOM
4155
O
HOH
W
376
32.233
−9.491
0.706
1.00
64.72
O


ATOM
4156
O
HOH
W
377
43.162
−20.025
−20.830
1.00
61.56
O


ATOM
4157
O
HOH
W
378
7.447
−21.877
−18.708
1.00
54.28
O


ATOM
4158
O
HOH
W
379
64.478
−20.926
−14.628
1.00
56.28
O


ATOM
4159
O
HOH
W
380
70.262
−45.646
1.731
1.00
65.26
O


ATOM
4160
O
HOH
W
381
20.516
12.524
8.760
1.00
43.73
O


ATOM
4161
O
HOH
W
382
74.928
8.949
−8.247
1.00
54.24
O


ATOM
4162
O
HOH
W
383
18.257
−25.208
−7.910
1.00
50.96
O


ATOM
4163
O
HOH
W
384
34.170
18.737
17.233
1.00
47.03
O


ATOM
4164
O
HOH
W
385
21.137
2.084
3.808
1.00
65.70
O


ATOM
4165
O
HOH
W
386
38.186
−4.444
−15.698
1.00
66.07
O


ATOM
4166
O
HOH
W
387
38.985
−6.466
−8.831
1.00
51.93
O


ATOM
4167
O
HOH
W
388
3.906
−16.558
−13.958
1.00
54.64
O


ATOM
4168
O
HOH
W
389
33.087
−21.326
−9.095
1.00
66.75
O


ATOM
4169
O
HOH
W
390
27.295
−14.177
5.542
1.00
58.06
O


ATOM
4170
O
HOH
W
391
41.013
−5.818
20.816
1.00
60.46
O


ATOM
4171
O
HOH
W
392
22.713
1.185
14.363
1.00
64.09
O


ATOM
4172
O
HOH
W
393
48.064
6.165
1.998
1.00
61.05
O


ATOM
4173
O
HOH
W
394
46.193
7.105
3.046
1.00
37.46
O

## Claims

1. An amyloid β-peptide-immunoglobulin new antigen receptor fusion molecule (Aβ-IgNAR molecule) having the amino acid sequence of any one of SEQ ID NOs: 15 to 24.

2. The Aβ-IgNAR molecule of claim 1 having the amino acid sequence of SEQ ID NO: 15.

3. The Aβ-IgNAR molecule of claim 1 having the amino acid sequence of SEQ ID NO: 16.

4. The Aβ-IgNAR molecule of claim 1 having the amino acid sequence of SEQ ID NO: 17.

5. The Aβ-IgNAR molecule of claim 1 having the amino acid sequence of SEQ ID NO: 18.

6. The Aβ-IgNAR molecule of claim 1 having the amino acid sequence of SEQ ID NO: 19.

7. The Aβ-IgNAR molecule of claim 1 having the amino acid sequence of SEQ ID NO: 20.

8. The Aβ-IgNAR molecule of claim 1 having the amino acid sequence of SEQ ID NO: 21.

9. The Aβ-IgNAR molecule of claim 1 having the amino acid sequence of SEQ ID NO: 22.

10. The Aβ-IgNAR molecule of claim 1 having the amino acid sequence of SEQ ID NO: 23.

11. The Aβ-IgNAR molecule of claim 1 having the amino acid sequence of SEQ ID NO: 24.

12. A composition comprising a crystal having the coordinates set forth in Appendix I in space group P32 with cell parameters a=b=79.40, c=84.89 Å, which is produced from the Aβ-IgNAR molecule having the amino acid sequence of SEQ ID NO:2.

13. The composition of claim 12 in which the crystal comprises an Aβ-IgNAR molecule monomer.

14. The composition of claim 12 in which the crystal comprises an Aβ-IgNAR molecule dimer.

15. The composition of claim 12 in which the crystal comprises an Aβ-IgNAR molecule tetramer.

16. An amyloid β-peptide-immunoglobulin new antigen receptor fusion molecule (Aβ-IgNAR molecule) comprising amino acids in the sequence of residues 1-87 of the IgNAR set forth as SEQ ID NO:3 fused to amino acids in the sequence of residues 18-41 set forth as SEQ ID NO:1, the sequence of residues 88-111 set forth as SEQ ID NO:19, the sequence of residues 88-111 set forth as SEQ ID NO:20, the sequence of residues 88-111 set forth as SEQ ID NO:21, the sequence of residues 88-111 set forth as SEQ ID NO:22, the sequence of residues 88-110 set forth as SEQ ID NO:23, or the sequence of residues 88-111 set forth as SEQ ID NO:24.

17. The Aβ-IgNAR molecule of claim 16 comprising amino acids in the sequence of residues 1-87 of the IgNAR set forth as SEQ ID NO:3 fused to amino acids in the sequence of residues 18-41 set forth as SEQ ID NO:1.

18. The Aβ-IgNAR molecule of claim 16 comprising amino acids in the sequence of residues 1-87 of the IgNAR set forth as SEQ ID NO:3 fused to amino acids in the sequence of residues 88-111 set forth as SEQ ID NO:19.

19. The Aβ-IgNAR molecule of claim 16 comprising amino acids in the sequence of residues 1-87 of the IgNAR set forth as SEQ ID NO:3 fused to amino acids in the sequence of residues 88-111 set forth as SEQ ID NO:20.

20. The Aβ-IgNAR molecule of claim 16 comprising amino acids in the sequence of residues 1-87 of the IgNAR set forth as SEQ ID N0:3 fused to amino acids in the sequence of residues 88-111 set forth as SEQ ID NO:21.

21. The Aβ-IgNAR molecule of claim 16 comprising amino acids in the sequence of residues 1-87 of the IgNAR set forth as SEQ ID NO:3 fused to amino acids in, the sequence of residues 88-111 set forth as SEQ ID NO:22.

22. The Aβ-IgNAR molecule of claim 16 comprising amino acids in the sequence of residues 1-87 of the IgNAR set forth as SEQ ID NO:3 fused to amino acids in the sequence of residues 88-110 set forth as SEQ ID NO:23.

23. The Aβ-IgNAR molecule of claim 16 comprising amino acids in the sequence of residues 1-87 of the IgNAR set forth as SEQ ID NO:3 fused to amino acids in the sequence of residues 88-111 set forth as SEQ ID NO:24.