Bactericidal/permeability-increasing protein: crystallization, x-ray diffraction, three-dimensional structure determination, rational drug design and molecular modeling of related proteins

[0003] The present invention generally pertains to the fields of protein crystallization, x-ray diffraction analysis, three-dimensional structural determination, rational drug design and molecular modeling of related proteins. The present invention solves the three-dimensional structure of bactericidal/permeability-increasing protein (BPI) and provides crystallization methods for BPI protein products. A crystallized BPI protein product was physically analyzed by x-ray diffraction techniques. The resulting x-ray diffraction patterns were of sufficiently high resolution to be useful for determining the three-dimensional structure of BPI and have yielded atomic coordinates for BPI. The present invention relates to uses of BPI coordinates for molecular modeling of related proteins and rational drug design (RDD) of mimetics and ligands for BPI and for related proteins. The present invention also relates to atomic coordinates of BPI, or portions thereof, to solve crystal forms of BPI proteins or their fragments, analogs, and variants thereof, or of related proteins, including lipid transfer proteins, or their fragments, analogs and variants.

BACKGROUND OF THE INVENTION

[0004] Bactericidal/permeability-increasing protein (BPI) is a protein isolated from the granules of mammalian polymorphonuclear leukocytes (PMNs or neutrophils), which are blood cells essential in the defense against invading microorganisms. BPI is known to bind the lipopolysaccharide (LPS), a major component of the outer membrane of gram-negative bacteria that stimulates a potent inflammatory response. Human BPI protein has been isolated from PMNs by acid extraction combined with either ion exchange chromatography [Elsbach, J. Biol. Chem., 254:11000 (1979)] or E. coli affinity chromatography [Weiss, et al., Blood, 69:652 (1987)]. BPI obtained in such a manner is referred to herein as natural BPI and has been shown to have potent bactericidal activity against a broad spectrum of gram-negative bacteria. The molecular weight of human BPI is approximately 55,000 daltons (55 kD). The amino acid sequence of the entire human BPI protein and the nucleic acid sequence of DNA encoding the protein have been reported in FIG. 1 of Gray et al., J. Biol. Chem., 264:9505 (1989), incorporated herein by reference. The Gray et al. amino acid sequence is set out in SEQ ID NO: 1 hereto. U.S. Pat. No. 5,198,541, EP0375724 and WO89/10486 (PCT/US88/02700) disclose recombinant genes encoding and methods for expression of BPI proteins, including BPI holoprotein and fragments of BPI.

[0005] A proteolytic N-terminal fragment of BPI having a molecular weight of about 25 kD possesses essentially all the anti-bacterial efficacy of the naturally-derived 55 kD human BPI holoprotein. [Ooi et al., J. Bio. Chem., 262: 14891-14894 (1987)]. In contrast to the N-terminal portion, the C-terminal region of the isolated human BPI protein displays only slightly detectable anti-bacterial activity against gram-negative organisms. [Ooi et al., J. Exp. Med., 174:649 (1991).] An N-terminal BPI fragment of approximately 23 kD, referred to as “rBPI23,” has been produced by recombinant means and also retains anti-bacterial activity against gram-negative organisms. [Gazzano-Santoro et al., Infect. Immun. 60:4754-4761 (1992).] An N-terminal analog of BPI, rBPI21, has been produced as described in Horwitz et al., Protein Expression Purification, 8:28-40 (1996).

[0006] The bactericidal effect of BPI has been reported to be highly specific to gram-negative species, e.g., in Elsbach and Weiss, Inflammation: Basic Principles and Clinical Correlates, eds. Gallin et al., Chapter 30, Raven Press, Ltd. (1992). This reported target cell specificity was believed to be the result of the strong attraction of BPI for LPS on the outer membrane (or envelope) of gram-negative organisms. Although BPI was commonly thought to be non-toxic for other microorganisms, including yeast and for higher eukaryotic cells, it has recently been discovered that BPI protein products exhibit activity against gram-positive bacteria, mycoplasma, mycobacteria, fungi, protozoa and chlamydia.

[0007] The precise mechanism by which BPI kills gram-negative bacteria is not yet completely elucidated, but it is believed that BPI must first bind to the surface of the bacteria through electrostatic and hydrophobic interactions between the cationic BPI protein and negatively charged sites on lipopolysaccharide. Bacterial LPS has been referred to as “endotoxin” because of the potent inflammatory response that it stimulates, i.e., the release of mediators by host inflammatory cells which may ultimately result in irreversible endotoxic shock. BPI binds to lipid A, reported to be the most toxic and most biologically active component of LPS.

[0008] In susceptible gram-negative bacteria, BPI binding is thought to disrupt LPS structure, leading to activation of bacterial enzymes that degrade phospholipids and peptidoglycans, altering the permeability of the cell's outer membrane, and initiating events that ultimately lead to cell death. [Elsbach and Weiss (1992), supra]. BPI has been proposed to act in two stages. The first stage proposed is a sublethal one that is characterized by immediate growth arrest, permeabilization of the outer membrane and selective activation of bacterial enzymes that hydrolyze phospholipids and peptidoglycans. Bacteria at this stage could be rescued by growth in serum albumin supplemented media [Mannion et al., J. Clin. Invest., 85:853-860 (1990)]. The second stage, defined by growth inhibition that cannot be reversed by serum albumin, is proposed to occur after prolonged exposure of the bacteria to BPI and characterized by extensive physiologic and structural changes, including apparent damage to the inner cytoplasmic membrane.

[0009] Initial binding of BPI to LPS leads to organizational changes that probably result from binding to the anionic groups of LPS, which normally stabilize the outer membrane through binding of Mg++ and Ca++. Attachment of BPI to the outer membrane of gram-negative bacteria produces rapid permeabilization of the outer membrane to hydrophobic agents such as actinomycin D. Binding of BPI and subsequent gram-negative bacterial killing depends, at least in part, upon the LPS polysaccharide chain length, with long O-chain bearing, “smooth” organisms being more resistant to BPI bactericidal effects than short O-chain bearing, “rough” organisms [Weiss et al., J. Clin. Invest. 65: 619-628 (1980)]. This permeabilization of the gram-negative outer envelope is reversible upon dissociation of the BPI, a process requiring high concentrations of divalent cations and synthesis of new LPS [Weiss et al., J. Immunol. 132: 3109-3115 (1984)]. Loss of gram-negative bacterial viability, however, is not reversed by processes which restore the envelope integrity, suggesting that the bactericidal action is mediated by additional lesions induced in the target organism and which may be situated at the cytoplasmic membrane (Mannion et al., J. Clin. Invest. 86: 631-641 (1990)). Specific investigation of this possibility has shown that on a molar basis BPI is at least as inhibitory of cytoplasmic membrane vesicle function as polymyxin B but the exact mechanism as well as the relevance of such vesicles to studies of intact organisms was not elucidated (In't Veld, et al., Infection and Immunity 56: 1203-1208 (1988)).

[0010] BPI is a member of a gene/protein family of lipopolysaccharide binding and lipid transfer proteins whose other currently known members include lipopolysaccharide binding protein (LBP), cholesteryl ester transfer protein (CETP) and phospholipid transfer protein (PLTP).

[0011] BPI protein products (which include naturally and recombinantly produced BPI protein; natural, synthetic, and recombinant biologically active polypeptide fragments of BPI protein; biologically active polypeptide variants of BPI protein or fragments thereof, including hybrid fusion proteins and dimers; biologically active polypeptide analogs of BPI protein or fragments or variants thereof, including cysteine-substituted analogs; and BPI-derived peptides) have been demonstrated to have a variety of beneficial activities. BPI protein products are known to be bactericidal for gram-negative bacteria, as described in U.S. Pat. Nos. 5,198,541 and 5,523,288, both of which are incorporated herein by reference. BPI protein products are also known to enhance the effectiveness of antibiotic therapy in gram-negative bacterial infections, as described in U.S. Pat. No. 5,523,288 and corresponding International Publication No. WO 95/08344 (PCT/US94/11225), which are incorporated herein by reference. BPI protein products are also known to be bactericidal for gram-positive bacteria and mycoplasma, and to enhance the effectiveness of antibiotics in gram-positive bacterial infections, as described in U.S. Pat. No. 5,578,572 and corresponding International Publication No. WO 95/19180 (PCT/US95/00656), which are incorporated herein by reference. BPI protein products are further known to exhibit anti-fungal activity, and to enhance the activity of other anti-fungal agents, as described in U.S. Pat. No. 5,627,153 and corresponding International Publication No. WO 95/19179 (PCT/US95/00498), and further as described for anti-fungal peptides in U.S. Pat. Nos. 6,156,730 and 5,858,974, which is in turn a continuation-in-part of U.S. application Ser. No. 08/504,841 filed Jul. 20, 1995 and corresponding International Publication Nos. WO 96/08509 (PCT/US95/09262) and WO 97/04008 (PCT/US96/03845), all of which are incorporated herein by reference. BPI protein products are further known to exhibit anti-protozoan activity, as described in U.S. Pat. Nos. 5,646,114 and 6,013,629 and corresponding International Publication No. WO 96/01647 (PCT/US95/08624), all of which are incorporated herein by reference. BPI protein products are known to exhibit anti-chlamydial activity, as described in U.S. Pat. Nos. 5,888,973 and 6,162,788, and corresponding International Publication No. WO 98/06415 (PCT/US97/13810), all of which are incorporated herein by reference. Finally, BPI protein products are known to exhibit anti-mycobacterial activity, as described in U.S. Pat. No. 6,214,289 which is in turn a continuation of U.S. application Ser. No. 08/285,803 filed Aug. 14, 1994, which is in turn a continuation-in-part of U.S. application Ser. No. 08/031,145 filed Mar. 12, 1993 and corresponding International Publication No. WO94/20129 (PCT/US94/02463), all of which are incorporated herein by reference.

[0012] The effects of BPI protein products in humans with endotoxin in circulation, including effects on TNF, IL-6 and endotoxin are described in U.S. Pat. Nos. 5,643,875, 5,753,620, 5,952,302 and 6,191,112 and corresponding International Publication No. WO 95/19784 (PCT/US95/01151), all of which are incorporated herein by reference.

[0013] BPI protein products are also known to be useful for treatment of specific disease conditions, such as meningococcemia in humans (as described in U.S. Pat. Nos. 5,888,977 and 5,990,086, and corresponding International Publication No. WO 97/42966 (PCT/US97/08016), which are incorporated herein by reference), hemorrhagic trauma in humans, (as described in U.S. Pat. No. 5,945,399, a continuation-in-part of U.S. application Ser. No. 08/652,292 filed May 23, 1996, now U.S. Pat. No. 5,756,464, and corresponding International Publication No. WO 97/44056 (PCT/US97/08941), all of which are incorporated herein by reference), burn injury (as described in U.S. Pat. No. 5,494,896 and corresponding International Publication No. WO 96/30037 (PCT/US96/02349), both of which are incorporated herein by reference), ischemia/reperfusion injury (as described in U.S. Pat. Nos. 5,578,568 and 6,017,881, incorporated herein by reference), and liver resection (as described in co-pending U.S. application Ser. No. 09/689,097 filed Oct. 12, 2000 which is a continuation of U.S. application Ser. No. 09/466,412 filed Dec. 17, 1999 which is a continuation of U.S. application Ser. No. 08/582,230 filed Mar. 16, 1998 which is a continued prosecution application of the same serial no. filed Jan. 3, 1996, which is in turn a continuation of U.S. application Ser. No. 08/318,357 filed Oct. 5, 1994, which is in turn a continuation-in-part of U.S. application Ser. No. 08/132,510 filed Oct. 5, 1993, and corresponding International Publication No. WO 95/10297 (PCT/US94/11404), all of which are incorporated herein by reference).

[0014] BPI protein products are also known to neutralize the anti-coagulant activity of exogenous heparin, as described in U.S. Pat. No. 5,348,942, incorporated herein by reference, as well as to be useful for treating chronic inflammatory diseases such as rheumatoid and reactive arthritis, as described in U.S. Pat. No. 5,639,727, incorporated herein by reference, and for inhibiting angiogenesis and for treating angiogenesis-associated disorders including malignant tumors, ocular retinopathy and endometriosis, as described in U.S. Pat. Nos. 5,807,818, 5,837,678 and 5,854,214, and corresponding International Publication No. WO 94/20128 (PCT/US94/02401), all of which are incorporated herein by reference.

[0015] BPI protein products are also known for use in antithrombotic methods, as described in U.S. Pat. Nos. 5,741,779, 5,935,930 and 6,107,280, and corresponding International Publication No. WO97/42967 (PCT/US97/08017), which are incorporated herein by reference.

[0016] U.S. Pat. Nos. 5,420,019, 5,827,816 and 5,674,834 and corresponding International Publication No. WO94/18323 (PCT/US94/01235), all of which are incorporated herein by reference, disclose that the replacement of the cysteine residue at amino acid position 132 or 135 with another amino acid renders the resulting BPI polypeptide resistant to dimerization and cysteine adduct formation. It also discloses that terminating the N-terminal BPI fragment at BPI amino acid position 193 resulted in an expression product with reduced carboxy-terminal heterogeneity.

[0017] Because of the multiplicity of valuable activities and uses of BPI protein products as exemplified above, a need continues to exist for new products with structures based on or mimicking a BPI protein product and having one or more of the activities and/or uses of BPI protein products, including use as anti-infective products, including antimicrobial agents (e.g., gram-negative bacteria [U.S. Pat. Nos. 5,198,541 and 5,523,288; WO95/08344 (PCT/US94/11225)] and gram-positive bacteria [U.S. Pat. Nos. 5,578,572, 5,783,561 and 6,054,431; WO95/19180 (PCT/US95/00656)], fungi [U.S. Pat. No. 5,627,153; WO95/19179 (PCT/US95/00498)], mycobacteria [U.S. Pat. No. 6,214,789, EP0690721; WO94/20129 (PCT/US94/02463)] and chlamydia [U.S. Pat. No. 6,162,788, WO96/01647 (PCT/US95/08624)] and endotoxin binding/neutralizing agents [WO95/019784 (PCT/US95/01151)], and as heparin binding/neutralizing products [U.S. Pat. Nos. 5,348,942 and 5,639,727; WO94/20128 (PCT/US94/02401)], including for the neutralization of exogenously administered heparin, inhibition of angiogenesis (normal or pathological) for the treatment of chronic inflammatory disease states, anticoagulant and thrombolytic agents for the treatment of thrombotic disorders [WO97/42976 (PCT/US97/08017)], for inhibiting H+/K+ ATPase activity [WO01/03724 (PCT/US00/09125)] for modulation of pericyte proliferation [U.S. application Ser. No. 60/250,542], for treating conditions associated with corneal injury [WO97/17990 (PCT/US96/18632)], for treating conditions associated with corneal transplantation [U.S. Pat. No. 5,686,414; WO97/17989 (PCT/US96/18416)], for use in ANCA-positive humans [U.S. application Ser. Nos. 08/742,985 and 09/255,245], for use in cystic fibrosis patients [WO98/19694 (PCT/US97/19850)], for treating chronic cardiac disease [WO00/43028 (PCT/US00/01515)], for treating BPI-deficient humans [U.S. Pat. No. 6,153,584; WO00/59531 (PCT/US00/08864)], and for use in humans with otitis media with effusion [WO00/71149 (PCT/US00/14496)]. All of the above-listed references regarding biological or functional activities of BPI, as well as therapeutic and diagnostic uses of BPI, are hereby incorporated by reference. One avenue of investigation toward solving the problem of new products based on BPI and fulfilling this need is the determination of the crystal structure of a BPI protein product.

SUMMARY OF THE INVENTION

[0018] The present invention solves the above problem and fulfills the need for designing and making new and useful products based on BPI. It is an object of this invention to solve the three-dimensional structure of BPI and thereby provide the atomic coordinates (i.e., structure coordinates) of BPI from the analysis of x-ray diffraction patterns of sufficiently high resolution to be useful for determining the three-dimensional protein structure.

[0019] It is an object of this invention to provide methods of expressing, purifying and crystallizing bactericidal/permeability-increasing protein (BPI) products, and thereby provide crystallized BPI proteins.

[0020] It is an object of this invention to provide the use of the structure coordinates of a BPI crystal to allow the design of compounds for mimicking a BPI protein product to reveal the atomic details of ligand binding sites of BPI (e.g. lipid-like or heparin-like molecules).

[0021] It is an object of this invention to provide use of the structure coordinates of a BPI crystal as described herein to solve the crystal structure of a crystal of a different BPI protein or fragment, analog or variant thereof, or a crystal of a related protein, including a BPI-related lipid transfer protein or a fragment, analog or variant thereof.

[0022] It is an object of this invention to provide mutants of BPI or fragments, analogs, or variants thereof characterized by one or more different properties as compared with wild-type BPI. These properties include altered surface charge, altered lipid binding pockets, altered specificity or higher activity. BPI mutants are useful to identify those amino acids that are most important for the lipid and heparin binding activity and other biological activities of BPI. This information, in turn, allows the design of new structures with one or more different properties based on BPI.

[0023] It is an object of this invention to provide the use of the structure coordinates and atomic details of BPI as described herein or its fragments, analogs or variants (including mutants or co-complexes) or of a BPI-related lipid transfer protein or its fragments, analogs or variants (including mutants or co-complexes) to design, evaluate computationally, synthesize and use new structures based on BPI with desirable properties of BPI, such as physical and pharmacological properties.

[0024] X-ray diffraction patterns of a related protein can be analyzed directly to provide the three-dimensional structure (if of sufficiently high resolution), however, the atomic coordinates for the crystallized BPI, as provided herein, can be used for structure determination. The x-ray diffraction patterns obtained by methods of the present invention, and provided on computer readable media, are used to provide electron density maps. The amino acid sequence is also useful for three-dimensional structure determination. The data is then used in combination with phase determination (e.g. using multiple isomorphous replacement (MIR) molecular replacement techniques) to generate electron density maps of BPI, using a suitable computer system. The electron density maps, provided by analysis of either the x-ray diffraction patterns or working backwards from the atomic coordinates, provided herein, are then fitted using suitable computer algorithms to generate secondary, tertiary and/or quaternary structures and/or domains of BPI, which structures and/or domains are then used to provide an overall three-dimensional structure, as well as binding and/or active sites of BPI.

[0025] It is also an object of this invention to specifically provide for the use of three-dimensional modeling of BPI and other members of the BPI protein family using the coordinates from the x-ray diffraction patterns. The coordinates and amino acid sequences are entered into one or more computer programs for molecular modeling. Such molecular modeling programs generate atomic coordinates that reflect the secondary, tertiary and/or quaternary structures of the protein which contribute to its overall three-dimensional structure and provide information related to binding and/or active sites of the protein.

[0026] It is a further object of this invention to specifically provide for the use of similar molecular modeling for rational drug design (RDD) of mimetics and ligands of BPI and other members of the BPI protein family. The drug design paradigm uses computer modeling programs to determine potential mimetics and ligands which are expected to interact with sites on the protein. The potential mimetics or ligands are then screened for activity and/or binding. For BPI-related mimetics or ligands, screening methods can be selected from assays for at least one biological activity of BPI, e.g., anti-microbial, LPS-binding/neutralizing, heparin binding/neutralizing, and/or anti-thrombotic activities, according to known method steps. Similarly for LBP-, CETP- or PLTP-related mimetics or ligands, such screening methods can be selected from assays for at least one biological activity of LBP, CETP or PLTP, according to known method steps. The resulting mimetics or ligands are then provided by methods of the present invention and are useful for treating, inhibiting or preventing BPI-modulated diseases (or LBP-, CETP- and PLTP-modulated) in animals, including humans.

[0027] Thus, as described herein, the present invention provides use of atomic coordinates of a BPI protein, or fragment, analog or variant thereof, to model a BPI protein or a related protein, including a BPI-related lipid transfer protein, such as LBP, CETP or PLTP, or fragment, analog or variant thereof.

[0028] The present invention also provides use of atomic coordinates of a BPI protein wherein the BPI protein comprises a binding site characterized by amino acid residues of at least one binding pocket as defined in Table 3, and/or wherein the BPI protein comprises a binding site characterized by at least one amino acid sequence, or variant of the sequence, selected from positions about 17 to about 45, positions about 65 to about 99 or positions about 142 to about 169 of BPI, or alternatively, a binding site characterized by at least one amino acid sequence, or variant of the sequence, selected from positions about 36 to about 54, positions about 84 to about 109 or positions about 142 to about 164 of BPI.

[0029] The present invention provides use of atomic coordinates of a BPI protein to computationally design a chemical compound for mimicking a BPI protein, or fragment, analog or variant thereof, or a BPI-related lipid transfer protein, or fragment, analog or variant thereof, including, for example, lipopolysaccharide-binding protein (LBP), cholesteryl ester transferase protein (CETP) or phospholipid transfer protein (PLTP), or fragment, analog, or variant thereof.

[0030] The present invention also provides use of atomic coordinates of BPI protein to design a chemical compound capable of associating with a BPI-related lipid binding protein, or fragment, analog or variant thereof, including, for example, bactericidal/permeability-increasing protein (BPI), lipopolysaccharide-binding protein (LBP), cholesteryl ester transferase protein (CETP) or phospholipid transfer protein (PLTP), or fragment, analog or variant thereof.

[0031] The present invention provides use of atomic coordinates of a BPI protein to design a model of ligands in an active site of a lipid binding protein, including, for example, BPI protein, lipopolysaccharide-binding protein (LBP), cholesteryl ester transferase protein (CETP) or phospholipid transfer protein (PLTP), or fragment, analog or variant thereof.

[0032] The present invention provides use of atomic coordinates of a bactericidal/permeability-increasing (“BPI”) protein, to design compounds with at least one activity of antibacterial, antifungal, antimycobacterial, antichlamydial, antiprotozoan, heparin-binding, endotoxin-binding, heparin-neutralizing, endotoxin-neutralizing, inhibition of tumor and endothelial cell proliferation, inhibition of angiogenesis, anti-inflammatory, anticoagulant or antithrombolytic, enhancement of pericyte cell proliferation, enhancement of antibiotic activity or susceptibility, or inhibition of H+/K+ ATPase activity. The coordinates disclosed herein are suitable for all of the aforementioned uses of atomic coordinates.

[0033] The present invention provides a method of three-dimensional modeling of a BPI protein or BPI-related lipid transfer protein comprising the steps of: (a) providing three-dimensional atomic coordinates derived from X-ray diffraction measurements of a BPI protein in a computer readable format; (b) inputting the data from step (a) into a computer with appropriate software programs; and (c) generating a three-dimensional structural representation of the BPI protein or BPI-related lipid transfer protein suitable for visualization and further computational manipulation; particularly wherein the BPI protein comprises a binding site characterized by amino acid residues of at least one binding pocket as defined in Table 3, or wherein the BPI protein comprises a binding site characterized by at least one amino acid sequence, or variant of the sequence, selected from positions about 17 to about 45, positions about 65 to about 99 or positions about 142 to about 169 of BPI or wherein the BPI protein comprises a binding site characterized by amino acid residues of at least one binding pocket as defined in Table 3 and a binding site characterized by at least one amino acid sequence, or variant of the sequence, selected from positions about 36 to about 54, positions about 84 to about 109 or positions about 142 to about 164 of BPI, or alternatively from about positions 36 to about 54, from about positions 84 to about 109, or about positions 142 to about 164.

[0034] The present invention provides a method for providing an atomic model of a BPI protein, BPI-related lipid binding protein, or fragment, analog or variant thereof, comprising (a) providing a computer readable medium having stored, thereon atomic coordinate/x-ray diffraction data of a BPI protein, or fragment, analog or variant thereof, in crystalline form, the data sufficient to model the three-dimensional structure of the BPI protein, or fragment, analog or variant thereof; (b) analyzing, on a computer using at least one subroutine executed in said computer, atomic coordinate/x-ray diffraction data from (a) to provide atomic coordinate data output defining an atomic model of said BPI protein, BPI-related binding lipid protein or fragment, analog or variant thereof, said analyzing utilizing at least one computing algorithm selected from the group consisting of data processing and reduction, auto-indexing, intensity scaling, intensity merging, amplitude conversion, truncation, molecular replacement, molecular alignment, molecular refinement, electron density map calculation, electron density modification, electron map visualization, model building, rigid body refinement, positional refinement; and (c) obtaining atomic coordinate data defining the three-dimensional structure of at least one of said BPI protein, BPI-related lipid binding protein, or fragment, analog or variant thereof; particularly wherein said computer readable medium further has stored thereon data corresponding to a nucleic acid sequence or an amino acid sequence data comprising at least one structural domain or functional domain of a BPI, LBP, CETP or PLTP corresponding to at least one BPI or mutant primary sequence or fragment, analog or variant thereof; and wherein said analyzing step further comprises analyzing said sequence data.

[0035] The present invention provides a computer-based system for providing atomic model data of the three-dimensional structure of a BPI protein, BPI-related lipid binding protein or fragment, analog or variant thereof, comprising the following elements: (a) at least one computer readable medium (CRM) having stored thereon atomic coordinate/x-ray diffraction data of a BPI protein, or fragment, analog or variant thereof; (b) at least one computing subroutine that, when executed in a computer, causes the computer to analyze atomic coordinate/x-ray diffraction data from (a) to provide atomic coordinate data output defining an atomic model of a BPI protein, BPI-related lipid binding protein or fragment, analog or variant thereof, said analyzing utilizing at least one computing subroutine selected from the group consisting of data processing and reduction, auto-indexing, intensity scaling, intensity merging, amplitude conversion, truncation, molecular replacement, molecular alignment, molecular refinement, electron density map calculation, electron density modification, electron map visualization, model building, rigid body refinement, positional refinement; and (c) retrieval means for obtaining atomic coordinate output data substantially defining the three-dimensional structure of said BPI protein, BPI-related lipid binding protein or fragment, analog or variant thereof.

[0036] The present invention provides a method for providing a computer atomic model of a ligand of a BPI protein, BPI-related lipid binding protein, or fragment, analog or variant thereof, comprising: (a) providing a computer readable medium (CRM) having stored thereon atomic coordinate data of a BPI protein, or fragment, analog, or variant thereof; (b) providing a CRM having stored thereon atomic coordinate data sufficient to generate atomic models of potential ligands of said BPI protein, BPI-related lipid binding protein, or fragment, analog, or variant thereof; (c) analyzing on a computer, using at least one subroutine executed in said computer, the atomic coordinate data from (a) and ligand data from (b), to determine binding sites of BPI protein, BPI-related lipid binding protein, or fragment, analog, or variant thereof, and to provide atomic coordinate data defining an atomic model of at least one ligand of said BPI protein, BPI-related lipid binding protein, or fragment, analog or variant thereof, said analyzing utilizing computing subroutines selected from the group consisting of data processing and reduction, auto-indexing, intensity scaling, intensity merging, amplitude conversion, truncation, molecular replacement, molecular alignment, molecular refinement, electron density map calculation, electron density modification, electron map visualization, model building, rigid body refinement, positional refinement; and (d) obtaining atomic coordinate model output data defining the three-dimensional structure of said at least one ligand of said BPI protein, BPI-related lipid binding protein, or fragment, analog, or variant thereof.

[0037] The present invention provides a computer-based system for providing an atomic model of at least one ligand of a BPI protein, BPI-related lipid binding protein, or fragment, analog or variant thereof, comprising the following elements: (a) a computer readable medium (CRM) having stored thereon atomic coordinate data of a BPI protein, fragment, analog or variant thereof; (b) a CRM having stored thereon atomic coordinate data sufficient to generate atomic models of potential ligands of a BPI protein, BPI-related lipid binding protein, or fragment, analog or variant thereof; (c) at least one computing subroutine for analyzing on a computer, the atomic coordinate data from (a) and (b), to determine binding sites of BPI protein, BPI-related lipid binding protein, or fragment, analog, or variant thereof, and to provide data output defining an atomic model of at least one potential ligand of BPI protein, BPI-related lipid binding protein, or fragment, analog, or variant thereof, said analyzing utilizing at least one computing subroutine selected from the group consisting of data processing and reduction, auto-indexing, intensity scaling, intensity merging, amplitude conversion, truncation, molecular replacement, molecular alignment, molecular refinement, electron density map calculation, electron density modification, electron map visualization, model building, rigid body refinement, positional refinement; and (d) retrieval means for obtaining atomic coordinate data of said at least one ligand of a BPI protein, BPI-related lipid binding protein, or fragment, analog or variant thereof.

[0038] Other objects of the invention will be apparent to one of ordinary skill in the art from the following detailed description and examples relating to the present invention.

BRIEF DESCRIPTION OF THE FIGURES

[0039]
FIG. 1(A) A ribbon diagram of residues 1-456 of BPI illustrating its boomerang shape. The NH2-terminal domain is shown; the COOH-terminal domain and the two phosphatidylcholine molecules are shown. The linker is also shown, and the disulfide bond is shown as a ball-and-stick model. (B) View after rotating (A) 70° about the long axis of the molecule. Figure produced with MOLSCRIPT [P. Krauliz, J. Appl. Cryst., 24:926 (1991)] and RASTER3D [E. A. Merrit and M. E. P. Murphy, Acta Crystallogr., D50:889 (1994); D. J. Bacon and W. F. Anderson, J. Mo. Graphics, 6:219 (1988)].

[0040]
FIG. 2(A) Schematic drawing of the novel BPI domain fold, shown in same orientation as the NH2-terminal domain in FIG. 1B (B) Superposition of the NH2- and COOH-terminal domains of BPI showing the overall topological similarity. Residues 1 to 230 and 250 to 456 are shown. The NH2-terminal domain is in the same orientation as FIG. 1A.

[0041]
FIG. 3 Electron density of the final 2.8 Å MIR map contoured at 1.0σ and superimposed on the refined model. The area shown is in the lipid binding pocket of the NH2-terminal domain of BPI. The phosphatidylcholine and the surrounding protein atoms are shown.

[0042]
FIG. 4(A) The covalent structure of phosphatidylcholine and the lipid A region of LPS from E. coli and S. typhimurium. Phosphate groups are indicated by P. Adapted with changes from [C. R. H. Raetz, Annu. Rev. Biochem, 59:129 (1990)]. (B) Slice through the interior of BPI showing the lipid binding pocket in the NH2-terminal domain. The solvent accessible surface of the protein was calculated without lipid present, the interior of the protein and the phosphatidylcholine are shown. Protein residues are shown as ball-and-stick. Figure produced with MSP [M. L. Connolly, Science, 221:709 (1983); M. L. Connolly, J. Am. Chem. Soc., 107:1118 (1985)].

[0043] FIGS. 5(A) and 5(B) The amino acid sequences of human BPI, LBP, PLTP, and CETP. The alignment was performed with CLUSTAL [D. G. Higgins and P. M. Sharp, Gene, 73:237 (1989)] using all eleven known protein sequences from mammals [R. R. Schuman, et al., Science, 249:1429 (1990); D. Drayna et al., Nature, 327:632 (1987); R. Day et al., J. Biol. Chem., 269:9388 (1994); S. R. Leong and T. Camerato, Nucleic Acids Res., 18:3052 (1990); M. Nagashima, J. W. McLean, R. M. Lawn, J. Lipid Res., 29:1643 (1988); M. E. Pape, E. F. Rehber, K. R. Marotti, G. W. Melchior, Artheriosclerosis 11:1759 (1991); G. Su et al., J. Immunol., 153:743 (1994); P. W. Gray et al., J. Biol. Chem. 264: 9505 (1989); Albers et al., Biochem. Biophys. Acta, 1258:27 (1995); X. C. Jiang et al., Biochemistry, 34:7258 (1995); L. B. Agellon et al., Biochemistry, 29:1372 (1990); X. C. Jiang et al., J. Biol. Chem., 266:4631 (1991)] but only the four human sequences are shown. Residues that are completely conserved in all proteins are indicated below the sequence *; those which are highly conserved are indicated by •. The secondary structure of BPI is indicated above the sequences. The β strands are indicated by arrows; strands which make up the central β sheet are shown with gray arrows. Because of the β bulges and pronounced twisting, some of the β strands have one or more residues that do not show classical H-bonding patterns or ΦΨ angles; these breaks are indicated by {circumflex over ( )} above the strands. The a helices are shown as cylinders, and one-residue breaks in helices B and B′ are indicated with a vertical dashed line. The horizontal dashed line indicates the linker region. Peptides from BPI and LBP with the highest LPS-binding activity (Little, et al., J. Biol. Chem. 268: 1865 (1994); Taylor et al., J. Biol. Chem. 270: 17934 (1995)) are in bold italics. The disulfide bond is indicated by S-S. Residues with atoms within 4 Å of the NH2-terminal lipid are highlighted with gray shading; residues within 4 Å of the COOH-terminal lipid are shown with white letters in black boxes.

[0044]
FIG. 6 Block diagram of a computer system 102 that can be used to implement the present invention. The computer system 102 includes a processor 106 connected to a bus 104. Also connected to the bus 104 are a main memory 108 (preferably implemented as random access memory, RAM) and a variety of secondary storage memory 110, such as a hard drive 112, a removable medium storage device 114, a command device 118, and a visualization device, 120. Also included is a removable storage medium 116.

[0045]
FIG. 7(A) A ribbon diagram of residues 1-456 of the 1.7 Å crystal structure of BPI. The NH2-terminal domain is blue, and the COOH-terminal is red. (B) Superposition of the NH2-terminal domain (blue) on the COOH-terminal domain (red). (C) Schematic drawing of BPI showing its elongated shape and two-domain structure. Residues 1 to 229 and 251 to 456 are shown.

[0046]
FIG. 8 Illustration of three major categories of pairs of 3D-1D environmentally conserved positions with dissimilar residues: (A) Conserved structural roles; (B) Auxiliary structural roles; (C) Different structural roles.

[0047]
FIG. 9 Examples (A), (B) and (C) of pairs of 3D-1D environmentally conserved residues with dissimilar residues and conserved structural roles from the BPI domain alignment. Residues and secondary structure elements from the NH2-terminal domain are blue; residues and secondary structure elements from the COOH-terminal domain are red.

[0048]
FIG. 10(A) Space-filling representation of BPI. The NH2-terminal domain is shown on the left. (B) View after rotating (A) 90° about the long axis of the molecule. (C) Ball-and-stick model and space-filling representation of the interaction of 3D-1D environmentally conserved positions in the NH2-terminal lipid-binding pocket. (D) Ball-and stick model and space-filling representation of the interaction of 3D-1D environmentally conserved positions in the COOH-terminal domain.

DETAILED DESCRIPTION

[0049] The present invention provides methods for crystallizing a BPI protein product where the crystals diffract x-rays with sufficiently high resolution to allow determination of the three-dimensional structure of the BPI protein product, including atomic coordinates. The three-dimensional structure (e.g, as provided on computer readable media as described herein) is useful for rational drug design of BPI-related (and LBP-, CETP-, PLTP-related) mimetics and/or ligands. Specifically provided is a method for crystallizing a recombinant non-glycosylated human BPI analog holoprotein comprising a 456 amino acid sequence wherein the amino acid serine at position 351 has been changed to alanine. The three-dimensional structure is useful for modeling and/or synthesizing BPI-related mimetics or ligands. Such BPI-related mimetics or ligands are useful for treating, inhibiting or preventing BPI-modulated diseases.

[0050] The present invention thus includes methods of expressing, purifying and crystallizing a BPI protein product from suitable sources, such as eukaryotic cells or tissues. The present invention also provides crystallized BPI protein products by these methods. The crystallized BPI is analyzed by x-ray diffraction techniques to obtain high resolution diffraction patterns and atomic coordinates that are suitable for molecular modeling.

[0051] As used herein, “BPI protein product” or “BPI protein” includes naturally and recombinantly produced BPI protein; natural, synthetic, and recombinant biologically active polypeptide fragments of BPI protein; biologically active polypeptide variants of BPI protein or fragments thereof, including hybrid fusion proteins and dimers; biologically active polypeptide analogs of BPI protein or fragments or variants thereof, including cysteine-substituted analogs; and BPI-derived peptides. The BPI protein products for therapeutic or diagnostic uses may be generated and/or isolated by any means known in the art. U.S. Pat. No. 5,198,541, the disclosure of which is incorporated herein by reference, discloses recombinant genes encoding and methods for expression of BPI proteins including recombinant BPI holoprotein, referred to as rBPI (also referred to as rBPI55 or simply rBPI50) and recombinant fragments of BPI. U.S. patent application Ser. No. 07/885,501, now abandoned, and a continuation-in-part thereof, U.S. patent application Ser. No. 08/072,063, filed May 19, 1993, issued as U.S. Pat. No. 5,439,807 on Aug, 8, 1995 and corresponding PCT Application No. 93/04752 filed May 19, 1993, which are all incorporated herein by reference, disclose novel methods for the purification of recombinant BPI protein products expressed in and secreted from genetically transformed mammalian host cells in culture and discloses how one may produce large quantities of recombinant BPI products suitable for incorporation into stable, homogeneous pharmaceutical preparations.

[0052] Biologically active fragments of BPI (BPI fragments) include biologically active molecules that have the same or similar amino acid sequence as a natural human BPI holoprotein, except that the fragment molecule lacks amino-terminal amino acids, internal amino acids, and/or carboxy-terminal amino acids of the holoprotein. Nonlimiting examples of such fragments include a N-terminal fragment of natural human BPI of approximately 25 kD, described in Ooi et al., J. Exp. Med., 174:649 (1991), and the recombinant expression product of DNA encoding N-terminal amino acids from 1 to about 193 or 199 of natural human BPI, described in Gazzano-Santoro et al., Infect. Immun. 60:4754-4761 (1992), and referred to as rBPI23. In that publication, an expression vector was used as a source of DNA encoding a recombinant expression product (rBPI23) having the 31-residue signal sequence and the first 199 amino acids of the N-terminus of the mature human BPI, as set out in FIG. 1 of Gray et al., supra, except that valine at position 151 is specified by GTG rather than GTC and residue 185 is glutamic acid (specified by GAG) rather than lysine (specified by AAG). Recombinant holoprotein (rBPI) has also been produced having the sequence (SEQ ID NOS: 1 and 2) set out in FIG. 1 of Gray et al., supra, with the exceptions noted for rBPI23 and with the exception that residue 417 is alanine (specified by GCT) rather than valine (specified by GTT). Other examples include dimeric forms of BPI fragments, as described in U.S. Pat. No. 5,447,913, and corresponding PCT Application No. PCT/US95/03125, the disclosures of which are incorporated herein by reference. Preferred dimeric products include dimeric BPI protein products wherein the monomers are amino-terminal BPI fragments having the N-terminal residues from about 1 to 175 to about 1 to 199 of BPI holoprotein. A particularly preferred dimeric product is the dimeric form of the BPI fragment having N-terminal residues 1 through 193, designated rBPI42 dimer.

[0053] Biologically active variants of BPI (BPI variants) include but are not limited to recombinant hybrid fusion proteins, comprising BPI holoprotein or biologically active fragment thereof and at least a portion of at least one other polypeptide, and dimeric forms of BPI variants. Examples of such hybrid fusion proteins and dimeric forms are described by Theofan et al. in U.S. patent application Ser. No. 07/885,911, now abandoned, and a continuation-in-part application thereof, U.S. patent application Ser. No. 08/064,693 filed May 19, 1993, issued as U.S. Pat. No. 5,643,570 on Jul. 1, 1997 and corresponding PCT Application No. US93/04754 filed May 19, 1993, which are all incorporated herein by reference and include hybrid fusion proteins comprising, at the amino-terminal end, a BPI protein or a biologically active fragment thereof and, at the carboxy-terminal end, at least one constant domain of an immunoglobulin heavy chain or allelic variant thereof. Similarly configured hybrid fusion proteins involving part or all Lipopolysaccharide Binding Protein (LBP) are also contemplated for use in the present invention.

[0054] Biologically active analogs of BPI (BPI analogs) include but are not limited to BPI protein products wherein one or more amino acid residues have been replaced by a different amino acid. For example, U.S. Pat. No. 5,420,019 and corresponding PCT Application No. US94/01235, filed Feb. 2, 1994, the disclosures of which are incorporated herein by reference, discloses polypeptide analogs of BPI and BPI fragments wherein a cysteine residue is replaced by a different amino acid. A preferred BPI protein product described by this application is the expression product of DNA encoding from amino acid 1 to approximately 193 or 199 of the N-terminal amino acids of BPI holoprotein, but wherein the cysteine at residue number 132 is substituted with alanine and is designated rBPI21Δcys or rBPI21. Other examples include dimeric forms of BPI analogs; e.g. U.S. patent application Ser. No. 08/212,132 filed Mar. 11, 1994, issued as U.S. Pat. No. 5,447,913 on Sep. 5, 1995 and corresponding PCT Application No. PCT/US95/03125, the disclosures of which are incorporated herein by reference.

[0055] Other BPI protein products useful according to the methods of the invention are peptides derived from or based on BPI produced by recombinant or synthetic means (BPI-derived peptides), such as those described in U.S. patent application Ser. No. 08/504,841 filed Jul. 20, 1995 and in PCT Application No. PCT/US94/10427 filed Sep. 15, 1994, which corresponds to U.S. patent application Ser. No. 08/306,473 filed Sep. 15, 1994, issued as U.S. Pat. No. 5,652,332 on Jul. 29, 1997, and PCT Application No. US94/02465 filed Mar. 11, 1994, which corresponds to U.S. patent application Ser. No. 08/209,762, filed Mar. 11, 1994, issued as U.S. Pat. No. 5,733,872 on Mar. 31, 1998, which is a continuation-in-part of U.S. patent application Ser. No. 08/183,222, filed Jan. 14, 1994, now abandoned, which is a continuation-in-part of U.S. patent application Ser. No. 08/093,202 filed Jul. 15, 1993, now abandoned, (for which the corresponding international application is PCT Application No. US94/02401 filed Mar. 11, 1994), which is a continuation-in-part of U.S. patent application Ser. No. 08/030,644 filed Mar. 12, 1993, issued as U.S. Pat. No. 5,348,942 on Sep. 20, 1994, the disclosures of all of which are incorporated herein by reference.

[0056] Presently preferred BPI protein products include recombinantly-produced N-terminal fragments of BPI, especially those having a molecular weight of approximately between 21 to 25 kD such as rBPI23 or rBPI21, or dimeric forms of these N-terminal fragments (e.g., rBPI42 dimer). Additionally, preferred BPI protein products include rBPI50 and BPI-derived peptides.

[0057] The administration of BPI protein products is preferably accomplished with a pharmaceutical composition comprising a BPI protein product and a pharmaceutically acceptable diluent, adjuvant, or carrier. The BPI protein product may be administered without or in conjunction with known surfactants, other chemotherapeutic agents or additional known anti-microbial agents. One pharmaceutical composition containing BPI protein products (e.g., rBPI50, rRBPI23) comprises the BPI protein product at a concentration of 1 mg/ml in citrate buffered saline (5 or 20 mM citrate, 150 mM NaCl, pH 5.0) comprising 0.1% by weight of poloxamer 188 (Pluronic F-68, BASF Wyandotte, Parsippany, N.J.) and 0.002% by weight of polysorbate 80 (Tween 80, ICI Americas Inc., Wilmington, Del.). Another pharmaceutical composition containing BPI protein products (e.g., rBPI21) comprises the BPI protein product at a concentration of 2 mg/mL in 5 mM citrate, 150 mM NaCl, 0.2% poloxamer 188 and 0.002% polysorbate 80. Such combinations are described in PCT Application No. US94/01239 filed Feb. 2, 1994, which corresponds to U.S. patent application Ser. No. 08/190,869 filed Feb. 2, 1994, issued as U.S. Pat. No. 5,488,034 on Jan. 30, 1996, and U.S. patent application Ser. No. 08/012,360 filed Feb. 2, 1993, now abandoned, the disclosures of all of which are incorporated herein by reference. Additional formulations are provided in U.S. patent application Ser. Nos. 08/372,104, filed Jan. 13, 1995, now abandoned, 08/530,599, filed Sep. 19, 1995, now abandoned, and 08/586,133, filed Jan. 12, 1996 and corresponding WO96/21436 (PCT/US96/01095).

[0058] The x-ray diffraction patterns of the invention are now discovered to be of sufficiently high resolution to be useful for three-dimensional modeling of a BPI. Preferably the resolution is in the range of 1.5 to 3.5 Å, preferably 1.5-3.0 Å and more preferably ≦2.6 Å.

[0059] Three-dimensional modeling is performed using the diffraction coordinates from these x-ray diffraction patterns. The coordinates are entered into one or more computer programs for molecular modeling, as known in the art. Such molecular modeling can utilize known x-ray diffraction molecular modeling algorithms or molecular modeling software to generate atomic coordinates corresponding to the three-dimensional structure of at least one BPI or a fragment thereof.

[0060] The entry of the coordinates of the x-ray diffraction patterns and the amino acid sequence into such programs results in the calculation of most probable secondary, tertiary and quaternary structures of the protein, including overall atomic coordinates of a BPI or a fragment thereof. These structures are combined and refined by additional calculations using such programs to determine the probable or actual three-dimensional structure of the BPI, including potential or actual active or binding sites of the protein.

[0061] Such molecular modeling (and related) programs useful for rational drug design of ligands or mimetics, are also provided by the present invention. The drug design uses computer modeling programs which calculate how different molecules interact with the various sites of the BPI. This procedure determines potential ligands or mimetics of a BPI or at least one fragment thereof. The actual BPI-ligand complexes or mimetics are crystallized and analyzed using x-ray diffraction. The diffraction pattern coordinates are similarly used to calculate the three-dimensional interaction of a ligand and the BPI or a mimetic, in order to confirm that the ligand binds to, or changes the conformation of, a particular site on the BPI, or where the mimetic has a similar three-dimensional structure to that of a BPI or a fragment thereof.

[0062] The potential ligands or mimetics are then screened for activity relating to a BPI. Such screening methods are selected from assays for at least one biological activity of the native BPI.

[0063] The resulting ligands or mimetics, provided by methods of the present invention, are useful for treating, screening or preventing bacterial infections in animals, such as mammals (including humans) and birds. Mimetics or ligands of a particular BPI will similarly react with other BPIs from other species, subgenera or genera of the BPI source organism.

[0064] Also provided are biologically active BPI proteins. A BPI protein is also provided as a crystallized protein suitable for x-ray diffraction analysis. The x-ray diffraction patterns obtained by the x-ray analysis are of moderately high to high resolution, e.g., 1.5-3.5 Å. The coordinates from these diffraction patterns are suitable and useful for three-dimensional modeling of the crystallized protein.

[0065] During the three-dimensional modeling of the BPI, these coordinates are entered with the BPI amino acid sequence into computer modeling programs to generate secondary, tertiary and quaternary structures of the BPI, as atomic coordinates. These structures together provide the three-dimensional structure of the BPI. The calculated and confirmed three-dimensional structure is then used for rational drug design of ligands or mimetics of the BPI or a fragment thereof.

[0066] The determination of the three-dimensional structure of a BPI protein thus has a broad-based utility. Significant sequence identity and conservation of important structural elements is expected to exist among the BPI proteins of a particular species, subgenus, genus, or family. Therefore, the three-dimensional structure from one or a few BPI proteins can be used to identify therapeutics with one or more of the biological activities of BPI (and/or those of related proteins such as LBP, CETP and PLTP).

[0067] Determination of Protein Structures

[0068] Different techniques give different and complementary information about protein structure. The primary structure is obtained by biochemical methods, either by direct determination of the amino acid sequence from the protein, or from the nucleotide sequence of the corresponding gene or cDNA. The quaternary structure of large proteins or aggregates can also be determined by electron microscopy. To obtain the secondary and tertiary structure, which requires detailed information about the arrangement of atoms within a protein, x-ray crystallography is preferred.

[0069] The first prerequisite for solving the three-dimensional structure of a protein by x-ray crystallography is a well-ordered crystal that will diffract x-rays strongly. The crystallographic method directs a beam of x-rays onto a regular, repeating array of many identical molecules so that the x-rays are diffracted from it in a pattern from which the structure of an individual molecule can be retrieved. Well-ordered crystals of globular protein molecules are large, spherical, or ellipsoidal objects with irregular surfaces, and crystals thereof contain large holes or channels that are formed between the individual molecules. These channels, which usually occupy more than half the volume of the crystal, are filled with disordered solvent molecules. The protein molecules are in contact with each other at only a few small regions. This is one reason why structures of proteins determined by x-ray crystallography are generally the same as those for the proteins in solution.

[0070] The formation of crystals is dependent on a number of different parameters, including pH, temperature, protein, concentration, the nature of the solvent and precipitant, as well as the presence of added ions or ligands to the protein. Many routine crystallization experiments may be needed to screen all these parameters for the few combinations that might give crystal suitable for x-ray diffraction analysis. Crystallization robots can automate and speed up the work of reproducibly setting up large number of crystallization experiments.

[0071] A pure and homogeneous protein sample is important for successful crystallization. Proteins obtained from cloned genes in efficient expression vectors can be purified quickly to homogeneity in large quantities in a few purification steps. A protein to be crystallized is preferably at least 93-99% pure according to standard criteria of homogeneity. Crystals form when molecules are precipitated very slowly from supersaturated solutions. The most frequently used procedure for making protein crystals is the hanging-drop method, in which a drop of protein solution is brought very gradually to supersaturation by loss of water from the droplet to the larger reservoir that contains salt or polyethylene glycol solution.

[0072] Different crystal forms can be more or less well-ordered and hence give diffraction patterns of different quality. As a general rule, the more closely the protein molecules pack, and consequently the less water the crystals contain, the better is the diffraction pattern because the molecules are better ordered in the crystal.

[0073] X-rays are electromagnetic radiation at short wavelengths, emitted when electrons jump from a higher to a lower energy state. In conventional sources in the laboratory, x-rays are produced by high-voltage tubes in which a metal plate, the anode, is bombarded with accelerating electrons and thereby caused to emit x-rays of a specific wavelength, so-called monochromatic x-rays. The high voltage rapidly heats up the metal plate, which therefore has to be cooled. Efficient cooling is achieved by so-called rotating anode x-ray generators, where the metal plate revolves during the experiment so that different parts are heated up.

[0074] More powerful x-ray beams can be produced in synchrotron storage rings where electrons (or positrons) travel close to the speed of light. These particles emit very strong radiation at all wavelengths from short gamma rays to visible light. When used as an x-ray source, only radiation within a window of suitable wavelengths is channeled from the storage ring. Polychromatic x-ray beams are produced by having a broad window that allows through x-ray radiation with wavelengths of 0.2-3.5 Å.

[0075] In diffraction experiments a narrow and parallel beam of x-rays is taken out from the x-ray source and directed onto the crystal to produce diffracted beams. The incident primary beam causes damage to both protein and solvent molecules. The crystal is, therefore, usually cooled to prolong its lifetime (e.g., −220 to −50° C.). The primary beam must strike the crystal from many different directions to produce all possible diffraction spots, and so the crystal is rotated in the beam during the experiment.

[0076] The diffracted spots are recorded either on a film, the classical method, or by an electronic detector. The exposed film has to be measured and digitized by a scanning device, whereas electronic detectors feed the signals they detect directly in a digitized form into a computer. Electronic area detectors (an electronic film) significantly reduce the time required to collect and measure diffraction data.

[0077] When the primary beam from an x-ray source strikes the crystal, some of the x-rays interact with the electrons on each atom and cause them to oscillate. The oscillating electrons serve as a new source of x-rays, which are emitted in almost all directions, referred to as scattering. When atoms (and hence their electrons) are arranged in a regular three-dimensional array, as in a crystal, the x-rays emitted from the oscillating electrons interfere with one another. In most cases, these x-rays, colliding from different directions, cancel each other out; those from certain directions, however, will add together to produce diffracted beams of radiation that can be recorded as a pattern on a photographic plate or detector.

[0078] The diffraction pattern obtained in an x-ray experiment is related to the crystal that caused the diffraction. X-rays that are reflected from adjacent planes travel different distances, and diffraction only occurs when the difference in distance is equal to the wavelength of the x-ray beam. This distance is dependent on the reflection angle, which is equal to the angle between the primary beam and the planes.

[0079] The relationship between the reflection angle (θ), the distance between the planes (d), and the wavelength (λ) is given by Bragg's law: 2d sin θ=λ. This relation can be used to determine the size of the unit cell in the crystal. Briefly, the position on the film of the diffraction data relates each spot to a specific set of planes through the crystal. By using Bragg's law, these positions can be used to determine the size of the unit call.

[0080] Each atom in a crystal scatters x-rays in all directions, and only those that positively interfere with one another, according to Bragg's law, give rise to diffracted beams that can be recorded as a distinct diffraction spot above background. Each diffraction spot is the result of interference of all x-rays with the same diffraction angle emerging from all atoms. For example, for the protein crystal of myoglobin, each of the about 20,000 diffracted beams that have been measured contain scattered x-rays from each of the around 1500 atoms in the molecule. To extract information about individual atoms from such a system requires considerable computation. The mathematical tool that is used to handle such problems is called the Fourier transform.

[0081] Each diffracted beam, which is recorded as a spot on the film, is defined by three properties: the amplitude, which we can measure from the intensity of the spot; the wavelength, which is set by the x-ray source; and the phase, which is lost in x-ray experiments. All three properties are needed for all of the diffracted beams, in order to determine the position of the atoms giving rise to the diffracted beams.

[0082] For larger molecules, protein crystallographers have determined the phases in many cases using a method called multiple isomorphous replacement (MIR) (including heavy metal scattering), which requires the introduction of new x-ray scatterers into the unit cell of the crystal. These additions are usually heavy atoms (so that they make a significant contribution to the diffraction pattern), such that there should not be too many of them (so that their positions can be located); and they should not change the structure of the molecule or of the crystal cell, i. e., the crystals should be isomorphous. Isomorphous replacement is usually done by diffusing different heavy-metal complexes into the channels of the preformed protein crystals. The protein molecules expose side chains (such as SH groups) into these solvent channels that are able to bind heavy metals. It is also possible to replace endogenous light metals in metalloproteins with heavier ones, e.g., zinc by mercury, or calcium by samarium.

[0083] Since such heavy metals contain many more electrons than the light atoms (H, N, C, O and S) of the protein, they scatter x-rays more strongly. All diffracted beams would therefore increase in intensity after heavy-metal substitution if all interference were positive. In fact, however, some interference is negative; consequently, following heavy-metal substitution, some spots measurably increase in intensity, others decrease, and many show no detectable difference.

[0084] Phase differences between diffracted spots can be determined from intensity changes following heavy-metal substitution. First, the intensity differences are used to deduce the positions of the heavy atoms in the crystal unit cell. Fourier summations of these intensity differences give maps of the vectors between the heavy atoms, the so-called Patterson maps. From these vector maps the atomic arrangement of the heavy atoms is deduced. From the positions of the heavy metals in the unit cell, one can calculate the amplitudes and phases of their contribution to the diffracted beams of protein crystals containing heavy metals.

[0085] This knowledge is then used to find the phase of the contribution from the protein in the absence of the heavy-metal atoms. As both the phase and amplitude of the heavy metals and the amplitude of the protein alone is known, as well as the amplitude of the protein plus heavy metals (i.e., protein heavy-metal complex), one phase and three amplitudes are known. From this, the interference of the x-rays scattered by the heavy metals and protein can be calculated to see if it is constructive or destructive. The extent of positive or negative interference, with knowledge of the phase of the heavy metal, given an estimate of the phase of the protein. Because two different phase angles are determined and are equally good solutions, a second heavy-metal complex can be used which also gives two possible phase angles. Only one of these will have the same value as one of the two previous phase angles; it therefore represents the correct phase angle. In practice, more than two different heavy-metal complexes are usually made in order to give a reasonably good phase determination for all reflections. Each individual phase estimate contains experimental errors arising from errors in the measured amplitudes. Furthermore, for many reflections, the intensity differences are too small to measure after one particular isomorphous replacement, and others can be tried.

[0086] The amplitudes and the phases of the diffraction data from the protein crystals are used to calculate an electron-density map of the repeating unit of the crystal. This map then has to be interpreted as a polypeptide chain with a particular amino acid sequence. The interpretation of the electron-density map is made more complex by several limitations of the data. First of all, the map itself contains errors, mainly due to errors in the phase angles. In addition, the quality of the map depends on the resolution of the diffraction data, which in turn depends on how well-ordered the crystals are. This directly influences the image that can be produced. The resolution is measured in A units; the smaller this number is, the higher the resolution and therefore the greater the amount of detail that can be seen.

[0087] Building the initial model is a trial-and-error process. First, one has to decide how the polypeptide chain weaves its way through the electron-density map. The resulting chain trace constitutes a hypothesis, by which one tries to match the density of the side chains to the known sequence of the polypeptide. When a reasonable chain trace has finally been obtained, an initial model is built to give the best fit of the atoms to the electron density. Computer graphics are used both for chain tracing and for model building to present the data and manipulated the models.

[0088] The initial model will contain some errors. Provided the protein crystals diffract to high enough resolution (e.g., better than 3.5 Å), most or substantially all of the errors can be removed by crystallographic refinement of the model using computer algorithms. In this process, the model is changed to minimize the difference between the experimentally observed diffraction amplitudes and those calculated for a hypothetical crystal containing the model (instead of the real molecule). This difference is expressed as an R factor (residual disagreement) which is 0.0 for exact agreement and about 0.59 for total disagreement.

[0089] In general, the R factor is preferably between 0.15 and 0.35 (such as less than about 0.24-0.28) for a well-determined protein structure. The residual difference is a consequence of errors and imperfections in the data. These derive from various sources, including slight variations in the conformation of the protein molecules, as well as inaccurate corrections both for the presence of solvent and for differences in the orientation of the microcrystals from which the crystal is built. This means that the final model represents an average of molecules that are slightly different both in conformation and orientation.

[0090] In refined structures at high resolution, there are usually no major errors in the orientation of individual residues, and the estimated errors in atomic positions are usually around 0.1-0.2 Å, provided the amino acid sequence is known. Hydrogen bonds, both within the protein and to bound ligands, can be identified with a high degree of confidence.

[0091] Those of skill in the art understand that a set of structure coordinates determined by X-ray crystallography is not without standard error. For the purpose of this invention, any set of structure coordinates for a BPI protein that have a root mean square deviation of protein backbone atoms (N, Cα, C and O) of less that 0.75 | when superimposed—using backbone atoms—on the structure coordinates listed in Table 4 or in Table 6 shall be considered identical.

[0092] Most x-ray structures are determined to a resolution between 1.7 Å and 3.5 Å. Electron-density maps with this resolution range are preferably interpreted by fitting the known amino acid sequences into regions of electron density in which individual atoms are not resolved.

[0093] An amino acid sequence is preferred for accurate x-ray structure determination. Thus, recombinant DNA techniques have had a double impact on x-ray structural work. When a protein is cloned and overexpressed for structural studies, the amino acid sequence, necessary for the x-ray work, is also quickly obtained via the nucleotide sequence. Recombinant DNA techniques give us not only abundant supplies of rare proteins, but also their amino acid sequence as a bonus.

[0094] Overview of BPI Purification and Crystallization Methods

[0095] In general, a BPI protein is purified as described in Example 1. The resulting BPI is in sufficient purity and concentration for crystallization. The BPI is then isolated and assayed for biological activity and for lack of aggregation (which interferes with crystallization). The purified BPI preferably runs as a single band under reducing or nonreducing polyacrylamide gel electrophoresis (PAGE) (nonreducing is used to evaluate the presence of cysteine bridges).

[0096] The purified BPI is preferably crystallized using the hanging drop method under varying conditions of at least one of the following: pH, buffer type, buffer concentration, salt type, polymer type, polymer concentration, other precipitating agents and concentration of purified and cleaved BPI. See, e.g., the methods provided in a commercial kit, such as CRYSTAL SCREEN (Hampton Research, Riverside, Calif.). Differently sized and shaped crystals are tested for suitability for x-ray diffraction. Generally, larger crystals provide better crystallography than smaller crystals, and thicker crystals provide better diffraction than thinner crystals.

[0097] Purified BPIs

[0098] The results of the purification are optionally analyzed by polyacrylamide gel electrophoresis (PAGE) under reducing or non-reducing conditions. A single band is preferably obtained. With disulfide-containing BPIs, it is preferred that the analysis of the cleaved BPI be under non-reducing conditions to indicate whether the cleaved protein formed disulfide linked dimers. The amino acid sequence can also be determined according to known methods, or otherwise obtained, as this sequence is important in determining the three-dimensional structure of the cleaved protein (in combination with crystallographic analysis), as described herein, using molecular modeling techniques.

[0099] Before crystallization, the purified protein is tested for one or more of the known biological activities of a BPI protein.

[0100] It is preferred that the biological activity exceed the activity of the native protein. The preferred result indicates that the BPI protein retains its native structure, which is important for determining the three-dimensional crystal structure of the biologically active molecule. To identify the protease cleavage site, the purified and cleaved protein can be sequenced using known techniques. See, e.g., Murti et al., Proc. Natl. Acad. Sci. USA 90:1523-1525 (1993); Takimoto et al. (1992), infra, entirely incorporated herein by reference.

[0101] Protein Crystallization Methods

[0102] The hanging drop method is preferably used to crystallize the purified protein. See, e.g., Taylor et al., J. Mol. Biol. 226:1287-1290 (1992); Takimoto et al. (1992), infra; CRYSTAL SCREEN, Hampton Research.

[0103] A mixture of the purified protein and precipitant can include the following:

[0104] pH (e.g., 4-9);

[0105] buffer type (e.g., phosphate, cacodylate, acetates, imidazole, Tris HCl, sodium HEPES);

[0106] buffer concentration (e.g., 10-200 mM);

[0107] salt type (e.g., calcium chloride, sodium citrate, magnesium chloride, ammonium acetate, ammonium sulfate, potassium phosphate, magnesium acetate, zinc acetate; calcium acetate)

[0108] polymer type and concentration: (e.g., polyethylene glycol (PEG) 1-50%, average molecular weight 200-10,000);

[0109] other precipitating agents (salts: K, Na tartrate, NH4SO4, NaAc, LiSO4, NaFormate, NaCitrate, MgFormate, NaPO4, KPO4 NH4PO4; organics: 2-propanol; non-volatile: 2-methyl-2,4-pentanediol); and

[0110] concentration of purified BPI (e.g., 1.0-100 mg/ml). See, e.g., CRYSTAL SCREEN, Hampton Research.

[0111] A non-limiting example of such crystallization conditions is the following:

[0112] purified protein (e.g., approximately 3-4 mg/ml);

[0113] H2O;

[0114] precipitant 10-14% Polyethylene glycol (PEG) 8000 buffered with 100 mM cacodylate buffer and 200 mM of Mg acetate;

[0115] at an overall pH of about 3.5-8.5.

[0116] The above mixtures are used and screened by varying at least one of pH, buffer type; buffer concentration, precipitating salt type or concentration, PEG type, PEG concentration, and protein concentration. Crystals ranging in size from 0.2-0.7 mm are formed in 1-7 days. These crystals diffract x-rays to at least 3.5 Å resolution, such as 1.5-3.5 Å, or any range of value therein, such as 1.5, 1.6, 1.7, 1.8, 1.9, 2.0, 2.1, 2.2, 2.3, 2.4, 2.5, 2.6, 2.7, 2.8, 2.9, or 3.0, with 3.0 Å or less being preferred.

[0117] Protein Crystals

[0118] Crystals appear after 1-4 days and grow to maximal size within a week. From one ten crystals are observed in one drop and crystal forms can occur, such as, but not limited to, bipyramidal, rhomboid, and cubic. Initial x-ray analyses indicate that such crystals diffract at moderately high to high resolution. When fewer crystals are produced in a drop, they can be much larger size, e.g., 0.4-0.9 mm.

[0119] X-ray Crystallography Methods and Molecular Modeling

[0120] The crystals so produced for BPI are x-ray analyzed using a suitable x-ray source. Diffraction patterns are obtained. Crystals are preferably stable for at least 10 hrs in the x-ray beam. Frozen crystals (e.g., −220 to −50° C.) could also be used for longer x-ray exposures (e.g., 24-72 hrs), the crystals being relatively more stable to the x-rays in the frozen state. To collect the maximum number of useful reflections, multiple frames are optionally collected as the crystal is rotated in the x-ray beam, e.g., for 24-72 hrs. Larger crystals (>0.2 mm) are preferred, to increase the resolution of the x-ray diffraction. Alternatively, crystals may be analyzed using a synchrotron high energy x-ray source. Using frozen crystals, x-ray diffraction data is collected on crystals that diffract to a relatively high resolution of 3.5 ↑ or less, sufficient to solve the three-dimensional structure of BPI in considerable detail, as presented herein.

[0121] Native and/or derivative x-ray diffraction data with medium resolution is collected on area detectors mounted on rotating anode x-ray sources. The alternative program DENZO is preferably used for data processing and reduction (Sawyer et al., eds., Proceedings of CCP4 Study Weekend, pp. 56-62, SERC Darsbary Lab., UK (1993)).

[0122] The resolution is optionally improved using larger crystals, e.g., 0.2 mm, making data collection more efficient, particularly for the determination of suitable heavy metal derivatives, such as Hg, Pt, Pb, Ba, Cd, and/or La derivatives.

[0123] The heavy metal derivatives are used to determine the phase, e.g., by the isomorphous replacement method. Heavy atom isomorphous derivatives of BPI are used for x-ray crystallography, where the structure is solved using one or several derivatives, which, (when combined) improves the overall figure of merit. Derivatives are identified through Patterson maps and/or cross-phase difference Fourier maps, e.g., using the CCP4 package (SERC Collaborative Computing Project No. 4, Daresbury Laboratory, UK, 1979).

[0124] Phases were also obtained or improved by optimization of the anomalous dispersion component of the x-ray scattering which can break the phase ambiguity which a single heavy atom derivative gives. In certain cases phase information may be obtained without the need of a native set of data, through the use of multiple wavelength with anomalous dispersion phasing (MAD phasing). The wavelength of the x-rays used may be selected at a synchrotron source to optimize this anomalous scattering. In this case data from a derivatised crystal or crystals is collected at typically three wavelengths, two of which are very close to the absorption edge of the heavy atom scatterer. One way of obtaining a suitable heavy atom derivatised crystal is to derivatise a known ligand of the protein.

[0125] The program MLPHARE (Wolf et al., eds., Isomorphous Replacement and Anomalous Scattering: Proceedings of CCP4 Study Weekend, pp. 80-86, SERC Daresbury Lab., UK (1991)) is optionally used for refinement of the heavy atom parameters and the phases derived from them by comparing at least one of completeness (%), resolution (Å), Rr (%), heavy atom concentration (mM), soaking time, heavy atom sites, phasing power (acentric, centric) (See Table 1 as an analogous example from The Crystal Structure of diphtheria toxin, Choe et al., Nature 357: 216-222 (1992). Addition of heavy atom derivatives produce an MIR map with recognizable features.

[0126] The initial phases are calculated to 3.2 Å, and then improved and extended to a higher resolution of 2.8 Å (e.g., <3.0 Å) using solvent flattening, histogram matching and/or Sayre's equation in the program DM (Cowtan and Main, Acta Crystallogr. D 49:148-157 (1993)). The skeletonization of DM procedure is optionally used to improve connectivity in the bulk of the protein envelope. Both the MIR and density modified maps are optionally used in subsequent stages, to provide sufficient resolution and/or modeling of surface structures.

[0127] Skeletonized representations of electron density maps are then computed. These maps are automatically or manually edited using suitable software, e.g., the graphics package FRODO (Jones et al. (1991), infra) to give a continuous Cα trace. The BPI sequence is then aligned to the trace. Initially pieces of idealized polypeptide backbone were placed into regions of the electron density map with obvious secondary structures (e.g., α-helix, β-sheet). After a polyalanine model was constructed for the protein, amino acid sidechains were added where density was present in the maps. The amino acid sequence of BPI was then examined for regions with distinct sidechain patterns (e.g., three consecutive aromatic rings). When a pattern in the sequence was found to match an area of the map, the correct sidechains were built onto the existing model. Eventually fragments containing recognizable sequence motifs were connected into a single chain, completing the tracing of the amino acid sequence into the maps.

[0128] X-ray diffraction data (e.g., to ≦3.0 Å) was collected on an RAXIS 11 C area detector (e.g., a Mar imaging plate) mounted on a RIGAKU rotating anode or alternatively a synchrotron x-ray source, and processed using a suitable oscillation data reduction program (DENZO, Sawyer et al. eds., Proceedings of CCP4 Study Weekend, pp. 56-62, SERC Darsbary Lab., UK (1993). Cycles of simulated annealing against these data were refined using the program X-PLOR for molecular dynamics for R-factor refinement (X-PLOR, Brünger et al., J. Mol. Biol. 203:803-816 (1987)). This refinement was followed by manual rebuilding with FRODO using experimental and 2Fo-Fc maps. The model can be optionally further refined using a least-squares refinement program, such as TNT (Tronrud et al., Acta Crystallogr. A 43:489-501 (1987)).

[0129] One or more of the above modeling steps is performed to provide a molecular 3-D model of BPI. It is preferred that the BPI model has no residues in disallowed regions of the Ramachandran plot, and gives a positive 3D-1D profile (Luthy et al., Nature 356:83-85 (1992)), suggesting that all the residues are in acceptable environments (Kraulis (1991), infra).

[0130] Multiple isomorphous replacement phase determination was used for solving the three-dimensional structure of BPI. This structure is then used for rational drug design of BPI ligands or mimetics of at least one BPI bactericidal activity, or other biological activity important in inactivating bacterial toxicity, replication and/or infection.

[0131] Computer Related Embodiments

[0132] An amino acid sequence of a BPI protein (or related protein such as LBP, CETP or PLTP) and/or x-ray diffraction data, useful for computer molecular modeling of BPI protein (or related protein such as LBP, CETP or PLTP) or a portion thereof, can be “provided” in a variety of mediums to facilitate use thereof. As used herein, provided refers to a manufacture, which contains, for example, a BPI amino acid sequence and/or atomic coordinate/x-ray diffraction data of the present invention, e.g., an amino acid sequence provided in FIG. 5, a representative fragment thereof, or an amino acid sequence having at least 80-100% overall identity to an amino acid fragment of an amino acid sequence of FIG. 5 or a variant thereof. Such a method provides the amino acid sequence and/or x-ray diffraction data in a form which allows a skilled artisan to analyze and molecular model the three-dimensional structure of a BPI-related protein, including a subdomain thereof.

[0133] In one application of this embodiment, BPI (or related protein such as LBP, CETP or PLTP), or at least one subdomain thereof, amino acid sequence and/or x-ray diffraction data of the present invention is recorded on computer readable medium. As used herein, “computer readable medium” refers to any medium which can be read and accessed directly by a computer. Such media include, but are not limited to: magnetic storage media, such as floppy discs, hard disc storage medium, and magnetic tape; optical storage media such as optical discs or CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media. A skilled artisan can readily appreciate how any of the presently known computer readable mediums can be used to create a manufacture comprising computer readable medium having recorded thereon an amino acid sequence and/or x-ray diffraction data of the present invention.

[0134] As used herein, “recorded” refers to a process for storing information on computer readable medium. A skilled artisan can readily adopt any of the presently know methods for recording information on computer readable medium to generate manufactures comprising an amino acid sequence and/or atomic coordinate/x-ray diffraction data information of the present invention.

[0135] A variety of data storage structures are available to a skilled artisan for creating a computer readable medium having recorded thereon an amino acid sequence and/or atomic coordinate/x-ray diffraction data of the present invention. The choice of the data storage structure will generally be based on the means chosen to access the stored information. In addition, a variety of data processor programs and formats can be used to store the sequence and x-ray data information of the present invention on computer readable medium. The sequence information can be represented in a word processing text file, formatted in commercially-available software such as WordPerfect and MICROSOFT Word, or represented in the form of an ASCII file, stored in a database application, such as DB2, Sybase, Oracle, or the like. A skilled artisan can readily adapt any number of dataprocessor structuring formats (e.g. text file or database) in order to obtain computer readable medium having recorded thereon the information of the present invention.

[0136] By providing computer readable medium having stored thereon a BPI or related sequence protein and/or atomic coordinates based on x-ray diffraction data, a skilled artisan can routinely access the sequence and atomic coordinate or x-ray diffraction data to model a BPI or related protein, a subdomain thereof, mimetic, or a ligand thereof. Computer algorithms are publicly and commercially available which allow a skilled artisan to access this data provided in a computer readable medium and analyze it for molecular modeling and/or RDD. See, e.g., Biotechnology Software Directory, MaryAnn Liebert Publ., New York (1995).

[0137] The present invention further provides systems, particularly computer-based systems, which contain the sequence and/or diffraction data described herein. Such systems are designed to do structure determination and RDD for a BPI or related protein or at least one subdomain thereof. Non-limiting examples are microcomputer workstations available from Silicon Graphics Incorporated and Sun Microsystems running UNIX based, Windows NT or IBM OS/2 operating systems.

[0138] As used herein, “a computer-based system” refers to the hardware means, software means, and data storage means used to analyze the sequence and/or x-ray diffraction data of the present invention. The minimum hardware means of the computer-based systems of the present invention comprises a central processing unit (CPU), input means, output means, and data storage means. A skilled artisan can readily appreciate which of the currently available computer-based systems are suitable for use in the present invention. A visualization device, such as a monitor, is optionally provided to visualize structure data.

[0139] As stated above, the computer-based systems of the present invention comprise a data storage means having stored therein a BPI or related protein or fragment sequence and/or atomic coordinate/x-ray diffraction data of the present invention and the necessary hardware means and software means for supporting and implementing an analysis means. As used herein, “data storage means” refers to memory which can store sequence or atomic coordinate/x-ray diffraction data of the present invention, or a memory access means which can access manufactures having recorded thereon the sequence or x-ray data of the present invention.

[0140] As used herein, “search means” or “analysis means” refers to one or more programs which are implemented on the computer-based system to compare a target sequence or target structural motif with the sequence or x-ray data stored within the data storage means. Search means are used to identify fragments or regions of a BPI or related protein which match a particular target sequence or target motif. A variety of known algorithms are disclosed publicly and a variety of commercially available software for conducting search means are and can be used in the computer-based systems of the present invention. A skilled artisan can readily recognize that any one of the available algorithms or implementing software packages for conducting computer analyses can be adapted for use in the present computer-based systems.

[0141] As used herein, “a target structural motif,” or “target motif,” refers to any rationally selected sequence or combination of sequences in which the sequence(s) are chosen based on a three-dimensional configuration or electron density map which is formed upon the folding of the target motif. There are a variety of target motifs known in the art. Protein target motifs include, but are not limited to, enzymic active sites, structural subdomains, epitopes, functional domains and signal sequences. A variety of structural formats for the input and output means can be used to input and output the information in the computer-based systems of the present invention.

[0142] A variety of comparing means can be used to compare a target sequence or target motif with the data storage means to identify structural motifs or electron density maps derived in part from the atomic coordinate/x-ray diffraction data. A skilled artisan can readily recognize that any one of the publicly available computer modeling programs can be used as the search means for the computer-based systems of the present invention.

[0143] One application of this embodiment is provided in FIG. 6. FIG. 6 provides a block diagram of a computer system 102 that can be used to implement the present invention. The computer system 102 includes a processor 106 connected to a bus 104. Also connected to the bus 104 are a main memory 108 (preferably implemented as random access memory, RAM) and a variety of secondary storage memory 110, such as a hard drive 112, a removable medium storage device 114, a command device 118, and a visualization device, 120. Also included is a removable storage medium 116. The removable medium storage device 114 may represent, for example, a floppy disk drive, a CD-ROM drive, a magnetic tape drive, etc. A removable storage medium 116 (such as a floppy disk, a compact disk, a magnetic tape, etc.) containing control logic and/or data recorded therein may be inserted into the removable storage device 114. The computer system 102 includes appropriate software for reading the control logic and/or the data from the removable storage medium 116 once inserted in the removable medium storage device 114.

[0144] Amino acid, encoding nucleotide or other sequence and/or atomic coordinate/x-ray diffraction data of the present invention may be stored in a well known manner in the main memory 108, or any of the secondary storage devices 110, and/or a removable storage medium 116. Software for accessing and processing the amino acid sequence and/or atomic coordinate/x-ray diffraction data (such as search tools, comparing tools, etc.) reside in main memory 108 during execution. User commands are implemented through a command device 118, such as a keyboard. The visualization device 120 is optionally used to visualize the structure data.

[0145] Structure Determination

[0146] One or more computational steps, computer programs and/or computer algorithms are used to provide a molecular 3-D model of BPI or related protein, using amino acid sequence data from FIG. 5 (or fragments or variants thereof) and/or atomic coordinate/x-ray diffraction data. In x-ray crystallography, x-ray diffraction data and phases are combined to produce electron density maps in which the three-dimensional structure of a BPI protein is then built or modeled. MIR Phase determination was used for solving the three-dimensional structure of BPI. This structure can then be used for RDD of mimetics or ligands of a BPI or related protein and its associated biological activity, which is relevant to a protein modulated disease.

[0147] Density Modification and Map Interpretation

[0148] Electron density maps were calculated by X-PLOR or alternatively using such programs as those from the CCP4 computing package (SERC (UK) Collaborative Computing Project 4, Daresbury Laboratory, UK, 1979). If non-crystallographic symmetry axes are present, cycles of symmetry averaging can further be used, such as with the program RAVE (Kleywegt & Jones, Bailey et al., eds., First Map to Final Model, SERC Daresbury Laboratory, UK, pp 59-66 (1994)) and gradual model expansion. For map visualization and model building the program FRODO was used or alternatively, a program such as “O” (Jones (1991), infra) can be used.

[0149] Refinement and Model Validation

[0150] Rigid body and positional refinement can be carried out using a program such as X-PLOR (Brünger (1992), infra), e.g., with the stereochemical parameters of Engh and Huber (Acta Ctyst. A47:392-400 (1991)). If the model at this stage in the averaged maps is still missing residues (e.g., at least 5-10 per subunit), some or all of the missing residues can be incorporated in the model during additional cycles of positional refinement and model building. The refinement procedure can start using data from lower resolution (e.g., 25-10 Å to 10-3.0 Å and then be gradually extended to include higher resolution data from 12-6Å to 3.0-1.5 Å). B-values (also termed temperature factors) for individual atoms were refined once data between 2.9 and 1.5 Å has been added. Subsequently waters were gradually added by manual inspection of electron density maps. Alternatively, a program such as ARP (Lamzin and Wilson, Acta Cryst. D49:129-147 (1993)) can be used to add crystallographic waters and as a tool to check for bad areas in the model. The programs PROCHECK (Lackowski et al., J. Appl. Cryst. 26:283-291 (1993)), WHATIF (Vriend, J. Mol. Graph. 8:52-56 (1990)), PROFILE 3D (Lüthy et al., Nature 356:83-85 (1992)), and ERRAT (Colovos & Yeates Protein Science, 2:1511-19 (1993)) as well as the geometrical analysis generated by X-PLOR were used to check the structure for errors. Anisotropic scaling between Fobs and Fcalc was applied after careful assessment of the quality and completeness of the data.

[0151] The program DSSP was used to assign the secondary structure elements (Kabsch and Sander, Biopolymers, 22:2577-2637 (1983)). A program such as SUPPOS (from the BIOMOL crystallographic computing package) can be used for some or all of the least-squares superpositions of various models and parts of models. The program ALIGN (Cohen J. Mol. Biol., 190: 593-604 (1986)) was used to superimpose N- and C-terminal domains of BPI. Solvent accessible surfaces and electrostatic potentials can be calculated using such programs as GRASP (Nicholls et al. (1991), infra).

[0152] The structure of BPI from different organisms and the related proteins LBP, CETP and PLTP can thus be solved with the molecular replacement procedure such as by using X-PLOR (Brünger (1992), infra). A partial search model for a portion or all of these proteins can be constructed using the structures of BPI. The rotation and translation function can be used to yield orientations and positions for these models. Symmetry averaging can also be done using the RAVE program and model expansion can also be used to add missing residues resulting in a model with 95-99.9% of the total number of residues. The model can be refined in a program such as X-PLOR (Brünger (1992), supra), to a suitable crystallographic Rfactor. The model data is then saved on computer readable medium for use in further analysis, such as rational drug design.

[0153] Rational Design of Mimetics or Ligands

[0154] The determination of the crystal structure of a BPI protein, as described herein, provides a basis for the design of new and specific agents, including proteins or organic compounds.

[0155] Several approaches can be taken for the use of the crystal structure of a BPI in the rational design of protein or organic analogs having a relevant activity similar to that of a BPI or related protein. A computer-assisted, manual examination of a BPI potential binding site structure is optionally done. The use of software such as GRID—Goodford, J. Med. Chem. 28:849-857 (1985) a program that determines probable interaction sites between probes with various functional group characteristics and the protein surface—is used to analyze the surface sites to determine structures of similar inhibiting proteins or compounds. The GRID calculations, with suitable inhibiting groups on molecules (e.g., protonated primary amines) as the probe, are used to identify potential hotspots around accessible positions at suitable energy contour levels.

[0156] A diagnostic or therapeutic BPI or related protein modulating ligand of the present invention can be, but is not limited to, at least one selected from a lipid, a nucleic acid, a compound, a protein, an element, an antibody, a saccharide, an isotope, a carbohydrate, an imaging agent, a lipoprotein, a glycoprotein, an enzyme, a detectable probe, and antibody or fragment thereof, or any combination thereof, which can be detectably labeled as for labeling antibodies. Such labels include, but are not limited to, enzymatic labels, radioisotope or radioactive compounds or elements, fluorescent compounds or metals, chemiluminescent compounds and bioluminescent compounds. Alternatively, any other known diagnostic or therapeutic agent can be used in a method of the invention. Suitable compounds are then tested for activities of a BPI protein or BPI mimetic.

[0157] The program DOCK (Kuntz et al. J. Mol. Biol., 161:269-288 (1982)) may be used to analyze an active site or ligand binding site and suggest ligands with complementary steric properties. Several methodologies for searching three-dimensional databases to test pharmacophore hypotheses and select compounds for screening are available. These include the program CAVEAT (Bacon et al. J. Mol Biol., 225: 849-858 (1992)) which uses databases of cyclic compounds which can act as “spacers” to connect any number of chemical fragments already positioned in the active site. This allows one skilled in the art to quickly generate hundreds of possible ways to connect the fragments already known or suspected to be necessary for tight binding. The program LUDI (Bohm et al. J. Comput. -Aid. Mol. Des., 6:61-78 (1992)) can determine a list of interactions sites into which to place both hydrogen bonding and hydrophobic fragments. LUDI then uses a library of approx. 600 linkers to connect up to four different interaction sites into fragments. Then smaller “bridging” groups such as —CH2— and —COO— are used to connect these fragments. For example, for the enzyme DHFR, the placements of key functional groups in the well-known inhibitor methotrexate were reproduced by LUDI. See also, Rotstein and Murcko, J. Med. Chem., 36:1700-1710 (1992)).

[0158] After preliminary experiments are done to determine the Kt of a ligand (e.g., a lipid ligand) by BPI (or related) protein to a BPI (or related) protein, mimetic or fragment, the time-dependent nature of the inhibition by the BPI or related protein (e.g., by the method of Henderson (Biochem. J. 127:321-333 (1972)) is determined.

[0159] For example, a lipid ligand and a BPI mimetic are pre-incubated in buffer. Reactions are initiated by the addition of detecting substrate. Aliquots are removed over a suitable time course and each quenched by addition into the aliquots of suitable quenching solution. The concentration of product are determined by known methods of detection. Plots of activity against time can be close to linear over the assay period, and are used to obtain values for the initial velocity in the presence (V1) or absence (V0) of, for example, a BPI mimetic. Error is present in both axes in a Henderson plot, making it inappropriate for standard regression analysis (Leatherbarrow, Trends Biochem. Sci. 15:455-458 (1990)). Therefore, K1 values are obtained from the data by fitting to a modified version of the Henderson equation for competitive inhibition:

Qr

2
+(Et−Q−It)r−Et=0

[0160] where (using the notation of Henderson (Biochem. J. 127:321-333 (1972)):

Q = K_{t} (\frac{A_{t} + K_{a}}{K_{a}}) and r = \frac{V_{o}}{V_{i}}

[0161] This equation is solved for the positive root with the constraint that Q=Kt((At+Ka)/Ka) using PROCNLIN from SAS (SAS Institute Inc., Cary, N.C., USA) which performs nonlinear regression using least-square techniques. The iterative method used is optionally the multivariate secant method, similar to the Gauss-Newton method, except that the derivatives in the Taylor series are estimated from the histogram of iterations rather than supplied analytically. A suitable convergence criterion is optionally used, e.g., where there is a change in loss function of less than 10−8.

[0162] Once modulating compounds are found, crystallographic studies of co-complexes, for example, BPI mimetics complexed to a ligand are performed. As used herein, a co-complex refers to a BPI protein, fragment, analog or variant thereof in covalent or non-covalent association with a chemical entity or compound. As a non-limiting example, BPI crystals are soaked for 2 days in 0.01-100 mM inhibitor compound and x-ray diffraction data are collected on an area detector and/or an image plate detector (e.g., a Mar image plate detector) using a rotating anode x-ray source. Data are collected to as high a resolution as possible, e.g., ≦3.0 Å, and merged with a suitable R-factor on intensities. An atomic model of the mimetic is built into the difference Fourier map (Finhibitor complex−Fnative). The model can be refined to convergence in a cycle of simulated annealing (Brünger (1987), infra) involving 10-100 cycles of energy refinement, 100-10,000 1-fs steps of room temperature dynamics and/or 10-100 more cycles of energy refinement. Harmonic restraints may be used for the atom refinement, except for atoms within a 10-15 Å radius of the inhibitor. An R-factor is calculated for the model as well as an r.m.s. deviation from the ideal bond lengths and angles.

[0163] Direct measurements of activity provide further confirmation that the modeled mimetic compounds are high-affinity inhibitors for the lipid ligands. Other suitable assays for biological activity known for BPI or related proteins may be used.

[0164] Preferably, little or no change in the structure of the BPI or mimetic occurs in the electron density map described above. Kt values are determined by a previously described method (Henderson (1972), infra) to evaluate mimetic proteins or organic compounds.

[0165] Atomic coordinates of BPI proteins are useful in the generation of molecular models of related proteins and of BPI mimetics. The atomic coordinates generated from the solved three-dimensional structure of BPI disclosed herein may be utilized in combination with additional structural and/or physicochemical information, such as amino acid sequence data, x-ray diffraction data, combinations of x-ray diffraction data from multiple isomorphous replacement molecular replacement techniques, or other phase determination techniques. These combinations may be used to generate other three-dimensional coordinate data useful to generate secondary, tertiary and/or quaternary structures and/or domains of BPI or related proteins, including BPI-related lipid binding proteins, or their fragments, analogs, or variants. These alternate coordinate sets are useful to provide overall three-dimensional structure, as well as binding and or active sites of a BPI or related protein, including BPI-related lipid binding proteins, or their fragments, analogs, or variants. These alternate coordinate data sets are also useful in molecular modeling computer-based systems and methods for rational drug design of mimetics and ligands of BPI and other related proteins, including other BPI-related lipid binding proteins. Utilizing CLUSTAL (a multiple sequence alignment program in PC-Gene) and the Homology module (a structure-based homology modeling program in Insightll on a Silicon Graphics Incorporated workstation, molecular models (and the corresponding three-dimensional coordinates files) of lipopolysaccharide binding protein (LBP), cholesteryl ester transfer protein (CETP) and phospholipid transfer protein (PLTP) are generated. With these files, existing mutants are mapped and new ones designed.

[0166] The results described herein demonstrate that tight-binding mimetics of a BPI or related protein, based on the crystal structure of BPI, are provided by the present invention. Demonstration of clinically relevant levels of a biological activity of the mimetic is also useful.

[0167] In evaluating mimetics for biological activity in animal models (e.g., mouse, rat, rabbit, baboon) various oral and parenteral routes of administration are evaluated. Using this approach, it is expected that a biological activity occurs in suitable animal models, e.g., using the inimetics discovered by structure determination and x-ray crystallography.

[0168] Having now generally described the invention, the same will be more readily understood through reference to the following examples which are provided by way of illustration, and are not intended to be limiting of the present invention.

EXAMPLE 1

Preparation and Purification for Crystallization Construction of Plasmids Containing BPI (S351A)

[0169] BPI contains a single N-linked glycosylation site at the asparagine at position 349 which was eliminated by genetic engineering of the DNA sequence of BPI as follows. For glycosylation to occur at this position, the asparagine must occur within the sequence Asn-X-Ser/Thr where X can be any amino acid, except proline. N-linked glycosylation can be eliminated by either changing the Asn to another amino acid such as glutamine or by changing the serine or threonine to an alternate amino acid. The latter strategy was used to construct vectors containing BPI with an alanine at position 351 instead of serine.

[0170] Construction of Plasmids for BPI Expression

[0171] The plasmid pIC108 containing a cDNA encoding BPI cloned in a T3T7 plasmid (Clontech, Palo Alto, Calif.) served as the starting point for the construction of a vector for expression of nonglycosylated rBPI in mammalian cells.

[0172] To allow insertion of BPI into an optimized mammalian expression vector, a unique XhoI site was first added to the 3′ end of the BPI gene in pIC108. Two oligonucleotides were synthesized for this purpose: BPI-53 (5′ ACT GGT TCC ATG GAG GTC AGC GCC 3′) encoding amino acids 361-370 of BPI and BPI-54 (5′ GAC AGA TCT CTC GAG TCA TTT ATA GAC AA 3′) encoding the last four amino acids of coding sequence, the stop codon (TGA), and incorporating an XhoI site immediately downstream of the stop codon. These oligonucleotides were used to PCR amplify a 280 bp fragment of the C-terminus of BPI and incorporate the XhoI site at the 3′ end of the gene. The amplified fragment was digested with NcoI and BglII and ligated to a ˜4100 bp NcoI-BamHI fragment from pIC108 to generate the plasmid pSS101.

[0173] Construction of Plasmid with BPI (S351A)

[0174] The glycosylation site was next removed by replacing the region from a unique XcmI site to a unique SphI site within the BPI gene in pSS101 with an annealed oligonucleotide that contained the codon (TCC) for the serine at amino acid position 351 changed to the codon (GCC) for alanine as shown below.

1Wild type XcmI SphI. . . CCC AAC TCC TCC CTG GCT TCC CTC TTC CTG ATT GGC ATG CAC. . . GGG TTC AGG AGG GAC CGA AGG GAG AAG GAC TAA CCG TAC GTG Pro Asn Ser Ser Leu Ala Ser Leu Phe Leu Ile Gly Met His 351Nonglycosylated XcmI SphI. . . CCC AAC TCC GCC CTG GCT TCC CTC TTC CTG ATT GGC ATG CAC. . . GGG TTC AGG CGG GAC CGA AGG GAG AAG GAC TAA CCG TAC GTG Pro Asn Ser Ala Leu Ala Ser Leu Phe Leu Ile Gly Met His 351

[0175] This step generated the plasmid pSS102.

[0176] To construct the vector, pING4322, for the expression of full length nonglycosylated holo BPI in mammalian cells, pSS102 was digested with BstBI and XhoI and a 596 bp fragment, which included the modified BPI sequence, was purified and ligated to the large BstBI-XhoI fragment from pING4147 which contains the gpt gene encoding resistance to mycophenolic acid, the human Ig enhancer, the human cytomegalovirus promoter (CMV) and the mouse light chain 3′ untranslated region and is identical to the vector, pING4144 as described in U.S. Pat. No. 5,420,019 and WO94/18323 (PCT/US94/01235) hereby incorporated by reference, except that it contains the codon for the native cysteine instead of an alanine at amino acid position 132 of the BPI gene.

[0177] Stable Transfection of Mammalian Cells for Expression of Nonglycosylated BPI

[0178] Mammalian cells are preferred hosts for production of rBPI protein analogs as described herein. Such cells permit proper secretion, folding, and post-translational modification of expressed proteins. Presently preferred mammalian host cells for production of BPI proteins include cells of fibroblast origin, such as CHO-K1 cells (ATCC CCL61), CHO-DG44 cells (a dihydrofolate reductase [DHFR] minus mutant of CHO Toronto obtained from Dr. Lawrence Chasin, Columbia University), CHO-DXB-11 (a DHFR− mutant of CHO-K1 obtained from Dr. Lawrence Chasin), Vero Cells (ATCC CRL81) and Baby Hamster Kidney (BHK) cells (ATCC CRL6281) and cells of lymphoid origin, such as the hybridoma Sp2/O-Ag14 (ATCC CRL1581) or the myeloma, NSO (ECACC No. 85110503).

[0179] Transfection of mammalian cells can be accomplished by a variety of methods. Two of the most common approaches involve calcium phosphate precipitation of the expression vector DNA which is subsequently taken by the cells and electroporation, which causes the cells to take up the DNA through membrane pores created by the generation of a strong electric field. Selection for transfected cells is facilitated by the incorporation in the expression vector of a gene whose product allows the transfected cells to survive and grow under selective conditions. A number of such genes have been identified including, among others, the bacterial Tn5 neo gene, which encodes resistance to the antibiotic G418 and the Escherichia coli guanine phosphoribosyl transferase (gpt) gene, which encodes resistance to mycophenolic acid (MPA) in the presence of xanthine (Mulligan and Berg, Proc. Natl. Acad. Sci. 78:2072-2076 (1981)), the dihydrofolate reductase (DHFR) gene, which allows for growth of DHFR− cells in the absence of nucleosides and gene amplification in the presence of increasing concentrations of methotrexate, the glutamine synthetase gene, which allows for growth of glutamine auxotrophs without glutamine and gene amplification in the presence of methionine sulfoximine and the Salmonella typhimurium hisD gene and the E. coli trpB gene (Hartman and Mulligan, Proc. Natl. Acad. Sci. 85: 8047-8051 (1988)), which allow growth in the presence of histidinol or without tryptophan (in the presence of indole), respectively. The availability of these selective markers provide significant flexibility for the generation of mammalian cell lines that express recombinant products, since they can be used either alone or in various combinations to provide cell lines with the highest possible productivity.

[0180] Transfection of CHO-K1 Cells with pING4322

[0181] The CHO-KI cell line was maintained in Ham's F12 medium plus 10% fetal bovine serum (FBS). Media were supplemented with glutamine/penicillin/strepto-mycin (Irvine Scientific, Irvine, Calif.).

[0182] CHO-K1 cells were transfected by electroporation with 40 μg of pING4322 DNA that was first digested with PvuI, phenol-chloroform extracted and ethanol precipitated. Following the electroporation, the cells were allowed to recover for 24 hours in non-selective Ham's F12 medium. The cells were then trypsinized, resuspended at a concentration of ˜5×104 cells/ml in Ham's F12 medium supplemented with MPA (25 μg/mL) and xanthine (250 μg/mL) and plated at ˜104 cells/well in 96 well plates. Untransfected CHO-K1 cells are unable to grow in this medium due to the inhibition of pyrimidine synthesis by the MPA. At ˜2 weeks, colonies consisting of transfected cells were observed in the 96 well plates. Supernatants from wells containing single colonies were analyzed for the presence of BPI-reactive protein by anti-BPI ELISA using BPI23 as a standard. In this assay, Immulon-II 96 well plates (Dynatech) were pre-coated with affinity purified rabbit anti-BPI23 antiserum, followed by supernatant samples and detection was with affinity purified, biotinylated rabbit anti-BPI23 antiserum followed by peroxidase-labeled avidin. A total of 100 colonies were screened in this manner. The top isolates were transferred to 24 well plates and productivity was assessed as follows. Cells were grown to confluence in a 24 well plate in Ham's F12 medium supplemented with 10% FBS. Once the cells reached confluence, the Ham's F12 medium was removed and 2 ml of HB-CHO serum free medium (Irvine Scientific) plus 40 μL of S-Sepharose beads (Pharmacia) were added. The cells were incubated for 7 days after which the S-Sepharose beads were removed and washed with 0.1 M NaCl in 10 mM Tris buffer (pH 7.5). BPI was eluted from the beads by addition of 1.0 M NaCl in Tris buffer. The top producers, designated Clones 37 and 91, secreted ˜17 and 14 μg/ml, respectively in this assay and were frozen as Research Cell Bank numbers C2020 and C2021, respectively. Purified protein was prepared for crystallization studies as follows.

[0183] Production and Purification of Nonglycosylated rBPI

[0184] The host cells used to prepare protein for crystallization studies were CHO-K1 cells transformed with the DNA vector pING4322 which includes DNA encoding the 456 amino acids of human BPI preceded by its endogenous 31 residue secretory signal as described above. During post-translational secretory processing, the signal sequence residues were removed by the host cell. The desired expression product, nonglycosylated rBPI, was a biologically active variant of the human BPI molecule in which the amino acid serine at position 351 in the human BPI protein has been replaced with an alanine.

[0185] Forty roller bottles were prepared which contained the transfected CHO-K1 host cells at 1.3×107 cells per bottle in DME/F12 media supplemented with 5% fetal bovine serum (FBS). The cells were grown for three days, at which time 500 ml of fresh media, DME/F12 with 2.5% FBS was added along with a 10 ml slurry (approximately 8 gr.) of sterilized S-Sepharose (Pharmacia, fast flow #17-0511-01, Uppsula, Sweden) and 1 ml of a 1 M solution of sodium butyrate. After two days, the old media plus the S-Sepharose was removed and fresh media, S-Sepharose and sodium butyrate were added to each roller bottle. This process of harvesting the expressed protein product with S-Sepharose was repeated for a total of three harvests, and the S-Sepharose removed during each harvest was pooled. The use of S-Sepharose beads to capture recombinant BPI protein products has been described in U.S. Pat. No. 5,439,807 and WO93/23540 (PCT/US93/04752).

[0186] The expressed nonglycosylated rBPI protein was purified from the pooled S-Sepharose by first removing it from the S-Sepharose resin followed by further purification and concentration on a series of Q-Sepharose (Pharmacia, fast flow #17-0510-01) and CM-Spherodex (Sepracor, #273431, Villeneuve la Garenne, France) columns. Following purification, the protein was buffer exchanged utilizing a Sephacryl S-100 (Pharmacia, high resolution #17-0612-01) column. Specifically, the pooled S-Sepharose resin from each harvest was allowed to settle for approximately 15 minutes. The media was removed by decanting and the settled resin was washed three times with approximately 400 ml of 20 mM MES, pH 6.8, 150 mM NaCl. For each wash, the buffer was added, the mixture was stirred gently and the resin was allowed to resettle for approximately 15 minutes. Each buffer wash was removed by decanting. The beads were then washed with 400 mL of 20 mM sodium acetate/acetic acid, 150 mM NaCl, pH 4.0 (acetate buffer), and then poured into a 2.5×50 cm liquid chromatography column (BIORAD, Econocolumn, Richmond, Calif.). The column was washed extensively with approximately 2 liters of 400 mM NaCl-acetate buffer, pH 4.0 until the A280 absorbance reading of the column eluate was equal to that of the buffer alone. The column was additionally washed with approximately 600 ml of 600 mM NaCl-acetate buffer until the A280 absorbance of the eluate was again equal to that of buffer alone. The protein was then eluted from the S-Sepharose in approximately 500 ml of 1.0 M NaCl-acetate buffer.

[0187] The S-Sepharose eluates from each harvest were pooled and diluted to a NaCl concentration of 300 mM. The diluted material was then loaded on to a two column, serial arrangement of a 100 ml Q-Sepharose column connected to a 12 ml CM-Spherodex column. Both columns were constructed using new, sterile resin and were pre-equilibrated with 20 mM MES, pH 5.5, 200 mM NaCl. The Q-Sepharose column served to remove any nucleic acid in the sample material, and the protein did not bind to this resin. After the approximate 3 liters of protein containing material had been loaded, the Q-Sepharose column was disconnected and the CM-Spherodex column was washed with buffer until the A280 absorbance of the eluate was the same as buffer alone. The protein was eluted from the column in 20 mM MES, 400 mM NaCl, pH 5.5 in a volume of approximately 180 ml. This eluted fraction was then reloaded on to a smaller (2 ml) CM-Spherodex column for protein concentration, and the bound protein removed in a single step of 20 mM MES, 1.2 M NaCl, pH 5.5 in a volume of approximately 12 mL. The protein was then loaded directly on to a 150 ml pyrogen-free Sephacryl S-100 column pre-equilibrated with 20 mM sodium citrate, 150 mM NaCl, pH 5.0 buffer. Column fractions, were analyzed by Coommassie-stained (0.5% Coommassie Brilliant Blue-R, 25% isopropanol, 10% methanol, 10% acetic acid) SDS-PAGE and Western analysis. Western analysis was performed using a 1:1000 dilution of a rabbit anti-human BPI antisera. Fractions which contained the nonglycosylated rBPI protein were pooled and resulted in a final lot which was greater than 95% pure as analyzed by Coommassie-stained SDS-PAGE.

[0188] The protein samples thus prepared and purified were filtered and/or concentrated for crystallization studies of the purified nonglycosylated rBPI protein. Protein samples were optionally filtered using a 0.2 μm syringe filter (Millipore Corp., Bedford, Mass.) or a 0.2 μm Nalgene filter (Nalge Corp., Rochester, N.Y.) to remove precipitate. Protein samples were concentrated in a Centricon 10 (Amicon Corp., Beverly, Mass.) or a Centriprep 10 (Amicon Corp., Beverly, Mass.). For the Centricon 10 concentrators, a JA 20 rotor (Beckman, Fullerton, Calif.) in a J2-21 Beckman centrifuge was used at 6000 rpm for 60 minutes. For the Centriprep 10 concentrators, a swinging bucket rotor in a J-6B Beckman centrifuge was used at 3000 rpm for 60 minutes. Final volumes for various protein samples prepared for crystallization studies described herein ranged from about 0.1 to 1 mL, and the protein concentrations were generally between about 10 and 20 mg/mL. Protein solutions may be diluted or concentrated for crystallization studies, for example, from about 5 to about 50 mg/ml.

EXAMPLE 2

Structure Determination of a Crystallized BPI Protein

[0189] Presented herein is the crystal structure of BPI and two bound phospholipids at 2.4 Å resolution. Our model provides the first structural information on the LPS-binding and lipid transport protein family and suggests a common mode of lipid binding for its members.

[0190] Purified, full-length, non-glycosylated, recombinant human BPI expressed in CHO cells was crystallized by hanging-drop vapor diffusion at room temperature. The protein concentration was 8.5 mg/ml and the crystallization buffer contained 12% (w/v) PEG 8000, 200 mM magnesium acetate, and 100 mM sodium cacodylate, pH 6.8. Two crystal forms with slightly different cell dimensions grew under the same conditions in space group C2, with one molecule per asymmetric unit. Form 1 crystals were reproducible and had cell dimensions of a=185.0, b=37.2, c=84.3 Å, and β=101.3°. Form 2 crystals appeared rarely and had cell dimensions of a 185.6, b=33.0, c=85.2 Å, and β=101.6°

[0191] For Table 1, x-ray diffraction data were collected at room temperature with the R-AXIS IIC imaging plate area detector mounted on a Rigaku RU200 rotating anode x-ray generator. Data were processed with DENZO and SCALEPACK [Z. Otwinski, in Proceedings of CCP4 Study Weekend: Data Collection and Processing, L. Sawyer, N. Isaacs, S. Baileys, Eds. (SERC Daresbury Laboratory, Warrington, UK, 1993), pp. 56]. For form 1 crystals, a native data set to 2.8 Å was collected from a single crystal, which was 92.4% complete overall (84.9% complete with an average I/σ(I)=2.3 in the outermost resolution shell). A native data set to 2.4 Å for form 2 was collected from two crystals and was 92.7% complete overall (94.6% complete with an average I/σ(I)=2.6 in the outermost shell). Because they could be reliably reproduced, form 1 crystals were used for all heavy atom soaks. The structure was solved by multiple isomorphous replacement (MIR) with anomalous scattering. Heavy atom sites were identified by difference-Patterson and difference-Fourier maps. Phase refinement was performed with [Collaborative Computational Project No. 4, Acta Crystallogr., D50:760 (1994)] producing a mean figure of merit (FOM) of 0.57. The MIR map (FIG. 3) was improved by density modification including solvent flattening, histogram matching, and phase extension using DM [Collaborative Computational Project No. 4, supra]. After a partial model was obtained with FRODO [T. A. Jones, J. Appl. Crystallogr., 11:268 (1978)], phase combination was performed with SIGMAA [Collaborative Computational Project No. 4, supra] (final FOM=0.89). CMNP is chloro-Hg-nitrophenol; DMM is dimethyl mercury; PCMBS is parachloromercury-benzene sulfonate; TELA is triethyl lead acetate.

2TABLE 1X-RAY DIFFRACTION DATADataResolutionComplete-Rsym*SitesRPhasingItem(Å)ness(%)(N)Cullis†PowerMid‡Native 12.892.48.6Native 22.492.77.2CMNP§3.284.86.1166.02.040.15DMM∥3.572.89.81165.01.490.26PCMBS¶3.166.49.4377.01.270.38HgCl23.086.56.9149.02.130.18K2PtCl43.293.38.2390.00.680.13K2PtBr63.194.85.8373.00.880.14TELA#3.394.011.3286.00.800.15TELA-HgCl23.391.49.6363.01.900.18Xenon3.498.218.9587.00.690.18K3UO2F53.075.08.6265.01.400.16*Rsym = 100 (Σh | |h − < | > |)/(Σh |h) where < | > is the mean intensity of all symmetry-related reflections |h. †RCullis= (Σ|FPH +/− FP | − FH(calc))/(Σ|FPH +/− FP |) for centric reflections, Phasing power = [Σ| FH(calc)2|/ (Σ |FPH(obs) − FPH(calc) |2]1/2.‡MID (mean isomorphous difference) = Σ | FPH − FP|/Σ FP, where FPH is the derivative structure factor and FP is the native structure factor and the sum is over all reflections common to both data sets. §CMNP, chloro-Hg-nitrophenol; ∥DMM, dimethyl mercury; ¶PCMBS, parachloromercurybenzene sulfonate; #TELA, triethyl lead acetate

[0192] Table 2 relates to model refinement and statistics. The model was refined at 2.8 Å through iterative cycles of simulated-annealing with X-PLOR [A. T. Brünger and A. Krukowski, Acta Crystallogr., A46:585 (1990)] and manual rebuilding. 10% of the data were set aside before refinement began for Rfree [A. T. Brünger Nature, 355:472 (1992)] calculations. When the model had been refined to an R-factor* of 20.4% (Rfree=32.6%) with the 2.8 Å data, rigid-body minimization was performed against the 2.4 Å data set (R=29.8% to 3.5 Å after minimization). Additional cycles of simulated annealing, positional refinement, correlated individual temperature factor refinement, and manual rebuilding reduced the R-factor to 22.7% and Rfree=31.3% (no intensity cutoff). An overall anisotropic temperature factor and bulk solvent correction were applied to the observed reflections when Rfree showed improvement. The model was confirmed by calculating simulated-annealing omit-maps for every part of the structure. The final model contains all 456 residues of the protein, 48 well-ordered waters, and 2 molecules of phosphatidylcholine. Regions of the backbone with poor electron density include residues 148, 232-236, 258-260, and parts of the loop between residues 281-311. Sidechains with poorly defined density were truncated to alanine. The model was examined by the programs PROCHECK [R. A. Laskowski, M. W. McArthur, D. S. Moss, J. M. Thornton, J. Appl. Crystallogr. 26:283 (1993)], VERIFY [R. Lüthy, J. U. Bowie, D. Eisenberg, Nature, 356:83 (1992)], and ERRAT [C. Colovos and T. Yeates, Protein Sci., 2:1511 (1993)].

3TABLE 2REFINEMENT STATISTICS FOR FORM 2 CRYSTALSDataResolution (Å)2.4Unique reflections (N)18,898Completeness (%)92.7Atoms in modelProtein (non-hydrogen)3532Phosphatidylcholine102Water48Refinement parametersResolution range (Å)50.0-2.4R-factor* (%)22.7Rfree(%)31.3Avg. atomic B factorsProtein36.9Lipid N, C49.4, 51.0†Waters44.6rms‡ deviation from idealityBonds (Å)0.006Angles (deg)1.4Dihedrals (deg)26.0Impropers (deg)1.2*R = 100 (Σ | Fobs − Fc |) / (Σ Fobs) where Fobs and Fc are the observed and calculated structure factors, respectively. †B factors for the lipids bound in the NH2— and COOH-terminal domains. ‡rms = root mean square

[0193] BPI is a boomerang-shaped molecule with approximate dimensions of 135 by 35 by 35 Å (FIGS. 1, A and B). It consists of two domains of similar size (NH2- and COOH-terminal) that are connected by a proline-rich linker of 21 residues (positions 230 to 250). The two domains form three structural units; barrels are found at each end of the protein, and a central β sheet forms an interface between the barrels. The secondary structure and topology of the two domains are similar, giving the protein pseudo-twofold symmetry.

[0194] Each barrel (residues 10 to 193 and 260 to 421) contains three common structural elements: a short α helix, a five-stranded antiparallel β sheet, and a long helix (FIG. 2A), in that order. We call these elements helix A, sheet N and helix B in the NH2-terminal domain, and helix A′, sheet C and helix B′ in the COOH-terminal domain. Sheets N and C have a series of β bulges that change the direction of their strands and cause a pronounced curve in the sheets. In each domain, the long helix lies along the concave face of the sheet, with the helical axis at ˜60° to the strands of the β sheet. A single disulfide bond between Cys135 and Cys175 anchors helix B to the final strand of sheet N. Situated between the NH2- and COOH-terminal barrels is a twisted, seven-stranded antiparallel β sheet composed of four strands from the NH2-terminal domain and three strands from the COOH-terminal domain. This central sheet forms an interface between the two domains and is thus reminiscent of several dimer interfaces stabilized by hydrogen bonds between strands of a β sheet [M. Leeson, B. Henderson, J. Gillig, J. Schwab and J. Smith, Structure, 4:253 (1996); D. Ohlendorf, W. F. Anderson, M. Lewis, C. O. Pabo, B. W. Matthews, J. Mol. Biol., 169:757 (1983); G. N. Reeke, J. W. Becker, G. M. Edelman, J. Biol. Chem., 250:1525 (1975)].

[0195] The structural similarity of the two domains of BPI is shown by the superposition [G. H. Cohen, J. Mol. Biol., 190:593 (1986)] in FIG. 2B; they are related by a rotation of 173° and have a root mean square deviation (rmsd) of 3.0 Å on the basis of superposition of 169 Cα pairs. The structure shared by these two domains does not resemble other protein folds; several structural alignment programs [N. N. Alexandrov and D. Fischer, Proteins, 25:354 (1996); D. Fischer, C. J. Tsai, R. Nussinov, Protein Eng., 8:981 (1995); L. Holm, C. Sander, Nucl. Acids Res., 22:3600 (1996)] failed to reveal a significant match to any known folds. Significant differences between the superimposed domains are found in two loop regions containing residues 45 and 96 in the NH2-terminal domain and residues 280 and 348 in the COOH-terminal domain. These differences may be functionally important because the loops around residues 45 and 96 in the NH2-terminal domain have been implicated in LPS binding and bactericidal activity (see below). This structural similarity of the two domains was unexpected, not only because of their lack of significant sequence identity (<20%), but also because of their functional differences. The NH2-terminal domain of BPI is cationic and retains the bactericidal, LPS-binding, and LPS-neutralization activities of the intact protein [A. H. Horwitz, et al., Protein Expr. and Purif., 8:28 (1996); C. E. Ooi, J. Weiss, P. Elsbach, B. Frangione and B. Mannion, J. Biol. Chem., 262:14891-14894 (1987); C. E. Ooi, J. Weiss, M. E. Doerfler and P. Elsbach, J. Exp. Med., 174:649 (1991)]. The COOH-terminal domain is essentially neutral and shows limited LPS-neutralization activity,[S. L. Abrahamson et al., J. Biol. Chem., 272:2149 (1997)]. However, the structural similarity of the two domains may reflect a previously undetected functional similarity: each domain contains a binding pocket for a phospholipid.

[0196] After the amino acid sequence had been traced in the electron density maps, two regions of extended electron density remained that could not be accounted for by protein atoms. This density, found in the interior of both domains, was present in the multiple isomorphous replacement (MIR) maps (FIG. 3) at an intensity similar to that of the protein density, and it became the predominant feature in Fobs-Fcalc maps after sequence fitting (both form 1 and form 2 crystals). Electrospray mass spectrometry of the sample used for crystallization revealed two molecules, with relative molecular masses of 522 and 787, in approximately equal amounts. Tandem mass spectrometric analysis was consistent with the two species being phosphoglycerides containing a phosphatidylcholine head group and either one or two 18-carbon acyl chains with one double bond. Phosphatidylcholine (FIG. 4A) is abundant in eukaryotic cells and is presumably bound by BPI in the cells from which the protein is isolated.

[0197] The two lipids are bound in extensive apolar pockets on the concave surface of the boomerang, situated between the NH2-terminal and COOH-terminal barrels and the central β sheet. In the NH2-terminal domain, the entrance to the pocket is formed by helices A and B. The back and sides are formed by sheet N and the central sheet. The two acyl chains insert ˜15 Å into the interior of the protein and are surrounded by apolar side chains (FIG. 4B). The head group lies at the entrance of the pocket and is exposed to solvent. The pocket in the COOH-terminal domain, which has a slightly larger opening, is formed by the analogous secondary structures. Both basic and acidic side chains found near the entrances of the pockets are available for electrostatic interactions with the zwitterionic head group. When the lipids are removed from the model, the pocket in NH2-terminal domain has a solvent accessible surface area [M. L. Connolly, Science, 221:709 (1983); M. L. Connolly, J. Am. Chem. Soc., 107:1118 (1985)] of 557 Å2, and the pocket in the COOH-terminal domain has an area of 413 Å2, for a total of 970 Å2. The intensity of the electron density for the two acyl chains in both pockets is similar and does not indicate whether the single acyl chain species is found predominantly in either pocket.

[0198] The discovery of bound phospholipid in our structure suggests a possible site of interaction between BPI and LPS. As seen in FIG. 4A, phosphatidylcholine and LPS share some structural similarity, including negatively charged phosphate groups and, most notably, acyl chains. Since BPI's function is to bind a lipid, LPS, and since lipid is bound in pockets of BPI, it seems reasonable that the acyl chains of LPS bind in the apolar pockets. The following observations support his hypothesis: i) the acyl chains of lipid A are known to be essential for binding by BPI [H. Gazzano-Santoro et al., Infection and Immunity, 63:2201 (1995)]; ii) the binding pockets of BPI are reminiscent of cavities in other lipid-binding proteins [L. Banaszak et al., Adv. Protein Chem., 45:89 (1994)]; and iii) BPI has a significant sequence similarity to two lipid transfer proteins (see below).

[0199] Our proposed site of interaction between BPI and the acyl chains of LPS differs from that suggested by previous work focusing on the NH2-terminal domain. Fragments containing the NH2-terminal domain of BPI have been identified with equivalent or greater bactericidal and LPS-binding activities relative to the full-length protein [A. H. Horwitz, et al., Protein Expression and Purification, 8:28 (1996); C. E. Ooi, J. Weiss, M. E. Doerfler and P. Elsbach, J. Exp. Med., 174:649 (1991)]. The activity of one NH2-terminal fragment was reduced when residues past positions 12 or between positions 169 and 199 were deleted [C. Capodici and J. Weiss, J. Immunol., 156:4789 (1996)]. The structure shows that these deletions affect elements of the barrel (at the beginning of helix A and from the middle to the end of helix B) and could significantly alter its structure. While the barrel seems to be the minimal structural unit with full activity, three smaller regions of this domain retain significant LPS-binding, LPS-neutralization, and bactericidal activity [R. G. Little, D. N. Kelner, E. Lim, D. J. Burke and P. J. Conlon, J. Biol. Chem., 268:1865 (1994)]: residues 17-45 (most of helix A and the first β strand of sheet N), residues 82-108 (a β hairpin [residues 82 to 106 of-BPI show limited sequence similarity with residues 32 to 51 of the limulus anti-LPS factor (LALF), and have been predicted to form an amphipathic β hairpin similar to that seen in the LALF structure [A. Hoess, S. Watson, G. R. Silber and R. Liddington, EMBO 12:3351 (1993)]. Although this region of BPI does form β hairpin, the strict amphipathic character of the loop seen in LALF is not maintained, and a structural superposition shows that the sequence of BPI must be shifted by one residue relative to the proposed sequence alignment] between strands 3 and 4 of sheet N), and residues 142-169 (a segment preceding and including part of helix B). These three regions include 18 basic residues (and only 4 acidic residues) and form a positively charged tip on the NH2-terminal domain (on the left of FIG. 1) which may make favorable electrostatic interactions with negatively charged groups of LPS. Further studies are necessary to determine the relative importance of the apolar pockets and positively charged NH2-terminal tip to BPI's LPS-binding and bactericidal activities.

[0200] BPI is the first member of the mammalian LPS-binding and lipid transfer family to have its three-dimensional structure determined. BPI and LBP are related to two lipid transfer proteins, cholesteryl ester transfer protein (CETP) and phospholipid transfer protein (PLTP) [A. Tall, Annu. Rev. Biochem., 64:235 (1995)]. Alignment of the amino acid sequences of human BPI, LBP, CETP, and PLTP with BPI's secondary structure (FIGS. 5, A and B) shows that structurally important residues are conserved in the four proteins. The two cysteines that form the single disulfide bond and are critical to the function of BPI [A. H. Horwitz, et al., Protein Expression and Purification, 8:28 (1996)] are completely conserved. Also, the pattern of hydrophobic/hydrophilic residues in the β strands indicates that the β bulges responsible for the extensive sheet twisting are preserved. The conserved sequences strongly suggest that members of the LPS-binding and lipid transfer family share BPI's two-domain structure and that the two domains are similar in topology.

[0201] It is likely that the lipid transfer proteins will also share the apolar binding pockets found in BPI. Striking parallels are found between our BPI-phosphatidylcholine structure and previous work showing that CETP copurifies with an equimolar amount of phosphatidylcholine [A. Tall, Annu. Rev. Biochem., 64:235 (1995)] and has two distinct binding sites [S. Wang, L. Deng, R. W. Milne and A. R. Tall, J. Biol. Chem., 267:17487 (1992)]—one for neutral lipids and another for phospholipids. The known ligands of CETP and PLTP (cholesteryl esters, triglycerides, retinyl esters and phospholipids) all contain at least one acyl chain which could bind in apolar pockets similar to those in BPI, suggesting a common mode of ligand binding in this family. Sequestration of these hydrophobic chains in interior pockets may be critical to the function of the lipid transfer proteins: transfer of apolar ligands in an aqueous environment. Thus, the structure of BPI illuminates the action of the plasma lipid transfer proteins, as well as offering possibilities for how BPI and LBP interact with LPS.

EXAMPLE 3

Molecular Modeling of BPI Ligands and Mimetics

[0202] We have used the information derived from the X-ray crystal structure of BPI presented herein, along with the teachings of the art, including, for example, WO94/20532 (PCT/US94/02465) to design various BPI-related proteins and peptides. These constructs may be divided into categories as illustrated below, including peptides and proteins, including fragments, analogs and variants of the protein, since they best describe the different ways in which different domains and portions may be assembled to achieve new molecules.

[0203] 1. Individual Peptide Domains

[0204] The overlapping BPI peptide data indicated that the N-terminal domain of BPI contains at least three independent functional domains that have one or more of the biological activities of BPI, including, for example, antibacterial, antifungal, anti-heparin and anti-angiogenic activities. Domain I is a region of amino acid residues from about 17 to about 45; Domain II is a region of amino acid residues from about 65 to about 99; and Domain III is a region of amino acid residues from about 142 to about 169. Hundreds of peptide sequences derived from these domains have been synthesized, including addition, deletion and substitution variants of the domain-derived sequences. Through further refinements, smaller “core” regions within these domains have been identified that still retain high levels of activity; for example, within Domain II residues 90-99 and within Domain III residues 148-161.

[0205] These peptides have included linear molecules that may or may not assume a conformation that maximally express activity. From the X-ray structure data, segments of BPI are designed that should preserve the three-dimensional structure of these domains when constructed outside the context of the intact protein. For example, both Domains I and II contain hairpin loop structures that are positioned adjacent to one another in space on the proximal tip of the molecule. In contrast, although Domain III is a helix+turn and not a loop, extensions from both ends of the domain are positioned near enough to each other to consider linking them together. As a result, peptides can be designed that reflect these structures by replacing selected residues in synthetic or recombinant peptides with cysteines, so as to create disulfide-stablized domain mimetics. Since this approach is based upon the actual structure of BPI, it differs from those of other groups that are based upon putative alignments between BPI and the structure of proteins such as the Limulus amoebocyte lysate factor (LALF). As examples of these embodiments, listed below are a series of exemplary peptides that, with cysteines added to the N- and C-terminus could assume structures similar to those seen in the intact protein: from Domain I: residues 36-54; from Domain II: residues 84-109, 85-108, 86-107, 87-106, 88-105, 89-104, or 90-103; and from Domain III: residues 142-164.

[0206]

2
. Peptide Domain Hybrids

[0207] It has also been demonstrated that certain peptide domain hybrids, which include repeats of the same sequence from a single domain or inter-domain combination of sequences, have enhanced activities. For example, linking Domain II- and III-derived peptides (such as XMP.29: 85-99::148-161) has enhanced biological activity. Interestingly, these domains in the crystal structure are closely associated in space, and peptide XMP.29 may represent a Domain II::III hybrid that actually shares some structural similarity to the intact protein. Based upon the X-ray structure, a Domain II-III peptide that consists of approximately residues 90-103::146-162 is constructed. Such a peptide may even more closely mimic what is seen in the protein.

[0208] 3. BPI “Tip” Mimetics

[0209] As discussed above, portions of all three peptide domains discovered and described in WO94/20532 come together on the proximal tip of the N-terminal fragment. As a result, a BPI “tip” mimetic is designed that essentially “slices” off the most extreme tip of the molecule but preserves the critical domain elements. Such a slice would lack the hydrophobic pockets found in the intact protein, but may exhibit activities beyond those of the individual segments. The following segments represent such a “slice” of the three peptide domains. However, to best preserve the geometry between the domains, it would be desirable to insert “linker” sequences between them so as to ensure proper positioning. By fixing these segments in space, programs such as InsightII (Molecular Simulations, Inc.) can identify possible linker sequences by i) searching protein databases for similar structures or ii) de novo designing appropriate linkers. In this regard it may be desirable to utilize residues that are not readily susceptible to proteolysis (Ala, Ser, Gly, etc.), or to utilize amino acids like Pro that impose additional spatial constraints on peptide structure. An exemplary peptide consists of Domain I-II-III-derived elements: 37-54:90-104:144-162.

[0210] Similarly, by analogy with the above-described cyclic domain structures, the fact that residues 37 and 162 are positioned near each other in the protein suggests that a cyclic tip mimetic could be created by replacing these residues with cysteines, for example, Cys::38-54:90-104:144-161::Cys.

[0211] 4. Extended N-terminal Domains of BPI

[0212] The three dimensional structure of BPI indicates that the molecule, which forms N- and C-terminal domains, can be divided into three structural units as described in Example 2. Two of these units represent the N- and C-terminal “barrels” that are formed by residues 10-193 and 260-421, respectively, whereas the third element is a central β sheet structure that forms the interface between the two barrels. Of interest is the fact that the two bound phospholipids in BPI occupy spaces between the two barrel structures and the central β sheet. As a result, the recombinant BPI protein product rBPI21, which essentially contains residues 1-193 lacks some of the structural components necessary to form a complete hydrophobic pocket. A new molecule is constructed that encodes residues 1 to approximately 260 which would contain most of the residues necessary to form a complete hydrophobic pocket.

[0213] 5. Mutants for Immobilizing rBPI21

[0214] One application for BPI protein products is their use as affinity removal ligands for endotoxin in solution. For example, immobilizing a BPI protein on a column or membrane matrix would allow removal of endotoxin from endotoxin-contaminated solutions by simply passing those solutions over the immobilized BPI protein. Some of the cysteine-mutated peptides described above may be useful for this purpose, as well as rBPI23. Alternatively, in order to selectively couple a stable, readily produced protein like rBPI21 to a column or membrane, a cysteine could be added to the N- or C-terminus, thus allowing site-specific conjugation and selective orientation of the binding “tip” away from the solid support. Such a construct is alternatively constructed by adding a short linker segment (such as Gly-Gly-Gly-Ser) to the C-terminal residue of the BPI protein product, for example, residue 193 of rBPI(1-193), followed by a cysteine residue. Such a construct would have a high probability of folding correctly, given the domain nature of residues 1-193, and be readily conjugatable. Similarly, a series of new conjugates between rBPI(1-193)C and other thiol-containing proteins or molecules is created for the purposes of evaluating new molecules.

[0215] 6. New N-terminal Dimeric Molecules

[0216] As an extension of the above analysis, a new series of N-terminal dimeric molecules can be constructed that take better advantage of the hydrophobic pockets. For example, by replacing the C-terminal barrel with another copy of the N-terminal barrel, an analog of BPI would be created that contains two functional barrels and possibly two functional hydrophobic pockets. One such dimer could be constructed by replacing residues 260-456 with residues 1-193. Alternatively, other more central locations may be identified within the β sheet structure where symmetry would dictate additional and even better points for duplication.

[0217] 7. C-terminal Fusion Proteins

[0218] The C-terminal domains of LBP and CETP appear to mediate interactions with CD14 and lipoproteins. Similarly, the C-terminal domain of BPI has LPS binding and neutralization activities. As a consequence, the C-terminal barrel of BPI (or other family members) could be fused to barrels or domains of other family members and/or to other proteins to alter/modify/enhance their action.

[0219] 8. Homology Modeling of BPI Family Members

[0220] The BPI coordinates have been useful in the generation of molecular models of other members of the BPI protein family. Utilizing CLUSTAL (a multiple sequence alignment program in PC-Gene) and the Homology module (a structure-based homology modeling program in InsightII on the SGI), molecular models (and the corresponding three-dimensional coordinates files) of lipopolysaccharide binding protein (LBP), cholesteryl ester transfer protein (CETP) and phospholipid transfer protein (PLTP) have been generated. With these files, existing mutants are mapped and new ones designed. Published data [Wang et al., Biochemistry 30:3484-3490, (1991)] indicate that insertional alterations in three locations of CETP severely impaired cholesteryl ester transfer activity: residues 48-53, residue 165, and residues 373-379. Since residues 48-53 and residue 165 of CETP coincide structurally with Domains I and III of BPI respectively, the functional domain structure of BPI extends to the other protein family members. Similarly, by virtue of the symmetry between the N- and C-terminal domains, it is likely that the corresponding residues on the C-terminal tip of BPI are involved in recognizing receptors and/or interacting with lipoproteins.

[0221] 9. Lipid Pocket Mutants

[0222] A detailed compilation of the residues in BPI which form the pockets is described in Table 3 as follows. Column 1 of Table 3 indicates the residue name and number. Column 2 shows checked residues which indicate the residues that show a change in solvent accessible surface area with lipid binding. Column 3 shows checked residues that indicate the residues that have some atom within 4 A of a lipid atom. If the contact is to the head-group of the lipid, the residues are listed at the end, under ENTRY ONLY. Column 4 indicates conservation in 3 BPI and 4 LBP sequences, e.g., for Ile 68, in 3 of the 7 sequences, the residue is similarly Ile; for the other 4 sequences, the residue is Leu (see also column 5). Column 5 indicates alternative residues which occur in BPI or LBP at that position for the 7 BPI and LBP sequences analyzed. Column 6 indicates residues for mutations to block the pockets, using residues selected to be well-conserved (especially in the N-terminal domain) and relatively small. The suggested mutations are all to large sidechains in order to decrease the size of the pocket by as much as possible.

4TABLE 3N-TERMINAL POCKET - residues contributing to interiorWithinConserva-Alterna-Muta-Residue1ΔSA24¶3tion4tives5tions6Val 7✓✓2/7A, TIle 9✓✓AllWGly 13✓✓AllLeu 14✓AllTyr 16✓AllAla 17✓✓AllFSer 18✓✓1/7C, AGly 21✓✓AllFAla 24✓✓4/7V, T, SY, HLeu 25✓AllIle 68✓✓3/7LLeu 76✓✓AllPhe 78✓✓1/7V, LLeu 117✓✓AllLeu 119✓AllPro 128✓5/7A, SIle 130✓1/7VVal 178✓2/7L, IVal 182✓AllGlu 185✓✓1/7 (allele)K, D, HLeu 186✓✓AllWTyr 189✓✓AllPhe 190✓✓2/7V, LLeu 193✓✓AllLeu 220✓✓AllVal 222✓5/7M, WVal 254✓✓6/7ILeu 256✓3/7FPro 428✓✓AllThr 429✓✓1/7M, LPro 430✓✓5/7LVal 433✓3/7ILeu 435✓AllVal 453✓6/7IENTRY ONLYGln 20✓✓3/7ELys 27✓✓3/7R, SGlu 28✓6/7KArg 31✓2/7K, ESer 181✓✓5/7T, AArg 432✓✓3/7K, Y, HTyr 455✓✓6/7HC-TERMINAL POCKET - residues contributing to interiorPhe 263✓✓AllAsn 264✓AllAla 266✓✓AllFGly 267✓✓2/7A, S, T,Val 275✓✓1/7A, YLeu 276✓✓5/7F, WF, WLys 277✓1/7G, NMet 278✓✓1/7L, FVal 318✓1/7L, I, GAla 320✓2/7VPro 324✓✓6/7QLeu 326✓✓6/7VPhe 335✓✓1/7L, V, EPro 337✓✓5/7A, FVal 339✓2/7L, MMet 360✓✓2/7L, VThr 362✓✓5/7LVal 368✓✓2/7I, LLeu 375✓✓3/7I, VVal 376✓✓2/7I, TGly 377✓AllLeu 379✓✓AllLeu 381✓✓3/7PVal 409✓✓1/7L, M, IVal 413✓✓1/7F, LFVal 417✓✓3/7I, FWLys 420✓✓5/7EY, HLeu 421✓✓5/7I, FPhe 425✓✓6/7LENTRY ONLYAsp 200✓AllSer 201✓✓4/7K, T, NVal 202✓4/7F, ITyr 270✓✓AllArg 416✓✓1/7K, V, DLys 423✓3/7R, E, Q1Residue name and number. 2Checked residues show a change in solvent accessible surface area with lipid binding. 3Checked residues have some atom within 4 A of a lipid atom (if the contact is to the head group of the lipid, the residues are listed at the end, under ENTRY ONLY). 4Conservation in 3 BPI and 4 LBP sequences, e.g., for Ile 68, in 3 of the 7 sequences, the residue is similarly Ile; for the other 4 sequences, the residue is Leu (see note 5). 5Indicates alternative residues which occur in BPI or LBP at that position for the 7 BPI and LBP sequences analyzed. 6Indicates residues for mutations to block the pockets using residues selected to be well-conserved (especially in the N-terminal domain) and relatively small. The suggested mutations are all to large sidechains in order to decrease the size of the pocket by as much as possible.

[0223]

5

TABLE 4

ATOM
1
CB
VAL
A
1
95.942
11.564
18.390
1.00
51.23

ATOM
2
CG1
VAL
A
1
97.217
12.313
18.805
1.00
48.90

ATOM
3
CG2
VAL
A
1
94.694
12.383
18.720
1.00
50.67

ATOM
4
C
VAL
A
1
96.124
12.502
16.083
1.00
47.46

ATOM
5
O
VAL
A
1
97.238
12.990
15.911
1.00
49.54

ATOM
8
N
VAL
A
1
97.161
10.372
16.554
1.00
51.03

ATOM
10
CA
VAL
A
1
95.982
11.216
16.876
1.00
48.79

ATOM
11
N
ASN
A
2
95.020
13.016
15.554
1.00
42.80

ATOM
13
CA
ASN
A
2
95.067
14.266
14.810
1.00
38.18

ATOM
14
CB
ASN
A
2
93.709
14.566
14.185
1.00
39.01

ATOM
15
CG
ASN
A
2
93.494
13.831
12.892
1.00
40.06

ATOM
16
OD1
ASN
A
2
94.323
13.020
12.487
1.00
42.94

ATOM
17
ND2
ASN
A
2
92.380
14.108
12.228
1.00
39.49

ATOM
20
C
ASN
A
2
95.439
15.376
15.786
1.00
34.97

ATOM
21
O
ASN
A
2
94.946
15.399
16.916
1.00
37.36

ATOM
22
N
PRO
A
3
96.373
16.260
15.397
1.00
30.80

ATOM
23
CD
PRO
A
3
97.144
16.244
14.143
1.00
28.90

ATOM
24
CA
PRO
A
3
96.806
17.367
16.252
1.00
28.19

ATOM
25
CB
PRO
A
3
98.083
17.830
15.571
1.00
26.30

ATOM
26
CG
PRO
A
3
97.765
17.619
14.128
1.00
26.17

ATOM
27
C
PRO
A
3
95.765
18.482
16.283
1.00
28.00

ATOM
28
O
PRO
A
3
95.104
18.758
15.275
1.00
28.89

ATOM
29
N
GLY
A
4
95.615
19.108
17.444
1.00
26.31

ATOM
31
CA
GLY
A
4
94.653
20.182
17.588
1.00
25.44

ATOM
32
C
GLY
A
4
95.178
21.508
17.091
1.00
25.34

ATOM
33
O
GLY
A
4
94.407
22.425
16.831
1.00
28.37

ATOM
34
N
VAL
A
5
96.494
21.621
16.981
1.00
23.98

ATOM
36
CA
VAL
A
5
97.134
22.842
16.519
1.00
21.80

ATOM
37
CB
VAL
A
5
97.671
23.681
17.689
1.00
18.63

ATOM
38
CG1
VAL
A
5
98.573
24.785
17.171
1.00
20.04

ATOM
39
CG2
VAL
A
5
96.526
24.283
18.468
1.00
20.89

ATOM
40
C
VAL
A
5
98.308
22.436
15.660
1.00
24.04

ATOM
41
O
VAL
A
5
99.014
21.486
15.984
1.00
27.65

ATOM
42
N
VAL
A
6
98.492
23.139
14.551
1.00
25.94

ATOM
44
CA
VAL
A
6
99.589
22.874
13.633
1.00
26.54

ATOM
45
CB
VAL
A
6
99.082
22.292
12.294
1.00
29.26

ATOM
46
CG1
VAL
A
6
100.253
22.038
11.357
1.00
31.93

ATOM
47
CG2
VAL
A
6
98.318
21.001
12.535
1.00
30.52

ATOM
48
C
VAL
A
6
100.289
24.191
13.355
1.00
24.99

ATOM
49
O
VAL
A
6
99.638
25.202
13.135
1.00
26.97

ATOM
50
N
VAL
A
7
101.611
24.183
13.416
1.00
26.91

ATOM
52
CA
VAL
A
7
102.404
25.371
13.156
1.00
27.18

ATOM
53
CB
VAL
A
7
103.401
25.637
14.298
1.00
27.59

ATOM
54
CG1
VAL
A
7
104.343
26.773
13.925
1.00
27.21

ATOM
55
CG2
VAL
A
7
102.659
25.967
15.575
1.00
27.05

ATOM
56
C
VAL
A
7
103.190
25.103
11.889
1.00
29.61

ATOM
57
O
VAL
A
7
103.863
24.084
11.777
1.00
32.24

ATOM
58
N
ARG
A
8
103.077
25.994
10.917
1.00
33.04

ATOM
60
CA
ARG
A
8
103.801
25.841
9.668
1.00
33.25

ATOM
61
CB
ARG
A
8
102.842
25.631
8.494
1.00
35.70

ATOM
62
CG
ARG
A
8
102.195
24.244
8.485
1.00
41.64

ATOM
63
CD
ARG
A
8
101.309
24.004
7.259
1.00
44.24

ATOM
64
NE
ARG
A
8
102.049
23.578
6.073
1.00
48.00

ATOM
66
CZ
ARG
A
8
101.565
23.626
4.835
1.00
51.86

ATOM
67
NH1
ARG
A
8
100.341
24.091
4.611
1.00
52.72

ATOM
70
NH2
ARG
A
8
102.293
23.177
3.820
1.00
53.10

ATOM
73
C
ARG
A
8
104.682
27.052
9.441
1.00
32.06

ATOM
74
O
ARG
A
8
104.196
28.168
9.288
1.00
32.62

ATOM
75
N
ILE
A
9
105.986
26.830
9.515
1.00
31.21

ATOM
77
CA
ILE
A
9
106.955
27.888
9.315
1.00
31.97

ATOM
78
CB
ILE
A
9
108.210
27.633
10.167
1.00
32.76

ATOM
79
CG2
ILE
A
9
109.208
28.781
10.012
1.00
29.90

ATOM
80
CG1
ILE
A
9
107.803
27.454
11.633
1.00
32.76

ATOM
81
CD1
ILE
A
9
108.945
27.087
12.554
1.00
36.13

ATOM
82
C
ILE
A
9
107.309
27.889
7.832
1.00
34.24

ATOM
83
O
ILE
A
9
107.650
26.845
7.265
1.00
37.01

ATOM
84
N
SER
A
10
107.179
29.045
7.195
1.00
34.50

ATOM
86
CA
SER
A
10
107.473
29.173
5.774
1.00
33.98

ATOM
87
CB
SER
A
10
106.536
30.200
5.146
1.00
33.86

ATOM
88
OG
SER
A
10
106.778
31.488
5.679
1.00
36.26

ATOM
90
C
SER
A
10
108.922
29.563
5.500
1.00
32.91

ATOM
91
O
SER
A
10
109.674
29.886
6.416
1.00
33.57

ATOM
92
N
GLN
A
11
109.300
29.550
4.225
1.00
34.16

ATOM
94
CA
GLN
A
11
110.653
29.912
3.811
1.00
35.54

ATOM
95
CB
GLN
A
11
110.792
29.845
2.283
1.00
35.39

ATOM
96
CG
GLN
A
11
112.212
30.070
1.746
1.00
36.23

ATOM
97
CD
GLN
A
11
113.164
28.920
2.040
1.00
35.94

ATOM
98
OE1
GLN
A
11
112.880
27.774
1.716
1.00
38.97

ATOM
99
NE2
GLN
A
11
114.310
29.230
2.624
1.00
35.28

ATOM
102
C
GLN
A
11
110.991
31.312
4.316
1.00
36.60

ATOM
103
O
GLN
A
11
112.116
31.559
4.740
1.00
41.10

ATOM
104
N
LYS
A
12
110.013
32.216
4.305
1.00
35.51

ATOM
106
CA
LYS
A
12
110.245
33.573
4.788
1.00
31.96

ATOM
107
CB
LYS
A
12
109.005
34.445
4.612
1.00
32.24

ATOM
108
CG
LYS
A
12
109.226
35.876
5.065
1.00
32.71

ATOM
109
CD
LYS
A
12
107.953
36.685
5.063
1.00
31.87

ATOM
110
CE
LYS
A
12
108.227
38.085
5.573
1.00
34.67

ATOM
111
NZ
LYS
A
12
106.998
38.914
5.627
1.00
37.88

ATOM
115
C
LYS
A
12
110.612
33.498
6.259
1.00
30.93

ATOM
116
O
LYS
A
12
111.482
34.227
6.728
1.00
32.37

ATOM
117
N
GLY
A
13
109.961
32.586
6.973
1.00
30.47

ATOM
119
CA
GLY
A
13
110.231
32.407
8.385
1.00
27.64

ATOM
120
C
GLY
A
13
111.593
31.791
8.610
1.00
29.49

ATOM
121
O
GLY
A
13
112.312
32.184
9.531
1.00
30.35

ATOM
122
N
LEU
A
14
111.952
30.817
7.779
1.00
28.87

ATOM
124
CA
LEU
A
14
113.248
30.170
7.912
1.00
28.53

ATOM
125
CB
LEU
A
14
113.361
28.941
7.011
1.00
25.60

ATOM
126
CG
LEU
A
14
112.564
27.698
7.419
1.00
25.99

ATOM
127
CD1
LEU
A
14
112.959
26.547
6.531
1.00
28.34

ATOM
128
CD2
LEU
A
14
112.829
27.330
8.855
1.00
23.90

ATOM
129
C
LEU
A
14
114.359
31.155
7.613
1.00
28.63

ATOM
130
O
LEU
A
14
115.346
31.207
8.335
1.00
31.86

ATOM
131
N
ASP
A
15
114.176
31.972
6.582
1.00
31.30

ATOM
133
CA
ASP
A
15
115.176
32.975
6.215
1.00
33.98

ATOM
134
CB
ASP
A
15
114.695
33.832
5.033
1.00
36.03

ATOM
135
CG
ASP
A
15
114.818
33.127
3.681
1.00
36.52

ATOM
136
OD1
ASP
A
15
115.662
32.209
3.515
1.00
37.01

ATOM
137
OD2
ASP
A
15
114.071
33.530
2.765
1.00
36.25

ATOM
138
C
ASP
A
15
115.473
33.882
7.413
1.00
35.08

ATOM
139
O
ASP
A
15
116.626
34.246
7.654
1.00
37.07

ATOM
140
N
TYR
A
16
114.433
34.244
8.162
1.00
34.55

ATOM
142
CA
TYR
A
16
114.598
35.098
9.337
1.00
34.48

ATOM
143
CB
TYR
A
16
113.239
35.554
9.865
1.00
34.89

ATOM
144
CG
TYR
A
16
113.320
36.661
10.891
1.00
35.28

ATOM
145
CD1
TYR
A
16
113.859
37.905
10.562
1.00
36.36

ATOM
146
CE1
TYR
A
16
113.921
38.936
11.496
1.00
34.26

ATOM
147
CD2
TYR
A
16
112.846
36.474
12.182
1.00
33.51

ATOM
148
CE2
TYR
A
16
112.903
37.498
13.118
1.00
34.97

ATOM
149
CZ
TYR
A
16
113.440
38.724
12.767
1.00
34.08

ATOM
150
OH
TYR
A
16
113.491
39.733
13.697
1.00
37.78

ATOM
152
C
TYR
A
16
115.348
34.340
10.427
1.00
35.46

ATOM
153
O
TYR
A
16
116.240
34.883
11.074
1.00
36.90

ATOM
154
N
ALA
A
17
114.982
33.081
10.625
1.00
36.20

ATOM
156
CA
ALA
A
17
115.632
32.250
11.617
1.00
35.77

ATOM
157
CB
ALA
A
17
115.025
30.870
11.615
1.00
33.78

ATOM
158
C
ALA
A
17
117.118
32.180
11.293
1.00
37.85

ATOM
159
O
ALA
A
17
117.957
32.330
12.178
1.00
40.31

ATOM
160
N
SER
A
18
117.447
32.008
10.017
1.00
39.36

ATOM
162
CA
SER
A
18
118.846
31.927
9.612
1.00
42.40

ATOM
163
CB
SER
A
18
118.993
31.399
8.175
1.00
43.78

ATOM
164
OG
SER
A
18
118.220
32.127
7.236
1.00
48.26

ATOM
166
C
SER
A
18
119.605
33.238
9.786
1.00
42.53

ATOM
167
O
SER
A
18
120.768
33.228
10.178
1.00
44.52

ATOM
168
N
GLN
A
19
118.959
34.367
9.509
1.00
42.42

ATOM
170
CA
GLN
A
19
119.630
35.652
9.665
1.00
42.67

ATOM
171
CB
GLN
A
19
118.805
36.806
9.089
1.00
47.13

ATOM
172
CG
GLN
A
19
118.810
36.864
7.563
1.00
57.52

ATOM
173
CD
GLN
A
19
118.457
38.238
7.012
1.00
62.74

ATOM
174
OE1
GLN
A
19
117.488
38.866
7.440
1.00
65.88

ATOM
175
NE2
GLN
A
19
119.248
38.710
6.051
1.00
64.58

ATOM
178
C
GLN
A
19
119.943
35.906
11.126
1.00
40.97

ATOM
179
O
GLN
A
19
121.030
36.378
11.456
1.00
41.85

ATOM
180
N
GLN
A
20
119.008
35.565
12.005
1.00
39.51

ATOM
182
CA
GLN
A
20
119.226
35.759
13.430
1.00
37.61

ATOM
183
CB
GLN
A
20
117.944
35.507
14.228
1.00
38.26

ATOM
184
CG
GLN
A
20
116.764
36.405
13.874
1.00
38.33

ATOM
185
CD
GLN
A
20
117.057
37.895
14.002
1.00
41.17

ATOM
186
OE1
GLN
A
20
116.912
38.642
13.040
1.00
43.42

ATOM
187
NE2
GLN
A
20
117.441
38.335
15.192
1.00
42.94

ATOM
190
C
GLN
A
20
120.325
34.805
13.878
1.00
36.56

ATOM
191
O
GLN
A
20
121.208
35.176
14.654
1.00
38.07

ATOM
192
N
GLY
A
21
120.285
33.587
13.348
1.00
36.41

ATOM
194
CA
GLY
A
21
121.276
32.585
13.688
1.00
33.84

ATOM
195
C
GLY
A
21
122.665
33.023
13.289
1.00
34.61

ATOM
196
O
GLY
A
21
123.520
33.199
14.140
1.00
36.02

ATOM
197
N
THR
A
22
122.879
33.221
11.994
1.00
35.98

ATOM
199
CA
THR
A
22
124.174
33.645
11.462
1.00
39.75

ATOM
200
CB
THR
A
22
24.036
34.109
9.983
1.00
41.34

ATOM
201
OG1
THR
A
22
123.400
33.082
9.212
1.00
40.97

ATOM
203
CG2
THR
A
22
125.397
34.408
9.377
1.00
40.54

ATOM
204
C
THR
A
22
124.780
34.785
12.285
1.00
40.46

ATOM
205
O
THR
A
22
125.954
34.741
12.667
1.00
41.11

ATOM
206
N
ALA
A
23
123.959
35.787
12.578
1.00
41.75

ATOM
208
CA
ALA
A
23
124.387
36.944
13.351
1.00
41.89

ATOM
209
CB
ALA
A
23
123.224
37.895
13.567
1.00
40.51

ATOM
210
C
ALA
A
23
124.919
36.461
14.678
1.00
43.71

ATOM
211
O
ALA
A
23
125.992
36.872
15.114
1.00
47.24

ATOM
212
N
ALA
A
24
124.175
35.554
15.298
1.00
43.71

ATOM
214
CA
ALA
A
24
124.570
34.991
16.574
1.00
43.02

ATOM
215
CB
ALA
A
24
123.413
34.238
17.185
1.00
43.37

ATOM
216
C
ALA
A
24
125.774
34.069
16.396
1.00
42.93

ATOM
217
O
ALA
A
24
126.549
33.868
17.328
1.00
45.41

ATOM
218
N
LEU
A
25
125.944
33.532
15.193
1.00
41.61

ATOM
220
CA
LEU
A
25
127.056
32.638
14.910
1.00
40.32

ATOM
221
CB
LEU
A
25
126.746
31.755
13.699
1.00
36.89

ATOM
222
CG
LEU
A
25
127.662
30.554
13.483
1.00
34.95

ATOM
223
CD1
LEU
A
25
127.636
29.653
14.703
1.00
34.64

ATOM
224
CD2
LEU
A
25
127.218
29.797
12.262
1.00
35.16

ATOM
225
C
LEU
A
25
128.331
33.438
14.676
1.00
40.69

ATOM
226
O
LEU
A
25
129.423
32.984
15.014
1.00
42.61

ATOM
227
N
GLN
A
26
128.194
34.644
14.138
1.00
41.51

ATOM
229
CA
GLN
A
26
129.352
35.494
13.878
1.00
45.29

ATOM
230
CB
GLN
A
26
128.920
36.850
13.317
1.00
46.09

ATOM
231
CG
GLN
A
26
130.087
37.811
13.108
1.00
48.70

ATOM
232
CD
GLN
A
26
129.650
39.240
12.861
1.00
50.15

ATOM
233
OE1
GLN
A
26
129.833
40.115
13.708
1.00
51.16

ATOM
234
NE2
GLN
A
26
129.078
39.489
11.692
1.00
51.55

ATOM
237
C
GLN
A
26
130.175
35.728
15.145
1.00
46.79

ATOM
238
O
GLN
A
26
131.403
35.587
15.136
1.00
46.74

ATOM
239
N
LYS
A
27
129.488
36.081
16.230
1.00
48.40

ATOM
241
CA
LYS
A
27
130.140
36.355
17.509
1.00
50.23

ATOM
242
CB
LYS
A
27
129.119
36.696
18.595
1.00
52.58

ATOM
243
CG
LYS
A
27
128.157
37.818
18.249
1.00
55.93

ATOM
244
CD
LYS
A
27
127.495
38.391
19.503
1.00
59.98

ATOM
245
CE
LYS
A
27
126.959
37.306
20.437
1.00
63.01

ATOM
246
NZ
LYS
A
27
125.911
36.452
19.807
1.00
66.76

ATOM
250
C
LYS
A
27
130.983
35.186
17.977
1.00
50.39

ATOM
251
O
LYS
A
27
132.121
35.369
18.398
1.00
52.00

ATOM
252
N
GLU
A
28
130.421
33.984
17.920
1.00
50.09

ATOM
254
CA
GLU
A
28
131.157
32.803
18.341
1.00
48.77

ATOM
255
CB
GLU
A
28
130.250
31.571
18.390
1.00
48.51

ATOM
256
CG
GLU
A
28
129.514
31.395
19.713
1.00
50.95

ATOM
257
CD
GLU
A
28
130.436
30.999
20.857
1.00
52.82

ATOM
258
OE1
GLU
A
28
130.687
29.789
21.030
1.00
55.51

ATOM
259
OE2
GLU
A
28
130.903
31.891
21.594
1.00
54.60

ATOM
260
C
GLU
A
28
132.343
32.564
17.421
1.00
46.96

ATOM
261
O
GLU
A
28
133.407
32.153
17.871
1.00
49.87

ATOM
262
N
LEU
A
29
132.177
32.868
16.140
1.00
43.03

ATOM
264
CA
LEU
A
29
133.257
32.674
15.189
1.00
39.75

ATOM
265
CB
LEU
A
29
132.740
32.817
13.763
1.00
36.79

ATOM
266
CG
LEU
A
29
131.832
31.658
13.360
1.00
33.73

ATOM
267
CD1
LEU
A
29
131.557
31.708
11.870
1.00
34.40

ATOM
268
CD2
LEU
A
29
132.499
30.347
13.720
1.00
31.01

ATOM
269
C
LEU
A
29
134.431
33.610
15.444
1.00
38.40

ATOM
270
O
LEU
A
29
135.584
33.204
15.348
1.00
38.06

ATOM
271
N
LYS
A
30
134.131
34.843
15.828
1.00
38.44

ATOM
273
CA
LYS
A
30
135.155
35.845
16.111
1.00
40.67

ATOM
274
CB
LYS
A
30
134.495
37.225
16.210
1.00
41.05

ATOM
275
CG
LYS
A
30
135.448
38.409
16.270
1.00
43.32

ATOM
276
CD
LYS
A
30
134.690
39.733
16.198
1.00
44.53

ATOM
277
CE
LYS
A
30
135.633
40.926
16.343
1.00
46.81

ATOM
278
NZ
LYS
A
30
134.912
42.238
16.331
1.00
50.27

ATOM
282
C
LYS
A
30
135.955
35.539
17.388
1.00
42.29

ATOM
283
O
LYS
A
30
136.979
36.166
17.654
1.00
42.94

ATOM
284
N
ARG
A
31
135.495
34.565
18.168
1.00
44.02

ATOM
286
CA
ARG
A
31
136.162
34.190
19.411
1.00
44.45

ATOM
287
CB
ARG
A
31
135.139
34.005
20.534
1.00
46.86

ATOM
288
CG
ARG
A
31
134.504
35.305
20.983
1.00
52.93

ATOM
289
CD
ARG
A
31
133.479
35.095
22.078
1.00
60.04

ATOM
290
NE
ARG
A
31
132.947
36.372
22.554
1.00
67.90

ATOM
292
CZ
ARG
A
31
131.839
36.505
23.279
1.00
71.80

ATOM
293
NH1
ARG
A
31
131.128
35.437
23.621
1.00
74.30

ATOM
296
NH2
ARG
A
31
131.444
37.710
23.672
1.00
73.67

ATOM
299
C
ARG
A
31
137.008
32.937
19.276
1.00
44.41

ATOM
300
O
ARG
A
31
137.339
32.293
20.273
1.00
46.21

ATOM
301
N
ILE
A
32
137.343
32.581
18.041
1.00
44.30

ATOM
303
CA
ILE
A
32
138.162
31.404
17.783
1.00
42.96

ATOM
304
CB
ILE
A
32
138.054
30.953
16.308
1.00
39.50

ATOM
305
CG2
ILE
A
32
139.146
29.950
15.973
1.00
36.12

ATOM
306
CG1
ILE
A
32
136.674
30.351
16.052
1.00
37.18

ATOM
307
CD1
ILE
A
32
136.431
29.975
14.624
1.00
37.20

ATOM
308
C
ILE
A
32
139.613
31.707
18.103
1.00
44.44

ATOM
309
O
ILE
A
32
140.109
32.794
17.798
1.00
45.60

ATOM
310
N
LYS
A
33
140.288
30.747
18.725
1.00
45.45

ATOM
312
CA
LYS
A
33
141.692
30.917
19.060
1.00
46.20

ATOM
313
CB
LYS
A
33
141.958
30.569
20.522
1.00
49.33

ATOM
314
CG
LYS
A
33
141.336
31.546
21.492
1.00
52.41

ATOM
315
CD
LYS
A
33
141.910
31.387
22.885
1.00
56.15

ATOM
316
CE
LYS
A
33
143.374
31.789
22.918
1.00
59.63

ATOM
317
NZ
LYS
A
33
143.891
31.817
24.313
1.00
63.31

ATOM
321
C
LYS
A
33
142.619
30.115
18.153
1.00
44.41

ATOM
322
O
LYS
A
33
142.563
28.884
18.102
1.00
42.99

ATOM
323
N
ILE
A
34
143.442
30.836
17.408
1.00
43.49

ATOM
325
CA
ILE
A
34
144.411
30.231
16.512
1.00
43.47

ATOM
326
CB
ILE
A
34
144.452
30.958
15.159
1.00
41.93

ATOM
327
CG2
ILE
A
34
143.322
30.464
14.280
1.00
41.39

ATOM
328
CG1
ILE
A
34
144.347
32.470
15.363
1.00
42.97

ATOM
329
CD1
ILE
A
34
143.967
33.234
14.108
1.00
44.59

ATOM
330
C
ILE
A
34
145.761
30.288
17.216
1.00
44.81

ATOM
331
O
ILE
A
34
146.142
31.319
17.778
1.00
46.96

ATOM
332
N
PRO
A
35
146.464
29.151
17.267
1.00
43.85

ATOM
333
CD
PRO
A
35
146.008
27.862
16.728
1.00
44.63

ATOM
334
CA
PRO
A
35
147.773
29.003
17.904
1.00
42.65

ATOM
335
CB
PRO
A
35
148.109
27.534
17.650
1.00
42.05

ATOM
336
CG
PRO
A
35
146.778
26.887
17.578
1.00
44.72

ATOM
337
C
PRO
A
35
148.860
29.899
17.334
1.00
43.14

ATOM
338
O
PRO
A
35
148.649
30.640
16.376
1.00
44.26

ATOM
339
N
ASP
A
36
150.026
29.827
17.959
1.00
42.32

ATOM
341
CA
ASP
A
36
151.181
30.584
17.535
1.00
41.85

ATOM
342
CB
ASP
A
36
151.933
31.125
18.745
1.00
43.04

ATOM
343
CG
ASP
A
36
151.155
32.196
19.485
1.00
45.33

ATOM
344
OD1
ASP
A
36
150.120
32.666
18.959
1.00
49.40

ATOM
345
OD2
ASP
A
36
151.591
32.584
20.588
1.00
46.99

ATOM
346
C
ASP
A
36
152.051
29.612
16.776
1.00
42.29

ATOM
347
O
ASP
A
36
152.175
28.450
17.159
1.00
43.32

ATOM
348
N
TYR
A
37
152.637
30.077
15.687
1.00
42.04

ATOM
350
CA
TYR
A
37
153.476
29.228
14.877
1.00
41.59

ATOM
351
CB
TYR
A
37
152.979
29.243
13.436
1.00
42.04

ATOM
352
CG
TYR
A
37
151.564
28.743
13.327
1.00
43.15

ATOM
353
CD1
TYR
A
37
151.295
27.378
13.256
1.00
42.32

ATOM
354
CE1
TYR
A
37
149.991
26.904
13.239
1.00
43.09

ATOM
355
CD2
TYR
A
37
150.487
29.626
13.370
1.00
44.59

ATOM
356
CE2
TYR
A
37
149.175
29.161
13.354
1.00
43.64

ATOM
357
CZ
TYR
A
37
148.938
27.799
13.291
1.00
42.12

ATOM
358
OH
TYR
A
37
147.651
27.327
13.307
1.00
43.31

ATOM
360
C
TYR
A
37
154.923
29.649
14.957
1.00
42.22

ATOM
361
O
TYR
A
37
155.311
30.692
14.443
1.00
43.15

ATOM
362
N
SER
A
38
155.714
28.833
15.634
1.00
44.23

ATOM
364
CA
SER
A
38
157.130
29.088
15.789
1.00
47.19

ATOM
365
CB
SER
A
38
157.466
29.330
17.257
1.00
47.44

ATOM
366
OG
SER
A
38
156.651
30.356
17.799
1.00
54.54

ATOM
368
C
SER
A
38
157.887
27.878
15.285
1.00
48.36

ATOM
369
O
SER
A
38
157.664
26.761
15.746
1.00
49.57

ATOM
370
N
ASP
A
39
158.773
28.103
14.327
1.00
50.18

ATOM
372
CA
ASP
A
39
159.569
27.030
13.763
1.00
52.06

ATOM
373
CB
ASP
A
39
158.822
26.402
12.579
1.00
53.01

ATOM
374
CG
ASP
A
39
159.375
25.043
12.179
1.00
54.91

ATOM
375
OD1
ASP
A
39
159.569
24.178
13.063
1.00
54.67

ATOM
376
OD2
ASP
A
39
159.600
24.837
10.969
1.00
56.72

ATOM
377
C
ASP
A
39
160.912
27.631
13.334
1.00
53.93

ATOM
378
O
ASP
A
39
161.100
28.853
13.384
1.00
54.67

ATOM
379
N
SER
A
40
161.868
26.771
13.003
1.00
54.19

ATOM
381
CA
SER
A
40
163.187
27.208
12.577
1.00
52.94

ATOM
382
CB
SER
A
40
164.255
26.307
13.202
1.00
52.97

ATOM
383
OG
SER
A
40
163.996
24.934
12.947
1.00
53.27

ATOM
385
C
SER
A
40
163.283
27.163
11.057
1.00
54.32

ATOM
386
O
SER
A
40
162.394
26.623
10.386
1.00
54.83

ATOM
387
N
PHE
A
41
164.358
27.730
10.516
1.00
55.12

ATOM
389
CA
PHE
A
41
164.580
27.742
9.074
1.00
55.04

ATOM
390
CB
PHE
A
41
163.908
28.967
8.424
1.00
50.91

ATOM
391
CG
PHE
A
41
164.564
30.285
8.756
1.00
46.23

ATOM
392
CD1
PHE
A
41
165.720
30.695
8.092
1.00
44.94

ATOM
393
CD2
PHE
A
41
164.019
31.124
9.719
1.00
44.37

ATOM
394
CE1
PHE
A
41
166.321
31.918
8.386
1.00
43.85

ATOM
395
CE2
PHE
A
41
164.614
32.350
10.018
1.00
43.51

ATOM
396
CZ
PHE
A
41
165.765
32.746
9.351
1.00
42.57

ATOM
397
C
PHE
A
41
166.071
27.724
8.756
1.00
56.75

ATOM
398
O
PHE
A
41
166.904
27.935
9.637
1.00
58.20

ATOM
399
N
LYS
A
42
166.391
27.455
7.496
1.00
59.71

ATOM
401
CA
LYS
A
42
167.768
27.427
7.010
1.00
63.27

ATOM
402
CB
LYS
A
42
168.474
26.129
7.425
1.00
64.98

ATOM
403
CG
LYS
A
42
169.984
26.140
7.215
1.00
68.46

ATOM
404
CD
LYS
A
42
170.706
25.591
8.449
1.00
70.94

ATOM
405
CE
LYS
A
42
172.227
25.630
8.298
1.00
71.66

ATOM
406
NZ
LYS
A
42
172.928
25.300
9.582
1.00
71.11

ATOM
410
C
LYS
A
42
167.706
27.552
5.487
1.00
64.24

ATOM
411
O
LYS
A
42
167.585
26.555
4.773
1.00
65.07

ATOM
412
N
ILE
A
43
167.725
28.792
5.003
1.00
64.98

ATOM
414
CA
ILE
A
43
167.652
29.070
3.570
1.00
64.79

ATOM
415
CB
ILE
A
43
166.721
30.282
3.282
1.00
65.08

ATOM
416
CG2
ILE
A
43
166.731
30.617
1.796
1.00
66.08

ATOM
417
CG1
ILE
A
43
165.293
29.965
3.745
1.00
64.11

ATOM
418
CD1
ILE
A
43
164.284
31.071
3.478
1.00
65.50

ATOM
419
C
ILE
A
43
169.039
29.291
2.956
1.00
64.78

ATOM
420
O
ILE
A
43
169.840
30.079
3.465
1.00
65.23

ATOM
421
N
LYS
A
44
169.273
28.631
1.825
1.00
64.51

ATOM
423
CA
LYS
A
44
170.539
28.672
1.093
1.00
63.65

ATOM
424
CB
LYS
A
44
170.328
28.232
−0.360
1.00
63.66

ATOM
425
CG
LYS
A
44
170.066
26.742
−0.553
1.00
63.81

ATOM
426
CD
LYS
A
44
170.064
26.396
−2.035
1.00
65.27

ATOM
427
CE
LYS
A
44
169.910
24.905
−2.289
1.00
65.86

ATOM
428
NZ
LYS
A
44
169.953
24.599
−3.751
1.00
66.87

ATOM
432
C
LYS
A
44
171.382
29.947
1.115
1.00
63.16

ATOM
433
O
LYS
A
44
172.600
29.876
1.274
1.00
65.20

ATOM
434
N
HIS
A
45
170.769
31.107
0.929
1.00
61.08

ATOM
436
CA
HIS
A
45
171.550
32.339
0.920
1.00
61.08

atom
437
CB
HIS
A
45
171.454
33.017
−0.447
1.00
64.62

ATOM
438
CG
HIS
A
45
172.039
32.214
−1.565
1.00
68.00

ATOM
439
CD2
HIS
A
45
171.695
32.126
−2.871
1.00
68.82

ATOM
440
ND1
HIS
A
45
173.124
31.380
−1.397
1.00
70.18

ATOM
442
CE1
HIS
A
45
173.425
30.815
−2.552
1.00
71.24

ATOM
443
NE2
HIS
A
45
172.572
31.250
−3.462
1.00
70.61

ATOM
445
C
HIS
A
45
171.167
33.337
1.994
1.00
59.87

ATOM
446
O
HIS
A
45
171.609
34.486
1.960
1.00
60.80

ATOM
447
N
LEU
A
46
170.345
32.900
2.940
1.00
57.18

ATOM
449
CA
LEU
A
46
169.881
33.767
4.012
1.00
53.69

ATOM
450
CB
LEU
A
46
168.362
33.699
4.103
1.00
53.23

ATOM
451
CG
LEU
A
46
167.715
34.609
5.135
1.00
51.73

ATOM
452
CG1
LEU
A
46
167.712
36.039
4.628
1.00
52.65

ATOM
453
CD2
LEU
A
46
166.310
34.126
5.390
1.00
51.01

ATOM
454
C
LEU
A
46
170.490
33.336
5.330
1.00
52.64

ATOM
455
O
LEU
A
46
170.908
34.168
6.136
1.00
52.10

ATOM
456
N
GLY
A
47
170.513
32.026
5.550
1.00
51.88

ATOM
458
CA
GLY
A
47
171.081
31.486
6.768
1.00
51.77

ATOM
459
C
GLY
A
47
170.107
30.643
7.564
1.00
51.44

ATOM
460
O
GLY
A
47
169.059
30.235
7.065
1.00
50.21

ATOM
461
N
LYS
A
48
170.484
30.357
8.802
1.00
52.15

ATOM
463
CA
LYS
A
48
169.664
29.572
9.711
1.00
52.12

ATOM
464
CB
LYS
A
48
170.497
28.479
10.407
1.00
56.73

ATOM
465
CG
LYS
A
48
171.878
28.907
10.938
1.00
62.50

ATOM
466
CD
LYS
A
48
172.953
28.876
9.843
1.00
65.46

ATOM
467
CE
LYS
A
48
174.332
29.252
10.380
1.00
66.23

ATOM
468
NZ
LYS
A
48
175.380
29.178
9.318
1.00
65.64

ATOM
472
C
LYS
A
48
169.041
30.510
10.738
1.00
49.63

ATOM
473
O
LYS
A
48
169.632
31.533
11.101
1.00
48.85

ATOM
474
N
GLY
A
49
167.846
30.174
11.200
1.00
46.79

ATOM
476
CA
GLY
A
49
167.197
31.026
12.169
1.00
47.22

ATOM
477
C
GLY
A
49
165.918
30.449
12.728
1.00
47.47

ATOM
478
O
GLY
A
49
165.594
29.285
12.506
1.00
46.51

ATOM
479
N
HIS
A
50
165.166
31.292
13.420
1.00
47.82

ATOM
481
CA
HIS
A
50
163.922
30.886
14.041
1.00
48.80

ATOM
482
CB
HIS
A
50
164.126
30.793
15.554
1.00
58.27

ATOM
483
CG
HIS
A
50
163.658
29.505
16.155
1.00
68.69

ATOM
484
CD2
HIS
A
50
164.349
28.453
16.657
1.00
72.98

ATOM
485
ND1
HIS
A
50
162.324
29.196
16.311
1.00
73.69

ATOM
487
CE1
HIS
A
50
162.212
28.010
16.885
1.00
76.58

ATOM
488
NE2
HIS
A
50
163.426
27.539
17.105
1.00
77.46

ATOM
490
C
HIS
A
50
162.905
31.965
13.742
1.00
45.89

ATOM
491
O
HIS
A
50
163.149
33.137
14.019
1.00
41.84

ATOM
492
N
TYR
A
51
161.785
31.585
13.143
1.00
46.60

ATOM
494
CA
TYR
A
51
160.746
32.555
12.824
1.00
48.52

ATOM
495
CB
TYR
A
51
160.308
32.420
11.354
1.00
50.04

ATOM
496
CG
TYR
A
51
159.360
31.280
11.098
1.00
51.79

ATOM
497
CD1
TYR
A
51
157.987
31.449
11.266
1.00
53.21

ATOM
498
CE1
TYR
A
51
157.111
30.396
11.103
1.00
56.71

ATOM
499
CD2
TYR
A
51
159.833
30.021
10.745
1.00
52.56

ATOM
500
CE2
TYR
A
51
158.959
28.955
10.573
1.00
56.44

ATOM
501
CZ
TYR
A
51
157.597
29.149
10.761
1.00
58.01

ATOM
502
OH
TYR
A
51
156.717
28.094
10.649
1.00
60.76

ATOM
504
C
TYR
A
51
159.566
32.330
13.763
1.00
47.31

ATOM
505
O
TYR
A
51
159.485
31.291
14.424
1.00
47.36

ATOM
506
N
SER
A
52
158.648
33.288
13.812
1.00
46.53

ATOM
508
CA
SER
A
52
157.480
33.163
14.669
1.00
43.69

ATOM
509
CB
SER
A
52
157.862
33.449
16.123
1.00
43.87

ATOM
510
OG
SER
A
52
156.759
33.233
16.986
1.00
42.88

ATOM
512
C
SER
A
52
156.344
34.083
14.253
1.00
41.60

ATOM
513
O
SER
A
52
156.558
35.261
13.981
1.00
42.86

ATOM
514
N
PHE
A
53
155.152
33.513
14.132
1.00
39.20

ATOM
516
CA
PHE
A
53
153.944
34.260
13.796
1.00
36.73

ATOM
517
CB
PHE
A
53
153.310
33.737
12.507
1.00
33.91

ATOM
518
CG
PHE
A
53
154.107
34.054
11.271
1.00
32.26

ATOM
519
CD1
PHE
A.
53
154.039
35.311
10.691
1.00
31.58

ATOM
520
CD2
PHE
A
53
154.912
33.092
10.682
1.00
30.53

ATOM
521
CE1
PHE
A
53
154.759
35.603
9.545
1.00
30.85

ATOM
522
CE2
PHE
A
53
155.637
33.373
9.533
1.00
30.45

ATOM
523
CZ
PHE
A
53
155.559
34.631
8.964
1.00
30.49

ATOM
524
C
PHE
A
53
153.071
33.965
15.006
1.00
35.40

ATOM
525
O
PHE
A
53
152.746
32.814
15.276
1.00
34.75

ATOM
526
N
TYR
A
54
152.720
34.998
15.757
1.00
34.80

ATOM
528
CA
TYR
A
54
151.960
34.798
16.974
1.00
37.29

ATOM
529
CB
TYR
A
54
152.947
34.533
18.103
1.00
39.38

ATOM
530
CG
TYR
A
54
153.841
35.721
18.375
1.00
42.01

ATOM
531
CD1
TYR
A
54
154.782
36.139
17.437
1.00
42.10

ATOM
532
CE1
TYR
A
54
155.552
37.270
17.649
1.00
40.85

ATOM
533
CD2
TYR
A
54
153.703
36.467
19.541
1.00
43.83

ATOM
534
CE2
TYR
A
54
154.472
37.600
19.763
1.00
43.33

ATOM
535
CZ
TYR
A
54
155.391
37.995
18.811
1.00
42.17

ATOM
536
OH
TYR
A
54
156.139
39.126
19.018
1.00
46.33

ATOM
538
C
TYR
A
54
151.100
35.990
17.362
1.00
38.69

ATOM
539
O
TYR
A
54
151.072
37.007
16.672
1.00
41.66

ATOM
540
N
SER
A
55
150.430
35.858
18.505
1.00
40.04

ATOM
542
CA
SER
A
55
149.562
36.894
19.056
1.00
40.41

ATOM
543
CB
SER
A
55
150.407
38.091
19.499
1.00
41.89

ATOM
544
OG
SER
A
55
149.708
38.923
20.409
1.00
46.68

ATOM
546
C
SER
A
55
148.489
37.318
18.051
1.00
41.35

ATOM
547
O
SER
A
55
148.115
38.492
17.973
1.00
40.80

ATOM
548
N
MET
A
56
147.984
36.346
17.299
1.00
42.39

ATOM
550
CA
MET
A
56
146.968
36.606
16.292
1.00
43.64

ATOM
551
CB
MET
A
56
146.996
35.513
15.225
1.00
42.07

ATOM
552
CG
MET
A
56
148.310
35.414
14.475
1.00
39.09

ATOM
553
SD
MET
A
56
148.335
34.056
13.289
1.00
41.60

ATOM
554
CE
MET
A
56
149.266
32.847
14.209
1.00
36.68

ATOM
555
C
MET
A
56
145.580
36.708
16.910
1.00
46.06

ATOM
556
O
MET
A
56
145.222
35.928
17.794
1.00
48.27

ATOM
557
N
ASP
A
57
144.820
37.700
16.463
1.00
47.20

ATOM
559
CA
ASP
A
57
143.466
37.930
16.941
1.00
47.94

ATOM
560
CB
ASP
A
57
143.408
39.167
17.848
1.00
52.70

ATOM
561
CG
ASP
A
57
143.578
38.831
19.324
1.00
58.73

ATOM
562
OD1
ASP
A
57
142.552
38.587
19.999
1.00
62.99

ATOM
563
OD2
ASP
A
57
144.729
38.835
19.818
1.00
59.77

ATOM
564
C
ASP
A
57
142.566
38.151
15.736
1.00
46.86

ATOM
565
O
ASP
A
57
143.001
38.684
14.712
1.00
44.98

ATOM
566
N
ILE
A
58
141.324
37.699
15.843
1.00
45.46

ATOM
568
CA
ILE
A
58
140.356
37.872
14.773
1.00
45.28

ATOM
569
CB
ILE
A
58
139.232
36.822
14.869
1.00
42.99

ATOM
570
CG2
ILE
A
58
138.200
37.052
13.782
1.00
41.93

ATOM
571
CG1
ILE
A
58
139.825
35.415
14.744
1.00
42.15

ATOM
572
CD1
ILE
A
58
138.803
34.306
14.802
1.00
41.09

ATOM
573
C
ILE
A
58
139.783
39.277
14.936
1.00
47.07

ATOM
574
O
ILE
A
58
139.271
39.615
15.999
1.00
48.46

ATOM
575
N
ARG
A
59
139.945
40.116
13.918
1.00
49.05

ATOM
577
CA
ARG
A
59
139.441
41.486
13.973
1.00
51.28

ATOM
578
CB
ARG
A
59
140.435
42.459
13.326
1.00
53.21

ATOM
579
CG
ARG
A
59
141.760
42.590
14.062
1.00
55.13

ATOM
580
CD
ARG
A
59
141.578
43.175
15.453
1.00
59.25

ATOM
581
NE
ARG
A
59
142.833
43.178
16.202
1.00
63.13

ATOM
583
CZ
ARG
A
59
142.981
43.681
17.424
1.00
66.00

ATOM
584
NH1
ARG
A
59
141.950
44.231
18.054
1.00
68.47

ATOM
587
NH2
ARG
A
59
144.164
43.631
18.022
1.00
67.15

ATOM
590
C
ARG
A
59
138.066
41.627
13.322
1.00
52.12

ATOM
591
O
ARG
A
59
137.256
42.456
13.746
1.00
54.45

ATOM
592
N
GLU
A
60
137.823
40.857
12.265
1.00
52.91

ATOM
594
CA
GLU
A
60
136.538
40.878
11.570
1.00
52.94

ATOM
595
CB
GLU
A
60
136.492
41.944
10.476
1.00
55.28

ATOM
596
CG
GLU
A
60
135.133
41.994
9.776
1.00
60.74

ATOM
597
CD
GLU
A
60
135.131
42.841
8.523
1.00
64.33

ATOM
598
OE1
GLU
A
60
135.450
44.046
8.618
1.00
67.37

ATOM
599
OE2
GLU
A
60
134.798
42.300
7.443
1.00
65.16

ATOM
600
C
GLU
A
60
136.279
39.518
10.948
1.00
51.42

ATOM
601
O
GLU
A
60
137.170
38.930
10.342
1.00
52.44

ATOM
602
N
PHE
A
61
135.052
39.035
11.093
1.00
50.66

ATOM
604
CA
PHE
A
61
134.646
37.741
10.558
1.00
49.14

ATOM
605
CB
PHE
A
61
134.536
36.736
11.707
1.00
44.10

ATOM
606
CG
PHE
A
61
134.679
35.308
11.289
1.00
37.41

ATOM
607
CD1
PHE
A
61
133.998
34.814
10.188
1.00
36.68

ATOM
608
CD2
PHE
A
61
135.486
34.448
12.018
1.00
34.73

ATOM
609
CE1
PHE
A
61
134.116
33.477
9.817
1.00
36.53

ATOM
610
CE2
PHE
A
61
135.612
33.115
11.658
1.00
34.86

ATOM
611
CZ
PHE
A
61
134.922
32.627
10.553
1.00
35.68

ATOM
612
C
PHE
A
61
133.278
37.962
9.924
1.00
50.95

ATOM
613
O
PHE
A
61
132.249
37.646
10.521
1.00
52.86

ATOM
614
N
GLN
A
62
133.259
38.540
8.729
1.00
51.57

ATOM
616
CA
GLN
A
62
131.993
38.813
8.080
1.00
51.07

ATOM
617
CB
GLN
A
62
132.097
39.993
7.120
1.00
54.59

ATOM
618
CG
GLN
A
62
130.727
40.463
6.639
1.00
62.31

ATOM
619
CD
GLN
A
62
130.775
41.665
5.708
1.00
67.35

ATOM
620
OE1
GLN
A
62
129.812
41.935
4.991
1.00
69.86

ATOM
621
NE2
GLN
A
62
131.884
42.401
5.727
1.00
71.01

ATOM
624
C
GLN
A
62
131.391
37.625
7.367
1.00
48.52

ATOM
625
O
GLN
A
62
132.065
36.912
6.629
1.00
48.13

ATOM
626
N
LEU
A
63
130.107
37.422
7.622
1.00
48.11

ATOM
628
CA
LEU
A
63
129.324
36.358
7.017
1.00
47.47

ATOM
629
CB
LEU
A
63
128.753
35.438
8.103
1.00
44.43

ATOM
630
CG
LEU
A
63
129.754
34.759
9.044
1.00
42.13

ATOM
631
CD1
LEU
A
63
129.021
34.080
10.181
1.00
42.20

ATOM
632
CD2
LEU
A
63
130.593
33.752
8.282
1.00
40.96

ATOM
633
C
LEU
A
63
128.208
37.122
6.314
1.00
48.35

ATOM
634
O
LEU
A
63
127.138
37.345
6.882
1.00
49.30

ATOM
635
N
PRO
A
64
128.471
37.585
5.082
1.00
49.75

ATOM
636
CD
PRO
A
64
129.686
37.302
4.297
1.00
50.27

ATOM
637
CA
PRO
A
64
127.508
38.347
4.283
1.00
50.73

ATOM
638
CB
PRO
A
64
128.309
38.687
3.026
1.00
50.48

ATOM
639
CG
PRO
A
64
129.210
37.513
2.878
1.00
49.49

ATOM
640
C
PRO
A
64
126.219
37.616
3.937
1.00
51.98

ATOM
641
O
PRO
A
64
125.129
38.167
4.083
1.00
54.28

ATOM
642
N
SER
A
65
126.341
36.375
3.488
1.00
51.59

ATOM
644
CA
SER
A
65
125.177
35.607
3.101
1.00
50.95

ATOM
645
CB
SER
A
65
125.217
35.356
1.599
1.00
52.70

ATOM
646
OG
SER
A
65
126.503
34.910
1.205
1.00
55.07

ATOM
648
C
SER
A
65
125.053
34.288
3.832
1.00
50.87

ATOM
649
O
SER
A
65
126.052
33.627
4.120
1.00
52.05

ATOM
650
N
SER
A
66
123.811
33.928
4.136
1.00
50.53

ATOM
652
CA
SER
A
66
123.477
32.680
4.805
1.00
48.85

ATOM
653
CB
SER
A
66
123.322
32.878
6.312
1.00
48.24

ATOM
654
OG
SER
A
66
122.307
33.820
6.615
1.00
49.82

ATOM
656
C
SER
A
66
122.154
32.244
4.202
1.00
49.43

ATOM
657
O
SER
A
66
121.365
33.080
3.745
1.00
48.59

ATOM
658
N
GLN
A
67
121.925
30.940
4.165
1.00
49.88

ATOM
660
CA
GLN
A
67
120.696
30.409
3.605
1.00
49.90

ATOM
661
CB
GLN
A
67
120.831
30.267
2.086
1.00
52.61

ATOM
662
CG
GLN
A
67
121.928
29.308
1.632
1.00
58.79

ATOM
663
CD
GLN
A
67
121.984
29.154
0.121
1.00
62.57

ATOM
664
OE1
GLN
A
67
122.550
29.997
−0.576
1.00
66.32

ATOM
665
NE2
GLN
A
67
121.407
28.073
−0.392
1.00
62.89

ATOM
668
C
GLN
A
67
120.337
29.065
4.221
1.00
48.02

ATOM
669
O
GLN
A
67
121.215
28.306
4.635
1.00
49.44

ATOM
670
N
ILE
A
68
119.040
28.803
4.328
1.00
45.23

ATOM
672
CA
ILE
A
68
118.551
27.544
4.864
1.00
42.63

ATOM
673
CB
ILE
A
68
117.826
27.721
6.220
1.00
44.01

ATOM
674
CG2
ILE
A
68
116.977
26.499
6.546
1.00
45.24

ATOM
675
CG1
ILE
A
68
118.850
27.925
7.333
1.00
44.56

ATOM
676
CD1
ILE
A
68
118.260
27.851
8.719
1.00
47.20

ATOM
677
C
ILE
A
68
117.613
26.935
3.835
1.00
40.01

ATOM
678
O
ILE
A
68
116.560
27.491
3.524
1.00
41.30

ATOM
679
N
SER
A
69
118.051
25.833
3.250
1.00
37.17

ATOM
681
CA
SER
A
69
117.264
25.140
2.258
1.00
34.46

ATOM
682
CB
SER
A
69
118.165
24.600
1.147
1.00
34.89

ATOM
683
OG
SER
A
69
118.890
25.640
0.511
1.00
40.63

ATOM
685
C
SER
A
69
116.570
23.984
2.939
1.00
33.71

ATOM
686
O
SER
A
69
117.085
23.414
3.896
1.00
34.03

ATOM
687
N
MET
A
70
115.405
23.625
2.430
1.00
33.11

ATOM
689
CA
MET
A
70
114.659
22.519
2.981
1.00
34.74

ATOM
690
CB
MET
A
70
113.166
22.841
3.012
1.00
36.59

ATOM
691
CG
MET
A
70
112.794
23.880
4.051
1.00
41.38

ATOM
692
SD
MET
A
70
111.050
24.288
4.028
1.00
47.62

ATOM
693
CE
MET
A
70
111.101
25.834
3.173
1.00
47.72

ATOM
694
C
MET
A
70
114.906
21.274
2.153
1.00
35.74

ATOM
695
O
MET
A
70
114.752
21.279
0.928
1.00
37.33

ATOM
696
N
VAL
A
71
115.366
20.226
2.820
1.00
35.02

ATOM
698
CA
VAL
A
71
115.613
18.957
2.165
1.00
32.82

ATOM
699
CB
VAL
A
71
116.938
18.343
2.637
1.00
30.47

ATOM
700
CG1
VAL
A
71
117.206
17.049
1.905
1.00
28.06

ATOM
701
CG2
VAL
A
71
118.069
19.324
2.404
1.00
28.88

ATOM
702
C
VAL
A
71
114.438
18.072
2.571
1.00
33.73

ATOM
703
O
VAL
A
71
114.430
17.505
3.664
1.00
35.31

ATOM
704
N
PRO
A
72
113.411
17.975
1.708
1.00
33.98

ATOM
705
CD
PRO
A
72
113.402
18.500
0.327
1.00
33.44

ATOM
706
CA
PRO
A
72
112.211
17.168
1.965
1.00
34.72

ATOM
707
CB
PRO
A
72
111.660
16.936
0.562
1.00
33.90

ATOM
708
CG
PRO
A
72
111.980
18.231
−0.124
1.00
32.49

ATOM
709
C
PRO
A
72
112.495
15.857
2.695
1.00
36.34

ATOM
710
O
PRO
A
72
113.417
15.131
2.340
1.00
39.70

ATOM
711
N
ASN
A
73
111.745
15.607
3.765
1.00
38.08

ATOM
713
CA
ASN
A
73
111.886
14.399
4.580
1.00
39.44

ATOM
714
CB
ASN
A
73
111.553
13.146
3.768
1.00
45.34

ATOM
715
CG
ASN
A
73
110.071
12.875
3.699
1.00
50.49

ATOM
716
OD1
ASN
A
73
109.392
13.317
2.770
1.00
53.54

ATOM
717
ND2
ASN
A
73
109.552
12.149
4.690
1.00
53.95

ATOM
720
C
ASN
A
73
113.231
14.192
5.252
1.00
38.00

ATOM
721
O
ASN
A
73
113.408
13.204
5.962
1.00
37.89

ATOM
722
N
VAL
A
74
114.165
15.116
5.050
1.00
37.67

ATOM
724
CA
VAL
A
74
115.498
14.995
5.632
1.00
36.66

ATOM
725
CB
VAL
A
74
116.598
15.041
4.525
1.00
37.47

ATOM
726
CG1
VAL
A
74
117.976
14.753
5.118
1.00
35.10

ATOM
727
CG2
VAL
A
74
116.280
14.046
3.402
1.00
33.69

ATOM
728
C
VAL
A
74
115.784
16.054
6.704
1.00
37.30

ATOM
729
O
VAL
A
74
116.106
15.717
7.848
1.00
39.11

ATOM
730
N
GLY
A
75
115.672
17.328
6.342
1.00
35.75

ATOM
732
CA
GLY
A
75
115.928
18.384
7.306
1.00
33.77

ATOM
733
C
GLY
A
75
116.279
19.698
6.647
1.00
33.37

ATOM
734
O
GLY
A
75
115.827
19.981
5.536
1.00
32.85

ATOM
735
N
LEU
A
76
117.075
20.509
7.338
1.00
34.22

ATOM
737
CA
LEU
A
76
117.504
21.811
6.828
1.00
33.33

ATOM
738
CB
LEU
A
76
117.329
22.894
7.897
1.00
30.43

ATOM
739
CG
LEU
A
76
115.958
23.105
8.524
1.00
28.67

ATOM
740
CD1
LEU
A
76
116.081
24.069
9.683
1.00
29.06

ATOM
741
CD2
LEU
A
76
114.995
23.633
7.481
1.00
31.34

ATOM
742
C
LEU
A
76
118.979
21.755
6.448
1.00
33.33

ATOM
743
O
LEU
A
76
119.736
20.942
6.967
1.00
34.06

ATOM
744
N
LYS
A
77
119.383
22.636
5.550
1.00
34.34

ATOM
746
CA
LYS
A
77
120.766
22.711
5.131
1.00
33.56

ATOM
747
CB
LYS
A
77
120.927
22.201
3.700
1.00
35.32

ATOM
748
CG
LYS
A
77
122.345
22.283
3.166
1.00
38.99

ATOM
749
CD
LYS
A
77
122.450
21.670
1.782
1.00
41.42

ATOM
750
CE
LYS
A
77
122.388
20.150
1.838
1.00
41.64

ATOM
751
NZ
LYS
A
77
123.630
19.565
2.421
1.00
43.94

ATOM
755
C
LYS
A
77
121.131
24.175
5.228
1.00
34.11

ATOM
756
O
LYS
A
77
120.556
25.013
4.538
1.00
34.01

ATOM
757
N
PHE
A
78
122.009
24.478
6.173
1.00
36.93

ATOM
759
CA
PHE
A
78
122.482
25.830
6.427
1.00
37.23

ATOM
760
CB
PHE
A
78
122.720
25.983
7.933
1.00
37.11

ATOM
761
CG
PHE
A
78
123.233
27.329
8.340
1.00
36.19

ATOM
762
CD1
PHE
A
78
122.536
28.481
8.016
1.00
35.10

ATOM
763
CD2
PHE
A
78
124.415
27.442
9.059
1.00
36.97

ATOM
764
CE1
PHE
A
78
123.008
29.725
8.400
1.00
33.97

ATOM
765
CE2
PHE
A
78
124.892
28.679
9.446
1.00
36.53

ATOM
766
CZ
PHE
A
78
124.185
29.824
9.115
1.00
36.23

ATOM
767
C
PHE
A
78
123.780
26.063
5.646
1.00
38.21

ATOM
768
O
PHE
A
78
124.706
25.256
5.731
1.00
37.35

ATOM
769
N
SER
A
79
123.845
27.160
4.892
1.00
39.48

ATOM
771
CA
SER
A
79
125.028
27.489
4.097
1.00
40.20

ATOM
772
CB
SER
A
79
124.802
27.126
2.625
1.00
41.51

ATOM
773
OG
SER
A
79
124.408
25.773
2.464
1.00
48.40

ATOM
775
C
SER
A
79
125.416
28.963
4.160
1.00
40.10

ATOM
776
O
SER
A
79
124.557
29.842
4.112
1.00
39.14

ATOM
777
N
ILE
A
80
126.713
29.219
4.297
1.00
40.97

ATOM
779
CA
ILE
A
80
127.263
30.575
4.309
1.00
41.40

ATOM
780
CB
ILE
A
80
128.002
30.885
5.612
1.00
39.45

ATOM
781
CG2
ILE
A
80
128.518
32.307
5.583
1.00
40.67

ATOM
782
CG1
ILE
A
80
127.057
30.714
6.797
1.00
38.41

ATOM
783
CD1
ILE
A
80
127.690
31.022
8.120
1.00
39.45

ATOM
784
C
ILE
A
80
128.246
30.524
3.143
1.00
43.93

ATOM
785
O
ILE
A
80
128.944
29.519
2.976
1.00
45.50

ATOM
786
N
SER
A
81
128.327
31.585
2.344
1.00
47.35

ATOM
788
CA
SER
A
81
129.193
31.541
1.168
1.00
49.22

ATOM
789
CB
SER
A
81
128.338
31.613
−0.097
1.00
49.49

ATOM
790
OG
SER
A
81
127.332
32.602
0.032
1.00
52.43

ATOM
792
C
SER
A
81
130.412
32.432
1.004
1.00
50.65

ATOM
793
O
SER
A
81
131.482
31.937
0.658
1.00
52.88

ATOM
794
N
ASN
A
82
130.276
33.738
1.185
1.00
52.50

ATOM
796
CA
ASN
A
82
131.442
34.599
0.995
1.00
54.71

ATOM
797
CB
ASN
A
82
131.104
35.767
0.061
1.00
58.34

ATOM
798
CG
ASN
A
82
132.342
36.391
−0.570
1.00
61.43

ATOM
799
OD1
ASN
A
82
132.462
37.613
−0.657
1.00
63.94

ATOM
800
ND2
ASN
A
82
133.257
35.550
−1.039
1.00
61.92

ATOM
803
C
ASN
A
82
132.040
35.098
2.303
1.00
54.00

ATOM
804
O
ASN
A
82
132.268
36.297
2.482
1.00
54.15

ATOM
805
N
ALA
A
83
132.325
34.162
3.205
1.00
53.37

ATOM
807
CA
ALA
A
83
132.892
34.501
4.506
1.00
52.11

ATOM
808
CB
ALA
A
83
132.952
33.273
5.402
1.00
51.81

ATOM
809
C
ALA
A
83
134.272
35.131
4.359
1.00
50.64

ATOM
810
O
ALA
A
83
135.124
34.640
3.610
1.00
49.58

ATOM
811
N
ASN
A
84
134.467
36.228
5.078
1.00
48.85

ATOM
813
CA
ASN
A
84
135.706
36.983
5.063
1.00
47.97

ATOM
814
CB
ASN
A
84
135.423
38.393
4.536
1.00
51.32

ATOM
815
CG
ASN
A
84
136.560
39.361
4.793
1.00
56.05

ATOM
816
OD1
ASN
A
84
137.470
39.499
3.978
1.00
61.24

ATOM
817
ND2
ASN
A
84
136.500
40.060
5.919
1.00
56.91

ATOM
820
C
ASN
A
84
136.243
37.042
6.485
1.00
45.82

ATOM
821
O
ASN
A
84
135.601
37.606
7.368
1.00
47.29

ATOM
822
N
ILE
A
85
137.405
36.438
6.703
1.00
43.85

ATOM
824
CA
ILE
A
85
138.052
36.402
8.014
1.00
41.41

ATOM
825
CB
ILE
A
85
138.495
34.952
8.386
1.00
35.61

ATOM
826
CG2
ILE
A
85
139.011
34.901
9.804
1.00
32.01

ATOM
827
CG1
ILE
A
85
137.342
33.965
8.222
1.00
30.72

ATOM
828
CD1
ILE
A
85
137.712
32.557
8.587
1.00
25.79

ATOM
829
C
ILE
A
85
139.315
37.272
8.017
1.00
43.73

ATOM
830
O
ILE
A
85
140.343
36.873
7.471
1.00
47.66

ATOM
831
N
LYS
A
86
139.239
38.471
8.578
1.00
42.83

ATOM
833
CA
LYS
A
86
140.420
39.313
8.645
1.00
43.65

ATOM
834
CB
LYS
A
86
140.090
40.779
8.363
1.00
47.39

ATOM
835
CG
LYS
A
86
139.895
41.055
6.873
1.00
54.31

ATOM
836
CD
LYS
A
86
140.065
42.528
6.509
1.00
58.05

ATOM
837
CE
LYS
A
86
138.937
43.394
7.045
1.00
61.18

ATOM
838
NZ
LYS
A
86
139.107
44.820
6.642
1.00
64.32

ATOM
842
C
LYS
A
86
141.100
39.135
9.996
1.00
43.61

ATOM
843
O
LYS
A
86
140.514
39.404
11.043
1.00
42.95

ATOM
844
N
ILE
A
87
142.327
38.627
9.961
1.00
43.89

ATOM
846
CA
ILE
A
87
143.104
38.373
11.165
1.00
44.27

ATOM
847
CB
ILE
A
87
143.568
36.895
11.206
1.00
43.55

ATOM
848
CG2
ILE
A
87
144.365
36.609
12.473
1.00
42.71

ATOM
849
CG1
ILE
A
87
142.358
35.964
11.129
1.00
41.65

ATOM
850
CD1
ILE
A
87
142.723
34.504
11.044
1.00
42.75

ATOM
851
C
ILE
A
87
144.327
39.291
11.212
1.00
44.82

ATOM
852
O
ILE
A
87
144.817
39.745
10.176
1.00
46.46

ATOM
853
N
SER
A
88
144.805
39.568
12.417
1.00
43.43

ATOM
855
CA
SER
A
88
145.970
40.414
12.606
1.00
44.37

ATOM
856
CB
SER
A
88
145.548
41.825
13.027
1.00
46.30

ATOM
857
OG
ser
a
88
144.757
42.451
12.029
1.00
50.16

ATOM
859
C
SER
A
88
146.830
39.795
13.690
1.00
43.85

ATOM
860
O
SER
A
88
146.327
39.073
14.549
1.00
43.41

ATOM
861
N
GLY
A
89
148.128
40.061
13.638
1.00
45.04

ATOM
863
CA
GLY
A
89
149.029
39.525
14.640
1.00
47.03

ATOM
864
C
GLY
A
89
150.415
40.123
14.532
1.00
47.50

ATOM
865
O
GLY
A
89
150.611
41.140
13.861
1.00
47.81

ATOM
866
N
LYS
A
90
151.377
39.497
15.200
1.00
47.62

ATOM
868
CA
LYS
A
90
152.759
39.957
15.176
1.00
47.17

ATOM
869
CB
LYS
A
90
153.197
40.427
16.567
1.00
47.20

ATOM
870
CG
LYS
A
90
152.328
41.514
17.189
1.00
49.57

ATOM
871
CD
LYS
A
90
152.708
41.723
18.651
1.00
53.99

ATOM
872
CE
LYS
A
90
151.725
42.625
19.391
1.00
57.45

ATOM
873
NZ
LYS
A
90
152.042
42.735
20.855
1.00
59.91

ATOM
877
C
LYS
A
90
153.629
38.787
14.738
1.00
45.69

ATOM
878
O
LYS
A
90
153.171
37.644
14.697
1.00
45.87

ATOM
879
N
TRP
A
91
154.874
39.078
14.389
1.00
44.12

ATOM
881
CA
TRP
A
91
155.817
38.052
13.969
1.00
43.19

ATOM
882
CB
TRP
A
91
155.734
37.824
12.456
1.00
39.90

ATOM
883
CG
TRP
A
91
156.078
39.038
11.694
1.00
37.85

ATOM
884
CD2
TRP
A
91
157.390
39.466
11.313
1.00
39.20

ATOM
885
CE2
TRP
A
91
157.251
40.722
10.682
1.00
39.17

ATOM
886
CE3
TRP
A
91
158.672
38.918
11.451
1.00
36.54

ATOM
887
CD1
TRP
A
91
155.222
40.012
11.286
1.00
39.46

ATOM
888
NE1
TRP
A
91
155.916
41.032
10.681
1.00
39.30

ATOM
890
CZ2
TRP
A
91
158.344
41.437
10.188
1.00
38.03

ATOM
891
CZ3
TRP
A
91
159.757
39.628
10.963
1.00
35.59

ATOM
892
CH2
TRP
A
91
159.585
40.876
10.338
1.00
36.22

ATOM
893
C
TRP
A
91
157.218
38.520
14.339
1.00
43.43

ATOM
894
O
TRP
A
91
157.460
39.717
14.509
1.00
44.14

ATOM
895
N
LYS
A
92
158.136
37.575
14.468
1.00
44.32

ATOM
897
CA
LYS
A
92
159.517
37.892
14.789
1.00
44.34

ATOM
898
CB
LYS
A
92
159.717
38.076
16.302
1.00
47.57

ATOM
899
CG
LYS
A
92
159.252
36.933
17.200
1.00
53.21

ATOM
900
CD
LYS
A
92
159.361
37.354
18.678
1.00
57.24

ATOM
901
CE
LYS
A
92
158.844
36.283
19.650
1.00
59.23

ATOM
902
NZ
LYS
A
92
158.816
36.742
21.083
1.00
59.30

ATOM
906
C
LYS
A
92
160.409
36.801
14.227
1.00
42.18

ATOM
907
O
LYS
A
92
160.052
35.623
14.255
1.00
43.11

ATOM
908
N
ALA
A
93
161.521
37.214
13.632
1.00
39.24

ATOM
910
CA
ALA
A
93
162.471
36.294
13.033
1.00
36.99

ATOM
911
CB
ALA
A
93
162.410
36.392
11.515
1.00
36.10

ATOM
912
C
ALA
A
93
163.850
36.675
13.525
1.00
37.81

ATOM
913
O
ALA
A
93
164.130
37.851
13.747
1.00
39.61

ATOM
914
N
GLN
A
94
164.706
35.679
13.705
1.00
39.81

ATOM
916
CA
GLN
A
94
166.060
35.919
14.173
1.00
41.70

ATOM
917
CB
GLN
A
94
166.184
35.541
15.647
1.00
45.63

ATOM
918
CG
GLN
A
94
167.552
35.803
16.237
1.00
55.83

ATOM
919
CD
GLN
A
94
167.559
35.745
17.750
1.00
63.01

ATOM
920
OE1
GLN
A
94
168.328
36.456
18.406
1.00
67.41

ATOM
921
NE2
GLN
A
94
166.703
34.899
18.320
1.00
66.99

ATOM
924
C
GLN
A
94
167.067
35.139
13.340
1.00
41.13

ATOM
925
O
GLN
A
94
166.952
33.921
13.194
1.00
41.48

ATOM
926
N
LYS
A
95
168.024
35.865
12.771
1.00
41.51

ATOM
928
CA
LYS
A
95
169.084
35.302
11.938
1.00
40.50

ATOM
929
CB
LYS
A
95
169.000
35.901
10.531
1.00
40.86

ATOM
930
CG
LYS
A
95
170.099
35.478
9.580
1.00
44.00

ATOM
931
CD
LYS
A
95
169.849
36.030
8.175
1.00
46.44

ATOM
932
CE
LYS
A
95
169.767
37.553
8.161
1.00
48.82

ATOM
933
NZ
LYS
A
95
169.529
38.117
6.799
1.00
49.76

ATOM
937
C
LYS
A
95
170.381
35.705
12.631
1.00
39.51

ATOM
938
O
LYS
A
95
170.781
36.869
12.594
1.00
39.68

ATOM
939
N
ARG
A
96
171.000
34.743
13.304
1.00
39.70

ATOM
941
CA
ARG
A
96
172.229
34.965
14.065
1.00
38.81

ATOM
942
CB
ARG
A
96
173.386
35.432
13.159
1.00
38.58

ATOM
943
CG
ARG
A
96
174.757
35.415
13.848
1.00
36.99

ATOM
944
CD
ARG
A
96
175.919
35.584
12.869
1.00
35.28

ATOM
945
NE
ARG
A
96
177.207
35.640
13.562
1.00
37.59

ATOM
947
CZ
ARG
A
96
177.887
34.582
14.004
1.00
38.32

ATOM
948
NH1
ARG
A
96
177.425
33.351
13.832
1.00
41.87

ATOM
951
NH2
ARG
A
96
179.024
34.758
14.658
1.00
34.85

ATOM
954
C
ARG
A
96
171.909
35.972
15.183
1.00
38.25

ATOM
955
O
ARG
A
96
171.091
35.672
16.048
1.00
38.45

ATOM
956
N
PHE
A
97
172.506
37.161
15.158
1.00
36.05

ATOM
958
CA
PHE
A
97
172.236
38.157
16.189
1.00
32.76

ATOM
959
CB
PHE
A
97
173.521
38.856
16.634
1.00
29.39

ATOM
960
CG
PHE
A
97
174.503
37.958
17.311
1.00
27.30

ATOM
961
CD1
PHE
A
97
174.214
37.392
18.538
1.00
26.91

ATOM
962
CD2
PHE
A
97
175.733
37.695
16.728
1.00
29.62

ATOM
963
CE1
PHE
A
97
175.140
36.578
19.175
1.00
28.35

ATOM
964
CE2
PHE
A
97
176.661
36.886
17.358
1.00
27.60

ATOM
965
CZ
PHE
A
97
176.364
36.327
18.582
1.00
28.30

ATOM
966
C
PHE
A
97
171.261
39.208
15.693
1.00
34.25

ATOM
967
O
PHE
A
97
171.016
40.199
16.387
1.00
33.16

ATOM
968
N
LEU
A
98
170.739
39.012
14.484
1.00
36.60

ATOM
970
CA
LEU
A
98
169.790
39.952
13.888
1.00
39.31

ATOM
971
CB
LEU
A
98
169.874
39.905
12.361
1.00
38.74

ATOM
972
CG
LEU
A
98
169.875
41.238
11.608
1.00
38.17

ATOM
973
CD1
LEU
A
98
169.883
40.951
10.128
1.00
40.67

ATOM
974
CD2
LEU
A
98
168.680
42.093
11.971
1.00
38.92

ATOM
975
C
LEU
A
98
168.366
39.631
14.317
1.00
40.51

ATOM
976
O
LEU
A
98
167.854
38.554
14.016
1.00
42.93

ATOM
977
N
LYS
A
99
167.737
40.570
15.018
1.00
41.98

ATOM
979
CA
LYS
A
99
166.365
40.410
15.488
1.00
42.37

ATOM
980
CB
LYS
A
99
166.258
40.705
16.989
1.00
41.90

ATOM
981
CG
LYS
A
99
166.690
39.566
17.898
1.00
45.06

ATOM
982
CD
LYS
A
99
166.389
39.882
19.361
1.00
47.68

ATOM
983
CE
LYS
A
99
166.638
38.671
20.250
1.00
51.09

ATOM
984
NZ
LYS
A
99
166.251
38.895
21.674
1.00
53.87

ATOM
988
C
LYS
A
99
165.440
41.351
14.727
1.00
43.86

ATOM
989
O
LYS
A
99
165.634
42.573
14.739
1.00
45.41

ATOM
990
N
MET
A
100
164.438
40.785
14.064
1.00
43.74

ATOM
992
CA
MET
A
100
163.479
41.575
13.310
1.00
43.78

ATOM
993
CB
MET
A
100
163.576
41.234
11.826
1.00
44.48

ATOM
994
CG
MET
A
100
164.885
41.651
11.195
1.00
45.32

ATOM
995
SD
MET
A
100
165.190
40.802
9.654
1.00
49.68

ATOM
996
CE
MET
A
100
165.736
39.168
10.290
1.00
44.16

ATOM
997
C
MET
A
100
162.078
41.292
13.832
1.00
44.78

ATOM
998
O
MET
A
100
161.693
40.132
13.987
1.00
44.97

ATOM
999
N
SER
A
101
161.335
42.352
14.140
1.00
46.57

ATOM
1001
CA
SER
A
101
159.971
42.221
14.650
1.00
47.86

ATOM
1002
CB
SER
A
101
159.934
42.469
16.162
1.00
49.20

ATOM
1003
OG
SER
A
101
160.560
43.693
16.509
1.00
51.70

ATOM
1005
C
SER
A
101
159.009
43.168
13.937
1.00
48.68

ATOM
1006
O
SER
A
101
159.428
44.161
13.332
1.00
48.84

ATOM
1007
N
GLY
A
102
157.722
42.839
13.986
1.00
49.46

ATOM
1009
CA
GLY
A
102
156.716
43.664
13.343
1.00
49.50

ATOM
1010
C
GLY
A
102
155.359
42.989
13.341
1.00
48.98

ATOM
1011
O
GLY
A
102
155.251
41.795
13.613
1.00
50.09

ATOM
1012
N
ASN
A
103
154.317
43.766
13.079
1.00
48.68

ATOM
1014
CA
ASN
A
103
152.957
43.243
13.042
1.00
47.35

ATOM
1015
CB
ASN
A
103
151.945
44.349
13.391
1.00
49.87

ATOM
1016
CG
ASN
A
103
152.061
44.837
14.840
1.00
51.69

ATOM
1017
OD1
ASN
A
103
153.067
45.423
15.234
1.00
53.03

ATOM
1018
ND2
ASN
A
103
151.014
44.621
15.625
1.00
53.17

ATOM
1021
C
ASN
A
103
152.703
42.743
11.625
1.00
46.11

ATOM
1022
O
ASN
A
103
153.459
43.073
10.708
1.00
45.99

ATOM
1023
N
PHE
A
104
151.667
41.926
11.451
1.00
44.40

ATOM
1025
CA
PHE
A
104
151.306
41.410
10.131
1.00
42.85

ATOM
1026
CB
PHE
A
104
151.987
40.051
9.835
1.00
42.59

ATOM
1027
CG
PHE
A
104
151.319
38.849
10.482
1.00
41.53

ATOM
1028
CD1
PHE
A
104
151.650
38.458
11.776
1.00
39.25

ATOM
1029
CD2
PHE
A
104
150.380
38.095
9.778
1.00
39.79

ATOM
1030
CE1
PHE
A
104
151.058
37.339
12.357
1.00
37.60

ATOM
1031
CE2
PHE
A
104
149.784
36.976
10.353
1.00
36.72

ATOM
1032
CZ
PHE
A
104
150.125
36.599
11.644
1.00
37.02

ATOM
1033
C
PHE
A
104
149.788
41.303
10.006
1.00
42.22

ATOM
1034
O
PHE
A
104
149.081
41.251
11.014
1.00
43.09

ATOM
1035
N
ASP
A
105
149.298
41.346
8.771
1.00
41.99

ATOM
1037
CA
ASP
A
105
147.874
41.227
8.475
1.00
41.67

ATOM
1038
CB
ASP
A
105
147.352
42.455
7.724
1.00
43.33

ATOM
1039
CG
ASP
A
105
146.986
43.602
8.648
1.00
46.56

ATOM
1040
OD1
ASP
A
105
146.898
43.395
9.876
1.00
49.37

ATOM
1041
OD2
ASP
A
105
146.770
44.720
8.141
1.00
51.38

ATOM
1042
C
ASP
A
105
147.658
39.985
7.622
1.00
41.95

ATOM
1043
O
ASP
A
105
148.470
39.655
6.758
1.00
42.85

ATOM
1044
N
LEU
A
106
146.538
39.322
7.841
1.00
40.99

ATOM
1046
CA
LEU
A
106
146.220
38.115
7.115
1.00
39.85

ATOM
1047
CB
LEU
A
106
146.424
36.934
8.058
1.00
38.87

ATOM
1048
CG
LEU
A
106
146.224
35.489
7.629
1.00
39.36

ATOM
1049
CD1
LEU
A
106
146.825
34.605
8.690
1.00
40.16

ATOM
1050
CD2
LEU
A
106
144.758
35.175
7.464
1.00
41.07

ATOM
1051
C
LEU
A
106
144.767
38.248
6.698
1.00
40.07

ATOM
1052
O
LEU
A
106
143.968
38.841
7.414
1.00
41.85

ATOM
1053
N
SER
A
107
144.427
37.748
5.523
1.00
41.19

ATOM
1055
CA
SER
A
107
143.054
37.830
5.061
1.00
43.48

ATOM
1056
CB
SER
A
107
142.911
38.907
3.979
1.00
45.09

ATOM
1057
OG
SER
A
107
143.440
40.155
4.402
1.00
50.35

ATOM
1059
C
SER
A
107
142.633
36.484
4.502
1.00
43.83

ATOM
1060
O
SER
A
107
143.290
35.957
3.610
1.00
44.06

ATOM
1061
N
ILE
A
108
141.587
35.900
5.077
1.00
45.70

ATOM
1063
CA
ILE
A
108
141.056
34.617
4.615
1.00
47.58

ATOM
1064
CB
ILE
A
108
140.829
33.644
5.789
1.00
46.97

ATOM
1065
CG2
ILE
A
108
140.174
32.368
5.296
1.00
46.17

ATOM
1066
CG1
ILE
A
108
142.157
33.327
6.474
1.00
47.60

ATOM
1067
CD1
ILE
A
108
142.042
32.368
7.637
1.00
49.72

ATOM
1068
C
ILE
A
108
139.716
34.922
3.959
1.00
48.97

ATOM
1069
O
ILE
A
108
138.818
35.433
4.619
1.00
51.76

ATOM
1070
N
GLU
A
109
139.582
34.652
2.664
1.00
50.18

ATOM
1072
CA
GLU
A
109
138.328
34.938
1.968
1.00
52.80

ATOM
1073
CB
GLU
A
109
138.506
36.067
0.956
1.00
58.29

ATOM
1074
CG
GLU
A
109
138.871
37.409
1.556
1.00
67.61

ATOM
1075
CD
GLU
A
109
138.896
38.510
0.518
1.00
72.52

ATOM
1076
OE1
GLU
A
109
139.591
38.345
−0.510
1.00
76.73

ATOM
1077
OE2
GLU
A
109
138.212
39.536
0.725
1.00
74.66

ATOM
1078
C
GLU
A
109
137.771
33.733
1.244
1.00
51.51

ATOM
1079
O
GLU
A
109
138.449
32.717
1.091
1.00
51.13

ATOM
1080
N
GLY
A
110
136.539
33.867
0.767
1.00
50.94

ATOM
1082
CA
GLY
A
110
135.904
32.778
0.051
1.00
49.27

ATOM
1083
C
GLY
A
110
135.714
31.551
0.920
1.00
48.08

ATOM
1084
O
GLY
A
110
135.972
30.419
0.488
1.00
47.03

ATOM
1085
N
MET
A
111
135.318
31.784
2.168
1.00
46.98

ATOM
1087
CA
MET
A
111
135.078
30.699
3.104
1.00
44.78

ATOM
1088
CB
MET
A
111
135.376
31.143
4.536
1.00
44.81

ATOM
1089
CG
MET
A
111
135.062
30.092
5.570
1.00
44.07

ATOM
1090
SD
MET
A
111
135.669
30.518
7.178
1.00
49.80

ATOM
1091
CE
MET
A
111
136.833
29.192
7.434
1.00
46.06

ATOM
1092
C
MET
A
111
133.630
30.242
2.970
1.00
42.64

ATOM
1093
O
MET
A
111
132.712
31.061
2.960
1.00
40.20

ATOM
1094
N
SER
A
112
133.446
28.935
2.846
1.00
41.52

ATOM
1096
CA
SER
A
112
132.133
28.334
2.708
1.00
41.82

ATOM
1097
CB
SER
A
112
132.045
27.607
1.360
1.00
43.85

ATOM
1098
OG
SER
A
112
130.997
26.648
1.321
1.00
49.86

ATOM
1100
C
SER
A
112
131.908
27.363
3.861
1.00
41.93

ATOM
1101
O
SER
A
112
132.725
26.467
4.097
1.00
41.84

ATOM
1102
N
ILE
A
113
130.816
27.569
4.592
1.00
42.07

ATOM
1104
CA
ILE
A
113
130.444
26.722
5.725
1.00
40.13

ATOM
1105
CB
ILE
A
113
130.310
27.546
7.027
1.00
39.38

ATOM
1106
CG2
ILE
A
113
130.227
26.620
8.231
1.00
39.63

ATOM
1107
CG1
ILE
A
113
131.505
28.480
7.190
1.00
35.78

ATOM
1108
CD1
ILE
A
113
131.284
29.547
8.225
1.00
38.78

ATOM
1109
C
ILE
A
113
129.083
26.105
5.405
1.00
40.48

ATOM
1110
O
ILE
A
113
128.118
26.821
5.117
1.00
40.10

ATOM
1111
N
SER
A
114
129.016
24.780
5.414
1.00
40.69

ATOM
1113
CA
SER
A
114
127.775
24.076
5.126
1.00
39.86

ATOM
1114
CB
SER
A
114
127.915
23.277
3.835
1.00
39.27

ATOM
1115
OG
SER
A
114
126.695
22.645
3.486
1.00
45.23

ATOM
1117
C
SER
A
114
127.489
23.152
6.297
1.00
40.43

ATOM
1118
O
SER
A
114
128.370
22.407
6.730
1.00
42.01

ATOM
1119
N
ALA
A
115
126.261
23.198
6.804
1.00
40.94

ATOM
1121
CA
ALA
A
115
125.863
22.380
7.947
1.00
40.28

ATOM
1122
CB
ALA
A
115
125.990
23.186
9.227
1.00
41.97

ATOM
1123
C
ALA
A
115
124.446
21.856
7.814
1.00
39.55

ATOM
1124
O
ALA
A
115
123.551
22.581
7.385
1.00
38.65

ATOM
1125
N
ASP
A
116
124.248
20.603
8.213
1.00
39.92

ATOM
1127
CA
ASP
A
116
122.943
19.954
8.155
1.00
40.51

ATOM
1128
CB
ASP
A
116
123.092
18.513
7.672
1.00
44.07

ATOM
1129
CG
ASP
A
116
123.359
18.421
6.184
1.00
48.91

ATOM
1130
OD1
ASP
A
116
124.455
18.829
5.741
1.00
53.18

ATOM
1131
OD2
ASP
A
116
122.467
17.940
5.455
1.00
52.27

ATOM
1132
C
ASP
A
116
122.241
19.956
9.504
1.00
39.36

ATOM
1133
O
ASP
A
116
122.804
19.501
10.495
1.00
40.86

ATOM
1134
N
LEU
A
117
121.009
20.459
9.537
1.00
38.66

ATOM
1136
CA
LEU
A
117
120.220
20.508
10.766
1.00
35.83

ATOM
1137
CB
LEU
A
117
119.578
21.888
10.944
1.00
34.68

ATOM
1138
CG
LEU
A
117
120.493
23.096
11.140
1.00
34.59

ATOM
1139
CD1
LEU
A
117
119.667
24.361
11.279
1.00
35.67

ATOM
1140
CD2
LEU
A
117
121.346
22.895
12.370
1.00
35.88

ATOM
1141
C
LEU
A
117
119.131
19.437
10.721
1.00
35.13

ATOM
1142
O
LEU
A
117
118.287
19.435
9.824
1.00
35.15

ATOM
1143
N
LYS
A
118
119.155
18.531
11.691
1.00
35.41

ATOM
1145
CA
LYS
A
118
118.180
17.450
11.776
1.00
34.03

ATOM
1146
CB
LYS
A
118
118.896
16.128
12.047
1.00
36.61

ATOM
1147
CG
LYS
A
118
118.027
14.904
11.907
1.00
41.84

ATOM
1148
CD
LYS
A
118
118.870
13.640
11.890
1.00
45.83

ATOM
1149
CE
LYS
A
118
117.998
12.400
11.773
1.00
49.70

ATOM
1150
NZ
LYS
A
118
117.098
12.434
10.576
1.00
52.85

ATOM
1154
C
LYS
A
118
117.184
17.760
12.884
1.00
32.08

ATOM
1155
O
LYS
A
118
117.572
18.045
14.014
1.00
30.72

ATOM
1156
N
LEU
A
119
115.900
17.737
12.545
1.00
34.05

ATOM
1158
CA
LEU
A
119
114.838
18.036
13.503
1.00
33.03

ATOM
1159
CB
LEU
A
119
113.782
18.917
12.844
1.00
30.64

ATOM
1160
CG
LEU
A
119
114.277
20.278
12.372
1.00
26.32

ATOM
1161
CD1
LEU
A
119
113.434
20.751
11.229
1.00
27.43

ATOM
1162
CD2
LEU
A
119
114.230
21.258
13.511
1.00
29.44

ATOM
1163
C
LEU
A
119
114.192
16.771
14.065
1.00
33.62

ATOM
1164
O
LEU
A
119
113.904
15.819
13.334
1.00
32.69

ATOM
1165
N
GLY
A
120
113.952
16.776
15.368
1.00
33.78

ATOM
1167
CA
GLY
A
120
113.353
15.624
16.000
1.00
33.21

ATOM
1168
C
GLY
A
120
112.431
16.059
17.109
1.00
34.60

ATOM
1169
O
GLY
A
120
112.238
17.250
17.340
1.00
34.75

ATOM
1170
N
SER
A
121
111.883
15.086
17.817
1.00
37.06

ATOM
1172
CA
SER
A
121
110.961
15.355
18.902
1.00
40.83

ATOM
1173
CB
SER
A
121
109.541
14.982
18.464
1.00
41.68

ATOM
1174
OG
SER
A
121
108.638
14.924
19.554
1.00
44.95

ATOM
1176
C
SER
A
121
111.357
14.527
20.108
1.00
43.32

ATOM
1177
O
SER
A
121
111.990
13.476
19.975
1.00
44.77

ATOM
1178
N
ASN
A
122
111.034
15.038
21.287
1.00
45.49

ATOM
1180
CA
ASN
A
122
111.308
14.330
22.525
1.00
48.51

ATOM
1181
CB
ASN
A
122
112.014
15.244
23.523
1.00
47.83

ATOM
1182
CG
ASN
A
122
112.693
14.474
24.633
1.00
49.31

ATOM
1183
OD1
ASN
A
122
112.445
13.283
24.827
1.00
48.55

ATOM
1184
ND2
ASN
A
122
113.574
15.146
25.359
1.00
52.06

ATOM
1187
C
ASN
A
122
109.925
13.955
23.040
1.00
50.18

ATOM
1188
O
ASN
A
122
109.197
14.810
23.534
1.00
51.08

ATOM
1189
N
PRO
A
123
109.530
12.678
22.895
1.00
51.66

ATOM
1190
CD
PRO
A
123
110.378
11.593
22.375
1.00
51.97

ATOM
1191
CA
PRO
A
123
108.229
12.152
23.323
1.00
51.81

ATOM
1192
CB
PRO
A
123
108.291
10.696
22.875
1.00
52.33

ATOM
1193
CG
PRO
A
123
109.744
10.377
22.996
1.00
52.53

ATOM
1194
C
PRO
A
123
107.903
12.255
24.808
1.00
52.83

ATOM
1195
O
PRO
A
123
106.777
12.593
25.171
1.00
54.24

ATOM
1196
N
THR
A
124
108.879
11.969
25.664
1.00
53.70

ATOM
1198
CA
THR
A
124
108.658
12.016
27.109
1.00
55.10

ATOM
1199
CB
THR
A
124
109.782
11.285
27.873
1.00
55.63

ATOM
1200
OG1
THR
A
124
111.038
11.556
27.244
1.00
57.26

ATOM
1202
CG2
THR
A
124
109.536
9.782
27.879
1.00
57.40

ATOM
1203
C
THR
A
124
108.467
13.418
27.687
1.00
54.39

ATOM
1204
O
THR
A
124
108.031
13.568
28.833
1.00
56.00

ATOM
1205
N
SER
A
125
108.794
14.439
26.901
1.00
52.41

ATOM
1207
CA
SER
A
125
108.647
15.824
27.345
1.00
49.57

ATOM
1208
CB
SER
A
125
110.023
16.448
27.598
1.00
49.34

ATOM
1209
OG
SER
A
125
110.859
16.328
26.459
1.00
50.88

ATOM
1211
C
SER
A
125
107.855
16.676
26.355
1.00
46.68

ATOM
1212
O
SER
A
125
107.366
17.747
26.702
1.00
46.69

ATOM
1213
N
GLY
A
126
107.734
16.191
25.123
1.00
44.84

ATOM
1215
CA
GLY
A
126
107.008
16.906
24.091
1.00
42.00

ATOM
1216
C
GLY
A
126
107.739
18.113
23.537
1.00
40.90

ATOM
1217
O
GLY
A
126
107.125
18.953
22.885
1.00
41.68

ATOM
1218
N
LYS
A
127
109.044
18.201
23.780
1.00
40.27

ATOM
1220
CA
LYS
A
127
109.846
19.330
23.303
1.00
38.06

ATOM
1221
CB
LYS
A
127
110.914
19.708
24.340
1.00
41.48

ATOM
1222
CG
LYS
A
127
110.408
20.194
25.705
1.00
44.59

ATOM
1223
CD
LYS
A
127
109.966
21.657
25.697
1.00
48.40

ATOM
1224
CE
LYS
A
127
109.668
22.142
27.118
1.00
49.68

ATOM
1225
NZ
LYS
A
127
109.045
23.498
27.151
1.00
50.76

ATOM
1229
C
LYS
A
127
110.533
18.984
21.980
1.00
36.38

ATOM
1230
O
LYS
A
127
110.916
17.827
21.751
1.00
36.93

ATOM
1231
N
PRO
A
128
110.705
19.980
21.093
1.00
33.49

ATOM
1232
CD
PRO
A
128
110.310
21.395
21.226
1.00
31.99

ATOM
1233
CA
PRO
A
128
111.354
19.747
19.803
1.00
31.41

ATOM
1234
CB
PRO
A
128
111.023
21.020
19.037
1.00
31.27

ATOM
1235
CG
PRO
A
128
111.085
22.056
20.109
1.00
29.23

ATOM
1236
C
PRO
A
128
112.853
19.611
20.007
1.00
31.58

ATOM
1237
O
PRO
A
128
113.389
20.080
21.010
1.00
31.45

ATOM
1238
N
THR
A
129
113.523
18.936
19.087
1.00
31.21

ATOM
1240
CA
THR
A
129
114.960
18.779
19.181
1.00
30.79

ATOM
1241
CB
THR
A
129
115.377
17.332
19.510
1.00
29.38

ATOM
1242
OG1
THR
A
129
114.952
16.451
18.467
1.00
30.58

ATOM
1244
CG2
THR
A
129
114.773
16.886
20.818
1.00
27.50

ATOM
1245
C
THR
A
129
115.568
19.185
17.856
1.00
32.76

ATOM
1246
O
THR
A
129
114.907
19.148
16.813
1.00
32.88

ATOM
1247
N
ILE
A
130
116.828
19.582
17.904
1.00
35.82

ATOM
1249
CA
ILE
A
130
117.554
19.999
16.717
1.00
37.64

ATOM
1250
CB
ILE
A
130
117.302
21.506
16.401
1.00
38.78

ATOM
1251
CG2
ILE
A
130
117.277
22.335
17.665
1.00
40.02

ATOM
1252
CG1
ILE
A
130
118.345
22.042
15.425
1.00
38.94

ATOM
1253
CD1
ILE
A
130
118.138
21.591
14.014
1.00
42.34

ATOM
1254
C
ILE
A
130
119.026
19.740
16.985
1.00
38.69

ATOM
1255
O
ILE
A
130
119.534
20.085
18.048
1.00
40.22

ATOM
1256
N
THR
A
131
119.681
19.039
16.069
1.00
39.62

ATOM
1258
CA
THR
A
131
121.098
18.748
16.217
1.00
40.39

ATOM
1259
CB
THR
A
131
121.351
17.318
16.747
1.00
40.39

ATOM
1260
OG1
THR
A
131
120.833
16.354
15.825
1.00
40.07

ATOM
1262
CG2
THR
A
131
120.696
17.124
18.113
1.00
43.21

ATOM
1263
C
THR
A
131
121.788
18.927
14.878
1.00
41.17

ATOM
1264
O
THR
A
131
121.139
18.951
13.839
1.00
41.86

ATOM
1265
N
CYS
A
132
123.099
19.107
14.911
1.00
42.72

ATOM
1267
CA
CYS
A
132
123.875
19.284
13.696
1.00
42.81

ATOM
1268
CB
CYS
A
132
124.963
20.326
13.932
1.00
42.56

ATOM
1269
SG
CYS
A
132
126.009
20.629
12.530
1.00
38.05

ATOM
1270
C
CYS
A
132
124.494
17.940
13.333
1.00
44.48

ATOM
1271
O
CYS
A
132
125.370
17.446
14.041
1.00
46.08

ATOM
1272
N
SER
A
133
124.019
17.344
12.244
1.00
45.05

ATOM
1274
CA
SER
A
133
124.508
16.045
11.794
1.00
45.93

ATOM
1275
CB
SER
A
133
123.410
15.315
11.015
1.00
47.62

ATOM
1276
OG
SER
A
133
122.962
16.082
9.908
1.00
51.90

ATOM
1278
C
SER
A
133
125.793
16.072
10.966
1.00
45.39

ATOM
1279
O
SER
A
133
126.512
15.078
10.916
1.00
46.00

ATOM
1280
N
SER
A
134
126.056
17.182
10.282
1.00
45.72

ATOM
1282
CA
SER
A
134
127.257
17.322
9.453
1.00
45.69

ATOM
1283
CB
SER
A
134
127.048
16.672
8.073
1.00
47.17

ATOM
1284
OG
SER
A
134
127.221
15.263
8.110
1.00
50.20

ATOM
1286
C
SER
A
134
127.642
18.788
9.265
1.00
44.02

ATOM
1287
O
SER
A
134
126.775
19.663
9.212
1.00
45.04

ATOM
1288
N
CYS
A
135
128.939
19.047
9.145
1.00
42.35

ATOM
1290
CA
CYS
A
135
129.442
20.398
8.941
1.00
40.67

ATOM
1291
C
CYS
A
135
130.728
20.345
8.144
1.00
41.67

ATOM
1292
O
CYS
A
135
131.469
19.361
8.216
1.00
40.71

ATOM
1293
CB
CYS
A
135
129.718
21.084
10.274
1.00
39.61

ATOM
1294
SG
CYS
A
135
130.296
22.800
10.094
1.00
34.66

ATOM
1295
N
SER
A
136
130.975
21.383
7.354
1.00
43.65

ATOM
1297
CA
SER
A
136
132.192
21.451
6.562
1.00
45.71

ATOM
1298
CB
SER
A
136
132.131
20.504
5.357
1.00
48.55

ATOM
1299
OG
SER
A
136
131.231
20.961
4.363
1.00
54.17

ATOM
1301
C
SER
A
136
132.465
22.874
6.114
1.00
45.23

ATOM
1302
O
SER
A
136
131.582
23.551
5.583
1.00
44.66

ATOM
1303
N
SER
A
137
133.673
23.339
6.411
1.00
45.29

ATOM
1305
CA
SER
A
137
134.110
24.671
6.040
1.00
45.90

ATOM
1306
CB
SER
A
137
134.896
25.302
7.186
1.00
45.32

ATOM
1307
OG
SER
A
137
135.302
26.620
6.867
1.00
46.54

ATOM
1309
C
SER
A
137
134.990
24.514
4.806
1.00
47.49

ATOM
1310
O
SER
A
137
135.330
23.392
4.416
1.00
48.14

ATOM
1311
N
HIS
A
138
135.371
25.630
4.200
1.00
48.87

ATOM
1313
CA
HIS
A
138
136.196
25.599
3.003
1.00
49.64

ATOM
1314
CB
HIS
A
138
135.338
25.149
1.811
1.00
53.41

ATOM
1315
CG
HIS
A
138
136.097
24.992
0.529
1.00
56.80

ATOM
1316
CD2
HIS
A
138
136.712
23.915
−0.016
1.00
58.14

ATOM
1317
ND1
HIS
A
138
136.268
26.025
−0.368
1.00
59.15

ATOM
1319
CE1
HIS
A
138
136.956
25.592
−1.412
1.00
59.11

ATOM
1320
NE2
HIS
A
138
137.238
24.316
−1.222
1.00
59.30

ATOM
1322
C
HIS
A
138
136.779
26.983
2.742
1.00
49.79

ATOM
1323
O
HIS
A
138
136.042
27.938
2.510
1.00
49.66

ATOM
1324
N
ILE
A
139
138.102
27.082
2.808
1.00
50.32

ATOM
1326
CA
ILE
A
139
138.822
28.330
2.565
1.00
50.43

ATOM
1327
CB
ILE
A
139
139.937
28.519
3.606
1.00
50.04

ATOM
1328
CG2
ILE
A
139
140.876
29.651
3.195
1.00
46.81

ATOM
1329
CG1
ILE
A
139
139.313
28.751
4.982
1.00
49.41

ATOM
1330
CD1
ILE
A
139
140.310
28.816
6.105
1.00
53.48

ATOM
1331
C
ILE
A
139
139.430
28.312
1.159
1.00
51.98

ATOM
1332
O
ILE
A
139
140.019
27.311
0.743
1.00
51.75

ATOM
1333
N
ASN
A
140
139.267
29.409
0.425
1.00
53.16

ATOM
1335
CA
ASN
A
140
139.792
29.503
−0.935
1.00
54.65

ATOM
1336
CB
ASN
A
140
138.824
30.291
−1.832
1.00
57.65

ATOM
1337
CG
ASN
A
140
139.311
30.400
−3.276
1.00
60.64

ATOM
1338
OD1
ASN
A
140
139.295
31.483
−3.867
1.00
61.18

ATOM
1339
ND2
ASN
A
140
139.742
29.279
−3.848
1.00
62.27

ATOM
1342
C
ASN
A
140
141.203
30.092
−1.024
1.00
53.67

ATOM
1343
O
ASN
A
140
142.097
29.463
−1.589
1.00
53.36

ATOM
1344
N
SER
A
141
141.401
31.289
−0.474
1.00
52.97

ATOM
1346
CA
SER
A
141
142.711
31.943
−0.518
1.00
52.86

ATOM
1347
CB
SER
A
141
142.728
33.051
−1.585
1.00
52.81

ATOM
1348
OG
SER
A
141
141.928
34.167
−1.218
1.00
50.44

ATOM
1350
C
SER
A
141
143.114
32.526
0.832
1.00
52.49

ATOM
1351
O
SER
A
141
142.263
32.778
1.684
1.00
54.02

atom
1352
N
VAL
A
142
144.415
32.724
1.023
1.00
52.25

ATOM
1354
CA
VAL
A
142
144.947
33.290
2.256
1.00
50.52

ATOM
1355
CB
VAL
A
142
145.583
32.203
3.152
1.00
49.93

ATOM
1356
CG1
VAL
A
142
146.214
32.826
4.380
1.00
49.68

ATOM
1357
CG2
VAL
A
142
144.533
31.197
3.577
1.00
50.61

ATOM
1358
C
VAL
A
142
145.990
34.335
1.880
1.00
51.54

ATOM
1359
O
VAL
A
142
147.083
34.000
1.418
1.00
50.89

ATOM
1360
N
HIS
A
143
145.611
35.603
2.021
1.00
54.44

ATOM
1362
CA
HIS
A
143
146.470
36.742
1.709
1.00
57.63

ATOM
1363
CB
HIS
A
143
145.639
37.904
1.154
1.00
60.05

ATOM
1364
CG
HIS
A
143
145.323
37.789
−0.306
1.00
65.61

ATOM
1365
CD2
HIS
A
143
145.600
38.615
−1.343
1.00
67.19

ATOM
1366
ND1
HIS
A
143
144.632
36.722
−0.841
1.00
67.65

ATOM
1368
CE1
HIS
A
143
144.498
36.896
−2.145
1.00
68.08

ATOM
1369
NE2
HIS
A
143
145.078
38.037
−2.473
1.00
67.35

ATOM
1371
C
HIS
A
143
147.229
37.232
2.936
1.00
58.93

ATOM
1372
O
HIS
A
143
146.663
37.914
3.791
1.00
58.93

ATOM
1373
N
VAL
A
144
148.510
36.893
3.012
1.00
60.40

ATOM
1375
CA
VAL
A
144
149.347
37.316
4.124
1.00
62.35

ATOM
1376
CB
VAL
A
144
150.423
36.270
4.441
1.00
61.34

ATOM
1377
CG1
VAL
A
144
151.245
36.703
5.641
1.00
62.08

ATOM
1378
CG2
VAL
A
144
149.771
34.938
4.709
1.00
62.01

ATOM
1379
C
VAL
A
144
150.000
38.632
3.724
1.00
64.53

ATOM
1380
O
VAL
A
144
150.971
38.658
2.971
1.00
64.35

ATOM
1381
N
HIS
A
145
149.440
39.729
4.214
1.00
67.48

ATOM
1383
CA
HIS
A
145
149.945
41.050
3.886
1.00
71.08

ATOM
1384
CB
HIS
A
145
148.791
42.045
3.771
1.00
72.13

ATOM
1385
CG
HIS
A
145
147.860
41.751
2.642
1.00
74.06

ATOM
1386
CD2
HIS
A
145
148.098
41.536
1.327
1.00
74.26

ATOM
1387
ND1
HIS
A
145
146.497
41.640
2.810
1.00
75.07

ATOM
1389
CE1
HIS
A
145
145.934
41.370
1.646
1.00
75.64

ATOM
1390
NE2
HIS
A
145
146.884
41.303
0.730
1.00
75.46

ATOM
1392
C
HIS
A
145
150.998
41.600
4.830
1.00
73.50

ATOM
1393
O
HIS
A
145
150.742
42.560
5.553
1.00
74.03

ATOM
1394
N
ILE
A
146
152.184
40.999
4.826
1.00
76.22

ATOM
1396
CA
ILE
A
146
153.277
41.497
5.660
1.00
78.65

ATOM
1397
CB
ILE
A
146
154.282
40.374
6.055
1.00
77.20

ATOM
1398
CG2
ILE
A
146
155.320
40.905
7.037
1.00
75.80

ATOM
1399
CG1
ILE
A
146
153.545
39.214
6.729
1.00
76.58

ATOM
1400
CD1
ILE
A
146
154.451
38.091
7.184
1.00
75.69

ATOM
1401
C
ILE
A
146
153.972
42.574
4.815
1.00
81.85

ATOM
1402
O
ILE
A
146
155.107
42.970
5.082
1.00
81.33

ATOM
1403
N
SER
A
147
153.273
43.023
3.774
1.00
85.84

ATOM
1405
CA
SER
A
147
153.758
44.049
2.864
1.00
89.73

ATOM
1406
CB
SER
A
147
152.736
44.267
1.737
1.00
89.11

ATOM
1407
OG
SER
A
147
152.396
43.046
1.097
1.00
89.21

ATOM
1409
C
SER
A
147
153.983
45.354
3.637
1.00
92.25

ATOM
1410
O
SER
A
147
153.080
46.188
3.753
1.00
94.01

ATOM
1411
N
ALA
A
148
155.182
45.494
4.197
1.00
92.99

ATOM
1413
CA
ALA
A
148
155.568
46.675
4.967
1.00
92.04

ATOM
1414
CB
ALA
A
148
155.027
46.577
6.395
1.00
92.57

ATOM
1415
C
ALA
A
148
157.092
46.778
4.982
1.00
91.03

ATOM
1416
O
ALA
A
148
157.657
47.869
5.086
1.00
92.24

ATOM
1417
N
ALA
A
149
157.749
45.628
4.875
1.00
88.25

ATOM
1419
CA
ALA
A
149
159.201
45.558
4.864
1.00
85.00

ATOM
1420
CB
ALA
A
149
159.720
45.237
6.263
1.00
85.37

ATOM
1421
C
ALA
A
149
159.624
44.474
3.874
1.00
82.20

ATOM
1422
O
ALA
A
149
158.888
43.508
3.650
1.00
83.34

ATOM
1423
N
SER
A
150
160.785
44.657
3.252
1.00
77.07

ATOM
1425
CA
SER
A
150
161.304
43.690
2.293
1.00
71.37

ATOM
1426
CB
SER
A
150
162.463
44.313
1.509
1.00
72.17

ATOM
1427
OG
SER
A
150
162.092
45.574
0.968
1.00
72.35

ATOM
1429
C
SER
A
150
161.768
42.434
3.037
1.00
66.95

ATOM
1430
O
SER
A
150
162.927
42.330
3.440
1.00
66.96

ATOM
1431
N
VAL
A
151
160.847
41.496
3.240
1.00
60.88

ATOM
1433
CA
VAL
A
151
161.146
40.257
3.949
1.00
54.82

ATOM
1434
CB
VAL
A
151
160.736
40.381
5.446
1.00
55.79

ATOM
1435
CG1
VAL
A
151
159.233
40.593
5.584
1.00
55.13

ATOM
1436
CG2
VAL
A
151
161.206
39.176
6.242
1.00
55.16

ATOM
1437
C
VAL
A
151
160.417
39.104
3.259
1.00
51.49

ATOM
1438
O
VAL
A
151
159.721
38.308
3.887
1.00
51.42

ATOM
1439
N
GLY
A
152
160.639
38.992
1.957
1.00
48.87

ATOM
1441
CA
GLY
A
152
159.994
37.961
1.167
1.00
45.39

ATOM
1442
C
GLY
A
152
160.100
36.531
1.656
1.00
42.87

ATOM
1443
O
GLY
A
152
159.144
35.766
1.543
1.00
43.01

ATOM
1444
N
TRP
A
153
161.245
36.160
2.211
1.00
41.58

ATOM
1446
CA
TRP
A
153
161.432
34.795
2.682
1.00
41.92

ATOM
1447
CB
TRP
A
153
162.853
34.591
3.196
1.00
42.78

ATOM
1448
CG
TRP
A
153
163.153
35.267
4.501
1.00
43.10

ATOM
1449
CD2
TRP
A
153
163.738
36.559
4.678
1.00
43.00

ATOM
1450
CE2
TRP
A
153
163.953
36.738
6.064
1.00
43.32

ATOM
1451
CE3
TRP
A
153
164.112
37.583
3.796
1.00
45.47

ATOM
1452
CD1
TRP
A
153
163.022
34.730
5.760
1.00
42.27

ATOM
1453
NE1
TRP
A
153
163.508
35.607
6.700
1.00
42.43

ATOM
1455
CZ2
TRP
A
153
164.528
37.897
6.587
1.00
44.70

ATOM
1456
CZ3
TRP
A
153
164.686
38.738
4.317
1.00
47.45

ATOM
1457
CH2
TRP
A
153
164.889
38.885
5.701
1.00
47.30

ATOM
1458
C
TRP
A
153
160.442
34.393
3.763
1.00
41.11

ATOM
1459
O
TRP
A
153
160.053
33.236
3.852
1.00
41.06

ATOM
1460
N
LEU
A
154
160.045
35.357
4.585
1.00
40.39

ATOM
1462
CA
LEU
A
154
159.109
35.103
5.669
1.00
38.88

ATOM
1463
CB
LEU
A
154
159.080
36.284
6.618
1.00
37.14

ATOM
1464
CG
LEU
A
154
158.607
35.931
8.011
1.00
35.27

ATOM
1465
CD1
LEU
A
154
159.491
34.860
8.602
1.00
35.45

ATOM
1466
CD2
LEU
A
154
158.655
37.166
8.838
1.00
37.10

ATOM
1467
C
LEU
A
154
157.721
34.847
5.115
1.00
38.87

ATOM
1468
O
LEU
A
154
156.997
33.985
5.611
1.00
39.93

ATOM
1469
N
ILE
A
155
157.357
35.596
4.079
1.00
40.01

ATOM
1471
CA
ILE
A
155
156.062
35.435
3.430
1.00
40.45

ATOM
1472
CB
ILE
A
155
155.765
36.579
2.454
1.00
39.45

ATOM
1473
CG2
ILE
A
155
154.467
36.307
1.721
1.00
39.70

ATOM
1474
CG1
ILE
A
155
155.679
37.906
3.215
1.00
39.53

ATOM
1475
CD1
ILE
A
155
155.426
39.114
2.337
1.00
39.05

ATOM
1476
C
ILE
A
155
156.048
34.106
2.686
1.00
42.61

ATOM
1477
O
ILE
A
155
155.015
33.435
2.619
1.00
44.53

ATOM
1478
N
GLN
A
156
157.187
33.745
2.100
1.00
43.49

ATOM
1480
CA
GLN
A
156
157.323
32.475
1.398
1.00
44.17

ATOM
1481
CB
GLN
A
156
158.708
32.368
0.760
1.00
48.67

ATOM
1482
CG
GLN
A
156
159.097
30.954
0.310
1.00
55.67

ATOM
1483
CD
GLN
A
156
160.369
30.440
0.988
1.00
59.91

ATOM
1484
OE1
GLN
A
156
160.673
30.802
2.125
1.00
61.96

ATOM
1485
NE2
GLN
A
156
161.114
29.593
0.285
1.00
60.94

ATOM
1488
C
GLN
A
156
157.163
31.384
2.452
1.00
43.64

ATOM
1489
O
GLN
A
156
156.445
30.408
2.249
1.00
43.84

ATOM
1490
N
LEU
A
157
157.834
31.581
3.585
1.00
43.44

ATOM
1492
CA
LEU
A
157
157.794
30.653
4.704
1.00
41.27

ATOM
1493
CB
LEU
A
157
158.644
31.175
5.866
1.00
42.44

ATOM
1494
CG
LEU
A
157
160.152
30.930
5.797
1.00
42.39

ATOM
1495
CD1
LEU
A
157
160.873
31.722
6.876
1.00
41.73

ATOM
1496
CD2
LEU
A
157
160.426
29.447
5.948
1.00
42.15

ATOM
1497
C
LEU
A
157
156.372
30.423
5.173
1.00
40.27

ATOM
1498
O
LEU
A
157
155.948
29.280
5.328
1.00
41.05

ATOM
1499
N
PHE
A
158
155.620
31.497
5.378
1.00
39.18

ATOM
1501
CA
PHE
A
158
154.246
31.341
5.821
1.00
41.38

ATOM
1502
CB
PHE
A
158
153.519
32.684
5.927
1.00
40.94

ATOM
1503
CG
PHE
A
158
152.145
32.570
6.537
1.00
43.98

ATOM
1504
CD1
PHE
A
158
151.068
32.087
5.788
1.00
44.07

ATOM
1505
CD2
PHE
A
158
151.939
32.886
7.878
1.00
43.45

ATOM
1506
CE1
PHE
A
158
149.814
31.915
6.367
1.00
42.96

ATOM
1507
CE2
PHE
A
158
150.690
32.718
8.465
1.00
41.63

ATOM
1508
CZ
PHE
A
158
149.626
32.231
7.707
1.00
43.20

ATOM
1509
C
PHE
A
158
153.472
30.409
4.893
1.00
42.96

ATOM
1510
O
PHE
A
158
152.862
29.443
5.350
1.00
44.53

ATOM
1511
N
HIS
A
159
153.513
30.682
3.594
1.00
45.12

ATOM
1513
CA
HIS
A
159
152.790
29.860
2.624
1.00
46.02

ATOM
1514
CB
HIS
A
159
152.808
30.507
1.230
1.00
45.21

ATOM
1515
CG
HIS
A
159
152.049
31.796
1.145
1.00
44.03

ATOM
1516
CD2
HIS
A
159
152.477
33.081
1.099
1.00
44.13

ATOM
1517
ND1
HIS
A
159
150.674
31.851
1.087
1.00
44.17

ATOM
1519
CE1
HIS
A
159
150.285
33.111
1.012
1.00
45.07

ATOM
1520
NE2
HIS
A
159
151.360
33.878
1.016
1.00
45.02

ATOM
1522
C
HIS
A
159
153.314
28.426
2.524
1.00
47.97

ATOM
1523
O
HIS
A
159
152.530
27.491
2.353
1.00
48.86

ATOM
1524
N
LYS
A
160
154.624
28.253
2.678
1.00
49.77

ATOM
1526
CA
LYS
A
160
155.246
26.935
2.562
1.00
50.79

ATOM
1527
CB
LYS
A
160
156.664
27.080
1.990
1.00
51.90

ATOM
1528
CG
LYS
A
160
157.285
25.768
1.539
1.00
53.77

ATOM
1529
CD
LYS
A
160
158.669
25.957
0.950
1.00
54.99

ATOM
1530
CE
LYS
A
160
159.130
24.690
0.231
1.00
57.16

ATOM
1531
NZ
LYS
A
160
158.253
24.330
−0.934
1.00
55.19

ATOM
1535
C
LYS
A
160
155.286
26.065
3.825
1.00
51.12

ATOM
1536
O
LYS
A
160
155.537
24.862
3.736
1.00
52.93

ATOM
1537
N
LYS
A
161
155.031
26.646
4.991
1.00
49.90

ATOM
1539
CA
LYS
A
161
155.086
25.873
6.229
1.00
48.78

ATOM
1540
CB
LYS
A
161
156.340
26.263
7.016
1.00
51.36

ATOM
1541
CG
LYS
A
161
157.660
25.983
6.310
1.00
55.24

ATOM
1542
CD
LYS
A
161
158.186
24.592
6.626
1.00
59.40

ATOM
1543
CE
LYS
A
161
158.484
24.443
8.114
1.00
61.04

ATOM
1544
NZ
LYS
A
161
159.015
23.095
8.464
1.00
62.60

ATOM
1548
C
LYS
A
161
153.875
26.012
7.149
1.00
47.20

ATOM
1549
O
LYS
A
161
153.460
25.042
7.787
1.00
46.35

ATOM
1550
N
ILE
A
162
153.311
27.214
7.209
1.00
46.07

ATOM
1552
CA
ILE
A
162
152.186
27.506
8.094
1.00
45.42

ATOM
1553
CB
ILE
A
162
152.421
28.854
8.806
1.00
45.05

ATOM
1554
CG2
ILE
A
162
151.211
29.251
9.646
1.00
45.73

ATOM
1555
CG1
ILE
A
162
153.679
28.764
9.670
1.00
43.35

ATOM
1556
CD1
ILE
A
162
154.015
30.042
10.353
1.00
43.37

ATOM
1557
C
ILE
A
162
150.764
27.483
7.520
1.00
45.58

ATOM
1558
O
ILE
A
162
149.849
26.960
8.157
1.00
45.52

ATOM
1559
N
GLU
A
163
150.570
28.036
6.329
1.00
46.35

ATOM
1561
CA
GLU
A
163
149.239
28.093
5.731
1.00
47.82

ATOM
1562
CB
GLU
A
153
149.310
28.624
4.302
1.00
49.25

ATOM
1563
CG
GLU
A
163
147.956
29.028
3.735
1.00
51.68

ATOM
1564
CD
GLU
A
163
147.965
29.204
2.224
1.00
52.54

ATOM
1565
OE1
GLU
A
163
149.007
29.597
1.658
1.00
53.57

ATOM
1566
OE2
GLU
A
163
146.918
28.941
1.599
1.00
53.52

ATOM
1567
C
GLU
A
163
148.470
26.775
5.746
1.00
47.94

ATOM
1568
O
GLU
A
163
147.289
26.757
6.069
1.00
49.00

ATOM
1569
N
SER
A
164
149.142
25.678
5.420
1.00
49.09

ATOM
1571
CA
SER
A
164
148.510
24.360
5.383
1.00
49.75

ATOM
1572
CB
SER
A
164
149.486
23.327
4.818
1.00
50.94

ATOM
1573
OG
SER
A
164
149.971
23.737
3.548
1.00
56.63

ATOM
1575
C
SER
A
164
147.953
23.865
6.717
1.00
49.89

ATOM
1576
O
SER
A
164
147.100
22.982
6.739
1.00
52.82

ATOM
1577
N
ALA
A
165
148.442
24.415
7.824
1.00
48.05

ATOM
1579
CA
ALA
A
165
147.978
24.017
9.151
1.00
44.58

ATOM
1580
CB
ALA
A
165
149.153
23.920
10.109
1.00
45.11

ATOM
1581
C
ALA
A
165
146.947
25.009
9.678
1.00
43.87

ATOM
1582
O
ALA
A
165
145.980
24.626
10.335
1.00
43.62

ATOM
1583
N
LEU
A
166
147.169
26.287
9.391
1.00
43.88

ATOM
1585
CA
LEU
A
166
146.267
27.349
9.812
1.00
44.57

ATOM
1586
CB
LEU
A
166
146.783
28.701
9.313
1.00
41.17

ATOM
1587
CG
LEU
A
166
145.977
29.957
9.655
1.00
39.43

ATOM
1588
CD1
LEU
A
166
146.438
30.508
10.979
1.00
40.32

ATOM
1589
CD2
LEU
A
166
146.165
31.005
8.577
1.00
39.33

ATOM
1590
C
LEU
A
166
144.870
27.094
9.246
1.00
47.80

ATOM
1591
O
LEU
A
166
143.899
27.003
9.995
1.00
50.31

ATOM
1592
N
ARG
A
167
144.777
26.946
7.927
1.00
49.83

ATOM
1594
CA
ARG
A
167
143.493
26.714
7.274
1.00
53.68

ATOM
1595
CB
ARG
A
167
143.659
26.564
5.753
1.00
54.31

ATOM
1596
CG
ARG
A
167
144.488
25.354
5.329
1.00
57.76

ATOM
1597
CD
ARG
A
167
144.282
24.966
3.869
1.00
58.03

ATOM
1598
NE
ARG
A
167
144.657
26.032
2.948
1.00
56.39

ATOM
1600
CZ
ARG
A
167
143.786
26.753
2.256
1.00
55.99

ATOM
1601
NH1
ARG
A
167
142.485
26.525
2.380
1.00
56.36

ATOM
1604
NH2
ARG
A
167
144.214
27.699
1.436
1.00
55.25

ATOM
1607
C
ARG
A
167
142.774
25.495
7.836
1.00
56.26

ATOM
1608
O
ARG
A
167
141.570
25.544
8.088
1.00
58.47

ATOM
1609
N
ASN
A
168
143.517
24.418
8.077
1.00
59.06

ATOM
1611
CA
ASN
A
168
142.924
23.188
8.596
1.00
60.42

ATOM
1612
CB
ASN
A
168
143.936
22.037
8.586
1.00
63.69

ATOM
1613
CG
ASN
A
168
143.264
20.670
8.594
1.00
69.44

ATOM
1614
OD1
ASN
A
168
142.186
20.491
8.021
1.00
73.41

ATOM
1615
ND2
ASN
A
168
143.902
19.696
9.232
1.00
71.02

ATOM
1618
C
ASN
A
168
142.358
23.378
9.995
1.00
58.54

ATOM
1619
O
ASN
A
168
141.291
22.857
10.312
1.00
59.34

ATOM
1620
N
LYS
A
169
143.059
24.138
10.826
1.00
56.61

ATOM
1622
CA
LYS
A
169
142.591
24.380
12.179
1.00
54.57

ATOM
1623
CB
LYS
A
169
143.732
24.882
13.065
1.00
56.85

ATOM
1624
CG
LYS
A
169
143.365
25.002
14.540
1.00
60.65

ATOM
1625
CD
LYS
A
169
144.599
24.927
15.425
1.00
65.37

ATOM
1626
CE
LYS
A
169
145.276
23.560
15.329
1.00
68.82

ATOM
1627
NZ
LYS
A
169
146.576
23.504
16.062
1.00
70.63

ATOM
1631
C
LYS
A
169
141.439
25.372
12.173
1.00
51.59

ATOM
1632
O
LYS
A
169
140.570
25.327
13.035
1.00
51.73

ATOM
1633
N
MET
A
170
141.426
26.264
11.192
1.00
49.16

ATOM
1635
CA
MET
A
170
140.362
27.251
11.090
1.00
47.96

ATOM
1636
CB
MET
A
170
140.733
28.340
10.087
1.00
49.44

ATOM
1637
CG
MET
A
170
139.792
29.528
10.105
1.00
52.89

ATOM
1638
SD
MET
A
170
139.730
30.289
11.734
1.00
55.23

ATOM
1639
CE
MET
A
170
141.170
31.310
11.695
1.00
55.26

ATOM
1640
C
MET
A
170
139.075
26.565
10.659
1.00
45.37

ATOM
1641
O
MET
A
170
137.989
26.892
11.139
1.00
46.51

ATOM
1642
N
ASN
A
171
139.207
25.601
9.759
1.00
42.65

ATOM
1644
CA
ASN
A
171
138.063
24.858
9.268
1.00
41.99

ATOM
1645
CB
ASN
A
171
138.448
24.034
8.039
1.00
42.92

ATOM
1646
CG
ASN
A
171
138.644
24.889
6.795
1.00
43.47

ATOM
1647
OD1
ASN
A
171
138.041
25.957
6.658
1.00
44.24

ATOM
1648
ND2
ASN
A
171
139.478
24.415
5.875
1.00
44.77

ATOM
1651
C
ASN
A
171
137.487
23.962
10.353
1.00
42.70

ATOM
1652
O
ASN
A
171
136.284
23.701
10.374
1.00
43.68

ATOM
1653
N
SER
A
172
138.341
23.502
11.263
1.00
44.20

ATOM
1655
CA
SER
A
172
137.898
22.645
12.358
1.00
45.11

ATOM
1656
CB
SER
A
172
139.069
21.841
12.935
1.00
46.36

ATOM
1657
OG
SER
A
172
140.094
22.685
13.438
1.00
49.96

ATOM
1659
C
SER
A
172
137.230
23.474
13.454
1.00
44.96

ATOM
1660
O
SER
A
172
136.204
23.069
14.005
1.00
47.71

ATOM
1661
N
GLN
A
173
137.811
24.635
13.759
1.00
43.91

ATOM
1663
CA
GLN
A
173
137.276
25.541
14.776
1.00
40.36

ATOM
1664
CB
GLN
A
173
138.214
26.730
14.990
1.00
41.61

ATOM
1665
CG
GLN
A
173
139.444
26.421
15.816
1.00
43.62

ATOM
1666
CD
GLN
A
173
139.095
25.943
17.205
1.00
46.78

ATOM
1667
OE1
GLN
A
173
138.657
26.722
18.052
1.00
50.29

ATOM
1668
NE2
GLN
A
173
139.279
24.654
17.448
1.00
48.32

ATOM
1671
C
GLN
A
173
135.893
26.047
14.386
1.00
38.81

ATOM
1672
O
GLN
A
173
134.990
26.098
15.218
1.00
38.42

ATOM
1673
N
VAL
A
174
135.734
26.423
13.120
1.00
36.59

ATOM
1675
CA
VAL
A
174
134.456
26.912
12.621
1.00
34.47

ATOM
1676
CB
VAL
A
174
134.559
27.328
11.147
1.00
32.46

ATOM
1677
CG1
VAL
A
174
133.183
27.559
10.564
1.00
32.42

ATOM
1678
CG2
VAL
A
174
135.380
28.601
11.037
1.00
31.13

ATOM
1679
C
VAL
A
174
133.363
25.861
12.810
1.00
34.32

ATOM
1680
O
VAL
A
174
132.350
26.130
13.445
1.00
36.14

ATOM
1681
N
CYS
A
175
133.586
24.652
12.308
1.00
35.02

ATOM
1683
CA
CYS
A
175
132.601
23.591
12.460
1.00
35.40

ATOM
1684
C
CYS
A
175
132.440
23.152
13.906
1.00
36.62

ATOM
1685
O
CYS
A
175
131.405
22.597
14.284
1.00
37.92

ATOM
1686
CB
CYS
A
175
132.925
22.396
11.573
1.00
33.94

ATOM
1687
SG
CYS
A
175
132.302
22.595
9.876
1.00
42.37

ATOM
1688
N
GLU
A
176
133.459
23.386
14.720
1.00
38.42

ATOM
1690
CA
GLU
A
176
133.365
23.034
16.123
1.00
40.14

ATOM
1691
CB
GLU
A
176
134.739
23.093
16.793
1.00
43.35

ATOM
1692
CG
GLU
A
176
134.747
22.502
18.193
1.00
50.93

ATOM
1693
CD
GLU
A
176
136.132
22.385
18.783
1.00
53.93

ATOM
1694
OE1
GLU
A
176
136.867
21.459
18.382
1.00
58.04

ATOM
1695
OE2
GLU
A
176
136.481
23.207
19.658
1.00
57.02

ATOM
1696
C
GLU
A
176
132.386
24.024
16.772
1.00
40.43

ATOM
1697
O
GLU
A
176
131.498
23.627
17.528
1.00
41.95

ATOM
1698
N
LYS
A
177
132.507
25.301
16.419
1.00
39.36

ATOM
1700
CA
LYS
A
177
131.625
26.332
16.956
1.00
38.66

ATOM
1701
CB
LYS
A
177
132.074
27.729
16.510
1.00
38.94

ATOM
1702
CG
LYS
A
177
133.403
28.194
17.089
1.00
40.75

ATOM
1703
CD
LYS
A
177
133.336
28.424
18.592
1.00
40.88

ATOM
1704
CE
LYS
A
177
134.694
28.852
19.152
1.00
40.13

ATOM
1705
NZ
LYS
A
177
134.688
28.995
20.637
1.00
40.04

ATOM
1709
C
LYS
A
177
130.190
26.099
16.503
1.00
37.24

ATOM
1710
O
LYS
A
177
129.277
26.078
17.318
1.00
39.39

ATOM
1711
N
VAL
A
178
130.002
25.901
15.204
1.00
35.46

ATOM
1713
CA
VAL
A
178
128.676
25.676
14.641
1.00
33.61

ATOM
1714
CB
VAL
A
178
128.747
25.442
13.124
1.00
31.21

ATOM
1715
CD1
VAL
A
178
127.365
25.166
12.568
1.00
32.70

ATOM
1716
CG2
VAL
A
178
129.346
26.652
12.446
1.00
31.16

ATOM
1717
C
VAL
A
178
127.960
24.505
15.299
1.00
34.02

ATOM
1718
O
VAL
A
178
126.844
24.656
15.784
1.00
36.09

ATOM
1719
N
THR
A
179
128.611
23.349
15.338
1.00
34.04

ATOM
1721
CA
THR
A
179
128.018
22.167
15.947
1.00
35.60

ATOM
1722
CB
THR
A
179
128.977
20.968
15.865
1.00
32.77

ATOM
1723
OG1
THR
A
179
129.372
20.775
14.505
1.00
32.73

ATOM
1725
CG2
THR
A
179
128.296
19.706
16.330
1.00
35.18

ATOM
1726
C
THR
A
179
127.634
22.428
17.408
1.00
39.92

ATOM
1727
O
THR
A
179
126.554
22.037
17.858
1.00
42.33

ATOM
1728
N
ASN
A
180
128.497
23.131
18.132
1.00
43.69

ATOM
1730
CA
ASN
A
180
128.244
23.435
19.537
1.00
44.92

ATOM
1731
CB
ASN
A
180
129.496
23.991
20.213
1.00
49.20

ATOM
1732
CG
ASN
A
180
130.522
22.920
20.532
1.00
53.34

ATOM
1733
OD1
ASN
A
180
131.550
23.213
21.140
1.00
58.92

ATOM
1734
ND2
ASN
A
180
130.258
21.680
20.126
1.00
53.15

ATOM
1737
C
ASN
A
180
127.101
24.406
19.738
1.00
44.35

ATOM
1738
O
ASN
A
180
126.252
24.194
20.593
1.00
46.90

ATOM
1739
N
SER
A
181
127.095
25.487
18.972
1.00
42.77

ATOM
1741
CA
SER
A
181
126.047
26.481
19.084
1.00
42.55

ATOM
1742
CB
SER
A
181
126.274
27.605
18.076
1.00
46.25

ATOM
1743
OG
SER
A
181
127.508
28.261
18.319
1.00
51.45

ATOM
1745
C
SER
A
181
124.686
25.841
18.869
1.00
41.46

ATOM
1746
O
SER
A
181
123.720
26.203
19.528
1.00
43.31

ATOM
1747
N
VAL
A
182
124.610
24.870
17.969
1.00
41.03

ATOM
1749
CA
VAL
A
182
123.346
24.195
17.712
1.00
40.50

ATOM
1750
CB
VAL
A
182
123.468
23.177
16.565
1.00
40.39

ATOM
1751
CG1
VAL
A
182
122.133
22.489
16.333
1.00
41.54

ATOM
1752
CG2
VAL
A
182
123.918
23.874
15.295
1.00
39.67

ATOM
1753
C
VAL
A
182
122.865
23.481
18.970
1.00
41.04

ATOM
1754
O
VAL
A
182
121.831
23.836
19.536
1.00
41.32

ATOM
1755
N
SER
A
183
123.647
22.510
19.429
1.00
42.02

ATOM
1757
CA
SER
A
183
123.311
21.735
20.616
1.00
41.82

ATOM
1758
CB
SER
A
183
124.339
20.620
20.828
1.00
42.01

ATOM
1759
OG
SER
A
183
124.180
19.588
19.867
1.00
47.44

ATOM
1761
C
SER
A
183
123.187
22.553
21.895
1.00
41.66

ATOM
1762
O
SER
A
183
122.251
22.358
22.673
1.00
43.45

ATOM
1763
N
SER
A
184
124.120
23.472
22.102
1.00
40.24

ATOM
1765
CA
SER
A
184
124.143
24.293
23.305
1.00
40.26

ATOM
1766
CB
SER
A
184
125.590
24.639
23.670
1.00
42.61

ATOM
1767
OG
SER
A
184
126.340
23.468
23.947
1.00
47.85

ATOM
1769
C
SER
A
184
123.307
25.567
23.312
1.00
39.22

ATOM
1770
O
SER
A
184
122.991
26.088
24.382
1.00
40.56

ATOM
1771
N
GLU
A
185
122.942
26.078
22.145
1.00
37.87

ATOM
1773
CA
GLU
A
185
122.169
27.313
22.098
1.00
37.71

ATOM
1774
CB
GLU
A
185
123.060
28.485
21.683
1.00
40.53

ATOM
1775
CG
GLU
A
185
124.010
28.960
22.768
1.00
45.79

ATOM
1776
CD
GLU
A
185
124.987
30.024
22.296
1.00
50.89

ATOM
1777
OE1
GLU
A
185
124.887
30.490
21.138
1.00
55.20

ATOM
1778
OE2
GLU
A
185
125.872
30.390
23.097
1.00
55.19

ATOM
1779
C
GLU
A
185
120.934
27.277
21.225
1.00
35.83

ATOM
1780
O
GLU
A
185
119.921
27.861
21.584
1.00
38.77

ATOM
1781
N
LEU
A
186
121.008
26.605
20.082
1.00
34.44

ATOM
1783
CA
LEU
A
186
119.864
26.533
19.187
1.00
33.39

ATOM
1784
CB
LEU
A
186
120.269
25.978
17.818
1.00
30.92

ATOM
1785
CG
LEU
A
186
119.709
26.645
16.553
1.00
26.02

ATOM
1786
CD1
LEU
A
186
119.228
25.581
15.601
1.00
23.97

ATOM
1787
CD2
LEU
A
186
118.581
27.619
16.867
1.00
25.38

ATOM
1788
C
LEU
A
186
118.794
25.652
19.802
1.00
34.20

ATOM
1789
O
LEU
A
186
117.655
26.083
19.963
1.00
35.35

ATOM
1790
N
GLN
A
187
119.168
24.433
20.181
1.00
35.06

ATOM
1792
CA
GLN
A
187
118.218
23.500
20.778
1.00
37.32

ATOM
1793
CB
GLN
A
187
118.856
22.130
21.031
1.00
38.08

ATOM
1794
CG
GLN
A
187
117.859
21.104
21.549
1.00
39.72

ATOM
1795
CD
GLN
A
187
118.388
19.696
21.506
1.00
39.64

ATOM
1796
OE1
GLN
A
187
118.203
18.984
20.520
1.00
42.24

ATOM
1797
NE2
GLN
A
187
119.031
19.272
22.585
1.00
43.70

ATOM
1800
C
GLN
A
187
117.548
24.041
22.041
1.00
36.63

ATOM
1801
O
GLN
A
187
116.325
24.022
22.138
1.00
40.27

ATOM
1802
N
PRO
A
188
118.333
24.493
23.038
1.00
36.32

ATOM
1803
CD
PRO
A
188
119.782
24.293
23.223
1.00
38.65

ATOM
1804
CA
PRO
A
188
117.748
25.033
24.268
1.00
35.72

ATOM
1805
CB
PRO
A
188
118.977
25.432
25.075
1.00
34.46

ATOM
1806
CG
PRO
A
188
119.933
24.364
24.730
1.00
35.29

ATOM
1807
C
PRO
A
188
116.829
26.231
24.030
1.00
36.20

ATOM
1808
O
PRO
A
188
115.933
26.490
24.835
1.00
38.62

ATOM
1809
N
TYR
A
189
117.062
26.983
22.957
1.00
35.08

ATOM
1811
CA
TYR
A
189
116.203
28.122
22.667
1.00
33.10

ATOM
1812
CB
TYR
A
189
116.799
29.059
21.625
1.00
30.49

ATOM
1813
CG
TYR
A
189
115.767
30.037
21.113
1.00
29.52

ATOM
1814
CD1
TYR
A
189
115.222
30.996
21.958
1.00
28.37

ATOM
1815
CE1
TYR
A
189
114.211
31.842
21.523
1.00
27.60

ATOM
1816
CD2
TYR
A
189
115.274
29.950
19.808
1.00
28.40

ATOM
1817
CE2
TYR
A
189
114.261
30.792
19.366
1.00
26.35

ATOM
1818
CZ
TYR
A
189
113.737
31.732
20.231
1.00
25.96

ATOM
1819
OH
TYR
A
189
112.735
32.568
19.815
1.00
27.51

ATOM
1821
C
TYR
A
189
114.841
27.660
22.186
1.00
34.73

ATOM
1822
O
TYR
A
189
113.824
28.113
22.694
1.00
38.35

ATOM
1823
N
PHE
A
190
114.811
26.771
21.197
1.00
36.21

ATOM
1825
CA
PHE
A
190
113.538
26.288
20.684
1.00
37.47

ATOM
1826
CB
PHE
A
190
113.697
25.649
19.302
1.00
38.76

ATOM
1827
CG
PHE
A
190
113.522
26.633
18.177
1.00
41.54

ATOM
1828
CD1
PHE
A
190
112.273
27.194
17.920
1.00
40.00

ATOM
1829
CD2
PHE
A
190
114.610
27.042
17.406
1.00
43.58

ATOM
1830
CE1
PHE
A
190
112.109
28.146
16.919
1.00
39.03

ATOM
1831
CE2
PHE
A
190
114.454
27.999
16.398
1.00
40.39

ATOM
1832
CZ
PHE
A
190
113.201
28.550
16.159
1.00
39.28

ATOM
1833
C
PHE
A
190
112.768
25.408
21.662
1.00
37.92

ATOM
1834
O
PHE
A
190
111.655
24.960
21.380
1.00
38.40

ATOM
1835
N
GLN
A
191
113.351
25.193
22.835
1.00
36.94

ATOM
1837
CA
GLN
A
191
112.685
24.425
23.869
1.00
36.24

ATOM
1838
CB
GLN
A
191
113.637
23.426
24.529
1.00
36.06

ATOM
1839
CG
GLN
A
191
113.987
22.259
23.609
1.00
37.66

ATOM
1840
CD
GLN
A
191
114.786
21.170
24.287
1.00
36.77

ATOM
1841
OE1
GLN
A
191
115.365
21.379
25.349
1.00
38.68

ATOM
1842
NE2
GLN
A
191
114.828
19.997
23.669
1.00
35.78

ATOM
1845
C
GLN
A
191
112.042
25.369
24.881
1.00
37.61

ATOM
1846
O
GLN
A
191
111.621
24.945
25.956
1.00
38.67

ATOM
1847
N
THR
A
192
111.992
26.659
24.541
1.00
38.44

ATOM
1849
CA
THR
A
192
111.338
27.650
25.392
1.00
37.16

ATOM
1850
CB
THR
A
192
111.946
29.055
25.263
1.00
36.82

ATOM
1851
OG1
THR
A
192
111.937
29.461
23.890
1.00
37.79

ATOM
1853
CG2
THR
A
192
113.357
29.083
25.802
1.00
36.99

ATOM
1854
C
THR
A
192
109.894
27.702
24.913
1.00
37.14

ATOM
1855
O
THR
A
192
109.082
28.485
25.403
1.00
38.53

ATOM
1856
N
LEU
A
193
109.604
26.884
23.906
1.00
38.31

ATOM
1858
CA
LEU
A
193
108.273
26.765
23.339
1.00
40.73

ATOM
1859
CB
LEU
A
193
108.325
25.772
22.174
1.00
42.93

ATOM
1860
CG
LEU
A
193
107.191
25.727
21.151
1.00
44.96

ATOM
1861
CD1
LEU
A
193
107.000
27.100
20.518
1.00
45.48

ATOM
1862
CD2
LEU
A
193
107.531
24.696
20.085
1.00
44.59

ATOM
1863
C
LEU
A
193
107.403
26.218
24.472
1.00
40.91

ATOM
1864
O
LEU
A
193
107.788
25.265
25.150
1.00
41.30

ATOM
1865
N
PRO
A
194
106.230
26.824
24.707
1.00
41.79

ATOM
1866
CD
PRO
A
194
105.632
27.950
23.974
1.00
41.39

ATOM
1867
CA
PRO
A
194
105.334
26.373
25.777
1.00
41.80

ATOM
1868
CB
PRO
A
194
104.217
27.420
25.754
1.00
42.00

ATOM
1869
CG
PRO
A
194
104.823
28.603
25.045
1.00
42.94

ATOM
1870
C
PRO
A
194
104.755
24.985
25.522
1.00
41.75

ATOM
1871
O
PRO
A
194
104.174
24.734
24.469
1.00
44.72

ATOM
1872
N
VAL
A
195
104.930
24.080
26.476
1.00
39.33

ATOM
1874
CA
VAL
A
195
104.383
22.738
26.338
1.00
37.64

ATOM
1875
CB
VAL
A
195
105.403
21.659
26.756
1.00
37.05

ATOM
1876
CG1
VAL
A
195
104.744
20.295
26.840
1.00
34.56

ATOM
1877
CG2
VAL
A
195
106.515
21.607
25.747
1.00
36.43

ATOM
1878
C
VAL
A
195
103.118
22.644
27.183
1.00
38.20

ATOM
1879
O
VAL
A
195
102.062
22.245
26.694
1.00
40.04

ATOM
1880
N
MET
A
196
103.234
23.007
28.454
1.00
38.05

ATOM
1882
CA
MET
A
196
102.103
22.987
29.370
1.00
37.71

ATOM
1883
CB
MET
A
196
102.414
22.128
30.592
1.00
40.52

ATOM
1884
CG
MET
A
196
102.756
20.681
30.283
1.00
43.85

ATOM
1885
SD
MET
A
196
101.356
19.738
29.695
1.00
42.31

ATOM
1886
CE
MET
A
196
100.644
19.226
31.232
1.00
41.10

ATOM
1887
C
MET
A
196
101.924
24.428
29.796
1.00
37.52

ATOM
1888
O
MET
A
196
102.521
24.877
30.771
1.00
40.72

ATOM
1889
N
THR
A
197
101.134
25.167
29.039
1.00
36.00

ATOM
1891
CA
THR
A
197
100.914
26.565
29.335
1.00
34.89

ATOM
1892
CB
THR
A
197
100.650
27.324
28.036
1.00
37.85

ATOM
1893
OG1
THR
A
197
101.329
26.660
26.963
1.00
41.31

ATOM
1895
CG2
THR
A
197
101.177
28.733
28.131
1.00
39.84

ATOM
1896
C
THR
A
197
99.751
26.772
30.302
1.00
32.85

ATOM
1897
O
THR
A
197
98.594
26.571
29.939
1.00
33.57

ATOM
1898
N
LYS
A
198
100.061
27.122
31.545
1.00
29.63

ATOM
1900
CA
LYS
A
198
99.036
27.372
32.551
1.00
27.13

ATOM
1901
CB
LYS
A
198
99.630
27.266
33.952
1.00
26.01

ATOM
1902
CG
LYS
A
198
98.609
27.379
35.047
1.00
26.97

ATOM
1903
CD
LYS
A
198
99.269
27.457
36.389
1.00
31.48

ATOM
1904
CE
LYS
A
198
98.232
27.489
37.482
1.00
33.31

ATOM
1905
NZ
LYS
A
198
97.393
26.263
37.448
1.00
38.94

ATOM
1909
C
LYS
A
198
98.555
28.789
32.307
1.00
26.60

ATOM
1910
O
LYS
A
198
99.365
29.706
32.264
1.00
27.53

ATOM
1911
N
ILE
A
199
97.248
28.975
32.154
1.00
26.62

ATOM
1913
CA
ILE
A
199
96.711
30.298
31.878
1.00
23.94

ATOM
1914
CB
ILE
A
199
95.817
30.283
30.613
1.00
25.54

ATOM
1915
CG2
ILE
A
199
96.561
29.614
29.477
1.00
26.32

ATOM
1916
CG1
ILE
A
199
94.543
29.487
30.843
1.00
23.67

ATOM
1917
CD1
ILE
A
199
93.795
29.189
29.564
1.00
22.95

ATOM
1918
C
ILE
A
199
95.992
30.954
33.041
1.00
25.86

ATOM
1919
O
ILE
A
199
95.827
32.169
33.061
1.00
28.61

ATOM
1920
N
ASP
A
200
95.561
30.148
34.007
1.00
27.99

ATOM
1922
CA
ASP
A
200
94.878
30.651
35.197
1.00
26.92

ATOM
1923
CB
ASP
A
200
93.484
31.220
34.867
1.00
26.06

ATOM
1924
CG
ASP
A
200
92.582
30.234
34.151
1.00
24.60

ATOM
1925
OD1
ASP
A
200
92.621
29.037
34.465
1.00
26.68

ATOM
1926
OD2
ASP
A
200
91.813
30.664
33.271
1.00
28.99

ATOM
1927
C
ASP
A
200
94.805
29.589
36.289
1.00
27.44

ATOM
1928
O
ASP
A
200
95.509
28.591
36.225
1.00
29.73

ATOM
1929
N
SER
A
201
93.966
29.808
37.294
1.00
28.30

ATOM
1931
CA
SER
A
201
93.825
28.859
38.397
1.00
30.40

ATOM
1932
CB
SER
A
201
93.032
29.507
39.531
1.00
31.85

ATOM
1933
OG
SER
A
201
91.882
30.170
39.026
1.00
39.39

ATOM
1935
C
SER
A
201
93.137
27.562
38.000
1.00
29.79

ATOM
1936
O
SER
A
201
93.230
26.557
38.695
1.00
31.67

ATOM
1937
N
VAL
A
202
92.430
27.604
36.884
1.00
30.29

ATOM
1939
CA
VAL
A
202
91.683
26.457
36.409
1.00
29.89

ATOM
1940
CB
VAL
A
202
90.284
26.911
35.932
1.00
28.59

ATOM
1941
CG1
VAL
A
202
89.426
25.723
35.568
1.00
30.45

ATOM
1942
CG2
VAL
A
202
89.613
27.740
36.998
1.00
28.22

ATOM
1943
C
VAL
A
202
92.346
25.667
35.282
1.00
31.71

ATOM
1944
O
VAL
A
202
92.752
24.520
35.470
1.00
33.93

ATOM
1945
N
ALA
A
203
92.463
26.291
34.115
1.00
31.10

ATOM
1947
CA
ALA
A
203
92.997
25.621
32.944
1.00
29.58

ATOM
1948
CB
ALA
A
203
92.039
25.821
31.767
1.00
29.01

ATOM
1949
C
ALA
A
203
94.416
25.908
32.497
1.00
28.91

ATOM
1950
O
ALA
A
203
95.096
26.807
33.001
1.00
27.86

ATOM
1951
N
GLY
A
204
94.822
25.124
31.503
1.00
26.23

ATOM
1953
CA
GLY
A
204
96.124
25.227
30.894
1.00
22.94

ATOM
1954
C
GLY
A
204
95.936
24.686
29.495
1.00
22.27

ATOM
1955
O
GLY
A
204
94.900
24.098
29.206
1.00
24.27

ATOM
1956
N
ILE
A
205
96.909
24.893
28.619
1.00
22.81

ATOM
1958
CA
ILE
A
205
96.817
24.402
27.250
1.00
21.62

ATOM
1959
CB
ILE
A
205
96.868
25.542
26.222
1.00
17.56

ATOM
1960
CG2
ILE
A
205
96.458
25.020
24.870
1.00
17.14

ATOM
1961
CG1
ILE
A
205
95.928
26.672
26.627
1.00
16.69

ATOM
1962
CD1
ILE
A
205
96.021
27.878
25.753
1.00
10.87

ATOM
1963
C
ILE
A
205
98.010
23.492
27.008
1.00
24.34

ATOM
1964
O
ILE
A
205
99.120
23.784
27.452
1.00
26.93

ATOM
1965
N
ASN
A
206
97.770
22.374
26.333
1.00
24.44

ATOM
1967
CA
ASN
A
206
98.817
21.414
26.039
1.00
20.90

ATOM
1968
CB
ASN
A
206
98.280
19.989
26.217
1.00
21.75

ATOM
1969
CG
ASN
A
206
99.359
18.921
26.099
1.00
22.44

ATOM
1970
OD1
ASN
A
206
99.077
17.727
26.218
1.00
26.27

ATOM
1971
ND2
ASN
A
206
100.593
19.337
25.878
1.00
24.68

ATOM
1974
C
ASN
A
206
99.285
21.629
24.614
1.00
22.48

ATOM
1975
O
ASN
A
206
98.579
21.296
23.664
1.00
23.50

ATOM
1976
N
TYR
A
207
100.458
22.239
24.475
1.00
23.09

ATOM
1978
CA
TYR
A
207
101.065
22.517
23.179
1.00
21.41

ATOM
1979
CB
TYR
A
207
101.647
23.927
23.165
1.00
17.69

ATOM
1980
CG
TYR
A
207
100.625
25.008
22.986
1.00
16.56

ATOM
1981
CD1
TYR
A
207
99.703
24.943
21.961
1.00
19.32

ATOM
1982
CE1
TYR
A
207
98.795
25.963
21.757
1.00
20.24

ATOM
1983
CD2
TYR
A
207
100.611
26.122
23.810
1.00
18.10

ATOM
1984
CE2
TYR
A
207
99.711
27.144
23.613
1.00
18.49

ATOM
1985
CZ
TYR
A
207
98.809
27.060
22.581
1.00
18.16

ATOM
1986
OH
TYR
A
207
97.939
28.089
22.332
1.00
21.72

ATOM
1988
C
TYR
A
207
102.181
21.532
22.868
1.00
24.14

ATOM
1989
O
TYR
A
207
103.111
21.851
22.134
1.00
25.16

ATOM
1990
N
GLY
A
208
102.083
20.328
23.418
1.00
28.50

ATOM
1992
CA
GLY
A
208
103.112
19.330
23.194
1.00
29.80

ATOM
1993
C
GLY
A
208
103.130
18.752
21.795
1.00
32.56

ATOM
1994
O
GLY
A
208
102.067
18.467
21.231
1.00
33.45

ATOM
1995
N
LEU
A
209
104.332
18.598
21.235
1.00
33.15

ATOM
1997
CA
LEU
A
209
104.512
18.038
19.899
1.00
31.79

ATOM
1998
CB
LEU
A
209
105.985
18.081
19.484
1.00
29.49

ATOM
1999
CG
LEU
A
209
106.491
19.337
18.773
1.00
28.06

ATOM
2000
CD1
LEU
A
209
106.302
20.558
19.641
1.00
24.35

ATOM
2001
CD2
LEU
A
209
107.953
19.158
18.416
1.00
24.06

ATOM
2002
C
LEU
A
209
104.052
16.599
19.941
1.00
31.52

ATOM
2003
O
LEU
A
209
104.416
15.863
20.854
1.00
33.82

ATOM
2004
N
VAL
A
210
103.254
16.199
18.961
1.00
29.87

ATOM
2006
CA
VAL
A
210
102.752
14.836
18.915
1.00
29.99

ATOM
2007
CB
VAL
A
210
101.226
14.817
18.732
1.00
30.37

ATOM
2008
CG1
VAL
A
210
100.559
15.363
19.972
1.00
31.24

ATOM
2009
CG2
VAL
A
210
100.824
15.642
17.522
1.00
30.83

ATOM
2010
C
VAL
A
210
103.430
13.992
17.837
1.00
30.78

ATOM
2011
O
VAL
A
210
103.038
12.854
17.578
1.00
32.27

ATOM
2012
N
ALA
A
211
104.460
14.552
17.221
1.00
30.97

ATOM
2014
CA
ALA
A
211
105.199
13.857
16.178
1.00
32.26

ATOM
2015
CB
ALA
A
211
104.324
13.661
14.941
1.00
34.28

ATOM
2016
C
ALA
A
211
106.417
14.692
15.839
1.00
31.64

ATOM
2017
O
ALA
A
211
106.463
15.884
16.145
1.00
32.86

ATOM
2018
N
PRO
A
212
107.437
14.077
15.232
1.00
30.38

ATOM
2019
CD
PRO
A
212
107.550
12.667
14.820
1.00
28.87

ATOM
2020
CA
PRO
A
212
108.642
14.824
14.876
1.00
30.59

ATOM
2021
CB
PRO
A
212
109.576
13.724
14.384
1.00
30.90

ATOM
2022
CG
PRO
A
212
108.628
12.731
13.785
1.00
31.64

ATOM
2023
C
PRO
A
212
108.345
15.824
13.774
1.00
31.31

ATOM
2024
O
PRO
A
212
107.483
15.574
12.938
1.00
33.01

ATOM
2025
N
PRO
A
213
109.005
16.996
13.802
1.00
30.25

ATOM
2026
CD
PRO
A
213
109.882
17.457
14.892
1.00
28.21

ATOM
2027
CA
PRO
A
213
108.832
18.056
12.803
1.00
29.74

ATOM
2028
CB
PRO
A
213
109.889
19.076
13.220
1.00
29.54

ATOM
2029
CG
PRO
A
213
109.896
18.958
14.690
1.00
26.77

ATOM
2030
C
PRO
A
213
109.115
17.526
11.398
1.00
30.72

ATOM
2031
O
PRO
A
213
110.187
16.975
11.140
1.00
33.55

ATOM
2032
N
ALA
A
214
108.157
17.700
10.495
1.00
30.16

ATOM
2034
CA
ALA
A
214
108.296
17.231
9.123
1.00
29.31

ATOM
2035
CB
ALA
A
214
106.964
16.701
8.609
1.00
27.36

ATOM
2036
C
ALA
A
214
108.771
18.336
8.212
1.00
30.52

ATOM
2037
O
ALA
A
214
108.229
19.440
8.235
1.00
32.72

ATOM
2038
N
THR
A
215
109.781
18.052
7.405
1.00
30.13

ATOM
2040
CA
THR
A
215
110.268
19.047
6.472
1.00
31.47

ATOM
2041
CB
THR
A
215
111.805
19.044
6.366
1.00
32.14

ATOM
2042
OG1
THR
A
215
112.381
19.228
7.665
1.00
36.33

ATOM
2044
CG2
THR
A
215
112.268
20.177
5.474
1.00
33.34

ATOM
2045
C
THR
A
215
109.656
18.698
5.127
1.00
32.34

ATOM
2046
O
THR
A
215
109.642
17.533
4.729
1.00
32.18

ATOM
2047
N
THR
A
216
109.103
19.692
4.451
1.00
34.34

ATOM
2049
CA
THR
A
216
108.489
19.463
3.154
1.00
36.27

ATOM
2050
CB
THR
A
216
106.996
19.862
3.167
1.00
36.83

ATOM
2051
OG1
THR
A
216
106.872
21.255
3.477
1.00
37.89

ATOM
2053
CG2
THR
A
216
106.241
19.055
4.216
1.00
36.73

ATOM
2054
C
THR
A
216
109.247
20.254
2.092
1.00
37.93

ATOM
2055
O
THR
A
216
110.390
20.642
2.307
1.00
36.96

ATOM
2056
N
ALA
A
217
108.610
20.483
0.948
1.00
40.73

ATOM
2058
CA
ALA
A
217
109.228
21.215
−0.151
1.00
41.25

ATOM
2059
CB
ALA
A
217
108.452
20.967
−1.437
1.00
42.73

ATOM
2060
C
ALA
A
217
109.302
22.704
0.125
1.00
40.38

ATOM
2061
O
ALA
A
217
110.218
23.379
−0.337
1.00
40.36

ATOM
2062
N
GLU
A
218
108.319
23.215
0.860
1.00
41.20

ATOM
2064
CA
GLU
A
218
108.271
24.633
1.170
1.00
40.88

ATOM
2065
CB
GLU
A
218
107.443
25.372
0.113
1.00
46.00

ATOM
2066
CG
GLU
A
218
108.304
26.058
−0.947
1.00
53.45

ATOM
2067
CD
GLU
A
218
107.610
26.213
−2.286
1.00
57.50

ATOM
2068
OE1
GLU
A
218
106.543
25.588
−2.487
1.00
60.01

ATOM
2069
OE2
GLU
A
218
108.149
26.945
−3.146
1.00
59.32

ATOM
2070
C
GLU
A
218
107.832
25.030
2.580
1.00
39.13

ATOM
2071
O
GLU
A
218
107.635
26.216
2.839
1.00
40.54

ATOM
2072
N
THR
A
219
107.668
24.066
3.488
1.00
37.20

ATOM
2074
CA
THR
A
219
107.295
24.388
4.875
1.00
35.55

ATOM
2075
CB
THR
A
219
105.762
24.464
5.103
1.00
32.68

ATOM
2076
OG1
THR
A
219
105.144
23.249
4.674
1.00
35.48

ATOM
2078
CG2
THR
A
219
105.151
25.641
4.387
1.00
33.81

ATOM
2079
C
THR
A
219
107.828
23.400
5.906
1.00
34.31

ATOM
2080
O
THR
A
219
108.013
22.217
5.614
1.00
34.57

ATOM
2081
N
LEU
A
220
108.087
23.903
7.109
1.00
31.67

ATOM
2083
CA
LEU
A
220
108.533
23.079
8.219
1.00
29.70

ATOM
2084
CB
LEU
A
220
109.587
23.834
9.033
1.00
29.62

ATOM
2085
CG
LEU
A
220
110.345
23.149
10.177
1.00
31.10

ATOM
2086
CD1
LEU
A
220
109.511
23.047
11.435
1.00
30.08

ATOM
2087
CD2
LEU
A
220
110.794
21.791
9.727
1.00
30.78

ATOM
2088
C
LEU
A
220
107.236
22.902
9.017
1.00
29.78

ATOM
2089
O
LEU
A
220
106.693
23.878
9.545
1.00
30.49

ATOM
2090
N
ASP
A
221
106.698
21.685
9.032
1.00
29.15

ATOM
2092
CA
ASP
A
221
105.441
21.397
9.728
1.00
30.48

ATOM
2093
CB
ASP
A
221
104.603
20.394
8.924
1.00
34.57

ATOM
2094
CG
ASP
A
221
104.178
20.924
7.557
1.00
37.91

ATOM
2095
OD1
ASP
A
221
104.480
22.090
7.222
1.00
37.84

ATOM
2096
OD2
ASP
A
221
103.534
20.158
6.811
1.00
42.30

ATOM
2097
C
ASP
A
221
105.607
20.865
11.143
1.00
30.64

ATOM
2098
O
ASP
A
221
106.274
19.852
11.350
1.00
31.22

ATOM
2099
N
VAL
A
222
104.950
21.519
12.100
1.00
29.81

ATOM
2101
CA
VAL
A
222
104.999
21.131
13.512
1.00
29.49

ATOM
2102
CB
VAL
A
222
105.588
22.261
14.389
1.00
29.52

ATOM
2103
CG1
VAL
A
222
105.617
21.831
15.845
1.00
28.17

ATOM
2104
CG2
VAL
A
222
106.988
22.632
13.914
1.00
26.55

ATOM
2105
C
VAL
A
222
103.586
20.791
14.016
1.00
29.65

ATOM
2106
O
VAL
A
222
102.686
21.620
13.958
1.00
31.27

ATOM
2107
N
GLN
A
223
103.400
19.560
14.485
1.00
29.35

ATOM
2109
CA
GLN
A
223
102.114
19.081
14.978
1.00
25.88

ATOM
2110
CB
GLN
A
223
101.870
17.649
14.488
1.00
29.16

ATOM
2111
CG
GLN
A
223
101.731
17.505
12.969
1.00
30.27

ATOM
2112
CD
GLN
A
223
101.704
16.052
12.510
1.00
32.10

ATOM
2113
OE1
GLN
A
223
100.832
15.275
12.897
1.00
31.46

ATOM
2114
NE2
GLN
A
223
102.668
15.681
11.686
1.00
37.75

ATOM
2117
C
GLN
A
223
102.081
19.116
16.494
1.00
24.57

ATOM
2118
O
GLN
A
223
102.910
18.490
17.147
1.00
23.51

ATOM
2119
N
MET
A
224
101.112
19.840
17.042
1.00
22.94

ATOM
2121
CA
MET
A
224
100.959
19.984
18.480
1.00
22.16

ATOM
2122
CB
MET
A
224
101.064
21.459
18.866
1.00
23.89

ATOM
2123
CG
MET
A
224
102.353
22.116
18.423
1.00
22.07

ATOM
2124
SD
MET
A
224
102.393
23.853
18.797
1.00
28.37

ATOM
2125
CE
MET
A
224
104.122
24.130
18.771
1.00
25.60

ATOM
2126
C
MET
A
224
99.620
19.408
18.927
1.00
23.31

ATOM
2127
O
MET
A
224
98.702
19.294
18.124
1.00
27.48

ATOM
2128
N
LYS
A
225
99.519
19.024
20.197
1.00
25.28

ATOM
2130
CA
LYS
A
225
98.292
18.440
20.735
1.00
27.30

ATOM
2131
CB
LYS
A
225
98.522
17.889
22.140
1.00
28.45

ATOM
2132
CG
LYS
A
225
97.613
16.724
22.452
1.00
30.88

ATOM
2133
CD
LYS
A
225
97.912
16.108
23.793
1.00
33.18

ATOM
2134
CE
LYS
A
225
97.153
14.802
23.938
1.00
38.68

ATOM
2135
NZ
LYS
A
225
95.741
14.928
23.460
1.00
43.39

ATOM
2139
C
LYS
A
225
97.135
19.434
20.726
1.00
27.30

ATOM
2140
O
LYS
A
225
96.052
19.123
20.238
1.00
29.51

ATOM
2141
N
GLY
A
226
97.364
20.617
21.286
1.00
26.18

ATOM
2143
CA
GLY
A
226
96.360
21.665
21.285
1.00
21.95

ATOM
2144
C
GLY
A
226
95.015
21.379
21.903
1.00
23.48

ATOM
2145
O
GLY
A
226
93.983
21.420
21.238
1.00
23.78

ATOM
2146
N
GLU
A
227
95.021
21.131
23.201
1.00
26.02

ATOM
2148
CA
GLU
A
227
93.792
20.882
23.915
1.00
26.24

ATOM
2149
CB
GLU
A
227
93.547
19.384
24.068
1.00
29.17

ATOM
2150
CG
GLU
A
227
94.467
18.697
25.052
1.00
25.81

ATOM
2151
CD
GLU
A
227
93.967
17.330
25.456
1.00
29.15

ATOM
2152
OE1
GLU
A
227
93.343
16.654
24.614
1.00
33.43

ATOM
2153
OE2
GLU
A
227
94.199
16.928
26.615
1.00
31.54

ATOM
2154
C
GLU
A
227
93.937
21.514
25.283
1.00
27.06

ATOM
2155
O
GLU
A
227
95.006
21.447
25.892
1.00
26.79

ATOM
2156
N
PHE
A
228
92.904
22.219
25.722
1.00
26.37

ATOM
2158
CA
PHE
A
228
92.942
22.816
27.034
1.00
24.07

ATOM
2159
CB
PHE
A
228
91.785
23.792
27.242
1.00
24.55

ATOM
2160
CG
PHE
A
228
91.987
25.134
26.592
1.00
23.72

ATOM
2161
CD1
PHE
A
228
92.066
25.251
25.207
1.00
21.59

ATOM
2162
CD2
PHE
A
228
92.045
26.287
27.366
1.00
21.39

ATOM
2163
CE1
PHE
A
228
92.193
26.498
24.607
1.00
21.74

ATOM
2164
CE2
PHE
A
228
92.172
27.531
26.779
1.00
21.24

ATOM
2165
CZ
PHE
A
228
92.246
27.640
25.395
1.00
24.55

ATOM
2166
C
PHE
A
228
92.779
21.630
27.949
1.00
25.56

ATOM
2167
O
PHE
A
228
92.069
20.680
27.624
1.00
26.15

ATOM
2168
N
TYR
A
229
93.479
21.655
29.067
1.00
29.13

ATOM
2170
CA
TYR
A
229
93.400
20.573
30.025
1.00
34.87

ATOM
2171
CB
TYR
A
229
94.735
19.820
30.084
1.00
32.93

ATOM
2172
CG
TYR
A
229
95.870
20.654
30.639
1.00
33.77

ATOM
2173
CD1
TYR
A
229
96.034
20.816
32.015
1.00
34.08

ATOM
2174
CE1
TYR
A
229
97.021
21.637
32.530
1.00
33.96

ATOM
2175
CD2
TYR
A
229
96.739
21.332
29.793
1.00
34.25

ATOM
2176
CE2
TYR
A
229
97.735
22.152
30.302
1.00
34.53

ATOM
2177
CZ
TYR
A
229
97.863
22.302
31.670
1.00
33.54

ATOM
2178
OH
TYR
A
229
98.819
23.138
32.185
1.00
38.50

ATOM
2180
C
TYR
A
229
93.097
21.196
31.380
1.00
39.53

ATOM
2181
O
TYR
A
229
93.192
22.414
31.545
1.00
39.55

ATOM
2182
N
SER
A
230
92.738
20.355
32.341
1.00
46.28

ATOM
2184
CA
SER
A
230
92.453
20.796
33.699
1.00
53.45

ATOM
2185
CB
SER
A
230
90.998
20.491
34.071
1.00
54.47

ATOM
2186
OG
SER
A
230
90.720
20.820
35.424
1.00
56.07

ATOM
2188
C
SER
A
230
93.396
19.996
34.582
1.00
58.48

ATOM
2189
O
SER
A
230
93.659
18.826
34.301
1.00
58.09

ATOM
2190
N
GLU
A
231
93.946
20.632
35.611
1.00
66.92

ATOM
2192
CA
GLU
A
231
94.860
19.940
36.517
1.00
74.85

ATOM
2193
CB
GLU
A
231
95.976
20.878
36.995
1.00
77.02

ATOM
2194
CG
GLU
A
231
97.377
20.450
36.548
1.00
81.62

ATOM
2195
CD
GLU
A
231
98.476
21.372
37.054
1.00
84.67

ATOM
2196
OE1
GLU
A
231
98.402
22.592
36.790
1.00
86.64

ATOM
2197
OE2
GLU
A
231
99.421
20.876
37.709
1.00
85.89

ATOM
2198
C
GLU
A
231
94.119
19.328
37.706
1.00
78.17

ATOM
2199
O
GLU
A
231
94.602
18.379
38.323
1.00
79.46

ATOM
2200
N
ALA
A
232
92.934
19.855
38.003
1.00
81.24

ATOM
2202
CA
ALA
A
232
92.131
19.363
39.118
1.00
84.16

ATOM
2203
CB
ALA
A
232
91.111
20.417
39.544
1.00
84.14

ATOM
2204
C
ALA
A
232
91.426
18.053
38.777
1.00
86.04

ATOM
2205
O
ALA
A
232
91.078
17.279
39.671
1.00
87.55

ATOM
2206
N
ALA
A
233
91.203
17.819
37.487
1.00
86.79

ATOM
2208
CA
ALA
A
233
90.534
16.608
37.023
1.00
88.81

ATOM
2209
CB
ALA
A
233
89.052
16.659
37.381
1.00
89.87

ATOM
2210
C
ALA
A
233
90.702
16.464
35.516
1.00
90.03

ATOM
2211
O
ALA
A
233
90.288
17.341
34.756
1.00
90.77

ATOM
2212
N
ALA
A
234
91.309
15.361
35.090
1.00
91.16

ATOM
2214
CA
ALA
A
234
91.536
15.106
33.670
1.00
91.66

ATOM
2215
CB
ALA
A
234
92.810
14.288
33.470
1.00
92.37

ATOM
2216
C
ALA
A
234
90.354
14.394
33.034
1.00
91.31

ATOM
2217
O
ALA
A
234
89.874
13.384
33.550
1.00
91.09

ATOM
2218
N
ALA
A
235
89.894
14.926
31.908
1.00
91.34

ATOM
2220
CA
ALA
A
235
88.774
14.346
31.180
1.00
90.88

ATOM
2221
CB
ALA
A
235
87.457
14.975
31.627
1.00
91.57

ATOM
2222
C
ALA
A
235
88.993
14.572
29.691
1.00
89.83

ATOM
2223
O
ALA
A
235
89.205
15.706
29.247
1.00
89.77

ATOM
2224
N
PRO
A
236
89.032
13.480
28.912
1.00
88.56

ATOM
2225
CD
PRO
A
236
88.962
12.083
29.376
1.00
88.69

ATOM
2226
CA
PRO
A
236
89.232
13.539
27.463
1.00
85.91

ATOM
2227
CB
PRO
A
236
89.511
12.080
27.104
1.00
86.56

ATOM
2228
CG
PRO
A
236
88.680
11.334
28.099
1.00
88.16

ATOM
2229
C
PRO
A
236
87.997
14.085
26.738
1.00
82.58

ATOM
2230
O
PRO
A
236
86.861
13.877
27.172
1.00
81.75

ATOM
2231
N
PRO
A
237
88.217
14.829
25.644
1.00
79.77

ATOM
2232
CD
PRO
A
237
89.551
15.264
25.202
1.00
80.44

ATOM
2233
CA
PRO
A
237
87.178
15.444
24.811
1.00
77.34

ATOM
2234
CB
PRO
A
237
87.985
16.332
23.863
1.00
77.69

ATOM
2235
CG
PRO
A
237
89.249
16.604
24.617
1.00
79.85

ATOM
2236
C
PRO
A
237
86.366
14.426
24.015
1.00
75.23

ATOM
2237
O
PRO
A
237
86.919
13.462
23.480
1.00
75.90

ATOM
2238
N
PRO
A
238
85.042
14.634
23.918
1.00
72.71

ATOM
2239
CD
PRO
A
238
84.282
15.606
24.724
1.00
72.84

ATOM
2240
CA
PRO
A
238
84.131
13.750
23.182
1.00
70.12

ATOM
2241
CB
PRO
A
238
82.774
14.086
23.793
1.00
71.89

ATOM
2242
CG
PRO
A
238
82.907
15.535
24.109
1.00
72.51

ATOM
2243
C
PRO
A
238
84.146
14.004
21.672
1.00
67.49

ATOM
2244
O
PRO
A
238
83.099
14.016
21.017
1.00
66.70

ATOM
2245
N
PHE
A
239
85.340
14.216
21.130
1.00
64.79

ATOM
2247
CA
PHE
A
239
85.521
14.472
19.706
1.00
61.01

ATOM
2248
CB
PHE
A
239
84.959
15.849
19.319
1.00
60.29

ATOM
2249
CG
PHE
A
239
85.172
16.923
20.362
1.00
57.87

ATOM
2250
CD1
PHE
A
239
86.307
17.721
20.339
1.00
56.42

ATOM
2251
CD2
PHE
A
239
84.216
17.159
21.343
1.00
55.75

ATOM
2252
CE1
PHE
A
239
86.484
18.737
21.274
1.00
53.82

ATOM
2253
CE2
PHE
A
239
84.387
18.171
22.279
1.00
53.85

ATOM
2254
CZ
PHE
A
239
85.522
18.960
22.243
1.00
52.72

ATOM
2255
C
PHE
A
239
86.989
14.355
19.307
1.00
58.61

ATOM
2256
O
PHE
A
239
87.873
14.266
20.164
1.00
58.11

ATOM
2257
N
ALA
A
240
87.234
14.314
18.002
1.00
55.15

ATOM
2259
CA
ALA
A
240
88.586
14.203
17.472
1.00
51.42

ATOM
2260
CB
ALA
A
240
88.716
12.936
16.631
1.00
51.91

ATOM
2261
C
ALA
A
240
88.884
15.441
16.629
1.00
49.88

ATOM
2262
O
ALA
A
240
87.972
16.034
16.048
1.00
48.56

ATOM
2263
N
PRO
A
241
90.155
15.885
16.604
1.00
48.54

ATOM
2264
CD
PRO
A
241
91.270
15.398
17.436
1.00
47.09

ATOM
2265
CA
PRO
A
241
90.567
17.064
15.830
1.00
46.53

ATOM
2266
CB
PRO
A
241
92.043
17.218
16.205
1.00
44.66

ATOM
2267
CG
PRO
A
241
92.113
16.633
17.574
1.00
45.79

ATOM
2268
C
PRO
A
241
90.412
16.864
14.322
1.00
46.25

ATOM
2269
O
PRO
A
241
90.536
15.743
13.819
1.00
47.76

ATOM
2270
N
PRO
A
242
90.118
17.947
13.582
1.00
45.32

ATOM
2271
CD
PRO
A
242
89.818
19.314
14.050
1.00
44.47

ATOM
2272
CA
PRO
A
242
89.959
17.844
12.130
1.00
44.33

ATOM
2273
CB
PRO
A
242
89.187
19.114
11.792
1.00
43.70

ATOM
2274
CG
PRO
A
242
89.769
20.107
12.755
1.00
43.85

ATOM
2275
C
PRO
A
242
91.325
17.835
11.442
1.00
45.10

ATOM
2276
O
PRO
A
242
92.331
18.261
12.019
1.00
44.03

ATOM
2277
N
VAL
A
243
91.370
17.302
10.228
1.00
45.79

ATOM
2279
CA
VAL
A
243
92.615
17.279
9.485
1.00
47.91

ATOM
2280
CB
VAL
A
243
92.613
16.226
8.347
1.00
48.72

ATOM
2281
CG1
VAL
A
243
92.629
14.827
8.934
1.00
50.59

ATOM
2282
CG2
VAL
A
243
91.403
16.401
7.446
1.00
51.20

ATOM
2283
C
VAL
A
243
92.753
18.679
8.926
1.00
48.35

ATOM
2284
O
VAL
A
243
91.939
19.122
8.116
1.00
48.79

ATOM
2285
N
MET
A
244
93.731
19.412
9.434
1.00
48.68

ATOM
2287
CA
MET
A
244
93.937
20.771
8.987
1.00
46.91

ATOM
2288
CB
MET
A
244
94.406
21.638
10.147
1.00
42.52

ATOM
2289
CG
MET
A
244
93.369
21.770
11.233
1.00
30.61

ATOM
2290
SD
MET
A
244
93.963
22.834
12.505
1.00
30.25

ATOM
2291
CE
MET
A
244
94.948
21.710
13.447
1.00
25.62

ATOM
2292
C
MET
A
244
94.884
20.877
7.811
1.00
50.14

ATOM
2293
O
MET
A
244
96.102
20.935
7.983
1.00
50.38

ATOM
2294
N
GLU
A
245
94.302
20.867
6.615
1.00
53.76

ATOM
2296
CA
GLU
A
245
95.046
20.985
5.367
1.00
58.60

ATOM
2297
CB
GLU
A
245
94.597
19.905
4.364
1.00
61.51

ATOM
2298
CG
GLU
A
245
93.085
19.861
4.078
1.00
67.59

ATOM
2299
CD
GLU
A
245
92.692
18.811
3.041
1.00
69.79

ATOM
2300
OE1
GLU
A
245
92.943
19.024
1.827
1.00
72.17

ATOM
2301
OE2
GLU
A
245
92.104
17.778
3.439
1.00
68.95

ATOM
2302
C
GLU
A
245
94.817
22.382
4.794
1.00
59.59

ATOM
2303
O
GLU
A
245
93.765
22.664
4.220
1.00
60.79

ATOM
2304
N
PHE
A
246
95.773
23.278
5.010
1.00
61.44

ATOM
2306
CA
PHE
A
246
95.637
24.635
4.510
1.00
63.27

ATOM
2307
CB
PHE
A
246
95.567
25.658
5.657
1.00
60.46

ATOM
2308
CG
PHE
A
246
96.689
25.567
6.663
1.00
56.43

ATOM
2309
CD1
PHE
A
246
97.850
26.319
6.502
1.00
54.28

ATOM
2310
CD2
PHE
A
246
96.532
24.825
7.834
1.00
53.72

ATOM
2311
CE1
PHE
A
246
98.829
26.342
7.497
1.00
51.24

ATOM
2312
CE2
PHE
A
246
97.506
24.841
8.834
1.00
51.21

ATOM
2313
CZ
PHE
A
246
98.653
25.602
8.667
1.00
48.89

ATOM
2314
C
PHE
A
246
96.676
25.022
3.473
1.00
67.53

ATOM
2315
O
PHE
A
246
97.723
24.382
3.357
1.00
68.37

ATOM
2316
N
PRO
A
247
96.375
26.050
2.664
1.00
71.27

ATOM
2317
CD
PRO
A
247
95.153
26.874
2.673
1.00
72.37

ATOM
2318
CA
PRO
A
247
97.297
26.511
1.624
1.00
74.18

ATOM
2319
CB
PRO
A
247
96.504
27.627
0.938
1.00
74.64

ATOM
2320
CG
PRO
A
247
95.626
28.147
2.038
1.00
73.71

ATOM
2321
C
PRO
A
247
98.620
27.016
2.180
1.00
76.26

ATOM
2322
O
PRO
A
247
98.661
28.002
2.920
1.00
76.91

ATOM
2323
N
ALA
A
248
99.691
26.299
1.858
1.00
78.37

ATOM
2325
CA
ALA
A
248
101.027
26.675
2.298
1.00
80.34

ATOM
2326
CB
ALA
A
248
102.025
25.578
1.963
1.00
80.57

ATOM
2327
C
ALA
A
248
101.385
27.950
1.556
1.00
81.06

ATOM
2328
O
ALA
A
248
101.463
27.962
0.325
1.00
81.92

ATOM
2329
N
ALA
A
249
101.564
29.030
2.300
1.00
80.72

ATOM
2331
CA
ALA
A
249
101.902
30.303
1.694
1.00
79.65

ATOM
2332
CB
ALA
A
249
100.799
31.319
1.964
1.00
80.65

ATOM
2333
C
ALA
A
249
103.232
30.799
2.234
1.00
78.22

ATOM
2334
O
ALA
A
249
103.799
30.201
3.150
1.00
78.60

ATOM
2335
N
ALA
A
250
103.734
31.878
1.643
1.00
76.27

ATOM
2337
CA
ALA
A
250
104.997
32.476
2.062
1.00
74.32

ATOM
2338
CB
ALA
A
250
106.093
32.174
1.042
1.00
75.66

ATOM
2339
C
ALA
A
250
104.840
33.985
2.249
1.00
71.97

ATOM
2340
O
ALA
A
250
105.815
34.732
2.160
1.00
72.98

ATOM
2341
N
ASP
A
251
103.606
34.422
2.496
1.00
67.46

ATOM
2343
CA
ASP
A
251
103.302
35.836
2.708
1.00
61.94

ATOM
2344
CB
ASP
A
251
101.797
36.090
2.568
1.00
66.00

ATOM
2345
CG
ASP
A
251
101.277
35.785
1.177
1.00
70.21

ATOM
2346
OD1
ASP
A
251
101.467
34.647
0.695
1.00
71.96

ATOM
2347
OD2
ASP
A
251
100.668
36.687
0.566
1.00
72.84

ATOM
2348
C
ASP
A
251
103.760
36.265
4.101
1.00
56.10

ATOM
2349
O
ASP
A
251
104.203
37.396
4.298
1.00
56.97

ATOM
2350
N
ARG
A
252
103.611
35.364
5.067
1.00
47.53

ATOM
2352
CA
ARG
A
252
104.009
35.622
6.441
1.00
39.41

ATOM
2353
CB
ARG
A
252
102.815
35.472
7.384
1.00
39.71

ATOM
2354
CG
ARG
A
252
101.668
36.426
7.129
1.00
39.66

ATOM
2355
CD
ARG
A
252
101.975
37.837
7.596
1.00
41.34

ATOM
2356
NE
ARG
A
252
100.830
38.714
7.375
1.00
42.20

ATOM
2358
CZ
ARG
A
252
100.628
39.416
6.263
1.00
44.51

ATOM
2359
NH1
ARG
A
252
101.498
39.358
5.263
1.00
45.26

ATOM
2362
NH2
ARG
A
252
99.542
40.163
6.141
1.00
44.83

ATOM
2365
C
ARG
A
252
105.070
34.594
6.798
1.00
34.91

ATOM
2366
O
ARG
A
252
105.315
33.667
6.035
1.00
31.70

ATOM
2367
N
MET
A
253
105.662
34.730
7.976
1.00
32.83

ATOM
2369
CA
MET
A
253
106.697
33.809
8.417
1.00
30.84

ATOM
2370
CB
MET
A
253
107.605
34.499
9.441
1.00
30.27

ATOM
2371
CG
MET
A
253
108.192
35.807
8.925
1.00
31.26

ATOM
2372
SD
MET
A
253
109.366
36.637
10.009
1.00
34.11

ATOM
2373
CE
MET
A
253
110.335
37.492
8.834
1.00
29.80

ATOM
2374
C
MET
A
253
106.130
32.501
8.979
1.00
31.42

ATOM
2375
O
MET
A
253
106.568
31.419
8.595
1.00
31.42

ATOM
2376
N
VAL
A
254
105.144
32.600
9.866
1.00
31.26

ATOM
2378
CA
VAL
A
254
104.540
31.419
10.480
1.00
32.17

ATOM
2379
CB
VAL
A
254
104.781
31.376
12.015
1.00
32.83

ATOM
2380
CG1
VAL
A
254
106.243
31.143
12.324
1.00
35.48

ATOM
2381
CG2
VAL
A
254
104.316
32.672
12.658
1.00
33.43

ATOM
2382
C
VAL
A
254
103.043
31.378
10.262
1.00
32.00

ATOM
2383
O
VAL
A
254
102.412
32.410
10.059
1.00
33.43

ATOM
2384
N
TYR
A
255
102.478
30.181
10.340
1.00
33.42

ATOM
2386
CA
TYR
A
255
101.044
29.979
10.179
1.00
32.60

ATOM
2387
CB
TYR
A
255
100.726
29.448
8.784
1.00
32.98

ATOM
2388
CG
TYR
A
255
100.746
30.482
7.694
1.00
32.36

ATOM
2389
CD1
TYR
A
255
101.913
30.756
6.987
1.00
31.99

ATOM
2390
CE1
TYR
A
255
101.921
31.674
5.947
1.00
33.10

ATOM
2391
CD2
TYR
A
255
99.587
31.154
7.335
1.00
31.03

ATOM
2392
CE2
TYR
A
255
99.583
32.072
6.298
1.00
32.21

ATOM
2393
CZ
TYR
A
255
100.750
32.325
5.607
1.00
33.29

ATOM
2394
OH
TYR
A
255
100.741
33.230
4.573
1.00
38.59

ATOM
2396
C
TYR
A
255
100.559
28.955
11.195
1.00
31.73

ATOM
2397
O
TYR
A
255
101.156
27.892
11.330
1.00
32.57

ATOM
2398
N
LEU
A
256
99.490
29.279
11.914
1.00
31.36

ATOM
2400
CA
LEU
A
256
98.916
28.370
12.893
1.00
29.13

ATOM
2401
CB
LEU
A
256
98.878
28.992
14.280
1.00
28.40

ATOM
2402
CG
LEU
A
256
100.206
29.125
15.014
1.00
28.89

ATOM
2403
CD1
LEU
A
256
101.045
30.208
14.375
1.00
32.20

ATOM
2404
CD2
LEU
A
256
99.938
29.462
16.471
1.00
32.12

ATOM
2405
C
LEU
A
256
97.509
27.984
12.489
1.00
30.86

ATOM
2406
O
LEU
A
256
96.748
28.814
11.987
1.00
30.77

ATOM
2407
N
GLY
A
257
97.203
26.701
12.652
1.00
31.62

ATOM
2409
CA
GLY
A
257
95.888
26.180
12.345
1.00
29.36

ATOM
2410
C
GLY
A
257
95.287
25.827
13.688
1.00
29.99

ATOM
2411
O
GLY
A
257
95.662
24.830
14.295
1.00
32.08

ATOM
2412
N
LEU
A
258
94.402
26.686
14.177
1.00
29.99

ATOM
2414
CA
LEU
A
258
93.742
26.507
15.463
1.00
26.58

ATOM
2415
CB
LEU
A
258
93.562
27.871
16.101
1.00
26.90

ATOM
2416
CG
LEU
A
258
94.866
28.668
16.049
1.00
28.57

ATOM
2417
CD1
LEU
A
258
94.583
30.144
16.176
1.00
29.14

ATOM
2418
CD2
LEU
A
258
95.808
28.177
17.139
1.00
29.78

ATOM
2419
C
LEU
A
258
92.397
25.838
15.253
1.00
28.27

ATOM
2420
O
LEU
A
258
91.404
26.499
14.936
1.00
29.90

ATOM
2421
N
SER
A
259
92.370
24.523
15.434
1.00
28.81

ATOM
2423
CA
SER
A
259
91.164
23.726
15.229
1.00
30.63

ATOM
2424
CB
SER
A
259
91.491
22.237
15.348
1.00
31.03

ATOM
2425
OG
SER
A
259
91.783
21.889
16.689
1.00
33.43

ATOM
2427
C
SER
A
259
90.003
24.041
16.152
1.00
31.95

ATOM
2428
O
SER
A
259
90.184
24.600
17.231
1.00
33.18

ATOM
2429
N
ASP
A
260
88.808
23.637
15.729
1.00
32.89

ATOM
2431
CA
ASP
A
260
87.616
23.844
16.530
1.00
31.93

ATOM
2432
CB
ASP
A
260
86.326
23.521
15.739
1.00
33.23

ATOM
2433
CG
ASP
A
260
86.327
22.127
15.080
1.00
32.26

ATOM
2434
OD1
ASP
A
260
87.138
21.246
15.425
1.00
33.22

ATOM
2435
OD2
ASP
A
260
85.473
21.904
14.203
1.00
32.09

ATOM
2436
C
ASP
A
260
87.725
23.015
17.807
1.00
30.67

ATOM
2437
O
ASP
A
260
87.234
23.417
18.856
1.00
34.53

ATOM
2438
N
TYR
A
261
88.414
21.881
17.715
1.00
27.04

ATOM
2440
CA
TYR
A
261
88.629
20.983
18.847
1.00
26.39

ATOM
2441
CB
TYR
A
261
89.490
19.789
18.382
1.00
27.42

ATOM
2442
CG
TYR
A
261
90.064
18.885
19.463
1.00
26.82

ATOM
2443
CD1
TYR
A
261
91.304
19.157
20.038
1.00
29.26

ATOM
2444
CE1
TYR
A
261
91.855
18.318
21.006
1.00
30.93

ATOM
2445
CD2
TYR
A
261
89.386
17.745
19.886
1.00
26.82

ATOM
2446
CE2
TYR
A
261
89.927
16.898
20.853
1.00
28.99

ATOM
2447
CZ
TYR
A
261
91.163
17.194
21.408
1.00
32.15

ATOM
2448
OH
TYR
A
261
91.715
16.368
22.364
1.00
36.84

ATOM
2450
C
TYR
A
261
89.345
21.796
19.917
1.00
25.35

ATOM
2451
O
TYR
A
261
88.939
21.824
21.076
1.00
31.74

ATOM
2452
N
PHE
A
262
90.361
22.525
19.488
1.00
23.54

ATOM
2454
CA
PHE
A
262
91.151
23.361
20.368
1.00
21.85

ATOM
2455
CB
PHE
A
262
92.141
24.158
19.514
1.00
19.79

ATOM
2456
CG
PHE
A
262
92.923
25.184
20.275
1.00
20.92

ATOM
2457
CD1
PHE
A
262
93.830
24.806
21.253
1.00
22.00

ATOM
2458
CD2
PHE
A
262
92.761
26.536
20.002
1.00
20.09

ATOM
2459
CE1
PHE
A
262
94.558
25.759
21.943
1.00
19.37

ATOM
2460
CE2
PHE
A
262
93.488
27.497
20.693
1.00
18.46

ATOM
2461
CZ
PHE
A
262
94.386
27.107
21.660
1.00
18.18

ATOM
2462
C
PHE
A
262
90.244
24.290
21.165
1.00
21.70

ATOM
2463
O
PHE
A
262
90.236
24.266
22.391
1.00
22.47

ATOM
2464
N
PHE
A
263
89.432
25.060
20.457
1.00
24.02

ATOM
2466
CA
PHE
A
263
88.522
26.014
21.079
1.00
23.57

ATOM
2467
CB
PHE
A
263
87.843
26.845
20.005
1.00
22.46

ATOM
2468
CG
PHE
A
263
88.783
27.712
19.241
1.00
21.39

ATOM
2469
CD1
PHE
A
263
89.462
28.740
19.870
1.00
25.06

ATOM
2470
CD2
PHE
A
263
88.982
27.510
17.887
1.00
23.84

ATOM
2471
CE1
PHE
A
263
90.326
29.555
19.159
1.00
26.31

ATOM
2472
CE2
PHE
A
263
89.843
28.319
17.169
1.00
25.34

ATOM
2473
CZ
PHE
A
263
90.514
29.345
17.804
1.00
25.18

ATOM
2474
C
PHE
A
263
87.457
25.378
21.933
1.00
25.63

ATOM
2475
O
PHE
A
263
87.103
25.892
22.992
1.00
29.04

ATOM
2476
N
ASN
A
264
86.926
24.264
21.463
1.00
27.70

ATOM
2478
CA
ASN
A
264
85.882
23.577
22.193
1.00
26.71

ATOM
2479
CB
ASN
A
264.
85.136
22.617
21.278
1.00
26.91

ATOM
2480
CG
ASN
A
264
84.183
23.338
20.345
1.00
26.18

ATOM
2481
OD1
ASN
A
264
83.115
23.779
20.755
1.00
29.25

ATOM
2482
ND2
ASN
A
264
84.563
23.462
19.087
1.00
30.59

ATOM
2485
C
ASN
A
264
86.359
22.898
23.470
1.00
26.40

ATOM
2486
O
ASN
A
264
85.587
22.763
24.414
1.00
27.80

ATOM
2487
N
THR
A
265
87.628
22.498
23.527
1.00
26.30

ATOM
2489
CA
THR
A
265
88.154
21.880
24.748
1.00
24.34

ATOM
2490
CB
THR
A
265
89.572
21.298
24.559
1.00
24.55

ATOM
2491
OG1
THR
A
265
90.453
22.296
24.033
1.00
26.59

ATOM
2493
CG2
THR
A
265
89.532
20.129
23.619
1.00
21.96

ATOM
2494
C
THR
A
265
88.175
22.924
25.865
1.00
23.53

ATOM
2495
O
THR
A
265
88.045
22.602
27.041
1.00
26.65

ATOM
2496
N
ALA
A
266
88.309
24.186
25.483
1.00
24.00

ATOM
2498
CA
ALA
A
266
88.315
25.276
26.437
1.00
22.35

ATOM
2499
CB
ALA
A
266
88.582
26.590
25.723
1.00
21.75

ATOM
2500
C
ALA
A
266
86.956
25.310
27.113
1.00
23.18

ATOM
2501
O
ALA
A
266
86.865
25.297
28.336
1.00
27.51

ATOM
2502
N
GLY
A
267
85.897
25.286
26.311
1.00
24.69

ATOM
2504
CA
GLY
A
267
84.549
25.323
26.852
1.00
24.20

ATOM
2505
C
GLY
A
267
84.251
24.188
27.812
1.00
27.46

ATOM
2506
O
GLY
A
267
83.637
24.381
28.869
1.00
27.80

ATOM
2507
N
LEU
A
268
84.699
22.997
27.445
1.00
28.36

ATOM
2509
CA
LEU
A
268
84.493
21.816
28.262
1.00
29.18

ATOM
2510
CB
LEU
A
268
84.996
20.580
27.520
1.00
32.75

ATOM
2511
CG
LEU
A
268
84.728
19.224
28.169
1.00
37.10

ATOM
2512
CD1
LEU
A
268
83.274
18.841
27.978
1.00
38.10

ATOM
2513
CD2
LEU
A
268
85.633
18.180
27.544
1.00
41.14

ATOM
2514
C
LEU
A
268
85.209
21.940
29.596
1.00
27.77

ATOM
2515
O
LEU
A
268
84.623
21.696
30.644
1.00
31.78

ATOM
2516
N
VAL
A
269
86.469
22.344
29.558
1.00
26.94

ATOM
2518
CA
VAL
A
269
87.256
22.478
30.774
1.00
26.89

ATOM
2519
CB
VAL
A
269
88.752
22.720
30.448
1.00
24.63

ATOM
2520
CG1
VAL
A
269
89.491
23.244
31.656
1.00
22.76

ATOM
2521
CG2
VAL
A
269
89.382
21.416
30.007
1.00
21.59

ATOM
2522
C
VAL
A
269
86.722
23.535
31.740
1.00
28.84

ATOM
2523
O
VAL
A
269
86.687
23.309
32.948
1.00
29.66

ATOM
2524
N
TYR
A
270
86.298
24.681
31.219
1.00
30.57

ATOM
2526
CA
TYR
A
270
85.769
25.734
32.080
1.00
28.60

ATOM
2527
CB
TYR
A
270
85.753
27.079
31.350
1.00
28.80

ATOM
2528
CG
TYR
A
270
87.111
27.734
31.265
1.00
27.47

ATOM
2529
CD1
TYR
A
270.
87.766
28.169
32.415
1.00
25.23

ATOM
2530
CE1
TYR
A
270
89.021
28.754
32.343
1.00
26.36

ATOM
2531
CD2
TYR
A
270
87.750
27.906
30.038
1.00
29.53

ATOM
2532
CE2
TYR
A
270
89.008
28.494
29.959
1.00
25.30

ATOM
2533
CZ
TYR
A
270
89.632
28.912
31.114
1.00
24.84

ATOM
2534
OH
TYR
A
270
90.877
29.492
31.047
1.00
30.89

ATOM
2536
C
TYR
A
270
84.385
25.405
32.631
1.00
29.08

ATOM
2537
O
TYR
A
270
84.034
25.836
33.729
1.00
28.17

ATOM
2538
N
GLN
A
271
83.609
24.628
31.882
1.00
30.32

ATOM
2540
CA
GLN
A
271
82.269
24.249
32.316
1.00
29.24

ATOM
2541
CB
GLN
A
271
81.464
23.689
31.139
1.00
27.20

ATOM
2542
CG
GLN
A
271
79.957
23.680
31.357
1.00
27.60

ATOM
2543
CD
GLN
A
271
79.427
22.387
31.946
1.00
31.03

ATOM
2544
OE1
GLN
A
271
79.982
21.306
31.724
1.00
35.11

ATOM
2545
NE2
GLN
A
271
78.318
22.484
32.668
1.00
28.89

ATOM
2548
C
GLN
A
271
82.329
23.226
33.438
1.00
30.41

ATOM
2549
O
GLN
A
271
81.839
23.473
34.539
1.00
32.81

ATOM
2550
N
GLU
A
272
82.976
22.098
33.168
1.00
33.61

ATOM
2552
CA
GLU
A
272
83.096
21.011
34.133
1.00
36.97

ATOM
2553
CB
GLU
A
272
83.807
19.822
33.492
1.00
40.58

ATOM
2554
CG
GLU
A
272
83.084
19.264
32.274
1.00
48.51

ATOM
2555
CD
GLU
A
272
83.781
18.051
31.674
1.00
55.01

ATOM
2556
OE1
GLU
A
272
84.998
18.129
31.405
1.00
59.64

ATOM
2557
OE2
GLU
A
272
83.112
17.016
31.468
1.00
57.25

ATOM
2558
C
GLU
A
272
83.761
21.376
35.460
1.00
36.60

ATOM
2559
O
GLU
A
272
83.674
20.622
36.425
1.00
40.35

ATOM
2560
N
ALA
A
273
84.429
22.522
35.512
1.00
35.77

ATOM
2562
CA
ALA
A
273
85.079
22.970
36.741
1.00
34.34

ATOM
2563
CB
ALA
A
273
86.316
23.798
36.418
1.00
32.87

ATOM
2564
C
ALA
A
273
84.104
23.778
37.594
1.00
34.54

ATOM
2565
O
ALA
A
273
84.459
24.252
38.679
1.00
35.72

ATOM
2566
N
GLY
A
274
82.879
23.930
37.086
1.00
35.04

ATOM
2568
CA
GLY
A
274
81.831
24.663
37.779
1.00
35.01

ATOM
2569
C
GLY
A
274
82.092
26.147
37.930
1.00
34.45

ATOM
2570
O
GLY
A
274
81.640
26.761
38.897
1.00
36.89

ATOM
2571
N
VAL
A
275
82.752
26.742
36.944
1.00
34.05

ATOM
2573
CA
VAL
A
275
83.083
28.157
37.018
1.00
34.43

ATOM
2574
CB
VAL
A
275
84.600
28.381
36.778
1.00
35.67

ATOM
2575
CG1
VAL
A
275
84.898
28.616
35.308
1.00
37.90

ATOM
2576
CG2
VAL
A
275
85.105
29.519
37.638
1.00
38.34

ATOM
2577
C
VAL
A
275
82.236
29.078
36.135
1.00
33.65

ATOM
2578
O
VAL
A
275
82.211
30.286
36.343
1.00
35.12

ATOM
2579
N
LEU
A
276
81.527
28.523
35.159
1.00
32.82

ATOM
2581
CA
LEU
A
276
80.683
29.352
34.307
1.00
29.38

ATOM
2582
CB
LEU
A
276
80.478
28.695
32.936
1.00
27.64

ATOM
2583
CG
LEU
A
276
81.739
28.482
32.082
1.00
25.37

ATOM
2584
CD1
LEU
A
276
81.370
27.883
30.757
1.00
24.34

ATOM
2585
CD2
LEU
A
276
82.459
29.793
31.858
1.00
28.39

ATOM
2586
C
LEU
A
276
79.363
29.548
35.049
1.00
29.83

ATOM
2587
O
LEU
A
276
78.323
29.007
34.674
1.00
30.32

ATOM
2588
N
LYS
A
277
79.443
30.271
36.158
1.00
29.10

ATOM
2590
CA
LYS
A
277
78.294
30.546
37.004
1.00
27.79

ATOM
2591
CB
LYS
A
277
78.327
29.656
38.246
1.00
29.34

ATOM
2592
CG
LYS
A
277
78.211
28.183
37.956
1.00
33.13

ATOM
2593
CD
LYS
A
277
78.269
27.369
39.230
1.00
39.28

ATOM
2594
CE
LYS
A
277
78.064
25.888
38.930
1.00
44.23

ATOM
2595
NZ
LYS
A
277
78.321
25.022
40.119
1.00
46.99

ATOM
2599
C
LYS
A
277
78.386
32.002
37.420
1.00
26.55

ATOM
2600
O
LYS
A
277
79.474
32.556
37.516
1.00
28.05

ATOM
2601
N
MET
A
278
77.251
32.608
37.723
1.00
25.90

ATOM
2603
CA
MET
A
278
77.251
33.999
38.111
1.00
26.31

ATOM
2604
CB
MET
A
278
77.350
34.854
36.864
1.00
25.28

ATOM
2605
CG
MET
A
278
77.496
36.310
37.129
1.00
30.09

ATOM
2606
SD
MET
A
278
77.760
37.127
35.586
1.00
37.76

ATOM
2607
CE
MET
A
278
77.452
38.822
36.056
1.00
34.82

ATOM
2608
C
MET
A
278
75.985
34.338
38.872
1.00
28.79

ATOM
2609
O
MET
A
278
74.910
33.858
38.533
1.00
30.81

ATOM
2610
N
THR
A
279
76.123
35.134
39.925
1.00
30.03

ATOM
2612
CA
THR
A
279
74.987
35.544
40.728
1.00
29.69

ATOM
2613
CB
THR
A
279
75.242
35.277
42.211
1.00
29.00

ATOM
2614
OG1
THR
A
279
75.286
33.864
42.431
1.00
31.54

ATOM
2616
CG2
THR
A
279
74.140
35.863
43.060
1.00
28.67

ATOM
2617
C
THR
A
279
74.714
37.025
40.515
1.00
31.93

ATOM
2618
O
THR
A
279
75.615
37.856
40.644
1.00
32.91

ATOM
2619
N
LEU
A
280
73.482
37.338
40.128
1.00
33.14

ATOM
2621
CA
LEU
A
280
73.062
38.715
39.893
1.00
33.77

ATOM
2622
CB
LEU
A
280
72.268
38.826
38.581
1.00
34.16

ATOM
2623
CG
LEU
A
280
72.930
38.757
37.194
1.00
33.72

ATOM
2624
CD1
LEU
A
280
74.391
38.394
37.271
1.00
33.08

ATOM
2625
CD2
LEU
A
280
72.186
37.766
36.333
1.00
30.96

ATOM
2626
C
LEU
A
280
72.196
39.173
41.064
1.00
35.73

ATOM
2627
O
LEU
A
280
71.223
38.508
41.438
1.00
33.09

ATOM
2628
N
ARG
A
281
72.584
40.290
41.666
1.00
39.95

ATOM
2630
CA
ARG
A
281
71.864
40.860
42.796
1.00
42.55

ATOM
2631
CB
ARG
A
281
72.823
41.091
43.975
1.00
44.48

ATOM
2632
CG
ARG
A
281
73.472
39.824
44.534
1.00
47.55

ATOM
2633
CD
ARG
A
281
74.406
40.109
45.712
1.00
50.80

ATOM
2634
NE
ARG
A
281
75.660
40.757
45.321
1.00
57.47

ATOM
2636
CZ
ARG
A
281
76.844
40.145
45.263
1.00
61.45

ATOM
2637
NH1
ARG
A
281
76.956
38.852
45.552
1.00
62.83

ATOM
2640
NH2
ARG
A
281
77.925
40.825
44.901
1.00
62.95

ATOM
2643
C
ARG
A
281
71.255
42.190
42.354
1.00
44.72

ATOM
2644
O
ARG
A
281
71.782
42.854
41.458
1.00
46.61

ATOM
2645
N
ASP
A
282
70.179
42.601
43.014
1.00
46.42

ATOM
2647
CA
ASP
A
282
69.491
43.849
42.702
1.00
47.87

ATOM
2648
CB
ASP
A
282
68.284
44.039
43.634
1.00
49.38

ATOM
2649
CG
ASP
A
282
67.472
45.280
43.302
1.00
51.57

ATOM
2650
OD1
ASP
A
282
66.898
45.349
42.195
1.00
54.37

ATOM
2651
OD2
ASP
A
282
67.408
46.191
44.150
1.00
54.52

ATOM
2652
C
ASP
A
282
70.394
45.080
42.762
1.00
48.67

ATOM
2653
O
ASP
A
282
70.090
46.089
42.141
1.00
51.13

ATOM
2654
N
ASP
A
283
71.506
44.996
43.488
1.00
49.71

ATOM
2656
CA
ASP
A
283
72.427
46.128
43.608
1.00
50.78

ATOM
2657
CB
ASP
A
283
73.111
46.138
44.987
1.00
52.25

ATOM
2658
CG
ASP
A
283
73.994
44.920
45.224
1.00
55.58

ATOM
2659
OD1
ASP
A
283
75.189
44.953
44.847
1.00
58.60

ATOM
2660
OD2
ASP
A
283
73.498
43.935
45.810
1.00
58.13

ATOM
2661
C
ASP
A
283
73.474
46.236
42.492
1.00
51.35

ATOM
2662
O
ASP
A
283
74.362
47.086
42.543
1.00
52.74

ATOM
2663
N
MET
A
284
73.395
45.359
41.500
1.00
51.07

ATOM
2665
CA
MET
A
284
74.342
45.404
40.399
1.00
50.50

ATOM
2666
CB
MET
A
284
74.629
43.994
39.887
1.00
48.87

ATOM
2667
CG
MET
A
284
75.169
43.058
40.956
1.00
46.76

ATOM
2668
SD
MET
A
284
75.494
41.398
40.353
1.00
43.76

ATOM
2669
CE
MET
A
284
76.804
40.895
41.457
1.00
47.06

ATOM
2670
C
MET
A
284
73.775
46.283
39.289
1.00
53.22

ATOM
2671
O
MET
A
284
74.515
46.824
38.466
1.00
55.85

ATOM
2672
N
ILE
A
285
72.455
46.433
39.285
1.00
55.37

ATOM
2674
CA
ILE
A
285
71.761
47.252
38.295
1.00
57.52

ATOM
2675
CB
ILE
A
285
70.287
46.792
38.141
1.00
55.38

ATOM
2676
CG2
ILE
A
285
69.583
47.611
37.070
1.00
56.70

ATOM
2677
CG1
ILE
A
285
70.235
45.303
37.783
1.00
53.28

ATOM
2678
CD1
ILE
A
285
68.838
44.723
37.732
1.00
50.41

ATOM
2679
C
ILE
A
285
71.787
48.707
38.776
1.00
59.50

ATOM
2680
O
ILE
A
285
71.358
48.998
39.889
1.00
60.66

ATOM
2681
N
PRO
A
286
72.304
49.635
37.951
1.00
61.05

ATOM
2682
CD
PRO
A
286
72.787
49.459
36.573
1.00
61.08

ATOM
2683
CA
PRO
A
286
72.360
51.048
38.350
1.00
62.59

ATOM
2684
CB
PRO
A
286
72.862
51.748
37.083
1.00
62.24

ATOM
2685
CG
PRO
A
286
72.481
50.801
35.974
1.00
63.04

ATOM
2686
C
PRO
A
286
71.004
51.583
38.817
1.00
64.15

ATOM
2687
O
PRO
A
286
69.986
51.400
38.154
1.00
63.39

ATOM
2688
N
LYS
A
287
71.016
52.268
39.956
1.00
67.25

ATOM
2690
CA
LYS
A
287
69.813
52.826
40.582
1.00
69.68

ATOM
2691
CB
LYS
A
287
70.204
53.622
41.838
1.00
72.51

ATOM
2692
CG
LYS
A
287
71.285
54.675
41.607
1.00
75.76

ATOM
2693
CD
LYS
A
287
71.483
55.570
42.826
1.00
78.18

ATOM
2694
CE
LYS
A
287
72.474
56.697
42.534
1.00
79.24

ATOM
2695
NZ
LYS
A
287
72.603
57.663
43.666
1.00
79.25

ATOM
2699
C
LYS
A
287
68.845
53.653
39.724
1.00
69.37

ATOM
2700
O
LYS
A
287
67.735
53.962
40.165
1.00
69.08

ATOM
2701
N
GLU
A
288
69.242
53.996
38.505
1.00
68.49

ATOM
2703
CA
GLU
A
288
68.386
54.792
37.635
1.00
69.17

ATOM
2704
CB
GLU
A
288
69.152
56.004
37.094
1.00
70.77

ATOM
2705
CG
GLU
A
288
69.897
56.826
38.142
1.00
73.92

ATOM
2706
CD
GLU
A
288
71.290
56.292
38.461
1.00
76.03

ATOM
2707
OE1
GLU
A
288
71.656
55.195
37.983
1.00
78.84

ATOM
2708
OE2
GLU
A
288
72.031
56.981
39.196
1.00
76.47

ATOM
2709
C
GLU
A
288
67.851
53.965
36.469
1.00
68.68

ATOM
2710
O
GLU
A
288
68.012
54.345
35.310
1.00
70.05

ATOM
2711
N
SER
A
289
67.194
52.852
36.772
1.00
68.09

ATOM
2713
CA
SER
A
289
66.655
51.985
35.727
1.00
67.82

ATOM
2714
CB
SER
A
289
67.516
50.728
35.593
1.00
69.68

ATOM
2715
OG
SER
A
289
68.868
51.064
35.327
1.00
73.68

ATOM
2717
C
SER
A
289
65.202
51.590
35.977
1.00
66.67

ATOM
2718
O
SER
A
289
64.695
51.730
37.090
1.00
67.98

ATOM
2719
N
ALA
A
290
64.537
51.110
34.928
1.00
63.49

ATOM
2721
CA
ALA
A
290
63.144
50.691
35.027
1.00
60.33

ATOM
2722
CB
ALA
A
290
62.525
50.598
33.644
1.00
60.15

ATOM
2723
C
ALA
A
290
63.026
49.353
35.744
1.00
58.83

ATOM
2724
O
ALA
A
290
62.236
49.208
36.673
1.00
59.19

ATOM
2725
N
PHE
A
291
63.839
48.390
35.321
1.00
57.41

ATOM
2727
CA
PHE
A
291
63.829
47.043
35.894
1.00
55.46

ATOM
2728
CB
PHE
A
291
64.441
46.044
34.902
1.00
54.51

ATOM
2729
CG
PHE
A
291
63.658
45.890
33.622
1.00
52.78

ATOM
2730
CD1
PHE
A
291
62.493
45.130
33.588
1.00
52.76

ATOM
2731
CD2
PHE
A
291
64.085
46.505
32.451
1.00
52.05

ATOM
2732
CE1
PHE
A
291
61.760
44.983
32.414
1.00
51.50

ATOM
2733
CE2
PHE
A
291
63.360
46.364
31.270
1.00
52.10

ATOM
2734
CZ
PHE
A
291
62.194
45.601
31.255
1.00
51.58

ATOM
2735
C
PHE
A
291
64.519
46.912
37.260
1.00
53.52

ATOM
2736
O
PHE
A
291
65.541
47.547
37.524
1.00
53.59

ATOM
2737
N
ARG
A
292
63.966
46.046
38.104
1.00
50.17

ATOM
2739
CA
ARG
A
292
64.494
45.799
39.438
1.00
46.66

ATOM
2740
CB
ARG
A
292
63.677
46.562
40.481
1.00
46.93

ATOM
2741
CG
ARG
A
292
63.793
48.065
40.434
1.00
47.97

ATOM
2742
CD
ARG
A
292
64.964
48.536
41.256
1.00
49.34

ATOM
2743
NE
ARG
A
292
65.959
49.215
40.438
1.00
51.19

ATOM
2745
CZ
ARG
A
292
67.266
48.993
40.521
1.00
52.32

ATOM
2746
NH1
ARG
A
292
67.735
48.102
41.385
1.00
52.06

ATOM
2749
NH2
ARG
A
292
68.106
49.674
39.750
1.00
52.32

ATOM
2752
C
ARG
A
292
64.317
44.322
39.715
1.00
46.15

ATOM
2753
O
ARG
A
292
63.333
43.720
39.278
1.00
47.65

ATOM
2754
N
LEU
A
293
65.278
43.725
40.409
1.00
44.69

ATOM
2756
CA
LEU
A
293
65.169
42.320
40.769
1.00
42.76

ATOM
2757
CB
LEU
A
293
66.546
41.648
40.819
1.00
37.95

ATOM
2758
CG
LEU
A
293
67.252
41.569
39.468
1.00
34.56

ATOM
2759
CD1
LEU
A
293
68.649
41.034
39.630
1.00
33.82

ATOM
2760
CD2
LEU
A
293
66.459
40.692
38.537
1.00
32.43

ATOM
2761
C
LEU
A
293
64.516
42.349
42.141
1.00
44.58

ATOM
2762
O
LEU
A
293
65.169
42.154
43.164
1.00
46.89

ATOM
2763
N
THR
A
294
63.239
42.716
42.150
1.00
44.93

ATOM
2765
CA
THR
A
294
62.453
42.804
43.370
1.00
45.20

ATOM
2766
CB
THR
A
294
62.220
44.271
43.781
1.00
44.99

ATOM
2767
OG1
THR
A
294
61.502
44.955
42.748
1.00
45.39

ATOM
2769
CG2
THR
A
294
63.547
44.983
44.012
1.00
46.79

ATOM
2770
C
THR
A
294
61.111
42.175
43.055
1.00
46.49

ATOM
2771
O
THR
A
294
60.639
42.269
41.922
1.00
48.98

ATOM
2772
N
THR
A
295
60.500
41.520
44.035
1.00
47.36

ATOM
2774
CA
THR
A
295
59.204
40.892
43.812
1.00
48.40

ATOM
2775
CB
THR
A
295
58.720
40.139
45.063
1.00
47.45

ATOM
2776
OG1
THR
A
295
58.837
40.986
46.210
1.00
47.38

ATOM
2778
CG2
THR
A
295
59.550
38.891
45.287
1.00
47.66

ATOM
2779
C
THR
A
295
58.179
41.952
43.410
1.00
49.59

ATOM
2780
O
THR
A
295
57.292
41.693
42.599
1.00
50.18

ATOM
2781
N
SER
A
296
58.347
43.157
43.950
1.00
51.29

ATOM
2783
CA
SER
A
296
57.468
44.288
43.667
1.00
52.78

ATOM
2784
CB
SER
A
296
57.978
45.538
44.390
1.00
54.54

ATOM
2785
OG
SER
A
296
57.219
46.688
44.056
1.00
55.48

ATOM
2787
C
SER
A
296
57.412
44.551
42.172
1.00
52.76

ATOM
2788
O
SER
A
296
56.340
44.532
41.562
1.00
52.27

ATOM
2789
N
PHE
A
297
58.579
44.779
41.583
1.00
52.83

ATOM
2791
CA
PHE
A
297
58.656
45.033
40.160
1.00
53.94

ATOM
2792
CB
PHE
A
297
60.093
45.286
39.730
1.00
55.28

ATOM
2793
CG
PHE
A
297
60.217
45.651
38.293
1.00
57.93

ATOM
2794
CD1
PHE
A
297
60.028
46.964
37.884
1.00
57.66

ATOM
2795
CD2
PHE
A
297
60.459
44.673
37.334
1.00
59.49

ATOM
2796
CE1
PHE
A
297
60.072
47.299
36.539
1.00
59.28

ATOM
2797
CE2
PHE
A
297
60.503
44.997
35.990
1.00
59.71

ATOM
2798
CZ
PHE
A
297
60.309
46.315
35.590
1.00
59.93

ATOM
2799
C
PHE
A
297
58.090
43.837
39.408
1.00
54.31

ATOM
2800
O
PHE
A
297
57.245
43.990
38.530
1.00
54.87

ATOM
2801
N
PHE
A
298
58.542
42.643
39.776
1.00
55.31

ATOM
2803
CA
PHE
A
298
58.058
41.420
39.149
1.00
55.92

ATOM
2804
CB
PHE
A
298
58.793
40.199
39.709
1.00
52.95

ATOM
2805
CG
PHE
A
298
60.118
39.943
39.057
1.00
49.79

ATOM
2806
CD1
PHE
A
298
61.094
40.934
39.019
1.00
46.14

ATOM
2807
CD2
PHE
A
298
60.384
38.716
38.463
1.00
47.97

ATOM
2808
CE1
PHE
A
298
62.312
40.709
38.400
1.00
44.36

ATOM
2809
CE2
PHE
A
298
61.600
38.482
37.842
1.00
46.94

ATOM
2810
CZ
PHE
A
298
62.567
39.482
37.810
1.00
45.78

ATOM
2811
C
PHE
A
298
56.556
41.274
39.364
1.00
58.12

ATOM
2812
O
PHE
A
298
55.904
40.453
38.716
1.00
58.39

ATOM
2813
N
GLY
A
299
56.019
42.067
40.287
1.00
60.34

ATOM
2815
CA
GLY
A
299
54.599
42.042
40.576
1.00
62.61

ATOM
2816
C
GLY
A
299
53.777
42.541
39.404
1.00
64.03

ATOM
2817
O
GLY
A
299
52.622
42.156
39.236
1.00
64.07

ATOM
2818
N
THR
A
300
54.377
43.379
38.571
1.00
65.39

ATOM
2820
CA
THR
A
300
53.672
43.904
37.416
1.00
67.18

ATOM
2821
CB
THR
A
300
54.532
44.935
36.658
1.00
66.57

ATOM
2822
OG1
THR
A
300
55.806
44.361
36.349
1.00
67.61

ATOM
2824
CG2
THR
A
300
54.736
46.181
37.503
1.00
67.44

ATOM
2825
C
THR
A
300
53.258
42.785
36.460
1.00
69.21

ATOM
2826
O
THR
A
300
52.234
42.896
35.777
1.00
72.16

ATOM
2827
N
PHE
A
301
54.055
41.774
36.384
1.00
69.34

ATOM
2829
CA
PHE
A
301
53.704
40.675
35.483
1.00
69.26

ATOM
2830
CB
PHE
A
301
54.608
40.680
34.241
1.00
66.47

ATOM
2831
CG
PHE
A
301
56.070
40.882
34.532
1.00
64.06

ATOM
2832
CD1
PHE
A
301
56.629
42.154
34.478
1.00
62.60

ATOM
2833
CD2
PHE
A
301
56.895
39.806
34.838
1.00
63.14

ATOM
2834
CE1
PHE
A
301
57.983
42.354
34.716
1.00
61.30

ATOM
2835
CE2
PHE
A
301
58.251
39.995
35.077
1.00
61.28

ATOM
2836
CZ
PHE
A
301
58.795
41.274
35.016
1.00
61.18

ATOM
2837
C
PHE
A
301
53.635
39.268
36.062
1.00
71.49

ATOM
2838
O
PHE
A
301
53.032
38.380
35.458
1.00
71.98

ATOM
2839
N
LEU
A
302
54.199
39.072
37.250
1.00
74.67

ATOM
2841
CA
LEU
A
302
54.198
37.748
37.866
1.00
77.56

ATOM
2842
CB
LEU
A
302
55.573
37.098
37.698
1.00
75.96

ATOM
2843
CG
LEU
A
302
55.833
36.472
36.337
1.00
75.33

ATOM
2844
CD1
LEU
A
302
57.217
35.860
36.332
1.00
75.78

ATOM
2845
CD2
LEU
A
302
54.767
35.425
36.070
1.00
74.63

ATOM
2846
C
LEU
A
302
53.782
37.667
39.338
1.00
80.50

ATOM
2847
O
LEU
A
302
54.567
37.228
40.173
1.00
81.63

ATOM
2848
N
PRO
A
303
52.551
38.075
39.678
1.00
82.47

ATOM
2849
CD
PRO
A
303
51.687
39.012
38.927
1.00
83.87

ATOM
2850
CA
PRO
A
303
52.127
38.002
41.087
1.00
82.85

ATOM
2851
CB
PRO
A
303
51.725
39.440
41.359
1.00
83.29

ATOM
2852
CG
PRO
A
303
50.963
39.803
40.046
1.00
84.24

ATOM
2853
C
PRO
A
303
50.924
37.070
41.346
1.00
82.81

ATOM
2854
O
PRO
A
303
49.809
37.403
40.953
1.00
84.47

ATOM
2855
N
GLU
A
304
51.087
35.893
41.943
1.00
81.68

ATOM
2857
CA
GLU
A
304
52.308
35.254
42.438
1.00
80.61

ATOM
2858
CB
GLU
A
304
52.767
34.203
41.437
1.00
83.61

ATOM
2859
CG
GLU
A
304
51.698
33.132
41.207
1.00
86.52

ATOM
2860
CD
GLU
A
304
51.179
32.502
42.499
1.00
88.36

ATOM
2861
OE1
GLU
A
304
50.103
32.923
42.977
1.00
89.84

ATOM
2862
OE2
GLU
A
304
51.847
31.594
43.036
1.00
89.41

ATOM
2863
C
GLU
A
304
53.501
35.887
43.175
1.00
78.52

ATOM
2864
O
GLU
A
304
53.383
36.142
44.361
1.00
78.12

ATOM
2865
N
VAL
A
305
54.817
36.106
42.616
1.00
76.19

ATOM
2867
CA
VAL
A
305
55.955
36.809
43.226
1.00
74.85

ATOM
2868
CB
VAL
A
305
56.904
37.447
42.170
1.00
74.41

ATOM
2869
CG1
VAL
A
305
57.405
36.392
41.202
1.00
74.39

ATOM
2870
CG2
VAL
A
305
56.218
38.578
41.433
1.00
75.20

ATOM
2871
C
VAL
A
305
55.622
37.833
44.316
1.00
74.68

ATOM
2872
O
VAL
A
305
56.110
37.711
45.438
1.00
75.57

ATOM
2873
N
ALA
A
306
54.746
38.790
44.011
1.00
73.53

ATOM
2875
CA
ALA
A
306
54.357
39.823
44.975
1.00
71.77

ATOM
2876
CB
ALA
A
306
53.893
41.068
44.248
1.00
71.20

ATOM
2877
C
ALA
A
306
53.273
39.348
45.935
1.00
71.50

ATOM
2878
O
ALA
A
306
53.087
39.924
47.005
1.00
70.71

ATOM
2879
N
LYS
A
307
52.563
38.300
45.529
1.00
71.78

ATOM
2881
CA
LYS
A
307
51.474
37.697
46.300
1.00
71.82

ATOM
2882
CB
LYS
A
307
50.508
37.010
45.324
1.00
72.68

ATOM
2883
CG
LYS
A
307
49.332
36.270
45.944
1.00
75.23

ATOM
2884
CD
LYS
A
307
48.473
35.638
44.848
1.00
76.97

ATOM
2885
CE
LYS
A
307
47.247
34.935
45.413
1.00
77.90

ATOM
2886
NZ
LYS
A
307
46.352
34.434
44.331
1.00
77.64

ATOM
2890
C
LYS
A
307
51.946
36.698
47.374
1.00
71.04

ATOM
2891
O
LYS
A
307
51.393
36.651
48.473
1.00
72.05

ATOM
2892
N
LYS
A
308
52.958
35.898
47.050
1.00
69.00

ATOM
2894
CA
LYS
A
308
53.480
34.903
47.979
1.00
66.59

ATOM
2895
CB
LYS
A
308
53.891
33.636
47.219
1.00
70.09

ATOM
2896
CG
LYS
A
308
53.887
32.346
48.046
1.00
75.24

ATOM
2897
CD
LYS
A
308
54.920
32.351
49.172
1.00
79.31

ATOM
2898
CE
LYS
A
308
54.842
31.091
50.027
1.00
81.43

ATOM
2899
NZ
LYS
A
308
55.760
31.141
51.206
1.00
82.05

ATOM
2903
C
LYS
A
308
54.680
35.467
48.722
1.00
64.17

ATOM
2904
O
LYS
A
308
54.840
35.240
49.921
1.00
65.45

ATOM
2905
N
PHE
A
309
55.526
36.200
48.007
1.00
60.99

ATOM
2907
CA
PHE
A
309
56.725
36.784
48.597
1.00
57.85

ATOM
2908
CB
PHE
A
309
57.974
36.274
47.853
1.00
53.07

ATOM
2909
CG
PHE
A
309
58.085
34.762
47.808
1.00
45.45

ATOM
2910
CD1
PHE
A
309
58.551
34.050
48.906
1.00
42.52

ATOM
2911
CD2
PHE
A
309
57.689
34.052
46.679
1.00
43.68

ATOM
2912
CE1
PHE
A
309
58.619
32.655
48.883
1.00
38.70

ATOM
2913
CE2
PHE
A
309
57.754
32.655
46.647
1.00
42.05

ATOM
2914
CZ
PHE
A
309
58.219
31.959
47.753
1.00
39.93

ATOM
2915
C
PHE
A
309
56.616
38.312
48.553
1.00
58.92

ATOM
2916
O
PHE
A
309
57.266
38.978
47.743
1.00
58.89

ATOM
2917
N
PRO
A
310
55.822
38.885
49.472
1.00
60.26

ATOM
2918
CD
PRO
A
310
55.173
38.142
50.569
1.00
61.34

ATOM
2919
CA
PRO
A
310
55.560
40.320
49.613
1.00
61.10

ATOM
2920
CB
PRO
A
310
54.522
40.358
50.736
1.00
62.64

ATOM
2921
CG
PRO
A
310
54.934
39.217
51.598
1.00
61.52

ATOM
2922
C
PRO
A
310
56.737
41.239
49.927
1.00
61.05

ATOM
2923
O
PRO
A
310
57.307
41.187
51.016
1.00
61.70

ATOM
2924
N
ASN
A
311
57.044
42.121
48.979
1.00
62.21

ATOM
2926
CA
ASN
A
311
58.116
43.111
49.111
1.00
63.11

ATOM
2927
CB
ASN
A
311
57.667
44.247
50.037
1.00
66.59

ATOM
2928
CG
ASN
A
311
58.589
45.448
49.976
1.00
69.63

ATOM
2929
OD1
ASN
A
311
58.596
46.186
48.991
1.00
71.72

ATOM
2930
ND2
ASN
A
311
59.373
45.651
51.027
1.00
71.51

ATOM
2933
C
ASN
A
311
59.458
42.547
49.583
1.00
61.81

ATOM
2934
O
ASN
A
311
59.855
42.737
50.738
1.00
63.25

ATOM
2935
N
MET
A
312
60.155
41.870
48.673
1.00
58.63

ATOM
2937
CA
MET
A
312
61.459
41.266
48.950
1.00
53.64

ATOM
2938
CB
MET
A
312
61.316
39.768
49.269
1.00
53.53

ATOM
2939
CG
MET
A
312
60.599
39.405
50.570
1.00
52.28

ATOM
2940
SD
MET
A
312
60.259
37.617
50.633
1.00
52.18

ATOM
2941
CE
MET
A
312
58.896
37.534
51.788
1.00
54.70

ATOM
2942
C
MET
A
312
62.320
41.411
47.699
1.00
49.72

ATOM
2943
O
MET
A
312
61.801
41.656
46.605
1.00
49.26

ATOM
2944
N
LYS
A
313
63.630
41.275
47.865
1.00
44.80

ATOM
2946
CA
LYS
A
313
64.549
41.363
46.741
1.00
41.81

ATOM
2947
CB
LYS
A
313
65.952
41.707
47.230
1.00
42.38

ATOM
2948
CG
LYS
A
313
66.050
43.081
47.846
1.00
47.04

ATOM
2949
CD
LYS
A
313
65.762
44.159
46.818
1.00
49.35

ATOM
2950
CE
LYS
A
313
65.599
45.515
47.481
1.00
53.10

ATOM
2951
NZ
LYS
A
313
66.805
45.897
48.268
1.00
56.75

ATOM
2955
C
LYS
A
313
64.562
40.018
46.026
1.00
39.61

ATOM
2956
O
LYS
A
313
64.133
39.013
46.592
1.00
38.93

ATOM
2957
N
ILE
A
314
65.040
40.005
44.786
1.00
37.30

ATOM
2959
CA
ILE
A
314
65.115
38.785
43.995
1.00
34.17

ATOM
2960
CB
ILE
A
314
64.224
38.865
42.716
1.00
33.93

ATOM
2961
CG2
ILE
A
314
64.607
37.783
41.708
1.00
32.86

ATOM
2962
CG1
ILE
A
314
62.745
38.728
43.093
1.00
33.03

ATOM
2963
CD1
ILE
A
314
61.824
38.459
41.920
1.00
32.90

ATOM
2964
C
ILE
A
314
66.567
38.565
43.604
1.00
33.46

ATOM
2965
O
ILE
A
314
67.272
39.512
43.271
1.00
32.77

ATOM
2966
N
GLN
A
315
67.024
37.321
43.698
1.00
32.44

ATOM
2968
CA
GLN
A
315
68.391
36.975
43.336
1.00
32.66

ATOM
2969
CB
GLN
A
315
69.118
36.366
44.529
1.00
34.35

ATOM
2970
CG
GLN
A
315
70.624
36.305
44.376
1.00
35.08

ATOM
2971
CD
GLN
A
315
71.317
35.839
45.639
1.00
33.95

ATOM
2972
OE1
GLN
A
315
71.579
36.620
46.548
1.00
34.44

ATOM
2973
NE2
GLN
A
315
71.607
34.554
45.701
1.00
37.53

ATOM
2976
C
GLN
A
315
68.307
35.964
42.207
1.00
33.04

ATOM
2977
O
GLN
A
315
67.520
35.024
42.271
1.00
35.05

ATOM
2978
N
ILE
A
316
69.116
36.155
41.175
1.00
34.76

ATOM
2980
CA
ILE
A
316
69.106
35.268
40.018
1.00
33.81

ATOM
2981
CB
ILE
A
316
68.711
36.067
38.750
1.00
35.72

ATOM
2982
CG2
ILE
A
316
68.944
35.247
37.498
1.00
37.16

ATOM
2983
CG1
ILE
A
316
67.249
36.518
38.864
1.00
36.98

ATOM
2984
CD1
ILE
A
316
66.695
37.179
37.633
1.00
38.34

ATOM
2985
C
ILE
A
316
70.445
34.548
39.823
1.00
32.92

ATOM
2986
O
ILE
A
316
71.513
35.160
39.900
1.00
33.03

ATOM
2987
N
HIS
A
317
70.386
33.238
39.609
1.00
33.55

ATOM
2989
CA
HIS
A
317
71.586
32.428
39.409
1.00
32.00

ATOM
2990
CB
HIS
A
317
71.532
31.162
40.264
1.00
32.50

ATOM
2991
CG
HIS
A
317
71.659
31.411
41.735
1.00
32.14

ATOM
2992
CD2
HIS
A
317
71.889
32.548
42.435
1.00
31.63

ATOM
2993
ND1
HIS
A
317
71.572
30.398
42.666
1.00
32.81

ATOM
2995
CE1
HIS
A
317
71.746
30.899
43.875
1.00
33.94

ATOM
2996
NE2
HIS
A
317
71.941
32.201
43.761
1.00
32.58

ATOM
2998
C
HIS
A
317
71.720
32.014
37.953
1.00
33.04

ATOM
2999
O
HIS
A
317
70.844
31.335
37.416
1.00
33.39

ATOM
3000
N
VAL
A
318
72.842
32.377
37.344
1.00
33.42

ATOM
3002
CA
VAL
A
318
73.129
32.059
35.952
1.00
31.61

ATOM
3003
CB
VAL
A
318
73.535
33.338
35.193
1.00
29.43

ATOM
3004
CG1
VAL
A
318
73.993
33.003
33.789
1.00
30.90

ATOM
3005
CG2
VAL
A
318
72.376
34.311
35.161
1.00
27.51

ATOM
3006
C
VAL
A
318
74.273
31.043
35.861
1.00
32.81

ATOM
3007
O
VAL
A
318
75.392
31.325
36.296
1.00
33.30

ATOM
3008
N
SER
A
319
73.990
29.858
35.329
1.00
32.14

ATOM
3010
CA
SER
A
319
75.021
28.836
35.175
1.00
32.12

ATOM
3011
CB
SER
A
319
74.919
27.778
36.271
1.00
28.41

ATOM
3012
OG
SER
A
319
73.723
27.039
36.158
1.00
29.90

ATOM
3014
C
SER
A
319
74.900
28.170
33.815
1.00
33.52

ATOM
3015
O
SER
A
319
73.834
28.174
33.210
1.00
37.50

ATOM
3016
N
ALA
A
320
76.005
27.632
33.319
1.00
35.33

ATOM
3018
CA
ALA
A
320
76.009
26.958
32.031
1.00
35.02

ATOM
3019
CB
ALA
A
320
77.417
26.914
31.461
1.00
36.41

ATOM
3020
C
ALA
A
320
75.466
25.547
32.210
1.00
36.23

ATOM
3021
O
ALA
A
320
75.955
24.786
33.047
1.00
35.14

ATOM
3022
N
SER
A
321
74.459
25.204
31.415
1.00
38.15

ATOM
3024
CA
SER
A
321
73.835
23.891
31.478
1.00
38.99

ATOM
3025
CB
SER
A
321
72.472
23.935
30.786
1.00
38.78

ATOM
3026
OG
SER
A
321
72.418
24.984
29.834
1.00
40.20

ATOM
3028
C
SER
A
321
74.724
22.824
30.848
1.00
40.78

ATOM
3029
O
SER
A
321
74.942
21.760
31.430
1.00
44.24

ATOM
3030
N
THR
A
322
75.249
23.126
29.666
1.00
39.66

ATOM
3032
CA
THR
A
322
76.119
22.214
28.939
1.00
36.30

ATOM
3033
CB
THR
A
322
75.355
21.553
27.750
1.00
39.80

ATOM
3034
OG1
THR
A
322
74.613
22.548
27.027
1.00
40.24

ATOM
3036
CG2
THR
A
322
74.398
20.473
28.253
1.00
41.99

ATOM
3037
C
THR
A
322
77.332
22.985
28.416
1.00
33.41

ATOM
3038
O
THR
A
322
77.372
24.214
28.487
1.00
31.80

ATOM
3039
N
PRO
A
323
78.378
22.272
27.966
1.00
32.97

ATOM
3040
CD
PRO
A
323
78.606
20.826
28.133
1.00
31.42

ATOM
3041
CA
PRO
A
323
79.581
22.925
27.439
1.00
31.79

ATOM
3042
CB
PRO
A
323
80.471
21.739
27.089
1.00
31.21

ATOM
3043
CG
PRO
A
323
80.099
20.740
28.128
1.00
31.27

ATOM
3044
C
PRO
A
323
79.279
23.757
26.191
1.00
33.72

ATOM
3045
O
PRO
A
323
78.727
23.237
25.218
1.00
35.68

ATOM
3046
N
PRO
A
324
79.650
25.053
26.196
1.00
34.41

ATOM
3047
CD
PRO
A
324
80.303
25.799
27.286
1.00
34.36

ATOM
3048
CA
PRO
A
324
79.407
25.933
25.050
1.00
36.18

ATOM
3049
CB
PRO
A
324
79.863
27.301
25.567
1.00
34.56

ATOM
3050
CG
PRO
A
324
80.913
26.963
26.551
1.00
34.54

ATOM
3051
C
PRO
A
324
80.186
25.511
23.811
1.00
39.38

ATOM
3052
O
PRO
A
324
81.397
25.278
23.871
1.00
43.04

ATOM
3053
N
HIS
A
325
79.468
25.364
22.704
1.00
39.27

ATOM
3055
CA
HIS
A
325
80.064
24.973
21.434
1.00
39.40

ATOM
3056
CB
HIS
A
325
79.045
24.236
20.562
1.00
44.72

ATOM
3057
CG
HIS
A
325
78.817
22.813
20.955
1.00
49.32

ATOM
3058
CD2
HIS
A
325
79.471
22.015
21.831
1.00
51.91

ATOM
3059
ND1
HIS
A
325
77.817
22.041
20.405
1.00
52.21

ATOM
3061
CE1
HIS
A
325
77.864
20.827
20.924
1.00
53.83

ATOM
3062
NE2
HIS
A
325
78.859
20.785
21.793
1.00
54.25

ATOM
3064
C
HIS
A
325
80.537
26.183
20.658
1.00
37.89

ATOM
3065
O
HIS
A
325
80.011
27.285
20.825
1.00
39.24

ATOM
3066
N
LEU
A
326
81.514
25.958
19.788
1.00
36.12

ATOM
3068
CA
LEU
A
326
82.056
26.993
18.928
1.00
34.45

ATOM
3069
CB
LEU
A
326
83.370
27.535
19.487
1.00
34.16

ATOM
3070
CG
LEU
A
326
83.906
28.758
18.745
1.00
34.49

ATOM
3071
CD1
LEU
A
326
82.912
29.878
18.854
1.00
36.18

ATOM
3072
CD2
LEU
A
326
85.220
29.194
19.321
1.00
38.20

ATOM
3073
C
LEU
A
326
82.285
26.329
17.569
1.00
34.87

ATOM
3074
O
LEU
A
326
82.981
25.311
17.469
1.00
35.31

ATOM
3075
N
SER
A
327
81.639
26.863
16.542
1.00
32.90

ATOM
3077
CA
SER
A
327
81.755
26.323
15.202
1.00
32.76

ATOM
3078
CB
SER
A
327
80.359
26.173
14.591
1.00
34.44

ATOM
3079
OG
SER
A
327
80.390
25.407
13.394
1.00
41.05

ATOM
3081
C
SER
A
327
82.607
27.247
14.343
1.00
30.57

ATOM
3082
O
SER
A
327
82.391
28.458
14.329
1.00
31.41

ATOM
3083
N
VAL
A
328
83.601
26.691
13.658
1.00
29.84

ATOM
3085
CA
VAL
A
328
84.452
27.502
12.795
1.00
28.60

ATOM
3086
CB
VAL
A
328
85.951
27.275
13.056
1.00
25.61

ATOM
3087
CG1
VAL
A
328
86.733
28.389
12.423
1.00
24.98

ATOM
3088
CG2
VAL
A
328
86.245
27.218
14.544
1.00
23.23

ATOM
3089
C
VAL
A
328
84.159
27.174
11.336
1.00
30.19

ATOM
3090
O
VAL
A
328
84.221
26.015
10.928
1.00
29.56

ATOM
3091
N
GLN
A
329
83.791
28.194
10.569
1.00
32.32

ATOM
3093
CA
GLN
A
329
83.479
28.038
9.150
1.00
34.28

ATOM
3094
CB
GLN
A
329
81.956
27.972
8.939
1.00
39.33

ATOM
3095
CG
GLN
A
329
81.222
26.924
9.774
1.00
48.55

ATOM
3096
CD
GLN
A
329
80.246
27.532
10.785
1.00
53.31

ATOM
3097
OE1
GLN
A
329
79.321
26.860
11.245
1.00
57.70

ATOM
3098
NE2
GLN
A
329
80.456
28.796
11.142
1.00
53.89

ATOM
3101
C
GLN
A
329
84.050
29.259
8.416
1.00
32.74

ATOM
3102
O
GLN
A
329
84.337
30.279
9.048
1.00
34.32

ATOM
3103
N
PRO
A
330
84.176
29.193
7.073
1.00
30.85

ATOM
3104
CD
PRO
A
330
83.896
28.019
6.226
1.00
27.63

ATOM
3105
CA
PRO
A
330
84.711
30.301
6.265
1.00
30.72

ATOM
3106
CB
PRO
A
330
84.597
29.765
4.842
1.00
27.09

ATOM
3107
CG
PRO
A
330
84.754
28.286
5.026
1.00
27.10

ATOM
3108
C
PRO
A
330
83.968
31.635
6.416
1.00
33.05

ATOM
3109
O
PRO
A
330
84.501
32.695
6.084
1.00
34.38

ATOM
3110
N
THR
A
331
82.733
31.575
6.904
1.00
36.91

ATOM
3112
CA
THR
A
331
81.918
32.767
7.106
1.00
39.55

ATOM
3113
CB
THR
A
331
80.414
32.414
7.065
1.00
41.23

ATOM
3114
OG1
THR
A
331
80.179
31.221
7.826
1.00
42.58

ATOM
3116
CG2
THR
A
331
79.959
32.180
5.630
1.00
42.18

ATOM
3117
C
THR
A
331
82.244
33.469
8.425
1.00
41.21

ATOM
3118
O
THR
A
331
82.114
34.691
8.535
1.00
44.22

ATOM
3119
N
GLY
A
332
82.671
32.691
9.418
1.00
39.90

ATOM
3121
CA
GLY
A
332
83.005
33.240
10.720
1.00
36.14

ATOM
3122
C
GLY
A
332
82.788
32.188
11.788
1.00
36.29

ATOM
3123
O
GLY
A
332
82.399
31.058
11.472
1.00
36.21

ATOM
3124
N
LEU
A
333
83.048
32.542
13.044
1.00
35.70

ATOM
3126
CA
LEU
A
333
82.875
31.606
14.153
1.00
34.12

ATOM
3127
CB
LEU
A
333
84.037
31.704
15.157
1.00
31.15

ATOM
3128
CG
LEU
A
333
85.438
32.183
14.766
1.00
30.79

ATOM
3129
CD1
LEU
A
333
86.402
31.841
15.886
1.00
29.93

ATOM
3130
CD2
LEU
A
333
85.908
31.539
13.492
1.00
32.11

ATOM
3131
C
LEU
A
333
81.570
31.889
14.889
1.00
34.02

ATOM
3132
O
LEU
A
333
81.283
33.037
15.233
1.00
35.28

ATOM
3133
N
THR
A
334
80.777
30.850
15.123
1.00
32.89

ATOM
3135
CA
THR
A
334
79.521
30.997
15.842
1.00
30.97

ATOM
3136
CB
THR
A
334
78.344
30.435
15.037
1.00
30.40

ATOM
3137
OG1
THR
A
334
78.673
29.124
14.568
1.00
36.09

ATOM
3139
CG2
THR
A
334
78.043
31.324
13.850
1.00
27.87

ATOM
3140
C
THR
A
334
79.649
30.274
17.184
1.00
30.59

ATOM
3141
O
THR
A
334
80.293
29.229
17.267
1.00
31.11

ATOM
3142
N
PHE
A
335
79.052
30.853
18.225
1.00
31.55

ATOM
3144
CA
PHE
A
335
79.095
30.334
19.598
1.00
30.95

ATOM
3145
CB
PHE
A
335
79.579
31.465
20.530
1.00
31.73

ATOM
3146
CG
PHE
A
335
80.138
31.001
21.853
1.00
32.43

ATOM
3147
CD1
PHE
A
335
81.224
30.134
21.907
1.00
34.10

ATOM
3148
CD2
PHE
A
335
79.611
31.483
23.044
1.00
33.32

ATOM
3149
CE1
PHE
A
335
81.779
29.755
23.124
1.00
36.27

ATOM
3150
CE2
PHE
A
335
80.156
31.113
24.267
1.00
36.93

ATOM
3151
CZ
PHE
A
335
81.243
30.248
24.308
1.00
36.83

ATOM
3152
C
PHE
A
335
77.674
29.910
19.975
1.00
29.88

ATOM
3153
O
PHE
A
335
76.722
30.616
19.666
1.00
29.27

ATOM
3154
N
TYR
A
336
77.533
28.779
20.658
1.00
30.87

ATOM
3156
CA
TYR
A
336
76.216
28.281
21.052
1.00
33.87

ATOM
3157
CB
TYR
A
336
75.936
26.953
20.345
1.00
35.86

ATOM
3158
CG
TYR
A
336
76.081
27.036
18.844
1.00
36.58

ATOM
3159
CD1
TYR
A
336
75.107
27.665
18.072
1.00
38.45

ATOM
3160
CE1
TYR
A
336
75.245
27.791
16.700
1.00
38.32

ATOM
3161
CD2
TYR
A
336
77.207
26.526
18.198
1.00
34.97

ATOM
3162
CE2
TYR
A
336
77.357
26.647
16.819
1.00
36.42

ATOM
3163
CZ
TYR
A
336
76.369
27.285
16.078
1.00
37.51

ATOM
3164
OH
TYR
A
336
76.494
27.435
14.715
1.00
41.83

ATOM
3166
C
TYR
A
336
76.104
28.096
22.565
1.00
36.66

ATOM
3167
O
TYR
A
336
76.280
26.988
23.074
1.00
39.11

ATOM
3168
N
PRO
A
337
75.858
29.187
23.309
1.00
36.71

ATOM
3169
CD
PRO
A
337
75.890
30.605
22.904
1.00
36.11

ATOM
3170
CA
PRO
A
337
75.740
29.069
24.761
1.00
35.26

ATOM
3171
CB
PRO
A
337
76.156
30.449
25.234
1.00
35.76

ATOM
3172
CG
PRO
A
337
75.564
31.327
24.192
1.00
36.30

ATOM
3173
C
PRO
A
337
74.325
28.751
25.198
1.00
36.60

ATOM
3174
O
PRO
A
337
73.358
29.231
24.604
1.00
39.83

ATOM
3175
N
ALA
A
338
74.218
27.909
26.218
1.00
36.08

ATOM
3177
CA
ALA
A
338
72.944
27.512
26.802
1.00
35.56

ATOM
3178
CB
ALA
A
338
72.671
26.039
26.533
1.00
36.41

ATOM
3179
C
ALA
A
338
73.116
27.752
28.294
1.00
36.55

ATOM
3180
O
ALA
A
338
74.059
27.241
28.902
1.00
37.65

ATOM
3181
N
VAL
A
339
72.256
28.576
28.878
1.00
36.13

ATOM
3183
CA
VAL
A
339
72.360
28.872
30.295
1.00
34.95

ATOM
3184
CB
VAL
A
339
72.771
30.346
30.538
1.00
33.81

ATOM
3185
CG1
VAL
A
339
74.046
30.667
29.776
1.00
36.08

ATOM
3186
CG2
VAL
A
339
71.658
31.293
30.139
1.00
33.93

ATOM
3187
C
VAL
A
339
71.071
28.578
31.043
1.00
35.50

ATOM
3188
O
VAL
A
339
69.990
28.553
30.451
1.00
38.45

ATOM
3189
N
ASP
A
340
71.208
28.295
32.335
1.00
33.66

ATOM
3191
CA
ASP
A
340
70.078
28.029
33.213
1.00
31.12

ATOM
3192
CB
ASP
A
340
70.318
26.785
34.067
1.00
31.54

ATOM
3193
CG
ASP
A
340
69.813
25.520
33.411
1.00
33.33

ATOM
3194
OD1
ASP
A
340
68.895
25.606
32.569
1.00
35.59

ATOM
3195
OD2
ASP
A
340
70.324
24.432
33.742
1.00
35.60

ATOM
3196
C
ASP
A
340
70.003
29.235
34.108
1.00
29.12

ATOM
3197
O
ASP
A
340
70.968
29.555
34.794
1.00
29.84

ATOM
3198
N
VAL
A
341
68.890
29.948
34.040
1.00
28.41

ATOM
3200
CA
VAL
A
341
68.687
31.133
34.846
1.00
28.82

ATOM
3201
CB
VAL
A
341
68.249
32.316
33.969
1.00
29.73

ATOM
3202
CG1
VAL
A
341
67.868
33.496
34.831
1.00
27.89

ATOM
3203
CG2
VAL
A
341
69.364
32.703
33.017
1.00
28.62

ATOM
3204
C
VAL
A
341
67.592
30.833
35.852
1.00
30.90

ATOM
3205
O
VAL
A
341
66.456
30.596
35.459
1.00
34.21

ATOM
3206
N
GLN
A
342
67.931
30.821
37.139
1.00
31.91

ATOM
3208
CA
GLN
A
342
66.948
30.546
38.191
1.00
31.19

ATOM
3209
CB
GLN
A
342
67.375
29.345
39.039
1.00
31.37

ATOM
3210
CG
GLN
A
342
66.319
28.867
40.028
1.00
31.56

ATOM
3211
CD
GLN
A
342
66.706
27.570
40.706
1.00
33.87

ATOM
3212
OE1
GLN
A
342
67.841
27.111
40.590
1.00
37.83

ATOM
3213
NE2
GLN
A
342
65.770
26.979
41.431
1.00
35.30

ATOM
3216
C
GLN
A
342
66.752
31.761
39.088
1.00
31.20

ATOM
3217
O
GLN
A
342
67.724
32.374
39.537
1.00
31.67

ATOM
3218
N
ALA
A
343
65.494
32.114
39.327
1.00
30.96

ATOM
3220
CA
ALA
A
343
65.169
33.254
40.169
1.00
28.72

ATOM
3221
CB
ALA
A
343
64.042
34.054
39.563
1.00
28.77

ATOM
3222
C
ALA
A
343
64.782
32.778
41.552
1.00
28.72

ATOM
3223
O
ALA
A
343
64.011
31.826
41.700
1.00
30.49

ATOM
3224
N
PHE
A
344
65.320
33.447
42.559
1.00
26.88

ATOM
3226
CA
PHE
A
344
65.040
33.125
43.945
1.00
26.71

ATOM
3227
CB
PHE
A
344
66.316
32.718
44.673
1.00
21.35

ATOM
3228
CG
PHE
A
344
66.891
31.428
44.210
1.00
19.20

ATOM
3229
CD1
PHE
A
344
67.806
31.396
43.173
1.00
20.33

ATOM
3230
CD2
PHE
A
344
66.547
30.247
44.834
1.00
15.57

ATOM
3231
CE1
PHE
A
344
68.372
30.198
42.766
1.00
19.57

ATOM
3232
CE2
PHE
A
344
67.106
29.049
44.438
1.00
17.79

ATOM
3233
CZ
PHE
A
344
68.023
29.026
43.401
1.00
19.23

ATOM
3234
C
PHE
A
344
64.523
34.382
44.608
1.00
29.77

ATOM
3235
O
PHE
A
344
64.847
35.495
44.189
1.00
33.20

ATOM
3236
N
ALA
A
345
63.712
34.206
45.637
1.00
29.97

ATOM
3238
CA
ALA
A
345
63.204
35.331
46.390
1.00
30.90

ATOM
3239
CB
ALA
A
345
61.720
35.147
46.685
1.00
32.55

ATOM
3240
C
ALA
A
345
64.030
35.266
47.669
1.00
31.52

ATOM
3241
O
ALA
A
345
64.230
34.186
48.220
1.00
32.91

ATOM
3242
N
VAL
A
346
64.588
36.395
48.082
1.00
32.21

ATOM
3244
CA
VAL
A
346
65.403
36.449
49.287
1.00
33.87

ATOM
3245
CB
VAL
A
346
66.490
37.559
49.176
1.00
34.53

ATOM
3246
CG1
VAL
A
346
67.430
37.537
50.383
1.00
32.13

ATOM
3247
CG2
VAL
A
346
67.276
37.394
47.892
1.00
33.38

ATOM
3248
C
VAL
A
346
64.497
36.755
50.474
1.00
36.21

ATOM
3249
O
VAL
A
346
63.985
37.871
50.597
1.00
38.00

ATOM
3250
N
LEU
A
347
64.278
35.759
51.327
1.00
37.36

ATOM
3252
CA
LEU
A
347
63.445
35.928
52.516
1.00
39.35

ATOM
3253
CB
LEU
A
347
63.172
34.567
53.162
1.00
37.87

ATOM
3254
CG
LEU
A
347
62.664
33.460
52.238
1.00
37.83

ATOM
3255
CD1
LEU
A
347
62.315
32.231
53.057
1.00
36.57

ATOM
3256
CD2
LEU
A
347
61.461
33.945
51.462
1.00
39.01

ATOM
3257
C
LEU
A
347
64.157
36.847
53.519
1.00
42.26

ATOM
3258
O
LEU
A
347
65.376
37.021
53.449
1.00
44.26

ATOM
3259
N
PRO
A
348
63.418
37.410
54.495
1.00
43.97

ATOM
3260
CD
PRO
A
348
61.973
37.254
54.728
1.00
43.89

ATOM
3261
CA
PRO
A
348
64.002
38.309
55.505
1.00
43.61

ATOM
3262
CB
PRO
A
348
62.796
38.689
56.364
1.00
44.62

ATOM
3263
CG
PRO
A
348
61.875
37.514
56.206
1.00
44.98

ATOM
3264
C
PRO
A
348
65.138
37.751
56.364
1.00
42.78

ATOM
3265
O
PRO
A
348
65.685
38.471
57.195
1.00
43.70

ATOM
3266
N
ASN
A
349
65.478
36.478
56.184
1.00
42.71

ATOM
3268
CA
ASN
A
349
66.556
35.849
56.947
1.00
41.55

ATOM
3269
CB
ASN
A
349
66.046
34.591
57.659
1.00
41.16

ATOM
3270
CG
ASN
A
349
65.583
33.518
56.689
1.00
43.53

ATOM
3271
OD1
ASN
A
349
65.524
33.748
55.479
1.00
44.53

ATOM
3272
ND2
ASN
A
349
65.256
32.339
57.210
1.00
43.58

ATOM
3275
C
ASN
A
349
67.731
35.482
56.038
1.00
41.09

ATOM
3276
O
ASN
A
349
68.662
34.801
56.469
1.00
41.04

ATOM
3277
N
SER
A
350
67.678
35.954
54.793
1.00
40.23

ATOM
3279
CA
SER
A
350
68.697
35.704
53.768
1.00
39.62

ATOM
3280
CB
SER
A
350
70.122
35.854
54.314
1.00
40.62

ATOM
3281
OG
SER
A
350
70.518
37.214
54.317
1.00
46.79

ATOM
3283
C
SER
A
350
68.561
34.364
53.067
1.00
37.74

ATOM
3284
O
SER
A
350
69.339
34.063
52.168
1.00
40.17

ATOM
3285
N
ALA
A
351
67.581
33.562
53.471
1.00
34.00

ATOM
3287
CA
ALA
A
351
67.373
32.266
52.846
1.00
31.70

ATOM
3288
CB
ALA
A
351
66.426
31.429
53.670
1.00
31.56

ATOM
3289
C
ALA
A
351
66.799
32.505
51.455
1.00
32.27

ATOM
3290
O
ALA
A
351
66.150
33.526
51.212
1.00
34.50

ATOM
3291
N
LEU
A
352
67.022
31.560
50.549
1.00
30.81

ATOM
3293
CA
LEU
A
352
66.541
31.681
49.179
1.00
27.71

ATOM
3294
CB
LEU
A
352
67.678
31.358
48.203
1.00
22.61

ATOM
3295
CG
LEU
A
352
69.026
32.057
48.373
1.00
14.74

ATOM
3296
CD1
LEU
A
352
69.958
31.612
47.280
1.00
13.29

ATOM
3297
CD2
LEU
A
352
68.853
33.554
48.306
1.00
14.68

ATOM
3298
C
LEU
A
352
65.348
30.775
48.886
1.00
29.37

ATOM
3299
O
LEU
A
352
65.375
29.573
49.179
1.00
30.14

ATOM
3300
N
ALA
A
353
64.309
31.349
48.289
1.00
31.25

ATOM
3302
CA
ALA
A
353
63.110
30.592
47.929
1.00
34.26

ATOM
3303
CB
ALA
A
353
61.882
31.226
48.554
1.00
35.51

ATOM
3304
C
ALA
A
353
62.982
30.555
46.403
1.00
36.03

ATOM
3305
O
ALA
A
353
62.793
31.587
45.764
1.00
37.52

ATOM
3306
N
SER
A
354
63.110
29.362
45.832
1.00
37.41

ATOM
3308
CA
SER
A
354
63.054
29.162
44.388
1.00
37.85

ATOM
3309
CB
SER
A
354
63.338
27.687
44.070
1.00
40.08

ATOM
3310
OG
SER
A
354
63.380
27.434
42.673
1.00
45.78

ATOM
3312
C
SER
A
354
61.744
29.601
43.741
1.00
37.70

ATOM
3313
O
SER
A
354
60.684
29.060
44.043
1.00
40.21

ATOM
3314
N
LEU
A
355
61.830
30.572
42.840
1.00
36.34

ATOM
3316
CA
LEU
A
355
60.657
31.074
42.137
1.00
35.04

ATOM
3317
CB
LEU
A
355
60.839
32.553
41.782
1.00
30.99

ATOM
3318
CG
LEU
A
355
60.830
33.547
42.939
1.00
28.58

ATOM
3319
CD1
LEU
A
355
61.028
34.955
42.423
1.00
28.81

ATOM
3320
CD2
LEU
A
355
59.520
33.441
43.678
1.00
30.20

ATOM
3321
C
LEU
A
355
60.399
30.255
40.868
1.00
36.96

ATOM
3322
O
LEU
A
355
59.363
29.592
40.745
1.00
36.42

ATOM
3323
N
PHE
A
356
61.356
30.286
39.939
1.00
37.24

ATOM
3325
CA
PHE
A
356
61.251
29.556
38.673
1.00
36.22

ATOM
3326
CB
PHE
A
356
60.315
30.291
37.699
1.00
33.82

ATOM
3327
CG
PHE
A
356
60.661
31.741
37.491
1.00
30.90

ATOM
3328
CD1
PHE
A
356
61.786
32.110
36.768
1.00
29.04

ATOM
3329
CD2
PHE
A
356
59.859
32.739
38.027
1.00
30.48

ATOM
3330
CE1
PHE
A
356
62.111
33.451
36.586
1.00
28.29

ATOM
3331
CE2
PHE
A
356
60.179
34.081
37.848
1.00
30.44

ATOM
3332
CZ
PHE
A
356
61.308
34.435
37.128
1.00
25.36

ATOM
3333
C
PHE
A
356
62.611
29.356
38.011
1.00
36.47

ATOM
3334
O
PHE
A
356
63.546
30.112
38.271
1.00
39.86

ATOM
3335
N
LEU
A
357
62.707
28.345
37.151
1.00
36.72

ATOM
3337
CA
LEU
A
357
63.937
28.035
36.423
1.00
35.97

ATOM
3338
CB
LEU
A
357
64.358
26.585
36.670
1.00
34.25

ATOM
3339
CG
LEU
A
357
65.593
26.104
35.904
1.00
32.69

ATOM
3340
CD1
LEU
A
357
66.828
26.854
36.354
1.00
30.30

ATOM
3341
CD2
LEU
A
357
65.784
24.620
36.120
1.00
34.02

ATOM
3342
C
LEU
A
357
63.721
28.252
34.925
1.00
36.64

ATOM
3343
O
LEU
A
357
62.805
27.678
34.333
1.00
39.03

ATOM
3344
N
ILE
A
358
64.585
29.054
34.318
1.00
35.88

ATOM
3346
CA
ILE
A
358
64.508
29.367
32.899
1.00
34.57

ATOM
3347
CB
ILE
A
358
64.510
30.903
32.672
1.00
33.20

ATOM
3348
CG2
ILE
A
358
64.653
31.239
31.208
1.00
31.65

ATOM
3349
CG1
ILE
A
358
63.220
31.510
33.207
1.00
33.82

ATOM
3350
CD1
ILE
A
358
61.978
30.907
32.602
1.00
34.80

ATOM
3351
C
ILE
A
358
65.677
28.748
32.143
1.00
36.24

ATOM
3352
O
ILE
A
358
66.784
28.628
32.666
1.00
36.67

ATOM
3353
N
GLY
A
359
65.405
28.338
30.912
1.00
38.02

ATOM
3355
CA
GLY
A
359
66.419
27.753
30.061
1.00
37.56

ATOM
3356
C
GLY
A
359
66.597
28.704
28.902
1.00
38.10

ATOM
3357
O
GLY
A
359
65.679
28.932
28.113
1.00
38.54

ATOM
3358
N
MET
A
360
67.769
29.305
28.830
1.00
37.31

ATOM
3360
CA
MET
A
360
68.060
30.252
27.785
1.00
36.92

ATOM
3361
CB
MET
A
360
68.515
31.560
28.405
1.00
38.52

ATOM
3362
CG
MET
A
360
68.813
32.656
27.421
1.00
42.50

ATOM
3363
SD
MET
A
360
69.679
33.987
28.246
1.00
49.37

ATOM
3364
CE
MET
A
360
68.747
34.125
29.725
1.00
46.11

ATOM
3365
C
MET
A
360
69.154
29.686
26.907
1.00
38.15

ATOM
3366
O
MET
A
360
69.986
28.899
27.347
1.00
38.64

ATOM
3367
N
HIS
A
361
69.114
30.054
25.641
1.00
39.81

ATOM
3369
CA
HIS
A
361
70.095
29.612
24.667
1.00
41.81

ATOM
3370
CB
HIS
A
361
69.766
28.215
24.131
1.00
45.81

ATOM
3371
CG
HIS
A
361
68.310
27.988
23.878
1.00
51.49

ATOM
3372
CD2
HIS
A
361
67.290
27.716
24.728
1.00
54.71

ATOM
3373
ND1
HIS
A
361
67.753
28.041
22.618
1.00
53.69

ATOM
3375
CE1
HIS
A
361
66.455
27.813
22.702
1.00
55.98

ATOM
3376
NE2
HIS
A
361
66.148
27.614
23.972
1.00
57.77

ATOM
3378
C
HIS
A
361
70.032
30.642
23.569
1.00
41.72

ATOM
3379
O
HIS
A
361
69.003
31.295
23.387
1.00
42.60

ATOM
3380
N
THR
A
362
71.132
30.816
22.858
1.00
40.54

ATOM
3382
CA
THR
A
362
71.168
31.803
21.803
1.00
38.28

ATOM
3383
CB
THR
A
362
71.452
33.206
22.399
1.00
38.27

ATOM
3384
OG1
THR
A
362
71.408
34.200
21.371
1.00
40.01

ATOM
3386
CG2
THR
A
362
72.799
33.241
23.082
1.00
38.36

ATOM
3387
C
THR
A
362
72.244
31.391
20.818
1.00
37.84

ATOM
3388
O
THR
A
362
72.692
30.245
20.829
1.00
38.47

ATOM
3389
N
THR
A
363
72.620
32.315
19.948
1.00
37.83

ATOM
3391
CA
THR
A
363
73.640
32.091
18.940
1.00
38.05

ATOM
3392
CB
THR
A
363
73.007
31.617
17.603
1.00
38.92

ATOM
3393
OG1
THR
A
363
73.993
31.618
16.567
1.00
41.55

ATOM
3395
CG2
THR
A
363
71.855
32.515
17.193
1.00
42.85

ATOM
3396
C
THR
A
363
74.333
33.436
18.773
1.00
36.99

ATOM
3397
O
THR
A
363
73.668
34.467
18.705
1.00
38.50

ATOM
3398
N
GLY
A
364
75.660
33.438
18.763
1.00
36.22

ATOM
3400
CA
GLY
A
364
76.377
34.692
18.626
1.00
35.40

ATOM
3401
C
GLY
A
364
77.639
34.632
17.794
1.00
35.46

ATOM
3402
O
GLY
A
364
78.075
33.561
17.395
1.00
35.68

ATOM
3403
N
SER
A
365
78.216
35.795
17.522
1.00
37.37

ATOM
3405
CA
SER
A
365
79.434
35.884
16.738
1.00
39.81

ATOM
3406
CB
SER
A
365
79.399
37.121
15.840
1.00
41.52

ATOM
3407
OG
SER
A
365
78.345
37.028
14.895
1.00
50.49

ATOM
3409
C
SER
A
365
80.627
35.975
17.669
1.00
40.48

ATOM
3410
O
SER
A
365
80.584
36.669
18.682
1.00
43.48

ATOM
3411
N
MET
A
366
81.685
35.259
17.330
1.00
40.04

ATOM
3413
CA
MET
A
366
82.898
35.271
18.118
1.00
40.25

ATOM
3414
CB
MET
A
366
83.254
33.836
18.509
1.00
41.64

ATOM
3415
CG
MET
A
366
84.524
33.688
19.310
1.00
44.41

ATOM
3416
SD
MET
A
366
84.378
34.496
20.881
1.00
48.93

ATOM
3417
CE
MET
A
366
83.512
33.252
21.833
1.00
49.58

ATOM
3418
C
MET
A
366
83.978
35.880
17.224
1.00
41.24

ATOM
3419
O
MET
A
366
84.400
35.262
16.249
1.00
43.55

ATOM
3420
N
GLU
A
367
84.347
37.129
17.482
1.00
42.13

ATOM
3422
CA
GLU
A
367
85.383
37.780
16.686
1.00
43.88

ATOM
3423
CB
GLU
A
367
85.148
39.288
16.608
1.00
47.79

ATOM
3424
CG
GLU
A
367
84.094
39.715
15.588
1.00
54.26

ATOM
3425
CD
GLU
A
367
84.551
39.555
14.143
1.00
57.86

ATOM
3426
OE1
GLU
A
367
85.768
39.681
13.872
1.00
60.11

ATOM
3427
OE2
GLU
A
367
83.683
39.315
13.273
1.00
59.61

ATOM
3428
C
GLU
A
367
86.724
37.492
17.336
1.00
43.57

ATOM
3429
O
GLU
A
367
86.822
37.491
18.562
1.00
44.51

ATOM
3430
N
VAL
A
368
87.752
37.256
16.526
1.00
42.06

ATOM
3432
CA
VAL
A
368
89.077
36.944
17.047
1.00
42.38

ATOM
3433
CB
VAL
A
368
89.412
35.454
16.810
1.00
42.31

ATOM
3434
CG1
VAL
A
368
90.866
35.167
17.146
1.00
44.40

ATOM
3435
CG2
VAL
A
368
88.509
34.581
17.660
1.00
41.44

ATOM
3436
C
VAL
A
368
90.204
37.822
16.491
1.00
43.82

ATOM
3437
O
VAL
A
368
90.306
38.039
15.279
1.00
44.42

ATOM
3438
N
SER
A
369
91.051
38.312
17.392
1.00
44.15

ATOM
3440
CA
SER
A
369
92.182
39.160
17.032
1.00
46.20

ATOM
3441
CB
SER
A
369
91.838
40.636
17.254
1.00
48.08

ATOM
3442
OG
SER
A
369
90.692
41.011
16.508
1.00
55.65

ATOM
3444
C
SER
A
369
93.376
38.773
17.896
1.00
46.39

ATOM
3445
O
SER
A
369
93.269
37.897
18.757
1.00
45.59

ATOM
3446
N
ALA
A
370
94.503
39.447
17.692
1.00
46.96

ATOM
3448
CA
ALA
A
370
95.705
39.151
18.455
1.00
46.86

ATOM
3449
CB
ALA
A
370
96.659
38.334
17.615
1.00
48.51

ATOM
3450
C
ALA
A
370
96.401
40.399
18.961
1.00
47.76

ATOM
3451
O
ALA
A
370
96.526
41.384
18.234
1.00
49.78

ATOM
3452
N
GLU
A
371
96.833
40.346
20.215
1.00
49.05

ATOM
3454
CA
GLU
A
371
97.546
41.429
20.889
1.00
52.58

ATOM
3455
CB
GLU
A
371
96.670
42.035
21.999
1.00
55.47

ATOM
3456
CG
GLU
A
371
97.394
42.954
23.010
1.00
61.82

ATOM
3457
CD
GLU
A
371
97.662
44.365
22.494
1.00
66.05

ATOM
3458
OE1
GLU
A
371
96.728
44.994
21.945
1.00
69.54

ATOM
3459
OE2
GLU
A
371
98.801
44.859
22.662
1.00
66.75

ATOM
3460
C
GLU
A
371
98.753
40.718
21.490
1.00
53.47

ATOM
3461
O
GLU
A
371
98.617
39.613
22.015
1.00
54.95

ATOM
3462
N
SER
A
372
99.926
41.337
21.418
1.00
54.76

ATOM
3464
CA
SER
A
372
101.145
40.718
21.932
1.00
54.93

ATOM
3465
CB
SER
A
372
101.080
40.570
23.462
1.00
56.19

ATOM
3466
OG
SER
A
372
100.788
41.803
24.098
1.00
57.76

ATOM
3468
C
SER
A
372
101.267
39.347
21.245
1.00
54.65

ATOM
3469
O
SER
A
372
101.364
39.275
20.017
1.00
56.14

ATOM
3470
N
ASN
A
373
101.207
38.271
22.023
1.00
51.39

ATOM
3472
CA
ASN
A
373
101.292
36.922
21.480
1.00
48.43

ATOM
3473
CB
ASN
A
373
102.606
36.249
21.891
1.00
49.96

ATOM
3474
CG
ASN
A
373
103.830
36.981
21.379
1.00
51.10

ATOM
3475
OD1
ASN
A
373
103.780
37.674
20.361
1.00
53.30

ATOM
3476
ND2
ASN
A
373
104.946
36.818
22.078
1.00
50.08

ATOM
3479
C
ASN
A
373
100.126
36.168
22.087
1.00
46.52

ATOM
3480
O
ASN
A
373
100.267
35.027
22.529
1.00
45.55

ATOM
3481
N
ARG
A
374
98.983
36.838
22.156
1.00
44.90

ATOM
3483
CA
ARG
A
374
97.780
36.255
22.730
1.00
43.78

ATOM
3484
CB
ARG
A
374
97.293
37.082
23.929
1.00
45.07

ATOM
3485
CG
ARG
A
374
98.263
37.183
25.090
1.00
47.75

ATOM
3486
CD
ARG
A
374
97.653
37.976
26.235
1.00
52.92

ATOM
3487
NE
ARG
A
374
97.293
39.342
25.857
1.00
58.67

ATOM
3489
CZ
ARG
A
374
97.737
40.439
26.468
1.00
62.31

ATOM
3490
NH1
ARG
A
374
98.568
40.347
27.500
1.00
63.80

ATOM
3493
NH2
ARG
A
374
97.345
41.637
26.047
1.00
62.63

ATOM
3496
C
ARG
A
374
96.660
36.163
21.706
1.00
41.67

ATOM
3497
O
ARG
A
374
96.660
36.866
20.698
1.00
42.40

ATOM
3498
N
LEU
A
375
95.720
35.268
21.972
1.00
39.53

ATOM
3500
CA
LEU
A
375
94.568
35.063
21.119
1.00
38.25

ATOM
3501
CB
LEU
A
375
94.366
33.568
20.886
1.00
40.19

ATOM
3502
CG
LEU
A
375
93.330
33.154
19.846
1.00
42.29

ATOM
3503
CD1
LEU
A
375
93.784
33.625
18.478
1.00
42.24

ATOM
3504
CD2
LEU
A
375
93.158
31.646
19.866
1.00
41.82

ATOM
3505
C
LEU
A
375
93.399
35.623
21.917
1.00
37.82

ATOM
3506
O
LEU
A
375
93.024
35.058
22.946
1.00
38.21

ATOM
3507
N
VAL
A
376
92.871
36.764
21.491
1.00
38.16

ATOM
3509
CA
VAL
A
376
91.752
37.384
22.193
1.00
38.06

ATOM
3510
CB
VAL
A
376
92.057
38.847
22.613
1.00
37.73

ATOM
3511
CG1
VAL
A
376
93.386
38.928
23.343
1.00
36.49

ATOM
3512
CG2
VAL
A
376
92.054
39.762
21.409
1.00
37.89

ATOM
3513
C
VAL
A
376
90.517
37.376
21.313
1.00
37.85

ATOM
3514
O
VAL
A
376
90.615
37.251
20.091
1.00
37.84

ATOM
3515
N
GLY
A
377
89.358
37.542
21.935
1.00
38.79

ATOM
3517
CA
GLY
A
377
88.120
37.548
21.186
1.00
38.96

ATOM
3518
C
GLY
A
377
87.034
38.334
21.880
1.00
38.86

ATOM
3519
O
GLY
A
377
87.235
38.860
22.976
1.00
40.46

ATOM
3520
N
GLU
A
378
85.881
38.426
21.235
1.00
39.21

ATOM
3522
CA
GLU
A
378
84.752
39.143
21.793
1.00
39.89

ATOM
3523
CB
GLU
A
378
84.762
40.601
21.335
1.00
42.06

ATOM
3524
CG
GLU
A
378
83.935
41.522
22.226
1.00
47.89

ATOM
3525
CD
GLU
A
378
83.384
42.725
21.488
1.00
51.11

ATOM
3526
OE1
GLU
A
378
84.142
43.357
20.718
1.00
53.99

ATOM
3527
OE2
GLU
A
378
82.184
43.031
21.679
1.00
52.17

ATOM
3528
C
GLU
A
378
83.481
38.456
21.315
1.00
40.11

ATOM
3529
O
GLU
A
378
83.352
38.132
20.133
1.00
40.78

ATOM
3530
N
LEU
A
379
82.569
38.211
22.249
1.00
40.26

ATOM
3532
CA
LEU
A
379
81.297
37.558
21.973
1.00
41.54

ATOM
3533
CB
LEU
A
379
80.935
36.651
23.155
1.00
43.08

ATOM
3534
CG
LEU
A
379
80.208
35.314
22.991
1.00
45.34

ATOM
3535
CD1
LEU
A
379
79.839
34.798
24.377
1.00
44.87

ATOM
3536
CD2
LEU
A
379
78.966
35.444
22.136
1.00
44.17

ATOM
3537
C
LEU
A
379
80.199
38.613
21.799
1.00
42.68

ATOM
3538
O
LEU
A
379
80.179
39.623
22.507
1.00
43.44

ATOM
3539
N
LYS
A
380
79.303
38.384
20.845
1.00
44.09

ATOM
3541
CA
LYS
A
380
78.171
39.276
20.588
1.00
46.18

ATOM
3542
CB
LYS
A
380
78.438
40.165
19.373
1.00
48.46

ATOM
3543
CG
LYS
A
380
79.444
41.279
19.660
1.00
54.25

ATOM
3544
CD
LYS
A
380
79.847
42.041
18.408
1.00
58.33

ATOM
3545
CE
LYS
A
380
80.817
43.172
18.734
1.00
60.62

ATOM
3546
NZ
LYS
A
380
81.332
43.851
17.509
1.00
63.04

ATOM
3550
C
LYS
A
380
76.968
38.367
20.369
1.00
46.00

ATOM
3551
O
LYS
A
380
77.042
37.418
19.591
1.00
45.80

ATOM
3552
N
LEU
A
381
75.877
38.630
21.082
1.00
46.45

ATOM
3554
CA
LEU
A
381
74.690
37.784
20.996
1.00
46.82

ATOM
3555
CB
LEU
A
381
74.115
37.545
22.400
1.00
45.07

ATOM
3556
CG
LEU
A
381
75.001
36.992
23.521
1.00
41.15

ATOM
3557
CD1
LEU
A
381
74.206
36.974
24.817
1.00
39.28

ATOM
3558
CD2
LEU
A
381
75.500
35.604
23.174
1.00
40.04

ATOM
3559
C
LEU
A
381
73.569
38.272
20.084
1.00
48.41

ATOM
3560
O
LEU
A
381
73.505
39.448
19.719
1.00
48.91

ATOM
3561
N
ASP
A
382
72.696
37.335
19.725
1.00
50.06

ATOM
3563
CA
ASP
A
382
71.527
37.591
18.894
1.00
54.68

ATOM
3564
CB
ASP
A
382
71.371
36.488
17.845
1.00
57.78

ATOM
3565
CG
ASP
A
382
71.718
36.953
16.453
1.00
61.73

ATOM
3566
OD1
ASP
A
382
72.846
37.455
16.258
1.00
65.65

ATOM
3567
OD2
ASP
A
382
70.862
36.809
15.552
1.00
62.89

ATOM
3568
C
ASP
A
382
70.325
37.565
19.836
1.00
56.30

ATOM
3569
O
ASP
A
382
70.465
37.827
21.030
1.00
57.37

ATOM
3570
N
ARG
A
383
69.147
37.244
19.304
1.00
57.17

ATOM
3572
CA
ARG
A
383
67.932
37.169
20.116
1.00
56.86

ATOM
3573
CB
ARG
A
383
66.710
36.913
19.221
1.00
61.20

ATOM
3574
CG
ARG
A
383
66.368
38.054
18.262
1.00
66.61

ATOM
3575
CD
ARG
A
383
65.158
37.721
17.389
1.00
68.98

ATOM
3576
NE
ARG
A
383
64.674
38.887
16.647
1.00
73.50

ATOM
3578
CZ
ARG
A
383
64.914
39.119
15.358
1.00
76.60

ATOM
3579
NH1
ARG
A
383
65.639
38.269
14.636
1.00
77.94

ATOM
3582
NH2
ARG
A
383
64.421
40.210
14.784
1.00
77.33

ATOM
3585
C
ARG
A
383
68.081
36.026
21.120
1.00
54.61

ATOM
3586
O
ARG
A
383
68.689
35.001
20.801
1.00
56.02

ATOM
3587
N
LEU
A
384
67.565
36.207
22.333
1.00
50.19

ATOM
3589
CA
LEU
A
384
67.654
35.163
23.353
1.00
47.21

ATOM
3590
CB
LEU
A
384
67.886
35.765
24.740
1.00
45.34

ATOM
3591
CG
LEU
A
384
69.072
36.707
24.951
1.00
44.13

ATOM
3592
CD1
LEU
A
384
69.089
37.136
26.403
1.00
48.33

ATOM
3593
CD2
LEU
A
384
70.386
36.036
24.587
1.00
44.37

ATOM
3594
C
LEU
A
384
66.366
34.355
23.360
1.00
46.05

ATOM
3595
O
LEU
A
384
65.287
34.910
23.175
1.00
46.98

ATOM
3596
N
LEU
A
385
66.477
33.044
23.536
1.00
45.63

ATOM
3598
CA
LEU
A
385
65.299
32.190
23.564
1.00
44.83

ATOM
3599
CB
LEU
A
385
65.417
31.034
22.577
1.00
47.07

ATOM
3600
CG
LEU
A
385
65.424
31.305
21.075
1.00
49.68

ATOM
3601
CD1
LEU
A
385
66.807
31.742
20.610
1.00
50.06

ATOM
3602
CD2
LEU
A
385
65.018
30.020
20.367
1.00
53.29

ATOM
3603
C
LEU
A
385
65.093
31.624
24.948
1.00
43.70

ATOM
3604
O
LEU
A
385
65.973
30.965
25.500
1.00
46.13

ATOM
3605
N
LEU
A
386
63.921
31.879
25.501
1.00
41.90

ATOM
3607
CA
LEU
A
386
63.586
31.399
26.819
1.00
40.93

ATOM
3608
CB
LEU
A
386
62.804
32.467
27.576
1.00
38.95

ATOM
3609
CG
LEU
A
386
63.610
33.573
28.251
1.00
38.87

ATOM
3610
CD1
LEU
A
386
64.732
34.076
27.364
1.00
36.69

ATOM
3611
CD2
LEU
A
386
62.671
34.690
28.636
1.00
38.24

ATOM
3612
C
LEU
A
386
62.754
30.140
26.711
1.00
41.89

ATOM
3613
O
LEU
A
386
62.154
29.861
25.677
1.00
44.73

ATOM
3614
N
GLU
A
387
62.777
29.354
27.773
1.00
42.45

ATOM
3616
CA
GLU
A
387
62.006
28.133
27.867
1.00
43.22

ATOM
3617
CB
GLU
A
387
62.773
26.932
27.306
1.00
44.48

ATOM
3618
CG
GLU
A
387
61.993
25.614
27.408
1.00
46.64

ATOM
3619
CD
GLU
A
387
62.699
24.436
26.762
1.00
48.74

ATOM
3620
OE1
GLU
A
387
62.622
24.305
25.520
1.00
53.50

ATOM
3621
OE2
GLU
A
387
63.311
23.629
27.495
1.00
48.42

ATOM
3622
C
GLU
A
387
61.791
27.966
29.359
1.00
45.59

ATOM
3623
O
GLU
A
387
62.697
28.232
30.150
1.00
47.68

ATOM
3624
N
LEU
A
388
60.574
27.618
29.750
1.00
47.18

ATOM
3626
CA
LEU
A
388
60.260
27.422
31.156
1.00
48.51

ATOM
3627
CB
LEU
A
388
58.795
27.778
31.418
1.00
49.74

ATOM
3628
CG
LEU
A
388
58.298
27.776
32.865
1.00
49.97

ATOM
3629
CG1
LEU
A
388
58.957
28.902
33.656
1.00
49.70

ATOM
3630
CD2
LEU
A
388
56.788
27.935
32.871
1.00
51.43

ATOM
3631
C
LEU
A
388
60.513
25.953
31.468
1.00
49.89

ATOM
3632
O
LEU
A
388
60.033
25.071
30.754
1.00
49.90

ATOM
3633
N
LYS
A
389
61.290
25.688
32.511
1.00
53.07

ATOM
3635
CA
LYS
A
389
61.599
24.312
32.883
1.00
57.61

ATOM
3636
CB
LYS
A
389
63.109
24.152
33.105
1.00
58.15

ATOM
3637
CG
LYS
A
389
63.933
24.486
31.864
1.00
58.89

ATOM
3638
CD
LYS
A
389
65.377
24.022
31.971
1.00
61.45

ATOM
3639
CE
LYS
A
389
66.104
24.202
30.640
1.00
63.53

ATOM
3640
NZ
LYS
A
389
67.507
23.692
30.664
1.00
66.07

ATOM
3644
C
LYS
A
389
60.800
23.813
34.094
1.00
60.00

ATOM
3645
O
LYS
A
389
60.351
22.663
34.122
1.00
61.33

ATOM
3646
N
HIS
A
390
60.622
24.679
35.086
1.00
61.51

ATOM
3648
CA
HIS
A
390
59.871
24.347
36.297
1.00
63.22

ATOM
3649
CB
HIS
A
390
60.713
23.474
37.242
1.00
68.01

ATOM
3650
CG
HIS
A
390
59.939
22.880
38.386
1.00
74.01

ATOM
3651
CD2
HIS
A
390
59.403
21.647
38.553
1.00
76.41

ATOM
3652
ND1
HIS
A
390
59.682
23.568
39.554
1.00
76.75

ATOM
3654
CE1
HIS
A
390
59.023
22.785
40.391
1.00
78.97

ATOM
3655
NE2
HIS
A
390
58.843
21.613
39.807
1.00
79.75

ATOM
3657
C
HIS
A
390
59.551
25.669
36.969
1.00
61.81

ATOM
3658
O
HIS
A
390
60.348
26.604
36.912
1.00
62.27

ATOM
3659
N
SER
A
391
58.375
25.762
37.572
1.00
60.92

ATOM
3661
CA
SER
A
391
57.978
26.980
38.257
1.00
59.76

ATOM
3662
CB
SER
A
391
57.005
27.793
37.403
1.00
58.20

ATOM
3663
OG
SER
A
391
56.639
28.996
38.059
1.00
55.50

ATOM
3665
C
SER
A
391
57.322
26.605
39.567
1.00
59.99

ATOM
3666
O
SER
A
391
56.486
25.699
39.618
1.00
60.83

ATOM
3667
N
ASN
A
392
57.753
27.260
40.636
1.00
59.65

ATOM
3669
CA
ASN
A
392
57.190
27.008
41.949
1.00
59.99

ATOM
3670
CB
ASN
A
392
58.241
27.234
43.039
1.00
58.88

ATOM
3671
CG
ASN
A
392
59.314
26.152
43.054
1.00
58.15

ATOM
3672
OD1
ASN
A
392
59.424
25.344
42.126
1.00
59.13

ATOM
3673
ND2
ASN
A
392
60.117
26.137
44.108
1.00
57.91

ATOM
3676
C
ASN
A
392
55.976
27.914
42.145
1.00
60.50

ATOM
3677
O
ASN
A
392
55.149
27.678
43.023
1.00
61.62

ATOM
3678
N
ILE
A
393
55.851
28.926
41.288
1.00
61.07

ATOM
3680
CA
ILE
A
393
54.730
29.861
41.351
1.00
60.89

ATOM
3681
CB
ILE
A
393
55.212
31.333
41.306
1.00
58.61

ATOM
3682
CG2
ILE
A
393
56.083
31.634
42.510
1.00
58.38

ATOM
3683
CG1
ILE
A
393
55.948
31.622
39.995
1.00
57.06

ATOM
3684
CD1
ILE
A
393
56.245
33.087
39.775
1.00
56.51

ATOM
3685
C
ILE
A
393
53.700
29.632
40.228
1.00
63.24

ATOM
3686
O
ILE
A
393
53.049
30.574
39.772
1.00
64.68

ATOM
3687
N
GLY
A
394
53.556
28.382
39.786
1.00
64.29

ATOM
3689
CA
GLY
A
394
52.603
28.061
38.731
1.00
62.76

ATOM
3690
C
GLY
A
394
53.046
28.426
37.323
1.00
62.37

ATOM
3691
O
GLY
A
394
53.985
29.202
37.147
1.00
62.54

ATOM
3692
N
PRO
A
395
52.412
27.848
36.291
1.00
62.40

ATOM
3693
CD
PRO
A
395
51.333
26.846
36.373
1.00
63.52

ATOM
3694
CA
PRO
A
395
52.758
28.130
34.894
1.00
60.73

ATOM
3695
CB
PRO
A
395
51.937
27.095
34.125
1.00
61.59

ATOM
3696
CG
PRO
A
395
50.728
26.910
34.992
1.00
63.08

ATOM
3697
C
PRO
A
395
52.405
29.554
34.470
1.00
59.25

ATOM
3698
O
PRO
A
395
51.353
30.081
34.834
1.00
59.47

ATOM
3699
N
PHE
A
396
53.295
30.171
33.702
1.00
57.50

ATOM
3701
CA
PHE
A
396
53.087
31.530
33.220
1.00
55.80

ATOM
3702
CB
PHE
A
396
53.684
32.555
34.200
1.00
54.39

ATOM
3703
CG
PHE
A
396
55.194
32.588
34.223
1.00
51.73

ATOM
3704
CD1
PHE
A
396
55.899
33.426
33.364
1.00
49.07

ATOM
3705
CD2
PHE
A
396
55.909
31.796
35.115
1.00
50.73

ATOM
3706
CE1
PHE
A
396
57.283
33.474
33.394
1.00
47.56

ATOM
3707
CE2
PHE
A
396
57.295
31.841
35.150
1.00
47.47

ATOM
3708
CZ
PHE
A
396
57.981
32.678
34.289
1.00
47.02

ATOM
3709
C
PHE
A
396
53.720
31.674
31.839
1.00
55.76

ATOM
3710
O
PHE
A
396
54.463
30.792
31.392
1.00
56.39

ATOM
3711
N
PRO
A
397
53.394
32.763
31.120
1.00
54.61

ATOM
3712
CD
PRO
A
397
52.354
33.768
31.393
1.00
54.50

ATOM
3713
CA
PRO
A
397
53.966
32.967
29.787
1.00
53.13

ATOM
3714
CB
PRO
A
397
53.167
34.159
29.252
1.00
53.76

ATOM
3715
CG
PRO
A
397
51.877
34.095
30.011
1.00
53.30

ATOM
3716
C
PRO
A
397
55.448
33.301
29.899
1.00
51.99

ATOM
3717
O
PRO
A
397
55.810
34.434
30.219
1.00
51.04

ATOM
3718
N
VAL
A
398
56.300
32.322
29.609
1.00
50.99

ATOM
3720
CA
VAL
A
398
57.747
32.506
29.686
1.00
50.88

ATOM
3721
CB
VAL
A
398
58.500
31.222
29.253
1.00
50.94

ATOM
3722
CG1
VAL
A
398
58.260
30.926
27.785
1.00
50.60

ATOM
3723
CG2
VAL
A
398
59.987
31.340
29.561
1.00
49.69

ATOM
3724
C
VAL
A
398
58.248
33.709
28.888
1.00
51.53

ATOM
3725
O
VAL
A
398
59.383
34.144
29.053
1.00
54.45

ATOM
3726
N
GLU
A
399
57.385
34.268
28.050
1.00
52.68

ATOM
3728
CA
GLU
A
399
57.741
35.427
27.236
1.00
52.46

ATOM
3729
CB
GLU
A
399
56.807
35.533
26.020
1.00
53.50

ATOM
3730
CG
GLU
A
399
56.637
34.234
25.210
1.00
53.56

ATOM
3731
CD
GLU
A
399
55.420
33.405
25.629
1.00
53.53

ATOM
3732
OE1
GLU
A
399
54.313
33.979
25.741
1.00
54.16

ATOM
3733
OE2
GLU
A
399
55.562
32.176
25.821
1.00
52.27

ATOM
3734
C
GLU
A
399
57.737
36.750
28.025
1.00
51.41

ATOM
3735
O
GLU
A
399
58.233
37.762
27.539
1.00
52.41

ATOM
3736
N
LEU
A
400
57.186
36.747
29.235
1.00
49.79

ATOM
3738
CA
LEU
A
400
57.148
37.955
30.060
1.00
49.44

ATOM
3739
CB
LEU
A
400
56.186
37.769
31.238
1.00
50.82

ATOM
3740
CG
LEU
A
400
54.683
38.030
31.086
1.00
49.58

ATOM
3741
CD1
LEU
A
400
54.427
39.510
30.867
1.00
50.78

ATOM
3742
CD2
LEU
A
400
54.114
37.220
29.954
1.00
50.81

ATOM
3743
C
LEU
A
400
58.539
38.330
30.589
1.00
50.26

ATOM
3744
O
LEU
A
400
58.800
39.487
30.931
1.00
50.71

ATOM
3745
N
LEU
A
401
59.428
37.344
30.656
1.00
50.41

ATOM
3747
CA
LEU
A
401
60.790
37.548
31.143
1.00
49.44

ATOM
3748
CB
LEU
A
401
61.310
36.255
31.766
1.00
48.32

ATOM
3749
CG
LEU
A
401
60.598
35.840
33.049
1.00
46.40

ATOM
3750
CD1
LEU
A
401
60.738
34.361
33.262
1.00
45.30

ATOM
3751
CD2
LEU
A
401
61.168
36.620
34.218
1.00
48.02

ATOM
3752
C
LEU
A
401
61.762
38.013
30.066
1.00
49.89

ATOM
3753
O
LEU
A
401
62.919
38.303
30.360
1.00
51.08

ATOM
3754
N
GLN
A
402
61.288
38.091
28.826
1.00
51.14

ATOM
3756
CA
GLN
A
402
62.107
38.511
27.686
1.00
52.43

ATOM
3757
CB
GLN
A
402
61.255
38.569
26.413
1.00
53.25

ATOM
3758
CG
GLN
A
402
60.908
37.211
25.810
1.00
55.42

ATOM
3759
CD
GLN
A
402
61.966
36.697
24.851
1.00
55.66

ATOM
3760
OE1
GLN
A
402
63.075
37.229
24.780
1.00
55.93

ATOM
3761
NE2
GLN
A
402
61.619
35.667
24.090
1.00
56.71

ATOM
3764
C
GLN
A
402
62.800
39.855
27.890
1.00
53.23

ATOM
3765
O
GLN
A
402
64.009
39.977
27.684
1.00
54.78

ATOM
3766
N
ASP
A
403
62.031
40.866
28.275
1.00
53.89

ATOM
3768
CA
ASP
A
403
62.578
42.198
28.505
1.00
54.40

ATOM
3769
CB
ASP
A
403
61.441
43.183
28.797
1.00
58.20

ATOM
3770
CG
ASP
A
403
60.524
43.394
27.597
1.00
60.37

ATOM
3771
OD1
ASP
A
403
61.001
43.915
26.563
1.00
60.48

ATOM
3772
OD2
ASP
A
403
59.325
43.045
27.691
1.00
61.61

ATOM
3773
C
ASP
A
403
63.615
42.204
29.638
1.00
53.27

ATOM
3774
O
ASP
A
403
64.669
42.836
29.525
1.00
53.59

ATOM
3775
N
ILE
A
404
63.318
41.487
30.719
1.00
51.11

ATOM
3777
CA
ILE
A
404
64.229
41.387
31.852
1.00
48.30

ATOM
3778
CB
ILE
A
404
63.545
40.668
33.055
1.00
45.31

ATOM
3779
CG2
ILE
A
404
64.352
39.468
33.530
1.00
47.52

ATOM
3780
CG1
ILE
A
404
63.337
41.654
34.203
1.00
42.01

ATOM
3781
CD1
ILE
A
404
64.620
42.234
34.752
1.00
36.04

ATOM
3782
C
ILE
A
404
65.497
40.656
31.400
1.00
48.48

ATOM
3783
O
ILE
A
404
66.611
41.108
31.667
1.00
51.31

ATOM
3784
N
MET
A
405
65.318
39.564
30.660
1.00
47.51

ATOM
3786
CA
MET
A
405
66.433
38.768
30.151
1.00
47.38

ATOM
3787
CB
MET
A
405
65.920
37.479
29.505
1.00
47.17

ATOM
3788
CG
MET
A
405
66.151
36.233
30.345
1.00
48.66

ATOM
3789
SD
MET
A
405
65.913
36.487
32.115
1.00
49.07

ATOM
3790
CE
MET
A
405
67.594
36.786
32.640
1.00
50.09

ATOM
3791
C
MET
A
405
67.291
39.540
29.160
1.00
46.62

ATOM
3792
O
MET
A
405
68.500
39.339
29.092
1.00
48.06

ATOM
3793
N
ASN
A
406
66.666
40.441
28.413
1.00
46.76

ATOM
3795
CA
ASN
A
406
67.383
41.239
27.433
1.00
47.68

ATOM
3796
CB
ASN
A
406
66.467
41.675
26.295
1.00
51.33

ATOM
3797
CG
ASN
A
406
66.534
40.732
25.115
1.00
54.24

ATOM
3798
OD1
ASN
A
406
67.448
40.813
24.290
1.00
55.58

ATOM
3799
ND2
ASN
A
406
65.580
39.814
25.039
1.00
54.80

ATOM
3802
C
ASN
A
406
68.134
42.430
27.999
1.00
46.60

ATOM
3803
O
ASN
A
406
68.803
43.148
27.263
1.00
48.59

ATOM
3804
N
TYR
A
407
67.993
42.674
29.293
1.00
45.78

ATOM
3806
CA
TYR
A
407
68.732
43.760
29.922
1.00
44.83

ATOM
3807
CB
TYR
A
407
67.825
44.613
30.829
1.00
46.29

ATOM
3808
CG
TYR
A
407
68.558
45.733
31.553
1.00
45.38

ATOM
3809
CD1
TYR
A
407
68.891
46.916
30.897
1.00
45.96

ATOM
3810
CE1
TYR
A
407
69.621
47.915
31.540
1.00
47.49

ATOM
3811
CD2
TYR
A
407
68.966
45.582
32.880
1.00
45.49

ATOM
3812
CE2
TYR
A
407
69.694
46.573
33.532
1.00
44.88

ATOM
3813
CZ
TYR
A
407
70.022
47.733
32.858
1.00
47.09

ATOM
3814
OH
TYR
A
407
70.771
48.701
33.493
1.00
48.41

ATOM
3816
C
TYR
A
407
69.837
43.080
30.730
1.00
43.05

ATOM
3817
O
TYR
A
407
71.024
43.262
30.462
1.00
42.68

ATOM
3818
N
ILE
A
408
69.423
42.229
31.661
1.00
41.43

ATOM
3820
CA
ILE
A
408
70.332
41.490
32.523
1.00
40.32

ATOM
3821
CB
ILE
A
408
69.580
40.371
33.272
1.00
40.57

ATOM
3822
CG2
ILE
A
408
70.550
39.445
33.978
1.00
42.21

ATOM
3823
CG1
ILE
A
408
68.613
40.974
34.281
1.00
41.88

ATOM
3824
CD1
ILE
A
408
67.762
39.937
34.976
1.00
46.39

ATOM
3825
C
ILE
A
408
71.480
40.861
31.746
1.00
39.97

ATOM
3826
O
ILE
A
408
72.639
41.158
32.006
1.00
40.89

ATOM
3827
N
VAL
A
409
71.155
40.027
30.767
1.00
39.94

ATOM
3829
CA
VAL
A
409
72.178
39.342
29.988
1.00
39.04

ATOM
3830
CB
VAL
A
409
71.560
38.354
28.961
1.00
38.16

ATOM
3831
CG1
VAL
A
409
72.656
37.687
28.142
1.00
37.45

ATOM
3832
CG2
VAL
A
409
70.741
37.291
29.686
1.00
36.14

ATOM
3833
C
VAL
A
409
73.252
40.227
29.343
1.00
38.82

ATOM
3834
O
VAL
A
409
74.426
40.093
29.675
1.00
39.64

ATOM
3835
N
PRO
A
410
72.881
41.145
28.432
1.00
38.89

ATOM
3836
CD
PRO
A
410
71.583
41.362
27.770
1.00
38.55

ATOM
3837
CA
PRO
A
410
73.917
41.984
27.818
1.00
38.75

ATOM
3838
CB
PRO
A
410
73.207
42.562
26.597
1.00
38.19

ATOM
3839
CG
PRO
A
410
71.806
42.667
27.051
1.00
38.80

ATOM
3840
C
PRO
A
410
74.535
43.083
28.685
1.00
40.43

ATOM
3841
O
PRO
A
410
75.607
43.593
28.359
1.00
41.27

ATOM
3842
N
ILE
A
411
73.870
43.461
29.771
1.00
41.44

ATOM
3844
CA
ILE
A
411
74.404
44.503
30.649
1.00
41.02

ATOM
3845
CB
ILE
A
411
73.285
45.380
31.239
1.00
40.99

ATOM
3846
CG2
ILE
A
411
73.890
46.497
32.086
1.00
41.83

ATOM
3847
CG1
ILE
A
411
72.418
45.967
30.122
1.00
42.47

ATOM
3848
CD1
ILE
A
411
73.112
47.005
29.264
1.00
45.28

ATOM
3849
C
ILE
A
411
75.212
43.923
31.809
1.00
40.15

ATOM
3850
O
ILE
A
411
76.254
44.460
32.186
1.00
39.92

ATOM
3851
N
LEU
A
412
74.716
42.831
32.379
1.00
39.13

ATOM
3853
CA
LEU
A
412
75.373
42.185
33.506
1.00
39.13

ATOM
3854
CB
LEU
A
412
74.335
41.817
34.570
1.00
39.71

ATOM
3855
CG
LEU
A
412
73.493
42.941
35.179
1.00
38.70

ATOM
3856
CD1
LEU
A
412
72.548
42.362
36.220
1.00
36.24

ATOM
3857
CD2
LEU
A
412
74.403
43.986
35.802
1.00
39.15

ATOM
3858
C
LEU
A
412
76.209
40.945
33.175
1.00
39.67

ATOM
3859
O
LEU
A
412
77.322
40.796
33.677
1.00
41.17

ATOM
3860
N
VAL
A
413
75.678
40.060
32.336
1.00
38.13

ATOM
3862
CA
VAL
A
413
76.369
38.818
31.991
1.00
37.18

ATOM
3863
CB
VAL
A
413
75.344
37.708
31.642
1.00
38.08

ATOM
3864
CG1
VAL
A
413
76.042
36.373
31.445
1.00
39.08

ATOM
3865
CG2
VAL
A
413
74.303
37.591
32.753
1.00
35.49

ATOM
3866
C
VAL
A
413
77.477
38.893
30.926
1.00
36.23

ATOM
3867
O
VAL
A
413
78.634
38.583
31.221
1.00
36.97

ATOM
3868
N
LEU
A
414
77.134
39.296
29.702
1.00
34.70

ATOM
3870
CA
LEU
A
414
78.108
39.394
28.610
1.00
32.37

ATOM
3871
CB
LEU
A
414
77.500
40.081
27.390
1.00
31.45

ATOM
3872
CG
LEU
A
414
77.451
39.326
26.062
1.00
31.86

ATOM
3873
CG1
LEU
A
414
77.167
40.338
24.952
1.00
34.05

ATOM
3874
CD2
LEU
A
414
78.751
38.585
25.790
1.00
30.36

ATOM
3875
C
LEU
A
414
79.403
40.109
28.972
1.00
33.92

ATOM
3876
O
LEU
A
414
80.485
39.643
28.619
1.00
36.82

ATOM
3877
N
PRO
A
415
79.314
41.285
29.619
1.00
34.56

ATOM
3878
CD
PRO
A
415
78.103
42.090
29.858
1.00
34.83

ATOM
3879
CA
PRO
A
415
80.503
42.046
30.011
1.00
35.76

ATOM
3880
CB
PRO
A
415
79.915
43.149
30.883
1.00
35.11

ATOM
3881
CG
PRO
A
415
78.673
43.467
30.151
1.00
35.76

ATOM
3882
C
PRO
A
415
81.583
41.263
30.748
1.00
36.22

ATOM
3883
O
PRO
A
415
82.760
41.387
30.418
1.00
37.32

ATOM
3884
N
ARG
A
416
81.194
40.466
31.739
1.00
39.00

ATOM
3886
CA
ARG
A
416
82.167
39.686
32.501
1.00
41.92

ATOM
3887
CB
ARG
A
416
81.517
39.047
33.731
1.00
46.13

ATOM
3888
CG
ARG
A
416
81.111
40.038
34.823
1.00
52.86

ATOM
3889
CD
ARG
A
416
82.299
40.830
35.366
1.00
60.47

ATOM
3890
NE
ARG
A
416
83.287
39.986
36.040
1.00
69.03

ATOM
3892
CZ
ARG
A
416
83.205
39.589
37.309
1.00
73.10

ATOM
3893
NH1
ARG
A
416
82.174
39.955
38.062
1.00
76.24

ATOM
3896
NH2
ARG
A
416
84.163
38.833
37.834
1.00
73.45

ATOM
3899
C
ARG
A
416
82.826
38.622
31.636
1.00
42.34

ATOM
3900
O
ARG
A
416
84.031
38.405
31.717
1.00
43.31

ATOM
3901
N
VAL
A
417
82.040
37.990
30.774
1.00
42.15

ATOM
3903
CA
VAL
A
417
82.554
36.955
29.886
1.00
41.06

ATOM
3904
CB
VAL
A
417
81.418
36.302
29.091
1.00
43.59

ATOM
3905
CG1
VAL
A
417
81.976
35.261
28.127
1.00
48.62

ATOM
3906
CG2
VAL
A
417
80.414
35.672
30.038
1.00
45.02

ATOM
3907
C
VAL
A
417
83.581
37.500
28.902
1.00
38.49

ATOM
3908
O
VAL
A
417
84.658
36.929
28.729
1.00
38.46

ATOM
3909
N
ASN
A
418
83.236
38.598
28.243
1.00
36.89

ATOM
3911
CA
ASN
A
418
84.130
39.206
27.273
1.00
34.67

ATOM
3912
CB
ASN
A
418
83.448
40.370
26.564
1.00
36.25

ATOM
3913
CG
ASN
A
418
82.506
39.913
25.475
1.00
37.58

ATOM
3914
OD1
ASN
A
418
82.585
38.776
25.014
1.00
39.99

ATOM
3915
ND2
ASN
A
418
81.613
40.796
25.055
1.00
36.92

ATOM
3918
C
ASN
A
418
85.426
39.671
27.896
1.00
34.68

ATOM
3919
O
ASN
A
418
86.421
39.831
27.199
1.00
35.38

ATOM
3920
N
GLU
A
419
85.426
39.895
29.206
1.00
35.06

ATOM
3922
CA
GLU
A
419
86.640
40.336
29.879
1.00
37.31

ATOM
3923
CB
GLU
A
419
86.351
40.788
31.304
1.00
41.20

ATOM
3924
CG
GLU
A
419
87.557
41.433
31.972
1.00
49.99

ATOM
3925
CD
GLU
A
419
87.312
41.800
33.419
1.00
54.63

ATOM
3926
OE1
GLU
A
419
86.182
42.226
33.751
1.00
59.06

ATOM
3927
OE2
GLU
A
419
88.257
41.666
34.227
1.00
59.31

ATOM
3928
C
GLU
A
419
87.682
39.222
29.889
1.00
37.58

ATOM
3929
O
GLU
A
419
88.882
39.486
29.785
1.00
38.06

ATOM
3930
N
LYS
A
420
87.232
37.980
30.049
1.00
37.28

ATOM
3932
CA
LYS
A
420
88.154
36.853
30.033
1.00
37.63

ATOM
3933
CB
LYS
A
420
87.492
35.591
30.587
1.00
37.80

ATOM
3934
CG
LYS
A
420
88.379
34.342
30.510
1.00
43.22

ATOM
3935
CD
LYS
A
420
89.698
34.521
31.265
1.00
46.31

ATOM
3936
CE
LYS
A
420
90.650
33.352
31.031
1.00
48.33

ATOM
3937
NZ
LYS
A
420
91.993
33.578
31.644
1.00
48.07

ATOM
3941
C
LYS
A
420
88.610
36.631
28.593
1.00
38.72

ATOM
3942
O
LYS
A
420
89.802
36.479
28.329
1.00
41.62

ATOM
3943
N
LEU
A
421
87.663
36.659
27.657
1.00
38.62

ATOM
3945
CA
LEU
A
421
87.975
36.466
26.246
1.00
38.52

ATOM
3946
CB
LEU
A
421
86.705
36.474
25.395
1.00
36.49

ATOM
3947
CG
LEU
A
421
85.770
35.278
25.539
1.00
34.05

ATOM
3948
CD1
LEU
A
421
84.533
35.489
24.703
1.00
31.56

ATOM
3949
CD2
LEU
A
421
86.492
34.014
25.113
1.00
36.95

ATOM
3950
C
LEU
A
421
88.941
37.525
25.744
1.00
40.94

ATOM
3951
O
LEU
A
421
89.797
37.237
24.917
1.00
43.18

ATOM
3952
N
GLN
A
422
88.783
38.756
26.218
1.00
44.55

ATOM
3954
CA
GLN
A
422
89.672
39.844
25.820
1.00
48.56

ATOM
3955
CB
GLN
A
422
89.036
41.210
26.101
1.00
52.32

ATOM
3956
CG
GLN
A
422
88.278
41.821
24.914
1.00
58.07

ATOM
3957
CD
GLN
A
422
89.197
42.459
23.863
1.00
62.49

ATOM
3958
OE1
GLN
A
422
90.361
42.770
24.133
1.00
63.36

ATOM
3959
NE2
GLN
A
422
88.661
42.673
22.665
1.00
63.04

ATOM
3962
C
GLN
A
422
91.037
39.725
26.501
1.00
49.05

ATOM
3963
O
GLN
A
422
92.013
40.323
26.045
1.00
50.57

ATOM
3964
N
LYS
A
423
91.096
38.996
27.615
1.00
49.71

ATOM
3966
CA
LYS
A
423
92.366
38.777
28.305
1.00
50.46

ATOM
3967
CB
LYS
A
423
92.151
38.125
29.670
1.00
52.85

ATOM
3968
CG
LYS
A
423
93.442
37.862
30.434
1.00
56.39

ATOM
3969
CD
LYS
A
423
93.156
37.388
31.845
1.00
59.26

ATOM
3970
CE
LYS
A
423
92.354
38.432
32.611
1.00
60.80

ATOM
3971
NZ
LYS
A
423
92.070
37.998
34.006
1.00
64.66

ATOM
3975
C
LYS
A
423
93.108
37.827
27.378
1.00
49.36

ATOM
3976
O
LYS
A
423
94.320
37.945
27.174
1.00
51.82

ATOM
3977
N
GLY
A
424
92.349
36.884
26.824
1.00
46.45

ATOM
3979
CA
GLY
A
424
92.883
35.939
25.868
1.00
40.64

ATOM
3980
C
GLY
A
424
93.484
34.658
26.377
1.00
38.23

ATOM
3981
O
GLY
A
424
93.364
34.303
27.552
1.00
36.91

ATOM
3982
N
PHE
A
425
94.111
33.950
25.445
1.00
36.95

ATOM
3984
CA
PHE
A
425
94.768
32.684
25.712
1.00
34.69

ATOM
3985
CB
PHE
A
425
93.986
31.530
25.075
1.00
38.25

ATOM
3986
CG
PHE
A
425
92.570
31.402
25.571
1.00
44.42

ATOM
3987
CD1
PHE
A
425
92.294
31.343
26.937
1.00
44.31

ATOM
3988
CD2
PHE
A
425
91.508
31.345
24.671
1.00
46.34

ATOM
3989
CE1
PHE
A
425
90.986
31.235
27.399
1.00
45.62

ATOM
3990
CE2
PHE
A
425
90.192
31.236
25.125
1.00
48.05

ATOM
3991
CZ
PHE
A
425
89.933
31.181
26.492
1.00
46.50

ATOM
3992
C
PHE
A
425
96.153
32.748
25.091
1.00
31.44

ATOM
3993
O
PHE
A
425
96.316
33.236
23.982
1.00
31.46

ATOM
3994
N
PRO
A
426
97.176
32.316
25.831
1.00
29.84

ATOM
3995
CD
PRO
A
426
97.076
31.978
27.259
1.00
30.24

ATOM
3996
CA
PRO
A
426
98.571
32.299
25.396
1.00
30.20

ATOM
3997
CB
PRO
A
426
99.269
31.630
26.570
1.00
28.60

ATOM
3998
CG
PRO
A
426
98.494
32.133
27.725
1.00
31.57

ATOM
3999
C
PRO
A
426
98.777
31.489
24.123
1.00
31.10

ATOM
4000
O
PRO
A
426
98.258
30.377
23.998
1.00
34.08

ATOM
4001
N
LEU
A
427
99.570
32.033
23.203
1.00
29.97

ATOM
4003
CA
LEU
A
427
99.878
31.377
21.935
1.00
29.50

ATOM
4004
CB
LEU
A
427
99.991
32.433
20.831
1.00
28.79

ATOM
4005
CG
LEU
A
427
99.106
32.365
19.576
1.00
31.67

ATOM
4006
CD1
LEU
A
427
97.713
31.822
19.854
1.00
29.49

ATOM
4007
CD2
LEU
A
427
99.020
33.753
18.977
1.00
30.38

ATOM
4008
C
LEU
A
427
101.189
30.602
22.095
1.00
28.95

ATOM
4009
O
LEU
A
427
102.012
30.939
22.943
1.00
30.17

ATOM
4010
N
PRO
A
428
101.396
29.548
21.293
1.00
29.54

ATOM
4011
CD
PRO
A
428
100.502
29.048
20.234
1.00
29.81

ATOM
4012
CA
PRO
A
428
102.614
28.734
21.368
1.00
31.77

ATOM
4013
CB
PRO
A
428
102.218
27.492
20.584
1.00
30.20

ATOM
4014
CG
PRO
A
428
101.382
28.073
19.490
1.00
27.41

ATOM
4015
C
PRO
A
428
103.843
29.405
20.753
1.00
35.74

ATOM
4016
O
PRO
A
428
104.361
28.950
19.731
1.00
39.47

ATOM
4017
N
THR
A
429
104.323
30.472
21.379
1.00
36.82

ATOM
4019
CA
THR
A
429
105.486
31.189
20.866
1.00
36.58

ATOM
4020
CB
THR
A
429
105.200
32.694
20.735
1.00
38.98

ATOM
4021
OG1
THR
A
429
104.616
33.183
21.953
1.00
37.38

ATOM
4023
CG2
THR
A
429
104.262
32.956
19.565
1.00
41.95

ATOM
4024
C
THR
A
429
106.686
31.024
21.769
1.00
35.72

ATOM
4025
O
THR
A
429
106.567
31.108
22.994
1.00
35.83

ATOM
4026
N
PRO
A
430
107.867
30.791
21.182
1.00
34.72

ATOM
4027
CD
PRO
A
430
108.180
30.643
19.753
1.00
36.21

ATOM
4028
CA
PRO
A
430
109.069
30.629
21.995
1.00
34.61

ATOM
4029
CB
PRO
A
430
110.124
30.235
20.963
1.00
33.90

ATOM
4030
CG
PRO
A
430
109.658
30.907
19.726
1.00
33.59

ATOM
4031
C
PRO
A
430
109.388
31.946
22.691
1.00
35.01

ATOM
4032
O
PRO
A
430
108.648
32.924
22.553
1.00
37.38

ATOM
4033
N
ALA
A
431
110.457
31.973
23.471
1.00
34.16

ATOM
4035
CA
ALA
A
431
110.824
33.190
24.173
1.00
36.53

ATOM
4036
CB
ALA
A
431
111.801
32.878
25.298
1.00
36.36

ATOM
4037
C
ALA
A
431
111.416
34.241
23.243
1.00
38.15

ATOM
4038
O
ALA
A
431
111.944
33.932
22.174
1.00
39.81

ATOM
4039
N
ARG
A
432
111.270
35.495
23.641
1.00
40.43

ATOM
4041
CA
ARG
A
432
111.819
36.620
22.902
1.00
41.66

ATOM
4042
CB
ARG
A
432
113.349
36.537
22.887
1.00
44.65

ATOM
4043
CG
ARG
A
432
113.990
36.686
24.262
1.00
51.96

ATOM
4044
CD
ARG
A
432
115.516
36.654
24.185
1.00
59.79

ATOM
4045
NE
ARG
A
432
116.029
35.372
23.700
1.00
63.72

ATOM
4047
CZ
ARG
A
432
117.302
34.993
23.777
1.00
67.96

ATOM
4048
NH1
ARG
A
432
118.212
35.795
24.320
1.00
70.88

ATOM
4051
NH2
ARG
A
432
117.668
33.804
23.314
1.00
68.07

ATOM
4054
C
ARG
A
432
111.293
36.898
21.499
1.00
40.87

ATOM
4055
O
ARG
A
432
111.963
37.567
20.721
1.00
42.99

ATOM
4056
N
VAL
A
433
110.103
36.414
21.166
1.00
40.50

ATOM
4058
CA
VAL
A
433
109.538
36.693
19.847
1.00
39.69

ATOM
4059
CB
VAL
A
433
109.325
35.415
18.982
1.00
39.93

ATOM
4060
CG1
VAL
A
433
110.588
34.575
18.943
1.00
39.03

ATOM
4061
CG2
VAL
A
433
108.134
34.608
19.470
1.00
39.91

ATOM
4062
C
VAL
A
433
108.206
37.399
20.024
1.00
41.27

ATOM
4063
O
VAL
A
433
107.538
37.240
21.048
1.00
43.57

ATOM
4064
N
GLN
A
434
107.845
38.223
19.053
1.00
41.32

ATOM
4066
CA
GLN
A
434
106.583
38.939
19.104
1.00
41.91

ATOM
4067
CB
GLN
A
434
106.802
40.411
19.454
1.00
45.76

ATOM
4068
CG
GLN
A
434
105.706
41.018
20.335
1.00
52.61

ATOM
4069
CD
GLN
A
434
105.850
40.687
21.829
1.00
56.74

ATOM
4070
OE1
GLN
A
434
105.372
41.436
22.681
1.00
58.13

ATOM
4071
NE2
GLN
A
434
106.512
39.579
22.149
1.00
57.45

ATOM
4074
C
GLN
A
434
106.005
38.804
17.716
1.00
40.30

ATOM
4075
O
GLN
A
434
106.745
38.821
16.732
1.00
40.86

ATOM
4076
N
LEU
A
435
104.695
38.614
17.642
1.00
39.20

ATOM
4078
CA
LEU
A
435
104.018
38.439
16.366
1.00
39.99

ATOM
4079
CB
LEU
A
435
102.965
37.338
16.501
1.00
38.11

ATOM
4080
CG
LEU
A
435
103.347
36.088
17.309
1.00
37.55

ATOM
4081
CD1
LEU
A
435
102.118
35.238
17.538
1.00
37.75

ATOM
4082
CD2
LEU
A
435
104.426
35.281
16.613
1.00
36.46

ATOM
4083
C
LEU
A
435
103.358
39.739
15.916
1.00
41.18

ATOM
4084
O
LEU
A
435
102.660
40.387
16.695
1.00
42.90

ATOM
4085
N
TYR
A
436
103.590
40.125
14.665
1.00
42.57

ATOM
4087
CA
TYR
A
436
103.004
41.348
14.116
1.00
43.80

ATOM
4088
CB
TYR
A
436
104.021
42.510
14.120
1.00
43.48

ATOM
4089
CG
TYR
A
436
105.232
42.328
13.224
1.00
43.66

ATOM
4090
CD1
TYR
A
436
106.259
41.452
13.573
1.00
43.96

ATOM
4091
CE1
TYR
A
436
107.364
41.271
12.743
1.00
44.63

ATOM
4092
CD2
TYR
A
436
105.345
43.028
12.020
1.00
43.04

ATOM
4093
CE2
TYR
A
436
106.448
42.852
11.181
1.00
43.53

ATOM
4094
CZ
TYR
A
436
107.452
41.970
11.549
1.00
44.29

ATOM
4095
OH
TYR
A
436
108.528
41.757
10.711
1.00
44.66

ATOM
4097
C
TYR
A
436
102.457
41.090
12.712
1.00
43.77

ATOM
4098
O
TYR
A
436
102.729
40.046
12.122
1.00
45.49

ATOM
4099
N
ASN
A
437
101.687
42.042
12.189
1.00
45.09

ATOM
4101
CA
ASN
A
437
101.069
41.932
10.865
1.00
45.97

ATOM
4102
CB
ASN
A
437
102.083
42.231
9.750
1.00
51.76

ATOM
4103
CG
ASN
A
437
102.161
43.720
9.416
1.00
57.75

ATOM
4104
OD1
ASN
A
437
102.832
44.492
10.105
1.00
59.59

ATOM
4105
ND2
ASN
A
437
101.450
44.131
8.370
1.00
60.25

ATOM
4108
C
ASN
A
437
100.385
40.581
10.665
1.00
44.47

ATOM
4109
O
ASN
A
437
100.743
39.797
9.786
1.00
44.02

ATOM
4110
N
VAL
A
438
99.360
40.344
11.475
1.00
44.00

ATOM
4112
CA
VAL
A
438
98.622
39.091
11.444
1.00
43.09

ATOM
4113
CB
VAL
A
438
98.214
38.646
12.871
1.00
43.35

ATOM
4114
CG1
VAL
A
438
99.425
38.629
13.786
1.00
43.74

ATOM
4115
CG2
VAL
A
438
97.143
39.562
13.433
1.00
43.99

ATOM
4116
C
VAL
A
438
97.374
39.101
10.579
1.00
41.42

ATOM
4117
O
VAL
A
438
96.740
40.139
10.377
1.00
39.58

ATOM
4118
N
VAL
A
439
97.018
37.912
10.110
1.00
41.86

ATOM
4120
CA
VAL
A
439
95.839
37.689
9.291
1.00
43.18

ATOM
4121
CB
VAL
A
439
96.202
37.377
7.829
1.00
42.54

ATOM
4122
CG1
VAL
A
439
96.568
38.646
7.104
1.00
46.06

ATOM
4123
CG2
VAL
A
439
97.351
36.391
7.770
1.00
41.82

ATOM
4124
C
VAL
A
439
95.117
36.482
9.866
1.00
43.37

ATOM
4125
O
VAL
A
439
95.733
35.446
10.103
1.00
45.02

ATOM
4126
N
LEU
A
440
93.829
36.631
10.141
1.00
43.45

ATOM
4128
CA
LEU
A
440
93.041
35.535
10.681
1.00
42.92

ATOM
4129
CB
LEU
A
440
92.355
35.956
11.978
1.00
42.49

ATOM
4130
CG
LEU
A
440
93.220
36.062
13.234
1.00
42.93

ATOM
4131
CD1
LEU
A
440
93.920
34.745
13.462
1.00
44.28

ATOM
4132
CD2
LEU
A
440
94.231
37.181
13.111
1.00
45.59

ATOM
4133
C
LEU
A
440
92.008
35.132
9.643
1.00
44.03

ATOM
4134
O
LEU
A
440
91.017
35.831
9.446
1.00
45.13

ATOM
4135
N
GLN
A
441
92.268
34.029
8.947
1.00
44.00

ATOM
4137
CA
GLN
A
441
91.363
33.536
7.910
1.00
43.66

ATOM
4138
CB
GLN
A
441
92.148
33.058
6.678
1.00
48.64

ATOM
4139
CG
GLN
A
441
92.881
34.113
5.860
1.00
54.68

ATOM
4140
CD
GLN
A
441
93.556
33.515
4.627
1.00
57.71

ATOM
4141
OE1
GLN
A
441
93.111
32.495
4.093
1.00
59.57

ATOM
4142
NE2
GLN
A
441
94.637
34.141
4.179
1.00
60.18

ATOM
4145
C
GLN
A
441
90.528
32.355
8.390
1.00
41.14

ATOM
4146
O
GLN
A
441
91.055
31.249
8.541
1.00
41.88

ATOM
4147
N
PRO
A
442
89.217
32.553
8.613
1.00
38.75

ATOM
4148
CD
PRO
A
442
88.444
33.805
8.553
1.00
39.00

ATOM
4149
CA
PRO
A
442
88.372
31.442
9.065
1.00
35.99

ATOM
4150
CB
PRO
A
442
87.049
32.131
9.381
1.00
36.27

ATOM
4151
CG
PRO
A
442
87.038
33.295
8.450
1.00
38.58

ATOM
4152
C
PRO
A
442
88.234
30.403
7.952
1.00
34.89

ATOM
4153
O
PRO
A
442
88.109
30.751
6.780
1.00
37.34

ATOM
4154
N
HIS
A
443
88.332
29.130
8.317
1.00
32.88

ATOM
4156
CA
HIS
A
443
88.242
28.036
7.361
1.00
30.71

ATOM
4157
CB
HIS
A
443
89.610
27.377
7.172
1.00
31.17

ATOM
4158
CG
HIS
A
443
90.508
28.103
6.225
1.00
29.53

ATOM
4159
CD2
HIS
A
443
91.098
27.702
5.076
1.00
27.37

ATOM
4160
ND1
HIS
A
443
90.868
29.421
6.400
1.00
31.12

ATOM
4162
CE1
HIS
A
443
91.635
29.804
5.397
1.00
30.58

ATOM
4163
NE2
HIS
A
443
91.790
28.779
4.580
1.00
29.90

ATOM
4165
C
HIS
A
443
87.263
27.003
7.863
1.00
31.31

ATOM
4166
O
HIS
A
443
86.698
27.157
8.936
1.00
36.03

ATOM
4167
N
GLN
A
444
87.058
25.948
7.086
1.00
33.00

ATOM
4169
CA
GLN
A
444
86.136
24.896
7.481
1.00
33.08

ATOM
4170
CB
GLN
A
444
85.802
24.000
6.282
1.00
35.23

ATOM
4171
CG
GLN
A
444
84.829
22.860
6.570
1.00
37.52

ATOM
4172
CD
GLN
A
444
83.436
23.337
6.954
1.00
41.28

ATOM
4173
OE1
GLN
A
444
83.142
24.531
6.941
1.00
42.98

ATOM
4174
NE2
GLN
A
444
82.570
22.395
7.298
1.00
44.68

ATOM
4177
C
GLN
A
444
86.735
24.069
8.613
1.00
32.22

ATOM
4178
O
GLN
A
444
87.720
23.360
8.416
1.00
34.24

ATOM
4179
N
ASN
A
445
86.175
24.230
9.808
1.00
29.86

ATOM
4181
CA
ASN
A
445
86.584
23.492
11.003
1.00
28.34

ATOM
4182
CB
ASN
A
445
86.628
21.984
10.714
1.00
27.65

ATOM
4183
CG
ASN
A
445
85.272
21.427
10.319
1.00
28.84

ATOM
4184
OD1
ASN
A
445
85.155
20.637
9.385
1.00
33.08

ATOM
4185
ND2
ASN
A
445
84.233
21.850
11.022
1.00
32.64

ATOM
4188
C
ASN
A
445
87.863
23.950
11.709
1.00
27.86

ATOM
4189
O
ASN
A
445
88.318
23.306
12.658
1.00
30.31

ATOM
4190
N
PHE
A
446
88.436
25.064
11.272
1.00
26.55

ATOM
4192
CA
PHE
A
446
89.639
25.582
11.904
1.00
25.16

ATOM
4193
CB
PHE
A
446
90.858
24.688
11.626
1.00
28.26

ATOM
4194
CG
PHE
A
446
91.407
24.796
10.233
1.00
29.75

ATOM
4195
CD1
PHE
A
446
90.953
23.956
9.223
1.00
29.14

ATOM
4196
CD2
PHE
A
446
92.413
25.711
9.940
1.00
32.05

ATOM
4197
CE1
PHE
A
446
91.492
24.020
7.950
1.00
26.24

ATOM
4198
CE2
PHE
A
446
92.961
25.784
8.662
1.00
30.94

ATOM
4199
CZ
PHE
A
446
92.500
24.936
7.667
1.00
29.55

ATOM
4200
C
PHE
A
446
89.906
27.020
11.506
1.00
25.07

ATOM
4201
O
PHE
A
446
89.372
27.508
10.513
1.00
24.16

ATOM
4202
N
LEU
A
447
90.718
27.697
12.306
1.00
26.36

ATOM
4204
CA
LEU
A
447
91.059
29.091
12.076
1.00
25.79

ATOM
4205
CB
LEU
A
447
90.825
29.880
13.365
1.00
27.64

ATOM
4206
CG
LEU
A
447
91.097
31.384
13.422
1.00
28.75

ATOM
4207
CD1
LEU
A
447
90.193
32.125
12.449
1.00
27.40

ATOM
4208
CD2
LEU
A
447
90.863
31.875
14.843
1.00
25.78

ATOM
4209
C
LEU
A
447
92.508
29.221
11.635
1.00
25.68

ATOM
4210
O
LEU
A
447
93.398
28.619
12.223
1.00
26.90

ATOM
4211
N
LEU
A
448
92.738
30.000
10.589
1.00
26.87

ATOM
4213
CA
LEU
A
448
94.080
30.199
10.084
1.00
26.96

ATOM
4214
CB
LEU
A
448
94.074
30.247
8.559
1.00
26.42

ATOM
4215
CG
LEU
A
448
95.432
30.045
7.886
1.00
25.05

ATOM
4216
CD1
LEU
A
448
96.040
28.738
8.331
1.00
25.88

ATOM
4217
CD2
LEU
A
448
95.273
30.049
6.396
1.00
29.10

ATOM
4218
C
LEU
A
448
94.627
31.493
10.651
1.00
29.88

ATOM
4219
O
LEU
A
448
94.005
32.552
10.530
1.00
28.70

ATOM
4220
N
PHE
A
449
95.788
31.386
11.283
1.00
32.23

ATOM
4222
CA
PHE
A
449
96.469
32.511
11.897
1.00
32.39

ATOM
4223
CB
PHE
A
449
96.655
32.234
13.394
1.00
31.41

ATOM
4224
CG
PHE
A
449
97.511
33.243
14.100
1.00
31.44

ATOM
4225
CD1
PHE
A
449
98.897
33.160
14.046
1.00
32.18

ATOM
4226
CD2
PHE
A
449
96.934
34.296
14.797
1.00
35.10

ATOM
4227
CE1
PHE
A
449
99.695
34.111
14.671
1.00
32.81

ATOM
4228
CE2
PHE
A
449
97.725
35.257
15.429
1.00
34.26

ATOM
4229
CZ
PHE
A
449
99.106
35.162
15.363
1.00
33.12

ATOM
4230
C
PHE
A
449
97.829
32.685
11.228
1.00
34.46

ATOM
4231
O
PHE
A
449
98.717
31.865
11.420
1.00
38.92

ATOM
4232
N
GLY
A
450
97.990
33.738
10.439
1.00
34.70

ATOM
4234
CA
GLY
A
450
99.262
33.982
9.781
1.00
33.42

ATOM
4235
C
GLY
A
450
99.901
35.207
10.397
1.00
35.08

ATOM
4236
O
GLY
A
450
99.194
36.140
10.784
1.00
36.42

ATOM
4237
N
ALA
A
451
101.225
35.234
10.491
1.00
33.89

ATOM
4239
CA
ALA
A
451
101.889
36.383
11.092
1.00
33.95

ATOM
4240
CB
ALA
A
451
101.649
36.384
12.587
1.00
31.78

ATOM
4241
C
ALA
A
451
103.382
36.454
10.815
1.00
34.43

ATOM
4242
O
ALA
A
451
103.986
35.489
10.335
1.00
36.02

ATOM
4243
N
ASP
A
452
103.954
37.628
11.055
1.00
33.44

ATOM
4245
CA
ASP
A
452
105.381
37.847
10.885
1.00
35.01

ATOM
4246
CB
ASP
A
452
105.670
39.186
10.196
1.00
37.76

ATOM
4247
CG
ASP
A
452
105.437
39.144
8.696
1.00
40.65

ATOM
4248
OD1
ASP
A
452
105.743
38.106
8.074
1.00
42.78

ATOM
4249
OD2
ASP
A
452
104.961
40.159
8.134
1.00
42.90

ATOM
4250
C
ASP
A
452
105.913
37.875
12.306
1.00
35.28

ATOM
4251
O
ASP
A
452
105.196
38.247
13.237
1.00
33.85

ATOM
4252
N
VAL
A
453
107.174
37.509
12.473
1.00
37.44

ATOM
4254
CA
VAL
A
453
107.771
37.468
13.798
1.00
38.73

ATOM
4255
CB
VAL
A
453
108.253
36.034
14.138
1.00
39.37

ATOM
4256
CG1
VAL
A
453
108.678
35.955
15.591
1.00
40.45

ATOM
4257
CG2
VAL
A
453
107.169
35.004
13.819
1.00
37.45

ATOM
4258
C
VAL
A
453
108.970
38.398
13.899
1.00
39.49

ATOM
4259
O
VAL
A
453
109.669
38.641
12.914
1.00
40.46

ATOM
4260
N
VAL
A
454
109.190
38.929
15.092
1.00
39.41

ATOM
4262
CA
VAL
A
454
110.324
39.796
15.331
1.00
40.55

ATOM
4263
CB
VAL
A
454
109.895
41.280
15.511
1.00
41.60

ATOM
4264
CG1
VAL
A
454
108.859
41.423
16.605
1.00
42.90

ATOM
4265
CG2
VAL
A
454
111.105
42.149
15.798
1.00
43.42

ATOM
4266
C
VAL
A
454
111.037
39.256
16.561
1.00
41.20

ATOM
4267
O
VAL
A
454
110.440
39.115
17.626
1.00
41.61

ATOM
4268
N
TYR
A
455
112.284
38.851
16.376
1.00
42.91

ATOM
4270
CA
TYR
A
455
113.084
38.309
17.460
1.00
45.62

ATOM
4271
CB
TYR
A
455
114.015
37.227
16.908
1.00
44.83

ATOM
4272
CG
TYR
A
455
115.038
36.684
17.881
1.00
44.58

ATOM
4273
CD1
TYR
A
455
114.682
35.774
18.875
1.00
43.02

ATOM
4274
CE1
TYR
A
455
115.644
35.246
19.739
1.00
44.27

ATOM
4275
CD2
TYR
A
455
116.377
37.053
17.778
1.00
46.42

ATOM
4276
CE2
TYR
A
455
117.341
36.535
18.631
1.00
46.69

ATOM
4277
CZ
TYR
A
455
116.973
35.634
19.607
1.00
46.43

ATOM
4278
OH
TYR
A
455
117.944
35.141
20.445
1.00
49.56

ATOM
4280
C
TYR
A
455
113.864
39.443
18.128
1.00
49.88

ATOM
4281
O
TYR
A
455
114.558
40.213
17.455
1.00
49.95

ATOM
4282
N
LYS
A
456
113.694
39.552
19.444
1.00
54.41

ATOM
4284
CA
LYS
A
456
114.337
40.570
20.270
1.00
59.38

ATOM
4285
CB
LYS
A
456
113.760
40.514
21.693
1.00
61.68

ATOM
4286
CG
LYS
A
456
114.401
41.475
22.692
1.00
66.56

ATOM
4287
CD
LYS
A
456
114.016
41.153
24.140
1.00
68.38

ATOM
4288
CE
LYS
A
456
112.538
41.396
24.409
1.00
70.09

ATOM
4289
NZ
LYS
A
456
112.154
41.067
25.812
1.00
71.48

ATOM
4293
C
LYS
A
456
115.855
40.382
20.311
1.00
62.37

ATOM
4294
OT1
LYS
A
456
116.324
39.430
20.976
1.00
64.57

ATOM
4295
OT2
LYS
A
456
116.559
41.196
19.673
1.00
66.00

ATOM
4296
C1
PC
A
777
121.817
32.468
19.343
1.00
72.53

ATOM
4297
C2
PC
A
777
121.094
31.121
19.465
1.00
63.82

ATOM
4298
C3
PC
A
777
119.917
31.017
18.492
1.00
59.16

ATOM
4299
C4
PC
A
777
123.302
33.354
23.035
1.00
94.69

ATOM
4300
C5
PC
A
777
124.151
34.553
23.445
1.00
98.10

ATOM
4301
C6
PC
A
777
125.683
33.126
24.652
1.00
99.68

ATOM
4302
C7
PC
A
777
126.361
35.328
24.003
1.00
100.00

ATOM
4303
C8
PC
A
777
126.086
33.627
22.335
1.00
100.00

ATOM
4304
C31
PC
A
777
122.736
29.776
18.047
1.00
54.84

ATOM
4305
C32
PC
A
777
122.337
30.654
16.869
1.00
51.64

ATOM
4306
C33
PC
A
777
122.254
29.878
15.549
1.00
47.76

ATOM
4307
C34
PC
A
777
123.590
29.237
15.169
1.00
42.03

ATOM
4308
C35
PC
A
777
123.429
28.173
14.085
1.00
39.41

ATOM
4309
C36
PC
A
777
122.582
28.674
12.916
1.00
36.18

ATOM
4310
C37
PC
A
777
121.581
27.622
12.463
1.00
33.16

ATOM
4311
C38
PC
A
777
120.679
28.158
11.377
1.00
31.40

ATOM
4312
C39
PC
A
777
119.610
29.062
11.951
1.00
36.47

ATOM
4313
C40
PC
A
777
118.543
28.263
12.682
1.00
40.19

ATOM
4314
C41
PC
A
777
117.191
28.383
12.004
1.00
39.41

ATOM
4315
C42
PC
A
777
116.468
27.050
11.956
1.00
41.86

ATOM
4316
C43
PC
A
777
115.409
26.958
13.041
1.00
43.49

ATOM
4317
C44
PC
A
777
114.326
25.951
12.669
1.00
46.22

ATOM
4318
C45
PC
A
777
113.126
26.048
13.604
1.00
47.77

ATOM
4319
C46
PC
A
777
112.271
24.786
13.561
1.00
48.67

ATOM
4320
C47
PC
A
777
111.948
24.277
14.964
1.00
48.62

ATOM
4321
C48
PC
A
777
110.492
24.449
15.368
1.00
45.72

ATOM
4322
C11
PC
A
777
118.509
32.389
17.081
1.00
49.62

ATOM
4323
C12
PC
A
777
117.647
31.121
17.072
1.00
45.91

ATOM
4324
C13
PC
A
777
116.542
31.091
16.014
1.00
42.05

ATOM
4325
C14
PC
A
777
115.753
32.392
15.973
1.00
37.88

ATOM
4326
C15
PC
A
777
114.269
32.149
16.004
1.00
39.34

ATOM
4327
C16
PC
A
777
113.573
32.877
14.874
1.00
39.38

ATOM
4328
C17
PC
A
777
112.066
32.688
14.951
1.00
43.09

ATOM
4329
C18
PC
A
777
111.446
32.535
13.566
1.00
45.42

ATOM
4330
C19
PC
A
777
111.500
31.093
13.082
1.00
47.16

ATOM
4331
C20
PC
A
777
110.158
30.413
13.236
1.00
46.62

ATOM
4332
C21
PC
A
777
109.917
30.004
14.673
1.00
46.65

ATOM
4333
C22
PC
A
777
108.444
29.836
14.942
1.00
46.97

ATOM
4334
C23
PC
A
777
107.922
30.916
15.868
1.00
47.30

ATOM
4335
C24
PC
A
777
106.409
30.835
16.001
1.00
50.05

ATOM
4336
C25
PC
A
777
105.996
29.898
17.121
1.00
50.59

ATOM
4337
C26
PC
A
777
105.783
28.490
16.612
1.00
53.56

ATOM
4338
C27
PC
A
777
106.972
27.593
16.941
1.00
56.03

ATOM
4339
C28
PC
A
777
107.348
26.625
15.831
1.00
55.75

ATOM
4340
O11
PC
A
777
118.194
33.427
16.467
1.00
52.98

ATOM
4341
O31
PC
A
777
123.576
28.862
17.906
1.00
56.48

ATOM
4342
O2
PC
A
777
122.068
30.020
19.350
1.00
61.36

ATOM
4343
O3
PC
A
777
119.731
32.307
17.866
1.00
53.04

ATOM
4344
O1P
PC
A
777
121.661
35.196
20.857
1.00
89.42

ATOM
4345
O2P
PC
A
777
120.059
33.339
21.280
1.00
90.46

ATOM
4346
O3P
PC
A
777
122.419
32.815
20.622
1.00
84.15

ATOM
4347
O4P
PC
A
777
121.916
33.769
22.889
1.00
91.71

ATOM
4348
N
PC
A
777
125.571
34.153
23.607
1.00
99.82

ATOM
4349
P
PC
A
777
121.516
33.779
21.409
1.00
89.00

ATOM
4350
C1
PC
A
778
87.797
32.791
33.686
1.00
88.29

ATOM
4351
C2
PC
A
778
86.274
32.868
33.502
1.00
83.64

ATOM
4352
C3
PC
A
778
85.739
31.590
32.830
1.00
80.89

ATOM
4353
C31
PC
A
778
84.282
33.619
34.787
1.00
76.37

ATOM
4354
C32
PC
A
778
83.704
33.859
33.391
1.00
70.52

ATOM
4355
C33
PC
A
778
82.344
33.215
33.178
1.00
63.44

ATOM
4356
C34
PC
A
778
81.311
34.250
32.803
1.00
56.98

ATOM
4357
C35
PC
A
778
80.231
34.364
33.854
1.00
51.89

ATOM
4358
C36
PC
A
778
79.088
33.400
33.593
1.00
48.39

ATOM
4359
C37
PC
A
778
78.611
33.453
32.155
1.00
47.51

ATOM
4360
C38
PC
A
778
77.593
32.352
31.868
1.00
47.46

ATOM
4361
C39
PC
A
778
78.231
31.153
31.171
1.00
45.28

ATOM
4362
C40
PC
A
778
78.154
31.261
29.654
1.00
43.25

ATOM
4363
C41
PC
A
778
79.381
31.957
29.099
1.00
40.88

ATOM
4364
C42
PC
A
778
79.324
32.082
27.589
1.00
42.02

ATOM
4365
C43
PC
A
778
78.064
32.803
27.130
1.00
43.52

ATOM
4366
C44
PC
A
778
77.971
34.223
27.684
1.00
42.21

ATOM
4367
C45
PC
A
778
76.563
34.546
28.171
1.00
42.30

ATOM
4368
C46
PC
A
778
75.523
34.335
27.077
1.00
42.97

ATOM
4369
C47
PC
A
778
74.121
34.185
27.662
1.00
42.80

ATOM
4370
C48
PC
A
778
73.131
33.504
26.727
1.00
43.31

ATOM
4371
C11
PC
A
778
86.101
31.542
30.412
1.00
71.27

ATOM
4372
C12
PC
A
778
84.804
32.359
30.441
1.00
66.82

ATOM
4373
C13
PC
A
778
83.700
31.845
29.548
1.00
59.12

ATOM
4374
C14
PC
A
778
83.836
32.380
28.141
1.00
55.92

ATOM
4375
C15
PC
A
778
82.896
31.671
27.184
1.00
53.76

ATOM
4376
C16
PC
A
778
82.613
30.248
27.633
1.00
52.97

ATOM
4377
C17
PC
A
778
83.562
29.250
26.990
1.00
50.51

ATOM
4378
C18
PC
A
778
84.990
29.415
27.480
1.00
47.60

ATOM
4379
C19
PC
A
778
85.860
30.046
26.408
1.00
47.69

ATOM
4380
C20
PC
A
778
86.359
29.011
25.411
1.00
44.90

ATOM
4381
C21
PC
A
778
85.271
28.598
24.439
1.00
44.44

ATOM
4382
C22
PC
A
778
85.574
29.064
23.038
1.00
44.15

ATOM
4383
C23
PC
A
778
86.167
30.453
23.044
1.00
43.99

ATOM
4384
C24
PC
A
778
87.670
30.411
22.853
1.00
42.63

ATOM
4385
C25
PC
A
778
88.068
31.161
21.599
1.00
43.28

ATOM
4386
C26
PC
A
778
87.733
32.642
21.693
1.00
41.66

ATOM
4387
C27
PC
A
778
88.852
33.492
21.119
1.00
40.33

ATOM
4388
C28
PC
A
778
90.094
33.503
21.969
1.00
37.09

ATOM
4389
O11
PC
A
778
86.692
31.253
29.343
1.00
72.85

ATOM
4390
O31
PC
A
778
83.619
33.857
35.833
1.00
78.26

ATOM
4391
O2
PC
A
778
85.652
33.065
34.823
1.00
81.22

ATOM
4392
O3
PC
A
778
86.615
31.154
31.736
1.00
75.71

ATOM
4393
O1P
PC
A
778
89.401
31.823
36.960
1.00
100.00

ATOM
4394
O2P
PC
A
778
89.563
33.853
35.511
1.00
100.00

ATOM
4395
O3P
PC
A
778
88.125
31.917
34.809
1.00
96.24

ATOM
4396
O4P
PC
A
778
87.424
33.342
36.757
1.00
100.00

ATOM
4397
P
PC
A
778
88.628
32.739
36.008
1.00
100.00

ATOM
4398
OH2
HOH
A
901
116.815
15.747
16.799
1.00
43.90

ATOM
4401
OH2
HOH
A
902
107.439
22.033
22.778
1.00
44.99

ATOM
4404
OH2
HOH
A
903
115.201
26.524
27.768
1.00
47.84

ATOM
4407
OH2
HOH
A
904
83.653
23.737
13.286
1.00
22.80

ATOM
4410
OH2
HOH
A
905
76.576
23.779
22.886
1.00
55.25

ATOM
4413
OH2
HOH
A
906
101.110
43.595
19.882
1.00
44.52

ATOM
4416
OH2
HOH
A
907
80.990
19.920
23.229
1.00
48.61

ATOM
4419
OH2
HOH
A
908
141.374
35.733
18.039
1.00
56.87

ATOM
4422
OH2
HOH
A
909
81.958
22.677
23.953
1.00
61.10

ATOM
4425
OH2
HOH
A
910
152.059
36.697
−0.688
1.00
62.06

ATOM
4428
OH2
HOH
A
911
139.649
24.807
2.271
1.00
53.67

ATOM
4431
OH2
HOH
A
912
124.594
31.177
0.772
1.00
55.59

ATOM
4434
OH2
HOH
A
913
121.471
25.892
1.624
1.00
38.62

ATOM
4437
OH2
HOH
A
914
114.402
25.412
0.380
1.00
31.16

ATOM
4440
OH2
HOH
A
915
147.939
35.177
−2.062
1.00
45.61

ATOM
4443
OH2
HOH
A
916
74.995
34.193
14.634
1.00
73.76

ATOM
4446
OH2
HOH
A
917
105.633
17.580
14.444
1.00
37.72

ATOM
4449
OH2
HOH
A
918
71.679
28.574
37.701
1.00
51.80

ATOM
4452
OH2
HOH
A
919
104.762
14.189
10.052
1.00
57.21

ATOM
4455
OH2
HOH
A
920
80.378
28.515
41.681
1.00
81.97

ATOM
4458
OH2
HOH
A
921
80.215
25.918
35.227
1.00
29.12

ATOM
4461
OH2
HOH
A
922
79.054
35.414
40.975
1.00
41.95

ATOM
4464
OH2
HOH
A
923
65.692
27.690
51.372
1.00
65.22

ATOM
4467
OH2
HOH
A
924
88.914
24.630
4.689
1.00
48.96

ATOM
4470
OH2
HOH
A
925
100.082
22.695
34.405
1.00
48.58

ATOM
4473
OH2
HOH
A
926
76.929
19.455
31.644
1.00
86.93

ATOM
4476
OH2
HOH
A
927
171.524
31.723
13.880
1.00
59.94

ATOM
4479
OH2
HOH
A
928
108.006
35.100
24.514
1.00
49.31

ATOM
4482
OH2
HOH
A
929
141.049
21.649
5.587
1.00
42.12

ATOM
4485
OH2
HOH
A
930
110.883
40.970
11.363
1.00
35.61

ATOM
4488
OH2
HOH
A
931
74.360
34.525
47.158
1.00
75.14

ATOM
4491
OH2
HOH
A
932
68.751
40.894
44.809
1.00
43.22

ATOM
4494
OH2
HOH
A
933
59.758
29.313
23.460
1.00
61.69

ATOM
4497
OH2
HOH
A
934
95.173
16.341
20.293
1.00
48.05

ATOM
4500
OH2
HOH
A
935
111.623
41.720
8.640
1.00
53.02

ATOM
4503
OH2
HOH
A
936
105.604
16.201
11.554
1.00
71.57

ATOM
4506
OH2
HOH
A
937
97.160
30.542
3.465
1.00
58.62

ATOM
4509
OH2
HOH
A
938
108.492
10.703
6.225
1.00
76.16

ATOM
4512
OH2
HOH
A
939
135.408
44.678
13.765
1.00
61.58

ATOM
4515
OH2
HOH
A
940
91.469
31.723
41.685
1.00
41.59

ATOM
4518
OH2
HOH
A
941
164.580
32.799
18.975
1.00
48.97

ATOM
4521
OH2
HOH
A
942
157.888
29.985
20.509
1.00
63.61

ATOM
4524
OH2
HOH
A
943
121.776
21.112
25.392
1.00
61.93

ATOM
4527
OH2
HOH
A
944
96.503
38.299
34.009
1.00
64.71

ATOM
4530
OH2
HOH
A
945
96.403
17.036
28.115
1.00
76.51

ATOM
4533
OH2
HOH
A
946
88.114
18.204
31.407
1.00
52.33

ATOM
4536
OH2
HOH
A
947
81.217
23.098
12.608
1.00
35.93

ATOM
4539
OH2
HOH
A
948
126.713
24.917
0.514
1.00
82.50

TER

END

[0224]

6

Atom

Type
Residue # X Y Z OCC B

REMARK
3

REMARK
3
REFINEMENT.

REMARK
3
PROGRAM
X-PLOR (online)
3.843

REMARK
3
AUTHORS
BRUNGER

REMARK
3

REMARK
3
DATA USED IN REFINEMENT.

REMARK
3
RESOLUTION RANGE HIGH (ANGSTROMS)
2.40

REMARK
3
RESOLUTION RANGE LOW (ANGSTROMS)
50.00

REMARK
3
DATA CUTOFF (SIGMA (F))
0.0

REMARK
3
DATA CUTOFF HIGH (ABS (F))
100000.00

REMARK
3
DATA CUTOFF LOW (ABS (F))
0.010000

REMARK
3
COMPLETENESS (WORKING + TEST) (%)
92.7

REMARK
3
NUMBER OF REFLECTIONS
18908

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 SET)
0.225

REMARK
3
FREE R VALUE
0.295

REMARK
3
FREE R VALUE TEST SET SIZE (%)
10.2

REMARK
3
FREE R VALUE TEST SET COUNT
1926

REMARK
3
ESTIMATED ERROR OF FREE R VALUE
0.007

REMARK
3

REMARK
3
FIT IN THE HIGHEST RESOLUTION BIN.

REMARK
3
TOTAL NUMBER OF BINS USED
6

REMARK
3
BIN RESOLUTION RANGE HIGH (A)
2.40

REMARK
3
BIN RESOLUTION RANGE LOW (A)
2.55

REMARK
3
BIN COMPLETENESS (WORKING + TEST) (%)
94.1

REMARK
3
REFLECTIONS IN BIN (WORKING SET)
2875

REMARK
3
BIN R VALUE (WORKING SET)
0.368

REMARK
3
BIN FREE R VALUE
0.455

REMARK
3
BIN FREE R VALUE TEST SET SIZE (%)
8.7

REMARK
3
BIN FREE R VALUE TEST SET COUNT
275

REMARK
3
ESTIMATED ERROR OF BIN FREE R VALUE
0.027

REMARK
3

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

REMARK
3
PROTEIN ATOMS
3531

REMARK
3
NUCLEIC ACID ATOMS
0

REMARK
3
HETEROGEN ATOMS
102

REMARK
3
SOLVENT ATOMS
48

REMARK
3

REMARK
3
B VALUES.

REMARK
3
FROM WILSON PLOT (A**2)
45.0

REMARK
3
MEAN B VALUE (OVERALL, A**2)
45.0

REMARK
3
OVERALL ANISOTROPIC B VALUE.

REMARK
3
B11 (A**2)
−11.35

REMARK
3
B22 (A**2)
6.33

REMARK
3
B33 (A**2)
5.02

REMARK
3
B12 (A**2)
0.00

REMARK
3
B13 (A**2)
7.70

REMARK
3
B23 (A**2)
0.00

REMARK
3

REMARK
3
ESTIMATED COORDINATE ERROR.

REMARK
3
ESD FROM LUZZATI PLOT (A)
0.34

REMARK
3
ESD FROM SIGMAA (A)
0.47

REMARK
3
LOW RESOLUTION CUTOFF (A)
5.00

REMARK
3

REMARK
3
CROSS-VALIDATED ESTIMATED COORDINATE ERROR.

REMARK
3
ESD FROM C-V LUZZATI PLOT (A)
0.45

REMARK
3
ESD FROM C-V SIGMAA (A)
0.46

REMARK
3

REMARK
3
RMS DEVIATIONS FROM IDEAL VALUES.

REMARK
3
BOND LENGTHS (A)
0.007

REMARK
3
BOND ANGLES (DEGREES)
1.4

REMARK
3
DIHEDRAL ANGLES (DEGREES)
26.1

REMARK
3
IMPROPER ANGLES (DEGREES)
1.24

REMARK
3

REMARK
3

REMARK
3
ISOTROPIC THERMAL FACTOR RESTRAINTS.
RMS
SIGMA

REMARK
3
MAIN-CHAIN BOND (A**2)
1.77;
1.50

REMARK
3
MAIN-CHAIN ANGLE (A**2)
3.00;
2.00

REMARK
3
SIDE-CHAIN BOND (A**2)
2.81;
2.00

REMARK
3
SIDE-CHAIN ANGLE (A**2)
4.53;
2.50

REMARK
3

REMARK
3
NCS MODEL
NONE

REMARK
3

REMARK
3
NCS RESTRAINTS.
RMS
SIGMA/WEIGHT

REMARK
3
GROUP 1 POSITIONAL (A)
NULL;
NULL

REMARK
3
GROUP 1 B-FACTOR (A**2)
NULL;
NULL

REMARK
3

REMARK
3
PARAMETER FILE 1
parhcsdx.pro

REMARK
3
PARAMETER FILE 2
paramll.wat

REMARK
3
TOPOLOGY FILE 1
tophcsdx.pro

REMARK
3
TOPOLOGY FILE 2
tophll.wat

REMARK
3

REMARK
3
OTHER REFINEMENT REMARKS
BULK SOLVENT MODEL USED

SEQRES
1
A
507
VAL
ASN
PRO
GLY
VAL
VAL
VAL
ARG
ILE
SER
GLN
LYS
GLY

SEQRES
2
A
507
LEU
ASP
TYR
ALA
SER
GLN
GLN
GLY
THR
ALA
ALA
LEU
GLN

SEQRES
3
A
507
LYS
GLU
LEU
LYS
ARG
ILE
LYS
ILE
PRO
ASP
TYR
SER
ASP

SEQRES
4
A
507
SER
PHE
LYS
ILE
LYS
HIS
LEU
GLY
LYS
GLY
HIS
TYR
SER

SEQRES
5
A
507
PHE
TYR
SER
MET
ASP
ILE
ARG
GLU
PHE
GLN
LEU
PRO
SER

SEQRES
6
A
507
SER
GLN
ILE
SER
MET
VAL
PRO
ASN
VAL
GLY
LEU
LYS
PHE

SEQRES
7
A
507
SER
ILE
SER
ASN
ALA
ASN
ILE
LYS
ILE
SER
GLY
LYS
TRP

SEQRES
8
A
507
LYS
ALA
GLN
LYS
ARG
PHE
LEU
LYS
MET
SER
GLY
ASN
PHE

SEQRES
9
A
507
ASP
LEU
SER
ILE
GLU
GLY
MET
SER
ILE
SER
ALA
ASP
LEU

SEQRES
10
A
507
LYS
LEU
GLY
SER
ASN
PRO
THR
SER
GLY
LYS
PRO
THR
ILE

SEQRES
11
A
507
THR
CYS
SER
SER
CYS
SER
SER
HIS
ILE
ASN
SER
VAL
HIS

SEQRES
12
A
507
VAL
HIS
ILE
SER
ALA
ALA
SER
VAL
GLY
TRP
LEU
ILE
GLN

SEQRES
13
A
507
LEU
PHE
HIS
LYS
LYS
ILE
GLU
SER
ALA
LEU
ARG
ASN
LYS

SEQRES
14
A
507
MET
ASN
SER
GLN
VAL
CYS
GLU
LYS
VAL
THR
ASN
SER
VAL

SEQRES
15
A
507
SER
SER
GLU
LEU
GLN
PRO
TYR
PHE
GLN
THR
LEU
PRO
VAL

SEQRES
16
A
507
MET
THR
LYS
ILE
ASP
SER
VAL
ALA
GLY
ILE
ASN
TYR
GLY

SEQRES
17
A
507
LEU
VAL
ALA
PRO
PRO
ALA
THR
THR
ALA
GLU
THR
LEU
ASP

SEQRES
18
A
507
VAL
GLN
MET
LYS
GLY
GLU
PHE
TYR
SER
GLU
ALA
ALA
ALA

SEQRES
19
A
507
ALA
PRO
PRO
PRO
PHE
ALA
PRO
PRO
VAL
MET
GLU
PHE
PRO

SEQRES
20
A
507
ALA
ALA
ALA
ASP
ARG
MET
VAL
TYR
LEU
GLY
LEU
SER
ASP

SEQRES
21
A
507
TYR
PHE
PHE
ASN
THR
ALA
GLY
LEU
VAL
TYR
GLN
GLU
ALA

SEQRES
22
A
507
GLY
VAL
LEU
LYS
MET
THR
LEU
ARG
ASP
ASP
MET
ILE
PRO

SEQRES
23
A
507
LYS
GLU
SER
ALA
PHE
ARG
LEU
THR
THR
SER
PHE
PHE
GLY

SEQRES
24
A
507
THR
PHE
LEU
PRO
GLU
VAL
ALA
LYS
LYS
PHE
PRO
ASN
MET

SEQRES
25
A
507
LYS
ILE
GLN
ILE
HIS
VAL
SER
ALA
SER
THR
PRO
PRO
HIS

SEQRES
26
A
507
LEU
SER
VAL
GLN
PRO
THR
GLY
LEU
THR
PHE
TYR
PRO
ALA

SEQRES
27
A
507
VAL
ASP
VAL
GLN
ALA
PHE
ALA
VAL
LEU
PRO
ASN
SER
ALA

SEQRES
28
A
507
LEU
ALA
SER
LEU
PHE
LEU
ILE
GLY
MET
HIS
THR
THR
GLY

SEQRES
29
A
507
SER
MET
GLU
VAL
SER
ALA
GLU
SER
ASN
ARG
LEU
VAL
GLY

SEQRES
30
A
507
GLU
LEU
LYS
LEU
ASP
ARG
LEU
LEU
LEU
GLU
LEU
LYS
HIS

SEQRES
31
A
507
SER
ASN
ILE
GLY
PRO
PHE
PRO
VAL
GLU
LEU
LEU
GLN
ASP

SEQRES
32
A
507
ILE
MET
ASN
TYR
ILE
VAL
PRO
ILE
LEU
VAL
LEU
PRO
ARG

SEQRES
33
A
507
VAL
ASN
GLU
LYS
LEU
GLN
LYS
GLY
PHE
PRO
LEU
PRO
THR

SEQRES
34
A
507
PRO
ALA
ARG
VAL
GLN
LEU
TYR
ASN
VAL
VAL
LEU
GLN
PRO

SEQRES
35
A
507
HIS
GLN
ASN
PHE
LEU
LEU
PHE
GLY
ALA
ASP
VAL
VAL
TYR

SEQRES
36
A
507
LYS
PC
PC
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH

SEQRES
37
A
507
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH

SEQRES
38
A
507
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH

SEQRES
39
A
507
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH
HOH

SSBOND 1 CYS A 135 CYS A 175

CRYST1 185.600 33.000 85.200 90.00 101.60 90.00 C 2 4

ORIGX1
1.000000
0.000000
0.000000
0.00000

ORIGX2
0.000000
1.000000
0.000000
0.00000

ORIGX3
0.000000
0.000000
1.000000
0.00000

SCALE1
0.005388
0.000000
0.001106
0.00000

SCALE2
0.000000
0.030303
0.000000
0.00000

SCALE3
0.000000
0.000000
0.011982
0.00000

[0225] The following abbreviations are used in Table 4 in accordance with the format and usage established by the Protein Data Bank (“PDB”), Brookhaven National Laboratory, Brookhaven, N.Y. These coordinates are on deposit with the PDB, ID code 1bp1. Atomic coordinates of a BPI protein as described herein appear at Table 4 (pages 62-171 herein) and refinement statistics also appear at the end of Table 4 (pages 172-173 herein). Table 4 corresponds to FIG. 6 (FIGS. 6.1-6.112) in U.S. patent application Ser. No. 08/879,565, filed Jun. 20, 1997.

[0226] “Atom type” refers to the element whose coordinates are measured. The first letter in the column defines the element.

[0227] “Residue” refers to the amino acid in the BPI protein sequence, using the standard three letter abbreviations known in the art.

[0228] “#” refers to the residue number.

[0229] “X, Y, Z” crystallographically define the atomic position, in three-dimensional space, of the element measured.

[0230] “OCC” is the occupancy value.

[0231] “B” is a thermal factor that measures movement of the atom around its atomic center.

[0232] 10. Organomimetics

[0233] Molecular modelling of BPI as described herein is useful for the preparation of organomimetics such as “surface” mimetics. As one example, organomimetics are prepared based on “tip” mimetics in which the three-dimensional coordinates of the tip, as described above, are used to create a “surface” (or complementary pocket) into which a computer program builds an organic molecule with similar characteristics.

EXAMPLE 4

Stnrcture Determination of a Crystallized BPI Protein at 1.7 Å Resolution

[0234] Additional studies were performed to extend the resolution of the crystal structure of a BPI protein beyond the 2.4 Å resolution described in Example 2. For these studies, a sample of BPI protein was crystallized and the crystal structure was determined at a resolution of 1.7 Å using cryo-crystallography diffraction data. This crystal structure was compared to the crystal structure of 2.4 Å resolution at room temperature as described in Example 2. An additional exemplary set of structure coordinates for a BPI protein are listed below in Table 6.

[0235] Crystals of recombinant human BPI were grown generally as described in Example 2. Specifically, crystals were equilibrated over-night to 25% (v/v) PEG 6000 by vapor diffusion, and then immediately into 45% PEG 6000 for approximately two minutes. The crystals were then mounted and frozen under a stream of liquid nitrogen.

[0236] X-ray diffraction data for these crystallized BPI were collected at the Brookhaven National Laboratory on beamline X-12B. Data were processed and scaled using the programs DENZO and SCALEPACK [Z. Otwinowski, in Proceedings of CCP4 Study Weekend: Data Collection and Processing, L. Sawyer, N. Isaacs, S. Balleys, Eds. (SERC Daresbury Laboratory, Warrington, UK, 1993) pp. 56-62].

[0237] The unit cell dimensions of frozen crystals differ from the room temperature crystal dimensions as described in Example 2, especially the b-axis which contracted 16%. Rigid-body refinement in X-PLOR [A. Brünger, et al., ActaCrystallog. Sect. D, 54:905 (1998)] was used to reorient the room-temperature BPI model (protein atoms only) in the smaller unit cell, followed by simulated annealing and individual B-factor refinement. This model had an R-factor of 28.4% and Rfree of 34.3%. Electron density for two molecules of phosphatidylcholine, each located in an apolar pocket in both domains of BPI, was apparent in both 2Fo-Fc and Fo-Fc maps. Both lipids were also found during tracing of the original model, and likely were introduced to BPI during protein purification. Modeling of the N-terminal phospholipid reduced the R-factor to 27.3%, and Rfree to 33.5%. Approximately 360 water molecules and the C-terminal phospholipid (excluding the disordered head) were gradually introduced into the model and refined to an R-factor of 21.3% and Rfree of 29.6%.

[0238] Once the R-factors could not be lowered using X-PLOR, the program CNS was used, which uses a maximum-likelihood target function to minimize the gap between R and Rfree [A. Brünger, et al., Acta Crystallog. Sect. D, 54:905 (1998)]. A noticeable improvement in the quality of the electron density maps was observed upon using CNS, which allowed for further rebuilding the model. Following a bulk-solvent and overall anisotropic B-factor correction, the final R-factor was 19.8% and final Rfree was 24.9%. Refinement statistics are summarized in Table 5.

7TABLE 5STATISTICS ON CRYSTALLOGRAPHICDATA AND REFINEMENT FOR BPIA. Data CollectionResolution range high (Å)1.7Resolution range low (Å)50.0Data cut-off (Sigma (F))0.0Overall completeness94.1 (77.2)(final res. shell)Rmerge (%)4.9Redundancy2.3Number of reflections (test set)4755Number of reflections (overall)47,197B. CrystalSpacegroupC2Unit cell parameters (Å2)a = 184.3, b = 31.2, c = 80.6,β = 103.2C. RefinementR-value (%)19.8Free R-value (%)24.9Mean B-value (all atoms) (Å2)29.8Estimated coordinate error0.20(Luzzati) (Å)rmsd from ideal valuesBond lengths (Å)0.017Bond angles (deg.)2.0Dihedral angles (deg.)25.9Improper angels (deg.)1.33

[0239] The following residues had weak density and therefore were not included in the refinement: K33, K44, K45, K86, K95, K118, K290, K307, K313. Multiple conformations were built for the following residues: Q26, D57, S79, S88, S107, H143, T179, S183, V243, H325, L326, T363, N373, R374, F425, N437, V453, V454.

[0240] Several structure validation methods were used to assess the quality of the high-resolution BPI model. No significant errors were found in the model using the programs VERIFY 3D, ERRAT, PROCHECK and WHAT IF (C. Colovos and T. Yeates, Protein Science, 2:1511-19 (1993); R. A. Lackowski et al., J. Appi. Crystallog. 26:283-291 (1993); R. Lüthy et al., Nature 356:83-85 (1992)]. Over 89% of the residues are in the most favorable position in a Ramachandran plot. Approximately 10% of the residues are in the additionally allowed regions. Composite, simulated-annealing omit maps were calculated for the entire molecule. Density from omit maps agreed very well with the atomic positions of nearly all residues.

[0241] Comparison of the higher resolution model of BPI, presented in this Example 4, with the room temperature model presented in Example 2 reveals little structural change, with the exception of residues 42 to 48. In the new structure, several side-chains on one side of the loop now pack against the protein, whereas these side chains in previous model were mostly exposed to solvent. The loop rearrangement may be due to conditioning the crystals with 45% PEG 6000 for cryo-protection, freezing, or a combination of the two. Equivalent main-chain atoms for the two models superimpose with an rmsd of 0.9 Å.

[0242]
FIG. 7(a) is a ribbon representation of the 1.7 Å crystal structure of human BPI, with an N-terminal domain (blue) and a C-terminal domain (red). As described in Example 2, and FIG. 1, residues 10 to 193 fold into a structural element called the N-terminal barrel. The barrel is composed of five anti-parallel β-strands which twist about the barrel axis. Two α-helices complete the barrel by closing a gap in the β-sheet. Residues 260 to 430 fold into a similar structure called the C-terminal barrel. Amino acid residues 201 to 229, as well as 431 to 456, fold into the central β-sheet of six strands, located in the center of the molecule, which interacts with both the N-terminal and C-terminal barrels. A linker of residues 230 to 250 (olive) connects the N-terminal and C-terminal domains. FIG. 7(b) shows the superposition of the N-terminal domain (blue) on the C-terminal domain (red). Residues 1-229 were structurally aligned to residues 251-456 using the algorithm ALIGN_V2 [Cohen, et al., J. Mol. Biol. 190:593-604 1986]. the two domains align with 3.0 Å root mean square deviation over the main-chain atoms of the 173 structurally corresponding residues. FIG. 7(c) is a schematic of BPI showing its elongated shape and two-domain structure. The two domains are related by a pseudodyad perpendicular to the page. Secondary structure units are represented by arrows (β-strands) and rectangles (helices). The N-terminal domain (residues 1-229) is gray; the C-terminal domain (residues 251 to 456) is black. Secondary structure units have been numbered, with the primes denoting the units in the C-terminal domain. Residue positions for the start and end of each secondary structure unit are shown. The three subdomains (N-terminal barrel, C-terminal barrel, and central sheet) are shown.

8TABLE 6ATOM1NVALA199.12312.60015.1571.0044.04NATOM2CAVALA198.69412.67713.7291.0040.54CATOM3CVALA197.85913.91713.4531.0038.35CATOM4OVALA198.15914.63512.5191.0038.36OATOM5CBVALA197.90311.41313.3191.0044.86CATOM6NASNA296.79714.14414.2331.0034.30NATOM7CAASNA295.95115.32914.0471.0033.52CATOM8CASNA296.04516.26215.2541.0028.68CATOM9OASNA295.36216.08116.2751.0031.83OATOM10CBASNA294.49614.94613.8301.0038.28CATOM11CGASNA294.29514.15612.5381.0045.11CATOM12OD1ASNA293.17813.74612.2001.0050.87OATOM13ND2ASNA295.38413.94611.8111.0047.51NATOM14NPROA396.93317.23715.1771.0023.64NATOM15CAPROA397.02618.14516.3191.0022.44CATOM16CPROA395.86419.15816.3451.0018.47CATOM17OPROA395.16519.34215.3391.0020.64OATOM18CBPROA398.37218.82816.0861.0023.56CATOM19CGPROA398.43918.92814.5761.0023.16CATOM20CDPROA398.00817.49014.2071.0025.78CATOM21NGLYA495.70119.80317.5001.0019.55NATOM22CAGLYA494.71320.88017.6611.0018.57CATOM23CGLYA495.22522.17517.0101.0018.22CATOM24OGLYA494.42723.04416.5201.0018.00OATOM25NVALA596.54522.31116.9791.0016.24NATOM26CAVALA597.20323.50516.4291.0016.48CATOM27CVALA598.47523.08215.6801.0020.26CATOM28OVALA599.22922.21316.1681.0017.97OATOM29CBVALA597.61024.45317.5801.0015.95CATOM30CG1VALA598.63925.52217.1281.0018.07CATOM31CG2VALA596.37125.11918.1191.0015.07CATOM32NVALA698.68823.65714.4971.0017.00NATOM33CAVALA699.93723.34413.7551.0020.95CATOM34CVALA6100.65524.63113.4081.0021.83CATOM35OVALA6100.01025.63413.1201.0020.53OATOM36CBVALA699.67022.48212.4721.0022.17CATOM37CG1VALA698.81223.24911.4561.0025.15CATOM38CG2VALA6100.99422.09611.8021.0022.54CATOM39NVALA7101.99024.61413.5071.0023.46NATOM40CAVALA7102.81325.76113.1171.0022.32CATOM41CVALA7103.70025.20311.9961.0022.10CATOM42OVALA7104.49424.26012.2141.0023.46OATOM43CBVALA7103.72226.28114.2551.0024.50CATOM44CG1VALA7104.70127.31013.7121.0026.73CATOM45CG2VALA7102.86626.94215.3391.0026.51CATOM46NARGA8103.49625.74010.7941.0019.55NATOM47CAARGA8104.25125.3579.6291.0019.01CATOM48CARGA8105.25326.4629.2881.0018.98CATOM49OARGA8104.85927.6209.0751.0022.70OATOM50CBARGA8103.30625.1418.4541.0023.41CATOM51CGARGA8104.00525.1537.1291.0030.34CATOM52CDARGA8103.05524.7246.0491.0036.53CATOM53NEARGA8102.51923.3826.2891.0033.62NATOM54CZARGA8101.73222.7525.4241.0036.64CATOM55NH1ARGA8101.41523.3624.2811.0037.02NATOM56NH2ARGA8101.27321.5345.7021.0032.05NATOM57NILEA9106.53726.1249.2621.0017.75NATOM58CAILEA9107.56227.1058.9031.0020.58CATOM59CILEA9107.94626.8837.4191.0023.60CATOM60OILEA9108.25825.7567.0051.0019.72OATOM61CBILEA9108.79726.9669.8241.0020.29CATOM62CG1ILEA9108.32927.01011.2911.0020.75CATOM63CG2ILEA9109.82728.0519.5101.0018.57CATOM64CD1ILEA9109.40926.61212.3001.0024.49CATOM65NSERA10107.87527.9656.6251.0019.29NATOM66CASERA10108.17427.9245.2011.0019.13CATOM67CSERA10109.67428.1414.9631.0019.57CATOM68OSERA10110.41828.4945.9011.0021.31OATOM69CBSERA10107.40829.0364.4321.0020.80CATOM70OGSERA10107.97230.3354.6751.0022.77OATOM71NGLNA11110.09227.9793.7101.0017.69NATOM72CAGLNA11111.50828.1953.3531.0019.09CATOM73CGLNA11111.82629.6693.6831.0020.86CATOM74OGLNA11112.90829.9844.1411.0019.21OATOM75CBGLNA11111.74127.9411.8671.0019.48CATOM76CGGLNA11113.19328.1511.4551.0017.84CATOM77CDGLNA11114.11827.0962.0181.0021.25CATOM78OE1GLNA11113.94825.9091.7531.0022.82OATOM79NE2GLNA11115.12827.5302.8001.0021.51NATOM80NLYSA12110.85430.5593.4701.0022.63NATOM81CALYSA12111.06631.9943.8111.0022.40CATOM82CLYSA12111.38132.1685.3121.0020.21CATOM83OLYSA12112.27232.9105.6981.0023.98OATOM84CBLYSA12109.82232.8143.4591.0025.65CATOM85CGLYSA12109.97334.3233.7901.0027.19CATOM86CDLYSA12108.69535.1253.4621.0031.07CATOM87CELYSA12108.95536.6343.5011.0034.80CATOM88NZLYSA12109.33037.0614.8661.0038.91NATOM89NGLYA13110.65531.4686.1711.0018.40NATOM90CAGLYA13110.92231.5617.5871.0016.33CATOM91CGLYA13112.26130.9557.9701.0017.16CATOM92OGLYA13112.97431.4718.8391.0017.11OATOM93NLEUA14112.61029.8367.3371.0018.18NATOM94CALEUA14113.89129.2327.6321.0019.55CATOM95CLEUA14114.99830.1287.0691.0021.19CATOM96OLEUA14116.05730.1587.6501.0024.39OATOM97CBLEUA14113.97227.8277.0441.0019.38CATOM98CGLEUA14113.03826.8427.7711.0021.89CATOM99CD1LEUA14113.09025.4167.1441.0023.91CATOM100CD2LEUA14113.48726.7679.2331.0022.76CATOM101NASPA15114.75130.8535.9611.0022.66NATOM102CAASPA15115.77731.7815.3701.0024.92CATOM103CASPA15116.02232.8836.4451.0025.67CATOM104OASPA15117.15433.3296.6821.0027.66OATOM105CBASPA15115.28632.5184.0951.0023.19CATOM106CGASPA15115.17531.6172.8371.0027.87CATOM107OD1ASPA15115.75530.5132.7741.0019.50OATOM108OD2ASPA15114.52332.0571.8721.0028.04OATOM109NTYRA16114.95333.3567.0671.0022.85NATOM110CATYRA16115.12134.3678.1221.0021.53CATOM111CTYRA16115.80933.7829.3701.0022.53CATOM112OTYRA16116.68834.41510.0021.0022.77OATOM113CBTYRA16113.75134.8908.5361.0019.47CATOM114CGTYRA16113.82936.0189.5391.0022.07CATOM115CD1TYRA16114.31237.2689.1751.0023.27CATOM116CD2TYRA16113.40735.82810.8431.0018.37CATOM117CE1TYRA16114.36438.31910.1131.0024.86CATOM118CE2TYRA16113.45336.84911.7801.0019.95CATOM119CZTYRA16113.93538.10211.4001.0022.39CATOM120OHTYRA16114.00239.11812.3241.0023.77OATOM121NALAA17115.42232.5689.7671.0022.91NATOM122CAALAA17116.04731.99510.9411.0022.31CATOM123CALAA17117.53631.81510.6881.0024.09CATOM124OALAA17118.36832.00611.6091.0026.66OATOM125CBALAA17115.40730.62511.3041.0023.16CATOM126NSERA18117.87431.4609.4481.0023.70NATOM127CASERA18119.28631.2339.0741.0027.25CATOM128CSERA18120.09732.5339.3071.0027.23CATOM129OSERA18121.15332.5009.9281.0027.40OATOM130CBSERA18119.37030.7637.6041.0023.88CATOM131OGSERA18120.71830.5987.1371.0027.24OATOM132NGLNA19119.54733.6578.8531.0029.26NATOM133CAGLNA19120.17834.9658.9701.0030.47CATOM134CGLNA19120.40735.31910.4411.0029.93CATOM135OGLNA19121.47435.83410.8001.0027.60OATOM136CBGLNA19119.29535.9928.2541.0034.56CATOM137CGGLNA19119.60737.4608.4711.0043.09CATOM138CDGLNA19118.50638.3567.8861.0048.28CATOM139OE1GLNA19118.52038.6926.6931.0053.27OATOM140NE2GLNA19117.54138.7188.7141.0049.14NATOM141NGLNA20119.43035.02311.3011.0027.81NATOM142CAGLNA20119.57935.33112.7201.0026.88CATOM143CGLNA20120.59134.43613.4101.0027.29CATOM144OGLNA20121.37434.90214.2461.0028.18OATOM145CBGLNA20118.22435.23313.4591.0027.06CATOM146CGGLNA20117.20136.12712.8631.0029.89CATOM147CDGLNA20117.69537.54212.7361.0030.73CATOM148OE1GLNA20117.61638.13211.6711.0042.34OATOM149NE2GLNA20118.22438.08713.8161.0027.79NATOM150NGLYA21120.57933.14313.0941.0026.15NATOM151CAGLYA21121.53232.24713.7441.0026.98CATOM152CGLYA21122.95232.53513.2511.0027.76CATOM153OGLYA21123.94332.36413.9761.0029.86OATOM154NTHRA22123.05632.98012.0071.0027.86NATOM155CATHRA22124.37633.29311.4531.0029.40CATOM156CTHRA22124.94234.51912.1831.0030.38CATOM157OTHRA22126.14734.58712.4701.0031.00OATOM158CBTHRA22124.28533.5919.9601.0028.72CATOM159OG1THRA22123.98032.3659.2531.0027.14OATOM160CG2THRA22125.62634.1769.4531.0026.69CATOM161NALAA23124.07035.47412.4931.0032.27NATOM162CAALAA23124.52236.68113.2051.0031.91CATOM163CALAA23125.08036.30014.5561.0031.53CATOM164OALAA23126.14836.79314.9471.0033.72OATOM165CBALAA23123.38837.68513.3711.0032.44CATOM166NALAA24124.37735.43215.2871.0030.88NATOM167CAALAA24124.86034.99916.5921.0031.01CATOM168CALAA24126.16334.23316.4491.0032.95CATOM169OALAA24127.13234.48717.1671.0030.51OATOM170CBALAA24123.83834.12917.2831.0033.04CATOM171NLEUA25126.20033.30915.5011.0030.79NATOM172CALEUA25127.38932.50315.3051.0032.62CATOM173CLEUA25128.63333.33014.9241.0032.00CATOM174OLEUA25129.75833.01215.3311.0032.68OATOM175CBLEUA25127.11031.45314.2291.0029.16CATOM176CGLEUA25128.25530.50113.9071.0031.29CATOM177CD1LEUA25128.58529.61915.0791.0025.06CATOM178CD2LEUA25127.82929.64512.7141.0026.52CATOM179NAGLNA26128.41334.38814.1510.5031.93NATOM180NBGLNA26128.42234.38814.1460.5032.36NATOM181CAAGLNA26129.49435.25813.7040.5032.03CATOM182CABGLNA26129.52035.23913.7010.5032.83CATOM183CAGLNA26130.25735.90214.8640.5033.14CATOM184CBGLNA26130.26635.89214.8720.5033.63CATOM185OAGLNA26131.48336.04614.8110.5031.31OATOM186OBGLNA26131.49336.02714.8350.5031.80OATOM187CBAGLNA26128.93336.33212.7630.5032.73CATOM188CBBGLNA26128.99836.30712.7300.5034.28CATOM189CGAGLNA26129.73437.61912.7050.5033.34CATOM190CGBGLNA26130.05037.29412.2680.5036.57CATOM191CDAGLNA26129.33938.62513.7840.5033.87CATOM192CDBGLNA26129.51638.33011.2970.5037.41CATOM193OE1AGLNA26130.17839.37414.2710.5035.74OATOM194OE1BGLNA26129.28938.04810.1220.5041.63OATOM195NE2AGLNA26128.05438.65714.1450.5035.30NATOM196NE2BGLNA26129.30739.54311.7900.5041.87NATOM197NLYSA27129.53236.29415.9101.0032.03NATOM198CALYSA27130.17536.90217.0691.0033.30CATOM199CLYSA27131.02735.85817.8131.0033.11CATOM200OLYSA27132.12036.16418.2921.0035.00OATOM201CBLYSA27129.13037.49218.0211.0035.38CATOM202CGLYSA27128.32538.63117.4081.0040.86CATOM203CDLYSA27127.53139.32618.4961.0041.98CATOM204CELYSA27126.56340.32517.9041.0045.37CATOM205NZLYSA27125.51039.59517.1371.0046.47NATOM206NGLUA28130.53634.62917.9031.0030.90NATOM207CAGLUA28131.26033.55318.5801.0031.44CATOM208CGLUA28132.47633.06717.7831.0030.26CATOM209OGLUA28133.50932.70918.3511.0033.05OATOM210CBGLUA28130.29432.38518.8201.0033.67CATOM211CGGLUA28129.12832.82319.6731.0040.80CATOM212CDGLUA28128.04331.77919.7811.0045.88CATOM213OE1GLUA28128.39330.62020.0681.0048.70OATOM214OE2GLUA28126.84732.13019.6011.0048.24OATOM215NLEUA29132.35233.04716.4661.0027.78NATOM216CALEUA29133.45832.61615.6281.0028.25CATOM217CLEUA29134.59533.61715.7351.0028.09CATOM218OLEUA29135.77833.26015.7391.0026.00OATOM219CBLEUA29132.99832.49614.1621.0026.14CATOM220CGLEUA29132.05731.30813.9321.0025.62CATOM221CD1LEUA29131.57031.32312.5021.0028.21CATOM222CD2LEUA29132.78830.01014.2821.0027.72CATOM223NLYSA30134.21334.88515.8051.0030.04NATOM224CALYSA30135.18435.94715.8981.0033.25CATOM225CLYSA30136.01235.84317.1721.0034.88CATOM226OLYSA30137.08936.45417.2531.0035.29OATOM227CBLYSA30134.45737.28815.8331.0036.23CATOM228CGLYSA30135.34838.47815.5531.0042.33CATOM229CDLYSA30134.49239.73715.4051.0045.91CATOM230CELYSA30135.27440.88614.8141.0047.06CATOM231NZLYSA30136.37141.32015.7151.0049.41NATOM232NARGA31135.53535.06618.1511.0033.63NATOM233CAARGA31136.25034.88819.4251.0036.10CATOM234CARGA31137.21233.68719.4241.0034.55CATOM235OARGA31137.88233.40920.4171.0035.67OATOM236CBARGA31135.26134.73820.6061.0037.98CATOM237CGARGA31134.59536.04421.1041.0041.56CATOM238CDARGA31133.50235.72322.1201.0045.50CATOM239NEARGA31133.25234.27722.1421.0052.02NATOM240CZARGA31132.08133.69222.4091.0053.02CATOM241NH1ARGA31131.00134.41422.6941.0053.23NATOM242NH2ARGA31131.98432.37022.3551.0054.81NATOM243NILEA32137.25632.94718.3301.0031.42NATOM244CAILEA32138.18131.82318.2591.0028.65CATOM245CILEA32139.59332.33818.5971.0032.86CATOM246OILEA32140.02033.39118.1251.0030.92OATOM247CBILEA32138.13831.20916.8411.0027.46CATOM248CG1ILEA32136.83230.38816.7061.0026.62CATOM249CG2ILEA32139.37130.33016.5821.0027.04CATOM250CD1ILEA32136.46130.01015.2601.0028.50CATOM251NLYSA33140.29331.59819.4461.0031.18NATOM252CALYSA33141.64331.96519.8121.0032.80CATOM253CLYSA33142.58931.13318.9391.0030.39CATOM254OLYSA33142.70029.90019.0871.0027.22OATOM255CBLYSA33141.87631.68821.2991.0033.91CATOM256NILEA34143.27931.81518.0231.0029.33NATOM257CAILEA34144.19631.12617.1191.0028.76CATOM258CILEA34145.55630.90817.8101.0029.96CATOM259OILEA34146.09331.84318.4151.0028.31OATOM260CBILEA34144.45131.94615.8891.0029.43CATOM261CG1ILEA34143.11632.38715.2611.0034.18CATOM262CG2ILEA34145.23831.12914.9051.0028.56CATOM263CD1ILEA34143.27933.05713.9071.0034.83CATOM264NPROA35146.09529.67617.7481.0025.45NATOM265CAPROA35147.38729.33318.3611.0024.11CATOM266CPROA35148.56730.03317.6471.0027.07CATOM267OPROA35148.47230.38416.4691.0025.07OATOM268CBPROA35147.53227.82518.1041.0029.74CATOM269CGPROA35146.16927.33817.7321.0031.75CATOM270CDPROA35145.49528.51817.0651.0026.30CATOM271NASPA36149.66830.22318.3741.0025.04NATOM272CAASPA36150.90930.75017.7911.0024.93CATOM273CASPA36151.54829.57917.0301.0023.50CATOM274OASPA36151.39128.42017.4381.0024.29OATOM275CBASPA36151.91331.13118.8901.0023.16CATOM276CGASPA36151.52432.34419.6471.0024.72CATOM277OD1ASPA36150.58633.08419.2221.0023.61OATOM278OD2ASPA36152.20132.57820.6941.0027.32OATOM279NTYRA37152.28129.87115.9511.0023.21NATOM280CATYRA37152.98428.84715.1671.0025.87CATOM281CTYRA37154.47729.18515.0581.0028.85CATOM282OTYRA37154.81530.24314.5561.0029.19OATOM283CBTYRA37152.40428.75713.7451.0028.54CATOM284CGTYRA37151.01128.15913.7011.0028.29CATOM285CD1TYRA37149.88828.93713.9681.0026.93CATOM286CD2TYRA37150.83826.78413.4941.0029.30CATOM287CE1TYRA37148.61228.35914.0491.0026.87CATOM288CE2TYRA37149.56326.20613.5711.0029.25CATOM289CZTYRA37148.46827.00313.8551.0028.52CATOM290OHTYRA37147.22126.44414.0231.0030.04OATOM291NSERA38155.37428.30815.5031.0025.37NATOM292CASERA38156.81528.59315.3861.0027.72CATOM293CSERA38157.46627.43814.6731.0028.75CATOM294OSERA38156.92226.33014.6881.0027.50OATOM295CBSERA38157.49528.76616.7611.0028.15CATOM296OGSERA38157.05229.91217.4751.0031.37OATOM297NASPA39158.60627.68814.0161.0028.33NATOM298CAASPA39159.34126.64613.3021.0028.25CATOM299CASPA39160.76927.08313.0171.0028.61CATOM300OASPA39161.18628.19513.3861.0029.37OATOM301CBASPA39158.63526.27611.9731.0028.54CATOM302CGASPA39158.75524.78111.6251.0033.76CATOM303OD1ASPA39159.81024.17711.8501.0027.92OATOM304OD2ASPA39157.78724.19311.0851.0038.71OATOM305NSERA40161.52626.20912.3641.0029.41NATOM306CASERA40162.92126.49912.0201.0029.70CATOM307CSERA40163.15726.37210.5151.0028.44CATOM308OSERA40162.33825.7939.7991.0029.16OATOM309CBSERA40163.85625.51712.7351.0028.29CATOM310OGSERA40163.80324.25012.0541.0033.28OATOM311NPHEA41164.28626.89610.0361.0026.94NATOM312CAPHEA41164.64426.8148.6301.0033.23CATOM313CPHEA41166.14526.7568.4001.0036.88CATOM314OPHEA41166.93326.9809.3091.0034.29OATOM315CBPHEA41164.09428.0427.8661.0031.34CATOM316CGPHEA41164.71529.3598.2831.0023.47CATOM317CD1PHEA41165.84929.8507.6491.0027.66CATOM318CD2PHEA41164.14230.1309.2761.0025.02CATOM319CE1PHEA41166.39231.0968.0071.0026.86CATOM320CE2PHEA41164.67731.3539.6261.0026.44CATOM321CZPHEA41165.81231.8368.9811.0026.39CATOM322NLYSA42166.48626.4947.1371.0042.47NATOM323CALYSA42167.84326.4406.5771.0047.56CATOM324CLYSA42167.47527.0215.2091.0050.97CATOM325OLYSA42167.34826.2894.2201.0052.20OATOM326CBLYSA42168.30924.9916.4151.0049.73CATOM327CGLYSA42167.82124.0757.5221.0053.87CATOM328CDLYSA42168.21922.6197.2781.0054.49CATOM329CELYSA42167.45421.7058.2341.0055.43CATOM330NZLYSA42167.51022.2109.6441.0054.91NATOM331NILEA43167.23128.3315.1751.0054.51NATOM332CAILEA43166.80229.0383.9541.0057.47CATOM333CILEA43166.81830.5444.2771.0060.72CATOM334OILEA43165.91931.1084.9121.0063.60OATOM335CBILEA43165.38128.4683.4401.0055.16CATOM336CG1ILEA43164.63529.4682.5451.0055.28CATOM337CG2ILEA43164.52028.0374.5941.0057.28CATOM338CD1ILEA43164.04830.6663.2201.0050.49CATOM339NLYSA44167.91631.1503.8461.0062.14NATOM340CALYSA44168.29232.5484.0251.0062.63CATOM341CLYSA44167.40933.7714.3491.0062.83CATOM342OLYSA44166.19133.7554.4591.0061.93OATOM343CBLYSA44169.24032.9302.8621.0063.36CATOM344NHISA45168.18634.8384.4531.0064.30NATOM345CAHISA45167.94436.2294.8001.0065.63CATOM346CHISA45169.34736.1415.4141.0066.88CATOM347OHISA45169.97737.1225.8361.0068.54OATOM348CBHISA45166.90336.3575.8961.0066.53CATOM349NLEUA46169.76434.8645.4201.0067.18NATOM350CALEUA46171.00834.2685.8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1.4451.0028.23CATOM1036OSERA134127.20518.73211.3941.0026.16OATOM1037CBSERA134127.81315.56310.5651.0031.49CATOM1038OGSERA134126.85815.9599.6201.0033.50OATOM1039NCYSA135129.37518.12511.1881.0024.39NATOM1040CACYSA135129.82619.44910.7971.0023.58CATOM1041CCYSA135131.12119.2539.9851.0022.61CATOM1042OCYSA135131.95118.38910.3171.0023.89OATOM1043CBCYSA135130.13720.27912.0521.0022.12CATOM1044SGCYSA135130.67821.98711.7601.0024.00SATOM1045NSERA136131.27120.0358.9221.0021.46NATOM1046CASERA136132.50420.0248.1261.0022.04CATOM1047CSERA136132.81521.5017.8191.0023.24CATOM1048OSERA136131.92222.3247.7861.0023.47OATOM1049CBSERA136132.36119.1816.8461.0027.15CATOM1050OGSERA136131.27719.5996.0631.0035.21OATOM1051NSERA137134.08221.8267.6371.0023.28NATOM1052CASERA137134.51923.2037.3571.0021.12CATOM1053CSERA137135.71423.0066.3991.0024.00CATOM1054OSERA137136.61322.1846.6761.0026.28OATOM1055CBSERA137135.00823.8718.6641.0024.86CATOM1056OGSERA137135.59225.1718.4661.0021.45OATOM1057NHISA138135.72023.7185.2741.0022.89NATOM1058CAHISA138136.81723.6034.3211.0022.59CATOM1059CHISA138137.27025.0333.9601.0021.69CATOM1060OHISA138136.48725.9864.1081.0022.19OATOM1061CBHISA138136.35122.8653.0491.0024.47CATOM1062CGHISA138136.00521.4293.2701.0031.02CATOM1063ND1HISA138136.93720.4143.1621.0034.51NATOM1064CD2HISA138134.82920.8313.5751.0030.58CATOM1065CE1HISA138136.34519.2543.3911.0031.58CATOM1066NE2HISA138135.06619.4833.6451.0035.06NATOM1067NILEA139138.50625.1773.4801.0022.03NATOM1068CAILEA139139.05626.4993.1251.0021.48CATOM1069CILEA139139.62226.4431.7241.0023.05CATOM1070OILEA139140.31025.4891.3921.0025.15OATOM1071CBILEA139140.19726.9024.0941.0024.43CATOM1072CG1ILEA139139.61827.2125.4731.0023.14CATOM1073CG2ILEA139141.00428.0913.5231.0021.83CATOM1074CD1ILEA139140.72627.4156.5841.0023.17CATOM1075NASNA140139.35027.4660.9091.0024.38NATOM1076CAASNA140139.86727.433−0.4641.0025.84CATOM1077CASNA140141.29727.943−0.6091.0026.82CATOM1078OASNA140142.12927.306−1.2801.0026.46OATOM1079CBASNA140138.92328.187−1.4091.0029.67CATOM1080CGASNA140139.43828.203−2.8381.0033.79CATOM1081OD1ASNA140139.88629.236−3.3431.0038.11OATOM1082ND2ASNA140139.41127.044−3.4781.0029.13NATOM1083NSERA141141.59229.0770.0281.0024.19NATOM1084CASERA141142.94329.620−0.0691.0021.42CATOM1085CSERA141143.30430.5111.1151.0021.81CATOM1086OSERA141142.42830.9581.8771.0020.83OATOM1087CBSERA141143.09530.385−1.3831.0025.08CATOM1088OGSERA141142.39431.609−1.3141.0024.68OATOM1089NVALA142144.61630.6871.3191.0020.93NATOM1090CAVALA142145.13731.5302.4131.0022.71CATOM1091CVALA142146.20632.4551.8551.0024.50CATOM1092OVALA142147.12931.9831.1481.0027.06OATOM1093CBVALA142145.81530.6543.5241.0022.95CATOM1094CG1VALA142146.36631.5364.6321.0026.66CATOM1095CG2VALA142144.79129.6444.0751.0023.86CATOM1096NAHISA143146.11333.7412.1830.5022.08NATOM1097NBHISA143146.11333.7502.1580.5022.98NATOM1098CAAHISA143147.08334.7041.6900.5023.19CATOM1099CABHISA143147.11234.7071.6820.5024.45CATOM1100CAHISA143147.67435.5512.8320.5022.83CATOM1101CBHISA143147.68335.5092.8520.5023.68CATOM1102OAHISA143146.93336.1163.6530.5022.06OATOM1103OBHISA143146.93935.9903.7180.5023.22OATOM1104CBAHISA143146.39235.5980.6640.5020.65CATOM1105CBBHISA143146.48335.6700.6680.5023.70CATOM1106CGAHISA143145.64434.841−0.4000.5022.32CATOM1107CGBHISA143147.41936.7260.1520.5027.00CATOM1108ND1AHISA143146.25734.353−1.5300.5025.97NATOM1109ND1BHISA143148.35136.481−0.8300.5028.37NATOM1110CD2AHISA143144.34034.482−0.4870.5021.56CATOM1111CD2BHISA143147.55538.0380.4730.5027.25CATOM1112CE1AHISA143145.36033.726−2.2760.5022.09CATOM1113CE1BHISA143149.01937.591−1.0960.5028.23CATOM1114NE2AHISA143144.19133.789−1.6650.5024.64NATOM1115NE2BHISA143148.55738.551−0.3170.5025.58NATOM1116NVALA144149.00635.6582.8551.0022.26NATOM1117CAVALA144149.71036.4323.8991.0023.31CATOM1118CVALA144150.28837.7163.2821.0023.12CATOM1119OVALA144150.85537.6682.1741.0022.14OATOM1120CBVALA144150.90935.6454.4761.0025.98CATOM1121CG1VALA144151.44636.3855.7101.0025.04CATOM1122CG2VALA144150.50534.1914.8281.0030.60CATOM1123NHISA145150.11838.8553.9491.0020.90NATOM1124CAHISA145150.69040.1173.4531.0020.43CATOM1125CHISA145151.52740.7274.5631.0020.71CATOM1126OHISA145151.09140.7925.7131.0021.06OATOM1127CBHISA145149.62041.1583.0691.0022.08CATOM1128CGHISA145150.17342.5422.8181.0026.10CATOM1129ND1HISA145150.05143.5753.7311.0028.27NATOM1130CD2HISA145150.88743.0421.7801.0027.55CATOM1131CE1HISA145150.66844.6463.2631.0025.47CATOM1132NE2HISA145151.18044.3542.0821.0028.96NATOM1133NILEA146152.74341.1394.2101.0018.59NATOM1134CAILEA146153.60941.8355.1671.0018.37CATOM1135CILEA146154.09443.1074.4671.0018.36CATOM1136OILEA146154.53843.0553.3381.0017.91OATOM1137CBILEA146154.80540.9205.6091.0018.23CATOM1138CG1ILEA146154.27739.8136.5481.0020.19CATOM1139CG2ILEA146155.88241.7506.2631.0019.05CATOM1140CD1ILEA146155.23938.6336.7871.0021.40CATOM1141NSERA147153.97344.2475.1441.0020.80NATOM1142CASERA147154.37845.5294.5541.0022.81CATOM1143CSERA147155.83745.5844.0901.0023.25CATOM1144OSERA147156.16946.2803.1081.0026.01OATOM1145CBSERA147154.10946.6835.5461.0025.27CATOM1146OGSERA147155.05746.6806.6071.0030.37OATOM1147NLYSA148156.72844.8784.7821.0024.52NATOM1148CALYSA148158.13644.8724.3591.0025.59CATOM1149CLYSA148158.29343.8503.2131.0025.07CATOM1150OLYSA148158.14242.6463.4161.0024.80OATOM1151CBLYSA148159.08344.4565.4891.0026.95CATOM1152CGLYSA148159.04845.2836.7651.0036.35CATOM1153CDLYSA148160.02744.6547.8151.0037.70CATOM1154CELYSA148160.10845.4639.1081.0042.14CATOM1155NZLYSA148158.82045.4519.8671.0044.10NATOM1156NSERA149158.64944.3432.0271.0023.82NATOM1157CASERA149158.80143.5010.8311.0023.15CATOM1158CSERA149159.93242.4950.9001.0025.21CATOM1159OSERA149159.89441.4590.2041.0024.56OATOM1160CBSERA149159.00244.388−0.4191.0027.76CATOM1161OGSERA149160.20545.136−0.3001.0022.89OATOM1162NLYSA150160.92442.7491.7541.0022.84NATOM1163CALYSA150162.06441.8251.7891.0023.22CATOM1164CLYSA150161.82340.4392.3891.0023.06CATOM1165OLYSA150162.76939.6222.3391.0021.71OATOM1166CBLYSA150163.23042.4392.5451.0027.64CATOM1167CGLYSA150162.93542.5724.0221.0031.09CATOM1168CDLYSA150164.13643.1134.8401.0040.99CATOM1169CELYSA150164.92444.1974.1091.0042.87CATOM1170NZLYSA150165.93843.6053.1921.0048.81NATOM1171NVALA151160.61840.1462.9071.0023.33NATOM1172CAVALA151160.41138.8203.5171.0024.28CATOM1173CVALA151159.56237.8122.7701.0023.01CATOM1174OVALA151158.87337.0013.3601.0020.36OATOM1175CBVALA151159.94338.9425.0041.0028.12CATOM1176CG1VALA151161.08639.6035.8201.0026.68CATOM1177CG2VALA151158.63739.7685.1081.0028.79CATOM1178NGLYA152159.64937.8891.4441.0021.86NATOM1179CAGLYA152158.95936.9640.5711.0021.76CATOM1180CGLYA152159.37035.5530.9481.0023.30CATOM1181OGLYA152158.54234.6440.9151.0020.77OATOM1182NTRPA153160.63935.3691.3331.0021.70NATOM1183CATRPA153161.11534.0361.7071.0021.21CATOM1184CTRPA153160.38233.5172.9511.0019.05CATOM1185OTRPA153160.12532.3243.0731.0021.95OATOM1186CBTRPA153162.65934.0311.9831.0019.77CATOM1187CGTRPA153163.11034.9593.1171.0021.64CATOM1188CD1TRPA153163.43036.2873.0141.0022.16CATOM1189CD2TRPA153163.19534.6334.5201.0023.76CATOM1190NE1TRPA153163.70936.8084.2531.0021.11NATOM1191CE2TRPA153163.56835.8235.2031.0022.73CATOM1192CE3TRPA153162.99633.4515.2641.0023.26CATOM1193CZ2TRPA153163.74935.8696.6141.0027.22CATOM1194CZ3TRPA153163.18133.4896.6681.0025.75CATOM1195CH2TRPA153163.55234.6987.3231.0028.15CATOM1196NLEUA154160.05034.4063.8721.0017.94NATOM1197CALEUA154159.36933.9865.1081.0020.50CATOM1198CLEUA154157.92133.6134.7821.0021.27CATOM1199OLEUA154157.37432.6685.3531.0022.45OATOM1200CBLEUA154159.42535.0986.1531.0019.41CATOM1201CGLEUA154158.70034.8967.4891.0022.12CATOM1202CD1LEUA154159.32033.6818.2301.0021.73CATOM1203CD2LEUA154158.83936.1718.3421.0023.69CATOM1204NILEA155157.28834.3453.8631.0018.31NATOM1205CAILEA155155.90933.9873.5191.0019.89CATOM1206CILEA155155.91532.6112.8121.0018.64CATOM1207OILEA155154.99531.8142.9801.0022.17OATOM1208CBILEA155155.28735.0972.6391.0020.74CATOM1209CG1ILEA155155.00536.3213.5211.0025.44CATOM1210CG2ILEA155154.01234.5791.9751.0021.41CATOM1211CD1ILEA155154.54337.6352.7851.0020.68CATOM1212NGLNA156156.95732.3352.0341.0018.94NATOM1213CAGLNA156157.07831.0241.3961.0018.98CATOM1214CGLNA156157.25229.9402.4851.0018.90CATOM1215OGLNA156156.67028.8342.3731.0021.67OATOM1216CBGLNA156158.27130.9810.4241.0019.59CATOM1217CGGLNA156158.40729.626−0.2591.0025.02CATOM1218CDGLNA156157.28729.292−1.2491.0028.00CATOM1219OE1GLNA156156.14629.766−1.1421.0030.44OATOM1220NE2GLNA156157.62228.435−2.2381.0033.99NATOM1221NLEUA157158.01330.2203.5511.0020.68NATOM1222CALEUA157158.12529.1894.6041.0021.82CATOM1223CLEUA157156.74828.9645.2511.0022.51CATOM1224OLEUA157156.38927.8395.5961.0023.51OATOM1225CBLEUA157159.15429.6125.6841.0023.40CATOM1226CGLEUA157160.60729.5585.1861.0025.25CATOM1227CD1LEUA157161.55430.1206.2511.0028.48CATOM1228CD2LEUA157160.97828.0864.8451.0032.84CATOM1229NPHEA158155.99230.0465.4241.0021.43NATOM1230CAPHEA158154.64729.9316.0001.0022.87CATOM1231CPHEA158153.80128.9535.1781.0022.22CATOM1232OPHEA158153.17328.0135.7321.0021.69OATOM1233CBPHEA158153.96031.3096.1021.0020.44CATOM1234CGPHEA158152.50431.2126.4411.0022.66CATOM1235CD1PHEA158151.56230.9105.4621.0023.07CATOM1236CD2PHEA158152.07931.4037.7391.0023.30CATOM1237CE1PHEA158150.19730.8045.7811.0022.87CATOM1238CE2PHEA158150.73131.3008.0851.0024.31CATOM1239CZPHEA158149.77531.0017.1081.0022.21CATOM1240NHISA159153.77829.1653.8581.0022.94NATOM1241CAHISA159153.03328.2622.9811.0023.08CATOM1242CHISA159153.55026.8133.0291.0024.35CATOM1243OHISA159152.76925.8713.1251.0023.24OATOM1244CBHISA159153.07428.7851.5411.0024.96CATOM1245CGHISA159152.23730.0051.3381.0024.81CATOM1246ND1HISA159150.86129.9731.4461.0028.89NATOM1247CD2HISA159152.56331.2801.0301.0027.35CATOM1248CE1HISA159150.37931.1821.2161.0025.70CATOM1249NE2HISA159151.39331.9940.9591.0024.73NATOM1250NLYSA160154.86726.6352.9741.0025.32NATOM1251CALYSA160155.41625.2853.0101.0028.19CATOM1252CLYSA160155.33224.5484.3371.0026.65CATOM1253OLYSA160155.13523.3304.3301.0027.81OATOM1254CBLYSA160156.87525.2722.5671.0030.97CATOM1255CGLYSA160157.03625.2401.0611.0037.66CATOM1256CDLYSA160158.49124.9470.6591.0040.59CATOM1257CELYSA160159.48425.8141.4561.0041.81CATOM1258NZLYSA160160.92025.5471.1051.0039.99NATOM1259NLYSA161155.47925.2555.4561.0023.14NATOM1260CALYSA161155.49124.5926.7561.0027.05CATOM1261CLYSA161154.40724.8707.8031.0026.50CATOM1262OLYSA161154.27224.1078.7601.0026.75OATOM1263CBLYSA161156.85224.8247.4151.0030.17CATOM1264CGLYSA161158.02524.5996.4601.0030.70CATOM1265CDLYSA161159.30325.2057.0241.0042.22CATOM1266CELYSA161159.66924.6048.3931.0043.48CATOM1267NZLYSA161160.12123.1708.3051.0050.98NATOM1268NILEA162153.62525.9347.6341.0024.98NATOM1269CAILEA162152.59526.2898.5911.0026.09CATOM1270CILEA162151.15226.2258.0481.0024.13CATOM1271OILEA162150.24225.7628.7391.0022.91OATOM1272CBILEA162152.86727.7329.1351.0020.66CATOM1273CG1ILEA162154.23827.7629.8291.0023.98CATOM1274CG2ILEA162151.69728.23110.0481.0022.51CATOM1275CD1ILEA162154.65529.11110.2811.0025.86CATOM1276NGLUA163150.94326.6646.8131.0023.29NATOM1277CAGLUA163149.58726.7386.2511.0023.82CATOM1278CGLUA163148.66325.5426.4771.0025.26CATOM1279OGLUA163147.52525.7236.9161.0025.68OATOM1280CBGLUA163149.62527.0504.7291.0023.25CATOM1281CGGLUA163148.24527.3444.1411.0023.18CATOM1282CDGLUA163148.28327.4732.6351.0027.42CATOM1283OE1GLUA163149.36727.7572.1111.0026.38OATOM1284OE2GLUA163147.23127.2971.9791.0033.94OATOM1285NSERA164149.11524.3306.1571.0024.25NATOM1286CASERA164148.26523.1636.3521.0026.69CATOM1287CSERA164147.80823.0047.7931.0025.60CATOM1288OSERA164146.62922.7668.0451.0025.68OATOM1289CBSERA164148.99221.8975.8941.0029.87CATOM1290OGSERA164149.12321.9224.4911.0038.03OATOM1291NALAA165148.74923.0898.7351.0026.04NATOM1292CAALAA165148.42922.97510.1461.0024.77CATOM1293CALAA165147.41724.04310.5841.0022.29CATOM1294OALAA165146.43223.76711.3171.0024.60OATOM1295CBALAA165149.74323.10610.9681.0023.75CATOM1296NLEUA166147.68125.28010.1651.0023.43NATOM1297CALEUA166146.85226.38110.5221.0021.35CATOM1298CLEUA166145.43726.1709.9341.0023.20CATOM1299OLEUA166144.44726.41110.6251.0024.09OATOM1300CBLEUA166147.50127.68010.0371.0023.96CATOM1301CGLEUA166146.83028.95710.5241.0022.68CATOM1302CD1LEUA166147.85230.15910.5531.0022.46CATOM1303CD2LEUA166145.66229.2629.5681.0028.35CATOM1304NARGA167145.35025.6888.6921.0022.59NATOM1305CAARGA167144.02925.4478.0951.0024.48CATOM1306CARGA167143.26324.3438.8361.0025.83CATOM1307OARGA167142.08024.5099.1391.0024.96OATOM1308CBARGA167144.13425.0086.6401.0024.06CATOM1309CGARGA167144.65526.0175.6341.0028.13CATOM1310CDARGA167144.77625.2274.3101.0034.69CATOM1311NEARGA167144.61426.0193.1011.0041.99NATOM1312CZARGA167143.89925.6492.0411.0042.97CATOM1313NH1ARGA167143.25324.4902.0221.0041.33NATOM1314NH2ARGA167143.83626.4450.9851.0045.06NATOM1315NASNA168143.94223.2329.1171.0026.42NATOM1316CAASNA168143.32222.1139.8221.0026.35CATOM1317CASNA168142.76622.53011.1671.0026.11CATOM1318OASNA168141.61022.18211.5591.0023.82OATOM1319CBASNA168144.35220.99010.0121.0027.98CATOM1320CGASNA168144.62920.2558.7271.0035.00CATOM1321OD1ASNA168143.87320.3877.7651.0037.41OATOM1322ND2ASNA168145.69419.4618.6991.0036.19NATOM1323NLYSA169143.57023.30211.8871.0023.11NATOM1324CALYSA169143.15523.76513.2051.0025.98CATOM1325CLYSA169141.97824.73413.1191.0022.95CATOM1326OLYSA169141.04824.67013.9251.0027.85OATOM1327CBLYSA169144.35024.41713.9301.0022.85CATOM1328CGLYSA169144.04324.89715.3401.0029.27CATOM1329CDLYSA169143.70723.73116.2671.0027.60CATOM1330CELYSA169143.55524.18717.7001.0033.35CATOM1331NZLYSA169143.21622.99518.5621.0037.61NATOM1332NMETA170142.01125.64012.1451.0022.68NATOM1333CAMETA170140.92926.60312.0071.0024.64CATOM1334CMETA170139.62125.86211.7061.0020.15CATOM1335OMETA170138.58126.18712.3031.0023.65OATOM1336CBMETA170141.23327.59210.8871.0026.04CATOM1337CGMETA170140.19628.71910.7411.0029.87CATOM1338SDMETA170140.03729.80912.2161.0035.30SATOM1339CEMETA170141.41130.72912.0641.0030.78CATOM1340NASNA171139.66924.89110.8011.0022.71NATOM1341CAASNA171138.45624.12910.4471.0024.07CATOM1342CASNA171137.91323.39511.6571.0025.60CATOM1343OASNA171136.68923.35411.8641.0023.50OATOM1344CBASNA171138.70823.1529.2801.0023.76CATOM1345CGASNA171138.84323.8977.9051.0023.11CATOM1346OD1ASNA171138.10124.8207.6201.0025.38OATOM1347ND2ASNA171139.80423.4767.0771.0026.17NATOM1348NSERA172138.80022.82812.4901.0024.48NATOM1349CASERA172138.29822.14213.6981.0026.82CATOM1350CSERA172137.74023.14714.7321.0022.82CATOM1351OSERA172136.69522.91115.3721.0025.07OATOM1352CBSERA172139.39921.25814.3241.0030.57CATOM1353OGSERA172140.43922.07314.8241.0039.62OATOM1354NGLNA173138.40624.27714.9191.0023.86NATOM1355CAGLNA173137.86425.23915.8631.0024.83CATOM1356CGLNA173136.50525.76315.3621.0025.26CATOM1357OGLNA173135.56025.98116.1501.0027.23OATOM1358CBGLNA173138.86426.37216.0651.0029.45CATOM1359CGGLNA173140.10325.91216.7741.0030.82CATOM1360CDGLNA173140.99627.09217.2181.0037.51CATOM1361OE1GLNA173141.63327.76916.4001.0044.33OATOM1362NE2GLNA173141.01027.35218.5091.0039.89NATOM1363NVALA174136.38725.96414.0581.0025.13NATOM1364CAVALA174135.10626.43213.5341.0024.65CATOM1365CVALA174133.99425.40713.7911.0021.41CATOM1366OVALA174132.94725.77014.2891.0024.63OATOM1367CBVALA174135.18426.75012.0231.0025.38CATOM1368CG1VALA174133.75426.83411.4201.0027.61CATOM1369CG2VALA174135.91128.06811.8261.0024.79CATOM1370NCYSA175134.21024.13113.5131.0021.16NATOM1371CACYSA175133.13523.15713.7801.0024.75CATOM1372CCYSA175132.84722.94015.2851.0026.89CATOM1373OCYSA175131.74222.55815.7021.0024.35OATOM1374CBCYSA175133.44421.85713.0691.0024.54CATOM1375SGCYSA175132.68921.82911.3991.0024.95SATOM1376NGLUA176133.85523.22916.1121.0029.43NATOM1377CAGLUA176133.71623.17917.5501.0029.98CATOM1378CGLUA176132.75724.29117.9851.0027.93CATOM1379OGLUA176131.83224.05418.8031.0031.72OATOM1380CBGLUA176135.09723.39518.1761.0032.55CATOM1381CGGLUA176135.18123.16519.6421.0039.70CATOM1382CDGLUA176136.52623.64320.1811.0046.95CATOM1383OE1GLUA176137.58723.31319.5501.0046.01OATOM1384OE2GLUA176136.50924.35721.2281.0051.19OATOM1385NLYSA177132.93725.49717.4491.0026.10NATOM1386CALYSA177132.06226.60517.8221.0027.23CATOM1387CLYSA177130.62126.32617.3421.0028.94CATOM1388OLYSA177129.65826.57418.0771.0029.06OATOM1389CBLYSA177132.54327.93417.2471.0031.86CATOM1390CGLYSA177133.81428.56317.9041.0034.63CATOM1391CDLYSA177133.54029.10519.3071.0038.85CATOM1392CELYSA177134.63330.08019.7631.0039.99CATOM1393NZLYSA177134.62030.31821.2271.0043.91NATOM1394NVALA178130.48525.78016.1321.0027.24NATOM1395CAVALA178129.15625.47915.5851.0026.07CATOM1396CVALA178128.43724.41016.4261.0024.57CATOM1397OVALA178127.30524.65316.9001.0024.46OATOM1398CBVALA178129.22924.99514.0981.0025.69CATOM1399CG1VALA178127.79924.54513.6301.0028.20CATOM1400CG2VALA178129.75426.13613.1931.0023.23CATOM1401NATHRA179129.08923.26816.6360.5025.08NATOM1402NBTHRA179129.08323.26716.6450.5025.39NATOM1403CAATHRA179128.47722.18917.4130.5027.71CATOM1404CABTHRA179128.45722.20117.4360.5028.23CATOM1405CATHRA179128.13522.62918.8480.5029.24CATOM1406CBTHRA179128.10422.67218.8470.5029.56CATOM1407OATHRA179127.07522.27519.3790.5030.28OATOM1408OBTHRA179127.01722.38119.3610.5030.62OATOM1409CBATHRA179129.38520.91917.4610.5026.44CATOM1410CBBTHRA179129.36620.94517.5770.5027.46CATOM1411OG1ATHRA179129.76320.52716.1350.5027.60OATOM1412OG1BTHRA179130.56421.29418.2850.5027.99OATOM1413CG2ATHRA179128.63519.77018.0650.5024.77CATOM1414CG2BTHRA179129.71720.37116.2120.5027.38CATOM1415NASNA180129.02123.39519.4781.0031.21NATOM1416CAASNA180128.77623.88920.8441.0033.89CATOM1417CASNA180127.56424.77220.8431.0033.19CATOM1418OASNA180126.75424.71621.7641.0037.55OATOM1419CBASNA180129.94024.74921.3741.0034.53CATOM1420CGASNA180129.69025.26822.8101.0040.24CATOM1421OD1ASNA180129.64124.48323.7711.0045.30OATOM1422ND2ASNA180129.52626.58622.9531.0040.51NATOM1423NSERA181127.44825.62119.8241.0030.38NATOM1424CASERA181126.34026.56119.7911.0030.09CATOM1425CSERA181124.96725.94619.6821.0026.83CATOM1426OSERA181124.01026.49420.2371.0025.07OATOM1427CBSERA181126.52027.56518.6691.0032.68CATOM1428OGSERA181127.65428.36218.9541.0044.77OATOM1429NVALA182124.87424.82918.9701.0024.75NATOM1430CAVALA182123.59324.14218.8301.0027.22CATOM1431CVALA182123.09523.60720.1981.0026.25CATOM1432OVALA182121.94323.82120.5881.0023.16OATOM1433CBVALA182123.71622.98117.7811.0027.55CATOM1434CG1VALA182122.42822.14217.7241.0026.04CATOM1435CG2VALA182124.00923.58416.3851.0026.42CATOM1436NASERA183123.98322.93620.9250.5026.36NATOM1437NBSERA183123.95922.92720.9400.5026.00NATOM1438CAASERA183123.64122.35822.2220.5028.23CATOM1439CABSERA183123.52622.38822.2240.5027.45CATOM1440CASERA183123.42923.41323.3100.5028.30CATOM1441CBSERA183123.37223.46523.3000.5027.70CATOM1442OASERA183122.46723.35124.0900.5026.71OATOM1443OBSERA183122.39423.47124.0640.5024.65OATOM1444CBASERA183124.74621.37822.6490.5029.05CATOM1445CBBSERA183124.49821.30222.6890.5028.26CATOM1446OGASERA183124.40220.66923.8330.5031.43OATOM1447OGBSERA183125.79621.82522.8660.5027.29OATOM1448NSERA184124.30324.41123.3261.0027.41NATOM1449CASERA184124.25825.44424.3461.0028.94CATOM1450CSERA184123.40126.68624.1221.0027.27CATOM1451OSERA184123.10827.42325.0721.0028.49OATOM1452CBSERA184125.68725.89424.6501.0032.28CATOM1453OGSERA184126.06126.95423.7991.0031.90OATOM1454NGLUA185122.97426.93422.9001.0024.34NATOM1455CAGLUA185122.19628.14022.6691.0021.04CATOM1456CGLUA185120.96227.86021.8001.0022.31CATOM1457OGLUA185119.86528.28922.1331.0022.95OATOM1458CBGLUA185123.09829.17821.9851.0023.67CATOM1459CGGLUA185124.39529.34922.7631.0031.02CATOM1460CDGLUA185125.32130.43122.2131.0035.91CATOM1461OE1GLUA185125.15230.87421.0461.0038.95OATOM1462OE2GLUA185126.23730.83322.9701.0041.06OATOM1463NLEUA186121.14627.10120.7321.0023.00NATOM1464CALEUA186120.03326.80919.8101.0023.22CATOM1465CLEUA186118.93225.95520.4211.0020.40CATOM1466OLEUA186117.76926.33020.3421.0022.38OATOM1467CBLEUA186120.53726.13818.5301.0022.39CATOM1468CGLEUA186120.05226.54417.1161.0032.01CATOM1469CD1LEUA186119.96325.34316.2401.0025.73CATOM1470CD2LEUA186118.75427.26217.1351.0026.16CATOM1471NGLNA187119.26324.81021.0091.0023.18NATOM1472CAGLNA187118.21223.98621.5971.0024.27CATOM1473CGLNA187117.47524.71722.7371.0025.94CATOM1474OGLNA187116.23724.69822.8181.0023.84OATOM1475CBGLNA187118.76122.64522.1031.0027.40CATOM1476CGGLNA187117.74421.84122.8741.0026.56CATOM1477CDGLNA187118.12720.36423.0081.0031.86CATOM1478OE1GLNA187117.91419.57222.1141.0029.13OATOM1479NE2GLNA187118.70019.99724.1691.0033.25NATOM1480NPROA188118.22225.34523.6461.0026.18NATOM1481CAPROA188117.56226.06924.7411.0027.85CATOM1482CPROA188116.65727.16824.1981.0024.86CATOM1483OPROA188115.61227.43024.7681.0025.50OATOM1484CBPROA188118.73726.65525.5201.0027.16CATOM1485CGPROA188119.79725.59225.3551.0027.45CATOM1486CDPROA188119.67325.23623.8851.0030.03CATOM1487NTYRA189117.07427.81523.1021.0024.19NATOM1488CATYRA189116.25628.87622.5021.0024.40CATOM1489CTYRA189114.92728.29622.0341.0025.09CATOM1490OTYRA189113.85228.78022.4141.0023.23OATOM1491CBTYRA189116.91429.55021.2751.0021.89CATOM1492CGTYRA189115.98330.59120.6201.0022.82CATOM1493CD1TYRA189115.64731.78321.2801.0024.28CATOM1494CD2TYRA189115.31130.29119.4441.0021.73CATOM1495CE1TYRA189114.63732.64720.7841.0023.47CATOM1496CE2TYRA189114.31531.12218.9481.0023.03CATOM1497CZTYRA189113.97632.31119.6321.0025.17CATOM1498OHTYRA189112.97133.10019.1231.0025.01OATOM1499NPHEA190114.96727.24021.2361.0022.83NATOM1500CAPHEA190113.68026.75120.7751.0025.66CATOM1501CPHEA190112.84426.14321.9291.0023.67CATOM1502OPHEA190111.60526.09921.8271.0022.61OATOM1503CBPHEA190113.85725.85519.5251.0026.98CATOM1504CGPHEA190113.93826.66718.2121.0027.82CATOM1505CD1PHEA190112.79527.25217.6591.0027.22CATOM1506CD2PHEA190115.17126.93217.6041.0028.89CATOM1507CE1PHEA190112.85728.10416.5121.0026.14CATOM1508CE2PHEA190115.26627.78816.4521.0026.83CATOM1509CZPHEA190114.09028.37715.9051.0023.06CATOM1510NGLNA191113.50325.74023.0201.0023.88NATOM1511CAGLNA191112.80525.25324.1971.0023.48CATOM1512CGLNA191112.12126.41424.9661.0022.32CATOM1513OGLNA191111.50726.18226.0011.0020.88OATOM1514CBGLNA191113.72924.43225.1091.0024.84CATOM1515CGGLNA191114.02123.07824.4611.0024.73CATOM1516CDGLNA191114.60522.03025.3961.0029.87CATOM1517OE1GLNA191115.07222.34126.4851.0030.16OATOM1518NE2GLNA191114.57820.76124.9581.0025.66NATOM1519NTHRA192112.20327.63524.4361.0021.04NATOM1520CATHRA192111.44428.74625.0331.0020.04CATOM1521CTHRA192110.02228.75024.4881.0020.79CATOM1522OTHRA192109.16829.55224.8901.0019.72OATOM1523CBTHRA192112.06930.15324.8071.0019.73CATOM1524OG1THRA192112.07830.52623.4141.0020.39OATOM1525CG2THRA192113.47430.16825.4371.0020.70CATOM1526NLEUA193109.74927.84923.5591.0021.88NATOM1527CALEUA193108.36327.71723.0741.0022.29CATOM1528CLEUA193107.53827.37324.3401.0020.07CATOM1529OLEUA193107.95826.56725.1791.0021.77OATOM1530CBLEUA193108.22026.54722.0661.0018.23CATOM1531CGLEUA193108.59826.79620.6031.0024.99CATOM1532CD1LEUA193108.40125.54019.7811.0020.37CATOM1533CD2LEUA193107.72127.88120.0531.0019.89CATOM1534NPROA194106.34927.98624.5061.0020.29NATOM1535CAPROA194105.57927.63925.7141.0019.31CATOM1536CPROA194104.88726.27225.6541.0018.13CATOM1537OPROA194104.41325.85924.5971.0021.37OATOM1538CBPROA194104.54928.78625.8351.0021.54CATOM1539CGPROA194104.30529.15624.3531.0022.99CATOM1540CDPROA194105.73729.10823.7501.0020.06CATOM1541NVALA195104.86625.56026.7781.0019.82NATOM1542CAVALA195104.10724.28426.7881.0021.94CATOM1543CVALA195102.73024.45527.4461.0023.92CATOM1544OVALA195101.71724.44126.7321.0025.89OATOM1545CBVALA195104.85023.16127.4901.0019.83CATOM1546CG1VALA195103.98921.90627.4541.0022.29CATOM1547CG2VALA195106.20022.92426.7721.0023.48CATOM1548NMETA196102.69324.55928.7851.0025.99NATOM1549CAMETA196101.43224.78829.5611.0025.86CATOM1550CMETA196101.41526.32229.7661.0027.21CATOM1551OMETA196102.09826.84830.6621.0028.87OATOM1552CBMETA196101.47824.07730.9251.0033.30CATOM1553CGMETA196101.62822.54130.8591.0030.15CATOM1554SDMETA196100.31821.66329.8911.0037.31SATOM1555CEMETA19699.17121.21031.1861.0036.65CATOM1556NTHRA197100.67327.04328.9221.0026.18NATOM1557CATHRA197100.63728.52128.9551.0023.64CATOM1558CTHRA19799.35329.08329.6211.0022.70CATOM1559OTHRA19798.23529.05429.0811.0017.43OATOM1560CBTHRA197101.01129.03327.5071.0032.57CATOM1561OG1THRA197100.03829.92426.9551.0032.53OATOM1562CG2THRA197101.26127.79926.6061.0021.87CATOM1563NLYSA19899.53829.56030.8551.0017.69NATOM1564CALYSA19898.41130.03431.6931.0016.55CATOM1565CLYSA19897.83231.37031.2251.0017.07CATOM1566OLYSA19898.54832.34430.9631.0020.17OATOM1567CBLYSA19898.87230.10933.1831.0015.78CATOM1568CGLYSA19897.72530.36534.1711.0017.55CATOM1569CDLYSA19898.24630.53535.6021.0019.54CATOM1570CELYSA19897.13030.88736.5691.0022.02CATOM1571NZLYSA19896.23629.69536.8491.0026.99NATOM1572NILEA19996.51731.42131.1101.0017.09NATOM1573CAILEA19995.81732.60530.6501.0018.15CATOM1574CILEA19995.32333.48131.8011.0019.51CATOM1575OILEA19995.51734.71331.8311.0021.21OATOM1576CBILEA19994.51732.19929.8191.0018.17CATOM1577CG1ILEA19994.87131.28728.6451.0023.48CATOM1578CG2ILEA19993.76033.44129.3841.0017.24CATOM1579CD1ILEA19993.54630.60528.0741.0017.53CATOM1580NASPA20094.65332.83732.7411.0014.93NATOM1581CAASPA20094.01333.50833.8641.0017.10CATOM1582CASPA20093.78332.50234.9761.0019.63CATOM1583OASPA20094.34431.39934.9241.0019.11OATOM1584CBASPA20092.66834.09733.4121.0017.71CATOM1585CGASPA20091.80033.08932.7041.0020.60CATOM1586OD1ASPA20091.78731.91833.1181.0018.71OATOM1587OD2ASPA20091.11533.47031.7401.0019.20OATOM1588NSERA20192.94432.85435.9511.0019.02NATOM1589CASERA20192.74731.93237.0931.0020.50CATOM1590CSERA20191.90230.73836.8171.0019.77CATOM1591OSERA20191.75429.86437.6881.0023.22OATOM1592CBSERA20192.17632.66038.3151.0021.90CATOM1593OGSERA20190.86633.13438.0761.0019.95OATOM1594NVALA20291.37830.66035.5951.0018.29NATOM1595CAVALA20290.51829.55335.2081.0016.71CATOM1596CVALA20291.09828.58934.1661.0017.73CATOM1597OVALA20290.90927.36734.3001.0017.56OATOM1598CBVALA20289.21330.10134.6631.0019.74CATOM1599CG1VALA20288.38829.02134.0021.0023.46CATOM1600CG2VALA20288.41630.68335.8641.0023.83CATOM1601NALAA20391.79929.12933.1681.0016.82NATOM1602CAALAA20392.32028.28432.0871.0015.01CATOM1603CALAA20393.73828.50531.6401.0017.70CATOM1604OALAA20394.35229.55031.9141.0015.33OATOM1605CBALAA20391.43128.45230.8921.0018.30CATOM1606NGLYA20494.22327.51330.9131.0015.41NATOM1607CAGLYA20495.54627.56530.2811.0017.66CATOM1608CGLYA20495.39126.90828.8871.0016.76CATOM1609OGLYA20494.31926.38228.5671.0014.75OATOM1610NILEA20596.42126.99228.0651.0014.46NATOM1611CAILEA20596.42726.34126.7661.0015.49CATOM1612CILEA20597.64225.42026.6981.0016.26CATOM1613OILEA20598.74625.84327.0281.0016.31OATOM1614CBILEA20596.58127.34125.6141.0015.07CATOM1615CG1ILEA20595.35128.26725.5531.0015.49CATOM1616CG2ILEA20596.67826.60324.2491.0017.51CATOM1617CD1ILEA20595.61629.53624.6411.0014.72CATOM1618NASNA20697.42624.15826.3031.0015.74NATOM1619CAASNA20698.51223.20026.1701.0019.28CATOM1620CASNA20699.02023.24224.7041.0017.73CATOM1621OASNA20698.29922.84423.7641.0015.25OATOM1622CBASNA20697.99421.79626.5271.0017.99CATOM1623CGASNA20699.10720.71226.5111.0021.23CATOM1624OD1ASNA206100.19320.91325.9981.0020.88OATOM1625ND2ASNA20698.77519.53727.1051.0024.75NATOM1626NTYRA207100.22023.77524.5231.0014.46NATOM1627CATYRA207100.85723.90223.2211.0014.21CATOM1628CTYRA207102.01122.89423.0811.0015.08CATOM1629OTYRA207102.85323.02522.1951.0015.16OATOM1630CBTYRA207101.41425.34923.0001.0016.89CATOM1631CGTYRA207100.36326.41822.6731.0015.13CATOM1632CD1TYRA20799.54226.32521.5381.0017.14CATOM1633CD2TYRA207100.26927.58623.4471.0018.54CATOM1634CE1TYRA20798.66327.37921.1631.0015.11CATOM1635CE2TYRA20799.38628.62023.0851.0016.50CATOM1636CZTYRA20798.59728.51621.9461.0017.52CATOM1637OHTYRA20797.75729.54821.5851.0017.06OATOM1638NGLYA208102.04621.90323.9641.0017.19NATOM1639CAGLYA208103.12820.89523.8761.0018.13CATOM1640CGLYA208103.15520.14722.5691.0017.53CATOM1641OGLYA208102.12619.90121.9981.0017.81OATOM1642NLEUA209104.35019.77822.0781.0016.77NATOM1643CALEUA209104.40519.06620.7851.0013.76CATOM1644CLEUA209103.85517.65820.9791.0017.46CATOM1645OLEUA209104.14517.05022.0201.0019.02OATOM1646CBLEUA209105.85818.98420.3161.0016.90CATOM1647CGLEUA209106.40820.11319.4751.0018.69CATOM1648CD1LEUA209106.33921.43520.2461.0020.90CATOM1649CD2LEUA209107.90619.75819.1061.0019.97CATOM1650NVALA210103.05717.19520.0111.0017.56NATOM1651CAVALA210102.47215.83020.0761.0016.69CATOM1652CVALA210103.22314.90619.0911.0021.90CATOM1653OVALA210102.86613.73718.9381.0018.52OATOM1654CBVALA210100.92115.84419.7641.0020.62CATOM1655CG1VALA210100.18516.49220.9321.0019.52CATOM1656CG2VALA210100.61016.60618.4491.0020.27CATOM1657NALAA211104.24015.44818.4141.0019.94NATOM1658CAALAA211105.08214.67817.4651.0019.38CATOM1659CALAA211106.37515.41117.2201.0021.07CATOM1660OALAA211106.47116.60117.4671.0019.58OATOM1661CBALAA211104.34914.51416.1251.0021.45CATOM1662NPROA212107.41914.71516.7411.0020.58NATOM1663CAPROA212108.65315.47016.4871.0019.71CATOM1664CPROA212108.46916.32715.2141.0020.34CATOM1665OPROA212107.69515.97814.3531.0018.95OATOM1666CBPROA212109.71814.35916.3671.0026.23CATOM1667CGPROA212108.93113.15915.8991.0022.32CATOM1668CDPROA212107.56213.26216.4921.0021.94CATOM1669NPROA213109.13917.48915.1131.0019.28NATOM1670CAPROA213109.00418.34513.9251.0019.81CATOM1671CPROA213109.32217.54012.6601.0020.67CATOM1672OPROA213110.34516.85612.6201.0022.30OATOM1673CBPROA213110.04519.45114.1441.0021.27CATOM1674CGPROA213110.14819.54215.6521.0021.58CATOM1675CDPROA213110.07618.05816.0931.0019.24CATOM1676NALAA214108.46517.63111.6501.0020.43NATOM1677CAALAA214108.63916.85510.4281.0021.64CATOM1678CALAA214109.03917.7579.2481.0024.37CATOM1679OALAA214108.35218.7308.9631.0022.63OATOM1680CBALAA214107.34316.11010.0961.0026.85CATOM1681NTHRA215110.11517.3828.5511.0020.66NATOM1682CATHRA215110.64718.1587.4321.0022.28CATOM1683CTHRA215110.24117.5486.0961.0021.26CATOM1684OTHRA215110.40016.3245.9091.0020.02OATOM1685CBTHRA215112.17818.1807.5151.0021.14CATOM1686OG1THRA215112.57618.7428.7731.0022.37OATOM1687CG2THRA215112.79219.0126.3851.0024.68CATOM1688NTHRA216109.65218.3745.2251.0021.25NATOM1689CATHRA216109.29017.9683.8721.0021.70CATOM1690CTHRA216110.06818.8652.9091.0019.85CATOM1691OTHRA216110.93119.6243.3661.0021.33OATOM1692CBTHRA216107.78618.0733.6141.0023.72CATOM1693OG1THRA216107.41419.4553.5791.0024.65OATOM1694CG2THRA216106.99917.3174.7201.0023.72CATOM1695NALAA217109.80818.7781.5931.0019.35NATOM1696CAALAA217110.58019.5720.6351.0021.35CATOM1697CALAA217110.35521.0530.8011.0022.61CATOM1698OALAA217111.25521.8740.5711.0021.02OATOM1699CBALAA217110.25019.183−0.7961.0025.10CATOM1700NGLUA218109.14521.3981.2131.0021.92NATOM1701CAGLUA218108.82422.8151.3561.0022.75CATOM1702CGLUA218108.28623.2932.6851.0023.86CATOM1703OGLUA218108.09624.5082.8571.0021.12OATOM1704CBGLUA218107.86123.2300.2471.0025.30CATOM1705CGGLUA218108.48323.034−1.1271.0030.46CATOM1706CDGLUA218107.64123.684−2.2071.0038.88CATOM1707OE1GLUA218106.47723.237−2.3811.0040.32OATOM1708OE2GLUA218108.15224.642−2.8541.0043.26OATOM1709NTHRA219108.07722.3763.6351.0022.78NATOM1710CATHRA219107.55222.7674.9251.0024.31CATOM1711CTHRA219108.22122.0966.1391.0024.94CATOM1712OTHRA219108.70220.9546.0451.0021.65OATOM1713CBTHRA219106.00122.4534.9931.0023.61CATOM1714OG1THRA219105.80321.0545.0241.0027.40OATOM1715CG2THRA219105.25922.9453.7051.0029.16CATOM1716NLEUA220108.29022.8247.2631.0024.74NATOM1717CALEUA220108.75822.2468.5361.0022.94CATOM1718CLEUA220107.50722.3809.4061.0019.99CATOM1719OLEUA220107.09123.5039.7051.0018.54OATOM1720CBLEUA220109.91423.0029.2081.0020.21CATOM1721CGLEUA220110.29622.51710.6201.0022.42CATOM1722CD1LEUA220110.58621.00810.6341.0024.61CATOM1723CD2LEUA220111.54323.25311.1011.0024.07CATOM1724NASPA221106.89521.2539.7791.0019.66NATOM1725CAASPA221105.65221.33010.5701.0023.35CATOM1726CASPA221105.82620.89712.0281.0023.88CATOM1727OASPA221106.38519.82212.3161.0023.57OATOM1728CBASPA221104.52220.5019.9461.0026.83CATOM1729CGASPA221104.19220.9318.5011.0038.55CATOM1730OD1ASPA221104.03122.1608.2361.0031.51OATOM1731OD2ASPA221104.09820.0177.6361.0042.67OATOM1732NVALA222105.34121.75312.9341.0021.22NATOM1733CAVALA222105.45921.53314.3711.0021.26CATOM1734CVALA222104.00821.31814.8541.0022.51CATOM1735OVALA222103.20522.24014.8541.0022.46OATOM1736CBVALA222106.11222.78215.0411.0023.65CATOM1737CG1VALA222106.35322.56316.5511.0025.96CATOM1738CG2VALA222107.46323.05114.3501.0023.60CATOM1739NGLNA223103.69520.11715.3051.0018.38NATOM1740CAGLNA223102.29619.77715.6961.0017.00CATOM1741CGLNA223102.11519.86917.1971.0018.33CATOM1742OGLNA223102.86319.23117.9441.0017.27OATOM1743CBGLNA223102.02918.36415.1661.0019.34CATOM1744CGGLNA223102.15718.33013.6321.0024.09CATOM1745CDGLNA223102.00916.92713.1271.0030.96CATOM1746OE1GLNA223102.86516.09913.3901.0033.92OATOM1747NE2GLNA223100.91716.64112.4121.0033.07NATOM1748NMETA224101.14320.69417.6321.0017.69NATOM1749CAMETA224100.94220.96019.0681.0017.18CATOM1750CMETA22499.56620.46919.5531.0014.46CATOM1751OMETA22498.58420.41018.7771.0015.86OATOM1752CBMETA224101.07922.49019.3431.0012.90CATOM1753CGMETA224102.28523.06418.7581.0015.35CATOM1754SDMETA224102.28324.89418.9171.0017.18SATOM1755CEMETA224104.02025.22918.9891.0020.82CATOM1756NLYSA22599.49720.11620.8261.0015.01NATOM1757CALYSA22598.25419.61521.4201.0017.20CATOM1758CLYSA22597.07920.57721.0751.0019.43CATOM1759OLYSA22595.99620.14520.5781.0017.01OATOM1760CBLYSA22598.43119.43822.9601.0016.86CATOM1761CGLYSA22597.19618.76623.6041.0018.08CATOM1762CDLYSA22596.97517.32123.0911.0024.51CATOM1763CELYSA22595.75416.71223.8091.0030.30CATOM1764NZLYSA22595.41115.31023.3951.0036.28NATOM1765NGLYA22697.30221.86721.3321.0017.33NATOM1766CAGLYA22696.31422.89821.0121.0017.08CATOM1767CGLYA22694.97622.66921.6821.0018.80CATOM1768OGLYA22693.92822.69521.0231.0018.72OATOM1769NGLUA22795.03422.48423.0011.0015.16NATOM1770CAGLUA22793.85722.25423.8421.0014.49CATOM1771CGLUA22793.81823.22125.0451.0014.65CATOM1772OGLUA22794.79323.29425.8111.0017.14OATOM1773CBGLUA22793.90320.79724.3831.0017.76CATOM1774CGGLUA22792.72020.41425.2481.0020.61CATOM1775CDGLUA22792.91419.07525.9851.0024.99CATOM1776OE1GLUA22793.89318.37725.6721.0027.11OATOM1777OE2GLUA22792.08218.74726.8681.0029.06OATOM1778NPHEA22892.70023.94525.2111.0016.67NATOM1779CAPHEA22892.52024.73926.4141.0015.56CATOM1780CPHEA22892.25023.72427.5631.0016.34CATOM1781OPHEA22891.56922.69127.3481.0018.01OATOM1782CBPHEA22891.28025.65826.3101.0014.54CATOM1783CGPHEA22891.51926.90725.5071.0014.31CATOM1784CD1PHEA22891.73826.86024.1341.0015.78CATOM1785CD2PHEA22891.53728.14626.1491.0017.56CATOM1786CE1PHEA22891.98928.02923.3891.0017.26CATOM1787CE2PHEA22891.78429.31425.4301.0016.11CATOM1788CZPHEA22892.01029.25324.0441.0015.69CATOM1789NTYRA22992.74424.00728.7721.0015.48NATOM1790CATYRA22992.51323.09929.9111.0019.84CATOM1791CTYRA22992.34423.88131.2291.0020.68CATOM1792OTYRA22992.66725.06831.3261.0018.45OATOM1793CBTYRA22993.70922.12030.0511.0020.47CATOM1794CGTYRA22994.98322.82630.4431.0022.62CATOM1795CD1TYRA22995.26323.13831.7881.0026.33CATOM1796CD2TYRA22995.85623.29529.4691.0020.54CATOM1797CE1TYRA22996.37623.91032.1281.0027.72CATOM1798CE2TYRA22996.95224.04629.7961.0024.80CATOM1799CZTYRA22997.21824.36431.1151.0026.20CATOM1800OHTYRA22998.31225.16831.3851.0032.46OATOM1801NSERA23091.79623.19732.2261.0023.78NATOM1802CASERA23091.61123.75033.5791.0026.93CATOM1803CSERA23092.69323.11534.4791.0031.83CATOM1804OSERA23093.08321.97534.2561.0031.61OATOM1805CBSERA23090.23223.36034.1141.0030.49CATOM1806OGSERA23090.18723.50135.5211.0031.30OATOM1807NGLUA23193.20923.82635.4751.0037.31NATOM1808CAGLUA23194.21223.17636.3301.0044.66CATOM1809CGLUA23193.50822.30137.3601.0048.25CATOM1810OGLUA23194.15321.52938.0721.0050.37OATOM1811CBGLUA23195.14024.19737.0031.0046.75CATOM1812CGGLUA23196.40524.42736.1761.0049.76CATOM1813CDGLUA23197.02625.79336.3911.0051.66CATOM1814OE1GLUA23197.51326.03937.5131.0051.75OATOM1815OE2GLUA23197.02726.61735.4351.0054.23OATOM1816NASNA23292.17722.39637.3991.0051.16NATOM1817CAASNA23291.36621.59738.3161.0053.91CATOM1818CASNA23290.81920.33837.6361.0055.63CATOM1819OASNA23290.82319.26038.2281.0057.18OATOM1820CBASNA23290.20022.44338.8701.0054.72CATOM1821NHISA23390.34720.46136.3981.0057.55NATOM1822CAHISA23389.79019.30635.6821.0058.37CATOM1823CHISA23390.87418.47634.9921.0058.77CATOM1824OHISA23392.02518.91434.8841.0060.07OATOM1825CBHISA23388.74519.76934.6511.0058.42CATOM1826NHISA23490.50717.28134.5191.0057.54NATOM1827CAHISA23491.47016.40033.8381.0055.46CATOM1828CHISA23490.95515.72532.5531.0053.71CATOM1829OHISA23491.74415.37231.6711.0054.83OATOM1830CBHISA23491.97115.32534.8151.0056.68CATOM1831NASNA23589.63815.55832.4491.0049.69NATOM1832CAASNA23588.99214.89731.3041.0045.13CATOM1833CASNA23589.28415.46229.9011.0040.67CATOM1834OASNA23589.23616.67129.6921.0040.43OATOM1835CBASNA23587.48514.88531.5361.0044.81CATOM1836NPROA23689.60514.58928.9211.0036.39NATOM1837CAPROA23689.86915.11727.5721.0033.34CATOM1838CPROA23688.50315.58727.0391.0028.17CATOM1839OPROA23687.47515.17227.5501.0027.99OATOM1840CBPROA23690.34613.88626.7891.0036.52CATOM1841CGPROA23690.83212.95427.8641.0036.76CATOM1842CDPROA23689.84313.13328.9621.0038.67CATOM1843NPROA23788.48916.46626.0311.0023.79NATOM1844CAPROA23787.23116.95025.4431.0020.12CATOM1845CPROA23786.59315.69724.8031.0022.36CATOM1846OPROA23787.29414.77624.4301.0020.34OATOM1847CBPROA23787.70917.90724.3551.0023.89CATOM1848CGPROA23789.08418.37424.8691.0028.62CATOM1849CDPROA23789.65217.07725.3861.0021.45CATOM1850NPROA23885.28015.66024.6811.0017.79NATOM1851CAPROA23884.68214.46224.0681.0018.04CATOM1852CPROA23884.67914.47822.5351.0023.31CATOM1853OPROA23884.26213.52021.9051.0025.60OATOM1854CBPROA23883.28514.44524.6591.0021.14CATOM1855CGPROA23882.96915.97424.8201.0021.29CATOM1856CDPROA23884.29916.43925.4511.0018.37CATOM1857NPHEA23985.16815.55321.9211.0021.27NATOM1858CAPHEA23985.23315.65820.4691.0021.01CATOM1859CPHEA23986.70815.58320.0601.0021.12CATOM1860OPHEA23987.58815.63220.9161.0020.28OATOM1861CBPHEA23984.54916.95820.0311.0022.95CATOM1862CGPHEA23984.90318.14220.8731.0021.34CATOM1863CD1PHEA23986.09418.81320.6511.0021.37CATOM1864CD2PHEA23984.04918.57621.8991.0023.79CATOM1865CE1PHEA23986.44319.92421.4551.0023.01CATOM1866CE2PHEA23984.38419.68022.6951.0022.92CATOM1867CZPHEA23985.58520.35122.4681.0021.34CATOM1868NALAA24086.97815.47918.7591.0023.40NATOM1869CAALAA24088.32715.29118.2461.0024.11CATOM1870CALAA24088.76016.34417.2571.0021.45CATOM1871OALAA24087.94616.96316.5951.0022.52OATOM1872CBALAA24088.43213.90917.5661.0028.44CATOM1873NPROA24190.06216.52117.1191.0021.88NATOM1874CAPROA24190.57817.51616.1801.0022.65CATOM1875CPROA24190.31517.06314.7311.0021.80CATOM1876OPROA24190.27015.82114.4441.0020.85OATOM1877CBPROA24192.08117.55816.4801.0022.51CATOM1878CGPROA24192.19016.95817.8741.0025.33CATOM1879CDPROA24191.12915.94517.9611.0024.33CATOM1880NPROA24290.14718.02213.8081.0019.29NATOM1881CAPROA24289.91117.70512.3891.0018.79CATOM1882CPROA24291.26717.57911.6831.0020.78CATOM1883OPROA24292.30017.93412.2371.0020.96OATOM1884CBPROA24289.14918.93511.8761.0019.96CATOM1885CGPROA24289.92420.07912.6241.0017.80CATOM1886CDPROA24290.14119.50414.0361.0019.04CATOM1887NAVALA24391.29017.02310.4780.5022.70NATOM1888NBVALA24391.26217.05710.4640.5022.06NATOM1889CAAVALA24392.57116.9609.7770.5021.31CATOM1890CABVALA24392.50916.9699.7040.5019.93CATOM1891CAVALA24392.70518.3769.1960.5021.94CATOM1892CBVALA24392.70018.3819.1320.5021.31CATOM1893OAVALA24391.70918.9818.7920.5022.85OATOM1894OBVALA24391.73418.9948.6680.5022.80OATOM1895CBAVALA24392.55915.8888.6400.5025.23CATOM1896CBBVALA24392.37615.8978.5720.5022.72CATOM1897CG1AVALA24391.43616.1717.6730.5023.84CATOM1898CG1BVALA24393.29816.2127.3980.5021.19CATOM1899CG2AVALA24393.91915.8557.9300.5024.59CATOM1900CG2BVALA24392.72214.5349.1520.5018.72CATOM1901NMETA24493.91318.9239.2041.0020.72NATOM1902CAMETA24494.13920.2548.6751.0023.41CATOM1903CMETA24495.18420.1077.5701.0026.71CATOM1904OMETA24496.37119.9017.8321.0030.28OATOM1905CBMETA24494.64621.2619.7601.0020.59CATOM1906CGMETA24493.68021.49010.9081.0022.85CATOM1907SDMETA24494.34622.80112.0201.0020.09SATOM1908CEMETA24495.45321.87713.0691.0019.59CATOM1909NGLUA24594.73620.2006.3281.0026.88NATOM1910CAGLUA24595.66620.0905.1871.0031.38CATOM1911CGLUA24595.58321.3384.3361.0031.54CATOM1912OGLUA24594.49021.8003.9991.0031.62OATOM1913CBGLUA24595.33318.8634.3271.0031.53CATOM1914CGGLUA24595.99118.8382.9281.0041.49CATOM1915CDGLUA24595.41619.8931.9301.0047.99CATOM1916OE1GLUA24594.19220.1912.0131.0052.97OATOM1917OE2GLUA24596.18120.4081.0531.0051.37OATOM1918NPHEA24696.74621.8994.0161.0033.99NATOM1919CAPHEA24696.82323.0783.1641.0034.20CATOM1920CPHEA24698.12723.0702.3731.0037.48CATOM1921OPHEA24699.17022.6052.8491.0034.14OATOM1922CBPHEA24696.66424.3743.9721.0032.58CATOM1923CGPHEA24697.54624.4635.1661.0029.18CATOM1924CD1PHEA24697.30923.6806.2871.0028.47CATOM1925CD2PHEA24698.58625.3705.1931.0028.19CATOM1926CE1PHEA24698.10723.8167.4131.0028.92CATOM1927CE2PHEA24699.37625.5136.3091.0026.95CATOM1928CZPHEA24699.14524.7447.4201.0029.16CATOM1929NPROA24798.08623.6331.1551.0040.99NATOM1930CAPROA24799.24423.6850.2611.0040.38CATOM1931CPROA247100.40924.4740.8101.0039.40CATOM1932OPROA247100.23725.4151.5911.0039.23OATOM1933CBPROA24798.65724.311−1.0021.0044.55CATOM1934CGPROA24797.75125.378−0.4011.0044.21CATOM1935CDPROA24797.06424.6220.7381.0043.41CATOM1936NALAA248101.60924.0680.4041.0038.78NATOM1937CAALAA248102.80024.7850.8091.0040.12CATOM1938CALAA248102.70326.1320.0641.0040.68CATOM1939OALAA248102.34926.190−1.1231.0040.32OATOM1940CBALAA248104.06124.0220.3821.0040.93CATOM1941NALAA249102.97827.2040.7911.0037.54NATOM1942CAALAA249102.95528.5570.2541.0038.92CATOM1943CALAA249104.27529.0870.7791.0037.54CATOM1944OALAA249104.76928.6001.7891.0035.55OATOM1945CBALAA249101.78529.3410.8221.0038.19CATOM1946NHISA250104.84630.0670.0891.0038.81NATOM1947CAHISA250106.14030.5940.4781.0039.15CATOM1948CHISA250106.12732.1040.6221.0038.15CATOM1949OHISA250107.16032.7100.8741.0036.45OATOM1950CBHISA250107.18230.201−0.5851.0043.01CATOM1951CGHISA250106.86828.920−1.2981.0045.37CATOM1952ND1HISA250107.03428.769−2.6581.0047.21NATOM1953CD2HISA250106.40327.730−0.8441.0047.20CATOM1954CE1HISA250106.68227.546−3.0111.0048.82CATOM1955NE2HISA250106.29426.893−1.9291.0046.58NATOM1956NASPA251104.96832.7140.4341.0034.36NATOM1957CAASPA251104.86434.1590.5491.0036.92CATOM1958CASPA251105.11434.6781.9741.0034.32CATOM1959OASPA251105.51535.8282.1641.0035.79OATOM1960CBASPA251103.48534.6000.0511.0041.81CATOM1961CGASPA251102.35433.6750.5321.0047.98CATOM1962OD1ASPA251101.71033.9361.5841.0049.24OATOM1963OD2ASPA251102.11032.655−0.1561.0055.44OATOM1964NARGA252104.83933.8622.9821.0028.81NATOM1965CAARGA252105.06434.2864.3551.0024.57CATOM1966CARGA252105.91533.2675.1121.0023.19CATOM1967OARGA252106.02532.1184.6881.0023.04OATOM1968CBARGA252103.73134.5135.0711.0028.63CATOM1969CGARGA252103.00835.7374.4471.0034.58CATOM1970CDARGA252101.94436.3035.3251.0042.10CATOM1971NEARGA252101.50337.6084.8341.0045.30NATOM1972CZARGA252100.88237.8213.6681.0051.24CATOM1973NH1ARGA252100.60336.8112.8341.0051.40NATOM1974NH2ARGA252100.53539.0563.3261.0049.75NATOM1975NMETA253106.48233.7136.2281.0019.98NATOM1976CAMETA253107.40632.8767.0441.0020.40CATOM1977CMETA253106.80331.7147.8361.0021.82CATOM1978OMETA253107.43830.6588.0011.0020.21OATOM1979CBMETA253108.17433.7578.0321.0017.57CATOM1980CGMETA253109.14734.7367.3671.0019.36CATOM1981SDMETA253110.11135.5578.6021.0022.77SATOM1982CEMETA253110.83836.9177.5471.0027.30CATOM1983NVALA254105.59431.9048.3331.0019.67NATOM1984CAVALA254104.98230.8599.1321.0023.94CATOM1985CVALA254103.48230.8118.9041.0022.95CATOM1986OVALA254102.83531.8338.5111.0022.10OATOM1987CBVALA254105.26031.02510.6851.0025.52CATOM1988CG1VALA254106.76231.00410.9981.0029.22CATOM1989CG2VALA254104.64632.33611.2121.0028.41CATOM1990NTYRA255102.92929.6059.0811.0020.57NATOM1991CATYRA255101.48929.4508.9191.0019.82CATOM1992CTYRA255100.96928.73610.1721.0024.29CATOM1993OTYRA255101.50827.71710.5721.0025.10OATOM1994CBTYRA255101.14728.6727.6271.0023.43CATOM1995CGTYRA255101.54429.4006.3611.0023.86CATOM1996CD1TYRA255102.82929.2835.8331.0024.68CATOM1997CD2TYRA255100.65630.2515.7321.0025.84CATOM1998CE1TYRA255103.21429.9854.7141.0028.52CATOM1999CE2TYRA255101.03830.9774.5931.0029.21CATOM2000CZTYRA255102.31030.8434.0981.0029.63CATOM2001OHTYRA255102.69531.6233.0391.0031.12OATOM2002NLEUA25699.97529.33710.8251.0022.20NATOM2003CALEUA25699.38728.78212.0521.0022.73CATOM2004CLEUA25698.03528.21011.7341.0020.05CATOM2005OLEUA25697.18228.95511.2701.0022.21OATOM2006CBLEUA25699.16229.91013.0651.0029.27CATOM2007CGLEUA25699.60229.64314.4851.0034.91CATOM2008CD1LEUA25698.80728.53715.1241.0036.90CATOM2009CD2LEUA256101.06529.28814.4271.0037.63CATOM2010NGLYA25797.83326.90911.9611.0020.18NATOM2011CAGLYA25796.50426.33011.7141.0020.14CATOM2012CGLYA25795.82526.22213.0601.0018.39CATOM2013OGLYA25796.32425.51013.9451.0020.61OATOM2014NLEUA25894.71026.91913.2441.0015.18NATOM2015CALEUA25893.99226.88614.5361.0015.25CATOM2016CLEUA25892.68426.14214.2731.0015.59CATOM2017OLEUA25891.75626.65813.6411.0016.49OATOM2018CBLEUA25893.66528.30815.0741.0016.51CATOM2019CGLEUA25894.92829.19915.2821.0016.07CATOM2020CD1LEUA25894.47730.54915.8531.0017.28CATOM2021CD2LEUA25895.90928.57216.3411.0017.48CATOM2022NSERA25992.62224.91714.7791.0017.23NATOM2023CASERA25991.45524.10414.5451.0016.74CATOM2024CSERA25990.18724.48215.2601.0016.58CATOM2025OSERA25990.21025.11616.3051.0015.07OATOM2026CBSERA25991.78422.63914.9001.0015.45CATOM2027OGSERA25991.87122.49616.3161.0015.99OATOM2028NASPA26089.04424.05614.6871.0016.41NATOM2029CAASPA26087.79424.31115.3691.0016.86CATOM2030CASPA26087.86523.70216.7781.0020.16CATOM2031OASPA26087.39524.28717.7621.0018.71OATOM2032CBASPA26086.57323.79114.5601.0015.50CATOM2033CGASPA26086.69022.31714.1081.0022.18CATOM2034OD1ASPA26087.62021.57614.5591.0017.28OATOM2035OD2ASPA26085.80821.94313.2811.0019.64OATOM2036NTYRA26188.51722.54616.8911.0015.22NATOM2037CATYRA26188.68621.87018.1681.0015.66CATOM2038CTYRA26189.32422.81619.2431.0016.80CATOM2039OTYRA26188.83022.95520.3601.0016.98OATOM2040CBTYRA26189.57020.64417.8741.0017.87CATOM2041CGTYRA26190.09219.94519.0771.0018.50CATOM2042CD1TYRA26191.27220.33519.6691.0019.08CATOM2043CD2TYRA26189.39518.83819.5981.0019.36CATOM2044CE1TYRA26191.78319.66520.7561.0024.09CATOM2045CE2TYRA26189.90218.15320.6731.0022.99CATOM2046CZTYRA26191.09118.57421.2441.0023.38CATOM2047OHTYRA26191.61317.89122.2981.0029.33OATOM2048NPHEA26290.39023.48718.8601.0015.63NATOM2049CAPHEA26291.09824.43719.7371.0014.26CATOM2050CPHEA26290.09725.43720.3511.0014.52CATOM2051OPHEA26289.97825.56121.5921.0015.62OATOM2052CBPHEA26292.15325.13018.8701.0015.43CATOM2053CGPHEA26292.85126.30119.5131.0019.33CATOM2054CD1PHEA26293.85226.11220.4631.0020.88CATOM2055CD2PHEA26292.52427.59219.1271.0022.45CATOM2056CE1PHEA26294.51927.21221.0091.0021.68CATOM2057CE2PHEA26293.18128.71319.6761.0023.10CATOM2058CZPHEA26294.16928.53120.6051.0021.28CATOM2059NPHEA26389.30926.07519.4841.0014.45NATOM2060CAPHEA26388.35227.07519.9431.0015.30CATOM2061CPHEA26387.25826.47920.8191.0015.97CATOM2062OPHEA26386.79627.09521.8141.0015.61OATOM2063CBPHEA26387.73627.80218.7281.0017.51CATOM2064CGPHEA26388.72428.62917.9551.0020.10CATOM2065CD1PHEA26389.24229.79618.5041.0020.71CATOM2066CD2PHEA26389.15128.23016.6881.0019.83CATOM2067CE1PHEA26390.20930.56517.7921.0020.61CATOM2068CE2PHEA26390.08728.97715.9691.0020.83CATOM2069CZPHEA26390.63330.15216.5231.0022.55CATOM2070NASNA26486.75625.30120.4241.0015.18NATOM2071CAASNA26485.72624.67521.2141.0016.06CATOM2072CASNA26486.22324.20522.6061.0015.79CATOM2073OASNA26485.42124.15223.5501.0017.13OATOM2074CBASNA26485.14323.49520.4281.0016.36CATOM2075CGASNA26484.11723.95219.3591.0021.05CATOM2076OD1ASNA26482.93124.18319.6881.0026.99OATOM2077ND2ASNA26484.55924.09718.1231.0021.79NATOM2078NTHRA26587.50623.80522.7321.0015.14NATOM2079CATHRA26587.99823.42524.0641.0013.57CATOM2080CTHRA26587.96224.67024.9801.0016.07CATOM2081OTHRA26587.73124.53126.1861.0013.96OATOM2082CBTHRA26589.43022.81224.0941.0014.49CATOM2083OG1THRA26590.40623.72223.5641.0016.61OATOM2084CG2THRA26589.45921.51223.2711.0014.99CATOM2085NALAA26688.15825.85324.4101.0015.69NATOM2086CAALAA26688.03127.06125.2621.0017.59CATOM2087CALAA26686.57927.20125.7691.0016.83CATOM2088OALAA26686.34827.45626.9381.0017.30OATOM2089CBALAA26688.43728.33124.4721.0016.62CATOM2090NGLYA26785.58127.05024.8911.0016.75NATOM2091CAGLYA26784.21527.13625.4011.0017.52CATOM2092CGLYA26783.92626.09526.4831.0017.67CATOM2093OGLYA26783.22626.35627.4381.0017.14OATOM2094NLEUA26884.44724.88026.3371.0015.09NATOM2095CALEUA26884.22523.80527.2881.0018.38CATOM2096CLEUA26884.81124.14528.6681.0014.86CATOM2097OLEUA26884.11624.07429.6811.0017.18OATOM2098CBLEUA26884.87722.52726.7491.0020.58CATOM2099CGLEUA26884.86721.35127.7191.0023.31CATOM2100CD1LEUA26883.43820.90227.8761.0031.11CATOM2101CD2LEUA26885.71620.17827.1321.0030.53CATOM2102NVALA26986.06424.59028.7051.0013.96NATOM2103CAVALA26986.72124.93129.9731.0016.30CATOM2104CVALA26986.02426.06530.7361.0015.45CATOM2105OVALA26985.73925.92731.9341.0016.25OATOM2106CBVALA26988.21825.27829.7691.0014.67CATOM2107CG1VALA26988.88325.76731.1681.0017.93CATOM2108CG2VALA26988.94524.01329.3021.0017.95CATOM2109NTYRA27085.74527.17030.0561.0015.81NATOM2110CATYRA27085.10328.29330.7551.0015.28CATOM2111CTYRA27083.65627.95031.1791.0015.51CATOM2112OTYRA27083.22628.31432.2601.0016.48OATOM2113CBTYRA27085.16629.55229.8661.0016.61CATOM2114CGTYRA27086.55930.17629.8171.0016.34CATOM2115CD1TYRA27087.05030.93830.8771.0018.08CATOM2116CD2TYRA27087.38629.97328.7331.0018.45CATOM2117CE1TYRA27088.33531.48030.8461.0018.60CATOM2118CE2TYRA27088.67330.51628.6901.0020.17CATOM2119CZTYRA27089.13531.27529.7591.0017.31CATOM2120OHTYRA27090.35631.87429.6641.0017.86OATOM2121NGLNA27182.92327.20330.3431.0014.05NATOM2122CAGLNA27181.56926.87830.7661.0017.26CATOM2123CGLNA27181.62625.95032.0081.0016.43CATOM2124OGLNA27180.84626.09432.9561.0016.56OATOM2125CBGLNA27180.78826.19629.6271.0017.91CATOM2126CGGLNA27179.25326.02529.9801.0019.55CATOM2127CDGLNA27178.98724.69430.5961.0029.59CATOM2128OE1GLNA27179.72223.74430.3351.0028.56OATOM2129NE2GLNA27177.92524.59431.4011.0030.36NATOM2130NGLUA27282.52924.96631.9731.0023.33NATOM2131CAGLUA27282.62424.03633.0951.0022.10CATOM2132CGLUA27283.08224.66534.4181.0024.10CATOM2133OGLUA27282.75624.18535.5181.0023.52OATOM2134CBGLUA27283.48322.81032.6741.0023.70CATOM2135CGGLUA27282.77821.96631.6411.0030.03CATOM2136CDGLUA27283.53420.67631.2351.0032.34CATOM2137OE1GLUA27284.76920.60131.3971.0035.51OATOM2138OE2GLUA27282.86619.74230.7381.0039.60OATOM2139NALAA27383.79925.77134.3201.0022.43NATOM2140CAALAA27384.30526.46435.4731.0020.25CATOM2141CALAA27383.20427.29936.1171.0020.10CATOM2142OALAA27383.41027.92037.1701.0021.65OATOM2143CBALAA27385.43227.35335.0571.0020.47CATOM2144NGLYA27482.07327.38335.4321.0018.17NATOM2145CAGLYA27480.98528.18535.9651.0022.05CATOM2146CGLYA27481.13629.69135.7991.0023.12CATOM2147OGLYA27480.43530.46336.4761.0026.02OATOM2148NVALA27582.00330.13934.9061.0018.92NATOM2149CAVALA27582.14431.56734.7131.0020.71CATOM2150CVALA27581.31332.20133.5901.0018.53CATOM2151OVALA27581.29933.45233.4601.0020.13OATOM2152CBVALA27583.60931.97434.5081.0024.08CATOM2153CG1VALA27584.40431.66035.7831.0027.69CATOM2154CG2VALA27584.18531.30033.3081.0025.66CATOM2155NLEUA27680.62031.38432.7921.0017.52NATOM2156CALEUA27679.78831.92031.7221.0018.05CATOM2157CLEUA27678.38832.17732.3101.0020.58CATOM2158OLEUA27677.38231.55031.9311.0021.55OATOM2159CBLEUA27679.73230.96330.5041.0019.61CATOM2160CGLEUA27681.05430.61429.8061.0018.97CATOM2161CD1LEUA27680.83829.83028.5071.0022.04CATOM2162CD2LEUA27681.79031.97329.4911.0020.31CATOM2163NLYSA27778.33533.09333.2711.0019.75NATOM2164CALYSA27777.06033.43433.9121.0021.66CATOM2165CLYSA27777.09234.87534.3701.0020.25CATOM2166OLYSA27778.16535.47434.5161.0022.40OATOM2167CBLYSA27776.76632.52435.1151.0024.15CATOM2168CGLYSA27777.62032.83236.3641.0029.16CATOM2169CDLYSA27777.15232.11337.6641.0038.12CATOM2170CELYSA27776.37330.80337.4271.0042.69CATOM2171NZLYSA27777.10129.78036.6001.0045.20NATOM2172NMETA27875.92035.44134.5841.0019.99NATOM2173CAMETA27875.82836.81735.0371.0016.84CATOM2174CMETA27874.49437.02935.7541.0018.46CATOM2175OMETA27873.49236.43335.3811.0019.35OATOM2176CBMETA27875.88937.71033.8111.0022.13CATOM2177CGMETA27876.51538.99433.9881.0029.72CATOM2178SDMETA27876.23439.84632.3601.0031.92SATOM2179CEMETA27875.78441.30733.0371.0033.53CATOM2180NTHRA27974.50037.83436.8091.0018.01NATOM2181CATHRA27973.25738.15837.5271.0019.46CATOM2182CTHRA27972.94639.63237.2301.0022.45CATOM2183OTHRA27973.80640.49837.3771.0022.57OATOM2184CBTHRA27973.43337.96539.0641.0019.32CATOM2185OG1THRA27973.55236.56239.3601.0018.84OATOM2186CG2THRA27972.19538.50739.8171.0023.38CATOM2187NLEUA28071.72939.89136.7771.0022.38NATOM2188CALEUA28071.28641.24936.4751.0024.48CATOM2189CLEUA28070.28841.69937.5481.0025.89CATOM2190OLEUA28069.33940.97137.8991.0024.93OATOM2191CBLEUA28070.61941.25335.1041.0025.82CATOM2192CGLEUA28071.53240.70833.9911.0032.45CATOM2193CD1LEUA28070.72140.36932.7521.0033.01CATOM2194CD2LEUA28072.58641.73133.6571.0032.87CATOM2195NARGA28170.51842.88438.1021.0027.91NATOM2196CAARGA28169.63543.48139.1251.0030.19CATOM2197CARGA28169.16344.81438.5341.0032.36CATOM2198OARGA28169.80845.34437.6071.0030.59OATOM2199CBARGA28170.40643.75940.4171.0032.39CATOM2200CGARGA28170.98242.49341.0941.0038.37CATOM2201CDARGA28172.17942.86242.0011.0047.28CATOM2202NEARGA28173.39142.07441.7091.0052.64NATOM2203CZARGA28173.60840.82442.1341.0057.96CATOM2204NH1ARGA28172.69440.19942.8801.0058.25NATOM2205NH2ARGA28174.74640.19141.8301.0058.24NATOM2206NASPA28268.04945.33039.0611.0031.98NATOM2207CAASPA28267.48746.59338.5631.0033.01CATOM2208CASPA28268.48347.75138.6251.0030.97CATOM2209OASPA28268.49848.60537.7431.0031.89OATOM2210CBASPA28266.21246.95239.3371.0033.48CATOM2211CGASPA28265.38648.04138.6411.0037.38CATOM2212OD1ASPA28264.80248.88039.3391.0043.48OATOM2213OD2ASPA28265.30048.07037.4091.0033.42OATOM2214NASPA28369.34347.78239.6331.0033.43NATOM2215CAASPA28370.32548.86239.7281.0035.26CATOM2216CASPA28371.33848.87638.5591.0035.13CATOM2217OASPA28372.03049.86738.3501.0035.69OATOM2218CBASPA28371.08248.76541.0681.0040.19CATOM2219CGASPA28371.85947.45541.2091.0043.35CATOM2220OD1ASPA28372.98947.36040.6571.0046.39OATOM2221OD2ASPA28371.33546.51541.8551.0045.72OATOM2222NMETA28471.43347.77337.8021.0029.89NATOM2223CAMETA28472.36147.67536.6771.0025.19CATOM2224CMETA28471.70648.06035.3451.0027.52CATOM2225OMETA28472.38348.13634.3131.0028.22OATOM2226CBMETA28472.91546.22736.5901.0027.31CATOM2227CGMETA28473.69645.75437.8331.0025.10CATOM2228SDMETA28473.83543.89337.9671.0029.95SATOM2229CEMETA28474.69443.57336.4641.0027.19CATOM2230NILEA28570.39948.27635.3571.0028.04NATOM2231CAILEA28569.66948.63034.1331.0030.56CATOM2232CILEA28569.75150.13433.9071.0032.39CATOM2233OILEA28569.09750.87034.6331.0031.53OATOM2234CBILEA28568.18048.28134.2751.0032.03CATOM2235CG1ILEA28568.05246.81734.7041.0032.08CATOM2236CG2ILEA28567.43348.58032.9711.0030.35CATOM2237CD1ILEA28568.77945.87033.7551.0035.58CATOM2238NPROA28670.54650.58132.9001.0032.61NATOM2239CAPROA28670.76451.98932.5111.0036.58CATOM2240CPROA28669.51652.83332.6661.0034.52CATOM2241OPROA28668.40352.40732.3761.0036.47OATOM2242CBPROA28671.21551.87931.0571.0035.24CATOM2243CGPROA28672.05050.63431.1021.0037.40CATOM2244CDPROA28671.21449.68331.9381.0033.96CATOM2245NLYSA28769.72054.04833.1511.0038.14NATOM2246CALYSA28768.63254.97233.3801.0038.21CATOM2247CLYSA28767.85255.18132.0901.0037.23CATOM2248OLYSA28766.63955.38832.1061.0034.13OATOM2249CBLYSA28769.22156.29433.8611.0039.11CATOM2250CGLYSA28768.22757.40634.0221.0039.87CATOM2251CDLYSA28768.52458.13235.3111.0039.55CATOM2252CELYSA28769.99958.43035.4261.0036.70CATOM2253NZLYSA28770.36958.98836.7551.0040.36NATOM2254NGLUA28868.56855.12730.9691.0038.24NATOM2255CAGLUA28867.93455.32029.6691.0039.72CATOM2256CGLUA28866.89254.25429.3301.0041.08CATOM2257OGLUA28866.06754.44028.4281.0039.85OATOM2258CBGLUA28868.97955.35828.5601.0039.55CATOM2259CGGLUA28869.86054.12228.4561.0042.79CATOM2260CDGLUA28870.29353.83527.0101.0044.13CATOM2261OE1GLUA28870.41754.80726.2171.0044.17OATOM2262OE2GLUA28870.52052.64726.6751.0042.82OATOM2263NSERA28966.87853.14830.0651.0041.55NATOM2264CASERA28965.91952.11629.7011.0041.57CATOM2265CSERA28964.53752.19530.3271.0040.41CATOM2266OSERA28964.38352.51031.5071.0041.76OATOM2267CBSERA28966.48750.73830.0041.0041.20CATOM2268OGSERA28965.49449.78229.6811.0046.03OATOM2269NLYSA29063.52851.86129.5341.0038.86NATOM2270CALYSA29062.16851.84830.0231.0040.53CATOM2271CLYSA29061.91150.54830.7761.0040.08CATOM2272OLYSA29061.03750.46331.6131.0041.53OATOM2273CBLYSA29061.19551.96228.8511.0043.06CATOM2274CGLYSA29061.80551.50127.5361.0045.88CATOM2275CDLYSA29061.15852.18926.3361.0048.41CATOM2276CELYSA29062.15052.26325.2021.0051.28CATOM2277NZLYSA29063.44452.80725.7331.0053.00NATOM2278NPHEA29162.69549.53330.4741.0039.87NATOM2279CAPHEA29162.52848.23431.1261.0040.45CATOM2280CPHEA29163.11448.35332.5401.0039.12CATOM2281OPHEA29164.25048.79032.6851.0041.30OATOM2282CBPHEA29163.27147.15930.2961.0039.31CATOM2283CGPHEA29162.90047.16228.8321.0038.38CATOM2284CD1PHEA29161.73046.56828.3961.0040.75CATOM2285CD2PHEA29163.69447.82227.8931.0041.33CATOM2286CE1PHEA29161.35246.63427.0541.0041.56CATOM2287CE2PHEA29163.31447.88926.5481.0038.64CATOM2288CZPHEA29162.15047.29926.1371.0040.41CATOM2289NARGA29262.33748.02733.5791.0034.25NATOM2290CAARGA29262.88348.07334.9431.0034.51CATOM2291CARGA29262.73846.67135.5151.0032.77CATOM2292OARGA29261.75146.00435.2461.0029.04OATOM2293CBARGA29262.09649.02635.8491.0036.30CATOM2294CGARGA29261.89350.44035.2971.0039.49CATOM2295CDARGA29263.14550.97834.6561.0041.52CATOM2296NEARGA29264.30550.80935.5061.0041.74NATOM2297CZARGA29265.53951.11335.1321.0043.04CATOM2298NH1ARGA29265.76951.61333.9061.0041.27NATOM2299NH2ARGA29266.54350.89935.9791.0041.81NATOM2300NLEUA29363.71146.22136.2961.0030.32NATOM2301CALEUA29363.59144.88036.9111.0031.40CATOM2302CLEUA29362.78144.91238.2281.0030.83CATOM2303OLEUA29363.33844.81139.3331.0029.32OATOM2304CBLEUA29364.99444.31037.1701.0030.23CATOM2305CGLEUA29365.78444.05735.8901.0030.94CATOM2306CD1LEUA29367.16043.38936.1981.0032.35CATOM2307CD2LEUA29364.97143.13635.0101.0032.47CATOM2308NTHRA29461.47045.09238.1011.0031.22NATOM2309CATHRA29460.58145.13539.2711.0030.79CATOM2310CTHRA29459.31644.40638.8591.0027.38CATOM2311OTHRA29458.98644.38037.6581.0027.61OATOM2312CBTHRA29460.21746.60539.6331.0033.98CATOM2313OG1THRA29459.42847.15638.5681.0035.88OATOM2314CG2THRA29461.49647.45439.8031.0032.33CATOM2315NTHRA29558.59743.83039.8221.0029.10NATOM2316CATHRA29557.35743.12139.5051.0030.44CATOM2317CTHRA29556.30844.17739.0531.0032.74CATOM2318OTHRA29555.45943.89238.2151.0031.08OATOM2319CBTHRA29556.79542.30440.7231.0033.75CATOM2320OG1THRA29556.52243.17641.8291.0034.41OATOM2321CG2THRA29557.81041.21341.1661.0027.88CATOM2322NLYSA29656.42045.38839.6021.0034.57NATOM2323CALYSA29655.51146.47239.2171.0036.19CATOM2324CLYSA29655.61446.62537.6981.0034.75CATOM2325OLYSA29654.62446.43536.9691.0032.70OATOM2326CBLYSA29655.90347.77939.9201.0037.02CATOM2327CGLYSA29654.90948.96039.7021.0042.72CATOM2328CDLYSA29655.12050.04340.7701.0041.86CATOM2329CELYSA29654.04551.12240.7251.0048.04CATOM2330NZLYSA29654.20252.12441.8471.0048.53NATOM2331NPHEA29756.82446.89937.2081.0035.27NATOM2332CAPHEA29757.00547.08935.7741.0034.42CATOM2333CPHEA29756.65145.85634.9761.0035.51CATOM2334OPHEA29755.92745.95333.9921.0036.39OATOM2335CBPHEA29758.42147.52935.4121.0037.81CATOM2336CGPHEA29758.61547.70633.9231.0037.97CATOM2337CD1PHEA29758.03148.78133.2531.0040.65CATOM2338CD2PHEA29759.29746.73933.1711.0039.24CATOM2339CE1PHEA29758.11048.89431.8561.0038.51CATOM2340CE2PHEA29759.37646.84631.7771.0038.45CATOM2341CZPHEA29758.77147.93731.1231.0039.10CATOM2342NPHEA29857.15844.68535.3671.0033.02NATOM2343CAPHEA29856.79643.49134.6141.0030.06CATOM2344CPHEA29855.28643.27934.5721.0033.42CATOM2345OPHEA29854.77542.68533.6241.0034.10OATOM2346CBPHEA29857.44542.23435.2211.0028.14CATOM2347CGPHEA29858.82641.97234.7031.0029.92CATOM2348CD1PHEA29859.76943.01334.6721.0029.49CATOM2349CD2PHEA29859.19740.69434.2741.0032.76CATOM2350CE1PHEA29861.08142.78934.2241.0029.96CATOM2351CE2PHEA29860.50440.45133.8221.0032.76CATOM2352CZPHEA29861.44741.49133.7941.0030.54CATOM2353NGLYA29954.58943.72635.6171.0036.32NATOM2354CAGLYA29953.13943.59035.6771.0040.46CATOM2355CGLYA29952.39144.26534.5311.0042.69CATOM2356OGLYA29951.26843.87934.1951.0043.32OATOM2357NTHRA30053.01445.27433.9331.0043.13NATOM2358CATHRA30052.41545.98932.8221.0043.17CATOM2359CTHRA30052.31145.08431.6111.0044.09CATOM2360OTHRA30051.45545.30730.7591.0043.97OATOM2361CBTHRA30053.23847.22232.4101.0043.86CATOM2362OG1THRA30054.47946.80231.8211.0044.49OATOM2363CG2THRA30053.51348.10833.6091.0042.85CATOM2364NPHEA30153.15944.05831.5061.0042.79NATOM2365CAPHEA30153.03443.19130.3451.0042.82CATOM2366CPHEA30152.75441.69830.5521.0045.27CATOM2367OPHEA30152.12041.06929.7051.0045.34OATOM2368CBPHEA30154.22843.38829.3861.0042.83CATOM2369CGPHEA30155.56342.99429.9501.0039.71CATOM2370CD1PHEA30156.27543.86530.7691.0040.02CATOM2371CD2PHEA30156.13841.78029.6061.0040.65CATOM2372CE1PHEA30157.54443.54431.2361.0039.74CATOM2373CE2PHEA30157.41941.44330.0701.0038.92CATOM2374CZPHEA30158.12242.32430.8841.0040.54CATOM2375NLEUA30253.18741.11931.6651.0046.34NATOM2376CALEUA30252.93339.69431.8861.0047.31CATOM2377CLEUA30251.79539.48832.8841.0049.46CATOM2378OLEUA30251.42740.40933.5961.0048.56OATOM2379CBLEUA30254.19638.98432.3791.0046.24CATOM2380CGLEUA30255.31738.81631.3541.0046.01CATOM2381CD1LEUA30256.56538.38532.0731.0045.05CATOM2382CD2LEUA30254.93537.81630.2931.0044.52CATOM2383NPROA30351.21838.26132.9311.0051.75NATOM2384CAPROA30350.10737.79733.7851.0051.76CATOM2385CPROA30350.07538.06035.3091.0052.16CATOM2386OPROA30349.83039.17835.7661.0052.37OATOM2387CBPROA30350.03736.30033.4581.0052.46CATOM2388CGPROA30350.35836.27332.0221.0053.97CATOM2389CDPROA30351.55337.21931.9341.0053.46CATOM2390NGLUA30450.31137.00736.0791.0051.38NATOM2391CAGLUA30450.26837.06437.5241.0049.34CATOM2392CGLUA30451.40837.73038.3231.0046.24CATOM2393OGLUA30451.28337.85939.5381.0045.66OATOM2394CBGLUA30450.06835.62938.0301.0052.96CATOM2395CGGLUA30448.64635.09137.8601.0058.63CATOM2396CDGLUA30447.71235.59238.9641.0062.56CATOM2397OE1GLUA30446.55935.10239.0691.0065.41OATOM2398OE2GLUA30448.14036.47939.7371.0065.37OATOM2399NVALA30552.48038.18737.6731.0041.53NATOM2400CAVALA30553.62338.74738.4191.0040.51CATOM2401CVALA30553.39739.80439.5001.0040.68CATOM2402OVALA30553.79439.57840.6541.0038.26OATOM2403CBVALA30554.73639.29537.4861.0038.34CATOM2404CG1VALA30555.96839.63638.3071.0037.60CATOM2405CG2VALA30555.10038.28036.4551.0035.65CATOM2406NALAA30652.80040.95239.1391.0041.04NATOM2407CAALAA30652.54242.03840.0951.0039.81CATOM2408CALAA30651.58341.57741.1911.0040.47CATOM2409OALAA30651.70141.97242.3461.0041.63OATOM2410CBALAA30651.96243.24439.3681.0040.00CATOM2411NLYSA30750.65140.71740.8121.0040.77NATOM2412CALYSA30749.65240.16741.7171.0043.28CATOM2413CLYSA30750.29239.18442.6841.0041.59CATOM2414OLYSA30750.22039.35443.9071.0042.23OATOM2415CBLYSA30748.58039.41540.9131.0045.70CATOM2416CGLYSA30748.66139.65939.4001.0049.68CATOM2417CDLYSA30747.62440.68638.9321.0051.15CATOM2418CELYSA30746.35839.99738.4021.0051.48CATOM2419NZLYSA30745.32041.01038.0521.0052.95NATOM2420NLYSA30850.91638.15142.1201.0039.65NATOM2421CALYSA30851.53837.12042.9281.0038.61CATOM2422CLYSA30852.70837.62843.7851.0036.78CATOM2423OLYSA30852.87437.18344.9121.0034.50OATOM2424CBLYSA30851.96135.96142.0251.0041.97CATOM2425CGLYSA30852.06434.63242.7541.0048.52CATOM2426CDLYSA30852.26833.45941.8091.0050.33CATOM2427CELYSA30852.86432.27642.5731.0053.68CATOM2428NZLYSA30852.05831.91243.7801.0055.31NATOM2429NPHEA30953.50138.56643.2651.0033.40NATOM2430CAPHEA30954.64039.12044.0091.0033.19CATOM2431CPHEA30954.64040.65244.0061.0034.89CATOM2432OPHEA30955.41541.29643.3081.0032.46OATOM2433CBPHEA30955.93638.60243.3941.0030.00CATOM2434CGPHEA30956.03637.12243.3871.0029.40CATOM2435CD1PHEA30956.52436.44144.4921.0030.17CATOM2436CD2PHEA30955.63136.38742.2581.0028.30CATOM2437CE1PHEA30956.61535.05144.4781.0031.47CATOM2438CE2PHEA30955.71835.00542.2351.0028.17CATOM2439CZPHEA30956.22034.32143.3611.0027.75CATOM2440NPROA31053.78741.25444.8411.0035.46NATOM2441CAPROA31053.66442.70144.9391.0034.26CATOM2442CPROA31054.85843.49345.4361.0033.31CATOM2443OPROA31055.43743.16946.4991.0031.12OATOM2444CBPROA31052.48242.88945.9141.0036.60CATOM2445CGPROA31051.75541.59945.8961.0040.32CATOM2446CDPROA31052.84940.57745.7561.0036.81CATOM2447NASNA31155.18044.55944.6921.0032.36NATOM2448CAASNA31156.23245.51945.0701.0035.60CATOM2449CASNA31157.54944.87945.4571.0035.30CATOM2450OASNA31158.12645.16946.5341.0035.48OATOM2451CBASNA31155.74046.40046.2401.0037.73CATOM2452CGASNA31154.41447.12045.9291.0042.62CATOM2453OD1ASNA31154.33647.96245.0251.0042.81OATOM2454ND2ASNA31153.37046.77846.6781.0041.05NATOM2455NMETA31257.99543.97344.5951.0034.53NATOM2456CAMETA31259.24943.26344.7951.0032.63CATOM2457CMETA31260.22443.56143.6601.0030.68CATOM2458OMETA31259.82343.91042.5501.0030.81OATOM2459CBMETA31258.98441.76244.8431.0031.25CATOM2460CGMETA31258.08241.35745.9781.0033.53CATOM2461SDMETA31258.11939.62146.2701.0033.54SATOM2462CEMETA31256.90139.53947.5771.0033.09CATOM2463NLYSA31361.50743.43643.9581.0029.20NATOM2464CALYSA31362.51643.65242.9421.0030.48CATOM2465CLYSA31362.64742.32942.1561.0029.98CATOM2466OLYSA31362.19641.26842.6091.0028.89OATOM2467CBLYSA31363.83044.03743.5941.0033.24CATOM2468CGLYSA31363.70345.15444.6281.0035.74CATOM2469CDLYSA31365.03745.85244.7851.0039.90CATOM2470CELYSA31365.32146.69643.5381.0042.68CATOM2471NZLYSA31366.75346.66943.0901.0046.41NATOM2472NILEA31463.21542.39840.9631.0028.60NATOM2473CAILEA31463.37741.17640.1731.0026.52CATOM2474CILEA31464.83541.02239.7961.0023.53CATOM2475OILEA31465.54742.00339.6101.0023.19OATOM2476CBILEA31462.52141.21938.8491.0024.04CATOM2477CG1ILEA31461.07840.89539.1431.0026.40CATOM2478CG2ILEA31462.99840.17637.8051.0024.56CATOM2479CD1ILEA31460.18240.98037.8751.0026.30CATOM2480NGLNA31565.29539.77339.7041.0023.51NATOM2481CAGLNA31566.66539.53239.2721.0019.49CATOM2482CGLNA31566.58038.56238.0741.0019.49CATOM2483OGLNA31565.69937.71038.0351.0018.23OATOM2484CBGLNA31567.49538.83540.3651.0024.40CATOM2485CGGLNA31567.74439.58941.6531.0026.52CATOM2486CDGLNA31568.85038.93342.4441.0027.12CATOM2487OE1GLNA31569.37837.87542.0541.0025.45OATOM2488NE2GLNA31569.21739.55643.5601.0026.68NATOM2489NILEA31667.47838.73637.0971.0022.89NATOM2490CAILEA31667.50937.89435.8971.0019.87CATOM2491CILEA31668.88037.25435.8921.0023.17CATOM2492OILEA31669.88637.96135.8351.0023.46OATOM2493CBILEA31667.32638.74234.6011.0024.31CATOM2494CG1ILEA31665.89139.29234.5301.0024.19CATOM2495CG2ILEA31667.59437.89233.3721.0023.47CATOM2496CD1ILEA31665.56739.91833.2151.0029.77CATOM2497NHISA31768.91835.92135.9751.0019.09NATOM2498CAHISA31770.17235.17735.9551.0016.10CATOM2499CHISA31770.35834.55634.5451.0018.62CATOM2500OHISA31769.50333.83934.0491.0017.53OATOM2501CBHISA31770.12034.05437.0241.0014.39CATOM2502CGHISA31770.06734.53938.4511.0021.51CATOM2503ND1HISA31770.30433.69639.5221.0020.77NATOM2504CD2HISA31769.79135.75738.9891.0022.21CATOM2505CE1HISA31770.18334.37240.6531.0018.38CATOM2506NE2HISA31769.87235.62540.3611.0023.87NATOM2507NVALA31871.51334.81433.9481.0018.27NATOM2508CAVALA31871.86434.36332.6201.0017.81CATOM2509CVALA31872.97533.34332.7921.0019.49CATOM2510OVALA31873.95133.60333.5291.0019.00OATOM2511CBVALA31872.41435.55631.7881.0020.65CATOM2512CG1VALA31872.83335.06330.3961.0026.11CATOM2513CG2VALA31871.33836.63531.6601.0023.64CATOM2514NSERA31972.84332.20732.1211.0018.81NATOM2515CASERA31973.88731.19432.2341.0022.45CATOM2516CSERA31973.92730.23631.0521.0022.89CATOM2517OSERA31972.99730.14630.2551.0022.67OATOM2518CBSERA31973.71530.40733.5671.0025.56CATOM2519OGSERA31972.46629.70033.6531.0028.71OATOM2520NALAA32075.05529.53330.9291.0026.30NATOM2521CAALAA32075.21628.54629.8691.0027.76CATOM2522CALAA32075.24627.15530.5381.0028.34CATOM2523OALAA32076.15126.85231.3141.0030.21OATOM2524CBALAA32076.54728.82729.0971.0026.62CATOM2525NSERA32174.24026.32730.2861.0026.00NATOM2526CASERA32174.26924.99630.8721.0030.50CATOM2527CSERA32174.93323.96329.9481.0032.26CATOM2528OSERA32175.07722.77930.3151.0034.46OATOM2529CBSERA32172.86224.55031.3071.0030.34CATOM2530OGSERA32171.95324.47730.2291.0030.32OATOM2531NTHRA32275.31624.40528.7491.0033.10NATOM2532CATHRA32276.04323.58727.7891.0032.40CATOM2533CTHRA32277.13924.46127.1661.0029.30CATOM2534OTHRA32276.95225.64126.9091.0025.36OATOM2535CBTHRA32275.15322.99926.6571.0037.96CATOM2536OG1THRA32274.68324.05225.8071.0039.60OATOM2537CG2THRA32273.97622.21427.2491.0039.13CATOM2538NPROA32378.30823.87726.9091.0029.98NATOM2539CAPROA32379.42824.62326.3241.0028.92CATOM2540CPROA32379.09725.13624.9371.0028.68CATOM2541OPROA32378.57724.40224.1051.0027.85OATOM2542CBPROA32380.55423.59526.3371.0030.45CATOM2543CGPROA32379.80622.33926.0001.0036.44CATOM2544CDPROA32378.57922.43526.9191.0032.60CATOM2545NPROA32479.36526.42724.6811.0028.46NATOM2546CAPROA32479.06426.99823.3681.0029.04CATOM2547CPROA32479.97226.47522.2491.0030.07CATOM2548OPROA32481.19726.41222.4091.0030.23OATOM2549CBPROA32479.18328.50323.6091.0028.06CATOM2550CGPROA32480.28928.58524.6601.0029.33CATOM2551CDPROA32480.00127.41125.5841.0028.96CATOM2552NAHISA32579.37426.09821.1210.5027.02NATOM2553NBHISA32579.33626.10221.1370.5028.68NATOM2554CAAHISA32580.15525.57820.0000.5026.87CATOM2555CABHISA32580.02025.56719.9620.5030.05CATOM2556CAHISA32580.55226.66218.9940.5024.15CATOM2557CBHISA32580.52526.66519.0190.5027.92CATOM2558OAHISA32579.85827.66918.8370.5024.29OATOM2559OBHISA32579.97527.76618.9670.5028.29OATOM2560CBAHISA32579.36624.50919.2230.5030.59CATOM2561CBBHISA32579.06624.67619.1400.5033.50CATOM2562CGAHISA32578.62723.52620.0790.5032.95CATOM2563CGBHISA32578.43223.55719.9110.5037.48CATOM2564ND1AHISA32579.13123.02421.2590.5032.44NATOM2565ND1BHISA32577.51223.76720.9170.5038.53NATOM2566CD2AHISA32577.43722.90619.8870.5034.27CATOM2567CD2BHISA32578.55022.21319.7880.5039.34CATOM2568CE1AHISA32578.28822.13821.7570.5034.55CATOM2569CE1BHISA32577.09122.60321.3790.5040.83CATOM2570NE2AHISA32577.25022.04820.9420.5036.30NATOM2571NE2BHISA32577.70621.64320.7100.5041.15NATOM2572NALEUA32681.65026.41518.2820.5020.47NATOM2573NBLEUA32681.54926.33118.2410.5025.62NATOM2574CAALEUA32682.13527.29817.2360.5021.63CATOM2575CABLEUA32682.10327.22617.2440.5025.44CATOM2576CALEUA32682.49726.46116.0010.5021.24CATOM2577CBLEUA32682.46926.42115.9970.5023.88CATOM2578OALEUA32683.09125.38616.1300.5022.62OATOM2579OBLEUA32683.05025.33616.1080.5024.48OATOM2580CBALEUA32683.37128.07217.7220.5022.23CATOM2581CBBLEUA32683.34427.93817.7890.5028.35CATOM2582CGALEUA32684.04329.12516.8360.5022.02CATOM2583CGBLEUA32683.05729.27418.4630.5030.00CATOM2584CD1ALEUA32684.83630.03917.7570.5021.82CATOM2585CD1BLEUA32684.08929.55419.5370.5033.17CATOM2586CD2ALEUA32684.94328.51215.7740.5024.66CATOM2587CD2BLEUA32683.04630.37317.3980.5030.86CATOM2588NSERA32782.08326.91014.8191.0021.24NATOM2589CASERA32782.45726.20913.5841.0020.71CATOM2590CSERA32783.26927.16012.6891.0020.90CATOM2591OSERA32783.18728.42812.7831.0020.02OATOM2592CBSERA32781.25525.60412.8141.0023.19CATOM2593OGSERA32780.48426.60712.2551.0029.56OATOM2594NVALA32884.15626.57711.8861.0020.65NATOM2595CAVALA32884.97127.38010.9591.0022.43CATOM2596CVALA32884.65026.9219.5351.0025.95CATOM2597OVALA32884.69325.7349.2511.0024.62OATOM2598CBVALA32886.49227.16011.1501.0023.21CATOM2599CG1VALA32887.28628.20010.3641.0024.86CATOM2600CG2VALA32886.82427.21612.5821.0024.31CATOM2601NGLNA32984.32027.8818.6771.0027.90NATOM2602CAGLNA32984.00827.6407.2621.0031.26CATOM2603CGLNA32984.81828.6726.4961.0029.53CATOM2604OGLNA32985.31829.6247.0791.0029.67OATOM2605CBGLNA32982.53227.9526.9611.0032.70CATOM2606CGGLNA32981.50027.1367.6861.0040.54CATOM2607CDGLNA32981.30627.5119.1581.0041.37CATOM2608OE1GLNA32981.20426.6249.9921.0042.86OATOM2609NE2GLNA32981.23328.8279.4771.0041.42NATOM2610NPROA33084.90428.5355.1521.0033.50NATOM2611CAPROA33085.66029.5064.3541.0033.92CATOM2612CPROA33085.12030.8974.5751.0033.13CATOM2613OPROA33085.83031.8644.3841.0035.50OATOM2614CBPROA33085.45329.0072.9281.0036.48CATOM2615CGPROA33085.49027.5073.1351.0035.94CATOM2616CDPROA33084.55027.3624.3301.0032.54CATOM2617NTHRA33183.87330.9755.0391.0036.17NATOM2618CATHRA33183.20032.2485.3251.0040.14CATOM2619CTHRA33183.71232.9456.6071.0041.02CATOM2620OTHRA33183.54034.1646.7941.0043.07OATOM2621CBTHRA33181.65932.0365.4591.0041.98CATOM2622OG1THRA33180.97433.2585.1531.0046.94OATOM2623CG2THRA33181.27131.6406.9021.0045.95CATOM2624NGLYA33284.34432.1787.4911.0036.57NATOM2625CAGLYA33284.82932.7558.7341.0036.42CATOM2626CGLYA33284.41631.8729.9071.0035.91CATOM2627OGLYA33283.95430.7369.7011.0036.09OATOM2628NLEUA33384.59132.37111.1271.0033.41NATOM2629CALEUA33384.22531.61312.3141.0031.55CATOM2630CLEUA33382.83531.99712.7621.0031.35CATOM2631OLEUA33382.46433.17812.7731.0028.77OATOM2632CBLEUA33385.18731.87813.4711.0033.13CATOM2633CGLEUA33386.67431.56813.3861.0038.69CATOM2634CD1LEUA33387.31131.76414.7711.0040.78CATOM2635CD2LEUA33386.87030.12812.9571.0042.94CATOM2636NTHRA33482.05930.98813.1301.0027.54NATOM2637CATHRA33480.70131.18813.5911.0027.09CATOM2638CTHRA33480.53830.59014.9701.0027.41CATOM2639OTHRA33480.98429.47815.2281.0025.09OATOM2640CBTHRA33479.76230.53512.6421.0029.52CATOM2641OG1THRA33479.99031.09411.3461.0034.40OATOM2642CG2THRA33478.35530.77513.0511.0030.58CATOM2643NPHEA33579.86731.33515.8451.0023.79NATOM2644CAPHEA33579.68130.95217.2341.0023.65CATOM2645CPHEA33578.18930.70917.4381.0022.59CATOM2646OPHEA33577.37531.47916.9381.0022.87OATOM2647CBPHEA33580.16932.15918.0841.0023.69CATOM2648CGPHEA33580.19331.91519.5311.0028.04CATOM2649CD1PHEA33581.06630.97120.0651.0034.71CATOM2650CD2PHEA33579.43732.69720.3871.0029.22CATOM2651CE1PHEA33581.19730.81521.4501.0035.43CATOM2652CE2PHEA33579.55032.55521.7701.0033.78CATOM2653CZPHEA33580.43231.61322.3041.0034.26CATOM2654NTYRA33677.81029.65218.1521.0022.23NATOM2655CATYRA33676.38729.34118.3471.0024.31CATOM2656CTYRA33676.04129.39319.8261.0026.09CATOM2657OTYRA33675.84728.36220.4431.0027.05OATOM2658CBTYRA33676.08627.93717.8191.0026.23CATOM2659CGTYRA33676.48727.76216.3961.0026.77CATOM2660CD1TYRA33675.65628.15415.3501.0027.06CATOM2661CD2TYRA33677.72827.24016.0891.0027.25CATOM2662CE1TYRA33676.08228.02114.0241.0031.18CATOM2663CE2TYRA33678.15327.10814.7961.0027.24CATOM2664CZTYRA33677.32927.50213.7721.0029.22CATOM2665OHTYRA33677.83527.39612.5131.0034.11OATOM2666NPROA33775.90330.59920.3871.0025.03NATOM2667CAPROA33775.58030.70421.8161.0027.13CATOM2668CPROA33774.17530.26822.1881.0024.60CATOM2669OPROA33773.22330.52221.4381.0025.96OATOM2670CBPROA33775.86332.18222.1341.0025.32CATOM2671CGPROA33775.58532.89420.8381.0025.23CATOM2672CDPROA33776.15631.92419.7861.0025.35CATOM2673NALAA33874.07729.50323.2761.0025.04NATOM2674CAALAA33872.79029.04923.8271.0027.02CATOM2675CALAA33872.83829.38125.3371.0025.47CATOM2676OALAA33873.76128.90726.0821.0025.07OATOM2677CBALAA33872.60527.56023.5961.0029.61CATOM2678NVALA33971.88030.20225.7881.0023.49NATOM2679CAVALA33971.85030.63827.1851.0024.36CATOM2680CVALA33970.51830.41727.8431.0022.40CATOM2681OVALA33969.49030.37527.1741.0020.04OATOM2682CBVALA33972.29132.14827.3291.0031.73CATOM2683CG1VALA33971.49033.02926.4791.0030.59CATOM2684CG2VALA33972.13032.61228.7221.0035.06CATOM2685NASPA34070.55130.16329.1511.0019.50NATOM2686CAASPA34069.33929.99129.9601.0020.79CATOM2687CASPA34069.12031.34930.6111.0018.51CATOM2688OASPA34070.08031.97331.0601.0018.68OATOM2689CBASPA34069.58328.95431.0701.0019.34CATOM2690CGASPA34069.96327.58630.4991.0030.04CATOM2691OD1ASPA34069.35627.22729.4661.0025.36OATOM2692OD2ASPA34070.85726.89831.0841.0030.87OATOM2693NVALA34167.87831.82630.6451.0019.16NATOM2694CAVALA34167.61733.11631.2881.0017.44CATOM2695CVALA34166.45332.86232.2411.0017.73CATOM2696OVALA34165.37232.46731.8081.0017.27OATOM2697CBVALA34167.16134.19530.2621.0019.03CATOM2698CG1VALA34166.92635.52130.9761.0020.90CATOM2699CG2VALA34168.23934.39529.1671.0020.47OATOM2700NGLNA34266.67033.10033.5251.0016.40NATOM2701CAGLNA34265.63532.84434.5251.0016.88CATOM2702CGLNA34265.37834.10235.3581.0018.10CATOM2703OGLNA34266.29834.75735.8191.0016.79OATOM2704CBGLNA34266.08131.69335.4501.0016.56CATOM2705CGGLNA34264.97531.15636.3301.0019.69CATOM2706CDGLNA34265.36029.82836.9871.0019.50CATOM2707OE1GLNA34266.51729.37536.8841.0020.28OATOM2708NE2GLNA34264.38929.18237.6391.0020.81NATOM2709NALAA34364.10634.42235.5581.0017.71NATOM2710CAALAA34363.72235.61236.2781.0018.52CATOM2711CALAA34363.23635.24137.6701.0016.11CATOM2712OALAA34362.52934.24737.8191.0020.52OATOM2713CBALAA34362.58636.28535.5101.0022.15CATOM2714NPHEA34463.63136.01138.6781.0017.89NATOM2715CAPHEA34463.20535.74540.0481.0018.07CATOM2716CPHEA34462.63936.98740.7511.0018.31CATOM2717OPHEA34463.09238.09540.4941.0022.64OATOM2718CBPHEA34464.40835.29040.9491.0018.87CATOM2719CGPHEA34465.12834.07040.4501.0015.76CATOM2720CD1PHEA34466.17234.18939.5431.0018.56CATOM2721CD2PHEA34464.75632.78740.9101.0015.58CATOM2722CE1PHEA34466.86133.05239.0771.0019.56CATOM2723CE2PHEA34465.46131.61440.4291.0014.75CATOM2724CZPHEA34466.49831.77539.5201.0017.68CATOM2725NALAA34561.65836.78941.6261.0020.02NATOM2726CAALAA34561.21837.89942.4681.0022.22CATOM2727CALAA34562.03837.79243.7941.0022.53CATOM2728OALAA34562.27236.67244.2941.0022.99OATOM2729CBALAA34559.74937.78242.7961.0024.65CATOM2730NVALA34662.47938.92544.3521.0022.02NATOM2731CAVALA34663.24438.92645.6281.0023.78CATOM2732CVALA34662.21238.95346.7961.0023.72CATOM2733OVALA34661.48939.94446.9841.0023.56OATOM2734CBVALA34664.20140.16445.7031.0024.25CATOM2735CG1VALA34665.05440.15147.0101.0023.26CATOM2736CG2VALA34665.13240.16444.5081.0021.14CATOM2737NLEUA34762.15737.88447.5831.0021.35NATOM2738CALEUA34761.15637.77248.6611.0021.40CATOM2739CLEUA34761.44538.58849.9021.0024.60CATOM2740OLEUA34762.55239.11150.0691.0024.52OATOM2741CBLEUA34761.00236.30349.0871.0023.44CATOM2742CGLEUA34760.38835.44747.9941.0021.52CATOM2743CD1LEUA34760.39233.95048.3801.0024.41CATOM2744CD2LEUA34758.98135.97047.7661.0025.57CATOM2745NPROA34860.43038.71950.8021.0024.16NATOM2746CAPROA34860.63139.48452.0411.0026.26CATOM2747CPROA34861.87839.03552.8551.0027.17CATOM2748OPROA34862.49539.88453.5281.0027.43OATOM2749CBPROA34859.30339.29552.7941.0027.70CATOM2750CGPROA34858.25139.23051.6151.0028.56CATOM2751CDPROA34859.01238.34350.6031.0025.60CATOM2752NASNA34962.24537.73752.8101.0025.56NATOM2753CAASNA34963.43637.25453.5361.0025.46CATOM2754CASNA34964.69437.15752.6301.0024.57CATOM2755OASNA34965.70436.56853.0281.0024.12OATOM2756CBASNA34963.16535.93354.2541.0022.97CATOM2757CGASNA34962.97334.79053.3251.0021.72CATOM2758OD1ASNA34962.92234.95952.1051.0022.91OATOM2759ND2ASNA34962.84233.58353.9001.0026.22NATOM2760NSERA35064.62337.81751.4581.0023.66NATOM2761CASERA35065.69837.93450.4461.0022.16CATOM2762CSERA35065.90936.68049.5701.0020.19CATOM2763OSERA35066.76736.66148.6601.0020.19OATOM2764CBSERA35067.03938.32251.0521.0025.96CATOM2765OGSERA35067.66537.20851.6681.0024.38OATOM2766NALAA35165.16735.63049.8661.0017.57NATOM2767CAALAA35165.24234.40149.0461.0017.43CATOM2768CALAA35164.69434.71047.6281.0019.61CATOM2769OALAA35163.83935.60847.4471.0019.94OATOM2770CBALAA35164.39233.34249.6521.0017.88CATOM2771NLEUA35265.12733.91846.6521.0017.19NATOM2772CALEUA35264.68434.14945.2491.0018.33CATOM2773CLEUA35263.58233.18244.8141.0017.86CATOM2774OLEUA35263.71731.96344.8811.0019.93OATOM2775CBLEUA35265.90034.05044.2901.0016.44CATOM2776CGLEUA35267.07534.95744.6401.0014.50CATOM2777CD1LEUA35268.21534.68843.7231.0016.06CATOM2778CD2LEUA35266.63636.48244.5801.0020.65CATOM2779NALAA35362.46933.75644.3701.0017.57NATOM2780CAALAA35361.31332.98343.9411.0021.06CATOM2781CALAA35361.30532.96742.4121.0020.69CATOM2782OALAA35361.23934.01541.8061.0020.98OATOM2783CBALAA35360.00933.64744.4651.0018.87CATOM2784NSERA35461.39831.78441.8131.0019.36NATOM2785CASERA35461.41631.69240.3561.0019.68CATOM2786CSERA35460.08432.12839.6961.0019.49CATOM2787OSERA35459.03231.69440.1211.0022.59OATOM2788CBSERA35461.69030.25639.9121.0023.90CATOM2789OGSERA35461.78230.22838.4791.0023.89OATOM2790NLEUA35560.16432.99338.6701.0020.43NATOM2791CALEUA35558.96033.44537.9281.0020.07CATOM2792CLEUA35558.82232.66536.6261.0021.96CATOM2793OLEUA35557.73932.15636.3031.0024.19OATOM2794CBLEUA35559.04334.94537.6381.0021.68CATOM2795CGLEUA35559.20635.85838.8491.0022.80CATOM2796CD1LEUA35559.47837.26038.3831.0023.43CATOM2797CD2LEUA35557.92135.79839.7491.0025.12CATOM2798NPHEA35659.89832.59235.8411.0019.57NATOM2799CAPHEA35659.89931.84034.5811.0020.80CATOM2800CPHEA35661.34431.56734.1381.0018.63CATOM2801OPHEA35662.29232.20734.5931.0019.60OATOM2802CBPHEA35659.12632.61433.4571.0020.93CATOM2803CGPHEA35659.67334.00933.1611.0023.84CATOM2804CD1PHEA35660.85834.18232.4751.0026.64CATOM2805CD2PHEA35658.98935.14033.6041.0024.03CATOM2806CE1PHEA35661.37535.45532.2291.0027.67CATOM2807CE2PHEA35659.48936.42133.3701.0025.15CATOM2808CZPHEA35660.67136.58932.6951.0026.42CATOM2809NLEUA35761.47830.59233.2511.0019.79NATOM2810CALEUA35762.75230.16932.6751.0021.15CATOM2811CLEUA35762.61530.04631.1501.0021.32CATOM2812OLEUA35761.77629.28930.6541.0020.75OATOM2813CBLEUA35763.13328.79133.2421.0022.34CATOM2814CGLEUA35764.32528.06632.6051.0027.32CATOM2815CD1LEUA35765.62228.73532.9991.0025.79CATOM2816CD2LEUA35764.34026.58633.1041.0029.65CATOM2817NILEA35863.45730.77030.4091.0021.21NATOM2818CAILEA35863.43130.67028.9341.0021.64CATOM2819CILEA35864.80430.27128.4151.0021.87CATOM2820OILEA35865.80730.38629.1261.0022.77OATOM2821CBILEA35863.07332.03028.2641.0020.59CATOM2822CG1ILEA35864.15833.08928.5051.0024.28CATOM2823CG2ILEA35861.79432.53028.8491.0019.95CATOM2824CD1ILEA35863.87934.38927.7231.0026.29CATOM2825NGLYA35964.83529.81627.1681.0020.62NATOM2826CAGLYA35966.08629.45526.5001.0020.37CATOM2827CGLYA35966.26230.50125.4011.0023.47CATOM2828OGLYA35965.26530.93824.7881.0022.13OATOM2829NMETA36067.49730.92025.1681.0020.48NATOM2830CAMETA36067.76531.93724.1691.0024.38CATOM2831CMETA36068.94331.53723.3301.0025.27CATOM2832OMETA36069.97331.11223.8661.0025.29OATOM2833CBMETA36068.06633.29124.8351.0024.51CATOM2834CGMETA36068.49934.36323.9051.0024.56CATOM2835SDMETA36068.53935.98024.8001.0034.34SATOM2836CEMETA36069.92835.75025.9431.0030.52CATOM2837NHISA36168.79731.60522.0051.0022.34NATOM2838CAHISA36169.96231.26621.1981.0023.47CATOM2839CHISA36170.03032.05919.9151.0020.15CATOM2840OHISA36169.05332.66719.4911.0019.89OATOM2841CBHISA36170.03729.77220.8641.0026.13CATOM2842CGHISA36169.02429.33419.8601.0028.93CATOM2843ND1HISA36167.69529.16520.1741.0033.10NATOM2844CD2HISA36169.14029.05518.5421.0032.51CATOM2845CE1HISA36167.02928.80219.0861.0033.63CATOM2846NE2HISA36167.88428.73218.0831.0034.52NATOM2847NTHRA36271.21332.04919.3221.0019.48NATOM2848CATHRA36271.42832.77618.0901.0019.69CATOM2849CTHRA36272.73132.29917.4431.0020.11CATOM2850OTHRA36273.40631.32817.9471.0021.70OATOM2851CBTHRA36271.48034.32318.4041.0022.62CATOM2852OG1THRA36271.37135.05617.1751.0027.64OATOM2853CG2THRA36272.81534.70319.0951.0026.71CATOM2854NATHRA36373.06432.89816.3050.5018.46NATOM2855NBTHRA36373.06032.90116.3080.5019.24NATOM2856CAATHRA36374.30332.60515.6080.5019.66CATOM2857CABTHRA36374.29732.62015.6060.5021.08CATOM2858CATHRA36375.08433.91415.6910.5022.23CATOM2859CBTHRA36375.08533.92315.6830.5022.94CATOM2860OATHRA36374.49634.99815.6960.5023.41OATOM2861OBTHRA36374.50835.01215.6660.5024.03OATOM2862CBATHRA36374.07132.24514.1200.5021.19CATOM2863CBBTHRA36374.06332.26914.1250.5023.38CATOM2864OG1ATHRA36373.18431.12614.0420.5022.34OATOM2865OG1BTHRA36373.04533.12113.5850.5023.47OATOM2866CG2ATHRA36375.38831.88013.4330.5016.25CATOM2867CG2BTHRA36373.64730.82513.9860.5023.11CATOM2868NGLYA36476.39633.82015.7811.0021.74NATOM2869CAGLYA36477.18635.03215.8511.0022.62CATOM2870CGLYA36478.45234.89215.0441.0024.44CATOM2871OGLYA36478.95633.78714.8431.0025.40OATOM2872NSERA36578.94536.00314.5271.0023.38NATOM2873CASERA36580.19235.94213.7921.0022.86CATOM2874CSERA36581.29036.24114.8021.0024.57CATOM2875OSERA36581.11237.08215.7031.0023.77OATOM2876CBSERA36580.21837.00312.6891.0024.97CATOM2877OGSERA36579.97738.29613.2241.0028.94OATOM2878NMETA36682.42635.56514.6591.0021.45NATOM2879CAMETA36683.55835.81415.5411.0023.58CATOM2880CMETA36684.71136.28714.6631.0022.96CATOM2881OMETA36685.32035.48913.9401.0024.69OATOM2882CBMETA36683.95834.52016.2511.0022.84CATOM2883CGMETA36685.05734.72817.2711.0026.18CATOM2884SDMETA36684.54035.60118.7411.0030.64SATOM2885CEMETA36683.53634.34819.6081.0029.02CATOM2886NGLUA36784.98937.58214.6841.0022.33NATOM2887CAGLUA36786.10138.13613.8961.0022.19CATOM2888CGLUA36787.35837.95614.7381.0022.50CATOM2889OGLUA36787.38238.40715.8631.0024.63OATOM2890CBGLUA36785.89539.62613.6601.0025.42CATOM2891CGGLUA36784.69439.93412.7581.0037.35CATOM2892CDGLUA36784.34041.41812.7521.0043.75CATOM2893OE1GLUA36783.56641.86513.6421.0044.58OATOM2894OE2GLUA36784.85242.14211.8601.0047.82OATOM2895NVALA36888.39037.32114.1921.0025.43NATOM2896CAVALA36889.63737.03214.9211.0025.46CATOM2897CVALA36890.82637.81114.3251.0031.07CATOM2898OVALA36891.00737.85313.0871.0033.39OATOM2899CBVALA36889.92235.49714.8461.0027.14CATOM2900CG1VALA36891.26435.14615.4851.0027.94CATOM2901CG2VALA36888.84334.75215.5731.0027.31CATOM2902NSERA36991.63538.41315.1981.0029.11NATOM2903CASERA36992.79939.17614.7771.0029.86CATOM2904CSERA36994.05738.86715.5981.0029.30CATOM2905OSERA36994.04038.01316.4861.0022.65OATOM2906CBSERA36992.47840.67414.8681.0034.13CATOM2907OGSERA36993.67041.42414.9681.0042.36OATOM2908NALAA37095.15739.57115.2851.0034.69NATOM2909CAALAA37096.45639.40516.0001.0036.73CATOM2910CALAA37096.83140.72516.6421.0038.68CATOM2911OALAA37096.54741.80416.1061.0039.76OATOM2912CBALAA37097.58238.98115.0441.0032.66CATOM2913NGLUA37197.50840.63817.7711.0038.55NATOM2914CAGLUA37197.87541.83318.4851.0039.00CATOM2915CGLUA37198.88541.42419.5281.0038.33CATOM2916OGLUA37198.55140.72920.4851.0039.69OATOM2917CBGLUA37196.62642.42119.1621.0043.20CATOM2918CGGLUA37196.33343.85118.7981.0048.61CATOM2919CDGLUA37197.05744.81619.7001.0051.48CATOM2920OE1GLUA37196.48745.19020.7581.0048.95OATOM2921OE2GLUA37198.19645.17519.3441.0050.85OATOM2922NSERA372100.13241.82119.3141.0035.49NATOM2923CASERA372101.19041.51120.2481.0031.31CATOM2924CSERA372101.32340.05220.6411.0027.35CATOM2925OSERA372101.29139.76621.8461.0027.78OATOM2926CBSERA372101.04442.34721.5411.0037.05CATOM2927OGSERA372101.10143.74721.2811.0043.04OATOM2928NAASNA373101.49039.16619.6510.5023.03NATOM2929NBASNA373101.46239.12819.6840.5021.92NATOM2930CAAASNA373101.66337.73619.8850.5020.77CATOM2931CABASNA373101.63837.72220.0520.5018.76CATOM2932CAASNA373100.50837.08420.6560.5021.04CATOM2933CBASNA373100.43537.08320.7420.5019.62CATOM2934OAASNA373100.69836.15821.4470.5021.27OATOM2935OBASNA373100.56636.14021.5320.5018.66OATOM2936CBAASNA373103.03137.47220.5660.5021.57CATOM2937CBBASNA373102.87437.56720.9540.5017.20CATOM2938CGAASNA373103.29338.38121.7340.5018.77CATOM2939CGBASNA373104.17137.69220.1790.5014.45CATOM2940OD1AASNA373104.36339.01621.8520.5027.43OATOM2941OD1BASNA373105.26237.51820.7350.5023.77OATOM2942ND2AASNA373102.33838.45822.6070.5024.72NATOM2943ND2BASNA373104.06437.99518.8830.5018.75NATOM2944NAARGA37499.29837.59320.4450.5021.03NATOM2945NBARGA37499.25237.61720.4970.5020.06NATOM2946CAAARGA37498.12137.00221.0690.5021.58CATOM2947CABARGA37498.08236.99821.0790.5021.50CATOM2948CAARGA37497.01137.02920.0220.5020.79CATOM2949CBARGA37496.99137.04620.0340.5020.80CATOM2950OAARGA37497.11837.77119.0360.5021.98OATOM2951OBARGA37497.08937.80719.0600.5022.34OATOM2952CBAARGA37497.71337.76622.3450.5025.48CATOM2953CBBARGA37497.66337.70222.3800.5025.76CATOM2954CGAARGA37497.01339.11922.2000.5029.02CATOM2955CGBARGA37497.25139.14922.2710.5030.43CATOM2956CDAARGA37496.94939.81723.6080.5030.65CATOM2957CDBARGA37497.48139.90723.6150.5030.79CATOM2958NEAARGA37496.04540.97323.6930.5034.22NATOM2959NEBARGA37498.90840.08223.8920.5032.09NATOM2960CZAARGA37496.30542.19723.2380.5034.15CATOM2961CZBARGA37499.40940.77824.9100.5033.07CATOM2962NH1AARGA37497.44642.47922.6370.5035.34NATOM2963NH1BARGA37498.60441.38425.7730.5035.29NATOM2964NH2AARGA37495.42443.16323.4200.5037.32NATOM2965NH2BARGA374100.71840.86625.0760.5031.01NATOM2966NLEUA37595.99336.19020.2131.0020.17NATOM2967CALEUA37594.83636.13219.3001.0020.90CATOM2968CLEUA37593.72636.90020.0151.0018.90CATOM2969OLEUA37593.48836.67921.2001.0018.99OATOM2970CBLEUA37594.34934.67119.1491.0023.32CATOM2971CGLEUA37593.36034.53917.9961.0033.86CATOM2972CD1LEUA37594.11334.78216.6771.0037.49CATOM2973CD2LEUA37592.70733.12218.0171.0036.55CATOM2974NVALA37693.02637.78419.3181.0017.78NATOM2975CAVALA37691.94938.53519.9771.0017.47CATOM2976CVALA37690.67338.35219.1221.0022.75CATOM2977OVALA37690.74738.09617.9091.0020.82OATOM2978CBVALA37692.33840.04420.1161.0023.91CATOM2979CG1VALA37693.60440.14220.9581.0023.51CATOM2980CG2VALA37692.58940.66118.8001.0023.25CATOM2981NGLYA37789.51638.46719.7701.0020.65NATOM2982CAGLYA37788.26338.29019.0481.0020.98CATOM2983CGLYA37787.19639.35319.2991.0020.73CATOM2984OGLYA37787.26340.09420.2921.0021.26OATOM2985NGLUA37886.19239.38818.4231.0019.36NATOM2986CAGLUA37885.05740.31318.5831.0019.80CATOM2987CGLUA37883.80439.53618.0861.0019.25CATOM2988OGLUA37883.76439.09516.9491.0020.85OATOM2989CBGLUA37885.31241.60017.7531.0020.50CATOM2990CGGLUA37884.15642.57117.7021.0026.76CATOM2991CDGLUA37884.02243.39918.9431.0032.24CATOM2992OE1GLUA37883.02044.15319.0381.0038.76OATOM2993OE2GLUA37884.93643.32519.8151.0035.19OATOM2994NLEUA37982.80939.38218.9711.0018.13NATOM2995CALEUA37981.56838.63318.6941.0018.29CATOM2996CLEUA37980.43039.59618.3611.0020.04CATOM2997OLEUA37980.24740.58419.0871.0018.78OATOM2998CBLEUA37981.17437.86919.9771.0017.99CATOM2999CGLEUA37980.30636.60719.9721.0029.39CATOM3000CD1LEUA37979.40236.56821.1811.0023.12CATOM3001CD2LEUA37979.63136.41418.6541.0023.47CATOM3002NLYSA38079.69839.32317.2601.0020.00NATOM3003CALYSA38078.52640.10616.8741.0020.24CATOM3004CLYSA38077.41739.13416.6531.0019.64CATOM3005OLYSA38077.62938.08816.0201.0023.51OATOM3006CBLYSA38078.73240.89415.5701.0026.90CATOM3007CGLYSA38079.75041.97915.7001.0032.63CATOM3008CDLYSA38081.13641.37615.9141.0036.57CATOM3009CELYSA38081.23740.01815.2161.0037.63CATOM3010NZLYSA38082.40239.80714.4501.0033.27NATOM3011NLEUA38176.23639.51717.1031.0018.63NATOM3012CALEUA38175.09938.60717.0981.0019.16CATOM3013CLEUA38173.97238.78916.1051.0021.37CATOM3014OLEUA38173.65639.89915.7141.0020.52OATOM3015CBLEUA38174.47638.64418.4641.0021.98CATOM3016CGLEUA38175.38938.38219.6581.0024.30CATOM3017CD1LEUA38174.62838.64420.9651.0026.03CATOM3018CD2LEUA38175.90236.94619.5811.0023.45CATOM3019NASPA38273.35737.68715.7151.0017.92NATOM3020CAASPA38272.16737.79214.8561.0020.04CATOM3021CASPA38270.91837.92615.7571.0021.87CATOM3022OASPA38271.00238.20116.9591.0022.38OATOM3023CBASPA38272.01336.58913.9171.0023.47CATOM3024CGASPA38273.12336.50212.8671.0029.81CATOM3025OD1ASPA38273.66037.55312.4451.0036.54OATOM3026OD2ASPA38273.46035.38312.4231.0031.44OATOM3027NARGA38369.72537.74715.1801.0024.00NATOM3028CAARGA38368.48237.88415.9281.0023.87CATOM3029CARGA38368.39836.89417.0941.0023.10CATOM3030OARGA38368.84035.75216.9521.0024.99OATOM3031CBARGA38367.30937.64814.9621.0028.83CATOM3032CGARGA38366.04738.25915.3971.0034.77CATOM3033CDARGA38365.02838.20314.2491.0039.89CATOM3034NEARGA38363.92437.29314.5571.0050.79NATOM3035CZARGA38363.61936.20113.8541.0052.55CATOM3036NH1ARGA38364.33335.86412.7811.0054.41NATOM3037NH2ARGA38362.60535.43714.2381.0054.44NATOM3038NLEUA38467.84637.33718.2281.0023.74NATOM3039CALEUA38467.73236.49119.4101.0023.25CATOM3040CLEUA38466.47035.64919.3401.0023.45CATOM3041OLEUA38465.35836.17419.2471.0025.21OATOM3042CBLEUA38467.76837.34920.7051.0022.74CATOM3043CGLEUA38468.96338.29920.8011.0022.83CATOM3044CD1LEUA38468.86739.11222.1321.0025.00CATOM3045CD2LEUA38470.29337.50220.7421.0024.54CATOM3046NLEUA38566.65034.33019.3841.0022.53NATOM3047CALEUA38565.50533.40019.3241.0024.05CATOM3048CLEUA38565.17132.87220.7111.0023.35CATOM3049OLEUA38566.01932.23821.3461.0024.19OATOM3050CBLEUA38565.82332.25218.3781.0020.91CATOM3051CGLEUA38566.21632.65916.9231.0026.56CATOM3052CD1LEUA38566.66831.41216.1571.0025.11CATOM3053CD2LEUA38565.00833.32716.2021.0028.62CATOM3054NLEUA38663.92633.09121.1461.0021.44NATOM3055CALEUA38663.49332.72722.5071.0022.95CATOM3056CLEUA38662.54431.53722.5311.0024.92CATOM3057OLEUA38661.76231.33921.5921.0023.54OATOM3058CBLEUA38662.80833.91123.1831.0020.20CATOM3059CGLEUA38663.48335.29823.0581.0021.58CATOM3060CD1LEUA38662.64236.33723.7711.0022.42CATOM3061CD2LEUA38664.92635.27623.6541.0021.55CATOM3062NGLUA38762.60130.77223.6171.0022.74NATOM3063CAGLUA38761.73429.59623.8181.0024.88CATOM3064CGLUA38761.34929.52625.3031.0024.48CATOM3065OGLUA38762.23029.62726.1751.0023.17OATOM3066CBGLUA38762.46428.31423.4561.0027.05CATOM3067CGGLUA38761.50327.12823.2371.0037.16CATOM3068CDGLUA38762.17225.74523.2681.0039.98CATOM3069OE1GLUA38763.20125.51622.5931.0044.18OATOM3070OE2GLUA38761.65024.85723.9721.0046.29OATOM3071NLEUA38860.06429.36725.6121.0022.53NATOM3072CALEUA38859.67929.27827.0311.0026.07CATOM3073CLEUA38859.88527.85027.5421.0027.75CATOM3074OLEUA38859.39526.87526.9351.0028.32OATOM3075CBLEUA38858.22429.68627.2811.0023.47CATOM3076CGLEUA38857.66629.64928.7241.0022.59CATOM3077CD1LEUA38858.48930.54929.6871.0022.03CATOM3078CD2LEUA38856.20430.10728.7511.0025.81CATOM3079NLYSA38960.62527.72028.6481.0024.86NATOM3080CALYSA38960.85626.38029.2281.0027.21CATOM3081CLYSA38959.92326.03230.4021.0026.84CATOM3082OLYSA38959.41424.90230.4971.0027.04OATOM3083CBLYSA38962.31026.24629.7351.0026.39CATOM3084CGLYSA38963.34626.51228.7011.0030.08CATOM3085CDLYSA38963.22625.53927.5571.0033.57CATOM3086CELYSA38964.36025.69926.5711.0035.29CATOM3087NZLYSA38965.68425.60327.2181.0036.25NATOM3088NHISA39059.71426.99431.2901.0025.51NATOM3089CAHISA39058.89326.80232.4761.0025.54CATOM3090CHISA39058.35528.13932.9901.0025.92CATOM3091OHISA39058.97629.18232.7761.0024.09OATOM3092CBHISA39059.74326.13033.5841.0029.77CATOM3093CGHISA39058.93925.72734.7821.0033.72CATOM3094ND1HISA39058.23124.54334.8361.0035.82NATOM3095CD2HISA39058.67326.38435.9391.0032.57CATOM3096CE1HISA39057.56124.48935.9751.0037.52CATOM3097NE2HISA39057.81425.59236.6621.0039.33NATOM3098NSERA39157.17528.12533.6241.0024.26NATOM3099CASERA39156.60029.34834.1621.0025.33CATOM3100CSERA39155.91129.07335.4901.0028.33CATOM3101OSERA39155.21228.06235.6211.0028.00OATOM3102CBSERA39155.53429.94033.2181.0024.65CATOM3103OGSERA39154.93831.04033.8531.0025.68OATOM3104NASNA39256.09129.97036.4581.0026.48NATOM3105CAASNA39255.39629.83337.7311.0028.76CATOM3106CASNA39254.34330.93037.8781.0031.72CATOM3107OASNA39253.78331.10938.9641.0033.11OATOM3108CBASNA39256.37229.88938.8991.0032.64CATOM3109CGASNA39257.07528.54939.1311.0035.08CATOM3110OD1ASNA39256.47327.48838.9481.0037.78OATOM3111ND2ASNA39258.33628.59639.5511.0036.07NATOM3112NILEA39354.08631.65236.7831.0030.18NATOM3113CAILEA39353.11032.74236.7351.0029.96CATOM3114CILEA39352.04432.46035.6421.0028.49CATOM3115OILEA39351.39433.39535.1551.0028.83OATOM3116CBILEA39353.74834.13136.3841.0030.32CATOM3117CG1ILEA39354.37834.07634.9751.0031.20CATOM3118CG2ILEA39354.72434.59237.5101.0030.02CATOM3119CD1ILEA39354.93535.39134.4481.0032.10CATOM3120NGLYA39451.86731.19735.2721.0027.26NATOM3121CAGLYA39450.89930.84934.2371.0031.55CATOM3122CGLYA39451.42430.85832.8001.0034.13CATOM3123OGLYA39452.57931.22732.5481.0031.23OATOM3124NPROA39550.61630.39531.8281.0036.02NATOM3125CAPROA39551.09530.39930.4371.0036.00CATOM3126CPROA39551.15731.83529.9181.0034.59CATOM3127OPROA39550.46732.70730.4351.0033.77OATOM3128CBPROA39550.02629.58229.6861.0038.95CATOM3129CGPROA39549.47128.67430.7371.0039.78CATOM3130CDPROA39549.38729.58931.9571.0036.96CATOM3131NPHEA39652.03332.07428.9421.0032.83NATOM3132CAPHEA39652.15133.37628.2811.0030.03CATOM3133CPHEA39653.03333.16627.0641.0030.18CATOM3134OPHEA39653.81432.21627.0031.0030.26OATOM3135CBPHEA39652.69534.47729.2191.0028.59CATOM3136CGPHEA39654.13334.29229.6431.0028.56CATOM3137CD1PHEA39655.18134.78828.8581.0029.91CATOM3138CD2PHEA39654.43433.63830.8371.0028.62CATOM3139CE1PHEA39656.55334.63629.2601.0028.42CATOM3140CE2PHEA39655.77633.47731.2571.0029.06CATOM3141CZPHEA39656.84333.98230.4501.0025.50CATOM3142NPROA39752.88234.01226.0391.0031.72NATOM3143CAPROA39753.69533.88124.8111.0030.99CATOM3144CPROA39755.08934.43725.0731.0025.03CATOM3145OPROA39755.20935.57725.5011.0025.74OATOM3146CBPROA39752.94934.74423.7821.0033.15CATOM3147CGPROA39751.58634.99924.4011.0036.83CATOM3148CDPROA39751.84735.04625.8931.0033.37CATOM3149NVALA39856.10833.64124.7981.0028.32NATOM3150CAVALA39857.49834.07225.0491.0027.81CATOM3151CVALA39857.85635.39524.3311.0027.85CATOM3152OVALA39858.75736.12324.7461.0024.15OATOM3153CBVALA39858.47432.88824.7021.0026.70CATOM3154CG1VALA39858.76632.84823.2151.0027.76CATOM3155CG2VALA39859.77432.99925.5581.0025.31CATOM3156NGLUA39957.10235.74223.2801.0026.71NATOM3157CAGLUA39957.34536.98522.5481.0028.24CATOM3158CGLUA39957.22838.23723.4011.0026.94CATOM3159OGLUA39957.78139.28823.0471.0030.28OATOM3160CBGLUA39956.36537.12221.3671.0029.28CATOM3161CGGLUA39956.61636.13420.2511.0033.82CATOM3162CDGLUA39956.40034.67720.6661.0036.50CATOM3163OE1GLUA39955.47034.41321.4831.0030.49OATOM3164OE2GLUA39957.17433.81120.1541.0037.52OATOM3165NLEUA40056.49338.15724.5051.0027.36NATOM3166CALEUA40056.36439.31225.3631.0029.08CATOM3167CLEUA40057.71939.68125.9631.0027.76CATOM3168OLEUA40057.89940.79326.3821.0029.05OATOM3169CBLEUA40055.36239.05326.4961.0029.59CATOM3170CGLEUA40053.94038.80726.0461.0032.52CATOM3171CD1LEUA40053.02738.50527.2411.0031.14CATOM3172CD2LEUA40053.48440.05625.3141.0036.13CATOM3173NLEUA40158.66838.74825.9931.0027.77NATOM3174CALEUA40159.99239.04726.5591.0025.80CATOM3175CLEUA40161.01439.49725.5261.0026.73CATOM3176OLEUA40162.15139.84225.8721.0027.57OATOM3177CBLEUA40160.54437.81527.2891.0022.41CATOM3178CGLEUA40159.72137.45128.5261.0023.32CATOM3179CD1LEUA40160.13336.05528.9691.0026.06CATOM3180CD2LEUA40159.92138.49729.6491.0022.32CATOM3181NGLNA40260.61839.51024.2531.0025.66NATOM3182CAGLNA40261.55439.90823.2071.0025.39CATOM3183CGLNA40262.17841.31123.4001.0023.36CATOM3184OGLNA40263.40341.45523.3061.0023.87OATOM3185CBGLNA40260.88439.81121.8191.0024.98CATOM3186CGGLNA40261.89639.85720.6751.0028.31CATOM3187CDGLNA40262.64538.53620.4921.0028.84CATOM3188OE1GLNA40262.03437.47720.2661.0028.57OATOM3189NE2GLNA40263.95738.59520.5791.0023.99NATOM3190NASPA40361.37942.34023.7001.0022.96NATOM3191CAASPA40361.97043.66423.8571.0024.09CATOM3192CASPA40363.00543.80024.9831.0025.21CATOM3193OASPA40364.04844.43824.8071.0024.96OATOM3194CBASPA40360.88444.73424.0801.0027.07CATOM3195CGASPA40359.96244.87722.8831.0031.43CATOM3196OD1ASPA40360.39144.47721.7681.0028.23OATOM3197OD2ASPA40358.83345.40323.0771.0032.56OATOM3198NILEA40462.70743.23126.1471.0023.69NATOM3199CAILEA40463.64143.38527.2441.0022.82CATOM3200CILEA40464.90242.58726.9231.0023.27CATOM3201OILEA40465.99343.04827.2181.0022.20OATOM3202CBILEA40462.98842.95628.5711.0024.00CATOM3203CG1ILEA40463.95843.22229.7231.0027.72CATOM3204CG2ILEA40462.51641.53328.4721.0023.88CATOM3205CD1ILEA40463.26843.63231.0341.0031.59CATOM3206NMETA40564.76241.42826.2731.0022.62NATOM3207CAMETA40565.94540.63525.9401.0023.69CATOM3208CMETA40566.77441.33024.8421.0023.83CATOM3209OMETA40568.00841.32224.8871.0021.48OATOM3210CBMETA40565.55839.18925.5411.0024.44CATOM3211CGMETA40564.83438.42426.6581.0026.47CATOM3212SDMETA40565.78238.42728.2491.0031.28SATOM3213CEMETA40566.98537.52927.6971.0027.02CATOM3214NASNA40666.10841.99723.8921.0025.32NATOM3215CAASNA40666.82142.70022.8031.0025.01CATOM3216CASNA40667.65943.86823.3391.0025.74CATOM3217OASNA40668.62244.30622.6851.0023.75OATOM3218CBASNA40665.82943.19821.7121.0024.29CATOM3219CGASNA40665.34142.06220.7891.0024.00CATOM3220OD1ASNA40665.83040.94220.8571.0028.11OATOM3221ND2ASNA40664.36342.36719.9061.0024.97NATOM3222NTYRA40767.29944.35624.5321.0023.43NATOM3223CATYRA40768.02949.43425.1661.0024.18CATOM3224CTYRA40769.14444.86126.0521.0022.82CATOM3225OTYRA40770.35445.11925.8291.0021.93OATOM3226CBTYRA40767.06646.27426.0101.0027.92CATOM3227CGTYRA40767.75147.43026.6901.0033.37CATOM3228CD1TYRA40768.16748.54525.9551.0034.55CATOM3229CD2TYRA40768.05847.38028.0491.0033.57CATOM3230CE1TYRA40768.87649.57426.5581.0038.53CATOM3231CE2TYRA40768.76148.40228.6561.0038.93CATOM3232CZTYRA40769.17049.49227.9141.0038.57CATOM3233OHTYRA40769.87950.50428.5291.0041.58OATOM3234NILEA40868.73844.06527.0341.0022.57NATOM3235CAILEA40869.68143.43927.9811.0024.17CATOM3236CILEA40870.89242.75327.3381.0023.46CATOM3237OILEA40872.00242.87327.8251.0024.38OATOM3238CBILEA40868.93642.42728.8871.0027.96CATOM3239CG1ILEA40868.21443.20429.9651.0031.20CATOM3240CG2ILEA40869.90041.38829.4981.0032.51CATOM3241CD1ILEA40867.23542.34730.7171.0034.27CATOM3242NVALA40970.69542.01726.2501.0024.76NATOM3243CAVALA40971.82841.33525.6451.0023.94CATOM3244CVALA40972.95342.19225.0831.0026.77CATOM3245OVALA40974.07442.09625.5541.0025.67OATOM3246CBVALA40971.31740.35324.6111.0030.46CATOM3247CG1VALA40972.44839.95123.6581.0028.71CATOM3248CG2VALA40970.67239.17525.3471.0024.93CATOM3249NPROA41072.68643.08524.0911.0026.72NATOM3250CAPROA41073.79943.89323.5651.0026.51CATOM3251CPROA41074.30044.99324.5151.0025.72CATOM3252OPROA41075.46845.43824.4511.0026.09OATOM3253CBPROA41073.21344.47022.2521.0029.07CATOM3254CGPROA41071.74144.61122.5761.0028.83CATOM3255CDPROA41071.45043.30823.3191.0027.31CATOM3256NILEA41173.42645.44725.4021.0022.55NATOM3257CAILEA41173.84246.48426.3331.0025.31CATOM3258CILEA41174.58745.98827.5851.0025.38CATOM3259OILEA41175.58846.57527.9711.0025.04OATOM3260CBILEA41172.63447.29426.8331.0030.13CATOM3261CG1ILEA41171.97048.00725.6511.0033.77CATOM3262CG2ILEA41173.07248.29127.8741.0031.49CATOM3263CD1ILEA41172.80449.14025.1031.0038.80CATOM3264NLEUA41274.10244.90028.1921.0023.47NATOM3265CALEUA41274.69844.42029.4311.0024.03CATOM3266CLEUA41275.42943.08229.3731.0024.12CATOM3267OLEUA41276.40442.90630.0891.0024.47OATOM3268CBLEUA41273.63844.31130.5121.0026.07CATOM3269CGLEUA41272.90445.58230.9461.0031.04CATOM3270CD1LEUA41271.76445.23631.8831.0028.70CATOM3271CD2LEUA41273.93146.49331.6811.0029.45CATOM3272NVALA41374.96642.14328.5501.0019.71NATOM3273CAVALA41375.63040.81528.5081.0020.71CATOM3274CVALA41376.77640.67727.5151.0019.12CATOM3275OVALA41377.89940.30927.9071.0020.36OATOM3276CBVALA41374.58839.66528.2471.0023.74CATOM3277CG1VALA41375.27738.30428.3981.0022.41CATOM3278CG2VALA41373.40839.79729.2041.0025.05CATOM3279NLEUA41476.52140.96426.2341.0016.47NATOM3280CALEUA41477.55140.90425.2171.0017.77CATOM3281CLEUA41478.84641.68625.5291.0017.11CATOM3282OLEUA41479.93841.19625.2261.0019.03OATOM3283CBLEUA41477.01541.34523.8321.0018.58CATOM3284CGLEUA41477.98941.22222.6461.0019.25CATOM3285CD1LEUA41478.43939.72522.4421.0024.16CATOM3286CD2LEUA41477.27041.70821.3971.0023.16CATOM3287NPROA41578.75242.89526.0891.0019.05NATOM3288CAPROA41579.99343.62026.3701.0019.48CATOM3289CPROA41580.94142.88627.3041.0021.66CATOM3290OPROA41582.16542.92627.1091.0019.36OATOM3291CBPROA41579.49444.93926.9971.0019.33CATOM3292CGPROA41578.22645.17926.3021.0024.09CATOM3293CDPROA41577.58343.77126.3311.0019.42CATOM3294NARGA41680.38942.20528.3041.0019.80NATOM3295CAARGA41681.27041.46629.2311.0021.10CATOM3296CARGA41682.01840.38728.4631.0019.17CATOM3297OARGA41683.17240.11628.7171.0019.00OATOM3298CBARGA41680.44840.83730.3511.0023.65CATOM3299CGARGA41679.58141.85231.0951.0027.82CATOM3300CDARGA41680.43542.70932.0231.0033.30CATOM3301NEARGA41680.99443.88131.3531.0039.79NATOM3302CZARGA41680.25944.87730.8371.0042.30CATOM3303NH1ARGA41678.91444.83930.9081.0040.30NATOM3304NH2ARGA41680.87445.91630.2531.0039.73NATOM3305NVALA41781.34839.79127.4951.0019.02NATOM3306CAVALA41781.96238.76826.6521.0022.54CATOM3307CVALA41783.08139.35125.7771.0016.77CATOM3308OVALA41784.19438.82825.7151.0016.49OATOM3309CBVALA41780.87938.14525.7791.0022.64CATOM3310CG1VALA41781.40737.77924.4381.0036.94CATOM3311CG2VALA41780.33836.93926.4781.0036.93CATOM3312NASNA41882.77040.44025.0751.0015.55NATOM3313CAASNA41883.72241.06524.2311.0014.24CATOM3314CASNA41884.91741.67524.9491.0014.58CATOM3315OASNA41885.96841.78224.3181.0014.77OATOM3316CBASNA41882.99742.08723.3051.0016.36CATOM3317CGASNA41882.40241.40422.0611.0019.97CATOM3318OD1ASNA41882.98040.42221.5531.0018.89OATOM3319ND2ASNA41881.30041.92021.5531.0017.82NATOM3320NGLUA41984.76942.09326.2171.0014.50NATOM3321CAGLUA41985.92842.59026.9861.0019.31CATOM3322CGLUA41986.93441.44327.1531.0016.18CATOM3323OGLUA41988.11141.62727.0101.0018.20OATOM3324CBGLUA41985.50143.08528.3541.0022.44CATOM3325CGGLUA41984.86844.43428.2991.0029.68CATOM3326CDGLUA41984.23444.74629.6291.0032.95CATOM3327OE1GLUA41984.85944.42330.6521.0041.89OATOM3328OE2GLUA41983.12045.29829.6341.0042.80OATOM3329NLYSA42086.42340.24627.4251.0018.41NATOM3330CALYSA42087.30539.09627.5681.0019.49CATOM3331CLYSA42087.91738.61726.2331.0019.26CATOM3332OLYSA42089.08538.24426.1801.0019.03OATOM3333CBLYSA42086.55937.95928.2721.0024.86CATOM3334CGLYSA42087.48536.74828.4411.0026.08CATOM3335CDLYSA42088.57636.97429.5261.0028.43CATOM3336CELYSA42089.51835.74329.6391.0033.40CATOM3337NZLYSA42090.69435.90430.6101.0023.76NATOM3338NLEUA42187.12638.65425.1391.0019.68NATOM3339CALEUA42187.62538.25323.8261.0021.74CATOM3340CLEUA42188.70039.23823.3381.0018.03CATOM3341OLEUA42189.65638.86422.6611.0018.45OATOM3342CBLEUA42186.44238.18522.8501.0020.55CATOM3343CGLEUA42185.48337.06023.2151.0021.71CATOM3344CD1LEUA42184.17937.24522.4331.0024.60CATOM3345CD2LEUA42186.14135.71922.8661.0022.63CATOM3346NGLNA42288.55040.50823.6921.0018.48NATOM3347CAGLNA42289.55741.49923.3271.0019.41CATOM3348CGLNA42290.84741.39724.1271.0018.53CATOM3349OGLNA42291.90741.75623.6031.0022.07OATOM3350CBGLNA42288.97842.93823.4211.0020.17CATOM3351CGGLNA42288.11543.24622.1791.0022.16CATOM3352CDGLNA42288.97943.47820.9081.0019.83CATOM3353OE1GLNA42289.84044.40220.8611.0026.58OATOM3354NE2GLNA42288.76342.65419.8871.0023.03NATOM3355NLYSA42390.76740.90925.3691.0019.30NATOM3356CALYSA42391.94540.71026.2111.0021.18CATOM3357CLYSA42392.75839.60525.5021.0023.74CATOM3358OLYSA42393.98339.59825.5201.0024.05OATOM3359CBLYSA42391.51940.26427.6191.0022.13CATOM3360CGLYSA42392.68339.87028.5011.0028.49CATOM3361CDLYSA42392.23939.22329.8421.0034.87CATOM3362CELYSA42393.42238.37330.3821.0036.10CATOM3363NZLYSA42393.19537.70231.6801.0041.82NATOM3364NGLYA42492.04038.68424.8731.0022.38NATOM3365CAGLYA42492.67937.64124.0791.0022.35CATOM3366CGLYA42493.35536.44024.7451.0019.62CATOM3367OGLYA42493.20036.20625.9471.0022.15OATOM3368NAPHEA42594.11935.69723.9480.5018.88NATOM3369NBPHEA42594.10735.70823.9230.5020.46NATOM3370CAAPHEA42594.82234.49724.4340.5016.32CATOM3371CABPHEA42594.79034.47324.3320.5019.97CATOM3372CAPHEA42596.19034.45823.7870.5015.57CATOM3373CBPHEA42596.20134.43923.7460.5017.46CATOM3374OAPHEA42596.36234.81622.6140.5018.72OATOM3375OBPHEA42596.41434.80222.5790.5019.98OATOM3376CBAPHEA42593.98133.24424.1010.5015.89CATOM3377CBBPHEA42593.98033.24723.8100.5022.42CATOM3378CGAPHEA42592.58333.33224.6500.5019.13CATOM3379CGBPHEA42592.48933.33524.0880.5030.09CATOM3380CD1APHEA42592.32733.04825.9880.5016.03CATOM3381CD1BPHEA42591.74634.45323.7030.5031.10CATOM3382CD2APHEA42591.54533.81823.8650.5020.90CATOM3383CD2BPHEA42591.84732.34524.8110.5033.54CATOM3384CE1APHEA42591.05133.24626.5510.5016.38CATOM3385CE1BPHEA42590.38734.58724.0540.5033.46CATOM3386CE2APHEA42590.25934.02524.4290.5021.73CATOM3387CE2BPHEA42590.49132.45925.1650.5035.61CATOM3388CZAPHEA42590.03333.73225.7730.5015.74CATOM3389CZBPHEA42589.76333.58324.7910.5035.59CATOM3390NPROA42697.19434.01324.5431.0015.33NATOM3391CAPROA42698.58733.93524.0581.0017.85CATOM3392CPROA42698.74932.89022.9441.0019.06CATOM3393OPROA42698.13531.82523.0211.0018.81OATOM3394CBPROA42699.39433.49225.3171.0020.75CATOM3395CGPROA42698.41533.39726.4181.0018.10CATOM3396CDPROA42697.02233.36725.8431.0016.62CATOM3397NLEUA42799.55633.25121.9321.0017.88NATOM3398CALEUA42799.94032.37920.8031.0019.44CATOM3399CLEUA427101.25531.73421.2941.0017.83CATOM3400OLEUA427101.91032.20122.2461.0017.76OATOM3401CBLEUA427100.19333.24119.5611.0022.15CATOM3402CGLEUA42799.16433.28918.4081.0027.60CATOM3403CD1LEUA42797.88832.59918.7521.0028.50CATOM3404CD2LEUA42799.02634.71517.8951.0026.30CATOM3405NPROA428101.66530.64920.6451.0017.74NATOM3406CAPROA428102.87929.95421.0411.0021.49CATOM3407CPROA428104.13730.52520.4451.0021.45CATOM3408OPROA428104.81429.86819.6541.0023.23OATOM3409CBPROA428102.61828.50520.5931.0017.24CATOM3410CGPROA428101.74828.70619.2751.0018.87CATOM3411CDPROA428100.94330.00919.5321.0018.18CATOM3412NTHRA429104.49131.72520.8701.0018.87NATOM3413CATHRA429105.68832.34520.3171.0020.98CATOM3414CTHRA429106.86632.11921.2361.0021.62CATOM3415OTHRA429106.71132.17922.4351.0024.02OATOM3416CBTHRA429105.50833.92020.1961.0024.02CATOM3417OG1THRA429104.88334.38821.3941.0023.58OATOM3418CG2THRA429104.64234.31519.0051.0021.06CATOM3419NPROA430108.05531.84620.6761.0023.16NATOM3420CAPROA430109.28131.63821.4611.0025.95CATOM3421CPROA430109.78233.00321.9001.0027.94CATOM3422OPROA430109.18434.02321.5601.0023.22OATOM3423CBPROA430110.23330.96520.4661.0023.91CATOM3424CGPROA430109.77831.49519.1131.0025.65CATOM3425CDPROA430108.25831.52119.2551.0025.14CATOM3426NALAA431110.88533.02222.6501.0027.17NATOM3427CAALAA431111.41434.28923.1511.0027.49CATOM3428CALAA431111.78735.29322.0521.0025.89CATOM3429OALAA431112.25834.92320.9691.0024.83OATOM3430CBALAA431112.62534.01124.0281.0024.28CATOM3431NARGA432111.57236.57022.3551.0028.54NATOM3432CAARGA432111.91137.68021.4581.0030.43CATOM3433CARGA432111.36737.63820.0261.0030.67CATOM3434OARGA432111.99238.22119.1141.0031.09OATOM3435CBARGA432113.43437.84021.3561.0034.94CATOM3436CGARGA432114.22537.83222.6561.0038.43CATOM3437CDARGA432115.59837.15922.3981.0043.63CATOM3438NEARGA432115.84836.05423.3201.0046.50NATOM3439CZARGA432116.79635.13623.1561.0048.68CATOM3440NH1ARGA432117.58635.19322.0991.0050.18NATOM3441NH2ARGA432116.95534.16024.0511.0051.79NATOM3442NVALA433110.24136.97019.7971.0021.77NATOM3443CAVALA433109.67736.90618.4591.0026.93CATOM3444CVALA433108.32937.59518.4231.0030.21CATOM3445OVALA433107.53037.37719.3141.0032.17OATOM3446CBVALA433109.51135.40517.9981.0026.51CATOM3447CG1VALA433108.35635.24017.0181.0031.84CATOM3448CG2VALA433110.84734.93017.3201.0023.21CATOM3449NGLNA434108.09538.43517.4061.0029.12NATOM3450CAGLNA434106.80839.10417.2221.0030.27CATOM3451CGLNA434106.28638.85315.7851.0031.28CATOM3452OGLNA434107.07538.75614.8271.0029.65OATOM3453CBGLNA434106.94740.61917.5191.0031.56CATOM3454CGGLNA434107.40440.93318.9691.0036.69CATOM3455CDGLNA434107.25042.42719.3761.0040.55CATOM3456OE1GLNA434106.12742.93819.4611.0036.93OATOM3457NE2GLNA434108.38343.11619.6271.0040.09NATOM3458NLEUA435104.96538.73615.6211.0030.10NATOM3459CALEUA435104.37838.46914.3081.0030.39CATOM3460CLEUA435103.92039.71113.5231.0030.20CATOM3461OLEUA435103.41340.62814.1261.0033.46OATOM3462CBLEUA435103.18137.53314.5061.0033.74CATOM3463CGLEUA435103.58136.31115.3421.0035.93CATOM3464CD1LEUA435102.34735.56015.7991.0035.75CATOM3465CD2LEUA435104.51535.43314.4871.0036.78CATOM3466NTYRA436104.08339.73912.1901.0029.33NATOM3467CATYRA436103.60540.86811.3831.0027.87CATOM3468CTYRA436103.17440.41010.0001.0030.05CATOM3469OTYRA436103.29739.2129.6761.0028.38OATOM3470CBTYRA436104.64442.02211.3181.0027.89CATOM3471CGTYRA436105.87041.80510.4721.0025.19CATOM3472CD1TYRA436106.91241.00910.9171.0028.80CATOM3473CD2TYRA436105.98142.3839.1981.0026.32CATOM3474CE1TYRA436108.02540.78710.1081.0025.24CATOM3475CE2TYRA436107.05942.1758.3921.0023.20CATOM3476CZTYRA436108.09341.3608.8481.0024.73CATOM3477OHTYRA436109.14941.0768.0401.0025.47OATOM3478NAASNA437102.66741.3439.1900.5028.37NATOM3479NBASNA437102.66841.3409.1860.5026.79NATOM3480CAAASNA437102.17941.0397.8480.5029.41CATOM3481CABASNA437102.20441.0337.8320.5026.48CATOM3482CAASNA437101.20739.8727.9300.5030.78CATOM3483CBASNA437101.21639.8667.9300.5029.14CATOM3484OAASNA437101.25438.9687.1050.5029.23OATOM3485OBASNA437101.25938.9557.1120.5027.72OATOM3486CBAASNA437103.32340.6496.9120.5032.27CATOM3487CBBASNA437103.40040.6396.9420.5026.39CATOM3488CGAASNA437104.11841.8356.4420.5036.64CATOM3489CGBASNA437103.01840.3675.4870.5025.88CATOM3490OD1AASNA437104.01942.9327.0100.5039.42OATOM3491OD1BASNA437103.78539.7424.7410.5027.37OATOM3492ND2AASNA437104.92741.6285.3990.5034.66NATOM3493ND2BASNA437101.86240.8425.0710.5026.13NATOM3494NVALA438100.31639.9138.9151.0030.56NATOM3495CAVALA43899.34838.8239.1081.0032.47CATOM3496CVALA43898.19438.7888.1271.0034.47CATOM3497OVALA43897.59839.8107.7611.0032.50OATOM3498CBVALA43898.77638.84710.5251.0031.87CATOM3499CG1VALA43899.88238.85811.5181.0031.13CATOM3500CG2VALA43897.88940.07210.7241.0036.41CATOM3501NVALA43997.90537.5887.6521.0031.32NATOM3502CAVALA43996.80037.4066.7591.0036.11CATOM3503CVALA43995.98636.2417.3451.0037.14CATOM3504OVALA43996.52235.3778.0711.0035.65OATOM3505CBVALA43997.27337.1045.3371.0038.19CATOM3506CG1VALA43998.22635.9155.3671.0043.13CATOM3507CG2VALA43996.07836.8334.4261.0041.07CATOM3508NLEUA44094.68536.2667.0891.0034.94NATOM3509CALEUA44093.82835.2077.5751.0036.32CATOM3510CLEUA44092.98434.6516.4451.0037.21CATOM3511OLEUA44092.42535.3835.6291.0034.43OATOM3512CBLEUA44092.90435.7108.6761.0036.50CATOM3513CGLEUA44091.65834.8128.8721.0038.03CATOM3514CD1LEUA44092.07533.4359.4711.0037.31CATOM3515CD2LEUA44090.64035.5099.7751.0038.88CATOM3516NGLNA44192.91633.3416.3861.0034.60NATOM3517CAGLNA44192.09832.7135.4091.0035.49CATOM3518CGLNA44191.34331.6106.1551.0035.54CATOM3519OGLNA44191.94430.6986.7541.0034.07OATOM3520CBGLNA44192.92932.1804.2071.0038.29CATOM3521CGGLNA44194.23231.3834.5121.0043.75CATOM3522CDGLNA44194.97730.8623.2381.0045.12CATOM3523OE1GLNA44194.46630.0192.4991.0039.90OATOM3524NE2GLNA44196.21031.3683.0131.0046.48NATOM3525NPROA44290.01731.7316.2201.0033.67NATOM3526CAPROA44289.39830.6216.9271.0030.02CATOM3527CPROA44289.34229.4305.9771.0029.82CATOM3528OPROA44289.25529.5844.7661.0029.81OATOM3529CBPROA44288.00031.1567.2731.0031.27CATOM3530CGPROA44288.22632.6457.3311.0034.90CATOM3531CDPROA44289.13332.9186.2101.0031.78CATOM3532NHISA44389.45728.2406.5251.0026.17NATOM3533CAHISA44389.32927.0305.7491.0025.42CATOM3534CHISA44388.25526.2346.4311.0023.53CATOM3535OHISA44387.79126.5747.5091.0025.93OATOM3536CBHISA44390.60326.1835.7341.0022.58CATOM3537CGHISA44391.66626.6914.8141.0026.96CATOM3538ND1HISA44392.22225.9113.8201.0027.56NATOM3539CD2HISA44392.26327.9044.7251.0025.93CATOM3540CE1HISA44393.11426.6293.1521.0028.01CATOM3541NE2HISA44393.15927.8383.6781.0029.23NATOM3542NGLNA44487.85425.1475.7921.0026.75NATOM3543CAGLNA44486.85424.2936.4151.0026.51CATOM3544CGLNA44487.49823.6317.6721.0024.96CATOM3545OGLNA44488.51322.9347.5781.0023.07OATOM3546CBGLNA44486.40123.2105.4281.0029.64CATOM3547CGGLNA44485.23822.3885.9361.0035.33CATOM3548CDGLNA44483.96323.2356.0891.0041.12CATOM3549OE1GLNA44483.12822.9736.9481.0043.39OATOM3550NE2GLNA44483.81624.2455.2411.0038.86NATOM3551NASNA44586.89523.8738.8291.0020.79NATOM3552CAASNA44587.34323.28910.1111.0020.60CATOM3553CASNA44588.58423.87910.7661.0020.05CATOM3554OASNA44589.01723.40311.8321.0016.72OATOM3555CBASNA44587.49821.7639.9971.0022.62CATOM3556CGASNA44586.21421.0999.5391.0026.79CATOM3557OD1ASNA44586.23620.0538.8681.0029.77OATOM3558ND2ASNA44585.09421.7079.8841.0019.91NATOM3559NPHEA44689.15124.90010.1481.0019.07NATOM3560CAPHEA44690.28525.57310.7981.0017.78CATOM3561CPHEA44690.55926.92510.1901.0020.51CATOM3562OPHEA44690.31727.1679.0111.0020.33OATOM3563CBPHEA44691.61324.75910.7481.0016.32CATOM3564CGPHEA44692.19124.5499.3361.0021.48CATOM3565CD1PHEA44691.67223.5258.4721.0020.65CATOM3566CD2PHEA44693.29125.3018.9091.0020.96CATOM3567CE1PHEA44692.25223.2647.2271.0020.84CATOM3568CE2PHEA44693.88925.0467.6341.0023.60CATOM3569CZPHEA44693.36624.0266.7991.0023.81CATOM3570NLEUA44791.11827.78711.0221.0018.73NATOM3571CALEUA44791.51529.11710.5891.0019.06CATOM3572CLEUA44793.01929.02610.2921.0021.79CATOM3573OLEUA44793.77728.50211.1181.0019.94OATOM3574CBLEUA44791.32330.08311.7361.0020.93CATOM3575CGLEUA44790.39431.26811.5611.0034.61CATOM3576CD1LEUA44789.16730.90310.7341.0031.44CATOM3577CD2LEUA44790.02131.77512.9721.0030.45CATOM3578NLEUA44893.43329.5769.1491.0019.34NATOM3579CALEUA44894.83929.6058.7811.0022.65CATOM3580CLEUA44895.35431.0268.8371.0026.10CATOM3581OLEUA44894.85431.8818.1031.0028.78OATOM3582CBLEUA44895.07129.0877.3511.0023.58CATOM3583CGLEUA44896.54028.9926.8961.0024.08CATOM3584CD1LEUA44897.35228.0547.8521.0026.56CATOM3585CD2LEUA44896.61128.4015.4441.0025.75CATOM3586NPHEA44996.35331.2529.6901.0022.16NATOM3587CAPHEA44997.00232.5489.8181.0027.70CATOM3588CPHEA44998.41332.4649.2591.0027.30CATOM3589OPHEA44999.20031.6259.6681.0030.52OATOM3590CBPHEA44997.07632.96311.2651.0031.43CATOM3591CGPHEA44995.84433.69111.7371.0035.96CATOM3592CD1PHEA44995.55134.97311.2611.0036.95CATOM3593CD2PHEA44994.96233.09012.6431.0040.57CATOM3594CE1PHEA44994.40035.65211.6641.0036.95CATOM3595CE2PHEA44993.80433.76813.0551.0038.38CATOM3596CZPHEA44993.53635.05812.5571.0036.99CATOM3597NGLYA45098.67933.3198.2931.0027.97NATOM3598CAGLYA45099.98933.4127.6521.0029.22CATOM3599CGLYA450100.63734.6808.1641.0029.80CATOM3600OGLYA45099.95235.7008.3451.0029.78OATOM3601NALAA451101.94534.6278.3941.0029.19NATOM3602CAALAA451102.64235.7738.9441.0025.12CATOM3603CALAA451104.14535.7548.8091.0027.49CATOM3604OALAA451104.73734.6868.6221.0021.59OATOM3605CBALAA451102.32735.87710.3531.0024.08CATOM3606NASPA452104.75236.9538.8981.0025.36NATOM3607CAASPA452106.20837.0568.8861.0025.80CATOM3608CASPA452106.61737.24610.3291.0024.82CATOM3609OASPA452105.78537.61011.1711.0027.57OATOM3610CBASPA452106.68438.1877.9451.0026.54CATOM3611CGASPA452106.42737.8386.4811.0024.14CATOM3612OD1ASPA452106.39036.6226.1331.0025.74OATOM3613OD2ASPA452106.22638.7565.6501.0025.90OATOM3614NAVALA453107.87936.95710.6090.5022.35NATOM3615NBVALA453107.87536.99110.6640.5022.88NATOM3616CAAVALA453108.42737.02511.9380.5021.03CATOM3617CABVALA453108.30537.13112.0420.5022.64CATOM3618CAVALA453109.58438.00112.0190.5022.27CATOM3619CBVALA453109.49938.05012.2210.5024.32CATOM3620OAVALA453110.37538.14611.0800.5019.85OATOM3621OBVALA453110.37538.14111.3560.5023.04OATOM3622CBAVALA453108.94335.60712.3800.5023.45CATOM3623CBBVALA453108.64235.73512.6810.5024.58CATOM3624CG1AVALA453109.94535.73013.5120.5022.91CATOM3625CG1BVALA453109.46134.89811.7200.5022.55CATOM3626CG2AVALA453107.78034.72812.7890.5022.07CATOM3627CG2BVALA453109.41435.92613.9940.5025.79CATOM3628NAVALA454109.65538.69713.1440.5021.67NATOM3629NBVALA454109.51038.75813.3440.5024.28NATOM3630CAAVALA454110.74739.61113.3870.5022.52CATOM3631CABVALA454110.60839.64613.6670.5025.20CATOM3632CAVALA454111.30039.16414.7470.5022.17CATOM3633CBVALA454111.30839.12714.8950.5024.52CATOM3634OAVALA454110.53938.97915.7020.5024.20OATOM3635OBVALA454110.67338.90115.9310.5026.42OATOM3636CBAVALA454110.28041.12813.3610.5020.96CATOM3637CBBVALA454110.15141.10313.9850.5026.07CATOM3638CG1AVALA454109.02041.34314.2070.5016.41CATOM3639CG1BVALA454111.27841.85614.6860.5026.68CATOM3640CG2AVALA454111.42342.00113.8320.5023.65CATOM3641CG2BVALA454109.78741.80712.7330.5021.85CATOM3642NTYRA455112.61538.92814.7861.0022.38NATOM3643CATYRA455113.37538.47015.9501.0022.98CATOM3644CTYRA455114.31539.57116.5041.0029.35CATOM3645OTYRA455114.93140.30315.7421.0027.45OATOM3646CBTYRA455114.25637.28715.5551.0026.26CATOM3647CGTYRA455115.20636.84716.6401.0024.63CATOM3648CD1TYRA455114.74836.18017.7961.0030.39CATOM3649CD2TYRA455116.57837.05016.5151.0027.09CATOM3650CE1TYRA455115.65335.73018.7841.0030.67CATOM3651CE2TYRA455117.47136.59617.4941.0028.49CATOM3652CZTYRA455117.02135.94318.6151.0031.62CATOM3653OHTYRA455117.94335.49119.5581.0032.04OATOM3654NLYSA456114.45339.68517.8221.0034.22NATOM3655CALYSA456115.36840.71018.3351.0040.96CATOM3656CLYSA456116.20740.24019.5311.0044.03CATOM3657OLYSA456117.45540.14319.4151.0045.32OATOM3658CBLYSA456114.57041.96718.6791.0040.55CATOM3659CGLYSA456113.67842.48217.5101.0039.39CATOM3660CDLYSA456112.42943.27217.9931.0044.56CATOM3661CELYSA456111.45742.39318.8371.0043.77CATOM3662NZLYSA456110.86841.20218.0971.0035.09NATOM3663OXTLYSA456115.59539.95520.5841.0049.29OTER3664LYSA456HETATM3665C1PC2577121.23532.73919.1041.0059.16CHETATM3666C2PC2577120.35631.50018.8161.0057.07CHETATM3667C3PC2577119.56831.65017.5031.0056.79CHETATM3668C4PC2577121.20533.40023.1821.0061.06CHETATM3669C5PC2577120.72833.40124.6741.0060.65CHETATM3670C6PC2577122.07235.34625.3941.0059.92CHETATM3671C7PC2577120.29234.46126.7801.0060.68CHETATM3672C8PC2577119.73635.66224.8471.0061.06CHETATM3673C11PC2577117.22132.51617.0641.0057.74CHETATM3674C12PC2577117.19831.72115.7381.0054.85CHETATM3675C13PC2577116.14532.25714.7321.0050.33CHETATM3676C14PC2577114.69231.93915.1501.0049.07CHETATM3677C15PC2577113.65433.00114.7151.0048.44CHETATM3678C16PC2577113.31032.88713.2231.0048.78CHETATM3679C17PC2577111.84632.60312.9541.0046.01CHETATM3680C18PC2577111.60131.17512.3801.0045.14CHETATM3681C19PC2577111.12330.13713.4341.0046.58CHETATM3682C20PC2577110.15030.71414.4591.0047.03CHETATM3683C21PC2577109.03529.76714.7971.0048.76CHETATM3684C22PC2577107.68930.36814.4171.0050.04CHETATM3685C23PC2577107.10831.18215.5471.0049.67CHETATM3686C24PC2577105.81030.57416.0641.0048.89CHETATM3687C25PC2577104.73431.63016.2441.0050.26CHETATM3688C26PC2577103.44730.99516.6911.0049.29CHETATM3689C27PC2577102.38232.02416.9751.0051.78CHETATM3690C28PC2577101.40932.28215.8101.0054.01CHETATM3691C31PC2577122.26529.71318.2561.0056.47CHETATM3692C32PC2577122.71930.43016.9851.0056.20CHETATM3693C33PC2577123.65529.52916.1411.0053.24CHETATM3694C34PC2577123.08229.29214.7541.0052.77CHETATM3695C35PC2577122.91327.81614.4081.0049.23CHETATM3696C36PC2577122.54127.62712.9191.0046.06CHETATM3697C37PC2577121.19228.22112.5421.0045.16CHETATM3698C38PC2577120.05527.32612.9451.0045.26CHETATM3699C39PC2577118.75227.80112.3281.0047.84CHETATM3700C40PC2577117.54327.46413.2001.0046.88CHETATM3701C41PC2577116.89726.13112.8331.0047.97CHETATM3702C42PC2577115.38926.19712.9941.0047.83CHETATM3703C43PC2577114.87325.00713.7661.0048.72CHETATM3704C44PC2577113.54825.32014.4161.0048.84CHETATM3705C45PC2577112.96424.12615.1431.0047.68CHETATM3706C46PC2577111.46724.30315.3041.0048.42CHETATM3707C47PC2577110.97223.73216.6071.0048.20CHETATM3708C48PC2577109.55224.19016.9381.0049.06CHETATM3709NPC2577120.72534.72525.4001.0060.84NHETATM3710O2PC2577121.10930.22819.0741.0057.05OHETATM3711O3PC2577118.44832.48017.9121.0058.04OHETATM3712O11PC2577116.22933.21617.4111.0061.98OHETATM3713O31PC2577122.84228.65018.5891.0058.09OHETATM3714O1PPC2577123.02734.65720.9631.0064.51OHETATM3715O2PPC2577120.83635.51820.0501.0062.32OHETATM3716O3PPC2577121.12533.00120.5351.0062.24OHETATM3717O4PPC2577121.01134.65422.4471.0063.16OHETATM3718PPC2577121.50234.46520.9811.0064.80PHETATM3719C1PC257886.99434.83031.9301.0061.62CHETATM3720C2PC257885.84134.96530.9011.0062.02CHETATM3721C3PC257885.86833.86229.8021.0062.35CHETATM3722C11PC257885.96033.70027.2851.0060.88CHETATM3723C12PC257885.31134.73526.3391.0059.32CHETATM3724C13PC257884.04335.41526.8181.0058.10CHETATM3725C14PC257882.91834.46227.1271.0056.18CHETATM3726C15PC257882.34533.86325.8601.0054.56CHETATM3727C16PC257882.79032.42125.7391.0052.22CHETATM3728C17PC257883.40832.15224.3921.0052.98CHETATM3729C18PC257883.87130.71724.2771.0051.10CHETATM3730C19PC257884.44830.48222.9171.0050.62CHETATM3731C20PC257885.94430.57022.8961.0049.23CHETATM3732C21PC257886.38231.22221.6211.0048.86CHETATM3733C22PC257887.86531.30821.5621.0051.74CHETATM3734C23PC257888.34332.69021.9281.0052.09CHETATM3735C24PC257889.64533.03121.2011.0053.34CHETATM3736C25PC257889.65134.46720.6571.0053.56CHETATM3737C26PC257889.28134.47719.1861.0053.09CHETATM3738C27PC257887.77834.27018.9551.0055.53CHETATM3739C28PC257887.40132.90518.3471.0054.69CHETATM3740C31PC257883.87236.20231.8061.0059.73CHETATM3741C32PC257882.86336.60430.6921.0056.28CHETATM3742C33PC257881.38636.61731.0791.0051.27CHETATM3743C34PC257880.52036.14629.9371.0047.45CHETATM3744C35PC257879.09136.66330.0711.0044.75CHETATM3745C36PC257878.13235.62730.6611.0042.16CHETATM3746C37PC257877.13835.05329.6441.0044.01CHETATM3747C38PC257877.70033.78929.0251.0048.55CHETATM3748C39PC257876.77933.14128.0051.0048.71CHETATM3749C40PC257877.57832.23027.0521.0050.41CHETATM3750C41PC257877.62832.76625.6261.0050.35CHETATM3751C42PC257878.63133.93025.4501.0050.71CHETATM3752C43PC257877.93835.32325.4401.0052.01CHETATM3753C44PC257877.11635.59424.1781.0048.11CHETATM3754C45PC257875.62535.64424.4891.0046.52CHETATM3755C46PC257874.77135.88423.2411.0048.58CHETATM3756C47PC257873.27235.76623.5431.0045.01CHETATM3757C48PC257872.56934.52322.9851.0044.41CHETATM3758O2PC257884.55534.89031.6201.0061.50OHETATM3759O3PC257886.54634.26628.5421.0061.85OHETATM3760O11PC257886.00732.47326.9791.0061.43OHETATM3761O31PC257884.11836.93732.8061.0062.13OHETATM3762OHOH60084.16523.66811.9671.0021.08OHETATM3763OHOH601118.12529.7913.8191.0027.75OHETATM3764OHOH60270.14931.10534.2701.0018.49OHETATM3765OHOH60379.51228.64733.0511.0018.96OHETATM3766OHOH60470.53830.94239.0431.0018.86OHETATM3767OHOH605119.57316.7468.9211.0027.63OHETATM3768OHOH606107.28222.98023.3401.0020.11OHETATM3769OHOH607109.39324.18724.8211.0023.06OHETATM3770OHOH608108.43826.9491.6541.0022.26OHETATM3771OHOH609150.55734.5080.7081.0023.00OHETATM3772OHOH61073.59733.32236.5721.0024.35OHETATM3773OHOH611115.49323.4751.0261.0017.94OHETATM3774OHOH612153.59740.7851.4061.0022.50OHETATM3775OHOH613151.67122.7517.9921.0029.22OHETATM3776OHOH614101.35727.24233.2671.0039.25OHETATM3777OHOH61575.75942.03518.0931.0025.98OHETATM3778OHOH61669.04230.29936.8341.0022.54OHETATM3779OHOH61766.88239.96818.3541.0024.93OHETATM3780OHOH618124.57713.5439.8031.0038.85OHETATM3781OHOH61958.11729.11723.6521.0026.70OHETATM3782OHOH620122.24024.3223.4071.0027.36OHETATM3783OHOH621151.72923.7614.6891.0027.10OHETATM3784OHOH622123.38137.4869.6171.0034.51OHETATM3785OHOH623105.19224.61822.2881.0020.50OHETATM3786OHOH624112.57717.03110.9501.0023.13OHETATM3787OHOH62568.25538.54347.3371.0028.60OHETATM3788OHOH626141.57623.5064.3191.0030.21OHETATM3789OHOH62794.88518.21212.9321.0029.78OHETATM3790OHOH62861.73732.25151.5741.0023.90OHETATM3791OHOH629105.80718.37015.6011.0022.56OHETATM3792OHOH630112.99335.4744.3441.0029.17OHETATM3793OHOH631113.57634.5481.9241.0029.34OHETATM3794OHOH63267.98642.71243.6741.0033.32OHETATM3795OHOH63388.01139.14333.3871.0049.94OHETATM3796OHOH634148.29233.43617.7931.0030.67OHETATM3797OHOH63558.38242.07323.5211.0028.36OHETATM3798OHOH636114.98427.28227.2221.0027.16OHETATM3799OHOH637156.45640.6622.2481.0025.44OHETATM3800OHOH63890.15446.36922.6901.0029.16OHETATM3801OHOH63962.25034.58519.6841.0025.07OHETATM3802OHOH64072.45327.09733.2041.0031.42OHETATM3803OHOH641114.90415.70512.0031.0021.58OHETATM3804OHOH642123.87718.90319.5871.0029.76OHETATM3805OHOH643156.47634.609−0.9861.0024.32OHETATM3806OHOH644110.54141.09721.0541.0047.68OHETATM3807OHOH64559.86242.71026.7611.0026.65OHETATM3808OHOH646121.79221.0630.9521.0028.87OHETATM3809OHOH647147.06319.37611.1101.0037.21OHETATM3810OHOH64880.11844.35322.8771.0024.05OHETATM3811OHOH64966.94943.85841.1681.0029.23OHETATM3812OHOH650121.85119.87421.0781.0027.34OHETATM3813OHOH65166.49627.38529.2011.0041.55OHETATM3814OHOH65257.73746.02742.0821.0029.12OHETATM3815OHOH653132.49622.5790.5881.0035.69OHETATM3816OHOH65479.72443.52119.1191.0039.42OHETATM3817OHOH655146.29639.1083.6591.0027.69OHETATM3818OHOH656157.24440.79416.3531.0034.49OHETATM3819OHOH657109.98012.91110.0441.0048.41OHETATM3820OHOH65876.98828.33033.2491.0033.22OHETATM3821OHOH659115.51324.74327.8381.0048.49OHETATM3822OHOH660152.44619.1484.9961.0045.90OHETATM3823OHOH661119.88231.345−0.4391.0031.38OHETATM3824OHOH66263.94029.42643.5581.0027.44OHETATM3825OHOH663108.56914.1567.4721.0031.27OHETATM3826OHOH66492.36423.2183.3961.0041.96OHETATM3827OHOH665129.32832.2492.0581.0034.24OHETATM3828OHOH66660.79027.04141.7881.0043.62OHETATM3829OHOH66755.15327.59026.2911.0057.69OHETATM3830OHOH668112.05324.7240.3811.0026.48OHETATM3831OHOH66971.53537.12043.4201.0036.10OHETATM3832OHOH670152.48538.6830.0951.0034.47OHETATM3833OHOH671155.05932.253−1.0421.0030.25OHETATM3834OHOH672111.13814.28413.0131.0029.81OHETATM3835OHOH67369.31547.56722.0311.0040.85OHETATM3836OHOH67488.89215.6859.4941.0029.01OHETATM3837OHOH67590.67734.77740.3151.0021.65OHETATM3838OHOH67669.17435.50049.4541.0026.98OHETATM3839OHOH677147.49723.71118.5791.0048.10OHETATM3840OHOH67853.79236.27220.2871.0052.58OHETATM3841OHOH67995.25537.13832.5741.0032.28OHETATM3842OHOH680118.97524.5740.2021.0027.94OHETATM3843OHOH681157.01543.62516.0851.0035.02OHETATM3844OHOH68271.01537.25250.2631.0030.20OHETATM3845OHOH683105.84426.50729.3321.0041.67OHETATM3846OHOH68472.61930.75837.1681.0029.31OHETATM3847OHOH68591.11736.65827.4891.0025.14OHETATM3848OHOH68659.82628.97436.4831.0026.96OHETATM3849OHOH687162.58136.737−0.2681.0020.53OHETATM3850OHOH68886.90824.08933.7841.0022.35OHETATM3851OHOH68990.94413.39914.8331.0028.37OHETATM3852OHOH690126.24020.00419.5761.0037.29OHETATM3853OHOH69190.23237.57732.8201.0031.92OHETATM3854OHOH692146.37229.58722.0481.0047.56OHETATM3855OHOH69359.62535.45052.7051.0028.99OHETATM3856OHOH69499.54623.46834.4801.0037.18OHETATM3857OHOH695111.56914.9559.1581.0020.48OHETATM3858OHOH696109.18135.81126.4321.0031.77OHETATM3859OHOH697146.41128.647−0.1651.0027.19OHETATM3860OHOH698107.04935.56922.9401.0026.40OHETATM3861OHOH69988.91325.89735.4661.0031.19OHETATM3862OHOH70080.94321.09722.7411.0044.09OHETATM3863OHOH70159.88452.26832.9331.0041.47OHETATM3864OHOH70288.60018.88128.8901.0048.28OHETATM3865OHOH703118.45916.80923.1651.0035.83OHETATM3866OHOH70475.86144.75919.6601.0049.00OHETATM3867OHOH705148.89641.40417.3231.0039.32OHETATM3868OHOH70657.70551.37337.5151.0042.86OHETATM3869OHOH70790.47020.84931.4541.0033.79OHETATM3870OHOH70898.71027.3001.9501.0057.96OHETATM3871OHOH709114.90913.69820.3641.0036.36OHETATM3872OHOH710128.22718.1227.6811.0041.51OHETATM3873OHOH71184.34340.33130.9871.0031.65OHETATM3874OHOH71264.87028.17841.4831.0035.92OHETATM3875OHOH71354.11530.04525.7161.0037.12OHETATM3876OHOH714170.80030.89513.6171.0044.37OHETATM3877OHOH715135.75919.4808.5841.0038.78OHETATM3878OHOH71661.41654.33733.0401.0040.11OHETATM3879OHOH71770.51331.23314.8971.0036.70OHETATM3880OHOH71859.42937.74919.2021.0029.70OHETATM3881OHOH71969.01843.57620.1861.0037.93OHETATM3882OHOH720152.68344.4397.8061.0023.28OHETATM3883OHOH72169.21526.26121.9401.0033.59OHETATM3884OHOH72298.70444.87723.4231.0044.80OHETATM3885OHOH72387.84636.23211.4021.0039.79OHETATM3886OHOH72476.29828.51225.2641.0039.88OHETATM3887OHOH72565.65627.13123.4511.0040.38OHETATM3888OHOH72676.95438.71837.7601.0029.18OHETATM3889OHOH72772.12744.46418.8451.0045.57OHETATM3890OHOH728121.81918.07623.4151.0040.29OHETATM3891OHOH729136.25134.5020.1261.0038.20OHETATM3892OHOH73090.07920.31327.6121.0032.09OHETATM3893OHOH73180.93022.1589.7641.0049.58OHETATM3894OHOH73267.09547.11620.8791.0049.75OHETATM3895OHOH733154.00547.58216.9841.0047.08OHETATM3896OHOH73493.49743.75922.4601.0036.22OHETATM3897OHOH735123.97516.02820.6911.0041.90OHETATM3898OHOH736138.14319.6926.3941.0036.56OHETATM3899OHOH73769.25228.06224.5611.0035.33OHETATM3900OHOH73888.97540.95116.5661.0030.91OHETATM3901OHOH73982.59424.01923.4961.0028.76OHETATM3902OHOH740142.67928.76514.4611.0037.71OHETATM3903OHOH741163.31538.75016.0381.0032.52OHETATM3904OHOH742140.47720.04910.6071.0039.02OHETATM3905OHOH74363.82226.62638.9931.0046.07OHETATM3906OHOH744155.84647.01213.0061.0039.84OHETATM3907OHOH745102.33921.432−1.5411.0065.06OHETATM3908OHOH746131.50440.36415.8351.0059.13OHETATM3909OHOH747132.51738.68819.0281.0036.09OHETATM3910OHOH748140.27236.15717.3981.0032.62OHETATM3911OHOH749145.02727.73413.1921.0030.23OHETATM3912OHOH750165.14539.3934.1381.0030.48OHETATM3913OHOH751149.28329.83221.0721.0034.58OHETATM3914OHOH752105.12216.94413.2111.0038.22OHETATM3915OHOH75399.52142.45910.1021.0035.81OHETATM3916OHOH754100.45040.94913.9861.0035.66OHETATM3917OHOH755108.93339.47322.7261.0044.20OHETATM3918OHOH75696.19919.26628.1271.0034.23OHETATM3919OHOH75798.86120.0134.5961.0036.98OHETATM3920OHOH75892.36935.71536.4731.0022.87OHETATM3921OHOH75984.12446.24316.8591.0046.81OHETATM3922OHOH760108.20440.6165.0661.0035.36OHETATM3923OHOH76193.50815.92921.1321.0036.61OHETATM3924OHOH76281.98035.32035.4821.0036.35OHETATM3925OHOH763140.23131.504−2.6681.0045.36OHETATM3926OHOH764103.51141.51718.3641.0041.85OHETATM3927OHOH76594.86620.22734.1491.0052.60OHETATM3928OHOH76692.14419.9425.8301.0030.00OHETATM3929OHOH76792.49344.76520.1321.0033.65OHETATM3930OHOH76875.82925.02423.4951.0037.74OHETATM3931OHOH769106.63013.65912.9561.0028.74OHETATM3932OHOH770151.37535.33921.8071.0044.52OHETATM3933OHOH771135.68225.7590.7581.0029.89OHETATM3934OHOH772152.82921.5785.8561.0036.44OHETATM3935OHOH77357.46441.46421.0701.0043.85OHETATM3936OHOH774139.89422.6733.4371.0028.84OHETATM3937OHOH775152.22646.9218.7201.0041.21OHETATM3938OHOH776109.85126.344−0.8181.0025.73OHETATM3939OHOH777165.14944.45612.1431.0038.51OHETATM3940OHOH778102.43518.84526.4271.0043.28OHETATM3941OHOH779100.11039.22916.7641.0031.02OHETATM3942OHOH78096.12917.75110.5891.0032.67OHETATM3943OHOH781131.01422.47721.4351.0042.25OHETATM3944OHOH782120.60415.44810.8011.0041.74OHETATM3945OHOH783163.46643.13515.3791.0046.48OHETATM3946OHOH784155.31745.30814.9921.0037.63OHETATM3947OHOH785150.23143.6787.0251.0046.11OHETATM3948OHOH786135.97220.07215.5471.0034.19OHETATM3949OHOH78785.51816.01328.7911.0034.72OHETATM3950OHOH788174.10837.91212.3161.0024.85OHETATM3951OHOH78961.09229.17343.2721.0031.17OHETATM3952OHOH79094.56928.60834.9771.0029.27OHETATM3953OHOH79174.23121.97332.9001.0050.90OHETATM3954OHOH792163.10435.04316.4411.0049.62OHETATM3955OHOH79388.90218.9028.0631.0029.96OHETATM3956OHOH794151.10337.44624.5131.0051.18OHETATM3957OHOH79570.94240.57718.4291.0039.55OHETATM3958OHOH796117.22031.09325.1821.0035.18OHETATM3959OHOH797110.20637.55924.7581.0032.16OHETATM3960OHOH79896.22515.83918.8081.0036.05OHETATM3961OHOH799113.51313.53512.7431.0043.83OHETATM3962OHOH800119.46132.0102.4901.0030.34OHETATM3963OHOH801162.42441.33717.3541.0036.07OHETATM3964OHOH802130.76122.3852.6921.0042.71OHETATM3965OHOH803121.91013.0548.7591.0048.96OHETATM3966OHOH804104.35517.0007.5781.0040.59OHETATM3967OHOH805148.59243.68610.4981.0038.17OHETATM3968OHOH806118.78633.8594.5801.0033.89OHETATM3969OHOH807121.31536.69816.4261.0030.64OHETATM3970OHOH808130.07028.16020.6741.0035.12OHETATM3971OHOH809130.54537.78221.8361.0045.09OHETATM3972OHOH810139.41029.13020.3081.0051.26OHETATM3973OHOH811150.22824.53119.2431.0036.32OHETATM3974OHOH812154.41826.49117.3871.0033.90OHETATM3975OHOH813155.13829.21419.8431.0044.59OHETATM3976OHOH814161.19228.68116.2931.0037.97OHETATM3977OHOH815167.54231.31715.8401.0047.80OHETATM3978OHOH816125.13828.0831.7101.0038.13OHETATM3979OHOH817115.71913.0051.7881.0047.10OHETATM3980OHOH818121.23117.0656.6621.0044.28OHETATM3981OHOH819148.45644.80515.4151.0052.81OHETATM3982OHOH820165.59732.63317.4891.0043.14OHETATM3983OHOH821162.65244.40011.6791.0041.81OHETATM3984OHOH822156.09244.4708.8051.0023.14OHETATM3985OHOH823151.41234.978−1.1771.0051.79OHETATM3986OHOH824146.29131.250−3.8111.0037.67OHETATM3987OHOH825146.65221.44612.9531.0029.77OHETATM3988OHOH826150.91421.63214.3301.0060.29OHETATM3989OHOH827147.76724.26415.6471.0037.90OHETATM3990OHOH828118.23922.19726.3361.0037.95OHETATM3991OHOH82963.71630.26247.0581.0022.34OHETATM3992OHOH830119.91338.53815.4781.0045.30OHETATM3993OHOH831111.31939.9539.4391.0026.28OHETATM3994OHOH832115.47542.29714.2321.0053.11OHETATM3995OHOH83392.73426.43135.9971.0043.59OHETATM3996OHOH83464.79854.40833.3231.0040.01OHETATM3997OHOH83573.05742.21519.4121.0036.23OHETATM3998OHOH83668.77241.71418.1861.0030.98OHETATM3999OHOH83764.28446.26022.8701.0033.08OHETATM4000OHOH83851.81946.80236.9721.0049.30OHETATM4001OHOH83961.81530.44149.4511.0025.71OHETATM4002OHOH840108.83330.0761.4731.0047.10OHETATM4003OHOH841152.52524.45415.4341.0034.70OHETATM4004OHOH842143.73942.75421.0231.0050.03OHETATM4005OHOH843149.17143.27913.6511.0038.57OHETATM4006OHOH844122.51034.7976.4761.0045.60OHETATM4007OHOH845143.68140.2447.0351.0039.12OHETATM4008OHOH846128.60916.21015.9791.0052.82OHETATM4009OHOH847147.97231.179−1.3051.0046.95OHETATM4010OHOH848150.69940.290−0.7411.0048.63OHETATM4011OHOH849152.28847.1322.6361.0054.66OHETATM4012OHOH850140.83620.5567.8511.0036.11OHETATM4013OHOH851145.79017.5836.0271.0048.50OHETATM4014OHOH852120.95121.86325.6321.0037.97OHETATM4015OHOH853126.46535.25819.9331.0044.79OHETATM4016OHOH85499.05026.09533.9491.0040.92OHETATM4017OHOH855101.57840.60117.4981.0042.01OHETATM4018OHOH85655.84031.04924.0841.0034.43OHETATM4019OHOH85754.57631.64921.8821.0037.29OHETATM4020OHOH858107.14738.14321.7771.0041.29OHETATM4021OHOH859105.90014.6197.1691.0035.18OHETATM4022OHOH860116.77016.25818.1551.0027.05OHETATM4023OHOH86169.22534.12414.7081.0033.72OHETATM4024OHOH862106.22919.2937.1051.0039.37OHETATM4025OHOH86377.22443.59732.8421.0040.57OHETATM4026OHOH864161.61745.5392.2731.0032.00OHETATM4027OHOH865161.92030.5711.6331.0031.06OHETATM4028OHOH866156.32724.68117.3701.0027.75OHETATM4029OHOH86796.18436.97815.1961.0041.87OHETATM4030OHOH86855.48025.73432.8791.0030.85OHETATM4031OHOH869106.58032.58925.6491.0034.75OHETATM4032OHOH87050.31240.61937.2931.0040.30OHETATM4033OHOH87161.88842.76946.6521.0033.46OHETATM4034OHOH872115.83318.45326.4681.0042.41OHETATM4035OHOH873117.28519.21928.3751.0051.17OHETATM4036OHOH874101.80126.9353.3291.0046.93OHETATM4037OHOH87572.83028.69818.6851.0039.82OHETATM4038OHOH876107.02520.94229.8561.0038.35OHETATM4039OHOH87777.24845.11722.6221.0033.37OHETATM4040OHOH878106.57520.0580.7841.0032.74OHETATM4041OHOH879113.14713.15215.2191.0041.45OHETATM4042OHOH880155.19624.18511.6501.0043.65OHETATM4043OHOH881154.33125.51513.6241.0032.54OHETATM4044OHOH882123.34638.13517.2291.0036.23OHETATM4045OHOH88352.76128.51836.3191.0040.91OHETATM4046OHOH88481.34034.43410.4561.0043.97OHETATM4047OHOH885164.64146.0491.6311.0040.97OHETATM4048OHOH886155.43721.3908.5381.0040.35OHETATM4049OHOH88763.91741.37150.0431.0039.24OHETATM4050OHOH888123.71032.17225.8321.0044.56OHETATM4051OHOH88958.71549.68238.9881.0047.00OHETATM4052OHOH890104.23014.5529.2311.0038.00OHETATM4053OHOH89189.12124.4533.2181.0044.48OHETATM4054OHOH89289.96322.1122.7151.0052.95OHETATM4055OHOH89380.30934.12337.1591.0041.56OHETATM4056OHOH89450.82042.13727.5171.0045.59OHETATM4057OHOH895132.40022.2174.4001.0033.87OHETATM4058OHOH896133.07319.59516.0211.0048.75OHETATM4059OHOH89760.29942.00149.5561.0044.94OHETATM4060OHOH898148.45322.26214.6491.0044.77OHETATM4061OHOH89981.57624.2018.3231.0069.20OHETATM4062OHOH90076.49426.18521.2001.0041.15OHETATM4063OHOH901110.52933.37226.3951.0039.74OHETATM4064OHOH90287.37343.06431.9081.0045.67OHETATM4065OHOH90380.82219.17424.9981.0048.54OHETATM4066OHOH904114.48616.48026.3131.0052.76OHETATM4067OHOH905102.66816.75924.6641.0033.84OHETATM4068OHOH90681.39522.73521.3531.0054.24OHETATM4069OHOH90792.26612.49817.0101.0041.25OHETATM4070OHOH908140.56622.48417.8741.0041.09OHETATM4071OHOH909108.74726.84027.7881.0037.32OHETATM4072OHOH91065.58229.27521.9571.0047.66OHETATM4073OHOH911105.92414.76521.3311.0030.45OHETATM4074OHOH91261.80538.63316.9171.0042.23OHETATM4075OHOH91371.33051.91224.0921.0050.84OHETATM4076OHOH91487.61239.99630.6921.0043.06OHETATM4077OHOH91576.32038.31812.9471.0049.95OHETATM4078OHOH91663.60626.20320.1931.0044.91OHETATM4079OHOH917128.92724.8252.7151.0037.40OHETATM4080OHOH918164.44024.9886.0341.0048.18OHETATM4081OHOH919158.91946.59612.2051.0041.72OHETATM4082OHOH920166.34344.6081.1071.0044.66OHETATM4083OHOH92163.77228.48718.8261.0044.56OHETATM4084OHOH92294.23913.85617.4941.0051.75OHETATM4085OHOH923112.64213.76429.7721.0053.93OHETATM4086OHOH924105.52826.3073.4121.0044.89OHETATM4087OHOH925112.57425.37428.4941.0046.08OHETATM4088OHOH926159.00247.2971.9941.0030.69OHETATM4089OHOH927168.73825.30712.1731.0047.73OHETATM4090OHOH928130.80215.54111.9981.0041.37OHETATM4091OHOH929125.65730.3491.5361.0048.67OHETATM4092OHOH93052.87840.90835.1371.0039.90OHETATM4093OHOH931173.40434.5148.7861.0045.88OHETATM4094OHOH932174.03832.2074.5161.0050.98OHETATM4095OHOH93358.94823.81539.0141.0048.58OHETATM4096OHOH934171.14125.82610.1921.0043.72OHETATM4097OHOH935138.81617.1146.2391.0051.73OHETATM4098OHOH93657.70330.55442.2471.0038.78OHETATM4099OHOH93773.18626.59227.7371.0041.12OHETATM4100OHOH938114.78641.33811.6051.0036.01OHETATM4101OHOH939112.71111.09510.1601.0029.76OHETATM4102OHOH940104.81324.02030.9841.0033.95OHETATM4103OHOH94159.40535.93816.8591.0046.75OHETATM4104OHOH94280.58644.46216.7301.0050.32OHETATM4105OHOH94395.24217.44220.2881.0048.12OHETATM4106OHOH944118.32913.40611.6591.0048.74OHETATM4107OHOH945102.78325.22634.7761.0056.86OHETATM4108OHOH94681.54848.31917.3581.0047.92OHETATM4109OHOH947111.45739.0654.7261.0044.11OHETATM4110OHOH948112.73939.7096.9311.0029.09OHETATM4111OHOH949133.43140.64211.1241.0034.53OHETATM4112OHOH950154.87731.26221.0081.0033.91OHETATM4113OHOH951124.15730.842−0.3201.0045.25OHETATM4114OHOH95279.25024.96935.2081.0037.33OHETATM4115OHOH95360.26026.41639.3041.0041.17OHETATM4116OHOH954144.35821.13314.0311.0046.73OHETATM4117OHOH95577.92535.18438.5551.0041.95OHETATM4118OHOH956164.91623.85210.1921.0049.14OHETATM4119OHOH95797.62219.48310.8771.0039.78OHETATM4120OHOH958154.79145.83310.7941.0041.16OHETATM4121OHOH959166.08630.4800.9031.0041.69OHETATM4122OHOH96070.53926.74026.8491.0037.97OHETATM4123OHOH96156.10343.12025.9161.0038.96OHETATM4124OHOH962149.86127.279−0.4551.0041.71OHETATM4125OHOH96359.43529.71520.9951.0034.53OHETATM4126OHOH964150.22726.12916.9901.0037.54OHETATM4127OHOH965133.29217.4374.0001.0039.92OHETATM4128OHOH966123.89614.40817.4401.0041.00OHETATM4129OHOH96751.06234.61720.3681.0041.20OHETATM4130OHOH968120.38037.55922.8711.0040.73OHETATM4131OHOH969126.20822.12725.5611.0045.32OHETATM4132OHOH970147.06123.5152.6631.0043.25OHETATM4133OHOH97181.18424.88638.2841.0041.16OHETATM4134OHOH97286.92421.73932.0711.0038.90OHETATM4135OHOH97377.13947.10730.4091.0040.17OHETATM4136OHOH974143.22634.62218.4131.0040.67OHETATM4137OHOH97549.42041.35032.0031.0045.02OHETATM4138OHOH976140.80640.1442.7371.0038.01OHETATM4139OHOH97761.97726.44536.5281.0039.65OHETATM4140OHOH978132.59628.11522.4441.0045.78OHETATM4141OHOH97989.59421.3095.5941.0043.15OHETATM4142OHOH980136.53327.24018.8591.0038.68OHETATM4143OHOH98181.63645.58120.5091.0038.28OHETATM4144OHOH982150.17623.1251.8281.0042.74OHETATM4145OHOH983102.46717.4465.5001.0041.73OHETATM4146OHOH98471.89154.91033.9321.0049.74OHETATM4147OHOH98584.86935.36011.3581.0040.38OHETATM4148OHOH986142.65336.2310.1851.0043.33OCONECT10441375CONECT13751044CONECT366536663716CONECT3666366536673710CONECT366736663711CONECT366836693717CONECT366936683709CONECT36703709CONECT36713709CONECT36723709CONECT3673367437113712CONECT367436733675CONECT367536743676CONECT367636753677CONECT367736763678CONECT367836773679CONECT367936783680CONECT368036793681CONECT368136803682CONECT368236813683CONECT368336823684CONECT368436833685CONECT368536843686CONECT368636853687CONECT368736863688CONECT368836873689CONECT368936883690CONECT36903689CONECT3691369237103713CONECT369236913693CONECT369336923694CONECT369436933695CONECT369536943696CONECT369636953697CONECT369736963698CONECT369836973699CONECT369936983700CONECT370036993701CONECT370137003702CONECT370237013703CONECT370337023704CONECT370437033705CONECT370537043706CONECT370637053707CONECT370737063708CONECT37083707CONECT37093669367036713672CONECT371036663691CONECT371136673673CONECT37123673CONECT37133691CONECT37143718CONECT37153718CONECT371636653718CONECT371736683718CONECT37183714371537163717CONECT37193720CONECT3720371937213758CONECT372137203759CONECT3722372337593760CONECT372337223724CONECT372437233725CONECT372537243726CONECT372637253727CONECT372737263728CONECT372837273729CONECT372937283730CONECT373037293731CONECT373137303732CONECT373237313733CONECT373337323734CONECT373437333735CONECT373537343736CONECT373637353737CONECT373737363738CONECT373837373739CONECT37393738CONECT3740374137583761CONECT374137403742CONECT374237413743CONECT374337423744CONECT374437433745CONECT374537443746CONECT374637453747CONECT374737463748CONECT374837473749CONECT374937483750CONECT375037493751CONECT375137503752CONECT375237513753CONECT375337523754CONECT375437533755CONECT375537543756CONECT375637553757CONECT37573756CONECT375837203740CONECT375937213722CONECT37603722CONECT37613740MASTER323021223006414719936END

[0243]

9

HEADER

ANTIBIOTIC 25-APR-00 1EWF

TITLE

THE 1.7 ANGSTROM CRYSTAL STRUCTURE OF BPI

COMPND

MOL_ID: 1;

COMPND
2
MOLECULE: BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN;

COMPND
3
CHAIN: A;

COMPND
4
SYNONYM: BPI;

COMPND
5
ENGINEERED: YES;

COMPND
6
MUTATION: YES

SOURCE

MOL_ID: 1;

SOURCE
2
ORGANISM_SCIENTIFIC: HOMO SAPIENS;

SOURCE
3
ORGANISM_COMMON: HUMAN;

SOURCE
4
EXPRESSION_SYSTEM: CRICETULUS GRISEUS;

SOURCE
5
EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;

SOURCE
6
EXPRESSION_SYSTEM_CELL: OVARY CELLS

KEYWDS

BACTERICIDAL, PERMEABILITY-INCREASING, LIPID-BINDING,

KEYWDS
2
LIPOPOLYSACCHARIDE-BINDING, ANTIBIOTIC

EXPDTA

X-RAY DIFFRACTION

AUTHOR

G. KLEIGER, L. J. BEAMER, R. GROTHE, P. MALLICK, D. EISENBERG

REVDAT
1
21-JUN-00
1EWF
0

JRNL

AUTH G. KLEIGER, L. J. BEAMER, R. GROTHE, P. MALLICK, D. EISENBERG

JRNL

TITL THE 1.7 ANGSTROM CRYSTAL STRUCTURE OF BPI: A STUDY

JRNL

TITL 2 OF HOW TWO DISSIMILAR AMINO ACID SEQUENCES CAN

JRNL

TITL 3 ADOPT THE SAME FOLD.

JRNL

REF J. MOL. BIOL. V. 299 1019 2000

JRNL

REFN ASTM JMOBAK UK ISSN 0022-2836

REMARK
1

REMARK
1
REFERENCE 1

REMARK
1
AUTH
L. J. BEAMER, S. F. CARROLL, D. EISENBERG

REMARK
1
TITL
CRYSTAL STRUCTURE OF HUMAN BPI AND TWO BOUND

REMARK
1
TITL 2
PHOSPHOLIPIDS AT 2.4 ANGSTROM RESOLUTION

REMARK
1
REF
SCIENCE
V. 276
1861
1997

REMARK
1
REFN ASTM SCIEAS US ISSN 0036-8075

REMARK
2

REMARK
2
RESOLUTION. 1.70 ANGSTROMS.

REMARK
3

REMARK
3
REFINEMENT.

REMARK
3
PROGRAM
CNS

REMARK
3
AUTHORS
BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE-

REMARK
3

KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU,

REMARK
3

READ, RICE, SIMONSON, WARREN

REMARK
3

REMARK
3
REFINEMENT TARGET
ENGH & HUBER

REMARK
3

REMARK
3
DATA USED IN REFINEMENT.

REMARK
3
RESOLUTION RANGE HIGH (ANGSTROMS)
1.70

REMARK
3
RESOLUTION RANGE LOW (ANGSTROMS)
50.00

REMARK
3
DATA CUTOFF (SIGMA(F))
0.000

REMARK
3
OUTLIER CUTOFF HIGH (RMS(ABS(F)))
NULL

REMARK
3
COMPLETENESS (WORKING + TEST) (%)
94.2

REMARK
3
NUMBER OF REFLECTIONS
47197

REMARK
3

REMARK
3

REMARK
3
FIT TO DATA USED IN REFINEMENT.

REMARK
3
CROSS-VALIDATION METHOD
NULL

REMARK
3
FREE R VALUE TEST SET SELECTION
RANDOM SELECTION OF

REMARK
3

10 PERCENT OF ALL DATA

REMARK
3
R VALUE (WORKING SET)
0.198

REMARK
3
FREE R VALUE
0.250

REMARK
3
FREE R VALUE TEST SET SIZE (%)
NULL

REMARK
3
FREE R VALUE TEST SET COUNT
4755

REMARK
3
ESTIMATED ERROR OF FREE R VALUE
NULL

REMARK
3

REMARK
3
FIT IN THE HIGHEST RESOLUTION BIN.

REMARK
3
TOTAL NUMBER OF BINS USED
NULL

REMARK
3
BIN RESOLUTION RANGE HIGH (A)
NULL

REMARK
3
BIN RESOLUTION RANGE LOW (A)
NULL

REMARK
3
BIN COMPLETENESS (WORKING + TEST)

(%)
NULL

REMARK
3
REFLECTIONS IN BIN (WORKING SET)
NULL

REMARK
3
BIN R VALUE (WORKING SET)
NULL

REMARK
3
BIN FREE R VALUE
NULL

REMARK
3
BIN FREE R VALUE TEST SET SIZE (%)
NULL

REMARK
3
BIN FREE R VALUE TEST SET COUNT
NULL

REMARK
3
ESTIMATED ERROR OF BIN FREE R VALUE
NULL

REMARK
3

REMARK
3
NUMBER OF NON-HYDROGEN ATOMS

USED IN REFINEMENT.

REMARK
3
PROTEIN ATOMS
3663

REMARK
3
NUCLEIC ACID ATOMS
0

REMARK
3
HETEROGEN ATOMS
97

REMARK
3
SOLVENT ATOMS
387

REMARK
3

REMARK
3
B VALUES.

REMARK
3
FROM WILSON PLOT (A**2)
24.00

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

REMARK
3
OVERALL ANISOTROPIC B VALUE.

REMARK
3
B11 (A**2)
NULL

REMARK
3
B22 (A**2)
NULL

REMARK
3
B33 (A**2)
NULL

REMARK
3
B12 (A**2)
NULL

REMARK
3
B13 (A**2)
NULL

REMARK
3
B23 (A**2)
NULL

REMARK
3

REMARK
3
ESTIMATED COORDINATE ERROR.

REMARK
3
ESD FROM LUZZATI PLOT (A)
NULL

REMARK
3
ESD FROM SIGMAA (A)
NULL

REMARK
3
LOW RESOLUTION CUTOFF (A)
NULL

REMARK
3

REMARK
3
CROSS-VALIDATED ESTIMATED

COORDINATE ERROR.

REMARK
3
ESD FROM C-V LUZZATI PLOT (A)
NULL

REMARK
3
ESD FROM C-V SIGMAA (A)
NULL

REMARK
3

REMARK
3
RMS DEVIATIONS FROM IDEAL VALUES.

REMARK
3
BOND LENGTHS (A)
0.017

REMARK
3
BOND ANGLES (DEGREES)
2.00

REMARK
3
DIHEDRAL ANGLES (DEGREES)
NULL

REMARK
3
IMPROPER ANGLES (DEGREES)
NULL

REMARK
3

REMARK
3
ISOTROPIC THERMAL MODEL
NULL

REMARK
3

REMARK
3
ISOTROPIC THERMAL FACTOR RESTRAINTS.
RMS
SIGMA

REMARK
3
MAIN-CHAIN BOND (A**2)
NULL
NULL

REMARK
3
MAIN-CHAIN ANGLE (A**2)
NULL
NULL

REMARK
3
SIDE-CHAIN BOND (A**2)
NULL
NULL

REMARK
3
SIDE-CHAIN ANGLE (A**2)
NULL
NULL

REMARK
3

REMARK
3

REMARK
3
BULK SOLVENT MODELING.

REMARK
3
METHOD USED
NULL

REMARK
3
KSOL
NULL

REMARK
3
BSOL
NULL

REMARK
3

REMARK
3
NCS MODEL
NULL

REMARK
3

REMARK
3
NCS RESTRAINTS.
RMS
SIGMA/WEIGHT

REMARK
3
GROUP 1 POSITIONAL (A)
NULL
NULL

REMARK
3
GROUP 1 B-FACTOR (A**2)
NULL
NULL

REMARK
3

REMARK
3
PARAMETER FILE 1
NULL

REMARK
3
TOPOLOGY FILE 1
NULL

REMARK
3

REMARK
3
OTHER REFINEMENT REMARKS
NULL

REMARK
4

REMARK
4
1EWF COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998

REMARK
6

REMARK
6
ELECTRON DENSITY WAS MISSING OR DIFFUSE FOR THE

REMARK
6
ATOMS LISTED IN REMARK 470.

REMARK
100

REMARK
100
THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-2000.

REMARK
100
THE RCSB ID CODE IS RCSB010960.

REMARK
200

REMARK
200
EXPERIMENTAL DETAILS

REMARK
200
EXPERIMENT TYPE
X-RAY DIFFRACTION

REMARK
200
DATE OF DATA COLLECTION
06-FEB-1998

REMARK
200
TEMPERATURE (KELVIN)
93.0

REMARK
200
PH
6.80

REMARK
200
NUMBER OF CRYSTALS USED
1

REMARK
200

REMARK
200
SYNCHROTRON (Y/N)
Y

REMARK
200
RADIATION SOURCE
NSLS

REMARK
200
BEAMLINE
X12B

REMARK
200
X-RAY GENERATOR MODEL
NULL

REMARK
200
MONOCHROMATIC OR LAUE (M/L)
M

REMARK
200
WAVELENGTH OR RANGE (A)
0.975

REMARK
200
MONOCHROMATOR
NULL

REMARK
200
OPTICS
NULL

REMARK
200

REMARK
200
DETECTOR TYPE
CCD

REMARK
200
DETECTOR MANUFACTURER
QUANTUM IV

REMARK
200
INTENSITY - INTEGRATION SOFTWARE
DENZO

REMARK
200
DATA SCALING SOFTWARE
SCALEPACK

REMARK
200

REMARK
200
NUMBER OF UNIQUE REFLECTIONS
47198

REMARK
200
RESOLUTION RANGE HIGH (A)
1.700

REMARK
200
RESOLUTION RANGE LOW (A)
100.000

REMARK
200
REJECTION CRITERIA (SIGMA(I))
−3.000

REMARK
200

REMARK
200
OVERALL.

REMARK
200
COMPLETENESS FOR RANGE (%)
94.2

REMARK
200
DATA REDUNDANCY
2.300

REMARK
200
R MERGE (I)
0.04800

REMARK
200
R SYM (I)
NULL

REMARK
200
<I/SIGMA(I)> FOR THE DATA SET
16.7000

REMARK
200

REMARK
200
IN THE HIGHEST RESOLUTION SHELL.

REMARK
200
HIGHEST RESOLUTION SHELL, RANGE HIGH (A)
1.70

REMARK
200
HIGHEST RESOLUTION SHELL, RANGE LOW (A)
1.76

REMARK
200
COMPLETENESS FOR SHELL (%)
67.0

REMARK
200
DATA REDUNDANCY IN SHELL
1.30

REMARK
200
R MERGE FOR SHELL (I)
0.20100

REMARK
200
R SYM FOR SHELL (I)
NULL

REMARK
200
<I/SIGMA(I)> FOR SHELL
NULL

REMARK
200

REMARK
200
DIFFRACTION PROTOCOL
SINGLE WAVELENGTH

REMARK
200
METHOD USED TO DETERMINE THE STRUCTURE
NULL

REMARK
200
SOFTWARE USED
X-PLOR

REMARK
200
STARTING MODEL
NULL

REMARK
200

REMARK
200
REMARK
NULL

REMARK
280

REMARK
280
CRYSTAL

REMARK
280
SOLVENT CONTENT, VS (%)
NULL

REMARK
280
MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA)
NULL

REMARK
280

REMARK
280
CRYSTALLIZATION CONDITIONS
12% PEG 6000, 0.2 M MG

REMARK
280
ACETATE, 0.1 M NA CACODYLATE, PH 6.8

REMARK
290

REMARK
290
CRYSTALLOGRAPHIC SYMMETRY

REMARK
290
SYMMETRY OPERATORS FOR SPACE GROUP C 1 2 1

REMARK
290

REMARK
290
SYMOP
SYMMETRY

REMARK
290
NNNMMM
OPERATOR

REMARK
290
1555
X,Y,Z

REMARK
290
2555
−X,Y,−Z

REMARK
290
3555
1/2 + X, 1/2 + Y, Z

REMARK
290
4555
1/2 − X, 1/2 + Y, −Z

REMARK
290

REMARK
290
WHERE NNN -> OPERATOR NUMBER

REMARK
290
MMM -> TRANSLATION VECTOR

REMARK
290

REMARK
290
CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS

REMARK
290
THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM

REMARK
290
RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY

REMARK
290
RELATED MOLECULES.

REMARK
290
SMTRY1
1
1.000000
0.000000
0.000000
0.00000

REMARK
290
SMTRY2
1
0.000000
1.000000
0.000000
0.00000

REMARK
290
SMTRY3
1
0.000000
0.000000
1.000000
0.00000

REMARK
290
SMTRY1
2
−1.000000
0.000000
0.000000
0.00000

REMARK
290
SMTRY2
2
0.000000
1.000000
0.000000
0.00000

REMARK
290
SMTRY3
2
0.000000
0.000000
−1.000000
0.00000

REMARK
290
SMTRY1
3
1.000000
0.000000
0.000000
92.16000

REMARK
290
SMTRY2
3
0.000000
1.000000
0.000000
15.61500

REMARK
290
SMTRY3
3
0.000000
0.000000
1.000000
0.00000

REMARK
290
SMTRY1
4
−1.000000
0.000000
0.000000
92.16000

REMARK
290
SMTRY2
4
0.000000
1.000000
0.000000
15.61500

REMARK
290
SMTRY3
4
0.000000
0.000000
−1.000000
0.00000

REMARK
290

REMARK
290
REMARK
NULL

REMARK
300

REMARK
300
BIOMOLECULE
1

REMARK
300
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT

REMARK
300
WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR

REMARK
300
INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).

REMARK
350

REMARK
350
GENERATING THE BIOMOLECULE

REMARK
350
COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN

REMARK
350
BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE

REMARK
350
MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS

REMARK
350
GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND

REMARK
350
CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.

REMARK
350

REMARK
350
BIOMOLECULE 1

REMARK
350
APPLY THE FOLLOWING TO CHAINS: A

REMARK
350
BIOMT1
1
1.000000
0.000000
0.000000
0.00000

REMARK
350
BIOMT2
1
0.000000
1.000000
0.000000
0.00000

REMARK
350
BIOMT3
1
0.000000
0.000000
1.000000
0.00000

REMARK
470

REMARK
470
MISSING ATOM

REMARK
470
THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M = MODEL NUMBER;

REMARK
470
RES = RESIDUE NAME; C = CHAIN IDENTIFIER; SSEQ = SEQUENCE NUMBER;

REMARK
470
I = INSERTION CODE):

REMARK
470
M RES CSSEQI ATOMS

REMARK
470
VAL
A
1
CG1
CG2

REMARK
470
LYS
A
33
CG
CD
CE
NZ

REMARK
470
LYS
A
44
CG
CD
CE
NZ

REMARK
470
HIS
A
45
CG
ND1
CD2
CE1
NE2

REMARK
470
LYS
A
86
CD
CE
NZ

REMARK
470
LYS
A
95
CG
CD
CE
NZ

REMARK
470
LYS
A
99
CG
CD
CE
NZ

REMARK
470
LYS
A
118
CG
CD
CE
NZ

REMARK
470
ASN
A
232
CG
OD1
ND2

REMARK
470
HIS
A
233
CG
ND1
CD2
CE1
NE2

REMARK
470
HIS
A
234
CG
ND1
CD2
CE1
NE2

REMARK
470
ASN
A
235
CG
OD1
ND2

REMARK
500

REMARK
500
GEOMETRY AND STEREOCHEMISTRY

REMARK
500
SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT

REMARK
500

REMARK
500
THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.

REMARK
500

REMARK
500
ATM1
RES
C
SSEQI
ATM2
RES
C
SSEQI

REMARK
500
O
HOH

626
O
HOH

774
2.07

REMARK
500
N
ASN
A
82
O
HOH

665
2.09

REMARK
500
O
HOH

609
O
HOH

823
2.12

REMARK
500
O
HOH

855
O
HOH

779
2.14

REMARK
500
O
HOH

870
O
PRO
A
303
2.15

REMARK
500
O
LEU
A
302
O
HOH

930
2.17

REMARK
500
O
HOH

906
O
HOH

700
2.19

REMARK
500

REMARK
500
GEOMETRY AND STEREOCHEMISTRY

REMARK
500
SUBTOPIC: COVALENT BOND LENGTHS

REMARK
500

REMARK
500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES

REMARK
500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE

REMARK
500
THAN 6 * RMSD (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN

REMARK
500
IDENTIFIER; SSEQ = SEQUENCE NUMBER; I = INSERTION CODE).

REMARK
500

REMARK
500
STANDARD TABLE:

REMARK
500
FORMAT: (10X, I3, 1X, 2 (A3, 1X, A1, I4, A1, 1X, A4, 3X), F6.3)

REMARK
500

REMARK
500
EXPECTED VALUES: ENGH AND HUBER, 1991

REMARK
500

REMARK
500
M RES C SSEQI ATM1 RES C SSEQI ATM2 DEVIATION

REMARK
500

MET
A
70
CE
MET
A
70
SD
−0.230

REMARK
500

MET
A
170
CE
MET
A
170
SD
−0.130

REMARK
500

VAL
A
269
CG1
VAL
A
269
CB
0.103

REMARK
500

MET
A
278
CE
MET
A
278
SD
−0.119

REMARK
500

MET
A
405
CE
MET
A
405
SD
−0.192

REMARK
500

REMARK
500
GEOMETRY AND STEREOCHEMISTRY

REMARK
500
SUBTOPIC: COVALENT BOND ANGLES

REMARK
500

REMARK
500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES

REMARK
500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE

REMARK
500
THAN 6 * RMSD (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN

REMARK
500
IDENTIFIER; SSEQ = SEQUENCE NUMBER; I = INSERTION CODE).

REMARK
500

REMARK
500
STANDARD TABLE:

REMARK
500
FORMAT: (10X, I3, 1X, A3, 1X, A1, I4, A1, 3 (1X, A4, 2X), (12X, F5.1)

REMARK
500

REMARK
500
EXPECTED VALUES: ENGH AND HUBER, 1991

REMARK
500

REMARK
500
M
RES
C
SSEQI
ATM1
ATM2
ATM3

REMARK
500
LYS
A
42
N
CA
C
ANGL. DEV. = −15.2 DEGREES

REMARK
500
LYS
A
44
N
CA
C
ANGL. DEV. = 18.4 DEGREES

REMARK
500
HIS
A
45
N
CA
C
ANGL. DEV. = −27.6 DEGREES

REMARK
500
HIS
A
45
C
N
CA
ANGL. DEV. = 12.1 DEGREES

REMARK
500
GLY
A
47
N
CA
C
ANGL. DEV. = 17.7 DEGREES

REMARK
500
LYS
A
48
N
CA
C
ANGL. DEV. = 20.9 DEGREES

REMARK
500
GLY
A
49
N
CA
C
ANGL. DEV. = 28.6 DEGREES

REMARK
500
SER
A
81
N
CA
C
ANGL. DEV. = 14.5 DEGREES

REMARK
500

REMARK
500
GEOMETRY AND STEREOCHEMISTRY

REMARK
500
SUBTOPIC: TORSION ANGLES

REMARK
500

REMARK
500
TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:

REMARK
500
(M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN IDENTIFIER;

REMARK
500
SSEQ = SEQUENCE NUMBER; I = INSERTION CODE).

REMARK
500

REMARK
500
STANDARD TABLE:

REMARK
500
FORMAT: (10X, I3, 1X, A3, 1X, A1, I4, A1, 4X, F7.2, 3X, F7.2)

REMARK
500

REMARK
500
M
RES
C
SSEQI
PSI
PHI

REMARK
500
HIS
A
45
146.65
−9.33

REMARK
500
LEU
A
46
141.72
106.25

REMARK
500
ARG
A
96
59.46
−115.40

REMARK
600

REMARK
600
HETEROGEN

REMARK
600
THE HEAD GROUP OF PC2 577 IS MISSING IN THE ELECTRON

REMARK
600
DENSITY MAPS.

REMARK
900

REMARK
900
RELATED ENTRIES

REMARK
900
RELATED ID: 1BP1 RELATED DB: PDB

REMARK
900
CRYSTAL STRUCTURE OF HUMAN BPI AT ROOM TEMPERATURE

REMARK
999

REMARK
999
SEQUENCE

REMARK
999
A NATURALLY OCCURING POLYMORPHISM EXISTS AT RESIDUE

REMARK
999
185 FOR HUMAN BPI. THE CLONE USED FOR EXPRESSION

REMARK
999
OF BPI HAS GLU AT THIS POSITION, ALTHOUGH THE CLONE

REMARK
999
FOR THE SWISSPROT ENTRY HAS LYS AT THE SAME POSITION.

DBREF
1EWF
A
1
456
SWS
P17213
BPI_HUMAN
28
483

SEQADV
1EWF
GLU
A
185
SWS
P17213
LYS
212
SEE REMARK 999

SEQADV
1EWF
ALA
A
351
SWS
P17213
SER
378
ENGINEERED

SEQRES
1
A
456
VAL
ASN
PRO
GLY
VAL
VAL
VAL
ARG
ILE
SER
GLN
LYS
GLY

SEQRES
2
A
456
LEU
ASP
TYR
ALA
SER
GLN
GLN
GLY
THR
ALA
ALA
LEU
GLN

SEQRES
3
A
456
LYS
GLU
LEU
LYS
ARG
ILE
LYS
ILE
PRO
ASP
TYR
SER
ASP

SEQRES
4
A
456
SER
PHE
LYS
ILE
LYS
HIS
LEU
GLY
LYS
GLY
HIS
TYR
SER

SEQRES
5
A
456
PHE
TYR
SER
MET
ASP
ILE
ARG
GLU
PHE
GLN
LEU
PRO
SER

SEQRES
6
A
456
SER
GLN
ILE
SER
MET
VAL
PRO
ASN
VAL
GLY
LEU
LYS
PHE

SEQRES
7
A
456
SER
ILE
SER
ASN
ALA
ASN
ILE
LYS
ILE
SER
GLY
LYS
TRP

SEQRES
8
A
456
LYS
ALA
GLN
LYS
ARG
PHE
LEU
LYS
MET
SER
GLY
ASN
PHE

SEQRES
9
A
456
ASP
LEU
SER
ILE
GLU
GLY
MET
SER
ILE
SER
ALA
ASP
LEU

SEQRES
10
A
456
LYS
LEU
GLY
SER
ASN
PRO
THR
SER
GLY
LYS
PRO
THR
ILE

SEORES
11
A
456
THR
CYS
SER
SER
CYS
SER
SER
HIS
ILE
ASN
SER
VAL
HIS

SEQRES
12
A
456
VAL
HIS
ILE
SER
LYS
SER
LYS
VAL
GLY
TRP
LEU
ILE
GLN

SEQRES
13
A
456
LEU
PHE
HIS
LYS
LYS
ILE
GLU
SER
ALA
LEU
ARG
ASN
LYS

SEQRES
14
A
456
MET
ASN
SER
GLN
VAL
CYS
GLU
LYS
VAL
THR
ASN
SER
VAL

SEQRES
15
A
456
SER
SER
GLU
LEU
GLN
PRO
TYR
PHE
GLN
THR
LEU
PRO
VAL

SEQRES
16
A
456
MET
THR
LYS
ILE
ASP
SER
VAL
ALA
GLY
ILE
ASN
TYR
GLY

SEQRES
17
A
456
LEU
VAL
ALA
PRO
PRO
ALA
THR
THR
ALA
GLU
THR
LEU
ASP

SEQRES
18
A
456
VAL
GLN
MET
LYS
GLY
GLU
PHE
TYR
SER
GLU
ASN
HIS
HIS

SEQRES
19
A
456
ASN
PRO
PRO
PRO
PHE
ALA
PRO
PRO
VAL
MET
GLU
PHE
PRO

SEQRES
20
A
456
ALA
ALA
HIS
ASP
ARG
MET
VAL
TYR
LEU
GLY
LEU
SER
ASP

SEQRES
21
A
456
TYR
PHE
PHE
ASN
THR
ALA
GLY
LEU
VAL
TYR
GLN
GLU
ALA

SEQRES
22
A
456
GLY
VAL
LEU
LYS
MET
THR
LEU
ARG
ASP
ASP
MET
ILE
PRO

SEQRES
23
A
456
LYS
GLU
SER
LYS
PHE
ARG
LEU
THR
THR
LYS
PHE
PHE
GLY

SEQRES
24
A
456
THR
PHE
LEU
PRO
GLU
VAL
ALA
LYS
LYS
PHE
PRO
ASN
MET

SEQRES
25
A
456
LYS
ILE
GLN
ILE
HIS
VAL
SER
ALA
SER
THR
PRO
PRO
HIS

SEQRES
26
A
456
LEU
SER
VAL
GLN
PRO
THR
GLY
LEU
THR
PHE
TYR
PRO
ALA

SEORES
27
A
456
VAL
ASP
VAL
GLN
ALA
PHE
ALA
VAL
LEU
PRO
ASN
SER
ALA

SEQRES
28
A
456
LEU
ALA
SER
LEU
PHE
LEU
ILE
GLY
MET
HIS
THR
THR
GLY

SEQRES
29
A
456
SER
MET
GLU
VAL
SER
ALA
GLU
SER
ASN
ARG
LEU
VAL
GLY

SEQRES
30
A
456
GLU
LEU
LYS
LEU
ASP
ARG
LEU
LEU
LEU
GLU
LEU
LYS
HIS

SEQRES
31
A
456
SER
ASN
ILE
GLY
PRO
PHE
PRO
VAL
GLU
LEU
LEU
GLN
ASP

SEQRES
32
A
456
ILE
MET
ASN
TYR
ILE
VAL
PRO
ILE
LEU
VAL
LEU
PRO
ARG

SEQRES
33
A
456
VAL
ASN
GLU
LYS
LEU
GLN
LYS
GLY
PHE
PRO
LEU
PRO
THR

SEQRES
34
A
456
PRO
ALA
ARG
VAL
GLN
LEU
TYR
ASN
VAL
VAL
LEU
GLN
PRO

SEQRES
35
A
456
HIS
GLN
ASN
PHE
LEU
LEU
PHE
GLY
ALA
ASP
VAL
VAL
TYR

SEQRES
36
A
456
LYS

HET
PC2
577
54

HET
PC2
578
43

HETNAM
PC2
DI-STEAROYL-3-SN-PHOSPHATIDYLCHOLINE

FORMUL
2
PC2
2(C44 H89 N1 O8 P1 1 + )

FORMUL
4
HOH
*387(H2 O1)

HELIX
1
1
GLN
A
11
LYS
A
30
1
20

HELIX
2
2
LYS
A
148
LYS
A
150
5
3

HELIX
3
3
VAL
A
151
ILE
A
162
1
12

HELIX
4
4
ILE
A
162
GLU
A
185
1
24

HELIX
5
5
GLU
A
185
GLN
A
191
1
7

HELIX
6
6
ASP
A
260
ALA
A
273
1
14

HELIX
7
7
ASP
A
283
ILE
A
285
5
3

HELIX
8
8
THR
A
294
THR
A
300
1
7

HELIX
9
9
GLU
A
304
PHE
A
309
1
6

HELIX
10
10
PRO
A
397
LEU
A
400
5
4

HELIX
11
11
LEU
A
401
VAL
A
413
1
13

HELIX
12
12
VAL
A
413
GLY
A
424
1
12

SHEET
1
A
6
ALA
A
214
THR
A
215
0

SHEET
2
A
6
THR
A
219
MET
A
224
−1
N
ASP
A
221
O
ALA
A
214

SHEET
3
A
6
VAL
A
5
SER
A
10
−1
O
VAL
A
5
N
MET
A
224

SHEET
4
A
6
VAL
A
254
SER
A
259
−1
O
TYR
A
255
N
ARG
A
8

SHEET
5
A
6
PHE
A
446
TYR
A
455
−1
O
LEU
A
447
N
LEU
A
258

SHEET
6
A
6
VAL
A
433
HIS
A
443
−1
N
GLN
A
434
O
VAL
A
454

SHEET
1
B
9
TYR
A
37
SER
A
40
0

SHEET
2
B
9
HIS
A
50
GLN
A
62
−1
N
TYR
A
51
O
ASP
A
39

SHEET
3
B
9
GLY
A
75
LYS
A
95
−1
O
ASN
A
84
N
GLN
A
62

SHEET
4
B
9
SER
A
66
VAL
A
71
−1
O
GLN
A
67
N
SER
A
79

SHEET
5
B
9
GLY
A
75
LYS
A
95
−1
O
GLY
A
75
N
VAL
A
71

SHEET
6
B
9
LEU
A
98
ASN
A
122
−1
N
LEU
A
98
O
LYS
A
95

SHEET
7
B
9
LYS
A
127
HIS
A
138
−1
O
LYS
A
127
N
ASN
A
122

SHEET
8
B
9
LEU
A
98
ASN
A
122
−1
O
SER
A
112
N
HIS
A
138

SHEET
9
B
9
SER
A
141
HIS
A
145
−1
O
SER
A
141
N
GLU
A
109

SHEET
1
C
3
MET
A
196
LYS
A
198
0

SHEET
2
C
3
GLY
A
204
ASN
A
206
−1
O
ILE
A
205
N
THR
A
197

SHEET
3
C
3
GLU
A
227
TYR
A
229
−1
O
GLU
A
227
N
ASN
A
206

SHEET
1
D
5
LYS
A
277
ARG
A
281
0

SHEET
2
D
5
ILE
A
314
SER
A
319
−1
O
ILE
A
316
N
LEU
A
280

SHEET
3
D
5
ALA
A
338
VAL
A
346
−1
N
ASP
A
340
O
SER
A
319

SHEET
4
D
5
LEU
A
352
HIS
A
361
−1
N
ALA
A
353
O
ALA
A
345

SHEET
5
D
5
LEU
A
385
SER
A
391
−1
N
LEU
A
385
O
HIS
A
361

SSBOND
1
CYS
A
135
CYS
A
175

CRYST1
184.320
31.230
80.660
90.00
103.20
90.00
C 1 2 1
4

ORIGX1
1.000000
0.000000
0.000000
0.00000

ORIGX2
0.000000
1.000000
0.000000
0.00000

ORIGX3
0.000000
0.000000
1.000000
0.00000

SCALE1
0.005425
0.000000
0.001273
0.00000

SCALE2
0.000000
0.032020
0.000000
0.00000

SCALE3
0.000000
0.000000
0.012734
0.00000

EXAMPLE 5

b 3D-1D Environment Classes and Comparison of Structually Equivalent Positions in BPI Domains

[0244] Additional analyses were performed to compare N-terminal and C-terminal domains of BPI using 3D-1D environments to analyze environmentally conserved positions in the BPI alignment as a function of environment class, to analyze the structural roles of 3D-1D environmentally conserved positions with dissimilar residue with BPI domain alignment and to analyze the clustering of 3D-1D environmentally conserved positions in both the BPI fold and the lipid binding pockets. Initially, for these analyses, a structural and sequence alignment was done for the two BPI domains, which have substantially the same fold but different sequences and statistical analyses were performed.

[0245] Coordinates for residues 1 to 229 corresponding to the N-terminal domain of BPI and residues 251 to 456 corresponding to the C-terminal domain were used for rigid-body alignment of the two domains. The program Align_v2 was used for the superposition, which outputs a structure-based sequence alignment of the two domains [G. Cohen, et al., J. Mol. Biol., 190:593-604 (1986)]. All main-chain atoms were used for both the superposition and calculation of rmsd. Initially 173 positions were aligned by the program. Nine pairs had no structurally equivalent main-chain atoms within 5 Å and were not considered aligned. Therefore, the length of the entire BPI domain alignment is 164 positions.

[0246] Based on the results of the structural alignment of the N-terminal and C-terminal BPI domains, a sequence alignment was generated between the two domains [S. Benner et al., Prot. Eng. 7:1323 (1994)]. Conservation between the two domains was first examined at the residue level. A total of 21 pairs of residues are identical out of 164 aligned positions between the two domains, corresponding to a sequence identity of 13%. This level of sequence identity is significantly higher than would be expected for two independently generated random sequences of this length. The sequence identity is too low to allow sequence alignment methods to predict an alignment, and in fact the structural identity of the two domains was unsuspected prior to the 2.4 Å resolution structure.

[0247] To understand the fold identity of the two BPI domains in the absence of strong sequence similarity, positional similarities were examined using 3D-1D environment classes. 3D-1D profiles were generated for both the N-terminal domain and the C-terminal domain [J. Bowie, et al., Science, 253:164-170 (1991)]. The boundaries used for calculating environment classes are shown in Table 7. The secondary structure at each residue was characterized using the program DSSP [W. Kabsch and C. Sander, Biopolymers, 22:2577-2637 (1983)]. 3D-1D profiles and secondary structures were calculated in a similar manner for examples from the distant aligned protein structures (DAPS) database. The environments for each position in the two domains are shown on the structure-derived sequence alignment of the two domains.

10TABLE 7Area BuriedEnvironment Class(Å2)Fraction PolarH:B1E:B1C:B1Ab ≧ 114Fp ≦ 0.33H:B2E:B2C:B2Ab ≧ 1140.33 ≦ Fp ≦ 0.46H:B3E:B3C:B3Ab ≧ 1140.46 ≦ Fp ≦ 0.57 H:P1 E:P1 C:P1 40 ≦ Ab ≦ 1140.46 ≦ Fp ≦ 0.57 H:P2 E:P2 C:P2 40 ≦ Ab ≦ 1140.57 ≦ Fp ≦ 1.00H:E E:E C:E Ab ≦ 400.00 ≦ Fp ≦ 1.00Boundaries for area buried (Ab) and fraction of the area buried by polar atoms (Fp) used for defining 3D-1D environment classes. Each position defined by values of Ab and Fb can be occupied by a residue that is in helix (H), β-strand (E), or coil (C)

[0248] Structurally equivalent positions with similar environments were reasoned to have similar structural roles in each BPI domain. Of the 164 structurally aligned positions, 51 have identical 3D-1D environments, corresponding to 31% of the structurally equivalent positions in the BPI domain alignment. This level of conservation is highly significant relative to an alignment of two independently generated random profiles of this length.

[0249] The % residue identity expected from two independently generated random sequences of 164 residues was calculated. The expected frequency of matches or % identity is given by:

⟨ P ⟩ = \sum_{i = 1}^{m} p_{i}^{2}

[0250] where pi is the probability of observing a residue of type i at a given position in a random sequence and m is the number of residue types, which in the case of a sequence alignment is 20 amino acid residues. The standard deviation, σp, in the frequency of matches is:

σp={square root}{square root over (P(1−P)/N)}

[0251] where P is given above and N is the length of the alignment. Probabilities for each amino acid residue, as well as each environment class, were derived from the DAPS database.

[0252] The Z-score is given by:

Z
=(Pobs−<P>)/σp

[0253] where Pobs is the observed % identity for either residues or environment classes between N-terminal and C-terminal domains of BPI. <P> and σp are both given above. The Z-score for the sequence identity of the N-terminal and C-terminal domains in BPI is 3.6; higher than expected for independently generated random sequences. A Z-score of 12.9 was calculated for the corresponding conservation of the 3D-1D environments in the 164 structurally aligned positions in BPI. Again, this level of conservation is higher than expected for the alignment of two independently generated random profiles of this length.

[0254] The next analyses involved environmentally conserved positions in the BPI alignment as a function of environmental class. To further compare and contrast structural properties between N-terminal and C-terminal domains, three statistical properties were computed for each environment class based upon the structural alignment of BPI. For each environment class, the statistical significance of observing pairs of positions (brought together by the alignment) both belonging to a given environment class was assessed by computing a p-value. The p-value for a given environment class is the probability that one would observe at least as many matches for that class in a random alignment where M is the number of observed matches of that type in the BPI domain structural alignment. The p-value is given by the following equation:

p = \sum_{(X_{12} = M)}^{Min (X_{1}, X_{2})} \frac{(N - X_{1})! (N - X_{2})! X_{1}! X_{2}!}{(X_{1} - X_{12})! (X_{2} - X_{12}) (N - X_{1} - X_{2} + X_{12})! X_{12}! N!}

[0255] where X1 is the number of observations for a given environment class from the N-terminal domain, X2 is the number of observations for the same environment class for the C-terminal domain, and N is the total number of pairs in the alignment. Gaps are not considered. Several of the environment classes have low p-values, and therefore when they are paired in the domain alignment it is of statistical significance, and indicate correlation between the environments of structurally aligned positions. P-values for each environment class are shown in Table 8.

11TABLE 8Log-Odds And Fractional Weighted Log-Odds (FWLO)Values For 3D-1D Environmental Classes (Env. Class)For The Alignment Of The N And C-Terminal DomainsOf BPI And For All Alignments FromThe DAPS DatabaseBPIDAPSEnv.databaseClassP-valueLog-oddsFWLOLog-oddsFWLOH:E5 × 10−21.70.051.40.03H:P22 × 10−82.00.241.20.11H:P1NONONO1.00.06H:B3NONONO1.00.02H:B2NONONO1.00.02H:B13 × 10−63.10.171.50.16E:E2 × 10−21.40.062.10.01E:P21 × 10−51.00.201.90.05E:P11 × 10−10.90.041.30.04E:B3NONONO1.50.03E:B2NONONO1.30.03E:B18 × 10−61.30.191.70.23C:E1 × 10−11.10.031.40.07C:P22 × 10−10.90.020.90.06C:P1NONONO0.90.03C:B3NONONO1.00.02C:B2NONONO1.10.01C:B1NONONO1.30.02

[0256] Residues important for stabilizing the cores of proteins tend to be hydrophobic and buried in apolar environments, that is, in the B1 environment class (Table 7). A low p-value for B1-B1 pairs was expected because the structural role of residues that pack in the protein core tend to be conserved. The p-values for the H:B1 and E:B1 environment classes are 3×10−6 and 8×10−6, respectively. In other words, observation of at least as many H:B1 matches for the BPI domains in a random alignment is expected only three out of one million times. Thus, positions that belong to the H:B1 or E:B1 classes are observed more often than expected at random. Therefore these positions have conserved structural roles (Table 9).

[0257] Positions which belong to the P2 environment class tend to be solvent exposed at the protein's surface. We observed low p-values for the P2 class. The p-values for the H:P2 and E:P2 environment classes are 2×10−5 and 1×10−5, respectively, which are as low as the values shown above for the H:B1 and E:B1 classes. While the structural conservation of residues in the protein core is well documented, the conservation of residues on the surface of proteins is not as well described.

[0258] Second, the log-odds value for each environment class was calculated. The log-odds ratio for a given pair of environment classes is a measure of how likely it is that any given instance of an environment class is conserved in an alignment. Scores well above zero imply significance, whereas scores near zero imply that the observation is likely to occur when environments are paired randomly. The log-odds value, LO(e) is given by:

LO (e) = \log \frac{⌈ P_{AB} (e) ⌉}{P_{A} (e) P_{B} (e)}

[0259] where PAB(e) is the joint probability of observing environment class e at aligned positions in both sequence A (N-terminal domain) and B (C-terminal domain). PA(e) is the probability of observing the environment class in sequence A, while PB(e) is the probability of observing the same class in sequence B. Results of the analysis are shown in Table 8.

[0260] Lastly, the fractional weighted log-odds value (weighted by the joint probability), FWLO(e), was calculated for each environment class. This value is expressed as a fraction of the total weighted log-odds scores for all environment classes. The FWLO(e) value is given by:

FWLO (e) = \frac{⌈ LO (e) \times P_{AB} (e) ⌉}{\sum_{env classes} LO (e) \times P_{AB} (e)}

[0261] a given pair may have a positive LO(e), but if it occurs only rarely in the structural alignment, the FWLO(e) value will be low. Table 9 lists the LO(e) and FWLO(e) values for all identical environment pairs for both the N-terminal and C-terminal domains of BPI.

[0262] The H:P2, H:B1, E:P2 and E:B1 environment classes dominate the distribution of LO(e) and FWLO(e) values for each identical environment pair. Large LO(e) values are observed for other environment classes, such as H:E or E:E, but these are relatively rare in BPI and thus unlikely to be as important. This is reflected in the low FWLO(e) values for the H:E and E:E pairs. High FWLO(e) values are observed for the H:P2, H:B1, E:P2 and E:B1 environment classes and are expected play a dominant structural role in the BPI domain.

[0263] To examine whether the H:P2, H:B1, E:P2 and E:B1 environment classes had structural significance to proteins other than BPI, we analyzed proteins in the database of aligned protein structures (DAPS) [D. Rice & D. Eisenberg, J. Mol. Biol., 267:1026 (1997)]. DAPS contains 1074 structurally-derived sequence alignments between structurally homologous proteins with less than 25% sequence identity.

[0264] LO(e) and FWLO(e) values were calculated over all protein pairs in DAPS (Table 8). The H:P2, H:Bl and E:B1 residue environments had large LO(e) and FWLO(e) values. However, the FWLO(e) value for the E:P2 class is only slightly higher than values for several of the other environment classes. The importance of positions belonging the E:P2 environment class is not general and may be unique to the BPI domain.

[0265] For the next analyses, the structural roles of 3D-1D environmentally conserved positions with dissimilar residues in the BPI domain alignment were examined. Thirty-one of the 51 3D-1D environmentally conserved pairs from the BPI domain alignment have similar or identical residues, defined by a positive substitution score from the GONNET matrix [S. Benner et al., Prot. Eng. 7:1323-32 (1994)]. However, 20 structurally equivalent positions with conserved 3D-1D environments have dissimilar residues. The structural roles for residues at these 20 positions were characterized and their importance for stabilizing the BPI fold was determined.

[0266] The structural roles for 3D-1D environmentally conserved positions with dissimilar residues were compared by analyzing the tertiary interactions they form with other residues. Favorable contacts were analyzed, including hydrogen bonds, salt bridges, disulfide bonds, van der Waals interactions, or aromatic ring stacking. The similarity in the structural roles was determined for each pair in the alignment.

[0267] The structural roles for these pairs fall into three major categories: (i) conserved structuralroles; (ii) auxiliary structural roles; and (iii) different structural roles.

[0268] The structural roles for a pair of dissimilar residues are defined as conserved when a residue at position i in the N-terminal domain of BPI forms a tertiary interaction with residue j in the N-terminal domain, and residue i′ in the C-terminal domain forms a tertiary interaction with residue j′. Both residues i and i′ and j and j′ must be at structurally equivalent positions in the alignment for the structural roles to be defined as conserved. The type of tertiary interaction does not have to be the same (FIG. 8(a)).

[0269] In auxiliary structural roles, residue i forms a tertiary interaction with residue j in the N-terminal domain, and residue i′ in the C-terminal domain forms a tertiary interaction with residue k′. Residues i and i′ must occupy structurally equivalent positions, but residues j and k′ do not have to be aligned (FIG. 8(b)).

[0270] For different structural roles, residues i and i′ belong to the same environment class but one or both of the residues have no corresponding structural role, or one or both residues are involved in stabilizing the interface between the domains in the BPI structure rather than the domain itself (FIG. 8(c)). For example, either residue i or i′ is solvent exposed, or residue i from the N-terminal domain interacts with residue l′ from the C-terminal domain. A summary of the structural roles for the 20 pairs of dissimilar residues is given in Table 9.

12TABLE 9Classification Of The Structural Roles For Equivalent PositionsWith Conserved 3D-1D Environment Classes And Dissimilar ResidueTypes. Comparison Of Structural Roles For The N-Terminal (N)And C-Terminal (C) Domains Of BPIResidueN-terminal domainC-terminal domain(n)AtomStructural roleResidue (c)AtomStructural roleA. Conserved structural roles Ser79OGH bond to Ser69 OG throughTyr336OHH bond to Ser327 OGa water moleculeSer112OGH bond to bb carbonyl groupHis361CE1VdW with Leu385 CB andof His138 through a waterCD1moleculeAsp116OD2H bond to Ser134 OGSer365OGH bond to Lys380 NZThr219OG1H bond to Thr216 OG1Phe446—Ring stacking with His443B. Auxiliary structural rolesTyr16OHH bond to Gln20 NH2Thr265OG1H bond to bb carbonyl groupof Phe262Glu19NE2H bond to Gln20 OE1Leu268CG, CD1VdW with Glu272 CD andCGAsp36OD1H bond to bb amide of Ser55Thr294OG1H bond to bb amide group ofMet312Lys77NZSalt bridge to Asp116 OD1Thr334OG1H bond to Gln329 NE2Ala83CBVdW with Leu63 CD2 andVal339CG1VdW with Met360 CBIle 80 CG2Asn180ND2H bond to Ser184 OGPro415CB, CDVdW with Arg416 CZ andLeu414 CBSer184OGH bond to Asn 180 ND2Glu419OE2Salt bridge to Arg416 NH2Pro188—Solvent exposed;Lys423—Solvent exposedAsn206CGVdW with Lys225 CB andVal433CG1, CG2VdW with Val453 CG1CGVal222CG1VdW with Leu209 CG andPhe449CD1, CE1, CE2VdW with Leu440 CB andCD1CD1 and Val368 CG1Glu227OE1Salt bridge to Lys225 NZVal454CBVdW with Tyr436 CE1C. Different Structural RolesVal1—Solvent exposedAsp251OD1H bond with Arg252 NH1and Tyr255 OHLys12NZSalt bridge with Asp452 OD1Tyr261CG, CD1,VdW w/Pro241 CG, CDCD2, CE2,CZGly120—Solvent exposed;Ser369OGH bond to bb carbonyl groupof Ala370His138—Solvent exposedLeu385CB, CD1VdW with His361 CE1Thr215OGH bond to ordered waterPro442CB, CGVdW with Leu447 CD1.H bond, Hydrogen-bond interaction; VdW, a van der Waals interaction; backbone, bb

[0271] Four pairs of 3D-1D environmentally conserved positions with dissimilar residue types fall into the conserved structural roles category. FIG. 9 shows examples of pairs of 3D-1D environmentally conserved residues with dissimilar residues yet conserved structural roles from the BPI domain alignment. Residues and secondary structure elements from the N-terminal domain are blue; residues and secondary structure elements from the C-terminal are red. The relationship of the secondary structure elements to the entire BPI molecule is shown in FIG. 7(c). Hydrogen bonds are shown as broken lines between the hydrogen bond donor and acceptor atoms. For example, Ser79 and Tyr336 both belong to the E:P2 environment class, however the substitution of serine for tyrosine in the GONNET matrix [S. Benner et al., Prot. Eng. 7:1323 (1994)] is not favorable. The conserved structural roles of both Ser79 and Tyr336 are to stabilize the domain by connecting adjacent β-strands. These residues are located on β-strands 4 and 4′ respectively (see FIGS. 7(c) and 9(al )). Ser79 (N-terminal domain) forms a 2.7 Å hydrogen bond to a water molecule which is hydrogen bonded to Ser69, located on β-strand 3. The crystallographic temperature factor for this water molecule is 27 Å2 so it is well ordered. In the C-terminal domain, Tyr336 forms a 2.8 Å hydrogen bond to Ser327, which lies on β-strand 3′. Ser69 and Ser327 are also paired in the BPI domain alignment. Therefore, Ser79 and Tyr336 interact with structurally equivalent residues in their respective domains, conserving the structural role for these dissimilar residues.

[0272] A similar example involves Asp116 and Ser365, located on β-strands 5 and 5′, respectively (FIG. 9(b)). The conserved structural roles of Asp116 and Ser365 connect adjacent β-strands in their respective domains. Asp116 forms a 2.9 Å hydrogen bond to Ser134 on β-strand 6. Ser365 forms a 3.1 Å hydrogen bond to Lys380 O on β-strand 6′. Ser134 and Lys380 are paired in the BPI domain alignment.

[0273] Conserved structural roles do not necessarily involve identical tertiary interactions. For example, Thr219 and Phe446 are structurally equivalent residues with identical environment classes (E:P2). Thr219 forms a 2.7 Å hydrogen bond with Thr216 which stabilizes a tight turn from β-strand 8 to β-strand 9 (FIG. 9(c)). In the C-terminal domain, the aromatic ring of Phe446 is approximately 4 Å from the ring of His443. Ring stacking of phenylalanine and histidine residues has been shown to be an energetically favorable interaction [J. Mitchell et al., J. Mol. Biol., 239:315 (1994)]. Therefore, the interaction of Phe446 with His443 stabilizes a tight turn from β-strand 7′ to β-strand 8′, similar to the interaction found in the N-terminal domain.

[0274] Eleven 3D-1D environmentally conserved positions with dissimilar residue types have auxiliary structural roles in the BPI domains. The structural roles of these residue pairs are auxiliary because they help stabilize the fold, even though the structural roles are not strictly conserved. An example is Lys77 and Thr334, located in β-strand 4 and 4′ respectively (FIG. 7(c)). Lys77 forms a salt bridge with Asp116 located on β-strand 5. Thr334 forms a hydrogen bond to Gln329 located on β-strand 3′. These interactions still support the fold of each BPI domain by connecting adjacent β-strands.

[0275] Five of the 3D-1D environmentally conserved positions with dissimilar residue types have different structural roles in the two domains. Some of these positions, such as His138, are completely exposed to bulk solvent and make no contacts with any ordered atoms in the BPI structure, whereas the structurally equivalent residue from the C-terminal domain, Leu385, makes van der Waals contacts with His361.

[0276] Another example of a pair of residues with different structural roles is Lys12 and Tyr261. Lys12 forms a salt bridge with Asp452, connecting the N-terminal domain of BPI with the C-terminal domain. Tyr261 forms van der Waals contacts with Pro241, located in the domain linker. The structural roles for these two residues are different because Lys12 stabilizes the interface between the two domains and Tyr261 interacts with the domain linker.

[0277] For the next analyses, the clustering of 3D-1D environmentally conserved positions in both the BPI fold and the lipid binding pockets was studied. FIG. 10(a) shows a space-filling representation of BPI. 3D-1D environmentally conserved positions are colored red. The two bound phospholipids are gold. The N-terminal domain is shown on the left. FIG. 10(b) shows a spaced-filling representation of BPI rotated 90° about the x-axis relative to FIG. 10(a). Positions colored dark blue: (1) have conserved 3D-1D environments and are paired in the structural alignment, (2) contain at least one atom in contact with at least one lipid atom; (3) both positions are in contact with at least one lipid atom. Positions that are colored cyan: (1) and (2) hold but not (3). Positions that are colored green: 3D-1D environmentally conserved positions from the C-terminal domain that are in contact with the lipid-binding pocket of the N-terminal domain. Positions colored purple: 3D-1D-conserved positions from the N-terminal domain that are in contact with the lipid-binding pocket of the C-terminal domain. FIG. 10(c) shows the interaction of 3D-1D environmentally conserved positions in the N-terminal lipid-binding pocket. These seven positions satisfy the following constraints: (1) have conserved 3D-1D environments and are paired in the structural alignment; (2) contain at least one atom in contact with at least one lipid atom; (3) structurally equivalent positions in the C-terminal domain are also in contact with at least one lipid atom. The residues occupying these positions are also shown in 10(b) as blue spheres. The van der Waals radii are also shown for the atoms. These residues form a cluster which interacts exclusively with only one acyl chain of the. phospholipid, shown as gray ball-and-sticks. FIG. 10(d) shows the interaction of 3D-1D environmentally conserved positions in the C-terminal lipid-binding pocket. These six positions also satisfy the same constraints as the equivalent N-terminal positions. The residues interact with only one acyl chain of the lipid.

[0278] Positions with conserved 3D-1D enviromnents tend to cluster in the BPI fold. The location of the 51 3D-1D environmentally conserved pairs are highlighted in FIG. 10(a). These positions tend to cluster around the core of each domain and the phospholipid binding pockets, while the two tips of the molecule contain very few 3D-1D environmentally conserved residues. Clustered positions predominantly belong to classes with mostly buried and apolar environments (H:B1 or E:B1) or mostly solvent accessible environments (H:P2, or E:P2).

[0279] The degree of clustering was assessed by calculating C∝-C∝ distances for all 3D-1D environmentally conserved positions in each domain. For this analysis, a position is considered a tertiary neighbor of another position if its C∝ atom is less than 7 Å away but is not within two residues on the peptide chain. 3D-1D environmentally conserved positions were found to have at least one other conserved tertiary neighbor 41 and 44% of the time for the N-terminal and C-terminal domains, respectively. In contrast, positions that were not 3D-1D environmentally conserved have tertiary neighbors that were conserved only 24 and 28%, confirming that 3D-1D environmentally conserved positions tend to cluster.

[0280] 3D-1D environmentally conserved positions in the lipid-binding pockets of each domain also cluster. The program CAST [J. Liang, et al., Prot. Sci., 7:1884-1897 (1998)] was used to identify all positions in contact with at least one lipid atom. Fifty-one positions contribute to the N-terminal lipid-binding pocket and 43 positions contribute to the C-terminal pocket. A total of 11 of these positions from the N-terminal pocket are 3D-1D environmentally conserved; 15 positions from the C-terminal pocket are 3D-1D environmentally conserved. While the number of 3D-1D environmentally conserved positions between the domains of BPI must be equal, the number of conserved positions in the lipid-binding pockets can differ. This is explained by the observation that some positions located in a lipid-binding pocket are aligned to positions that are not located in the other pocket. Therefore, only eight of the environmentally conserved positions in each pocket are paired in the BPI domain alignment.

[0281] The eight structurally equivalent positions from the lipid-binding pockets cluster in each domain (FIG. 10(b)). Seven of the eight residues at these positions in the N-terminal lipid-binding pocket interact exclusively with only one acyl chain of the phospholipid (FIG. 10(c)). Six of the eight residues at these positions in the C-terminal pocket interact exclusively with only one acyl chain of the lipid (FIG. 10(d)).

[0282] Nearly all of the 3D-1D environmentally conserved positions in the lipid-binding pockets belong to either the H:B1 (helical secondary structure and buried) or E:B1 (□-strand secondary structure and buried) environment classes. This is as one would expect because buried, hydrophobic residues contribute to pockets which bind apolar molecules. An exception occurs at the Phe228-Tyr455 pair, where the conserved environment class is E:P2. These residues are near the mouth of the lipid-binding pockets and are exposed to solvent.

[0283] The structure coordinates described in Example 4 and listed in Table 6 and the analyses described in this Example are useful for the designing and making of new and useful products based on BPI, including a BPI protein, including a fragment, analog or variant thereof, or of a BPI related lipid transfer protein, including a fragment, analog or variant thereof.

	Number	Date	Country
Parent	09872128	May 2001	US
Child	10162743	Jun 2002	US
Parent	08879565	Jun 1997	US
Child	09518598	Mar 2000	US

	Number	Date	Country
Parent	09518598	Mar 2000	US
Child	09872128	May 2001	US
Parent	09446415	Jul 2000	US
Child	09518598	Mar 2000	US
Parent	08879565	Jun 1997	US
Child	09518598	Mar 2000	US

Bactericidal/permeability-increasing protein: crystallization, x-ray diffraction, three-dimensional structure determination, rational drug design and molecular modeling of related proteins

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