BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN: CRYSTALLIZATION, X-RAY DIFFRACTION, THREE-DIMENSIONAL STRUCTURE DETERMINATION, RATIONAL DRUG DESIGN AND MOLECULAR MODELING OF RELATED PROTEINS

Abstract: The present invention solves the three-dimensional structure of BPI and thereby provides atomic coordinates of BPI from the analysis of x-ray diffraction patterns of sufficiently high resolution for three-dimensional structure determination of the protein, as well as methods for rational drug design, based on using amino acid sequence data and/or x-ray diffraction data provided on computer readable media, as analyzed on a computer system having suitable computer algorithms; and atomic coordinates are provided yielding structural information on related proteins, including the lipid binding and lipid transport protein family that includes BPI, LBP, CETP and PLTP.

Description: BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN: CRYSTALLIZATION, X-RAY DIFFRACTION, THREE- DIMENSIONAL STRUCTURE DETERMINATION, RATIONAL DRUG DESIGN AND MOLECULAR MODELING OF RELATED PROTEINS This is a continuation-in-part application of U.S. Application Serial No. 08/879,565, filed June 20, 1997, which is hereby incorporated by reference in its entirety. 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. Part of the work performed during development of this invention utilized U.S. Government funds. The U.S. Government has certain rights in this invention. Background of the Invention 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 Figure 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. Patent 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. 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 "rBPI 23 ," 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, rBPI 21 , has been produced as described in Horwitz et al., Protein Expression Purification, S:28-40 (1996). 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. 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. 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., 55:853-860 (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. 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)). 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) . 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. Patent 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. Patent 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. Patent 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. Patent No. 5,627,153 and corresponding International Publication No. WO 95/19179 (PCT/US95/00498), and further as described for anti-fungal peptides in co-pending U.S. Application Serial No. 08/621,259 filed March 21, 1996, which is in turn a continuation- in-part of U.S. Application Serial No. 08/504,841 filed July 20, 1994 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. Patent No. 5,646, 114 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 co-pending U.S. Application Serial No. 08/694,843 filed August 9, 1996 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 co-pending U.S. Application Serial No. 08/626,646 filed April 1, 1996, which is in turn a continuation of U.S. Application Serial No. 08/285,803 filed August 14, 1994, which is in turn a continuation-in-part of U.S. Application Serial No. 08/031,145 filed March 12, 1993 and corresponding International Publication No. WO94/20129 (PCT/US94/02463), all of which are incorporated herein by reference. 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. Patent Nos. 5,643,875 and 5,753,620 and corresponding International Publication No. WO 95/19784 (PCT/US95/01151), all of which are incorporated herein by reference. BPI protein products are also known to be useful for treatment of specific disease conditions, such as meningococcemia in humans (as described in co-pending U.S. Application Serial No. 08/644,287 filed May 10, 1996 and corresponding International Publication No. WO 97/42966 (PCT/US97/08016), which are incorporated herein by reference), hemorrhagic trauma in humans, (as described in co-pending U.S. Application Serial No. 08/862,785, a continuation-in-part of U.S. Serial No. 08/652,292 filed May 23, 1996, now U.S. Patent 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. Patent 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. Patent No. 5,578,568, incorporated herein by reference), and liver resection (as described in co-pending U.S. Application Serial No. 08/582,230 filed March 16, 1998 which is a continued prosecution application of the same serial no. filed January 3, 1996, which is in turn a continuation of U.S. Application Serial No. 08/318,357 filed October 5, 1994, which is in turn a continuation-in-part of U.S. Application Serial No. 08/132,510 filed October 5, 1993, and corresponding International Publication No. WO 95/10297 (PCT/US94/ 11404), all of which are incorporated herein by reference). BPI protein products are also known to neutralize the anti-coagulant activity of exogenous heparin, as described in U.S. Patent 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. Patent 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 co-pending U.S. Application Serial Nos. 08/435,855, 08/466,624 and 08/466,826, and corresponding International Publication No. WO 94/20128 (PCT/US94/02401), all of which are incorporated herein by reference. BPI protein products are also known for use in antithrombotic methods, as described in U.S. Patent No. 5,741,779 and corresponding International Publication No. WO97/42967 (PCT/US97/08017), which are incorporated herein by reference. U.S. Patent Nos. 5,420,019 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. 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. Patent Nos. 5,198,541 and 5,523,288; WO95/08344 (PCT/US94/ 11225)] and gram-positive bacteria [U.S. Patent No. 5,578,572; WO95/19180 (PCT/US95/00656)] , fungi [U.S. PatentNo. 5,627,153; WO95/19179 (PCT/US95/00498)] , mycobacteria [EP0690721; WO94/20129 (PCT/US94/02463)] and chlamydia [WO96/01647 (PCT/US95/08624)] and endotoxin binding/neutralizing agents [WO95/019784 (PCT/US95/01151)], and as heparin binding/neutralizing products [U.S. Patent 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, and anticoagulant and thrombolytic agents for the treatment of thrombotic disorders [PCT/US97/08017]. 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 The present invention solves the above problem and fulfills the need for designating 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. 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. 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). 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. The present invention provides use of atomic coordinates of a bactericidal/permeability-increasing ("BPI") protein, to design compounds with at least one activity selected from the group consisting of antibacterial, antifungal, antimycobacterial, antichlamydial, antiprotozoan, heparin-binding, endotoxin-binding, hepar in-neutralizing, endotoxin-neutralizing, inhibition of tumor and endothelial cell proliferation, inhibition of angiogenesis, anti-inflammatory, anticoagulant and antithrombolytic. The coordinates disclosed herein are suitable for all of the aforementioned uses of atomic coordinates. 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. 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. 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. 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. 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. said at least one ligand of a BPI protein, BPI-related lipid binding protein, or fragment, analog or variant thereof. 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 Fig. 1 (A) A ribbon diagram of residues 1-456 of BPI illustrating its boomerang shape. The NH 2 -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., .050:889 (1994); D. J. Bacon and W. F. Anderson, J. Mo. Graphics, 6:219 (1988)]. Fig. 2 (A) Schematic drawing of the novel BPI domain fold, shown in same orientation as the NH 2 - terminal domain in Fig. IB (B) Superposition of the NH 2 - and COOH-terminal domains of BPI showing the overall topological similarity. Residues 1 to 230 and 250 to 456 are shown. The NH 2 -terminal domain is in the same orientation as Fig. 1A. Fig. 3 Electron density of the final 2.8 A MIR map contoured at 1.0 σ and superimposed on the refined model. The area shown is in the lipid binding pocket of the NH 2 -terminal domain of BPI. The phosphatidylcholine and the surrounding protein atoms are shown. 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 NH 2 - 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, 221:109 (1983); M. L. Connolly, J. Am. Chem. Soc, 07: 1118 (1985)]. 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, J27:632 (1987); R. Day et al., J. Biol. Chem., 269:9388 (1994); S.R. Leong and T. Camerato, Nucleic Acids Res., 18:3052 (1990); M. Νagashima, 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 11:1159 (1991); G. Su et al., J. Immunol., 153:143 (1994); P. W. Gray et al., J. Biol. Chem. 264: 9505 (1989); Albers et al., Biochem. Biophys. Acta, 1258:21 (1995); X. C. Jiang et al., Biochemistry, 34:1258 (1995); L. B. Agellon et al., Biochemistry, 29:1372 (1990); X. C. Jiang et al., /. 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 Λ above the strands. The α 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 A of the ΝH 2 - terminal lipid are highlighted with gray shading; residues within 4 A of the COOH- terminal lipid are shown with white letters in black boxes. 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. Detailed Description 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. 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. 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. Patent 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 rBPI 55 or simply rBPI 50 ) 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. Patent 5,439,807 on August 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. 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 rBPI 23 . In that publication, an expression vector was used as a source of DNA encoding a recombinant expression product (rBPI 23 ) 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 Figure 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 Figure 1 of Gray et al. , supra, with the exceptions noted for rBPI 23 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. Patent 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 rBPI 42 dimer. 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 Serial No. 07/885,911, now abandoned, and a continuation-in-part application thereof, U.S. Patent Application Serial No. 08/064,693 filed May 19, 1993, issued as U.S. Patent 5,643,570 on July 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. 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. Patent No. 5,420,019 and corresponding PCT Application No. US94/01235, filed February 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 rBPI 21 Δcys or rBPI 21 . Other examples include dimeric forms of BPI analogs; e.g. U.S. Patent Application Serial No. 08/212,132 filed March 11, 1994, issued as U.S. Patent 5,447,913 on September 5, 1995 and corresponding PCT Application No. PCT/US95/03125, the disclosures of which are incorporated herein by reference. 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 Serial No. 08/504,841 filed July 20, 1995 and in PCT Application No. PCT/US94/ 10427 filed September 15, 1994, which corresponds to U.S. Patent Application Serial No. 08/306,473 filed September 15, 1994, issued as U.S. Patent 5,652,332 on July 29, 1997, and PCT Application No. US94/02465 filed March 11, 1994, which corresponds to U.S. Patent Application Serial No. 08/209,762, filed March 11, 1994, issued as U.S. Patent 5,733,872 on March 31, 1998, which is a continuation-in-part of U.S. Patent Application Serial No. 08/183,222, filed January 14, 1994, now abandoned, which is a continuation-in-part of U.S. Patent Application Ser. No. 08/093,202 filed July 15, 1993, now abandoned, (for which the corresponding international application is PCT Application No. US94/02401 filed March 11, 1994), which is a continuation-in-part of U.S. Patent Application Ser. No. 08/030,644 filed March 12, 1993, issued as U.S. Patent 5,348,942 on September 20, 1994, the disclosures of all of which are incorporated herein by reference. 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 rBPI 23 or rBPI 2 j, or dimeric forms of these N-terminal fragments (e.g., rBPI 42 dimer). Additionally, preferred BPI protein products include rBPI 50 and BPI-derived peptides. 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. , rBPI 50 , rRBPI 23 ) 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, NJ) and 0.002% by weight of polysorbate 80 (Tween 80, ICI Americas Inc., Wilmington, DE). Another pharmaceutical composition containing BPI protein products (e.g. , rBPI 21 ) 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 February 2, 1994, which corresponds to U.S. Patent Application Ser. No. 08/190,869 filed February 2, 1994, issued as U.S. Patent 5,488,034 on January 30, 1996, and U.S. Patent Application Ser. No. 08/012,360 filed February 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 January 13, 1995, now abandoned, 08/530,599, filed September 19, 1995, now abandoned, and 08/586, 133, filed January 12, 1996 and corresponding WO96/21436 (PCT/US96/01095). 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 A, preferably 1.5-3.0 A and more preferably < 2.6 A. 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. 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. 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. 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. 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. 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 A. The coordinates from these diffraction patterns are suitable and useful for three-dimensional modeling of the crystallized protein. 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. 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). Determination of Protein Structures 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. 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. 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. 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. 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. 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. 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 0.2-3.5A. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. The initial model will contain some errors. Provided the protein crystals diffract to high enough resolution (e.g., better than 3.5 A), 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. 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. 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 A, 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. 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 BPI-protein that have a root mean square deviation of protein backbone atoms (N, Co., C and O) of less that 0.75 A when superimposed — using backbone atoms — on the structure coordinates listed in Table 4 shall be considered identical. Most x-ray structures are determined to a resolution between 1.7 A and 3.5 A. 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. 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. Overview of BPI Purification and Crystallization Methods 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) . 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, CA). 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. Purified BPIs 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. Before crystallization, the purified protein is tested for one or more of the known biological activities of a BPI protein. 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. Protein Crystallization Methods 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. A mixture of the purified protein and precipitant can include the following: pH (e.g. , 4-9); • buffer type (e.g. , phosphate, cacodylate, acetates, imidazole, Tris HCI, sodium HEPES); • buffer concentration (e.g. , 10-200 mM); • salt type (e.g. , calcium chloride, sodium citrate, magnesium chloride, ammonium acetate, ammonium sulfate, potassium phosphate, magnesium acetate, zinc acetate; calcium acetate) • polymer type and concentration: (e.g., polyethylene glycol (PEG) 1-50%, average molecular weight 200-10,000); • other precipitating agents (salts: K, Na tartrate, NH 4 SO 4 , NaAc, LiSO 4 , NaFormate, NaCitrate, MgFormate, NaPO 4 , KPO 4 NH 4 PO 4 ; organics: 2-propanol; non-volatile: 2-methyl-2,4-pentanediol); and • concentration of purified BPI (e.g. , 1.0-100 mg/ml). See, e.g. , CRYSTAL SCREEN, Hampton Research. A non-limiting example of such crystallization conditions is the following: • purified protein (e.g. , approximately 3-4 mg/ml); H 2 O; • precipitant 10-14% Polyethylene glycol (PEG) 8000 buffered with 100 mM cacodylate buffer and 200 mM of Mg acetate; • at an overall pH of about 3.5-8.5. 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 A resolution, such as 1.5 -3.5 A, 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 A or less being preferred. Protein Crystals 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. X-ray Crystallography Methods and Molecular Modeling 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 A or less, sufficient to solve the three-dimensional structure of BPI in considerable detail, as presented herein. 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)). The resolution is optionally improved using larger crystals, e.g., 0.2mm, 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. 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). 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. 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 (A), R r (%), 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. The initial phases are calculated to 3.2 A, and then improved and extended to a higher resolution of 2.8 A (e.g. , <3.0 A) 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. 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 Ccv 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, /3-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. X-ray diffraction data (e.g. , to < 3.0 A) was collected on an RAXIS 1 IC 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, Briinger et al , J. Mol. Biol. 203:803- 816 (1987)). This refinement was followed by manual rebuilding with FRODO using experimental and 2F 0 -F C maps. The model can be optionally further refined using a least-squares refinement program, such as TNT (Tronrud et al. , Ada Crystallogr. A 43:489-501 (1987)). 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). 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. Computer Related Embodiments 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 Figure 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 Figure 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. 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. 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. 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. 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, Mary Ann Liebert Publ., New York (1995). 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. 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. 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. 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. 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. 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. One application of this embodiment is provided in Figure 6. Figure 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. 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. Structure Determination 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 Figure 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. Density Modification and Map Interpretation 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. Refinement and Model Validation Rigid body and positional refinement can be carried out using a program such as X-PLOR (Briinger (1992), infra), e.g., with the stereochemical parameters of Engh and Huber (Acta Cryst. .447:392-400 (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-lθA to 10-3.0 A and then be gradually extended to include higher resolution data from 12-6 A to 3.0-1.5 A). B- values (also termed temperature factors) for individual atoms were refined once data between 2.9 and 1.5 A 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. δ:52-56 (1990)), PROFILE 3D (Lϋthy 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 F obs and F calc was applied after careful assessment of the quality and completeness of the data. 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). 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 (Briinger (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 (Briinger (1992), supra), to a suitable crystallographic R factor . The model data is then saved on computer readable medium for use in further analysis, such as rational drug design. Rational Design of Mimetics or Ligands 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. 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, . Med. Chem. 28:849-851 (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. 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, radio isotope 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. 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)). After preliminary experiments are done to determine the K, 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. 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 (V,) or absence (V 0 ) 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. 75:455-458 (1990)). Therefore, K, values are obtained from the data by fitting to a modified version of the Henderson equation for competitive inhibition: O 2 + (E t - Q - l t ) r - E t = 0 where (using the notation of Henderson (Biochem. J. 727:321-333 (1972)): and A V, This equation is solved for the positive root with the constraint that Q = K,((A t + K a ) / K a ) using PROCNLIN from SAS (SAS Institute Inc., Cary, North Carolina, 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 lO 8 . 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 A, and merged with a suitable R-factor on intensities. An atomic model of the mimetic is built into the difference Fourier map (E, nhlbltor comple χ -E natιve )- The model can be refined to convergence in a cycle of simulated annealing (Briinger (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 A 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. 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. Preferably, little or no change in the structure of the BPI or mimetic occurs in the electron density map described above. K, values are determined by a previously described method (Henderson (1972), infra) to evaluate mimetic proteins or organic compounds. 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. 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. 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 mimetics discovered by structure determination and x-ray crystallography. 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) 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. Construction of Plasmids for BPI Expression The plasmid pIC108 containing a cDNA encoding BPI cloned in a T3T7 plasmid (Clontech, Palo Alto, CA) served as the starting point for the construction of a vector for expression of nonglycosylated rBPI in mammalian cells. To allow insertion of BPI into an optimized mammalian expression vector, a unique Xhol 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 Xhol 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 Xhol site at the 3 ' end of the gene. The amplified fragment was digested with Ncol and BgUl and ligated to a -4100 bp ΝcoI-BamHI fragment from pIC108 to generate the plasmid pSSlOl. Construction of Plasmid with BPI (S351A) The glycosylation site was next removed by replacing the region from a unique Xcml site to a unique SphI site within the BPI gene in pSSlOl 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. Wild type Xcml 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 lie Gly Met His 351 Νonglycosylated Xcml 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 lie Gly Met His 351 This step generated the plasmid pSS102. To construct the vector, pIΝG4322, for the expression of full length nonglycosylated holo BPI in mammalian cells, pSS102 was digested with BstBl and Xhol and a 596 bp fragment, which included the modified BPI sequence, was purified and ligated to the large Bst l-Xhol 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. Patent 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. Stable Transfection of Mammalian Cells for Expression of Nonglycosylated BPI 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-Agl4 (ATCC CRL1581) or the myeloma, NSO (ECACC No. 85110503). 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. Transfection of CHO-K1 Cells with pING4322 The CHO-K1 cell line was maintained in Ham's F12 medium plus 10% fetal bovine serum (FBS). Media were supplemented with glutamine/penicillin/ streptomycin (Irvine Scientific, Irvine, California). CHO-K1 cells were transfected by electroporation with 40 μg of pING4322 DNA that was first digested with Pvul, 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 X 10 4 cells/ml in Ham's F12 medium supplemented with MPA (25 μg/mL) and xanthine (250 μg/mL) and plated at - 10 4 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 BPI 23 as a standard. In this assay, Immulon-II 96 well plates (Dynatech) were pre-coated with affinity purified rabbit anti-BPI 23 antiserum, followed by supernatant samples and detection was with affinity purified, biotinylated rabbit anti-BPI 23 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. Production and Purification of Nonglycosylated rBPI. 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. Forty roller bottles were prepared which contained the transfected CHO-K1 host cells at 1.3 x 10 7 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. Patent No. 5,439,807 and WO93/23540 (PCT/US93/04752). 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 x 50 cm liquid chromatography column (BIORAD, Econocolumn, Richmond, California). 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. 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. 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, MA) or a 0.2 μm Nalgene filter (Nalge Corp., Rochester, NY) to remove precipitate. Protein samples were concentrated in a Centricon 10 (Amicon Corp., Beverly, MA) or a Centriprep 10 (Amicon Corp. , Beverly, MA). For the Centricon 10 concentrators, a JA 20 rotor (Beckman, Fullerton, CA) 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 Presented herein is the crystal structure of BPI and two bound phospholipids at 2.4 A 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. 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 C 2 , with one molecule per asymmetric unit. Form 1 crystals were reproducible and had cell dimensions of a = 185.0, b=31.2, c=84.3 A, and 0 = 101.3 ° . Form 2 crystals appeared rarely and had cell dimensions of = 185.6, b=33.0, c=85.2 A, and 0 = 101.6' 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 A 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 A 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., 77:268 (1978)], phase combination was performed with SIGMA A [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. TABLE 1: X-RAY DIFFRACTION DATA *Rsym= 100 (∑ h | | h - < | > | )/(∑h |h) where < | > is the mean intensity of all symmetry-related reflections |h. tRc u s = (∑ |F PH +/-Fp | - F H(calc) )/(Σ | F PH +/-Fp I ) for centric reflections, Phasing power =[∑| F H(caIC) 2 |/ (Σ |F PH(obs) - F PH(ca]c) | 2 ]" 2 ' φMID (mean isomorphous difference) = Σ | F PH - F P | /Σ F P , where F PH is the derivative structure factor and F P is the native structure factor and the sum is over all reflections common to both data sets. §CMNP, chloro-Hg-nitrophenol; || DMM, dimethyl mercury; 1JPCMBS, parachloromercurybenzene sulfonate; #TELA, triethyl lead acetate Table 2 relates to model refinement and statistics. The model was refined at 2.8 A through iterative cycles of simulated-annealing with X-PLOR [A. T. Briinger and A. Krukowski, Ada Crystallogr., .446:585 (1990)] and manual rebuilding. 10% of the data were set aside before refinement began for R free [A. T. Briinger Nature, 355:412 (1992)] calculations. When the model had been refined to an R-factor* of 20.4% (R free =32.6%) with the 2.8 A data, rigid-body minimization was performed against the 2.4 A data set (R= 29.8% to 3.5 A 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 R free =31.3% (no intensity cutoff). An overall anisotropic temperature factor and bulk solvent correction were applied to the observed reflections when R free 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, /. Appl. Crystallogr. 26:283 (1993)], VERIFY [R. Luthy, J. U. Bowie, D. Eisenberg, Nature, 356:83 (1992)], and ERRAT [C. Colovos and T. Yeates, Protein Sci., 2: 1511 (1993)]. TABLE 2: REFINEMENT STATISTICS FOR FORM 2 CRYSTALS Data Resolution (A) 2.4 Unique reflections (N) 18,898 Completeness (%) 92.7 Atoms in model Protein (non-hydrogen) 3532 Phosphatidylcholine 102 Water 48 Refinement parameters Resolution range (A) 50.0-2.4 R-factor* (%) 22.7 RfreeW 31.3 Avg. atomic B factors Protein 36.9 Lipid N, C 49.4, 51. Ot Waters 44.6 rmsφ deviation from ideality Bonds (A) 0.006 Angles (deg) 1.4 Dihedrals (deg) 26.0 Impropers (deg) 1.2 *R = 100 (Σ I F_ bs - F c | )/(Σ F obs ) where F obs and F c are the observed and calculated structure factors, respectively |B factors for the lipids bound in the NH 2 - and COOH-terminal domains Jrms=root mean square BPI is a boomerang-shaped molecule with approximate dimensions of 135 by 35 by 35 A (Fig. 1 , A and B). It consists of two domains of similar size (NH 2 - 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. Each barrel (residues 10 to 193 and 260 to 421) contains three common structural elements: a short 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 NH 2 -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 Cys 135 and Cys 175 anchors helix B to the final strand of sheet N. Situated between the NH 2 - and COOH-terminal barrels is a twisted, seven-stranded antiparallel β sheet composed of four strands from the NH 2 -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, /. Mol. Biol., 169:151 (1983); G. N. Reeke, J. W. Becker, G. M. Edelman, J. Biol. Chem., 250: 1525 (1975)]. 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 A 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 NH 2 -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 NH 2 -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 NH 2 -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., 774:649 (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. 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 F obs -F calc 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. The two lipids are bound in extensive apolar pockets on the concave surface of the boomerang, situated between the NH 2 - terminal and COOH-terminal barrels and the central β sheet. In the NH 2 -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 A 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 NH 2 -terminal domain has a solvent accessible surface area [M. L. Connolly, Science, 221:109 (1983); M. L. Connolly, J. Am. Chem. Soc, 707: 1118 (1985)] of 557 A 2 , and the pocket in the COOH-terminal domain has an area of 413 A 2 , for a total of 970 A 2 . 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. 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). Our proposed site of interaction between BPI and the acyl chains of LPS differs from that suggested by previous work focusing on the NH 2 -terminal domain. Fragments containing the NH 2 -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., 774:649 (1991)]. The activity of one NH 2 -terminal fragment was reduced when residues past positions 12 or between positions 169 and 199 were deleted [C. Capodici and J. Weiss, J. Immunol., 156:4189 (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 a 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 NH 2 -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 NH 2 - terminal tip to BPI's LPS-binding and bactericidal activities. 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. Tail, Annu. Rev. Biochem., 64:235 (1995)]. Alignment of the amino acid sequences of human BPI, LBP, CETP, and PLTP with BPI's secondary structure (Fig. 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. 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: 11481 (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 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. 1. Individual Peptide Domains: 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. 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. 2. Peptide Domain Hybrids: 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 Ill-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. 3. BPI "Tip" Mimetics: 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 Insightll (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. 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. 4. Extended N-terminal Domains of BPI: 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 rBPI 21 . 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. 5. Mutants for Immobilizing rBPI 21 : 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 rBPI 23 . Alternatively, in order to selectively couple a stable, readily produced protein like rBPI 21 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(l-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(l-193)C and other thiol-containing proteins or molecules is created for the purposes of evaluating new molecules. 6. New N-terminal Dimeric Molecules: 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. 7. C-terminal Fusion Proteins: 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. 8. Homology modeling of BPI family members: 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 Insightll 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. 9. Lipid Pocket Mutants: 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 He 68, in 3 of the 7 sequences, the residue is similarly He; 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. TABLE 3 Residue name and number. Checked residues show a change in solvent accessible surface area with lipid binding. Checked 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). Conservation in 3 BPI and 4 LBP sequences, e.g. , for He 68, in 3 of the 7 sequences, the residue is similarly He; for the other 4 sequences, the residue is Leu (see note 5). Indicates alternative residues which occur in BPI or LBP at that position for the 7 BPI and LBP sequences analyzed. 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. i/58961 66 f'ci/uayβ/ijuu/ TABLE 4 ATOM 1 CB VAL A 1 95.942 11.564 18.390 1.00 51.23 ATOM 2 CGI 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 TOM 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 CGI 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 TOM 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 CGI 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 CGI 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 CGI 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 OEl 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 OEl 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 22 124 .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 OEl 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 OEl 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 NHl 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 CGI 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 CGI 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 CGI 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 NDl 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 CD1 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 NDl HIS A 50 162, .324 29, .196 16, .311 1. ,00 73, .69 ATOM 487 CEl 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 CDl TYR A 51 157 .987 31 .449 11 .266 1 .00 53 .21 ATOM 498 CEl 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 CDl 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 CEl 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 CDl TYR A 54 154.782 36.139 17.437 1.00 42.10 ATOM 532 CEl 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 ODl 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 CGI ILE A 58 139.825 35.415 14.744 1.00 42.15 ATOM 572 CDl 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 NHl 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 0 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 OEl 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 CDl 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 CEl 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 OEl 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 CDl 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 OEl 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 CGI ILE A 68 118.850 27.925 7, .333 1. ,00 44. .56 ATOM 676 CDl 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 CGI 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 ODl 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 CGI 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 CDl 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 CDl 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 CEl 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 CGI ILE A 80 127.057 30.714 6.797 1.00 38.41 ATOM 783 CDl 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 ODl 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 ODl 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 CGI ILE A 85 137.342 33.965 8.222 1.00 30.72 ATOM 828 CDl 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 CGI ILE A 87 142.358 35.964 11.129 1.00 41.65 ATOM 850 CDl 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 CDl 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 OEl 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 NHl 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 CDl 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 CEl 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 CDl 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 ODl 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 CDl 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 CEl 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 ODl 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 CDl 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 CGI ILE A 108 142.157 33.327 6.474 1.00 47.60 ATOM 1067 CDl 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 OEl 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 CGI ILE A 113 131.505 28.480 7.190 1.00 35.78 ATOM 1108 CDl 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 ODl 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 CDl 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 CDl 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 ODl 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 OGl 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 OGl 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 CGI ILE A 130 118.345 22.042 15.425 1.00 38.94 ATOM 1253 CDl 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 5 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 10 ATOM 1259 CB THR A 131 121. .351 17. ,318 16. 747 1. 00 40. 39 ATOM 1260 OGl THR A 131 120. .833 16. .354 15. ,825 1. 00 40. 07 15 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 25 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 35 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 40 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 45 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 50 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 55 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 60 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 65 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 NDl HIS A 138 136.268 26.025 -0.368 1.00 59.15 ATOM 1319 CEl 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 CGI ILE A 139 139.313 28.751 4.982 1.00 49.41 ATOM 1330 CDl 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 ODl 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 CGI 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 NDl HIS A 143 144 .632 36 .722 -0 .841 1.00 67 .65 ATOM 1368 CEl 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 CGI 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 NDl HIS A 145 146. 497 41. 640 2. 810 1. 00 75. 07 ATOM 1389 CEl 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 CGI ILE A 146 153. .545 39. .214 6, .729 1. .00 76. .58 ATOM 1400 CDl 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 CGI 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 CDl TRP A 153 163.022 34.730 5.760 1.00 42.27 ATOM 1453 NEl 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 CDl 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 CGI ILE A 155 155.679 37.906 3.215 1.00 39.53 ATOM 1475 CDl 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 OEl 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 CDl 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 CDl 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 CEl 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 NDl HIS A 159 150.674 31.851 1 .087 1 .00 44 .17 ATOM 1519 CEl 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 CGI ILE A 162 153. 679 28. 764 9. 670 1. 00 43. 35 ATOM 1556 CDl 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 163 149. .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 OEl 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 CDl 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 NHl 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 ODl 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 ODl 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 OEl 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 CGI 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 OEl 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 CGI 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 OGl 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 ODl 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 CGI 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 OEl 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 CDl 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 OEl 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 0 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 CDl TYR A 189 115.222 30.996 21.958 1.00 28.37 ATOM 1815 CEl 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 CDl 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 CEl 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 OEl 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 OGl 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 CDl 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 CGI 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 OGl 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 CGI ILE A 199 94 .543 29 .487 30 .843 1 .00 23 .67 ATOM 1917 CDl 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 25.81S " 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 ODl 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 CGI 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 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 CGI ILE A 205 95.928 26.672 26.627 1.00 16.69 ATOM 1962 CDl 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 ODl 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 CDl TYR A 207 99.703 24.943 21.961 1.00 19.32 ATOM 1982 CEl 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 CDl 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 CGI 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 0 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 OGl 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 OGl 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 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 OEl 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 OGl 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 CDl 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 ODl 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 CGI 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 OEl 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 OEl 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 CDl 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 CEl 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 CDl TYR A 229 96.034 20.816 32.015 1.00 34.08 ATOM 2174 CEl 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 OEl 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 CDl 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 CEl 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 CGI 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 OEl 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 60.4? " ATOM 2308 CG PHE A 246 96.689 25.567 6.663 1.00 56.43 ATOM 2309 CDl 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 CEl 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 ODl 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 NHl 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 CGI 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 CDl TYR A 255 101. 913 30. 756 6. 987 1.00 31. 99 ATOM 2390 CEl 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 CDl 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 CDl 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 ODl 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 CDl TYR A 261 91.304 19.157 20.038 1.00 29.26 ATOM 2444 CEl 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 CDl 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 CEl 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 CDl 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 CEl 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 ODl 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 OGl 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 CDl 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 CGI 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 CDl TYR A 270 87 .766 28 .169 32 .415 1.00 25 .23 ATOM 2530 CEl 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 OEl 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 OEl 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 CGI 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 CDl 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 OGl 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 CDl 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 NHl 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 ODl 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 ODl 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 0 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 CGI ILE A 285 70. ,235 45. 303 37. ,783 1. 00 53. 28 ATOM 2678 CDl 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 OEl 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 CDl 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 CEl 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 NHl 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 CDl 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 OGl 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 OGl 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 CDl 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 CEl 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 CDl 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 CEl 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 OGl 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 CDl 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 CEl 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 CDl 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 OEl 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 CGI 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 CDl . 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 CEl 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 ODl 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 CGI ILE A 314 62. 745 38. 728 43. 093 1. 00 33. 03 ATOM 2963 CDl 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 OEl 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 CGI ILE A 316 67 .249 36 .518 38 .864 1 .00 36 .98 ATOM 2984 CDl 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 NDl HIS A 317 71.572 30.398 42.666 1.00 32.81 ATOM 2995 CEl 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 CGI 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 OGl 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 NDl HIS A 325 77 .817 22 .041 20 .405 1 .00 52 .21 ATOM 3061 CEl 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 CDl 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 CGI 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 OEl 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 OGl 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 CDl 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 OGl 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 CDl 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 CEl 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 CDl TYR A 336 75. 107 27. 665 18. 072 1. 00 38. 45 ATOM 3160 CEl 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 CGI 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 .12 144 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 5 ATOM 3194 ODl 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 1 1U0 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 15 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 CGI VAL A 341 67.868 33. 496 34. 831 1. 00 27. 89 9 Δ\0) 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 25 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 35 ATOM 3211 CD GLN A 342 66.706 27. ,570 40. .706 1. .00 33. .87 ATOM 3212 OEl 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 45 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 0 ALA A 343 64.011 31 .826 41 .700 1 .00 30 .49 55 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 60 ATOM 3228 CG PHE A 344 66.891 31 .428 44 .210 1 .00 19 .20 ATOM 3229 CDl PHE A 344 67.806 31 .396 43 .173 1 .00 20 .33 65 ATOM 3230 CD2 PHE A 344 66.547 30 .247 44 .834 1 .00 15 .57 ATOM 3231 CEl 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 CGI 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 CDl 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 ODl 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 CDl 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 CDl 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 CDl 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 CEl 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 CDl 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 CGI ILE A 358 63.220 31.510 33.207 1.00 33.8-2- ATOM 3350 CDl 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 NDl HIS A 361 67 .753 28 .041 22 .618 1 .00 53 .69 ATOM 3375 CEl 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 OGl 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 OGl 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 OEl 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 CGI 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 OEl 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 ODl 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 NHl 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 CDl 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 CGI 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 OEl 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 CDl 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 CDl 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 ODl 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 NHl 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 CDl 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 CDl 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 CDl 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 OEl 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 CDl 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 NDl HIS A 390 59.682 23.568 39.554 1.00 76.75 ATOM 3654 CEl 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 ODl 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 CGI ILE A 393 55.948 31.622 39.995 1.00 57.06 ATOM 3684 CDl 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 CDl 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 CEl 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 CGI 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 OEl 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 CDl 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 CDl 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 OEl 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 ODl 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 CGI ILE A 404 63.337 41.654 34.203 1.00 42.01 ATOM 3781 CDl 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 ODl 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 CDl TYR A 407 68. 891 46. ,916 30. ,897 1. ,00 45. .96 ATOM 3810 CEl 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 CGI ILE A 408 68 .613 40 .974 34 .281 1 .00 41 .88 ATOM 3824 CDl 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 CGI 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 5 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 1 10 ATOM 3840 C PRO A 410 74.535 43. 083 28.685 1.00 40.43 ATOM 3841 0 PRO A 410 75.607 43. 593 28.359 1.00 41.27 15 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 70 ATOM 3846 CG2 ILE A 411 73.890 46. 497 32.086 1.00 41.83 ATOM 3847 CGI ILE A 411 72.418 45. 967 30.122 1.00 42.47 25 ATOM 3848 CDl 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 0 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 35 TOM 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 CDl 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 45 ATOM 3859 0 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 JOυ ATOM 3863 CB VAL A 413 75.344 37 .708 31.642 1.00 38.08 ATOM 3864 CGI VAL A 413 76.042 36 .373 31.445 1.00 39.08 55 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 0 VAL A 413 78.634 38 .583 31.221 1.00 36.97 60 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 65 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 CDl 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 NHl 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 CGI 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 ODl 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 5 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 10 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 15 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 OEl GLU A 419 86.182 42.226 33.751 1.00 59.06 9 Iλ0J 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 25 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 30 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 35 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 40 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 45 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 50 ATOM 3947 CG LEU A 421 85.770 35.278 25.539 1.00 34.05 ATOM 3948 CDl LEU A 421 84.533 35.489 24.703 1.00 31.56 55 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 60 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 65 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 OEl 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 CDl 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 CEl 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 CDl 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 OGl 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 NHl 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 CGI 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 OEl 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 CDl 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 CDl TYR A 436 106.259 41.452 13.573 1.00 43.96 ATOM 4091 CEl 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 ODl 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 CGI 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 CGI 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 CDl 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 OEl 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 NDl HIS A 443 90.868 29.421 6.400 1.00 31.12 ATOM 4162 CEl 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 OEl 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 ODl 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 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 CDl 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 CEl 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 CDl 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 CDl 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 CDl 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 CEl 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 5 ATOM 4242 0 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 1ι0u 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 15 ATOM 4248 ODl 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 7 __0u ATOM 4251 0 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 25 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 CGI 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 35 ATOM 4259 0 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 4 -r0U ATOM 4263 CB VAL A 454 109.895 41.280 15 .511 1.00 41 .60 ATOM 4264 CGI VAL A 454 108.859 41.423 16 .605 1.00 42 .90 45 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 0 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 55 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 CDl TYR A 455 114.682 35.774 18 .875 1.00 43 .02 ATOM 4274 CEl 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 65 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 ATQM_ 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 OTl 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 Cl 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 1.00100.00 ATOM 4303 C8 PC A 777 126.086 33.627 22.335 1.00100.00 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 Cll 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 C 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 Oil PC A 777 118.194 33.427 16.467 1.00 52.98 ATOM 4341 031 PC A 777 123.576 28.862 17.906 1.00 56.48 ATOM 4342 02 PC A 777 122.068 30.020 19.350 1.00 61.36 ATOM 4343 03 PC A 777 119.731 32.307 17.866 1.00 53.04 ATOM 4344 OIP PC A 777 121.661 35.196 20.857 1.00 89.42 ATOM 4345 02P PC A 777 120.059 33.339 21.280 1.00 90.46 ATOM 4346 03P PC A 777 122.419 32.815 20.622 1.00 84.15 ATOM 4347 04P 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 Cl 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 Cll 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 Oil PC A 778 86.692 31.253 29.343 1.00 72.85 ATOM 4390 031 PC A 778 83.619 33.857 35.833 1.00 78.26 ATOM 4391 02 PC A 778 85.652 33.065 34.823 1.00 81.22 ATOM 4392 03 PC A 778 86.615 31.154 31.736 1.00 75.71 ATOM 4393 01P PC A 778 89.401 31.823 36.960 1.00100.00 ATOM 4394 02P PC A 778 89.563 33.853 35.511 1.00100.00 ATOM 4395 03P PC A 778 88.125 31.917 34.809 1.00 96.24 ATOM 4396 04P PC A 778 87.424 33.342 36.757 1.00100.00 ATOM 4397 P PC A 778 88.628 32.739 36.008 1.00100.00 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 Aoo 61. .69 ATOM 4497 OH2 HOH A 934 95. .173 16, .341 20. .293 1.00 48. .05 ATOM 4500 OH2 HOH A 935 Ill .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 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. REMARK 3 MEAN B VALUE (OVERALL, A**2) 45. REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 Bll (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 LUZZATI PLOT (A) 0.45 REMARK 3 ESD FROM 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 ISOTROPIC THERMAL MODEL : RESTRAINED 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 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 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 1 507 VAL ASN PRO GLY VAL VAL VAL ARG ILE SER GLN LYS GLY SEQRES 2 507 LEU ASP TYR ALA SER GLN GLN GLY THR ALA ALA LEU GLN SEQRES 3 507 LYS GLU LEU LYS ARG ILE LYS ILE PRO ASP TYR SER ASP SEQRES 4 507 SER PHE LYS ILE LYS HIS LEU GLY LYS GLY HIS TYR SER SEQRES 5 507 PHE TYR SER MET ASP ILE ARG GLU PHE GLN LEU PRO SER SEQRES 6 507 SER GLN ILE SER MET VAL PRO ASN VAL GLY LEU LYS PHE SEQRES 7 507 SER ILE SER ASN ALA ASN ILE LYS ILE SER GLY LYS TRP SEQRES 8 507 LYS ALA GLN LYS ARG PHE LEU LYS MET SER GLY ASN PHE SEQRES 9 507 ASP LEU SER ILE GLU GLY MET SER ILE SER ALA ASP LEU SEQRES 10 507 LYS LEU GLY SER ASN PRO THR SER GLY LYS PRO THR ILE SEQRES 11 507 THR CYS SER SER CYS SER SER HIS ILE ASN SER VAL HIS SEQRES 12 507 VAL HIS ILE SER ALA ALA SER VAL GLY TRP LEU ILE GLN SEQRES 13 507 LEU PHE HIS LYS LYS ILE GLU SER ALA LEU ARG ASN LYS SEQRES 14 507 MET ASN SER GLN VAL CYS GLU LYS VAL THR ASN SER VAL SEQRES 15 507 SER SER GLU LEU GLN PRO TYR PHE GLN THR LEU PRO VAL SEQRES 16 507 MET THR LYS ILE ASP SER VAL ALA GLY ILE ASN TYR GLY SEQRES 17 507 LEU VAL ALA PRO PRO ALA THR THR ALA GLU THR LEU ASP SEQRES 18 507 VAL GLN MET LYS GLY GLU PHE TYR SER GLU ALA ALA ALA SEQRES 19 507 ALA PRO PRO PRO PHE ALA PRO PRO VAL MET GLU PHE PRO SEQRES 20 507 ALA ALA ALA ASP ARG MET VAL TYR LEU GLY LEU SER ASP SEQRES 21 507 TYR PHE PHE ASN THR ALA GLY LEU VAL TYR GLN GLU ALA SEQRES 22 507 GLY VAL LEU LYS MET THR LEU ARG ASP ASP MET ILE PRO SEQRES 23 507 LYS GLU SER ALA PHE ARG LEU THR THR SER PHE PHE GLY SEQRES 24 507 THR PHE LEU PRO GLU VAL ALA LYS LYS PHE PRO ASN MET SEQRES 25 507 LYS ILE GLN ILE HIS VAL SER ALA SER THR PRO PRO HIS SEQRES 26 507 LEU SER VAL GLN PRO THR GLY LEU THR PHE TYR PRO ALA SEQRES 27 507 VAL ASP VAL GLN ALA PHE ALA VAL LEU PRO ASN SER ALA SEQRES 28 507 LEU ALA SER LEU PHE LEU ILE GLY MET HIS THR THR GLY SEQRES 29 507 SER MET GLU VAL SER ALA GLU SER ASN ARG LEU VAL GLY SEQRES 30 507 GLU LEU LYS LEU ASP ARG LEU LEU LEU GLU LEU LYS HIS SEQRES 31 507 SER ASN ILE GLY PRO PHE PRO VAL GLU LEU LEU GLN ASP SEQRES 32 507 ILE MET ASN TYR ILE VAL PRO ILE LEU VAL LEU PRO ARG SEQRES 33 507 VAL ASN GLU LYS LEU GLN LYS GLY PHE PRO LEU PRO THR SEQRES 34 507 PRO ALA ARG VAL GLN LEU TYR ASN VAL VAL LEU GLN PRO SEQRES 35 507 HIS GLN ASN PHE LEU LEU PHE GLY ALA ASP VAL VAL TYR SEQRES 36 507 LYS PC PC HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 37 507 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 38 507 HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH HOH SEQRES 39 507 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 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 000000 0.000000 0.00000 ORIGX3 0.000000 000000 1.000000 0.00000 SCALE1 0.005388 000000 0.001106 0.00000 SCALE2 0.000000 030303 0.000000 0.00000 SCALE3 0.000000 000000 0.011982 0.00000 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 lbpl . 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 Figure 6 (Figs. 6.1-6.112) in United States patent application serial no. 08/879,565, filed June 20, 1997. "Atom type" refers to the element whose coordinates are measured. The first letter in the column defines the element. "Residue" refers to the amino acid in the BPI protein sequence, using the standard three letter abbreviations known in the art. "#" refers to the residue number. "X, Y, Z" crystallographically define the atomic position, in three-dimensional space, of the element measured. "OCC" is the occupancy value. "B" is a thermal factor that measures movement of the atom around its atomic center. 10. Organomimetics 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. Numerous modifications and variations in the practice of the invention are expected to occur to those skilled in the art upon consideration of the foregoing description and the presently preferred embodiments thereof. Consequently, the scope of the present invention is to be defined by the appended claims. SEQUENCE LISTING (1) GENERAL INFORMATION: (i) APPLICANT: XOMA Corporation; (Beamer, Lesa J., Carroll, Stephen F., Eisenberg, David, U.S. only) (ii) TITLE OF INVENTION: Bactericidal/Permeability-Increasing Protein: Crystallization, X-Ray Diffraction, Three-Dimensional Structure Determination, Rational Drug Design and Molecular Modeling of Related Proteins (iii) NUMBER OF SEQUENCES: 2 (iv) CORRESPONDENCE ADDRESS: (A) ADDRESSEE: McAndrews , Held & Malloy (B) STREET: 500 West Madison, 34th Floor (C) CITY: Chicago (D) STATE: Illinois (E) COUNTRY: United States of America (F) ZIP: 60661 (v) COMPUTER READABLE FORM: (A) MEDIUM TYPE: Floppy disk (B) COMPUTER: IBM PC compatible (C) OPERATING SYSTEM: PC-DOS/MS-DOS (D) SOFTWARE: Patentln Release #1.0, Version #1.25 (vi) CURRENT APPLICATION DATA: (A) APPLICATION NUMBER: (B) FILING DATE: (C) CLASSIFICATION: (vii) PRIOR APPLICATION DATA: (A) APPLICATION NUMBER: U.S. Serial No. 08/879,565 (B) FILING DATE: June 20, 1997 (C) CLASSIFICATION: (viii) ATTORNEY/AGENT INFORMATION: (A) NAME: McNicholas, Janet M. (B) REGISTRATION NUMBER: 32,918 (C) REFERENCE/DOCKET NUMBER: 11034WO01/100-248. PCT (ix) TELECOMMUNICATION INFORMATION: (A) TELEPHONE: 312/707-8889 (B) TELEFAX: 312/707-9155 (C) TELEX: (2) INFORMATION FOR SEQ ID NO:l: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1813 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 31..1491 ( ix) FEATURE : (A) NAME/KEY : mat__peptide (B) LOCATION: 124..1491 (ix) FEATURE: (A) NAME/KEY: misc_feature (D) OTHER INFORMATION: "rBPI" (xi) SEQUENCE DESCRIPTION: SEQ ID NO:l: CAGGCCTTGA GGTTTTGGCA GCTCTGGAGG ATG AGA GAG AAC ATG GCC AGG GGC 54 Met Arg Glu Asn Met Ala Arg Gly -31 -30 -25 CCT TGC AAC GCG CCG AGA TGG GTG TCC CTG ATG GTG CTC GTC GCC ATA 102 Pro Cys Asn Ala Pro Arg Trp Val Ser Leu Met Val Leu Val Ala He -20 -15 -10 GGC ACC GCC GTG ACA GCG GCC GTC AAC CCT GGC GTC GTG GTC AGG ATC 150 Gly Thr Ala Val Thr Ala Ala Val Asn Pro Gly Val Val Val Arg He -5 1 5 TCC CAG AAG GGC CTG GAC TAC GCC AGC CAG CAG GGG ACG GCC GCT CTG 198 Ser Gin Lys Gly Leu Asp Tyr Ala Ser Gin Gin Gly Thr Ala Ala Leu 10 15 20 25 CAG AAG GAG CTG AAG AGG ATC AAG ATT CCT GAC TAC TCA GAC AGC TTT 246 Gin Lys Glu Leu Lys Arg He Lys He Pro Asp Tyr Ser Asp Ser Phe 30 35 40 AAG ATC AAG CAT CTT GGG AAG GGG CAT TAT AGC TTC TAC AGC ATG GAC 294 Lys He Lys His Leu Gly Lys Gly His Tyr Ser Phe Tyr Ser Met Asp 45 50 55 ATC CGT GAA TTC CAG CTT CCC AGT TCC CAG ATA AGC ATG GTG CCC AAT 342 He Arg Glu Phe Gin Leu Pro Ser Ser Gin He Ser Met Val Pro Asn 60 65 70 GTG GGC CTT AAG TTC TCC ATC AGC AAC GCC AAT ATC AAG ATC AGC GGG 390 Val Gly Leu Lys Phe Ser He Ser Asn Ala Asn He Lys He Ser Gly 75 80 85 AAA TGG AAG GCA CAA AAG AGA TTC TTA AAA ATG AGC GGC AAT TTT GAC 438 Lys Trp Lys Ala Gin Lys Arg Phe Leu Lys Met Ser Gly Asn Phe Asp 90 95 100 105 CTG AGC ATA GAA GGC ATG TCC ATT TCG GCT GAT CTG AAG CTG GGC AGT 486 Leu Ser He Glu Gly Met Ser He Ser Ala Asp Leu Lys Leu Gly Ser 110 115 120 AAC CCC ACG TCA GGC AAG CCC ACC ATC ACC TGC TCC AGC TGC AGC AGC 534 Asn Pro Thr Ser Gly Lys Pro Thr He Thr Cys Ser Ser Cys Ser Ser 125 130 135 CAC ATC AAC AGT GTC CAC GTG CAC ATC TCA AAG AGC AAA GTC GGG TGG 582 His He Asn Ser Val His Val His He Ser Lys Ser Lys Val Gly Trp 140 145 150 CTG ATC CAA CTC TTC CAC AAA AAA ATT GAG TCT GCG CTT CGA AAC AAG 630 Leu He Gin Leu Phe His Lys Lys He Glu Ser Ala Leu Arg Asn Lys 155 160 165 ATG AAC AGC CAG GTC TGC GAG AAA GTG ACC AAT TCT GTA TCC TCC AAG 678 Met Asn Ser Gin Val Cys Glu Lys Val Thr Asn Ser Val Ser Ser Lys 170 175 180 185 CTG CAA CCT TAT TTC CAG ACT CTG CCA GTA ATG ACC AAA ATA GAT TCT 726 Leu Gin Pro Tyr Phe Gin Thr Leu Pro Val Met Thr Lys He Asp Ser 190 195 200 GTG GCT GGA ATC AAC TAT GGT CTG GTG GCA CCT CCA GCA ACC ACG GCT 774 Val Ala Gly He Asn Tyr Gly Leu Val Ala Pro Pro Ala Thr Thr Ala 205 210 215 GAG ACC CTG GAT GTA CAG ATG AAG GGG GAG TTT TAC AGT GAG AAC CAC 822 Glu Thr Leu Asp Val Gin Met Lys Gly Glu Phe Tyr Ser Glu Asn His 220 225 230 CAC AAT CCA CCT CCC TTT GCT CCA CCA GTG ATG GAG TTT CCC GCT GCC 870 His Asn Pro Pro Pro Phe Ala Pro Pro Val Met Glu Phe Pro Ala Ala 235 240 245 CAT GAC CGC ATG GTA TAC CTG GGC CTC TCA GAC TAC TTC TTC AAC ACA 918 His Asp Arg Met Val Tyr Leu Gly Leu Ser Asp Tyr Phe Phe Asn Thr 250 255 260 265 GCC GGG CTT GTA TAC CAA GAG GCT GGG GTC TTG AAG ATG ACC CTT AGA 966 Ala Gly Leu Val Tyr Gin Glu Ala Gly Val Leu Lys Met Thr Leu Arg 270 275 280 GAT GAC ATG ATT CCA AAG GAG TCC AAA TTT CGA CTG ACA ACC AAG TTC 1014 Asp Asp Met He Pro Lys Glu Ser Lys Phe Arg Leu Thr Thr Lys Phe 285 290 295 TTT GGA ACC TTC CTA CCT GAG GTG GCC AAG AAG TTT CCC AAC ATG AAG 1062 Phe Gly Thr Phe Leu Pro Glu Val Ala Lys Lys Phe Pro Asn Met Lys 300 305 310 ATA CAG ATC CAT GTC TCA GCC TCC ACC CCG CCA CAC CTG TCT GTG CAG 1110 He Gin He His Val Ser Ala Ser Thr Pro Pro His Leu Ser Val Gin 315 320 325 CCC ACC GGC CTT ACC TTC TAC CCT GCC GTG GAT GTC CAG GCC TTT GCC 1158 Pro Thr Gly Leu Thr Phe Tyr Pro Ala Val Asp Val Gin Ala Phe Ala 330 335 340 345 GTC CTC CCC AAC TCC TCC CTG GCT TCC CTC TTC CTG ATT GGC ATG CAC 1206 Val Leu Pro Asn Ser Ser Leu Ala Ser Leu Phe Leu He Gly Met His 350 355 360 ACA ACT GGT TCC ATG GAG GTC AGC GCC GAG TCC AAC AGG CTT GTT GGA 1254 Thr Thr Gly Ser Met Glu Val Ser Ala Glu Ser Asn Arg Leu Val Gly 365 370 375 GAG CTC AAG CTG GAT AGG CTG CTC CTG GAA CTG AAG CAC TCA AAT ATT 1302 Glu Leu Lys Leu Asp Arg Leu Leu Leu Glu Leu Lys His Ser Asn He 380 385 390 GGC CCC TTC CCG GTT GAA TTG CTG CAG GAT ATC ATG AAC TAC ATT GTA 1350 Gly Pro Phe Pro Val Glu Leu Leu Gin Asp He Met Asn Tyr He Val 395 400 405 CCC ATT CTT GTG CTG CCC AGG GTT AAC GAG AAA CTA CAG AAA GGC TTC 1398 Pro He Leu Val Leu Pro Arg Val Asn Glu Lys Leu Gin Lys Gly Phe 410 415 420 425 CCT CTC CCG ACG CCG GCC AGA GTC CAG CTC TAC AAC GTA GTG CTT CAG 1446 Pro Leu Pro Thr Pro Ala Arg Val Gin Leu Tyr Asn Val Val Leu Gin 430 435 440 CCT CAC CAG AAC TTC CTG CTG TTC GGT GCA GAC GTT GTC TAT AAA 1491 Pro His Gin Asn Phe Leu Leu Phe Gly Ala Asp Val Val Tyr Lys 445 450 455 TGAAGGCACC AGGGGTGCCG GGGGCTGTCA GCCGCACCTG TTCCTGATGG GCTGTGGGGC 1551 ACCGGCTGCC TTTCCCCAGG GAATCCTCTC CAGATCTTAA CCAAGAGCCC CTTGCAAACT 1611 TCTTCGACTC AGATTCAGAA ATGATCTAAA CACGAGGAAA CATTATTCAT TGGAAAAGTG 1671 CATGGTGTGT ATTTTAGGGA TTATGAGCTT CTTTCAAGGG CTAAGGCTGC AGAGATATTT 1731 CCTCCAGGAA TCGTGTTTCA ATTGTAACCA AGAAATTTCC ATTTGTGCTT CATGAAAAAA 1791 AACTTCTGGT TTTTTTCATG TG 1813 (2) INFORMATION FOR SEQ ID NO: 2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 487 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO : 2 : Met Arg Glu Asn Met Ala Arg Gly Pro Cys Asn Ala Pro Arg Trp Val -31 -30 -25 -20 Ser Leu Met Val Leu Val Ala He Gly Thr Ala Val Thr Ala Ala Val -15 -10 -5 1 Asn Pro Gly Val Val Val Arg He Ser Gin Lys Gly Leu Asp Tyr Ala 5 10 15 Ser Gin Gin Gly Thr Ala Ala Leu Gin Lys Glu Leu Lys Arg He Lys 20 25 30 He Pro Asp Tyr Ser Asp Ser Phe Lys He Lys His Leu Gly Lys Gly 35 40 45 His Tyr Ser Phe Tyr Ser Met Asp He Arg Glu Phe Gin Leu Pro Ser 50 55 60 65 Ser Gin He Ser Met Val Pro Asn Val Gly Leu Lys Phe Ser He Ser 70 75 80 Asn Ala Asn He Lys He Ser Gly Lys Trp Lys Ala Gin Lys Arg Phe 85 90 95 Leu Lys Met Ser Gly Asn Phe Asp Leu Ser He Glu Gly Met Ser He 100 105 110 Ser Ala Asp Leu Lys Leu Gly Ser Asn Pro Thr Ser Gly Lys Pro Thr 115 120 125 He Thr Cys Ser Ser Cys Ser Ser His He Asn Ser Val His Val His 130 135 140 145 He Ser Lys Ser Lys Val Gly Trp Leu He Gin Leu Phe His Lys Lys 150 155 160 He Glu Ser Ala Leu Arg Asn Lys Met Asn Ser Gin Val Cys Glu Lys 165 170 175 Val Thr Asn Ser Val Ser Ser Lys Leu Gin Pro Tyr Phe Gin Thr Leu 180 185 190 Pro Val Met Thr Lys He Asp Ser Val Ala Gly He Asn Tyr Gly Leu 195 200 205 Val Ala Pro Pro Ala Thr Thr Ala Glu Thr Leu Asp Val Gin Met Lys 210 215 220 225 Gly Glu Phe Tyr Ser Glu Asn His His Asn Pro Pro Pro Phe Ala Pro 230 235 240 Pro Val Met Glu Phe Pro Ala Ala His Asp Arg Met Val Tyr Leu Gly 245 250 255 Leu Ser Asp Tyr Phe Phe Asn Thr Ala Gly Leu Val Tyr Gin Glu Ala 260 265 270 Gly Val Leu Lys Met Thr Leu Arg Asp Asp Met He Pro Lys Glu Ser 275 280 285 Lys Phe Arg Leu Thr Thr Lys Phe Phe Gly Thr Phe Leu Pro Glu Val 290 295 300 305 Ala Lys Lys Phe Pro Asn Met Lys He Gin He His Val Ser Ala Ser 310 315 320 Thr Pro Pro His Leu Ser Val Gin Pro Thr Gly Leu Thr Phe Tyr Pro 325 330 335 Ala Val Asp Val Gin Ala Phe Ala Val Leu Pro Asn Ser Ser Leu Ala 340 345 350 Ser Leu Phe Leu He Gly Met His Thr Thr Gly Ser Met Glu Val Ser 355 360 365 Ala Glu Ser Asn Arg Leu Val Gly Glu Leu Lys Leu Asp Arg Leu Leu 370 375 380 385 Leu Glu Leu Lys His Ser Asn He Gly Pro Phe Pro Val Glu Leu Leu 390 395 400 Gin Asp He Met Asn Tyr He Val Pro He Leu Val Leu Pro Arg Val 405 410 415 Asn Glu Lys Leu Gin Lys Gly Phe Pro Leu Pro Thr Pro Ala Arg Val 420 425 430 Gin Leu Tyr Asn Val Val Leu Gin Pro His Gin Asn Phe Leu Leu Phe 435 440 445 Gly Ala Asp Val Val Tyr Lys 450 455

Claims: CLAIMS What Is Claimed Is: 1. Use of atomic coordinates of bactericidal/permeability-increasing ("BPI") protein, or fragment, analog or variant thereof, to model a BPI protein. 2. Use of atomic coordinates of bactericidal/permeability-increasing ("BPI") protein, or fragment, analog or variant thereof, to model a BPI-related lipid transfer protein. 3. The use according to claim 2, wherein the BPI-related lipid transfer protein is lipopolysaccharide-binding protein (LBP), cholesteryl ester transferase protein (CETP) or phospholipid transfer protein (PLTP), or fragment, analog or variant thereof. 4. The use according to any of claims 1-3, wherein the BPI protein comprises a binding site characterized by amino acid residues of at least one binding pocket as defined in Table 31. 5. The use according to any of claims 1-3, 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 36 to about 54, positions about 65 to about 99, positions about 84 to about 109, positions about 142 to about 164, or positions about 142 to about 169 of BPI. 6. The use according to any of claims 1-3, 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 17 to about 45, positions about 36 to about 54, positions about 65 to about 99, positions about 84 to about 109, positions about 142 to about 164, or positions about 142 to about 169 of BPI. 7. Use of atomic coordinates of bactericidal/permeability-increasing ("BPI") protein to computationally design a chemical compound for mimicking BPI protein, or fragment, analog or variant thereof. 8. Use of atomic coordinates of bactericidal/permeability-increasing ("BPI") protein to computationally design a chemical compound for mimicking a BPI-related lipid transfer protein, or fragment, analog or variant thereof. 9. The use according to claim 8, wherein the BPI-related lipid transfer protein is lipopolysaccharide-binding protein (LBP), cholesteryl ester transferase protein (CETP) or phospholipid transfer protein (PLTP). 10. Use of atomic coordinates of bactericidal/permeability-increasing ("BPI") protein, to design a chemical compound capable of associating with a BPI-related lipid binding protein, or fragment, analog or variant thereof. 11. The use according to claim 10, wherein the BPI-related lipid binding protein is lipopolysaccharide-binding protein (LBP), cholesteryl ester transferase protein (CETP) or phospholipid transfer protein (PLTP), or fragment, analog or variant thereof. 12. Use of atomic coordinates of bactericidal/permeability-increasing ("BPI") protein to design a model of ligands in an active site of a lipid binding protein. 13. The use according to claim 12, wherein the lipid binding protein is 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. 14. Use of atomic coordinates of bactericidal/permeability-increasing ("BPI") protein, to design compounds with at least one activity selected from the group consisting 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_and antithrombolytic. 15. The use according to any of claims 1 - 14, wherein said atomic coordinates are according to Table 4. 16. A method of three-dimensional modeling of a bactericidal/permeability- increasing ("BPI") 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; (c) generating a three-dimensional structural representation of the BPI protein suitable for visualization and further computational manipulation. 17. A method of three-dimensional modeling of a bactericidal/permeability- increasing ("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; (c) generating a three-dimensional structural representation of the BPI-related lipid transfer protein suitable for visualization and further computational manipulation. 18. The use according to any of claims 16-17, wherein the BPI protein comprises a binding site characterized by amino acid residues of at least one binding pocket as defined in Table 3. 19. The use according to any of claims 16-17, 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 36 to about 54, positions about 65 to about 99, positions about 84 to about 109, positions about 142 to about 164, or positions about 142 to about 169 of BPI. 20. The use according to any of claims 16-17, 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 17 to about 45, positions about 36 to about 54, positions about 65 to about 99, positions about 84 to about 109, positions about 142 to about 164, or positions about 142 to about 169 of BPI. 21. A method for providing an atomic model of a BPI protein, or fragment, analog or variant thereof, comprising (a) providing a computer readable medium having stored thereon atomic coordinate/x-ray diffraction data of the 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, 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, or fragment, analog or variant thereof. 22. A method according to claim 21 , 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 of Figures 2- 20 or Table 2, or a fragment thereof; and wherein said analyzing step further comprises analyzing said sequence data. 23. A computer-based system for providing atomic model data of the three- dimensional structure of BPI protein, or fragment, analog or variant thereof, a BPI mutant or a BPI fragment, comprising the following elements: (a) at least one computer readable medium (CRM) having stored thereon atomic coordinate/x-ray diffraction data of said 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 said BPI 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, or fragment, analog or variant thereof. 24. A method for providing a computer atomic model of a ligand of a BPI 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, 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, or fragment, analog, or variant thereof, and to provide atomic coordinate data defining an atomic model of at least one ligand of said BPI, BPI mutant or a fragment 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, or fragment, analog, or variant thereof. 25. A computer-based system for providing an atomic model of at least one ligand of a BPI, BPI mutant or a fragment thereof, comprising the following elements; (a) a computer readable medium (CRM) having stored thereon atomic coordinate data of a BPI, mutant or fragment thereof; (b) a CRM having stored thereon atomic coordinate data sufficient to generate atomic models of potential ligands of a BPI, mutant or fragment; ' (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, or fragment, analog, or variant thereof, and to provide data output defining an atomic model of at least one potential ligand of BPI 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, or fragment, analog or variant thereof.

Inventors: BEAMER LESA J, CARROLL STEPHEN F, ELSENBERG DAVID, BEAMER, LESA, J., CARROLL, STEPHEN, F., ELSENBERG, DAVID
Applicants: BEAMER LESA J, CARROLL STEPHEN F, ELSENBERG DAVID, UNIV CALIFORNIA, XOMA CORP, BEAMER, LESA, J., CARROLL, STEPHEN, F., ELSENBERG, DAVID, THE REGENTS OF THE UNIVERSITY OF CALIFORNIA, XOMA CORPORATION
Application year: 1998
Main classification: C07K14
IPC codes: C07K1, C07K14, G06F17